ID  E2RU97;
PN  14-3-3 protein;
GN  GL50803_006430;
OS  184922;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:19861170, ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:24147113, ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28932813}. Nucleus {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:22452640}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:28932813}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:28932813}. Nucleus envelope {ECO:0000269|PubMed:28932813}. Endoplasmic reticulum {ECO:0000269|PubMed:28932813}. Note=In trophozoites and cysts, localizes intensely in the cytoplasm. Not detected in the central area of the cell corresponding to the median body nor in flagella. Detected in the nuclei of the encysting cells. Nuclear localization increases during the transition of cells from the early to the late encysting stage. Does not localize to the encystation-specific vesicles of the encysting cells (PubMed:16368691, PubMed:19733174). In interphase cells, detected throughout the cell with somewhat enriched at the cortex and perinuclear region. Associates with the intracytoplasmic axonemes of all flagella, but it is most apparent in the anterior flagella of interphase cells. Localizes also to the nuclear envelope/endoplasmic reticulum and to the microtubule bare area of the ventral disc during interphase. In mitotic cells, disassociates from the intracytoplasmic axonemes and localizes around the spindle. During cytokinesis, localizes with the ingressing furrow, which does not utilize a contractile ring (PubMed:28932813). Does no colocalize with F-actin (PubMed:24728194, PubMed:28932813). {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}.
DR  UNIPROT: E2RU97;
DR  PDB: 4F7R;
DR  PDB: 4ZQ0;
DR  PDB: 5BY9;
DR  Pfam: PF00244;
DR  PROSITE: PS00796;
DE  Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Binds with varying affinity to various synthetic phosphopeptides having a consensus binding motif RSX(pS/pT)XP, called mode-1, where X is any residue and pS/pT is a phosphorylated serine/threonine, and to synthetic phosphopeptides having a consensus binding motif Xp(S/T)X1-2-COOH, called mode-3, in which the phosphorylated residue occupies the penultimate C-terminal position in the target protein, but does not bind to their unphosphorylated counterparts (PubMed:19733174). Binds to synthetic human RAF1 phosphopeptides, but not to their unphosphorylated forms. Binds to difopein, a polypeptide containing a phosphorylation- independent binding motif (PubMed:16368691, PubMed:19733174). Involved in encystation (PubMed:19733174). Involved in cell proliferation. Required for actin and tubulin cytoskeletal organization. Regulates actin filament formation and nuclear size (PubMed:28932813). {ECO:0000250|UniProtKB:P62261, ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:28932813}.
DE  Reference Proteome: Yes;
GO  GO:0005930;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005783;
GO  GO:0031514;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0003779;
GO  GO:0042802;
GO  GO:0019900;
GO  GO:0051219;
GO  GO:0050815;
GO  GO:0042803;
GO  GO:0030036;
GO  GO:1990051;
GO  GO:0030010;
GO  GO:0000165;
GO  GO:0051495;
GO  GO:0051289;
GO  GO:0070207;
GO  GO:0008104;
GO  GO:0097298;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEAFTREDYVFMAQLNENAERYDEMVETMRKISGMEGELSDKERNLLSVAYKNVIGPRRAAWRIVSSIEAKEKGRQKPN
SQ  AKRIEQIRVYRQKIEKELSDICNDILKLLQEQFVPRSTNADAKVFYYKMQGDYYRYLAEYSSGEDKEKIAGSALNAYNSA
SQ  FEISQQLPPTHPIRLGLALNFSVFYYEILASPDRACELARKAFDAAITDLDKLTEESYKDSTLIMQLLRDNLNLWVTDSA
SQ  GDDNAEEK
//
ID  F1P963;
PN  Oxidized purine nucleoside triphosphate hydrolase;
GN  NUDT1;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P53369}. Nucleus {ECO:0000250|UniProtKB:P53369}. Nucleus membrane {ECO:0000250|UniProtKB:P53369}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P53369}.
DR  UNIPROT: F1P963;
DR  PDB: 5MZF;
DR  Pfam: PF00293;
DR  PROSITE: PS51462;
DR  PROSITE: PS00893;
DE  Function: Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool (PubMed:30304478, PubMed:32144205, PubMed:29281266). Catalyzes the hydrolysis of 2-oxo- dATP (2-hydroxy-dATP) into 2-oxo-dAMP (By similarity). Has also a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo- dATP (PubMed:30304478, PubMed:32144205, PubMed:29281266). Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A (PubMed:30304478, PubMed:32144205, PubMed:29281266). Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA (PubMed:30304478, PubMed:32144205). Through this antimutagenic activity protects cells from oxidative stress (PubMed:30304478, PubMed:32144205, PubMed:29281266). {ECO:0000250|UniProtKB:P36639, ECO:0000269|PubMed:29281266, ECO:0000269|PubMed:30304478, ECO:0000269|PubMed:32144205}.
DE  Reference Proteome: Yes;
GO  GO:0001669;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005759;
GO  GO:0031965;
GO  GO:0106377;
GO  GO:0106378;
GO  GO:0035539;
GO  GO:0008413;
GO  GO:0047693;
GO  GO:0008828;
GO  GO:0016818;
GO  GO:0046872;
GO  GO:0030515;
GO  GO:0042262;
GO  GO:0006152;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGTSRLYTLVLVLQPERVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELREESGLTVDTLHKVGQIMFEFVGEPEL
SQ  MDVHIFCTDSVQGTPVESDEMRPQWFQLDQIPFTDMWPDDSYWFPLLLQKKKFHGYFRFQGPNTILDYTLREVDKL
//
ID  P53368;
PN  Oxidized purine nucleoside triphosphate hydrolase;
GN  Nudt1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P53369}. Nucleus {ECO:0000250|UniProtKB:P53369}. Nucleus membrane {ECO:0000250|UniProtKB:P53369}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P53369}.
DR  UNIPROT: P53368;
DR  UNIPROT: P97795;
DR  UNIPROT: Q542J4;
DR  UNIPROT: Q8VDG0;
DR  PDB: 5MZE;
DR  PDB: 5MZG;
DR  PDB: 6EHH;
DR  Pfam: PF00293;
DR  PROSITE: PS51462;
DR  PROSITE: PS00893;
DE  Function: Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool (PubMed:11572992, PubMed:29281266, PubMed:7592783, PubMed:30304478). Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP (By similarity). Has also a significant hydrolase activity toward 2-oxo- ATP, 8-oxo-dGTP and 8-oxo-dATP (PubMed:11572992, PubMed:29281266, PubMed:7592783, PubMed:30304478). Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A (PubMed:11572992, PubMed:29281266, PubMed:7592783, PubMed:30304478). Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA (PubMed:30304478, PubMed:32144205). Through this antimutagenic activity protects cells from oxidative stress (PubMed:11572992, PubMed:29281266, PubMed:7592783, PubMed:30304478, PubMed:32144205). {ECO:0000250|UniProtKB:P36639, ECO:0000269|PubMed:11572992, ECO:0000269|PubMed:29281266, ECO:0000269|PubMed:30304478, ECO:0000269|PubMed:32144205, ECO:0000269|PubMed:7592783}.
DE  Reference Proteome: Yes;
GO  GO:0001669;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0005759;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0106377;
GO  GO:0106378;
GO  GO:0035539;
GO  GO:0008413;
GO  GO:0047693;
GO  GO:0008828;
GO  GO:0016818;
GO  GO:0046872;
GO  GO:0030515;
GO  GO:0007568;
GO  GO:0042262;
GO  GO:0008584;
GO  GO:0006152;
GO  GO:0046686;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTSRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELLEESGLSVDTLHKVGHISFEFVGSPEL
SQ  MDVHIFSADHVHGTPTESEEMRPQWFQLDQIPFADLWPDDSYWFPLLLQKKKFCGHFKFQDQDTILSYSLREVDSF
//
ID  P53369;
PN  Oxidized purine nucleoside triphosphate hydrolase;
GN  Nudt1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11817101}. Nucleus {ECO:0000269|PubMed:11817101}. Nucleus membrane {ECO:0000269|PubMed:11817101}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:11817101}.
DR  UNIPROT: P53369;
DR  Pfam: PF00293;
DR  PROSITE: PS51462;
DR  PROSITE: PS00893;
DE  Function: Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool (PubMed:7586133). Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP (PubMed:7586133). Has also a significant hydrolase activity toward 2- oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP (By similarity). Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A (PubMed:7586133). Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA (PubMed:30304478, PubMed:32144205). Through this antimutagenic activity protects cells from oxidative stress (PubMed:7586133, PubMed:30304478, PubMed:32144205). {ECO:0000250|UniProtKB:P36639, ECO:0000269|PubMed:30304478, ECO:0000269|PubMed:32144205, ECO:0000269|PubMed:7586133}.
DE  Reference Proteome: Yes;
GO  GO:0001669;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0005759;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0106377;
GO  GO:0106378;
GO  GO:0035539;
GO  GO:0008413;
GO  GO:0047693;
GO  GO:0008828;
GO  GO:0016818;
GO  GO:0046872;
GO  GO:0030515;
GO  GO:0007568;
GO  GO:0042262;
GO  GO:0008584;
GO  GO:0006152;
GO  GO:0046686;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTSRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELLEESGLRVDTLHKVGHISFEFVGSPEL
SQ  MDVHIFSTDHVHGTPTESEEMRPQWFQLDQIPFADMWPDDSYWFPLLLQKKKFCGHFKFHGQDTILSYSLREVDEF
//
ID  Q8GWR1;
PN  Aladin;
GN  AAAS;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8GWR1;
DR  UNIPROT: Q9LER8;
DR  Pfam: PF00400;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9LXJ0; IntAct: EBI-4496544; Score: 0.37
DE  Interaction: Q9SJH7; IntAct: EBI-4496552; Score: 0.37
DE  Interaction: Q8GWK2; IntAct: EBI-25521640; Score: 0.56
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASFPHPGSVTVCEINRDLITAQNLSDERAQETYGKVLGMVFSPVSFDSTPSSLQENEGQENGDKASGESKGLVATLQMK
SQ  VADSLKQILQPTDVTLLSEIDLQGVSWHQGKHIIAFISGANQVTIRDYEDKDEKEPCILTSDSQRNVKALEWRPNGGKSL
SQ  SIACRGGICIWAASYPGNMALVRSGGSALRGSLSRGSGTRWILVDFLRCQNDEQISALSWSPCGRYLASASYDSSSFTIW
SQ  DVSQGAGTPIRRGLGGISMLKWSPTGDYFFAARFDGTFCLWETNTWTSEPWSLSSGSGSVTGAIWDPEGRFILISFSKSS
SQ  TLGSVHFSSKPPSLDAHLLPVELPEIASLTGCEGIEKIAWDASGERLAVSYKGGDENYKGLIAIYDTRRTPIVSASLVGF
SQ  IRGPGENPKALSFSFHDKFKQGPLLSVCWSTGFCCTYPLIFRSHVLP
//
ID  Q9W351;
PN  Aladin;
GN  Aladin;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9NRG9}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26246606}. Note=During mitosis localizes throughout the spindle, is excluded from chromatin, and is enriched on the nuclear envelope remnants that surround the spindle. Present in a ring that surrounds the centrosome in prometaphase and metaphase cells. {ECO:0000269|PubMed:26246606}.
DR  UNIPROT: Q9W351;
DR  Pfam: PF00400;
DE  Function: Involved in mitotic spindle assembly. {ECO:0000269|PubMed:26246606}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8SXP8; IntAct: EBI-201616; Score: 0.00
DE  Interaction: Q95TJ9; IntAct: EBI-468503; Score: 0.00
DE  Interaction: O97143; IntAct: EBI-468506; Score: 0.00
DE  Interaction: P50445; IntAct: EBI-468509; Score: 0.00
DE  Interaction: Q9VTU3; IntAct: EBI-468512; Score: 0.00
DE  Interaction: Q9VEH1; IntAct: EBI-468515; Score: 0.00
DE  Interaction: Q95TP4; IntAct: EBI-470843; Score: 0.00
DE  Interaction: P34082; IntAct: EBI-9928090; Score: 0.35
GO  GO:0005737;
GO  GO:0012505;
GO  GO:0072686;
GO  GO:0005643;
GO  GO:0000922;
GO  GO:0001578;
GO  GO:0090307;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:1902365;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALSNLKQCPPFSTLPDLALRHNHIPELERYPQINLNSELLANPAGQRYYGGQSFVSVNEGVLKRIARSFFNGGFWKTL
SQ  EEARSPETREQAPLIAQAGDLIAQFLGLATGLRILPHTQQLSAERIAQFVETRDWLNSDVRYLAWNQHFFCLAVAGVDDV
SQ  VRIYTKSSSATTATVLKSPSQTQITCMAWRPLCASEIVIGCRQGLCFWEVDSTLHLGRTNAPSEIFKYPNNLPITSMQWN
SQ  KDGTQLATASIGDRSIIIWQPDTGMMQPLKRLGPPGSLLKWSPDNDWLFAATVDRVFRVWNCHQQWTTERWVCGPGGYVQ
SQ  TACWSPCGRFLLFVSSAEPILYRLQFVQQSLLSSSADEKEILPIADLNACSIDANRTLVGGPAQQLAWDPHGNYLVVTFK
SQ  ATNCIAVFRTFIQKFDLQISAAYYLSGETAAEHPSFICFQPLYEDNDRSVLTIAWSSGRIQYYAFD
//
ID  Q9NRG9;
PN  Aladin;
GN  AAAS;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:19782045}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:26246606}. Nucleus envelope {ECO:0000269|PubMed:27754849}. Note=In metaphase cells localizes within the spindle with some accumulation around spindle poles, with the highest concentration between the centrosome and metaphase plate (PubMed:26246606). The localization to the spindle is microtubule- mediated (PubMed:26246606). {ECO:0000269|PubMed:26246606}.
DR  UNIPROT: Q9NRG9;
DR  UNIPROT: Q5JB47;
DR  UNIPROT: Q9NWI6;
DR  UNIPROT: Q9UG19;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 231550;
DR  OMIM: 605378;
DR  DisGeNET: 8086;
DE  Function: Plays a role in the normal development of the peripheral and central nervous system (PubMed:11062474, PubMed:11159947, PubMed:16022285). Required for the correct localization of aurora kinase AURKA and the microtubule minus end-binding protein NUMA1 as well as a subset of AURKA targets which ensures proper spindle formation and timely chromosome alignment (PubMed:26246606). {ECO:0000269|PubMed:11062474, ECO:0000269|PubMed:11159947, ECO:0000269|PubMed:16022285, ECO:0000269|PubMed:26246606}.
DE  Disease: Achalasia-addisonianism-alacrima syndrome (AAAS) [MIM:231550]: An autosomal recessive disorder characterized by adreno-corticotropic hormone (ACTH)-resistant adrenal failure, achalasia of the esophageal cardia and alacrima. The syndrome is associated with variable and progressive neurological impairment involving the central, peripheral, and autonomic nervous system. Other features such as palmoplantar hyperkeratosis, short stature, facial dysmorphy and osteoporosis may also be present. {ECO:0000269|PubMed:11159947}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P0DTD1; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-11888192; Score: 0.37
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q04864; IntAct: EBI-3912907; Score: 0.37
DE  Interaction: Q9Y266; IntAct: EBI-9484795; Score: 0.40
DE  Interaction: Q8IVD9; IntAct: EBI-9484780; Score: 0.40
DE  Interaction: Q16659; IntAct: EBI-12502733; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-28955513; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: O15146; IntAct: EBI-32724025; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000922;
GO  GO:0009566;
GO  GO:0007612;
GO  GO:0001578;
GO  GO:0090307;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0046822;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCSLGLFPPPPPRGQVTLYEHNNELVTGSSYESPPPDFRGQWINLPVLQLTKDPLKTPGRLDHGTRTAFIHHREQVWKRC
SQ  INIWRDVGLFGVLNEIANSEEEVFEWVKTASGWALALCRWASSLHGSLFPHLSLRSEDLIAEFAQVTNWSSCCLRVFAWH
SQ  PHTNKFAVALLDDSVRVYNASSTIVPSLKHRLQRNVASLAWKPLSASVLAVACQSCILIWTLDPTSLSTRPSSGCAQVLS
SQ  HPGHTPVTSLAWAPSGGRLLSASPVDAAIRVWDVSTETCVPLPWFRGGGVTNLLWSPDGSKILATTPSAVFRVWEAQMWT
SQ  CERWPTLSGRCQTGCWSPDGSRLLFTVLGEPLIYSLSFPERCGEGKGCVGGAKSATIVADLSETTIQTPDGEERLGGEAH
SQ  SMVWDPSGERLAVLMKGKPRVQDGKPVILLFRTRNSPVFELLPCGIIQGEPGAQPQLITFHPSFNKGALLSVGWSTGRIA
SQ  HIPLYFVNAQFPRFSPVLGRAQEPPAGGGGSIHDLPLFTETSPTSAPWDPLPGPPPVLPHSPHSHL
//
ID  P58742;
PN  Aladin;
GN  Aaas;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9NRG9}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9NRG9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NRG9}. Note=In metaphase cells localizes within the spindle with some accumulation around spindle poles, with the highest concentration between the centrosome and metaphase plate. The localization to the spindle is microtubule-mediated. {ECO:0000250|UniProtKB:Q9NRG9}.
DR  UNIPROT: P58742;
DR  UNIPROT: Q544M6;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50294;
DE  Function: Plays a role in the normal development of the peripheral and central nervous system. Required for the correct localization of aurora kinase AURKA and the microtubule minus end-binding protein NUMA1 as well as a subset of AURKA targets which ensures proper spindle formation and timely chromosome alignment. {ECO:0000250|UniProtKB:Q9NRG9}.
DE  Reference Proteome: Yes;
DE  Interaction: P45561; IntAct: EBI-22091982; Score: 0.35
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0000922;
GO  GO:0009566;
GO  GO:0007612;
GO  GO:0001578;
GO  GO:0090307;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCSLGLFPPPPPRGQVTLYEHNNELVTGNSYESPPPDFRGQWINLPVLHLTKDPLKAPGRLDHGTRTAFIHHREQVWKRC
SQ  INVWHDVGLFGVLNEIANSEEEVFEWVKTACSWALALCGRASSLHGSLFPHLSLRSEDLIAEFAQVTNWSSCCLRVFAWH
SQ  PHTNKFAVALLDDSIRVYNANSTIVPSLKHRLQRNVAALAWKPLSASVLAVACQSCILIWTLDPTSLSTRPSSGCAQVLS
SQ  HPGHTPVTSLAWAPNGGWLLSASPVDAVILVWDVSTETCVPLPWFRGGGVTNLLWSPDGSKVLATTPSAVFRVWEAQMWT
SQ  CEAWPTLSGRCQTGCWSPDGNRLLFTVLGEALIYSLSFPERCGTGKGHVGGAKSATIVADLSETTIQTPDGEERLGGEAH
SQ  SMVWDPSGERLAVLMKGNPQVQDGNPVILLFRTRNSPVFELLPCGIIQGEPGAQAQLITFHPSFNKGALLSVCWSTGRIT
SQ  HIPLYFVNAQFPRFSPVLGRAQEPPAGGGGSIHEVPLFTETSPTSAPWDPLPGQSSAQPHSPHSHL
//
ID  Q39134;
PN  Amino acid permease 3;
GN  AAP3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:15361541}. Nucleus membrane {ECO:0000269|PubMed:15361541}. Endomembrane system {ECO:0000269|PubMed:15361541}. Note=Not found in vacuole membrane.
DR  UNIPROT: Q39134;
DR  UNIPROT: Q8LE75;
DR  Pfam: PF01490;
DE  Function: Amino acid-proton symporter. Stereospecific transporter with a broad specificity for GABA, tryptophan and both neutral and basic amino acids. High affinity transport of cationic amino acids. {ECO:0000269|PubMed:7608199}.
DE  Reference Proteome: Yes;
DE  Interaction: F4JN35; IntAct: EBI-4491128; Score: 0.37
DE  Interaction: Q94F58; IntAct: EBI-4491136; Score: 0.37
DE  Interaction: Q39222; IntAct: EBI-17000145; Score: 0.37
DE  Interaction: Q84N34; IntAct: EBI-17000085; Score: 0.37
DE  Interaction: Q8LAA6; IntAct: EBI-17000073; Score: 0.37
DE  Interaction: Q9SHI7; IntAct: EBI-17000820; Score: 0.37
DE  Interaction: Q9LSP7; IntAct: EBI-17000808; Score: 0.37
DE  Interaction: Q9FN48; IntAct: EBI-17001567; Score: 0.37
DE  Interaction: Q9FNH6; IntAct: EBI-17001531; Score: 0.37
DE  Interaction: P57752; IntAct: EBI-17001519; Score: 0.37
DE  Interaction: F4I1Z0; IntAct: EBI-17002230; Score: 0.37
DE  Interaction: Q9LPN5; IntAct: EBI-17002206; Score: 0.37
DE  Interaction: Q9C7D7; IntAct: EBI-17002194; Score: 0.37
DE  Interaction: Q8GW19; IntAct: EBI-17001990; Score: 0.37
DE  Interaction: O04265; IntAct: EBI-17002290; Score: 0.37
DE  Interaction: O64852; IntAct: EBI-17002266; Score: 0.37
DE  Interaction: Q8RY98; IntAct: EBI-17002869; Score: 0.37
DE  Interaction: Q94F23; IntAct: EBI-17002821; Score: 0.37
DE  Interaction: Q9FJB4; IntAct: EBI-17002761; Score: 0.37
DE  Interaction: Q93Z82; IntAct: EBI-17002749; Score: 0.37
DE  Interaction: Q9LHA6; IntAct: EBI-17002737; Score: 0.37
DE  Interaction: Q1JPM5; IntAct: EBI-17002353; Score: 0.37
DE  Interaction: Q8L8T2; IntAct: EBI-17002677; Score: 0.37
DE  Interaction: Q9LVU1; IntAct: EBI-17002629; Score: 0.37
DE  Interaction: Q8L9S0; IntAct: EBI-17002605; Score: 0.37
DE  Interaction: C0LGW2; IntAct: EBI-17002581; Score: 0.37
DE  Interaction: Q9SVG8; IntAct: EBI-17002557; Score: 0.37
DE  Interaction: Q9LMN8; IntAct: EBI-17002545; Score: 0.37
DE  Interaction: Q9AST5; IntAct: EBI-17002497; Score: 0.37
DE  Interaction: Q8H129; IntAct: EBI-17002485; Score: 0.37
DE  Interaction: Q944J0; IntAct: EBI-17002449; Score: 0.37
DE  Interaction: Q9C835; IntAct: EBI-17002401; Score: 0.37
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0015171;
GO  GO:0015174;
GO  GO:0015293;
GO  GO:0003333;
GO  GO:0015802;
GO  GO:0006952;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVQNHQTVLAVDMPQTGGSKYLDDDGKNKRTGSVWTASAHIITAVIGSGVLSLAWATAQLGWLAGPVVMLLFSAVTYFTS
SQ  SLLAACYRSGDPISGKRNYTYMDAVRSNLGGVKVTLCGIVQYLNIFGVAIGYTIASAISMMAIKRSNCFHKSGGKDPCHM
SQ  NSNPYMIAFGLVQILFSQIPDFDQLWWLSILAAVMSFTYSSAGLALGIAQVVVNGKVKGSLTGISIGAVTETQKIWRTFQ
SQ  ALGDIAFAYSYSIILIEIQDTVKSPPSEEKTMKKATLVSVSVTTMFYMLCGCMGYAAFGDLSPGNLLTGFGFYNPYWLLD
SQ  IANAAIVIHLIGAYQVYCQPLFAFIEKQASIQFPDSEFIAKDIKIPIPGFKPLRLNVFRLIWRTVFVIITTVISMLLPFF
SQ  NDVVGLLGALGFWPLTVYFPVEMYIAQKKIPRWSTRWVCLQVFSLGCLVVSIAAAAGSIAGVLLDLKSYKPFRSEY
//
ID  Q8NE71;
PN  ATP-binding cassette sub-family F member 1;
GN  ABCF1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19570978}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19570978}. Nucleus envelope {ECO:0000269|PubMed:19570978}.
DR  UNIPROT: Q8NE71;
DR  UNIPROT: A2BF75;
DR  UNIPROT: O14897;
DR  UNIPROT: Q69YP6;
DR  PDB: 5ZXD;
DR  Pfam: PF00005;
DR  PROSITE: PS00211;
DR  PROSITE: PS50893;
DR  OMIM: 603429;
DR  DisGeNET: 23;
DE  Function: Isoform 2 is required for efficient Cap- and IRES-mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis. {ECO:0000269|PubMed:19570978}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13352; IntAct: EBI-734862; Score: 0.00
DE  Interaction: Q96BK5; IntAct: EBI-1069655; Score: 0.00
DE  Interaction: Q9NX58; IntAct: EBI-1069968; Score: 0.00
DE  Interaction: Q9Y478; IntAct: EBI-1078286; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: P51858; IntAct: EBI-4409719; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q96SB4; IntAct: EBI-6660614; Score: 0.44
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: O75807; IntAct: EBI-9976880; Score: 0.35
DE  Interaction: Q16666; IntAct: EBI-9995438; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770028; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: A5YKK6; IntAct: EBI-11005861; Score: 0.35
DE  Interaction: P35550; IntAct: EBI-11044604; Score: 0.35
DE  Interaction: Q17RP2; IntAct: EBI-11051402; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-11069711; Score: 0.35
DE  Interaction: O75530; IntAct: EBI-11070890; Score: 0.35
DE  Interaction: Q15006; IntAct: EBI-11130215; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q68CZ1; IntAct: EBI-12452141; Score: 0.35
DE  Interaction: O60341; IntAct: EBI-16191678; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: Q96JN8; IntAct: EBI-16813376; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: Q6UW60; IntAct: EBI-20905064; Score: 0.40
DE  Interaction: P05204; IntAct: EBI-20907640; Score: 0.40
DE  Interaction: Q93079; IntAct: EBI-20926618; Score: 0.40
DE  Interaction: P0C0S5; IntAct: EBI-20926610; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-20926626; Score: 0.40
DE  Interaction: Q5TID7; IntAct: EBI-20928496; Score: 0.40
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: O96013; IntAct: EBI-26962273; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P17813; IntAct: EBI-22197411; Score: 0.44
DE  Interaction: P16333; IntAct: EBI-25385626; Score: 0.35
DE  Interaction: Q9UER7; IntAct: EBI-25477958; Score: 0.35
DE  Interaction: P0DTC2; IntAct: EBI-26495778; Score: 0.40
DE  Interaction: P0DTC9; IntAct: EBI-26994159; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27111302; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-28938584; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0042788;
GO  GO:0005524;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0008494;
GO  GO:0008135;
GO  GO:0006954;
GO  GO:0045727;
GO  GO:0006412;
GO  GO:0006413;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPKAPKQQPPEPEWIGDGESTSPSDKVVKKGKKDKKIKKTFFEELAVEDKQAGEEEKVLKEKEQQQQQQQQQQKKKRDTR
SQ  KGRRKKDVDDDGEEKELMERLKKLSVPTSDEEDEVPAPKPRGGKKTKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNR
SQ  INKAVSEEQQPALKGKKGKEEKSKGKAKPQNKFAALDNEEEDKEEEIIKEKEPPKQGKEKAKKAEQGSEEEGEGEEEEEE
SQ  GGESKADDPYAHLSKKEKKKLKKQMEYERQVASLKAANAAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFV
SQ  NADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQ
SQ  LEQGDDTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTN
SQ  HLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKE
SQ  LKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEAPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYQGQKPL
SQ  FKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQ
SQ  DARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDAR
SQ  LITETNCQLWVVEEQSVSQIDGDFEDYKREVLEALGEVMVSRPRE
//
ID  Q6P542;
PN  ATP-binding cassette sub-family F member 1;
GN  Abcf1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NE71}.
DR  UNIPROT: Q6P542;
DR  UNIPROT: Q6NV71;
DR  Pfam: PF00005;
DR  Pfam: PF12848;
DR  PROSITE: PS00211;
DR  PROSITE: PS50893;
DE  Function: Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P47713; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9D2E2; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q921K2; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q8BIQ5; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P14869; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q80ZH7; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P34022; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q8BX17; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q8BG79; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q3UHD6; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q3TZX8; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9EQU5; IntAct: EBI-6909752; Score: 0.51
DE  Interaction: Q6P9Q4; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9DCN2; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: O35309; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q3URQ0; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q3UL36; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9JLI8; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9D8C4; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q04690; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: A2BE28; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P62918; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P14148; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P47911; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: O35381; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P06151; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P15092; IntAct: EBI-6909752; Score: 0.46
DE  Interaction: Q99MD9; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P36371; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P30681; IntAct: EBI-6909752; Score: 0.46
DE  Interaction: Q9QZ85; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q3UX10; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q7TPD0; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: D3Z7P3; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9ESU7; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: B1ARD6; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q8CD98; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9D2Y4; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: O35613; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q62036; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9Z2X8; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: O08749; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q61735; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q8CCF0; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q99K01; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9R099; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9Z0E6; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q8BQ30; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P70227; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q3UPN1; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q62293; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P05064; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q9Z1M2; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: P60122; IntAct: EBI-26898362; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0042788;
GO  GO:0005840;
GO  GO:0005524;
GO  GO:0043022;
GO  GO:0008494;
GO  GO:0045727;
GO  GO:0006413;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPKGPKQQPPEPEWIGDGEGTSPADKVVKKGKKDKKTKKTFFEELAVEDKQAGEEEKLQKEKEQQQQQQQQKKKRDTRKG
SQ  RRKKDVDDDSDERVLMERLKQLSVPASDEEDEVPAPIPRGRKKAKGGNVFEALIQDDSEEEEEEEENRVLKPAKPEKNRI
SQ  NKAVAEEPPGLRSKKGKEEKSKGKAKSKPAAADSEGEEEEEDTAKEKEPPQQGKDRDKKEAEQGSGEEKEEKEGDLKAND
SQ  PYANLSKKEKKKLKKQMDYERQVESLKAANAAENDFSVSQAEVSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVA
SQ  GRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLRLLEEERRLQGQLEQGDDTA
SQ  AEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVI
SQ  WLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKST
SQ  KQAEKQTKEVLTRKQQKCRRKNQDEESQEPPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKPLFKNLDFGI
SQ  DMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQLHMEETPTEYLQRSFNLPYQDARKCLGR
SQ  FGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKGAVIVVSHDARLITETNCQ
SQ  LWVVEEQGVSQIDGDFDDYKREVLEALGEVMVNRPRD
//
ID  Q7YR37;
PN  ATP-binding cassette sub-family F member 1;
GN  ABCF1;
OS  9598;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NE71}.
DR  UNIPROT: Q7YR37;
DR  UNIPROT: Q1XI20;
DR  Pfam: PF00005;
DR  PROSITE: PS00211;
DR  PROSITE: PS50893;
DE  Function: Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0042788;
GO  GO:0005524;
GO  GO:0043022;
GO  GO:0008494;
GO  GO:0045727;
GO  GO:0006413;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPKAPKQQPPEPEWIGDGESTSPSDKVVKKGKKDKKIKKTFFEELAVEDKQAGEEEKVLKEKEQQQQQQQVQQKKKRDTR
SQ  KGRRKKDVDDDGEEKELMERLKKLSVPASDEEDEVPAPKPRGGKKTKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNR
SQ  INKAVSEEQQPALKGKKGKEEKSKGKAKPQNKFAALDNEEEDKEEEIIKEKEPPKQGKEKAKKAEQMEYERQVASLKAAN
SQ  AAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVASRRYGLVGPNGKGKTTLLKHIANRALSIPP
SQ  NIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQGDDTAAERLEKVYEELRATGAAAAEAKARRILAGL
SQ  GFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDI
SQ  IHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEA
SQ  PELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPT
SQ  HGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELAC
SQ  REPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFEDYKREVLEALGEV
SQ  MVSRPRE
//
ID  Q767L0;
PN  ATP-binding cassette sub-family F member 1;
GN  ABCF1;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NE71}.
DR  UNIPROT: Q767L0;
DR  Pfam: PF00005;
DR  PROSITE: PS00211;
DR  PROSITE: PS50893;
DE  Function: Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0042788;
GO  GO:0005524;
GO  GO:0043022;
GO  GO:0008494;
GO  GO:0045727;
GO  GO:0006413;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPKGPKQQPPEPEWIGDGESTSPTDKVVKKGKKDKKTKKTFFEELAVEDRQAGEEEKVLKEKEQQQQHQQQQQKKKRDTR
SQ  KGRRKKDVDDDDGEEKELMERLKKLSVPASDEEEEAPAPVPRGGKKNKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKN
SQ  RINKAVSQEQQPGPKGRKGKEEKSKGKAKPQNKFAALDDEEEQDEEEIKEKEPPKQGKEKAKKAEQMEYERQVASLKAAN
SQ  AAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPP
SQ  NIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQGDDTAADRLEKVYEELRATGAAAAEAKARRILAGL
SQ  GFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDI
SQ  IHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEA
SQ  PELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPT
SQ  RGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELAC
SQ  REPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFDDYKREVLEALGEV
SQ  MVSRPRE
//
ID  Q6MG08;
PN  ATP-binding cassette sub-family F member 1;
GN  Abcf1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NE71}.
DR  UNIPROT: Q6MG08;
DR  UNIPROT: Q9ERQ2;
DR  Pfam: PF00005;
DR  Pfam: PF12848;
DR  PROSITE: PS00211;
DR  PROSITE: PS50893;
DE  Function: Required for efficient Cap- and IRES-mediated mRNA translation initiation. Not involved in the ribosome biogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:10931828}.
DE  Reference Proteome: Yes;
DE  Interaction: P11362; IntAct: EBI-22243924; Score: 0.35
DE  Interaction: P08069; IntAct: EBI-22245613; Score: 0.35
DE  Interaction: O75096; IntAct: EBI-22258804; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0042788;
GO  GO:0005840;
GO  GO:0005524;
GO  GO:0043022;
GO  GO:0008494;
GO  GO:0045727;
GO  GO:0006412;
GO  GO:0006413;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPKGPKQQPPEPEWIGDGEGTSPADKVVKKGKKDKKTKKTFFEELAVEDKQAGEEEKLQKEKEQQQQQQQQKKKRDTRKG
SQ  RRKKDVDDDDDGDERVLMERLKQLSVPASDEEDEVPVPVPRGRKKAKGGNVFEALIQDESEEEKEEEEEKPVLKPAKPEK
SQ  NRINKAVAEEPPGLRNKKGKEEKSKGKAKNKPSATDSEGEDDEDMTKEKEPPRPGKDKDKKGAEQGSEEEKEEKEGEVKA
SQ  NDPYAHLSKKEKKKLKKQMDYERQVESLKAANAAENDFSVSQAEVSSRQAMLENASDIKLEKFSISAHGKELFVNADLYI
SQ  VAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLRLLEEEKRLQGQLEQGDD
SQ  TAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA
SQ  VIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGK
SQ  STKQAEKQTKEVLTRKQQKCRRKNQDEESQDPPELLKRPREYTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKPLFKNLDF
SQ  GIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQLHMEETPTEYLQRGFNLPYQDARKCL
SQ  GRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETN
SQ  CQLWVVEEQSVSQIDGDFDDYKREVLEALGEVMVNRPRD
//
ID  P00519;
PN  Tyrosine-protein kinase ABL1;
GN  ABL1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm depending on environmental signals. Sequestered into the cytoplasm through interaction with 14-3-3 proteins. Localizes to mitochondria in response to oxidative stress (By similarity). {ECO:0000250}. [Isoform IB]: Nucleus membrane; Lipid-anchor. Note=The myristoylated c-ABL protein is reported to be nuclear.
DR  UNIPROT: P00519;
DR  UNIPROT: A3KFJ3;
DR  UNIPROT: Q13869;
DR  UNIPROT: Q13870;
DR  UNIPROT: Q16133;
DR  UNIPROT: Q17R61;
DR  UNIPROT: Q45F09;
DR  PDB: 1AB2;
DR  PDB: 1AWO;
DR  PDB: 1BBZ;
DR  PDB: 1JU5;
DR  PDB: 1OPL;
DR  PDB: 1ZZP;
DR  PDB: 2ABL;
DR  PDB: 2E2B;
DR  PDB: 2F4J;
DR  PDB: 2FO0;
DR  PDB: 2G1T;
DR  PDB: 2G2F;
DR  PDB: 2G2H;
DR  PDB: 2G2I;
DR  PDB: 2GQG;
DR  PDB: 2HIW;
DR  PDB: 2HYY;
DR  PDB: 2HZ0;
DR  PDB: 2HZ4;
DR  PDB: 2HZI;
DR  PDB: 2O88;
DR  PDB: 2V7A;
DR  PDB: 3CS9;
DR  PDB: 3EG0;
DR  PDB: 3EG1;
DR  PDB: 3EG2;
DR  PDB: 3EG3;
DR  PDB: 3EGU;
DR  PDB: 3K2M;
DR  PDB: 3PYY;
DR  PDB: 3QRI;
DR  PDB: 3QRJ;
DR  PDB: 3QRK;
DR  PDB: 3T04;
DR  PDB: 3UE4;
DR  PDB: 3UYO;
DR  PDB: 4J9B;
DR  PDB: 4J9C;
DR  PDB: 4J9D;
DR  PDB: 4J9E;
DR  PDB: 4J9F;
DR  PDB: 4J9G;
DR  PDB: 4J9H;
DR  PDB: 4J9I;
DR  PDB: 4JJB;
DR  PDB: 4JJC;
DR  PDB: 4JJD;
DR  PDB: 4TWP;
DR  PDB: 4WA9;
DR  PDB: 4XEY;
DR  PDB: 4YC8;
DR  PDB: 4ZOG;
DR  PDB: 5DC0;
DR  PDB: 5DC4;
DR  PDB: 5DC9;
DR  PDB: 5HU9;
DR  PDB: 5MO4;
DR  PDB: 5NP2;
DR  PDB: 5OAZ;
DR  PDB: 6AMV;
DR  PDB: 6AMW;
DR  PDB: 6BL8;
DR  PDB: 6NPE;
DR  PDB: 6NPU;
DR  PDB: 6NPV;
DR  PDB: 6XR6;
DR  PDB: 6XR7;
DR  PDB: 6XRG;
DR  PDB: 7CC2;
DR  PDB: 7DT2;
DR  Pfam: PF08919;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DR  OMIM: 189980;
DR  OMIM: 608232;
DR  OMIM: 617602;
DR  DisGeNET: 25;
DE  Function: Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9 (PubMed:22810897). Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (PubMed:28428613). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage- induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner (By similarity). Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (By similarity). Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (By similarity). {ECO:0000250|UniProtKB:P00520, ECO:0000269|PubMed:10391250, ECO:0000269|PubMed:11971963, ECO:0000269|PubMed:12379650, ECO:0000269|PubMed:12531427, ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:15556646, ECO:0000269|PubMed:15657060, ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16424036, ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:16943190, ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:17623672, ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:18945674, ECO:0000269|PubMed:19891780, ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:20417104, ECO:0000269|PubMed:22810897, ECO:0000269|PubMed:28428613, ECO:0000269|PubMed:9037071, ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9461559}.
DE  Disease: Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal myeloproliferative disorder of a pluripotent stem cell with a specific cytogenetic abnormality, the Philadelphia chromosome (Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid, and sometimes T- lymphoid cells, but not marrow fibroblasts. Note=The gene represented in this entry is involved in disease pathogenesis. Note=A chromosomal aberration involving ABL1 has been found in patients with chronic myeloid leukemia. Translocation t(9;22)(q34;q11) with BCR. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL). {ECO:0000269|PubMed:3021337}. Note=A chromosomal aberration involving ABL1 is found in a form of acute lymphoblastic leukemia (PubMed:15361874). Translocation t(9;9)(q34;q34) with NUP214 (PubMed:15361874). {ECO:0000269|PubMed:15361874}. Congenital heart defects and skeletal malformations syndrome (CHDSKM) [MIM:617602]: An autosomal dominant disorder characterized by congenital heart disease with atrial and ventricular septal defects, variable skeletal abnormalities, and failure to thrive. Skeletal defects include pectus excavatum, scoliosis, and finger contractures. Some patient exhibit joint laxity. {ECO:0000269|PubMed:28288113}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q92558; IntAct: EBI-7380789; Score: 0.57
DE  Interaction: P08631; IntAct: EBI-7296396; Score: 0.40
DE  Interaction: P05067; IntAct: EBI-7810061; Score: 0.35
DE  Interaction: Q9XSK8; IntAct: EBI-7047340; Score: 0.31
DE  Interaction: Q8CBW3; IntAct: EBI-375573; Score: 0.40
DE  Interaction: Q8IZP0; IntAct: EBI-375643; Score: 0.90
DE  Interaction: P22681; IntAct: EBI-7392045; Score: 0.31
DE  Interaction: P62258; IntAct: EBI-593829; Score: 0.53
DE  Interaction: P31946; IntAct: EBI-593829; Score: 0.53
DE  Interaction: P63104; IntAct: EBI-593829; Score: 0.62
DE  Interaction: P31947; IntAct: EBI-593829; Score: 0.50
DE  Interaction: P61981; IntAct: EBI-593829; Score: 0.74
DE  Interaction: Q04917; IntAct: EBI-593829; Score: 0.64
DE  Interaction: Q9BX66; IntAct: EBI-624110; Score: 0.52
DE  Interaction: Q15303; IntAct: EBI-7872165; Score: 0.44
DE  Interaction: P04626; IntAct: EBI-7881352; Score: 0.44
DE  Interaction: P00533; IntAct: EBI-7887814; Score: 0.69
DE  Interaction: P21860; IntAct: EBI-7896542; Score: 0.44
DE  Interaction: Q05655; IntAct: EBI-8488876; Score: 0.40
DE  Interaction: Q07817; IntAct: EBI-8488890; Score: 0.40
DE  Interaction: P78524; IntAct: EBI-962642; Score: 0.40
DE  Interaction: Q09472; IntAct: EBI-8504608; Score: 0.27
DE  Interaction: O60504; IntAct: EBI-8565293; Score: 0.54
DE  Interaction: P15941; IntAct: EBI-8597680; Score: 0.66
DE  Interaction: Q13315; IntAct: EBI-1005980; Score: 0.70
DE  Interaction: P54274; IntAct: EBI-1005991; Score: 0.40
DE  Interaction: Q13671; IntAct: EBI-1102754; Score: 0.61
DE  Interaction: O15350; IntAct: EBI-7807114; Score: 0.40
DE  Interaction: Q9NYB9; IntAct: EBI-7088267; Score: 0.52
DE  Interaction: Q63767; IntAct: EBI-1176858; Score: 0.44
DE  Interaction: P12931; IntAct: EBI-7286298; Score: 0.59
DE  Interaction: P35222; IntAct: EBI-7286271; Score: 0.54
DE  Interaction: O43900; IntAct: EBI-1957060; Score: 0.40
DE  Interaction: Q9HCM9; IntAct: EBI-1957076; Score: 0.40
DE  Interaction: Q9Y697; IntAct: EBI-1957120; Score: 0.40
DE  Interaction: Q92918; IntAct: EBI-1957132; Score: 0.57
DE  Interaction: P78345; IntAct: EBI-1957144; Score: 0.40
DE  Interaction: Q8NFP9; IntAct: EBI-1957156; Score: 0.40
DE  Interaction: O43390; IntAct: EBI-1957168; Score: 0.40
DE  Interaction: O00254; IntAct: EBI-1957180; Score: 0.40
DE  Interaction: Q9Y5Y3; IntAct: EBI-1957192; Score: 0.40
DE  Interaction: Q9UL51; IntAct: EBI-1957204; Score: 0.40
DE  Interaction: P78357; IntAct: EBI-1957216; Score: 0.40
DE  Interaction: Q96NS5; IntAct: EBI-1957228; Score: 0.40
DE  Interaction: Q07890; IntAct: EBI-1957240; Score: 0.40
DE  Interaction: O94856; IntAct: EBI-1957252; Score: 0.40
DE  Interaction: Q9NZV5; IntAct: EBI-1957264; Score: 0.40
DE  Interaction: P49450; IntAct: EBI-1957276; Score: 0.40
DE  Interaction: Q92874; IntAct: EBI-1957288; Score: 0.40
DE  Interaction: Q7Z408; IntAct: EBI-1957319; Score: 0.40
DE  Interaction: P98161; IntAct: EBI-1957300; Score: 0.40
DE  Interaction: P43699; IntAct: EBI-1957331; Score: 0.40
DE  Interaction: P50570; IntAct: EBI-1957343; Score: 0.40
DE  Interaction: Q96GP6; IntAct: EBI-1957367; Score: 0.40
DE  Interaction: Q14315; IntAct: EBI-1957355; Score: 0.40
DE  Interaction: P31273; IntAct: EBI-1957391; Score: 0.40
DE  Interaction: Q92664; IntAct: EBI-1957379; Score: 0.40
DE  Interaction: Q9UJV9; IntAct: EBI-1957403; Score: 0.40
DE  Interaction: O43493; IntAct: EBI-1957415; Score: 0.40
DE  Interaction: Q15427; IntAct: EBI-1957427; Score: 0.40
DE  Interaction: Q12979; IntAct: EBI-1957439; Score: 0.40
DE  Interaction: Q13023; IntAct: EBI-1957451; Score: 0.40
DE  Interaction: P15586; IntAct: EBI-1957463; Score: 0.40
DE  Interaction: P23760; IntAct: EBI-1957487; Score: 0.40
DE  Interaction: Q9UIF9; IntAct: EBI-1957475; Score: 0.40
DE  Interaction: Q9UM47; IntAct: EBI-1957499; Score: 0.40
DE  Interaction: Q13415; IntAct: EBI-1957511; Score: 0.40
DE  Interaction: P06865; IntAct: EBI-1957523; Score: 0.40
DE  Interaction: Q9H2X0; IntAct: EBI-1957535; Score: 0.40
DE  Interaction: P51587; IntAct: EBI-1957563; Score: 0.40
DE  Interaction: Q9UMN6; IntAct: EBI-1957551; Score: 0.40
DE  Interaction: Q12947; IntAct: EBI-1957575; Score: 0.40
DE  Interaction: Q9BYB0; IntAct: EBI-1957587; Score: 0.40
DE  Interaction: Q9UBS5; IntAct: EBI-1957599; Score: 0.40
DE  Interaction: Q8IZD9; IntAct: EBI-1957611; Score: 0.40
DE  Interaction: P28340; IntAct: EBI-1957623; Score: 0.40
DE  Interaction: Q9NYQ7; IntAct: EBI-1957635; Score: 0.40
DE  Interaction: P78329; IntAct: EBI-1957659; Score: 0.40
DE  Interaction: O43708; IntAct: EBI-1957647; Score: 0.40
DE  Interaction: Q9H5I1; IntAct: EBI-1957671; Score: 0.40
DE  Interaction: P46013; IntAct: EBI-1957683; Score: 0.40
DE  Interaction: O76039; IntAct: EBI-1957707; Score: 0.40
DE  Interaction: Q14008; IntAct: EBI-1957719; Score: 0.40
DE  Interaction: Q13087; IntAct: EBI-1957755; Score: 0.40
DE  Interaction: O14513; IntAct: EBI-1957743; Score: 0.40
DE  Interaction: O95886; IntAct: EBI-1957767; Score: 0.40
DE  Interaction: Q9Y5X2; IntAct: EBI-1957793; Score: 0.40
DE  Interaction: P42566; IntAct: EBI-1957805; Score: 0.40
DE  Interaction: Q96RL7; IntAct: EBI-1957817; Score: 0.40
DE  Interaction: Q9UMY4; IntAct: EBI-1957829; Score: 0.40
DE  Interaction: Q9C0E4; IntAct: EBI-1957853; Score: 0.40
DE  Interaction: Q15036; IntAct: EBI-1957841; Score: 0.40
DE  Interaction: P34820; IntAct: EBI-1957877; Score: 0.40
DE  Interaction: P30260; IntAct: EBI-1957865; Score: 0.40
DE  Interaction: O75751; IntAct: EBI-1957889; Score: 0.40
DE  Interaction: Q86UR5; IntAct: EBI-1957906; Score: 0.40
DE  Interaction: Q9NZQ3; IntAct: EBI-1957930; Score: 0.40
DE  Interaction: P26992; IntAct: EBI-1957918; Score: 0.40
DE  Interaction: P50851; IntAct: EBI-1957942; Score: 0.40
DE  Interaction: O76081; IntAct: EBI-1957956; Score: 0.40
DE  Interaction: Q92988; IntAct: EBI-1957968; Score: 0.40
DE  Interaction: Q96PC5; IntAct: EBI-1957980; Score: 0.40
DE  Interaction: Q9BQ89; IntAct: EBI-1958016; Score: 0.40
DE  Interaction: P20810; IntAct: EBI-1957992; Score: 0.40
DE  Interaction: Q9H1R2; IntAct: EBI-1958004; Score: 0.40
DE  Interaction: P02765; IntAct: EBI-1958028; Score: 0.40
DE  Interaction: Q9Y3S1; IntAct: EBI-1958040; Score: 0.40
DE  Interaction: Q13905; IntAct: EBI-1958052; Score: 0.66
DE  Interaction: Q9UQ16; IntAct: EBI-1958064; Score: 0.40
DE  Interaction: Q9Y5K6; IntAct: EBI-1958076; Score: 0.40
DE  Interaction: O15255; IntAct: EBI-1958088; Score: 0.40
DE  Interaction: Q8TB24; IntAct: EBI-1958100; Score: 0.40
DE  Interaction: O95157; IntAct: EBI-1958112; Score: 0.40
DE  Interaction: O43281; IntAct: EBI-1958124; Score: 0.40
DE  Interaction: O15085; IntAct: EBI-1958148; Score: 0.40
DE  Interaction: P08047; IntAct: EBI-1958160; Score: 0.40
DE  Interaction: P98164; IntAct: EBI-1958172; Score: 0.40
DE  Interaction: Q86SG6; IntAct: EBI-1958184; Score: 0.40
DE  Interaction: Q9H0X9; IntAct: EBI-1958196; Score: 0.40
DE  Interaction: Q9NQC3; IntAct: EBI-1958208; Score: 0.40
DE  Interaction: O60244; IntAct: EBI-1958225; Score: 0.40
DE  Interaction: Q9UK85; IntAct: EBI-1958237; Score: 0.40
DE  Interaction: Q9BXM0; IntAct: EBI-1958249; Score: 0.40
DE  Interaction: O43918; IntAct: EBI-1958261; Score: 0.40
DE  Interaction: Q96AC6; IntAct: EBI-1958273; Score: 0.40
DE  Interaction: Q9HCQ7; IntAct: EBI-1958285; Score: 0.40
DE  Interaction: O15056; IntAct: EBI-1958297; Score: 0.40
DE  Interaction: P32239; IntAct: EBI-1958309; Score: 0.40
DE  Interaction: Q15027; IntAct: EBI-1958333; Score: 0.40
DE  Interaction: O14490; IntAct: EBI-1958369; Score: 0.40
DE  Interaction: Q8WX92; IntAct: EBI-1958345; Score: 0.40
DE  Interaction: Q9NUR3; IntAct: EBI-1958357; Score: 0.40
DE  Interaction: P13671; IntAct: EBI-1958381; Score: 0.40
DE  Interaction: P42167; IntAct: EBI-1958393; Score: 0.40
DE  Interaction: Q99572; IntAct: EBI-1958405; Score: 0.40
DE  Interaction: O15117; IntAct: EBI-1958417; Score: 0.40
DE  Interaction: Q14767; IntAct: EBI-1958429; Score: 0.40
DE  Interaction: Q9NQ76; IntAct: EBI-1958441; Score: 0.40
DE  Interaction: Q9Y2J2; IntAct: EBI-1958453; Score: 0.40
DE  Interaction: O60493; IntAct: EBI-1958465; Score: 0.40
DE  Interaction: Q9UHL9; IntAct: EBI-1958477; Score: 0.40
DE  Interaction: Q05193; IntAct: EBI-1958489; Score: 0.40
DE  Interaction: Q9ULH1; IntAct: EBI-1958501; Score: 0.40
DE  Interaction: Q9UN86; IntAct: EBI-1958513; Score: 0.40
DE  Interaction: P49916; IntAct: EBI-1958525; Score: 0.40
DE  Interaction: Q9P1A6; IntAct: EBI-1958537; Score: 0.40
DE  Interaction: Q9Y2H0; IntAct: EBI-1958551; Score: 0.40
DE  Interaction: Q9BZM3; IntAct: EBI-1958563; Score: 0.40
DE  Interaction: Q9UJT2; IntAct: EBI-1958575; Score: 0.40
DE  Interaction: P12018; IntAct: EBI-1958587; Score: 0.40
DE  Interaction: Q9ULD4; IntAct: EBI-1958599; Score: 0.40
DE  Interaction: Q9Y3Q4; IntAct: EBI-1958635; Score: 0.40
DE  Interaction: Q9NRJ4; IntAct: EBI-1958611; Score: 0.40
DE  Interaction: O60721; IntAct: EBI-1958623; Score: 0.40
DE  Interaction: O75326; IntAct: EBI-1958647; Score: 0.40
DE  Interaction: Q08209; IntAct: EBI-1958680; Score: 0.40
DE  Interaction: Q14999; IntAct: EBI-1958704; Score: 0.40
DE  Interaction: Q9BWW9; IntAct: EBI-1958716; Score: 0.40
DE  Interaction: Q8TAS1; IntAct: EBI-1958728; Score: 0.40
DE  Interaction: P21333; IntAct: EBI-1958740; Score: 0.40
DE  Interaction: P29074; IntAct: EBI-1958764; Score: 0.40
DE  Interaction: Q9UN72; IntAct: EBI-1958776; Score: 0.40
DE  Interaction: P52803; IntAct: EBI-1958788; Score: 0.40
DE  Interaction: P20774; IntAct: EBI-1958800; Score: 0.40
DE  Interaction: Q99259; IntAct: EBI-1958816; Score: 0.40
DE  Interaction: P46108; IntAct: EBI-1959666; Score: 0.67
DE  Interaction: P06241; IntAct: EBI-1961835; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-1963179; Score: 0.40
DE  Interaction: P16333; IntAct: EBI-1967005; Score: 0.40
DE  Interaction: P27986; IntAct: EBI-1969653; Score: 0.40
DE  Interaction: P19174; IntAct: EBI-1970973; Score: 0.40
DE  Interaction: P18031; IntAct: EBI-8174353; Score: 0.44
DE  Interaction: Q06609; IntAct: EBI-6995587; Score: 0.40
DE  Interaction: Q15464; IntAct: EBI-7100971; Score: 0.52
DE  Interaction: O43196; IntAct: EBI-7989580; Score: 0.82
DE  Interaction: O15457; IntAct: EBI-7989665; Score: 0.37
DE  Interaction: P46109; IntAct: EBI-8046579; Score: 0.67
DE  Interaction: Q06830; IntAct: EBI-7319754; Score: 0.37
DE  Interaction: P38398; IntAct: EBI-7319796; Score: 0.37
DE  Interaction: Q9Y3L3; IntAct: EBI-7319868; Score: 0.40
DE  Interaction: P70218; IntAct: EBI-8670837; Score: 0.37
DE  Interaction: Q13444; IntAct: EBI-8061278; Score: 0.40
DE  Interaction: Q71SY5; IntAct: EBI-8595983; Score: 0.44
DE  Interaction: O35158; IntAct: EBI-7016759; Score: 0.58
DE  Interaction: Q4KMG0; IntAct: EBI-7016887; Score: 0.52
DE  Interaction: P05107; IntAct: EBI-8576224; Score: 0.52
DE  Interaction: Q9Y4G6; IntAct: EBI-8576260; Score: 0.60
DE  Interaction: P15498; IntAct: EBI-8576308; Score: 0.60
DE  Interaction: P04370; IntAct: EBI-7727798; Score: 0.40
DE  Interaction: Q7Z434; IntAct: EBI-7599276; Score: 0.59
DE  Interaction: P11387; IntAct: EBI-7328831; Score: 0.60
DE  Interaction: P35326; IntAct: EBI-7743121; Score: 0.44
DE  Interaction: Q9QUM7; IntAct: EBI-7004732; Score: 0.37
DE  Interaction: P55194; IntAct: EBI-7094170; Score: 0.44
DE  Interaction: Q64010; IntAct: EBI-2642542; Score: 0.35
DE  Interaction: P97465; IntAct: EBI-2642676; Score: 0.35
DE  Interaction: Q38SD2; IntAct: EBI-2906661; Score: 0.59
DE  Interaction: Q04929; IntAct: EBI-5278171; Score: 0.44
DE  Interaction: O95758; IntAct: EBI-7850130; Score: 0.35
DE  Interaction: P78362; IntAct: EBI-6657338; Score: 0.44
DE  Interaction: P08238; IntAct: EBI-6423900; Score: 0.40
DE  Interaction: Q99497; IntAct: EBI-8544196; Score: 0.44
DE  Interaction: P37840; IntAct: EBI-27101585; Score: 0.60
DE  Interaction: O55042; IntAct: EBI-9212687; Score: 0.27
DE  Interaction: P10275; IntAct: EBI-9451938; Score: 0.44
DE  Interaction: P10721; IntAct: EBI-9467046; Score: 0.44
DE  Interaction: P14618; IntAct: EBI-9354876; Score: 0.44
DE  Interaction: Q5S007; IntAct: EBI-9659734; Score: 0.44
DE  Interaction: Q15637; IntAct: EBI-11299755; Score: 0.00
DE  Interaction: P53999; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: P26641; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: Q9Y295; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: Q01844; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: P63220; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: Q12906; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: P52272; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: P35637; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: Q9BY44; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: P05386; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: P61604; IntAct: EBI-10101341; Score: 0.35
DE  Interaction: P17844; IntAct: EBI-10101379; Score: 0.35
DE  Interaction: P12956; IntAct: EBI-10101379; Score: 0.35
DE  Interaction: Q96AG4; IntAct: EBI-10101379; Score: 0.35
DE  Interaction: Q07065; IntAct: EBI-10101379; Score: 0.35
DE  Interaction: Q6VGS8; IntAct: EBI-11733617; Score: 0.35
DE  Interaction: Q8BTZ4; IntAct: EBI-11003821; Score: 0.35
DE  Interaction: Q8BL66; IntAct: EBI-11027295; Score: 0.35
DE  Interaction: Q1H9T6; IntAct: EBI-11104278; Score: 0.35
DE  Interaction: Q15323; IntAct: EBI-24307132; Score: 0.56
DE  Interaction: P48165; IntAct: EBI-24796696; Score: 0.56
DE  Interaction: Q03135; IntAct: EBI-15875070; Score: 0.44
DE  Interaction: P42229; IntAct: EBI-15965981; Score: 0.44
DE  Interaction: P53355; IntAct: EBI-20588441; Score: 0.44
DE  Interaction: P36888; IntAct: EBI-20639282; Score: 0.44
DE  Interaction: Q03468; IntAct: EBI-21017040; Score: 0.66
DE  Interaction: O14672; IntAct: EBI-21223666; Score: 0.54
DE  Interaction: Q9BY11; IntAct: EBI-21376479; Score: 0.00
DE  Interaction: P51692; IntAct: EBI-25432371; Score: 0.56
DE  Interaction: P60006; IntAct: EBI-27039580; Score: 0.37
DE  Interaction: O14641; IntAct: EBI-27039584; Score: 0.37
DE  Interaction: Q9H4M7; IntAct: EBI-27039588; Score: 0.37
DE  Interaction: Q8IYX8; IntAct: EBI-27039592; Score: 0.37
DE  Interaction: Q8TAP6; IntAct: EBI-27039596; Score: 0.37
DE  Interaction: O14595; IntAct: EBI-27039600; Score: 0.37
DE  Interaction: O94818; IntAct: EBI-27039604; Score: 0.37
DE  Interaction: P46531; IntAct: EBI-27039608; Score: 0.37
DE  Interaction: P56279; IntAct: EBI-27039612; Score: 0.37
DE  Interaction: Q96GJ1; IntAct: EBI-27039616; Score: 0.37
DE  Interaction: P42684; IntAct: EBI-27039620; Score: 0.37
DE  Interaction: Q13619; IntAct: EBI-30863570; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-30863806; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-32719716; Score: 0.35
GO  GO:0015629;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005783;
GO  GO:0030426;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0032991;
GO  GO:0001726;
GO  GO:0051015;
GO  GO:0003785;
GO  GO:0005524;
GO  GO:0000405;
GO  GO:0070097;
GO  GO:0003677;
GO  GO:0046875;
GO  GO:0000400;
GO  GO:0016301;
GO  GO:0000287;
GO  GO:0030145;
GO  GO:0051019;
GO  GO:0038191;
GO  GO:0004515;
GO  GO:0004715;
GO  GO:0001784;
GO  GO:0070064;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0005080;
GO  GO:0043621;
GO  GO:0004713;
GO  GO:1990837;
GO  GO:0042169;
GO  GO:0017124;
GO  GO:0019905;
GO  GO:0003713;
GO  GO:0030036;
GO  GO:0030041;
GO  GO:0050798;
GO  GO:1990051;
GO  GO:0046632;
GO  GO:0008306;
GO  GO:0006914;
GO  GO:0002322;
GO  GO:0050853;
GO  GO:0001922;
GO  GO:0060020;
GO  GO:0030509;
GO  GO:0060038;
GO  GO:0098609;
GO  GO:0006974;
GO  GO:1903351;
GO  GO:0070301;
GO  GO:0071222;
GO  GO:0034599;
GO  GO:0071560;
GO  GO:0090398;
GO  GO:0021587;
GO  GO:1904157;
GO  GO:0071103;
GO  GO:0006975;
GO  GO:0006897;
GO  GO:0043542;
GO  GO:0007173;
GO  GO:0070371;
GO  GO:0051649;
GO  GO:0038096;
GO  GO:0007249;
GO  GO:0007229;
GO  GO:0008630;
GO  GO:0030035;
GO  GO:0006298;
GO  GO:0051882;
GO  GO:0000278;
GO  GO:0051450;
GO  GO:0030514;
GO  GO:0022408;
GO  GO:2000773;
GO  GO:2000352;
GO  GO:0070373;
GO  GO:0043124;
GO  GO:1900272;
GO  GO:0045930;
GO  GO:1900275;
GO  GO:0071901;
GO  GO:0051444;
GO  GO:0001843;
GO  GO:0060563;
GO  GO:0050885;
GO  GO:0070997;
GO  GO:0030182;
GO  GO:0038189;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0035791;
GO  GO:1903210;
GO  GO:2000251;
GO  GO:1904531;
GO  GO:0043065;
GO  GO:1905555;
GO  GO:0090050;
GO  GO:0007204;
GO  GO:1900006;
GO  GO:0010595;
GO  GO:0070374;
GO  GO:1903905;
GO  GO:1903055;
GO  GO:0048146;
GO  GO:0051894;
GO  GO:1901300;
GO  GO:0043123;
GO  GO:0032729;
GO  GO:0032743;
GO  GO:1904528;
GO  GO:0045931;
GO  GO:0043525;
GO  GO:0033690;
GO  GO:0051353;
GO  GO:0050731;
GO  GO:0001934;
GO  GO:0051281;
GO  GO:0051496;
GO  GO:1900026;
GO  GO:2000406;
GO  GO:0045944;
GO  GO:0045907;
GO  GO:2000096;
GO  GO:0009791;
GO  GO:0046777;
GO  GO:1904518;
GO  GO:0036211;
GO  GO:0006468;
GO  GO:0032956;
GO  GO:2000249;
GO  GO:0042981;
GO  GO:0010506;
GO  GO:0030516;
GO  GO:0032489;
GO  GO:0030155;
GO  GO:0051726;
GO  GO:2000145;
GO  GO:0006355;
GO  GO:0030100;
GO  GO:1902036;
GO  GO:0031113;
GO  GO:1905244;
GO  GO:2001020;
GO  GO:0045580;
GO  GO:0034976;
GO  GO:0071871;
GO  GO:0006979;
GO  GO:0009410;
GO  GO:0042770;
GO  GO:0048536;
GO  GO:0034446;
GO  GO:0050852;
GO  GO:0048538;
GO  GO:0002333;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis;
SQ  MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTL
SQ  SITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQ
SQ  RSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERT
SQ  DITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTY
SQ  GNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAK
SQ  FPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNP
SQ  SDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESD
SQ  PLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRD
SQ  ISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSAS
SQ  CVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKD
SQ  IMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKH
SQ  SSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVL
SQ  PATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALC
SQ  LAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSS
SQ  VKEISDIVQR
//
ID  Q07912;
PN  Activated CDC42 kinase 1;
GN  TNK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20979614}. Nucleus {ECO:0000269|PubMed:14733946, ECO:0000269|PubMed:20333297}. Endosome {ECO:0000250|UniProtKB:O54967}. Cell junction, adherens junction {ECO:0000305}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:16137687}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:16137687, ECO:0000269|PubMed:18262180}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:21169560}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20110370}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O54967}. Note=The Tyr-284 phosphorylated form is found both in the membrane and nucleus (By similarity). Co-localizes with EGFR on endosomes (PubMed:20333297). Nuclear translocation is CDC42-dependent (By similarity). Detected in long filamentous cytosolic structures where it co-localizes with CTPS1 (By similarity). {ECO:0000250|UniProtKB:O54967, ECO:0000269|PubMed:20333297}.
DR  UNIPROT: Q07912;
DR  UNIPROT: Q6ZMQ0;
DR  UNIPROT: Q8N6U7;
DR  UNIPROT: Q96H59;
DR  PDB: 1CF4;
DR  PDB: 1U46;
DR  PDB: 1U4D;
DR  PDB: 1U54;
DR  PDB: 3EQP;
DR  PDB: 3EQR;
DR  PDB: 4EWH;
DR  PDB: 4HZR;
DR  PDB: 4HZS;
DR  PDB: 4ID7;
DR  PDB: 5ZXB;
DR  PDB: 6VQM;
DR  PDB: 7KP6;
DR  Pfam: PF09027;
DR  Pfam: PF11555;
DR  Pfam: PF07714;
DR  Pfam: PF14604;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50002;
DR  OMIM: 606994;
DR  DisGeNET: 10188;
DE  Function: Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr-287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR. Phosphorylates WASP (PubMed:20110370). {ECO:0000269|PubMed:10652228, ECO:0000269|PubMed:11278436, ECO:0000269|PubMed:16247015, ECO:0000269|PubMed:16257963, ECO:0000269|PubMed:16472662, ECO:0000269|PubMed:17038317, ECO:0000269|PubMed:18262180, ECO:0000269|PubMed:18435854, ECO:0000269|PubMed:19815557, ECO:0000269|PubMed:20110370, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20383201}.
DE  Reference Proteome: Yes;
DE  Interaction: O14976; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: O43426; IntAct: EBI-7809036; Score: 0.27
DE  Interaction: P00533; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P60953; IntAct: EBI-603486; Score: 0.59
DE  Interaction: Q9Y5X1; IntAct: EBI-7808593; Score: 0.54
DE  Interaction: P62993; IntAct: EBI-7808665; Score: 0.66
DE  Interaction: P16333; IntAct: EBI-7808721; Score: 0.59
DE  Interaction: Q00610; IntAct: EBI-7808962; Score: 0.79
DE  Interaction: P51690; IntAct: EBI-736241; Score: 0.00
DE  Interaction: Q969R8; IntAct: EBI-736244; Score: 0.00
DE  Interaction: Q8N431; IntAct: EBI-736247; Score: 0.00
DE  Interaction: Q02543; IntAct: EBI-736250; Score: 0.00
DE  Interaction: Q53EL9; IntAct: EBI-736253; Score: 0.00
DE  Interaction: Q13243; IntAct: EBI-736256; Score: 0.00
DE  Interaction: Q9UEU0; IntAct: EBI-736259; Score: 0.00
DE  Interaction: P08575; IntAct: EBI-2257200; Score: 0.00
DE  Interaction: Q12913; IntAct: EBI-2265049; Score: 0.00
DE  Interaction: Q05209; IntAct: EBI-2266438; Score: 0.00
DE  Interaction: P56945; IntAct: EBI-7040520; Score: 0.52
DE  Interaction: P46108; IntAct: EBI-7040708; Score: 0.40
DE  Interaction: Q07912; IntAct: EBI-8071904; Score: 0.59
DE  Interaction: Q13177; IntAct: EBI-8143865; Score: 0.44
DE  Interaction: Q8IUQ4; IntAct: EBI-3934992; Score: 0.37
DE  Interaction: P08238; IntAct: EBI-6424981; Score: 0.56
DE  Interaction: Q8WXH5; IntAct: EBI-10692509; Score: 0.49
DE  Interaction: Q96JZ2; IntAct: EBI-10697958; Score: 0.37
DE  Interaction: O60880; IntAct: EBI-10187478; Score: 0.56
DE  Interaction: P07902; IntAct: EBI-10195306; Score: 0.56
DE  Interaction: P29972; IntAct: EBI-10205037; Score: 0.56
DE  Interaction: Q7Z3S9; IntAct: EBI-10224749; Score: 0.56
DE  Interaction: Q9HC98; IntAct: EBI-10310684; Score: 0.56
DE  Interaction: G3X972; IntAct: EBI-11079358; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: O95817; IntAct: EBI-11135110; Score: 0.35
DE  Interaction: Q9BQC3; IntAct: EBI-24322875; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-24423586; Score: 0.56
DE  Interaction: O14796; IntAct: EBI-24542932; Score: 0.56
DE  Interaction: Q92569; IntAct: EBI-24656100; Score: 0.56
DE  Interaction: O43639; IntAct: EBI-21521290; Score: 0.35
DE  Interaction: Q58FF7; IntAct: EBI-21831391; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-21831391; Score: 0.35
DE  Interaction: P05161; IntAct: EBI-21831391; Score: 0.35
DE  Interaction: P10275; IntAct: EBI-15636365; Score: 0.40
DE  Interaction: P16749; IntAct: EBI-15832981; Score: 0.41
DE  Interaction: Q01968; IntAct: EBI-16412116; Score: 0.35
DE  Interaction: P85968; IntAct: EBI-22241111; Score: 0.35
DE  Interaction: B2RZ33; IntAct: EBI-22241111; Score: 0.35
DE  Interaction: D4A3M8; IntAct: EBI-22241111; Score: 0.35
DE  Interaction: P97573; IntAct: EBI-22241127; Score: 0.35
DE  Interaction: O35244; IntAct: EBI-22241127; Score: 0.35
DE  Interaction: Q6UY14; IntAct: EBI-22141818; Score: 0.37
DE  Interaction: Q7Z7F7; IntAct: EBI-25377008; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-25377008; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-25377008; Score: 0.35
DE  Interaction: P17987; IntAct: EBI-25377008; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-25377008; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-25377008; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-25377008; Score: 0.35
DE  Interaction: P78371; IntAct: EBI-25377008; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-25388582; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-25388582; Score: 0.35
DE  Interaction: P49411; IntAct: EBI-25388582; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-25388582; Score: 0.35
DE  Interaction: Q58FF8; IntAct: EBI-25388582; Score: 0.35
DE  Interaction: O43264; IntAct: EBI-28939183; Score: 0.35
DE  Interaction: Q9Y262; IntAct: EBI-28939183; Score: 0.35
DE  Interaction: Q9BZD4; IntAct: EBI-28939183; Score: 0.35
DE  Interaction: Q2NL82; IntAct: EBI-28939183; Score: 0.35
DE  Interaction: Q13330; IntAct: EBI-28939183; Score: 0.35
DE  Interaction: P56134; IntAct: EBI-28939183; Score: 0.35
DE  Interaction: P25205; IntAct: EBI-28939183; Score: 0.35
DE  Interaction: O15075; IntAct: EBI-28939183; Score: 0.35
DE  Interaction: P46937; IntAct: EBI-30846635; Score: 0.44
DE  Interaction: P07947; IntAct: EBI-30849214; Score: 0.44
GO  GO:0005912;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0097268;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0031234;
GO  GO:0070436;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0005154;
GO  GO:0005095;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0004715;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0004712;
GO  GO:0004713;
GO  GO:0005102;
GO  GO:0031625;
GO  GO:0050699;
GO  GO:0030154;
GO  GO:0007166;
GO  GO:0006897;
GO  GO:0045087;
GO  GO:0016310;
GO  GO:0050731;
GO  GO:2000369;
GO  GO:0007264;
GO  GO:0007169;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNVTRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKALCKRKSWMSKVF
SQ  SGKRLEAEFPPHHSQSTFRKTSPAPGGPAGEGPLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCL
SQ  KPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGM
SQ  GYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTL
SQ  WEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFE
SQ  EPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPD
SQ  RIDELYLGNPMDPPDLLSVELSTSRPPQHLGGVKKPTYDPVSEDQDPLSSDFKRLGLRKPGLPRGLWLAKPSARVPGTKA
SQ  SRGSGAEVTLIDFGEEPVVPALRPCAPSLAQLAMDACSLLDETPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQ
SQ  DEDDFEICSINSTLVGAGVPAGPSQGQTNYAFVPEQARPPPPLEDNLFLPPQGGGKPPSSAQTAEIFQALQQECMRQLQA
SQ  PAGSPAPSPSPGGDDKPQVPPRVPIPPRPTRPHVQLSPAPPGEEETSQWPGPASPPRVPPREPLSPQGSRTPSPLVPPGS
SQ  SPLPPRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGKKVSSTHYYLLPERPSYLERYQRFLREAQ
SQ  SPEEPTPLPVPLLLPPPSTPAPAAPTATVRPMPQAALDPKANFSTNNSNPGARPPPPRATARLPQRGCPGDGPEAGRPAD
SQ  KIQMAMVHGVTTEECQAALQCHGWSVQRAAQYLKVEQLFGLGLRPRGECHKVLEMFDWNLEQAGCHLLGSWGPAHHKR
//
ID  A5D7D1;
PN  Alpha-actinin-4;
GN  ACTN4;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O43707}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:O43707, ECO:0000250|UniProtKB:P57780}.
DR  UNIPROT: A5D7D1;
DR  Pfam: PF00307;
DR  Pfam: PF08726;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions. May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA. {ECO:0000250|UniProtKB:O43707}.
DE  Reference Proteome: Yes;
DE  Interaction: A6QLL8; IntAct: EBI-1220272; Score: 0.35
DE  Interaction: P20909; IntAct: EBI-5281033; Score: 0.35
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0003779;
GO  GO:0005509;
GO  GO:0030374;
GO  GO:0035357;
GO  GO:0015031;
GO  GO:0048384;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYHAANQSYQYGPSSGSNGAGGGGTMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRD
SQ  GLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISV
SQ  EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKM
SQ  LDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRV
SQ  PQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEW
SQ  LLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQEL
SQ  NELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTI
SQ  EEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEE
SQ  QSKQQSNEHLRRQFASQANIVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIF
SQ  DNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYD
SQ  VENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCI
SQ  ARMAPYQGPDAVPGALDYKSFSTALYGESDL
//
ID  Q90734;
PN  Alpha-actinin-4;
GN  ACTN4;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}.
DR  UNIPROT: Q90734;
DR  Pfam: PF00307;
DR  Pfam: PF08726;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS50222;
DE  Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. Involved in tight junction assembly in epithelial cells. May also function as a transcriptional coactivator, stimulating transcription mediated by nuclear hormone receptors. {ECO:0000250|UniProtKB:O43707}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030054;
GO  GO:0042995;
GO  GO:0030864;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0051015;
GO  GO:0005509;
GO  GO:0030374;
GO  GO:0030036;
GO  GO:0055001;
GO  GO:0035357;
GO  GO:0015031;
GO  GO:1903506;
GO  GO:0048384;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYHSAGQPYPYGGNGPGPNGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLL
SQ  LEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVNVVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKE
SQ  GLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIV
SQ  NTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRSPQKTIQE
SQ  MQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINTGWQHLEQAEKGYEEWLLNEIRR
SQ  LEPLDHLAEKFRQKASIHEAWTEGKEAMLKQKDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYD
SQ  SPSVNARCQKICDQWDVLGSLTHSRREALEKTEKQLETIDELHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLI
SQ  AAHDQFKATLPDADREREAILGIQREAQRIADLHSIKLSGNNPYTSVTPQVINSKWERVQQLVPTRDRALQDEQSRQQCN
SQ  ERLRRQFAGQANIVGPWMQTKMEEIGRISIEMHGTLEDQLQHLKHYEQSIVDYKPNLELLEHEHQLVEEALIFDNKHTNY
SQ  TMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHCGALGPEEFKACLISLGYDVENDRQG
SQ  DAEFNRIMSLVDPNGSGSVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNYITAEELRRELPPEQAEYCIARMAPYR
SQ  GPDAAPGALDYKSFSTALYGESDL
//
ID  O43707;
PN  Alpha-actinin-4;
GN  ACTN4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:9508771}. Cytoplasm {ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:9508771}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:9508771}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). Nuclear translocation can be induced by the PI3 kinase inhibitor wortmannin or by cytochalasin D. Exclusively localized in the nucleus in a limited number of cell lines (breast cancer cell line MCF-7, oral floor cancer IMC-2, and bladder cancer KU- 7). {ECO:0000250|UniProtKB:P57780, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:9508771}.
DR  UNIPROT: O43707;
DR  UNIPROT: A4K467;
DR  UNIPROT: D6PXK4;
DR  UNIPROT: O76048;
DR  PDB: 1WLX;
DR  PDB: 1YDI;
DR  PDB: 2R0O;
DR  PDB: 6O31;
DR  PDB: 6OA6;
DR  Pfam: PF00307;
DR  Pfam: PF08726;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 603278;
DR  OMIM: 604638;
DR  DisGeNET: 81;
DE  Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (PubMed:22351778). {ECO:0000250|UniProtKB:P57780, ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:22351778, ECO:0000305|PubMed:9508771}.
DE  Disease: Focal segmental glomerulosclerosis 1 (FSGS1) [MIM:603278]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:10700177, ECO:0000269|PubMed:18164029, ECO:0000269|PubMed:18436095, ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:22732337, ECO:0000269|PubMed:23014460, ECO:0000269|PubMed:23890478}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P62993; IntAct: EBI-350217; Score: 0.35
DE  Interaction: Q99759; IntAct: EBI-362163; Score: 0.00
DE  Interaction: Q9Y572; IntAct: EBI-363781; Score: 0.00
DE  Interaction: Q9NPC6; IntAct: EBI-756484; Score: 0.93
DE  Interaction: Q9NP98; IntAct: EBI-759703; Score: 0.37
DE  Interaction: O00151; IntAct: EBI-760309; Score: 0.67
DE  Interaction: P12830; IntAct: EBI-727492; Score: 0.50
DE  Interaction: P38432; IntAct: EBI-952558; Score: 0.00
DE  Interaction: Q9NZJ4; IntAct: EBI-953488; Score: 0.00
DE  Interaction: P63104; IntAct: EBI-7197640; Score: 0.40
DE  Interaction: Q07157; IntAct: EBI-1103214; Score: 0.60
DE  Interaction: P35222; IntAct: EBI-1537638; Score: 0.68
DE  Interaction: P42771; IntAct: EBI-1641665; Score: 0.35
DE  Interaction: Q69139; IntAct: EBI-2623676; Score: 0.37
DE  Interaction: Q8TDR0; IntAct: EBI-2650416; Score: 0.35
DE  Interaction: P29474; IntAct: EBI-3385333; Score: 0.37
DE  Interaction: P42224; IntAct: EBI-3451685; Score: 0.00
DE  Interaction: O15265; IntAct: EBI-3866243; Score: 0.37
DE  Interaction: Q9NUX5; IntAct: EBI-3925821; Score: 0.37
DE  Interaction: P52292; IntAct: EBI-3944055; Score: 0.37
DE  Interaction: Q13164; IntAct: EBI-3944105; Score: 0.37
DE  Interaction: P42677; IntAct: EBI-3944125; Score: 0.37
DE  Interaction: P10599; IntAct: EBI-3944155; Score: 0.44
DE  Interaction: Q8WZ42; IntAct: EBI-5665670; Score: 0.00
DE  Interaction: Q3UQN2; IntAct: EBI-6097080; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6191076; Score: 0.53
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-6870912; Score: 0.37
DE  Interaction: P46940; IntAct: EBI-6897999; Score: 0.60
DE  Interaction: Q5L4H4; IntAct: EBI-9512219; Score: 0.59
DE  Interaction: P03466; IntAct: EBI-9512541; Score: 0.40
DE  Interaction: C3W6D7; IntAct: EBI-9513951; Score: 0.40
DE  Interaction: Q91U50; IntAct: EBI-9514006; Score: 0.40
DE  Interaction: Q6DPG0; IntAct: EBI-9513984; Score: 0.40
DE  Interaction: B2BU63; IntAct: EBI-9513930; Score: 0.40
DE  Interaction: C9S3S8; IntAct: EBI-9513909; Score: 0.40
DE  Interaction: Q8JR21; IntAct: EBI-9514040; Score: 0.27
DE  Interaction: Q38SD2; IntAct: EBI-9656528; Score: 0.35
DE  Interaction: O41957; IntAct: EBI-9640710; Score: 0.37
DE  Interaction: Q92754; IntAct: EBI-9680045; Score: 0.37
DE  Interaction: P05549; IntAct: EBI-9679922; Score: 0.37
DE  Interaction: P00533; IntAct: EBI-9689686; Score: 0.55
DE  Interaction: P67809; IntAct: EBI-9985228; Score: 0.35
DE  Interaction: A8K571; IntAct: EBI-10174341; Score: 0.56
DE  Interaction: B2R8Y4; IntAct: EBI-10175592; Score: 0.56
DE  Interaction: P03372; IntAct: EBI-9996267; Score: 0.35
DE  Interaction: Q92731; IntAct: EBI-9996422; Score: 0.35
DE  Interaction: Q9UH99; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11004631; Score: 0.35
DE  Interaction: Q9NQW6; IntAct: EBI-11009421; Score: 0.35
DE  Interaction: Q9CQ49; IntAct: EBI-11022137; Score: 0.35
DE  Interaction: Q60634; IntAct: EBI-11025478; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-11030093; Score: 0.35
DE  Interaction: O00159; IntAct: EBI-11030803; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: P21333; IntAct: EBI-11038784; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q80X90; IntAct: EBI-11053320; Score: 0.35
DE  Interaction: Q9ERG0; IntAct: EBI-11054044; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062262; Score: 0.35
DE  Interaction: Q9JHJ0; IntAct: EBI-11063313; Score: 0.35
DE  Interaction: P58771; IntAct: EBI-11063826; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: Q9P2K5; IntAct: EBI-11077096; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: O75182; IntAct: EBI-11085017; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: Q15691; IntAct: EBI-11091481; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-11092730; Score: 0.35
DE  Interaction: Q9WTI7; IntAct: EBI-11093786; Score: 0.35
DE  Interaction: Q61879; IntAct: EBI-11099615; Score: 0.35
DE  Interaction: Q9NQX4; IntAct: EBI-11100755; Score: 0.35
DE  Interaction: Q9NR12; IntAct: EBI-11105742; Score: 0.53
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-11142496; Score: 0.35
DE  Interaction: Q15599; IntAct: EBI-12452194; Score: 0.51
DE  Interaction: Q14160; IntAct: EBI-11794686; Score: 0.40
DE  Interaction: Q9NWQ9; IntAct: EBI-24303215; Score: 0.56
DE  Interaction: Q8IY33; IntAct: EBI-24365113; Score: 0.56
DE  Interaction: Q08043; IntAct: EBI-24497993; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-24475492; Score: 0.56
DE  Interaction: O94875; IntAct: EBI-12689671; Score: 0.60
DE  Interaction: O60294; IntAct: EBI-12697987; Score: 0.56
DE  Interaction: P50222; IntAct: EBI-12702268; Score: 0.56
DE  Interaction: O15297; IntAct: EBI-14024588; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: P10276; IntAct: EBI-15971728; Score: 0.52
DE  Interaction: P37231; IntAct: EBI-15971696; Score: 0.40
DE  Interaction: O43707; IntAct: EBI-15971763; Score: 0.40
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: O00429; IntAct: EBI-20305770; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: P69968; IntAct: EBI-20817323; Score: 0.37
DE  Interaction: Q8D0P1; IntAct: EBI-20818271; Score: 0.37
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: P35408; IntAct: EBI-20811214; Score: 0.37
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21024514; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-26966879; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P04156; IntAct: EBI-21014477; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: P12931; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q8N5H7; IntAct: EBI-25387159; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9H3R0; IntAct: EBI-25479978; Score: 0.35
DE  Interaction: P83105; IntAct: EBI-25745135; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: P53355; IntAct: EBI-28938354; Score: 0.35
DE  Interaction: Q05513; IntAct: EBI-28938998; Score: 0.35
DE  Interaction: Q86V86; IntAct: EBI-28942203; Score: 0.35
DE  Interaction: Q8TEA7; IntAct: EBI-28943849; Score: 0.35
DE  Interaction: Q8TF76; IntAct: EBI-28943924; Score: 0.35
DE  Interaction: Q9Y2U5; IntAct: EBI-28947216; Score: 0.35
DE  Interaction: Q8WYL5; IntAct: EBI-27116808; Score: 0.27
GO  GO:0015629;
GO  GO:0030054;
GO  GO:0042995;
GO  GO:0030864;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005925;
GO  GO:0043005;
GO  GO:0016604;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031093;
GO  GO:0032991;
GO  GO:0031143;
GO  GO:1990904;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0005509;
GO  GO:0031490;
GO  GO:0005178;
GO  GO:0016922;
GO  GO:0030374;
GO  GO:0042974;
GO  GO:0001882;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0003723;
GO  GO:0000977;
GO  GO:0003713;
GO  GO:0044325;
GO  GO:0030036;
GO  GO:0055001;
GO  GO:1900025;
GO  GO:0035357;
GO  GO:0030335;
GO  GO:1901224;
GO  GO:0032417;
GO  GO:0015031;
GO  GO:0042981;
GO  GO:1903506;
GO  GO:0001666;
GO  GO:0048384;
GO  GO:0033209;
GO  GO:0030050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRD
SQ  GLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISV
SQ  EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKM
SQ  LDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRV
SQ  PQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEW
SQ  LLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQEL
SQ  NELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTI
SQ  EEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEE
SQ  QSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIF
SQ  DNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYD
SQ  VENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCI
SQ  ARMAPYQGPDAVPGALDYKSFSTALYGESDL
//
ID  P57780;
PN  Alpha-actinin-4;
GN  Actn4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000269|PubMed:18332111}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O43707}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:33228246}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (PubMed:33228246). {ECO:0000250|UniProtKB:O43707, ECO:0000269|PubMed:33228246}.
DR  UNIPROT: P57780;
DR  Pfam: PF00307;
DR  Pfam: PF08726;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (By similarity). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (PubMed:18332111). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (By similarity). {ECO:0000250|UniProtKB:O43707, ECO:0000269|PubMed:18332111}.
DE  Reference Proteome: Yes;
DE  Interaction: P39447; IntAct: EBI-1103365; Score: 0.54
DE  Interaction: O08601; IntAct: EBI-1183624; Score: 0.40
DE  Interaction: P09103; IntAct: EBI-1183624; Score: 0.40
DE  Interaction: Q62468; IntAct: EBI-1183624; Score: 0.40
DE  Interaction: Q3TN34; IntAct: EBI-1779866; Score: 0.64
DE  Interaction: P51153; IntAct: EBI-1780138; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-2307988; Score: 0.35
DE  Interaction: O35400; IntAct: EBI-8174161; Score: 0.35
DE  Interaction: Q8BP00; IntAct: EBI-4282064; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16750831; Score: 0.35
DE  Interaction: O08749; IntAct: EBI-20313604; Score: 0.35
DE  Interaction: Q8K1M6; IntAct: EBI-20313833; Score: 0.35
DE  Interaction: P35486; IntAct: EBI-20313969; Score: 0.35
DE  Interaction: P08228; IntAct: EBI-20314123; Score: 0.35
DE  Interaction: P51637; IntAct: EBI-20565496; Score: 0.35
DE  Interaction: P97493; IntAct: EBI-26500418; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-26573447; Score: 0.35
DE  Interaction: A0A0F6B063; IntAct: EBI-27034862; Score: 0.35
DE  Interaction: Q8K4E0; IntAct: EBI-27076664; Score: 0.51
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0015629;
GO  GO:0030054;
GO  GO:0042995;
GO  GO:0005911;
GO  GO:0030864;
GO  GO:0030863;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0043005;
GO  GO:0016604;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0031143;
GO  GO:1990904;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0051015;
GO  GO:0005509;
GO  GO:0031490;
GO  GO:0016922;
GO  GO:0030374;
GO  GO:0042974;
GO  GO:0001882;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0044877;
GO  GO:0000977;
GO  GO:0005200;
GO  GO:0003713;
GO  GO:0044325;
GO  GO:0030036;
GO  GO:0051017;
GO  GO:0070830;
GO  GO:0032835;
GO  GO:0055001;
GO  GO:1900025;
GO  GO:0035357;
GO  GO:0090521;
GO  GO:0030335;
GO  GO:1901224;
GO  GO:0048549;
GO  GO:1902396;
GO  GO:0015031;
GO  GO:0042981;
GO  GO:1903506;
GO  GO:0048384;
GO  GO:0033209;
GO  GO:0030050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYHAANQAYQYGPNSGGGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFR
SQ  DGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDIS
SQ  VEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPK
SQ  MLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDR
SQ  VPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNGWQHLEQAEKGYEE
SQ  WLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKQRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQE
SQ  LNELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHT
SQ  IEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLE
SQ  EQSKQQSNEHLRRQFASQANMVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPSLDLLEQQHQLIQEALI
SQ  FDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGY
SQ  DVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYC
SQ  IARMAPYQGPDAAPGALDYKSFSTALYGESDL
//
ID  Q5RCS6;
PN  Alpha-actinin-4;
GN  ACTN4;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O43707}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:O43707, ECO:0000250|UniProtKB:P57780}.
DR  UNIPROT: Q5RCS6;
DR  Pfam: PF00307;
DR  Pfam: PF08726;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions. May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA. {ECO:0000250|UniProtKB:O43707}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0003779;
GO  GO:0005509;
GO  GO:0030374;
GO  GO:0035357;
GO  GO:0015031;
GO  GO:0048384;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYHAASQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRD
SQ  GLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISV
SQ  EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKM
SQ  LDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICRVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRV
SQ  PQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEW
SQ  LLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQEL
SQ  NELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTI
SQ  EEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEE
SQ  QSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIF
SQ  DNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYD
SQ  VENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCI
SQ  ARMAPYQGPDAVPGALDYKSFSTALYGESDL
//
ID  Q9QXQ0;
PN  Alpha-actinin-4;
GN  Actn4;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O43707}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:O43707, ECO:0000250|UniProtKB:P57780}.
DR  UNIPROT: Q9QXQ0;
DR  UNIPROT: Q6P786;
DR  Pfam: PF00307;
DR  Pfam: PF08726;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions. May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA. {ECO:0000250|UniProtKB:O43707}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.54
DE  Interaction: P21708; IntAct: EBI-7617257; Score: 0.35
DE  Interaction: P54645; IntAct: EBI-16399805; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16400563; Score: 0.35
GO  GO:0015629;
GO  GO:0030054;
GO  GO:0042995;
GO  GO:0005911;
GO  GO:0030864;
GO  GO:0030863;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0043005;
GO  GO:0016604;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0031143;
GO  GO:1990904;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0051015;
GO  GO:0005509;
GO  GO:0031490;
GO  GO:0016922;
GO  GO:0030374;
GO  GO:0042974;
GO  GO:0001882;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0044877;
GO  GO:0000977;
GO  GO:0003713;
GO  GO:0044325;
GO  GO:0030036;
GO  GO:0051017;
GO  GO:0070830;
GO  GO:0055001;
GO  GO:1900025;
GO  GO:0035357;
GO  GO:0030335;
GO  GO:1901224;
GO  GO:0048549;
GO  GO:1902396;
GO  GO:0015031;
GO  GO:0042981;
GO  GO:1903506;
GO  GO:0001666;
GO  GO:0048384;
GO  GO:0033209;
GO  GO:0030050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYHAANQAYQYGPSSGGNGTGGGGGMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRD
SQ  GLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISV
SQ  EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKM
SQ  LDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRV
SQ  PQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNGWQHLEQAEKGYEEW
SQ  LLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQEL
SQ  NELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTI
SQ  EEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTSVTPQIINSKWEKVQQLVPKRDHALLEE
SQ  QSKQQSNEHLRRQFASQANMVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIF
SQ  DNKHTNYTMEHLRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYD
SQ  VENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCI
SQ  ARMAPYQGPDAAPGALDYKSFSTALYGESDL
//
ID  O76329;
PN  Interaptin;
GN  abpD;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Single-pass type IV membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane. Golgi apparatus, Golgi stack membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated either with the nuclear envelope, the Golgi membrane or the endoplasmic reticulum membrane.
DR  UNIPROT: O76329;
DR  UNIPROT: Q54KE8;
DR  Pfam: PF00307;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DE  Function: May function as linker between cellular membranes and the actin cytoskeleton. Required for normal development of fruiting bodies. {ECO:0000269|PubMed:10704840}.
DE  Reference Proteome: Yes;
DE  Interaction: Q54CH1; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55FK4; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55CS9; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q23858; IntAct: EBI-922911; Score: 0.40
DE  Interaction: P34122; IntAct: EBI-922911; Score: 0.40
DE  Interaction: P25870; IntAct: EBI-922911; Score: 0.40
DE  Interaction: P34121; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54HL0; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54KG1; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54T81; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54NB6; IntAct: EBI-922911; Score: 0.40
DE  Interaction: P46800; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q552M5; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q557E0; IntAct: EBI-922911; Score: 0.40
DE  Interaction: P54651; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55GF9; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q6RZZ9; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54BF6; IntAct: EBI-922911; Score: 0.40
DE  Interaction: P34118; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q86HW7; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q869Y7; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q23921; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54JM5; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54BH4; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54BP1; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54DL5; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54FU0; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54G01; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54G31; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54GS4; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54GY1; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54H23; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54I73; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54NB4; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54R55; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54RZ4; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54SP3; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54TQ6; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54U97; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54U98; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54VJ7; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54VQ1; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54W02; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54XP9; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q556V8; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55CE3; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55CZ0; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55DZ5; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55F82; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55F84; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55GC0; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55GC5; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q75JY8; IntAct: EBI-922911; Score: 0.40
DE  Interaction: P33519; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q86K01; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q559R0; IntAct: EBI-922911; Score: 0.40
DE  Interaction: P52285; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q95ZG4; IntAct: EBI-922911; Score: 0.40
DE  Interaction: P32255; IntAct: EBI-922911; Score: 0.40
DE  Interaction: P32256; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55AR3; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54TH8; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54LP7; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q54WN5; IntAct: EBI-922911; Score: 0.40
DE  Interaction: Q55EX9; IntAct: EBI-922911; Score: 0.40
GO  GO:0005789;
GO  GO:0032580;
GO  GO:0016021;
GO  GO:0005815;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0003779;
GO  GO:0098609;
GO  GO:0030587;
GO  GO:0009847;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MEHSTPLNEEIVHKKNDENWVIAQKKVFTNWCNIFLNQRSQKIEDLETDLYDGILLGSLLEILSGKNVILSKCKQLKTRL
SQ  HYINNLNFSLKFIGDEGLRLVGVASEDITDGNLKLILGLVWTLILRYQIQSMQNSKSSQQNLHSSTKPSELMLNWVKSQI
SQ  SDYGHHIKDLTTSFQNGLLFCALVHKLVPEKLDYKSLSESDSLGNLTLAFEVANKELGIPSILDPHDIITTPDELSILTY
SQ  ISLFPKVYQQTLEPLNNNNNISPSLSSSSSSLLNTPNKRNSIQLSKSTSFEQQNQQQQQQNLLSPNSYRNSISFSKSPSF
SQ  EGSQSTGSSRSISPISSPIKNSTTGNSNLSKSTSFEKIEASNTTNNNTIIIAEESRVIEKIVEKIIEVEKIVEVEKIVEV
SQ  EKIVEVEKIVEVEKIVKVDDIEKLTNLQDQLTEQQQQYQEKSLKLVNLELELQEKSNQLVDKSNQLSTMQATNSELMEKI
SQ  GGLMNDLTDIPTQDIKEKDEIIANLKIESEKNLKCFQDDFNALQSRYSLTIEQTSQLQDRIKQLINELQERDDKFIEFTN
SQ  SSNQSLADNQRVIDQLTNEKQSITLQLQDQQDIKEKEFQFEKQQLLSQIDSITTNIQEYQDKFNNLQQEFNTQQTLNQQE
SQ  THRLTQQLYQINTDYNEKQTQLQSEIKDNQTINEQLNKQLSEKDKEIEKLSNQQEQQQDEKINNLLLEIKEKDCLIERIN
SQ  QQLLENIDLNSKYQQLLLEFENFKLNSSKEKENQLNELQSKQDERFNQLNDEKLEKEKQLQSIEDEFNQYKQQQLSSNSN
SQ  IDQQLQSTIIELSELKEQKELNDSKLIEKEKQLQQLQQEFDQLNEKNQKDHQDQLELLEKQLKQLQQEYDQLNETNQSIE
SQ  NQLNQQNLINKENLNEKEQELLKLQNQLNQQIEKIQFDQQEFSKQNSINIELVNEKNEKLIQLQQDYDQLKQQNRSNDEK
SQ  DENDLIEKENQLKSIQNELNQLIEKNESDHKEQQLKQQSIENDLIEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLI
SQ  EKNQFDQKEQQLKQQSIENDLFEKENQIQQLQSQLNEQRQQQSNQLSEKDQQLNQLIEKNESDQKEQQLKQQSIENDLIE
SQ  KENQIQQLQLQLNEQRQLQSEVSIDNDKILELEKQLKQCQSDLLKLNDEKQQQDKQLQDKQIEFDQLQLTFNQFKNDKDS
SQ  QFIQLQDDQKQQLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQFENQEKEKQLSEKDEKLQSIQQNLNQLNDENQEKV
SQ  KQFSEKDEKLQSIQQDLNQLKQENQEKEKQLSEKDEKLQSIQQDLNQLNDDQIKKNEKLKEKEEQLLKLQQDFNDQQSQQ
SQ  LKQLEEKLSEKENQLQQLKQENEINQLNQQQQSNEIIQQLKDQLLKQQQQEQQENNNEKEIERLIQEIEQLKQQQEIDQS
SQ  ELSNKEIKIQTTQQEFDQLSHNRSKDQLHLQQLQQELDQLKQSFDDQDHQFKKVIDERYNLQLQLEQSTLSNNQLDQLLK
SQ  EKLKPLELDSNEKQKTIDDLLSNISNLQISLQNDKDLISERNNSIKTLESRITQQLSLLDEKDNLIKDLQQQKQQQQQPP
SQ  TASSSPSSSPSLLSSTPTPKPQRPNQIEIDRLVNEIVNRNQDLIRKNKTKFYKLENGDYIVNSIIYRLSLDDDNDSDLIA
SQ  QEYENGNSTTFEKSLRIFPSKNTRPIFDWRALFFIGAAVLAISTLFSSSRPIKYEKPT
//
ID  P18130;
PN  Alpha-1A adrenergic receptor;
GN  ADRA1A;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK- mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: P18130;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0004937;
GO  GO:0004930;
GO  GO:0046982;
GO  GO:0071880;
GO  GO:0007267;
GO  GO:0007200;
GO  GO:0007204;
GO  GO:0001996;
GO  GO:0043410;
GO  GO:0045907;
GO  GO:0055117;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVFLSGNASDSSNCTHPPPPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVL
SQ  PFSAIFEILGYWAFGRVFCNVWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQKRGLMALLCVWALSLVISIG
SQ  PLFGWRQPAPEDETICQINEEPGYVLFSALGSFYVPLTIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKN
SQ  AQVGGSGVTSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFRPSETVFKIAFWLGYLNSC
SQ  INPIIYPCSSQEFKKAFQNVLRIQCLRRKQSSKHTLGYTLHAPSHVLEGQHKDLVRIPVGSAETFYKISKTDGVCEWKIF
SQ  SSLPRGSARMAVARDPSACTTARVRSKSFLQVCCCLGPSTPSHGENHQIPTIKIHTISLSENGEEV
//
ID  O77621;
PN  Alpha-1A adrenergic receptor;
GN  ADRA1A;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK- mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: O77621;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0004937;
GO  GO:0004930;
GO  GO:0046982;
GO  GO:0071880;
GO  GO:0007267;
GO  GO:0007200;
GO  GO:0007204;
GO  GO:0001996;
GO  GO:0043410;
GO  GO:0045907;
GO  GO:0055117;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVFLSGNASDSSNCTHPPAPVNISKAILLGVILGGLIIFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVL
SQ  PFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQKRGLMALLCVWALSLVISIG
SQ  PLFGWRQPAPEDETICQITEEPGYVLFSALGSFYVPLTIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKN
SQ  APVGGTGVSSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIG
//
ID  Q9WU25;
PN  Alpha-1A adrenergic receptor;
GN  ADRA1A;
OS  10141;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK- mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9WU25;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0004937;
GO  GO:0046982;
GO  GO:0043410;
GO  GO:0055117;
GO  GO:0019229;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVFLSGNASDSSNCTQPPAPVNIPKAILLGVILGVLILFGVPGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVL
SQ  PFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIMSLCIISIDRYIGVSYPLRYPTIVTQRRGLRALLCLWALSLVISIG
SQ  PLFGWRQPAPQDETICQINEDPSYVLFSALGSFYVPLAIILVMYCRVYVVAKRESRGLTSGLKTDKSDSEQVTLRIHRKN
SQ  APLGGSGVASSKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSC
SQ  INPIIYPCSSQEFKKAFQNVLKIQCLRRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYKISKTDGVCEWKFF
SQ  SSMPRGSARITVPKDQSACTTARVRSKSFLQVCCCVGPSTPNPGENHQVPTIKIHTISLSENGEEV
//
ID  P35348;
PN  Alpha-1A adrenergic receptor;
GN  ADRA1A;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:24567387}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:24567387}. Membrane, caveola {ECO:0000269|PubMed:24567387}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK- mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes.
DR  UNIPROT: P35348;
DR  UNIPROT: A8K0I3;
DR  UNIPROT: B0ZBD1;
DR  UNIPROT: B0ZBD2;
DR  UNIPROT: B0ZBD4;
DR  UNIPROT: B0ZBD5;
DR  UNIPROT: B0ZBD6;
DR  UNIPROT: B0ZBD8;
DR  UNIPROT: B0ZBD9;
DR  UNIPROT: O60451;
DR  UNIPROT: Q13675;
DR  UNIPROT: Q13729;
DR  UNIPROT: Q4VBM7;
DR  UNIPROT: Q6RUJ4;
DR  UNIPROT: Q6RUJ5;
DR  UNIPROT: Q6RUJ7;
DR  UNIPROT: Q6RUJ8;
DR  UNIPROT: Q6RUJ9;
DR  UNIPROT: Q96RE8;
DR  UNIPROT: Q9UD63;
DR  UNIPROT: Q9UD67;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  OMIM: 104221;
DR  DisGeNET: 148;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes. {ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526}.
DE  Reference Proteome: Yes;
DE  Interaction: P13497; IntAct: EBI-489882; Score: 0.00
DE  Interaction: Q12979; IntAct: EBI-489946; Score: 0.00
DE  Interaction: Q14315; IntAct: EBI-489983; Score: 0.00
DE  Interaction: P29066; IntAct: EBI-15953886; Score: 0.40
DE  Interaction: O75787; IntAct: EBI-20801320; Score: 0.37
DE  Interaction: P60033; IntAct: EBI-20801330; Score: 0.37
DE  Interaction: Q8WY98; IntAct: EBI-20801340; Score: 0.37
DE  Interaction: Q9Y247; IntAct: EBI-20801360; Score: 0.37
DE  Interaction: Q96D05; IntAct: EBI-20801350; Score: 0.37
DE  Interaction: Q9NZC3; IntAct: EBI-20801390; Score: 0.37
DE  Interaction: O15354; IntAct: EBI-20801380; Score: 0.37
DE  Interaction: Q8IWK6; IntAct: EBI-20801370; Score: 0.37
DE  Interaction: Q9HCP6; IntAct: EBI-20801400; Score: 0.37
DE  Interaction: Q53GT1; IntAct: EBI-20801411; Score: 0.37
DE  Interaction: Q8IYS2; IntAct: EBI-20801421; Score: 0.37
DE  Interaction: Q96BZ9; IntAct: EBI-20801471; Score: 0.37
DE  Interaction: Q96N66; IntAct: EBI-20801431; Score: 0.37
DE  Interaction: Q9HCE9; IntAct: EBI-20801481; Score: 0.37
DE  Interaction: Q8NHX9; IntAct: EBI-20801491; Score: 0.37
DE  Interaction: Q16585; IntAct: EBI-20801451; Score: 0.37
DE  Interaction: Q07699; IntAct: EBI-20801461; Score: 0.37
DE  Interaction: Q96CW9; IntAct: EBI-20801441; Score: 0.37
DE  Interaction: Q16880; IntAct: EBI-20801511; Score: 0.37
DE  Interaction: Q5T4S7; IntAct: EBI-20801501; Score: 0.37
DE  Interaction: Q13636; IntAct: EBI-20902904; Score: 0.40
DE  Interaction: P08670; IntAct: EBI-20929296; Score: 0.40
DE  Interaction: Q00610; IntAct: EBI-21283112; Score: 0.46
DE  Interaction: P09496; IntAct: EBI-21283119; Score: 0.46
DE  Interaction: P09497; IntAct: EBI-21283123; Score: 0.46
DE  Interaction: P25106; IntAct: EBI-21283763; Score: 0.42
DE  Interaction: P61073; IntAct: EBI-21283881; Score: 0.61
DE  Interaction: Q96HD1; IntAct: EBI-21288883; Score: 0.37
DE  Interaction: P35348; IntAct: EBI-21282711; Score: 0.40
DE  Interaction: P35368; IntAct: EBI-21282743; Score: 0.40
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098691;
GO  GO:0098982;
GO  GO:0098978;
GO  GO:0005887;
GO  GO:0099055;
GO  GO:0099056;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0030315;
GO  GO:0030018;
GO  GO:0004937;
GO  GO:0004930;
GO  GO:0046982;
GO  GO:0007202;
GO  GO:0071880;
GO  GO:0007512;
GO  GO:0007568;
GO  GO:0006915;
GO  GO:0060402;
GO  GO:0061049;
GO  GO:0007267;
GO  GO:0007186;
GO  GO:0035556;
GO  GO:0000165;
GO  GO:0060073;
GO  GO:0010259;
GO  GO:0010507;
GO  GO:0008285;
GO  GO:0001985;
GO  GO:0035024;
GO  GO:0150099;
GO  GO:0001994;
GO  GO:0007200;
GO  GO:0097195;
GO  GO:0045760;
GO  GO:0060452;
GO  GO:0010613;
GO  GO:0007204;
GO  GO:0070374;
GO  GO:0001996;
GO  GO:0043410;
GO  GO:1903997;
GO  GO:0090037;
GO  GO:0045987;
GO  GO:0032230;
GO  GO:0003084;
GO  GO:0001997;
GO  GO:0045907;
GO  GO:2000300;
GO  GO:0009725;
GO  GO:0009410;
GO  GO:0007165;
GO  GO:0006939;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVFLSGNASDSSNCTQPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVL
SQ  PFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIG
SQ  PLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKN
SQ  APAGGSGMASAKTKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSC
SQ  INPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFF
SQ  SSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV
//
ID  P97718;
PN  Alpha-1A adrenergic receptor;
GN  Adra1a;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:22120526}; Multi-pass membrane protein {ECO:0000269|PubMed:22120526}. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: P97718;
DR  UNIPROT: O54913;
DR  UNIPROT: Q8BV77;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P70658; IntAct: EBI-21294249; Score: 0.27
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098691;
GO  GO:0098982;
GO  GO:0098978;
GO  GO:0005887;
GO  GO:0099055;
GO  GO:0099056;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0030315;
GO  GO:0030018;
GO  GO:0004937;
GO  GO:0004930;
GO  GO:0046982;
GO  GO:0007202;
GO  GO:0071880;
GO  GO:0007512;
GO  GO:0007568;
GO  GO:0060402;
GO  GO:0061049;
GO  GO:0007267;
GO  GO:0000165;
GO  GO:0060073;
GO  GO:0010259;
GO  GO:0010507;
GO  GO:0001985;
GO  GO:0035024;
GO  GO:0150099;
GO  GO:0001994;
GO  GO:0035265;
GO  GO:0007200;
GO  GO:0097195;
GO  GO:0045760;
GO  GO:0060452;
GO  GO:0010613;
GO  GO:0007204;
GO  GO:0070374;
GO  GO:0010460;
GO  GO:0001996;
GO  GO:0043410;
GO  GO:1903997;
GO  GO:0090037;
GO  GO:0045987;
GO  GO:0032230;
GO  GO:0003084;
GO  GO:0001997;
GO  GO:0045907;
GO  GO:0008217;
GO  GO:2000300;
GO  GO:0009725;
GO  GO:0009410;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVLLSENASEGSNCTHPPAQVNISKAILLGVILGGLIIFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVL
SQ  PFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGVRALLCVWALSLVISIG
SQ  PLFGWRQQAPEDETICQINEEPGYVLFSALGSFYVPLTIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKN
SQ  VPAEGSGVSSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPNFKPPETVFKIVFWLGYLNSC
SQ  INPIIYPCSSQEFKKAFQNVLRIQCLRRRQSSKHALGYTLHPPSQAVEGQHRGMVRIPVGSGETFYKISKTDGVREWKFF
SQ  SSMPQGSARITMPKDQSACTTARVRSKSFLQVCCCVGSSTPRPEENHQVPTIKIHTISLGENGEEV
//
ID  O02824;
PN  Alpha-1A adrenergic receptor;
GN  ADRA1A;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK- mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: O02824;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0004937;
GO  GO:0046982;
GO  GO:0007512;
GO  GO:0061049;
GO  GO:0000165;
GO  GO:0010259;
GO  GO:0010507;
GO  GO:0001985;
GO  GO:0150099;
GO  GO:0001994;
GO  GO:0007200;
GO  GO:0097195;
GO  GO:0010613;
GO  GO:0001996;
GO  GO:0043410;
GO  GO:1903997;
GO  GO:0045987;
GO  GO:0001997;
GO  GO:0055117;
GO  GO:0019229;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVFLSGNASDSSNCTHPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVL
SQ  PFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIISLCVISIDRYIGVSYPLRYPTIVTQRRGLRALLCVWAFSLVISVG
SQ  PLFGWRQPAPDDETICQINEEPGYVLFSALGSFYVPLTIILAMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKN
SQ  APAGGSGVASAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPPETVFKIVFWLGYLNSC
SQ  INPIIYPCSSQEFKKAFQNVLKIQCLRRKQSSKHALGYTLHAPSQALEGQHKDMVRIPVGSGETFYKISKTDGVCEWKFF
SQ  SSMPRGSARITVPKDQSACTTARVRSKSFLQVCCCVGPSTPNPGENHQVPTIKIHTISLSENGEEV
//
ID  P43140;
PN  Alpha-1A adrenergic receptor;
GN  Adra1a;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK- mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: P43140;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: O08565; IntAct: EBI-21284814; Score: 0.27
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098691;
GO  GO:0098982;
GO  GO:0098978;
GO  GO:0005887;
GO  GO:0099055;
GO  GO:0099056;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0030315;
GO  GO:0030018;
GO  GO:0004937;
GO  GO:0004930;
GO  GO:0046982;
GO  GO:0007202;
GO  GO:0071880;
GO  GO:0071875;
GO  GO:0007512;
GO  GO:0007568;
GO  GO:0060402;
GO  GO:0061049;
GO  GO:0007267;
GO  GO:0000165;
GO  GO:0060073;
GO  GO:0010259;
GO  GO:0010507;
GO  GO:0001985;
GO  GO:0035024;
GO  GO:0150099;
GO  GO:0001994;
GO  GO:0035265;
GO  GO:0007200;
GO  GO:0097195;
GO  GO:0045760;
GO  GO:0060452;
GO  GO:0010613;
GO  GO:0007204;
GO  GO:0070374;
GO  GO:0010460;
GO  GO:0001996;
GO  GO:0043410;
GO  GO:1903997;
GO  GO:0090037;
GO  GO:0045987;
GO  GO:0032230;
GO  GO:0003084;
GO  GO:0001997;
GO  GO:0045907;
GO  GO:0008217;
GO  GO:2000300;
GO  GO:0009725;
GO  GO:0009410;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVLLSENASEGSNCTHPPAPVNISKAILLGVILGGLIIFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVL
SQ  PFSAIFEILGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGVRALLCVWVLSLVISIG
SQ  PLFGWRQPAPEDETICQINEEPGYVLFSALGSFYVPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKN
SQ  VPAEGGGVSSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSC
SQ  INPIIYPCSSQEFKKAFQNVLRIQCLRRRQSSKHALGYTLHPPSQALEGQHRDMVRIPVGSGETFYKISKTDGVCEWKFF
SQ  SSMPQGSARITVPKDQSACTTARVRSKSFLQVCCCVGSSAPRPEENHQVPTIKIHTISLGENGEEV
//
ID  P11615;
PN  Alpha-1B adrenergic receptor;
GN  ADRA1B;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P35368}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35368}. Membrane, caveola {ECO:0000250|UniProtKB:P35368}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: P11615;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0004937;
GO  GO:0004930;
GO  GO:0046982;
GO  GO:0071880;
GO  GO:0007267;
GO  GO:0007200;
GO  GO:0007204;
GO  GO:0001996;
GO  GO:0043410;
GO  GO:0045907;
GO  GO:0055117;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  VLPFSAALEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLGVWVLSTVIS
SQ  IGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHS
SQ  KNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLG
SQ  YFNSCLNPIIYPCSSKEFKRAFVRILGCQCRGRRRRRRRRRLGGCAYTYRPWTRGGSLERSQSRKDSLDDSGSCLSGSQR
SQ  TLPSASPSPGYLGRAAPPPVELCAVPEWKAPGALLSLPAPQPPGRRGRRDSGPLFTFRLLAERGSPAAGDGACRPAPDAA
SQ  NGQPGFKTNMPLAPGQF
//
ID  P35368;
PN  Alpha-1B adrenergic receptor;
GN  ADRA1B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:24567387}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:24567387}. Membrane, caveola {ECO:0000269|PubMed:24567387}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK- mediated signaling in cardiac myocytes. signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes.
DR  UNIPROT: P35368;
DR  UNIPROT: B0LPE1;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  OMIM: 104220;
DR  DisGeNET: 147;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes. {ECO:0000269|PubMed:18802028, ECO:0000269|PubMed:22120526}.
DE  Reference Proteome: Yes;
DE  Interaction: P35348; IntAct: EBI-21282743; Score: 0.40
DE  Interaction: Q14315; IntAct: EBI-490031; Score: 0.00
DE  Interaction: P02768; IntAct: EBI-1220884; Score: 0.35
DE  Interaction: P01857; IntAct: EBI-1222317; Score: 0.35
DE  Interaction: Q96SB3; IntAct: EBI-7385236; Score: 0.40
DE  Interaction: P21917; IntAct: EBI-15989057; Score: 0.47
DE  Interaction: P25106; IntAct: EBI-21283831; Score: 0.42
DE  Interaction: P61073; IntAct: EBI-21284190; Score: 0.61
DE  Interaction: P35368; IntAct: EBI-21282722; Score: 0.40
DE  Interaction: P25100; IntAct: EBI-21282754; Score: 0.40
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0004937;
GO  GO:0004930;
GO  GO:0046982;
GO  GO:0071880;
GO  GO:0007188;
GO  GO:0007267;
GO  GO:0007186;
GO  GO:0035556;
GO  GO:0150099;
GO  GO:0007200;
GO  GO:0007204;
GO  GO:0001996;
GO  GO:0043410;
GO  GO:0045907;
GO  GO:0055117;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MNPDLDTGHNTSAPAHWGELKNANFTGPNQTSSNSTLPQLDITRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPT
SQ  NYFIVNLAMADLLLSFTVLPFSAALEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRR
SQ  KAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAG
SQ  VMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLF
SQ  STLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFVRILGCQCRGRGRRRRRRRRRLGGCAYTYRPWTRGGSLERS
SQ  QSRKDSLDDSGSCLSGSQRTLPSASPSPGYLGRGAPPPVELCAFPEWKAPGALLSLPAPEPPGRRGRHDSGPLFTFKLLT
SQ  EPESPGTDGGASNGGCEAAADVANGQPGFKSNMPLAPGQF
//
ID  P18841;
PN  Alpha-1B adrenergic receptor;
GN  ADRA1B;
OS  10036;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P35368}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35368}. Membrane, caveola {ECO:0000250|UniProtKB:P35368}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: P18841;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: O35796; IntAct: EBI-6391260; Score: 0.54
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0004937;
GO  GO:0046982;
GO  GO:0043410;
GO  GO:0055117;
GO  GO:0019229;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MNPDLDTGHNTSAPAQWGELKDANFTGPNQTSSNSTLPQLDVTRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPT
SQ  NYFIVNLAIADLLLSFTVLPFSATLEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRR
SQ  KAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAG
SQ  VMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLF
SQ  STLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFMRILGCQCRSGRRRRRRRRLGACAYTYRPWTRGGSLERSQS
SQ  RKDSLDDSGSCMSGSQRTLPSASPSPGYLGRGAQPPLELCAYPEWKSGALLSLPEPPGRRGRLDSGPLFTFKLLGEPESP
SQ  GTEGDASNGGCDATTDLANGQPGFKSNMPLAPGHF
//
ID  P97717;
PN  Alpha-1B adrenergic receptor;
GN  Adra1b;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:22120526}; Multi-pass membrane protein {ECO:0000269|PubMed:22120526}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:P35368}. Membrane, caveola {ECO:0000250|UniProtKB:P35368}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: P97717;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P70658; IntAct: EBI-21294339; Score: 0.27
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0014704;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0030315;
GO  GO:0004937;
GO  GO:0004930;
GO  GO:0046982;
GO  GO:0071880;
GO  GO:0007512;
GO  GO:0048148;
GO  GO:0001974;
GO  GO:0061049;
GO  GO:0007267;
GO  GO:0042593;
GO  GO:0005980;
GO  GO:0007626;
GO  GO:0010259;
GO  GO:0045818;
GO  GO:0035024;
GO  GO:0150099;
GO  GO:0035265;
GO  GO:0007200;
GO  GO:0007204;
GO  GO:0045819;
GO  GO:0001996;
GO  GO:0043410;
GO  GO:0001997;
GO  GO:0045907;
GO  GO:0008217;
GO  GO:0055117;
GO  GO:0001975;
GO  GO:0009725;
GO  GO:0043278;
GO  GO:0048545;
GO  GO:0001987;
GO  GO:0008542;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MNPDLDTGHNTSAPAHWGELKDANFTGPNQTSSNSTLPQLDVTRAISVGCLGAFILFAIVGNILVILSVACNRHLRTPTN
SQ  YFIVNLAIADLLLSFTDLPFSATLEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRK
SQ  AILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGV
SQ  MKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFS
SQ  TLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFMRILGCQCRGGRRRRRRRRLGACAYTYRPWTRGGSLERSQSR
SQ  KDSLDDSGSCMSGSQRTLPSASPSPGYLGRGTQPPVELCAFPEWKPGALLSLPEPPGRRGRLDSGPLFTFKLLGEPESPG
SQ  TEGDASNGGCDTTTDLANGQPGFKSNMPLAPGHF
//
ID  P15823;
PN  Alpha-1B adrenergic receptor;
GN  Adra1b;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P35368}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35368}. Membrane, caveola {ECO:0000250|UniProtKB:P35368}. Note=Location at the nuclear membrane facilitates heterooligomerization and regulates ERK-mediated signaling in cardiac myocytes. Colocalizes with GNAQ, PLCB1 as well as LAP2 at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: P15823;
DR  UNIPROT: Q63215;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocytes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P30729; IntAct: EBI-15989124; Score: 0.47
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0014704;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0030315;
GO  GO:0004937;
GO  GO:0004930;
GO  GO:0046982;
GO  GO:0071880;
GO  GO:0071875;
GO  GO:0007512;
GO  GO:0048148;
GO  GO:0001974;
GO  GO:0061049;
GO  GO:0007267;
GO  GO:0042593;
GO  GO:0005980;
GO  GO:0007626;
GO  GO:0010259;
GO  GO:0045818;
GO  GO:0035024;
GO  GO:0150099;
GO  GO:0035265;
GO  GO:0007200;
GO  GO:0007204;
GO  GO:0045819;
GO  GO:0001996;
GO  GO:0043410;
GO  GO:0001997;
GO  GO:0045907;
GO  GO:0008217;
GO  GO:0055117;
GO  GO:0001975;
GO  GO:0043627;
GO  GO:0009725;
GO  GO:0043278;
GO  GO:0048545;
GO  GO:0009410;
GO  GO:0001987;
GO  GO:0008542;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MNPDLDTGHNTSAPAHWGELKDDNFTGPNQTSSNSTLPQLDVTRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPT
SQ  NYFIVNLAIADLLLSFTVLPFSATLEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRR
SQ  KAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAG
SQ  VMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLF
SQ  STLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFMRILGCQCRGGRRRRRRRRLGACAYTYRPWTRGGSLERSQS
SQ  RKDSLDDSGSCMSGTQRTLPSASPSPGYLGRGTQPPVELCAFPEWKPGALLSLPEPPGRRGRLDSGPLFTFKLLGDPESP
SQ  GTEGDTSNGGCDTTTDLANGQPGFKSNMPLAPGHF
//
ID  Q96PN6;
PN  Adenylate cyclase type 10;
GN  ADCY10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:15659711}; Peripheral membrane protein {ECO:0000269|PubMed:15659711}; Cytoplasmic side {ECO:0000269|PubMed:15659711}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12475901, ECO:0000269|PubMed:15659711}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12475901, ECO:0000269|PubMed:15659711}. Nucleus {ECO:0000269|PubMed:12475901, ECO:0000269|PubMed:15659711}. Cell projection, cilium {ECO:0000269|PubMed:17591988}. Cytoplasm {ECO:0000269|PubMed:12475901}. Mitochondrion {ECO:0000269|PubMed:12475901}. Note=Distributed to subcellular compartments containing cAMP targets. Found as a plasma membrane-associated protein, protein concentrated in the perinuclear region and protein colocalized with actin or tubulin. {ECO:0000269|PubMed:12475901, ECO:0000269|PubMed:15659711}.
DR  UNIPROT: Q96PN6;
DR  UNIPROT: B4DZF0;
DR  UNIPROT: F5GWS5;
DR  UNIPROT: O95558;
DR  UNIPROT: Q5R329;
DR  UNIPROT: Q5R330;
DR  UNIPROT: Q8WXV4;
DR  UNIPROT: Q9NNX0;
DR  PDB: 4CLF;
DR  PDB: 4CLK;
DR  PDB: 4CLL;
DR  PDB: 4CLP;
DR  PDB: 4CLS;
DR  PDB: 4CLT;
DR  PDB: 4CLU;
DR  PDB: 4CLW;
DR  PDB: 4CLY;
DR  PDB: 4CLZ;
DR  PDB: 4CM0;
DR  PDB: 4CM2;
DR  PDB: 4OYA;
DR  PDB: 4OYB;
DR  PDB: 4OYI;
DR  PDB: 4OYM;
DR  PDB: 4OYO;
DR  PDB: 4OYP;
DR  PDB: 4OYW;
DR  PDB: 4OYX;
DR  PDB: 4OYZ;
DR  PDB: 4OZ2;
DR  PDB: 4OZ3;
DR  PDB: 4UST;
DR  PDB: 4USU;
DR  PDB: 4USV;
DR  PDB: 4USW;
DR  PDB: 5D0R;
DR  PDB: 5IV3;
DR  PDB: 5IV4;
DR  PDB: 7OVD;
DR  Pfam: PF00211;
DR  PROSITE: PS50125;
DR  OMIM: 143870;
DR  OMIM: 605205;
DR  DisGeNET: 55811;
DE  Function: Catalyzes the formation of the signaling molecule cAMP (PubMed:12609998, PubMed:15659711, PubMed:24616449, PubMed:25040695, PubMed:24567411). May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels (PubMed:15659711, PubMed:17591988). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP-responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (By similarity). Involved in ciliary beat regulation (PubMed:17591988). {ECO:0000250|UniProtKB:Q8C0T9, ECO:0000269|PubMed:15659711, ECO:0000269|PubMed:17591988, ECO:0000269|PubMed:24567411, ECO:0000269|PubMed:24616449, ECO:0000269|PubMed:25040695}.
DE  Disease: Hypercalciuria absorptive 2 (HCA2) [MIM:143870]: A common type of hypercalciuria, a condition characterized by excessive urinary calcium excretion. Absorptive hypercalciuria is due to gastrointestinal hyperabsorption of calcium and is a frequent cause of calcium oxalate nephrolithiasis. {ECO:0000269|PubMed:11932268}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P12270; IntAct: EBI-20930080; Score: 0.40
GO  GO:0016324;
GO  GO:0045178;
GO  GO:0005929;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005576;
GO  GO:0030426;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004016;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0071890;
GO  GO:0000287;
GO  GO:0030145;
GO  GO:0006171;
GO  GO:0071241;
GO  GO:0003351;
GO  GO:0035556;
GO  GO:0043065;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:15659711};
SQ  MNTPKEEFQDWPIVRIAAHLPDLIVYGHFSPERPFMDYFDGVLMFVDISGFTAMTEKFSSAMYMDRGAEQLVEILNYHIS
SQ  AIVEKVLIFGGDILKFAGDALLALWRVERKQLKNIITVVIKCSLEIHGLFETQEWEEGLDIRVKIGLAAGHISMLVFGDE
SQ  THSHFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIESVPDQRAVKVNFLKPPPNFNFDEFFTKCTTFMHYY
SQ  PSGEHKNLLRLACTLKPDPELEMSLQKYVMESILKQIDNKQLQGYLSELRPVTIVFVNLMFEDQDKAEEIGPAIQDAYMH
SQ  ITSVLKIFQGQINKVFMFDKGCSFLCVFGFPGEKVPDELTHALECAMDIFDFCSQVHKIQTVSIGVASGIVFCGIVGHTV
SQ  RHEYTVIGQKVNLAARMMMYYPGIVTCDSVTYNGSNLPAYFFKELPKKVMKGVADSGPLYQYWGRTEKVMFGMACLICNR
SQ  KEDYPLLGRNKEINYFMYTMKKFLISNSSQVLMYEGLPGYGKSQILMKIEYLAQGKNHRIIAISLNKISFHQTFYTIQMF
SQ  MANVLGLDTCKHYKERQTNLRNKVMTLLDEKFYCLLNDIFHVQFPISREISRMSTLKKQKQLEILFMKILKLIVKEERII
SQ  FIIDEAQFVDSTSWRFMEKLIRTLPIFIIMSLCPFVNIPCAAARAVIKNRNTTYIVIGAVQPNDISNKICLDLNVSCISK
SQ  ELDSYLGEGSCGIPFYCEELLKNLEHHEVLVFQQTESEEKTNRTWNNLFKYSIKLTEKLNMVTLHSDKESEEVCHLTSGV
SQ  RLKNLSPPTSLKEISLIQLDSMRLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKTLATLVESNIFYCFRNGKELQ
SQ  KALKQNDPSFEVHYRSLSLKPSEGMDHGEEEQLRELENEVIECHRIRFCNPMMQKTAYELWLKDQRKAMHLKCARFLEED
SQ  AHRCDHCRGRDFIPYHHFTVNIRLNALDMDAIKKMAMSHGFKTEEKLILSNSEIPETSAFFPENRSPEEIREKILNFFDH
SQ  VLTKMKTSDEDIIPLESCQCEEILEIVILPLAHHFLALGENDKALYYFLEIASAYLIFCDNYMAYMYLNEGQKLLKTLKK
SQ  DKSWSQTFESATFYSLKGEVCFNMGQIVLAKKMLRKALKLLNRIFPYNLISLFLHIHVEKNRHFHYVNRQAQESPPPGKK
SQ  RLAQLYRQTVCLSLLWRIYSYSYLFHCKYYAHLAVMMQMNTALETQNCFQIIKAYLDYSLYHHLAGYKGVWFKYEVMAME
SQ  HIFNLPLKGEGIEIVAYVAETLVFNKLIMGHLDLAIELGSRALQMWALLQNPNRHYQSLCRLSRCLLLNSRYPQLIQVLG
SQ  RLWELSVTQEHIFSKAFFYFVCLDILLYSGFVYRTFEECLEFIHQYENNRILKFHSGLLLGLYSSVAIWYARLQEWDNFY
SQ  KFSNRAKNLLPRRTMTLTYYDGISRYMEGQVLHLQKQIKEQSENAQASGEELLKNLENLVAQNTTGPVFCPRLYHLMAYV
SQ  CILMGDGQKCGLFLNTALRLSETQGNILEKCWLNMNKESWYSTSELKEDQWLQTILSLPSWEKIVAGRVNIQDLQKNKFL
SQ  MRANTVDNHF
//
ID  Q8C0T9;
PN  Adenylate cyclase type 10;
GN  Adcy10;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q96PN6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96PN6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12475901}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12475901}. Nucleus {ECO:0000269|PubMed:12475901}. Cell projection, cilium {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm {ECO:0000269|PubMed:12475901}. Mitochondrion {ECO:0000269|PubMed:12475901}. Note=Distributed to subcellular compartments containing cAMP targets. Found as a plasma membrane- associated protein, protein concentrated in the perinuclear region and protein colocalized with actin or tubulin. {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:12475901}.
DR  UNIPROT: Q8C0T9;
DR  UNIPROT: B2RRJ9;
DR  UNIPROT: Q3V0F8;
DR  Pfam: PF00211;
DR  PROSITE: PS50125;
DE  Function: Catalyzes the formation of the signaling molecule cAMP. May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels (By similarity). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP- responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (PubMed:14976244, PubMed:16054031). Involved in ciliary beat regulation (By similarity). {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:14976244, ECO:0000269|PubMed:16054031}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6UJY2; IntAct: EBI-15639120; Score: 0.52
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0030424;
GO  GO:0045178;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005576;
GO  GO:0030426;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0005739;
GO  GO:0031514;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004016;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0071890;
GO  GO:0000287;
GO  GO:0030145;
GO  GO:0006171;
GO  GO:0071241;
GO  GO:0003351;
GO  GO:0035556;
GO  GO:0043065;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q96PN6};
SQ  MSARRQELQDRAIVKIAAHLPDLIVYGDFSPERPSVKCFDGVLMFVDISGFTAMTEKFSTAMYMDRGAEQLVEILNYYIS
SQ  AIVEKVLIFGGDILKFAGDALLALWKVERKQLKNIITVVIKCSLEIHGLFEAKEAEEGLDIRVKIGLAAGHITMLVFGDE
SQ  TRNYFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIERIPDQRAVKVSFLKPPPTFNFDEFFTKCMGFMDYY
SQ  PSGDHKNFLRLACMLESDPELELSLQKYVMEIILKQIDDKQLRGYLSELRPVTIVFVNLMFKEQDKVEVIGSAIQAACVH
SQ  ITSVLKVFRGQINKVFMFDKGCSFLCVFGFPGEKAPDEITHALESAVDIFDFCSQVHKIRTVSIGVASGIVFCGIVGHTV
SQ  RHEYTVIGQKVNIAARMMMYYPGIVSCDSVTYDGSNLPAYFFKELPKKVMKGVADPGPVYQCLGLNEKVMFGMAYLICNR
SQ  YEGYPLLGRVREIDYFMSTMKDFLMTNCSRVLMYEGLPGYGKSQVLMEIEYLASQHENHRAVAIALTKISFHQNFYTIQI
SQ  LMANVLGLDTCKHYKERQTNLQNRVKTLLDEKFHCLLNDIFHVQFPVSREMSRMSKIRKQKQLEALFMKILAQTVREERI
SQ  IFIIDEAQFVDGTSWAFIEKLIRSMPIFIVMSLAPFSEVPCAAANAIMKNRNTTYITLGTMQPQEIRDKVCVDLSVSSIP
SQ  RELDSYLVEGSCGIPYYCEELLKNLDHHRVLLFQQAETEQKTNVTWNNMFKHSVRPTDDMQLFTSISEGQKEVCYLVSGV
SQ  RLNNLSPPASLKEISLVQLDSMSLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKALATLVESNVFNCFRSSKDLQ
SQ  LALKQNVPTFEVHYRSLALKLKEGLTYGEEEELREMEGEVVECRILRFCRPIMQKTAYELWLKDQKKVLHLKCARFLEES
SQ  AHRCNHCRNVDFIPYHHFIVDIRLNTLDMDTVKRMVTSQGFKIDEEEAIFSKSELPRKYKFPENLSITEIREKILHFFDN
SQ  VILKMKSSPNDIIPLESCQCKELLQIVILPLAQHFVALEENNKALYYFLELASAYLILGDNYNAYMYLGEGERLLKSLTN
SQ  EDSWSQTFEYATFYSLKAEVCFNMGQMVLAKKMLRKALKLLNRMFPCNLLTLTFQMHVEKNRLSHFMNQHTQEGSVPGKK
SQ  LAQLYLQASCFSLLWRIYSLNFFFHYKYYGHLAAMMEMNTSLETQNDFQIIKAYLDFSLYHHLAGYQGVWFKYEILVMEQ
SQ  LLNLPLKGEAIEIMAYTADTLGHIKFLMGHLDLAIELGSRAHRMWSLLRNPNKYQMVLCRLSKPLFLKSRYKHLVQVLGW
SQ  LWDLSVTEEDIFSKAFFYFVCLDIMLYSGFIYRTFEECLEFIHHNEDNRILKFQSGLLLGLYSCIAVWYARLQEWDNFNK
SQ  FSDRAKHLVTRRTPTVLYYEGISRYMEGQVLHLQKQIEEQAENAQDSGVEILKALETLVAQNTTGPVFYPRLYHLMAYVC
SQ  ILMGDGHSCDFFLNTALELSETHGNLLEKCWLSMSKEWWYSASELTGDQWLQTVLSLPSWDKIVSGKGGQRKRSWSWFCP
SQ  PNFSMVSWSQPQCA
//
ID  Q866F4;
PN  Adenylate cyclase type 10;
GN  ADCY10;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q96PN6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96PN6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PN6}. Nucleus {ECO:0000250|UniProtKB:Q96PN6}. Cell projection, cilium {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm {ECO:0000250|UniProtKB:Q96PN6}. Note=Distributed to subcellular compartments containing cAMP targets. Found as a plasma membrane- associated protein, protein concentrated in the perinuclear region and protein colocalized with actin or tubulin. {ECO:0000250|UniProtKB:Q96PN6}.
DR  UNIPROT: Q866F4;
DR  Pfam: PF00211;
DR  PROSITE: PS50125;
DE  Function: Catalyzes the formation of the signaling molecule cAMP. May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels (By similarity). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP- responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (By similarity). Involved in ciliary beat regulation (By similarity). {ECO:0000250|UniProtKB:Q8C0T9, ECO:0000250|UniProtKB:Q96PN6}.
DE  Reference Proteome: Yes;
GO  GO:0005929;
GO  GO:0005856;
GO  GO:0005576;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0004016;
GO  GO:0005524;
GO  GO:0071890;
GO  GO:0000287;
GO  GO:0006171;
GO  GO:0071241;
GO  GO:0003351;
GO  GO:0035556;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q96PN6};
SQ  MNTRKEELQDRAIVRIAAHLPDLIVYGDFSPQRPSVDYFDGVLMFVDISGFTAMTEKFSTAMYMDRGAEQLVEILNYYIS
SQ  AIVEKVLIFGGDILKFAGDALLALWKVERKQLKNIITVVIKCSLEIHGLFGTQESEEGLDIRVKIGLAAGHISMLVFGDE
SQ  TRNHFLVIGQAVDDVRLAQNMARMNDVILSPNCWQLCDRSMIEIERIPDQRAVKVNFLKPPPSFNFDEFFNKCMTFMDYY
SQ  PSGDHKNLLRLACMLESDPDLELSLQKYVMESILKQIDDKQLRGYLSELRPVTIVFVNLMFQDQNKAEVIGSAIQDACVH
SQ  ISSVLKVFRGQINKVFMFDKGCSFLCVFGFPGEKAPDEVTHALESAVDIFDFCSQVHKIHTVSIGVASGIVFCGIVGHTV
SQ  RHEYTVIGQKVNIAARMMMYYPGIVTCDSVTYNGSNLPPYFFKELPKKLMKGVGDSGPVYQCLGLNEKVMFGMAYLTCNR
SQ  NEGYPLLGRDKEIKYFMCTMKEFLMSNCSRVLMYEGLSGFGKSRILMEIEYLAQGENHRTIAIALTKVSFHQNFYTIQIL
SQ  MANVLGLDTCKHYKERQTNLQNKVKTLLDEKFHCLLNDIFHVQFPISREISKMSTFRKQKQLEALFMKILEQTVKEERII
SQ  FIIDEAQFVDYASWIFMEKLIRTVPIFIIMSLSPFTEIPCAAASAIMKNRNTTYVTLGAVQPNDIRNKVCLDLNVSSIPK
SQ  ELDLYLVEGSCGIPFYCEELVKNLDHHRVLVFQQMETEEKTKVTWNNLFKNFIKPTEEFKMSGLGNEEGTEEICKLASGV
SQ  RLKNLSPPASLKEISLVQLDSMSLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKALATLVESNIFDCFRDGKDLR
SQ  LALKQNAASFEVHNRSLSLQPTEGIAHGEEEELRELESEVIECHIIRFCKPMMQKTAYELWLKDQKKAMHLKCARFLEEN
SQ  AHRCDHCRSGDFIPYHHFTVDIRLNTLDMDTIKKMATSHGFETEEEIKISRAGIPKNSELFSENLSPEEIGERILGFFDV
SQ  ILTKMKTSKEDIIPLESCQCEEILEIVILPLAQHFLALGENNKALYYFLEITSAYLTLGDNYMAYMYLNEGERLLKTLKK
SQ  EKSWSQTFESATFYSLKGQVCFNMGQMVLAKKMLRKALKLLNRIFPYNLISLFLHTHMEKNRHFHYVTQQAQESSPPGKK
SQ  RLAHLYQQTACFSLLWQIYSLNYFFHHKYYGHLAAMMELNTALETQNDFQIIKAYLDYAMYHHLAGYQGVWFKYEVKAME
SQ  QIFNLPLKGEGIEIVAYVAGKLSYIKLMMGYLDLAIELGARAHKMWALLQNPNQHYVVLCRLSKSLFLKNRYKHLIQMLR
SQ  RLWDLSVAEGHIISKAFFYLVCLDIMLYSGFVYRTFEECLEFIIQNEDNRILKFQSGLLLGLYSSIAIWYGRLQEWDNFY
SQ  VFSNRAKTLVSRRTPTILYYDGVSRYMEGQVLQLQKQIEEQSETAQDSGVELLKSLESLVAQNTTGPVFYPRLYHLMAYI
SQ  CILMGDGQNCDLFLNTALKLSEIQGNVLEKCWLNMSKEWWYSNCTLTEDQWLHTILSLPAWEKIVSGKVNIHDVQKNKFL
SQ  MRVNILDNPF
//
ID  Q9Z286;
PN  Adenylate cyclase type 10;
GN  Adcy10;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q96PN6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96PN6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PN6}. Nucleus {ECO:0000269|PubMed:12475901}. Cell projection, cilium {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm {ECO:0000269|PubMed:9874775}. Mitochondrion {ECO:0000269|PubMed:12475901}. Note=Distributed to subcellular compartments containing cAMP targets. Found as a plasma membrane- associated protein, protein concentrated in the perinuclear region and protein colocalized with actin or tubulin. {ECO:0000250|UniProtKB:Q96PN6}.
DR  UNIPROT: Q9Z286;
DR  Pfam: PF00211;
DR  PROSITE: PS50125;
DE  Function: Catalyzes the formation of the signaling molecule cAMP (PubMed:9874775). May function as sensor that mediates responses to changes in cellular bicarbonate and CO(2) levels (By similarity). Has a critical role in mammalian spermatogenesis by producing the cAMP which regulates cAMP-responsive nuclear factors indispensable for sperm maturation in the epididymis. Induces capacitation, the maturational process that sperm undergo prior to fertilization (By similarity). Involved in ciliary beat regulation (By similarity). {ECO:0000250|UniProtKB:Q8C0T9, ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:9874775}.
DE  Reference Proteome: Yes;
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0030424;
GO  GO:0045178;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005576;
GO  GO:0030426;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0005739;
GO  GO:0031514;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004016;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0071890;
GO  GO:0000287;
GO  GO:0030145;
GO  GO:0006171;
GO  GO:0071241;
GO  GO:0003351;
GO  GO:0035556;
GO  GO:0043065;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q96PN6};
SQ  MSARRQELQDRAIVKIAAHLPDLIVYGDFSPERPSVKCFDGVLMFVDISGFTAMTEKFSTAMYMDRGAEQLVEILNYYIS
SQ  AIVEKVLIFGGDILKFAGDALLALWKVERKQLKNIITVVIKCSLEIHGLFEAKEVEEGLDIRVKIGLAAGHITMLVFGDE
SQ  TRNYFLVIGQAVDDVRLAQNMAQMNDVILSPNCWQLCDRSMIEIERIPDQRAVKVSFLKPPPTFNFDEFFAKCMAFMDYY
SQ  PSGDHKNFLRLACMLESDPELELSLQKYVMEIILKQIDDKQLRGYLSELRPVTIVFVNLMFKEQDKAEVIGSAIQAACVH
SQ  ITSVLKVFRGQINKVFMFDKGCSFLCVFGFPGEKAPDEITHALESAVDIFDFCSQVHKIRTVSIGVASGIVFCGIVGHTV
SQ  RHEYTVIGQKVNIAARMMMYYPGIVTCDSVTYDGSNLPAYFFKELPKKVMKGVADPGPVYQCLGLNEKVMFGMAYLICNR
SQ  YEGYPLLGRVREIDYFMSTMKDFLMTNCSRVLMYEGLPGYGKSQVLMEIEYLASQHENHRAVAIALTKISFHQNFYTIQI
SQ  LMANVLGLDTCKHYKERQTNLQNRVKTLLDDKYHCLLNDIFHVQFPVSREMSRMSKIRKQKQLEALFMKILEQTVREERI
SQ  IFIIDEAQFVDVASWAFIEKLIRSMPIFIVMSLCPFPETPCAAANAIMKNRNTTYITLGTMQPQEIRDKVCVDLSVSSIP
SQ  RELDSYLVEGSCGIPYYCEELLKNLDHHRILIFQQAEAEEKTNVTWNNLFKYSVKPTEDMYLYTSIAAGQKEACYLTSGV
SQ  RLKNLSPPASLKEISLVQLDSMSLSHQMLVRCAAIIGLTFTTELLFEILPCWNMKMMIKALATLVESNVFDCFRSSKDLQ
SQ  LALKQNVTTFEVHYRSLSLKSKEGLAYSEEEQLREMEGEVIECRILRFCRPIMQKTAYELWLKDQKKVLHLKCARFLEES
SQ  AHRCNHCRNRDFIPYHHFIADIRLNTLDMDTVKKMVKSHGFKTEDEVIFSKSEIPRKFKFPENISITETREKILHFFDNV
SQ  IIKMRTSQDDVIPLESCHCEELLQIVILPLAQHFVALEENNKALYYFLELASAYLILGDNYNAYMYLGEGERLLKSLTNE
SQ  DSWSQTFEYATFYSLKGEICFNMGQMVLAKKMLRKALKLLNRMFPCNLLSLTFQMHIEKNRLSHFMNQHTQEGSLPGKKL
SQ  AQLFLQSSCFSLLWKIYSLNFFFHYKYYGRLAAIMQMNTSLETQNNFQIIKAFLDFSLYRHLAGYEGVWFKYEILVMEQL
SQ  LNLPLKGEAFEIMAYAADALGHIKFLTGHLDLAIELGSRAHKMWSLLRNPNKYHMVLCRLSKPLFLKSRYKHLVQVLGWL
SQ  WDLSVTEEHIFSKAFFYFVCLDIMLYSGFIYRTFEECLEFIHHNEDNRILKFQSGLLLGLYSCIAVWYARLQEWDNFYKF
SQ  SNRAKTLVTRRTPTVLYYEGISRYMEGQVLHLQKQIEEQAENAQDSGVELLKALETLVAQNTTGPVFYPRLYHLMAYVCI
SQ  LMGDGHSCDFFLNTALELSETQGNLLEKCWLSMSKEWWYSAPELTGDQWLQTVLSLPSWDKIVSGNVTLQDVQKNKFLMR
SQ  VNILDNPF
//
ID  P24935;
PN  Adenovirus death protein;
GN  ADP;
OS  10515;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host nucleus membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:1448922}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:1448922}. Host Golgi apparatus membrane; Single- pass type I membrane protein {ECO:0000269|PubMed:1448922}. Note=Initially associates with the endoplasmic reticulum and Golgi apparatus and ultimately localizes to the nuclear membrane. {ECO:0000269|PubMed:1448922}.
DR  UNIPROT: P24935;
DR  Pfam: PF05393;
DE  Function: Promotes the release of progeny virus from the host cell nucleus by accelerating the lysis and death of the host cell. {ECO:0000269|PubMed:24198418}.
DE  Reference Proteome: Yes;
GO  GO:0044167;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0016021;
GO  GO:0044659;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTGSTIAPTTDYRNTTATGLTSALNLPQVHAFVNDWASLDMWWFSIALMFVCLIIMWLICCLKRRRARPPIYRPIIVLNP
SQ  HNEKIHRLDGLKPCSLLLQYD
//
ID  Q99222;
PN  ARF3-interacting protein 1;
GN  AFI1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Cytoplasm, cell cortex. Note=Enriched at the nuclear envelope and at the plasma membrane, especially in daughter cells and at the bud neck.
DR  UNIPROT: Q99222;
DR  UNIPROT: D6W2I7;
DR  UNIPROT: Q92274;
DR  Pfam: PF07792;
DR  PROSITE: PS50211;
DE  Function: Involved in actin patch polarization. Required for maintaining a proper budding pattern in yeast cells. Required for proper polarized localization of the ADP-ribosylation factor ARF3 at the plasma membrane. {ECO:0000269|PubMed:18397879}.
DE  Reference Proteome: Yes;
DE  Interaction: P53865; IntAct: EBI-1781812; Score: 0.55
DE  Interaction: P29366; IntAct: EBI-7365092; Score: 0.37
DE  Interaction: P11484; IntAct: EBI-3700856; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3732939; Score: 0.35
GO  GO:0005938;
GO  GO:0005935;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0051666;
GO  GO:0000282;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLRRELNNSISNRSIENESFPFERPNVSYIISAEFDNKLGPILKHQYPKDIPGFNQFSHEQRNGNTSVSMNLASLMIPSS
SQ  IERNPGKQDITVFTLYYNKFTQNYQLFPVPKDPRFSFNLHHREQSDGSVTNSIYYDAENHQDAKNNRYTIVLEDDELECQ
SQ  EVQNNQKAIDNEPLFFINVANTVLDTTNDRGAVIKSIAIGTPLKTFFAFKNIIVLVLDLYMKAPTQAAATDILLDCFNML
SQ  NSIDLTLINDIHSKSSIQEVLHSIHDESIITKVFLDPDSTLKKLFCINGFDTKDKYGNIVTFHDQLIQYHFTRFQPKTLP
SQ  PFLLKIPLQFNMIRREPIYIENDYNELVLKFLDKFVPYLLKAGQKVNAWKLVINSTKLSKEDLCAFILSLANITATYASD
SQ  PQSYFKGNAALIFPYMDISLVDGLRAYVASNSDFVGCFAIIGTANPIFRYQLDIWDYYYDVDEGVFYENNSPEKEKPDTV
SQ  AEVKIGPNPLRKIFNRPHFSTNAVNESQVNLGQKLFSLLIDEYHDSDTIMSVLRRLNVLQLENLLDALKRREIPPNIALK
SQ  DEYIMFYKDFFIFPEFFDYFTLHSIELLSNLDNCLFSLGNTCQLFSTEQIYSQLSQILDIVKELFRMVSVSRTNIEKFLN
SQ  ACLNYSPFKILPTAQLHGDNISRWSFESEVRQGFDNFNSYMGIEKDPHGVIVSAIDLFTQIYSFDILAFFLTFITKESGQ
SQ  DLPFTKSLSRRRTYLTRIAQSSSLRQFLQLSTRPNIRILGGNGQGTGNSNYPEFTNASSVISPKLRASPLLERRASKICY
SQ  AITKLLYRLECHPIGMALLKKYLHNQLREAYLESKRHFISKKGDSTNTSSTIASSSFAGASVPLSSNESGMLNGLKQINE
SQ  QQESTLETTQKED
//
ID  Q6ULP2;
PN  Aftiphilin;
GN  AFTPH;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:15758025}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15758025}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15758025}. Note=Co-localizes with AP1G1/AP- 1 in the cytoplasm (PubMed:14665628, PubMed:15758025). Recruited to the perinuclear region by AP1G1/AP-1 (PubMed:15758025). {ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:15758025}.
DR  UNIPROT: Q6ULP2;
DR  UNIPROT: D6W5E9;
DR  UNIPROT: Q6ZM66;
DR  UNIPROT: Q86VW3;
DR  UNIPROT: Q8TCF3;
DR  UNIPROT: Q9H7E3;
DR  UNIPROT: Q9HAB9;
DR  UNIPROT: Q9NXS4;
DR  Pfam: PF15045;
DR  OMIM: 619628;
DR  DisGeNET: 54812;
DE  Function: Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269|PubMed:15758025}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8ZJ79; IntAct: EBI-2848711; Score: 0.00
DE  Interaction: A0A380PPP8; IntAct: EBI-2876267; Score: 0.00
DE  Interaction: A0A3N4B631; IntAct: EBI-2876260; Score: 0.00
DE  Interaction: P51692; IntAct: EBI-3940316; Score: 0.37
DE  Interaction: Q05086; IntAct: EBI-7412469; Score: 0.37
DE  Interaction: P41241; IntAct: EBI-11013851; Score: 0.35
DE  Interaction: P56377; IntAct: EBI-11037753; Score: 0.53
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-21550215; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9Y6Q5; IntAct: EBI-21760726; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-30816846; Score: 0.44
DE  Interaction: Q9H492; IntAct: EBI-30829101; Score: 0.44
DE  Interaction: Q9GZQ8; IntAct: EBI-30831123; Score: 0.44
DE  Interaction: O75381; IntAct: EBI-30835687; Score: 0.44
DE  Interaction: Q6ZMQ8; IntAct: EBI-32723474; Score: 0.27
GO  GO:0030121;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0032588;
GO  GO:0030276;
GO  GO:0046907;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEPDIIRMYSSSPPPLDNGAEDDDDDEFGEFGGFSEVSPSGVGFVDFDTPDYTRPKEEFVPSNHFMPIHEFSENVDSLTS
SQ  FKSIKNGNDKDITAELSAPVKGQSDVLLSTTSKEIISSEMLATSIDGMERPGNLNKVVEQRQNVGTLESFSPGDFRTNMN
SQ  VVHQNKQLESCNGEKPPCLEILTNGFAVLETVNPQGTDDLDNVADSKGRKPLSTHSTEYNLDSVPSPAEEFADFATFSKK
SQ  ERIQLEEIECAVLNDREALTIRENNKINRVNELNSVKEVALGRSLDNKGDTDGEDQVCVSEISIVTNRGFSVEKQGLPTL
SQ  QQDEFLQSGVQSKAWSLVDSADNSEAIRREQCKTEEKLDLLTSKCAHLCMDSVKTSDDEVGSPKEESRKFTNFQSPNIDP
SQ  TEENDLDDSLSVKNGDSSNDFVTCNDINEDDFGDFGDFGSASGSTPPFVTGTQDSMSDATFEESSEHFPHFSEPGDDFGE
SQ  FGDINAVSCQEETILTKSDLKQTSDNLSEECQLARKSSGTGTEPVAKLKNGQEGEIGHFDSVPNIQDDCNGFQDSDDFAD
SQ  FSSAGPSQVVDWNAFEDEQKDSCSWAAFGDQQATESHHRKEAWQSHRTDENIDTPGTPKTHSVPSATSKGAVASGHLQES
SQ  ATSVQTALLNRLERIFEACFPSILVPDAEEEVTSLKHLLETSTLPIKTREALPESGELLDVWTELQDIHDAHGLRYQWGG
SQ  SHSNKKLLSSLGIDTRNILFTGNKKQPVIVPMYAAGLGMLEPTKEPLKPLSAAEKIASIGQTATMSPDMNTCTSDQFQES
SQ  LPPVQFDWSSSGLTNPLDASGGSTLLNLDFFGPVDDSSSSSSTTIPGVDPELYELTTSKLEISTSSLKVTDAFARLMSTV
SQ  EKTSTSTRKPKREEHLSEEAIKVIAGLPDLTFMHAKVLMFPATLTPSTSSQEKADG
//
ID  Q80WT5;
PN  Aftiphilin;
GN  Aftph;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q6ULP2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6ULP2}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q6ULP2}. Note=Co-localizes with AP1G1/AP-1 in the cytoplasm (By similarity). Recruited to the perinuclear region by AP1G1/AP-1 (By similarity). {ECO:0000250|UniProtKB:Q6ULP2}.
DR  UNIPROT: Q80WT5;
DR  UNIPROT: Q5SSE6;
DR  UNIPROT: Q99KJ1;
DR  Pfam: PF15045;
DE  Function: Component of clathrin-coated vesicles (By similarity). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (By similarity). {ECO:0000250|UniProtKB:Q6ULP2}.
DE  Reference Proteome: Yes;
DE  Interaction: P18484; IntAct: EBI-7578021; Score: 0.52
DE  Interaction: Q9R0Z7; IntAct: EBI-7578129; Score: 0.56
DE  Interaction: P52303; IntAct: EBI-7578394; Score: 0.40
GO  GO:0030121;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0032588;
GO  GO:0030276;
GO  GO:0046907;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEPDIIRMYSSSPPPLDNGAEDDEEDEFGEFGGFSEVSPSGVGFVDFDTPDYTRPKEDFVPSNHFMPIHEYSEDVDSLTS
SQ  FKSVQNGNDKDITAELSTPVKSQSDVVLSTTSKEMIPSKTLDPSIDGMESLEDLDKVVVQGPSTGQLRSFSPGDFRTDKN
SQ  IVHQTKQLESCNGEKPPCLEILTNGFAGLETVNPQGTDDLDNVADSKGSKPLNTCGTECILESAASHATEFADFSTFSQT
SQ  ERTQLEEIECPVLNDGDTLTIQGNSKGPRVKELNCVKEVTLDGSFEDTGNTEREHQVCVSEIHAVADRGLSVEKQDLQTL
SQ  QQDEFLNSRIQSEAWSLVDSSENSEAITKERCKMEKNDLFASKCADLSMDSVKTSDVNEIGSSKEENRKLTNPKSPDPDP
SQ  TGQNALDDSAASMKNGDSGNGFVTCHDTNEDDFGDFGTANGTTPPFVTSTQDSMSDVTFEDSSEHFLHLSEPGDDFGEFE
SQ  DTNAVSCQEEMRFTESDLRQTSDGLSEECPLAGESGGKDSKPDSKLKNGQDSEFGDFDSVPNTQGSAFQDSDDFADFSSA
SQ  GPSQAVDWNAFEDEQKDGCSWAAFGDQQETESHHLKEVWQSQRTDETMGTLGTPKMHSVSSAASKGAVASGHLQEPGTSV
SQ  QTALLNRLERIFEACFPSVFVPDVEEEVSSLKHLLETHSSPAKTREALADRGELRGVWTELQDIHDAHGLRYQWGGSHSN
SQ  KKLLCSLGIDTRNILFTGNKKQPVIVPMYAAGLGMLEPTKEPLKPLSAAEKIASIGQTTVMTPEINTCTSDPFQESLPPV
SQ  QFDWSSSGLTNPLDASGGSTLLNLDFFGPVDDSSSSSSTIPGVDPELYELTTAKLETSTSSLRVTDAFAKLMSTVEKTST
SQ  STRKPKREEHLSEEAMKVIASLPDLTFMHAKVLMFPATLTPSMSSQEQADA
//
ID  P14998;
PN  Agnoprotein;
GN  AGNO;
OS  10631;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host cytoplasm {ECO:0000305}. Host nucleus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host rough endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Mostly perinuclear. {ECO:0000250}.
DR  UNIPROT: P14998;
DR  Pfam: PF01736;
DE  Function: Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0044169;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0003677;
GO  GO:0005216;
GO  GO:0039707;
GO  GO:0051259;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFCEPKNLVVLRQLSRQASVKVGKTWTGTKKRAQRIFIFILELLLEFCRGEDSVDGKNKSTTALPAVKDSVKDS
//
ID  P03085;
PN  Agnoprotein;
GN  AGNO;
OS  1891762;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host cytoplasm {ECO:0000305}. Host nucleus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host rough endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Mostly perinuclear. {ECO:0000250}.
DR  UNIPROT: P03085;
DR  Pfam: PF01736;
DE  Function: Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0044169;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0003677;
GO  GO:0005216;
GO  GO:0039707;
GO  GO:0051259;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVLRQLSRQASVKVGKTWTGTKKRAQRIFIFILELLLEFCRGEDSVDGKNKSTTALPAVKDSVKDS
//
ID  P03086;
PN  Agnoprotein;
GN  AGNO;
OS  10632;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host cytoplasm {ECO:0000305}. Host nucleus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host rough endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Mostly perinuclear. {ECO:0000269|PubMed:11517407, ECO:0000269|PubMed:15864296, ECO:0000269|PubMed:20300659}.
DR  UNIPROT: P03086;
DR  PDB: 2MJ2;
DR  PDB: 5NHQ;
DR  Pfam: PF01736;
DE  Function: Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins. {ECO:0000269|PubMed:11517407, ECO:0000269|PubMed:12165856, ECO:0000269|PubMed:20300659}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0044169;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0003677;
GO  GO:0005216;
GO  GO:0039707;
GO  GO:0051259;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVLRQLSRKASVKVSKTWSGTKKRAQRILIFLLEFLLDFCTGEDSVDGKKRQRHSGLTEQTYSALPEPKAT
//
ID  Q3L6L9;
PN  Agnoprotein;
GN  AGNO;
OS  557605;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host cytoplasm {ECO:0000305}. Host nucleus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host rough endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Mostly perinuclear. {ECO:0000250}.
DR  UNIPROT: Q3L6L9;
DR  UNIPROT: Q1W5X4;
DR  Pfam: PF01736;
DE  Function: Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0044169;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0003677;
GO  GO:0005216;
GO  GO:0039707;
GO  GO:0051259;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVLRQLSRQASVKVGKTWTGTKRRAQRIFIFILELLLDFCRGEDSVDGKKKKDSLTDKTETVTEKKES
//
ID  P03084;
PN  Agnoprotein;
GN  AGNO;
OS  1891767;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host cytoplasm {ECO:0000305}. Host nucleus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host rough endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Mostly perinuclear. {ECO:0000269|PubMed:6296448}.
DR  UNIPROT: P03084;
DR  Pfam: PF01736;
DE  Function: Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:3023658, ECO:0000269|PubMed:3023661, ECO:0000269|PubMed:6286139}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0044169;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0003677;
GO  GO:0005216;
GO  GO:0039707;
GO  GO:0051259;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVLRRLSRQASVKVRRSWTESKKTAQRLFVFVLELLLQFCEGEDTVDGKRKKPERLTEKPES
//
ID  O95831;
PN  Apoptosis-inducing factor 1, mitochondrial;
GN  AIFM1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion intermembrane space {ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:26004228}. Mitochondrion inner membrane. Cytoplasm {ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:33168626}. Nucleus {ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:33168626}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17094969}. Note=Proteolytic cleavage during or just after translocation into the mitochondrial intermembrane space (IMS) results in the formation of an inner-membrane-anchored mature form (AIFmit). During apoptosis, further proteolytic processing leads to a mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis (PubMed:15775970). Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (By similarity). Translocation into the nucleus is promoted by interaction with (auto- poly-ADP-ribosylated) processed form of PARP1 (PubMed:33168626). Colocalizes with EIF3G in the nucleus and perinuclear region (PubMed:17094969). {ECO:0000250|UniProtKB:Q9Z0X1, ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:33168626}. [Isoform 3]: Mitochondrion intermembrane space {ECO:0000269|PubMed:20111043}. Mitochondrion inner membrane {ECO:0000269|PubMed:20111043}. Note=Has a stronger membrane anchorage than isoform 1. {ECO:0000269|PubMed:20111043}. [Isoform 4]: Mitochondrion {ECO:0000269|PubMed:16644725}. Cytoplasm, cytosol {ECO:0000269|PubMed:16644725}. Note=In pro-apoptotic conditions, is released from mitochondria to cytosol in a calpain/cathepsin-dependent manner. {ECO:0000269|PubMed:16644725}. [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:16365034}.
DR  UNIPROT: O95831;
DR  UNIPROT: A4QPB4;
DR  UNIPROT: B1ALN1;
DR  UNIPROT: B2RB08;
DR  UNIPROT: D3DTE9;
DR  UNIPROT: E9PRR0;
DR  UNIPROT: Q1L6K4;
DR  UNIPROT: Q1L6K6;
DR  UNIPROT: Q2QKE4;
DR  UNIPROT: Q5JUZ7;
DR  UNIPROT: Q6I9X6;
DR  UNIPROT: Q9Y3I3;
DR  UNIPROT: Q9Y3I4;
DR  PDB: 1M6I;
DR  PDB: 4BUR;
DR  PDB: 4BV6;
DR  PDB: 4FDC;
DR  PDB: 4LII;
DR  PDB: 5FMH;
DR  PDB: 5FS6;
DR  PDB: 5FS7;
DR  PDB: 5FS8;
DR  PDB: 5FS9;
DR  PDB: 5KVH;
DR  PDB: 5KVI;
DR  Pfam: PF14721;
DR  Pfam: PF07992;
DR  OMIM: 300169;
DR  OMIM: 300232;
DR  OMIM: 300614;
DR  OMIM: 300816;
DR  OMIM: 310490;
DR  DisGeNET: 9131;
DE  Function: Functions both as NADH oxidoreductase and as regulator of apoptosis (PubMed:20362274, PubMed:23217327, PubMed:17094969, PubMed:33168626). In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase- independent pathway (PubMed:20362274). Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (By similarity). The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA (PubMed:20362274). Binds to DNA in a sequence-independent manner (PubMed:27178839). Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis (PubMed:17094969). Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells (PubMed:19418225). In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (PubMed:26004228). {ECO:0000250|UniProtKB:Q9Z0X1, ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:19418225, ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:26004228, ECO:0000269|PubMed:27178839, ECO:0000269|PubMed:33168626}. [Isoform 4]: Has NADH oxidoreductase activity. Does not induce nuclear apoptosis. {ECO:0000269|PubMed:16644725}. [Isoform 5]: Pro-apoptotic isoform. {ECO:0000269|PubMed:16365034}.
DE  Disease: Combined oxidative phosphorylation deficiency 6 (COXPD6) [MIM:300816]: A mitochondrial disease resulting in a neurodegenerative disorder characterized by psychomotor delay, hypotonia, areflexia, muscle weakness and wasting. Some patients manifest prenatal ventriculomegaly and severe postnatal encephalomyopathy. {ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:22019070, ECO:0000269|PubMed:25583628, ECO:0000269|PubMed:26004228, ECO:0000269|PubMed:26173962, ECO:0000269|PubMed:27178839}. Note=The disease is caused by variants affecting the gene represented in this entry. Charcot-Marie-Tooth disease, X-linked recessive, 4, with or without cerebellar ataxia (CMTX4) [MIM:310490]: A neuromuscular disorder characterized by progressive sensorimotor axonal neuropathy, distal sensory impairment, difficulty walking due to peripheral neuropathy and/or cerebellar ataxia, and deafness due to auditory neuropathy. Additional features include cognitive impairment, cerebellar atrophy, dysarthria, abnormal extraocular movements, tremor, dysmetria and spasticity. The age at onset ranges from infancy to young adulthood. {ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:26004228}. Note=The disease is caused by variants affecting the gene represented in this entry. Deafness, X-linked, 5, with peripheral neuropathy (DFNX5) [MIM:300614]: A form of hearing loss characterized by absent or severely abnormal auditory brainstem response, abnormal middle ear reflexes, abnormal speech discrimination, loss of outer hair cell function, and cochlear nerve hypoplasia. DFNX5 patients manifest auditory neuropathy with childhood onset, associated with distal sensory impairment affecting the peripheral nervous system. {ECO:0000269|PubMed:25986071}. Note=The disease is caused by variants affecting the gene represented in this entry. Spondyloepimetaphyseal dysplasia, X-linked, with hypomyelinating leukodystrophy (SEMDHL) [MIM:300232]: An X-linked recessive developmental disorder characterized by slowly progressive skeletal and neurologic abnormalities, including short stature, large and deformed joints, significant motor impairment, visual defects, and sometimes cognitive deficits. Affected individuals typically have normal early development in the first year or so of life, followed by development regression and the development of symptoms. Brain imaging shows white matter abnormalities consistent with hypomyelinating leukodystrophy. {ECO:0000269|PubMed:28842795}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O00165; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: O15027; IntAct: EBI-16786589; Score: 0.42
DE  Interaction: O75821; IntAct: EBI-7083391; Score: 0.60
DE  Interaction: P08107; IntAct: EBI-7947560; Score: 0.54
DE  Interaction: Q13233; IntAct: EBI-361788; Score: 0.00
DE  Interaction: Q99759; IntAct: EBI-362055; Score: 0.00
DE  Interaction: Q00653; IntAct: EBI-362688; Score: 0.00
DE  Interaction: Q04206; IntAct: EBI-363205; Score: 0.00
DE  Interaction: Q9Y572; IntAct: EBI-363715; Score: 0.00
DE  Interaction: P20333; IntAct: EBI-364540; Score: 0.00
DE  Interaction: Q15628; IntAct: EBI-364813; Score: 0.00
DE  Interaction: Q9NX70; IntAct: EBI-394875; Score: 0.35
DE  Interaction: Q15047; IntAct: EBI-732770; Score: 0.00
DE  Interaction: O76061; IntAct: EBI-732773; Score: 0.00
DE  Interaction: Q8NC60; IntAct: EBI-737306; Score: 0.00
DE  Interaction: Q8IX03; IntAct: EBI-737309; Score: 0.00
DE  Interaction: Q9Y3Q8; IntAct: EBI-946353; Score: 0.51
DE  Interaction: O75365; IntAct: EBI-1060356; Score: 0.00
DE  Interaction: Q15773; IntAct: EBI-16786283; Score: 0.60
DE  Interaction: Q9HAW0; IntAct: EBI-1070570; Score: 0.00
DE  Interaction: Q9BRX2; IntAct: EBI-1071657; Score: 0.00
DE  Interaction: Q92956; IntAct: EBI-1075816; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1077732; Score: 0.00
DE  Interaction: Q9BUV8; IntAct: EBI-1083497; Score: 0.00
DE  Interaction: O95831; IntAct: EBI-5651205; Score: 0.40
DE  Interaction: P13569; IntAct: EBI-1170380; Score: 0.35
DE  Interaction: P83887; IntAct: EBI-2561869; Score: 0.40
DE  Interaction: P16104; IntAct: EBI-2564373; Score: 0.35
DE  Interaction: Q8N0X7; IntAct: EBI-2643801; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-2878124; Score: 0.35
DE  Interaction: P40692; IntAct: EBI-2932395; Score: 0.37
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-3045543; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-3050465; Score: 0.35
DE  Interaction: Q14197; IntAct: EBI-7825470; Score: 0.35
DE  Interaction: Q96HA7; IntAct: EBI-8522027; Score: 0.35
DE  Interaction: P62937; IntAct: EBI-4533343; Score: 0.46
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: Q8JPQ9; IntAct: EBI-6159460; Score: 0.35
DE  Interaction: Q63ZY3; IntAct: EBI-6223407; Score: 0.60
DE  Interaction: O95747; IntAct: EBI-6255369; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-6256400; Score: 0.53
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q93034; IntAct: EBI-21331078; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: P21860; IntAct: EBI-8770321; Score: 0.57
DE  Interaction: Q96KQ7; IntAct: EBI-8832899; Score: 0.35
DE  Interaction: Q96JM2; IntAct: EBI-8837110; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.53
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: O75807; IntAct: EBI-9976880; Score: 0.35
DE  Interaction: P10398; IntAct: EBI-10101513; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-10103481; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770028; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-11322719; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: O43920; IntAct: EBI-10762907; Score: 0.57
DE  Interaction: P03220; IntAct: EBI-11722152; Score: 0.35
DE  Interaction: P03225; IntAct: EBI-11722220; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P0CK49; IntAct: EBI-11725356; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: Q2MG95; IntAct: EBI-11733653; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-11155257; Score: 0.35
DE  Interaction: Q5JTV8; IntAct: EBI-11159793; Score: 0.53
DE  Interaction: Q96NL6; IntAct: EBI-11376636; Score: 0.27
DE  Interaction: O94905; IntAct: EBI-11425731; Score: 0.35
DE  Interaction: Q13509; IntAct: EBI-11897134; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-11897791; Score: 0.35
DE  Interaction: O14829; IntAct: EBI-14023711; Score: 0.35
DE  Interaction: Q05322; IntAct: EBI-16214737; Score: 0.35
DE  Interaction: Q400G9; IntAct: EBI-21768785; Score: 0.35
DE  Interaction: O95470; IntAct: EBI-21820286; Score: 0.35
DE  Interaction: Q05209; IntAct: EBI-21820311; Score: 0.35
DE  Interaction: Q8NI37; IntAct: EBI-21820367; Score: 0.35
DE  Interaction: Q8WY91; IntAct: EBI-21820422; Score: 0.35
DE  Interaction: Q9HAS0; IntAct: EBI-21820465; Score: 0.35
DE  Interaction: Q6UXV4; IntAct: EBI-21859075; Score: 0.35
DE  Interaction: Q9BV35; IntAct: EBI-21859075; Score: 0.35
DE  Interaction: Q6JQN1; IntAct: EBI-21859075; Score: 0.35
DE  Interaction: Q658Y4; IntAct: EBI-21859075; Score: 0.35
DE  Interaction: Q08357; IntAct: EBI-21859075; Score: 0.35
DE  Interaction: P55789; IntAct: EBI-21859075; Score: 0.35
DE  Interaction: P54819; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: P24468; IntAct: EBI-21859075; Score: 0.35
DE  Interaction: Q9UID3; IntAct: EBI-16150241; Score: 0.35
DE  Interaction: P36405; IntAct: EBI-16180991; Score: 0.35
DE  Interaction: O43615; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q8IXI1; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q7Z434; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P00403; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: O75431; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9Y3D9; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9NVH1; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q9BYN8; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q99618; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q96EY7; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q8N4Q1; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q16891; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q16775; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q13011; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q02952; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P82650; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P50454; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P36542; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: P31689; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P18085; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P16615; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P13804; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O95721; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O76031; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: O75683; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: A8MXV4; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9Y5L4; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q9Y5J9; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q9Y512; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q9Y4W6; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9Y2W6; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9Y2S7; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q9Y2Q9; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9ULX6; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9UJS0; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9P0J0; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q9P032; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9NX63; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9NX40; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9NX14; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9NVI7; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9NSE4; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q9NS69; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9NPL8; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9H845; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9H078; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q9BW72; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9BSH4; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q9BPX6; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q99714; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q96TA2; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q96EX1; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q96EL2; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q96E52; IntAct: EBI-16786283; Score: 0.41
DE  Interaction: Q96C36; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q96C01; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q96BR5; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q96A73; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q92667; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q92665; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q8IYU8; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q8IUX1; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q86TX2; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q7L0Y3; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q7KZN9; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q70CQ3; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q6UB35; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q6KCM7; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q6DKK2; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q5TC12; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q5T9A4; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q5JTJ3; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q4VC31; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q49B96; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q3ZCQ8; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q16795; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q16740; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q16718; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q14249; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q14061; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q12849; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q04837; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P99999; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P83111; IntAct: EBI-16786283; Score: 0.41
DE  Interaction: P62072; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P61088; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P56381; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P56277; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P53701; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P51970; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: P49821; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P49753; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P48047; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P46199; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P38117; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P36957; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P36551; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P35232; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P34897; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P32322; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P31930; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P31040; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P30405; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P28331; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P25705; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P24539; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P22695; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P20674; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P19404; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P19367; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P18859; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P14854; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: P13073; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P10606; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P10599; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: P09669; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P08574; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P07919; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P06576; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P05023; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P00367; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O96008; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: O96000; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O95202; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O94925; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O94826; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O75964; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O75947; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O75746; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O75616; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: O75489; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O75380; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O75306; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O60313; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O60220; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: O43819; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: O43715; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O43464; IntAct: EBI-16786283; Score: 0.41
DE  Interaction: O00429; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: O00217; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: Q69YU5; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P27694; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: P35244; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: P15927; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: Q9BSD7; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: Q96HS1; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: Q6PI48; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: Q10713; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: P49411; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: P18887; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: P0DMV8; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: P00374; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: O43813; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: P45880; IntAct: EBI-16786589; Score: 0.35
DE  Interaction: Q02539; IntAct: EBI-16786761; Score: 0.27
DE  Interaction: P53004; IntAct: EBI-16786761; Score: 0.27
DE  Interaction: Q9HAV7; IntAct: EBI-16786761; Score: 0.27
DE  Interaction: Q9H0I3; IntAct: EBI-16786761; Score: 0.27
DE  Interaction: Q92522; IntAct: EBI-16786761; Score: 0.27
DE  Interaction: P83881; IntAct: EBI-16786761; Score: 0.27
DE  Interaction: P61604; IntAct: EBI-16786761; Score: 0.27
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-20307233; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-20307902; Score: 0.35
DE  Interaction: Q9UI95; IntAct: EBI-20219138; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: Q8IYE1; IntAct: EBI-20902736; Score: 0.40
DE  Interaction: Q9HCD5; IntAct: EBI-20905384; Score: 0.40
DE  Interaction: O75311; IntAct: EBI-20905664; Score: 0.40
DE  Interaction: P08621; IntAct: EBI-20907472; Score: 0.40
DE  Interaction: Q86X27; IntAct: EBI-20908104; Score: 0.40
DE  Interaction: Q9Y6X8; IntAct: EBI-20910808; Score: 0.40
DE  Interaction: Q9H2G2; IntAct: EBI-20932552; Score: 0.40
DE  Interaction: Q13061; IntAct: EBI-20932784; Score: 0.40
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q9BZR8; IntAct: EBI-21258469; Score: 0.35
DE  Interaction: Q8IY21; IntAct: EBI-21259607; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21132308; Score: 0.35
DE  Interaction: O60260; IntAct: EBI-21135687; Score: 0.35
DE  Interaction: Q13153; IntAct: EBI-25379067; Score: 0.35
DE  Interaction: P05129; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: Q05513; IntAct: EBI-25380056; Score: 0.35
DE  Interaction: Q13322; IntAct: EBI-25382050; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-25382473; Score: 0.35
DE  Interaction: Q13547; IntAct: EBI-25394148; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.61
DE  Interaction: C3W5S0; IntAct: EBI-26452157; Score: 0.35
DE  Interaction: P15659; IntAct: EBI-26452167; Score: 0.35
DE  Interaction: Q6DNN3; IntAct: EBI-25773258; Score: 0.35
DE  Interaction: Q6DNT7; IntAct: EBI-25773258; Score: 0.35
DE  Interaction: Q8TB24; IntAct: EBI-26518569; Score: 0.35
DE  Interaction: Q6ZNK6; IntAct: EBI-26453464; Score: 0.35
DE  Interaction: O60303; IntAct: EBI-26582514; Score: 0.35
DE  Interaction: P34972; IntAct: EBI-26880846; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27049069; Score: 0.27
DE  Interaction: Q96LU5; IntAct: EBI-27049466; Score: 0.27
DE  Interaction: Q9H300; IntAct: EBI-27049982; Score: 0.27
DE  Interaction: Q8N488; IntAct: EBI-27111302; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: A4FU01; IntAct: EBI-27113520; Score: 0.35
DE  Interaction: Q99952; IntAct: EBI-27114698; Score: 0.35
DE  Interaction: Q9Y603; IntAct: EBI-29000341; Score: 0.35
DE  Interaction: P41162; IntAct: EBI-29000231; Score: 0.35
DE  Interaction: P48742; IntAct: EBI-29000712; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
DE  Interaction: Q86V87; IntAct: EBI-34575191; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005743;
GO  GO:0005758;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003677;
GO  GO:0071949;
GO  GO:0016174;
GO  GO:0003954;
GO  GO:0016651;
GO  GO:0072572;
GO  GO:0046983;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:1904045;
GO  GO:0071392;
GO  GO:0070301;
GO  GO:0071732;
GO  GO:0090650;
GO  GO:0030261;
GO  GO:0070059;
GO  GO:0033108;
GO  GO:0032981;
GO  GO:0051402;
GO  GO:0030182;
GO  GO:0043065;
GO  GO:0060545;
GO  GO:0043525;
GO  GO:0012501;
GO  GO:0045041;
GO  GO:1902510;
GO  GO:0002931;
GO  GO:1902065;
GO  GO:0009636;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRCGGLAAGALKQKLVPLVRTVCVRSPRQRNRLPGNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLSTVGA
SQ  GAYAYKTMKEDEKRYNERISGLGLTPEQKQKKAALSASEGEEVPQDKAPSHVPFLLIGGGTAAFAAARSIRARDPGARVL
SQ  IVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRD
SQ  NMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALG
SQ  RKARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVAAVGL
SQ  EPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQS
SQ  MFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSTPAVPQAPVQGEDY
SQ  GKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED
//
ID  Q9Z0X1;
PN  Apoptosis-inducing factor 1, mitochondrial;
GN  Aifm1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion intermembrane space {ECO:0000269|PubMed:9989411}. Mitochondrion inner membrane {ECO:0000269|PubMed:30830864}. Cytoplasm {ECO:0000269|PubMed:21467298}. Nucleus {ECO:0000269|PubMed:12114629}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95831}. Note=Proteolytic cleavage during or just after translocation into the mitochondrial intermembrane space (IMS) results in the formation of an inner-membrane-anchored mature form (AIFmit) (By similarity). During apoptosis, further proteolytic processing leads to a mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol) (By similarity). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis (PubMed:12114629). Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (PubMed:21467298). Translocation into the nucleus is promoted by interaction with (auto-poly-ADP-ribosylated) processed form of PARP1 (By similarity). Colocalizes with EIF3G in the nucleus and perinuclear region. {ECO:0000250|UniProtKB:O95831, ECO:0000269|PubMed:12114629}. [Isoform 2]: Mitochondrion {ECO:0000269|PubMed:16644725}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O95831}. Note=In pro-apoptotic conditions, is released from mitochondria to cytosol in a calpain/cathepsin-dependent manner. {ECO:0000250|UniProtKB:O95831}.
DR  UNIPROT: Q9Z0X1;
DR  UNIPROT: Q1L6K5;
DR  PDB: 1GV4;
DR  PDB: 3GD3;
DR  PDB: 3GD4;
DR  PDB: 5MIU;
DR  PDB: 5MIV;
DR  Pfam: PF14721;
DR  Pfam: PF07992;
DE  Function: Functions both as NADH oxidoreductase and as regulator of apoptosis (By similarity). In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway (PubMed:9989411, PubMed:12114629, PubMed:21467298). Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (PubMed:21467298). The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA (PubMed:9989411, PubMed:12114629, PubMed:21467298). Binds to DNA in a sequence-independent manner (PubMed:21467298). Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis (By similarity). Plays a critical role in caspase- independent, pyknotic cell death in hydrogen peroxide-exposed cells (By similarity). In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (PubMed:19447115). {ECO:0000250|UniProtKB:O95831, ECO:0000269|PubMed:12114629, ECO:0000269|PubMed:19447115, ECO:0000269|PubMed:21467298, ECO:0000269|PubMed:9989411}.
DE  Reference Proteome: Yes;
DE  Interaction: P10909; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: P17742; IntAct: EBI-5326750; Score: 0.40
DE  Interaction: P27661; IntAct: EBI-5326744; Score: 0.56
DE  Interaction: P16104; IntAct: EBI-5326687; Score: 0.44
DE  Interaction: Q9Z0X1; IntAct: EBI-5326701; Score: 0.44
DE  Interaction: Q8BP00; IntAct: EBI-4282570; Score: 0.35
DE  Interaction: P09874; IntAct: EBI-4412377; Score: 0.44
DE  Interaction: P10111; IntAct: EBI-4533329; Score: 0.40
DE  Interaction: P62937; IntAct: EBI-4533382; Score: 0.44
DE  Interaction: Q9EQN3; IntAct: EBI-8296981; Score: 0.50
DE  Interaction: P14854; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: P09429; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: Q9UJZ1; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: P54819; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: Q9BRQ6; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: Q9Y266; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: P35232; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: Q16891; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: Q8N4Q1; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: Q9NX63; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: Q16082; IntAct: EBI-15182189; Score: 0.35
DE  Interaction: P51637; IntAct: EBI-20565496; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005743;
GO  GO:0005758;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003677;
GO  GO:0004174;
GO  GO:0071949;
GO  GO:0016174;
GO  GO:0003954;
GO  GO:0016651;
GO  GO:0072572;
GO  GO:0046983;
GO  GO:0006919;
GO  GO:0008637;
GO  GO:0006915;
GO  GO:1904045;
GO  GO:0071392;
GO  GO:0070301;
GO  GO:0071732;
GO  GO:0090650;
GO  GO:0070059;
GO  GO:0033108;
GO  GO:0032981;
GO  GO:0051402;
GO  GO:0030182;
GO  GO:0043065;
GO  GO:0060545;
GO  GO:0043525;
GO  GO:0012501;
GO  GO:0045041;
GO  GO:1902510;
GO  GO:0002931;
GO  GO:1902065;
GO  GO:0006979;
GO  GO:0009636;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRCGGLAGAFKQKLVPLVRTVYVQRPKQRNRLPGNLFQQWRVPLELQMARQMASSGSSGGKMDNSVLVLIVGLSTIGAG
SQ  AYAYKTIKEDQKRYNERVMGLGLSPEEKQRRAIASATEGGSVPQIRAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLI
SQ  VSEDPELPYMRPPLSKELWFSDDPNVTKTLQFRQWNGKERSIYFQPPSFYVSAQDLPNIENGGVAVLTGKKVVHLDVRGN
SQ  MVKLNDGSQITFEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRALEKISREVKSITVIGGGFLGSELACALGR
SQ  KSQASGIEVIQLFPEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGRLLIKLKDGRKVETDHIVTAVGLE
SQ  PNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSM
SQ  FWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSAPAVPQVPVEGEDYG
SQ  KGVIFYLRDKVVVGIVLWNVFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED
//
ID  Q9JM53;
PN  Apoptosis-inducing factor 1, mitochondrial;
GN  Aifm1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q9Z0X1}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9Z0X1}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z0X1}. Nucleus {ECO:0000250|UniProtKB:Q9Z0X1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95831}. Note=Proteolytic cleavage during or just after translocation into the mitochondrial intermembrane space (IMS) results in the formation of an inner-membrane-anchored mature form (AIFmit) (By similarity). During apoptosis, further proteolytic processing leads to a mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol) (By similarity). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis. Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (By similarity). Translocation into the nucleus is promoted by interaction with (auto-poly-ADP-ribosylated) processed form of PARP1 (By similarity). Colocalizes with EIF3G in the nucleus and perinuclear region (By similarity). {ECO:0000250|UniProtKB:O95831, ECO:0000250|UniProtKB:Q9Z0X1}.
DR  UNIPROT: Q9JM53;
DR  UNIPROT: Q548E3;
DR  Pfam: PF14721;
DR  Pfam: PF07992;
DE  Function: Functions both as NADH oxidoreductase and as regulator of apoptosis (By similarity). In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway. Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA. Binds to DNA in a sequence- independent manner (By similarity). Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis (By similarity). Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide- exposed cells (By similarity). In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (By similarity). {ECO:0000250|UniProtKB:O95831, ECO:0000250|UniProtKB:Q9Z0X1}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005743;
GO  GO:0005758;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003677;
GO  GO:0071949;
GO  GO:0016174;
GO  GO:0003954;
GO  GO:0016651;
GO  GO:0072572;
GO  GO:0046983;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:1904045;
GO  GO:0071392;
GO  GO:0070301;
GO  GO:0071732;
GO  GO:0090650;
GO  GO:0070059;
GO  GO:0033108;
GO  GO:0032981;
GO  GO:0051402;
GO  GO:0010942;
GO  GO:0060545;
GO  GO:0043525;
GO  GO:0012501;
GO  GO:0045041;
GO  GO:1902510;
GO  GO:0002931;
GO  GO:1902065;
GO  GO:0009636;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRCGGLAGAFKQKLVPLVRSVCVQRPKQRNRLPGNLFQQWRVPLELQMARQMASSGPSGGKMDNSVLVLIVGLSTIGAG
SQ  AYAYKTIKEDQKRYNERIMGLGLSPEEKQRRAIASAAEGGSVPPIRVPSHVPFLLIGGGTAAFAAARSIRARDPGARVLI
SQ  VSEDPELPYMRPPLSKELWFSDDPNVTKTLQFRQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVHLDVRGN
SQ  MVKLNDGSQITFEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRALEKISREVKSITVIGGGFLGSELACALGR
SQ  KSQASGIEVIQLFPEKGNMGKILPEYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGKLLIKLKDGRKVETDHIVTAVGLE
SQ  PNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSM
SQ  FWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSDPAVPQVPVEGEDYG
SQ  KGVIFYLRDKVVVGIVLWNVFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED
//
ID  Q13023;
PN  A-kinase anchor protein 6;
GN  AKAP6;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum. Nucleus membrane. Note=In heart muscle. Participation of multiple targeting signals allow correct intracellular targeting. These may be repeated motifs rich in basic and hydrophobic amino acids, palmitoylated/myristoylated motifs or alternatively splice targeting sequences.
DR  UNIPROT: Q13023;
DR  UNIPROT: A7E242;
DR  UNIPROT: A7E2D4;
DR  UNIPROT: O15028;
DR  OMIM: 604691;
DR  DisGeNET: 9472;
DE  Function: Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the nuclear membrane or sarcoplasmic reticulum. May act as an adapter for assembling multiprotein complexes.
DE  Reference Proteome: Yes;
DE  Interaction: P00519; IntAct: EBI-1957451; Score: 0.40
DE  Interaction: P12931; IntAct: EBI-1960946; Score: 0.40
DE  Interaction: Q06787; IntAct: EBI-21392373; Score: 0.00
DE  Interaction: Q96EV8; IntAct: EBI-1105409; Score: 0.00
DE  Interaction: P46108; IntAct: EBI-1959534; Score: 0.40
DE  Interaction: P06241; IntAct: EBI-1961210; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-1964442; Score: 0.40
DE  Interaction: P16333; IntAct: EBI-1968724; Score: 0.40
DE  Interaction: P27986; IntAct: EBI-1970517; Score: 0.40
DE  Interaction: A0A6L8PLI9; IntAct: EBI-2838568; Score: 0.00
DE  Interaction: Q96CV9; IntAct: EBI-5357521; Score: 0.45
DE  Interaction: Q92736; IntAct: EBI-8758107; Score: 0.27
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-21392414; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-21392402; Score: 0.00
DE  Interaction: Q8TDR0; IntAct: EBI-21392387; Score: 0.00
GO  GO:0034704;
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0014704;
GO  GO:0014701;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0016529;
GO  GO:0030315;
GO  GO:0008179;
GO  GO:0060090;
GO  GO:0051018;
GO  GO:0034237;
GO  GO:0043495;
GO  GO:0044325;
GO  GO:0001508;
GO  GO:0019933;
GO  GO:0071320;
GO  GO:0071345;
GO  GO:0070886;
GO  GO:0030307;
GO  GO:0061051;
GO  GO:1902261;
GO  GO:1901381;
GO  GO:0051281;
GO  GO:0060316;
GO  GO:0006605;
GO  GO:0060306;
GO  GO:0010738;
GO  GO:0010880;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLTMSVTLSPLRSQDLDPMATDASPMAINMTPTVEQGEGEEAMKDMDSDQQYEKPPPLHTGADWKIVLHLPEIETWLRMT
SQ  SERVRDLTYSVQQDSDSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLV
SQ  LRERILQGLQDANGNYTRQTDILQAFSEETKEGRLDSLTEVDDSGQLTIKCSQNYLSLDCGITAFELSDYSPSEDLLSGL
SQ  GDMTSSQVKTKPFDSWSYSEMEKEFPELIRSVGLLTVAADSISTNGSEAVTEEVSQVSLSVDDKGGCEEDNASAVEEQPG
SQ  LTLGVSSSSGEALTNAAQPSSETVQQESSSSSHHDAKNQQPVPCENATPKRTIRDCFNYNEDSPTQPTLPKRGLFLKEET
SQ  FKNDLKGNGGKRQMVDLKPEMSRSTPSLVDPPDRSKLCLVLQSSYPNSPSAASQSYECLHKVGNGNLENTVKFHIKEISS
SQ  SLGRLNDCYKEKSRLKKPHKTSEEVPPCRTPKRGTGSGKQAKNTKSSAVPNGELSYTSKAIEGPQTNSASTSSLEPCNQR
SQ  SWNAKLQLQSETSSSPAFTQSSESSVGSDNIMSPVPLLSKHKSKKGQASSPSHVTRNGEVVEAWYGSDEYLALPSHLKQT
SQ  EVLALKLENLTKLLPQKPRGETIQNIDDWELSEMNSDSEIYPTYHVKKKHTRLGRVSPSSSSDIASSLGESIESGPLSDI
SQ  LSDEESSMPLAGMKKYADEKSERASSSEKNESHSATKSALIQKLMQDIQHQDNYEAIWEKIEGFVNKLDEFIQWLNEAME
SQ  TTENWTPPKAEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRMIASQWKELQRQIKRQHS
SQ  WILRALDTIKAEILATDVSVEDEEGTGSPKAEVQLCYLEAQRDAVEQMSLKLYSEQYTSSSKRKEEFADMSKVHSVGSNG
SQ  LLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEKVDS
SQ  INEKWELLGKTLGEKIQDTMAGHSGSSPRDLLSPESGSLVRQLEVRIKELKGWLRDTELFIFNSCLRQEKEGTMNTEKQL
SQ  QYFKSLCREIKQRRRGVASILRLCQHLLDDRETCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESETLN
SQ  VIDPGLMDLNGMSEDALEWDEMDISNKLISLNEESNDLDQELQPVIPSLKLGETSNEDPGYDEEADNHGGSQYASNITAP
SQ  SSPHIYQVYSLHNVELYEDNHMPFLKNNPKVTGMTQPNVLTKSLSKDSSFSSTKSLPDLLGGSNLVKPCACHGGDMSQNS
SQ  GSESGIVSEGDTETTTNSEMCLLNAVDGSPSNLETEHLDPQMGDAVNVLKQKFTDEGESIKLPNSSQSSISPVGCVNGKV
SQ  GDLNSITKHTPDCLGEELQGKHDVFTFYDYSYLQGSKLKLPMIMKQSQSEKAHVEDPLLRGFYFDKKSCKSKHQTTELQP
SQ  DVPPHERILASASHEMDRISYKSGNIEKTFTGMQNAKQLSLLSHSSSIESLSPGGDLFGLGIFKNGSDSLQRSTSLESWL
SQ  TSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFTGQMSLDIASSI
SQ  NEDSAASLTELSSSDELSLCSEDIVLHKNKIPESNASFRKRLTRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSST
SQ  LTLTEEELCIKDEDDDSSIATDDEIYEDCTLMSGLDYIKNELQTWIRPKLSLTRDKKRCNVSDEMKGSKDISSSEMTNPS
SQ  DTLNIETLLNGSVKRVSENNGNGKNSSHTHELGTKRENKKTIFKVNKDPYVADMENGNIEGIPERQKGKPNVTSKVSENL
SQ  GSHGKEISESEHCKCKALMDSLDDSNTAGKEFVSQDVRHLPKKCPNHHHFENQSTASTPTEKSFSELALETRFNNRQDSD
SQ  ALKSSDDAPSMAGKSAGCCLALEQNGTEENASISNISCCNCEPDVFHQKDAEDCSVHNFVKEIIDMASTALKSKSQPENE
SQ  VAAPTSLTQIKEKVLEHSHRPIQLRKGDFYSYLSLSSHDSDCGEVTNYIEEKSSTPLPLDTTDSGLDDKEDIECFFEACV
SQ  EGDSDGEEPCFSSAPPNESAVPSEAAMPLQATACSSEFSDSSLSADDADTVALSSPSSQERAEVGKEVNGLPQTSSGCAE
SQ  NLEFTPSKLDSEKESSGKPGESGMPEEHNAASAKSKVQDLSLKANQPTDKAALHPSPKTLTCEENLLNLHEKRHRNMHR
//
ID  Q9WVC7;
PN  A-kinase anchor protein 6;
GN  Akap6;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum. Nucleus membrane. Note=In heart muscle. Participation of multiple targeting signals allow correct intracellular targeting. These may be repeated motifs rich in basic and hydrophobic amino acids, palmitoylated/myristoylated motifs or alternatively splice targeting sequences.
DR  UNIPROT: Q9WVC7;
DR  Pfam: PF00435;
DE  Function: Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the nuclear membrane or sarcoplasmic reticulum. May act as an adapter for assembling multiprotein complexes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P20651; IntAct: EBI-7559869; Score: 0.52
DE  Interaction: P48453; IntAct: EBI-7559943; Score: 0.44
DE  Interaction: F1LMY4; IntAct: EBI-16420846; Score: 0.35
GO  GO:0034704;
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0014704;
GO  GO:0014701;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0042383;
GO  GO:0016529;
GO  GO:0030315;
GO  GO:0008179;
GO  GO:0019899;
GO  GO:0060090;
GO  GO:0051018;
GO  GO:0034237;
GO  GO:0051721;
GO  GO:0043495;
GO  GO:0044325;
GO  GO:0071320;
GO  GO:0071345;
GO  GO:0071872;
GO  GO:0007194;
GO  GO:0070886;
GO  GO:2000481;
GO  GO:0030307;
GO  GO:0061051;
GO  GO:1902261;
GO  GO:1901381;
GO  GO:0001934;
GO  GO:0051281;
GO  GO:0060316;
GO  GO:0045727;
GO  GO:0031503;
GO  GO:0086004;
GO  GO:0060306;
GO  GO:0010738;
GO  GO:1901897;
GO  GO:0010880;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLTMSVTLSPLRSQGPDPMATDASPMAINMTPTVEQEEGEGEEAVKAIDAEQQYGKPPPLHTAADWKIVLHLPEIETWLR
SQ  MTSERVRDLTYSVQQDADSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSV
SQ  LVLRERILQGLQDANGNYTRQTDILQAFSEETTEGRLDSLTEVDDSGQLTIKCSQDYLSLDCGITAFELSDYSPSEDLLG
SQ  GLGDMTTSQAKTKSFDSWSYSEMEKEFPELIRSVGLLTVATEPVPSSCGEANEDSSQASLSDDHKGEHGEDGAPVPGQQL
SQ  DSTVGMSSLDGTLANAAEHPSETAKQDSTSSPQLGAKKTQPGPCEITTPKRSIRDCFNYNEDSPTQPTLPKRGLFLKETQ
SQ  KNERKGSDRKGQVVDLKPELSRSTPSLVDPPDRSKLCLVLQSSYPSSPSAASQSYECLHKVGLGNLENIVRSHIKEISSS
SQ  LGRLTDCHKEKLRLKKPHKTLAEVSLCRIPKQGGGSGKRSESTGSSAGPSMVSPGAPKATMRPETDSASTASGGLCHQRN
SQ  RSGQLPVQSKASSSPPCSHSSESSLGSDSIKSPVPLLSKNKSQKSSPPAPCHATQNGQVVEAWYGSDEYLALPSHLKQTE
SQ  VLALKLESLTKLLPQKPRGETIQDIDDWELSEMNSDSEIYPTYHIKKKHTRLGTVSPSSSSDIASSLGESIESGPLSDIL
SQ  SDEDLCLPLSSVKKFTDEKSERPSSSEKNESHSATRSALIQKLMHDIQHQENYEAIWERIEGFVNKLDEFIQWLNEAMET
SQ  TENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVSHKAGLKDTLRMIASQWKELQRQIKRQHSW
SQ  ILRALDTIKAEILATDVSVEDEEGTGSPKAEVQLCHLETQRDAVEQMSLKLYSEQYTSGSKRKEEFANMSKAHAEGSNGL
SQ  LDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKSELLSKVEALKKGGLSLPDDILEKVDSI
SQ  NEKWELLGKTLREKIQDTIAGHSGSGPRDLLSPESGSLVRQLEVRIKELKRWLRDTELFIFNSCLRQEKEGTSAEKQLQY
SQ  FKSLCREIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESETLNVI
SQ  DPGLMDLNGMSEDALEWDETDISNKLISVHEESNDLDQDPEPMLPAVKLEETHHKDSGYEEEAGDCGGSPYTSNITAPSS
SQ  PHIYQVYSLHNVELHEDSHTPFLKSSPKFTGTTQPTVLTKSLSKDSSFSSTKSLPDLLGGSGLVRPYSCHSGDLSQNSGS
SQ  ESGIVSEGDNEMPTNSDMSLFSMVDGSPSNPETEHPDPQMGDAANVLEQKFKDNGESIKLSSVSRASVSPVGCVNGKAGD
SQ  LNSVTKHTADCLGEELQGKHDVFTFYDYSYLQGSKLKLPMIMKQPQSEKAHVEDPLLGGFYFDKKSCKAKHQASESQPDA
SQ  PPHERILASAPHEMGRSAYKSSDIEKTFTGIQSARQLSLLSRSSSVESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTS
SQ  YKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDMTLQSSSQKMPFAGQMSLDVASSINE
SQ  DSPASLTELSSSDELSLCSEDIVLHKNKIPESNASFRKRLNRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLT
SQ  LTEEELCLKDEDDDSSIATDDEIYEESNLMSGLDYIKNELQTWIRPKLSLTREKKRSGVTDEIKVNKDGGGNEKANPSDT
SQ  LDIEALLNGSIRCLSENNGNGKTPPRTHGSGTKGENKKSTYDVSKDPHVADMENGNIESTPEREREKPQGLPEVSENLAS
SQ  NVKTISESELSEYEAVMDGSEDSSVARKEFCPPNDRHPPQMGPKLQHPENQSGDCKPVQNPCPGLLSEAGVGSRQDSNGL
SQ  KSLPNDAPSGARKPAGCCLLEQNETEESASISSNASCCNCKPDVFHQKDDEDCSVHDFVKEIIDMASTALKSKSQPESEV
SQ  AAPTSLTQIKEKVLEHSHRPIHLRKGDFYSYLSLSSHDSDCGEVTNYIDEKSSTPLPPDAVDSGLDDKEDMDCFFEACVE
SQ  DEPVNEEAGLPGALPNESAIEDGAEQKSEQKTASSPVLSDKTDLVPLSGLSPQKGADDAKEGDDVSHTSQGCAESTEPTT
SQ  PSGKANAEGRSRMQGVSATPEENAASAKPKIQAFSLNAKQPKGKVAMRYPSPQTLTCKEKLVNFHEDRHSNMHR
//
ID  Q148F2;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  ALOX5AP;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q148F2;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0004464;
GO  GO:0019370;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDQEAVGNIVLLAIVTLISVVQNGFFAHKVEHESKTHNGRSFQRTGTLAFERVYTANQNCVDAYPTFLVMLWSAGLLCSQ
SQ  VPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFAMSLAGILNYFFIALFGSDFENYIKTVTTTISPLLLI
SQ  P
//
ID  P30353;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  ALOX5AP;
OS  9796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: P30353;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0004464;
GO  GO:0019370;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDQETVGNVVLLAIVTLISVIQNGFFAHKVEHESKTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLVMLWSAGLLCSQ
SQ  VPAAFAGLMYLFVRQKYFVGYLGERRQSTPGYIFGKRIILFLFLMSLAGIFNYYLILFFGSDFENYIKTITTT
//
ID  P20292;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  ALOX5AP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
DR  UNIPROT: P20292;
DR  UNIPROT: Q5VV04;
DR  PDB: 2Q7M;
DR  PDB: 2Q7R;
DR  PDB: 6VGC;
DR  PDB: 6VGI;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DR  OMIM: 601367;
DR  OMIM: 603700;
DR  DisGeNET: 241;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes. {ECO:0000269|PubMed:2300173, ECO:0000269|PubMed:8440384}.
DE  Disease: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Note=Genetic variations in ALOX5AP may be associated with susceptibility to myocardial infarction. Involvement in myocardial infarction is however unclear: according to some authors (PubMed:14770184), a 4-SNP haplotype in ALOX5AP confers risk of myocardial infarction, while according to other (PubMed:17304054) ALOX5AP is not implicated in this condition. {ECO:0000269|PubMed:14770184, ECO:0000269|PubMed:17304054}.
DE  Reference Proteome: Yes;
DE  Interaction: A0PK00; IntAct: EBI-24765164; Score: 0.56
DE  Interaction: O00299; IntAct: EBI-3904626; Score: 0.37
DE  Interaction: Q9H115; IntAct: EBI-24738406; Score: 0.56
DE  Interaction: Q96FB2; IntAct: EBI-24768960; Score: 0.56
DE  Interaction: O15529; IntAct: EBI-24778364; Score: 0.56
DE  Interaction: P35372; IntAct: EBI-24571720; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24799898; Score: 0.56
DE  Interaction: O15552; IntAct: EBI-24808129; Score: 0.56
DE  Interaction: Q70Z53; IntAct: EBI-21893005; Score: 0.40
DE  Interaction: P20292; IntAct: EBI-26452342; Score: 0.40
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0004051;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0042802;
GO  GO:0004464;
GO  GO:0047485;
GO  GO:0044877;
GO  GO:0071277;
GO  GO:0019370;
GO  GO:0002540;
GO  GO:0019372;
GO  GO:0002675;
GO  GO:0070207;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQ
SQ  VPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTISTTISPLLLI
SQ  P
//
ID  Q2PG08;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  ALOX5AP;
OS  9541;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q2PG08;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0047485;
GO  GO:0071277;
GO  GO:0019370;
GO  GO:0002540;
GO  GO:0070207;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQ
SQ  VPAAFAGLMYLLVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTVTTTISPLLLI
SQ  P
//
ID  P30354;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  ALOX5AP;
OS  9544;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: P30354;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0004464;
GO  GO:0019370;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQ
SQ  VPAAFAGLMYLLVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTVTTT
//
ID  P30355;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  Alox5ap;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:19075240}; Multi-pass membrane protein {ECO:0000269|PubMed:19075240}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: P30355;
DR  UNIPROT: Q9D138;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250, ECO:0000269|PubMed:19075240}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0004051;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0042802;
GO  GO:0004464;
GO  GO:0047485;
GO  GO:0044877;
GO  GO:0071277;
GO  GO:0019370;
GO  GO:0002540;
GO  GO:0019372;
GO  GO:0002675;
GO  GO:0070207;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDQEAVGNVVLLALVTLISVVQNAFFAHKVEHESKAHNGRSFQRTGTLAFERVYTANQNCVDAYPTFLVVLWTAGLLCSQ
SQ  VPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSFAGILNHYLIFFFGSDFENYIRTVSTTISPLLLI
SQ  P
//
ID  P30356;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  ALOX5AP;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: P30356;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0004464;
GO  GO:0019370;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDQEAMGNIVLLAIVTLISVVQNAFFAHKVEHESKTHNGRSFQRTGTPAFERVYTANQNCVDAYPTFLVVLWSAGLFCSQ
SQ  VPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGIFNYFLILFFGSDFENYIKTITTT
//
ID  P30357;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  ALOX5AP;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: P30357;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0019370;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDQEAVGNVVLLAIVTLISVVQNGFFAHKVEHESRNQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWTAGLLCSQ
SQ  VPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGILNYCLILLFGSDFENYIKTISTT
//
ID  P20291;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  Alox5ap;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: P20291;
DR  UNIPROT: Q5RJL3;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P12527; IntAct: EBI-15746644; Score: 0.49
DE  Interaction: P20291; IntAct: EBI-15746661; Score: 0.40
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0042802;
GO  GO:0004464;
GO  GO:0047485;
GO  GO:0044877;
GO  GO:0071277;
GO  GO:0019370;
GO  GO:0002540;
GO  GO:0019372;
GO  GO:0002675;
GO  GO:0070207;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDQEAVGNVVLLAIVTLISVVQNAFFAHKVELESKAQSGRSFQRTGTLAFERVYTANQNCVDAYPTFLVVLWTAGLLCSQ
SQ  VPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGILNHYLIFFFGSDFENYIRTITTTISPLLLI
SQ  P
//
ID  P30358;
PN  Arachidonate 5-lipoxygenase-activating protein;
GN  ALOX5AP;
OS  9940;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: P30358;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Required for leukotriene biosynthesis by ALOX5 (5- lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0050544;
GO  GO:0008047;
GO  GO:0019370;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDQETVGNIVLLAIVTLISVVQNGFFAHKVEHESKTHNGRSFQRTGPLAFERVYTANQNCVDAYPTFLVMLWSAGLLCSQ
SQ  VPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFAMSLAGILNYFLIAFFGSDFENYIKTVTTT
//
ID  Q750Y9;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q750Y9;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0004577;
GO  GO:0043495;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAWLAIVCLLAATTALCVRMAALAPGVYGPAVCGGRSGGGRGPPRHVMIFLGSGGHTGEMLRLLEVYGAALVAGATVRVG
SQ  YTDEASAERGRQSAALRAARGVEYVPLLKAREVGAGAGAAVRSTVRAAAQAFSAVRRARRALHTGPHVVVLNGPGTSVVV
SQ  LFWLRVLDLLSLRRTRVVYVESLARTESLSLSGRLAYPFADEFVVQWPDLAQRYRRARWFGALV
//
ID  Q4WNB5;
PN  UDP-N-acetylglucosamine transferase subunit alg14;
GN  alg14;
OS  330879;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q4WNB5;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit alg13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFSMLRRMKLDPSTYTYRTYVVSSGDNFSAARAVEFETEWLKQSPKLSFPANGSNSTESYAVVTVPRARRVHQSYLTAPL
SQ  STLQCFYACFLVLCGRHPEQKSPLPTTNSPYPDVILTNGPATAVCMVLAAKSLRLFHYLKSLFYIKDHQDRDSSRSSQVK
SQ  RSEDAPAPVHFQLRTIYVESWARVTTFSLSGKLLLPFADRFLVQWPDLAGKQAWRGMRETEYAGTLVD
//
ID  Q5A5N6;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  237561;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q5A5N6;
DR  UNIPROT: A0A1D8PIT0;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDIETAACFSIAFIATPILIVLVRLLFILPSLRLPTSVKKKKKLIQECQLSILLGSGGHTGEMMRIISKLDMGKVSRTWI
SQ  YTSGDNASLAKAQDYERKSGTSSQYIPIPRARTVGQSYISSIPTTIYSFLFSAIAMLKHRPAVILLNGPGTCVPVAYILF
SQ  LYKLLGLCNTKIIYIESLARVNKLSLSGLLLLPISDRFIVQWESLYQQYSRVEYYGILI
//
ID  Q6FV75;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q6FV75;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0004577;
GO  GO:0043495;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPFLSTAHLCALLLILGCFYIGRLIKVIPILRFACAGEAEIKPLFIQPKSNDGIHLFVFLGSGGHTGEMLRLLQNHQEVL
SQ  LNKRNTFYIGYSDDDSKARFLSMVEKYDFKAERIHFYPFAKAREVNAGPIASIVTISKTLLTGFTNVLSIKMNTLGQPHL
SQ  TLLNGPGTCCIINFWLKLLEWLIYIPYLSNGSNVVYIESLARIESLSLTGKILYLLADVFVVQWEELKVRKAPRSEYYGI
SQ  LV
//
ID  P0CM11;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  283643;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: P0CM11;
DR  UNIPROT: Q55XH5;
DR  UNIPROT: Q5KMF9;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLGRYIGWSILAFTYLVLAILLRLIFLQPSKTSRASYRPKDAKCSLGVFLGSGGHTSEMKALLSTLDYERYQPRTYIYC
SQ  HGDDLSLRAVSDIESSKGGLISSKMYYLLSLPRARRVGQPLLSTMVSVLKTLYIAALRLFLIPLLKNPRRPFVDLLIVNG
SQ  PGTCVVLVLVSYIRRVRLEYTRIIYVESFARVKSLSLSGKMIRPLADRFLVQWPDASDSDNVIHKGLLV
//
ID  P0CM10;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  214684;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: P0CM10;
DR  UNIPROT: Q55XH5;
DR  UNIPROT: Q5KMF9;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLGRYIGWSILAFTYLVLAILLRLIFLQPSKTSRASYRPKDAKCSLGVFLGSGGHTSEMKALLSTLDYERYQPRTYIYC
SQ  HGDDLSLRAVSDIESSKGGLISSKMYYLLSLPRARRVGQPLLSTMVSVLKTLYIAALRLFLIPLLKNPRRPFVDLLIVNG
SQ  PGTCVVLVLVSYIRRVRLEYTRIIYVESFARVKSLSLSGKMIRPLADRFLVQWPDASDSDNVIHKGLLV
//
ID  Q6BMD0;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  284592;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q6BMD0;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDFESQLCIKVVLLLLPFFIIGIRLLWVLPAVNSPAMGSEKEKGLSQIPSELRGSNIMIFLGSGGHTGEMMRILANVDLN
SQ  NFNRTWVTSSGDSTSILKCKKYEDERLTSGQNKSDYLVLHRARTVGESIISSVFSTVRSLISTIKHLYELPQFPSILLLN
SQ  GPGTSVPLAYIIFLLKFLGLCKTRIIYIESLARVKQLSVSGLLILPITDRFIVQWKQLAVKYKRAEYYGILI
//
ID  Q96F25;
PN  UDP-N-acetylglucosamine transferase subunit ALG14 homolog;
GN  ALG14;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q96F25;
DR  UNIPROT: A8K030;
DR  Pfam: PF08660;
DR  OMIM: 612866;
DR  OMIM: 616227;
DR  OMIM: 619031;
DR  OMIM: 619036;
DR  DisGeNET: 199857;
DE  Function: Involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER. {ECO:0000269|PubMed:16100110}.
DE  Disease: Myasthenic syndrome, congenital, 15 (CMS15) [MIM:616227]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre- synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. {ECO:0000269|PubMed:23404334}. Note=The disease is caused by variants affecting the gene represented in this entry. Intellectual developmental disorder with epilepsy, behavioral abnormalities, and coarse facies (IDDEBF) [MIM:619031]: An autosomal recessive neurodevelopmental disorder that manifests in early infancy with infantile spasms and developmental delay. Clinical features include severely impaired intellectual development, epilepsy, autism, hyperactivity and other behavioral problems, and coarse facies. Brain MRI findings may include delayed myelination in the deep parietal lobes. {ECO:0000269|PubMed:30221345}. Note=The disease may be caused by variants affecting the gene represented in this entry. Myopathy, epilepsy, and progressive cerebral atrophy (MEPCA) [MIM:619036]: An autosomal recessive disorder characterized by severe, early lethal neurodegeneration, myasthenic and myopathic features, progressive cerebral atrophy with myelination defects, and intractable epilepsy. {ECO:0000269|PubMed:28733338}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q99871; IntAct: EBI-21670231; Score: 0.35
DE  Interaction: Q9Y5Q0; IntAct: EBI-21766826; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.53
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVCVLVLAAAAGAVAVFLILRIWVVLRSMDVTPRESLSILVVAGSGGHTTEILRLLGSLSNAYSPRHYVIADTDEMSANK
SQ  INSFELDRADRDPSNMYTKYYIHRIPRSREVQQSWPSTVFTTLHSMWLSFPLIHRVKPDLVLCNGPGTCVPICVSALLLG
SQ  ILGIKKVIIVYVESICRVETLSMSGKILFHLSDYFIVQWPALKEKYPKSVYLGRIV
//
ID  Q6CJG3;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q6CJG3;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0004577;
GO  GO:0043495;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLTTAWCLLIWSVTLLLVRICLVIPIFHSSREAGPLTKDKDNVGGRMKNLVLFIFLGSGGHTGEMLRLIEHYQGMLLES
SQ  AVTIHVGYSDDDSIIKFKNKIHQISVSNTLRAKVIYHRFDKARDVGSSLAGSIKSIIKTAIRSMVLTYRIKSSMRGHPNL
SQ  TLLNGPGTCCIITFWLKLYHIFLWQPSKIVYVESLARTNRLSLTGMILYPLADEFVVQWADLLPIYPKAKYYGVLV
//
ID  Q9D081;
PN  UDP-N-acetylglucosamine transferase subunit ALG14 homolog;
GN  Alg14;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9D081;
DR  UNIPROT: Q8CEP2;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLSILILAATAAGLVILLFQRLWTVLGPHHVTPRESLRLLIVAGSGGHTTEILRLVGSLSNAYSPRHYVIAESDEMSAKK
SQ  IHSLEELSRAQNDSTTEYPKYHLHRIPRSREVRQSWLSSVFTTFYSMWFSFPLVLRIKPDLVLCNGPGTCVPICVSALLL
SQ  GILGVKKVIIVYVESICRVETLSLSGKILRHLSDYFIVQWPTLKEKYPKSVYLGRIV
//
ID  Q6AY85;
PN  UDP-N-acetylglucosamine transferase subunit ALG14 homolog;
GN  Alg14;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q6AY85;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVCVLTLAASAGGLAVLLIVRLWAVLRSHPVTPRQSLGLLIVAGSGGHTAEILRLVGSLSGAYSPRHYVIAESDEMSAKK
SQ  IHSLELARAQNDSTTEHTEYYLHRIPRSREVRQSWLSSVFTTLYSIWFSFPLVHRIKPDLVLCNGPGTCVPICVSALLLG
SQ  ILGIKKVIIVYVESICRVETLSLSGKILWHLSDYFIVQWPTLKEKYPKSVYLGRIV
//
ID  O14199;
PN  UDP-N-acetylglucosamine transferase subunit alg14;
GN  alg14;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: O14199;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit alg13 to the ER (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNTYVLTAIAVLASLIILLVGRNAIKSSKKKPFQKHLLVFFGSGGHTGEMLNLLNALDDKLYSVRSYVAGSDDTMSVSKA
SQ  SLLSNSLPSVKSKIFKVPRARYVKQSWLTTPFTAFWSLLGSISVIFWNPFGIPDVILCNGPGTCVFICLLGYLAKFLGKN
SQ  VKIVYVESFARVKSLSLSGKILMPFVDRFLVQWPDLATKYKRAEYIGIVA
//
ID  Q6CF02;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  284591;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q6CF02;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043541;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVTTILIAASAILVLLLLRLLFVLPASNRFGFLYRPKHSNPKLMVMMGSGGHTGEMLRMLKTLKLQSYAKRVYVSSSGDV
SQ  DSLEKVKVLESTTKTDIKTMVLENIPRARKVGQSYPSSVITSAVSFAVAVKLVHKHKPHVIVCNGPATCVMLCYAAFLLR
SQ  FMALIDTRIIYVESLARVNRLSLSGLILLPFCDRFLVQWPQLAEKYPRAEYHGILV
//
ID  P38242;
PN  UDP-N-acetylglucosamine transferase subunit ALG14;
GN  ALG14;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:16100110, ECO:0000269|PubMed:17686769}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:15282802}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: P38242;
DR  UNIPROT: D6VQ69;
DR  Pfam: PF08660;
DE  Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER. {ECO:0000269|PubMed:15615718, ECO:0000269|PubMed:16100110}.
DE  Reference Proteome: Yes;
DE  Interaction: P11484; IntAct: EBI-804270; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-804270; Score: 0.35
DE  Interaction: P40069; IntAct: EBI-804270; Score: 0.35
DE  Interaction: P53178; IntAct: EBI-989509; Score: 0.46
DE  Interaction: P53223; IntAct: EBI-6336679; Score: 0.00
DE  Interaction: P25294; IntAct: EBI-3660139; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3667000; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3723318; Score: 0.35
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0031227;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0043541;
GO  GO:0043495;
GO  GO:0006488;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKTAYLASLVLIVSTAYVIRLIAILPFFHTQAGTEKDTKDGVNLLKIRKSSKKPLKIFVFLGSGGHTGEMIRLLENYQDL
SQ  LLGKSIVYLGYSDEASRQRFAHFIKKFGHCKVKYYEFMKAREVKATLLQSVKTIIGTLVQSFVHVVRIRFAMCGSPHLFL
SQ  LNGPGTCCIISFWLKIMELLLPLLGSSHIVYVESLARINTPSLTGKILYWVVDEFIVQWQELRDNYLPRSKWFGILV
//
ID  Q9UTK5;
PN  Nucleoporin alm1;
GN  alm1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:28974540}. Nucleus envelope {ECO:0000269|PubMed:28974540}.
DR  UNIPROT: Q9UTK5;
DR  UNIPROT: O13313;
DR  UNIPROT: Q9UTT8;
DE  Function: Maintains the proteasome and its anchor cut8 at the nucleus envelope and is required for kinetochore component proteostasis (PubMed:28974540). Proper kinetochore stoichiometry ensures the correct attachment of kinetochores to spindle microtubules during cytokinesis (PubMed:28974540, PubMed:10660053). Required for the localization of spindle assembly checkpoint (SAC) protein mad2 and bub1 to the nucleus envelope during interphase, but not their localization during mitosis (PubMed:28974540). {ECO:0000269|PubMed:10660053, ECO:0000269|PubMed:28974540}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0140602;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSGGLEDDIQLVHEFLDVSFEDIKPLVSVNGFAVFISAIKTKVKDINALKDQLVLQEVNHEHKENVLTKKINFLEQQLQ
SQ  SSNNQAEESRNLISVLRNENESLKTNLENQNKRFDALTTENQSLRRANSELQEQSKIASEQLSIAKDQIEALQNENSHLG
SQ  EQVQSAHQALSDIEERKKQHMFASSSSRVKEEILVQEKSALVSDLASLQSDHSKVCEKLEVSSRQVQDLEKKLAGLAQQN
SQ  TELNEKIQLFEQKRSNYSSDGNISKILETDPTSIKELEEEVETQKRLTALWESKSSELQSEVAALQEKLTSQQSLYNNVT
SQ  EELNNNKQQLLISENSLRELQEKYDSVVSELQVVKENKNTSVSAGVGLFSPLAQKLSAVQNPEFSFTKVYSDNMKLQQKV
SQ  SSLKLQLDRLTNKFSSFCEQVKQRIPVVKQQRSEIVRNNIYMNFLSESLETSNNNLTKVQAELLSTKMRQEACYLQLTAS
SQ  RTQCSDLSREVICLMAELDHLNETKSRNVPATVQVALDEYAQNPSTASETLVNKELANFSSIKEAVSKTLELREKVRALE
SQ  CDVEIQKQTVQYQISNAVKENSNTLSEQIKNLESELNSSKIKNESLLNERNLLKEMLATSRSSILSHNSSAGNIDDKMKS
SQ  IDESTRELEKNYEVYRNEMTAIQESLSKRNQDLLSEMEAIRKELENSKYQQQLSTDRLTNANNDVEAFKKEAKELRSINQ
SQ  NLQDIISRQDQRASKFAEELLHVNSLAERLKGELNASKGEKDLRKRTQERLISENDKLLAERERLMSLVSDLQTFLNQQQ
SQ  LSDAARKVKFESEKESLSLSLQKLKESNEKMSNDLHSLQKSLEKSGIEYSSRIKTLMLEKQSLSEDNRKLLDNQQMMEIK
SQ  LQELNGVIELEKQRFSTLEAKFTQQKNTSYSEREALLESSLSDLQSKHTSLESQYNYSLRNIEQLQAASKLAEEMVERVK
SQ  TEYDEYRLQTSESLEKNHLKITSLEQRIVILQDEIASSSLRCENITKDSETRVALLLEENKHLNNELSSHRNAEKQHLEK
SQ  ENDYKQQLLLVTEDLRKTREDYEKELLRHADARSTLQKLREDYTKALEQVEDLNKEIALKAGINESQPFPISEKEDPLRQ
SQ  EVYVLKKQNAMLLTQLQSSNLNFAEITSPSPDLDSVMKLGLSDLQNHVKRISKEMEIISCQRQLLFLENKKLKRTVESSN
SQ  RVIADLQRGITEKDVSSTSESVGERSNYLNMVALLNESNKSLRENLERNEEVITELREKIETLKTDLANFRLNKEQLESQ
SQ  LQTEKAAVKKLENSNEEYKRHNQEILLSLNSSTSTSSDASRLKNELVSKENLIEELNQEIGHLKSELETVKSKSEDLENE
SQ  RAQNQSKIEQLELKNTKLAAAWRTKYEQVVNKSLEKHNQIRQQLSQKTSELEAKVAECHQLNEQLNKPSATPTATTQSEP
SQ  STVSLEEFNSTKEELSSTQRKLSEIMDILNTTKEELEKVRQNSNKSEGTSKDTEIPNEEEMERKKVMQQEVLRLRSRIAK
SQ  ELQKNELLRKQNQVLQDQVKALQETVVSSEEAESASVHADTKDLENLKKTEEMLSVTFQVIFNESISDFSTSTADFTTFV
SQ  QKEWEKRREILQKDVEEQVAQSHQKQLDNIRKELEMRNKLKLSMLEKNLARVRAELEQSKKKDSPAILSLEASKNTDSNK
SQ  SNSEVPAAQVKEKKLIAKTHSVDTNSPPKRSSSDAGMDVSNDVKKAK
//
ID  P00978;
PN  Trypstatin;
GN  AMBP;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Alpha-1-microglobulin]: Secreted {ECO:0000250|UniProtKB:P02760}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P02760}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02760}. Cell membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Nucleus membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02760}. Note=The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. {ECO:0000250|UniProtKB:P02760}.
DR  UNIPROT: P00978;
DR  UNIPROT: P35420;
DR  UNIPROT: Q28020;
DR  UNIPROT: Q3SZZ4;
DR  Pfam: PF00014;
DR  Pfam: PF00061;
DR  PROSITE: PS00280;
DR  PROSITE: PS50279;
DR  PROSITE: PS00213;
DE  Function: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species- induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis. Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential. Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage. Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures. Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria. Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (By similarity). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}. [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion. Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule- stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases. As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (By similarity). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}. [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000250|UniProtKB:Q64240}.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0031314;
GO  GO:0005743;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0016209;
GO  GO:0035374;
GO  GO:0098633;
GO  GO:0020037;
GO  GO:0019862;
GO  GO:0016491;
GO  GO:0016653;
GO  GO:0042803;
GO  GO:0004867;
GO  GO:0098869;
GO  GO:0034614;
GO  GO:1903606;
GO  GO:0020027;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P02760};
SQ  MRSLSGLLLLLTACLAVNASSVPTLPDDIQVQENFDLSRIYGKWFNVAVGSTCPWLKRFKEKMTMSTVVLIAGPTSKEIS
SQ  VTNTHRRKGVCESISGTYEKTSADGKFLYHKAKWNITMESYVVHTNYDEYAIFLTKKLSRRHGPTITVKLYGREPQLRES
SQ  LLEEFREVALGVGIPEDAIFTMPDRGECVPGEQDPVPTPLSRARRAVLTQEEEGSGAGQPVTNFSKKADSCQLDYSQGPC
SQ  LGLFKRYFYNGTSMACETFLYGGCMGNGNNFLSEKECLQTCRTVEACNLPIVQGPCRSYIQLWAFDAVKGKCVRFSYGGC
SQ  KGNGNKFYSEKECKEYCGIPGEADEELLRFSN
//
ID  P02760;
PN  Trypstatin;
GN  AMBP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Alpha-1-microglobulin]: Secreted {ECO:0000269|PubMed:11877257, ECO:0000269|PubMed:32092412}. Endoplasmic reticulum {ECO:0000269|PubMed:22096585}. Cytoplasm, cytosol {ECO:0000269|PubMed:32092412}. Cell membrane {ECO:0000269|PubMed:22096585, ECO:0000269|PubMed:32092412}; Peripheral membrane protein {ECO:0000305|PubMed:22096585, ECO:0000305|PubMed:32092412}. Nucleus membrane {ECO:0000269|PubMed:22096585}; Peripheral membrane protein {ECO:0000305|PubMed:22096585}. Mitochondrion inner membrane {ECO:0000305|PubMed:23157686}; Peripheral membrane protein {ECO:0000305|PubMed:23157686}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:22096585}. Note=The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. {ECO:0000269|PubMed:22096585}.
DR  UNIPROT: P02760;
DR  UNIPROT: P00977;
DR  UNIPROT: P02759;
DR  UNIPROT: P78491;
DR  UNIPROT: Q2TU33;
DR  UNIPROT: Q5TBD7;
DR  UNIPROT: Q9UC58;
DR  UNIPROT: Q9UDI8;
DR  PDB: 1BIK;
DR  PDB: 3QKG;
DR  PDB: 4ES7;
DR  PDB: 4U30;
DR  PDB: 6EJ7;
DR  PDB: 6EJ8;
DR  PDB: 6EJ9;
DR  PDB: 6EJA;
DR  PDB: 6EJB;
DR  PDB: 6EJC;
DR  PDB: 6EJD;
DR  Pfam: PF00014;
DR  Pfam: PF00061;
DR  PROSITE: PS00280;
DR  PROSITE: PS50279;
DR  PROSITE: PS00213;
DR  OMIM: 176870;
DR  DisGeNET: 259;
DE  Function: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments (PubMed:11877257, PubMed:15683711, PubMed:22096585, PubMed:23157686, PubMed:23642167, PubMed:25698971, PubMed:32823731, PubMed:32092412). Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis (PubMed:11877257, PubMed:32092412). Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential (PubMed:15683711). Upon acute inflammation, inhibits oxidation of low- density lipoprotein particles by MPO and limits vascular damage (PubMed:25698971). Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures (PubMed:23642167, PubMed:22096585). Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation (PubMed:21356557). Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria (PubMed:23157686, PubMed:32823731). Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (PubMed:15683711). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). {ECO:0000250|UniProtKB:Q07456, ECO:0000269|PubMed:11877257, ECO:0000269|PubMed:15683711, ECO:0000269|PubMed:21356557, ECO:0000269|PubMed:22096585, ECO:0000269|PubMed:23157686, ECO:0000269|PubMed:23642167, ECO:0000269|PubMed:25698971, ECO:0000269|PubMed:32092412, ECO:0000269|PubMed:32823731}. [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion (PubMed:25301953, PubMed:20463016). Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases (PubMed:16873769, PubMed:10480954, PubMed:15917224). As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (PubMed:16873769). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (PubMed:7676539). {ECO:0000250|UniProtKB:Q07456, ECO:0000269|PubMed:10480954, ECO:0000269|PubMed:15917224, ECO:0000269|PubMed:16873769, ECO:0000269|PubMed:20463016, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:7676539}. [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000250|UniProtKB:Q64240}.
DE  Reference Proteome: Yes;
DE  Interaction: P69616; IntAct: EBI-7810311; Score: 0.53
DE  Interaction: P07858; IntAct: EBI-7970369; Score: 0.60
DE  Interaction: Q92569; IntAct: EBI-2115171; Score: 0.00
DE  Interaction: P62993; IntAct: EBI-2115716; Score: 0.00
DE  Interaction: P42336; IntAct: EBI-2116612; Score: 0.00
DE  Interaction: P10176; IntAct: EBI-3904736; Score: 0.37
DE  Interaction: Q9Y4D1; IntAct: EBI-3908964; Score: 0.37
DE  Interaction: P40763; IntAct: EBI-3926609; Score: 0.37
DE  Interaction: Q99XU0; IntAct: EBI-8852714; Score: 0.35
DE  Interaction: Q13643; IntAct: EBI-10193895; Score: 0.56
DE  Interaction: P14335; IntAct: EBI-11422579; Score: 0.37
DE  Interaction: Q99IB8; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-16716791; Score: 0.40
GO  GO:0072562;
GO  GO:0009986;
GO  GO:0062023;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0031314;
GO  GO:0005743;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0016209;
GO  GO:0019855;
GO  GO:0046904;
GO  GO:0030246;
GO  GO:0035374;
GO  GO:0098633;
GO  GO:0020037;
GO  GO:0019862;
GO  GO:0016491;
GO  GO:0016653;
GO  GO:0042803;
GO  GO:0004867;
GO  GO:0007155;
GO  GO:0098869;
GO  GO:0034614;
GO  GO:1903606;
GO  GO:0007565;
GO  GO:0042167;
GO  GO:0020027;
GO  GO:0050777;
GO  GO:0046329;
GO  GO:0030163;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:23157686};
SQ  MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEIS
SQ  MTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRET
SQ  LLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPC
SQ  MGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGC
SQ  QGNGNKFYSEKECREYCGVPGDGDEELLRFSN
//
ID  Q62577;
PN  Trypstatin;
GN  AMBP;
OS  10047;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Alpha-1-microglobulin]: Secreted {ECO:0000250|UniProtKB:P02760}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P02760}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02760}. Cell membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Nucleus membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02760}. Note=The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. {ECO:0000250|UniProtKB:P02760}.
DR  UNIPROT: Q62577;
DR  UNIPROT: Q62576;
DR  Pfam: PF00014;
DR  Pfam: PF00061;
DR  PROSITE: PS00280;
DR  PROSITE: PS50279;
DE  Function: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species- induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis. Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential. Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage. Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures. Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria. Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (By similarity). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}. [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion. Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule- stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases. As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (By similarity). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}. [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000250|UniProtKB:Q64240}.
DE  Reference Proteome: No;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0031314;
GO  GO:0005743;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0016209;
GO  GO:0035374;
GO  GO:0098633;
GO  GO:0020037;
GO  GO:0019862;
GO  GO:0016491;
GO  GO:0016653;
GO  GO:0042803;
GO  GO:0004867;
GO  GO:0098869;
GO  GO:0034614;
GO  GO:1903606;
GO  GO:0020027;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P02760};
SQ  MKGLGTLFLLLTACLASRADDAATLPDIQVQENFIESLIYGKWFNLAVGSTCPWLRRIKDKMSMSTLVLQEGATEAEISM
SQ  TSTRWRRGVCEEISGAYEKTDIDGKFLYHKSKWNITLETYVVHTNYDEYAIFLTKKFSHYHGPTITLKLYGREPKLRDSL
SQ  LLEFREVALSMGIPENSIVFMADKGECVPGDQEVKPSPHLRARRAVLPQENEGSGSEPLVTGILKKEDSCQLTYSEGPCL
SQ  GMMERYHYNGTSMACETFQYGGCLGNGNNFISEKECLQTCRTVAACNLPIVQGPCRAYIKLWAFDAAQGKCIQFTYGGCK
SQ  GNGNKFYSEKECKEYCGVPGDGDKTN
//
ID  Q60559;
PN  Trypstatin;
GN  AMBP;
OS  10036;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Alpha-1-microglobulin]: Secreted {ECO:0000250|UniProtKB:P02760}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P02760}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02760}. Cell membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Nucleus membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02760}. Note=The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. {ECO:0000250|UniProtKB:P02760}.
DR  UNIPROT: Q60559;
DR  UNIPROT: Q60558;
DR  UNIPROT: Q9QW86;
DR  UNIPROT: Q9QW87;
DR  Pfam: PF00014;
DR  Pfam: PF00061;
DR  PROSITE: PS00280;
DR  PROSITE: PS50279;
DR  PROSITE: PS00213;
DE  Function: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species- induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis. Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential. Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage. Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures. Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria. Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (By similarity). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}. [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion. Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule- stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases. As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (By similarity). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}. [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000250|UniProtKB:Q64240}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0031314;
GO  GO:0005743;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0016209;
GO  GO:0035374;
GO  GO:0098633;
GO  GO:0020037;
GO  GO:0019862;
GO  GO:0016491;
GO  GO:0016653;
GO  GO:0042803;
GO  GO:0004867;
GO  GO:0098869;
GO  GO:0034614;
GO  GO:1903606;
GO  GO:0020027;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P02760};
SQ  MLGLGTLFLLLAACPASRADPVPALPDIQVQENFNESRIYGKWFNLAVGSTCPWLSRIKNKMSMSTLVLREGATGAEIST
SQ  TSTRWRRGVCEEVSGTYEKTDMDGKFLYHKSKWNVTLESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGREPQLRDSL
SQ  LQEFREVALSVGIPENSIVFMEDRGECVPGDLEQKSTSLLRARRAVLPQENEGSGTGPLVTDVLKKEDSCQLSYSEGPCL
SQ  GMIEKYYYNGASMACETFHYGGCLGNGNNFNSEKECLQTCRTVAACSLPIVQGPCRAYVELWAFDAAQGKCVQFSYGGCK
SQ  GNGNKFYSEKECKEYCGVPGDGYEELTRS
//
ID  Q07456;
PN  Trypstatin;
GN  Ambp;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Alpha-1-microglobulin]: Secreted {ECO:0000250|UniProtKB:P02760}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P02760}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02760}. Cell membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Nucleus membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02760}. Note=The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. {ECO:0000250|UniProtKB:P02760}.
DR  UNIPROT: Q07456;
DR  UNIPROT: Q61294;
DR  UNIPROT: Q925W1;
DR  UNIPROT: Q9DBJ9;
DR  Pfam: PF00014;
DR  Pfam: PF00061;
DR  PROSITE: PS00280;
DR  PROSITE: PS50279;
DR  PROSITE: PS00213;
DE  Function: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species- induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis. Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential. Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage. Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures. Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria. Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (By similarity). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (PubMed:32092411). {ECO:0000250|UniProtKB:P02760, ECO:0000269|PubMed:32092411}. [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion. Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule- stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases. As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (By similarity). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (PubMed:11145954, PubMed:11243855). Also inhibits calcium oxalate crystallization (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000269|PubMed:11145954, ECO:0000269|PubMed:11243855}. [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000250|UniProtKB:Q64240}.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0062023;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005615;
GO  GO:0031314;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0016209;
GO  GO:0035374;
GO  GO:0098633;
GO  GO:0020037;
GO  GO:0019862;
GO  GO:0016653;
GO  GO:0042803;
GO  GO:0004867;
GO  GO:0098869;
GO  GO:0034614;
GO  GO:1903606;
GO  GO:0020027;
GO  GO:0030163;
GO  GO:0051604;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P02760};
SQ  MQGLRTLFLLLTACLASRADPASTLPDIQVQENFSESRIYGKWYNLAVGSTCPWLSRIKDKMSVSTLVLQEGATETEISM
SQ  TSTRWRRGVCEEITGAYQKTDIDGKFLYHKSKWNITLESYVVHTNYDEYAIFLTKKSSHHHGLTITAKLYGREPQLRDSL
SQ  LQEFKDVALNVGISENSIIFMPDRGECVPGDREVEPTSIARARRAVLPQESEGSGTEPLITGTLKKEDSCQLNYSEGPCL
SQ  GMQERYYYNGASMACETFQYGGCLGNGNNFISEKDCLQTCRTIAACNLPIVQGPCRAFIKLWAFDAAQGKCIQFHYGGCK
SQ  GNGNKFYSEKECKEYCGVPGDGYEELIRS
//
ID  P04366;
PN  Trypstatin;
GN  AMBP;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Alpha-1-microglobulin]: Secreted {ECO:0000250|UniProtKB:P02760}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P02760}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02760}. Cell membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Nucleus membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02760}. Note=The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. {ECO:0000250|UniProtKB:P02760}.
DR  UNIPROT: P04366;
DR  UNIPROT: P34954;
DR  Pfam: PF00014;
DR  Pfam: PF00061;
DR  PROSITE: PS00280;
DR  PROSITE: PS50279;
DR  PROSITE: PS00213;
DE  Function: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species- induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis. Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential. Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage. Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures. Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria. Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (By similarity). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}. [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion. Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule- stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases. As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (By similarity). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}. [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000250|UniProtKB:Q64240}.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0031314;
GO  GO:0005743;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0016209;
GO  GO:0035374;
GO  GO:0098633;
GO  GO:0020037;
GO  GO:0019862;
GO  GO:0016491;
GO  GO:0016653;
GO  GO:0042803;
GO  GO:0004867;
GO  GO:0098869;
GO  GO:0034614;
GO  GO:1903606;
GO  GO:0020027;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P02760};
SQ  AVSASPVLTLPNDIQVQENFDLSRIYGKWFHVAVGSTCPWLKRFKDKMTMGTLMLGEGATEREISVTKTHRRKGICEVIS
SQ  GAYEKTSTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRRHGPTLTAKLYGREPQLRESLLEEFREVALGVGIP
SQ  EDSIFTMPDRGECVPGEQEPEPTLLSRARRAVLPQEEEGSGAGQPVADFSKKEDSCQLGYSQGPCLGMIKRYFYNGSSMA
SQ  CETFHYGGCMGNGNNFVSEKECLQTCRTVEACSLPIVSGPCRGFFQLWAFDAVQGKCVLFNYGGCQGNGNQFYSEKECKE
SQ  YCGVPGEEDEELLRSSN
//
ID  Q64240;
PN  Trypstatin;
GN  Ambp;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Alpha-1-microglobulin]: Secreted {ECO:0000250|UniProtKB:P02760}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P02760}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02760}. Cell membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Nucleus membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02760}. Note=The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. {ECO:0000250|UniProtKB:P02760}.
DR  UNIPROT: Q64240;
DR  UNIPROT: P19603;
DR  UNIPROT: Q63336;
DR  Pfam: PF00014;
DR  Pfam: PF00061;
DR  PROSITE: PS00280;
DR  PROSITE: PS50279;
DR  PROSITE: PS00213;
DE  Function: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species- induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis. Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential. Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage. Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures. Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria. Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (By similarity). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}. [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion. Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule- stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases. As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (By similarity). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (By similarity). {ECO:0000250|UniProtKB:P02760, ECO:0000250|UniProtKB:Q07456}. [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000269|PubMed:3263966}.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005615;
GO  GO:0031314;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0016209;
GO  GO:0035374;
GO  GO:0098633;
GO  GO:0020037;
GO  GO:0019862;
GO  GO:0016491;
GO  GO:0016653;
GO  GO:0042803;
GO  GO:0004867;
GO  GO:0098869;
GO  GO:0034614;
GO  GO:1903606;
GO  GO:0020027;
GO  GO:0030163;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P02760};
SQ  MQGLGALFLLLTACLTLKADNVPTLPDIQVQENFNEARIYGKWFNLAVGSTCPWLRRIKNKMSVSTLVLQEGATEAEISV
SQ  TSTQWRKGVCEEISGVYQKTDIDGKFLYHKSKWNATLESYVVHTNYDEYAIFLTKKFSHRHGPTITAKLYGREPQLRDSL
SQ  LQEFREVALSVGIPENSIVFMADRGECVPGDREVESTSFARARRAVLPQENEGSGSEPLITGTLKKEDSCQLNYSEGPCL
SQ  GMQQKYYYNGASMACETFQYGGCLGNGNNFASEKECLQTCRTIAACNLPIVQGPCRAFAELWAFDAAQGKCIQFIYGGCK
SQ  GNGNKFYSEKECKEYCGVPGDGYEELTRS
//
ID  G0S381;
PN  Nucleoporin AMO1;
GN  AMO1;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49686}. Nucleus membrane {ECO:0000250|UniProtKB:P49686}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49686}; Cytoplasmic side {ECO:0000250|UniProtKB:P49686}.
DR  UNIPROT: G0S381;
DR  UNIPROT: G0ZGU0;
DR  PDB: 6B4G;
DR  PDB: 6B4H;
DR  Pfam: PF00642;
DR  PROSITE: PS50103;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). AMO1 is specifically important for nuclear protein and mRNA export. {ECO:0000250|UniProtKB:P49686}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046872;
GO  GO:0034641;
GO  GO:0043170;
GO  GO:0051028;
GO  GO:0044238;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P49686};
SQ  MTVCRFWQQGYCRNGNACKFEHPPKGGQNYNRFGALSGSGQGMGGRVSEPPHYPGLSEDAIQKDLTSELPTWILSCYGPG
SQ  RDAPEQLFGGYPREQSFEEIRLHFYNGLMAGNPQGALNEIQAAYQAAQQQIQNTLQNIPAAVQFILDAANKHPNRIDICR
SQ  ESSKGSSTGGSVFGRNVNPFQQSSAAPLNPFGAPSTPSTSAFGQPSPLGQKSSAFGTPAFGQPSQPVSAFGKPSALGGGS
SQ  AFGSPQTGSTFGQPSVLGAKPSAFGQPAFGQPAFGQPAFGQSAFGQPSALGPKPGAFGTSAGSAFGASTTTAPSPFGAAA
SQ  QATQPANPFGQPSQQAANSFGKPAAPASAFGQPSTTTAQNPFGQPSTQSSAFGQQQPQQAGTFGSPSLFGQQQQQPSNVF
SQ  GQPSTTSAFGSQAATSGFSQLGNATSTIGASPAGAQAPASKSPYHPGSTRQHPDLLSYATKNPAGGLDTFKGKPVVYETP
SQ  KGAAKPVPHIRQFDGTLVRIWMPDGAPAYTADTEAEDPKVYEDEGVKRQWQSFLEKGRFEGGMPEVPPRREWCVWDF
//
ID  Q9N4M4;
PN  Nuclear anchorage protein 1;
GN  anc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:15773756, ECO:0000305|PubMed:12169658}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:15773756}. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated either with the nuclear envelope, most probably the outer nuclear membrane, or with mitochondrial membrane. {ECO:0000305|PubMed:12169658}.
DR  UNIPROT: Q9N4M4;
DR  UNIPROT: O61841;
DR  UNIPROT: O61842;
DR  UNIPROT: Q6IMP3;
DR  Pfam: PF00307;
DR  Pfam: PF10541;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS51049;
DE  Function: Plays a central role in nuclear and mitochondrial anchoring (PubMed:12169658, PubMed:6889924, PubMed:10375507, PubMed:22298703). Probably connects nuclei to the cytoskeleton by interacting with unc-84 at the nuclear envelope and with F-actin in the cytoplasm, creating a bridge across the nuclear envelope between the cytoskeleton and the nucleus (PubMed:15773756). Has a role in positioning of the cell body of the PVQ lumbar interneuron (PubMed:22298703). {ECO:0000269|PubMed:10375507, ECO:0000269|PubMed:12169658, ECO:0000269|PubMed:22298703, ECO:0000269|PubMed:6889924, ECO:0000303|PubMed:15773756}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0051087;
GO  GO:0007010;
GO  GO:0051179;
GO  GO:0051647;
GO  GO:0006997;
GO  GO:0035046;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MSSSPPARPCCVCFRFRPHEDEKAQKNTFTRWINFHLEEHSSSGRIEDLFEDIRDGVLLCHLIEVLTGEALAVHKGRVSK
SQ  RVHHIANLTTALTVLRRRGLELINNNAADIADGNPRIVLGLIWQIILHFQIETNMILLREWGWAATGTEEPTSSAQPEVV
SQ  VTAPSPTPSSKKSHSKVSSLSGSKTSLASGEKAPSSPLRQRIASFLTPTKKAPKLTAQPVKQSVEQVFLRWINAEIGDLV
SQ  GGRRVENMDKQWRDGILFCALVSRWRPDVISMREVTNANPRDNLELAFNLAHQHLGVRRLLAVEDMMIEKPDKRSVITYV
SQ  SQFVRMFGERSPMQGREQHEIFLAWLEATYLLCTRHELNSQECSRIRREFIEHRPLFNTIIVTKVNYDVEELVEIEKKWD
SQ  CIRETLEKYARRSERDLPEPFASIATWIAGAEHILSRPLDLDATDAKKTVTMLQKLISEHQKYMEDLPKRQEDFEEAVKH
SQ  GGLGGRPVAPEFSEPLRARFAQIEEENEPRISTLRILTTHYILLQYLQHIDEKIILWRTADSVTLLLRWIKEYTQLNAEN
SQ  PQAKCASYINKITLTMANDQNSKLDKEAILNTSNEKTAETLKRFESLWIELKLLKVEWVEWETHVSQLEEIIEERRRNGV
SQ  PPTPEDEQALAVITAGADQLAPKLGASARLSNNQRLDVLTHSFKKLTKTTIKIGGRLVVELEPSTSEQASKISYSWQASD
SQ  ELLKVEMQLRDRIQRDADSSDREQLEYRAETFRNIRDKLIELERLNEIYDNHSRDQVDTPNRNLIRHDMGTIIYGLQAGQ
SQ  YANFVDLSCYAFVYDEYNQVPVNLTENVLSEDYVREIVNRKKAILTRRENNEDEIRESIRDMEECDRIIEGWQSTEIEEL
SQ  RAEWNIKLSEFESWHEMMQQVEVLSQTIQTRLDVTVIQTIWILKERSYDIKHSELGGTLRESLEQLATTSETSVNRHLQN
SQ  LELSNEQDCPDAIEFLEEVGRESVSKLSAAVDDRYIYTLHVLRTKMELFRRLQNFCDAVKILRSQNTKWNGIKISQIDQV
SQ  QSEIDTLIVRLDEEWTQDANQLRAELASIHGSFFQLEFDRLNEKLNMLIHDKDKLRELMVHRRHYLTAANELITDSKTDL
SQ  AQRATSSDHPDDILRATDEVTKALDIKGEELRRLGELAEMNITDLVVVALILSFRRRQLGSEGEPEVEELRRALREIIAR
SQ  PITEPRDVSPDAIVADILRMKDEKKRDEKTIDEIQATTLTDEQRASFAPLIEDYRRRADRHRIVFEHLVMIYLDWLSRQF
SQ  DELEDEIGMTIQTSRADDLRRMNSTEWNKWKTDLANIERQVGPDTKKALSAELADLHRKRDSMEARINKYLTHSAKINAK
SQ  LTQFEKWLNAIEEDIEQTERQFEDPERSYRFGSLHEVALAKQRLVAKLERLNVANKEEVLRLCERYHTIMHKLTPFQTAV
SQ  GLPLHVSTNLDRNGPFQSQISVSSIASSELERPESVMSLTSSIGVIPADVAELSPFEAKINKLLQKLHIIEDSYLKGPKP
SQ  IDTVREDVKQLEKYRNRGAEILQQLSTSNIEDAEKEGLKHRFVLMLNNYDDILRSIENEIRDDNELTAKNQEILAELSNA
SQ  EQTLQNSPLEDLDISAELDRLQMQLDLVKVMCNKPRKYVECELIDSSREGSPQERRRRKKKVMVMVSNTITTIIHVVEER
SQ  LEASDISRNPDVQQKLVAVKENLRELDTTTVTPHPPSIMSPLGTENRNDLEEVKRLAAEIDRAIDTASSMYEDAPTDEDA
SQ  LKSAIHLLDDQKVTLNHLHVVLEGIPEKNEQDRTDAIDIASSVGEKLGNLKSAVEEVYEEVLASTNPVKEDQPLQHIQEV
SQ  QTTPAEQSNWDTDEFSRQPPVLSDERIELKTDPSAIDKFEVRSDEDPVPKIIDLFGQLQTAVNEASPLACEGTDDVDALQ
SQ  VASDKLTKQDRTIRKIHAILDTIDDPVQKPAIIESLDKIKDQINNARDNINRQIDNLNYNQTPVVVPKESTKTPLNEIED
SQ  AVRQASTVVSDELCNTEKLLSARQTLANVKPQVDSVEANVWSNPETIETVTPILEEYTTLVDNIEKKLANEIEVPTNDPS
SQ  RQDLVQQLQDVILECEEVVVNCDNIEKLEESKLKLEKARPLLDQIGDNVEKLSREQSPDTSDAIDALSNVHQQYNATIMS
SQ  IDDKIDELKNPEEDTSAADQLISELHVISEMPAVTIDLSMLNAIEEGLSTLPAHQAENVQAKIDELRQKKEVADQTEQIL
SQ  SDLNAFGDMPAITLDLDLLKSVEDGIAVLPVEDSERIKAKIVDLRKKKEDADQAEALLQELSVISDMPISTLDLNMLQGI
SQ  EDNLNSLPAEESDEIREKLNELRRRKQESDQAEALLQELSVISDMPISTLDLNMLQGVEDNLNSLPTEEADKIREKINDL
SQ  RRRKQESDLAEALLQELSVIYDMPTSTIDLNMLQGIEDNLNSLPAEESDKIREKINDLRRRKQESDLAEALLQELSVIYD
SQ  MPTSTIDLNMLQGIEDNLNSLPAEESDKIREKINDLRRRKQESDQAEALLQELSVVSDMPASTIDINMLQSIEDGLSTLL
SQ  SEDRSKIQQAIDSLRKKKSDSDLAQHALEALSVQSKLPSVSINLEELKKLEETLSTVPVEDSKVIRDKIAELKTEKALAD
SQ  HAENYLVELKKIEDMPISAVGSDVLATIEDQILQMPVQYQPSVKETLDKLKQAKEEDDKLAGVYDELEKIAKLPARDYDN
SQ  KLLAKIDEKLNSLPKDQIAETHRKVEDIKVTKADIVAQIDVLDKLPAKDIDEHLLNSIEEKLPTIPSDSSDQLQIAIGKL
SQ  RDRKQANIDEGKKILNELAEIQKMPADSLNEHALNLLATESDKFGSEISDKIMQEIDVLREKQNNHEVARLNAESVLQQL
SQ  DKISEEPHLSLTEERLAPFLQNIDTVPACFVDKIRNKINEVQKLHDEAVQDEKDELKEKLVAKVQNIGKTSIDDVNVSDF
SQ  EEIEREINGSLEAFEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSA
SQ  KVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVP
SQ  SSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDV
SQ  VSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDR
SQ  LNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNK
SQ  AAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQ
SQ  LGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYND
SQ  LLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKA
SQ  VIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRN
SQ  NSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKM
SQ  IDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLI
SQ  LSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAK
SQ  ESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKL
SQ  NNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTG
SQ  DDEKRADELKNDDGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELL
SQ  QALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLV
SQ  VGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPEND
SQ  PTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDRGRSTGSAVG
SQ  DKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLA
SQ  TAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAP
SQ  SSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLS
SQ  DLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDP
SQ  ERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLN
SQ  ISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKK
SQ  KKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDA
SQ  IKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRA
SQ  DELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKA
SQ  IPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEK
SQ  VFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADEL
SQ  RQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVS
SQ  GVKPDELDDKERAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQ
SQ  YAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQ
SQ  PKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLL
SQ  KQSASQVANEIDDISKMIDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTE
SQ  LDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAA
SQ  HDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFV
SQ  KDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRD
SQ  RAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDP
SQ  QVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSN
SQ  NEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVE
SQ  NQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNAARKNAEDALLDITREDGGDDNKS
SQ  PDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIV
SQ  SRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERARLWNEFL
SQ  AARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQRISELLDPLESAYADVRFFDVDAE
SQ  QTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDPERSILDTIAKSDIPALKAQINRIKDRIVNADASR
SQ  KHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQLKSDDLKTAEKEITNSLKPEEAE
SQ  PLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEMIDELSAKVVEAKALIPKIEEAAK
SQ  NENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDAEKTVVPSSVPALSEFKDRIAPHL
SQ  ATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAVKNVEDVVSKYQNQPQPLDVAKDD
SQ  ANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQAEINDRLNNLEKELTKVDEFKPE
SQ  DALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDKKQALNKAAAVNEIAPKLQLVSQQ
SQ  LQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRLKDLLKQLGSAVGDKLAALAAFNA
SQ  ARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKERAEYNDLLARLATAADVLKNKRA
SQ  ELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKEVEAAKAVIANAPSSDAHVQQLEQ
SQ  AVATAETLIPDLEERARLWNEFLAARNDIDALIEQLQQPLDAVLAQPKRSAEEAAQDVENLRNNSQQLSDLDNKIANLQR
SQ  ISELLDPLESAYADVRFFDVDAEQTRHQYDDVLNDVAAELEDETLLKQSASQVANEIDDISKMIDSTDPERSILDTIAKS
SQ  DIPALKAQINRIKDRIVNADASRKHVTTDPKIAEDLDNKLAKLQTELDDAIKTSDEHDKEQLILSLKLNISQFEQIPLDQ
SQ  LKSDDLKTAEKEITNSLKPEEAEPLLAKIQELREAKRVGDEARSAAHDQIVALEKEAEDVTAKESAKKKKKDKKKSPQEM
SQ  IDELSAKVVEAKALIPKIEEAAKNENLPADDKPKAEQLVSNLEAFVKDVETQVSEKQDELDKLNNANDAIKRLGDALDDA
SQ  EKTVVPSSVPALSEFKDRIAPHLATLVEAVNDVPASVEPSAVALRDRAAKFVSDLEKNIQKTGDDEKRADELKNDVGNAV
SQ  KNVEDVVSKYQNQPQPLDVAKDDANKLKATVEQLTKLAESSDKIDPQVAKDIKDSKTKAKELLQALEKAIPQEDAIRREQ
SQ  AEINDRLNKLEKELTKVDEFKPEDALPIVDQLAANTNTLKTATDSNNEKAVAPSSLISHDDLVVGLPEKVFQLQHAIDDK
SQ  KQALNKAAAVNEIAPKLQLVSQQLQSVPQEVPASLDEQKQLLEDVENQKHNLENLLANLPENDPTADELRQKSQWDLSRL
SQ  KDLLKQLGSAVGEKLAALAAFNAARKNAEDALLDITREDGGDDNKSPDELIDDLAKKEETVAKLLDTVSGVKPDELDDKE
SQ  RAEYNDLLARLATAADVLKNKRAELEQAVKAKADEKSLHDSVDRIVSRLVPLVRESDELRHNAEAVPTQYAPKAEELKKE
SQ  VEAAKAVIANAPSSDAHVQQLEQAVATAETLIPDLEERASIWERFVKAKDDLYDYLEKLENNVSDVLNRPRLPVSQAQQR
SQ  FNKLKEQSYLLDRIRDLKIDFDDLGEALLPLTVAEDELRFMHVHVESIERQYEDTMDKLNAEITAEVELLRTLDILSNEL
SQ  SQCKEDINNPSVDVDELSRATMLNDAIAHLENQKVVVARSEKDRKFVESSTSIDLDQLLAEAKRLLKEIEPRLQLAQPDH
SQ  DNEDDEDEEKGSDEKPYDVRAAAEVLSALYPDEHPHNVLRNIGFEELPSDSESRSEFDSLDSRSDGLLSPIPDDSTLSEE
SQ  QLRRQRSRWRRVLRTALPLQALLVLLMGAACLVPHCDDEYCCQLLNNFAKSFDPSLEFVNGPPPF
//
ID  H2KZB2;
PN  Ankyrin repeat and LEM domain-containing protein 2 homolog;
GN  lem;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:22770216}; Single-pass membrane protein {ECO:0000269|PubMed:22770216}.
DR  UNIPROT: H2KZB2;
DR  UNIPROT: Q5W7E5;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of baf-1 during mitotic exit. Coordinates the control of baf-1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of baf-1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex. {ECO:0000269|PubMed:22770216}.
DE  Reference Proteome: Yes;
DE  Interaction: Q03565; IntAct: EBI-6258976; Score: 0.44
DE  Interaction: Q19848; IntAct: EBI-6258976; Score: 0.56
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0051721;
GO  GO:0051301;
GO  GO:0007084;
GO  GO:0042326;
GO  GO:0035307;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGRKSAILAVILAIIYFRSNFSKMSNTPVQETEGPVYVAYSMEDMLKSPRDLYKSVKEVAKFVNSAEGKSMSARFKKFGT
SQ  PREAMDFLAYGDAPTTPKTVPPVAPTEPNSPFSGVNRIQMNEFKKYVEKGDMENFLRLVDSNPRFLVNTGGDVASIVMEG
SQ  FRYNALHIAAKAGQTEIIAKILELIQNIDFLIRLYGTGADDVTLRKINILDSYLNTPDKGNSDTPLHFASKFGKIGVVRV
SQ  LTENSATDRTLLNKSGKSALDCAGERYTGEDKDMVQRDIHLAIEGFYVFLHRNPTTGSTQLTVSQKPPATYSTSPTTATV
SQ  TVSAQAGPFFTEREARDFAKSWQTAGKELKRTDFDKGWERVGRVLAEQSEAMWRETWHFLGSMELLDLGSEQGLGVLEAF
SQ  LREKRRGNLRNSEISEISTKKSIFRRGIHARKLDFGILDGEKSAEISENLTPDGSDSADDEDDDDIFYDTFSEIPAAAEK
SQ  SINDPDDTLGSLTDRFAAISIFSPLPPPPPPQWSNSPNFDYSEGEDSFATPPTTPPPTFVADDEPCKIDNDLFEVLAQIS
SQ  SELISKFPLTQDYVQKLGKLTAHDRSTWRPIDSPARCDSRRKI
//
ID  Q8MQX9;
PN  Ankyrin repeat and LEM domain-containing protein 2 homolog;
GN  Ankle2;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum {ECO:0000269|PubMed:31735666}. Nucleus envelope {ECO:0000269|PubMed:31735666}. Cytoplasm {ECO:0000269|PubMed:31735666}. Note=In neuroblasts, recruited to the nuclear envelope at the initiation of mitosis and remains associated with it until the beginning of cytokinesis. {ECO:0000269|PubMed:31735666}.
DR  UNIPROT: Q8MQX9;
DR  UNIPROT: Q0KHR1;
DR  UNIPROT: Q9VX44;
DR  UNIPROT: X2JCC5;
DR  Pfam: PF13637;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Involved in brain development probably by regulating asymmetric division of neuroblasts (PubMed:31735666, PubMed:30550790, PubMed:25259927). Regulates neuroblast asymmetric cell division by controlling asymmetric protein localization of Mira, Baz, Par-6 and aPKC, and spindle alignment (PubMed:31735666). Also, regulates the localization of kinase Ball during mitosis, specifically maintaining Ball in the nucleus during interphase (PubMed:31735666). Required for proper ER and nuclear envelope morphology in neuroblasts (PubMed:31735666). {ECO:0000269|PubMed:25259927, ECO:0000269|PubMed:30550790, ECO:0000269|PubMed:31735666}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VXY7; IntAct: EBI-9936142; Score: 0.35
GO  GO:0005737;
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0051721;
GO  GO:0055059;
GO  GO:0045167;
GO  GO:0000902;
GO  GO:0007029;
GO  GO:0042326;
GO  GO:0031468;
GO  GO:0035307;
GO  GO:0051653;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTYFGVYIPTSKAGCFEGSVSQCIGSIAAVNIKPSNPASGSASVASGSPSGSAASVQTGNADDGSAATKYEDPDYPPDS
SQ  PLWLIFTEKSKALDILRHYKEARLREFPNLEQAESYVQFGFESIEALKRFCKAKPESKPIPIISGSGYKSSPTSTDNSCS
SQ  SSPTGNGSGFIIPLGSNSSMSNLLLSDSPTSSPSSSSNVIANGRQQQMQQQQQQQPQQPDVSGEGPPFRAPTKQELVEFR
SQ  KQIEGGHIDRVKRIIWENPRFLISSGDTPTSLKEGCRYNAMHICAQVNKARIAQLLLKTISDREFTQLYVGKKGSGKMCA
SQ  ALNISLLDYYLNMPDKGRGETPLHFAAKNGHVAMVEVLVSYPECKSLRNHEGKEPKEIICLRNANATHVTIKKLELLLYD
SQ  PHFVPVLRSQSNTLPPKVGQPFSPKDPPNLQHKADDYEGLSVDLAISALAGPMSREKAMNFYRRWKTPPRVSNNVMSPLA
SQ  GSPFSSPVKVTPSKSIFDRSAGNSSPVHSGRRVLFSPLAEATSSPKPTKNVPNGTNECEHNNNNVKPVYPLEFPATPIRK
SQ  MKPDLFMAYRNNNSFDSPSLADDSQILDMSLSRSLNASLNDSFRERHIKNTDIEKGLEVVGRQLARQEQLEWREYWDFLD
SQ  SFLDIGTTEGLARLEAYFLEKTEQQADKSETVWNFAHLHQYFDSMAGEQQQQLRKDKNEAAGATSPSAGVMTPYTCVEKS
SQ  LQVFAKRITKTLINKIGNMVSINDTLLCELKRLKSLIVSFKDDARFISVDFSKVHSRIAHLVASYVTHSQEVSVAMRLQL
SQ  LQMLRSLRQLLADERGREQHLGCVCASLLLMLEQAPTSAVHLPDTLKTEELCCAAWETEQCCACLWDANLSRKTSRRKRT
SQ  KSLRAAAVVQSQGQLQDTSGSTGSSALHASLGVGSTSLGASRVVASASKDAWRRQQSDDEDYDSDEQVIFFDCTNVTLPY
SQ  GSSSEDEENFRTPPQSLSPGISMDLEPRYELFIFGNEPTKRDLDVLNALSNVDIDKETLPHVYAWKTAMESYSCAEMNLF
SQ  PSPRNVKVQKPEPWYSGTSSSHNSQPLLHPKRLLATPKLNAVVSGRRGSGPLTAPVTPRLARTPSAASIQVASETNGESV
SQ  GTAVTPASPILSFAALTAATQSFQTPLNKVRGLFSQYRDQRSYNEGDTPLGNRN
//
ID  P27214;
PN  Annexin A11;
GN  ANXA11;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. Nucleus envelope {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus. Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent. {ECO:0000250}.
DR  UNIPROT: P27214;
DR  UNIPROT: P27215;
DR  UNIPROT: Q0VD55;
DR  Pfam: PF00191;
DR  PROSITE: PS00223;
DR  PROSITE: PS51897;
DE  Function: Binds specifically to calcyclin in a calcium-dependent manner. Required for midbody formation and completion of the terminal phase of cytokinesis. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0042470;
GO  GO:0016020;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005819;
GO  GO:0005509;
GO  GO:0005544;
GO  GO:0044548;
GO  GO:0032506;
GO  GO:0006909;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSYPGYPPPAGGYPPGAPGGGAWGGAGYPPPTMPPIGLDNVANYAGQFNQDYLSGVAANMSGTFGGANVPNLYPGAPGGG
SQ  YPPVPPGGFGQPPPAQQPVPSYGMYPPPGGNPTSGMPSYPPYPGAPVPGQPMLPPGQQPPGVYPGQPPMTYPGQSPVPPP
SQ  GQQPVPSYPGYSGSGTVTPAVSPAQFGNRGTITDASGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSF
SQ  KTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDAYEIKEAIKGAGTDEACLIEILASRSNEHIRELNRVYKTEFKKTL
SQ  EEAIRSDTSGHFQRLLISLSQGNRDESTNVDMTLVQRDVQELYAAGENRLGTDESKFNAILCSRSRAHLVAVFNEYQRMT
SQ  GRDIEKSICREMSGDLEQGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSEIDLLDIRAEYKRLYGKSLY
SQ  HDITGDTSGDYRKILLKICGGND
//
ID  P50995;
PN  Annexin A11;
GN  ANXA11;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:28469040}. Melanosome. Nucleus envelope. Nucleus, nucleoplasm {ECO:0000269|PubMed:28469040}. Cytoplasm, cytoskeleton, spindle. Note=Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus (By similarity). Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent. {ECO:0000250}.
DR  UNIPROT: P50995;
DR  UNIPROT: B4DVE7;
DR  Pfam: PF00191;
DR  PROSITE: PS00223;
DR  PROSITE: PS51897;
DR  OMIM: 602572;
DR  OMIM: 617839;
DR  DisGeNET: 311;
DE  Function: Binds specifically to calcyclin in a calcium-dependent manner (By similarity). Required for midbody formation and completion of the terminal phase of cytokinesis. {ECO:0000250, ECO:0000269|PubMed:15197175}.
DE  Disease: Amyotrophic lateral sclerosis 23 (ALS23) [MIM:617839]: A form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. ALS23 is an autosomal dominant form with incomplete penetrance. {ECO:0000269|PubMed:28469040}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-752707; Score: 0.55
DE  Interaction: P00533; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: P09104; IntAct: EBI-731812; Score: 0.00
DE  Interaction: P31942; IntAct: EBI-734775; Score: 0.00
DE  Interaction: O75340; IntAct: EBI-2338752; Score: 0.75
DE  Interaction: Q5NHS4; IntAct: EBI-2808973; Score: 0.00
DE  Interaction: A0A6L8PQC3; IntAct: EBI-2838236; Score: 0.00
DE  Interaction: A0A380PL96; IntAct: EBI-2843651; Score: 0.00
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q93034; IntAct: EBI-21331078; Score: 0.35
DE  Interaction: Q8IUH5; IntAct: EBI-9090498; Score: 0.37
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: P08563; IntAct: EBI-11477906; Score: 0.40
DE  Interaction: Q9WVM1; IntAct: EBI-11008211; Score: 0.35
DE  Interaction: Q80UG5; IntAct: EBI-11121465; Score: 0.35
DE  Interaction: Q91ZJ0; IntAct: EBI-11131714; Score: 0.35
DE  Interaction: Q8NI38; IntAct: EBI-24751877; Score: 0.56
DE  Interaction: Q96AE4; IntAct: EBI-24374647; Score: 0.56
DE  Interaction: Q53EZ4; IntAct: EBI-24386584; Score: 0.78
DE  Interaction: Q3LI66; IntAct: EBI-24537226; Score: 0.56
DE  Interaction: Q9NZC7; IntAct: EBI-24573309; Score: 0.56
DE  Interaction: Q52LG2; IntAct: EBI-24587720; Score: 0.56
DE  Interaction: P15289; IntAct: EBI-24600393; Score: 0.56
DE  Interaction: Q92734; IntAct: EBI-12700650; Score: 0.67
DE  Interaction: P36810; IntAct: EBI-26503730; Score: 0.49
DE  Interaction: P60033; IntAct: EBI-20568535; Score: 0.35
DE  Interaction: Q15828; IntAct: EBI-21887792; Score: 0.40
DE  Interaction: Q12888; IntAct: EBI-20207896; Score: 0.27
DE  Interaction: O60260; IntAct: EBI-21135687; Score: 0.35
DE  Interaction: P83105; IntAct: EBI-25745135; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
GO  GO:0042582;
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0042470;
GO  GO:0016020;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0045335;
GO  GO:0042581;
GO  GO:0005819;
GO  GO:0005509;
GO  GO:0005544;
GO  GO:0048306;
GO  GO:0023026;
GO  GO:0008429;
GO  GO:0003723;
GO  GO:0044548;
GO  GO:0032506;
GO  GO:0006909;
GO  GO:0051592;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSYPGYPPPPGGYPPAAPGGGPWGGAAYPPPPSMPPIGLDNVATYAGQFNQDYLSGMAANMSGTFGGANMPNLYPGAPGA
SQ  GYPPVPPGGFGQPPSAQQPVPPYGMYPPPGGNPPSRMPSYPPYPGAPVPGQPMPPPGQQPPGAYPGQPPVTYPGQPPVPL
SQ  PGQQQPVPSYPGYPGSGTVTPAVPPTQFGSRGTITDAPGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILL
SQ  SFKTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDIYEIKEAIKGVGTDEACLIEILASRSNEHIRELNRAYKAEFKK
SQ  TLEEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLAQRDAQELYAAGENRLGTDESKFNAVLCSRSRAHLVAVFNEYQR
SQ  MTGRDIEKSICREMSGDLEEGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSETDLLDIRSEYKRMYGKS
SQ  LYHDISGDTSGDYRKILLKICGGND
//
ID  P97384;
PN  Annexin A11;
GN  Anxa11;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. Nucleus envelope {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus. Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent. {ECO:0000250}.
DR  UNIPROT: P97384;
DR  UNIPROT: Q921F1;
DR  Pfam: PF00191;
DR  PROSITE: PS00223;
DR  PROSITE: PS51897;
DE  Function: Required for midbody formation and completion of the terminal phase of cytokinesis (By similarity). Binds specifically to calcyclin in a calcium-dependent manner. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0042582;
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0042470;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0045335;
GO  GO:0042581;
GO  GO:0005819;
GO  GO:0005509;
GO  GO:0005544;
GO  GO:0048306;
GO  GO:0008429;
GO  GO:0044548;
GO  GO:0032506;
GO  GO:0006909;
GO  GO:0051592;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSYPGYPPPAGGYPPAAPGGGPWGGAGYPPPSMPPIGLDNVANYAGQFNQDYLSGMAANMSGTFGGANVPNLYPGAPGGG
SQ  YPPVPPGGFGQPPPAQQPVPPYGMYPPPGGNPPPGMPSYPAYPGAPVPGQPMPPTGQQPPGAYPGQPPMTYPGQSPMPPP
SQ  GQQPVPSYPGYSGSSTITPAVPPAQFGNRGTITAASGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSF
SQ  KTAYGKDLIKDLKSELSGNFEKTILALMKTPVLFDVYEIKEAIKGAGTDEACLIEIFASRSNEHIRELSRAYKTEFQKTL
SQ  EEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLVQRDVQELYAAGENRLGTDESKFNAILCSRSRAHLVAVFNEYQRMT
SQ  GRDIEKSICREMSGDLEQGMLAVVKCLKNTPAFFAERLNKAMRGAGTKDRTLIRIMVSRSELDLLDIRAEYKRMYGKSLY
SQ  HDITGDTSGDYRKILLKICGGND
//
ID  P33477;
PN  Annexin A11;
GN  ANXA11;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. Nucleus envelope {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus. Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent. {ECO:0000250}.
DR  UNIPROT: P33477;
DR  Pfam: PF00191;
DR  PROSITE: PS00223;
DR  PROSITE: PS51897;
DE  Function: Required for midbody formation and completion of the terminal phase of cytokinesis (By similarity). Binds specifically to calcyclin in a calcium-dependent manner. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0042470;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005819;
GO  GO:0005509;
GO  GO:0005544;
GO  GO:0044548;
GO  GO:0032506;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSYPGYPPPPGGYPPAPGGGAWGGAGYPPPSMPPIGLDNVANYAGQFNQDYLSGMAANMSGTFGGANVPPNLYPGAPGGG
SQ  YPPVPPGGFGQPPPTQPSVPPYGVYPPPGGNPPSGVPSYPPFPGAPVPGQPMPPPGHQPPGPYPGQLPVTYPGQSPVPPP
SQ  GQQPMPSYPGYPGSGTVTPAVPPVQFGNRGTITDASGFDPLRDAEVLRKAMKGFGTDEQAIIDCLGSRSNKQRQQILLSF
SQ  KTAYGKDLIKDLKSELSGNFEKTILALMKTPILFDAYEIKEAIKGAGTDEACLIEILASRSNEHIRELNKAYKTEFKKTL
SQ  EEAIRSDTSGHFQRLLISLSQGNRDESTNVDMSLVQRDVQELYAAGENRLGTDESKFNAVLCSRSRAHLVAVFNEYQRMT
SQ  GRDIEKSICREMSGDLEQGMLAVVKCLKNTPAFFAERLNRAMRGAGTKDRTLIRIMVSRSEIDLLDIRAEYKRMYGKSLY
SQ  HDISGDTSGDYRKILLKICGGND
//
ID  O43747;
PN  AP-1 complex subunit gamma-1;
GN  AP1G1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:12773381}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:12773381}; Peripheral membrane protein {ECO:0000269|PubMed:12773381}; Cytoplasmic side {ECO:0000269|PubMed:12773381}. Cytoplasm {ECO:0000269|PubMed:15758025}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15758025, ECO:0000269|PubMed:34102099}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15758025}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:34102099}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex (PubMed:12773381). Co-localizes with AFTPH/aftiphilin in the cytoplasm (PubMed:15758025). {ECO:0000269|PubMed:12773381, ECO:0000269|PubMed:15758025}.
DR  UNIPROT: O43747;
DR  UNIPROT: O75709;
DR  UNIPROT: O75842;
DR  UNIPROT: Q9UG09;
DR  UNIPROT: Q9Y3U4;
DR  PDB: 1IU1;
DR  Pfam: PF01602;
DR  Pfam: PF02883;
DR  PROSITE: PS50180;
DR  OMIM: 603533;
DR  OMIM: 619467;
DR  OMIM: 619548;
DR  DisGeNET: 164;
DE  Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. In association with AFTPH/aftiphilin in the aftiphilin/p200/gamma-synergin complex, involved in the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269|PubMed:15758025, ECO:0000269|PubMed:34102099}.
DE  Disease: Usmani-Riazuddin syndrome, autosomal dominant (USRISD) [MIM:619467]: A neurodevelopmental disorder characterized by global developmental delay with impaired intellectual development and speech delay, hypotonia, and behavioral abnormalities. More variable additional features may include seizures and distal limb anomalies. {ECO:0000269|PubMed:34102099}. Note=The disease is caused by variants affecting the gene represented in this entry. Usmani-Riazuddin syndrome, autosomal recessive (USRISR) [MIM:619548]: A neurodevelopmental disorder characterized by global developmental delay with impaired intellectual development and speech delay, hypotonia, spasticity, and behavioral abnormalities. More variable additional features may include seizures, scoliosis, and joint laxity. {ECO:0000269|PubMed:34102099}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O18973; IntAct: EBI-447608; Score: 0.37
DE  Interaction: Q15276; IntAct: EBI-448309; Score: 0.51
DE  Interaction: Q9DB50; IntAct: EBI-516318; Score: 0.37
DE  Interaction: P61967; IntAct: EBI-516322; Score: 0.37
DE  Interaction: P61106; IntAct: EBI-6962654; Score: 0.27
DE  Interaction: Q6VY07; IntAct: EBI-6971116; Score: 0.44
DE  Interaction: Q96G01; IntAct: EBI-7141935; Score: 0.27
DE  Interaction: Q9JIF3; IntAct: EBI-7048115; Score: 0.40
DE  Interaction: A0A6L7H5N1; IntAct: EBI-2811290; Score: 0.00
DE  Interaction: A0A6L8P1I7; IntAct: EBI-2813482; Score: 0.00
DE  Interaction: Q81MS2; IntAct: EBI-2817920; Score: 0.00
DE  Interaction: Q81LQ9; IntAct: EBI-2817913; Score: 0.00
DE  Interaction: A0A2C3GDM9; IntAct: EBI-2838167; Score: 0.00
DE  Interaction: A0A2P0HDJ9; IntAct: EBI-2838153; Score: 0.00
DE  Interaction: A0A6L7HG24; IntAct: EBI-2838146; Score: 0.00
DE  Interaction: Q81S14; IntAct: EBI-2838160; Score: 0.00
DE  Interaction: A0A2U2GVV5; IntAct: EBI-2848665; Score: 0.00
DE  Interaction: A0A380SBC9; IntAct: EBI-2875986; Score: 0.00
DE  Interaction: Q77M19; IntAct: EBI-6268389; Score: 0.35
DE  Interaction: Q10567; IntAct: EBI-6868018; Score: 0.27
DE  Interaction: P56377; IntAct: EBI-10185817; Score: 0.67
DE  Interaction: Q96S82; IntAct: EBI-10185831; Score: 0.72
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: Q9NYX4; IntAct: EBI-10918009; Score: 0.40
DE  Interaction: Q10589; IntAct: EBI-10960854; Score: 0.27
DE  Interaction: P19554; IntAct: EBI-10960854; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q6PD74; IntAct: EBI-24507122; Score: 0.67
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q96CW1; IntAct: EBI-21520588; Score: 0.35
DE  Interaction: A0JP26; IntAct: EBI-21540656; Score: 0.35
DE  Interaction: O75170; IntAct: EBI-21664775; Score: 0.35
DE  Interaction: Q9Y6Q5; IntAct: EBI-21760726; Score: 0.35
DE  Interaction: Q01968; IntAct: EBI-16412116; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P10644; IntAct: EBI-25387530; Score: 0.35
DE  Interaction: P20339; IntAct: EBI-25391898; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P54253; IntAct: EBI-25978906; Score: 0.56
DE  Interaction: P0DTC5; IntAct: EBI-27127936; Score: 0.27
GO  GO:0030121;
GO  GO:0030136;
GO  GO:0030665;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0005765;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0032588;
GO  GO:0140312;
GO  GO:0035615;
GO  GO:0030742;
GO  GO:0019894;
GO  GO:0031267;
GO  GO:0110010;
GO  GO:0035646;
GO  GO:0090160;
GO  GO:0006896;
GO  GO:0006886;
GO  GO:1903232;
GO  GO:0032438;
GO  GO:0060155;
GO  GO:0043323;
GO  GO:0045954;
GO  GO:0006898;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:12773381};
SQ  MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFT
SQ  DKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALC
SQ  AVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGI
SQ  SDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNN
SQ  DKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADC
SQ  ASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCI
SQ  GEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQ
SQ  QRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPTEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPV
SQ  IPTAPTSKPSSAGGELLDLLGDINLTGAPAAAPAPASVPQISQPPFLLDGLSSQPLFNDIAAGIPSITAYSKNGLKIEFT
SQ  FERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKVLNPQKQQLRMRIKLTY
SQ  NHKGSAMQDLAEVNNFPPQSWQ
//
ID  P22892;
PN  AP-1 complex subunit gamma-1;
GN  Ap1g1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250|UniProtKB:O43747}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:O43747}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43747}; Cytoplasmic side {ECO:0000250|UniProtKB:O43747}. Cytoplasm {ECO:0000250|UniProtKB:O43747}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43747}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:O43747}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:O43747}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex (By similarity). Co-localizes with AFTPH/aftiphilin in the cytoplasm (By similarity). {ECO:0000250|UniProtKB:O43747}.
DR  UNIPROT: P22892;
DR  PDB: 1GYU;
DR  PDB: 1GYV;
DR  PDB: 1GYW;
DR  PDB: 1W63;
DR  PDB: 2A7B;
DR  PDB: 3ZY7;
DR  PDB: 4HMY;
DR  PDB: 4P6Z;
DR  PDB: 6CM9;
DR  PDB: 6CRI;
DR  PDB: 6D83;
DR  PDB: 6D84;
DR  PDB: 6DFF;
DR  Pfam: PF01602;
DR  Pfam: PF02883;
DR  PROSITE: PS50180;
DE  Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. In association with AFTPH/aftiphilin in the aftiphilin/p200/gamma-synergin complex, involved in the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (By similarity). {ECO:0000250|UniProtKB:O43747}.
DE  Reference Proteome: Yes;
DE  Interaction: Q07113; IntAct: EBI-7855082; Score: 0.44
DE  Interaction: P52303; IntAct: EBI-1040301; Score: 0.40
DE  Interaction: Q14677; IntAct: EBI-7071326; Score: 0.54
DE  Interaction: Q9JIF3; IntAct: EBI-7048197; Score: 0.40
DE  Interaction: P46096; IntAct: EBI-7837071; Score: 0.27
DE  Interaction: Q62277; IntAct: EBI-7837084; Score: 0.27
DE  Interaction: Q10567; IntAct: EBI-6863559; Score: 0.74
DE  Interaction: P84077; IntAct: EBI-6864775; Score: 0.35
DE  Interaction: Q96PC3; IntAct: EBI-6864775; Score: 0.35
DE  Interaction: P35585; IntAct: EBI-6864775; Score: 0.66
DE  Interaction: O75379; IntAct: EBI-6868249; Score: 0.35
DE  Interaction: O54774; IntAct: EBI-9103779; Score: 0.35
DE  Interaction: P18242; IntAct: EBI-9103779; Score: 0.35
DE  Interaction: Q68FD5; IntAct: EBI-9103779; Score: 0.35
DE  Interaction: P11438; IntAct: EBI-9103779; Score: 0.35
DE  Interaction: Q8BKC8; IntAct: EBI-9103779; Score: 0.35
DE  Interaction: Q9CQD1; IntAct: EBI-9103779; Score: 0.35
DE  Interaction: O88384; IntAct: EBI-9103735; Score: 0.35
DE  Interaction: P61966; IntAct: EBI-10960176; Score: 0.40
GO  GO:0030121;
GO  GO:0030136;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0005765;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0032588;
GO  GO:0140312;
GO  GO:0035615;
GO  GO:0030742;
GO  GO:0019894;
GO  GO:0031267;
GO  GO:0110010;
GO  GO:0035646;
GO  GO:0090160;
GO  GO:0006896;
GO  GO:0006886;
GO  GO:1903232;
GO  GO:0060155;
GO  GO:0043323;
GO  GO:0045954;
GO  GO:0006898;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O43747};
SQ  MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFT
SQ  DKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALC
SQ  AVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGI
SQ  SDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNN
SQ  DKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADC
SQ  ASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCI
SQ  GEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQ
SQ  QRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPSEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPV
SQ  IPTAPTSKPASAGGELLDLLGDITLTGAPAAAPTPASVPQISQPPFLLDGLSSQPLFNDIAPGIPSITAYSKNGLKIEFT
SQ  FERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFNTGTITQVIKVLNPQKQQLRMRIKLTY
SQ  NHKGSAMQDLAEVNNFPPQSWQ
//
ID  Q5R5M2;
PN  AP-1 complex subunit gamma-1;
GN  AP1G1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250|UniProtKB:O43747}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:O43747}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43747}; Cytoplasmic side {ECO:0000250|UniProtKB:O43747}. Cytoplasm {ECO:0000250|UniProtKB:O43747}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43747}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:O43747}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:O43747}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex (By similarity). Co-localizes with AFTPH/aftiphilin in the cytoplasm (By similarity). {ECO:0000250|UniProtKB:O43747}.
DR  UNIPROT: Q5R5M2;
DR  Pfam: PF01602;
DR  Pfam: PF02883;
DR  PROSITE: PS50180;
DE  Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. In association with AFTPH/aftiphilin in the aftiphilin/p200/gamma-synergin complex, involved in the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (By similarity). {ECO:0000250|UniProtKB:O43747}.
DE  Reference Proteome: Yes;
GO  GO:0030121;
GO  GO:0048471;
GO  GO:0006886;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O43747};
SQ  MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFT
SQ  DKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALC
SQ  AVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMPAHFRKLVPQLVRILKNLIMSGYSPEHDVSGI
SQ  SDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNN
SQ  DKNIRYVALTSLLKTVRTDHNTVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADC
SQ  ASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCI
SQ  GEYGDLLVSGQCEEEGPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQ
SQ  QRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPTEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPV
SQ  IPTAPTSKPSSAGGELLDLLGDINLTGAPAAAPAPASVPQISQPPFLLDGLSSQPLFNDIAAGIPSITAYSKNGLKIEFT
SQ  FERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKVLNPQKQQLRMRIKLTY
SQ  NHKGSAMQDLAEVNNFPPQSWQ
//
ID  Q02410;
PN  Amyloid-beta A4 precursor protein-binding family A member 1;
GN  APBA1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:20531236}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20531236}. Nucleus {ECO:0000269|PubMed:20531236}. Note=Only about 5% of the protein is located in the nucleus. [Isoform 2]: Golgi apparatus {ECO:0000269|PubMed:23737971}.
DR  UNIPROT: Q02410;
DR  UNIPROT: O14914;
DR  UNIPROT: O60570;
DR  UNIPROT: Q5VYR8;
DR  PDB: 1AQC;
DR  PDB: 1U37;
DR  PDB: 1U38;
DR  PDB: 1U39;
DR  PDB: 1U3B;
DR  PDB: 1X11;
DR  PDB: 1X45;
DR  PDB: 1Y7N;
DR  Pfam: PF00595;
DR  Pfam: PF00640;
DR  PROSITE: PS50106;
DR  PROSITE: PS01179;
DR  OMIM: 602414;
DR  DisGeNET: 320;
DE  Function: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. Component of the LIN-10- LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). {ECO:0000250|UniProtKB:B2RUJ5}.
DE  Reference Proteome: Yes;
DE  Interaction: P05067; IntAct: EBI-368901; Score: 0.65
DE  Interaction: P49768; IntAct: EBI-7693425; Score: 0.70
DE  Interaction: Q00975; IntAct: EBI-7693446; Score: 0.44
DE  Interaction: Q02410; IntAct: EBI-7693492; Score: 0.37
DE  Interaction: Q5NGR3; IntAct: EBI-2808888; Score: 0.00
DE  Interaction: Q8ZD84; IntAct: EBI-2840135; Score: 0.00
DE  Interaction: A0A2S9PLH1; IntAct: EBI-2875941; Score: 0.00
DE  Interaction: P97887; IntAct: EBI-6674509; Score: 0.40
DE  Interaction: Q9NRW1; IntAct: EBI-8840227; Score: 0.62
DE  Interaction: P20340; IntAct: EBI-8840230; Score: 0.62
DE  Interaction: P35279; IntAct: EBI-8841337; Score: 0.27
DE  Interaction: O14936; IntAct: EBI-9084378; Score: 0.40
DE  Interaction: Q9NUP9; IntAct: EBI-21627409; Score: 0.35
DE  Interaction: Q99767; IntAct: EBI-21817505; Score: 0.35
DE  Interaction: K9N5R3; IntAct: EBI-26973521; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0048787;
GO  GO:0098685;
GO  GO:0008021;
GO  GO:0001540;
GO  GO:0008088;
GO  GO:0007155;
GO  GO:0007268;
GO  GO:0014051;
GO  GO:0014047;
GO  GO:0001701;
GO  GO:0006886;
GO  GO:0007626;
GO  GO:0035264;
GO  GO:0007399;
GO  GO:0065003;
GO  GO:0010468;
GO  GO:2000300;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNHLEGSAEVEVTDEAAGGEVNESVEADLEHPEVEEEQQQPPQQQHYVGRHQRGRALEDLRAQLGQEEEERGECLARSAS
SQ  TESGFHNHTDTAEGDVIAAARDGYDAERAQDPEDESAYAVQYRPEAEEYTEQAEAEHAEATHRRALPNHLHFHSLEHEEA
SQ  MNAAYSGYVYTHRLFHRGEDEPYSEPYADYGGLQEHVYEEIGDAPELDARDGLRLYEQERDEAAAYRQEALGARLHHYDE
SQ  RSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERPPTPAGGRPDSPGLQAPA
SQ  GQQRAVGPAGGGEAGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPMDGD
SQ  SPSPGSSSPLGAESSSTSLHPSDPVEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKN
SQ  VRMMQAQEAVSRIKMAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQETMMDHPLRTISYIADIGNIVVLMAR
SQ  RRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDM
SQ  YNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLS
SQ  TCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATP
SQ  HEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI
//
ID  B2RUJ5;
PN  Amyloid-beta A4 precursor protein-binding family A member 1;
GN  Apba1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. [Isoform 3]: Golgi apparatus.
DR  UNIPROT: B2RUJ5;
DR  UNIPROT: Q3UH49;
DR  UNIPROT: Q8BMF2;
DR  PDB: 6LNM;
DR  Pfam: PF00595;
DR  Pfam: PF00640;
DR  PROSITE: PS50106;
DR  PROSITE: PS01179;
DE  Function: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of AAP-beta (By similarity). Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D- aspartate (NMDA) receptor subunit NR2B along microtubules (PubMed:10846156). {ECO:0000250, ECO:0000269|PubMed:10846156}.
DE  Reference Proteome: Yes;
DE  Interaction: P61294; IntAct: EBI-8840212; Score: 0.27
DE  Interaction: P20340; IntAct: EBI-8840609; Score: 0.44
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0048787;
GO  GO:0032991;
GO  GO:0098685;
GO  GO:0008021;
GO  GO:0001540;
GO  GO:0030165;
GO  GO:0005546;
GO  GO:0044877;
GO  GO:0007268;
GO  GO:0051649;
GO  GO:0014051;
GO  GO:0014047;
GO  GO:0001701;
GO  GO:0006886;
GO  GO:0007626;
GO  GO:0035264;
GO  GO:0065003;
GO  GO:0010468;
GO  GO:2000300;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVVEGQQPSPSPPPPAGHEPEDHRGHPAPPPPPPPQEEEEEERGECLA
SQ  RSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHVEAAQRRALPNHLHFHSLE
SQ  HEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLH
SQ  HYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGL
SQ  PAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQR
SQ  PVDGDSPSPGSSSPLGAESSSIPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDK
SQ  TPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIV
SQ  VLMARRRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLL
SQ  NTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLV
SQ  GLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQS
SQ  VVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI
//
ID  O35430;
PN  Amyloid-beta A4 precursor protein-binding family A member 1;
GN  Apba1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20531236}. Note=Only a small proportion of the protein is nuclear. [Isoform 2]: Golgi apparatus {ECO:0000250}.
DR  UNIPROT: O35430;
DR  PDB: 4DBB;
DR  PDB: 6KMH;
DR  Pfam: PF00595;
DR  Pfam: PF00640;
DR  PROSITE: PS50106;
DR  PROSITE: PS01179;
DE  Function: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta.
DE  Reference Proteome: Yes;
DE  Interaction: P26010; IntAct: EBI-8611689; Score: 0.44
DE  Interaction: P05106; IntAct: EBI-8611732; Score: 0.44
DE  Interaction: P05556; IntAct: EBI-8611776; Score: 0.44
DE  Interaction: Q99PW8; IntAct: EBI-7293493; Score: 0.64
DE  Interaction: Q00975; IntAct: EBI-7076778; Score: 0.51
DE  Interaction: Q02294; IntAct: EBI-7076897; Score: 0.40
DE  Interaction: Q62889; IntAct: EBI-7414748; Score: 0.44
DE  Interaction: Q63373; IntAct: EBI-7414873; Score: 0.27
DE  Interaction: P49768; IntAct: EBI-8513481; Score: 0.40
DE  Interaction: P05067; IntAct: EBI-8513444; Score: 0.52
DE  Interaction: P52188; IntAct: EBI-704679; Score: 0.35
DE  Interaction: P32851; IntAct: EBI-8545713; Score: 0.66
DE  Interaction: P61765; IntAct: EBI-2027999; Score: 0.62
DE  Interaction: Q24008; IntAct: EBI-4307047; Score: 0.56
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0048787;
GO  GO:0032991;
GO  GO:0098685;
GO  GO:0008021;
GO  GO:0001540;
GO  GO:0030165;
GO  GO:0005546;
GO  GO:0044877;
GO  GO:0007268;
GO  GO:0051649;
GO  GO:0014051;
GO  GO:0014047;
GO  GO:0001701;
GO  GO:0006886;
GO  GO:0007626;
GO  GO:0035264;
GO  GO:0065003;
GO  GO:0010468;
GO  GO:2000300;
GO  GO:0016079;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVEEEQQPSPPPPAGHAPEDHRAHPAPPPPPPPQEEEEERGECLARSA
SQ  STESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHAEAAQRRALPNHLHFHSLEHEE
SQ  AMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYD
SQ  ERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGLPAP
SQ  AGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPVD
SQ  GDSPSPGSSSPLGAESSITPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPS
SQ  KNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIVVLM
SQ  ARRRMPRSNSQENVEASHPSQDAKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQ
SQ  DMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLP
SQ  LSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVA
SQ  TPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI
//
ID  O96018;
PN  Amyloid-beta A4 precursor protein-binding family A member 3;
GN  APBA3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19726677}.
DR  UNIPROT: O96018;
DR  UNIPROT: O60483;
DR  UNIPROT: Q9UPZ2;
DR  PDB: 2YT7;
DR  PDB: 2YT8;
DR  PDB: 5UWS;
DR  Pfam: PF00595;
DR  Pfam: PF00640;
DR  PROSITE: PS50106;
DR  PROSITE: PS01179;
DR  OMIM: 604262;
DR  DisGeNET: 9546;
DE  Function: May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN. {ECO:0000269|PubMed:19726677}.
DE  Reference Proteome: Yes;
DE  Interaction: P11274; IntAct: EBI-7358205; Score: 0.61
DE  Interaction: P00533; IntAct: EBI-7877395; Score: 0.44
DE  Interaction: Q9QYP6; IntAct: EBI-6115837; Score: 0.50
DE  Interaction: A7MCY6; IntAct: EBI-6116450; Score: 0.50
DE  Interaction: Q92844; IntAct: EBI-6116592; Score: 0.50
DE  Interaction: Q9H6Z9; IntAct: EBI-12503146; Score: 0.35
DE  Interaction: P16152; IntAct: EBI-11153984; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q96P71; IntAct: EBI-15098872; Score: 0.60
DE  Interaction: Q8NCP5; IntAct: EBI-15098805; Score: 0.37
DE  Interaction: Q06481; IntAct: EBI-15098809; Score: 0.37
DE  Interaction: P78545; IntAct: EBI-15098813; Score: 0.37
DE  Interaction: P14061; IntAct: EBI-15098817; Score: 0.37
DE  Interaction: Q9UN79; IntAct: EBI-15098821; Score: 0.37
DE  Interaction: Q9H6I2; IntAct: EBI-15098825; Score: 0.37
DE  Interaction: P52747; IntAct: EBI-15098829; Score: 0.37
DE  Interaction: Q9NWT6; IntAct: EBI-15099018; Score: 0.75
DE  Interaction: P78552; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q9NSD9; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q9H6S1; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q9BY42; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q9BSJ5; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q99590; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q99569; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q8TEU7; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q8TBX8; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q8N9R8; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q6PD62; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q6P5Z2; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q5JTD0; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q12986; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q08AH1; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: P55789; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: P29803; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: P17029; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-25936284; Score: 0.56
DE  Interaction: O94985; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: O75319; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: Q96BW9; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: P32320; IntAct: EBI-21622979; Score: 0.35
DE  Interaction: Q86VW1; IntAct: EBI-21721972; Score: 0.35
DE  Interaction: Q9BZB8; IntAct: EBI-21821951; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-30828353; Score: 0.44
DE  Interaction: Q93009; IntAct: EBI-30841267; Score: 0.44
GO  GO:0005737;
GO  GO:0043197;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001540;
GO  GO:0019899;
GO  GO:0004857;
GO  GO:0007268;
GO  GO:0001701;
GO  GO:0043086;
GO  GO:0015031;
GO  GO:0010468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDFPTISRSPSGPPAMDLEGPRDILVPSEDLTPDSQWDPMPGGPGSLSRMELDESSLQELVQQFEALPGDLVGPSPGGAP
SQ  CPLHIATGHGLASQEIADAHGLLSAEAGRDDLLGLLHCEECPPSQTGPEEPLEPAPRLLQPPEDPDEDSDSPEWVEGASA
SQ  EQEGSRSSSSSPEPWLETVPLVTPEEPPAGAQSPETLASYPAPQEVPGPCDHEDLLDGVIFGARYLGSTQLVSERNPPTS
SQ  TRMAQAREAMDRVKAPDGETQPMTEVDLFVSTKRIKVLTADSQEAMMDHALHTISYTADIGCVLVLMARRRLARRPAPQD
SQ  HGRRLYKMLCHVFYAEDAQLIAQAIGQAFAAAYSQFLRESGIDPSQVGVHPSPGACHLHNGDLDHFSNSDNCREVHLEKR
SQ  RGEGLGVALVESGWGSLLPTAVIANLLHGGPAERSGALSIGDRLTAINGTSLVGLPLAACQAAVRETKSQTSVTLSIVHC
SQ  PPVTTAIIHRPHAREQLGFCVEDGIICSLLRGGIAERGGIRVGHRIIEINGQSVVATPHARIIELLTEAYGEVHIKTMPA
SQ  ATYRLLTGQEQPVYL
//
ID  O88888;
PN  Amyloid-beta A4 precursor protein-binding family A member 3;
GN  Apba3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: O88888;
DR  UNIPROT: Q3TDI1;
DR  UNIPROT: Q8BR09;
DR  Pfam: PF00595;
DR  Pfam: PF00640;
DR  PROSITE: PS50106;
DR  PROSITE: PS01179;
DE  Function: May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P0C6X9; IntAct: EBI-25509102; Score: 0.37
GO  GO:0005737;
GO  GO:0043197;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001540;
GO  GO:0019899;
GO  GO:0004857;
GO  GO:0007268;
GO  GO:0001701;
GO  GO:0043086;
GO  GO:0015031;
GO  GO:0010468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEFLPGPQHPPGPPTMDLEEPKGPEVPSENHPSNTQSALGPGGPVTLSEMELDTSSVQELVQQLEALPSDLGGPFPDGAP
SQ  CPLHIATGQGLATQENPDAGGLLSAEAGGDDLLGLLRDEASSPAQSVPQDPAQTAPRLLQPPEDPDGDPGWMEGASAEPA
SQ  DSRSSSSSPEPWLETAPLVTQQEPPVGTQSRETLASCPAVTEVPGPCGPEELMDGVIFGAKYLGSTQLLSERSPAPSTRM
SQ  GQAQEAMDRVKAPEGETQPMVEVDIFISTKRVKVLAADSQDALMDHALQTISYIADIGPVLVLMARRRLARRTTPQDRQR
SQ  RLYKMLCHVFHSEDAQLIAQAIGQAFSIAYSQFLQENRIDPSQVGTQPSTAASHPHNGDLDHFCNSQNCREVCIQKRPGE
SQ  GLGVALVESGWGSLLPTAVIANLLHGGPAERCGALSIGDRVTAINGTSLVGLSLAACQAAVREVRRLSSVTLSIIHCPPV
SQ  TTAVIRRPHVREQLGFCVEDGIICSLLRGGAAERGGVRVGHRIIEVNGQSVVAMPHARIIQLLTETREIHIKTMPAATYR
SQ  LLTGQEQPVYL
//
ID  O70248;
PN  Amyloid-beta A4 precursor protein-binding family A member 3;
GN  Apba3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: O70248;
DR  UNIPROT: B1WBQ3;
DR  Pfam: PF00595;
DR  Pfam: PF00640;
DR  PROSITE: PS50106;
DR  PROSITE: PS01179;
DE  Function: May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P05067; IntAct: EBI-8513424; Score: 0.52
DE  Interaction: P49768; IntAct: EBI-8513544; Score: 0.40
DE  Interaction: Q16832; IntAct: EBI-22241781; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: P11362; IntAct: EBI-22243924; Score: 0.35
DE  Interaction: P06241; IntAct: EBI-22245123; Score: 0.35
GO  GO:0005737;
GO  GO:0043197;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0001540;
GO  GO:0019899;
GO  GO:0004857;
GO  GO:0007268;
GO  GO:0001701;
GO  GO:0043086;
GO  GO:0015031;
GO  GO:0010468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEFLPEPQHPPGPPTMDLEEPKGPEVPSEDHPSNTQWALGPRGPDTLSEMELDTSSVRALVQQLEALPSDLGGQFPDGAP
SQ  CPLHIATGQGLATQENLDAGGLLSAEAGGDNLLGLLRCEASLPAQSVPPDPAQAAPRLLQPPEDPGGDPGWMEGTEPADN
SQ  RSSSSSPELWLETAPLVTHRDPPVGTQSQETLASCPAVSEVPGPCGQEELMDGVLFGAKYLGSTQLLSERNPPPSTRMGQ
SQ  AQEAMDRVKAPEGETQPMTEVDIFISTKRVKVLAADSQDALMDHALQTISYIADIGPVLVLMARRRLAKRTTSQDRQRQL
SQ  YKMLCHVFHSEDAQLIAQAIGQAFSIAYSQFLQENRIDPSQVGMQPSASASHPHNGDLDHFCNSQNCREVCIQKRPGEGL
SQ  GVALVESGWGSLLPTAVIANLLHGGPAERCGALSIGDRVTAINGTSLVGLSLAACQAAVREVRRHSSVTLSIIHCPPVTT
SQ  AVIHRPHVREQLGFCVENGIICSLLRGSAAERGGVRVGHRIIEVNGQSVVAMPHARIIQLLTETREIHIKTMPAATYRLL
SQ  TGQEQPVYL
//
ID  O95996;
PN  Adenomatous polyposis coli protein 2;
GN  APC2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423}. Golgi apparatus {ECO:0000269|PubMed:11691822}. Cytoplasm {ECO:0000269|PubMed:11691822}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10646860}. Note=Associated with actin filaments (PubMed:11691822, PubMed:25753423). Associated with microtubule network (PubMed:10644998, PubMed:11691822, PubMed:25753423). {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423}.
DR  UNIPROT: O95996;
DR  UNIPROT: Q05BW4;
DR  UNIPROT: Q9UBZ1;
DR  UNIPROT: Q9UEM8;
DR  UNIPROT: Q9UQJ8;
DR  UNIPROT: Q9UQJ9;
DR  UNIPROT: Q9Y632;
DR  Pfam: PF05956;
DR  Pfam: PF16689;
DR  Pfam: PF05923;
DR  Pfam: PF18797;
DR  Pfam: PF00514;
DR  Pfam: PF05924;
DR  OMIM: 612034;
DR  OMIM: 617169;
DR  OMIM: 618677;
DR  DisGeNET: 10297;
DE  Function: Stabilizes microtubules and may regulate actin fiber dynamics through the activation of Rho family GTPases (PubMed:25753423). May also function in Wnt signaling by promoting the rapid degradation of CTNNB1 (PubMed:10021369, PubMed:11691822, PubMed:9823329). {ECO:0000269|PubMed:10021369, ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423, ECO:0000269|PubMed:9823329}.
DE  Disease: Intellectual developmental disorder, autosomal recessive 74 (MRT74) [MIM:617169]: A disorder characterized by intellectual impairment, macrocephaly, and dysmorphic features. Epilepsy with eyelid myoclonus has also been reported. {ECO:0000269|PubMed:25753423}. Note=The disease is caused by variants affecting the gene represented in this entry. Cortical dysplasia, complex, with other brain malformations 10 (CDCBM10) [MIM:618677]: An autosomal recessive disorder of aberrant neuronal migration during brain development. CDCBM10 is clinically characterized by onset in infancy of global developmental delay, impaired intellectual development, seizures, inability to ambulate, and absent language. Brain imaging shows lissencephaly, cortical dysplasia, subcortical heterotopia, and paucity of white matter. {ECO:0000269|PubMed:31585108}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P16035; IntAct: EBI-1077756; Score: 0.00
DE  Interaction: P67809; IntAct: EBI-5325180; Score: 0.35
DE  Interaction: Q13625; IntAct: EBI-8830464; Score: 0.54
DE  Interaction: Q9UPY8; IntAct: EBI-8842039; Score: 0.61
DE  Interaction: Q15691; IntAct: EBI-8840634; Score: 0.53
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21369738; Score: 0.00
DE  Interaction: P51114; IntAct: EBI-26509879; Score: 0.37
DE  Interaction: Q9NZ94; IntAct: EBI-26513299; Score: 0.37
DE  Interaction: P51531; IntAct: EBI-26515204; Score: 0.37
DE  Interaction: P46934; IntAct: EBI-30832261; Score: 0.44
DE  Interaction: P46937; IntAct: EBI-30846273; Score: 0.44
GO  GO:0005884;
GO  GO:0030877;
GO  GO:0016342;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0045171;
GO  GO:0031258;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0008013;
GO  GO:0045295;
GO  GO:0008017;
GO  GO:0090630;
GO  GO:0001708;
GO  GO:0016477;
GO  GO:0000226;
GO  GO:0090090;
GO  GO:0007026;
GO  GO:0007399;
GO  GO:0007389;
GO  GO:0045732;
GO  GO:0043161;
GO  GO:0045595;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASSVAPYEQLVRQVEALKAENSHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQ
SQ  MDITSLYNLKFQPPTLGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDRERCFLLNEIEKEEKEKLWYYSQLQ
SQ  GLSKRLDELPHVETQFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQA
SQ  LLAVKSVPVDEDPETEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQI
SQ  LHGTEAAAGGRAGAPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDGGPEGGGA
SQ  GSAPIPIEPQICQATCAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTRDPLNLALRRYAGMTLTNLTFGDVAN
SQ  KATLCARRGCMEAIVAQLASDSEELHQVVSSILRNLSWRADINSKKVLREAGSVTALVQCVLRATKESTLKSVLSALWNL
SQ  SAHSTENKAAICQVDGALGFLVSTLTYKCQSNSLAIIESGGGILRNVSSLVATREDYRQVLRDHNCLQTLLQHLTSHSLT
SQ  IVSNACGTLWNLSARSARDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKHQAAATAVSPGSCVPSLYV
SQ  RKQRALEAELDARHLAQALEHLEKQGPPAAEAATKKPLPPLRHLDGLAQDYASDSGCFDDDDAPSSLAAAAATGEPASPA
SQ  ALSLFLGSPFLQGQALARTPPTRRGGKEAEKDTSGEAAVAAKAKAKLALAVARIDQLVEDISALHTSSDDSFSLSSGDPG
SQ  QEAPREGRAQSCSPCRGPEGGRREAGSRAHPLLRLKAAHASLSNDSLNSGSASDGYCPREHMLPCPLAALASRREDPRCG
SQ  QPRPSRLDLDLPGCQAEPPAREATSADARVRTIKLSPTYQHVPLLEGASRAGAEPLAGPGISPGARKQAWLPADHLSKVP
SQ  EKLAAAPLSVASKALQKLAAQEGPLSLSRCSSLSSLSSAGRPGPSEGGDLDDSDSSLEGLEEAGPSEAELDSTWRAPGAT
SQ  SLPVAIPAPRRNRGRGLGVEDATPSSSSENYVQETPLVLSRCSSVSSLGSFESPSIASSIPSEPCSGQGSGTISPSELPD
SQ  SPGQTMPPSRSKTPPLAPAPQGPPEATQFSLQWESYVKRFLDIADCRERCRLPSELDAGSVRFTVEKPDENFSCASSLSA
SQ  LALHEHYVQQDVELRLLPSACPERGGGAGGAGLHFAGHRRREEGPAPTGSRPRGAADQELELLRECLGAAVPARLRKVAS
SQ  ALVPGRRALPVPVYMLVPAPAPAQEDDSCTDSAEGTPVNFSSAASLSDETLQGPPRDQPGGPAGRQRPTGRPTSARQAMG
SQ  HRHKAGGAGRSAEQSRGAGKNRAGLELPLGRPPSAPADKDGSKPGRTRGDGALQSLCLTTPTEEAVYCFYGNDSDEEPPA
SQ  AAPTPTHRRTSAIPRAFTRERPQGRKEAPAPSKAAPAAPPPARTQPSLIADETPPCYSLSSSASSLSEPEPSEPPAVHPR
SQ  GREPAVTKDPGPGGGRDSSPSPRAAEELLQRCISSALPRRRPPVSGLRRRKPRATRLDERPAEGSRERGEEAAGSDRASD
SQ  LDSVEWRAIQEGANSIVTWLHQAAAATREASSESDSILSFVSGLSVGSTLQPPKHRKGRQAEGEMGSARRPEKRGAASVK
SQ  TSGSPRSPAGPEKPRGTQKTTPGVPAVLRGRTVIYVPSPAPRAQPKGTPGPRATPRKVAPPCLAQPAAPAKVPSPGQQRS
SQ  RSLHRPAKTSELATLSQPPRSATPPARLAKTPSSSSSQTSPASQPLPRKRPPVTQAAGALPGPGASPVPKTPARTLLAKQ
SQ  HKTQRSPVRIPFMQRPARRGPPPLARAVPEPGPRGRAGTEAGPGARGGRLGLVRVASALSSGSESSDRSGFRRQLTFIKE
SQ  SPGLRRRRSELSSAESAASAPQGASPRRGRPALPAVFLCSSRCEELRAAPRQGPAPARQRPPAARPSPGERPARRTTSES
SQ  PSRLPVRAPAARPETVKRYASLPHISVARRPDGAVPAAPASADAARRSSDGEPRPLPRVAAPGTTWRRIRDEDVPHILRS
SQ  TLPATALPLRGSTPEDAPAGPPPRKTSDAVVQTEEVAAPKTNSSTSPSLETREPPGAPAGGQLSLLGSDVDGPSLAKAPI
SQ  SAPFVHEGLGVAVGGFPASRHGSPSRSARVPPFNYVPSPMVVAATTDSAAEKAPATASATLLE
//
ID  Q9Z1K7;
PN  Adenomatous polyposis coli protein 2;
GN  Apc2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O95996}. Golgi apparatus {ECO:0000250|UniProtKB:O95996}. Cytoplasm {ECO:0000250|UniProtKB:O95996}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95996}. Note=Associated with actin filaments. Associated with microtubule network. {ECO:0000250|UniProtKB:O95996}.
DR  UNIPROT: Q9Z1K7;
DR  Pfam: PF05956;
DR  Pfam: PF16689;
DR  Pfam: PF05923;
DR  Pfam: PF18797;
DR  Pfam: PF00514;
DR  Pfam: PF05924;
DE  Function: Stabilizes microtubules and may regulate actin fiber dynamics through the activation of Rho family GTPases. May also function in Wnt signaling by promoting the rapid degradation of CTNNB1. {ECO:0000250|UniProtKB:O95996}.
DE  Reference Proteome: Yes;
DE  Interaction: P35922; IntAct: EBI-16728828; Score: 0.35
GO  GO:0005884;
GO  GO:0030877;
GO  GO:0016342;
GO  GO:0005737;
GO  GO:0005881;
GO  GO:0005829;
GO  GO:0031941;
GO  GO:0005794;
GO  GO:0045171;
GO  GO:0031258;
GO  GO:0015630;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0008013;
GO  GO:0045295;
GO  GO:0008017;
GO  GO:0090630;
GO  GO:0001708;
GO  GO:0016477;
GO  GO:0000226;
GO  GO:0090090;
GO  GO:0007026;
GO  GO:0007399;
GO  GO:0007389;
GO  GO:0045732;
GO  GO:0043161;
GO  GO:0045595;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTSSMASYEQLVRQVEALKAENTHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQ
SQ  TDISSLYNLKFHAPALGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDQERCFLLSEIEKEEKEKLWYYSQLQ
SQ  GLSKRLDELPHVDTFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQAL
SQ  LAVKPVAVEEEQEAEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQIL
SQ  HGTEAGSVGRAGIPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDSGTETPVPI
SQ  EPQICQATCAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTRDPLNLALRRYAGMTLTNLTFGDVANKATLCAR
SQ  RGCMEAIVAQLGSESEELHQVVSSILRNLSWRADINSKKVLREVGSMTALMECVLRASKESTLKSVLSALWNLSAHSTEN
SQ  KAAICQVDGALGFLVSTLTYRCQGNSLAVIESGGGILRNVSSLIATREDYRQVLRDHNCLQTLLQHLTSHSLTIVSNACG
SQ  TLWNLSARSPRDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKYQAAAMAVSPGTCVPSLYVRKQRALE
SQ  AELDTRHLVHALGHLEKQSLPEAETTSKKPLPPLRHLDGLVQDYASDSGCFDDDDAPSLAAAATTAEPASPAVMSMFLGG
SQ  PFLQGQALARTPPARQGGLEAEKEAGGEAAVAAKAKAKLALAVARIDRLVEDISALHTSSDDSFSLSSGDPGQEAPREGR
SQ  AQSCSPCRGTEGGRREAGSRAHPLLRLKAAHTSLSNDSLNSGSTSDGYCTREHMTPCPLAALAEHRDDPVRGQTRPRRLD
SQ  LDLPSRAELPARDTAATDARVRTIKLSPTYQHVPLLDGAAGAGVRPLVGPGTSPGARKQAWIPADSLSKVPEKLVASPLP
SQ  IASKVLQKLVAQDGPMSLSRCSSLSSLSSTGHAVPSQAENLDSDSSLEGLEEAGPGEAELGRAWRASGSTSLPVSIPAPQ
SQ  RGRSRGLGVEDATPSSSSENCVQETPLVLSRCSSVSSLGSFESRSIASSIPSDPCSGLGSGTVSPSELPDSPGQTMPPSR
SQ  SKTPPAPPGQPETSQFSLQWESYVKRFLDIADCRERCQPPSELDAGSVRFTVEKPDENFSCASSLSALALHELYVQQDVE
SQ  LRLRPPACPERAVGGGGHRRRDEAASRLDGPAPAGSRARSATDKELEALRECLGAAMPARLRKVASALVPGRRSLPVPVY
SQ  MLVPAPARGDDSGTDSAEGTPVNFSSAASLSDETLQGPSRDKPAGPGDRQKPTGRAAPARQTRSHRPKAAGAGKSTEHTR
SQ  GPCRNRAGLELPLSRPQSARSNRDSSCQTRTRGDGALQSLCLTTPTEEAVYCFYDSDEEPPATAPPPRRASAIPRALKRE
SQ  KPAGRKETPSRAAQPATLPVRAQPRLIVDETPPCYSLTSSASSLSEPEAPEQPANHARGPEQGSKQDSSPSPRAEEELLQ
SQ  RCISLAMPRRRTQVPGSRRRKPRALRSDIRPTEITQKCQEEVAGSDPASDLDSVEWQAIQEGANSIVTWLHQAAAKASLE
SQ  ASSESDSLLSLVSGVSAGSTLQPSKLRKGRKPAAEAGGAWRPEKRGTTSTKINGSPRLPNGPEKAKGTQKMMAGESTMLR
SQ  GRTVIYSAGPASRTQSKGISGPCTTPKKTGTSGTTQPETVTKAPSPEQQRSRSLHRPGKISELAALRHPPRSATPPARLA
SQ  KTPSSSSSQTSPASQPLPRRSPLATPTGGPLPGPGGSLVPKSPARALLAKQHKTQKSPVRIPFMQRPARRVPPPLARPSP
SQ  EPGSRGRAGAEGTPGARGSRLGLVRMASARSSGSESSDRSGFRRQLTFIKESPGLLRRRRSELSSADSTASTSQAASPRR
SQ  GRPALPAVFLCSSRCDELRVSPRQPLAAQRSPQAKPGLAPLAPRRTSSESPSRLPVRASPGRPETVKRYASLPHISVSRR
SQ  SDSAVSVPTTQANATRRGSDGEARPLPRVAPPGTTWRRIKDEDVPHILRSTLPATALPLRVSSPEDSPAGTPQRKTSDAV
SQ  VQTEDVATSKTNSSTSPSLESRDPPQAPASGPVAPQGSDVDGPVLTKPPASAPFPHEGLSAVIAGFPTSRHGSPSRAARV
SQ  PPFNYVPSPMAAATMASDSAVEKAPVSSPASLLE
//
ID  O94353;
PN  Nuclear membrane organization protein apq12;
GN  apq12;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94353;
DR  Pfam: PF12716;
DE  Function: Involved in the regulation of lipid homeostasis in the endoplasmic reticulum, thereby impacting nuclear pore complex biogenesis and localization, and nucleocytoplasmic mRNA transport. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0140599;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0097038;
GO  GO:0006643;
GO  GO:0007077;
GO  GO:0051028;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLTSVLWNFVAKLAVDHGLNTNPDQVFQTVENVGKSFEKYETSFLKSLFNGNLGLSLPSAINILTLIIVLYFSLVIVNK
SQ  TTSIALALFKTLAVISFFLLIGCLFAYWFINNGSF
//
ID  P40532;
PN  Nuclear membrane organization protein APQ12;
GN  APQ12;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
DR  UNIPROT: P40532;
DR  UNIPROT: D6VVP2;
DR  Pfam: PF12716;
DE  Function: Involved in the regulation of lipid homeostasis in the endoplasmic reticulum, thereby impacting nuclear pore complex biogenesis and localization, and nucleocytoplasmic mRNA transport. {ECO:0000269|PubMed:15273328, ECO:0000269|PubMed:17724120, ECO:0000269|PubMed:20016074}.
DE  Reference Proteome: Yes;
DE  Interaction: P11484; IntAct: EBI-3685195; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3723382; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0055088;
GO  GO:0051028;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDATQPQYELSVVTQCLKSAIDVIQWLIPTITKFSQSHPLVFQLLFIFFTFYVFYKLLMNFITLVKRFLYLTLVVTCIGI
SQ  YMRGSQQFLTVDLLNFYNFVMSNRYYAFKIYTLFINALEREINTVYHLAQMKMEQLLK
//
ID  F6S3G9;
PN  Aquaporin-11;
GN  AQP11;
OS  9796;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Cell membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Cytoplasm {ECO:0000250|UniProtKB:Q8BHH1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BHH1}. Note=Localizes mainly to the periphery of lipid droplets. it accumulates partly in mitochondrial-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:Q8NBQ7}.
DR  UNIPROT: F6S3G9;
DR  Pfam: PF00230;
DE  Function: Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain. In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway (By similarity). Plays a role by maintaining an environment suitable for translation or protein foldings in the ER lumen namely by participating in the PKD1 glycosylation processing resulting in regulation of PKD1 membrane trafficking thereby preventing the accumulation of unfolding protein in ER. Plays a role in the proximal tubule function by regulating its endosomal acidification. May play a role in postnatal kidney development (By similarity). {ECO:0000250|UniProtKB:Q8BHH1, ECO:0000250|UniProtKB:Q8NBQ7}.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0015267;
GO  GO:0015254;
GO  GO:0015250;
GO  GO:0009992;
GO  GO:0048388;
GO  GO:0080170;
GO  GO:0050680;
GO  GO:1904293;
GO  GO:0032364;
GO  GO:0008284;
GO  GO:0006486;
GO  GO:0051260;
GO  GO:0006612;
GO  GO:0072014;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTALRALWSEMQDTCTSLGLMLSVVLLAGLARVVARQQQLHRPMAHAFVLEFLATLQLCCCTHELLLLSEQEPAHPTWPL
SQ  TLIYFFTLVHGLTLVGTSSNPCGVMMQMMLGGMSPEMGAVRLLAQLIGALGSRYCIGALWSLGLTKYHVSERSFACKNPI
SQ  QVDLPKAVIVEALCSFIFHSALLNFQEVRPKLRIHLLAALITFLVYAGGSLTGAVFNPALALSLHFKCFDEAFLQFFIVY
SQ  WLAPSLGILLMILMFSFFLPWLYNNHTINKKE
//
ID  Q8NBQ7;
PN  Aquaporin-11;
GN  AQP11;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:28042826}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24918044, ECO:0000269|PubMed:31546170}; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein {ECO:0000269|PubMed:24918044}. Cytoplasm {ECO:0000250|UniProtKB:Q8BHH1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BHH1}. Note=Localizes mainly to the periphery of lipid droplets (PubMed:24845055). it accumulates partly in mitochondrial-associated endoplasmic reticulum membranes (PubMed:31546170). {ECO:0000269|PubMed:24845055, ECO:0000269|PubMed:31546170}.
DR  UNIPROT: Q8NBQ7;
DR  Pfam: PF00230;
DR  OMIM: 609914;
DR  DisGeNET: 282679;
DE  Function: Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain (PubMed:24845055, PubMed:24918044, PubMed:31546170). In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway (PubMed:31546170). Plays a role by maintaining an environment suitable for translation or protein foldings in the ER lumen namely by participating in the PKD1 glycosylation processing resulting in regulation of PKD1 membrane trafficking thereby preventing the accumulation of unfolding protein in ER (By similarity). Plays a role in the proximal tubule function by regulating its endosomal acidification (By similarity). May play a role in postnatal kidney development (By similarity). {ECO:0000250|UniProtKB:Q8BHH1, ECO:0000269|PubMed:24845055, ECO:0000269|PubMed:24918044, ECO:0000269|PubMed:31546170}.
DE  Reference Proteome: Yes;
DE  Interaction: P42229; IntAct: EBI-3943260; Score: 0.37
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0015267;
GO  GO:0015254;
GO  GO:0015250;
GO  GO:0009992;
GO  GO:0048388;
GO  GO:0015793;
GO  GO:0080170;
GO  GO:0050680;
GO  GO:1904293;
GO  GO:1903573;
GO  GO:0032364;
GO  GO:0008284;
GO  GO:0006486;
GO  GO:0051260;
GO  GO:0006612;
GO  GO:0072014;
GO  GO:0030104;
GO  GO:0006833;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSPLLGLRSELQDTCTSLGLMLSVVLLMGLARVVARQQLHRPVAHAFVLEFLATFQLCCCTHELQLLSEQHPAHPTWTLT
SQ  LVYFFSLVHGLTLVGTSSNPCGVMMQMMLGGMSPETGAVRLLAQLVSALCSRYCTSALWSLGLTQYHVSERSFACKNPIR
SQ  VDLLKAVITEAVCSFLFHSALLHFQEVRTKLRIHLLAALITFLVYAGGSLTGAVFNPALALSLHFMCFDEAFPQFFIVYW
SQ  LAPSLGILLMILMFSFFLPWLHNNHTINKKE
//
ID  Q8BHH1;
PN  Aquaporin-11;
GN  Aqp11;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16107722, ECO:0000269|PubMed:21118806, ECO:0000269|PubMed:24854278}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Cell membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Cytoplasm {ECO:0000269|PubMed:16107722}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16107722}. Note=Localizes mainly to the periphery of lipid droplets. it accumulates partly in mitochondrial-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:Q8NBQ7}.
DR  UNIPROT: Q8BHH1;
DR  UNIPROT: Q8JZU1;
DR  Pfam: PF00230;
DE  Function: Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain (PubMed:21118806, PubMed:21251984). In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway (PubMed:23275615, PubMed:30656220). Plays a role by maintaining an environment suitable for translation or protein foldings in the ER lumen namely by participating in the PKD1 glycosylation processing resulting in regulation of PKD1 membrane trafficking thereby preventing the accumulation of unfolding protein in ER (PubMed:24854278, PubMed:18606867). Plays a role in the proximal tubule function by regulating its endosomal acidification (PubMed:16107722). May play a role in postnatal kidney development (PubMed:18701606, PubMed:23486012, PubMed:27582095). {ECO:0000269|PubMed:16107722, ECO:0000269|PubMed:18606867, ECO:0000269|PubMed:18701606, ECO:0000269|PubMed:21118806, ECO:0000269|PubMed:21251984, ECO:0000269|PubMed:23275615, ECO:0000269|PubMed:23486012, ECO:0000269|PubMed:24854278, ECO:0000269|PubMed:27582095, ECO:0000269|PubMed:30656220}.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0015267;
GO  GO:0015254;
GO  GO:0042802;
GO  GO:0015250;
GO  GO:0009992;
GO  GO:0048388;
GO  GO:0015793;
GO  GO:0080170;
GO  GO:0001822;
GO  GO:0050680;
GO  GO:1904293;
GO  GO:1903573;
GO  GO:0032364;
GO  GO:0008284;
GO  GO:0006486;
GO  GO:0051260;
GO  GO:0006612;
GO  GO:0072014;
GO  GO:0030104;
GO  GO:0006833;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSALLGLRPEVQDTCISLGLMLLFVLFVGLARVIARQQLHRPVVHAFVLEFLATFQLCCCTHELQVLSEQDSAHPTWTLT
SQ  LIYFFSLVHGLTLVGTASNPCGVMMQMILGGMSPEMGAVRLLAQLVSALCSRYCISALWSLSLTKYHYDERILACRNPIH
SQ  TDMSKAIIIEAICSFIFHSALLHFQEVRTKLRIHLLAALITFLAYAGGSLTGALFNPALALSLHFPCFDELFYKFFVVYW
SQ  LAPSVGVLMMILMFSFFLPWLHNNQMTNKKE
//
ID  Q8CHM1;
PN  Aquaporin-11;
GN  Aqp11;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Cell membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Cytoplasm {ECO:0000250|UniProtKB:Q8BHH1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BHH1}. Note=Localizes mainly to the periphery of lipid droplets. it accumulates partly in mitochondrial-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:Q8NBQ7}.
DR  UNIPROT: Q8CHM1;
DR  UNIPROT: Q6AZ79;
DR  Pfam: PF00230;
DE  Function: Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain. In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway (By similarity). Plays a role by maintaining an environment suitable for translation or protein foldings in the ER lumen namely by participating in the PKD1 glycosylation processing resulting in regulation of PKD1 membrane trafficking thereby preventing the accumulation of unfolding protein in ER. Plays a role in the proximal tubule function by regulating its endosomal acidification. May play a role in postnatal kidney development (By similarity). {ECO:0000250|UniProtKB:Q8BHH1, ECO:0000250|UniProtKB:Q8NBQ7}.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0015267;
GO  GO:0015254;
GO  GO:0042802;
GO  GO:0015250;
GO  GO:0009992;
GO  GO:0048388;
GO  GO:0015793;
GO  GO:0080170;
GO  GO:0001822;
GO  GO:0050680;
GO  GO:1904293;
GO  GO:1903573;
GO  GO:0032364;
GO  GO:0008284;
GO  GO:0006486;
GO  GO:0051260;
GO  GO:0006612;
GO  GO:0072014;
GO  GO:0055085;
GO  GO:0030104;
GO  GO:0006833;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSALLGLPPEVQDTCISLGLMLLVVLFMGLARVIARQQLHRPMVHAFVLEFLATFQLCYCTHELQLLSEQDSGHPTWTLT
SQ  LIYFFSLVHGLTLVGTASNPCGVMMQMILGGMSPEMGAVRLMAQLVSALCSRYCISALWSLSLTKYHFDERILACRNPIN
SQ  TDISKAIIIEAICSFIFHSALLHFQEVRTKLRIHVLAALITFLAYAGGSLTGALFNPALALSLHFPCFDESFYKFFVVYW
SQ  VAPSLGVLLMILMFSFFLPWLHNNQLSNKKE
//
ID  Q3MHM8;
PN  ADP-ribosylation factor-like protein 6-interacting protein 6;
GN  ARL6IP6;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q8BH07}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q3MHM8;
DR  Pfam: PF15062;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFVESGRRSAPLRRRPGTPVPFARPAYSVFSQGDSWGEGEVEEEEGCDQVARDLRAEFSAGSSSKLRKDPVLQPDGDGS
SQ  PVLPDKRNGIFSADAGGKALARRWPVQVLSILCSLLFAILLACLLAITYLIVKELHAENLKNEDDVNTGLLGFWSLLIIS
SQ  LTAGFSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKMTGHSFHMGYSMAILNGIVAALTVAWCLM
//
ID  Q8N6S5;
PN  ADP-ribosylation factor-like protein 6-interacting protein 6;
GN  ARL6IP6;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q8BH07}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q8N6S5;
DR  UNIPROT: B2RDS6;
DR  UNIPROT: Q7Z4G7;
DR  Pfam: PF15062;
DR  OMIM: 616495;
DR  DisGeNET: 151188;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q15125; IntAct: EBI-24694418; Score: 0.56
DE  Interaction: Q5NEB4; IntAct: EBI-2808841; Score: 0.00
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: Q9BZJ8; IntAct: EBI-24509770; Score: 0.56
DE  Interaction: A0PK11; IntAct: EBI-25264604; Score: 0.56
DE  Interaction: Q14973; IntAct: EBI-24664535; Score: 0.56
DE  Interaction: Q96HE8; IntAct: EBI-24679228; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-23703606; Score: 0.56
DE  Interaction: Q96GQ5; IntAct: EBI-24752673; Score: 0.56
DE  Interaction: Q6UW68; IntAct: EBI-24780992; Score: 0.56
DE  Interaction: Q0VAB0; IntAct: EBI-25279584; Score: 0.56
DE  Interaction: O14880; IntAct: EBI-25284176; Score: 0.56
DE  Interaction: Q8TAZ6; IntAct: EBI-24555520; Score: 0.56
DE  Interaction: P48165; IntAct: EBI-24802824; Score: 0.56
DE  Interaction: Q9NPL8; IntAct: EBI-24809431; Score: 0.56
DE  Interaction: Q8N661; IntAct: EBI-25273194; Score: 0.56
DE  Interaction: O43291; IntAct: EBI-21587968; Score: 0.35
DE  Interaction: Q9NVS9; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: Q9GZZ1; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: Q9BY43; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: Q15126; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: Q13951; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: P55957; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: P51452; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: P30043; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: P09488; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: O60493; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: O60361; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: O15498; IntAct: EBI-21736268; Score: 0.35
DE  Interaction: Q16853; IntAct: EBI-21784415; Score: 0.35
DE  Interaction: P14416; IntAct: EBI-20805470; Score: 0.37
DE  Interaction: P0DTC3; IntAct: EBI-25491278; Score: 0.64
DE  Interaction: P46108; IntAct: EBI-30820700; Score: 0.44
GO  GO:0016021;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFAESGWRSALRRRGPGTPGPVARPSYSSFTQGDSWGEGEVDEEEGCDQVARDLRAEFSAGAWSEPRKRSVLPPDGNGS
SQ  PVLPDKRNGIFPAAAGSRAQPRRWPVQVLSILCSLLFAILLAFLLAIAYLIVKELHAENLKNEDDVDTGLLGFWTLLIIS
SQ  LTAGFSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKLTGHSFHMGYSMAILNGIVAALTVAWCLM
//
ID  Q8BH07;
PN  ADP-ribosylation factor-like protein 6-interacting protein 6;
GN  Arl6ip6;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:31142202}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q8BH07;
DR  UNIPROT: Q8BSK7;
DR  UNIPROT: Q8VCL3;
DR  UNIPROT: Q9CY07;
DR  UNIPROT: Q9D4R5;
DR  UNIPROT: Q9WUH0;
DR  Pfam: PF15062;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFVESWRFAGARRRRQVTPGPATRPGYSDYTQGDSWGEGEGDEDEGCDQVARDLRAEFSARASSETKRAPLLPRVGDGS
SQ  PVLPDKRNGIFPATAAKRTQARRWPIQALSILCSLLFAVLLAFLLAIAYMIVKELHAENLKNEDDIHTGLLGFWSLLIIS
SQ  LTAGLSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKLTGHSFHMGYSMAILNGIVAALTVAWCLM
//
ID  Q68FV2;
PN  ADP-ribosylation factor-like protein 6-interacting protein 6;
GN  Arl6ip6;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q8BH07}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q68FV2;
DR  Pfam: PF15062;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFVESWRSVGPRRRRQVTPGPVTRSVYSDYTQGNSWSEDGDEGCDQVARDLRAEFSARASSESKRAPLLPRIGDGSPVL
SQ  PDKRNGIFPATAAKRTQARRWPIQALSILCSLLFAVLLAFLLAIAYLIVKELHTENSKNEDVVDTGLLGFWSLLIISLTA
SQ  GLSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKLTGHSFHMGYSMAILNGVVAALTVAWCLM
//
ID  A3KNS9;
PN  All-trans retinoic acid-induced differentiation factor;
GN  atraid;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q6UW56}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6UW56}.
DR  UNIPROT: A3KNS9;
DR  UNIPROT: Q502E7;
DR  UNIPROT: Q5RID6;
DR  PROSITE: PS00022;
DE  Function: Involved in osteoblast cell differentiation. May play a role in inducing the cell cycle arrest (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0048856;
GO  GO:0030154;
GO  GO:0033689;
GO  GO:0042177;
GO  GO:0030501;
GO  GO:0045669;
GO  GO:0010468;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTANVTVSSMYLFTVLLLLFNVYVNSQDTDAQLCQMCEGTIRHDSPVWSFCITKGYVKGHCCFKNNTSDVDTIIGLDLSN
SQ  CSISHVEHLYNSSTALIIDLSNNPISNLSDYVFQGFSQLTQLLLPSKLECPGGRASWEKVEVKSITRICEGQKNACNQTV
SQ  QMPLVCPENSLCSPYGPGFFECSCLNNFHGYKCMRQGEFPLVKVLGILTASTVVVSSVLWFTQRRKVKNT
//
ID  Q6UW56;
PN  All-trans retinoic acid-induced differentiation factor;
GN  ATRAID;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21723284}. Cell membrane {ECO:0000269|PubMed:17524364}; Single-pass membrane protein {ECO:0000269|PubMed:17524364}. Note=Colocalizes with NELL1 on the nuclear envelope and the perinuclear region (PubMed:21723284).
DR  UNIPROT: Q6UW56;
DR  UNIPROT: A8C1S2;
DR  UNIPROT: A8K779;
DR  UNIPROT: Q96FF6;
DR  UNIPROT: Q96RT2;
DR  UNIPROT: Q9Y2R7;
DR  UNIPROT: Q9Y5L7;
DR  PROSITE: PS00022;
DR  PROSITE: PS01186;
DR  PROSITE: PS50026;
DR  OMIM: 619682;
DR  DisGeNET: 51374;
DE  Function: Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway. {ECO:0000269|PubMed:21723284}.
DE  Reference Proteome: Yes;
DE  Interaction: Q93052; IntAct: EBI-736289; Score: 0.00
DE  Interaction: Q9Y5X1; IntAct: EBI-7876576; Score: 0.52
DE  Interaction: A0A6L8PDJ5; IntAct: EBI-2838097; Score: 0.00
DE  Interaction: Q92832; IntAct: EBI-7001256; Score: 0.61
DE  Interaction: Q00013; IntAct: EBI-24627560; Score: 0.56
DE  Interaction: Q8NCC5; IntAct: EBI-21822465; Score: 0.35
DE  Interaction: Q16236; IntAct: EBI-22030894; Score: 0.35
DE  Interaction: Q14145; IntAct: EBI-22030903; Score: 0.35
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005765;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030154;
GO  GO:0033689;
GO  GO:0042177;
GO  GO:0030501;
GO  GO:0045669;
GO  GO:0010468;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPHDPGSLTTLVPWAAALLLALGVERALALPEICTQCPGSVQNLSKVAFYCKTTRELMLHARCCLNQKGTILGLDLQNC
SQ  SLEDPGPNFHQAHTTVIIDLQANPLKGDLANTFRGFTQLQTLILPQHVNCPGGINAWNTITSYIDNQICQGQKNLCNNTG
SQ  DPEMCPENGSCVPDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGATTLSVSILLWATQRRKAKTS
//
ID  Q6PGD0;
PN  All-trans retinoic acid-induced differentiation factor;
GN  Atraid;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q6UW56}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6UW56}. Note=Colocalizes with NELL1 on the nuclear envelope and the perinuclear region. {ECO:0000250|UniProtKB:Q6UW56}.
DR  UNIPROT: Q6PGD0;
DR  UNIPROT: Q3UAH4;
DR  UNIPROT: Q810Q3;
DR  UNIPROT: Q9DD14;
DR  PROSITE: PS00022;
DR  PROSITE: PS01186;
DR  PROSITE: PS50026;
DE  Function: Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005765;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030154;
GO  GO:0033689;
GO  GO:0042177;
GO  GO:0030501;
GO  GO:0045669;
GO  GO:0010468;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASRESGGSRAAALLLVLGVERALALPEICTLCPGGMHNLSRVAAYCEDTSKLMQARCCLNQKGTILGLDLQNCSLKDPG
SQ  PNFLQAYTAIIIDLQANPLKDDLANTFRGFTQLQTLILPQDVPCPGGSNAWDNVTSFKDKQICQGQRDLCNSTGSPEMCP
SQ  ENGSCASDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGSTTLAISILLWGTQRRKAKAS
//
ID  Q5E9I6;
PN  ADP-ribosylation factor 3;
GN  ARF3;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q5E9I6;
DR  UNIPROT: Q0VCG1;
DR  Pfam: PF00025;
DR  PROSITE: PS51417;
DE  Function: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006886;
GO  GO:0006890;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRH
SQ  YFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCA
SQ  TSGDGLYEGLDWLANQLKNKK
//
ID  P61204;
PN  ADP-ribosylation factor 3;
GN  ARF3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:17555535}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}.
DR  UNIPROT: P61204;
DR  UNIPROT: A8K6G8;
DR  UNIPROT: B7ZB63;
DR  UNIPROT: P16587;
DR  PDB: 6II6;
DR  Pfam: PF00025;
DR  PROSITE: PS51417;
DR  OMIM: 103190;
DR  DisGeNET: 377;
DE  Function: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
DE  Reference Proteome: Yes;
DE  Interaction: P54259; IntAct: EBI-951076; Score: 0.00
DE  Interaction: P53365; IntAct: EBI-640718; Score: 0.37
DE  Interaction: O15264; IntAct: EBI-2255044; Score: 0.35
DE  Interaction: O35071; IntAct: EBI-2557531; Score: 0.40
DE  Interaction: P97302; IntAct: EBI-2559511; Score: 0.40
DE  Interaction: Q8VD62; IntAct: EBI-2562857; Score: 0.40
DE  Interaction: Q5PRE5; IntAct: EBI-2563058; Score: 0.40
DE  Interaction: Q14186; IntAct: EBI-8836223; Score: 0.35
DE  Interaction: Q8TBB1; IntAct: EBI-24495699; Score: 0.56
DE  Interaction: A2A935; IntAct: EBI-21024514; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P53367; IntAct: EBI-25568957; Score: 0.40
DE  Interaction: Q96CS3; IntAct: EBI-25770166; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-25937879; Score: 0.56
DE  Interaction: Q01995; IntAct: EBI-26878675; Score: 0.35
DE  Interaction: P34972; IntAct: EBI-26880846; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: Q96ED9; IntAct: EBI-34575530; Score: 0.27
GO  GO:0070062;
GO  GO:0000139;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006886;
GO  GO:0006890;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRH
SQ  YFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCA
SQ  TSGDGLYEGLDWLANQLKNKK
//
ID  P61205;
PN  ADP-ribosylation factor 3;
GN  Arf3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: P61205;
DR  UNIPROT: P16587;
DR  Pfam: PF00025;
DR  PROSITE: PS51417;
DE  Function: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
DE  Reference Proteome: Yes;
DE  Interaction: P35922; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.53
DE  Interaction: Q7TMB8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: F6SEU4; IntAct: EBI-16733301; Score: 0.53
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16726570; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006886;
GO  GO:0015031;
GO  GO:0006890;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRH
SQ  YFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCA
SQ  TSGDGLYEGLDWLANQLKNKK
//
ID  Q5R5P7;
PN  ADP-ribosylation factor 3;
GN  ARF3;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q5R5P7;
DR  Pfam: PF00025;
DR  PROSITE: PS51417;
DE  Function: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRH
SQ  YFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCA
SQ  TSGDGLYEGLDWLANQLKNKK
//
ID  P61206;
PN  ADP-ribosylation factor 3;
GN  Arf3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: P61206;
DR  UNIPROT: P16587;
DR  Pfam: PF00025;
DR  PROSITE: PS51417;
DE  Function: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16400563; Score: 0.35
DE  Interaction: P19332; IntAct: EBI-26374040; Score: 0.35
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006886;
GO  GO:0006890;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGNIFGNLLKSLIGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRH
SQ  YFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCA
SQ  TSGDGLYEGLDWLANQLKNKK
//
ID  P84085;
PN  ADP-ribosylation factor 5;
GN  ARF5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:17555535}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P84084}; Lipid-anchor {ECO:0000250|UniProtKB:P84084}.
DR  UNIPROT: P84085;
DR  UNIPROT: P26437;
DR  PDB: 2B6H;
DR  Pfam: PF00025;
DR  PROSITE: PS51417;
DR  OMIM: 103188;
DR  DisGeNET: 381;
DE  Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. {ECO:0000250|UniProtKB:P84084}. (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. {ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-25367743; Score: 0.37
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6191076; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: P61006; IntAct: EBI-11822843; Score: 0.35
DE  Interaction: Q96HD9; IntAct: EBI-24488061; Score: 0.56
DE  Interaction: Q8N9I9; IntAct: EBI-25277416; Score: 0.56
DE  Interaction: Q8WVK2; IntAct: EBI-21500567; Score: 0.35
DE  Interaction: Q9UNA3; IntAct: EBI-21543010; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-21559824; Score: 0.35
DE  Interaction: P46059; IntAct: EBI-21560916; Score: 0.35
DE  Interaction: Q9UHF4; IntAct: EBI-21590820; Score: 0.35
DE  Interaction: P54219; IntAct: EBI-21609589; Score: 0.35
DE  Interaction: P30550; IntAct: EBI-21613281; Score: 0.35
DE  Interaction: Q9Y5M8; IntAct: EBI-21633655; Score: 0.35
DE  Interaction: Q9NU53; IntAct: EBI-21700986; Score: 0.35
DE  Interaction: P56559; IntAct: EBI-21709189; Score: 0.35
DE  Interaction: P21589; IntAct: EBI-21722916; Score: 0.35
DE  Interaction: P55290; IntAct: EBI-21736384; Score: 0.35
DE  Interaction: P25445; IntAct: EBI-21766342; Score: 0.35
DE  Interaction: Q96GM1; IntAct: EBI-21806142; Score: 0.35
DE  Interaction: O60259; IntAct: EBI-21828465; Score: 0.35
DE  Interaction: P09923; IntAct: EBI-21831497; Score: 0.35
DE  Interaction: O94955; IntAct: EBI-21879222; Score: 0.35
DE  Interaction: Q86YS3; IntAct: EBI-15605267; Score: 0.40
DE  Interaction: P62491; IntAct: EBI-15605371; Score: 0.35
DE  Interaction: O75154; IntAct: EBI-15605449; Score: 0.40
DE  Interaction: Q71U36; IntAct: EBI-16800060; Score: 0.27
DE  Interaction: P14854; IntAct: EBI-21933521; Score: 0.35
DE  Interaction: O00746; IntAct: EBI-21934323; Score: 0.35
DE  Interaction: Q9H944; IntAct: EBI-25472954; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21132574; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: O95931; IntAct: EBI-25477072; Score: 0.35
DE  Interaction: Q96CS3; IntAct: EBI-25770808; Score: 0.35
DE  Interaction: Q96LU5; IntAct: EBI-27050332; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006886;
GO  GO:0006890;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:25255805};
SQ  MGLTVSALFSRIFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRH
SQ  YFQNTQGLIFVVDSNDRERVQESADELQKMLQEDELRDAVLLVFANKQDMPNAMPVSELTDKLGLQHLRSRTWYVQATCA
SQ  TQGTGLYDGLDWLSHELSKR
//
ID  P84084;
PN  ADP-ribosylation factor 5;
GN  Arf5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P84085}. Membrane {ECO:0000250|UniProtKB:P84085}; Lipid-anchor {ECO:0000250|UniProtKB:P84085}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}.
DR  UNIPROT: P84084;
DR  UNIPROT: A2RTC5;
DR  UNIPROT: P26437;
DR  Pfam: PF00025;
DR  PROSITE: PS51417;
DE  Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. {ECO:0000269|PubMed:11950392}.
DE  Reference Proteome: Yes;
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: Q9JKK1; IntAct: EBI-7569455; Score: 0.27
DE  Interaction: Q8BYR5; IntAct: EBI-7569528; Score: 0.60
DE  Interaction: F6SEU4; IntAct: EBI-16733301; Score: 0.53
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006886;
GO  GO:0015031;
GO  GO:0006890;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P84085};
SQ  MGLTVSALFSRIFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRH
SQ  YFQNTQGLIFVVDSNDRERVQESADELQKMLQEDELRDAVLLVFANKQDMPNAMPVSELTDKLGLQHLRSRTWYVQATCA
SQ  TQGTGLYDGLDWLSHELSKR
//
ID  P84083;
PN  ADP-ribosylation factor 5;
GN  Arf5;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250|UniProtKB:P84084}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P84085}. Membrane {ECO:0000250|UniProtKB:P84085}; Lipid-anchor {ECO:0000250|UniProtKB:P84085}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P84084}; Lipid-anchor {ECO:0000250|UniProtKB:P84084}.
DR  UNIPROT: P84083;
DR  UNIPROT: P26437;
DR  Pfam: PF00025;
DR  PROSITE: PS51417;
DE  Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. {ECO:0000250|UniProtKB:P84084}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-22241891; Score: 0.35
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-22248078; Score: 0.35
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0006886;
GO  GO:0006890;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P84085};
SQ  MGLTVSALFSRIFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRH
SQ  YFQNTQGLIFVVDSNDRERVQESADELQKMLQEDELRDAVLLVFANKQDMPNAMPVSELTDKLGLQHLRSRTWYVQATCA
SQ  TQGTGLYDGLDWLSHELSKR
//
ID  P54074;
PN  ERAD-associated E3 ubiquitin-protein ligase ASI1;
GN  ASI1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16735580, ECO:0000269|PubMed:17085444, ECO:0000269|PubMed:27831485}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16735580, ECO:0000269|PubMed:17085444}.
DR  UNIPROT: P54074;
DR  UNIPROT: D6VZU2;
DE  Function: E3 ubiquitin-protein ligase which transfers ubiquitin to substrates promoting their degradation. Part of the nuclear inner membrane (INM)-specific branch of the ER-associated degradation (ERAD) pathway, required for the elimination of misfolded proteins in the INM, a specialized ER subdomain. Required for ERG11 degradation (PubMed:25236469). Negative regulator of SPS-sensor signaling. Together with ASI2 and ASI3, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor- regulated genes in the absence of inducing signals (PubMed:16735580, PubMed:17085444). Controls amino acid permease (AAP) gene expression in response to amino acid availability, a process mediated by the transcription factors STP1 and STP1 (PubMed:11454748). {ECO:0000269|PubMed:11454748, ECO:0000269|PubMed:16735580, ECO:0000269|PubMed:17085444, ECO:0000269|PubMed:25236469}.
DE  Reference Proteome: Yes;
DE  Interaction: P53895; IntAct: EBI-10096457; Score: 0.46
DE  Interaction: P53983; IntAct: EBI-10096480; Score: 0.56
DE  Interaction: P02829; IntAct: EBI-3810442; Score: 0.35
DE  Interaction: P10614; IntAct: EBI-10096413; Score: 0.40
DE  Interaction: Q969F0; IntAct: EBI-11533969; Score: 0.56
GO  GO:0097658;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0034399;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0071230;
GO  GO:0016567;
GO  GO:0036369;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSSTSSENVFINSFSYLNQTSQAVISGNSTFANVINFPYRLGLSFIGAVNLQYEQTVKSEEIPPTLRSVFDTIGFFFSP
SQ  YAIFCFVIAIVLNRFVVFYAVLNNGSRRTLPLWLSNVFHVSAVVVLAMVSLGPLTLGKDFKILGDPAFAQEKFLLNIFYA
SQ  FAYSYCVETIFTIMRNSSPLEGTDYSLFELSIQFYTMTNNNTKFLDSPDYIIDCSMAILSRILIHLVEIFRLRNYRLLFS
SQ  TIMNLCHICYLGIRVKQGGWKSLPFSVKFRHFPKLFSVSIICLSLLIFKLSCLIRWDPFGKSRNSCELLQFYPLSRNWKK
SQ  YLNYTGEEDFSAMATKFALLLCSGTELMEKGIRREFPAINIPDNVNEKFFISGYLNELSKPYKENTSISFPKKNSSILKQ
SQ  RFFLMFPKSIIWIMKKLVGQVFFGFRDNKDEDIPDNDPSKMLKITKTNSLNNSAGHKEDIELELLNTSDDEYSEDYEPSE
SQ  VESLGDSDEENLEEDSLIFNETRDALLDLFSSEDNEVHTDYNWIMSTSRILQQKLLSDKTLTRASILDTKLSEVDETFGT
SQ  ESDFDLSCAVCKVNERNTVLWPCRCFAICEDCRISLGLRGFSTCVCCRSKVHGYCKVHPVSDSK
//
ID  P53895;
PN  Protein ASI2;
GN  ASI2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:17085444}; Multi-pass membrane protein {ECO:0000269|PubMed:17085444}.
DR  UNIPROT: P53895;
DR  UNIPROT: D6W124;
DE  Function: Part of the nuclear inner membrane (INM)-specific branch of the ER-associated degradation (ERAD) pathway, required for the elimination of misfolded proteins in the INM, a specialized ER subdomain. Required for ERG11 degradation (PubMed:25236469). Negative regulator of SPS-sensor signaling. Together with ASI2 and ASI3, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes in the absence of inducing signals (PubMed:17085444). Controls amino acid permease (AAP) gene expression in response to amino acid availability, a process mediated by the transcription factors STP1 and STP1 (PubMed:11454748). {ECO:0000269|PubMed:11454748, ECO:0000269|PubMed:17085444, ECO:0000269|PubMed:25236469}.
DE  Reference Proteome: Yes;
DE  Interaction: P38074; IntAct: EBI-855745; Score: 0.00
DE  Interaction: P25294; IntAct: EBI-3762277; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3793098; Score: 0.35
DE  Interaction: P10614; IntAct: EBI-10096421; Score: 0.40
DE  Interaction: P53983; IntAct: EBI-10096480; Score: 0.46
DE  Interaction: P54074; IntAct: EBI-10096457; Score: 0.46
GO  GO:0097658;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0071230;
GO  GO:0036369;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Curator Inference {ECO:0000305|PubMed:17085444};
SQ  MARPQNHRRSNWTERDDNDDYLFQRFLEESETRHSREPSPVTEQSQQELQQDVQQAIDGIFNSLRRNMSSTSNINRAANM
SQ  DATTNGNGGINADTIRATNANTADSPFTARQQSPLRTFLRNLFILDYFIGLILFPFSVYNILRSGFNSMTFSENDFIIEI
SQ  VGYWKFAKIFGSGGTTLIAYKDTGKLGLLGKFHNIIVFYSSPVIKHIMKSRDGNEPNLNWIRLMFAKAFELFVKVSTILI
SQ  YLAYGVSGTVYMVTAGFFFVLCLLFTVIRRYKGVHRMLVSQRITGPGVF
//
ID  P53983;
PN  Probable ERAD-associated E3 ubiquitin-protein ligase ASI1;
GN  ASI3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17085444}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17085444}.
DR  UNIPROT: P53983;
DR  UNIPROT: D6W1G9;
DE  Function: Part of the nuclear inner membrane (INM)-specific branch of the ER-associated degradation (ERAD) pathway, required for the elimination of misfolded proteins in the INM, a specialized ER subdomain. Required for ERG11 degradation (PubMed:25236469). Negative regulator of SPS-sensor signaling. Together with ASI2 and ASI3, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes in the absence of inducing signals (PubMed:17085444). Controls amino acid permease (AAP) gene expression in response to amino acid availability, a process mediated by the transcription factors STP1 and STP1 (PubMed:11454748). {ECO:0000269|PubMed:11454748, ECO:0000269|PubMed:17085444, ECO:0000269|PubMed:25236469}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-3763707; Score: 0.35
DE  Interaction: P53895; IntAct: EBI-10096480; Score: 0.46
DE  Interaction: P25346; IntAct: EBI-7752898; Score: 0.37
DE  Interaction: P38156; IntAct: EBI-7752951; Score: 0.37
DE  Interaction: P49626; IntAct: EBI-787273; Score: 0.35
DE  Interaction: P0C2I0; IntAct: EBI-787273; Score: 0.35
DE  Interaction: Q02159; IntAct: EBI-860284; Score: 0.00
DE  Interaction: P25294; IntAct: EBI-3660235; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3667430; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3777888; Score: 0.35
DE  Interaction: P39077; IntAct: EBI-3824502; Score: 0.35
DE  Interaction: P54074; IntAct: EBI-10096480; Score: 0.56
DE  Interaction: P10614; IntAct: EBI-10096429; Score: 0.40
DE  Interaction: P53846; IntAct: EBI-16291965; Score: 0.35
GO  GO:0097658;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0034399;
GO  GO:0046872;
GO  GO:0004842;
GO  GO:0071230;
GO  GO:0036369;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSTNILQHVKQLLHNRDVFSFFHNKTGNLNYLDNTTQKPEVFVSPNSTIVSAPTLDSFQALMEKGNFTTLQLAKVGIRMF
SQ  FSYSVSKYAVLCFSTAIILNRLTVMSSLRSNSTNIRLPLWSKTLLHLVATLSLVKALLQILSQFGLMHELHVSDTDFYAL
SQ  SVYLFVALSDCIEIFISSTTNVPSLICSDFSIWGLSLNLYIISKMPAGQQHIGDNVELLGAVFHRLVIHLVELFHIRAYR
SQ  LCGEVILNAGFFTAFVTRTYLNGLDFINICLIHNYFPGFFYISTILLASIGIFLKALFTSNPFRSLYSRYKNLEKWWRSN
SQ  NYNGEEEFNEIALSLCLLLTSNDYKIFKKSDNVKSVDEVAAFSNSYVVSGHLNQLQSTPEDLLSRKEMTTDSQLPGFART
SQ  YLGLFELVRTIILTYSRLLKNLLWSKNFESSIDKKPRVGKRKKRDLNKYVTEKNYKKFLYKPDVKELNIESDLRSLELLL
SQ  PEDDSSKDYFPPRKIDESVSDEEFDSDMESQLIIDEEKELTHLSSNAVDSDDLEEIAWNISMWSILNYEMDVHNKVNGPL
SQ  TRSQYGKRNPQGVLVDVVIERLLHHTNSRYMYKRLNMKDDDKLEFKFDFAFDSCDEVEEMDLSCLICKVNKRNIVTWPCR
SQ  CLALCDDCRISLGYKGFATCVSCDSEVKGYSKLNIV
//
ID  Q13625;
PN  Apoptosis-stimulating of p53 protein 2;
GN  TP53BP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. Sequester in the cytoplasm on overexpression of DDX42.
DR  UNIPROT: Q13625;
DR  UNIPROT: B4DG66;
DR  UNIPROT: Q12892;
DR  UNIPROT: Q86X75;
DR  UNIPROT: Q96KQ3;
DR  PDB: 1YCS;
DR  PDB: 2UWQ;
DR  PDB: 4A63;
DR  PDB: 4IRV;
DR  PDB: 6GHM;
DR  PDB: 6HKP;
DR  Pfam: PF12796;
DR  Pfam: PF00018;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS50002;
DR  OMIM: 602143;
DR  DisGeNET: 7159;
DE  Function: Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions with proteins such as TP53 (PubMed:12524540). Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of NAE1 to conjugate NEDD8 to CUL1, and thereby decreases NAE1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42. {ECO:0000269|PubMed:11684014, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12694406, ECO:0000269|PubMed:19377511}.
DE  Reference Proteome: Yes;
DE  Interaction: O95996; IntAct: EBI-8830464; Score: 0.54
DE  Interaction: P10415; IntAct: EBI-15723849; Score: 0.65
DE  Interaction: P27958; IntAct: EBI-9389968; Score: 0.64
DE  Interaction: P29991; IntAct: EBI-8828390; Score: 0.37
DE  Interaction: P49790; IntAct: EBI-9688225; Score: 0.35
DE  Interaction: P61970; IntAct: EBI-9688225; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-9692277; Score: 0.64
DE  Interaction: Q07817; IntAct: EBI-15723914; Score: 0.56
DE  Interaction: Q12840; IntAct: EBI-731035; Score: 0.00
DE  Interaction: P05067; IntAct: EBI-77660; Score: 0.58
DE  Interaction: P62136; IntAct: EBI-7267006; Score: 0.86
DE  Interaction: P68104; IntAct: EBI-731032; Score: 0.00
DE  Interaction: P21246; IntAct: EBI-731038; Score: 0.00
DE  Interaction: Q9BVJ6; IntAct: EBI-731041; Score: 0.00
DE  Interaction: Q13432; IntAct: EBI-731044; Score: 0.00
DE  Interaction: Q9BYC9; IntAct: EBI-733610; Score: 0.00
DE  Interaction: Q13107; IntAct: EBI-736082; Score: 0.00
DE  Interaction: O15265; IntAct: EBI-952468; Score: 0.00
DE  Interaction: P04637; IntAct: EBI-1026207; Score: 0.90
DE  Interaction: P46937; IntAct: EBI-6912563; Score: 0.78
DE  Interaction: P46936; IntAct: EBI-7804125; Score: 0.40
DE  Interaction: P63104; IntAct: EBI-7195756; Score: 0.67
DE  Interaction: P46108; IntAct: EBI-1960202; Score: 0.40
DE  Interaction: Q04917; IntAct: EBI-1644092; Score: 0.64
DE  Interaction: Q04206; IntAct: EBI-1749490; Score: 0.56
DE  Interaction: P35570; IntAct: EBI-1751169; Score: 0.57
DE  Interaction: P81122; IntAct: EBI-1751281; Score: 0.48
DE  Interaction: O08724; IntAct: EBI-1751296; Score: 0.35
DE  Interaction: O14654; IntAct: EBI-1751296; Score: 0.35
DE  Interaction: P35569; IntAct: EBI-1751450; Score: 0.52
DE  Interaction: Q13625; IntAct: EBI-7907803; Score: 0.62
DE  Interaction: P36873; IntAct: EBI-7908028; Score: 0.85
DE  Interaction: Q92843; IntAct: EBI-7908070; Score: 0.68
DE  Interaction: Q81ZG1; IntAct: EBI-2838000; Score: 0.00
DE  Interaction: Q14457; IntAct: EBI-3257986; Score: 0.35
DE  Interaction: P31016; IntAct: EBI-7966630; Score: 0.44
DE  Interaction: Q09472; IntAct: EBI-8632299; Score: 0.50
DE  Interaction: Q8IUQ4; IntAct: EBI-10261292; Score: 0.56
DE  Interaction: P67870; IntAct: EBI-7137665; Score: 0.37
DE  Interaction: Q13387; IntAct: EBI-7240832; Score: 0.37
DE  Interaction: P53350; IntAct: EBI-7314465; Score: 0.37
DE  Interaction: Q8NEY8; IntAct: EBI-7317291; Score: 0.37
DE  Interaction: Q8TEW0; IntAct: EBI-6911368; Score: 0.53
DE  Interaction: A6NKD9; IntAct: EBI-6911368; Score: 0.35
DE  Interaction: P41236; IntAct: EBI-6911368; Score: 0.35
DE  Interaction: O75901; IntAct: EBI-6911368; Score: 0.35
DE  Interaction: Q9H3G5; IntAct: EBI-6911368; Score: 0.35
DE  Interaction: P34932; IntAct: EBI-6911368; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-6911368; Score: 0.67
DE  Interaction: Q8NHQ8; IntAct: EBI-6911368; Score: 0.53
DE  Interaction: Q92598; IntAct: EBI-6911368; Score: 0.35
DE  Interaction: Q02833; IntAct: EBI-6911368; Score: 0.35
DE  Interaction: Q15834; IntAct: EBI-6911368; Score: 0.35
DE  Interaction: P04083; IntAct: EBI-6911368; Score: 0.35
DE  Interaction: A6NK89; IntAct: EBI-6912271; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-8796749; Score: 0.35
DE  Interaction: Q9Y2J4; IntAct: EBI-8797381; Score: 0.35
DE  Interaction: Q7TSJ6; IntAct: EBI-8798662; Score: 0.27
DE  Interaction: Q4VCS5; IntAct: EBI-8799893; Score: 0.27
DE  Interaction: Q9WMX2; IntAct: EBI-9082105; Score: 0.37
DE  Interaction: Q2TBE0; IntAct: EBI-10175037; Score: 0.56
DE  Interaction: Q8WWY3; IntAct: EBI-10177388; Score: 0.56
DE  Interaction: O14777; IntAct: EBI-10181501; Score: 0.56
DE  Interaction: P17031; IntAct: EBI-10199685; Score: 0.56
DE  Interaction: P40222; IntAct: EBI-10207929; Score: 0.56
DE  Interaction: P56279; IntAct: EBI-10215275; Score: 0.56
DE  Interaction: P57075; IntAct: EBI-10215824; Score: 0.56
DE  Interaction: P61968; IntAct: EBI-10219004; Score: 0.56
DE  Interaction: P62807; IntAct: EBI-10219796; Score: 0.56
DE  Interaction: P62875; IntAct: EBI-10219932; Score: 0.56
DE  Interaction: P62993; IntAct: EBI-10220253; Score: 0.56
DE  Interaction: Q86Y26; IntAct: EBI-10230509; Score: 0.56
DE  Interaction: Q494U1; IntAct: EBI-10241572; Score: 0.56
DE  Interaction: Q53HC0; IntAct: EBI-10242635; Score: 0.56
DE  Interaction: Q8N5A5; IntAct: EBI-10265979; Score: 0.56
DE  Interaction: Q8N5M1; IntAct: EBI-10266628; Score: 0.56
DE  Interaction: Q8NCE2; IntAct: EBI-10269256; Score: 0.56
DE  Interaction: Q92844; IntAct: EBI-10279575; Score: 0.56
DE  Interaction: Q96DC9; IntAct: EBI-10284602; Score: 0.56
DE  Interaction: Q96GG9; IntAct: EBI-10286368; Score: 0.56
DE  Interaction: Q9BUJ2; IntAct: EBI-10298924; Score: 0.56
DE  Interaction: Q9BUZ4; IntAct: EBI-10299140; Score: 0.56
DE  Interaction: Q9NU19; IntAct: EBI-10313701; Score: 0.56
DE  Interaction: Q9UBU9; IntAct: EBI-10319914; Score: 0.56
DE  Interaction: Q9UQB8; IntAct: EBI-10324972; Score: 0.56
DE  Interaction: Q9Y2D8; IntAct: EBI-10326054; Score: 0.56
DE  Interaction: Q96J02; IntAct: EBI-10635597; Score: 0.40
DE  Interaction: Q9BYG5; IntAct: EBI-11002976; Score: 0.35
DE  Interaction: Q9NPB6; IntAct: EBI-11011731; Score: 0.35
DE  Interaction: Q9JK83; IntAct: EBI-11052294; Score: 0.35
DE  Interaction: P46938; IntAct: EBI-11138299; Score: 0.35
DE  Interaction: O75665; IntAct: EBI-11365691; Score: 0.27
DE  Interaction: Q15154; IntAct: EBI-11366535; Score: 0.27
DE  Interaction: Q5BJF6; IntAct: EBI-11367291; Score: 0.27
DE  Interaction: Q5JU00; IntAct: EBI-11367780; Score: 0.27
DE  Interaction: Q6ZU80; IntAct: EBI-11370150; Score: 0.27
DE  Interaction: Q7Z7A1; IntAct: EBI-11371427; Score: 0.27
DE  Interaction: Q8N4C6; IntAct: EBI-11374469; Score: 0.27
DE  Interaction: Q8TES7; IntAct: EBI-11374846; Score: 0.27
DE  Interaction: Q96KN7; IntAct: EBI-11376202; Score: 0.27
DE  Interaction: Q96NL6; IntAct: EBI-11376636; Score: 0.27
DE  Interaction: Q96ST8; IntAct: EBI-11377220; Score: 0.27
DE  Interaction: Q9Y2I6; IntAct: EBI-11379511; Score: 0.27
DE  Interaction: O60308; IntAct: EBI-11380299; Score: 0.27
DE  Interaction: O94986; IntAct: EBI-11381405; Score: 0.27
DE  Interaction: Q5TB80; IntAct: EBI-11385924; Score: 0.27
DE  Interaction: Q66GS9; IntAct: EBI-11386281; Score: 0.27
DE  Interaction: Q68CZ1; IntAct: EBI-11386978; Score: 0.27
DE  Interaction: Q8IW35; IntAct: EBI-11391901; Score: 0.27
DE  Interaction: Q8N137; IntAct: EBI-11392655; Score: 0.27
DE  Interaction: Q8N960; IntAct: EBI-11393386; Score: 0.27
DE  Interaction: Q9C0F1; IntAct: EBI-11397104; Score: 0.27
DE  Interaction: Q9HC77; IntAct: EBI-11397411; Score: 0.27
DE  Interaction: Q15435; IntAct: EBI-12451625; Score: 0.51
DE  Interaction: O43295; IntAct: EBI-21563971; Score: 0.35
DE  Interaction: Q7Z4N8; IntAct: EBI-21583801; Score: 0.35
DE  Interaction: Q86YM7; IntAct: EBI-21671273; Score: 0.35
DE  Interaction: Q9UMS4; IntAct: EBI-21763056; Score: 0.35
DE  Interaction: Q96ES7; IntAct: EBI-21781962; Score: 0.35
DE  Interaction: Q96NE9; IntAct: EBI-21880697; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: Q8N3R9; IntAct: EBI-21911830; Score: 0.35
DE  Interaction: Q9H3D4; IntAct: EBI-15685239; Score: 0.44
DE  Interaction: O15350; IntAct: EBI-15685344; Score: 0.44
DE  Interaction: P12830; IntAct: EBI-16124887; Score: 0.35
DE  Interaction: P35222; IntAct: EBI-16124887; Score: 0.58
DE  Interaction: Q05086; IntAct: EBI-16814851; Score: 0.35
DE  Interaction: P16403; IntAct: EBI-20919284; Score: 0.40
DE  Interaction: Q15149; IntAct: EBI-20926194; Score: 0.40
DE  Interaction: Q9NPJ6; IntAct: EBI-25472202; Score: 0.27
DE  Interaction: Q6NSK7; IntAct: EBI-21387894; Score: 0.00
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P46934; IntAct: EBI-30832503; Score: 0.44
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0051059;
GO  GO:0002039;
GO  GO:0017124;
GO  GO:0007049;
GO  GO:0072332;
GO  GO:0045786;
GO  GO:1900119;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMPMFLTVYLSNNEQHFTEVPVTPETICRDVVDLCKEPGESDCHLAEVWCGSERPVADNERMFDVLQRFGSQRNEVRFFL
SQ  RHERPPGRDIVSGPRSQDPSLKRNGVKVPGEYRRKENGVNSPRMDLTLAELQEMASRQQQQIEAQQQLLATKEQRLKFLK
SQ  QQDQRQQQQVAEQEKLKRLKEIAENQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNNLFQQKQRELVLAVSKVEELTR
SQ  QLEMLKNGRIDSHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVNELRDRLWKKKAALQ
SQ  QKENLPVSSDGNLPQQAASAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLVIQASEGPMKIQTLPNMRSGAASQ
SQ  TKGSKIHPVGPDWSPSNADLFPSQGSASVPQSTGNALDQVDDGEVPLREKEKKVRPFSMFDAVDQSNAPPSFGTLRKNQS
SQ  SEDILRDAQVANKNVAKVPPPVPTKPKQINLPYFGQTNQPPSDIKPDGSSQQLSTVVPSMGTKPKPAGQQPRVLLSPSIP
SQ  SVGQDQTLSPGSKQESPPAAAVRPFTPQPSKDTLLPPFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTHTRGPH
SQ  FSSVYGKPVIAAAQNQQQHPENIYSNSQGKPGSPEPETEPVSSVQENHENERIPRPLSPTKLLPFLSNPYRNQSDADLEA
SQ  LRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSYPSKSASVTASSESPVEIQNPYLHVEPEKEV
SQ  VSLVPESLSPEDVGNASTENSDMPAPSPGLDYEPEGVPDNSPNLQNNPEEPNPEAPHVLDVYLEEYPPYPPPPYPSGEPE
SQ  GPGEDSVSMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGI
SQ  TALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGY
SQ  TQCSQFLYGVQEKMGIMNKGVIYALWDYEPQNDDELPMKEGDCMTIIHREDEDEIEWWWARLNDKEGYVPRNLLGLYPRI
SQ  KPRQRSLA
//
ID  Q8CG79;
PN  Apoptosis-stimulating of p53 protein 2;
GN  Tp53bp2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. {ECO:0000250}.
DR  UNIPROT: Q8CG79;
DR  UNIPROT: Q3UYM7;
DR  UNIPROT: Q8K2L5;
DR  Pfam: PF12796;
DR  Pfam: PF14604;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS50002;
DE  Function: Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions with proteins such as TP53 (By similarity). Regulates p53/TP53 by enhancing the DNA binding and transactivation function of p53/TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis- stimulating activity is inhibited by its interaction with DDX42 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q13625}.
DE  Reference Proteome: Yes;
DE  Interaction: O35626; IntAct: EBI-4325310; Score: 0.37
DE  Interaction: Q9EQ32; IntAct: EBI-654281; Score: 0.37
DE  Interaction: P35569; IntAct: EBI-1751427; Score: 0.40
DE  Interaction: Q80YT7; IntAct: EBI-16732484; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16750831; Score: 0.35
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0051059;
GO  GO:0002039;
GO  GO:0017124;
GO  GO:0007049;
GO  GO:0007417;
GO  GO:0009792;
GO  GO:0007507;
GO  GO:0072332;
GO  GO:1900119;
GO  GO:1901216;
GO  GO:0010212;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMPMFLTVYLSNSEQHFTEVPVTPETICRDVVDLCKEPGENDCHLAEVWCGSERPVADNERMFDVLQRFGSQRNEVRFFL
SQ  RHERPPNRDIVSGPRSQDPSVKRNGVKVPGEHRRKENGVNSPRLDLTLAELQEMASRQQQQIEAQQQMLATKEQRLKFLK
SQ  QQDQRQQQQAAEQEKLKRLREIAESQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNSLFQQKQRELVLAVSKVEELTR
SQ  QLEMLKNGRIDGHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVSELRDRLWKKKAALQ
SQ  QKENLPVSPDGNLPQQAVSAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLLMQSAEGPMKIQTLPNMRSGAASQ
SQ  SKGSKAHPASPDWNPSNADLLPSQGSSVPQSAGTALDQVDDGEIAVREKEKKVRPFSMFDTVDQCAAPPSFGTLRKNQSS
SQ  EDILRDAQAVNKNVAKVPPPVPTKPKQIHLPYFGQTAQSPSDMKPDGNAQQLPIAATSVGAKLKPAGPQARMLLSPGAPS
SQ  GGQDQVLSPASKQESPPAAAVRPFTPQPSKDTFPPAFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTQPRGPHF
SQ  SSVYGKPVIAAAQNPQQHPENIYSCSQGKPGSPEPETETVSSVHESHENERIPRPLSPTKLLPFLSNPYRNQSDADLEAL
SQ  RKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSHPSKSPGSVTVNPESSVEIPNPYLHVEPEKEV
SQ  GSLVPEPLSPEDMGSASTENSDVPAPSAGLEYVSEGVTDSSTNLQNNVEETNPEAPHLLEVYLEEYPPYPPPPYPSGEPE
SQ  VSEEDSARMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGI
SQ  TALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGY
SQ  TQCSQFLYGVQEKMGIMNKGVIYALWDYEPQHDDELLMKEGDCMTVIRREDEEEIEWWWARLNDKEGYVPRNLLGLYPRI
SQ  KPRQRSLA
//
ID  Q9N0Z4;
PN  Phospholipid-transporting ATPase IF;
GN  ATP11B;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Recycling endosome membrane {ECO:0000250|UniProtKB:Q9Y2G3}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000250|UniProtKB:Q9Y2G3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2G3}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9Y2G3}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A, mainly located in recycling endosomes. {ECO:0000250|UniProtKB:Q9Y2G3}. [Isoform 2]: Nucleus inner membrane {ECO:0000269|PubMed:11058586}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9N0Z4;
DR  UNIPROT: Q8WMR2;
DR  Pfam: PF16212;
DR  Pfam: PF16209;
DR  PROSITE: PS00154;
DE  Function: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of intracellular membranes. May contribute to the maintenance of membrane lipid asymmetry in endosome compartment. {ECO:0000250|UniProtKB:Q9Y2G3}. [Isoform 2]: Appears to play a role in the subnuclear trafficking of transcription factors with RING motifs. {ECO:0000269|PubMed:11058586, ECO:0000269|PubMed:18584949}.
DE  Reference Proteome: Yes;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0055038;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000287;
GO  GO:0090555;
GO  GO:0090556;
GO  GO:0015917;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  LGFDPPHQSDTRTIYIANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLFEQFRRVANFYFLIIFLVQLMIDTPTSPI
SQ  TSGLPLFFVITVTAIKQGYEDWLRHNSDNEVNGAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDG
SQ  SCHVTTASLDGETNLKTHVAVPETAVLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPESLLLRGAR
SQ  LKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLIILISEAIISTILKYTWQAEEKWDEPWYNQKTEH
SQ  QRNSSKILRFISDFLAFLVLYNFIIPISLYVTVEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDK
SQ  TGTLTENEMQFRECSIHGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHVNSLSHLTSSSSFRTSPENDTELIKEHDLF
SQ  FKAVSLCHTVQISSVQTDGIGDGPWQSSLAPSQLEYYASSPDEKALVEAAARIGIVFVGNTEETMEVKILGKLERYKLLH
SQ  VLEFDSDRRRMSVIVQAPSGERFLFAKGAESSILPKCIGGEIEKTRIHVDEFALKGLRTLCVAYRQFTSKEYEVIDRRLF
SQ  EARTALQQREEKLADVFHYIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSCGHFHRTMN
SQ  ILELTNQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLFMEVCRNCSAVLCCRMAPLQKAKVIRLIK
SQ  ISPEKPITIGCWDGANDVSMIQEAHVGIGIMGKERRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVC
SQ  FITPQFLYQFYCLFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHIDPHILQNKPTLYRDISKNRLLSIKTFLYWTILG
SQ  FSRSFIFLFGSYFLIGKDASLLGNGQMFGNWTFGTLVFTVMVITVTVKMALETHFWTWINHLVTWGSIIFYFVFSLFYGG
SQ  ILWPFLGSQNMYFVFIQLVSSGSAWFAIILMVVTCLFLDVMKKVFDRQLHPTSTEKAQLTETNSSIKCVDSLCCFPEGET
SQ  TCTSVRRMLERVIGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC
//
ID  A7MB71;
PN  Protein ATP1B4;
GN  ATP1B4;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Detected in nuclear envelops. {ECO:0000250}.
DR  UNIPROT: A7MB71;
DR  Pfam: PF00287;
DR  PROSITE: PS00390;
DR  PROSITE: PS00391;
DE  Function: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005637;
GO  GO:0005890;
GO  GO:0006813;
GO  GO:0006355;
GO  GO:0006814;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRQLRSRRAPALPYGYRYRLDDQDEVNQNYLADEEEEAEEEARVMVVPDLEEEEEEEEEKEEEEKEEEDSHSQETDSAW
SQ  WRKLQIVNEYLWDPEKRTSLARTGQSWSLILVIYFFFYASLAAVITLCMYTLFLTISPYMPTFTERVKPPGVMIRPFAHS
SQ  LNFNFNVSEPDTWQHYVISLNGFLQGYNDSLQEEMNVDCPPGQYFIQDGDEDEDKKACQFKRSFLKNCSGLEDPTFGYST
SQ  GQPCILLKMNRIVGFRPERGDPVKVSCKVQRGDENDIRSINYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVKN
SQ  QAVPVQCQLKGKGIINDVINDRFVGRVIFTLNIET
//
ID  Q9UN42;
PN  Protein ATP1B4;
GN  ATP1B4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Detected in nuclear envelops. {ECO:0000269|PubMed:14656723, ECO:0000269|PubMed:17592128}.
DR  UNIPROT: Q9UN42;
DR  UNIPROT: Q17RR0;
DR  UNIPROT: Q9UN41;
DR  Pfam: PF00287;
DR  PROSITE: PS00390;
DR  PROSITE: PS00391;
DR  OMIM: 301073;
DR  DisGeNET: 23439;
DE  Function: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit. {ECO:0000269|PubMed:17592128}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9H1E5; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q5BVD1; IntAct: EBI-24610156; Score: 0.56
DE  Interaction: P07306; IntAct: EBI-24622793; Score: 0.56
DE  Interaction: Q7Z2K6; IntAct: EBI-24534258; Score: 0.56
DE  Interaction: Q9BZL3; IntAct: EBI-24550199; Score: 0.56
DE  Interaction: O60636; IntAct: EBI-24576756; Score: 0.56
DE  Interaction: Q8N6G5; IntAct: EBI-24583309; Score: 0.56
DE  Interaction: Q07325; IntAct: EBI-24593256; Score: 0.56
DE  Interaction: Q8WVV5; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q9Y219; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q9UK28; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q9NQZ7; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q9HCN3; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q9BZ76; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q96J42; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q8TCT7; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q8N766; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q86UD1; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q5HYA8; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q14393; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q13733; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q13683; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q03167; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: P55899; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: O75298; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: Q9CSN1; IntAct: EBI-15644307; Score: 0.40
GO  GO:0005887;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005890;
GO  GO:0022890;
GO  GO:0006813;
GO  GO:0006355;
GO  GO:0006814;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRQLRSRRAPSFPYSYRYRLDDPDEANQNYLADEEEEAEEEARVTVVPKSEEEEEEEEKEEEEEEEKEEEEGQGQPTGN
SQ  AWWQKLQIMSEYLWDPERRMFLARTGQSWSLILLIYFFFYASLAAVITLCMYTLFLTISPYIPTFTERVKPPGVMIRPFA
SQ  HSLNFNFNVSEPDTWQHYVISLNGFLQGYNDSLQEEMNVDCPPGQYFIQDGNEDEDKKACQFKRSFLKNCSGLEDPTFGY
SQ  STGQPCILLKMNRIVGFRPELGDPVKVSCKVQRGDENDIRSISYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVV
SQ  KNQAVPVQCQLKGKGVINDVINDRFVGRVIFTLNIET
//
ID  Q99ME6;
PN  Protein ATP1B4;
GN  Atp1b4;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Detected in nuclear envelops. {ECO:0000250}.
DR  UNIPROT: Q99ME6;
DR  UNIPROT: Q543D0;
DR  UNIPROT: Q99ME5;
DR  Pfam: PF00287;
DR  PROSITE: PS00390;
DR  PROSITE: PS00391;
DE  Function: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6ZWR6; IntAct: EBI-15644511; Score: 0.37
DE  Interaction: Q921T2; IntAct: EBI-15644413; Score: 0.37
DE  Interaction: Q9CSN1; IntAct: EBI-15644494; Score: 0.37
GO  GO:0000785;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0005890;
GO  GO:0006813;
GO  GO:0006355;
GO  GO:0006814;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRQLRSRRAPAFPYGYRYRLDDQDEANHNYLADEEEEAEEEAQVMMVPGLEEEEEEEEGKEEEEEREEEEGQGQSTGSA
SQ  WWRKLQIVNEYLWDPEKRMSLARTGQSRSLILVIYFFFYASLAAVITLFIYMLFLAISPYMPTFTEQVKPPGVMIRPFAH
SQ  SLNFNFNVSEPETWQRYVISLNGFLQGYNDSLQEEMNIDCPPGRYFIQDGDEDEDKKACQFKRSFLKNCSGLEDPTFGYS
SQ  TGQPCILLKMNRIVGFRPEFGDPVKVSCKVQKGDENDIRSINYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVK
SQ  NQAVPVQCQLKGKGIVNDVINDRFVGRIIFTLNIET
//
ID  Q9BDK6;
PN  Protein ATP1B4;
GN  ATP1B4;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:14656723}; Single-pass type II membrane protein {ECO:0000269|PubMed:14656723}. Note=Detected in nuclear envelops.
DR  UNIPROT: Q9BDK6;
DR  UNIPROT: Q9BDK5;
DR  Pfam: PF00287;
DR  PROSITE: PS00390;
DR  PROSITE: PS00391;
DE  Function: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005890;
GO  GO:0006813;
GO  GO:0006355;
GO  GO:0006814;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRQLRSRRAPAFPYGYGYRLDDQDEVNQNYLADEEEEAEEARVMVVPDLEEEEKEEEEEKEEDEKEEEESHHQDTRSAW
SQ  WQKLQIVNEYLWDPEKRMSLARTGQSLSLLLVIYFFFYASLAAVITLCMYTLFLTISPYVPTFTERVKPPGVMIRPFAHS
SQ  LNFNFNVSEPDTWQHYVISLNGFLQGYNDSLQEEMNVDCPPGQYFIQDGDEDEDKKACQFKRSFLKNCSGLEDPTFGYST
SQ  GQPCILLKMNRIVGFRPELGDPVKVSCKVQRGDENDIRSISYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVKN
SQ  QAVPVQCQLKGKGIINDVINDRFVGRVIFTLNIET
//
ID  Q9R193;
PN  Protein ATP1B4;
GN  Atp1b4;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Detected in nuclear envelops. {ECO:0000250}.
DR  UNIPROT: Q9R193;
DR  UNIPROT: Q9R192;
DR  Pfam: PF00287;
DR  PROSITE: PS00390;
DR  PROSITE: PS00391;
DE  Function: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5PQX1; IntAct: EBI-15644460; Score: 0.40
DE  Interaction: D4A8G7; IntAct: EBI-15644371; Score: 0.40
GO  GO:0000785;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0005890;
GO  GO:0006813;
GO  GO:0006355;
GO  GO:0006814;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRQLRSRRAPAFPYGYRYRLDDQDEMNHNYLADEEEEAEEEAQVMMVPGLEEEEEEEEGKEEEEEREEEEGQGQSTGNA
SQ  WWRKLQIVNEYLWDPEKRMSLARTGQSRSLILVIYFFFYASLAAVITLFIYMLFLAISPYMPTFTEQVKPPGVMIRPFAH
SQ  SLNFNFNVSEPETWQRYVISLNGFLQGYNDSLQEEMNIDCPPGQYFIQDGDEDEDKKACQFKRSFLKNCSGLEDPTFGYS
SQ  TGQPCILLKMNRIVGFRPEFGDPVKVSCKVQKGDENDIRSINYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVK
SQ  NQEVPVQCQLKGKGIVNDVINDRFVGRIIFTLNIET
//
ID  Q93084;
PN  Sarcoplasmic/endoplasmic reticulum calcium ATPase 3;
GN  ATP2A3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15028735}; Multi-pass membrane protein {ECO:0000269|PubMed:15028735}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15028735}; Multi-pass membrane protein {ECO:0000269|PubMed:15028735}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:15028735}; Multi-pass membrane protein {ECO:0000269|PubMed:15028735}.
DR  UNIPROT: Q93084;
DR  UNIPROT: A8MZG0;
DR  UNIPROT: D3DTJ8;
DR  UNIPROT: O60900;
DR  UNIPROT: O60901;
DR  UNIPROT: O75501;
DR  UNIPROT: O75502;
DR  UNIPROT: Q16115;
DR  UNIPROT: Q6JHX1;
DR  UNIPROT: Q8TEX5;
DR  UNIPROT: Q8TEX6;
DR  Pfam: PF00689;
DR  Pfam: PF00690;
DR  PROSITE: PS00154;
DR  OMIM: 601929;
DR  DisGeNET: 489;
DE  Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction. {ECO:0000269|PubMed:11956212, ECO:0000269|PubMed:15028735}.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-26496082; Score: 0.35
DE  Interaction: Q9HAW0; IntAct: EBI-1064949; Score: 0.00
DE  Interaction: Q9P2S5; IntAct: EBI-1079489; Score: 0.00
DE  Interaction: P04439; IntAct: EBI-1079517; Score: 0.00
DE  Interaction: P13569; IntAct: EBI-1171098; Score: 0.35
DE  Interaction: P16333; IntAct: EBI-1967197; Score: 0.40
DE  Interaction: P15336; IntAct: EBI-5529812; Score: 0.35
DE  Interaction: P04578; IntAct: EBI-6177436; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: Q20MH8; IntAct: EBI-12586007; Score: 0.35
DE  Interaction: P22460; IntAct: EBI-21505491; Score: 0.35
DE  Interaction: Q86UE6; IntAct: EBI-21507777; Score: 0.35
DE  Interaction: Q9UN75; IntAct: EBI-21537575; Score: 0.35
DE  Interaction: Q7KYR7; IntAct: EBI-21541130; Score: 0.35
DE  Interaction: Q2Y0W8; IntAct: EBI-21566582; Score: 0.35
DE  Interaction: Q9C099; IntAct: EBI-21571999; Score: 0.35
DE  Interaction: Q6UXE8; IntAct: EBI-21583647; Score: 0.35
DE  Interaction: Q9UN71; IntAct: EBI-21584146; Score: 0.35
DE  Interaction: O43291; IntAct: EBI-21587968; Score: 0.35
DE  Interaction: Q8TDD5; IntAct: EBI-21589012; Score: 0.35
DE  Interaction: Q8WW62; IntAct: EBI-21589315; Score: 0.35
DE  Interaction: P58658; IntAct: EBI-21588759; Score: 0.35
DE  Interaction: Q9BQ31; IntAct: EBI-21590203; Score: 0.35
DE  Interaction: Q96FT7; IntAct: EBI-21589962; Score: 0.35
DE  Interaction: Q9NRJ7; IntAct: EBI-21590428; Score: 0.35
DE  Interaction: Q96FV3; IntAct: EBI-21591007; Score: 0.35
DE  Interaction: Q9Y5M8; IntAct: EBI-21633655; Score: 0.35
DE  Interaction: Q9Y5F2; IntAct: EBI-21658599; Score: 0.35
DE  Interaction: Q16281; IntAct: EBI-21687526; Score: 0.35
DE  Interaction: Q8NAC3; IntAct: EBI-21687716; Score: 0.35
DE  Interaction: Q9Y5H8; IntAct: EBI-21695064; Score: 0.35
DE  Interaction: Q9Y5G8; IntAct: EBI-21697051; Score: 0.35
DE  Interaction: P14778; IntAct: EBI-21700570; Score: 0.35
DE  Interaction: P08754; IntAct: EBI-21709056; Score: 0.35
DE  Interaction: Q86XK7; IntAct: EBI-21739948; Score: 0.35
DE  Interaction: Q8IV01; IntAct: EBI-21748151; Score: 0.35
DE  Interaction: Q6P9F7; IntAct: EBI-21762226; Score: 0.35
DE  Interaction: P40967; IntAct: EBI-21773380; Score: 0.35
DE  Interaction: Q99675; IntAct: EBI-21775037; Score: 0.35
DE  Interaction: Q5T2D2; IntAct: EBI-21777947; Score: 0.35
DE  Interaction: Q8NAU1; IntAct: EBI-21799562; Score: 0.35
DE  Interaction: A5X5Y0; IntAct: EBI-21800698; Score: 0.35
DE  Interaction: O43521; IntAct: EBI-21803818; Score: 0.35
DE  Interaction: Q9NRM6; IntAct: EBI-21807235; Score: 0.35
DE  Interaction: Q16445; IntAct: EBI-21828581; Score: 0.35
DE  Interaction: O76096; IntAct: EBI-21835330; Score: 0.35
DE  Interaction: Q8TEQ8; IntAct: EBI-21840858; Score: 0.35
DE  Interaction: Q9Y5E4; IntAct: EBI-21877083; Score: 0.35
DE  Interaction: Q9Y227; IntAct: EBI-21891924; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-20937172; Score: 0.40
DE  Interaction: P0DTC5; IntAct: EBI-25685699; Score: 0.53
DE  Interaction: P37173; IntAct: EBI-25892533; Score: 0.56
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0031090;
GO  GO:0031095;
GO  GO:0016529;
GO  GO:0033017;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0015085;
GO  GO:0030899;
GO  GO:0008656;
GO  GO:0046872;
GO  GO:0005388;
GO  GO:0015662;
GO  GO:0044325;
GO  GO:0006919;
GO  GO:0070588;
GO  GO:0006816;
GO  GO:1903515;
GO  GO:0006874;
GO  GO:0070059;
GO  GO:0034220;
GO  GO:1900121;
GO  GO:1903779;
GO  GO:0150104;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MEAAHLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDLLVRILLLAALVSFVLAWFEE
SQ  GEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALKEYEPEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVP
SQ  ADLRLIEIKSTTLRVDQSILTGESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMA
SQ  AVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAVALAVAAIPEGLPAVITTCLA
SQ  LGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFVVAEADAGSCLLHEFTISGTTYTPEGEVRQGDQ
SQ  PVRCGQFDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLQALSRVERAGACNTVIKQLMR
SQ  KEFTLEFSRDRKSMSVYCTPTRPHPTGQGSKMFVKGAPESVIERCSSVRVGSRTAPLTPTSREQILAKIRDWGSGSDTLR
SQ  CLALATRDAPPRKEDMELDDCSKFVQYETDLTFVGCVGMLDPPRPEVAACITRCYQAGIRVVMITGDNKGTAVAICRRLG
SQ  IFGDTEDVAGKAYTGREFDDLSPEQQRQACRTARCFARVEPAHKSRIVENLQSFNEITAMTGDGVNDAPALKKAEIGIAM
SQ  GSGTAVAKSAAEMVLSDDNFASIVAAVEEGRAIYSNMKQFIRYLISSNVGEVVCIFLTAILGLPEALIPVQLLWVNLVTD
SQ  GLPATALGFNPPDLDIMEKLPRSPREALISGWLFFRYLAIGVYVGLATVAAATWWFVYDAEGPHINFYQLRNFLKCSEDN
SQ  PLFAGIDCEVFESRFPTTMALSVLVTIEMCNALNSVSENQSLLRMPPWMNPWLLVAVAMSMALHFLILLVPPLPLIFQVT
SQ  PLSGRQWVVVLQISLPVILLDEALKYLSRNHMHEEMSQK
//
ID  P54259;
PN  Atrophin-1;
GN  ATN1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm, perinuclear region. Cell junction {ECO:0000250|UniProtKB:P54258}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell- cell junctions and leading edges of cells (By similarity). Colocalizes with MTG8 in discrete nuclear dots. Proteolytic fragment F1 appears to remain in nucleus. Fragment F2 is exported into the cytoplasm. Fragment F2 from mutant sequences with longer poly-Gln (polyQ) tracts are additionally located to the cytoplasmic membrane and to certain organelles. {ECO:0000250}.
DR  UNIPROT: P54259;
DR  UNIPROT: Q99495;
DR  UNIPROT: Q99621;
DR  UNIPROT: Q9UEK7;
DR  Pfam: PF03154;
DR  OMIM: 125370;
DR  OMIM: 607462;
DR  OMIM: 618494;
DR  DisGeNET: 1822;
DE  Function: Transcriptional corepressor. Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation (By similarity). Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of poly-Gln (polyQ) repeats. {ECO:0000250|UniProtKB:O35126, ECO:0000269|PubMed:10085113, ECO:0000269|PubMed:10973986}.
DE  Disease: Dentatorubral-pallidoluysian atrophy (DRPLA) [MIM:125370]: Autosomal dominant neurodegenerative disorder characterized by a loss of neurons in the dentate nucleus, rubrum, glogus pallidus and Luys'body. Clinical features are myoclonus epilepsy, dementia, and cerebellar ataxia. Onset of the disease occurs usually in the second decade of life and death in the fourth. {ECO:0000269|PubMed:7842016, ECO:0000269|PubMed:8136840}. Note=The disease is caused by variants affecting the gene represented in this entry. Congenital hypotonia, epilepsy, developmental delay, and digital anomalies (CHEDDA) [MIM:618494]: An autosomal dominant neurodevelopmental syndrome characterized by severe global developmental delay, impaired intellectual development, poor or absent language, significant motor disability with inability to walk, dysmorphic facial features, skeletal anomalies, and variable congenital malformations. Most patients also have seizures and structural brain abnormalities. {ECO:0000269|PubMed:30827498}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-956422; Score: 0.00
DE  Interaction: P14335; IntAct: EBI-11422698; Score: 0.37
DE  Interaction: Q9UQB8; IntAct: EBI-6997364; Score: 0.63
DE  Interaction: Q06455; IntAct: EBI-955342; Score: 0.00
DE  Interaction: Q01844; IntAct: EBI-955350; Score: 0.00
DE  Interaction: Q96CN9; IntAct: EBI-955358; Score: 0.00
DE  Interaction: Q96PV6; IntAct: EBI-955366; Score: 0.00
DE  Interaction: Q99750; IntAct: EBI-955374; Score: 0.00
DE  Interaction: Q9BSW2; IntAct: EBI-955382; Score: 0.00
DE  Interaction: O43639; IntAct: EBI-955390; Score: 0.00
DE  Interaction: P61964; IntAct: EBI-8836498; Score: 0.74
DE  Interaction: O00308; IntAct: EBI-955406; Score: 0.00
DE  Interaction: Q9BQ66; IntAct: EBI-956398; Score: 0.00
DE  Interaction: Q9HAU0; IntAct: EBI-946360; Score: 0.51
DE  Interaction: P61289; IntAct: EBI-956430; Score: 0.00
DE  Interaction: Q93062; IntAct: EBI-956438; Score: 0.00
DE  Interaction: Q15654; IntAct: EBI-946367; Score: 0.51
DE  Interaction: Q9NWB1; IntAct: EBI-946549; Score: 0.51
DE  Interaction: O00468; IntAct: EBI-950710; Score: 0.00
DE  Interaction: P54259; IntAct: EBI-950716; Score: 0.00
DE  Interaction: P46379; IntAct: EBI-950722; Score: 0.00
DE  Interaction: Q02641; IntAct: EBI-950728; Score: 0.00
DE  Interaction: O43439; IntAct: EBI-950734; Score: 0.00
DE  Interaction: Q9HC77; IntAct: EBI-950740; Score: 0.00
DE  Interaction: Q9H2X0; IntAct: EBI-950746; Score: 0.00
DE  Interaction: P52943; IntAct: EBI-950752; Score: 0.00
DE  Interaction: O14641; IntAct: EBI-950758; Score: 0.00
DE  Interaction: Q12805; IntAct: EBI-950764; Score: 0.00
DE  Interaction: O95967; IntAct: EBI-950770; Score: 0.00
DE  Interaction: O75095; IntAct: EBI-950776; Score: 0.00
DE  Interaction: Q7Z7M0; IntAct: EBI-950782; Score: 0.00
DE  Interaction: P23142; IntAct: EBI-950794; Score: 0.00
DE  Interaction: Q5ZEY4; IntAct: EBI-950800; Score: 0.00
DE  Interaction: P28799; IntAct: EBI-950806; Score: 0.00
DE  Interaction: P98160; IntAct: EBI-950812; Score: 0.00
DE  Interaction: Q9Y219; IntAct: EBI-950818; Score: 0.00
DE  Interaction: O60290; IntAct: EBI-950824; Score: 0.00
DE  Interaction: Q14766; IntAct: EBI-950830; Score: 0.00
DE  Interaction: Q8N2S1; IntAct: EBI-950836; Score: 0.00
DE  Interaction: P02686; IntAct: EBI-950842; Score: 0.00
DE  Interaction: A6BM72; IntAct: EBI-950848; Score: 0.00
DE  Interaction: Q92832; IntAct: EBI-950854; Score: 0.00
DE  Interaction: Q99435; IntAct: EBI-950860; Score: 0.00
DE  Interaction: O75420; IntAct: EBI-950866; Score: 0.00
DE  Interaction: P17858; IntAct: EBI-950872; Score: 0.00
DE  Interaction: Q96PM5; IntAct: EBI-950878; Score: 0.00
DE  Interaction: O75093; IntAct: EBI-950884; Score: 0.00
DE  Interaction: Q6ZWJ1; IntAct: EBI-950890; Score: 0.00
DE  Interaction: Q86TM6; IntAct: EBI-950896; Score: 0.00
DE  Interaction: Q99973; IntAct: EBI-950902; Score: 0.00
DE  Interaction: Q9ULU4; IntAct: EBI-950914; Score: 0.00
DE  Interaction: P98175; IntAct: EBI-950926; Score: 0.00
DE  Interaction: Q9NP73; IntAct: EBI-950944; Score: 0.00
DE  Interaction: Q9UBX5; IntAct: EBI-950980; Score: 0.00
DE  Interaction: P98164; IntAct: EBI-951010; Score: 0.00
DE  Interaction: Q92824; IntAct: EBI-951040; Score: 0.00
DE  Interaction: P25788; IntAct: EBI-951046; Score: 0.00
DE  Interaction: Q9H0M0; IntAct: EBI-951064; Score: 0.00
DE  Interaction: Q08117; IntAct: EBI-951070; Score: 0.00
DE  Interaction: P61204; IntAct: EBI-951076; Score: 0.00
DE  Interaction: P48634; IntAct: EBI-951088; Score: 0.00
DE  Interaction: Q9H9J5; IntAct: EBI-951100; Score: 0.00
DE  Interaction: Q09013; IntAct: EBI-951106; Score: 0.00
DE  Interaction: Q16610; IntAct: EBI-951112; Score: 0.00
DE  Interaction: P98095; IntAct: EBI-951130; Score: 0.00
DE  Interaction: Q3KQU3; IntAct: EBI-951142; Score: 0.00
DE  Interaction: Q5JSZ5; IntAct: EBI-951148; Score: 0.00
DE  Interaction: A7E2V4; IntAct: EBI-951154; Score: 0.00
DE  Interaction: Q15323; IntAct: EBI-951160; Score: 0.00
DE  Interaction: Q92794; IntAct: EBI-951166; Score: 0.00
DE  Interaction: Q8WYB5; IntAct: EBI-951172; Score: 0.00
DE  Interaction: O43251; IntAct: EBI-951190; Score: 0.00
DE  Interaction: Q9P2R6; IntAct: EBI-951196; Score: 0.00
DE  Interaction: Q96EP0; IntAct: EBI-951202; Score: 0.00
DE  Interaction: Q8IUQ4; IntAct: EBI-3928819; Score: 0.55
DE  Interaction: O43255; IntAct: EBI-951214; Score: 0.00
DE  Interaction: Q96R06; IntAct: EBI-951220; Score: 0.00
DE  Interaction: Q9Y4B4; IntAct: EBI-951226; Score: 0.00
DE  Interaction: Q70EL1; IntAct: EBI-951232; Score: 0.00
DE  Interaction: O75081; IntAct: EBI-1190259; Score: 0.37
DE  Interaction: A0A6L8P747; IntAct: EBI-2817819; Score: 0.00
DE  Interaction: A0A6L7HHZ0; IntAct: EBI-2837958; Score: 0.00
DE  Interaction: A0A5P8YJG2; IntAct: EBI-2848559; Score: 0.00
DE  Interaction: A0A3N4BEU0; IntAct: EBI-2875462; Score: 0.00
DE  Interaction: A0A0H2W2I9; IntAct: EBI-2875448; Score: 0.00
DE  Interaction: A0A3N4AY03; IntAct: EBI-2875455; Score: 0.00
DE  Interaction: Q8ZA76; IntAct: EBI-2875469; Score: 0.00
DE  Interaction: P31016; IntAct: EBI-7968802; Score: 0.44
DE  Interaction: O75360; IntAct: EBI-9030447; Score: 0.37
DE  Interaction: Q14457; IntAct: EBI-14690094; Score: 0.35
DE  Interaction: Q9ULD9; IntAct: EBI-15637634; Score: 0.44
DE  Interaction: Q8WXX7; IntAct: EBI-16135059; Score: 0.35
DE  Interaction: P61417; IntAct: EBI-20817140; Score: 0.37
DE  Interaction: Q8ZG77; IntAct: EBI-20818229; Score: 0.37
DE  Interaction: P51114; IntAct: EBI-26509906; Score: 0.37
DE  Interaction: P51116; IntAct: EBI-26511575; Score: 0.37
DE  Interaction: Q9BYB0; IntAct: EBI-26513830; Score: 0.37
DE  Interaction: Q92574; IntAct: EBI-26515443; Score: 0.37
DE  Interaction: P10275; IntAct: EBI-26965611; Score: 0.27
DE  Interaction: P46934; IntAct: EBI-30832404; Score: 0.44
DE  Interaction: Q99816; IntAct: EBI-30839191; Score: 0.44
DE  Interaction: P46937; IntAct: EBI-30846537; Score: 0.44
DE  Interaction: O15178; IntAct: EBI-29014443; Score: 0.27
DE  Interaction: P55771; IntAct: EBI-29704799; Score: 0.27
DE  Interaction: Q8TDD2; IntAct: EBI-29740517; Score: 0.27
DE  Interaction: P31314; IntAct: EBI-29779038; Score: 0.27
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0016363;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0019904;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0001906;
GO  GO:0016477;
GO  GO:0007417;
GO  GO:0008340;
GO  GO:0030011;
GO  GO:0008584;
GO  GO:0035264;
GO  GO:0000122;
GO  GO:0051402;
GO  GO:0009791;
GO  GO:0032094;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEEASTPKVNKQGRSEEISESE
SQ  SEETNAPKKTKTEQELPRPQSPSDLDSLDGRSLNDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYH
SQ  PPPLFPPSPQPPDSTPRQPEASFEPHPSVTPTGYHAPMEPPTSRMFQAPPGAPPPHPQLYPGGTGGVLSGPPMGPKGGGA
SQ  ASSVGGPNGGKQHPPPTTPISVSSSGASGAPPTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLNNASASPPGL
SQ  GAQPLPGHLPSPHAMGQGMGGLPPGPEKGPTLAPSPHSLPPASSSAPAPPMRFPYSSSSSSSAAASSSSSSSSSSASPFP
SQ  ASQALPSYPHSFPPPTSLSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANSNAHPGPFPPSTGAQSTAHPPVSTHH
SQ  HHHQQQQQQQQQQQQQQQQQQQHHGNSGPPPPGAFPHPLEGGSSHHAHPYAMSPSLGSLRPYPPGPAHLPPPHSQVSYSQ
SQ  AGPNGPPVSSSSNSSSSTSQGSYPCSHPSPSQGPQGAPYPFPPVPTVTTSSATLSTVIATVASSPAGYKTASPPGPPPYG
SQ  KRAPSPGAYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASGPP
SQ  LSATQIKQEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLV
SQ  EKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDT
SQ  PALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPL
SQ  HGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLA
SQ  RLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFA
SQ  APYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL
//
ID  O35126;
PN  Atrophin-1;
GN  Atn1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P54258}. Cell junction {ECO:0000250|UniProtKB:P54258}. Nucleus {ECO:0000250|UniProtKB:P54258}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells. Colocalizes with MTG8 in discrete nuclear dots (By similarity). {ECO:0000250|UniProtKB:P54258}.
DR  UNIPROT: O35126;
DR  UNIPROT: P70200;
DR  UNIPROT: Q80YQ0;
DR  Pfam: PF03154;
DE  Function: Transcriptional corepressor. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of the poly-Q repeats (By similarity). Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation. {ECO:0000250|UniProtKB:P54259, ECO:0000269|PubMed:16702404, ECO:0000269|PubMed:19131340}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0031252;
GO  GO:0005737;
GO  GO:0016363;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0008432;
GO  GO:0019904;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0001906;
GO  GO:0016477;
GO  GO:0008340;
GO  GO:0030011;
GO  GO:0008584;
GO  GO:0035264;
GO  GO:0000122;
GO  GO:0051402;
GO  GO:0009791;
GO  GO:0045664;
GO  GO:0032094;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARIEEPSAPKASKQGRSEEISESE
SQ  SEETSAPKKTKTEQELPRPQSPSDLDSLDGRSINDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYH
SQ  PPPLFPPSPPPPDSTPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHPQLYPGNASGGVLSGPPMGPKGG
SQ  AAASSVGAPSGGKQHPPPTTPIPISSSGASGAPPAKPPSAPVGGGSLPSAPPPASFPHVTPNLPPPPALRPLNNASASPP
SQ  GMGAQPIPGHLPSPHAMGQGMSGLPPGPEKGPTLAPSPHPLPPASSSAPGPPMRYPYSSSSSSAAASSSSSSSSASQYPA
SQ  SQALPSYPHSFPPPTSMSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANNNTHPGPFPPTGGQSTAHPAAPTHHHH
SQ  QQQPQQQHHHGNSGPPPPGAYPHPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPPHGQVSYNQAGPNGPPVSSSNSS
SQ  GSSSQASYSCSHPSSSQGPQGASYPFPPVPPVTTSSATLSTVIATVASSPAGYKTASPPGPPQYSKRAPSPGSYKTATPP
SQ  GYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTGPPLTATQIKQEPAEEYE
SQ  PPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEK
SQ  EREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVM
SQ  SPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHG
SQ  GLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHS
SQ  HIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMS
SQ  AAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL
//
ID  Q5IS70;
PN  Atrophin-1;
GN  ATN1;
OS  9598;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P54258}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P54258}. Cell junction {ECO:0000250|UniProtKB:P54258}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell- cell junctions and leading edges of cells. Colocalizes with MTG8 in discrete nuclear dots (By similarity). {ECO:0000250|UniProtKB:O35126, ECO:0000250|UniProtKB:P54258}.
DR  UNIPROT: Q5IS70;
DR  Pfam: PF03154;
DE  Function: Transcriptional corepressor. Corepressor of MTG8 transcriptional repression. Recruits NR2E1 to repress transcription. Has some intrinsic repression activity. Promotes vascular smooth cell (VSMC) migration and orientation (By similarity). {ECO:0000250|UniProtKB:O35126}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003714;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEEASTPKVNKQGRSEEISESE
SQ  SEETNAPKKTKTEELPRPQSPSDLDSLDGRSLNDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHP
SQ  PPLFPPSPQPPDSTPRQPEASFEPHPSVTPTGYHAPMEPPTSRMFQAPPGAPPPHPQLYPGGTGGVLSGPPMGPKGGGAA
SQ  SSVGGPNGGKQHPPPTTPISVSSSGASGAPPTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLNNASASPPGLG
SQ  AQPLPGHLPSPHAMGQGMGGLPPGPEKGPTLAPSPHSLPPASSSAPAPPMRFPYSSSSSSSAAASSSSSSSSSSASPFPA
SQ  SQALPSYPHSFPPPTSLSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANSNAHPGPFPPSTGAQSTAHPPVSTHHH
SQ  HHQQQQQQQQQQQQQQQQHHGNSGPPPPGAFPHPLEGGSSHHAHPYAMSPSLGSLRPYPPGPAHLPPPHSQVSYSQAGPN
SQ  GPPVSSSSNSSSSTSQGSYPCSHPSPSQGPQGAPYPFPPVPTVTTSSATLSTVIATVASSPAGYKTASPPGPPPYGKRAP
SQ  SPGAYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASGPPLSAT
SQ  QIKQEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVR
SQ  REAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALR
SQ  TLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVP
SQ  GPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQM
SQ  LNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYR
SQ  DLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL
//
ID  P54258;
PN  Atrophin-1;
GN  Atn1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:19131340}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19131340}. Cell junction {ECO:0000269|PubMed:19131340}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with MTG8 in discrete nuclear dots (By similarity). Colocalizes with FAT1 in the perinuclear area, at cell- cell junctions and leading edges of cells. {ECO:0000250|UniProtKB:O35126}.
DR  UNIPROT: P54258;
DR  Pfam: PF03154;
DE  Function: Transcriptional corepressor. Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity (By similarity). {ECO:0000250|UniProtKB:O35126}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6GMN2; IntAct: EBI-6997460; Score: 0.40
DE  Interaction: Q9BYV2; IntAct: EBI-21999534; Score: 0.35
GO  GO:0070161;
GO  GO:0031252;
GO  GO:0005737;
GO  GO:0016363;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0008432;
GO  GO:0019904;
GO  GO:0090729;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0001906;
GO  GO:0016477;
GO  GO:0008340;
GO  GO:0030011;
GO  GO:0008584;
GO  GO:0035264;
GO  GO:0045892;
GO  GO:0000122;
GO  GO:0051402;
GO  GO:0045893;
GO  GO:0009791;
GO  GO:0045664;
GO  GO:0032094;
GO  GO:0007283;
GO  GO:0009404;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEETSTPKANKQGRSEEISESE
SQ  SEETSAPKKTKTEELPRPQSPSDLDSLDGRSINDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHP
SQ  PPLFPPSPPPPDSIPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPPHPQLYPGSAGGGVLSGPPMGPKGGA
SQ  AASSVGPPSGGKQHPPPTTPIPISSSGASGAPPAKPPNTPVGAGNLPSAPPPATFPHVTPNLPPPPALRPLNNASASPPG
SQ  MGAQPIPGHLPSPHAMGQGMSGLPPGPEKGPTLAPSPHPLPPASSSAPGPPMRYPYSSCSSSSVAASSSSSAATSQYPAS
SQ  QTLPSYPHSFPPPTSMSVSNQPPKYTQPSLPSQAVWSQGPPPPPPPYGRLLPNNNTHPGPFPPTGGQSTAHPPAPAHHHH
SQ  QQQQQPQPQPQPQQHHHGNSGPPPPGAYPHPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPSHGQVSYSQAGPNGPP
SQ  VSSSSNSSGSSSQAAYSCSHPSSSQGPQGASYPFPPVPPITTSSATLSTVIATVASSPAGYKTASPPGPPQYSKRAPSPG
SQ  SYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTGPPLTATQIK
SQ  QEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREA
SQ  EQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLS
SQ  EYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPG
SQ  LDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNV
SQ  TPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLP
SQ  ASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL
//
ID  Q2TBW0;
PN  Ataxin-10;
GN  ATXN10;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q2TBW0;
DR  Pfam: PF09759;
DE  Function: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAPRPPPGRLSGVMMPAPIQDLEALRALTALFKEQRNRDTAPRTIFQRVLDILKKSSHAVELACRDPSQVEHLASSLQL
SQ  ITECFRCLRNACIECSVNQNSIRNLGTIGVAVDLILLFRELRVEQDSLLTAFRCGLQFLGNIASRNEDSQSVVWMHAFPE
SQ  LFLSCLNHPDRKIVAYSSMILFTSLNSERMKELEENLNIAIDVVEAHQKQPESEWPFLIITDHFLKSPELVKAMYAKMSN
SQ  QERVTLLDLMIAKIVGDEPLTKDDAPVFLSHAELIASTFVDQCKIVLKLTSEQHTDDEEALATIRLLDVLCEKTANTDLL
SQ  GYLQVFPGLLERVIDLLRLIHVAGNDSTNIFSACASIKADGDVSSVAEGFKSHLIRLIGNLCYKNKDNQDKVNELDGIPL
SQ  ILDSCGLDDSNPFLTQWVVYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKMGFEVEKRGDKLILKSTSDTPQL
//
ID  Q9UBB4;
PN  Ataxin-10;
GN  ATXN10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16498633}.
DR  UNIPROT: Q9UBB4;
DR  UNIPROT: A6NLC4;
DR  UNIPROT: B4DG05;
DR  UNIPROT: O14998;
DR  UNIPROT: O15009;
DR  UNIPROT: Q6I9X4;
DR  Pfam: PF09759;
DR  OMIM: 603516;
DR  OMIM: 611150;
DR  DisGeNET: 25814;
DE  Function: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}.
DE  Disease: Spinocerebellar ataxia 10 (SCA10) [MIM:603516]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA10 is an autosomal dominant cerebellar ataxia (ADCA). {ECO:0000269|PubMed:11017075}. Note=The disease is caused by variants affecting the gene represented in this entry. Note=Defects in ATXN1 may be a cause of nephronophthisis a chronic tubulo-interstitial nephropathy that leads to anemia, polyuria, polydipsia, isosthenuria and death in uremia. {ECO:0000269|PubMed:21565611}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q14693; IntAct: EBI-25917615; Score: 0.56
DE  Interaction: Q15049; IntAct: EBI-25917631; Score: 0.56
DE  Interaction: Q99IB8; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: O75365; IntAct: EBI-1060045; Score: 0.00
DE  Interaction: Q9Y5J5; IntAct: EBI-1060584; Score: 0.00
DE  Interaction: Q9BUV8; IntAct: EBI-1061278; Score: 0.00
DE  Interaction: P43360; IntAct: EBI-1067847; Score: 0.00
DE  Interaction: Q13418; IntAct: EBI-1068425; Score: 0.00
DE  Interaction: Q9Y6J8; IntAct: EBI-1071021; Score: 0.00
DE  Interaction: P35613; IntAct: EBI-1071495; Score: 0.00
DE  Interaction: Q9Y5V3; IntAct: EBI-1075883; Score: 0.00
DE  Interaction: Q92956; IntAct: EBI-1076016; Score: 0.00
DE  Interaction: Q99623; IntAct: EBI-1079000; Score: 0.00
DE  Interaction: Q9Y2Q3; IntAct: EBI-1079777; Score: 0.00
DE  Interaction: Q9P2S5; IntAct: EBI-1079870; Score: 0.00
DE  Interaction: O00422; IntAct: EBI-1083812; Score: 0.00
DE  Interaction: P48059; IntAct: EBI-5660392; Score: 0.00
DE  Interaction: P05919; IntAct: EBI-6175288; Score: 0.46
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-6870186; Score: 0.37
DE  Interaction: Q16666; IntAct: EBI-9995438; Score: 0.35
DE  Interaction: Q9Z1B5; IntAct: EBI-10996176; Score: 0.35
DE  Interaction: Q8BFY9; IntAct: EBI-11018381; Score: 0.35
DE  Interaction: P49459; IntAct: EBI-11040518; Score: 0.35
DE  Interaction: P83887; IntAct: EBI-11057297; Score: 0.35
DE  Interaction: Q9D1H7; IntAct: EBI-11064973; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-11105437; Score: 0.67
DE  Interaction: Q13751; IntAct: EBI-11135011; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-11139064; Score: 0.35
DE  Interaction: Q6ZU80; IntAct: EBI-11370150; Score: 0.27
DE  Interaction: Q96NL6; IntAct: EBI-11376636; Score: 0.27
DE  Interaction: O94986; IntAct: EBI-11381405; Score: 0.27
DE  Interaction: Q5TB80; IntAct: EBI-11385924; Score: 0.27
DE  Interaction: Q9HC77; IntAct: EBI-11397411; Score: 0.27
DE  Interaction: Q9WMX2; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P27105; IntAct: EBI-12452286; Score: 0.51
DE  Interaction: P03452; IntAct: EBI-12577294; Score: 0.35
DE  Interaction: P03485; IntAct: EBI-12577388; Score: 0.35
DE  Interaction: P06821; IntAct: EBI-12577493; Score: 0.35
DE  Interaction: P03468; IntAct: EBI-12577881; Score: 0.35
DE  Interaction: Q6DPW5; IntAct: EBI-12582145; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581941; Score: 0.35
DE  Interaction: C5E519; IntAct: EBI-12583021; Score: 0.35
DE  Interaction: C5E526; IntAct: EBI-12584981; Score: 0.35
DE  Interaction: C5E527; IntAct: EBI-12585279; Score: 0.35
DE  Interaction: Q20MH8; IntAct: EBI-12586007; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: F5HFG5; IntAct: EBI-14063444; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-16794405; Score: 0.42
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: P50406; IntAct: EBI-20809027; Score: 0.37
DE  Interaction: P35408; IntAct: EBI-20811409; Score: 0.37
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21132308; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21376713; Score: 0.00
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q969R5; IntAct: EBI-25480413; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: P19739; IntAct: EBI-25685423; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25773054; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-25917448; Score: 0.56
DE  Interaction: O75925; IntAct: EBI-25917565; Score: 0.56
DE  Interaction: Q9BZZ5; IntAct: EBI-25917557; Score: 0.56
DE  Interaction: Q9UNS2; IntAct: EBI-25917549; Score: 0.56
DE  Interaction: Q96E88; IntAct: EBI-25917541; Score: 0.56
DE  Interaction: Q13772; IntAct: EBI-25917531; Score: 0.56
DE  Interaction: Q9UNY5; IntAct: EBI-25917523; Score: 0.56
DE  Interaction: Q16611; IntAct: EBI-25917456; Score: 0.56
DE  Interaction: Q04724; IntAct: EBI-25917507; Score: 0.56
DE  Interaction: O14974; IntAct: EBI-25917499; Score: 0.56
DE  Interaction: P55198; IntAct: EBI-25917481; Score: 0.56
DE  Interaction: P61978; IntAct: EBI-25917473; Score: 0.56
DE  Interaction: P29017; IntAct: EBI-25917464; Score: 0.56
DE  Interaction: P08670; IntAct: EBI-25917515; Score: 0.56
DE  Interaction: Q12891; IntAct: EBI-25917573; Score: 0.56
DE  Interaction: Q6NX45; IntAct: EBI-25917763; Score: 0.56
DE  Interaction: Q7Z7K6; IntAct: EBI-25917755; Score: 0.56
DE  Interaction: Q8N6K7; IntAct: EBI-25917747; Score: 0.56
DE  Interaction: Q96KN4; IntAct: EBI-25917739; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-25917729; Score: 0.56
DE  Interaction: Q8IYU4; IntAct: EBI-25917719; Score: 0.56
DE  Interaction: Q71DI3; IntAct: EBI-25917711; Score: 0.56
DE  Interaction: Q8IUW3; IntAct: EBI-25917703; Score: 0.56
DE  Interaction: Q8WVJ9; IntAct: EBI-25917695; Score: 0.56
DE  Interaction: Q8NHS9; IntAct: EBI-25917687; Score: 0.56
DE  Interaction: Q9GZS3; IntAct: EBI-25917679; Score: 0.56
DE  Interaction: Q9H347; IntAct: EBI-25917671; Score: 0.56
DE  Interaction: Q9UHD9; IntAct: EBI-25917663; Score: 0.56
DE  Interaction: Q5T6S3; IntAct: EBI-25917655; Score: 0.56
DE  Interaction: Q9BR01; IntAct: EBI-25917647; Score: 0.56
DE  Interaction: Q9Y2L8; IntAct: EBI-25917639; Score: 0.56
DE  Interaction: Q14689; IntAct: EBI-25917623; Score: 0.56
DE  Interaction: Q9BVJ6; IntAct: EBI-25917607; Score: 0.56
DE  Interaction: O95391; IntAct: EBI-25917599; Score: 0.56
DE  Interaction: O94851; IntAct: EBI-25917591; Score: 0.56
DE  Interaction: Q9UJX2; IntAct: EBI-25917581; Score: 0.56
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q8NCE2; IntAct: EBI-27113554; Score: 0.35
DE  Interaction: P23771; IntAct: EBI-29000509; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005615;
GO  GO:0016020;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0060271;
GO  GO:0007399;
GO  GO:0031175;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAPRPPPARLSGVMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSSHAVELACRDPSQVENLASSLQL
SQ  ITECFRCLRNACIECSVNQNSIRNLDTIGVAVDLILLFRELRVEQESLLTAFRCGLQFLGNIASRNEDSQSIVWVHAFPE
SQ  LFLSCLNHPDKKIVAYSSMILFTSLNHERMKELEENLNIAIDVIDAYQKHPESEWPFLIITDLFLKSPELVQAMFPKLNN
SQ  QERVTLLDLMIAKITSDEPLTKDDIPVFLRHAELIASTFVDQCKTVLKLASEEPPDDEEALATIRLLDVLCEMTVNTELL
SQ  GYLQVFPGLLERVIDLLRVIHVAGKETTNIFSNCGCVRAEGDISNVANGFKSHLIRLIGNLCYKNKDNQDKVNELDGIPL
SQ  ILDNCNISDSNPFLTQWVIYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKVGFEVEKKGEKLILKSTRDTPKP
//
ID  Q4R4Y2;
PN  Ataxin-10;
GN  ATXN10;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q4R4Y2;
DR  Pfam: PF09759;
DE  Function: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAPRPPPARLSGIMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSSHAVELACRDPSQVENLASSLQL
SQ  ITECFRCLRNACIECSVNQNSIRNLDTIGVAVDLILLFRELRVEQEALLTAFRCGLQFLGNIASRNEDSQSIVWVHAFPE
SQ  LFLSCLNHPDKKIVAYSSMILFTSLNHERMKELEENLNIAIDVIDAYQKHPESEWPVLIITDLFLKSPELVQAMFPKLNN
SQ  QERVTLLDLMIAKITSDEPLTTDDIPVFLRHAELIASTFVDQCKTVLKLASEEPPDDEEALATIRLLDVLCEMTANTELL
SQ  GYLQVFPGLLERVIDLLRVIHVTGKETTNIFSNCGCVRAEGDISNVAEGFKSHLIRLIGNLCYKNKDNQDKVNELDGIPL
SQ  ILDNCNISDSNPFLTQWVIYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKVGFEVEKKGEKLILKSTRDTPKP
//
ID  P28658;
PN  Ataxin-10;
GN  Atxn10;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: P28658;
DR  UNIPROT: Q543S3;
DR  UNIPROT: Q99LP5;
DR  UNIPROT: Q9D1I1;
DR  Pfam: PF09759;
DE  Function: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8BP00; IntAct: EBI-4283417; Score: 0.50
DE  Interaction: Q8CG73; IntAct: EBI-4284701; Score: 0.35
DE  Interaction: Q83B01; IntAct: EBI-21287600; Score: 0.37
DE  Interaction: Q83A33; IntAct: EBI-21288114; Score: 0.37
DE  Interaction: Q83A11; IntAct: EBI-21288333; Score: 0.37
DE  Interaction: Q6P1J9; IntAct: EBI-20729673; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0060271;
GO  GO:0007399;
GO  GO:0031175;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAPRMPPSRLSGIMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSTHAVELACRDPSQVEHLASSLQL
SQ  ITECFRCLRNACIECSVNQNSIRNLDTIGVAVDLVLLFRELRVEQDSLLTAFRCGLQFLGNVASRNEESQSIVWVHAFPE
SQ  LFMSCLNHPDKKIVAYCSMILFTSLNAERMKDLEENLNIAINVIEAHQKHPASEWPFLIISDHFLKSPELVEAMYGKLSN
SQ  QERITLLDIVIAKLVGEEQLTKDDISIFVRHAELIANSFMDQCRNVLKLTSEPHTEDKEALVTIRLLDVLCEMTSNTELL
SQ  GYLQVFPGLMERVIDVLRVIHEVGKESTNIFSPSDSLKAEGDIEHMTEGFKSHLIRLIGNLCYKNKENQDKVNELDGIPL
SQ  ILDSSNIDDNNPFMMQWVVYAVRNLTEDNSQNQDVIAKMEEQGLADASLLKKMGFEIEKSGDKLILKSNNDIPPP
//
ID  Q5RE06;
PN  Ataxin-10;
GN  ATXN10;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q5RE06;
DR  Pfam: PF09759;
DE  Function: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAPRLPPARALSGVMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSSHAVELACRDPSQVENLASSLQ
SQ  LITECFRCLRNACIECSVNQNSIRNLDAIGVAVDLILLFRELRVEQESLLTAFRCGLQFLGNIASRNEDSQSIVWVHAFP
SQ  ELFLSCLNHPDKKIVAYSSMILFTSLNHERMKELEENLNIAIDVIDAYQKHPESEWPFLIITDLFLKSPELVQAMFPKLN
SQ  NQERVTLLDLMIAKITSDEPLTKDDIPVFLRHAELIASTFVDQCKTVLKLASEEPPDDEEALATIRLLDVLCEMTVNTEL
SQ  LGYLQVFPGLLERVIDLLRVIHVAGKETTNIFSNCGCVRAEGDISNVAEGFKSHLIRLIGNLCYKNKDNQDKVNELDGIP
SQ  LILDNCNISDSNPFLTQWVIYAIRNLTEDNSQNQDLIAKMEEQGLADASLLKKVGFEVEKKGEKLILKSTRDTPKP
//
ID  Q9ER24;
PN  Ataxin-10;
GN  Atxn10;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15201271}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q9ER24;
DR  Pfam: PF09759;
DE  Function: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000269|PubMed:15201271, ECO:0000269|PubMed:16498633, ECO:0000269|PubMed:16714295}.
DE  Reference Proteome: Yes;
DE  Interaction: Q969Q1; IntAct: EBI-21997483; Score: 0.35
DE  Interaction: P35968; IntAct: EBI-22252817; Score: 0.35
DE  Interaction: Q92835; IntAct: EBI-22260778; Score: 0.35
DE  Interaction: P42681; IntAct: EBI-22265546; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0060271;
GO  GO:0007399;
GO  GO:0031175;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAPRMPPSRLSGIMVPAPIQDLEALRALTALFKEQRNRETAPRTIFQRVLDILKKSTQAVELACRDPSQVEHLASSLQL
SQ  ITECFRCLRNACIECSVNQNSIRNLDTIGVAVDLVLLFRELRVEQDSLLTAFRCGLQFLGNVASRNEDSQSIVWVHAFPE
SQ  LFMSCLNHPDKKIVAYCSMILFTSLNSERMKDLEENLNIAINVIEAHQKHPESEWPFLIITDHFLKSPELVEAMYGKLSN
SQ  QERVTLLDIMIAKIVGDEQLTKDDISIFLRHAELIANSFVDQCRNVLKLTSEPQTEDKEALVTIRLLDVLCEMTSNTELL
SQ  GYLQVFPGLMERVIDVLRVIHSVGKDSTNIFSPSDSLKAEGDIEHMTEGFKSHLIRLIGNLCYKNKENQDKVNELDGIPL
SQ  ILDSSNIDDNNPFMMQWVVYAVRNLTEDNSQNQDFIAKMEEQGLADASLLKKMGFEVEKSGDKLILKSNNDIPPP
//
ID  Q5FVB0;
PN  Ataxin-10;
GN  atxn10;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q5FVB0;
DR  Pfam: PF09759;
DE  Function: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0031175;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAPVERLAGVCAELEQWLGEESGQRNDWAEGEGIVWRLSELFREAQYRELAEPRIFRLILQILSRVSCEIKVATLPAGA
SQ  FTDTHCQLPAECFRCLRNACVQCASNQDSVRNVGLIEESVRLIQIFGAPHVLQEPALVAFRCGLQFLGNTAAGNRDSQNA
SQ  VWACAFPDLFLSCLVHDDEKVVTYSSMVLFTCINREKVSTLQDPSKLDVALSVVTAYSKYPDAEWMYLIVMDHFLLCPDL
SQ  VKAVYLSQSSPERVTLLELILGKISQKEPLSAEESEALQAIAAFLSDCFQTQCKTILKLTSPSACDEEEPIVVTRLLDIL
SQ  CEVTSKNEHLSCLQTCPGLLEAAVDILRLTHLAGKQSMNVFTAAHTMSMGQDLTHAAVGFKAHLIRLIGNLCYQNKENQE
SQ  KVYQLDGIALILDNCSIDDNNPFLNQWAVFAIRNLTENNDKNQELIASMERQGLADSSLLKSMGLQAEERDGKLLLKSVK
SQ  KSPAL
//
ID  Q9C5X4;
PN  Histone H3-lysine(4) N-trimethyltransferase ATX1;
GN  ATX1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Nucleus {ECO:0000269|PubMed:16585509, ECO:0000269|PubMed:17881378}. Cytoplasm {ECO:0000269|PubMed:16585509}. Note=Shifts from nucleus to cytoplasm as PIP5 levels increase. When in the nucleus, associated with chromatin. When cytoplasmic, mostly localized along the plasma membrane, associated with PIP5. {ECO:0000269|PubMed:16585509}. [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:21245040}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21245040}.
DR  UNIPROT: Q9C5X4;
DR  UNIPROT: Q84WP4;
DR  UNIPROT: Q9SIP3;
DR  Pfam: PF05965;
DR  Pfam: PF05964;
DR  Pfam: PF09465;
DR  Pfam: PF00855;
DR  Pfam: PF00856;
DR  PROSITE: PS51805;
DR  PROSITE: PS51543;
DR  PROSITE: PS51542;
DR  PROSITE: PS50868;
DR  PROSITE: PS50812;
DR  PROSITE: PS50280;
DR  PROSITE: PS50081;
DR  PROSITE: PS01359;
DR  PROSITE: PS50016;
DE  Function: [Isoform 1]: Binds to the promoter and regulates the transcription of target genes, maintaining them in an active state; at promoters, required for TATA binding proteins (TBPs, e.g. TBP1 and TBP2) and RNA polymerase II (Pol II) recruitment, and, in a subsequent event, is recruited by a phosphorylated form of Pol II to the +300-bp region of transcribed sequences to trimethylates nucleosomes (PubMed:21266657, PubMed:23284292). Histone trimethyltransferase that trimethylates 'Lys-4' of histone H3 (H3K4me3); H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation and is required for efficient elongation of transcription but not for transcription initiation (PubMed:17965588, PubMed:17881378, PubMed:18375658, PubMed:23284292). Methylates only a limited fraction of nucleosomes of target genes (e.g. FLC, NAP, XTH33 and WRKY70) (PubMed:18375658). Necessary for WDR5A occupancy at WRKY70 and LTP7 genes (PubMed:23284292). Required to maintain the active state of class A (AP1 and AP2), class B (PI and AP3) and class C (AG, AGAMOUS) floral homeotic genes at early stages of flower development (PubMed:17881378). Together with CLF, modulates AG nucleosome methylation statement (PubMed:17881378). Involved in epigenetic regulation (e.g. H3K4me3) of the floral repressors FLC, FT and SOC1 to prevent the transition from vegetative to reproductive development, independently of the photoperiod; binds the active FLC locus before flowering, but this interaction is released upon the transition to flowering (PubMed:18375656, PubMed:24102415, PubMed:30150325). Regulates floral organ identity and flowering transition. Functions as a receptor for the lipid messenger phosphatidylinositol 5-phosphate (PI5P), which regulates negatively its transcriptional activation activity. Exhibits histone methylase activity and subsequent transcriptional regulation on WRKY70 gene, and, to a lower extent on secondary defense-response targets salicylic acid (SA)-responsive gene PR1 and jasmonic acid (JA)- responsive gene THI2.1 (PubMed:17965588). Involved in response to dehydration stress-response in both abscisic acid (ABA)-dependent and ABA-independent pathways; this includes specific genes (e.g. COR15A, ADH1, CBF4, RD29A, RD29B, RD26, ABF3, NCED3 and ABA3) epigenetic regulation (e.g. H3K4me3 and Pol II recruitment) to promotes their transcription and influence ABA production (PubMed:19901554, PubMed:21309869). Implicated in stomatal closure regulation (PubMed:21309869). Indirect repressor of XTH genes (XTH33) (PubMed:19154201). Necessary for the phosphorylation of Pol II NRPB1 (e.g. Ser5P and Ser2P) at the promoters of target genes, thus regulating both early and late stages of transcription (PubMed:21266657). Controls root growth and architecture by regulating the timing of root development, stem cell niche maintenance (e.g. quiescent center (QC)), and cell patterning during primary and lateral root development (PubMed:25205583). Modulates cell cycle duration, cell production, and the transition from cell proliferation in the root apical meristem (RAM) to cell elongation (PubMed:25205583). {ECO:0000269|PubMed:12699618, ECO:0000269|PubMed:16585509, ECO:0000269|PubMed:17881378, ECO:0000269|PubMed:17965588, ECO:0000269|PubMed:18375656, ECO:0000269|PubMed:18375658, ECO:0000269|PubMed:19154201, ECO:0000269|PubMed:19901554, ECO:0000269|PubMed:21266657, ECO:0000269|PubMed:21309869, ECO:0000269|PubMed:23284292, ECO:0000269|PubMed:24102415, ECO:0000269|PubMed:25205583, ECO:0000269|PubMed:30150325}. [Isoform 3]: Trimethylates A4/EF1A post-translationally at Lys-396 (PubMed:21245040). Required for actin cytoskeleton organization (PubMed:21245040). {ECO:0000269|PubMed:21245040}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0048188;
GO  GO:0003682;
GO  GO:0018024;
GO  GO:0046872;
GO  GO:0010314;
GO  GO:0008276;
GO  GO:0000976;
GO  GO:0009738;
GO  GO:0030036;
GO  GO:0051568;
GO  GO:0080182;
GO  GO:0009910;
GO  GO:0018022;
GO  GO:1904961;
GO  GO:0006355;
GO  GO:0009909;
GO  GO:0040029;
GO  GO:2000023;
GO  GO:2000280;
GO  GO:2000067;
GO  GO:0090333;
GO  GO:0006357;
GO  GO:0009414;
GO  GO:0010093;
GO  GO:0010228;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MACFSNETQIEIDVHDLVEAPIRYDSIESIYSIPSSALCCVNAVGSHSLMSKKVKAQKLPMIEQFEIEGSGVSASDDCCR
SQ  SDDYKLRIQRPEIVRVYYRRRKRPLRECLLDQAVAVKTESVELDEIDCFEEKKRRKIGNCELVKSGMESIGLRRCKENNA
SQ  FSGNKQNGSSRRKGSSSKNQDKATLASRSAKKWVRLSYDGVDPTSFIGLQCKVFWPLDALWYEGSIVGYSAERKRYTVKY
SQ  RDGCDEDIVFDREMIKFLVSREEMELLHLKFCTSNVTVDGRDYDEMVVLAATLDECQDFEPGDIVWAKLAGHAMWPAVIV
SQ  DESIIGERKGLNNKVSGGGSLLVQFFGTHDFARIKVKQAISFIKGLLSPSHLKCKQPRFEEGMQEAKMYLKAHRLPERMS
SQ  QLQKGADSVDSDMANSTEEGNSGGDLLNDGEVWLRPTEHVDFRHIIGDLLIINLGKVVTDSQFFKDENHIWPEGYTAMRK
SQ  FTSLTDHSASALYKMEVLRDAETKTHPLFIVTADSGEQFKGPTPSACWNKIYNRIKKVQNSDSPNILGEELNGSGTDMFG
SQ  LSNPEVIKLVQDLSKSRPSSHVSMCKNSLGRHQNQPTGYRPVRVDWKDLDKCNVCHMDEEYENNLFLQCDKCRMMVHAKC
SQ  YGELEPCDGALWLCNLCRPGAPDMPPRCCLCPVVGGAMKPTTDGRWAHLACAIWIPETCLSDVKKMEPIDGVNKVSKDRW
SQ  KLMCTICGVSYGACIQCSNNSCRVAYHPLCARAAGLCVELENDMSVEGEEADQCIRMLSFCKRHRQTSTACLGSEDRIKS
SQ  ATHKTSEYLPPPNPSGCARTEPYNCFGRRGRKEPEALAAASSKRLFVENQPYVIGGYSRLEFSTYKSIHGSKVSQMNTPS
SQ  NILSMAEKYRYMRETYRKRLAFGKSGIHGFGIFAKLPHRAGDMMIEYTGELVRPSIADKREQLIYNSMVGAGTYMFRIDD
SQ  ERVIDATRTGSIAHLINHSCVPNCYSRVITVNGDEHIIIFAKRHIPKWEELTYDYRFFSIGERLSCSCGFPGCRGVVNDT
SQ  EAEEQHAKICVPRCDLIDWTAE
//
ID  Q9M077;
PN  Serine/threonine-protein kinase Aurora-1;
GN  AUR1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, phragmoplast. Note=Nuclear membrane in interphase cells, spindle poles at prophase, mitotic spindle from metaphase to telophase and equatorial cell plate at telophase.
DR  UNIPROT: Q9M077;
DR  UNIPROT: Q8LBX4;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Phosphorylates specifically 'Ser-10' of histone H3 in vitro and colocalizes with phosphorylated histone H3 during mitosis. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle. Colocalizes also with gamma-tubulin and function in microtubule organizing centers (MTOCs). In contrast with the mammalian B-type Aurora, AUR1 has no kinase activity toward 'Ser-28' of histone H3. {ECO:0000269|PubMed:15722465, ECO:0000269|PubMed:16028112, ECO:0000269|PubMed:22150830}.
DE  Reference Proteome: Yes;
GO  GO:0009504;
GO  GO:0032133;
GO  GO:0005874;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0009524;
GO  GO:0005819;
GO  GO:0005876;
GO  GO:0051233;
GO  GO:0000922;
GO  GO:0005524;
GO  GO:0035175;
GO  GO:0035174;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0051301;
GO  GO:0007052;
GO  GO:0006468;
GO  GO:0032465;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAIPTETQHQEKEASDASAAAAQKRWTLSDFDIGKPLGRGKFGHVYLAREKRSNHVVALKVLFKSQLQQSQVEHQLRREV
SQ  EIQSHLRHPNILRLYGYFYDQKRVYLILEYAARGELYKDLQKCKYFSERRAATYVASLARALIYCHGKHVIHRDIKPENL
SQ  LIGAQGELKIADFGWSVHTFNRRRTMCGTLDYLPPEMVESVEHDASVDIWSLGILCYEFLYGVPPFEAMEHSDTYRRIVQ
SQ  VDLKFPPKPIISASAKDLISQMLVKESSQRLPLHKLLEHPWIVQNADPSGIYRV
//
ID  Q683C9;
PN  Serine/threonine-protein kinase Aurora-2;
GN  AUR2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Nuclear membrane in interphase cells, spindle poles at prophase and mitotic spindle from metaphase to telophase.
DR  UNIPROT: Q683C9;
DR  UNIPROT: O82309;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Phosphorylates specifically 'Ser-10' of histone H3 in vitro. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle. Might colocalize with gamma-tubulin and function in microtubule organizing centers (MTOCs). {ECO:0000269|PubMed:16028112}.
DE  Reference Proteome: Yes;
DE  Interaction: O23160; IntAct: EBI-25517190; Score: 0.56
DE  Interaction: Q9SSA8; IntAct: EBI-25519383; Score: 0.56
GO  GO:0032133;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005876;
GO  GO:0051233;
GO  GO:0000922;
GO  GO:0005524;
GO  GO:0035175;
GO  GO:0035174;
GO  GO:0106310;
GO  GO:0007052;
GO  GO:0006468;
GO  GO:0032465;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLYQAASEAAQKRWTTSDFDIGKPLGRGKFGHVYLAREKRSDHIVALKVLFKAQLQQSQVEHQLRREVEIQSHLRHPNIL
SQ  RLYGYFYDQKRVYLILEYAVRGELYKELQKCKYFSERRAATYVASLARALIYCHGKHVIHRDIKPENLLIGAQGELKIAD
SQ  FGWSVHTFNRRRTMCGTLDYLPPEMVESVEHDASVDIWSLGILCYEFLYGVPPFEAREHSETYKRIVQVDLKFPPKPIVS
SQ  SSAKDLISQMLVKESTQRLALHKLLEHPWIVQNADPSGLYRG
//
ID  O64629;
PN  Serine/threonine-protein kinase Aurora-3;
GN  AUR3;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus. Chromosome. Chromosome, centromere. Note=Cytoplasmic perinuclear region or in dots around the nucleolus and at the nuclear periphery in interphase cells, associated to centromeric regions of condensed chromosomes at metaphase and dispersed along the entire length of the chromosomes during anaphase (PubMed:16028112). Nucleus (PubMed:15722465). {ECO:0000269|PubMed:15722465, ECO:0000269|PubMed:16028112}.
DR  UNIPROT: O64629;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Phosphorylates in vitro histone H3 at 'Ser-10' (H3S10ph) and 'Ser-28' (H3S28ph), but not at 'Thr-3' (H3T3ph) or 'Thr-11' (H3T11ph). Colocalizes with phosphorylated histone H3 during mitosis. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle. {ECO:0000269|PubMed:16028112, ECO:0000269|PubMed:17087760}.
DE  Reference Proteome: Yes;
GO  GO:0032133;
GO  GO:0000775;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0005876;
GO  GO:0051233;
GO  GO:0005524;
GO  GO:0035175;
GO  GO:0044022;
GO  GO:0035174;
GO  GO:0106310;
GO  GO:0007059;
GO  GO:0007052;
GO  GO:0016310;
GO  GO:0006468;
GO  GO:0032465;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKKSTESDAGNTEKQWSLADFEIGRPLGKGKFGRVYLAREAKSKYIVALKVIFKEQIEKYKIHHQLRREMEIQTSLRHP
SQ  NILRLFGWFHDNERIFLILEYAHGGELYGVLKQNGHLTEQQAATYIASLSQALAYCHGKCVIHRDIKPENLLLDHEGRLK
SQ  IADFGWSVQSSNKRKTMCGTLDYLAPEMVENRDHDYAVDNWTLGILCYEFLYGNPPFEAESQKDTFKRILKIDLSFPLTP
SQ  NVSEEAKNLISQLLVKDPSKRLSIEKIMQHPWIVKNADPKGVCASIDI
//
ID  P14975;
PN  Protein AV2;
GN  AV2;
OS  10818;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: P14975;
DR  Pfam: PF01524;
DR  Pfam: PF03716;
DE  Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0019048;
GO  GO:0060967;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWDPLVNEFPDSVHGLRCMLAIKYLQALEDTYEPSTLGHELVRDLVSVIRARNYVEATRRYHHFHSRIQGSSKTELRQPI
SQ  QEPCYCPHCPRHKSKTGLGEQAHVQKAHDVQDV
//
ID  P14967;
PN  Uncharacterized 13.1 kDa protein;
GN  AV2;
OS  222073;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: P14967;
DR  Pfam: PF01524;
DR  Pfam: PF03716;
DE  Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0019048;
GO  GO:0060967;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWDPLVNEFPDSVHGLRCMLAIKYLQALEDTYEPSTLGHDLVRDLISVIRARNYVEATRRYHHFHSRLEGSSKAELRQPI
SQ  QEPCYCPHCPRHKSKTGLDEQAHVQKAHDVQDV
//
ID  Q08593;
PN  Protein AV2;
GN  AV2;
OS  31600;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: Q08593;
DR  Pfam: PF01524;
DR  Pfam: PF03716;
DE  Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0019048;
GO  GO:0060967;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWDPLLNEFPESVHGFRCMLAVKYLQLVECTYSPDTLGYDLIRDLFSVIRAKNYVEATSRYHNFYSRLEGSSPSELRQPI
SQ  QQPCGCPYCPRHKKTILDKQTHQSEAQVVSDV
//
ID  Q9YPS6;
PN  Protein AV2;
GN  AV2;
OS  223295;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9YPS6;
DR  Pfam: PF01524;
DE  Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0019048;
GO  GO:0060967;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWDPLVNDFPKSLHGFRCMLAIKYLQYIQENYPSNSLGFVYLTELIQVLRIRKHAKAELRYRLLYPDVECAEEADLRHPA
SQ  FLTCHCGKCPCQREKEEVDQPTHVEETEILSVIPLS
//
ID  P36282;
PN  Protein V2;
GN  V2;
OS  223353;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: P36282;
DR  Pfam: PF01524;
DR  Pfam: PF03716;
DE  Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0019048;
GO  GO:0060967;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWDPLVHEFPETVHGFRCMLANKYLLAVESKYAPDTLGYELIRDCIGVVRSRNYEQATSRYRDIYTRLQGATEAELQQSV
SQ  QERCCCPHCPRHKKADMGESAHVQKAHDVQAVQKP
//
ID  P61512;
PN  Protein V2;
GN  V2;
OS  37139;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: P61512;
DR  UNIPROT: P27270;
DR  Pfam: PF01524;
DR  Pfam: PF03716;
DE  Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0019048;
GO  GO:0060967;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWDPLLNEFPDSVHGLRCMLAIKYLQLVEETYEPNTLGHDLIRDLISVIRARDYAEANRRYTNFNARLEGSSKTELRQPV
SQ  YQPCCCPHCPRHQASIMDLQAHVSKAADVQNVQKP
//
ID  Q67616;
PN  Protein V2;
GN  V2;
OS  221538;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: Q67616;
DR  Pfam: PF01524;
DR  Pfam: PF03716;
DE  Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0019048;
GO  GO:0060967;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWDPLLNEFPDSVHGLRCMLAIKYLQLVEETYEPNTLGHDLIRDLISVIRARDYAEANRRYTNVKPALEVSSKTELRQPV
SQ  YQPCCCPHCPRHQASIMDLQAHVSKAADVQNVQKP
//
ID  P61511;
PN  Protein V2;
GN  V2;
OS  123735;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: P61511;
DR  UNIPROT: P27270;
DR  Pfam: PF01524;
DR  Pfam: PF03716;
DE  Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0019048;
GO  GO:0060967;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWDPLLNEFPDSVHGLRCMLAIKYLQLVEETYEPNTLGHDLIRDLISVIRARDYAEANRRYTNFNARLEGSSKTELRQPV
SQ  YQPCCCPHCPRHQASIMDLQAHVSKAADVQNVQKP
//
ID  Q9DXE9;
PN  Protein V2;
GN  V2;
OS  185793;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9DXE9;
DR  Pfam: PF01524;
DR  Pfam: PF03716;
DE  Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0019048;
GO  GO:0060967;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWDPLLNEFPETVHGFRCMLAIKYLQLVENTYSPDTLGYDLIRDLISVIRARDYGETSRRYCHFHSRLEGASPAELRQPL
SQ  YGSCCCPHCPRHQKTNVVKQAHVPEAHDVPDVQKP
//
ID  P27269;
PN  Protein V2;
GN  V2;
OS  66366;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:11878881, ECO:0000269|PubMed:16979684}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery.
DR  UNIPROT: P27269;
DR  Pfam: PF01524;
DR  Pfam: PF03716;
DE  Function: Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000269|PubMed:16979684, ECO:0000269|PubMed:18165314}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0019048;
GO  GO:0060967;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWDPLLNEFPESVHGFRCMLAIKYLQSVEETYEPNTLGHDLIRDLISVVRARDYVEATRRYNHFHARLEGSPKAELRQPI
SQ  QQPCCCPHCPRHKQATIMDVQAHVPKAQNIQNVSKP
//
ID  Q96A70;
PN  Antizyme inhibitor 2;
GN  AZIN2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region. Membrane {ECO:0000250}. Cytoplasmic vesicle. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000250}. Golgi apparatus, trans-Golgi network. Cytoplasmic granule. Cell projection, axon. Cell projection, dendrite. Perikaryon. Note=Colocalizes with KDEL receptors in ER-Golgi intermediate compartment (ERGIC). Translocates from the ERGIC structure to the cytoplasm in an antizyme-dependent manner. Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules (By similarity). Detected as vesicle-like pattern in neurite outgrowths. Localizes to the vesicular compartments of the secretory pathway, predominantly in the trans-Golgi network (TGN). Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. {ECO:0000250}.
DR  UNIPROT: Q96A70;
DR  UNIPROT: B2RDU5;
DR  UNIPROT: D3DPQ9;
DR  UNIPROT: Q5TIF4;
DR  UNIPROT: Q5TIF5;
DR  UNIPROT: Q5TIF6;
DR  UNIPROT: Q8TF56;
DR  UNIPROT: Q96L54;
DR  UNIPROT: Q96L55;
DR  UNIPROT: Q96L56;
DR  UNIPROT: Q96L57;
DR  UNIPROT: Q96MD9;
DR  Pfam: PF02784;
DR  Pfam: PF00278;
DR  PROSITE: PS00878;
DR  PROSITE: PS00879;
DR  OMIM: 608353;
DR  DisGeNET: 113451;
DE  Function: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding (PubMed:17900240). Inhibits antizyme- dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production (PubMed:17900240). Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking (PubMed:20188728). {ECO:0000269|PubMed:17900240, ECO:0000269|PubMed:20188728}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UMX2; IntAct: EBI-10281607; Score: 0.56
DE  Interaction: Q9NZC9; IntAct: EBI-21811703; Score: 0.35
DE  Interaction: Q96FC9; IntAct: EBI-21811703; Score: 0.35
DE  Interaction: Q8ND04; IntAct: EBI-21811703; Score: 0.35
DE  Interaction: Q5T3J3; IntAct: EBI-21811703; Score: 0.35
DE  Interaction: Q16890; IntAct: EBI-21811703; Score: 0.35
DE  Interaction: P78395; IntAct: EBI-21811703; Score: 0.35
DE  Interaction: P57737; IntAct: EBI-21811703; Score: 0.35
DE  Interaction: P54368; IntAct: EBI-21811703; Score: 0.35
DE  Interaction: O95190; IntAct: EBI-21811703; Score: 0.35
GO  GO:0030424;
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0033116;
GO  GO:1990005;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005802;
GO  GO:0030133;
GO  GO:0008792;
GO  GO:0042978;
GO  GO:0097055;
GO  GO:0042177;
GO  GO:0043085;
GO  GO:1902269;
GO  GO:0033387;
GO  GO:0007283;
GO  GO:0098629;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGYLSESDFVMVEEGFSTRDLLKELTLGASQATTDEVAAFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKV
SQ  LAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDD
SQ  SHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFP
SQ  GTEGAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQPGREEENGSTSKTIVYHLD
SQ  EGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWG
SQ  TQACHITYAMSRVAWEALRRQLMAAEQEDDVEGVCKPLSCGWEITDTLCVGPVFTPASIM
//
ID  Q8BVM4;
PN  Antizyme inhibitor 2;
GN  Azin2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Membrane. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment. Golgi apparatus, cis-Golgi network. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic granule. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Perikaryon {ECO:0000250}. Note=Detected as vesicle-like pattern in neurite outgrowths. Localizes to the vesicular compartments of the secretory pathway, predominantly in the trans-Golgi network (TGN). Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules (By similarity). Colocalizes with KDEL receptors in ER-Golgi intermediate compartment (ERGIC). Translocates from the ERGIC structure to the cytoplasm in a antizyme- dependent manner. Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin- containing secretory granules. {ECO:0000250}.
DR  UNIPROT: Q8BVM4;
DR  UNIPROT: A2A823;
DR  Pfam: PF02784;
DR  Pfam: PF00278;
DR  PROSITE: PS00879;
DE  Function: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding (PubMed:18062773, PubMed:18508777, PubMed:18973822). Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production (PubMed:16916800, PubMed:24967154). Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking (By similarity). {ECO:0000250|UniProtKB:Q96A70, ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18508777, ECO:0000269|PubMed:18973822, ECO:0000269|PubMed:24967154}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9R109; IntAct: EBI-9656867; Score: 0.59
DE  Interaction: P54369; IntAct: EBI-9660716; Score: 0.40
DE  Interaction: O08608; IntAct: EBI-9660680; Score: 0.40
GO  GO:0030424;
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0033116;
GO  GO:1990005;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005802;
GO  GO:0030133;
GO  GO:0003824;
GO  GO:0042978;
GO  GO:0042177;
GO  GO:0006591;
GO  GO:0043085;
GO  GO:1902269;
GO  GO:0033387;
GO  GO:0098629;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGYLSESDFVMVEEGFSTRDLLEELTLGASQATSGKVAAFFVADLGAVVRKHFCFLKHLPRVRPFYAVGCNSSLGVLKV
SQ  LAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQVAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKMVLCIATQD
SQ  SHSLNHLSLRFGASLKSCRHLLENAKKSHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFQMGEELGHTMNILDLGGGFP
SQ  GLEGAKVRFEEMASVINSALDLYFPEGCGVDILAELGRYYVTSAFTVAVSIVAKREVLDQASREEQTGAAPKSIVYYLDE
SQ  GVYGVFNSVLFDNTCPTPALQKKPSADQPLYSSSLWGPAVEGCDCVAEGLWLPQLQVGDWLVFDNMGAYTVDTKSLLGGT
SQ  QARRVTYAMSRLAWEALRGQLLPAEEDQDAEGVCKPLSCGWEITDTLCVGPVFTPASIM
//
ID  D4A693;
PN  Antizyme inhibitor 2;
GN  Azin2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:19718454}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000250}. Golgi apparatus, trans- Golgi network {ECO:0000250}. Cytoplasmic granule {ECO:0000269|PubMed:19718454}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Perikaryon {ECO:0000250}. Note=Colocalizes with KDEL receptors in ER-Golgi intermediate compartment (ERGIC). Translocates from the ERGIC structure to the cytoplasm in a antizyme-dependent manner. Localizes with vesicle- associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. Detected as vesicle-like pattern in neurite outgrowths. Localizes to the vesicular compartments of the secretory pathway, predominantly in the trans-Golgi network (TGN) (By similarity). Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. {ECO:0000250}.
DR  UNIPROT: D4A693;
DR  Pfam: PF02784;
DR  Pfam: PF00278;
DR  PROSITE: PS00879;
DE  Function: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding. Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production. Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking. {ECO:0000250|UniProtKB:Q8BVM4, ECO:0000250|UniProtKB:Q96A70}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0030425;
GO  GO:0033116;
GO  GO:1990005;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005802;
GO  GO:0030133;
GO  GO:0003824;
GO  GO:0042978;
GO  GO:0042177;
GO  GO:0006591;
GO  GO:0043085;
GO  GO:1902269;
GO  GO:0033387;
GO  GO:0050790;
GO  GO:0098629;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGYLSESDFVMVEEGFSTRDLLEELTLGASQATTGKVAAFFVADAVVRKHFCFLKYLPRVRPFYAVRCNSSLGVLKVLA
SQ  ELGLGFSCASKAEMELVQHIGVPASKIICANPCKQVAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKSWGEVLTLDAL
SQ  GLHHTHRRVGCSLMFQASVIASVAQGYLELVCQPFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPGL
SQ  EGAKVRFEEVTSVIGKNIPFYTPPPCHVPLRTHATKKMTSSDFCCRVHVTAKEKPLFSPFLTEQTGAAPKSIVYHLDEGV
SQ  YGVFNSVLFDNTCPTPALQKKPSADQPLYSSSLWGPAVDGCDCVAEGLWLPQLQVGDWLVFDNMGAYTVDTKSLLGGTQA
SQ  CRVTYAMSRLAWEALQGQLLPAEEDQDAEGVCKPLSCGWEITDSLCVGPVFTPASIM
//
ID  Q9I8S4;
PN  Antizyme inhibitor 2;
GN  azin2;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:D4A693}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000250}. Golgi apparatus, trans- Golgi network {ECO:0000250}. Cytoplasmic granule {ECO:0000250|UniProtKB:D4A693}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Perikaryon {ECO:0000250}.
DR  UNIPROT: Q9I8S4;
DR  Pfam: PF02784;
DR  Pfam: PF00278;
DR  PROSITE: PS00878;
DR  PROSITE: PS00879;
DE  Function: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizyme (AZ) on ODC activity by competing with ODC for antizyme-binding. Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production. Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking. {ECO:0000250|UniProtKB:Q8BVM4, ECO:0000250|UniProtKB:Q96A70}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0030425;
GO  GO:0033116;
GO  GO:1990005;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005802;
GO  GO:0030133;
GO  GO:0016831;
GO  GO:0042978;
GO  GO:0006596;
GO  GO:0043085;
GO  GO:1902269;
GO  GO:0098629;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQGYIQESDFNLVEEGFLARDLMEEIINEVSQTEDRDAFFVADLGDVVRKHLRFLKALPRVKPFYAVKCNSSKGVVKILA
SQ  ELGAGFDCASKTEIELVQDVGVAPERIIYANPCKQISQIKYAAKNGVQMMTFDNEVELSKVSRSHPNARMVLRIATDDSK
SQ  SSARLSVKFGAPLKSCRRLLEMAKNLSVDVIGVSFHVGSGCTDSKAYTQAISDARLVFEMASEFGYKMWLLDIGGGFPGT
SQ  EDSKIRFEEIAGVINPALDMYFPESSDVQIIAEPGRYYVASAFSLAVNVIAKKEVEHSVSDDEENESSKSIMYYVNDGVY
SQ  GSFNCLVFDHAHPKPILHKKPSPDQPLYTSSLWGPTCDGLDQIAERVQLPELHVGDWLLFENMGAYTIAASSNFNGFQQS
SQ  PVHYAMPRAAWKAVQLLQRGLQQTEEKENVCTPMSCGWEISDSLCFTRTFAATSII
//
ID  Q07816;
PN  Bcl-2-like protein 1;
GN  BCL2L1;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single- pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. {ECO:0000250}.
DR  UNIPROT: Q07816;
DR  UNIPROT: Q98908;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DE  Function: Dominant regulator of apoptotic cell death. The long form displays cell death repressor activity, whereas the short isoform promotes apoptosis. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0097136;
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005759;
GO  GO:0005741;
GO  GO:0031965;
GO  GO:0030672;
GO  GO:0051434;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0071839;
GO  GO:0071312;
GO  GO:0071230;
GO  GO:0071480;
GO  GO:0051607;
GO  GO:0097048;
GO  GO:0044565;
GO  GO:0035234;
GO  GO:0050673;
GO  GO:0097192;
GO  GO:0009566;
GO  GO:0007281;
GO  GO:0097284;
GO  GO:0008630;
GO  GO:0008584;
GO  GO:0070584;
GO  GO:2000669;
GO  GO:0051093;
GO  GO:1902236;
GO  GO:1900118;
GO  GO:1902042;
GO  GO:2001243;
GO  GO:1902230;
GO  GO:0043524;
GO  GO:1903077;
GO  GO:2000242;
GO  GO:0051402;
GO  GO:0001541;
GO  GO:0032946;
GO  GO:0032465;
GO  GO:0040008;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0001836;
GO  GO:0046898;
GO  GO:0034097;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSSNRELVIDFVSYKLSQRGHCWSELEEEDENRTDTAAEAEMDSVLNGSPSWHPPAGHVVNGATVHRSSLEVHEIVRAS
SQ  DVRQALRDAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFHDGVNWGRIVAFFSFGGALCVESVDKEMRVLVG
SQ  RIVSWMTTYLTDHLDPWIQENGGWERFVDLYGNNAAAELRKGQETFNKWLLTGATVAGVLLLGSLLSRK
//
ID  Q07817;
PN  Bcl-2-like protein 1;
GN  BCL2L1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform Bcl-X(L)]: Mitochondrion inner membrane {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner (By similarity). Localizes to the centrosome when phosphorylated at Ser-49. {ECO:0000250}.
DR  UNIPROT: Q07817;
DR  UNIPROT: E1P5L6;
DR  UNIPROT: Q5CZ89;
DR  UNIPROT: Q5TE65;
DR  UNIPROT: Q92976;
DR  PDB: 1BXL;
DR  PDB: 1G5J;
DR  PDB: 1LXL;
DR  PDB: 1MAZ;
DR  PDB: 1R2D;
DR  PDB: 1R2E;
DR  PDB: 1R2G;
DR  PDB: 1R2H;
DR  PDB: 1R2I;
DR  PDB: 1YSG;
DR  PDB: 1YSI;
DR  PDB: 1YSN;
DR  PDB: 2B48;
DR  PDB: 2LP8;
DR  PDB: 2LPC;
DR  PDB: 2M03;
DR  PDB: 2M04;
DR  PDB: 2ME8;
DR  PDB: 2ME9;
DR  PDB: 2MEJ;
DR  PDB: 2O1Y;
DR  PDB: 2O2M;
DR  PDB: 2O2N;
DR  PDB: 2P1L;
DR  PDB: 2PON;
DR  PDB: 2YJ1;
DR  PDB: 2YQ6;
DR  PDB: 2YQ7;
DR  PDB: 2YXJ;
DR  PDB: 3CVA;
DR  PDB: 3FDL;
DR  PDB: 3FDM;
DR  PDB: 3INQ;
DR  PDB: 3IO8;
DR  PDB: 3PL7;
DR  PDB: 3QKD;
DR  PDB: 3R85;
DR  PDB: 3SP7;
DR  PDB: 3SPF;
DR  PDB: 3WIZ;
DR  PDB: 3ZK6;
DR  PDB: 3ZLN;
DR  PDB: 3ZLO;
DR  PDB: 3ZLR;
DR  PDB: 4A1U;
DR  PDB: 4A1W;
DR  PDB: 4AQ3;
DR  PDB: 4BPK;
DR  PDB: 4C52;
DR  PDB: 4C5D;
DR  PDB: 4CIN;
DR  PDB: 4EHR;
DR  PDB: 4HNJ;
DR  PDB: 4IEH;
DR  PDB: 4PPI;
DR  PDB: 4QVE;
DR  PDB: 4QVF;
DR  PDB: 4QVX;
DR  PDB: 4TUH;
DR  PDB: 4Z9V;
DR  PDB: 5AGW;
DR  PDB: 5AGX;
DR  PDB: 5B1Z;
DR  PDB: 5C3G;
DR  PDB: 5FMJ;
DR  PDB: 5FMK;
DR  PDB: 5VAY;
DR  PDB: 5VX3;
DR  PDB: 6BF2;
DR  PDB: 6DCN;
DR  PDB: 6DCO;
DR  PDB: 6F46;
DR  PDB: 6HJL;
DR  PDB: 6IJQ;
DR  PDB: 6LHD;
DR  PDB: 6O0K;
DR  PDB: 6O0L;
DR  PDB: 6O0M;
DR  PDB: 6O0O;
DR  PDB: 6O0P;
DR  PDB: 6RNU;
DR  PDB: 6ST2;
DR  PDB: 6UVC;
DR  PDB: 6UVD;
DR  PDB: 6UVE;
DR  PDB: 6UVF;
DR  PDB: 6UVG;
DR  PDB: 6UVH;
DR  PDB: 6VWC;
DR  PDB: 6X7I;
DR  PDB: 6YLI;
DR  PDB: 6ZHC;
DR  PDB: 7CA4;
DR  PDB: 7JGV;
DR  PDB: 7JGW;
DR  PDB: 7LH7;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DR  OMIM: 600039;
DR  DisGeNET: 598;
DE  Function: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage- dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785). {ECO:0000269|PubMed:17418785}. Isoform Bcl-X(S) promotes apoptosis.
DE  Reference Proteome: Yes;
DE  Interaction: P00519; IntAct: EBI-8488890; Score: 0.40
DE  Interaction: P10415; IntAct: EBI-2126646; Score: 0.44
DE  Interaction: P10909; IntAct: EBI-4322676; Score: 0.61
DE  Interaction: P30429; IntAct: EBI-494146; Score: 0.40
DE  Interaction: P49810; IntAct: EBI-7072489; Score: 0.54
DE  Interaction: P49768; IntAct: EBI-7072509; Score: 0.37
DE  Interaction: P70444; IntAct: EBI-15708450; Score: 0.44
DE  Interaction: Q92934; IntAct: EBI-7986686; Score: 0.97
DE  Interaction: O54918; IntAct: EBI-15616455; Score: 0.59
DE  Interaction: Q9NP97; IntAct: EBI-526396; Score: 0.35
DE  Interaction: P51572; IntAct: EBI-78034; Score: 0.40
DE  Interaction: P45983; IntAct: EBI-7497515; Score: 0.52
DE  Interaction: Q14318; IntAct: EBI-7497660; Score: 0.44
DE  Interaction: Q07817; IntAct: EBI-700842; Score: 0.59
DE  Interaction: Q64373; IntAct: EBI-700869; Score: 0.40
DE  Interaction: Q07812; IntAct: EBI-701131; Score: 0.97
DE  Interaction: Q16611; IntAct: EBI-760384; Score: 0.95
DE  Interaction: O43521; IntAct: EBI-701297; Score: 0.93
DE  Interaction: O00198; IntAct: EBI-701309; Score: 0.70
DE  Interaction: Q9BXH1; IntAct: EBI-707945; Score: 0.86
DE  Interaction: Q91ZE9; IntAct: EBI-708056; Score: 0.44
DE  Interaction: Q13323; IntAct: EBI-760279; Score: 0.91
DE  Interaction: P55957; IntAct: EBI-708176; Score: 0.86
DE  Interaction: Q61337; IntAct: EBI-709145; Score: 0.59
DE  Interaction: Q13794; IntAct: EBI-709305; Score: 0.68
DE  Interaction: P02340; IntAct: EBI-728086; Score: 0.50
DE  Interaction: Q99ML1; IntAct: EBI-728086; Score: 0.50
DE  Interaction: P04637; IntAct: EBI-727854; Score: 0.88
DE  Interaction: P62136; IntAct: EBI-1206864; Score: 0.00
DE  Interaction: P36873; IntAct: EBI-1207054; Score: 0.00
DE  Interaction: Q9C000; IntAct: EBI-1246322; Score: 0.65
DE  Interaction: Q14457; IntAct: EBI-5234817; Score: 0.70
DE  Interaction: Q9H2V7; IntAct: EBI-1386556; Score: 0.46
DE  Interaction: O15304; IntAct: EBI-1393098; Score: 0.57
DE  Interaction: O35303; IntAct: EBI-1767441; Score: 0.40
DE  Interaction: O00429; IntAct: EBI-1767523; Score: 0.44
DE  Interaction: A0A2S9PFE9; IntAct: EBI-2874931; Score: 0.00
DE  Interaction: O43889; IntAct: EBI-8645414; Score: 0.37
DE  Interaction: P48558; IntAct: EBI-5275391; Score: 0.40
DE  Interaction: P60709; IntAct: EBI-7102779; Score: 0.37
DE  Interaction: Q3B7T1; IntAct: EBI-7102826; Score: 0.37
DE  Interaction: Q86XA0; IntAct: EBI-7102889; Score: 0.37
DE  Interaction: Q96N67; IntAct: EBI-7102942; Score: 0.37
DE  Interaction: P09467; IntAct: EBI-7102996; Score: 0.37
DE  Interaction: Q9HC38; IntAct: EBI-7103053; Score: 0.37
DE  Interaction: Q6PKG0; IntAct: EBI-7103101; Score: 0.37
DE  Interaction: P13667; IntAct: EBI-7103233; Score: 0.37
DE  Interaction: Q8IV08; IntAct: EBI-7103438; Score: 0.37
DE  Interaction: Q8NEY8; IntAct: EBI-7103564; Score: 0.37
DE  Interaction: P21246; IntAct: EBI-7103628; Score: 0.37
DE  Interaction: P52756; IntAct: EBI-7103707; Score: 0.37
DE  Interaction: Q04724; IntAct: EBI-7103774; Score: 0.37
DE  Interaction: Q13625; IntAct: EBI-15723914; Score: 0.56
DE  Interaction: Q8IWV7; IntAct: EBI-7103907; Score: 0.37
DE  Interaction: Q9HBF4; IntAct: EBI-7103940; Score: 0.37
DE  Interaction: Q9UKY1; IntAct: EBI-7104013; Score: 0.37
DE  Interaction: Q9P2Y4; IntAct: EBI-7104091; Score: 0.37
DE  Interaction: Q96PU4; IntAct: EBI-6051471; Score: 0.40
DE  Interaction: Q86Y07; IntAct: EBI-6476114; Score: 0.50
DE  Interaction: P99999; IntAct: EBI-6589621; Score: 0.27
DE  Interaction: P04049; IntAct: EBI-6592472; Score: 0.27
DE  Interaction: P55211; IntAct: EBI-6593000; Score: 0.27
DE  Interaction: Q96LC9; IntAct: EBI-10290553; Score: 0.81
DE  Interaction: Q61699; IntAct: EBI-11091301; Score: 0.35
DE  Interaction: P49286; IntAct: EBI-11577578; Score: 0.00
DE  Interaction: Q7L3V2; IntAct: EBI-11509563; Score: 0.46
DE  Interaction: P03496; IntAct: EBI-11519828; Score: 0.37
DE  Interaction: Q20MH3; IntAct: EBI-11520043; Score: 0.37
DE  Interaction: Q0A2H0; IntAct: EBI-11520223; Score: 0.37
DE  Interaction: Q8NBJ4; IntAct: EBI-24661651; Score: 0.56
DE  Interaction: P56557; IntAct: EBI-24667028; Score: 0.56
DE  Interaction: Q9GZR5; IntAct: EBI-23702709; Score: 0.56
DE  Interaction: P22749; IntAct: EBI-24691348; Score: 0.56
DE  Interaction: Q7KZS0; IntAct: EBI-24702746; Score: 0.56
DE  Interaction: P27469; IntAct: EBI-23766185; Score: 0.56
DE  Interaction: Q9Y282; IntAct: EBI-24743336; Score: 0.56
DE  Interaction: Q9H2K0; IntAct: EBI-24748533; Score: 0.56
DE  Interaction: Q9H6H4; IntAct: EBI-24749484; Score: 0.56
DE  Interaction: Q8IYJ2; IntAct: EBI-24779286; Score: 0.56
DE  Interaction: P78317; IntAct: EBI-24796078; Score: 0.56
DE  Interaction: Q7Z5B4; IntAct: EBI-23915698; Score: 0.56
DE  Interaction: P0C671; IntAct: EBI-24555838; Score: 0.56
DE  Interaction: Q6NTF9; IntAct: EBI-24646649; Score: 0.56
DE  Interaction: Q5T7V8; IntAct: EBI-25269471; Score: 0.56
DE  Interaction: P24830; IntAct: EBI-16046634; Score: 0.37
DE  Interaction: P06921; IntAct: EBI-16047315; Score: 0.00
DE  Interaction: P06422; IntAct: EBI-16048535; Score: 0.00
DE  Interaction: P36780; IntAct: EBI-16049904; Score: 0.00
DE  Interaction: P04015; IntAct: EBI-16050562; Score: 0.00
DE  Interaction: P06790; IntAct: EBI-16051663; Score: 0.00
DE  Interaction: P06423; IntAct: EBI-16052407; Score: 0.00
DE  Interaction: P03118; IntAct: EBI-16053329; Score: 0.00
DE  Interaction: P36778; IntAct: EBI-16054563; Score: 0.00
DE  Interaction: Q29RF7; IntAct: EBI-21755538; Score: 0.35
DE  Interaction: Q99MI6; IntAct: EBI-15572392; Score: 0.56
DE  Interaction: Q8BWF2; IntAct: EBI-15572411; Score: 0.56
DE  Interaction: Q99104; IntAct: EBI-15666413; Score: 0.35
DE  Interaction: Q07813; IntAct: EBI-15666413; Score: 0.53
DE  Interaction: Q8VDD5; IntAct: EBI-15666432; Score: 0.35
DE  Interaction: P42345; IntAct: EBI-15828862; Score: 0.69
DE  Interaction: P21796; IntAct: EBI-15828900; Score: 0.35
DE  Interaction: Q64010; IntAct: EBI-15959690; Score: 0.40
DE  Interaction: O08734; IntAct: EBI-16176197; Score: 0.35
DE  Interaction: Q14790; IntAct: EBI-16211903; Score: 0.40
DE  Interaction: O15530; IntAct: EBI-16594603; Score: 0.35
DE  Interaction: P59637; IntAct: EBI-25487800; Score: 0.40
DE  Interaction: P59635; IntAct: EBI-25494122; Score: 0.40
DE  Interaction: P37840; IntAct: EBI-25940857; Score: 0.56
DE  Interaction: Q9HB09; IntAct: EBI-27086218; Score: 0.37
DE  Interaction: Q9H492; IntAct: EBI-30828681; Score: 0.44
DE  Interaction: Q9GZQ8; IntAct: EBI-30830914; Score: 0.44
DE  Interaction: O75381; IntAct: EBI-30835456; Score: 0.44
GO  GO:0070161;
GO  GO:0097136;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005743;
GO  GO:0005759;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0097143;
GO  GO:0030672;
GO  GO:0051434;
GO  GO:0042802;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0008637;
GO  GO:0071839;
GO  GO:0071312;
GO  GO:0071230;
GO  GO:0071480;
GO  GO:0051607;
GO  GO:0097048;
GO  GO:0044565;
GO  GO:0035234;
GO  GO:0006897;
GO  GO:0050673;
GO  GO:0097192;
GO  GO:0009566;
GO  GO:0007281;
GO  GO:0097284;
GO  GO:0001701;
GO  GO:0008630;
GO  GO:0008584;
GO  GO:0070584;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:0010507;
GO  GO:2000669;
GO  GO:0051093;
GO  GO:1902236;
GO  GO:1900118;
GO  GO:2001240;
GO  GO:1902042;
GO  GO:2001243;
GO  GO:1902230;
GO  GO:1901029;
GO  GO:0043524;
GO  GO:1903077;
GO  GO:0090201;
GO  GO:2000242;
GO  GO:0051402;
GO  GO:0001541;
GO  GO:0032946;
GO  GO:0032465;
GO  GO:0040008;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0001836;
GO  GO:0046898;
GO  GO:0034097;
GO  GO:0007283;
GO  GO:0019050;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREV
SQ  IPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQ
SQ  VLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK
//
ID  Q64373;
PN  Bcl-2-like protein 1;
GN  Bcl2l1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion membrane {ECO:0000269|PubMed:7607090}; Single-pass membrane protein {ECO:0000269|PubMed:7607090}. Nucleus membrane {ECO:0000250}; Single- pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:7607090}. Note=Localizes to the centrosome when phosphorylated at Ser-49. [Isoform Bcl-X(L)]: Mitochondrion inner membrane. Mitochondrion outer membrane. Mitochondrion matrix {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. {ECO:0000250}. [Isoform Bcl-X(delta-TM)]: Cytoplasm.
DR  UNIPROT: Q64373;
DR  UNIPROT: O35844;
DR  UNIPROT: Q60657;
DR  UNIPROT: Q60658;
DR  UNIPROT: Q61338;
DR  PDB: 1PQ0;
DR  PDB: 1PQ1;
DR  PDB: 2BZW;
DR  PDB: 3IHC;
DR  PDB: 3IHD;
DR  PDB: 3IHE;
DR  PDB: 3IHF;
DR  PDB: 3IIG;
DR  PDB: 3IIH;
DR  PDB: 3ILB;
DR  PDB: 3ILC;
DR  PDB: 4YJ4;
DR  PDB: 4YK9;
DR  PDB: 5C3G;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DE  Function: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage- dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. {ECO:0000269|PubMed:9390687}. Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles (By similarity). May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q07817}. Isoform Bcl-X(S) promotes apoptosis. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q07817; IntAct: EBI-700869; Score: 0.40
DE  Interaction: Q99ML1; IntAct: EBI-727813; Score: 0.35
DE  Interaction: P02340; IntAct: EBI-727813; Score: 0.35
DE  Interaction: O54918; IntAct: EBI-1037127; Score: 0.44
DE  Interaction: P63087; IntAct: EBI-1202891; Score: 0.00
DE  Interaction: O54926; IntAct: EBI-1393194; Score: 0.40
DE  Interaction: O00198; IntAct: EBI-6375860; Score: 0.40
DE  Interaction: Q61337; IntAct: EBI-6693214; Score: 0.40
DE  Interaction: P59637; IntAct: EBI-25487713; Score: 0.40
GO  GO:0070161;
GO  GO:0097136;
GO  GO:0005813;
GO  GO:0005905;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005740;
GO  GO:0005743;
GO  GO:0005759;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0098793;
GO  GO:0097143;
GO  GO:0030672;
GO  GO:0051400;
GO  GO:0051434;
GO  GO:0030276;
GO  GO:0043027;
GO  GO:0051020;
GO  GO:0042802;
GO  GO:0097371;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0006915;
GO  GO:0071839;
GO  GO:0071312;
GO  GO:0071230;
GO  GO:0071480;
GO  GO:0051607;
GO  GO:0097048;
GO  GO:0044565;
GO  GO:0035234;
GO  GO:0050673;
GO  GO:0097192;
GO  GO:0009566;
GO  GO:0007281;
GO  GO:0097284;
GO  GO:0001701;
GO  GO:0008630;
GO  GO:0008584;
GO  GO:0070584;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:2000669;
GO  GO:0051093;
GO  GO:1902236;
GO  GO:1900118;
GO  GO:1902042;
GO  GO:2001243;
GO  GO:1902230;
GO  GO:1901029;
GO  GO:0043524;
GO  GO:1903077;
GO  GO:0090201;
GO  GO:2000242;
GO  GO:0051402;
GO  GO:0001541;
GO  GO:0043065;
GO  GO:2001171;
GO  GO:0032946;
GO  GO:2000809;
GO  GO:1900244;
GO  GO:2000302;
GO  GO:0042981;
GO  GO:0032465;
GO  GO:0040008;
GO  GO:1900452;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0001836;
GO  GO:0046898;
GO  GO:0034097;
GO  GO:0002931;
GO  GO:0009314;
GO  GO:0009615;
GO  GO:0007283;
GO  GO:0019050;
GO  GO:0036466;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEAERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREV
SQ  IPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQ
SQ  VLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK
//
ID  O77737;
PN  Bcl-2-like protein 1;
GN  BCL2L1;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single- pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. Localizes to the centrosome when phosphorylated at Ser-49 (By similarity). {ECO:0000250}.
DR  UNIPROT: O77737;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DE  Function: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage- dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1- inflammasome activation, hence CASP1 activation and IL1B release (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q07817}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0005759;
GO  GO:0005741;
GO  GO:0031965;
GO  GO:0030672;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0006897;
GO  GO:0097192;
GO  GO:0008630;
GO  GO:1902236;
GO  GO:1900118;
GO  GO:2001243;
GO  GO:0032465;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSQSNRELVVDFLSYKLSQKGYSWSQFTDVEENRTEAPEGTESEAETPSAINGNPSWHLADSPAVNGATGHSSSLDAREV
SQ  IPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVLNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQ
SQ  VLVSRIATWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTLAGVVLLGSLFSRK
//
ID  P53563;
PN  Bcl-2-like protein 1;
GN  Bcl2l1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform Bcl-X(L)]: Mitochondrion inner membrane. Mitochondrion outer membrane. Mitochondrion matrix. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane. Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes to the centrosome when phosphorylated at Ser-49 (By similarity). After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. {ECO:0000250}.
DR  UNIPROT: P53563;
DR  UNIPROT: P70613;
DR  UNIPROT: P70614;
DR  UNIPROT: Q52KS0;
DR  UNIPROT: Q62678;
DR  UNIPROT: Q62836;
DR  UNIPROT: Q64087;
DR  UNIPROT: Q64128;
DR  PDB: 1AF3;
DR  PDB: 4QNQ;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DE  Function: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage- dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity). {ECO:0000250|UniProtKB:Q07817, ECO:0000269|PubMed:18250306, ECO:0000269|PubMed:21926988, ECO:0000269|PubMed:23792689, ECO:0000269|PubMed:7828536, ECO:0000269|PubMed:8662675}. Isoform Bcl-X(S) promotes apoptosis.
DE  Reference Proteome: Yes;
DE  Interaction: O88498; IntAct: EBI-79058; Score: 0.37
DE  Interaction: O35303; IntAct: EBI-1767505; Score: 0.56
DE  Interaction: O35147; IntAct: EBI-15693744; Score: 0.40
DE  Interaction: P08081; IntAct: EBI-16062715; Score: 0.50
DE  Interaction: Q4KM98; IntAct: EBI-16062732; Score: 0.35
GO  GO:0070161;
GO  GO:0097136;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005740;
GO  GO:0005743;
GO  GO:0005759;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0098793;
GO  GO:0030672;
GO  GO:0051400;
GO  GO:0051434;
GO  GO:0030276;
GO  GO:0043027;
GO  GO:0051020;
GO  GO:0042802;
GO  GO:0097371;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0007568;
GO  GO:0006915;
GO  GO:0071839;
GO  GO:0008283;
GO  GO:0071312;
GO  GO:0071230;
GO  GO:1905218;
GO  GO:0071320;
GO  GO:0071549;
GO  GO:0036018;
GO  GO:0071480;
GO  GO:0071456;
GO  GO:0071347;
GO  GO:1990646;
GO  GO:1904579;
GO  GO:0071356;
GO  GO:0071466;
GO  GO:0021987;
GO  GO:0051607;
GO  GO:0097048;
GO  GO:0044565;
GO  GO:0035234;
GO  GO:0006897;
GO  GO:0050673;
GO  GO:0097192;
GO  GO:0009566;
GO  GO:0007281;
GO  GO:0097284;
GO  GO:0001701;
GO  GO:0008630;
GO  GO:0008584;
GO  GO:0070584;
GO  GO:0043066;
GO  GO:2000669;
GO  GO:0051093;
GO  GO:1902236;
GO  GO:1900118;
GO  GO:1902042;
GO  GO:2001243;
GO  GO:1902230;
GO  GO:0043524;
GO  GO:1903077;
GO  GO:2000242;
GO  GO:0051402;
GO  GO:0001541;
GO  GO:0043065;
GO  GO:2001171;
GO  GO:0008284;
GO  GO:0032946;
GO  GO:2000809;
GO  GO:1900244;
GO  GO:2000302;
GO  GO:0042981;
GO  GO:0032465;
GO  GO:0040008;
GO  GO:1900452;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0001836;
GO  GO:0046898;
GO  GO:0034097;
GO  GO:0051602;
GO  GO:0036017;
GO  GO:0042542;
GO  GO:0001666;
GO  GO:0010035;
GO  GO:0002931;
GO  GO:0010288;
GO  GO:0032496;
GO  GO:0014070;
GO  GO:0010243;
GO  GO:0006979;
GO  GO:0043434;
GO  GO:0009314;
GO  GO:0009615;
GO  GO:0009410;
GO  GO:0007283;
GO  GO:0036466;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEPERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREV
SQ  IPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQ
SQ  VLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK
//
ID  Q9HD36;
PN  Bcl-2-like protein 10;
GN  BCL2L10;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion {ECO:0000269|PubMed:11593390, ECO:0000269|PubMed:21705382, ECO:0000269|PubMed:22233804, ECO:0000269|PubMed:22498477, ECO:0000269|PubMed:23563182}. Nucleus membrane {ECO:0000269|PubMed:11593390}. Endoplasmic reticulum {ECO:0000269|PubMed:22498477, ECO:0000269|PubMed:27995898}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9Z0F3}. Note=Localizes to mitochondria-associated endoplasmic reticulum membranes (MAMs) (PubMed:27995898). Localization to MAMs is greatly reduced under apoptotic stress conditions (PubMed:27995898). {ECO:0000269|PubMed:27995898}.
DR  UNIPROT: Q9HD36;
DR  UNIPROT: Q3SX80;
DR  UNIPROT: Q52LQ9;
DR  UNIPROT: Q8TCS9;
DR  PDB: 4B4S;
DR  Pfam: PF00452;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  OMIM: 606910;
DR  DisGeNET: 10017;
DE  Function: Promotes cell survival by suppressing apoptosis induced by BAX but not BAK (PubMed:11689480, PubMed:11278245). Increases binding of AHCYL1/IRBIT to ITPR1 (PubMed:27995898). Reduces ITPR1-mediated calcium release from the endoplasmic reticulum cooperatively with AHCYL1/IRBIT under normal cellular conditions (PubMed:27995898). Under apoptotic stress conditions, dissociates from ITPR1 and is displaced from mitochondria-associated endoplasmic reticulum membranes, leading to increased Ca(2+) transfer to mitochondria which promotes apoptosis (PubMed:27995898). Required for the correct formation of the microtubule organizing center during oocyte cell division, potentially via regulation of protein abundance and localization of other microtubule organizing center components such as AURKA and TPX2 (By similarity). {ECO:0000250|UniProtKB:Q9Z0F3, ECO:0000269|PubMed:11278245, ECO:0000269|PubMed:11689480, ECO:0000269|PubMed:27995898}.
DE  Reference Proteome: Yes;
DE  Interaction: Q14643; IntAct: EBI-22188044; Score: 0.66
DE  Interaction: P22736; IntAct: EBI-2126371; Score: 0.40
DE  Interaction: Q14790; IntAct: EBI-9064052; Score: 0.37
DE  Interaction: O43521; IntAct: EBI-11304337; Score: 0.78
DE  Interaction: Q07812; IntAct: EBI-11304362; Score: 0.40
DE  Interaction: Q13323; IntAct: EBI-11304411; Score: 0.70
DE  Interaction: Q96LC9; IntAct: EBI-24617832; Score: 0.56
DE  Interaction: Q5PRF9; IntAct: EBI-24664926; Score: 0.56
DE  Interaction: Q99735; IntAct: EBI-23758524; Score: 0.56
DE  Interaction: Q86VY9; IntAct: EBI-24795275; Score: 0.56
DE  Interaction: Q14571; IntAct: EBI-22188055; Score: 0.40
DE  Interaction: Q14573; IntAct: EBI-22188066; Score: 0.40
DE  Interaction: O43865; IntAct: EBI-22196627; Score: 0.59
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0044233;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005819;
GO  GO:0005509;
GO  GO:0089720;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:0097192;
GO  GO:0007292;
GO  GO:0008630;
GO  GO:0031023;
GO  GO:0043066;
GO  GO:2001243;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVDQLRERTTMADPLRERTELLLADYLGYCAREPGTPEPAPSTPEAAVLRSAAARLRQIHRSFFSAYLGYPGNRFELVAL
SQ  MADSVLSDSPGPTWGRVVTLVTFAGTLLERGPLVTARWKKWGFQPRLKEQEGDVARDCQRLVALLSSRLMGQHRAWLQAQ
SQ  GGWDGFCHFFRTPFPLAFWRKQLVQAFLSCLLTTAFIYLWTRLL
//
ID  Q9Z0F3;
PN  Bcl-2-like protein 10;
GN  Bcl2l10;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion {ECO:0000250|UniProtKB:Q9HD36}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HD36}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9HD36}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:27753540}. Note=Localizes to mitochondria- associated endoplasmic reticulum membranes (MAMs) (By similarity). Localization to MAMs is greatly reduced under apoptotic stress conditions (By similarity). {ECO:0000250|UniProtKB:Q9HD36}.
DR  UNIPROT: Q9Z0F3;
DR  UNIPROT: Q3ULP5;
DR  UNIPROT: Q7TPY8;
DR  PDB: 2KUA;
DR  Pfam: PF00452;
DR  PROSITE: PS50062;
DE  Function: Promotes cell survival by suppressing apoptosis induced by BAX but not BAK (By similarity). Increases binding of AHCYL1/IRBIT to ITPR1 (By similarity). Reduces ITPR1-mediated calcium release from the endoplasmic reticulum cooperatively with AHCYL1/IRBIT under normal cellular conditions (By similarity). Under apoptotic stress conditions, dissociates from ITPR1 and is displaced from mitochondria-associated endoplasmic reticulum membranes, leading to increased Ca(2+) transfer to mitochondria which promotes apoptosis (By similarity). Required for the correct formation of the microtubule organizing center during oocyte cell division, potentially via regulation of protein abundance and localization of other microtubule organizing center components such as AURKA and TPX2 (PubMed:27753540). {ECO:0000250|UniProtKB:Q9HD36, ECO:0000269|PubMed:27753540}.
DE  Reference Proteome: Yes;
DE  Interaction: O14727; IntAct: EBI-8658689; Score: 0.51
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0044233;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005819;
GO  GO:0005509;
GO  GO:0089720;
GO  GO:0042802;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0006915;
GO  GO:0097192;
GO  GO:0097193;
GO  GO:0008630;
GO  GO:0031023;
GO  GO:0043066;
GO  GO:2001240;
GO  GO:2001243;
GO  GO:0043065;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADSQDPLHERTRRLLSDYIFFCAREPDTPEPPPTSVEAALLRSVTRQIQQEHQEFFSSFCESRGNRLELVKQMADKLLS
SQ  KDQDFSWSQLVMLLAFAGTLMNQGPYMAVKQKRDLGNRVIVTRDCCLIVNFLYNLLMGRRHRARLEALGGWDGFCRFFKN
SQ  PLPLGFWRRLLIQAFLSGFFATAIFFIWKRL
//
ID  Q99M66;
PN  Bcl-2-like protein 10;
GN  Bcl2l10;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion {ECO:0000250|UniProtKB:Q9HD36}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HD36}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9HD36}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9Z0F3}. Note=Localizes to mitochondria- associated endoplasmic reticulum membranes (MAMs) (By similarity). Localization to MAMs is greatly reduced under apoptotic stress conditions (By similarity). {ECO:0000250|UniProtKB:Q9HD36}.
DR  UNIPROT: Q99M66;
DR  Pfam: PF00452;
DR  PROSITE: PS50062;
DR  PROSITE: PS01258;
DE  Function: Promotes cell survival by suppressing apoptosis induced by BAX but not BAK (By similarity). Increases binding of AHCYL1/IRBIT to ITPR1 (By similarity). Reduces ITPR1-mediated calcium release from the endoplasmic reticulum cooperatively with AHCYL1/IRBIT under normal cellular conditions (By similarity). Under apoptotic stress conditions, dissociates from ITPR1 and is displaced from mitochondria-associated endoplasmic reticulum membranes, leading to increased Ca(2+) transfer to mitochondria which promotes apoptosis (By similarity). Required for the correct formation of the microtubule organizing center during oocyte cell division, potentially via regulation of protein abundance and localization of other microtubule organizing center components such as AURKA and TPX2 (By similarity). {ECO:0000250|UniProtKB:Q9HD36, ECO:0000250|UniProtKB:Q9Z0F3}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0044233;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005819;
GO  GO:0005509;
GO  GO:0089720;
GO  GO:0042802;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0006915;
GO  GO:0097192;
GO  GO:0097193;
GO  GO:0008630;
GO  GO:0031023;
GO  GO:0043066;
GO  GO:2001240;
GO  GO:2001243;
GO  GO:0048709;
GO  GO:0043065;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGDPLQDRTRRLLTDYILFCARAPNTPEPLPTSVEAALLRSVTSQIQQEHQDLFNSFRDYQGNRLELVTQMADELLSNDQ
SQ  EFNWGRLVMLLAFVGTLMNQDRTVKRRRDQRNRLLLERDCYLIVSLLYNRLTGRHRSWLEAHGGWDGFCQFFKNPLPPGF
SQ  WRRLLIRAILSCFFATAIFYIWKCL
//
ID  Q6NTS2;
PN  Barrier-to-autointegration factor A;
GN  banf1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:19167377}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. {ECO:0000250|UniProtKB:O75531}.
DR  UNIPROT: Q6NTS2;
DR  UNIPROT: A3KNC4;
DR  Pfam: PF02961;
DE  Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response; acts by inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. {ECO:0000250|UniProtKB:O75531}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005635;
GO  GO:0003677;
GO  GO:0010836;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSTSQKHRDFVAEPMGEKSVQCLAGIGEALGHRLEEKGFDKAYVVLGQFLVLKKDEELFKEWLKDICSANAKQSRDCYG
SQ  CLKEWCDAFL
//
ID  Q66KV4;
PN  Barrier-to-autointegration factor B;
GN  banf1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:19167377}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. {ECO:0000250|UniProtKB:O75531}.
DR  UNIPROT: Q66KV4;
DR  Pfam: PF02961;
DE  Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response; acts by inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. {ECO:0000250|UniProtKB:O75531}.
DE  Reference Proteome: Yes;
DE  Interaction: B9X187; IntAct: EBI-12596342; Score: 0.46
DE  Interaction: Q7ZTB4; IntAct: EBI-12596356; Score: 0.40
GO  GO:0000785;
GO  GO:0005635;
GO  GO:0003677;
GO  GO:0010836;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSTSQKHRDFVAEPMGEKSVQCLAGIGDTLGRRLEEKGFDKAYVVLGQFLVLKKDEELFKEWLKDACSANAKQSRDCYG
SQ  CLKEWCDAFL
//
ID  P61283;
PN  Barrier-to-autointegration factor, N-terminally processed;
GN  BANF1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O75531}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000250|UniProtKB:O75531}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus. May be included in HIV-1 virions via its interaction with viral GAG polyprotein. {ECO:0000250|UniProtKB:O75531}.
DR  UNIPROT: P61283;
DR  UNIPROT: Q5E9E5;
DR  Pfam: PF02961;
DE  Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication. {ECO:0000250|UniProtKB:O75531}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0003677;
GO  GO:0006325;
GO  GO:0030261;
GO  GO:0007059;
GO  GO:0007084;
GO  GO:0010836;
GO  GO:0032480;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGC
SQ  LREWCDAFL
//
ID  Q6P026;
PN  Barrier-to-autointegration factor;
GN  banf1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O75531}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000250|UniProtKB:O75531}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. {ECO:0000250|UniProtKB:O75531}.
DR  UNIPROT: Q6P026;
DR  Pfam: PF02961;
DE  Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response; acts by inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. {ECO:0000250|UniProtKB:O75531}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0003677;
GO  GO:0006325;
GO  GO:0030261;
GO  GO:0007059;
GO  GO:0007084;
GO  GO:0010836;
GO  GO:0032480;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSTSQKHKDFVAEPMGEKSVMALAGIGEVLGKRLEEKGFDKAYVVLGQFLVLRKDEELFREWLKDTCGANTKQQGDCYS
SQ  CLREWCDSFL
//
ID  O75531;
PN  Barrier-to-autointegration factor, N-terminally processed;
GN  BANF1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}. Chromosome {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32792394}. Nucleus envelope {ECO:0000269|PubMed:24600006}. Cytoplasm {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase (PubMed:16495336, PubMed:24600006). The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus (PubMed:16495336, PubMed:24600006). May be included in HIV-1 virions via its interaction with viral GAG polyprotein (PubMed:14645565). {ECO:0000269|PubMed:14645565, ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:24600006}.
DR  UNIPROT: O75531;
DR  UNIPROT: O60558;
DR  UNIPROT: Q6FGG7;
DR  PDB: 1CI4;
DR  PDB: 1QCK;
DR  PDB: 2BZF;
DR  PDB: 2EZX;
DR  PDB: 2EZY;
DR  PDB: 2EZZ;
DR  PDB: 2ODG;
DR  PDB: 6GHD;
DR  PDB: 6RPR;
DR  PDB: 6UNT;
DR  PDB: 6URE;
DR  PDB: 6URJ;
DR  PDB: 6URK;
DR  PDB: 6URL;
DR  PDB: 6URN;
DR  PDB: 6URR;
DR  PDB: 6URZ;
DR  PDB: 6US0;
DR  PDB: 6US1;
DR  PDB: 6US7;
DR  PDB: 6USB;
DR  PDB: 6USD;
DR  PDB: 6USI;
DR  PDB: 7ABM;
DR  PDB: 7NDY;
DR  Pfam: PF02961;
DR  OMIM: 603811;
DR  OMIM: 614008;
DR  DisGeNET: 8815;
DE  Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA (PubMed:10908652, PubMed:11792822, PubMed:12163470, PubMed:18005698, PubMed:25991860, PubMed:28841419, PubMed:31796734, PubMed:32792394). Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging (PubMed:9465049). Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner (PubMed:28841419). Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface (PubMed:28841419). Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity (PubMed:32792394). Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses (PubMed:32792394). Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1 (PubMed:31796734). Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy (PubMed:25991860). In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication (PubMed:18005698). {ECO:0000269|PubMed:10908652, ECO:0000269|PubMed:11792822, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:25991860, ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32792394, ECO:0000269|PubMed:9465049}. (Microbial infection) Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome (PubMed:9465049, PubMed:11005805, PubMed:16680152). EMD and BAF are cooperative cofactors of HIV-1 infection (PubMed:16680152). Association of EMD with the viral DNA requires the presence of BAF and viral integrase (PubMed:16680152). The association of viral DNA with chromatin requires the presence of BAF and EMD (PubMed:16680152). {ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:9465049}.
DE  Disease: Nestor-Guillermo progeria syndrome (NGPS) [MIM:614008]: An atypical progeroid syndrome characterized by normal development in the first years of life, later followed by the emergence of generalized lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic facial subcutaneous fat pad and the marked osteolysis of the maxilla and mandible result in a typical pseudosenile facial appearance with micrognathia, prominent subcutaneous venous patterning, a convex nasal ridge, and proptosis. Cognitive development is completely normal. Patients do not have cardiovascular dysfunction, atherosclerosis, or metabolic anomalies. {ECO:0000269|PubMed:21549337}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q96JB5; IntAct: EBI-1076230; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1083050; Score: 0.00
DE  Interaction: P38606; IntAct: EBI-4324466; Score: 0.35
DE  Interaction: O95758; IntAct: EBI-7851121; Score: 0.35
DE  Interaction: O14862; IntAct: EBI-9995694; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-10759397; Score: 0.94
DE  Interaction: P60033; IntAct: EBI-10766934; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: Q9D752; IntAct: EBI-11004099; Score: 0.35
DE  Interaction: P83917; IntAct: EBI-11012671; Score: 0.35
DE  Interaction: P97470; IntAct: EBI-11029414; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: Q9CPQ5; IntAct: EBI-11051123; Score: 0.35
DE  Interaction: Q80UF4; IntAct: EBI-11074854; Score: 0.35
DE  Interaction: Q8N0Z3; IntAct: EBI-11392023; Score: 0.27
DE  Interaction: Q8N137; IntAct: EBI-11392655; Score: 0.27
DE  Interaction: Q9H503; IntAct: EBI-25251388; Score: 0.56
DE  Interaction: O75531; IntAct: EBI-15556735; Score: 0.62
DE  Interaction: O15155; IntAct: EBI-16788578; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P51151; IntAct: EBI-16798596; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16789225; Score: 0.27
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-20306992; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-20307233; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-20307902; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: E7ELX2; IntAct: EBI-20625922; Score: 0.35
DE  Interaction: Q96N64; IntAct: EBI-20910224; Score: 0.40
DE  Interaction: Q8NEL9; IntAct: EBI-20920812; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P68431; IntAct: EBI-25471577; Score: 0.27
DE  Interaction: Q9UBI1; IntAct: EBI-21259462; Score: 0.35
DE  Interaction: Q9BWW4; IntAct: EBI-21265722; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q8WUJ0; IntAct: EBI-21945299; Score: 0.35
DE  Interaction: Q15311; IntAct: EBI-25375541; Score: 0.35
DE  Interaction: Q01995; IntAct: EBI-26878675; Score: 0.35
DE  Interaction: Q8NAG6; IntAct: EBI-27052189; Score: 0.40
DE  Interaction: P42166; IntAct: EBI-27052224; Score: 0.40
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q99502; IntAct: EBI-27113432; Score: 0.35
DE  Interaction: P11831; IntAct: EBI-28997377; Score: 0.35
DE  Interaction: P23769; IntAct: EBI-29000495; Score: 0.35
DE  Interaction: P40763; IntAct: EBI-29000558; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-29373058; Score: 0.35
DE  Interaction: P08047; IntAct: EBI-29385496; Score: 0.35
DE  Interaction: P21709; IntAct: EBI-32717758; Score: 0.35
DE  Interaction: P54764; IntAct: EBI-32717864; Score: 0.35
DE  Interaction: P54756; IntAct: EBI-32717888; Score: 0.35
DE  Interaction: Q15375; IntAct: EBI-32718158; Score: 0.35
DE  Interaction: P29322; IntAct: EBI-32718189; Score: 0.35
DE  Interaction: P29323; IntAct: EBI-32718255; Score: 0.35
DE  Interaction: P21802; IntAct: EBI-32718470; Score: 0.35
DE  Interaction: P22607; IntAct: EBI-32718522; Score: 0.35
DE  Interaction: P17948; IntAct: EBI-32718591; Score: 0.35
DE  Interaction: P36888; IntAct: EBI-32718602; Score: 0.35
DE  Interaction: Q12866; IntAct: EBI-32719029; Score: 0.35
DE  Interaction: Q16288; IntAct: EBI-32719212; Score: 0.35
DE  Interaction: P08581; IntAct: EBI-32723963; Score: 0.27
GO  GO:0000785;
GO  GO:0000793;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0003690;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0097726;
GO  GO:0008022;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0006325;
GO  GO:0030261;
GO  GO:0007059;
GO  GO:0007084;
GO  GO:0045824;
GO  GO:0010836;
GO  GO:0032480;
GO  GO:0045071;
GO  GO:0006979;
GO  GO:0009615;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGC
SQ  LREWCDAFL
//
ID  O54962;
PN  Barrier-to-autointegration factor, N-terminally processed;
GN  Banf1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O75531}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000250|UniProtKB:O75531}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus. May be included in HIV-1 virions via its interaction with viral GAG polyprotein. {ECO:0000250|UniProtKB:O75531}.
DR  UNIPROT: O54962;
DR  UNIPROT: Q542E6;
DR  Pfam: PF02961;
DE  Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA (By similarity). Contains two non-specific double-stranded DNA (dsDNA)- binding sites which promote DNA cross-bridging (By similarity). Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner (By similarity). Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface (By similarity). Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity (PubMed:32156810). Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses (By similarity). Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP- ribosyltransferase activity of PARP1 (By similarity). Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy (By similarity). {ECO:0000250|UniProtKB:O75531, ECO:0000269|PubMed:32156810}.
DE  Reference Proteome: Yes;
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885060; Score: 0.35
GO  GO:0000785;
GO  GO:0000793;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0003690;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0097726;
GO  GO:0008022;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0006325;
GO  GO:0030261;
GO  GO:0007059;
GO  GO:0015074;
GO  GO:0075713;
GO  GO:0007084;
GO  GO:0045824;
GO  GO:0010836;
GO  GO:0032480;
GO  GO:0045071;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGC
SQ  LREWCDAFL
//
ID  Q5RBU9;
PN  Barrier-to-autointegration factor, N-terminally processed;
GN  BANF1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O75531}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000250|UniProtKB:O75531}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus. May be included in HIV-1 virions via its interaction with viral GAG polyprotein. {ECO:0000250|UniProtKB:O75531}.
DR  UNIPROT: Q5RBU9;
DR  Pfam: PF02961;
DE  Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication. {ECO:0000250|UniProtKB:O75531}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0000793;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0003690;
GO  GO:0019899;
GO  GO:0097726;
GO  GO:0008022;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0006325;
GO  GO:0007084;
GO  GO:0045824;
GO  GO:0010836;
GO  GO:0032480;
GO  GO:0045071;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGC
SQ  LREWCDAFL
//
ID  Q9R1T1;
PN  Barrier-to-autointegration factor, N-terminally processed;
GN  Banf1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O75531}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000250|UniProtKB:O75531}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus. May be included in HIV-1 virions via its interaction with viral GAG polyprotein. {ECO:0000250|UniProtKB:O75531}.
DR  UNIPROT: Q9R1T1;
DR  Pfam: PF02961;
DE  Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. {ECO:0000250|UniProtKB:O75531}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0000793;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0003690;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0097726;
GO  GO:0008022;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0006325;
GO  GO:0030261;
GO  GO:0007059;
GO  GO:0015074;
GO  GO:0007084;
GO  GO:0045824;
GO  GO:0010836;
GO  GO:0032480;
GO  GO:0045071;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTSQKHRDFVAEPMGEKPVGSLAGIGDALGKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGC
SQ  LREWCDAFL
//
ID  O95999;
PN  B-cell lymphoma/leukemia 10;
GN  BCL10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17287217}. Membrane raft {ECO:0000269|PubMed:17287217}. Note=Appears to have a perinuclear, compact and filamentous pattern of expression. Also found in the nucleus of several types of tumor cells. Colocalized with DPP4 in membrane rafts. {ECO:0000269|PubMed:17287217}.
DR  UNIPROT: O95999;
DR  UNIPROT: Q5VUF1;
DR  PDB: 2MB9;
DR  PDB: 6BZE;
DR  PDB: 6GK2;
DR  Pfam: PF00619;
DR  PROSITE: PS50209;
DR  OMIM: 137245;
DR  OMIM: 603517;
DR  OMIM: 616098;
DR  DisGeNET: 8915;
DE  Function: Plays a key role in both adaptive and innate immune signaling by bridging CARD domain-containing proteins to immune activation (PubMed:10187770, PubMed:10364242, PubMed:10400625, PubMed:25365219, PubMed:24074955). Acts by channeling adaptive and innate immune signaling downstream of CARD domain-containing proteins CARD9, CARD11 and CARD14 to activate NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:24074955). Recruited by activated CARD domain-containing proteins: homooligomerized CARD domain-containing proteins form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10, subsequent recruitment of MALT1 and formation of a CBM complex (PubMed:24074955). This leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:18287044, PubMed:27777308, PubMed:24074955). Activated by CARD9 downstream of C-type lectin receptors; CARD9-mediated signals are essential for antifungal immunity (PubMed:26488816). Activated by CARD11 downstream of T-cell receptor (TCR) and B-cell receptor (BCR) (PubMed:18264101, PubMed:18287044, PubMed:27777308, PubMed:24074955). Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK (PubMed:10187815). {ECO:0000269|PubMed:10187770, ECO:0000269|PubMed:10187815, ECO:0000269|PubMed:10364242, ECO:0000269|PubMed:10400625, ECO:0000269|PubMed:18264101, ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:24074955, ECO:0000269|PubMed:25365219, ECO:0000269|PubMed:26488816, ECO:0000269|PubMed:27777308}.
DE  Disease: Note=A chromosomal aberration involving BCL10 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(1;14)(p22;q32). Although the BCL10/IgH translocation leaves the coding region of BCL10 intact, frequent BCL10 mutations could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions. {ECO:0000269|PubMed:9989495}. Immunodeficiency 37 (IMD37) [MIM:616098]: A form of primary combined immunodeficiency, a group of disorders characterized by severe recurrent infections, with normal numbers or an absence of T and B lymphocytes, and impaired cellular and humoral immunity. IMD37 is characterized by hypogammaglobulinemia without lymphopenia, but with profoundly reduced memory B cells and memory T cells, and increased numbers of circulating naive lymphocytes. Inheritance is autosomal recessive. {ECO:0000269|PubMed:25365219}. Note=The disease is caused by variants affecting the gene represented in this entry. Lymphoma, mucosa-associated lymphoid type (MALTOMA) [MIM:137245]: A subtype of non-Hodgkin lymphoma, originating in mucosa- associated lymphoid tissue. MALT lymphomas occur most commonly in the gastro-intestinal tract but have been described in a variety of extranodal sites including the ocular adnexa, salivary gland, thyroid, lung, thymus, and breast. Histologically, they are characterized by an infiltrate of small to medium-sized lymphocytes with abundant cytoplasm and irregularly shaped nuclei. Scattered transformed blasts (large cells) also are present. Non-malignant reactive follicles are observed frequently. A pivotal feature is the presence of lymphoepithelial lesions, with invasion and partial destruction of mucosal glands and crypts by aggregates of tumor cells. {ECO:0000269|PubMed:9989495}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q96LW7; IntAct: EBI-7443946; Score: 0.60
DE  Interaction: P31749; IntAct: EBI-958921; Score: 0.69
DE  Interaction: P20749; IntAct: EBI-959017; Score: 0.52
DE  Interaction: Q14525; IntAct: EBI-1077929; Score: 0.00
DE  Interaction: P62807; IntAct: EBI-1084020; Score: 0.00
DE  Interaction: Q9Y6K9; IntAct: EBI-7334387; Score: 0.79
DE  Interaction: Q04759; IntAct: EBI-7334619; Score: 0.40
DE  Interaction: Q9BXL7; IntAct: EBI-7661911; Score: 0.86
DE  Interaction: Q9UDY8; IntAct: EBI-7661911; Score: 0.92
DE  Interaction: Q92905; IntAct: EBI-7006208; Score: 0.35
DE  Interaction: P50750; IntAct: EBI-3906788; Score: 0.37
DE  Interaction: Q13261; IntAct: EBI-3910825; Score: 0.37
DE  Interaction: Q07955; IntAct: EBI-3913288; Score: 0.37
DE  Interaction: Q8WUM9; IntAct: EBI-3913379; Score: 0.37
DE  Interaction: O14745; IntAct: EBI-3914094; Score: 0.37
DE  Interaction: Q9BZD6; IntAct: EBI-3921644; Score: 0.37
DE  Interaction: Q8N6Y0; IntAct: EBI-3941289; Score: 0.44
DE  Interaction: Q14790; IntAct: EBI-6253103; Score: 0.35
DE  Interaction: Q9H257; IntAct: EBI-6665220; Score: 0.55
DE  Interaction: Q9ULZ3; IntAct: EBI-6253113; Score: 0.35
DE  Interaction: Q92688; IntAct: EBI-8995108; Score: 0.37
DE  Interaction: Q14032; IntAct: EBI-8995121; Score: 0.37
DE  Interaction: P09467; IntAct: EBI-8995160; Score: 0.37
DE  Interaction: Q9BU70; IntAct: EBI-8995134; Score: 0.37
DE  Interaction: O60729; IntAct: EBI-8995147; Score: 0.37
DE  Interaction: Q9BXL5; IntAct: EBI-8995173; Score: 0.37
DE  Interaction: Q9P1Z9; IntAct: EBI-8995186; Score: 0.37
DE  Interaction: Q9NR45; IntAct: EBI-8995209; Score: 0.37
DE  Interaction: P20936; IntAct: EBI-8995222; Score: 0.37
DE  Interaction: P01137; IntAct: EBI-8995235; Score: 0.37
DE  Interaction: Q12933; IntAct: EBI-10193048; Score: 0.81
DE  Interaction: O95999; IntAct: EBI-10483822; Score: 0.75
DE  Interaction: Q05513; IntAct: EBI-10689973; Score: 0.52
DE  Interaction: P06930; IntAct: EBI-11737514; Score: 0.37
DE  Interaction: P33215; IntAct: EBI-10993316; Score: 0.35
DE  Interaction: O95684; IntAct: EBI-11381827; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9Y2V7; IntAct: EBI-11773232; Score: 0.70
DE  Interaction: Q9H0F6; IntAct: EBI-11692014; Score: 0.40
DE  Interaction: Q66677; IntAct: EBI-11709450; Score: 0.51
DE  Interaction: Q9Y297; IntAct: EBI-15618375; Score: 0.35
DE  Interaction: O14920; IntAct: EBI-15618375; Score: 0.35
DE  Interaction: P48729; IntAct: EBI-15748832; Score: 0.35
DE  Interaction: P17813; IntAct: EBI-22197897; Score: 0.35
DE  Interaction: Q96PU8; IntAct: EBI-26969026; Score: 0.35
GO  GO:0032449;
GO  GO:0005737;
GO  GO:0005881;
GO  GO:0005829;
GO  GO:0001772;
GO  GO:0005764;
GO  GO:0045121;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0002096;
GO  GO:0032991;
GO  GO:0050700;
GO  GO:0019899;
GO  GO:0140296;
GO  GO:0042802;
GO  GO:0019900;
GO  GO:0051059;
GO  GO:0002020;
GO  GO:0008022;
GO  GO:0043422;
GO  GO:0019901;
GO  GO:0043621;
GO  GO:0044877;
GO  GO:0003713;
GO  GO:0031625;
GO  GO:0002250;
GO  GO:0061760;
GO  GO:0001783;
GO  GO:0008219;
GO  GO:0006968;
GO  GO:0071222;
GO  GO:0071260;
GO  GO:0007249;
GO  GO:0016064;
GO  GO:0045087;
GO  GO:0031663;
GO  GO:0002906;
GO  GO:0001843;
GO  GO:0043065;
GO  GO:0043280;
GO  GO:0045893;
GO  GO:2001238;
GO  GO:0043123;
GO  GO:0032755;
GO  GO:0032757;
GO  GO:0033674;
GO  GO:0032761;
GO  GO:0032765;
GO  GO:0051092;
GO  GO:0042327;
GO  GO:0031398;
GO  GO:0050870;
GO  GO:0050862;
GO  GO:0051260;
GO  GO:0032094;
GO  GO:0070231;
GO  GO:0050852;
GO  GO:0002224;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEPTAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLD
SQ  TLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFPDGATNNLSRSNSDESNFSEKLRASTVMYHPEGES
SQ  STTPFFSTNSSLNLPVLEVGRTENTIFSSTTLPRPGDPGAPPLPPDLQLEEEGTCANSSEMFLPLRSRTVSRQ
//
ID  Q9QYN5;
PN  B-cell lymphoma/leukemia 10;
GN  Bcl10;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95999}. Membrane raft {ECO:0000250|UniProtKB:O95999}. Note=Appears to have a perinuclear, compact and filamentous pattern of expression. Also found in the nucleus of several types of tumor cells. Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:O95999}.
DR  UNIPROT: Q9QYN5;
DR  Pfam: PF00619;
DR  PROSITE: PS50209;
DE  Function: Plays a key role in both adaptive and innate immune signaling by bridging CARD domain-containing proteins to immune activation. Acts by channeling adaptive and innate immune signaling downstream of CARD domain-containing proteins CARD9, CARD11 and CARD14 to activate NF- kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines. Recruited by activated CARD domain-containing proteins: homooligomerized CARD domain-containing proteins form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10, subsequent recruitment of MALT1 and formation of a CBM complex. This leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines. Activated by CARD9 downstream of C-type lectin receptors; CARD9-mediated signals are essential for antifungal immunity. Activated by CARD11 downstream of T- cell receptor (TCR) and B-cell receptor (BCR). Promotes apoptosis, pro- caspase-9 maturation and activation of NF-kappa-B via NIK and IKK. {ECO:0000250|UniProtKB:O95999}.
DE  Reference Proteome: Yes;
GO  GO:0032449;
GO  GO:0005737;
GO  GO:0005881;
GO  GO:0005829;
GO  GO:0001772;
GO  GO:0005764;
GO  GO:0045121;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0002096;
GO  GO:0032991;
GO  GO:0050700;
GO  GO:0019899;
GO  GO:0140296;
GO  GO:0042802;
GO  GO:0019209;
GO  GO:0019900;
GO  GO:0051059;
GO  GO:0002020;
GO  GO:0008022;
GO  GO:0043422;
GO  GO:0019901;
GO  GO:0043621;
GO  GO:0044877;
GO  GO:0003713;
GO  GO:0031625;
GO  GO:0002250;
GO  GO:0061760;
GO  GO:0001783;
GO  GO:0008219;
GO  GO:0006968;
GO  GO:0071222;
GO  GO:0071260;
GO  GO:0007249;
GO  GO:0016064;
GO  GO:0045087;
GO  GO:0031663;
GO  GO:0002906;
GO  GO:0001843;
GO  GO:0043065;
GO  GO:0043280;
GO  GO:0001819;
GO  GO:0045893;
GO  GO:2001238;
GO  GO:0043123;
GO  GO:0032757;
GO  GO:0051092;
GO  GO:0042327;
GO  GO:0031398;
GO  GO:0050870;
GO  GO:0050862;
GO  GO:0051260;
GO  GO:0050856;
GO  GO:0032094;
GO  GO:0009620;
GO  GO:0070231;
GO  GO:0050852;
GO  GO:0002224;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEAPAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLD
SQ  TLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFAAGATNNLSRSNSDESNFSEKQRPSTVIYHPEGES
SQ  STAPFFSTESSLNLPVLEVGRLENSSFSSASLPRPGDPGAPPLPPDLRLEEGGSCGNSSEMFLPLRSRALSRQ
//
ID  O02718;
PN  Apoptosis regulator Bcl-2;
GN  BCL2;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single- pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}.
DR  UNIPROT: O02718;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DE  Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function. May attenuate inflammation by impairing NLRP1- inflammasome activation, hence CASP1 activation and IL1B release. {ECO:0000250|UniProtKB:P10415}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0097192;
GO  GO:0008630;
GO  GO:0043066;
GO  GO:0010507;
GO  GO:0032848;
GO  GO:2001243;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0001836;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAHAGGTGYDNREIVMKYIHYKLSQRGYEWDAGDAGAAPPGAAPAPGILSSQPGRTPAPSRTSPPPPPAAAAGPAPSPVP
SQ  PVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARERFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLV
SQ  DSIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKALLSLALVGACITLGAYLGHK
//
ID  Q6R755;
PN  Apoptosis regulator Bcl-2;
GN  BCL2;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single- pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}.
DR  UNIPROT: Q6R755;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DE  Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function. May attenuate inflammation by impairing NLRP1- inflammasome activation, hence CASP1 activation and IL1B release. {ECO:0000250|UniProtKB:P10415}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0031965;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0097192;
GO  GO:0008630;
GO  GO:0010507;
GO  GO:2001243;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDVGDVDAAPLGAAPTPGIFSFQPESNPTPAVHRDMAARTSPLRPIVATTG
SQ  PTLSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVN
SQ  REMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPTMQPLFDFSWLSLKALLSLALVGACITLGAYLGHK
//
ID  Q00709;
PN  Apoptosis regulator Bcl-2;
GN  BCL2;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single- pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}.
DR  UNIPROT: Q00709;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DE  Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1).
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0043209;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0046930;
GO  GO:0051434;
GO  GO:0015267;
GO  GO:0016248;
GO  GO:0140297;
GO  GO:0002020;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0051721;
GO  GO:0043565;
GO  GO:0031625;
GO  GO:0007015;
GO  GO:0031103;
GO  GO:0007409;
GO  GO:0001783;
GO  GO:0001782;
GO  GO:0002326;
GO  GO:0042100;
GO  GO:0050853;
GO  GO:0001662;
GO  GO:0001658;
GO  GO:0060402;
GO  GO:0043375;
GO  GO:0098609;
GO  GO:0042149;
GO  GO:0071456;
GO  GO:0071310;
GO  GO:0021747;
GO  GO:0051607;
GO  GO:0097048;
GO  GO:0048546;
GO  GO:0043583;
GO  GO:0032469;
GO  GO:1904019;
GO  GO:0097192;
GO  GO:0008625;
GO  GO:0048041;
GO  GO:0000082;
GO  GO:0022612;
GO  GO:0032835;
GO  GO:0060218;
GO  GO:0048873;
GO  GO:0008630;
GO  GO:0070059;
GO  GO:0008631;
GO  GO:0070306;
GO  GO:0002320;
GO  GO:0008584;
GO  GO:0006582;
GO  GO:0030318;
GO  GO:0014031;
GO  GO:0001656;
GO  GO:0097049;
GO  GO:0033028;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:0010507;
GO  GO:0002903;
GO  GO:0010523;
GO  GO:0030308;
GO  GO:0030336;
GO  GO:0032848;
GO  GO:2000669;
GO  GO:1904036;
GO  GO:2001240;
GO  GO:2000134;
GO  GO:2001243;
GO  GO:2000672;
GO  GO:0033033;
GO  GO:0030279;
GO  GO:0033689;
GO  GO:2000378;
GO  GO:0046671;
GO  GO:0070233;
GO  GO:0042551;
GO  GO:0048599;
GO  GO:0035265;
GO  GO:0001503;
GO  GO:0033687;
GO  GO:0001541;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0048753;
GO  GO:0030890;
GO  GO:0043085;
GO  GO:0030307;
GO  GO:0045636;
GO  GO:0040018;
GO  GO:0014042;
GO  GO:0033138;
GO  GO:0048743;
GO  GO:0014911;
GO  GO:0009791;
GO  GO:0006470;
GO  GO:0000209;
GO  GO:0072593;
GO  GO:0001952;
GO  GO:0010468;
GO  GO:0010559;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0006808;
GO  GO:0032880;
GO  GO:0031647;
GO  GO:0022898;
GO  GO:0045069;
GO  GO:0001836;
GO  GO:0003014;
GO  GO:0034097;
GO  GO:0010332;
GO  GO:0051384;
GO  GO:0042542;
GO  GO:0010039;
GO  GO:0002931;
GO  GO:1904373;
GO  GO:0035094;
GO  GO:0009636;
GO  GO:0010224;
GO  GO:0009410;
GO  GO:0046666;
GO  GO:0048741;
GO  GO:0014909;
GO  GO:0048536;
GO  GO:0048864;
GO  GO:0070231;
GO  GO:0033077;
GO  GO:0043029;
GO  GO:0048538;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAHPGRRGYDNREIVLKYIHYKLSQRGYDWAAGEDRPPVPPAPAPAAAPAAVAAAGASSHHRPEPPGSAAASEVPPAEGL
SQ  RPAPPGVHLALRQAGDEFSRRYQRDFAQMSGQLHLTPFTAHGRFVAVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREM
SQ  SPLVDNIATWMTEYLNRHLHNWIQDNGGWDAFVELYGNSMRPLFDFSWISLKTILSLVLVGACITLGAYLGHK
//
ID  Q9JJV8;
PN  Apoptosis regulator Bcl-2;
GN  BCL2;
OS  10029;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single- pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}.
DR  UNIPROT: Q9JJV8;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DE  Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function. May attenuate inflammation by impairing NLRP1- inflammasome activation, hence CASP1 activation and IL1B release. {ECO:0000250|UniProtKB:P10415}.
DE  Reference Proteome: No;
DE  Interaction: Q14790; IntAct: EBI-1749111; Score: 0.40
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005741;
GO  GO:0043209;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0046930;
GO  GO:0051434;
GO  GO:0015267;
GO  GO:0016248;
GO  GO:0140297;
GO  GO:0042802;
GO  GO:0002020;
GO  GO:0046982;
GO  GO:0051721;
GO  GO:0043565;
GO  GO:0031625;
GO  GO:0007015;
GO  GO:0031103;
GO  GO:0007409;
GO  GO:0001783;
GO  GO:0001782;
GO  GO:0002326;
GO  GO:0042100;
GO  GO:0050853;
GO  GO:0001662;
GO  GO:0001658;
GO  GO:0060402;
GO  GO:0043375;
GO  GO:0098609;
GO  GO:0042149;
GO  GO:0071456;
GO  GO:0071310;
GO  GO:0021747;
GO  GO:0051607;
GO  GO:0097048;
GO  GO:0048546;
GO  GO:0043583;
GO  GO:0032469;
GO  GO:1904019;
GO  GO:0097192;
GO  GO:0008625;
GO  GO:0048041;
GO  GO:0000082;
GO  GO:0022612;
GO  GO:0032835;
GO  GO:0031069;
GO  GO:0060218;
GO  GO:0048873;
GO  GO:0008630;
GO  GO:0070059;
GO  GO:0008631;
GO  GO:0002320;
GO  GO:0008584;
GO  GO:0006582;
GO  GO:0030318;
GO  GO:0014031;
GO  GO:0001656;
GO  GO:0097049;
GO  GO:0033028;
GO  GO:2000811;
GO  GO:0010507;
GO  GO:0002903;
GO  GO:0010523;
GO  GO:0030308;
GO  GO:0030336;
GO  GO:0032848;
GO  GO:2000669;
GO  GO:1904036;
GO  GO:2001240;
GO  GO:2000134;
GO  GO:2001243;
GO  GO:2000672;
GO  GO:0033033;
GO  GO:0030279;
GO  GO:0033689;
GO  GO:2000378;
GO  GO:0046671;
GO  GO:0070233;
GO  GO:0042551;
GO  GO:0048599;
GO  GO:0035265;
GO  GO:0001503;
GO  GO:0033687;
GO  GO:0001541;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0048753;
GO  GO:0030890;
GO  GO:0043085;
GO  GO:0030307;
GO  GO:0045636;
GO  GO:0040018;
GO  GO:0014042;
GO  GO:0033138;
GO  GO:0048743;
GO  GO:0014911;
GO  GO:0009791;
GO  GO:0006470;
GO  GO:0000209;
GO  GO:0072593;
GO  GO:0001952;
GO  GO:0010468;
GO  GO:0010559;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0006808;
GO  GO:0032880;
GO  GO:0031647;
GO  GO:0022898;
GO  GO:0045069;
GO  GO:0001836;
GO  GO:0003014;
GO  GO:0034097;
GO  GO:0010332;
GO  GO:0051384;
GO  GO:0042542;
GO  GO:0010039;
GO  GO:0002931;
GO  GO:1904373;
GO  GO:0035094;
GO  GO:0009636;
GO  GO:0010224;
GO  GO:0009410;
GO  GO:0046666;
GO  GO:0048741;
GO  GO:0014909;
GO  GO:0048536;
GO  GO:0048864;
GO  GO:0070231;
GO  GO:0033077;
GO  GO:0043029;
GO  GO:0048538;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDVGDVDAAPLGAAPTPGIFSFQPESNPTPAVHRDMAARTSPLRPIVATTG
SQ  PTLSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVN
SQ  REMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSVRPLFDFSWLSLKTLLSLALVGACITLGTYLGHK
//
ID  P10415;
PN  Apoptosis regulator Bcl-2;
GN  BCL2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000269|PubMed:21358617, ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21358617, ECO:0000269|PubMed:2250705}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}.
DR  UNIPROT: P10415;
DR  UNIPROT: C9JHD5;
DR  UNIPROT: P10416;
DR  UNIPROT: Q13842;
DR  UNIPROT: Q16197;
DR  PDB: 1G5M;
DR  PDB: 1GJH;
DR  PDB: 1YSW;
DR  PDB: 2O21;
DR  PDB: 2O22;
DR  PDB: 2O2F;
DR  PDB: 2W3L;
DR  PDB: 2XA0;
DR  PDB: 4AQ3;
DR  PDB: 4IEH;
DR  PDB: 4LVT;
DR  PDB: 4LXD;
DR  PDB: 4MAN;
DR  PDB: 5AGW;
DR  PDB: 5AGX;
DR  PDB: 5FCG;
DR  PDB: 5JSN;
DR  PDB: 5VAU;
DR  PDB: 5VAX;
DR  PDB: 5VAY;
DR  PDB: 6GL8;
DR  PDB: 6IWB;
DR  PDB: 6O0K;
DR  PDB: 6O0L;
DR  PDB: 6O0M;
DR  PDB: 6O0O;
DR  PDB: 6O0P;
DR  PDB: 7LHB;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DR  OMIM: 151430;
DR  DisGeNET: 596;
DE  Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells (PubMed:1508712, PubMed:8183370). Regulates cell death by controlling the mitochondrial membrane permeability (PubMed:11368354). Appears to function in a feedback loop system with caspases (PubMed:11368354). Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1) (PubMed:11368354). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function (PubMed:18570871, PubMed:21358617, PubMed:20889974). May attenuate inflammation by impairing NLRP1- inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785). {ECO:0000269|PubMed:1508712, ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:18570871, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:21358617, ECO:0000269|PubMed:8183370, ECO:0000303|PubMed:11368354}.
DE  Disease: Note=A chromosomal aberration involving BCL2 has been found in chronic lymphatic leukemia. Translocation t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations found in non-Hodgkin lymphomas carrying the chromosomal translocation could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions. {ECO:0000269|PubMed:2875799, ECO:0000269|PubMed:3285301}.
DE  Reference Proteome: Yes;
DE  Interaction: O60238; IntAct: EBI-850662; Score: 0.44
DE  Interaction: O54918; IntAct: EBI-707531; Score: 0.44
DE  Interaction: Q9DAJ5; IntAct: EBI-526356; Score: 0.35
DE  Interaction: P51572; IntAct: EBI-77682; Score: 0.52
DE  Interaction: P28482; IntAct: EBI-7210282; Score: 0.49
DE  Interaction: P67775; IntAct: EBI-7210303; Score: 0.49
DE  Interaction: P45983; IntAct: EBI-7497436; Score: 0.31
DE  Interaction: Q14318; IntAct: EBI-7497544; Score: 0.51
DE  Interaction: P55957; IntAct: EBI-519684; Score: 0.87
DE  Interaction: Q9BXH1; IntAct: EBI-707957; Score: 0.82
DE  Interaction: P63098; IntAct: EBI-7517885; Score: 0.49
DE  Interaction: Q07813; IntAct: EBI-700706; Score: 0.40
DE  Interaction: Q07812; IntAct: EBI-700753; Score: 0.94
DE  Interaction: Q16611; IntAct: EBI-700762; Score: 0.61
DE  Interaction: Q92934; IntAct: EBI-700785; Score: 0.81
DE  Interaction: Q13323; IntAct: EBI-700803; Score: 0.82
DE  Interaction: P10415; IntAct: EBI-700826; Score: 0.59
DE  Interaction: O43521; IntAct: EBI-707839; Score: 0.92
DE  Interaction: Q91ZE9; IntAct: EBI-708044; Score: 0.62
DE  Interaction: Q61337; IntAct: EBI-709166; Score: 0.72
DE  Interaction: Q12982; IntAct: EBI-849945; Score: 0.37
DE  Interaction: Q12983; IntAct: EBI-849952; Score: 0.37
DE  Interaction: O60551; IntAct: EBI-8173465; Score: 0.40
DE  Interaction: Q63690; IntAct: EBI-8496082; Score: 0.40
DE  Interaction: P62136; IntAct: EBI-1206840; Score: 0.00
DE  Interaction: P36873; IntAct: EBI-1207036; Score: 0.00
DE  Interaction: P62140; IntAct: EBI-1207176; Score: 0.00
DE  Interaction: Q86Y07; IntAct: EBI-1207847; Score: 0.37
DE  Interaction: Q9C000; IntAct: EBI-1246113; Score: 0.75
DE  Interaction: Q14457; IntAct: EBI-5234827; Score: 0.95
DE  Interaction: Q9H2V7; IntAct: EBI-1386538; Score: 0.46
DE  Interaction: O15304; IntAct: EBI-1393040; Score: 0.40
DE  Interaction: Q14790; IntAct: EBI-1749080; Score: 0.37
DE  Interaction: P22736; IntAct: EBI-2126295; Score: 0.67
DE  Interaction: Q07817; IntAct: EBI-2126646; Score: 0.44
DE  Interaction: P04637; IntAct: EBI-7044574; Score: 0.56
DE  Interaction: O15151; IntAct: EBI-7044604; Score: 0.50
DE  Interaction: Q8N5K1; IntAct: EBI-7676229; Score: 0.54
DE  Interaction: Q0WGQ5; IntAct: EBI-2874959; Score: 0.00
DE  Interaction: P27797; IntAct: EBI-8537109; Score: 0.35
DE  Interaction: P38646; IntAct: EBI-8537109; Score: 0.35
DE  Interaction: Q07820; IntAct: EBI-8537109; Score: 0.35
DE  Interaction: Q9C0C7; IntAct: EBI-8600088; Score: 0.66
DE  Interaction: Q13794; IntAct: EBI-4370379; Score: 0.54
DE  Interaction: Q96LC9; IntAct: EBI-5488187; Score: 0.40
DE  Interaction: P29117; IntAct: EBI-6465503; Score: 0.40
DE  Interaction: P30405; IntAct: EBI-6465542; Score: 0.37
DE  Interaction: Q9NYF8; IntAct: EBI-6621256; Score: 0.50
DE  Interaction: P38398; IntAct: EBI-8757170; Score: 0.38
DE  Interaction: P0DM65; IntAct: EBI-8839562; Score: 0.40
DE  Interaction: A8MW95; IntAct: EBI-8839552; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-10055396; Score: 0.44
DE  Interaction: Q7L3V2; IntAct: EBI-11509550; Score: 0.35
DE  Interaction: Q13625; IntAct: EBI-15723849; Score: 0.65
DE  Interaction: P11881; IntAct: EBI-15801106; Score: 0.52
DE  Interaction: Q14643; IntAct: EBI-15801089; Score: 0.40
DE  Interaction: P21796; IntAct: EBI-15801214; Score: 0.40
DE  Interaction: Q92570; IntAct: EBI-20939354; Score: 0.40
DE  Interaction: P59635; IntAct: EBI-25495801; Score: 0.40
DE  Interaction: P00441; IntAct: EBI-25934648; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25936674; Score: 0.56
DE  Interaction: Q9HB09; IntAct: EBI-27086233; Score: 0.37
DE  Interaction: Q13619; IntAct: EBI-30863570; Score: 0.35
DE  Interaction: Q8WV16; IntAct: EBI-30863977; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0043209;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0046930;
GO  GO:0032991;
GO  GO:0051434;
GO  GO:0015267;
GO  GO:0016248;
GO  GO:0140297;
GO  GO:0042802;
GO  GO:0060090;
GO  GO:0002020;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0051721;
GO  GO:0043565;
GO  GO:0031625;
GO  GO:0007015;
GO  GO:0006915;
GO  GO:0031103;
GO  GO:0007409;
GO  GO:0001783;
GO  GO:0001782;
GO  GO:0002326;
GO  GO:0042100;
GO  GO:0050853;
GO  GO:0001662;
GO  GO:0001658;
GO  GO:0060402;
GO  GO:0043375;
GO  GO:0098609;
GO  GO:0006974;
GO  GO:0042149;
GO  GO:0071456;
GO  GO:0071310;
GO  GO:0021747;
GO  GO:0051607;
GO  GO:0097048;
GO  GO:0048546;
GO  GO:0043583;
GO  GO:0032469;
GO  GO:1904019;
GO  GO:0097192;
GO  GO:0008625;
GO  GO:0007565;
GO  GO:0048041;
GO  GO:0000082;
GO  GO:0022612;
GO  GO:0032835;
GO  GO:0031069;
GO  GO:0060218;
GO  GO:0048873;
GO  GO:0006959;
GO  GO:0008630;
GO  GO:0070059;
GO  GO:0008631;
GO  GO:0002320;
GO  GO:0008584;
GO  GO:0006582;
GO  GO:0030318;
GO  GO:0014031;
GO  GO:0001656;
GO  GO:0097049;
GO  GO:0033028;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:2001234;
GO  GO:0010507;
GO  GO:0002903;
GO  GO:0010523;
GO  GO:0030308;
GO  GO:0030336;
GO  GO:0032848;
GO  GO:2000669;
GO  GO:1904036;
GO  GO:2001240;
GO  GO:2000134;
GO  GO:2001243;
GO  GO:1902166;
GO  GO:0051902;
GO  GO:2000672;
GO  GO:0033033;
GO  GO:0043524;
GO  GO:0030279;
GO  GO:0033689;
GO  GO:2000378;
GO  GO:0046671;
GO  GO:0070233;
GO  GO:0051402;
GO  GO:0042551;
GO  GO:0048599;
GO  GO:0035265;
GO  GO:0001503;
GO  GO:0033687;
GO  GO:0001541;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0048753;
GO  GO:0030890;
GO  GO:0043085;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0045636;
GO  GO:0040018;
GO  GO:0014042;
GO  GO:0033138;
GO  GO:0048743;
GO  GO:0014911;
GO  GO:0009791;
GO  GO:0006470;
GO  GO:0000209;
GO  GO:0072593;
GO  GO:0051924;
GO  GO:0001952;
GO  GO:0010468;
GO  GO:0010559;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0006808;
GO  GO:0032880;
GO  GO:0031647;
GO  GO:0022898;
GO  GO:0045069;
GO  GO:0001836;
GO  GO:0003014;
GO  GO:0034097;
GO  GO:0010332;
GO  GO:0051384;
GO  GO:0042542;
GO  GO:0010039;
GO  GO:0002931;
GO  GO:1904373;
GO  GO:0035094;
GO  GO:0009314;
GO  GO:0009636;
GO  GO:0010224;
GO  GO:0009410;
GO  GO:0046666;
GO  GO:0048741;
GO  GO:0014909;
GO  GO:0048536;
GO  GO:0048864;
GO  GO:0070231;
GO  GO:0033077;
GO  GO:0043029;
GO  GO:0048538;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGA
SQ  AAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVE
SQ  SVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK
//
ID  P10417;
PN  Apoptosis regulator Bcl-2;
GN  Bcl2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single- pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29020630}.
DR  UNIPROT: P10417;
DR  UNIPROT: P10418;
DR  UNIPROT: Q4VBF6;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DE  Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function (By similarity). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785). {ECO:0000250|UniProtKB:P10415, ECO:0000269|PubMed:17418785}.
DE  Reference Proteome: Yes;
DE  Interaction: P70444; IntAct: EBI-7986755; Score: 0.40
DE  Interaction: P62137; IntAct: EBI-1202230; Score: 0.00
DE  Interaction: P63087; IntAct: EBI-1202999; Score: 0.00
DE  Interaction: Q07813; IntAct: EBI-8067327; Score: 0.57
DE  Interaction: O54918; IntAct: EBI-8538239; Score: 0.51
DE  Interaction: O08734; IntAct: EBI-5394637; Score: 0.40
DE  Interaction: Q61337; IntAct: EBI-5395607; Score: 0.37
DE  Interaction: O88597; IntAct: EBI-10714637; Score: 0.73
DE  Interaction: P63158; IntAct: EBI-10714676; Score: 0.35
DE  Interaction: Q99MI6; IntAct: EBI-15572329; Score: 0.56
DE  Interaction: Q8BWF2; IntAct: EBI-15572373; Score: 0.56
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0030061;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0043209;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046930;
GO  GO:0032991;
GO  GO:0051400;
GO  GO:0051434;
GO  GO:0015267;
GO  GO:0016248;
GO  GO:0140297;
GO  GO:0042802;
GO  GO:0002020;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0051721;
GO  GO:0019903;
GO  GO:0044877;
GO  GO:0043565;
GO  GO:0031625;
GO  GO:0007015;
GO  GO:0009887;
GO  GO:0008637;
GO  GO:0006915;
GO  GO:0031103;
GO  GO:0007409;
GO  GO:0001783;
GO  GO:0030183;
GO  GO:0001782;
GO  GO:0002326;
GO  GO:0042100;
GO  GO:0050853;
GO  GO:0001662;
GO  GO:0001658;
GO  GO:0060402;
GO  GO:0043375;
GO  GO:0016477;
GO  GO:0000902;
GO  GO:0008283;
GO  GO:0098609;
GO  GO:0006874;
GO  GO:0006974;
GO  GO:0042149;
GO  GO:0071456;
GO  GO:0071310;
GO  GO:0021747;
GO  GO:0051607;
GO  GO:0097048;
GO  GO:0048589;
GO  GO:0048066;
GO  GO:0048546;
GO  GO:0043583;
GO  GO:0032469;
GO  GO:1904019;
GO  GO:0051649;
GO  GO:0097192;
GO  GO:0008625;
GO  GO:0048041;
GO  GO:0000082;
GO  GO:0022612;
GO  GO:0032835;
GO  GO:0031069;
GO  GO:0060218;
GO  GO:0030097;
GO  GO:0048873;
GO  GO:0002520;
GO  GO:0008630;
GO  GO:0070059;
GO  GO:0008631;
GO  GO:0001822;
GO  GO:0001776;
GO  GO:0070227;
GO  GO:0002260;
GO  GO:0002320;
GO  GO:0008584;
GO  GO:0006582;
GO  GO:0030318;
GO  GO:0014031;
GO  GO:0001656;
GO  GO:0000278;
GO  GO:0097049;
GO  GO:0033028;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:2001234;
GO  GO:0010507;
GO  GO:0002903;
GO  GO:0010523;
GO  GO:0010667;
GO  GO:0030308;
GO  GO:0030336;
GO  GO:0008285;
GO  GO:0032848;
GO  GO:2000669;
GO  GO:1904036;
GO  GO:2001240;
GO  GO:2000134;
GO  GO:2001243;
GO  GO:0070229;
GO  GO:0045930;
GO  GO:2000672;
GO  GO:0033033;
GO  GO:0043524;
GO  GO:1901215;
GO  GO:0030279;
GO  GO:0033689;
GO  GO:2000378;
GO  GO:0046671;
GO  GO:0070233;
GO  GO:0051402;
GO  GO:0070997;
GO  GO:0042551;
GO  GO:0048599;
GO  GO:0035265;
GO  GO:0001503;
GO  GO:0033687;
GO  GO:0001541;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0048753;
GO  GO:0043473;
GO  GO:0030890;
GO  GO:0043085;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0048087;
GO  GO:0045636;
GO  GO:0040018;
GO  GO:0014042;
GO  GO:0033138;
GO  GO:0048743;
GO  GO:0014911;
GO  GO:0009791;
GO  GO:0006470;
GO  GO:0000209;
GO  GO:0072593;
GO  GO:0042981;
GO  GO:0010506;
GO  GO:0051924;
GO  GO:0050790;
GO  GO:0051726;
GO  GO:0001952;
GO  GO:0048070;
GO  GO:0010468;
GO  GO:0010559;
GO  GO:0040008;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0006808;
GO  GO:0043067;
GO  GO:0032880;
GO  GO:0031647;
GO  GO:0022898;
GO  GO:0045069;
GO  GO:0001836;
GO  GO:0003014;
GO  GO:0034097;
GO  GO:0045471;
GO  GO:0010332;
GO  GO:0051384;
GO  GO:0042542;
GO  GO:0010039;
GO  GO:0002931;
GO  GO:1904373;
GO  GO:0035094;
GO  GO:0006979;
GO  GO:0048545;
GO  GO:0009636;
GO  GO:0010224;
GO  GO:0009410;
GO  GO:0046666;
GO  GO:0048741;
GO  GO:0014909;
GO  GO:0048536;
GO  GO:0048864;
GO  GO:0070231;
GO  GO:0030217;
GO  GO:0033077;
GO  GO:0043029;
GO  GO:0002360;
GO  GO:0048538;
GO  GO:0001657;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDADAAPLGAAPTPGIFSFQPESNPMPAVHRDMAARTSPLRPLVATAG
SQ  PALSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVN
SQ  REMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK
//
ID  P49950;
PN  Apoptosis regulator Bcl-2;
GN  Bcl2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single- pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}.
DR  UNIPROT: P49950;
DR  UNIPROT: Q62837;
DR  UNIPROT: Q64032;
DR  Pfam: PF00452;
DR  Pfam: PF02180;
DR  PROSITE: PS50062;
DR  PROSITE: PS01080;
DR  PROSITE: PS01258;
DR  PROSITE: PS01259;
DR  PROSITE: PS01260;
DR  PROSITE: PS50063;
DE  Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function. May attenuate inflammation by impairing NLRP1- inflammasome activation, hence CASP1 activation and IL1B release. {ECO:0000250|UniProtKB:P10415}.
DE  Reference Proteome: Yes;
DE  Interaction: O88498; IntAct: EBI-79017; Score: 0.37
DE  Interaction: P29117; IntAct: EBI-6465491; Score: 0.40
DE  Interaction: P06536; IntAct: EBI-15756525; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0030061;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0043209;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046930;
GO  GO:0032991;
GO  GO:0051400;
GO  GO:0051434;
GO  GO:0015267;
GO  GO:0016248;
GO  GO:0140297;
GO  GO:0042802;
GO  GO:0002020;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0051721;
GO  GO:0019903;
GO  GO:0044877;
GO  GO:0043565;
GO  GO:0031625;
GO  GO:0007015;
GO  GO:0007568;
GO  GO:0009887;
GO  GO:0008637;
GO  GO:0006915;
GO  GO:0031103;
GO  GO:0007409;
GO  GO:0001783;
GO  GO:0030183;
GO  GO:0001782;
GO  GO:0002326;
GO  GO:0042100;
GO  GO:0050853;
GO  GO:0001662;
GO  GO:0007420;
GO  GO:0001658;
GO  GO:0060402;
GO  GO:0043375;
GO  GO:0016477;
GO  GO:0000902;
GO  GO:0008283;
GO  GO:0098609;
GO  GO:0006874;
GO  GO:0006974;
GO  GO:1902618;
GO  GO:0042149;
GO  GO:0071333;
GO  GO:0070301;
GO  GO:0071456;
GO  GO:0071407;
GO  GO:0071310;
GO  GO:0021987;
GO  GO:0021747;
GO  GO:0051607;
GO  GO:0097048;
GO  GO:0048589;
GO  GO:0048066;
GO  GO:0048546;
GO  GO:0043583;
GO  GO:0032469;
GO  GO:1904019;
GO  GO:0051649;
GO  GO:0097192;
GO  GO:0008625;
GO  GO:0048041;
GO  GO:0000082;
GO  GO:0022612;
GO  GO:0034349;
GO  GO:0032835;
GO  GO:0031069;
GO  GO:0060218;
GO  GO:0030097;
GO  GO:0048873;
GO  GO:0002520;
GO  GO:0008630;
GO  GO:0070059;
GO  GO:0008631;
GO  GO:0001822;
GO  GO:0001776;
GO  GO:0097421;
GO  GO:0070227;
GO  GO:0002260;
GO  GO:0002320;
GO  GO:0008584;
GO  GO:0006582;
GO  GO:0030318;
GO  GO:0014031;
GO  GO:0001656;
GO  GO:0000278;
GO  GO:0097049;
GO  GO:0033028;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:2001234;
GO  GO:0010507;
GO  GO:0002903;
GO  GO:0010523;
GO  GO:0010667;
GO  GO:0030308;
GO  GO:0030336;
GO  GO:0008285;
GO  GO:0032848;
GO  GO:2000669;
GO  GO:1904036;
GO  GO:2001240;
GO  GO:2000134;
GO  GO:2001243;
GO  GO:0070229;
GO  GO:0045930;
GO  GO:2000672;
GO  GO:0033033;
GO  GO:0043524;
GO  GO:1901215;
GO  GO:0030279;
GO  GO:0033689;
GO  GO:2000378;
GO  GO:0046671;
GO  GO:0070233;
GO  GO:0051402;
GO  GO:0070997;
GO  GO:0042551;
GO  GO:0048709;
GO  GO:0048599;
GO  GO:0035265;
GO  GO:0001503;
GO  GO:0033687;
GO  GO:0001541;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0048753;
GO  GO:0043473;
GO  GO:0030890;
GO  GO:0043085;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0048087;
GO  GO:0045636;
GO  GO:0040018;
GO  GO:0014042;
GO  GO:0033138;
GO  GO:0048743;
GO  GO:0014911;
GO  GO:0009791;
GO  GO:0006470;
GO  GO:0000209;
GO  GO:0072593;
GO  GO:0042981;
GO  GO:0010506;
GO  GO:0051924;
GO  GO:0050790;
GO  GO:0051726;
GO  GO:0001952;
GO  GO:0048070;
GO  GO:0010468;
GO  GO:0010559;
GO  GO:0040008;
GO  GO:0046902;
GO  GO:0051881;
GO  GO:0006808;
GO  GO:0043067;
GO  GO:0032880;
GO  GO:0031647;
GO  GO:0022898;
GO  GO:0045069;
GO  GO:0001836;
GO  GO:0003014;
GO  GO:0010044;
GO  GO:1904645;
GO  GO:0031000;
GO  GO:0051591;
GO  GO:0046688;
GO  GO:0051412;
GO  GO:0034097;
GO  GO:0051602;
GO  GO:0036017;
GO  GO:0043627;
GO  GO:0045471;
GO  GO:0051593;
GO  GO:0010332;
GO  GO:0051384;
GO  GO:0009408;
GO  GO:0042542;
GO  GO:0001666;
GO  GO:0010035;
GO  GO:0032868;
GO  GO:0010039;
GO  GO:0002931;
GO  GO:1904373;
GO  GO:0033591;
GO  GO:0034284;
GO  GO:0035094;
GO  GO:0007584;
GO  GO:0014070;
GO  GO:0010033;
GO  GO:0006979;
GO  GO:0043434;
GO  GO:0080184;
GO  GO:0048545;
GO  GO:0009636;
GO  GO:0010224;
GO  GO:0033197;
GO  GO:0009410;
GO  GO:0046666;
GO  GO:0048741;
GO  GO:0014909;
GO  GO:0048536;
GO  GO:0048864;
GO  GO:0070231;
GO  GO:0030217;
GO  GO:0033077;
GO  GO:0043029;
GO  GO:0002360;
GO  GO:0048538;
GO  GO:0001657;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDTGDEDSAPLRAAPTPGIFSFQPESNRTPAVHRDTAARTSPLRPLVANAG
SQ  PALSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVN
SQ  REMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK
//
ID  P20749;
PN  B-cell lymphoma 3 protein;
GN  BCL3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Ubiquitination via 'Lys-63'- linked ubiquitin chains is required for nuclear accumulation. {ECO:0000250}.
DR  UNIPROT: P20749;
DR  PDB: 1K1A;
DR  PDB: 1K1B;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  OMIM: 109560;
DR  DisGeNET: 602;
DE  Function: Contributes to the regulation of transcriptional activation of NF-kappa-B target genes. In the cytoplasm, inhibits the nuclear translocation of the NF-kappa-B p50 subunit. In the nucleus, acts as transcriptional activator that promotes transcription of NF-kappa-B target genes. Contributes to the regulation of cell proliferation (By similarity). {ECO:0000250, ECO:0000269|PubMed:8453667}.
DE  Disease: Note=A chromosomal aberration involving BCL3 may be a cause of B-cell chronic lymphocytic leukemia (B-CLL). Translocation t(14;19)(q32;q13.1) with immunoglobulin gene regions. {ECO:0000269|PubMed:2180580, ECO:0000269|PubMed:7896265}.
DE  Reference Proteome: Yes;
DE  Interaction: O95999; IntAct: EBI-959017; Score: 0.52
DE  Interaction: P06239; IntAct: EBI-7785707; Score: 0.59
DE  Interaction: P06241; IntAct: EBI-7785768; Score: 0.40
DE  Interaction: P56545; IntAct: EBI-3926425; Score: 0.51
DE  Interaction: O15084; IntAct: EBI-5653696; Score: 0.00
DE  Interaction: O00625; IntAct: EBI-10713595; Score: 0.44
DE  Interaction: Q92598; IntAct: EBI-21258808; Score: 0.35
DE  Interaction: Q00653; IntAct: EBI-21258808; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-21258808; Score: 0.35
DE  Interaction: P17066; IntAct: EBI-21258808; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-25907809; Score: 0.56
DE  Interaction: Q13619; IntAct: EBI-30863570; Score: 0.35
GO  GO:0032996;
GO  GO:0033257;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0030496;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0140297;
GO  GO:0042826;
GO  GO:0030674;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0019730;
GO  GO:0006974;
GO  GO:0042742;
GO  GO:0042832;
GO  GO:0030330;
GO  GO:0030198;
GO  GO:0002268;
GO  GO:0002467;
GO  GO:0002455;
GO  GO:0007249;
GO  GO:0042771;
GO  GO:0002315;
GO  GO:0043066;
GO  GO:0045892;
GO  GO:0032717;
GO  GO:0032088;
GO  GO:0046426;
GO  GO:0070233;
GO  GO:0032720;
GO  GO:0045893;
GO  GO:0032729;
GO  GO:0032733;
GO  GO:0045944;
GO  GO:0045727;
GO  GO:0006606;
GO  GO:0042981;
GO  GO:0051101;
GO  GO:1901222;
GO  GO:0010225;
GO  GO:0009615;
GO  GO:0048536;
GO  GO:0070231;
GO  GO:0042088;
GO  GO:0045064;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPRCPAGAMDEGPVDLRTRPKAAGLPGAALPLRKRPLRAPSPEPAAPRGAAGLVVPLDPLRGGCDLPAVPGPPHGLARPE
SQ  ALYYPGALLPLYPTRAMGSPFPLVNLPTPLYPMMCPMEHPLSADIAMATRADEDGDTPLHIAVVQGNLPAVHRLVNLFQQ
SQ  GGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAAPGTLDLEARNY
SQ  DGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRG
SQ  LLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILRGKATRPASTSQPDPSPDRSANTSPESSSRLSSNGLLSASPS
SQ  SSPSQSPPRDPPGFPMAPPNFFLPSPSPPAFLPFAGVLRGPGRPVPPSPAPGGS
//
ID  Q9Z2F6;
PN  B-cell lymphoma 3 protein homolog;
GN  Bcl3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:16713561}. Cytoplasm {ECO:0000269|PubMed:16713561}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16713561}. Note=Ubiquitination via 'Lys-63'-linked ubiquitin chains is required for nuclear accumulation.
DR  UNIPROT: Q9Z2F6;
DR  Pfam: PF00023;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Contributes to the regulation of transcriptional activation of NF-kappa-B target genes. In the cytoplasm, inhibits the nuclear translocation of the NF-kappa-B p50 subunit (By similarity). In the nucleus, acts as transcriptional activator that promotes transcription of NF-kappa-B target genes. Contributes to the regulation of cell proliferation. {ECO:0000250, ECO:0000269|PubMed:16713561}.
DE  Reference Proteome: Yes;
DE  Interaction: Q80TQ2; IntAct: EBI-943890; Score: 0.67
GO  GO:0032996;
GO  GO:0033257;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0030496;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0140297;
GO  GO:0042826;
GO  GO:0030674;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0019730;
GO  GO:0006974;
GO  GO:0042742;
GO  GO:0042832;
GO  GO:0030330;
GO  GO:0030198;
GO  GO:0002268;
GO  GO:0002467;
GO  GO:0002455;
GO  GO:0007249;
GO  GO:0042771;
GO  GO:0002315;
GO  GO:0043066;
GO  GO:0045892;
GO  GO:0032717;
GO  GO:0032088;
GO  GO:0046426;
GO  GO:0070233;
GO  GO:0032720;
GO  GO:0045893;
GO  GO:0032729;
GO  GO:0032733;
GO  GO:0045944;
GO  GO:0045727;
GO  GO:0006606;
GO  GO:0042981;
GO  GO:0051101;
GO  GO:1901222;
GO  GO:0010225;
GO  GO:0009615;
GO  GO:0048536;
GO  GO:0070231;
GO  GO:0042088;
GO  GO:0045064;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPRCPAGAMDEGPVDLRTRPKGTPGAALPLRKRPLRPASPEPATTRSPAGPLDALRSGCDVPVVPGPPHCVARPEALYYQ
SQ  GPLMPIYSTPTMAPHFPLLNLPTHPYSMICPMEHPLSADIAMATRVDEDGDTPLHIAVVQNNIAAVYRILSLFKLGSREV
SQ  DVHNNLRQTPLHLAVITTLPDMVRLLVTAGASPMALDRHGQTAIHLACEHRSPSCLQALLDSATSGSVDLEVRNYEGLTA
SQ  LHVAVNTGCQEAVLLLLERGADIDAVDIKSGRSPLIHAVENNSLNMVQLLLLHGANVNAQMYSGSSALHSASGRGLLPLV
SQ  RTLVRSGADSGLKNCHNDTPLMVARSRRVIDILRGKASRAASGSQPEPSPDQSATNSPESSSRLSSNGLQSSPSSSPSLS
SQ  PPKDAPGFPATPQNFFLPTTSTPAFLPFPGVLRGPGRPVPPSPAPGSS
//
ID  O74907;
PN  Protein bcp1;
GN  bcp1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O74907;
DR  Pfam: PF13862;
DE  Function: Involved in nuclear export, actin cytoskeleton organization and vesicular transport. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0006611;
GO  GO:0000055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAKRHAEENEDTVMSESLKVVDTDFINVDFEFFDPQPIDFHAFKNLLKQLLGYDHTNVNLSALADLILSQPLLGSTVKVD
SQ  GNNSDPYAMLSVINLNTRRDEPVIKQLTSYIISRLAKSNSRLENELQKLLEPNSGSQVGLIVNERLINMPVQVIPPMYNM
SQ  LLEEMQWAINENEPYNFTHYLLLSRTYTEIESKLMDDERPSKKGKKSKKTSGEEVMFFHPEDEQFREVAIDIADYPFANQ
SQ  DFNPDANRVFQDAGIKPQGELLLMTNEDFKNLVPKLMEIYSA
//
ID  P16278;
PN  Beta-galactosidase;
GN  GLB1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Lysosome {ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:3084261}. [Isoform 2]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:2511208}. Note=Localized to the perinuclear area of the cytoplasm but not to lysosomes. {ECO:0000269|PubMed:2511208}.
DR  UNIPROT: P16278;
DR  UNIPROT: B2R7H8;
DR  UNIPROT: B7Z6B0;
DR  UNIPROT: P16279;
DR  PDB: 3THC;
DR  PDB: 3THD;
DR  PDB: 3WEZ;
DR  PDB: 3WF0;
DR  PDB: 3WF1;
DR  PDB: 3WF2;
DR  PDB: 3WF3;
DR  PDB: 3WF4;
DR  Pfam: PF13364;
DR  Pfam: PF01301;
DR  PROSITE: PS01182;
DR  OMIM: 230500;
DR  OMIM: 230600;
DR  OMIM: 230650;
DR  OMIM: 253010;
DR  OMIM: 611458;
DR  DisGeNET: 2720;
DE  Function: [Isoform 1]: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8200356}. [Isoform 2]: Has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers. {ECO:0000269|PubMed:10841810, ECO:0000269|PubMed:8922281}.
DE  Disease: GM1-gangliosidosis 1 (GM1G1) [MIM:230500]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. {ECO:0000269|PubMed:10338095, ECO:0000269|PubMed:10737981, ECO:0000269|PubMed:10839995, ECO:0000269|PubMed:1487238, ECO:0000269|PubMed:15365997, ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:15791924, ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:1928092, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8213816, ECO:0000269|Ref.28, ECO:0000269|Ref.31}. Note=The disease is caused by variants affecting the gene represented in this entry. GM1-gangliosidosis 2 (GM1G2) [MIM:230600]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. {ECO:0000269|PubMed:10737981, ECO:0000269|PubMed:12644936, ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8213816}. Note=The disease is caused by variants affecting the gene represented in this entry. GM1-gangliosidosis 3 (GM1G3) [MIM:230650]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. {ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:15986423, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8198123, ECO:0000269|Ref.28, ECO:0000269|Ref.30}. Note=The disease is caused by variants affecting the gene represented in this entry. Mucopolysaccharidosis 4B (MPS4B) [MIM:253010]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. {ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:12393180, ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:1928092, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:7586649}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P04985; IntAct: EBI-989686; Score: 0.35
DE  Interaction: Q99519; IntAct: EBI-989719; Score: 0.37
DE  Interaction: Q9NSA3; IntAct: EBI-1066502; Score: 0.00
DE  Interaction: P01023; IntAct: EBI-7183126; Score: 0.35
DE  Interaction: P16104; IntAct: EBI-2564373; Score: 0.35
DE  Interaction: P02866; IntAct: EBI-2908516; Score: 0.35
DE  Interaction: P01100; IntAct: EBI-3909100; Score: 0.37
DE  Interaction: P67870; IntAct: EBI-7133497; Score: 0.37
DE  Interaction: P53350; IntAct: EBI-7312891; Score: 0.37
DE  Interaction: P04183; IntAct: EBI-7398255; Score: 0.37
DE  Interaction: P24668; IntAct: EBI-10999951; Score: 0.35
DE  Interaction: O75787; IntAct: EBI-11037152; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P08670; IntAct: EBI-12452764; Score: 0.51
DE  Interaction: P62699; IntAct: EBI-12452923; Score: 0.51
DE  Interaction: Q9BRI3; IntAct: EBI-24521461; Score: 0.56
DE  Interaction: Q3KNW5; IntAct: EBI-24662545; Score: 0.56
DE  Interaction: P30825; IntAct: EBI-24732260; Score: 0.56
DE  Interaction: Q8NBJ4; IntAct: EBI-25278037; Score: 0.56
DE  Interaction: Q9NQH7; IntAct: EBI-11905895; Score: 0.00
DE  Interaction: P10619; IntAct: EBI-11905886; Score: 0.00
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: O92597; IntAct: EBI-14062645; Score: 0.35
DE  Interaction: Q9WRJ7; IntAct: EBI-14062674; Score: 0.35
DE  Interaction: Q8IUR0; IntAct: EBI-21546443; Score: 0.35
DE  Interaction: Q9Y5R8; IntAct: EBI-21546787; Score: 0.35
DE  Interaction: Q03405; IntAct: EBI-21577545; Score: 0.35
DE  Interaction: P24941; IntAct: EBI-21606933; Score: 0.35
DE  Interaction: P51449; IntAct: EBI-21635113; Score: 0.35
DE  Interaction: P25686; IntAct: EBI-21643743; Score: 0.35
DE  Interaction: Q9UM11; IntAct: EBI-21645901; Score: 0.35
DE  Interaction: Q9Y296; IntAct: EBI-21692555; Score: 0.35
DE  Interaction: Q9UL33; IntAct: EBI-21692555; Score: 0.35
DE  Interaction: Q96Q05; IntAct: EBI-21692555; Score: 0.35
DE  Interaction: Q8WVR3; IntAct: EBI-21692555; Score: 0.35
DE  Interaction: Q86SZ2; IntAct: EBI-21692555; Score: 0.35
DE  Interaction: P48553; IntAct: EBI-21692555; Score: 0.35
DE  Interaction: P04439; IntAct: EBI-21692555; Score: 0.35
DE  Interaction: O43617; IntAct: EBI-21692555; Score: 0.35
DE  Interaction: Q9UDY4; IntAct: EBI-21720121; Score: 0.35
DE  Interaction: P08134; IntAct: EBI-21721227; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-21721324; Score: 0.35
DE  Interaction: P25685; IntAct: EBI-21801194; Score: 0.35
DE  Interaction: Q8TD22; IntAct: EBI-21843206; Score: 0.35
DE  Interaction: Q8NEP7; IntAct: EBI-21843169; Score: 0.35
DE  Interaction: Q96NY8; IntAct: EBI-21851548; Score: 0.35
DE  Interaction: P50053; IntAct: EBI-21851528; Score: 0.40
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: Q8N5S9; IntAct: EBI-28943380; Score: 0.35
DE  Interaction: Q9UL54; IntAct: EBI-28946956; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-34581889; Score: 0.35
GO  GO:0035578;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:1904813;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0043202;
GO  GO:0048471;
GO  GO:0005773;
GO  GO:0004565;
GO  GO:0016936;
GO  GO:0042803;
GO  GO:0044262;
GO  GO:0019388;
GO  GO:0006027;
GO  GO:0006687;
GO  GO:0042340;
GO  GO:0051413;
GO  GO:1904016;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAI
SQ  QTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDK
SQ  WLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTV
SQ  DFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGA
SQ  NSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKS
SQ  LYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENM
SQ  GRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPS
SQ  GIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVD
SQ  RPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV
//
ID  Q8TD16;
PN  Protein bicaudal D homolog 2;
GN  BICD2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664119}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11864968}. Cytoplasm {ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664120}. Nucleus envelope {ECO:0000269|PubMed:20386726}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:20386726}. Note=In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends (By similarity). Localizes to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae in a RANBP2-dependent manner during G2 phase of the cell cycle (PubMed:20386726). {ECO:0000250|UniProtKB:Q921C5, ECO:0000269|PubMed:11864968, ECO:0000269|PubMed:20386726}.
DR  UNIPROT: Q8TD16;
DR  UNIPROT: O75181;
DR  UNIPROT: Q5TBQ2;
DR  UNIPROT: Q5TBQ3;
DR  UNIPROT: Q96LH2;
DR  UNIPROT: Q9BT84;
DR  UNIPROT: Q9H561;
DR  PDB: 6OFP;
DR  PDB: 6PSE;
DR  Pfam: PF09730;
DR  OMIM: 609797;
DR  OMIM: 615290;
DR  OMIM: 618291;
DR  DisGeNET: 23299;
DE  Function: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates and stabilizes the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (By similarity). Facilitates the binding of RAB6A to the Golgi by stabilizing its GTP-bound form. Regulates coat complex coatomer protein I (COPI)-independent Golgi- endoplasmic reticulum transport via its interaction with RAB6A and recruitment of the dynein-dynactin motor complex (PubMed:25962623). Contributes to nuclear and centrosomal positioning prior to mitotic entry through regulation of both dynein and kinesin-1. During G2 phase of the cell cycle, associates with RANBP2 at the nuclear pores and recruits dynein and dynactin to the nuclear envelope to ensure proper positioning of the nucleus relative to centrosomes prior to the onset of mitosis (By similarity). {ECO:0000250|UniProtKB:Q921C5, ECO:0000269|PubMed:25962623}.
DE  Disease: Spinal muscular atrophy, lower extremity-predominant 2A, childhood onset, autosomal dominant (SMALED2A) [MIM:615290]: An autosomal dominant form of spinal muscular atrophy characterized by early-childhood onset of muscle weakness and atrophy predominantly affecting the proximal and distal muscles of the lower extremity, although some patients may show upper extremity involvement. The disorder results in delayed walking, waddling gait, difficulty walking, and loss of distal reflexes. Some patients may have foot deformities or hyperlordosis, and some show mild upper motor signs, such as spasticity. Sensation, bulbar function, and cognitive function are preserved. The disorder shows very slow progression throughout life. {ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664119, ECO:0000269|PubMed:23664120, ECO:0000269|PubMed:28635954}. Note=The disease is caused by variants affecting the gene represented in this entry. Spinal muscular atrophy, lower extremity-predominant, 2B, prenatal onset, autosomal dominant (SMALED2B) [MIM:618291]: An autosomal dominant neuromuscular disorder characterized by decreased fetal movements, fractures in utero, severe congenital joint contractures, arthrogryposis multiplex congenita, severe hypotonia, muscle atrophy, and respiratory insufficiency and failure due to muscle weakness. Some patients may have dysmorphic facial features and/or abnormalities on brain imaging. Death in early childhood may occur. {ECO:0000269|PubMed:27751653, ECO:0000269|PubMed:28635954, ECO:0000269|PubMed:30054298}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O75604; IntAct: EBI-25254904; Score: 0.56
DE  Interaction: P0DTD1; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-15847951; Score: 0.40
DE  Interaction: P53350; IntAct: EBI-2372594; Score: 0.53
DE  Interaction: Q9UGI0; IntAct: EBI-2511131; Score: 0.40
DE  Interaction: Q9ERU9; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: Q9D0F1; IntAct: EBI-2558810; Score: 0.40
DE  Interaction: Q07832; IntAct: EBI-2560950; Score: 0.40
DE  Interaction: A0A5P8YL50; IntAct: EBI-2841923; Score: 0.00
DE  Interaction: A0A380PMY4; IntAct: EBI-2874899; Score: 0.00
DE  Interaction: Q9Q2G4; IntAct: EBI-6176962; Score: 0.35
DE  Interaction: Q6ZU80; IntAct: EBI-11370150; Score: 0.27
DE  Interaction: Q15154; IntAct: EBI-11382763; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: P55081; IntAct: EBI-24273176; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-24278102; Score: 0.56
DE  Interaction: Q8IVT4; IntAct: EBI-24279124; Score: 0.56
DE  Interaction: Q96IZ5; IntAct: EBI-24282407; Score: 0.56
DE  Interaction: Q96BR6; IntAct: EBI-24299149; Score: 0.56
DE  Interaction: Q13573; IntAct: EBI-24303486; Score: 0.56
DE  Interaction: O43602; IntAct: EBI-24327875; Score: 0.56
DE  Interaction: P56524; IntAct: EBI-24330514; Score: 0.56
DE  Interaction: O43309; IntAct: EBI-24331439; Score: 0.56
DE  Interaction: Q3SY00; IntAct: EBI-24333322; Score: 0.56
DE  Interaction: Q5T619; IntAct: EBI-24351080; Score: 0.56
DE  Interaction: Q99633; IntAct: EBI-24356006; Score: 0.56
DE  Interaction: Q96MY7; IntAct: EBI-24361254; Score: 0.56
DE  Interaction: Q8TAU3; IntAct: EBI-25251198; Score: 0.56
DE  Interaction: Q8TD31; IntAct: EBI-25253133; Score: 0.56
DE  Interaction: Q96NC0; IntAct: EBI-24494537; Score: 0.56
DE  Interaction: Q8N8B7; IntAct: EBI-24371967; Score: 0.56
DE  Interaction: Q9NRW1; IntAct: EBI-24383386; Score: 0.56
DE  Interaction: Q9P2J8; IntAct: EBI-24385190; Score: 0.56
DE  Interaction: Q9Y247; IntAct: EBI-24386038; Score: 0.56
DE  Interaction: Q6NYC8; IntAct: EBI-24395125; Score: 0.56
DE  Interaction: Q3B820; IntAct: EBI-24407148; Score: 0.56
DE  Interaction: Q3MJ62; IntAct: EBI-24410326; Score: 0.56
DE  Interaction: P00540; IntAct: EBI-25262612; Score: 0.56
DE  Interaction: Q6P1K2; IntAct: EBI-24417481; Score: 0.67
DE  Interaction: Q8WUT1; IntAct: EBI-24419281; Score: 0.56
DE  Interaction: Q9BQ89; IntAct: EBI-24423630; Score: 0.56
DE  Interaction: Q8WWY3; IntAct: EBI-24431378; Score: 0.56
DE  Interaction: Q5TAP6; IntAct: EBI-24433469; Score: 0.56
DE  Interaction: P07947; IntAct: EBI-24435343; Score: 0.56
DE  Interaction: Q15560; IntAct: EBI-24438200; Score: 0.56
DE  Interaction: Q9BS34; IntAct: EBI-24441307; Score: 0.56
DE  Interaction: Q969Z0; IntAct: EBI-24460855; Score: 0.56
DE  Interaction: Q53FD0; IntAct: EBI-24470675; Score: 0.56
DE  Interaction: O75828; IntAct: EBI-24472069; Score: 0.56
DE  Interaction: Q92619; IntAct: EBI-24473457; Score: 0.56
DE  Interaction: Q9Y6Q1; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: Q9Y3C0; IntAct: EBI-21617288; Score: 0.35
DE  Interaction: Q8TDR4; IntAct: EBI-21617027; Score: 0.35
DE  Interaction: Q9NYP9; IntAct: EBI-21663541; Score: 0.35
DE  Interaction: Q9Y5N6; IntAct: EBI-21663753; Score: 0.35
DE  Interaction: Q9Y2V7; IntAct: EBI-21673529; Score: 0.35
DE  Interaction: Q8IV45; IntAct: EBI-21699883; Score: 0.35
DE  Interaction: P07196; IntAct: EBI-21716934; Score: 0.35
DE  Interaction: Q9HCH3; IntAct: EBI-21757216; Score: 0.35
DE  Interaction: Q96GS4; IntAct: EBI-21795617; Score: 0.35
DE  Interaction: P31146; IntAct: EBI-21859808; Score: 0.35
DE  Interaction: Q8TD19; IntAct: EBI-20908056; Score: 0.40
DE  Interaction: P16401; IntAct: EBI-20908000; Score: 0.40
DE  Interaction: P16403; IntAct: EBI-20911880; Score: 0.40
DE  Interaction: P10412; IntAct: EBI-20912702; Score: 0.40
DE  Interaction: P61163; IntAct: EBI-20912662; Score: 0.40
DE  Interaction: Q8N4N8; IntAct: EBI-20913996; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-20922400; Score: 0.40
DE  Interaction: Q8TE73; IntAct: EBI-20924962; Score: 0.40
DE  Interaction: Q71DI3; IntAct: EBI-20924954; Score: 0.40
DE  Interaction: Q16778; IntAct: EBI-20924946; Score: 0.40
DE  Interaction: Q93079; IntAct: EBI-20924938; Score: 0.40
DE  Interaction: O94989; IntAct: EBI-20924930; Score: 0.40
DE  Interaction: O95858; IntAct: EBI-20929440; Score: 0.40
DE  Interaction: Q02539; IntAct: EBI-20931216; Score: 0.40
DE  Interaction: O15021; IntAct: EBI-20934244; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q14204; IntAct: EBI-21991405; Score: 0.40
DE  Interaction: O14576; IntAct: EBI-21992400; Score: 0.52
DE  Interaction: P20340; IntAct: EBI-21992535; Score: 0.46
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568044; Score: 0.35
DE  Interaction: Q8NHP6; IntAct: EBI-25617558; Score: 0.35
GO  GO:0005642;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005886;
GO  GO:0008093;
GO  GO:0034452;
GO  GO:0070840;
GO  GO:0051959;
GO  GO:0031267;
GO  GO:0051642;
GO  GO:0072393;
GO  GO:0007018;
GO  GO:0072385;
GO  GO:0051028;
GO  GO:0034067;
GO  GO:0033365;
GO  GO:0015031;
GO  GO:0070507;
GO  GO:0006890;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKE
SQ  AFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQR
SQ  GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL
SQ  EEALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTP
SQ  KKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRL
SQ  QASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQA
SQ  LTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYREG
SQ  QGGAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRADGGTGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKH
SQ  LQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKA
SQ  MVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLE
SQ  LDHEQTRRGRAKAAPKTKPATPSL
//
ID  Q921C5;
PN  Protein bicaudal D homolog 2;
GN  Bicd2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:11483508, ECO:0000269|PubMed:12447383, ECO:0000269|PubMed:25962623}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11483508}. Cytoplasm {ECO:0000250|UniProtKB:Q8TD16}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8TD16}. Nucleus envelope {ECO:0000250|UniProtKB:Q8TD16}. Note=In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends (PubMed:11483508). Localizes to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae in a RANBP2-dependent manner during G2 phase of the cell cycle (By similarity). {ECO:0000250|UniProtKB:Q8TD16, ECO:0000269|PubMed:11483508}.
DR  UNIPROT: Q921C5;
DR  UNIPROT: Q80TU1;
DR  UNIPROT: Q8BTE3;
DR  UNIPROT: Q9DCL3;
DR  Pfam: PF09730;
DE  Function: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates and stabilizes the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (PubMed:11483508, PubMed:25035494, PubMed:24986880, PubMed:22956769). Facilitates the binding of RAB6A to the Golgi by stabilizing its GTP-bound form (PubMed:25962623). Regulates coat complex coatomer protein I (COPI)- independent Golgi-endoplasmic reticulum transport via its interaction with RAB6A and recruitment of the dynein-dynactin motor complex (PubMed:12447383, PubMed:25962623). Contributes to nuclear and centrosomal positioning prior to mitotic entry through regulation of both dynein and kinesin-1. During G2 phase of the cell cycle, associates with RANBP2 at the nuclear pores and recruits dynein and dynactin to the nuclear envelope to ensure proper positioning of the nucleus relative to centrosomes prior to the onset of mitosis (PubMed:20386726). {ECO:0000269|PubMed:11483508, ECO:0000269|PubMed:12447383, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:22956769, ECO:0000269|PubMed:24986880, ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25962623}.
DE  Reference Proteome: Yes;
DE  Interaction: P46060; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-15847872; Score: 0.63
DE  Interaction: Q12840; IntAct: EBI-15847851; Score: 0.41
DE  Interaction: Q14203; IntAct: EBI-7894652; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: Q9JL25; IntAct: EBI-650530; Score: 0.37
DE  Interaction: P35279; IntAct: EBI-7893837; Score: 0.51
DE  Interaction: O14576; IntAct: EBI-7894652; Score: 0.35
DE  Interaction: Q8VHQ4; IntAct: EBI-11569919; Score: 0.35
DE  Interaction: Q5SW79; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: O60447; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: O75122; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: O60333; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: O00159; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: Q86SQ0; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: O43896; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: P20340; IntAct: EBI-15847968; Score: 0.41
DE  Interaction: Q8BUK6; IntAct: EBI-25297227; Score: 0.36
GO  GO:0005642;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005886;
GO  GO:0008093;
GO  GO:0034452;
GO  GO:0070840;
GO  GO:0051959;
GO  GO:0031267;
GO  GO:0051642;
GO  GO:0072393;
GO  GO:0007018;
GO  GO:0072385;
GO  GO:0051028;
GO  GO:0034067;
GO  GO:0033365;
GO  GO:0015031;
GO  GO:0070507;
GO  GO:0006890;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKE
SQ  AFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQR
SQ  GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL
SQ  EEALETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDDTVTAEPNNDAEALVNGFEHSGLVKSSLDNKTS
SQ  TPRKDGLAPPSPSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVNRLTENLSALR
SQ  RLQAGKERQTSLDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEG
SQ  QALTEKISLLEKASHQDRELLAHLEKELKKVSDVAGETQGSLNVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYR
SQ  EGQGKAGRTSPEGRGRRSPVLLPKGLLATEVGRADGGTGDNSPSPSSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAA
SQ  VDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTE
SQ  TMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHE
SQ  QTRRGRSKAASKAKPASPSL
//
ID  V6CJ04;
PN  Protein bicaudal D homolog;
GN  bicd;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000305|PubMed:20005871}. Perikaryon {ECO:0000269|PubMed:21205795}. Cell projection, dendrite {ECO:0000269|PubMed:21205795}. Note=Probably recruited to the nuclear envelope by unc-83. {ECO:0000305|PubMed:20005871}.
DR  UNIPROT: V6CJ04;
DR  UNIPROT: V6CK55;
DR  Pfam: PF09730;
DE  Function: Part of a complex with dlc-1 and egal-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migration in hypodermal precursor cells (PubMed:20005871) (Probable). Required for the formation of dendritic branches of PVD sensory neurons (PubMed:21205795). {ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:21205795, ECO:0000305|PubMed:27697906}.
DE  Reference Proteome: Yes;
DE  Interaction: Q17902; IntAct: EBI-2903351; Score: 0.51
DE  Interaction: Q23064; IntAct: EBI-2905267; Score: 0.51
DE  Interaction: O01590; IntAct: EBI-2414739; Score: 0.49
DE  Interaction: Q22771; IntAct: EBI-2414746; Score: 0.49
DE  Interaction: Q9N4I1; IntAct: EBI-6460281; Score: 0.37
DE  Interaction: Q9XVN3; IntAct: EBI-6534816; Score: 0.37
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005794;
GO  GO:0005875;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0043204;
GO  GO:0008093;
GO  GO:0034452;
GO  GO:0070840;
GO  GO:0072393;
GO  GO:0007399;
GO  GO:0030473;
GO  GO:0033365;
GO  GO:0048814;
GO  GO:0070507;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAESELEKLRQDIAILTEKYEQAKEDIHKAANAGLELLRQKEDLEKRLAEMQAELDLARTEIDKTNQTLAEYRSQHQRST
SQ  RSELENEESLLEESSAKEEEYLQRIAKLEADLKKKEQELAEKKEELESIEKKHSKEIDSGAALEDERRKLRAELKETKER
SQ  EQRLISEYSELEEENIGLQKTVANLRGSQVEYESLRIDNNRLEETIEIMKMAAEEDEILRVIADKQLEEALLTAQQERDQ
SQ  RLAMKRELEQTRNAEHISSLNDMLFGLERLGEDGELPPPQPGASDLFSELQGSSDVKVRELEAAKEGLQEELKSREKIFI
SQ  EFVTGLADTLNIHRPTNELDYMHARQQKDVVLEKIQNIARDTDRHDKEGEEKRSGILKADLRTLVLVAGEKSAQLAAAQD
SQ  AMIQVSDQLYQFYHQMTQNQGVQTEKSVQEIVKKLRLLARANAEDVPRVSLADEGVESGTETDVNASRSIPLNSDRLVIA
SQ  PSFAKEIEKKLASVKIGDVLSETDLRQRILTEGNAISETTESLKKMIQVVKRTSEQAFNQAVMASGAENEIEMQNMKLRS
SQ  LLSTKRDQISTLRTVLKSNKLTAESALTSMREKYESEKKMMMEINDKMRRELKQLKEDAATFASHRAMFTARGEELKSKV
SQ  EELSNELRANEEEKKTLNQLLRLAIQQKLTLTQRLEEVEVDRDRQVFKRSSTRAPTRETYQPPRAVRYPGSTTTAQQPAP
SQ  SSSGGSRGGPRRGDNQQ
//
ID  O46382;
PN  Brefeldin A-inhibited guanine nucleotide-exchange protein 1;
GN  ARFGEF1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from cytoplasm to membranes and nucleus upon cAMP treatment. {ECO:0000250}.
DR  UNIPROT: O46382;
DR  Pfam: PF16213;
DR  Pfam: PF09324;
DR  Pfam: PF01369;
DR  Pfam: PF12783;
DR  PROSITE: PS50190;
DE  Function: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0000139;
GO  GO:0016363;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0030532;
GO  GO:0005802;
GO  GO:0005085;
GO  GO:0034237;
GO  GO:0010256;
GO  GO:0007030;
GO  GO:0030837;
GO  GO:0034260;
GO  GO:0090303;
GO  GO:0006486;
GO  GO:0015031;
GO  GO:0032012;
GO  GO:2000114;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKY
SQ  FLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVT
SQ  SQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKERHRQHHHLLQSPVSHHE
SQ  PESPQLRYLPPQTVDHIPQEHEGDLDPQTNDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNDILYDGENHD
SQ  CEEKPQDIVQSIVEEMVNIVVGDTGERTTINVSADGNNGTIEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDT
SQ  QESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPIFGTNEMFINA
SQ  IKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQ
SQ  SVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTL
SQ  GQEKPSEQETSEMKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFTKKPKRGIQYL
SQ  QEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRL
SQ  MEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGK
SQ  KISMKETKELTIPAKSSKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAF
SQ  SVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYL
SQ  GNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGAKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQS
SQ  VVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGC
SQ  NPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFS
SQ  VFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQA
SQ  FKEYTSDDMNVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGYTYEKHWWQDLFRIVFRIFDNMKL
SQ  PEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIW
SQ  DKTCNCTLDIFKTTIPHALLTWRPISGETAPPTPSPVSENQLDTISQKSVDIHDSIQPRSADNRQQAPLASVSTVNEEIS
SQ  KIKPTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSRKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLF
SQ  KLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYTDESRASAWEEVQQRLLNVCSE
SQ  ALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGVVFQISQPP
SQ  EQELGINKQ
//
ID  Q9Y6D6;
PN  Brefeldin A-inhibited guanine nucleotide-exchange protein 1;
GN  ARFGEF1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus {ECO:0000269|PubMed:12571360}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:27373159, ECO:0000269|PubMed:27436755}. Nucleus {ECO:0000269|PubMed:14973189}. Nucleus, nucleolus {ECO:0000269|PubMed:14973189}. Nucleus matrix {ECO:0000269|PubMed:14973189}. Note=Translocates from cytoplasm to membranes and nucleus upon cAMP treatment.
DR  UNIPROT: Q9Y6D6;
DR  UNIPROT: Q9NV46;
DR  UNIPROT: Q9UFV2;
DR  UNIPROT: Q9UNL0;
DR  PDB: 3LTL;
DR  PDB: 5EE5;
DR  PDB: 5J5C;
DR  Pfam: PF16213;
DR  Pfam: PF09324;
DR  Pfam: PF01369;
DR  Pfam: PF12783;
DR  PROSITE: PS50190;
DR  OMIM: 604141;
DR  DisGeNET: 10565;
DE  Function: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269|PubMed:12571360, ECO:0000269|PubMed:15644318, ECO:0000269|PubMed:17227842, ECO:0000269|PubMed:20360857, ECO:0000269|PubMed:22084092}.
DE  Reference Proteome: Yes;
DE  Interaction: D4A631; IntAct: EBI-6251296; Score: 0.40
DE  Interaction: P0DTC7; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-15687558; Score: 0.35
DE  Interaction: Q13459; IntAct: EBI-6251244; Score: 0.56
DE  Interaction: Q5SQN1; IntAct: EBI-11294278; Score: 0.37
DE  Interaction: Q9Y6D5; IntAct: EBI-6249183; Score: 0.79
DE  Interaction: O75365; IntAct: EBI-1074175; Score: 0.00
DE  Interaction: P0DPB3; IntAct: EBI-2679560; Score: 0.00
DE  Interaction: A0A6L7HGG4; IntAct: EBI-2837534; Score: 0.00
DE  Interaction: A0A3N4AWL6; IntAct: EBI-2848506; Score: 0.00
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P05919; IntAct: EBI-6175288; Score: 0.46
DE  Interaction: Q7Z4S6; IntAct: EBI-6251652; Score: 0.71
DE  Interaction: Q99417; IntAct: EBI-6251879; Score: 0.54
DE  Interaction: Q9UQV4; IntAct: EBI-21563011; Score: 0.35
DE  Interaction: P49146; IntAct: EBI-21569349; Score: 0.35
DE  Interaction: Q8N7X8; IntAct: EBI-21585341; Score: 0.35
DE  Interaction: P01889; IntAct: EBI-21611619; Score: 0.35
DE  Interaction: P24530; IntAct: EBI-21672284; Score: 0.35
DE  Interaction: O95988; IntAct: EBI-21767396; Score: 0.35
DE  Interaction: Q6DKI7; IntAct: EBI-21808409; Score: 0.35
DE  Interaction: Q8TDX6; IntAct: EBI-21888284; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-15627579; Score: 0.40
DE  Interaction: P19338; IntAct: EBI-15687524; Score: 0.50
DE  Interaction: P22087; IntAct: EBI-15687576; Score: 0.35
DE  Interaction: P05455; IntAct: EBI-15687649; Score: 0.35
DE  Interaction: Q14432; IntAct: EBI-15766317; Score: 0.58
DE  Interaction: P10644; IntAct: EBI-15766462; Score: 0.50
DE  Interaction: Q14678; IntAct: EBI-15953570; Score: 0.63
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: Q00839; IntAct: EBI-20927272; Score: 0.40
DE  Interaction: P05787; IntAct: EBI-20930720; Score: 0.40
DE  Interaction: Q9NU19; IntAct: EBI-21228134; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21370268; Score: 0.00
DE  Interaction: P0DTC5; IntAct: EBI-25685699; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.35
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016363;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0030532;
GO  GO:0005802;
GO  GO:0005085;
GO  GO:0017022;
GO  GO:0034237;
GO  GO:0010256;
GO  GO:0006887;
GO  GO:0007030;
GO  GO:0030837;
GO  GO:0034260;
GO  GO:0090303;
GO  GO:0006486;
GO  GO:0015031;
GO  GO:0032012;
GO  GO:2000114;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKY
SQ  FLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVT
SQ  SQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKERHRQHHHLLQSPVSHHE
SQ  PESPQLRYLPPQTVDHISQEHEGDLDLHTNDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNEVLYDGENHD
SQ  CEEKPQDIVQNIVEEMVNIVVGDMGEGTTINASADGNIGTIEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDT
SQ  QESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPIFRTNEMFINA
SQ  IKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQ
SQ  SVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTL
SQ  GQEKPSEQEMSEIKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYL
SQ  QEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRL
SQ  MEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGK
SQ  KISMKETKELTIPTKSSKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAF
SQ  SVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYL
SQ  GNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQS
SQ  VVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGC
SQ  NPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFS
SQ  VFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQA
SQ  FKEYTSDDMNVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKL
SQ  PEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIW
SQ  DKTCNCTLDIFKTTIPHALLTWRPNSGETAPPPPSPVSEKPLDTISQKSVDIHDSIQPRSVDNRPQAPLVSASAVNEEVS
SQ  KIKSTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLF
SQ  KLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYMDESRVSAWEEVQQRLLNVCSE
SQ  ALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGVVFQISQPP
SQ  EQELGINKQ
//
ID  G3X9K3;
PN  Brefeldin A-inhibited guanine nucleotide-exchange protein 1;
GN  Arfgef1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from cytoplasm to membranes and nucleus upon cAMP treatment. {ECO:0000250}.
DR  UNIPROT: G3X9K3;
DR  UNIPROT: Q8BKL2;
DR  Pfam: PF16213;
DR  Pfam: PF09324;
DR  Pfam: PF01369;
DR  Pfam: PF12783;
DR  PROSITE: PS50190;
DE  Function: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A0F6B5H5; IntAct: EBI-27034767; Score: 0.46
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016363;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0030532;
GO  GO:0005802;
GO  GO:0005085;
GO  GO:0017022;
GO  GO:0034237;
GO  GO:0010256;
GO  GO:0007030;
GO  GO:0030837;
GO  GO:0034260;
GO  GO:0031175;
GO  GO:0051897;
GO  GO:0090303;
GO  GO:0006486;
GO  GO:0015031;
GO  GO:0032012;
GO  GO:2000114;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKVETEKQSPPHGEAKAGSGTLPPVKSKTNFIEADKY
SQ  FLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGRAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVT
SQ  SQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMERERHRQQQHLLQSPVSHHE
SQ  PESPHLRYLPPQTVDHINQEHEGDLEPQTHDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNDILYDGDYEE
SQ  KPLDIVQSIVEEMVNIIVGDMGEGMAISASTEGNTGTVEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQES
SQ  GNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPVFRTNEMFINAIKQ
SQ  YLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVV
SQ  DIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQE
SQ  KPSEQEISEVKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQ
SQ  GMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRLFLEGFRLPGEAQKIDRLMEK
SQ  FAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKIS
SQ  MKETKELTIPTKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVG
SQ  LQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNS
SQ  WHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVV
SQ  AVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPN
SQ  EDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFH
SQ  LAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKE
SQ  YTSDDMSVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQ
SQ  QTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKT
SQ  CNCTLDIFKTTIPHALLTWRPTSGEAEPPSPSAVSEKPLDAISQKSVDIHDSIQPRSSDNRQQAPLVSVSTVSEEVSKVK
SQ  STAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLL
SQ  DCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYMDESRVSAWEEVQQRLLNVCREALS
SQ  YFLTLTSESHREAWTNLLLLFLTKVLKISDSRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGIVFQISQPPEQE
SQ  LGINRQ
//
ID  D4A631;
PN  Brefeldin A-inhibited guanine nucleotide-exchange protein 1;
GN  Arfgef1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:11809827}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11809827}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from cytoplasm to membranes and nucleus upon cAMP treatment (By similarity). PRKAR1B. {ECO:0000250}.
DR  UNIPROT: D4A631;
DR  Pfam: PF16213;
DR  Pfam: PF09324;
DR  Pfam: PF01369;
DR  Pfam: PF12783;
DR  PROSITE: PS50190;
DE  Function: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q63358; IntAct: EBI-6251135; Score: 0.51
DE  Interaction: Q13459; IntAct: EBI-6251284; Score: 0.40
DE  Interaction: Q9Y6D6; IntAct: EBI-6251296; Score: 0.40
DE  Interaction: P00533; IntAct: EBI-22084260; Score: 0.35
GO  GO:0005829;
GO  GO:0000139;
GO  GO:0016363;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0030532;
GO  GO:0005802;
GO  GO:0005085;
GO  GO:0017022;
GO  GO:0034237;
GO  GO:0010256;
GO  GO:0007030;
GO  GO:0030837;
GO  GO:0034260;
GO  GO:0031175;
GO  GO:0051897;
GO  GO:0090303;
GO  GO:0006486;
GO  GO:0015031;
GO  GO:0032012;
GO  GO:2000114;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKVETEKQSPPHGEAKAGSGTLPPVKSKTNFIEADKY
SQ  FLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGSAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVT
SQ  SQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMERERHRQQHHLLQSPVSHHE
SQ  PESPHLRYLPPQTVDHIAQEQEGDLDPQTHDVDKSLQDDIEPENGSDISSAENEQTEADQATAAETLSKDDVLCDGECEE
SQ  KPQDIVQSIVEEMVDIIVGDMGEGTAVSASADGNAGAVEDGSDSENVQANGIPGTPISAAYTPSLPDDRLSVSSNDTQES
SQ  GNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPVFRTNEMFINAIKQ
SQ  YLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVV
SQ  DIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQE
SQ  KPSEQEISEIKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQ
SQ  GMLGTTPEDIAQFLHQEERLDSTQAGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRLFLEGFRLPGEAQKIDRLMEK
SQ  FAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKIS
SQ  MKETKELTIPTKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVG
SQ  LQDCDDTDVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNS
SQ  WHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVV
SQ  AVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPN
SQ  EDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFH
SQ  LAASDQDESIVELAFQTSGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKE
SQ  YTSDDMNVAPEDRVWVRGWFPILFELSCVINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQ
SQ  QTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKT
SQ  CNCTLDIFKTTIPHALLTWRPTSGEAAPPSPSAMSEKQLDAISQKSVDIHDSAQPRSSDNRQQAPLVSVSPASEEVSKGR
SQ  PTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLL
SQ  DCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYTDESRVSAWEEVQQRLLNVCSEALS
SQ  YFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGIVFQISQPPEQE
SQ  LGINKQ
//
ID  Q9Y6D5;
PN  Brefeldin A-inhibited guanine nucleotide-exchange protein 2;
GN  ARFGEF2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Membrane. Golgi apparatus. Cytoplasm, perinuclear region. Golgi apparatus, trans-Golgi network {ECO:0000250}. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell projection, dendrite {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Synapse {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Translocates from cytoplasm to membranes upon cAMP treatment. Localized in recycling endosomes.
DR  UNIPROT: Q9Y6D5;
DR  UNIPROT: Q5TFT9;
DR  UNIPROT: Q9NTS1;
DR  PDB: 3L8N;
DR  PDB: 3SWV;
DR  Pfam: PF16213;
DR  Pfam: PF09324;
DR  Pfam: PF01369;
DR  Pfam: PF12783;
DR  PROSITE: PS50190;
DR  OMIM: 605371;
DR  OMIM: 608097;
DR  DisGeNET: 10564;
DE  Function: Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. {ECO:0000269|PubMed:12051703, ECO:0000269|PubMed:12571360, ECO:0000269|PubMed:15385626, ECO:0000269|PubMed:16477018, ECO:0000269|PubMed:17276987, ECO:0000269|PubMed:18625701, ECO:0000269|PubMed:20360857}.
DE  Disease: Periventricular nodular heterotopia 2 (PVNH2) [MIM:608097]: A developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH2 is an autosomal recessive form characterized by microcephaly (small brain), severe developmental delay and recurrent infections. No anomalies extrinsic to the central nervous system, such as dysmorphic features or grossly abnormal endocrine or other conditions, are associated with PVNH2. {ECO:0000269|PubMed:14647276, ECO:0000269|PubMed:23812912, ECO:0000269|PubMed:25160555}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P10909; IntAct: EBI-21370252; Score: 0.00
DE  Interaction: O75400; IntAct: EBI-7243480; Score: 0.37
DE  Interaction: A0A3P1UC63; IntAct: EBI-2837508; Score: 0.00
DE  Interaction: A0A6L7HB40; IntAct: EBI-2837541; Score: 0.00
DE  Interaction: A0A6L8PCK7; IntAct: EBI-2837527; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P05919; IntAct: EBI-6175288; Score: 0.46
DE  Interaction: Q9Y6D6; IntAct: EBI-6249183; Score: 0.79
DE  Interaction: Q9UPT5; IntAct: EBI-6251422; Score: 0.51
DE  Interaction: P19438; IntAct: EBI-6251604; Score: 0.46
DE  Interaction: Q99417; IntAct: EBI-6251858; Score: 0.54
DE  Interaction: P31323; IntAct: EBI-6258808; Score: 0.46
DE  Interaction: Q15116; IntAct: EBI-21506827; Score: 0.35
DE  Interaction: Q13477; IntAct: EBI-21555701; Score: 0.35
DE  Interaction: P06028; IntAct: EBI-21557067; Score: 0.35
DE  Interaction: Q9UQV4; IntAct: EBI-21563011; Score: 0.35
DE  Interaction: P05362; IntAct: EBI-21568860; Score: 0.35
DE  Interaction: Q8N7X8; IntAct: EBI-21585341; Score: 0.35
DE  Interaction: P01889; IntAct: EBI-21611619; Score: 0.35
DE  Interaction: Q96G30; IntAct: EBI-21633324; Score: 0.35
DE  Interaction: Q6EMK4; IntAct: EBI-21651359; Score: 0.35
DE  Interaction: P40259; IntAct: EBI-21668943; Score: 0.35
DE  Interaction: P24530; IntAct: EBI-21672284; Score: 0.35
DE  Interaction: Q86XD5; IntAct: EBI-21711466; Score: 0.35
DE  Interaction: Q9BRK5; IntAct: EBI-21763329; Score: 0.35
DE  Interaction: Q9BZW8; IntAct: EBI-21787892; Score: 0.35
DE  Interaction: Q9NQ34; IntAct: EBI-21788287; Score: 0.35
DE  Interaction: Q8TDX6; IntAct: EBI-21888284; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-15627562; Score: 0.40
DE  Interaction: Q14432; IntAct: EBI-15766317; Score: 0.50
DE  Interaction: P10644; IntAct: EBI-15766425; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: P0DTC5; IntAct: EBI-26495256; Score: 0.53
GO  GO:0070161;
GO  GO:0032279;
GO  GO:0005879;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005815;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0032280;
GO  GO:0005802;
GO  GO:0050811;
GO  GO:0005085;
GO  GO:0017022;
GO  GO:0034237;
GO  GO:0010256;
GO  GO:0007032;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0035556;
GO  GO:0032760;
GO  GO:0015031;
GO  GO:0001881;
GO  GO:0032012;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAEIEKQRLGTAAPPKANFIEADKYFLPFELACQSKS
SQ  PRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETICSCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTIL
SQ  QTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPIQSKPQSPVIQAAAVSPKFVRLKHSQAQS
SQ  KPTTPEKTDLTNGEHARSDSGKVSTENGDAPRERGSSLSGTDDGAQEVVKDILEDVVTSAIKEAAEKHGLTEPERVLGEL
SQ  ECQECAIPPGVDENSQTNGIADDRQSLSSADNLESDAQGHQVAARFSHVLQKDAFLVFRSLCKLSMKPLGEGPPDPKSHE
SQ  LRSKVVSLQLLLSVLQNAGPVFRTHEMFINAIKQYLCVALSKNGVSSVPDVFELSLAIFLTLLSNFKMHLKMQIEVFFKE
SQ  IFLNILETSTSSFEHRWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRSGHELGMTPLQELSLR
SQ  KKGLECLVSILKCMVEWSKDLYVNPNHQTSLGQERLTDQEIGDGKGLDMARRCSVTSMESTVSSGTQTTVQDDPEQFEVI
SQ  KQQKEIIEHGIELFNKKPKRGIQFLQEQGMLGTSVEDIAQFLHQEERLDSTQVGDFLGDSARFNKEVMYAYVDQLDFCEK
SQ  EFVSALRTFLEGFRLPGEAQKIDRLMEKFAARYIECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKM
SQ  NRGINDSKDLPEEYLSSIYEEIEGKKIAMKETKELTIATKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHAKAP
SQ  FTSATHLDHVRPMFKLVWTPLLAAYSIGLQNCDDTEVASLCLEGIRCAIRIACIFGMQLERDAYVQALARFSLLTASSSI
SQ  TEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKTRYLSGSGREREGSLKGHTLAGEEFMGLGL
SQ  GNLVSGGVDKRQMASFQESVGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSLQKIVEIS
SQ  YYNMNRIRLQWSRIWHVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKKNRSPTIR
SQ  DMAIRCIAQMVNSQAANIRSGWKNIFAVFHQAASDHDGNIVELAFQTTCHIVTTIFQHHFPAAIDSFQDAVKCLSEFACN
SQ  AAFPDTSMEAIRLIRFCGKYVSERPRVLQEYTSDDMNVAPGDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMK
SQ  SYGHTFEKHWWQDLFRIVFRIFDNMKLPEQLSEKSEWMTTTCNHALYAICDVFTQFYEALNEVLLSDVFAQLQWCVKQDN
SQ  EQLARSGTNCLENLVISNGEKFSPEVWDETCNCMLDIFKTTIPHVLLTWRPVGMEEDSSEKHLDVDLDRQSLSSIDKNPS
SQ  ERGQSQLSNPTDDSWKGRPYANQKLFASLLIKCVVQLELIQTIDNIVFYPATSKKEDAEHMVAAQQDTLDADIHIETEDQ
SQ  GMYKYMSSQHLFKLLDCLQESHSFSKAFNSNYEQRTVLWRAGFKGKSKPNLLKQETSSLACCLRILFRMYVDENRRDSWE
SQ  EIQQRLLTVCSEALAYFITVNSESHREAWTSLLLLLLTKTLKINDEKFKAHASMYYPYLCEIMQFDLIPELRAVLRKFFL
SQ  RIGVVYKIWIPEEPSQVPAALSPVW
//
ID  A2A5R2;
PN  Brefeldin A-inhibited guanine nucleotide-exchange protein 2;
GN  Arfgef2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Synapse {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Translocates from cytoplasm to membranes upon cAMP treatment. Localized in recycling endosomes (By similarity). {ECO:0000250}.
DR  UNIPROT: A2A5R2;
DR  Pfam: PF16213;
DR  Pfam: PF09324;
DR  Pfam: PF01369;
DR  Pfam: PF12783;
DR  PROSITE: PS50190;
DE  Function: Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8BP00; IntAct: EBI-4283417; Score: 0.35
DE  Interaction: Q91WZ8; IntAct: EBI-16749137; Score: 0.35
GO  GO:0070161;
GO  GO:0032279;
GO  GO:0005879;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005815;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0032280;
GO  GO:0005802;
GO  GO:0050811;
GO  GO:0005085;
GO  GO:0017022;
GO  GO:0034237;
GO  GO:0010256;
GO  GO:0007032;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0035556;
GO  GO:0032760;
GO  GO:0015031;
GO  GO:0001881;
GO  GO:0032012;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAELEKQRLGAAAPPKANFIEADKYFLPFELACQSKS
SQ  PRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETICNCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTIL
SQ  QTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPMQSKPQSPVIQATAGSPKFSRLKQSQAQS
SQ  KPTTPEKAELPNGDHAQSGLGKVSLENGEAPRERGSPVSGRAEPSRGTDSGAQEVVKDILEDVVTSAVKEAAEKHGLPEP
SQ  DRALGALECQECAVPPGVDENSQTNGIADDRQSLSSADNLEPDVQGHQVAARFSHILQKDAFLVFRSLCKLSMKPLGEGP
SQ  PDPKSHELRSKVVSLQLLLSVLQNAGPVFRSHEMFVTAIKQYLCVALSKNGVSSVPDVFELSLAIFLTLLSNFKMHLKMQ
SQ  IEVFFKEIFLNILETSTSSFEHRWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRSGHELGMTP
SQ  LQELSLRKKGLECLVSILKCMVEWSKDLYVNPNHQATLGQERLPDQEMGDGKGLDMARRCSVTSVESTVSSGTQTAIQDD
SQ  PEQFEVIKQQKEIIEHGIELFNKKPKRGIQFLQEQGMLGAAVEDIAQFLHQEERLDSTQVGEFLGDSTRFNKEVMYAYVD
SQ  QLDFCEKEFVSALRTFLEGFRLPGEAQKIDRLMEKFAARYIECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMT
SQ  KEQYIKMNRGINDSKDLPEEYLSSIYDEIEGKKIAMKETKEHTIATKSTKQSVASEKQRRLLYNVEMEQMAKTAKALMEA
SQ  VSHAKAPFTSATHLDHVRPMFKLVWTPLLAAYSIGLQNCDDTEVASLCLEGIRCAVRIACIFGMQLERDAYVQALARFSL
SQ  LTASSSITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKTRYLSGSGREREGSLKGHSLAGE
SQ  EFMGLGLGNLVSGGVDKRQMASFQESVGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSL
SQ  QKIVEISYYNMNRIRLQWSRIWHVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKK
SQ  NRSPTIRDMVIRCIAQMVSSQAANIRSGWKNIFAVFHQAASDHDGNIVELAFQTTGHIVSTIFQHHFPAAIDSFQDAVKC
SQ  LSEFACNAAFPDTSMEAIRLIRFCGKYVSERPRVLQEYTSDDMNVAPGDRVWVRGWFPILFELSCIINRCKLDVRTRGLT
SQ  VMFEIMKSYGHTFAKHWWQDLFRIVFRIFDNMKLPEQQSEKSEWMTTTCNHALYAICDVFTQFYEALHEVLLSDVFAQLQ
SQ  WCVKQDNEQLARSGTNCLENLVISNGEKFSPAVWDETCNCMLDIFKTTIPHVLLTWRPAGMEEEVSDRHLDVDLDRQSLS
SQ  SIDRNASERGQSQLSNPTDDSWKGAPYAHQKLLASLLIKCVVQLELIQTIDNIVFYPATSKKEDAEHMVAAQQDTLDAEI
SQ  HIETENQGMYKFMSSQHLFKLLDCLQESHSFSKAFNSNYEQRTVLWRAGFKGKSKPNLLKQETSSLACCLRILFRMYVDE
SQ  NRRDSWDEIQQRLLRVCSEALAYFITVNSESHREAWTSLLLLLLTKTLKISDEKFKAHASMYYPYLCEIMQFDLIPELRA
SQ  VLRKFFLRIGLVYKIWIPEEPSQVPAALSSTW
//
ID  Q7TSU1;
PN  Brefeldin A-inhibited guanine nucleotide-exchange protein 2;
GN  Arfgef2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, trans-Golgi network. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection, dendrite. Cytoplasmic vesicle. Synapse. Cytoplasm, cytoskeleton. Note=Translocates from cytoplasm to membranes upon cAMP treatment. Localized in recycling endosomes (By similarity). {ECO:0000250}.
DR  UNIPROT: Q7TSU1;
DR  Pfam: PF16213;
DR  Pfam: PF09324;
DR  Pfam: PF01369;
DR  Pfam: PF12783;
DR  PROSITE: PS50190;
DE  Function: Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. {ECO:0000269|PubMed:15198677}.
DE  Reference Proteome: Yes;
DE  Interaction: P15431; IntAct: EBI-6257990; Score: 0.37
DE  Interaction: P63079; IntAct: EBI-6257978; Score: 0.53
DE  Interaction: P63138; IntAct: EBI-6258080; Score: 0.37
DE  Interaction: P62813; IntAct: EBI-6258190; Score: 0.40
DE  Interaction: P14867; IntAct: EBI-6258248; Score: 0.27
DE  Interaction: P28472; IntAct: EBI-6258248; Score: 0.27
DE  Interaction: P40748; IntAct: EBI-21282580; Score: 0.35
DE  Interaction: P22607; IntAct: EBI-22244643; Score: 0.35
DE  Interaction: P15498; IntAct: EBI-22257448; Score: 0.35
GO  GO:0070161;
GO  GO:0032279;
GO  GO:0005879;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0000139;
GO  GO:0016020;
GO  GO:0005815;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0032280;
GO  GO:0005802;
GO  GO:0050811;
GO  GO:0005085;
GO  GO:0017022;
GO  GO:0034237;
GO  GO:0010256;
GO  GO:0007032;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0035556;
GO  GO:0032760;
GO  GO:0015031;
GO  GO:0001881;
GO  GO:0032012;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAELEKQRLGAAAPPKANFIEADKYFLPFELACQSKS
SQ  PRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETVCNCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTIL
SQ  QTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPIQSKPQSPVIQATAGSPKFSRLKQSQAQS
SQ  KPTTPEKTELPNGDHARSSLGKVNSENGEAHRERGSSISGRAEPSGGSDNGAQEVVKDILEDVVTSAVKEAAEKQGLPEP
SQ  DQAPGVPECQECTVPPAVDENSQTNGIADDRQSLSSADNLEPDAQGHPVAARFSHILQKDAFLVFRSLCKLSMKPLGEGP
SQ  PDPKSHELRSKVVSLQLLLSVLQNAGPVFRSHEMFVTAIKQYLCVALSKNGVSSVPDVFELSLAIFLTLLSNFKMHLKMQ
SQ  IEVFFKEIFLNILETSTSSFEHRWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRSGHELGMTP
SQ  LQELSLRKKGLECLVSILKCMVEWSKDLYVNPNHQATLGQERLPDQEMGDGKGLDMARRCSVTSVESTVSSGTQTAIPDD
SQ  PEQFEVIKQQKEIIEHGIELFNKKPKRGIQFLQEQGMLGAAVEDIAQFLHQEERLDSTQVGEFLGDSTRFNKEVMYAYVD
SQ  QLDFCEKEFVSALRTFLEGFRLPGEAQKIDRLMEKFAARYIECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMT
SQ  KEQYIKMNRGINDSKDLPEEYLSSIYEEIEGKKIAMKETKEHTMATKSTKQNVASEKQRRLLYNVEMEQMAKTAKALMEA
SQ  VSHAKAPFTSATHLDHVRPMFKLVWTPLLAAYSIGLQNCDDTEVASLCLEGIRCAVRIACIFGMQLERDAYVQALARFSL
SQ  LTASSSITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKTRYLSGSGREREGSLKGHSLAGE
SQ  EFMGLGLGNLVSGGVDKRQMASFQESVGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSL
SQ  QKIVEISYYNMNRIRLQWSRIWHVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKK
SQ  NRSPTIRDMVIRCIAQMVSSQAANIRSGWKNIFAVFHQAASDHDGNIVELAFQTTGHIVSTIFQHHFPAAIDSFQDAVKC
SQ  LSEFACNAAFPDTSMEAIRLIRFCGKYVSERPRVLQEYTSDDMNVAPGDRVWVRGWFPILFELSCIINRCKLDVRTRGLT
SQ  VMFEIMKSYGHTFAKHWWQDLFRIVFRIFDNMKLPEQQSEKSEWMTTTCNHALYAICDVFTQFYEALHEVLLSDVFAQLQ
SQ  WCVKQDNEQLARSGTNCLENLVISNGEKFSPAVWDETCNCMLDIFRTTIPHVLLTWRPAGMEEEVSDRHLDVDLDRQSLS
SQ  SIDRNASERGQSQLSNPTDDSWKGAPYANQKLLASLLIKCVVQLELIQTIDNIVFYPATSKKEDAEHMVAAQQDTLDADI
SQ  HIETENQGMYKFMSSQHLFKLLDCLQESHSFSKAFNSNYEQRTVLWRAGFKGKSKPNLLKQETSSLACCLRILFRMYVDE
SQ  NRRDSWGEIQQRLLTVCSEALAYFITVNSESHREAWTSLLLLLLTKTLKINDEKFKAHASVYYPYLCEMMQFDLIPELRA
SQ  VLRKFFLRIGLVYKIWVPEEPSQVPAASTAW
//
ID  I6V1W0;
PN  Protein brambleberry;
GN  bmb;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:22863006}; Multi-pass membrane protein {ECO:0000269|PubMed:22863006}. Note=During metaphase, localizes near the mitotic spindle region, and its localization shifts to the chromosomes as they reach the end of the spindle. During karyomere fusion, detected in prominent puncta, mainly at karyomere-karyomere interfaces corresponding to putative fusion sites.
DR  UNIPROT: I6V1W0;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000269|PubMed:22863006}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0061472;
GO  GO:0007344;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALWFVLLWVSSLQYAEVEAFFDWLKKADPAPTPPPAESIVPILLHGEAPAFEMSVVDEKFLAEAKQMELSPLDSCHFRV
SQ  VAQLKATCSGLSEEQLAKLGVALFNCQSEVEGRRTYPCTEEMSIKECTADMDSDTWNAYHIVSNRARSVCYATRQQHFRK
SQ  RAELTVNALISTATSQLDAMKDLKEGQKELRDMTAASLDKLLEGHGALQIQQGALKEGQEQLDASISENLQRLAQEKALI
SQ  STGQQLVAQLIQGITQRMENVSGQLKDQTAEVQEGHQAILEDLAVVRGSAQDIYEKMELNLNGFLQQQNTTAHFYTELMR
SQ  KLELMNGTLGYMLTYLDNMQTRLEDRLHMIQGYLGWAGLSLRALWTCVMHAGYFLLCAVLLSFLQCTTFSRVTLLLSVPI
SQ  NAIAEINQQAALDLISLTLLLFTLSLGRWFVLQLLWALSKIKGRTCSRPPHLSIYPPKEKTPEKQHEFGEKCPASSSTPV
SQ  QSDPVCDLEVESFMMGDPCVLGVSPSRCPPKFSHHHLGGTPNHSTPRLKSRHSIAATELDNIPQRNLGVFLETVNRSRSS
SQ  SPNQSLASSSSFSGRSLCSGITRLGQPCKKRAVVGQDYCRVHEGGHTSYSRL
//
ID  Q3T013;
PN  BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like;
GN  BNIP3L;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the mitochondrion outer membrane. {ECO:0000250}.
DR  UNIPROT: Q3T013;
DR  UNIPROT: A5D9C5;
DR  Pfam: PF06553;
DE  Function: Induces apoptosis. Interacts with viral and cellular anti- apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). May function as a tumor suppressor (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0042802;
GO  GO:0051607;
GO  GO:0097345;
GO  GO:0035694;
GO  GO:0043065;
GO  GO:0043067;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSHLVEQPPPPHNNNNNCEEGEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQH
SQ  ESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSKDHSSQSEEEVAEGEKEVDALKKSVDWVSDWSSRPENIPPKEFHFRH
SQ  PKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
//
ID  O60238;
PN  BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like;
GN  BNIP3L;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope. Endoplasmic reticulum. Mitochondrion outer membrane. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the mitochondrion outer membrane.
DR  UNIPROT: O60238;
DR  UNIPROT: B0AZS9;
DR  UNIPROT: Q5JW63;
DR  UNIPROT: Q8NF87;
DR  Pfam: PF06553;
DR  OMIM: 605368;
DR  DisGeNET: 665;
DE  Function: Induces apoptosis. Interacts with viral and cellular anti- apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor. {ECO:0000269|PubMed:10381623, ECO:0000269|PubMed:21264228}.
DE  Reference Proteome: Yes;
DE  Interaction: A0PK00; IntAct: EBI-24405238; Score: 0.56
DE  Interaction: Q6NUQ1; IntAct: EBI-737555; Score: 0.00
DE  Interaction: Q9P104; IntAct: EBI-752488; Score: 0.37
DE  Interaction: Q01844; IntAct: EBI-753931; Score: 0.37
DE  Interaction: O60238; IntAct: EBI-755134; Score: 0.86
DE  Interaction: Q12983; IntAct: EBI-757996; Score: 0.96
DE  Interaction: P17152; IntAct: EBI-758767; Score: 0.84
DE  Interaction: P03247; IntAct: EBI-849900; Score: 0.65
DE  Interaction: Q12982; IntAct: EBI-849923; Score: 0.37
DE  Interaction: P02545; IntAct: EBI-849933; Score: 0.37
DE  Interaction: Q92934; IntAct: EBI-850652; Score: 0.44
DE  Interaction: P10415; IntAct: EBI-850662; Score: 0.44
DE  Interaction: P38182; IntAct: EBI-7679661; Score: 0.67
DE  Interaction: Q9H492; IntAct: EBI-7680248; Score: 0.61
DE  Interaction: Q81X61; IntAct: EBI-2817764; Score: 0.00
DE  Interaction: Q81TT4; IntAct: EBI-2837471; Score: 0.00
DE  Interaction: A0A2U2GZW8; IntAct: EBI-2848492; Score: 0.00
DE  Interaction: Q7CIP6; IntAct: EBI-2874847; Score: 0.00
DE  Interaction: A0A380PE22; IntAct: EBI-2874840; Score: 0.00
DE  Interaction: Q9NRQ5; IntAct: EBI-8640186; Score: 0.78
DE  Interaction: Q9BXN2; IntAct: EBI-8656262; Score: 0.67
DE  Interaction: P51452; IntAct: EBI-3904946; Score: 0.37
DE  Interaction: Q16610; IntAct: EBI-3904966; Score: 0.37
DE  Interaction: O14936; IntAct: EBI-3906243; Score: 0.37
DE  Interaction: Q8IU85; IntAct: EBI-3912671; Score: 0.37
DE  Interaction: P32456; IntAct: EBI-7104878; Score: 0.37
DE  Interaction: O14775; IntAct: EBI-7104942; Score: 0.37
DE  Interaction: Q8NBE8; IntAct: EBI-7105008; Score: 0.37
DE  Interaction: Q9HCK4; IntAct: EBI-7105110; Score: 0.37
DE  Interaction: Q9NQ11; IntAct: EBI-6377441; Score: 0.51
DE  Interaction: Q5T700; IntAct: EBI-10186247; Score: 0.67
DE  Interaction: Q969F0; IntAct: EBI-10186257; Score: 0.56
DE  Interaction: Q9H2S6; IntAct: EBI-24287972; Score: 0.56
DE  Interaction: Q13021; IntAct: EBI-25259116; Score: 0.56
DE  Interaction: P60520; IntAct: EBI-24378093; Score: 0.56
DE  Interaction: O43169; IntAct: EBI-24422195; Score: 0.56
DE  Interaction: Q9H0R8; IntAct: EBI-24427438; Score: 0.56
DE  Interaction: Q9NRS4; IntAct: EBI-24447859; Score: 0.56
DE  Interaction: Q15848; IntAct: EBI-12697535; Score: 0.56
DE  Interaction: Q9Y4P8; IntAct: EBI-21766966; Score: 0.35
DE  Interaction: P22736; IntAct: EBI-16085278; Score: 0.54
DE  Interaction: Q8NI37; IntAct: EBI-21934639; Score: 0.35
DE  Interaction: P41595; IntAct: EBI-20808451; Score: 0.37
DE  Interaction: Q96H55; IntAct: EBI-25476634; Score: 0.35
DE  Interaction: Q9P0W8; IntAct: EBI-25476634; Score: 0.35
DE  Interaction: O43464; IntAct: EBI-25476634; Score: 0.35
DE  Interaction: Q96IX5; IntAct: EBI-25476634; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
DE  Interaction: A0A663DJA2; IntAct: EBI-28953729; Score: 0.56
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0031224;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0042803;
GO  GO:0071456;
GO  GO:0051607;
GO  GO:0097345;
GO  GO:0035694;
GO  GO:0043066;
GO  GO:0060548;
GO  GO:0043065;
GO  GO:0016239;
GO  GO:1903146;
GO  GO:0043067;
GO  GO:1903214;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQH
SQ  ESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRH
SQ  PKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
//
ID  Q9Z2F7;
PN  BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like;
GN  Bnip3l;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the mitochondrion outer membrane. {ECO:0000250}.
DR  UNIPROT: Q9Z2F7;
DR  UNIPROT: Q545J6;
DR  Pfam: PF06553;
DE  Function: Induces apoptosis. Interacts with viral and cellular anti- apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). May function as a tumor suppressor (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q69ZI1; IntAct: EBI-1774643; Score: 0.58
DE  Interaction: Q9GZQ8; IntAct: EBI-7679879; Score: 0.61
DE  Interaction: Q9H0R8; IntAct: EBI-7679924; Score: 0.57
DE  Interaction: P60520; IntAct: EBI-7679985; Score: 0.54
DE  Interaction: O95166; IntAct: EBI-7679950; Score: 0.54
DE  Interaction: Q9H492; IntAct: EBI-7680044; Score: 0.65
DE  Interaction: P38182; IntAct: EBI-7680182; Score: 0.44
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0042803;
GO  GO:0071456;
GO  GO:0051607;
GO  GO:0097345;
GO  GO:0035694;
GO  GO:0043066;
GO  GO:0060548;
GO  GO:0010917;
GO  GO:0043065;
GO  GO:0016239;
GO  GO:0035794;
GO  GO:1903146;
GO  GO:0043067;
GO  GO:1903214;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSHLVEPPPPLHNNNNNCEEGEQPLPPPAGLNSSWVELPMNSSNGNENGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHE
SQ  SGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHP
SQ  KRAASLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
//
ID  Q12982;
PN  BCL2/adenovirus E1B 19 kDa protein-interacting protein 2;
GN  BNIP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Note=Localizes to the nuclear envelope region and to other cytoplasmic structures.
DR  UNIPROT: Q12982;
DR  UNIPROT: B4DS94;
DR  Pfam: PF12496;
DR  Pfam: PF13716;
DR  PROSITE: PS50191;
DR  OMIM: 603292;
DR  DisGeNET: 663;
DE  Function: Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins.
DE  Reference Proteome: Yes;
DE  Interaction: O14681; IntAct: EBI-24742623; Score: 0.56
DE  Interaction: O60238; IntAct: EBI-849923; Score: 0.37
DE  Interaction: P03247; IntAct: EBI-849887; Score: 0.37
DE  Interaction: P10415; IntAct: EBI-849945; Score: 0.37
DE  Interaction: O43889; IntAct: EBI-760141; Score: 0.37
DE  Interaction: Q8ZAE1; IntAct: EBI-2874833; Score: 0.00
DE  Interaction: P42685; IntAct: EBI-8640766; Score: 0.83
DE  Interaction: P08107; IntAct: EBI-5659534; Score: 0.00
DE  Interaction: B2R9H7; IntAct: EBI-10175714; Score: 0.56
DE  Interaction: Q07866; IntAct: EBI-10224717; Score: 0.56
DE  Interaction: Q969F0; IntAct: EBI-10227522; Score: 0.72
DE  Interaction: Q9ULV0; IntAct: EBI-10227532; Score: 0.56
DE  Interaction: Q8IUY3; IntAct: EBI-24286337; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24288305; Score: 0.56
DE  Interaction: Q92520; IntAct: EBI-24296511; Score: 0.56
DE  Interaction: O75477; IntAct: EBI-24319282; Score: 0.56
DE  Interaction: P50221; IntAct: EBI-24506124; Score: 0.56
DE  Interaction: O95070; IntAct: EBI-24520784; Score: 0.56
DE  Interaction: O15499; IntAct: EBI-24526443; Score: 0.56
DE  Interaction: Q9NRZ7; IntAct: EBI-24609790; Score: 0.56
DE  Interaction: Q6P587; IntAct: EBI-24614147; Score: 0.56
DE  Interaction: Q96Q45; IntAct: EBI-24619126; Score: 0.56
DE  Interaction: P0C671; IntAct: EBI-24627238; Score: 0.56
DE  Interaction: Q6ZPD8; IntAct: EBI-24631723; Score: 0.56
DE  Interaction: H3BQL7; IntAct: EBI-23670177; Score: 0.56
DE  Interaction: Q8TED1; IntAct: EBI-24667727; Score: 0.56
DE  Interaction: Q9UH17; IntAct: EBI-24673525; Score: 0.56
DE  Interaction: Q8TB40; IntAct: EBI-23694319; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-24684836; Score: 0.56
DE  Interaction: Q7Z769; IntAct: EBI-24696473; Score: 0.56
DE  Interaction: P00387; IntAct: EBI-24717088; Score: 0.56
DE  Interaction: Q7Z7G2; IntAct: EBI-24717755; Score: 0.56
DE  Interaction: P21579; IntAct: EBI-24733989; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-23808606; Score: 0.56
DE  Interaction: Q9NUM3; IntAct: EBI-24742735; Score: 0.56
DE  Interaction: Q5T7V8; IntAct: EBI-24753105; Score: 0.56
DE  Interaction: O95562; IntAct: EBI-24755839; Score: 0.56
DE  Interaction: Q9BSY9; IntAct: EBI-24793885; Score: 0.56
DE  Interaction: Q5JX71; IntAct: EBI-25279273; Score: 0.56
DE  Interaction: Q8N9I0; IntAct: EBI-25280067; Score: 0.56
DE  Interaction: Q12983; IntAct: EBI-24385418; Score: 0.56
DE  Interaction: Q5T700; IntAct: EBI-24407207; Score: 0.56
DE  Interaction: Q8TDF6; IntAct: EBI-24570628; Score: 0.56
DE  Interaction: P32243; IntAct: EBI-24572235; Score: 0.56
DE  Interaction: Q96LJ7; IntAct: EBI-24573986; Score: 0.56
DE  Interaction: O15393; IntAct: EBI-24575163; Score: 0.56
DE  Interaction: Q9H9P2; IntAct: EBI-24641706; Score: 0.56
DE  Interaction: Q8TBB6; IntAct: EBI-24647910; Score: 0.56
DE  Interaction: Q53GL0; IntAct: EBI-24648150; Score: 0.56
DE  Interaction: Q9H400; IntAct: EBI-24652262; Score: 0.56
DE  Interaction: O00623; IntAct: EBI-24758990; Score: 0.56
DE  Interaction: O95279; IntAct: EBI-24798641; Score: 0.56
DE  Interaction: Q07960; IntAct: EBI-20733446; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0005096;
GO  GO:0006915;
GO  GO:0043066;
GO  GO:0090649;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGVELKEEWQDEDFPIPLPEDDSIEADILAITGPEDQPGSLEVNGNKVRKKLMAPDISLTLDPSDGSVLSDDLDESGEI
SQ  DLDGLDTPSENSNEFEWEDDLPKPKTTEVIRKGSITEYTAAEEKEDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYY
SQ  GDGLNAIVVFAVCFMPESSQPNYRYLMDNLFKYVIGTLELLVAENYMIVYLNGATTRRKMPSLGWLRKCYQQIDRRLRKN
SQ  LKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQVDQELNGKQDEPKNEQ
//
ID  O54940;
PN  BCL2/adenovirus E1B 19 kDa protein-interacting protein 2;
GN  Bnip2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localizes to the nuclear envelope region and to other cytoplasmic structures. {ECO:0000250}.
DR  UNIPROT: O54940;
DR  UNIPROT: Q8K4H0;
DR  Pfam: PF12496;
DR  Pfam: PF13716;
DR  PROSITE: PS50191;
DE  Function: Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0031616;
GO  GO:0006915;
GO  GO:0001824;
GO  GO:0007098;
GO  GO:0043410;
GO  GO:0045666;
GO  GO:0051057;
GO  GO:0051146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGVELKEEWQDEDFPIPLPEDDSIEADTLDGTDPDRQPGSLEVNGNKVRKKLMAPDISLTLDPGEDSLWSDDLDEAGEV
SQ  DLEGLDTPSENSDEFEWEDDLPKPKTTEVIRKGSITEYTATEEKGDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYY
SQ  GDGLNAIVVFAVCFMPESGQPNYRYLMDNLFKYVIGTLELLVAENYMIIYLNGATTRRKMPSLGWLRRCYQQIDRRLRKN
SQ  LKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQYEEEKFKKRQKRVDQELNGKQE
SQ  PPKSEQ
//
ID  Q709R6;
PN  LEM domain-containing protein Bocksbeutel;
GN  bocks;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:24700158}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16439308}. Note=Detected in the nucleus envelope and cytoplasm. In the cytoplasm, it appears to localize to discrete foci. {ECO:0000269|PubMed:15035436, ECO:0000305|PubMed:15035436}. [Isoform A]: Nucleus, nucleoplasm {ECO:0000269|PubMed:15035436}. Cytoplasm {ECO:0000269|PubMed:15035436}. Note=Predominantly expressed in the nucleoplasm with very low expression levels in the cytoplasm. {ECO:0000269|PubMed:15035436}. [Isoform B]: Nucleus inner membrane {ECO:0000269|PubMed:15035436}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:15035436}. Note=Appears to be predominantly expressed in the nucleus envelope but expression is not uniform. Outside of the nucleus it is located to discrete foci which may be the endoplasmic reticulum. {ECO:0000269|PubMed:15035436, ECO:0000305|PubMed:15035436}.
DR  UNIPROT: Q709R6;
DR  UNIPROT: Q8SZZ5;
DR  UNIPROT: Q9VHA7;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Inner nuclear membrane protein (PubMed:15035436, PubMed:24700158). May have a role in maintaining the structural integrity of the nuclear lamina (PubMed:24700158). During pupal development, plays essential and redundant functions with the other LEM domain proteins; MAN1 and Ote (PubMed:24700158). Also has a redundant but important role with Ote in larval development (PubMed:24700158). {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:24700158}.
DE  Reference Proteome: Yes;
DE  Interaction: O76454; IntAct: EBI-256393; Score: 0.00
DE  Interaction: Q7JR34; IntAct: EBI-268668; Score: 0.00
DE  Interaction: Q9VC86; IntAct: EBI-279174; Score: 0.00
DE  Interaction: Q06559; IntAct: EBI-281575; Score: 0.00
DE  Interaction: Q9VVQ1; IntAct: EBI-282628; Score: 0.00
DE  Interaction: Q9VLU0; IntAct: EBI-282809; Score: 0.00
DE  Interaction: O01666; IntAct: EBI-283293; Score: 0.00
DE  Interaction: Q94524; IntAct: EBI-26751768; Score: 0.49
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0007049;
GO  GO:0051301;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSDLSYLDTLGNKELLAKCLEHGLPGVPVTDSTRSVIIRRLKAKITGVPLNKSKSASKKAIPRRETVHGSQVTTPTSEPV
SQ  RRTPGKSAGRTSSNNNKISEQSRRTIAYGLDNTSISGRSVQTTTTVSDMSSQSEDDDSYMVDSPVPNYSKDQQPRRYVSL
SQ  AKSGVLTTSYTREVDQPLYEQEDIPRSYTYERPHVPAATLHALPTYEPRIEPSTYRPTDLGFSRPLLTQTNLNSTSYEES
SQ  STYNPKLSPISPRNTFSGSARPFGGPAPAPAPIRQRQSVPVSGSNLARGRLLQPTTAVNTLYPQLNEFYDQPNDAGEPME
SQ  TESESEVEEVPINSHFQKNRFSPLARKPLVRHHDQVSPMAQFRALAVSLDQKYNLKFYLILVVSVMLATMVYVVLTPNA
//
ID  Q9UMX3;
PN  Bcl-2-related ovarian killer protein;
GN  BOK;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: [Isoform 1]: Mitochondrion membrane {ECO:0000250|UniProtKB:O35425}; Single-pass membrane protein {ECO:0000250|UniProtKB:O35425}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27076518}; Single-pass membrane protein {ECO:0000250|UniProtKB:O35425}. Mitochondrion inner membrane {ECO:0000269|PubMed:24113155}. Cytoplasm {ECO:0000269|PubMed:15868100, ECO:0000269|PubMed:16302269, ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:20673843, ECO:0000269|PubMed:24113155}. Nucleus {ECO:0000269|PubMed:16302269, ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:20673843}. Mitochondrion {ECO:0000269|PubMed:15102863, ECO:0000269|PubMed:15868100, ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:27076518}. Endoplasmic reticulum {ECO:0000269|PubMed:16302269}. Mitochondrion outer membrane {ECO:0000269|PubMed:27076518}. Early endosome membrane {ECO:0000250|UniProtKB:O35425}. Recycling endosome membrane {ECO:0000250|UniProtKB:O35425}. Nucleus outer membrane {ECO:0000250|UniProtKB:O35425}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:O35425}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:O35425}. Membrane {ECO:0000269|PubMed:19942931}. Note=Nuclear and cytoplasmic compartments in the early stages of apoptosis and during apoptosis it associates with mitochondria (PubMed:19942931). In healthy cells, associates loosely with the membrane in a hit-and-run mode. The insertion and accumulation on membranes is enhanced through the activity of death signals, resulting in the integration of the membrane-bound protein into the membrane (PubMed:15868100). The transmembrane domain controls subcellular localization; constitutes a tail-anchor. Localizes in early and late endosome upon blocking of apoptosis. Must localize to the mitochondria to induce mitochondrial outer membrane permeabilization and apoptosis (By similarity). {ECO:0000250|UniProtKB:O35425, ECO:0000269|PubMed:15868100, ECO:0000269|PubMed:19942931}. [Isoform 2]: Membrane {ECO:0000269|PubMed:19942931}. Cytoplasm {ECO:0000269|PubMed:19942931}.
DR  UNIPROT: Q9UMX3;
DR  PDB: 6CKV;
DR  Pfam: PF00452;
DR  PROSITE: PS50062;
DR  OMIM: 605404;
DR  DisGeNET: 666;
DE  Function: [Isoform 1]: Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:27076518, PubMed:15102863, PubMed:20673843). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner (PubMed:27076518, PubMed:15102863). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (By similarity). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD- proteasome degradation system, resulting in cytochrome c release (PubMed:27076518). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner (PubMed:15102863). Plays a role in granulosa cell apoptosis by CASP3 activation (PubMed:20673843). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (By similarity). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression (PubMed:19942931). May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (PubMed:24113155). {ECO:0000250|UniProtKB:O35425, ECO:0000269|PubMed:15102863, ECO:0000269|PubMed:19942931, ECO:0000269|PubMed:20673843, ECO:0000269|PubMed:24113155, ECO:0000269|PubMed:27076518}. [Isoform 2]: Pro-apoptotic molecule exerting its function through the mitochondrial pathway. {ECO:0000269|PubMed:15775999}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8NC60; IntAct: EBI-7105200; Score: 0.37
DE  Interaction: A2RU30; IntAct: EBI-21861544; Score: 0.35
DE  Interaction: P13637; IntAct: EBI-25832700; Score: 0.56
DE  Interaction: P50570; IntAct: EBI-25844480; Score: 0.56
DE  Interaction: Q86V38; IntAct: EBI-25846172; Score: 0.56
DE  Interaction: P10809; IntAct: EBI-25872088; Score: 0.56
DE  Interaction: P16284; IntAct: EBI-25881099; Score: 0.56
DE  Interaction: Q8TB36; IntAct: EBI-25923268; Score: 0.56
GO  GO:0033106;
GO  GO:0005737;
GO  GO:0031901;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005743;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005640;
GO  GO:0005634;
GO  GO:0055038;
GO  GO:0032588;
GO  GO:0051400;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0031625;
GO  GO:0006919;
GO  GO:0008635;
GO  GO:0006915;
GO  GO:0007420;
GO  GO:0006921;
GO  GO:0097192;
GO  GO:0072332;
GO  GO:0008630;
GO  GO:0008584;
GO  GO:0051902;
GO  GO:1901029;
GO  GO:0060546;
GO  GO:0043524;
GO  GO:0051402;
GO  GO:0048709;
GO  GO:0043065;
GO  GO:1902237;
GO  GO:1900119;
GO  GO:2001244;
GO  GO:1901030;
GO  GO:1903899;
GO  GO:0051259;
GO  GO:0010506;
GO  GO:1901382;
GO  GO:0051480;
GO  GO:1904708;
GO  GO:0001836;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERAAPVPGRLAEVCAVLLRLGDELEMI
SQ  RPSVYRNVARQLHISLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYAVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKT
SQ  LATWLRRRGGWTDVLKCVVSTDPGLRSHWLVAALCSFGRFLKAAFFVLLPER
//
ID  O35425;
PN  Bcl-2-related ovarian killer protein;
GN  Bok;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Mitochondrion membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass membrane protein {ECO:0000269|PubMed:26949185}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass membrane protein {ECO:0000269|PubMed:26949185}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UMX3}. Cytoplasm {ECO:0000250|UniProtKB:Q9UMX3}. Nucleus {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion {ECO:0000250|UniProtKB:Q9UMX3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9UMX3}. Early endosome membrane {ECO:0000269|PubMed:23429263}. Recycling endosome membrane {ECO:0000269|PubMed:23429263}. Nucleus outer membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23429263}. Membrane {ECO:0000250|UniProtKB:Q9UMX3}. Note=Nuclear and cytoplasmic compartments in the early stages of apoptosis and during apoptosis associates with mitochondria. In healthy cells, associates loosely with the membrane in a hit-and-run mode. The insertion and accumulation on membranes is enhanced through the activity of death signals, resulting in the integration of the membrane-bound protein into the membrane (By similarity). The transmembrane domain controls subcellular localization; constitutes a tail-anchor (PubMed:23429263, PubMed:26949185). Localizes in early and late endosome upon blocking of apoptosis (PubMed:23429263). Must localize to the mitochondria to induce mitochondrial outer membrane permeabilization and apoptosis (PubMed:26949185). {ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}.
DR  UNIPROT: O35425;
DR  Pfam: PF00452;
DR  PROSITE: PS50062;
DE  Function: Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:23429263, PubMed:26015568, PubMed:26949185, PubMed:27098698, PubMed:9535847). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1- independent manner (PubMed:23429263, PubMed:26015568, PubMed:26949185). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (PubMed:26015568). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD- proteasome degradation system, resulting in cytochrome c release (PubMed:9535847, PubMed:26949185). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner. Plays a role in granulosa cell apoptosis by CASP3 activation (By similarity). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (PubMed:27098698). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression.May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (By similarity). {ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26015568, ECO:0000269|PubMed:26949185, ECO:0000269|PubMed:27098698, ECO:0000269|PubMed:9535847}.
DE  Reference Proteome: Yes;
GO  GO:0033106;
GO  GO:0005737;
GO  GO:0031901;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005743;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005640;
GO  GO:0005634;
GO  GO:0055038;
GO  GO:0032588;
GO  GO:0051400;
GO  GO:0046983;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0031625;
GO  GO:0006919;
GO  GO:0008635;
GO  GO:0006915;
GO  GO:0007420;
GO  GO:0006921;
GO  GO:0097192;
GO  GO:0072332;
GO  GO:0008630;
GO  GO:0008584;
GO  GO:0051902;
GO  GO:1901029;
GO  GO:0060546;
GO  GO:0043524;
GO  GO:0051402;
GO  GO:0048709;
GO  GO:0043065;
GO  GO:1902237;
GO  GO:1900119;
GO  GO:2001244;
GO  GO:1901030;
GO  GO:1903899;
GO  GO:0051259;
GO  GO:0010506;
GO  GO:1901382;
GO  GO:0051480;
GO  GO:1904708;
GO  GO:0001836;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQ
SQ  IRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRK
SQ  TLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER
//
ID  Q792S6;
PN  Bcl-2-related ovarian killer protein;
GN  Bok;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Mitochondrion membrane {ECO:0000250|UniProtKB:O35425}; Single-pass membrane protein {ECO:0000250|UniProtKB:O35425}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UMX3}; Single-pass membrane protein {ECO:0000250|UniProtKB:O35425}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UMX3}. Cytoplasm {ECO:0000250|UniProtKB:Q9UMX3}. Nucleus {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion {ECO:0000250|UniProtKB:Q9UMX3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9UMX3}. Early endosome membrane {ECO:0000250|UniProtKB:O35425}. Recycling endosome membrane {ECO:0000250|UniProtKB:O35425}. Nucleus outer membrane {ECO:0000250|UniProtKB:O35425}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:O35425}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:O35425}. Membrane {ECO:0000250|UniProtKB:Q9UMX3}. Note=Nuclear and cytoplasmic compartments in the early stages of apoptosis and during apoptosis it associates with mitochondria. In healthy cells, associates loosely with the membrane in a hit-and-run mode. The insertion and accumulation on membranes is enhanced through the activity of death signals, resulting in the integration of the membrane-bound protein into the membrane (By similarity). The transmembrane domain controls subcellular localization; constitutes a tail-anchor. Localizes in early and late endosome upon blocking of apoptosis. Must localize to the mitochondria to induce mitochondrial outer membrane permeabilization and apoptosis (By similarity). {ECO:0000250|UniProtKB:O35425, ECO:0000250|UniProtKB:Q9UMX3}.
DR  UNIPROT: Q792S6;
DR  UNIPROT: O88857;
DR  Pfam: PF00452;
DR  PROSITE: PS50062;
DE  Function: Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:9356461, PubMed:9804769). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner (By similarity). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (By similarity). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD- proteasome degradation system, resulting in cytochrome c release (By similarity). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner. Plays a role in granulosa cell apoptosis by CASP3 activation (By similarity). Plays a roles as anti- apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (By similarity). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression. May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (By similarity). {ECO:0000250|UniProtKB:O35425, ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:9356461, ECO:0000269|PubMed:9804769}. [Isoform 2]: Positively regulates apoptotic process in an heterodimerization-independent manner with antiapoptotic Bcl-2 proteins. {ECO:0000269|PubMed:9804769}.
DE  Reference Proteome: Yes;
GO  GO:0033106;
GO  GO:0005737;
GO  GO:0031901;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005743;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005640;
GO  GO:0005634;
GO  GO:0055038;
GO  GO:0032588;
GO  GO:0051400;
GO  GO:0046983;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0031625;
GO  GO:0006919;
GO  GO:0008635;
GO  GO:0006915;
GO  GO:0007420;
GO  GO:0006921;
GO  GO:0097192;
GO  GO:0072332;
GO  GO:0008630;
GO  GO:0008584;
GO  GO:0051902;
GO  GO:1901029;
GO  GO:0060546;
GO  GO:0043524;
GO  GO:0051402;
GO  GO:0048709;
GO  GO:0043065;
GO  GO:1902237;
GO  GO:1900119;
GO  GO:2001244;
GO  GO:1901030;
GO  GO:1903899;
GO  GO:0051259;
GO  GO:0010506;
GO  GO:1901382;
GO  GO:0051480;
GO  GO:1904708;
GO  GO:0001836;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQ
SQ  IRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRK
SQ  TLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER
//
ID  P42674;
PN  Blastula protease 10;
GN  BP10;
OS  7656;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Cytoplasm, cell cortex. Secreted, extracellular space. Note=First detected in a perinuclear region, then in an apical and submembranous position just before its secretion into the perivitelline space.
DR  UNIPROT: P42674;
DR  Pfam: PF01400;
DR  Pfam: PF00431;
DR  PROSITE: PS51864;
DR  PROSITE: PS01180;
DR  PROSITE: PS00022;
DR  PROSITE: PS01186;
DR  PROSITE: PS50026;
DR  PROSITE: PS00142;
DE  Function: Could be involved in the differentiation of ectodermal lineages and subsequent patterning of the embryo.
DE  Reference Proteome: No;
GO  GO:0005938;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0004222;
GO  GO:0008270;
GO  GO:0006508;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKLILFLSGLVSLVLCTLAAPTGDQKEIHTETPPPKKPSETTTPGALKTPQPEPKDEEPTPGAFQGDMMLTEDQQRESKE
SQ  AIDDEMTGRKKRKATIYESQRWPYKVIPYVISPSSSGQSSLIRNAMDHWEQNTCLRFEPRTSSHSRQLGHNAYLSFFRGS
SQ  GCWSYVGKAFNGEQQISIGNGCAYFGTIVHEIGHAIGFHHEQSRPDRDDYINVLYQNIQSGRQHNFAKYTWGRVTSRNVE
SQ  YDVGSIMHYGGYGFSSNGRPTITTRDPRLNSRLGQRIALSPADIELANLIYECDDIEDCAGANECLNGGYHDTECNCVCP
SQ  SGYNGDLCEDAVTTTRPDCSERFTEMTGVITSPNWPGRYEDNMACVYQIEGPPGSTIELTFTEMNIENHAACRYDAVEVR
SQ  KDDINSDGEKFCGNTLPAVQISSGNQMLISFTSDPSITGRGFRATYRIVILTTTQIPDTTTISTTTPVPTTTQATTDETV
SQ  VGSCGGSFGGTQGRVATPNYPNNYDNDLECVYVIEVEIGRRVELDFIDFVLEDETNCRWDSLSINLGDGIKIDMKMCGRE
SQ  YPAASLVSIGNNMELTLISDRSVTDRGFMADYRAIDL
//
ID  O74510;
PN  Bouquet formation protein 3;
GN  bqt3;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19948484}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:19948484}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: O74510;
DE  Function: Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase. {ECO:0000269|PubMed:19948484}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005637;
GO  GO:1990862;
GO  GO:0140473;
GO  GO:0051301;
GO  GO:0045141;
GO  GO:0032200;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGSKCCSSSNTIKVSIYLFLHTLTYGLLNYHLNPRLLASTGVVESDIPYWMSYLSIIMHVGQSLLLQKFNLGYGWLLLT
SQ  KYPVYVLLSTYYLTPLSQIAWAFIIDAISLLVARCFSRANPIKCSNQVNTQYSVSFLFTIMASVLISVLNYISQKIFLNG
SQ  LILGNSHNVVTSLVAPPLPLQYLAHVPIGYVIQRVVFSERPIPQSLFLMIFLTLWNCFIPYSILFSMNWSAMFQVVGAYL
SQ  SQIWIITFICWALSL
//
ID  O60158;
PN  Bouquet formation protein 4;
GN  bqt4;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. Nucleus inner membrane {ECO:0000269|PubMed:19948484}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: O60158;
DR  UNIPROT: Q9USF5;
DR  PDB: 5YBX;
DR  PDB: 5YC2;
DR  PDB: 5YCA;
DR  PDB: 6A6W;
DR  PROSITE: PS51299;
DE  Function: Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase. {ECO:0000269|PubMed:19948484}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:1990862;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0140473;
GO  GO:0051301;
GO  GO:0070197;
GO  GO:0045141;
GO  GO:0044820;
GO  GO:0000723;
GO  GO:0032200;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MTENEKSRSLPAERNPLYKDDTLDHTPLIPKCRAQVIEFPDGPATFVRLKCTNPESKVPHFLMRMAKDSSISATSMFRSA
SQ  FPKATQEEEDLEMRWIRDNLNPIEDKRVAGLWVPPADALALAKDYSMTPFINALLEASSTPSTYATPSRPTAQKSETSEG
SQ  EPESSTSATTTSVARRTRQRLAEHLENSKKTILQHDNKEEDKEIHSEENETKDEIKSEKKEPEIKKQEGGSSTEKVGQPS
SQ  SSDDKAKGSTSKDQPSEEEEKTSDIQDRKIKTPIKPSLLGKIRSSVNKGMTDVASQVNRGMTDVASQVNKGVNGVASQVN
SQ  KGMNGVANQVNKGVTGVASQVRKPVGKLEKKFENLEKSIGDTLKSSIRSSPKSKKRSREDFEENEDYNAMVPVKRSRITK
SQ  LESEVYYEKRKVRALGGIAIGLGVGAILPFLF
//
ID  Q32L83;
PN  Brain protein I3;
GN  BRI3;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Lysosome membrane {ECO:0000250|UniProtKB:O95415}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95415}. Note=Co-localizes with MGAT1 and IFITM3 at the perinuclear region. {ECO:0000250|UniProtKB:O95415}.
DR  UNIPROT: Q32L83;
DR  Pfam: PF10164;
DE  Function: Participates in tumor necrosis factor-alpha (TNF)-induced cell death. May be a target of Wnt/beta-catenin signaling in the liver. {ECO:0000250|UniProtKB:O95415}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0048471;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDHKPLLQERPPAYNLEAGQGEFACAPHGYGAIAAAPPPPYPYLVTGIPTHHPRVYNIHSRNVTRYPANSIVVVGGCPVC
SQ  RVGVLEDSFTFLGIFLAIVLFPFGFICCFALRKRRCPNCGANFT
//
ID  Q99N46;
PN  Brain protein I3;
GN  I3;
OS  10141;
SL  Nucleus Position: SL-0198;
SL  Comments: Lysosome membrane {ECO:0000250|UniProtKB:O95415}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95415}. Note=Co-localizes with MGAT1 and IFITM3 at the perinuclear region. {ECO:0000250|UniProtKB:O95415}.
DR  UNIPROT: Q99N46;
DR  Pfam: PF10164;
DE  Function: Participates in tumor necrosis factor-alpha (TNF)-induced cell death. May be a target of Wnt/beta-catenin signaling in the liver. {ECO:0000250|UniProtKB:O95415}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0048471;
GO  GO:0042802;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDHKPLLQERPPAYNLEAGQGDYACGAPGYGAIPSAPPPPPYPYLVTGIPTPHPRVYSIHSRTVTRYPANSIVVVGGCPV
SQ  CRVGVLEDCFTFLGIFLAIILFPFGFICCFALRKRRCPNCGATFT
//
ID  O95415;
PN  Brain protein I3;
GN  BRI3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Lysosome membrane {ECO:0000305|PubMed:14592447}; Multi-pass membrane protein {ECO:0000255}. [Isoform 1]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:30983867}. Note=Co-localizes with MGAT1 and IFITM3 at the perinuclear region. {ECO:0000269|PubMed:30983867}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:30983867}. Nucleus {ECO:0000269|PubMed:30983867}. Note=Diffuse localization in the cytoplasm and nucleus. {ECO:0000269|PubMed:30983867}.
DR  UNIPROT: O95415;
DR  UNIPROT: D6W5R8;
DR  UNIPROT: F5GXW6;
DR  UNIPROT: Q8WV52;
DR  UNIPROT: Q9UIC6;
DR  Pfam: PF10164;
DR  OMIM: 615628;
DR  DisGeNET: 25798;
DE  Function: Participates in tumor necrosis factor-alpha (TNF)-induced cell death (PubMed:14592447). May be a target of Wnt/beta-catenin signaling in the liver (PubMed:20538055). {ECO:0000269|PubMed:14592447, ECO:0000269|PubMed:20538055}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A380PDF6; IntAct: EBI-2874795; Score: 0.00
DE  Interaction: Q13021; IntAct: EBI-24525743; Score: 0.56
DE  Interaction: O95870; IntAct: EBI-24537575; Score: 0.56
DE  Interaction: Q01628; IntAct: EBI-25503997; Score: 0.54
DE  Interaction: P26572; IntAct: EBI-25504004; Score: 0.54
DE  Interaction: P16871; IntAct: EBI-25507926; Score: 0.37
DE  Interaction: Q8WY22; IntAct: EBI-25504211; Score: 0.57
DE  Interaction: P46934; IntAct: EBI-30832228; Score: 0.44
DE  Interaction: P46937; IntAct: EBI-30846229; Score: 0.44
GO  GO:0035577;
GO  GO:0016021;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0042802;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDHKPLLQERPPAYNLEAGQGDYACGPHGYGAIPAAPPPPPYPYLVTGIPTHHPRVYNIHSRTVTRYPANSIVVVGGCPV
SQ  CRVGVLEDCFTFLGIFLAIILFPFGFICCFALRKRRCPNCGATFA
//
ID  P28662;
PN  Brain protein I3;
GN  Bri3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Lysosome membrane {ECO:0000250|UniProtKB:O95415}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95415}. Note=Co-localizes with MGAT1 and IFITM3 at the perinuclear region. {ECO:0000250|UniProtKB:O95415}.
DR  UNIPROT: P28662;
DR  UNIPROT: Q501N3;
DR  UNIPROT: Q9Z1S1;
DR  Pfam: PF10164;
DE  Function: Participates in tumor necrosis factor-alpha (TNF)-induced cell death (Ref.4). May be a target of Wnt/beta-catenin signaling in the liver (By similarity). {ECO:0000250|UniProtKB:O95415, ECO:0000269|Ref.4}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0048471;
GO  GO:0042802;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDHKPLLQERPPAYNLEAGQGDYACGPHGYGAIPTAPPPPPYPYLVTGIPTSHPRVYNIHSRTVTRYPANSIVVVGGCPV
SQ  CRVGVLEYCFTCLGIFLAIVLFPFGFLCCFALRKRRCPNCGAVFT
//
ID  Q5PPK1;
PN  Brain protein I3;
GN  Bri3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Lysosome membrane {ECO:0000250|UniProtKB:O95415}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95415}. Note=Co-localizes with MGAT1 and IFITM3 at the perinuclear region. {ECO:0000250|UniProtKB:O95415}.
DR  UNIPROT: Q5PPK1;
DR  Pfam: PF10164;
DE  Function: Participates in tumor necrosis factor-alpha (TNF)-induced cell death. May be a target of Wnt/beta-catenin signaling in the liver. {ECO:0000250|UniProtKB:O95415}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0048471;
GO  GO:0042802;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDHKPLLQERPPAYNLEAGQGDYACGPHGYGAIPTAPPPPPYPYLVTGIPTSHPRVYNIHSRAVTRYPANSIVVVGGCPV
SQ  CRVGVLEYCFTCLGIFLAIVLFPFGFLCCFALRKRRCPNCGAVFT
//
ID  P38770;
PN  Nucleus export protein BRL1;
GN  BRL1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15882446}; Multi-pass membrane protein {ECO:0000269|PubMed:15882446}.
DR  UNIPROT: P38770;
DR  UNIPROT: D3DKY3;
DR  Pfam: PF10104;
DE  Function: Involved in mRNA and protein export from nucleus. {ECO:0000269|PubMed:15882446}.
DE  Reference Proteome: Yes;
DE  Interaction: P16140; IntAct: EBI-800112; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-800112; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-800112; Score: 0.53
DE  Interaction: P11484; IntAct: EBI-800112; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-800112; Score: 0.53
DE  Interaction: P12709; IntAct: EBI-800112; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-800112; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-800112; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-800112; Score: 0.35
DE  Interaction: P47088; IntAct: EBI-856804; Score: 0.00
DE  Interaction: P02829; IntAct: EBI-864646; Score: 0.00
DE  Interaction: P13393; IntAct: EBI-7738433; Score: 0.44
DE  Interaction: P29056; IntAct: EBI-8224002; Score: 0.22
DE  Interaction: P46985; IntAct: EBI-2347758; Score: 0.37
DE  Interaction: P10591; IntAct: EBI-3667891; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3743771; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3750479; Score: 0.35
DE  Interaction: Q9UJW9; IntAct: EBI-11529461; Score: 0.56
DE  Interaction: Q9BXL8; IntAct: EBI-11529452; Score: 0.56
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0055088;
GO  GO:0051028;
GO  GO:0006998;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESFENLSIRDSFTSGMEHVDEELGGLSDLSISKQGPTLSPQLINRFMPHFPSSPSPLRNTLDFSAAKADEEEDDRMEID
SQ  EVDDTSFEEEYNNEPIETHTEATENAVVEEIEATPEERQKQEKNESQDQSVEEVENIVSPHRSTVIKALLSPTDLGVAAA
SQ  TKVEGVVPLPPSANQDDNESSNNNAEGEDIIRNEEVEDEIKSSLGNHKSSQYANAFDSEIIKRELRSRSKYQPIQVSFNT
SQ  HNYFYSDKDGIKTYSLTKPNHNKIDEFYDQNEAFKLPKPWSPNSHPASRASYALMSYLQLFLNAITTVVIFSFILSFIIA
SQ  LQKDLKSTWEQRKHELQYESRICQEQYLTNRCNQTPGLPALGEQCAIWKQCMDRNNDIFFRARSTLSAKLFGDIINSFID
SQ  PLNWKTLFVIFCGVITWCFSSNFLLGFVRAKSYYGNGIKTYPLPSSPKSPTSEETHSSMTASGEDSHLLKQ
//
ID  Q9UT30;
PN  Nucleus export protein brr6;
GN  brr6;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Multi- pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9UT30;
DR  Pfam: PF10104;
DE  Function: Involved in mRNA and protein export from nucleus. {ECO:0000250|UniProtKB:P38770, ECO:0000269|PubMed:17993570}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0044732;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:1990578;
GO  GO:0055088;
GO  GO:0140480;
GO  GO:0051028;
GO  GO:0006998;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEMYVEDVPMPDIGPDSVLNTPIRPKYEILKSKKKTQNENDPEPMDISMSPDEKNLKKSTVRRKLRKSKPNSSSNQVSSR
SQ  TRALTKRSNSSNAIIKANNQDSVYVSDWTNVHRDIPIVVSGYLQLMFNACVASIFLYFLFKIVFGIQNDVRNRVEYHKIL
SQ  QEEQAADCQREYLSINCDSPGPAIFEVCQKLKQCKMESSNNVGSTKLAALVFAEIIDAFISHISYKTMVFSLILVFGSLL
SQ  TSNYAFGLYRARHSQNIHDYAANAIPAMIPSSRFLPSNLSDISNRNLIEAASQEEEI
//
ID  P53062;
PN  Nucleus export protein BRR6;
GN  BRR6;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:14562095}.
DR  UNIPROT: P53062;
DR  UNIPROT: D6VV88;
DR  Pfam: PF10104;
DE  Function: Required for mRNA nuclear export. Involved in the nuclear pore complex (NPC) distribution and nuclear envelope morphology. {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:15882446}.
DE  Reference Proteome: Yes;
DE  Interaction: P25611; IntAct: EBI-2347149; Score: 0.37
DE  Interaction: P11484; IntAct: EBI-3778254; Score: 0.35
GO  GO:0071944;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0055088;
GO  GO:0051028;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELRSFSRQPDGILANPRLGREEVLEGEHPQDARLARQSIWLSPSLIAEYIQLFFNFIIGTIGLSLAIKFILMIRNDVNL
SQ  KLEHNVREELDKIATCKSRYFENQCEPHMRVPALEVRCNEWSKCMNKEIVSGSDYQWAKAWARTLAEVINAFFEAFSIRS
SQ  FLFILISIIGIIFVTNTSFGSYRVYLNNKDTKSVRHA
//
ID  Q8IWQ3;
PN  Serine/threonine-protein kinase BRSK2;
GN  BRSK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Endoplasmic reticulum. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin.
DR  UNIPROT: Q8IWQ3;
DR  UNIPROT: B3KVE9;
DR  UNIPROT: E9PLM7;
DR  UNIPROT: O60843;
DR  UNIPROT: O95099;
DR  UNIPROT: Q5J5B4;
DR  UNIPROT: Q6ZMQ4;
DR  UNIPROT: Q8TB60;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 609236;
DR  DisGeNET: 9024;
DE  Function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr- 174 can inhibit insulin secretion (PubMed:22798068), BRSK2 phosphorylated at Thr-260 can promote insulin secretion (PubMed:22669945). Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress. {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:22798068, ECO:0000269|PubMed:23029325}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8WVZ9; IntAct: EBI-3232144; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: Q9Y4K3; IntAct: EBI-24471109; Score: 0.56
DE  Interaction: Q96RY5; IntAct: EBI-28942454; Score: 0.35
DE  Interaction: P61769; IntAct: EBI-28942454; Score: 0.35
DE  Interaction: P02452; IntAct: EBI-28942454; Score: 0.35
DE  Interaction: Q8TDC3; IntAct: EBI-28943702; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-30872909; Score: 0.64
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0150034;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0060590;
GO  GO:0000287;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0048156;
GO  GO:0050321;
GO  GO:0031532;
GO  GO:0007409;
GO  GO:0051301;
GO  GO:0042149;
GO  GO:0036503;
GO  GO:0030010;
GO  GO:0006887;
GO  GO:0000086;
GO  GO:0035556;
GO  GO:0070059;
GO  GO:0090176;
GO  GO:0030182;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0043462;
GO  GO:0050770;
GO  GO:0061178;
GO  GO:0010975;
GO  GO:1904152;
GO  GO:2000807;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTSTGKDGGAQHAQYVGPYRLEKTLGKGQTGLVKLGVHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLK
SQ  LHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDEKNNIRIADF
SQ  GMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIP
SQ  PDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQ
SQ  DLLSEEENQEKMIYFLLLDRKERYPSQEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRA
SQ  IEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRARLN
SQ  SIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFISLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPSL
SQ  SHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDPP
SQ  AAQHLSDTTNCMEMMTGRLSKCGSPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGPGGDAEYPTG
SQ  KDTAKMGPPTARREQP
//
ID  Q69Z98;
PN  Serine/threonine-protein kinase BRSK2;
GN  Brsk2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin (By similarity). {ECO:0000250}.
DR  UNIPROT: Q69Z98;
DR  UNIPROT: Q699J3;
DR  UNIPROT: Q699J4;
DR  UNIPROT: Q6DMN7;
DR  UNIPROT: Q6PHM0;
DR  PDB: 4YNZ;
DR  PDB: 4YOM;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-504' and 'Ser-554'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr- 175 can inhibit insulin secretion (PubMed:22798068), BRSK2 phosphorylated at Thr-261 can promote insulin secretion (PubMed:22669945). Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress. {ECO:0000269|PubMed:15705853, ECO:0000269|PubMed:17482548, ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:22798068}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0150034;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0000287;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0050321;
GO  GO:0031532;
GO  GO:0007409;
GO  GO:0051301;
GO  GO:0042149;
GO  GO:0036503;
GO  GO:0030010;
GO  GO:0006887;
GO  GO:0000086;
GO  GO:0035556;
GO  GO:0070059;
GO  GO:0090176;
GO  GO:0030182;
GO  GO:0048812;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0050770;
GO  GO:0061178;
GO  GO:0010975;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTSTGKDGGGAQHAQYVGPYRLEKTLGKGQTGLVKLGIHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVL
SQ  KLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDERNNIRIAD
SQ  FGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFI
SQ  PPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLL
SQ  QDLLSEEENQEKMIYFLLLDRKERYPSHEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARR
SQ  AIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRTRL
SQ  NSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFINLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPS
SQ  LSHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDQ
SQ  PSAQHLSDTTNCMEVMTGRLSKCGTPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGGDTEYPMGK
SQ  DMAKMGPPAARREQP
//
ID  D3ZML2;
PN  Serine/threonine-protein kinase BRSK2;
GN  Brsk2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin (By similarity). {ECO:0000250}.
DR  UNIPROT: D3ZML2;
DR  UNIPROT: E9PTC7;
DR  UNIPROT: Q4A1P4;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-523' and 'Ser-573'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr- 175 can inhibit insulin secretion, BRSK2 phosphorylated at Thr-261 can promote insulin secretion. Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P49286; IntAct: EBI-11578535; Score: 0.00
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0150034;
GO  GO:0005783;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0000287;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0050321;
GO  GO:0031532;
GO  GO:0007409;
GO  GO:0051301;
GO  GO:0006974;
GO  GO:0042149;
GO  GO:0036503;
GO  GO:0030010;
GO  GO:0006887;
GO  GO:0000086;
GO  GO:0035556;
GO  GO:0070059;
GO  GO:0090176;
GO  GO:0007095;
GO  GO:0030182;
GO  GO:0048812;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0050770;
GO  GO:0061178;
GO  GO:0010975;
GO  GO:0009411;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTSTGKDGGGAQHAQYVGPYRLEKTLGKGQTGLVKLGIHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVL
SQ  KLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDERNNIRIAD
SQ  FGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFI
SQ  PPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLL
SQ  QDLLSEEENQEKMIYFLLLDRKERYPSHEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARR
SQ  AIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRTRL
SQ  NSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELGHLQLFGNPVSKVRSVAMELVILVQTLAYTSFRLLGTFLPVRY
SQ  LRHSVLSRPPERARLVLRGAPCTHMGPVWNMVGMAYTQNPPIMGETGVYGSQWVMSSAPSKHYTSLGLSVPSPSCSLSPS
SQ  LFPFCAPDTTNCMEVMTGRLSKCGTPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGGDTEYPMGK
SQ  DMAKMGPPAARREQP
//
ID  Q58DP0;
PN  Probable 18S rRNA (guanine-N(7))-methyltransferase;
GN  BUD23;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43709}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O43709}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43709}. Cytoplasm {ECO:0000250|UniProtKB:O43709}. Note=Localized diffusely throughout the nucleus and the cytoplasm. Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes. Localization is not affected by glucocorticoid treatment. {ECO:0000250|UniProtKB:O43709}.
DR  UNIPROT: Q58DP0;
DR  UNIPROT: Q2TBN2;
DR  Pfam: PF08241;
DR  Pfam: PF12589;
DE  Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA- modifying catalytic activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. Locus-specific steroid receptor coactivator. Potentiates transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) receptors. Required for the maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the response elements. Required for maintenance of dimethylation on histone H3 'Lys-79' (H3K79me2), although direct histone methyltransferase activity is not observed in vitro. {ECO:0000250, ECO:0000250|UniProtKB:O43709}.
DE  Reference Proteome: Yes;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0046982;
GO  GO:0016435;
GO  GO:0006325;
GO  GO:2000234;
GO  GO:0070476;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAFRGRRPELRGPPELYYDKNEARKYVRNSRMIDVQIKMTGRALELLCVPEDKPCYVLDIGCGTGLSGDYLSDEGHYWVG
SQ  IDISPAMLDEALDRETQGDVILGDMGQGIPFKPGTFDACISISAVQWLCNANKKSDIPAKRLYCFFSSLYSVLVRGGRAV
SQ  LQLYPENSEQLELITTQATRAGFTGGVVVDYPNSAKAKKFYLCLFSGPSTSLPEGLSEDTEEEKPAESTFTADRIPYRIA
SQ  RRGVVRKSREWVLEKKARRRRQGKEVCPDTQYTGRKRKPRF
//
ID  Q55DA6;
PN  Probable 18S rRNA (guanine-N(7))-methyltransferase;
GN  DDB_G0269722;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43709}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O43709}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43709}. Cytoplasm {ECO:0000250|UniProtKB:O43709}.
DR  UNIPROT: Q55DA6;
DR  Pfam: PF08241;
DR  Pfam: PF12589;
DE  Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity (By similarity). {ECO:0000250}. S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA- modifying catalytic activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. {ECO:0000250, ECO:0000250|UniProtKB:O43709}.
DE  Reference Proteome: Yes;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0016435;
GO  GO:0070476;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRPEHIAPPEIFYDDVESKKYSSNSRIIEIQTKMAERAYELLAIPETAEGLMLLDIGCGSGISGDVITDAGHYWIGCDI
SQ  SQHMLDVAIDREVEGDVMLRDIGQGFPFRAGSFDAAISISAIQWLCNAEKSHHNPRKRLHTFFQSLFNVLTRGGKAILQF
SQ  YPENSAQIEMITASALRCGFSGGLLIDFPNSSKAKKYFLVLFTGNNNIMPSAKGVEGEEYEQQEEEDSNEVKYSNRKRDR
SQ  RRVTKSKGSAQHKTKEWIMNKKDRQRKQGREIKNDSKFSGRKRGPKF
//
ID  O43709;
PN  Probable 18S rRNA (guanine-N(7))-methyltransferase;
GN  BUD23;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:24086612, ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:34948388}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25851604}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25851604}. Cytoplasm {ECO:0000269|PubMed:24488492}. Note=Localized diffusely throughout the nucleus and the cytoplasm (PubMed:24488492). Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes (PubMed:25851604). Localization is not affected by glucocorticoid treatment (PubMed:24488492). {ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:25851604}.
DR  UNIPROT: O43709;
DR  UNIPROT: A8K501;
DR  UNIPROT: C9K060;
DR  UNIPROT: Q96P12;
DR  UNIPROT: Q9BQ58;
DR  UNIPROT: Q9HBP9;
DR  PDB: 6G4W;
DR  Pfam: PF08241;
DR  Pfam: PF12589;
DR  OMIM: 194050;
DR  OMIM: 615733;
DR  DisGeNET: 114049;
DE  Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA (PubMed:25851604). Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity (PubMed:25851604). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA-modifying catalytic activity (PubMed:25851604). Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity (PubMed:24086612). Locus-specific steroid receptor coactivator. Potentiates transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) receptors (PubMed:24488492). Required for the maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the response elements (PubMed:24488492). Required for maintenance of dimethylation on histone H3 'Lys-79' (H3K79me2), although direct histone methyltransferase activity is not observed in vitro (PubMed:24488492). {ECO:0000250, ECO:0000269|PubMed:24086612, ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:25851604}.
DE  Disease: Note=BUD23 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of BUD23 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. {ECO:0000305|PubMed:11978965}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y478; IntAct: EBI-1079549; Score: 0.00
DE  Interaction: P01100; IntAct: EBI-2692676; Score: 0.00
DE  Interaction: Q5NHY6; IntAct: EBI-2799823; Score: 0.00
DE  Interaction: P00973; IntAct: EBI-3942303; Score: 0.37
DE  Interaction: Q16512; IntAct: EBI-3942313; Score: 0.37
DE  Interaction: P55072; IntAct: EBI-3942323; Score: 0.37
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-11145880; Score: 0.35
DE  Interaction: Q9UI30; IntAct: EBI-23853163; Score: 0.83
DE  Interaction: D0UZS0; IntAct: EBI-14064021; Score: 0.35
DE  Interaction: Q9C0C9; IntAct: EBI-21894427; Score: 0.35
DE  Interaction: Q8IUE6; IntAct: EBI-21894427; Score: 0.35
DE  Interaction: Q9IK91; IntAct: EBI-25747231; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-27129711; Score: 0.35
DE  Interaction: P59595; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P15130; IntAct: EBI-27131516; Score: 0.35
DE  Interaction: Q0ZME3; IntAct: EBI-27131755; Score: 0.35
DE  Interaction: Q6Q1R8; IntAct: EBI-27132003; Score: 0.35
DE  Interaction: K9N4V7; IntAct: EBI-27132270; Score: 0.35
DE  Interaction: P33469; IntAct: EBI-27132272; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0008168;
GO  GO:0046982;
GO  GO:0003723;
GO  GO:0016435;
GO  GO:0006325;
GO  GO:2000234;
GO  GO:0070476;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASRGRRPEHGGPPELFYDETEARKYVRNSRMIDIQTRMAGRALELLYLPENKPCYLLDIGCGTGLSGSYLSDEGHYWVG
SQ  LDISPAMLDEAVDREIEGDLLLGDMGQGIPFKPGTFDGCISISAVQWLCNANKKSENPAKRLYCFFASLFSVLVRGSRAV
SQ  LQLYPENSEQLELITTQATKAGFSGGMVVDYPNSAKAKKFYLCLFSGPSTFIPEGLSENQDEVEPRESVFTNERFPLRMS
SQ  RRGMVRKSRAWVLEKKERHRRQGREVRPDTQYTGRKRKPRF
//
ID  Q9CY21;
PN  Probable 18S rRNA (guanine-N(7))-methyltransferase;
GN  Bud23;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43709}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P25627}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43709}. Cytoplasm {ECO:0000250|UniProtKB:O43709}. Note=Localized diffusely throughout the nucleus and the cytoplasm. Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes. Localization is not affected by glucocorticoid treatment. {ECO:0000250|UniProtKB:O43709}.
DR  UNIPROT: Q9CY21;
DR  UNIPROT: Q3U915;
DR  Pfam: PF08241;
DR  Pfam: PF12589;
DE  Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA- modifying catalytic activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. Locus-specific steroid receptor coactivator. Potentiates transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) receptors. Required for the maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the response elements. Required for maintenance of dimethylation on histone H3 'Lys-79' (H3K79me2), although direct histone methyltransferase activity is not observed in vitro. {ECO:0000250|UniProtKB:O43709}.
DE  Reference Proteome: Yes;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046982;
GO  GO:0016435;
GO  GO:0006325;
GO  GO:2000234;
GO  GO:0070476;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASRSRRPEHSGPPELFYDQNEARKYVRNSRMIDIQTKMTERALELLCLPEGQPSYLLDIGCGSGLSGDYISEEGHYWVG
SQ  IDISPAMLDAALDRDTEGDLLLGDMGQGVPFRPGSFDGCISISAVQWLCNANKKSDVPARRLYCFFSSLYSALVRGARAV
SQ  LQLYPENSEQLELITTQATRAGFTGGVVVDFPNSAKAKKFYLCLFSGPSTSLPKGLTESQDADQASESMFTSERAPHKKA
SQ  RRDLVKKSREWVLEKKERRRRQGKEVRPDTQYTGRKRKPRF
//
ID  O22873;
PN  bZIP transcription factor 18;
GN  BZIP18;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27896439}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27896439}. Cytoplasm {ECO:0000269|PubMed:27896439}.
DR  UNIPROT: O22873;
DR  UNIPROT: O23726;
DR  Pfam: PF00170;
DR  PROSITE: PS50217;
DE  Function: Transcription factor that may participate with bZIP34 in the gametophytic control of pollen development. {ECO:0000269|PubMed:27896439}.
DE  Reference Proteome: Yes;
DE  Interaction: Q94AY3; IntAct: EBI-4509008; Score: 0.37
DE  Interaction: Q9LZW4; IntAct: EBI-25522576; Score: 0.56
GO  GO:0005737;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0031490;
GO  GO:0003700;
GO  GO:0043621;
GO  GO:0000976;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDPSNPQPNQSNLSQCPPLATAPTPAPVRGPYHRRAHSEVQFRLPEDLDLSEPFGGFDELGSEDDLFCSYMDIEKLGSG
SQ  SGSASDSAGPSAPRSDNPFSAENGGAEAGNSRPRHRHSLSVDGSSTLESIEAKKAMAPDKLAELWVVDPKRAKRIIANRQ
SQ  SAARSKERKARYILELERKVQTLQTEATTLSAQLSLFQRDTTGLSSENTELKLRLQVMEQQAKLRDALNEQLKKEVERLK
SQ  FATGEVSPADAYNLGMAHMQYQQQPQQSFFQHHHQQQTDAQNLQQMTHQFHLFQPNNNQNQSSRTNPPTAHQLMHHATSN
SQ  APAQSHSYSEAMHEDHLGRLQGLDISSCGRGSNFGRSDTVSESSSTM
//
ID  Q9FWS3;
PN  Zinc finger CCCH domain-containing protein 16;
GN  CG1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q9FWS3;
DR  UNIPROT: F4HZ22;
DR  UNIPROT: Q94C30;
DR  Pfam: PF18044;
DR  PROSITE: PS50103;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9XFM0; IntAct: EBI-25527299; Score: 0.56
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0016567;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRKELCRNFQRGSCRYGENCRFLHPQQAKPNNPFGFGTQNQQQQQQQQQQNSSNPFGFGVQSGGSSRPNQFQNTWSRTAS
SQ  TPTGGGAAASTQQTGKQTQPADHKCTDPAACKRVMQDDFKNERPMWKLTCYGHWKYFPCDVTGDISYEELRAVAYEEAKR
SQ  GIPLQSIVERERNLQNSKIAEFENFLRNPYKGSVTANQSPFAATTPSIFPQSSQINSPSPAFSGFNQQTAFSNTNAGGLS
SQ  SSGPPNAFASFNQQTTFPNTNAGGVSSSGPPNPFASFTQQSNNQQTAFSNTNAGGLSSSGPPNAFASFNKQPNAFSVNTP
SQ  QPVPSGPSGFQTNPSTTFKPASFGPGPGFATTPQNNNIFGQSTPTPATNTSQNNQTAFNFNVPVASFTAPAINTTNTSSG
SQ  TELQIGGDPVDSSIWLKEKWNPGEIPEQAPPDAFV
//
ID  Q9N1R0;
PN  Calcium-binding protein 1;
GN  CABP1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid- anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Postsynaptic density {ECO:0000250}.
DR  UNIPROT: Q9N1R0;
DR  UNIPROT: Q9N1R1;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Modulates calcium-dependent activity of inositol 1,4,5- triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium- dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L- type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but has an opposite effect on channel function. Suppresses the calcium-dependent inactivation of CACNA1D. Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration. Required for the normal transfer of light signals through the retina. {ECO:0000250|UniProtKB:O88751, ECO:0000250|UniProtKB:Q9JLK7, ECO:0000250|UniProtKB:Q9NZU7}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0005246;
GO  GO:0005509;
GO  GO:0048306;
GO  GO:0008139;
GO  GO:0042308;
GO  GO:1901385;
GO  GO:0050896;
GO  GO:0007601;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9NZU7};
SQ  MGNCVKSPLRNLSRKMRQEETSYTVVQTSEEGLAASGELPGPLLMLAQNCAVMHNLLGPACIFLRKGFAENRQPDRSLRP
SQ  EEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGV
SQ  KELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR
//
ID  Q9NZU7;
PN  Calcium-binding protein 1;
GN  CABP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10625670}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14685260}. Cell membrane {ECO:0000269|PubMed:10625670, ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:14685260}; Lipid-anchor; Cytoplasmic side. Golgi apparatus {ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:14685260}. Postsynaptic density {ECO:0000305}. Note=L-CaBP1 is associated most likely with the cytoskeletal structures, whereas S-CaBP1 is localized at or near the plasma membrane. {ECO:0000269|PubMed:10625670}. [Isoform L-CaBP1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10625670}. Note=L-CaBP1 is associated most likely with the cytoskeletal structures. {ECO:0000269|PubMed:10625670}. [Isoform S-CaBP1]: Cytoplasm, cell cortex. Cell membrane {ECO:0000305|PubMed:10625670}; Lipid-anchor {ECO:0000305}. Note=S-CaBP1 is localized at or near the plasma membrane.
DR  UNIPROT: Q9NZU7;
DR  UNIPROT: O95663;
DR  UNIPROT: Q8N6H5;
DR  UNIPROT: Q9NZU8;
DR  PDB: 2K7B;
DR  PDB: 2K7C;
DR  PDB: 2K7D;
DR  PDB: 2LAN;
DR  PDB: 2LAP;
DR  PDB: 3OX5;
DR  PDB: 3OX6;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 605563;
DR  DisGeNET: 9478;
DE  Function: Modulates calcium-dependent activity of inositol 1,4,5- triphosphate receptors (ITPRs)(PubMed:14570872). Inhibits agonist- induced intracellular calcium signaling (PubMed:15980432). Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels (PubMed:11865310). Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C- terminal domain of CACNA1C, but has an opposite effect on channel function (PubMed:15140941). Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels (PubMed:15895247). Prevents NMDA receptor-induced cellular degeneration. Required for the normal transfer of light signals through the retina (By similarity). {ECO:0000250|UniProtKB:O88751, ECO:0000250|UniProtKB:Q9JLK7, ECO:0000269|PubMed:11865310, ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:15140941, ECO:0000269|PubMed:15895247, ECO:0000269|PubMed:15980432}.
DE  Reference Proteome: Yes;
DE  Interaction: P06623; IntAct: EBI-907917; Score: 0.40
DE  Interaction: Q13936; IntAct: EBI-15896764; Score: 0.54
DE  Interaction: P08047; IntAct: EBI-2679915; Score: 0.00
DE  Interaction: P01100; IntAct: EBI-2681402; Score: 0.00
DE  Interaction: Q13107; IntAct: EBI-21883326; Score: 0.40
GO  GO:0070161;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005615;
GO  GO:0000139;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0005246;
GO  GO:0005509;
GO  GO:0048306;
GO  GO:0004857;
GO  GO:0008139;
GO  GO:0042308;
GO  GO:1901385;
GO  GO:0050896;
GO  GO:0007601;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGGGDGAAFKRPGDGARLQRVLGLGSRREPRSLPAGGPAPRRTAPPPPGHASAGPAAMSSHIAKSESKTSLLKAAAAAAS
SQ  GGSRAPRHGPARDPGLPSRRLPGSCPATPQSSGDPSSRRPLCRPAPREEGARGSQRVLPQAHCRPREALPAAASRPSPSS
SQ  PLPPARGRDGEERGLSPALGLRGSLRARGRGDSVPAAASEADPFLHRLRPMLSSAFGQDRSLRPEEIEELREAFREFDKD
SQ  KDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDG
SQ  EISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR
//
ID  Q9N1Q9;
PN  Calcium-binding protein 2;
GN  CABP2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: Q9N1Q9;
DR  Pfam: PF00036;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Required for sound encoding at inner hair cells (IHCs) synapses, likely via inhibition of the inactivation of voltage-gated calcium channel of type 1.3 (Cav1.3) in the IHCs. Required for the normal transfer of light signals through the retina. {ECO:0000250|UniProtKB:Q9JLK4}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005246;
GO  GO:0005509;
GO  GO:1901385;
GO  GO:0050896;
GO  GO:0007605;
GO  GO:0007601;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGNCAKRPRHRAPKDRELRPEEIEELQAAFQEFDRDRDGYIGYQELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFV
SQ  ELMGPKLLAETADMIGVRELRDAFREFDTNGDGCISLGELRAALKALLGERLSQREVDEILRDIDLNGDGLVDFEEFVRM
SQ  MSR
//
ID  Q9NPB3;
PN  Calcium-binding protein 2;
GN  CABP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19338761}. Cell membrane {ECO:0000269|PubMed:19338761}; Lipid-anchor {ECO:0000269|PubMed:19338761}; Cytoplasmic side {ECO:0000269|PubMed:19338761}. Golgi apparatus {ECO:0000269|PubMed:19338761}.
DR  UNIPROT: Q9NPB3;
DR  Pfam: PF00036;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 607314;
DR  OMIM: 614899;
DR  DisGeNET: 51475;
DE  Function: Required for sound encoding at inner hair cells (IHCs) synapses, likely via inhibition of the inactivation of voltage-gated calcium channel of type 1.3 (Cav1.3) in the IHCs (PubMed:28183797). Required for the normal transfer of light signals through the retina (By similarity). {ECO:0000250|UniProtKB:Q9JLK4, ECO:0000269|PubMed:28183797}.
DE  Disease: Deafness, autosomal recessive, 93 (DFNB93) [MIM:614899]: A form of non-syndromic deafness characterized by stable, bilateral, symmetric, prelingual moderate to severe deafness. Hearing impairment is slightly more pronounced in the mid-frequencies, resulting in a distinctive shallow U-shaped audiogram. {ECO:0000269|PubMed:22981119, ECO:0000269|PubMed:28183797}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q7Z3Z2; IntAct: EBI-24796266; Score: 0.56
DE  Interaction: Q5JST6; IntAct: EBI-24280036; Score: 0.56
DE  Interaction: Q9H257; IntAct: EBI-24349898; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-24354781; Score: 0.56
DE  Interaction: Q96ED9; IntAct: EBI-24363653; Score: 0.56
DE  Interaction: P86480; IntAct: EBI-25247799; Score: 0.56
DE  Interaction: Q96M29; IntAct: EBI-25252219; Score: 0.56
DE  Interaction: Q9NPE3; IntAct: EBI-23679380; Score: 0.56
DE  Interaction: Q5T686; IntAct: EBI-23682258; Score: 0.56
DE  Interaction: Q9H1P6; IntAct: EBI-24667738; Score: 0.56
DE  Interaction: Q8IZF2; IntAct: EBI-23695711; Score: 0.56
DE  Interaction: Q9BRK3; IntAct: EBI-23698200; Score: 0.56
DE  Interaction: Q5JTJ3; IntAct: EBI-23706738; Score: 0.56
DE  Interaction: Q6NX45; IntAct: EBI-24681698; Score: 0.56
DE  Interaction: A8K8V0; IntAct: EBI-23728536; Score: 0.56
DE  Interaction: P52738; IntAct: EBI-23735866; Score: 0.56
DE  Interaction: O43623; IntAct: EBI-24705441; Score: 0.56
DE  Interaction: Q9BU61; IntAct: EBI-24705993; Score: 0.56
DE  Interaction: Q9BRJ7; IntAct: EBI-24717821; Score: 0.56
DE  Interaction: Q8NCR6; IntAct: EBI-24726274; Score: 0.56
DE  Interaction: Q8N6D5; IntAct: EBI-24738691; Score: 0.56
DE  Interaction: O00746; IntAct: EBI-23809170; Score: 0.56
DE  Interaction: P19237; IntAct: EBI-24741126; Score: 0.56
DE  Interaction: Q9UPQ4; IntAct: EBI-24765776; Score: 0.56
DE  Interaction: A0A0U1RQF7; IntAct: EBI-25278632; Score: 0.56
DE  Interaction: Q9H9P5; IntAct: EBI-24548110; Score: 0.56
DE  Interaction: Q8TBB0; IntAct: EBI-24654317; Score: 0.56
DE  Interaction: Q68EA5; IntAct: EBI-24654686; Score: 0.56
DE  Interaction: Q9H0A9; IntAct: EBI-24789004; Score: 0.56
DE  Interaction: Q6P5X5; IntAct: EBI-25202133; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-25267170; Score: 0.56
DE  Interaction: P35452; IntAct: EBI-25241483; Score: 0.56
DE  Interaction: Q8TAG6; IntAct: EBI-25275160; Score: 0.56
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005246;
GO  GO:0005509;
GO  GO:1901385;
GO  GO:0007605;
GO  GO:0007165;
GO  GO:0007601;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10625670};
SQ  MGNCAKRPWRRGPKDPLQWLGSPPRGSCPSPSSSPKEQGDPAPGVQGYSVLNSLVGPACIFLRPSIAATQLDRELRPEEI
SQ  EELQVAFQEFDRDRDGYIGCRELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDA
SQ  FREFDTNGDGRISVGELRAALKALLGERLSQREVDEILQDVDLNGDGLVDFEEFVRMMSR
//
ID  Q9JLK4;
PN  Calcium-binding protein 2;
GN  Cabp2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: Q9JLK4;
DR  UNIPROT: Q3KNX9;
DR  UNIPROT: Q9JLK5;
DR  Pfam: PF00036;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Required for sound encoding at inner hair cells (IHCs) synapses, likely via inhibition of the inactivation of voltage-gated calcium channel of type 1.3 (Cav1.3) in the IHCs (PubMed:28183797). Required for the normal transfer of light signals through the retina (PubMed:27822497). {ECO:0000269|PubMed:27822497, ECO:0000269|PubMed:28183797}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005246;
GO  GO:0005509;
GO  GO:1901385;
GO  GO:0050896;
GO  GO:0007605;
GO  GO:0007601;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGNCAKTPWHRGSKERWQWPGSPLGGSRPSPGPRTEEQEGTQGYSVLGSLVGPACIFLRPSIAATQLDRELRPEEIEELQ
SQ  IAFQEFDRDRDGYIGYRELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDAFREF
SQ  DTNGDGCISVGELRAALKALLGERLSQREVDEILQDIDLNGDGLVDFEEFVRMMSR
//
ID  Q86V35;
PN  Calcium-binding protein 7;
GN  CABP7;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000305|PubMed:19338761}; Single-pass type IV membrane protein {ECO:0000305|PubMed:19338761}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19338761}. Cell membrane {ECO:0000305|PubMed:19338761}; Single-pass type IV membrane protein {ECO:0000305|PubMed:19338761}.
DR  UNIPROT: Q86V35;
DR  PDB: 2LV7;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 618759;
DE  Function: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9H2K0; IntAct: EBI-23900572; Score: 0.56
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032588;
GO  GO:0005509;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPFHPVTAALMYRGIYTVPNLLSEQRPVDIPEDELEEIREAFKVFDRDGNGFISKQELGTAMRSLGYMPNEVELEVIIQR
SQ  LDMDGDGQVDFEEFVTLLGPKLSTSGIPEKFHGTDFDTVFWKCDMQKLTVDELKRLLYDTFCEHLSMKDIENIIMTEEES
SQ  HLGTAEECPVDVETCSNQQIRQTCVRKSLICAFAIAFIISVMLIAANQVLRSGMK
//
ID  Q91ZM8;
PN  Calcium-binding protein 7;
GN  Cabp7;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
DR  UNIPROT: Q91ZM8;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032588;
GO  GO:0005509;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPFHPVTAALMYRGIYTVPNLLSEQRPVDIPEDELEEIREAFKVFDRDGNGFISKQELGTAMRSLGYMPNEVELEVIIQR
SQ  LDMDGDGQVDFEEFVTLLGPKLSTSGIPEKFHGTDFDTVFWKCDMQKLTVDELKRLLYDTFCEHLSMKDIENIIMTEEES
SQ  HLGTAEECPVDVETCSNQQIRQTCVRKSLICAFAIAFIISVMLIAANQVLRSGMK
//
ID  Q866X0;
PN  Calcium-binding protein 7;
GN  CABP7;
OS  9555;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
DR  UNIPROT: Q866X0;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032588;
GO  GO:0005509;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPFHPVTAALMYRGIYTVPNLLSEQRPVDIPEDELEEIREAFKVFDRDGNGFISKQELGTAMRSLGYMPNEVELEVIIQR
SQ  LDMDGDGQVDFEEFVTLLGPKLSTSGIPEKFHGTDFDTVFWKCDMQKLTVDELKRLLYDTFCEHLSMKDIENIIMTEEES
SQ  HLGTAEECPVDVETCSNQQIRQTCVRKSLICAFAIAFIISVMLIAANQVLRSGMK
//
ID  Q66H96;
PN  Calcium-binding protein 7;
GN  Cabp7;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000305|PubMed:19458041}; Single-pass type IV membrane protein {ECO:0000305|PubMed:19458041}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
DR  UNIPROT: Q66H96;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. {ECO:0000269|PubMed:19458041}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032588;
GO  GO:0005509;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPFHPVTAALMYRGIYTVPNLLSEQRPVDIPEDELEEIREAFKVFDRDGNGFISKQELGTAMRSLGYMPNEVELEVIIQR
SQ  LDMDGDGQVDFEEFVTLLGPKLSTSGIPEKFHGTDFDTVFWKCDMQKLTVDELKRLLYDTFCEHLSMKDIENIIMTEEES
SQ  HLGTAEECPVDVETCSNQQIRQTCVRKSLICAFAIAFIISVMLIAANQVLRSGMK
//
ID  Q9BXU9;
PN  Calcium-binding protein 8;
GN  CALN1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000305|PubMed:19338761}; Single-pass type IV membrane protein {ECO:0000305|PubMed:19338761}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19338761}. Cell membrane {ECO:0000305|PubMed:19338761}; Single-pass type IV membrane protein {ECO:0000305|PubMed:19338761}.
DR  UNIPROT: Q9BXU9;
DR  UNIPROT: J3KQA7;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 607176;
DR  DisGeNET: 83698;
DE  Function: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. May play a role in the physiology of neurons and is potentially important in memory and learning. {ECO:0000250|UniProtKB:Q06BI3}.
DE  Reference Proteome: Yes;
DE  Interaction: P62166; IntAct: EBI-21458640; Score: 0.27
DE  Interaction: Q96LL9; IntAct: EBI-24625155; Score: 0.56
DE  Interaction: Q9NZ43; IntAct: EBI-24630791; Score: 0.56
DE  Interaction: Q969F0; IntAct: EBI-24388353; Score: 0.56
DE  Interaction: Q96IW7; IntAct: EBI-24542608; Score: 0.56
DE  Interaction: P60201; IntAct: EBI-24602587; Score: 0.56
DE  Interaction: P21145; IntAct: EBI-24638394; Score: 0.56
DE  Interaction: P03973; IntAct: EBI-24807681; Score: 0.56
DE  Interaction: Q9H400; IntAct: EBI-25271079; Score: 0.56
DE  Interaction: Q58WW2; IntAct: EBI-21889878; Score: 0.40
DE  Interaction: P21554; IntAct: EBI-21458285; Score: 0.38
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032588;
GO  GO:0005509;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRLPEQPGEGKPENEKKGDGGALGGGEEPPRSQAPDFPTWEKMPFHHVTAGLLYKGNYLNRSLSAGSDSEQLANISVEEL
SQ  DEIREAFRVLDRDGNGFISKQELGMAMRSLGYMPSEVELAIIMQRLDMDGDGQVDFDEFMTILGPKLVSSEGRDGFLGNT
SQ  IDSIFWQFDMQRITLEELKHILYHAFRDHLTMKDIENIIINEEESLNETSGNCQTEFEGVHSQKQNRQTCVRKSLICAFA
SQ  MAFIISVMLIAANQILRSGME
//
ID  Q9JJG7;
PN  Calcium-binding protein 8;
GN  Caln1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9BXU9}; Single-pass type IV membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9BXU9}. Cell membrane {ECO:0000250|UniProtKB:Q9BXU9}; Single-pass type IV membrane protein {ECO:0000255}.
DR  UNIPROT: Q9JJG7;
DR  UNIPROT: F8WHE1;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. May play a role in the physiology of neurons and is potentially important in memory and learning. {ECO:0000250|UniProtKB:Q06BI3}.
DE  Reference Proteome: Yes;
DE  Interaction: P47746; IntAct: EBI-21458692; Score: 0.27
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032588;
GO  GO:0005509;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRLPEQPGDGKPENETKGDQETPERGEEPRRSPAPDFPTWEKMPFHHVTAGLLYKGNYLNRSLSAGSDSEQLANISVEEL
SQ  DEIREAFRVLDRDGNGFISKQELGMAMRSLGYMPSEVELAIIMQRLDMDGDGQVDFDEFMTILGPKLVSSEGRDGFLGNT
SQ  IDSIFWQFDMQRVTLEELKHILYHAFRDHLTMKDIENIIINEEESLNETSGNCQTEFEGVHSQKQNRQTCVRKSLICAFA
SQ  MAFIISVMLIAANQILRSGME
//
ID  Q06BI3;
PN  Calcium-binding protein 8;
GN  Caln1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000305|PubMed:19458041}; Single-pass type IV membrane protein {ECO:0000305|PubMed:19458041}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9BXU9}. Cell membrane {ECO:0000250|UniProtKB:Q9BXU9}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9BXU9}.
DR  UNIPROT: Q06BI3;
DR  UNIPROT: Q06BI2;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. May play a role in the physiology of neurons and is potentially important in memory and learning. {ECO:0000269|PubMed:19458041}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032588;
GO  GO:0005509;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRLPEQPGDGKPENETKGDQETPERGEEPRRSPAPDFPTWEKMPFHHVTAGLLYKGNYLNRSLSAGSDSEQLANISVEEL
SQ  DEIREAFRVLDRDGNGFISKQELGMAMRSLGYMPSEVELAIIMQRLDMDGDGQVDFDEFMTILGPKLVSSEGRDGFLGNT
SQ  IDSIFWQFDMQRVTLEELKHILYHAFRDHLTMKDIENIIINEEESLNETSGNCQTEFEGVHSQKQNRQTCVRKSLICAFA
SQ  MAFIISVMLIAANQILRSGME
//
ID  O18737;
PN  Calcium-binding and coiled-coil domain-containing protein 2;
GN  CALCOCO2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13137}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13137}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q13137}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: O18737;
DR  Pfam: PF17751;
DR  PROSITE: PS51905;
DE  Function: Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation (By similarity). Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy (By similarity). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen- containing autophagosome maturation (By similarity). Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C (By similarity). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (By similarity). {ECO:0000250|UniProtKB:Q13137}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0046872;
GO  GO:1901098;
GO  GO:0098792;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEETVDDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDITCYYTLTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPVD
SQ  LNSESAKQQEVQFKAYYLPKDDEYYQFCYVDQDGVVRGASIPFQFRPENEEDILVVTTQSEVEEIEQHNKELCKENRELK
SQ  DSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQ
SQ  GREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMII
SQ  HDVLQREKEKMEKENDYLKRENNRLLSYMGLDCDSLSYQVPTSNQGGTRQDPGLVFGNPYSGIQESSAPSLLSIKKCPTC
SQ  KSDFAADVFDHNLALEQHLQTLSLNCPICDKTFPAKEKQIFEDHVFCHTL
//
ID  Q13137;
PN  Calcium-binding and coiled-coil domain-containing protein 2;
GN  CALCOCO2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12869526, ECO:0000269|PubMed:17635994, ECO:0000269|PubMed:9230084}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17635994}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:25771791}; Peripheral membrane protein {ECO:0000305}. Note=According to PubMed:7540613, localizes to nuclear dots. According to PubMed:9230084 and PubMed:12869526, it is not a nuclear dot-associated protein but localizes predominantly in the cytoplasm with a coarse-grained distribution preferentially close to the nucleus. {ECO:0000269|PubMed:12869526, ECO:0000269|PubMed:7540613, ECO:0000269|PubMed:9230084}.
DR  UNIPROT: Q13137;
DR  UNIPROT: B2RBT0;
DR  UNIPROT: B4DDC4;
DR  UNIPROT: B4DDT4;
DR  UNIPROT: B4DP36;
DR  UNIPROT: B4E0C0;
DR  UNIPROT: E7ENK0;
DR  UNIPROT: E7ETP5;
DR  UNIPROT: E9PBE5;
DR  UNIPROT: Q53FQ5;
DR  UNIPROT: Q53HB5;
DR  UNIPROT: Q6IBN9;
DR  UNIPROT: Q9BTF7;
DR  PDB: 2MXP;
DR  PDB: 3VVV;
DR  PDB: 3VVW;
DR  PDB: 4GXL;
DR  PDB: 4HAN;
DR  PDB: 4XKL;
DR  PDB: 5AAQ;
DR  PDB: 5Z7A;
DR  PDB: 5Z7L;
DR  PDB: 7EAA;
DR  Pfam: PF17751;
DR  PROSITE: PS51905;
DR  OMIM: 604587;
DR  DisGeNET: 10241;
DE  Function: Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy (PubMed:22246324). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen-containing autophagosome maturation (PubMed:23022382, PubMed:25771791). Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C (PubMed:23022382, PubMed:25771791). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (PubMed:17635994). {ECO:0000269|PubMed:17635994, ECO:0000269|PubMed:22246324, ECO:0000269|PubMed:23022382, ECO:0000269|PubMed:23386746, ECO:0000269|PubMed:25771791}.
DE  Reference Proteome: Yes;
DE  Interaction: O75604; IntAct: EBI-24334992; Score: 0.56
DE  Interaction: O75716; IntAct: EBI-10189253; Score: 0.56
DE  Interaction: P29991; IntAct: EBI-8829245; Score: 0.37
DE  Interaction: P50613; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: Q02821; IntAct: EBI-11534474; Score: 0.56
DE  Interaction: Q06787; IntAct: EBI-6115370; Score: 0.55
DE  Interaction: Q9Y3C5; IntAct: EBI-7220121; Score: 0.37
DE  Interaction: Q96S44; IntAct: EBI-752485; Score: 0.74
DE  Interaction: O00214; IntAct: EBI-752575; Score: 0.85
DE  Interaction: Q53FD0; IntAct: EBI-752725; Score: 0.37
DE  Interaction: Q8N715; IntAct: EBI-752740; Score: 0.37
DE  Interaction: Q8TBB1; IntAct: EBI-753001; Score: 0.55
DE  Interaction: Q8N2W9; IntAct: EBI-753673; Score: 0.37
DE  Interaction: Q8N5R6; IntAct: EBI-753856; Score: 0.37
DE  Interaction: P25786; IntAct: EBI-753919; Score: 0.67
DE  Interaction: P26599; IntAct: EBI-754081; Score: 0.37
DE  Interaction: Q3YEC7; IntAct: EBI-754117; Score: 0.37
DE  Interaction: Q9UBL6; IntAct: EBI-24292126; Score: 0.56
DE  Interaction: Q96F93; IntAct: EBI-754906; Score: 0.37
DE  Interaction: Q9Y4Z0; IntAct: EBI-754981; Score: 0.78
DE  Interaction: P29353; IntAct: EBI-755236; Score: 0.55
DE  Interaction: P60520; IntAct: EBI-755311; Score: 0.78
DE  Interaction: Q15906; IntAct: EBI-755386; Score: 0.37
DE  Interaction: Q9Y4E5; IntAct: EBI-755704; Score: 0.37
DE  Interaction: Q9BQY9; IntAct: EBI-755827; Score: 0.37
DE  Interaction: Q14966; IntAct: EBI-755848; Score: 0.37
DE  Interaction: Q96D16; IntAct: EBI-755989; Score: 0.67
DE  Interaction: O95201; IntAct: EBI-756364; Score: 0.37
DE  Interaction: P51116; IntAct: EBI-756460; Score: 0.37
DE  Interaction: Q7L590; IntAct: EBI-756649; Score: 0.37
DE  Interaction: Q9UNA4; IntAct: EBI-756718; Score: 0.37
DE  Interaction: Q9UKA9; IntAct: EBI-756841; Score: 0.37
DE  Interaction: O95251; IntAct: EBI-757276; Score: 0.37
DE  Interaction: Q9BSM1; IntAct: EBI-757711; Score: 0.37
DE  Interaction: P56279; IntAct: EBI-757792; Score: 0.87
DE  Interaction: Q96GM5; IntAct: EBI-757918; Score: 0.67
DE  Interaction: Q8IYF1; IntAct: EBI-757939; Score: 0.55
DE  Interaction: O14639; IntAct: EBI-757951; Score: 0.37
DE  Interaction: Q13137; IntAct: EBI-758068; Score: 0.37
DE  Interaction: Q9H0I2; IntAct: EBI-758104; Score: 0.67
DE  Interaction: Q9BUY5; IntAct: EBI-758131; Score: 0.37
DE  Interaction: Q9BVV2; IntAct: EBI-758146; Score: 0.67
DE  Interaction: P30626; IntAct: EBI-758236; Score: 0.74
DE  Interaction: Q9BWD7; IntAct: EBI-758320; Score: 0.37
DE  Interaction: Q12933; IntAct: EBI-758476; Score: 0.37
DE  Interaction: Q9H9D4; IntAct: EBI-758947; Score: 0.67
DE  Interaction: Q15038; IntAct: EBI-759250; Score: 0.67
DE  Interaction: Q8TCX5; IntAct: EBI-759364; Score: 0.37
DE  Interaction: Q9UBV8; IntAct: EBI-759700; Score: 0.67
DE  Interaction: Q9UBZ4; IntAct: EBI-759748; Score: 0.37
DE  Interaction: Q9H0R8; IntAct: EBI-759847; Score: 0.78
DE  Interaction: O95990; IntAct: EBI-760045; Score: 0.37
DE  Interaction: Q7Z3B3; IntAct: EBI-760072; Score: 0.74
DE  Interaction: Q5NEX4; IntAct: EBI-2808427; Score: 0.00
DE  Interaction: A0A3N4B896; IntAct: EBI-2840104; Score: 0.00
DE  Interaction: Q9UNI6; IntAct: EBI-8633706; Score: 0.74
DE  Interaction: Q15884; IntAct: EBI-8636634; Score: 0.37
DE  Interaction: Q13671; IntAct: EBI-8641704; Score: 0.67
DE  Interaction: Q8WUI4; IntAct: EBI-10276459; Score: 0.56
DE  Interaction: Q99471; IntAct: EBI-8644653; Score: 0.67
DE  Interaction: Q6PF05; IntAct: EBI-8656859; Score: 0.37
DE  Interaction: Q86YD7; IntAct: EBI-8656891; Score: 0.78
DE  Interaction: P01106; IntAct: EBI-3962281; Score: 0.35
DE  Interaction: O43913; IntAct: EBI-3935022; Score: 0.37
DE  Interaction: P15927; IntAct: EBI-3935032; Score: 0.37
DE  Interaction: Q9Y4K3; IntAct: EBI-3935052; Score: 0.37
DE  Interaction: Q9Y6K9; IntAct: EBI-3935062; Score: 0.37
DE  Interaction: Q14161; IntAct: EBI-3935072; Score: 0.37
DE  Interaction: Q8TDY2; IntAct: EBI-3935082; Score: 0.37
DE  Interaction: Q15051; IntAct: EBI-4286917; Score: 0.35
DE  Interaction: Q7Z434; IntAct: EBI-6115370; Score: 0.58
DE  Interaction: Q8NCU4; IntAct: EBI-6115370; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-6115370; Score: 0.75
DE  Interaction: P48634; IntAct: EBI-6115370; Score: 0.35
DE  Interaction: A7MCY6; IntAct: EBI-6115370; Score: 0.53
DE  Interaction: Q9H6S1; IntAct: EBI-6115370; Score: 0.53
DE  Interaction: Q9NVV4; IntAct: EBI-6115370; Score: 0.50
DE  Interaction: Q9QYP6; IntAct: EBI-6115837; Score: 0.35
DE  Interaction: Q99IB8; IntAct: EBI-6928172; Score: 0.37
DE  Interaction: Q9WMX2; IntAct: EBI-9081202; Score: 0.57
DE  Interaction: O41947; IntAct: EBI-9640332; Score: 0.37
DE  Interaction: A8KA13; IntAct: EBI-10174899; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-10175027; Score: 0.56
DE  Interaction: B2R9Y1; IntAct: EBI-10175744; Score: 0.56
DE  Interaction: Q8WWY3; IntAct: EBI-10177378; Score: 0.72
DE  Interaction: O00560; IntAct: EBI-10180081; Score: 0.56
DE  Interaction: O43189; IntAct: EBI-10183509; Score: 0.56
DE  Interaction: O43324; IntAct: EBI-10183831; Score: 0.56
DE  Interaction: O43602; IntAct: EBI-10184475; Score: 0.56
DE  Interaction: O95363; IntAct: EBI-10191564; Score: 0.78
DE  Interaction: P00540; IntAct: EBI-10193294; Score: 0.78
DE  Interaction: P14678; IntAct: EBI-10198485; Score: 0.56
DE  Interaction: P17482; IntAct: EBI-10199927; Score: 0.56
DE  Interaction: P25791; IntAct: EBI-10202872; Score: 0.56
DE  Interaction: P26196; IntAct: EBI-10203823; Score: 0.72
DE  Interaction: P26640; IntAct: EBI-10204357; Score: 0.56
DE  Interaction: P32969; IntAct: EBI-10206135; Score: 0.56
DE  Interaction: P41227; IntAct: EBI-10208549; Score: 0.78
DE  Interaction: P49901; IntAct: EBI-10211623; Score: 0.56
DE  Interaction: P50539; IntAct: EBI-10212007; Score: 0.72
DE  Interaction: P51946; IntAct: EBI-10212597; Score: 0.56
DE  Interaction: P61968; IntAct: EBI-10218982; Score: 0.56
DE  Interaction: P62979; IntAct: EBI-10220080; Score: 0.56
DE  Interaction: Q02040; IntAct: EBI-10222670; Score: 0.56
DE  Interaction: Q05CH4; IntAct: EBI-10223754; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-10224979; Score: 0.56
DE  Interaction: Q12774; IntAct: EBI-10227037; Score: 0.56
DE  Interaction: Q14997; IntAct: EBI-10234580; Score: 0.56
DE  Interaction: Q14D33; IntAct: EBI-10234924; Score: 0.72
DE  Interaction: Q17RB8; IntAct: EBI-10238780; Score: 0.56
DE  Interaction: Q3B820; IntAct: EBI-10240301; Score: 0.72
DE  Interaction: Q5U5U6; IntAct: EBI-10247590; Score: 0.56
DE  Interaction: Q6NYC8; IntAct: EBI-10251814; Score: 0.56
DE  Interaction: Q6P4J0; IntAct: EBI-10252829; Score: 0.56
DE  Interaction: Q6PIY7; IntAct: EBI-10253897; Score: 0.56
DE  Interaction: Q7Z4I7; IntAct: EBI-10257703; Score: 0.56
DE  Interaction: Q86TG7; IntAct: EBI-10258559; Score: 0.67
DE  Interaction: Q86W54; IntAct: EBI-10259956; Score: 0.56
DE  Interaction: Q8IVS8; IntAct: EBI-10261677; Score: 0.56
DE  Interaction: Q8IYX8; IntAct: EBI-10264302; Score: 0.56
DE  Interaction: Q8N4T4; IntAct: EBI-10265711; Score: 0.67
DE  Interaction: Q8NBM4; IntAct: EBI-10269199; Score: 0.56
DE  Interaction: Q8TBE0; IntAct: EBI-10273199; Score: 0.56
DE  Interaction: Q8TBZ8; IntAct: EBI-10273829; Score: 0.56
DE  Interaction: Q8TES7; IntAct: EBI-10275340; Score: 0.56
DE  Interaction: Q8WU02; IntAct: EBI-10276217; Score: 0.56
DE  Interaction: Q8WXI9; IntAct: EBI-10278009; Score: 0.56
DE  Interaction: Q92567; IntAct: EBI-10278631; Score: 0.56
DE  Interaction: Q92608; IntAct: EBI-10278809; Score: 0.56
DE  Interaction: Q969Z0; IntAct: EBI-10281521; Score: 0.56
DE  Interaction: Q96A72; IntAct: EBI-10281716; Score: 0.72
DE  Interaction: Q96BZ8; IntAct: EBI-10282682; Score: 0.56
DE  Interaction: Q96C32; IntAct: EBI-10283082; Score: 0.56
DE  Interaction: Q96D03; IntAct: EBI-10284252; Score: 0.56
DE  Interaction: Q96T37; IntAct: EBI-10293900; Score: 0.56
DE  Interaction: Q99732; IntAct: EBI-10294748; Score: 0.72
DE  Interaction: Q9BU23; IntAct: EBI-10298573; Score: 0.56
DE  Interaction: Q9BV47; IntAct: EBI-10299234; Score: 0.56
DE  Interaction: Q9BXF9; IntAct: EBI-10301058; Score: 0.67
DE  Interaction: Q9BXY8; IntAct: EBI-10301594; Score: 0.56
DE  Interaction: Q9H7H0; IntAct: EBI-10308833; Score: 0.78
DE  Interaction: Q9HC52; IntAct: EBI-10310384; Score: 0.72
DE  Interaction: Q9NQT4; IntAct: EBI-10312366; Score: 0.56
DE  Interaction: Q9NU19; IntAct: EBI-10313689; Score: 0.56
DE  Interaction: Q9NX63; IntAct: EBI-10316161; Score: 0.56
DE  Interaction: Q9P0T4; IntAct: EBI-10317870; Score: 0.56
DE  Interaction: Q9P2K6; IntAct: EBI-10318921; Score: 0.56
DE  Interaction: Q9UIM3; IntAct: EBI-10322118; Score: 0.56
DE  Interaction: Q9UJV3; IntAct: EBI-10322427; Score: 0.56
DE  Interaction: Q9UJW0; IntAct: EBI-10322497; Score: 0.56
DE  Interaction: Q9UMS0; IntAct: EBI-10324153; Score: 0.56
DE  Interaction: Q9Y3M9; IntAct: EBI-10327900; Score: 0.56
DE  Interaction: Q9Y4X0; IntAct: EBI-10328456; Score: 0.67
DE  Interaction: P30566; IntAct: EBI-21246927; Score: 0.37
DE  Interaction: Q9HBZ2; IntAct: EBI-21247102; Score: 0.37
DE  Interaction: X5DP31; IntAct: EBI-21247566; Score: 0.37
DE  Interaction: X5D7R7; IntAct: EBI-21250303; Score: 0.37
DE  Interaction: X5DP17; IntAct: EBI-21250609; Score: 0.37
DE  Interaction: Q99608; IntAct: EBI-21250960; Score: 0.37
DE  Interaction: O43741; IntAct: EBI-21251734; Score: 0.37
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P30119; IntAct: EBI-11736591; Score: 0.37
DE  Interaction: P05759; IntAct: EBI-11522944; Score: 0.56
DE  Interaction: P0CH08; IntAct: EBI-11523121; Score: 0.56
DE  Interaction: P32902; IntAct: EBI-11526925; Score: 0.56
DE  Interaction: P38815; IntAct: EBI-11529521; Score: 0.56
DE  Interaction: P39518; IntAct: EBI-11529902; Score: 0.56
DE  Interaction: P40302; IntAct: EBI-11530551; Score: 0.56
DE  Interaction: P40325; IntAct: EBI-11530725; Score: 0.56
DE  Interaction: P41911; IntAct: EBI-11531747; Score: 0.56
DE  Interaction: Q06630; IntAct: EBI-11535826; Score: 0.56
DE  Interaction: Q06707; IntAct: EBI-11535920; Score: 0.56
DE  Interaction: Q07821; IntAct: EBI-11536127; Score: 0.56
DE  Interaction: Q12342; IntAct: EBI-11537295; Score: 0.56
DE  Interaction: P28702; IntAct: EBI-16433077; Score: 0.56
DE  Interaction: A0A0S2Z4M1; IntAct: EBI-16433037; Score: 0.56
DE  Interaction: O15169; IntAct: EBI-16433027; Score: 0.56
DE  Interaction: A0A0S2Z5X4; IntAct: EBI-16433137; Score: 0.56
DE  Interaction: Q3SY00; IntAct: EBI-24288555; Score: 0.56
DE  Interaction: P57086; IntAct: EBI-24289178; Score: 0.56
DE  Interaction: P47897; IntAct: EBI-24292527; Score: 0.56
DE  Interaction: Q7L5A3; IntAct: EBI-24308054; Score: 0.56
DE  Interaction: Q5JVL4; IntAct: EBI-24316916; Score: 0.56
DE  Interaction: P56524; IntAct: EBI-24325092; Score: 0.56
DE  Interaction: Q9P1Z0; IntAct: EBI-24331244; Score: 0.56
DE  Interaction: Q96HB5; IntAct: EBI-24332120; Score: 0.56
DE  Interaction: P54646; IntAct: EBI-24338182; Score: 0.56
DE  Interaction: Q9BSH4; IntAct: EBI-24338552; Score: 0.56
DE  Interaction: Q96FJ0; IntAct: EBI-25243983; Score: 0.56
DE  Interaction: P51504; IntAct: EBI-24480415; Score: 0.56
DE  Interaction: Q8NE01; IntAct: EBI-24488458; Score: 0.56
DE  Interaction: Q8NA54; IntAct: EBI-24496225; Score: 0.56
DE  Interaction: Q14005; IntAct: EBI-24503792; Score: 0.56
DE  Interaction: Q96IQ9; IntAct: EBI-24507508; Score: 0.56
DE  Interaction: Q494U1; IntAct: EBI-24374123; Score: 0.56
DE  Interaction: Q9BWG6; IntAct: EBI-24383955; Score: 0.56
DE  Interaction: Q6NX45; IntAct: EBI-24388156; Score: 0.56
DE  Interaction: Q6VB84; IntAct: EBI-24390683; Score: 0.56
DE  Interaction: Q9C0A6; IntAct: EBI-24391757; Score: 0.56
DE  Interaction: O00311; IntAct: EBI-24403310; Score: 0.56
DE  Interaction: P08218; IntAct: EBI-24406407; Score: 0.56
DE  Interaction: P09067; IntAct: EBI-24427120; Score: 0.56
DE  Interaction: Q5T619; IntAct: EBI-24430220; Score: 0.56
DE  Interaction: Q9H7X3; IntAct: EBI-24432271; Score: 0.56
DE  Interaction: Q6PF15; IntAct: EBI-24453693; Score: 0.56
DE  Interaction: Q9BXW4; IntAct: EBI-24455075; Score: 0.56
DE  Interaction: Q99633; IntAct: EBI-24456947; Score: 0.56
DE  Interaction: P28676; IntAct: EBI-24461986; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q53EZ4; IntAct: EBI-21572102; Score: 0.35
DE  Interaction: P0CG47; IntAct: EBI-21572102; Score: 0.35
DE  Interaction: Q3KP66; IntAct: EBI-21617875; Score: 0.35
DE  Interaction: Q9H7C4; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q9BU40; IntAct: EBI-21739567; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-21787335; Score: 0.35
DE  Interaction: E9PKR8; IntAct: EBI-21872066; Score: 0.35
DE  Interaction: Q9UHQ4; IntAct: EBI-21883433; Score: 0.40
DE  Interaction: P29972; IntAct: EBI-21268671; Score: 0.37
DE  Interaction: Q9H788; IntAct: EBI-21268710; Score: 0.37
DE  Interaction: P15622; IntAct: EBI-21268658; Score: 0.37
DE  Interaction: Q96HA8; IntAct: EBI-21268697; Score: 0.37
DE  Interaction: P61417; IntAct: EBI-20817146; Score: 0.37
DE  Interaction: Q83DE4; IntAct: EBI-21285435; Score: 0.37
DE  Interaction: P21580; IntAct: EBI-20737339; Score: 0.35
DE  Interaction: Q9UKE5; IntAct: EBI-28946906; Score: 0.55
DE  Interaction: Q14296; IntAct: EBI-22127120; Score: 0.37
DE  Interaction: P0CG48; IntAct: EBI-22146758; Score: 0.37
DE  Interaction: Q92574; IntAct: EBI-26515497; Score: 0.37
DE  Interaction: Q8N612; IntAct: EBI-34574737; Score: 0.27
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0046872;
GO  GO:0042803;
GO  GO:1901098;
GO  GO:0034341;
GO  GO:0016032;
GO  GO:0098792;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEETIKDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPID
SQ  LNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELK
SQ  DSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQ
SQ  EKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEII
SQ  CNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGARQNPGLAYGNPYSGIQESSSPSPLSIKKCPIC
SQ  KADDICDHTLEQQQMQPLCFNCPICDKIFPATEKQIFEDHVFCHSL
//
ID  Q4R914;
PN  Calcium-binding and coiled-coil domain-containing protein 2;
GN  CALCOCO2;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13137}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13137}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q13137}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: Q4R914;
DR  Pfam: PF17751;
DR  PROSITE: PS51905;
DE  Function: Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation (By similarity). Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy (By similarity). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen- containing autophagosome maturation (By similarity). Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C (By similarity). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (By similarity). {ECO:0000250|UniProtKB:Q13137}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:1901098;
GO  GO:0098792;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEKTIEDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDVTCRYTFTQNFIPRQKDWIGIFRVGWKTVREYYTFMWVTLPID
SQ  LNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDQDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELK
SQ  DSCVSLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETEQLEHLKKENGHLFLSLTEQRKDQKKLEQTVEE
SQ  MKQNETTAMKKQQELMDENFDLSRRLSEKKMIYNALQREKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGA
SQ  GQNPGLVYGNPYSGIQESSSPSQLSIKKCPICKADDICDHTLEQQQMQALCLNCPICDKIFPATEKQIFEDHVFCHSL
//
ID  A2A6M5;
PN  Calcium-binding and coiled-coil domain-containing protein 2;
GN  Calcoco2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13137}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13137}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q13137}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: A2A6M5;
DR  UNIPROT: Q3TK36;
DR  UNIPROT: Q3TKZ6;
DR  UNIPROT: Q3TL30;
DR  UNIPROT: Q9CWE3;
DR  Pfam: PF17751;
DE  Function: Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation (By similarity). Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy (By similarity). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen- containing autophagosome maturation (By similarity). Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C (By similarity). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (By similarity). {ECO:0000250|UniProtKB:Q13137}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0042803;
GO  GO:1901098;
GO  GO:0034341;
GO  GO:0098792;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MDQCPIPTLLEHGNFSQVLFNNVEKFYAPRGDIMCYYTLTEKFIPRRKDWIGIFKVGWKTTQEYYTFMWAPLPKDQNKDS
SQ  ATQQEIQFKAYYLPKDVERYQFCYVDEDGLVRGTSVPFQFCPDPDEDIMVVINKEKVEEMEQLSEELYQQNQELKDKYAD
SQ  LHEQLQRKQVALEATQRVNKTLEHKVEEKASWEKEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKAS
SQ  WEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEKEKASWEEEKASWEKEKAPWEVEKAPWKE
SQ  VKAYWWNDLHR
//
ID  Q5R7H1;
PN  Calcium-binding and coiled-coil domain-containing protein 2;
GN  CALCOCO2;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13137}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13137}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q13137}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: Q5R7H1;
DR  Pfam: PF17751;
DR  PROSITE: PS51905;
DE  Function: Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation (By similarity). Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy (By similarity). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen- containing autophagosome maturation (By similarity). Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C (By similarity). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (By similarity). {ECO:0000250|UniProtKB:Q13137}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:1901098;
GO  GO:0098792;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEETIEDPPTSAVLLDHCHFSQVIFSSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPID
SQ  LNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDQDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELK
SQ  DNCVSLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQ
SQ  EKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENKII
SQ  CNALQREKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGAGQNPGLVYGNPYSGIQESSSPSPLSIKKCPIC
SQ  KADDICDHILEQQQMQPLCLNCPICDKIFPATEKQIFEDHVFCHSL
//
ID  Q6DF48;
PN  Calcium-binding and coiled-coil domain-containing protein 2;
GN  calcoco2;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13137}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13137}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q13137}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: Q6DF48;
DR  Pfam: PF17751;
DR  PROSITE: PS51905;
DE  Function: Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation (By similarity). Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens upon entry into the cytosol by targeting galectin-associated bacteria for autophagy (By similarity). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen- containing autophagosome maturation (By similarity). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (By similarity). {ECO:0000250|UniProtKB:Q13137}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:1901098;
GO  GO:0098792;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MASDAPPTSMLQPEERNYSQVVFSRVEQSYVPGIDIICYFTYTSGFHPAKKDWVGIFKVSWKTTREYYTWVSADCEEQGL
SQ  EKRVTFKAYYLPKESDDYYQFCYVDQKGEVRGVSIPFQLCRKIQDEGEEDILLVTTEEEAQGMKEKQRVLEEKVAALEKD
SQ  KCTLQDECTQLALEQKNKAALIESLQAQQLECAKKNEELDQQNQELERQLEEEKCKNGSLHLKVVSAEEERERVQNDIRS
SQ  LQLEQNQLKEENMELHKHTNDMEFSLKKYSEEAKNQEEEVQELKDKLWDAEAKHHLLQVQLQDIQMEKKKDKYSIELLTK
SQ  EAEKVADLRQNLEKKDKTMETMEKQLAQLQRENATVLRQMEDLSYTLELRKAEISDMQQQRVRDGAEIEHLNRLLTEQSS
SQ  STPRNQGLFFQNPYESESLISFANEPQPGEAPGGSSVRHVQMQCPECGSEFENFQVFQDHIFCHDLESTE
//
ID  A8XA40;
PN  Calnexin;
GN  cnx;
OS  6238;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}; Single- pass type I membrane protein {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}.
DR  UNIPROT: A8XA40;
DR  Pfam: PF00262;
DR  PROSITE: PS00803;
DR  PROSITE: PS00804;
DR  PROSITE: PS00805;
DE  Function: Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death (By similarity). {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0051082;
GO  GO:0030968;
GO  GO:0006457;
GO  GO:0009408;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLNRKWSFVFLTFLLVISVNANDDVFEDEDEASESGVEKDEFVPSNFVAPKLADTSKPNFFDYFPVGSKIGQTWIKSLAK
SQ  KDDVDSEIAKYNGEWSIGAPTKVSIEGDYGLIVKTKARHHAIAAKLETPFVFGSNKFIAQYDVKFEEGQECGGGYLKLLS
SQ  EGAEKDLASFQDKTPYTIMFGPDKCGASGQVHLIFRYKNPVNGTVSEYHAKQPASIGTAYWDDHNTHLFTLVVKPTGEYS
SQ  VSVDGKSLYYGNMLSDISPSLTPPKEIFDETDLKPEDWDEREQIEDETASKPDDWDENEPQNVVDESATKPYDWNEEENE
SQ  LIPDPEAQKPQDWDEDMDGSWEAPLIDNPACKGLSGCGTWKPPTIKNPKYRGKWVRPKIANPAYKGKWSPRLIDNPNYFE
SQ  PKPFDGLAPISAVGIELWTMSENILFDNILITSSEQDASEIAKQTFYIKQQEEYRLAAATGSSNGIFQQIVDATNEKPWL
SQ  WAVYILCILLPLIAIGVFCFGKGSKPAPNFAKKSDTYSPDDDRVPNLVDDQEEEIIAEDEEDNQPGPSGTQNQPPIDEDE
SQ  QDEVEQQPSSSKTASSESSSAAEEEDNDHVVHENEPVQPTEEVAKKSPRVTGGAKRRTARRGD
//
ID  P34652;
PN  Calnexin;
GN  cnx;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16256074}. Cytoplasmic vesicle {ECO:0000269|PubMed:16256074}. Note=Perinuclear localization in excretory and germ cells. In intestinal cells, clustered signals around vacuoles with vesicles are detected.
DR  UNIPROT: P34652;
DR  Pfam: PF00262;
DR  PROSITE: PS00803;
DR  PROSITE: PS00804;
DR  PROSITE: PS00805;
DE  Function: Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death. {ECO:0000250, ECO:0000269|PubMed:11580896, ECO:0000269|PubMed:16256074}.
DE  Reference Proteome: Yes;
DE  Interaction: Q18953; IntAct: EBI-335408; Score: 0.00
DE  Interaction: Q9NH52; IntAct: EBI-343937; Score: 0.00
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0030246;
GO  GO:0051082;
GO  GO:0030968;
GO  GO:0006457;
GO  GO:0009408;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVNRKWMYIFIQFLLVSSIRSDDDVFEDDEEEVTKGSDDKEEFVPSLFVAPKLSDKSTPNFFDYFPVGSKIGLTWIKSLA
SQ  KKDDVDSDIAKYNGEWSIGAPTKVSIEGDLGLIVKTKARHHAIAAKLNTPFAFDANTFVVQYDIKFEEGQECGGGYLKLL
SQ  SEGAEKDLANFQDKTAYTIMFGPDKCGATGKVHLIFRYKNPINGTISEYHANQPTTIGSTYWDDHNTHLFTLVVKPTGEY
SQ  SVSVDGKSLYYGNMMSDVTPALTPPKQIFDETDLKPVDWDERENIEDESAVKPDDWDENEPQSVVDEAATKPYDWNEEEN
SQ  ELIADPEAKKPQDWDEDMDGSWEAPLIDNPACKGLSGCGTWKAPTIKNPKYKGKWIRPKISNPAFKGKWTARLIDNPNYF
SQ  EPKPFAGLAPITAVGIEMWTMSENILFDNILITSSEEDSSDVAKQTFYVKQKEEYRLAAATGNGNGFFQQIIDATNEKPW
SQ  LWAVYILCVLLPLVAIGVFCFGKQSKPTPNFAKKSDAYSADDDRVPNLVDDDEEEIIGDEEDDVNQPGPSGSQSNPEPQD
SQ  EEENAEQQSANSSQSSAAEEEDDEHVVPENEPVKPTEEFAKKSPKNTGGAKRRTARRGD
//
ID  Q9Y6Q1;
PN  Calpain-6;
GN  CAPN6;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17210638}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17210638}. Note=During mitose associated with the mitotic spindle. At telophase colocalized to the midbody spindle.
DR  UNIPROT: Q9Y6Q1;
DR  UNIPROT: D3DUY7;
DR  UNIPROT: Q9UEQ1;
DR  UNIPROT: Q9UJA8;
DR  Pfam: PF00168;
DR  Pfam: PF01067;
DR  Pfam: PF00648;
DR  PROSITE: PS50004;
DR  PROSITE: PS50203;
DR  OMIM: 300146;
DR  DisGeNET: 827;
DE  Function: Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues (By similarity). {ECO:0000250, ECO:0000269|PubMed:17210638}.
DE  Reference Proteome: Yes;
DE  Interaction: O94901; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: Q8TD16; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: Q8WXH0; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: O14745; IntAct: EBI-7814911; Score: 0.40
DE  Interaction: P15311; IntAct: EBI-7814930; Score: 0.40
DE  Interaction: P01023; IntAct: EBI-7183126; Score: 0.35
DE  Interaction: O43829; IntAct: EBI-24469714; Score: 0.56
DE  Interaction: Q6PJG9; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: P21333; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: Q9ULT8; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: Q9NRL2; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: Q9NRG0; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: Q8N5W9; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: Q5TB80; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: P23378; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: A0AVT1; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: P19338; IntAct: EBI-20905504; Score: 0.40
DE  Interaction: P16403; IntAct: EBI-20920500; Score: 0.40
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0005876;
GO  GO:0004198;
GO  GO:0008017;
GO  GO:0001578;
GO  GO:0051493;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGPPLKLFKNQKYQELKQECIKDSRLFCDPTFLPENDSLFYNRLLPGKVVWKRPQDICDDPHLIVGNISNHQLTQGRLGH
SQ  KPMVSAFSCLAVQESHWTKTIPNHKEQEWDPQKTEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWN
SQ  ALLEKAYAKLLGCYEALDGLTITDIIVDFTGTLAETVDMQKGRYTELVEEKYKLFGELYKTFTKGGLICCSIESPNQEEQ
SQ  EVETDWGLLKGHTYTMTDIRKIRLGERLVEVFSAEKVYMVRLRNPLGRQEWSGPWSEISEEWQQLTASDRKNLGLVMSDD
SQ  GEFWMSLEDFCRNFHKLNVCRNVNNPIFGRKELESVLGCWTVDDDPLMNRSGGCYNNRDTFLQNPQYIFTVPEDGHKVIM
SQ  SLQQKDLRTYRRMGRPDNYIIGFELFKVEMNRKFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTS
SQ  EFLLRIFSEVPVQLRELTLDMPKMSCWNLARGYPKVVTQITVHSAEDLEKKYANETVNPYLVIKCGKEEVRSPVQKNTVH
SQ  AIFDTQAIFYRRTTDIPIIVQVWNSRKFCDQFLGQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLTE
SQ  L
//
ID  O35646;
PN  Calpain-6;
GN  Capn6;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:20814968}.
DR  UNIPROT: O35646;
DR  UNIPROT: Q3UM55;
DR  Pfam: PF00168;
DR  Pfam: PF01067;
DR  Pfam: PF00648;
DR  PROSITE: PS50004;
DR  PROSITE: PS50203;
DE  Function: Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues. {ECO:0000269|PubMed:17210638, ECO:0000269|PubMed:21406564}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0005876;
GO  GO:0008017;
GO  GO:0001578;
GO  GO:0051493;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGPPLKLFKNQKYQELKQECMKDGRLFCDPTFLPENDSLFFNRLLPGKVVWKRPQDISDDPHLIVGNISNHQLIQGRLGN
SQ  KAMISAFSCLAVQESHWTKAIPNHKDQEWDPRKPEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWN
SQ  ALLEKAYAKLLGCYEALDGLTITDIIMDFTGTLAEIIDMQKGRYTDLVEEKYKLFGELYKTFTKGGLICCSIESPSQEEQ
SQ  EVETDWGLLKGYTYTMTDIRKLRLGERLVEVFSTEKLYMVRLRNPLGRQEWSGPWSEISEEWQQLTVTDRKNLGLVMSDD
SQ  GEFWMSLEDFCHNFHKLNVCRNVNNPVFGRKELESVVGCWTVDDDPLMNRSGGCYNNRDTFLQNPQYIFTVPEDGHKVIM
SQ  SLQQKDLRTYRRMGRPDNYIIGFELFKVEMNRRFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGSYVLVPTMFQHGRTS
SQ  EFLLRIFSEVPVQLRELTLDMPKMSCWNLARGYPKVVTQITVHSAEGLEKKYANETVNPYLIIKCGKEEVRSPVQKNTVH
SQ  AIFDTQAIFYRRTTDIPIIIQVWNSRKFCDQFLGQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLTE
SQ  L
//
ID  O88501;
PN  Calpain-6;
GN  Capn6;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
DR  UNIPROT: O88501;
DR  Pfam: PF00168;
DR  Pfam: PF01067;
DR  Pfam: PF00648;
DR  PROSITE: PS50004;
DR  PROSITE: PS50203;
DE  Function: Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0005876;
GO  GO:0008017;
GO  GO:0001578;
GO  GO:0051493;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGPPLKLFKNQKYQELKQDCMKDGRLFCDPTFLPENDSLFFNRLLPGKVVWKRPQDISDDPHLIVGNISNHQLIQGRLGN
SQ  KAMISAFSCLAVQESHWTKAIPNHKEQEWDPRKPEKYAGIFRFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWN
SQ  ALLEKAYAKLLGCYEALDGLTITDIIMDFTGTLAEIIDMQKGRYTDLVEEKYKLFGELYKTFTKGGLISCSIESPSQEEQ
SQ  EVETDWGLLKGYTYTMTDIRKLRLGERLVEVFSTEKLYMVRLRNPLGRQEWSGPWSEISEEWQQLTVTDRKNLGLVMSDD
SQ  GEFWMSLEDFCHNFHKLNVCRNVNNPVFGRKELESVVGCWTVDDDPLMNRSGGCYNNRDTFLQNPQYIFTVPEDGHKVIM
SQ  SLQQKDLRTYRRMGRPDNYIIGFELFKVEMNRRFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTS
SQ  EFLLRIFSEVPVQLRELTLDMPKMSCWNLARGYPKVVTQITVHSAEGLEKKYANETVNPYLTIKCGKEEVRSPVQKNTVH
SQ  AIFDTQAIFYRRTTDIPIIIQVWNSRKFCDQFLGQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLTE
SQ  L
//
ID  A5D7H5;
PN  Protein CASC3;
GN  CASC3;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O15234}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus {ECO:0000250|UniProtKB:O15234}. Nucleus speckle {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q8K3X0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8K3X0}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. In nuclear speckles, colocalizes with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules (By similarity). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:O15234, ECO:0000250|UniProtKB:Q8K3X0}.
DR  UNIPROT: A5D7H5;
DR  Pfam: PF09405;
DE  Function: Required for pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon- exon junctions. Binds poly(G) and poly(U) RNA homomer. {ECO:0000250|UniProtKB:O15234}.
DE  Reference Proteome: Yes;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:0035145;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0071006;
GO  GO:0003729;
GO  GO:0000398;
GO  GO:0051028;
GO  GO:0000184;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRRRQRASQDTEDEESGASGSDSGGSPARGGGSCSGSVGGGGSGSLPSQRGGRAGALHLRRVESGGAKSAEESECESE
SQ  DGIEGDAVLSDYESAEDSEGDDGEYSEEENSKVELKSEANDAANSSAKDEKGEEKPDTKGTVTGERQSGDGQESTEPVEN
SQ  KVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALY
SQ  GYDIRSAHNPDDIKPRRIRKPRFGSPPQRDPSWIGERPNKSHRHQGPGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFK
SQ  EGRTGFRPAEAGGQHAGRSGETVKHETSYRSRHLEQTPVRDPSPEADAQVLGSPEKEEVAPEIPNPAPDTAPPVPDRPVE
SQ  KKSYSRARRTRIKAGDAGKVAEEVPPPPEGLTPAPPVPEATPPTPAKTGNWEAPVDSTTGGLEQDVAQLNITEQNWSPGQ
SQ  PAFLQSRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTH
SQ  GDSPAPLPPQGMIVQPEMHLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPG
SQ  ALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS
//
ID  Q1ECZ4;
PN  Protein CASC3;
GN  casc3;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O15234}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus {ECO:0000250|UniProtKB:O15234}. Nucleus speckle {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q8K3X0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8K3X0}. Note=Shuttles between the nucleus and the cytoplasm in a xpo1/crm1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (By similarity). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:O15234, ECO:0000250|UniProtKB:Q8K3X0}.
DR  UNIPROT: Q1ECZ4;
DR  UNIPROT: Q7T1P0;
DR  Pfam: PF09405;
DE  Function: Required for pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. {ECO:0000250|UniProtKB:O15234}.
DE  Reference Proteome: Yes;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:0035145;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0071006;
GO  GO:0003729;
GO  GO:0000398;
GO  GO:0051028;
GO  GO:0000184;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRRRRRRRASQDSEEEDESASGSESGRSFSASRKTRGREPEPVESPAERVAAKSDDESECVSEDGVGEAVLSDYDSAD
SQ  LEENGSHTEGGEEEEEAEHFSEEEASRPAAESKPVADAPTEELVEGEERDESVKEVKADEKGNLAGERQSGDGQESTEDP
SQ  ENKGSKGQKLDDDEDRKNPAYIPRKGLFFEHDVRGQATEEERPKGRNRKLWKDEGRWEHDKFREEEQAPKSRDELIAFYG
SQ  YDIRNGTGPSDGRSYRSRKPRHAGSPSREPRRYREGDKSVRSSWQGPPPGHRNAPQSVTVQSGQPLAPLSAPKPSGRPST
SQ  QPPQRSFQGSRAPSAPHRTEGRGPSKPSLDGAPLRGPRSQPVEGERGPRLRGRSSHAVHADRSPSLVVEDICSEEEEEEG
SQ  EIPTATTTYTAHHYKTEKERVPSPRKQDSGMVMEGGSAAGQVRELSPPQERQVEKKSYSRARRATRTRPSDLSKQASLDD
SQ  SSSAVQQAPVAAKSESWQEQSEAGTQSGLTGLDQDLARLSLTGQNWAQNPPSYLQAEMRGIRGSMHMAGGPPQYGNMEDM
SQ  GVGGGRAKRYSSQRQRPVPEPAPMHIGVMEGHYYEPMTFQGPIYTHGESPAALPPQGMLVQPEMHLPHPTHPGLHPHQSG
SQ  GPLPNPAIYAAPPVSLSPGQPPPQQLLPPPFYPPPGVMTFGNTNYPYPAGGTLPPMYPNPQAQSQVYGGVTYYDTIQQQA
SQ  QPKRSPPRRSSNPVTVRPPPPEDQSRKAAEEIRS
//
ID  O15234;
PN  Protein CASC3;
GN  CASC3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12080473}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus {ECO:0000269|PubMed:12080473, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. Nucleus speckle {ECO:0000269|PubMed:16170325}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17652158}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q8K3X0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8K3X0}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (PubMed:15166247). In nuclear speckles, colocalizes with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules (PubMed:17652158). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:Q8K3X0, ECO:0000269|PubMed:15166247, ECO:0000269|PubMed:17652158}.
DR  UNIPROT: O15234;
DR  UNIPROT: A8K8R0;
DR  PDB: 2HYI;
DR  PDB: 2J0Q;
DR  PDB: 2J0S;
DR  PDB: 2J0U;
DR  PDB: 2XB2;
DR  PDB: 3EX7;
DR  PDB: 5XJC;
DR  PDB: 5YZG;
DR  PDB: 6ICZ;
DR  Pfam: PF09405;
DR  OMIM: 606504;
DR  DisGeNET: 22794;
DE  Function: Required for pre-mRNA splicing as component of the spliceosome (PubMed:28502770, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homomer. {ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:17652158, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}.
DE  Reference Proteome: Yes;
DE  Interaction: P38919; IntAct: EBI-299122; Score: 0.98
DE  Interaction: P61326; IntAct: EBI-299142; Score: 0.96
DE  Interaction: O95793; IntAct: EBI-536629; Score: 0.35
DE  Interaction: Q9Y5S9; IntAct: EBI-15556968; Score: 0.86
DE  Interaction: Q9BZI7; IntAct: EBI-15674292; Score: 0.79
DE  Interaction: Q9H1J1; IntAct: EBI-3869363; Score: 0.35
DE  Interaction: P62993; IntAct: EBI-3937731; Score: 0.37
DE  Interaction: Q00534; IntAct: EBI-5292877; Score: 0.44
DE  Interaction: P04578; IntAct: EBI-6176374; Score: 0.35
DE  Interaction: Q9Y2W1; IntAct: EBI-6464350; Score: 0.40
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: P31749; IntAct: EBI-9065079; Score: 0.37
DE  Interaction: P25054; IntAct: EBI-9065274; Score: 0.37
DE  Interaction: Q14790; IntAct: EBI-9066600; Score: 0.37
DE  Interaction: P42771; IntAct: EBI-9067082; Score: 0.37
DE  Interaction: Q92731; IntAct: EBI-9067732; Score: 0.37
DE  Interaction: P22455; IntAct: EBI-9068122; Score: 0.37
DE  Interaction: O60934; IntAct: EBI-9068798; Score: 0.37
DE  Interaction: P35232; IntAct: EBI-9069474; Score: 0.37
DE  Interaction: P18031; IntAct: EBI-9069851; Score: 0.37
DE  Interaction: Q12913; IntAct: EBI-9070007; Score: 0.37
DE  Interaction: P67809; IntAct: EBI-9985228; Score: 0.35
DE  Interaction: P41218; IntAct: EBI-9996028; Score: 0.35
DE  Interaction: Q6P1M3; IntAct: EBI-11024291; Score: 0.35
DE  Interaction: Q9CWZ3; IntAct: EBI-11033143; Score: 0.35
DE  Interaction: Q93074; IntAct: EBI-11039728; Score: 0.35
DE  Interaction: Q9D902; IntAct: EBI-11096128; Score: 0.35
DE  Interaction: Q8NB78; IntAct: EBI-11101709; Score: 0.35
DE  Interaction: Q7LFX5; IntAct: EBI-11123526; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q3LI66; IntAct: EBI-24633422; Score: 0.56
DE  Interaction: Q9UEU0; IntAct: EBI-21525256; Score: 0.35
DE  Interaction: P47902; IntAct: EBI-21581572; Score: 0.35
DE  Interaction: Q12926; IntAct: EBI-21666158; Score: 0.35
DE  Interaction: Q8IYD1; IntAct: EBI-21666681; Score: 0.35
DE  Interaction: Q96AK3; IntAct: EBI-21666867; Score: 0.35
DE  Interaction: Q13595; IntAct: EBI-21690239; Score: 0.35
DE  Interaction: P26368; IntAct: EBI-21718427; Score: 0.35
DE  Interaction: P49760; IntAct: EBI-21726948; Score: 0.35
DE  Interaction: Q6ZUT1; IntAct: EBI-21727187; Score: 0.35
DE  Interaction: Q8N6W0; IntAct: EBI-21727590; Score: 0.35
DE  Interaction: Q8TAD8; IntAct: EBI-21727669; Score: 0.35
DE  Interaction: Q9H307; IntAct: EBI-21728050; Score: 0.35
DE  Interaction: Q9NQ29; IntAct: EBI-21728243; Score: 0.35
DE  Interaction: Q9BRP8; IntAct: EBI-21727928; Score: 0.35
DE  Interaction: Q9NQX1; IntAct: EBI-21728580; Score: 0.35
DE  Interaction: Q9Y383; IntAct: EBI-21728858; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-21728803; Score: 0.35
DE  Interaction: Q92900; IntAct: EBI-15784788; Score: 0.70
DE  Interaction: Q9HAU5; IntAct: EBI-15855293; Score: 0.70
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21302175; Score: 0.35
DE  Interaction: Q92574; IntAct: EBI-26515506; Score: 0.37
DE  Interaction: O60306; IntAct: EBI-26901687; Score: 0.32
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0035145;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0071006;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0031625;
GO  GO:0008298;
GO  GO:0006406;
GO  GO:0000398;
GO  GO:0000184;
GO  GO:2000622;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESE
SQ  DGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVEN
SQ  KVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALY
SQ  GYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFK
SQ  EGRAGFRPVEAGGQHGGRSGETVKHEISYRSRRLEQTSVRDPSPEADAPVLGSPEKEEAASEPPAAAPDAAPPPPDRPIE
SQ  KKSYSRARRTRTKVGDAVKLAEEVPPPPEGLIPAPPVPETTPTPPTKTGTWEAPVDSSTSGLEQDVAQLNIAEQNWSPGQ
SQ  PSFLQPRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTH
SQ  GDSPAPLPPQGMLVQPGMNLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPG
SQ  ALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS
//
ID  Q8K3W3;
PN  Protein CASC3;
GN  Casc3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12843282}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12843282}. Nucleus {ECO:0000269|PubMed:12843282}. Nucleus speckle {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:12843282}. Cell projection, dendrite {ECO:0000269|PubMed:12843282}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner (PubMed:12843282). Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. In nuclear speckles, colocalizes with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules (By similarity). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (Probable). {ECO:0000250|UniProtKB:O15234, ECO:0000269|PubMed:12843282, ECO:0000305|PubMed:12843282}.
DR  UNIPROT: Q8K3W3;
DR  UNIPROT: A3KFP7;
DR  UNIPROT: Q3UT99;
DR  UNIPROT: Q8K219;
DR  UNIPROT: Q99NF0;
DR  Pfam: PF09405;
DE  Function: Required for pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon- exon junctions. Binds poly(G) and poly(U) RNA homomer. {ECO:0000250|UniProtKB:O15234}.
DE  Reference Proteome: Yes;
DE  Interaction: P35922; IntAct: EBI-16728828; Score: 0.35
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:0035145;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0071006;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0003729;
GO  GO:0031625;
GO  GO:0008298;
GO  GO:0006406;
GO  GO:0000398;
GO  GO:0000184;
GO  GO:2000622;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRRRQRASQDTEDEESGASGSDSGSPARGGGSCSGSVGGGGSGSLPSQRGGRGGGLHLRRVESGGAKSAEESECESED
SQ  GMEGDAVLSDYESAEDSEGEEDYSEEENSKVELKSEANDAADSSAKEKGEEKPESKGTVTGERQSGDGQESTEPVENKVG
SQ  KKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYD
SQ  IRSAHNPDDIKPRRIRKPRFGSSPQRDPNWIGDRSSKSHRHQGPGGNLPPRTFINRNTAGTGRMSASRNYSRSGGFKDGR
SQ  TSFRPVEVAGQHGGRSAETLKHEASYRSRRLEQTPVRDPSPEPDAPLLGSPEKEEVASETPAAVPDITPPAPDRPIEKKS
SQ  YSRARRTRTKVGDAVKAAEEVPPPSEGLASTATVPETTPAAKTGNWEAPVDSTTGGLEQDVAQLNIAEQSWSPSQPSFLQ
SQ  PRELRGVPNHIHMGAGPPPQFNRMEEMGVQSGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPA
SQ  PLPPQGMIVQPEMHLPHPGLHPHQSPGPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPNYPYAPGALPPP
SQ  PPPHLYPNTQAPPQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVSIKPPPPEVVSRGSS
//
ID  Q8K3X0;
PN  Protein CASC3;
GN  Casc3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12843282}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12843282}. Nucleus {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus speckle {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O15234}. Cell projection, dendrite {ECO:0000269|PubMed:12843282}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner (By similarity). Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. In nuclear speckles, colocalizes with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules (By similarity). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (Probable). {ECO:0000250|UniProtKB:O15234, ECO:0000250|UniProtKB:Q8K3W3, ECO:0000305|PubMed:12843282}.
DR  UNIPROT: Q8K3X0;
DR  Pfam: PF09405;
DE  Function: Required for pre-mRNA splicing as component of the spliceosome (By similarity). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon- exon junctions. Binds poly(G) and poly(U) RNA homomer (By similarity). Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. {ECO:0000250|UniProtKB:O15234, ECO:0000269|PubMed:12843282}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:0035145;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0071006;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0003729;
GO  GO:0031625;
GO  GO:0008298;
GO  GO:0000398;
GO  GO:0051028;
GO  GO:0000184;
GO  GO:2000622;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRRRQRASQDTEDEESGASGSDSGSPARGGGSCSGSAGGGGSGSLPSQRGGRGGGLHLRRVESGGAKSAEESECESED
SQ  GMEGDAVLSDYESAEDSEGEEEYSEEENSKVELKSEANDAADSSAKEKGEEKPESKGTVTGERQSGDGQESTEPVENKVG
SQ  KKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYD
SQ  IRSAHNPDDIKPRRIRKPRFGSPPQRDPNWIGDRSSKSHRHQGPGGNLPPRTFINRNAAGTGRMSTSRNYSRSGGFKEGR
SQ  TSFRPVEVGGQHGARSGETLKHEANYRSRRLEQTPMRDPSPEPDAPLLGSPEKEEVASETPAAVPDITPPAPDRPIEKKS
SQ  YSRARRTRTKVGDAVKAAEEVPPPSEGLTSAATVPESTPPAAKTGNWEAPVDSTTGGLEQDVAQLNIAEQNWSPGQPSFL
SQ  QPRELRGMPNHIHMGAGPPPQFNRMEEMGVQSGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSP
SQ  APLPPQGMIVQPEMHLPHPGLHPHQSPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPP
SQ  PPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVSIKPPPSEVVSRGSS
//
ID  A0JMU8;
PN  Protein CASC3;
GN  casc3;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O15234}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus {ECO:0000250|UniProtKB:O15234}. Nucleus speckle {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q8K3X0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8K3X0}. Note=Shuttles between the nucleus and the cytoplasm in a xpo1/crm1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (By similarity). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:O15234, ECO:0000250|UniProtKB:Q8K3X0}.
DR  UNIPROT: A0JMU8;
DR  UNIPROT: B7ZRY2;
DR  Pfam: PF09405;
DE  Function: Required for pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. {ECO:0000250|UniProtKB:O15234}.
DE  Reference Proteome: Yes;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:0035145;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0071006;
GO  GO:0003729;
GO  GO:0000398;
GO  GO:0051028;
GO  GO:0000184;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRRRRRRRASQDSEGEEEEEESGSDSVGSGGESGAPVRQERSEQGNRKAEPPREGKESECESEDGIEGDAVLSDYESA
SQ  DESEIVPTKEVEEAHYNEEEPLKATLKQENNVEEAPAARDQKPKSKGTVTGERQSGDGQESNEPEEDKTIQKSQKQLDDD
SQ  EDRKNPAYIPRKGLFFEHDLRGHVNDEEVRPKGRHPRKLWKDEGRWVHDRFHEDEQAPKSREELISIYGYDIRSSKNPEE
SQ  IRPRRPRKPRFSSPSRREENNEKASWPLNRYQDSGDAQPLRPYTNRSAPPSNKVVPSRTYSRQGGYKENRASYQSEEEAS
SQ  LHTYERRQVYGGHRARSSEQGPPPPREFSPEADPIVKEEAVIEKQAAEPSPPPPDRPVEKKSYSRARRSRIKVGDTGKSM
SQ  EDTTAAELPPPPLMPPAVAAEFTPAPLNVKQGNWEPPAEGGMSGIDEELSQMNLTEQSWNQGQPAYISPRGIPNPMHMGN
SQ  GPPQYSRMEGMAVQGGRVKRYSSQRQRPVPDPAAMHISLMESHYYDPLQFQGPIYTHGDSSSSMPPQGMIVPPEMHLSHP
SQ  GMHPHPSPATMSTPNLYPAPVSLPPGQQPPQQLLPPPYFPAPPNVMNFGNPTYPYPPGALPPPPAHLYPNAQAQSQVYGG
SQ  VTYYNPVQQQVQPKPSPPRRTSQPVTIKPPPPEENRHLKMNEKINS
//
ID  Q5CZI8;
PN  Protein CASC3;
GN  casc3;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O15234}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus {ECO:0000250|UniProtKB:O15234}. Nucleus speckle {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q8K3X0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8K3X0}. Note=Shuttles between the nucleus and the cytoplasm in a xpo1/crm1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (By similarity). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). {ECO:0000250|UniProtKB:O15234, ECO:0000250|UniProtKB:Q8K3X0}.
DR  UNIPROT: Q5CZI8;
DR  Pfam: PF09405;
DE  Function: Required for pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. {ECO:0000250|UniProtKB:O15234}.
DE  Reference Proteome: Yes;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:0035145;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0071006;
GO  GO:0003729;
GO  GO:0000398;
GO  GO:0051028;
GO  GO:0000184;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRRRRRRRAFQDSEEEEDEESGSESAGSGGQPAAPSRQESREPGTKRAEPPREGKESECESEDGIEGDAVLSDYESAE
SQ  SEEEEAHLSEEEPLKTTLKQENNVEEAPATREQKPKSKGAVTGERQSGDGQESTEPEENKTSKKSQKQLDDDEDRKNPAY
SQ  IPRKGLFFEHDLRGHVNDEEVRPKGRHPRKLWKDEGRWEHDRFREDEQAPKSREELISIYGYDIRSSKNSEEIRPRRPRK
SQ  PRFGSPTRREEISEKPSRPSNRYQDSGISQPLRPYTNRNAPPSNKVGPSRTYSRQGGYKENRSSYQSEEEAPPHPSERRQ
SQ  DYGGHRARSTEQGPAPPREFSPEADPIIKEEPVIEKQAAEPSPPPPDRPVEKKSYSRVRRSRIKVGDTGKSMEDTTVTEL
SQ  PPPPPVPPAVAAEFTPAPLNVKQGNWEPPSEGGMSGIEEELSQMNLSEQSWNPGQPAYISPRGIPNPMHMGGGPPQYNRM
SQ  EGMAVQGGRVKRYSTQRQRPVPDPAAMHISLMESHYYDPLQFQGPIYAHGDSPSSMPPQGMIVQPEMHLSHPGIHPHQPP
SQ  ATISTPNLYPAPVSLPPGQPPPQQLLPPPYFTAPPNVMNFGNPTYPYPPGALPPPPAHLYPNAQAQSQVYGGVTYYNPVQ
SQ  QQVQPKPSPPRRTSQPVTIKPPPPEENRHVKMKEKSNS
//
ID  Q5H8A6;
PN  Ion channel CASTOR;
GN  CASTOR;
OS  34305;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15616514, ECO:0000269|PubMed:19106374}; Multi-pass membrane protein {ECO:0000269|PubMed:15616514, ECO:0000269|PubMed:19106374}. Note=The chloroplastic localization proposed by PubMed:15616514 is probably an overexpression artifact.
DR  UNIPROT: Q5H8A6;
DR  PDB: 6O6J;
DR  PDB: 6O7A;
DR  PDB: 6O7C;
DR  Pfam: PF06241;
DE  Function: Ion channel with a moderate preference for potassium over sodium and calcium. Involved in perinuclear calcium spiking but not in cytosolic calcium influx. Closed at negative voltages in presence of magnesium. Required for early signal transduction events leading to endosymbiosis. Acts early in a signal transduction chain leading from the perception of Nod factor to the activation of calcium spiking. Also involved in fungal entry into root epidermal cells during the establishment of the arbuscular mycorrhizal symbiosis. {ECO:0000269|PubMed:16903357, ECO:0000269|PubMed:19106374}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006811;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLDSEVSVSSSSGRDWFFPSPSFFRSSPSQYGRRFHTNSNTHSAPSSTYPSGIRHRRRVKFSRTPTTSSNEKPQISIVS
SQ  DKPSAISKNNLNWLSQFGLQFALVTLTIVFLLLLLLRNTHLESQVNKLQGEILRLHACHQLDTLNVSSSTAHKSQDTHPC
SQ  SCENFKRNLALFLSFMLLLIPLIIFKYIDYVSRSRLSENISEQVSLNKQIAYRVDVFLSVYPYAKPLVLLVATLLLIFLG
SQ  GLTLFGVTTEDLGHCLWLSWTYVADSGNHASSEGIGPRLVAVSISFGGMLIFAMMLGLVSDAISEKFDSLRKGKSEVVEQ
SQ  NHTLILGWSDKLGSLLNQLAIANESLGGGTIAVMAERDKEDMELDIGKMEFDFKGTSVICRSGSPLILADLKKVSVSKAR
SQ  TIIVLAEDGNADQSDARALRTVLSLTGVKEGLRGHIVVEMSDLDNEVLVKLVGGDLVETVVAHDVIGRLMIQCARQPGLA
SQ  QIWEDILGFENCEFYIKRWPQLDGMLFEDVLISFPAAIPCGIKVASYGGKIILNPDDSYVLQEGDEVLVIAEDDDTYAPA
SQ  PLPMVRRGSLPKDFVYPKSPERILFCGWRRDMEDMITVLDASLAPDSELWMFNDVPEKEREKKLIDGGLDISRLENISLV
SQ  NREGNAVIRRHLESLPLESFDSILILADESVEDSAIQADSRSLATLLLIRDIQARRLPYVAMASQTQGGNFSKGSWIGEM
SQ  KQASDKTVIISEILDPRTKNLLSMSKISDYVLSNELVSMALAMVAEDRQINDVLEELFAEEGNEMHIRQADIYLREGEEM
SQ  SFYEIMLRARQRREILIGYRLANAERAVINPPAKTGRRKWSLKDVFVVITEKE
//
ID  Q75LD5;
PN  Probable ion channel CASTOR;
GN  OSJNBa0032G11;
OS  39947;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q75LD5;
DR  UNIPROT: Q10AR8;
DR  Pfam: PF06241;
DE  Function: Required for mycorrhizal symbiosis. {ECO:0000269|PubMed:18852152, ECO:0000269|PubMed:18978069}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006811;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPLDPDSSPAPPHRDWFFPPAPPFLPSSRARTPRAPFPSTSRSSNPYSFPDRRPPPTPRSRSRSPLPPPEQQKQQQPPPT
SQ  TPPPAPRRRDPRYAGVRRGDVRTLTAEKAAAAAAVPTAAQVHGSKSAASATTLRWSGMVSVAAIVLCFSSLVRSNSSLHD
SQ  QVHHLKAQLAEATTKLQSCITESSMDMSSILSYQSNNSTSQNRGLKNFSLLLSLSTLYAPLLILKYMDLFLKLRSSQDSE
SQ  EEVPINKRLAYRVDIFLSLQPYAKPLVLLVATLLLIGLGGLALYGVNDDSLLDCLWLSWTFVADSGNHANAEGFGPKLVS
SQ  VSISIGGMLVFAMMLGLVTDSISEKFDSLRKGRSEVIEQSHTLVLGWSDKLGSLLNQIAIANESLGGGTIVVMAEKDKEE
SQ  MEADIAKMEFDLKGTAIICRSGSPLILADLKKVSVSKARAIVVLAEEGNADQSDARALRTVLSLTGVKEGLRGHIVVELS
SQ  DLDNEVLVKLVGGDLVETVVAHDVIGRLMIQCARQPGLAQIWEDILGFENCEFYIKRWPQLDGMQFEDVLISFPDAIPCG
SQ  IKVASYGGKIILNPDDFYVLQEGDEVLVIAEDDDTYAPAPLPKVMRGYLPKDFVVPKSPERILFCGWRRDMEDMIMVLDA
SQ  FLAPGSELWMFNDVPEMDRERKLIDGGLDFSRLENITLVHREGNAVIRRHLESLPLESFDSILILADESVEDSAIQADSR
SQ  SLATLLLIRDIQAKRLPFREAMVSHVTRGSFCEGSWIGEMQQASDKSVIISEILDPRTKNLLSVSKISDYVLSNELVSMA
SQ  LAMVAEDRQINDVLEELFAEQGNEMQIRPADLYLREDEELNFFEVMLRGRQRKEIVIGYRLVDAERAIINPPDKVSRRRW
SQ  SAKDVFVVITEKE
//
ID  Q91ZF2;
PN  Cathepsin 7;
GN  Cts7;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endosome {ECO:0000269|PubMed:18776147, ECO:0000305}. Lysosome {ECO:0000269|PubMed:18776147, ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18776147}. Golgi apparatus {ECO:0000269|PubMed:18776147, ECO:0000305}. Nucleus {ECO:0000269|PubMed:18776147}. Secreted, extracellular space {ECO:0000269|PubMed:18776147}.
DR  UNIPROT: Q91ZF2;
DR  UNIPROT: Q9JI84;
DR  Pfam: PF08246;
DR  Pfam: PF00112;
DR  PROSITE: PS00139;
DR  PROSITE: PS00639;
DE  Function: Involved in trophoblast cell proliferation and differentiation probably by affecting mitotic cell cycle progression. Proteolytic activity and nuclear localization are essential for its role in cell cycle progression. {ECO:0000269|PubMed:18776147}.
DE  Reference Proteome: Yes;
GO  GO:0005768;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0005764;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004197;
GO  GO:0008233;
GO  GO:0051301;
GO  GO:0006955;
GO  GO:0000278;
GO  GO:0045930;
GO  GO:0006508;
GO  GO:0051603;
GO  GO:0060707;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTPTVFLSILCLGVALAAPAPDYNLDAEWEEWKRSNDRTYSPEEEKQRRAVWEGNVKWIKQHIMENGLWMNNFTIEMNEF
SQ  GDMTGEEMKMLTESSSYPLRNGKHIQKRNPKIPPTLDWRKEGYVTPVRRQGSCGACWAFSVTACIEGQLFKKTGKLIPLS
SQ  VQNLMDCSVSYGTKGCDGGRPYDAFQYVKNNGGLEAEATYPYEAKAKHCRYRPERSVVKVNRFFVVPRNEEALLQALVTH
SQ  GPIAVAIDGSHASFHSYRGGIYHEPKCRKDTLDHGLLLVGYGYEGHESENRKYWLLKNSHGERWGENGYMKLPRGQNNYC
SQ  GIASYAMYPAL
//
ID  D3ZZ07;
PN  Cathepsin 7;
GN  Cts7;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Endosome {ECO:0000250|UniProtKB:Q91ZF2}. Lysosome {ECO:0000250|UniProtKB:Q91ZF2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q91ZF2}. Golgi apparatus {ECO:0000250|UniProtKB:Q91ZF2}. Nucleus {ECO:0000250|UniProtKB:Q91ZF2}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q91ZF2}.
DR  UNIPROT: D3ZZ07;
DR  Pfam: PF08246;
DR  Pfam: PF00112;
DR  PROSITE: PS00139;
DR  PROSITE: PS00639;
DE  Function: Involved in trophoblast cell proliferation and differentiation probably by affecting mitotic cell cycle progression. Proteolytic activity and nuclear localization are essential for its role in cell cycle progression (By similarity). {ECO:0000250|UniProtKB:Q91ZF2}.
DE  Reference Proteome: Yes;
GO  GO:0005768;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0005764;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004197;
GO  GO:0051301;
GO  GO:0006955;
GO  GO:0000278;
GO  GO:0045930;
GO  GO:0051603;
GO  GO:0060707;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVAVFLAILCLRAALAAPRPDYSLDAEWEEWKRNNAKTYSPEEEKQRRAVWEENVKMIKWHTMQNGLWMNNFTIEMNEF
SQ  GDMTGEEMRMMTDSSALTLRNGKHIQKRNVKIPKTLDWRDTGCVAPVRSQGGCGACWAFSVAASIESQLFKKTGKLIPLS
SQ  VQNLIDCTVTYGNNDCSGGKPYTAFQYVKNNGGLEAEATYPYEAKLRHCRYRPERSVVKIARFFVVPRNEEALMQALVTY
SQ  GPIAVAIDGSHASFKRYRGGIYHEPKCRRDTLDHGLLLVGYGYEGHESENRKYWLLKNSHGEQWGERGYMKLPRDQNNYC
SQ  GIASYAMYPLL
//
ID  Q8IX12;
PN  Cell division cycle and apoptosis regulator protein 1;
GN  CCAR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12816952}.
DR  UNIPROT: Q8IX12;
DR  UNIPROT: A0JLT7;
DR  UNIPROT: A1L4P7;
DR  UNIPROT: A8K9D4;
DR  UNIPROT: B4DNP8;
DR  UNIPROT: B4DRK8;
DR  UNIPROT: Q32NE3;
DR  UNIPROT: Q5EBM3;
DR  UNIPROT: Q5VUP6;
DR  UNIPROT: Q6PIZ0;
DR  UNIPROT: Q6X935;
DR  UNIPROT: Q9H8N4;
DR  UNIPROT: Q9NVA7;
DR  UNIPROT: Q9NVQ0;
DR  UNIPROT: Q9NWM6;
DR  Pfam: PF19257;
DR  Pfam: PF14443;
DR  Pfam: PF19256;
DR  Pfam: PF14444;
DR  Pfam: PF02037;
DR  PROSITE: PS50800;
DR  OMIM: 612569;
DR  DisGeNET: 55749;
DE  Function: Associates with components of the Mediator and p160 coactivator complexes that play a role as intermediaries transducing regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Recruited to endogenous nuclear receptor target genes in response to the appropriate hormone. Also functions as a p53 coactivator. May thus play an important role in transcriptional regulation (By similarity). May be involved in apoptosis signaling in the presence of the reinoid CD437. Apoptosis induction involves sequestration of 14-3-3 protein(s) and mediated altered expression of multiple cell cycle regulatory genes including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or cell proliferation (PubMed:12816952). In association with CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). Can act as a both a coactivator and corepressor of AR-mediated transcription. Contributes to chromatin looping and AR transcription complex assembly by stabilizing AR-GATA2 association on chromatin and facilitating MED1 and RNA polymerase II recruitment to AR-binding sites. May play an important role in the growth and tumorigenesis of prostate cancer cells (PubMed:23887938). {ECO:0000250|UniProtKB:Q8CH18, ECO:0000269|PubMed:12816952, ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:24245781}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P07948; IntAct: EBI-25379971; Score: 0.35
DE  Interaction: Q8IWX8; IntAct: EBI-7721515; Score: 0.37
DE  Interaction: Q9Y6K9; IntAct: EBI-21708976; Score: 0.35
DE  Interaction: Q9BTT4; IntAct: EBI-394793; Score: 0.35
DE  Interaction: Q920D3; IntAct: EBI-394916; Score: 0.35
DE  Interaction: Q15428; IntAct: EBI-7292802; Score: 0.40
DE  Interaction: Q969Q1; IntAct: EBI-7745325; Score: 0.51
DE  Interaction: Q9BYV6; IntAct: EBI-7745490; Score: 0.40
DE  Interaction: Q9HAU4; IntAct: EBI-7746831; Score: 0.37
DE  Interaction: E9Q5G3; IntAct: EBI-2561306; Score: 0.40
DE  Interaction: P29692; IntAct: EBI-2688113; Score: 0.00
DE  Interaction: A0A6L7HJW4; IntAct: EBI-2813341; Score: 0.00
DE  Interaction: A0A6L8PAG8; IntAct: EBI-2836932; Score: 0.00
DE  Interaction: Q92731; IntAct: EBI-2880601; Score: 0.35
DE  Interaction: Q9GZV5; IntAct: EBI-2927886; Score: 0.40
DE  Interaction: Q9EPK5; IntAct: EBI-2928071; Score: 0.46
DE  Interaction: P05131; IntAct: EBI-2931831; Score: 0.35
DE  Interaction: Q9BQS8; IntAct: EBI-3242919; Score: 0.35
DE  Interaction: P26368; IntAct: EBI-7718617; Score: 0.37
DE  Interaction: P98175; IntAct: EBI-7723515; Score: 0.37
DE  Interaction: P61978; IntAct: EBI-7723565; Score: 0.37
DE  Interaction: O15541; IntAct: EBI-7723603; Score: 0.37
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-10262415; Score: 0.72
DE  Interaction: Q9NQM4; IntAct: EBI-10262427; Score: 0.56
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: Q7TSY8; IntAct: EBI-11011396; Score: 0.35
DE  Interaction: Q9EP53; IntAct: EBI-11016226; Score: 0.35
DE  Interaction: O00159; IntAct: EBI-11030803; Score: 0.35
DE  Interaction: Q1H9T6; IntAct: EBI-11104278; Score: 0.35
DE  Interaction: A0A286YCX6; IntAct: EBI-11119288; Score: 0.35
DE  Interaction: P09450; IntAct: EBI-11127973; Score: 0.35
DE  Interaction: Q15006; IntAct: EBI-11130215; Score: 0.35
DE  Interaction: Q8N4V1; IntAct: EBI-11130635; Score: 0.35
DE  Interaction: Q9Y2D8; IntAct: EBI-11363757; Score: 0.35
DE  Interaction: Q5JR59; IntAct: EBI-24372606; Score: 0.56
DE  Interaction: Q13643; IntAct: EBI-21785384; Score: 0.35
DE  Interaction: Q15942; IntAct: EBI-21889175; Score: 0.35
DE  Interaction: Q92609; IntAct: EBI-20919940; Score: 0.40
DE  Interaction: Q7Z422; IntAct: EBI-20924474; Score: 0.40
DE  Interaction: Q9BY12; IntAct: EBI-20929648; Score: 0.40
DE  Interaction: Q96HF1; IntAct: EBI-20930680; Score: 0.40
DE  Interaction: Q8TCG1; IntAct: EBI-20933820; Score: 0.40
DE  Interaction: Q9NPJ6; IntAct: EBI-25472377; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P09429; IntAct: EBI-21461848; Score: 0.37
DE  Interaction: P05771; IntAct: EBI-25379671; Score: 0.35
DE  Interaction: Q5SSL4; IntAct: EBI-25409695; Score: 0.35
DE  Interaction: Q6B0I6; IntAct: EBI-25480104; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-26398473; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-26398788; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27046166; Score: 0.35
DE  Interaction: P78362; IntAct: EBI-28948274; Score: 0.35
DE  Interaction: O15178; IntAct: EBI-29014443; Score: 0.27
DE  Interaction: P15976; IntAct: EBI-29016000; Score: 0.27
DE  Interaction: P23771; IntAct: EBI-29016184; Score: 0.27
DE  Interaction: Q8TDD2; IntAct: EBI-29740517; Score: 0.27
GO  GO:0005641;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030374;
GO  GO:0003723;
GO  GO:0000978;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0006915;
GO  GO:0007049;
GO  GO:0043065;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQFGGQKNPPWATQFTATAVSQPAALGVQQPSLLGASPTIYTQQTALAAAGLTTQTPANYQLTQTAALQQQAAAAAAAL
SQ  QQQYSQPQQALYSVQQQLQQPQQTLLTQPAVALPTSLSLSTPQPTAQITVSYPTPRSSQQQTQPQKQRVFTGVVTKLHDT
SQ  FGFVDEDVFFQLSAVKGKTPQVGDRVLVEATYNPNMPFKWNAQRIQTLPNQNQSQTQPLLKTPPAVLQPIAPQTTFGVQT
SQ  QPQPQSLLQAQISAASITPLLQTQPQPLLQQPQQKAGLLQPPVRIVSQPQPARRLDPPSRFSGRNDRGDQVPNRKDDRSR
SQ  ERERERRRSRERSPQRKRSRERSPRRERERSPRRVRRVVPRYTVQFSKFSLDCPSCDMMELRRRYQNLYIPSDFFDAQFT
SQ  WVDAFPLSRPFQLGNYCNFYVMHREVESLEKNMAILDPPDADHLYSAKVMLMASPSMEDLYHKSCALAEDPQELRDGFQH
SQ  PARLVKFLVGMKGKDEAMAIGGHWSPSLDGPDPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRPEETHKGR
SQ  TVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGERKEADGEQDEEEKDDGEAKEISTPTHWSKLDPKTMK
SQ  VNDLRKELESRALSSKGLKSQLIARLTKQLKVEEQKEEQKELEKSEKEEDEDDDRKSEDDKEEEERKRQEEIERQRRERR
SQ  YILPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSLLSLPEKEDKK
SQ  EKDKKSKKDERKDKKEERDDETDEPKPKRRKSGDDKDKKEDRDERKKEDKRKDDSKDDDETEEDNNQDEYDPMEAEEAED
SQ  EEDDRDEEEMTKRDDKRDINRYCKERPSKDKEKEKTQMITINRDLLMAFVYFDQSHCGYLLEKDLEEILYTLGLHLSRAQ
SQ  VKKLLNKVVLRESCFYRKLTDTSKDEENHEESESLQEDMLGNRLLLPTPTVKQESKDVEENVGLIVYNGAMVDVGSLLQK
SQ  LEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVKKDLSQLQENLKISENMNLQFENQMNKTIRNLST
SQ  VMDEIHTVLKKDNVKNEDKDQKSKENGASV
//
ID  Q8CH18;
PN  Cell division cycle and apoptosis regulator protein 1;
GN  Ccar1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q8CH18;
DR  UNIPROT: Q05BR1;
DR  UNIPROT: Q05DK6;
DR  UNIPROT: Q6AXC9;
DR  UNIPROT: Q6PAR2;
DR  UNIPROT: Q80XE4;
DR  UNIPROT: Q8BJY0;
DR  UNIPROT: Q8BVN2;
DR  UNIPROT: Q8CGG1;
DR  UNIPROT: Q9CSR5;
DR  Pfam: PF19257;
DR  Pfam: PF14443;
DR  Pfam: PF19256;
DR  Pfam: PF14444;
DR  Pfam: PF02037;
DR  PROSITE: PS50800;
DE  Function: Associates with components of the Mediator and p160 coactivator complexes that play a role as intermediaries transducing regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Recruited to endogenous nuclear receptor target genes in response to the appropriate hormone. Also functions as a p53 coactivator. May thus play an important role in transcriptional regulation. May be involved in apoptosis signaling in the presence of the retinoid CD437. Apoptosis induction involves sequestration of 14-3-3 protein(s) and mediated altered expression of multiple cell cycle regulatory genes including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or cell proliferation (By similarity). In association with CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). Can act as a both a coactivator and corepressor of AR-mediated transcription. Contributes to chromatin looping and AR transcription complex assembly by stabilizing AR-GATA2 association on chromatin and facilitating MED1 and RNA polymerase II recruitment to AR-binding sites. May play an important role in the growth and tumorigenesis of prostate cancer cells (PubMed:23887938). {ECO:0000250|UniProtKB:Q8IX12, ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:24245781}.
DE  Reference Proteome: Yes;
DE  Interaction: P47811; IntAct: EBI-654069; Score: 0.37
DE  Interaction: P59240; IntAct: EBI-4287460; Score: 0.35
DE  Interaction: P70326; IntAct: EBI-16360068; Score: 0.35
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
DE  Interaction: Q14B62; IntAct: EBI-27105988; Score: 0.35
GO  GO:0005641;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030374;
GO  GO:0000978;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0006915;
GO  GO:0007049;
GO  GO:0043065;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQFGGQKNPPWATQFTATAVSQPAALGVQQPSLLGASPTIYTQQTALAAAGLTTQTPANYQLTQTAALQQQAAAVLQQQ
SQ  YSQPQQALYSVQQQLQQPQQTILTQPAVALPTSLSLSTPQPAAQITVSYPTPRSSQQQTQPQKQRVFTGVVTKLHDTFGF
SQ  VDEDVFFQLGAVKGKTPQVGDRVLVEATYNPNMPFKWNAQRIQTLPNQNQSQTQPLLKTPTAVIQPIVPQTTFGVQAQPQ
SQ  PQSLLQAQISAASITPLLQTQPQPLLQQPQQKAGLLQPPVRIVSQPQPARRLDPPSRFSGRNDRGDQVPNRKDDRSRERD
SQ  RERRRSRERSPQRKRSRERSPRRERERSPRRVRRVVPRYTVQFSKFSLDCPSCDMMELRRRYQNLYIPSDFFDAQFTWVD
SQ  AFPLSRPFQLGNYCNFYVMHREVESLEKNMAVLDPPDADHLYSAKVMLMASPSMEDLYHKSCALAEDPQDLRDGFQHPAR
SQ  LVKFLVGMKGKDEAMAIGGHWSPSLDGPNPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRPEETHKGRTVP
SQ  AHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGERKKADGEQDEEEKDDGEVKEIATPTHWSKLDPKAMKVND
SQ  LRKELESRALSSKGLKSQLIARLTKQLKIEEQKEEQKELEKSEKEEEDEDDKKSEDDKEEEERKRQEEVERQRQERRYIL
SQ  PDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSLLSLPEKEDKKDKE
SQ  KKSKKEERKDKKEEREDDIDEPKPKRRKSGDDKDKKEDRDERKKEEKRKDDSKDDDETEEDNNQDEYDPMEAEEAEDEDD
SQ  DREEEEVKRDDKRDVSRYCKDRPAKDKEKEKPQMVTVNRDLLMAFVYFDQSHCGYLLEKDLEEILYTLGLHLSRAQVKKL
SQ  LNKVVLRESCFYRKLTDTSKDDENHEESEALQEDMLGNRLLLPTPTIKQESKDGEENVGLIVYNGAMVDVGSLLQKLEKS
SQ  EKVRAEVEQKLQLLEEKTDEDGKTILNLENSNKSLSGELREVKKDLGQLQENLEVSENMNLQFENQLNKTLRNLSTVMDD
SQ  IHTVLKKDNVKSEDRDEKSKENGSGV
//
ID  Q641G3;
PN  Cell division cycle and apoptosis regulator protein 1;
GN  ccar1;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IX12}.
DR  UNIPROT: Q641G3;
DR  Pfam: PF19257;
DR  Pfam: PF14443;
DR  Pfam: PF19256;
DR  Pfam: PF14444;
DR  Pfam: PF02037;
DR  PROSITE: PS50800;
DE  Function: Transcriptional coactivator for nuclear receptors which may play an important role in regulating cell growth and apoptosis. {ECO:0000250|UniProtKB:Q8IX12}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6P5F9; IntAct: EBI-11606853; Score: 0.35
GO  GO:0048471;
GO  GO:0007049;
GO  GO:0006355;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQFGGQKNPPPWATQFTATAVSQPGPLAVQQSSLLGASPTIYTQQSALAAAGLASPSPANYQLSQTAALQQQAAAAAAA
SQ  AAAALQQQYTQPQQTIYSVQQQLQPPPQAILTQPAVALPTSLALSTPQQAAQITVSYPTPRSNQQQTQPQKQRVFTGVVT
SQ  KLHETFGFVDEDVFFQLTAVKGKSPQAGDRVLVEATYNPNMPFKWNAQRIQTLPNQNPASAQSLIKNPAAVMQPVAQPTA
SQ  YAVQTQPPPQAQTLLQAQISAATLTPLLQTQTSPLLQQPQQKAGLLQTPVRIVSQPQPVRRIEPPSRFSVRNDRGDSILS
SQ  RKDDRNRERERERRRSRDRSPQRKRSRERSPRRERERSPRRPRRVVPRYTVQISKFCLDCPGCDTMELRRRYQNLYIPSD
SQ  FFDAQFTWVDAFPISRPFQLGNYSNFYIMHKEVDPLEKNTAIVDPPDADHTYSAKVMLLASPSLEELYHKSCALAEDPIE
SQ  VREGFQHPARLIKFLVGMKGKDEAMAIGGHWSPSLDGPNPDKDPSVLIRTAVRCCKALTGIELSLCTQWYRFAEIRYHRP
SQ  EETHKGRTVPAHVETVVLFFPDVWHCLPTRSEWENLCHGYKQQLVDKLQGDRKEADGEQEEEDKEDGDAKEISTPTHWSK
SQ  LDPKIMKVNDLRKELESRTLSSKGLKSQLIARLTKQLRIEEQKEEQKELEKCEKEEEEEEERKSEDDKEEEERKRQEELE
SQ  RQRREKRYMLPDEPAIIVHPNWSAKNGKFDCSIMSLSVLLDYRIEDNKEHSFEVSLFAELFNEMLQRDFGVRIYRELLAL
SQ  PEKEEKKDKEKKCKKEDKRERKEDKDDDDEPKPKRRKSSDDKIKLEEKEERKRDDRRKEDYREEDDPDYENQDDYEPIAA
SQ  EEDDGDYDDREDDDDDSSSKDKREDKRDGNRYSKERQSKDKEKDKKQMVTVNRDLLMAFVYFDQSHCGYLLEKDLEEILY
SQ  TLGLHLSRAQVKKLFTKILLKESLLYRKLTDTATEDGSHEETDPLHNDILGNCSLLPSKAVRTGLSTVEDKGGLIVYKGA
SQ  MVDVGSLLQKLEKSEKTRTELEHRLQTLESKTEEDEKTISQLEASNRNLSEELKQTKDDVGHLKDSLKAAEDTRSLYEDQ
SQ  LTNTIKNLSAAMGEIQVVLNKNPSTTEDQKSKENGSS
//
ID  A2IDD5;
PN  Coiled-coil domain-containing protein 78;
GN  CCDC78;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, perinuclear region. Cell membrane, sarcolemma. Sarcoplasmic reticulum. Note=Localizes to centrioles and deuterosome. Found primarily in the perinuclear region as well as along the sarcolemmal membrane and in reticular pattern within the sarcoplasm.
DR  UNIPROT: A2IDD5;
DR  UNIPROT: B4DNY4;
DR  UNIPROT: B4E1U6;
DR  UNIPROT: Q05BY7;
DR  UNIPROT: Q05CA0;
DR  UNIPROT: Q6T2V5;
DR  UNIPROT: Q6ZR33;
DR  UNIPROT: Q8IUR3;
DR  UNIPROT: Q8NAY7;
DR  UNIPROT: Q96S12;
DR  Pfam: PF14739;
DR  OMIM: 614666;
DR  OMIM: 614807;
DR  DisGeNET: 124093;
DE  Function: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome. {ECO:0000269|PubMed:24075808}.
DE  Disease: Myopathy, centronuclear, 4 (CNM4) [MIM:614807]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. {ECO:0000269|PubMed:22818856}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q8D194; IntAct: EBI-2874016; Score: 0.00
DE  Interaction: Q0VD86; IntAct: EBI-24727262; Score: 0.56
DE  Interaction: Q9NQ75; IntAct: EBI-21371981; Score: 0.00
GO  GO:0005814;
GO  GO:0005737;
GO  GO:0098536;
GO  GO:0048471;
GO  GO:0042383;
GO  GO:0016529;
GO  GO:0030030;
GO  GO:0098535;
GO  GO:0003009;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEHAATTGPRPGPPSRRVENVVLRAKDWLPGAPGGTAVWATSLEAEVPPDLALNKEQQLQISKELVDIQITTHHLHEQHE
SQ  AEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQHR
SQ  LGSGLQGEVKWALEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKLK
SQ  DEYVLRLQHCAWQAVEHADGAGQAPATTALRTFLEATLEDIRAAHRSREQQLARAARSYHKRLVDLSRRHEELLVAYRAP
SQ  GNPQAIFDIASLDLEPLPVPLVTDFSHREDQHGGPGALLSSPKKRPGGASQGGTSEPQGLDAASWAQIHQKLRDFSRSTQ
SQ  SWNGSGHSCWSGPRWLKSNFLSYRSTWTSTWAGTSTKS
//
ID  D3Z5T1;
PN  Coiled-coil domain-containing protein 78;
GN  Ccdc78;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250}. Note=Localizes to centrioles and deuterosome. Found primarily in the perinuclear region as well as along the sarcolemmal membrane and in reticular pattern within the sarcoplasm (By similarity). {ECO:0000250}.
DR  UNIPROT: D3Z5T1;
DR  Pfam: PF14739;
DE  Function: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005737;
GO  GO:0098536;
GO  GO:0048471;
GO  GO:0042383;
GO  GO:0016529;
GO  GO:0030030;
GO  GO:0098535;
GO  GO:0003009;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDQRPELLSSMEYVASPDPKPGVPLRVAENVAPGAEDWLPSASGHLAWATSLETEHQTHLELSEEQRLQISKELVDLQIA
SQ  THHLREQHEAEVFELRREILRLESRVLELELHGNGACQGHKVQPMANLGQHQVPPLEPPGGQQKLQEELKWLLEHHRARQ
SQ  QALETQVGVLSQQLQGAREEARTTGQQLASQAMVLASCKGQLRQAEAENTQLQLQLKKMNEEYAVRLQHYARETVENASS
SQ  TNQAALQAFLESTLQDIRAAHRTREQQLAQAARTYRKRLADLNQRQELLLTTCRATFATAINLEPLPMHWATELSHPREN
SQ  EYGRHRTLLLYPEKGSGETSKENKSQPLALDTASWAQIQQRLQDFSQDTQAELERERAQLMVRATMAEQQLSELQEYVDQ
SQ  HLGRYKQEILKLRKLVNIGDPQGVEAVSSPGSGGARL
//
ID  Q2KI22;
PN  G1/S-specific cyclin-D1;
GN  CCND1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P24385}. Cytoplasm {ECO:0000250|UniProtKB:P24385}. Nucleus membrane {ECO:0000250|UniProtKB:P24385}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P24385}.
DR  UNIPROT: Q2KI22;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DE  Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner. {ECO:0000250|UniProtKB:P24385}.
DE  Reference Proteome: Yes;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0017053;
GO  GO:0016538;
GO  GO:0003714;
GO  GO:0051301;
GO  GO:0006974;
GO  GO:0000082;
GO  GO:0044772;
GO  GO:0031571;
GO  GO:0000122;
GO  GO:0045737;
GO  GO:1900087;
GO  GO:0010971;
GO  GO:0001934;
GO  GO:0000079;
GO  GO:0070141;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHQLLCCEMETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEILPSMRKIVATWMLEVCEEQKCEEEVFPL
SQ  AMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPDELLHMELVLVNKLKWNLAAMTPHDF
SQ  IEHFLSKMPVAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVAAAAQGLHLGSANGFLSYHRLTRFLSKVIRCD
SQ  PDCLRACQEQIEALLESSLRQAQQQNLDPKAAEEEEEEEEVDLACTPTDVRDVNI
//
ID  Q64HP0;
PN  G1/S-specific cyclin-D1;
GN  CCND1;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P24385}. Cytoplasm {ECO:0000250|UniProtKB:P24385}. Nucleus membrane {ECO:0000250|UniProtKB:P24385}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P24385}.
DR  UNIPROT: Q64HP0;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DE  Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner. {ECO:0000250|UniProtKB:P24385}.
DE  Reference Proteome: Yes;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0017053;
GO  GO:0016538;
GO  GO:0003714;
GO  GO:0051301;
GO  GO:0006974;
GO  GO:0000082;
GO  GO:0044772;
GO  GO:0031571;
GO  GO:0000122;
GO  GO:0045737;
GO  GO:1900087;
GO  GO:0010971;
GO  GO:0001934;
GO  GO:0000079;
GO  GO:0070141;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEILPSMRKIVATWMLEVCEEQKCEEEVFPL
SQ  AMNYLNRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPDELLQMELLLVNKLKWNLAAMTPHDF
SQ  IEHFLSKMPVAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLHLGSSNSFLSYHRLTRFLSKVIKCD
SQ  ADCLRACQEQIEALLESSLRQAQQQSLDPKAAEEEEEEEEADLACTPTDVRDVNI
//
ID  P24385;
PN  G1/S-specific cyclin-D1;
GN  CCND1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:20399237, ECO:0000269|PubMed:9106657}. Cytoplasm {ECO:0000269|PubMed:9106657}. Nucleus membrane {ECO:0000269|PubMed:9106657}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated to the nucleus through interaction with KIP/CIP family members. {ECO:0000269|PubMed:9106657}.
DR  UNIPROT: P24385;
DR  UNIPROT: Q6LEF0;
DR  PDB: 2W96;
DR  PDB: 2W99;
DR  PDB: 2W9F;
DR  PDB: 2W9Z;
DR  PDB: 5VZU;
DR  PDB: 6P8E;
DR  PDB: 6P8F;
DR  PDB: 6P8G;
DR  PDB: 6P8H;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DR  OMIM: 168461;
DR  OMIM: 254500;
DR  DisGeNET: 595;
DE  Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition (PubMed:1833066, PubMed:1827756, PubMed:8114739, PubMed:8302605, PubMed:19412162, PubMed:33854235). Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase (PubMed:1833066, PubMed:1827756, PubMed:8114739, PubMed:8302605, PubMed:19412162). Hypophosphorylates RB1 in early G(1) phase (PubMed:1833066, PubMed:1827756, PubMed:8114739, PubMed:8302605, PubMed:19412162). Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals (PubMed:1833066, PubMed:1827756, PubMed:8302605, PubMed:19412162). Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity (PubMed:15241418). Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (PubMed:9106657). Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner (PubMed:16569215, PubMed:18417529). {ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:16569215, ECO:0000269|PubMed:1827756, ECO:0000269|PubMed:1833066, ECO:0000269|PubMed:18417529, ECO:0000269|PubMed:19412162, ECO:0000269|PubMed:33854235, ECO:0000269|PubMed:8114739, ECO:0000269|PubMed:8302605, ECO:0000269|PubMed:9106657}.
DE  Disease: Note=A chromosomal aberration involving CCND1 may be a cause of B-lymphocytic malignancy, particularly mantle-cell lymphoma (MCL). Translocation t(11;14)(q13;q32) with immunoglobulin gene regions. Activation of CCND1 may be oncogenic by directly altering progression through the cell cycle. {ECO:0000269|PubMed:1826542, ECO:0000269|PubMed:8204893, ECO:0000269|PubMed:8695815}. Note=A chromosomal aberration involving CCND1 may be a cause of parathyroid adenomas. Translocation t(11;11)(q13;p15) with the parathyroid hormone (PTH) enhancer. {ECO:0000269|PubMed:1826542}. Multiple myeloma (MM) [MIM:254500]: A malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence- Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia. {ECO:0000269|PubMed:8695815}. Note=The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving CCND1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus.
DE  Reference Proteome: Yes;
DE  Interaction: P11802; IntAct: EBI-375341; Score: 0.98
DE  Interaction: O43929; IntAct: EBI-375191; Score: 0.44
DE  Interaction: Q7L590; IntAct: EBI-375236; Score: 0.44
DE  Interaction: P38936; IntAct: EBI-375359; Score: 0.96
DE  Interaction: Q00534; IntAct: EBI-375368; Score: 0.73
DE  Interaction: P46527; IntAct: EBI-519440; Score: 0.86
DE  Interaction: P36873; IntAct: EBI-1207106; Score: 0.00
DE  Interaction: P62140; IntAct: EBI-1207225; Score: 0.00
DE  Interaction: P24941; IntAct: EBI-1245713; Score: 0.74
DE  Interaction: P38398; IntAct: EBI-1381572; Score: 0.46
DE  Interaction: P30285; IntAct: EBI-6988572; Score: 0.40
DE  Interaction: Q9BQA1; IntAct: EBI-2940933; Score: 0.35
DE  Interaction: O60477; IntAct: EBI-3904862; Score: 0.37
DE  Interaction: P06858; IntAct: EBI-3905646; Score: 0.37
DE  Interaction: Q9H9Y6; IntAct: EBI-3912891; Score: 0.37
DE  Interaction: Q15276; IntAct: EBI-3927352; Score: 0.37
DE  Interaction: Q61193; IntAct: EBI-3956268; Score: 0.40
DE  Interaction: P11233; IntAct: EBI-3956368; Score: 0.27
DE  Interaction: Q62796; IntAct: EBI-3958451; Score: 0.40
DE  Interaction: O15211; IntAct: EBI-3970188; Score: 0.44
DE  Interaction: P06400; IntAct: EBI-4479659; Score: 0.73
DE  Interaction: Q96PU4; IntAct: EBI-6051700; Score: 0.60
DE  Interaction: P51668; IntAct: EBI-6051865; Score: 0.44
DE  Interaction: Q29504; IntAct: EBI-6051865; Score: 0.44
DE  Interaction: O95273; IntAct: EBI-7803086; Score: 0.40
DE  Interaction: P11142; IntAct: EBI-6557805; Score: 0.40
DE  Interaction: P49841; IntAct: EBI-6594575; Score: 0.27
DE  Interaction: Q13761; IntAct: EBI-8874899; Score: 0.46
DE  Interaction: Q9BU70; IntAct: EBI-8996209; Score: 0.37
DE  Interaction: Q5T7W7; IntAct: EBI-8996222; Score: 0.37
DE  Interaction: O60729; IntAct: EBI-8996235; Score: 0.37
DE  Interaction: P49336; IntAct: EBI-8996248; Score: 0.37
DE  Interaction: P17936; IntAct: EBI-8996274; Score: 0.37
DE  Interaction: Q00597; IntAct: EBI-8996261; Score: 0.37
DE  Interaction: Q15797; IntAct: EBI-8996300; Score: 0.37
DE  Interaction: Q96LZ3; IntAct: EBI-8996287; Score: 0.37
DE  Interaction: Q9BYX2; IntAct: EBI-8996313; Score: 0.37
DE  Interaction: Q8NHU6; IntAct: EBI-8996326; Score: 0.37
DE  Interaction: Q9Y2H8; IntAct: EBI-8996339; Score: 0.37
DE  Interaction: Q9H6U6; IntAct: EBI-9066887; Score: 0.37
DE  Interaction: P55290; IntAct: EBI-9066900; Score: 0.37
DE  Interaction: P49862; IntAct: EBI-9066913; Score: 0.37
DE  Interaction: Q9UKQ9; IntAct: EBI-9066926; Score: 0.37
DE  Interaction: P42771; IntAct: EBI-9691857; Score: 0.49
DE  Interaction: Q96TE0; IntAct: EBI-10201598; Score: 0.56
DE  Interaction: P20020; IntAct: EBI-11132222; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-11132222; Score: 0.35
DE  Interaction: P43251; IntAct: EBI-11132222; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-11132222; Score: 0.53
DE  Interaction: O60673; IntAct: EBI-11132222; Score: 0.35
DE  Interaction: Q5VK71; IntAct: EBI-11602009; Score: 0.40
DE  Interaction: O43823; IntAct: EBI-11602073; Score: 0.40
DE  Interaction: P49815; IntAct: EBI-11687054; Score: 0.40
DE  Interaction: Q9UJK0; IntAct: EBI-21832810; Score: 0.35
DE  Interaction: Q07283; IntAct: EBI-21832810; Score: 0.35
DE  Interaction: Q00535; IntAct: EBI-21832810; Score: 0.35
DE  Interaction: P49918; IntAct: EBI-21832810; Score: 0.35
DE  Interaction: P42773; IntAct: EBI-21832810; Score: 0.35
DE  Interaction: P10275; IntAct: EBI-15566960; Score: 0.54
DE  Interaction: O15379; IntAct: EBI-15567015; Score: 0.54
DE  Interaction: Q16656; IntAct: EBI-15593340; Score: 0.51
DE  Interaction: Q5XUX0; IntAct: EBI-15777409; Score: 0.58
DE  Interaction: P30260; IntAct: EBI-15851991; Score: 0.50
DE  Interaction: P12830; IntAct: EBI-15852068; Score: 0.40
DE  Interaction: Q02224; IntAct: EBI-16716754; Score: 0.35
DE  Interaction: O95239; IntAct: EBI-16716754; Score: 0.35
DE  Interaction: O94880; IntAct: EBI-16716754; Score: 0.35
DE  Interaction: Q9UH17; IntAct: EBI-25296686; Score: 0.27
DE  Interaction: P59595; IntAct: EBI-25746873; Score: 0.58
DE  Interaction: P12004; IntAct: EBI-26956397; Score: 0.44
GO  GO:0005923;
GO  GO:0097128;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0017053;
GO  GO:0016538;
GO  GO:0019899;
GO  GO:0042826;
GO  GO:0070064;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0003714;
GO  GO:0051301;
GO  GO:0006974;
GO  GO:0030968;
GO  GO:0045444;
GO  GO:0000082;
GO  GO:0007595;
GO  GO:0033327;
GO  GO:0097421;
GO  GO:0060749;
GO  GO:0033598;
GO  GO:0044772;
GO  GO:0031571;
GO  GO:0030857;
GO  GO:0043524;
GO  GO:0000122;
GO  GO:0030182;
GO  GO:0045737;
GO  GO:1900087;
GO  GO:0010971;
GO  GO:0033601;
GO  GO:0001934;
GO  GO:0006468;
GO  GO:0000320;
GO  GO:0000079;
GO  GO:0051592;
GO  GO:0051412;
GO  GO:0032355;
GO  GO:0043627;
GO  GO:0045471;
GO  GO:0010039;
GO  GO:0044321;
GO  GO:0032026;
GO  GO:0010243;
GO  GO:0070141;
GO  GO:0033197;
GO  GO:0010165;
GO  GO:0009410;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPL
SQ  AMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDF
SQ  IEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCD
SQ  PDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI
//
ID  P25322;
PN  G1/S-specific cyclin-D1;
GN  Ccnd1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:19767775}. Cytoplasm {ECO:0000250|UniProtKB:P24385}. Nucleus membrane {ECO:0000250|UniProtKB:P24385}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P24385}.
DR  UNIPROT: P25322;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DE  Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner. {ECO:0000250|UniProtKB:P24385}.
DE  Reference Proteome: Yes;
DE  Interaction: P30285; IntAct: EBI-1005778; Score: 0.94
DE  Interaction: Q64261; IntAct: EBI-1005805; Score: 0.35
DE  Interaction: P46414; IntAct: EBI-1005805; Score: 0.35
DE  Interaction: P97377; IntAct: EBI-1005805; Score: 0.35
DE  Interaction: P63087; IntAct: EBI-1202844; Score: 0.00
DE  Interaction: Q99J09; IntAct: EBI-2939789; Score: 0.35
DE  Interaction: Q8CIG8; IntAct: EBI-2939789; Score: 0.61
DE  Interaction: O14744; IntAct: EBI-2941110; Score: 0.35
DE  Interaction: Q9BQA1; IntAct: EBI-2941649; Score: 0.40
DE  Interaction: P63321; IntAct: EBI-3956288; Score: 0.46
DE  Interaction: P11234; IntAct: EBI-3956307; Score: 0.40
DE  Interaction: Q6KAR6; IntAct: EBI-3956307; Score: 0.46
DE  Interaction: Q9JIW9; IntAct: EBI-3956328; Score: 0.27
DE  Interaction: P11233; IntAct: EBI-3956335; Score: 0.27
DE  Interaction: P09055; IntAct: EBI-3956355; Score: 0.27
DE  Interaction: Q62796; IntAct: EBI-3956408; Score: 0.40
DE  Interaction: Q01101; IntAct: EBI-9253124; Score: 0.35
DE  Interaction: O88895; IntAct: EBI-9253173; Score: 0.40
DE  Interaction: P13405; IntAct: EBI-11508299; Score: 0.40
DE  Interaction: Q9DBR0; IntAct: EBI-11602084; Score: 0.40
DE  Interaction: Q9WU00; IntAct: EBI-15593322; Score: 0.35
DE  Interaction: P11440; IntAct: EBI-15652518; Score: 0.40
GO  GO:0005923;
GO  GO:0097128;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0017053;
GO  GO:0016538;
GO  GO:0019899;
GO  GO:0042826;
GO  GO:0016301;
GO  GO:0070064;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0003714;
GO  GO:0051301;
GO  GO:0008283;
GO  GO:0006974;
GO  GO:0071310;
GO  GO:0030968;
GO  GO:0045444;
GO  GO:0000082;
GO  GO:0007595;
GO  GO:0033327;
GO  GO:0097421;
GO  GO:0060749;
GO  GO:0033598;
GO  GO:0044772;
GO  GO:0031571;
GO  GO:0030857;
GO  GO:0043524;
GO  GO:0000122;
GO  GO:0030182;
GO  GO:0008284;
GO  GO:0045737;
GO  GO:1900087;
GO  GO:0010971;
GO  GO:0033601;
GO  GO:0001934;
GO  GO:0006468;
GO  GO:0000320;
GO  GO:0051726;
GO  GO:0000079;
GO  GO:2000045;
GO  GO:0051592;
GO  GO:0051412;
GO  GO:0032355;
GO  GO:0043627;
GO  GO:0045471;
GO  GO:0010039;
GO  GO:0044321;
GO  GO:0032026;
GO  GO:0010243;
GO  GO:0070141;
GO  GO:0033197;
GO  GO:0010165;
GO  GO:0009410;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEHQLLCCEVETIRRAYPDTNLLNDRVLRAMLKTEETCAPSVSYFKCVQKEIVPSMRKIVATWMLEVCEEQKCEEEVFPL
SQ  AMNYLDRFLSLEPLKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDF
SQ  IEHFLSKMPEADENKQTIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAMQGLNLGSPNNFLSCYRTTHFLSRVIKCD
SQ  PDCLRACQEQIEALLESSLRQAQQNVDPKATEEEGEVEEEAGLACTPTDVRDVDI
//
ID  Q5R6J5;
PN  G1/S-specific cyclin-D1;
GN  CCND1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P24385}. Cytoplasm {ECO:0000250|UniProtKB:P24385}. Nucleus membrane {ECO:0000250|UniProtKB:P24385}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P24385}.
DR  UNIPROT: Q5R6J5;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DE  Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner. {ECO:0000250|UniProtKB:P24385}.
DE  Reference Proteome: Yes;
GO  GO:0005923;
GO  GO:0097128;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0017053;
GO  GO:0016538;
GO  GO:0042826;
GO  GO:0070064;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0003714;
GO  GO:0051301;
GO  GO:0006974;
GO  GO:0030968;
GO  GO:0045444;
GO  GO:0000082;
GO  GO:0007595;
GO  GO:0097421;
GO  GO:0060749;
GO  GO:0033598;
GO  GO:0031571;
GO  GO:0030857;
GO  GO:0043524;
GO  GO:0000122;
GO  GO:0030182;
GO  GO:0045737;
GO  GO:0010971;
GO  GO:0033601;
GO  GO:0001934;
GO  GO:0006468;
GO  GO:0000320;
GO  GO:0044321;
GO  GO:0070141;
GO  GO:0009410;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPL
SQ  AMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAALTPHDF
SQ  IEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNSFLSYYRLTRFLSRVIKCD
SQ  PDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI
//
ID  P39948;
PN  G1/S-specific cyclin-D1;
GN  Ccnd1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P24385}. Cytoplasm {ECO:0000250|UniProtKB:P24385}. Nucleus membrane {ECO:0000250|UniProtKB:P24385}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P24385}.
DR  UNIPROT: P39948;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DE  Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner. {ECO:0000250|UniProtKB:P24385}.
DE  Reference Proteome: Yes;
DE  Interaction: P63322; IntAct: EBI-3956381; Score: 0.27
GO  GO:0005923;
GO  GO:0097128;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0017053;
GO  GO:0016538;
GO  GO:0019899;
GO  GO:0042826;
GO  GO:0016301;
GO  GO:0070064;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0003714;
GO  GO:0031100;
GO  GO:0051301;
GO  GO:0008283;
GO  GO:0006974;
GO  GO:0071310;
GO  GO:0030968;
GO  GO:0045444;
GO  GO:0000082;
GO  GO:0007595;
GO  GO:0033327;
GO  GO:0001889;
GO  GO:0097421;
GO  GO:0060749;
GO  GO:0033598;
GO  GO:0044772;
GO  GO:0031571;
GO  GO:0030857;
GO  GO:0043524;
GO  GO:0000122;
GO  GO:0030182;
GO  GO:0008284;
GO  GO:0045737;
GO  GO:1900087;
GO  GO:0010971;
GO  GO:0033601;
GO  GO:0001934;
GO  GO:0006468;
GO  GO:0000320;
GO  GO:0050790;
GO  GO:0051726;
GO  GO:0000079;
GO  GO:2000045;
GO  GO:0051592;
GO  GO:0051412;
GO  GO:0032355;
GO  GO:0043627;
GO  GO:0045471;
GO  GO:0051384;
GO  GO:0010039;
GO  GO:0044321;
GO  GO:0032026;
GO  GO:0014070;
GO  GO:0010033;
GO  GO:0010243;
GO  GO:0048545;
GO  GO:0070141;
GO  GO:0033197;
GO  GO:0010165;
GO  GO:0009410;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEHQLLCCEVETIRRAYPDTNLLNDRVLRAMLKTEETCAPSVSYFKCVQREIVPSMRKIVATWMLEVCEEQKCEEEVFPL
SQ  AMNYLDRFLSLEPLKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDF
SQ  IEHFLSKMPEADENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAMQGLNLGSPNNFLSCYRTTHFLSRVIKCD
SQ  PDCLRACQEQIEALLESSLRQAQQNIDPKATEEEGEVEEEAGLACTPTDVRDVDI
//
ID  Q0P5D3;
PN  G1/S-specific cyclin-D2;
GN  CCND2;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P30279}. Cytoplasm {ECO:0000250|UniProtKB:P30279}. Nucleus membrane {ECO:0000250|UniProtKB:P30279}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P30279}.
DR  UNIPROT: Q0P5D3;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DE  Function: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. {ECO:0000250|UniProtKB:P30279}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0097129;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016538;
GO  GO:0019901;
GO  GO:0008344;
GO  GO:0051301;
GO  GO:0071481;
GO  GO:0007616;
GO  GO:0044772;
GO  GO:0043066;
GO  GO:0008284;
GO  GO:0045737;
GO  GO:1900087;
GO  GO:0000079;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELLCGEVEPVRRAVPDANLLHDDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLA
SQ  INYLDRFLAGVPTPKTHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFI
SQ  EHILRKLPQPSEKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEDVSSLTGDALVDLLAKITNTDV
SQ  DCLKACQEQIEVVLLNSLQQYRQDQGDGSKSEDELDQASTPTDVRDIDL
//
ID  P49706;
PN  G1/S-specific cyclin-D2;
GN  CCND2;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P30279}. Cytoplasm {ECO:0000250|UniProtKB:P30279}. Nucleus membrane {ECO:0000250|UniProtKB:P30279}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P30279}.
DR  UNIPROT: P49706;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DE  Function: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. {ECO:0000250|UniProtKB:P30279}.
DE  Reference Proteome: Yes;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0016538;
GO  GO:0051301;
GO  GO:0044772;
GO  GO:1900087;
GO  GO:0000079;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELLCCEVDPMRRALPDPNLLYDDRVLHNLLTIEERYLPQCSYFKCVQKDIQPFMRRMVATWMLEVCEEQKCEEEVFPLA
SQ  MNYLDRFLAVVPTRKCHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFI
SQ  EHILRKLPLPKDKLVLIRKHAQTFIALCATDFNFAMYPPSMIATGSVGAAICGLQLDDGDRSLSGDSLTDFLAKITSTDV
SQ  DCLKACQEQIESVLVSNLRQVRQQQQQSNPSKTIEELDQASTPTDVRDINL
//
ID  P30279;
PN  G1/S-specific cyclin-D2;
GN  CCND2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:18827403}. Cytoplasm {ECO:0000269|PubMed:18827403}. Nucleus membrane {ECO:0000269|PubMed:18827403}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000269|PubMed:18827403}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:17873913}.
DR  UNIPROT: P30279;
DR  UNIPROT: A8K531;
DR  UNIPROT: Q13955;
DR  UNIPROT: Q5U035;
DR  PDB: 6EI2;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DR  OMIM: 123833;
DR  OMIM: 615938;
DR  DisGeNET: 894;
DE  Function: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition (PubMed:8114739, PubMed:18827403). Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase (PubMed:8114739, PubMed:18827403). Hypophosphorylates RB1 in early G(1) phase (PubMed:8114739, PubMed:18827403). Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals (PubMed:8114739, PubMed:18827403). {ECO:0000269|PubMed:18827403, ECO:0000269|PubMed:8114739}.
DE  Disease: Megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome 3 (MPPH3) [MIM:615938]: A syndrome characterized by megalencephaly, ventriculomegaly that may lead to hydrocephalus, and polymicrogyria; polydactyly may also be seen. There is considerable phenotypic similarity between this disorder and the megalencephaly- capillary malformation syndrome. {ECO:0000269|PubMed:24705253}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P11802; IntAct: EBI-768365; Score: 0.93
DE  Interaction: P35227; IntAct: EBI-7823662; Score: 0.59
DE  Interaction: P38936; IntAct: EBI-756799; Score: 0.95
DE  Interaction: P46527; IntAct: EBI-758509; Score: 0.77
DE  Interaction: P24941; IntAct: EBI-1245720; Score: 0.55
DE  Interaction: Q00535; IntAct: EBI-6256270; Score: 0.96
DE  Interaction: Q00534; IntAct: EBI-6380828; Score: 0.35
DE  Interaction: Q5VK71; IntAct: EBI-11601998; Score: 0.40
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q08999; IntAct: EBI-21848702; Score: 0.35
DE  Interaction: P49918; IntAct: EBI-21848702; Score: 0.35
DE  Interaction: P07550; IntAct: EBI-20801651; Score: 0.37
GO  GO:0000785;
GO  GO:0097129;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016538;
GO  GO:0019901;
GO  GO:0008344;
GO  GO:0051301;
GO  GO:0071481;
GO  GO:0000082;
GO  GO:0007616;
GO  GO:0044772;
GO  GO:0043066;
GO  GO:0008284;
GO  GO:0045737;
GO  GO:1900087;
GO  GO:0001934;
GO  GO:0000079;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELLCHEVDPVRRAVRDRNLLRDDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLA
SQ  MNYLDRFLAGVPTPKSHLQLLGAVCMFLASKLKETSPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFI
SQ  EHILRKLPQQREKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEEVSSLTCDALTELLAKITNTDV
SQ  DCLKACQEQIEAVLLNSLQQYRQDQRDGSKSEDELDQASTPTDVRDIDL
//
ID  P30280;
PN  G1/S-specific cyclin-D2;
GN  Ccnd2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P30279}. Cytoplasm {ECO:0000250|UniProtKB:P30279}. Nucleus membrane {ECO:0000250|UniProtKB:P30279}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P30279}.
DR  UNIPROT: P30280;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DE  Function: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. {ECO:0000250|UniProtKB:P30279}.
DE  Reference Proteome: Yes;
DE  Interaction: P30285; IntAct: EBI-1005844; Score: 0.53
DE  Interaction: Q01105; IntAct: EBI-1371868; Score: 0.35
DE  Interaction: Q64261; IntAct: EBI-6932163; Score: 0.46
DE  Interaction: P11440; IntAct: EBI-15652535; Score: 0.40
GO  GO:0000785;
GO  GO:0097129;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016538;
GO  GO:0019901;
GO  GO:0008344;
GO  GO:0051301;
GO  GO:0071481;
GO  GO:0000082;
GO  GO:0007616;
GO  GO:0044772;
GO  GO:0043066;
GO  GO:2000726;
GO  GO:0060045;
GO  GO:0008284;
GO  GO:0045737;
GO  GO:0050679;
GO  GO:1900087;
GO  GO:0001934;
GO  GO:0051726;
GO  GO:0000079;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELLCCEVDPVRRAVPDRNLLEDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAM
SQ  NYLDRFLAGVPTPKTHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSVKPQELLEWELVVLGKLKWNLAAVTPHDFIE
SQ  HILRKLPQQKEKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDDEVNTLTCDALTELLAKITHTDVD
SQ  CLKACQEQIEALLLNSLQQFRQEQHNAGSKSVEDPDQATTPTDVRDVDL
//
ID  Q8WNW2;
PN  G1/S-specific cyclin-D2;
GN  CCND2;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P30279}. Cytoplasm {ECO:0000250|UniProtKB:P30279}. Nucleus membrane {ECO:0000250|UniProtKB:P30279}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P30279}.
DR  UNIPROT: Q8WNW2;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DE  Function: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. {ECO:0000250|UniProtKB:P30279}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0097129;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016538;
GO  GO:0019901;
GO  GO:0008344;
GO  GO:0051301;
GO  GO:0071481;
GO  GO:0007616;
GO  GO:0044772;
GO  GO:0043066;
GO  GO:0008284;
GO  GO:0045737;
GO  GO:1900087;
GO  GO:0000079;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELLCCEVDPVRRAVPDANLLHDDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLA
SQ  INYLDRFLAGVPTPKTHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFI
SQ  EHILRKLPQPNEKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEDVSSLTGDALVDLLARITNTDV
SQ  DCLKACQEQIEVVLLNSLQQYRQDQDGSKSEDELDQASTPTDVRDIDL
//
ID  Q04827;
PN  G1/S-specific cyclin-D2;
GN  Ccnd2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P30279}. Cytoplasm {ECO:0000250|UniProtKB:P30279}. Nucleus membrane {ECO:0000250|UniProtKB:P30279}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P30279}.
DR  UNIPROT: Q04827;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DE  Function: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. {ECO:0000250|UniProtKB:P30279}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0097129;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0016538;
GO  GO:0019901;
GO  GO:0008344;
GO  GO:0051301;
GO  GO:0071549;
GO  GO:0071372;
GO  GO:0071378;
GO  GO:0032869;
GO  GO:0071394;
GO  GO:0071481;
GO  GO:0000082;
GO  GO:0001889;
GO  GO:0007616;
GO  GO:0044772;
GO  GO:0043066;
GO  GO:2000726;
GO  GO:0001541;
GO  GO:0060045;
GO  GO:0008284;
GO  GO:0045737;
GO  GO:0050679;
GO  GO:1900087;
GO  GO:0001934;
GO  GO:0051726;
GO  GO:0000079;
GO  GO:0045664;
GO  GO:0051591;
GO  GO:0032355;
GO  GO:0043627;
GO  GO:0045471;
GO  GO:0032354;
GO  GO:0044752;
GO  GO:0014070;
GO  GO:0043434;
GO  GO:0033574;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELLCCEVDPVRRAVPDRNLLEDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAM
SQ  NYLDRFLAGVPTPKTHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSVKPQELLEWELVVLGKLKWNLAAVTPHDFIE
SQ  HILRKLPQQKEKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEEVNALTCDALTELLTKITHTDVD
SQ  CLKACQEQIEAVLLNSLQQFRQEQHNGSKSVEDPDQATTPTDVRDVDL
//
ID  P53782;
PN  G1/S-specific cyclin-D2;
GN  ccnd2;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P30279}. Cytoplasm {ECO:0000250|UniProtKB:P30279}. Nucleus membrane {ECO:0000250|UniProtKB:P30279}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P30279}.
DR  UNIPROT: P53782;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  PROSITE: PS00292;
DE  Function: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. {ECO:0000250|UniProtKB:P30279}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0007049;
GO  GO:0051301;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELLCCEGDTVRRAQPDPALLLDDRVLHNLLTVEERYLPQCSYFKCVQKDIQPFMRRMVATWMLEVCEEQRCEEEVFPMA
SQ  MNYLDRFLAVIPTRKCHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFI
SQ  EHILRKLPLPKDKLLLIRKHAQTFIALCATDFNFAMYPPSMIATGSVGAAICGLQLDVGETSLSGDSLTEHLAKITSTDV
SQ  DCLKACQEQIESVLVSSLRQTRQQTQQRNSSKSVDELDQASTPTDVQDINL
//
ID  A5PK16;
PN  Cyclin-F;
GN  CCNF;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P41002}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41002}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P41002}. Note=Localization in the centrosome is rare in S phase cells and increases in G2 cells, Localizes on both the mother and daughter centrioles. Localization to centrosomes is not dependent on CP110. Localizes to the nucleus in G2 phase. {ECO:0000250|UniProtKB:P41002}.
DR  UNIPROT: A5PK16;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  Pfam: PF00646;
DR  PROSITE: PS00292;
DR  PROSITE: PS50181;
DE  Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). The SCF(CCNF) E3 ubiquitin-protein ligase complex is an integral component of the ubiquitin proteasome system (UPS) and links proteasome degradation to the cell cycle (By similarity). Mediates the substrate recognition and the proteasomal degradation of various target proteins involved in the regulation of cell cycle progression and in the maintenance of genome stability (By similarity). Mediates the ubiquitination and subsequent proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication (By similarity). In G2, mediates the ubiquitination and proteasomal degradation of CDC6, thereby suppressing DNA re-replication and preventing genome instability (By similarity). Involved in the ubiquitination and degradation of the substrate adapter CDH1 of the anaphase-promoting complex (APC/C), thereby acting as an antagonist of APC/C in regulating G1 progression and S phase entry (By similarity). May play a role in the G2 cell cycle checkpoint control after DNA damage, possibly by promoting the ubiquitination of MYBL2/BMYB (By similarity). {ECO:0000250|UniProtKB:P41002}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0010826;
GO  GO:0016567;
GO  GO:0051726;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGSGGVIHCRCAKCFCYPSKRRIRRRPRNLTILNLPEDALFHILKWLSVGDILAVRAVHSHLKYLVDNHASVWACASFQE
SQ  LWPSPGNLKLFERAAEKGNFEAAVKLGIAYLYNEGLSVSDEARAEVNGLRASRYFSLAERLNVGAAPFIWLFIRPPWSVS
SQ  GSCCKAVVHESLRAECQLQKTHRASILHCLGRVLSLFEDEEKQKQARKLFEESANQGCLTSSYLLWESDRRMDMLDPGRC
SQ  LHSFRKLRDFAAKGCWEAQLSLAKACAHGHQLGLEAKASSEIVCQLFQASHAVNKQRVFSVQKGLNDTMRYILIDWLVEV
SQ  ATMKDFSSLCLHLTVECVDRYLRRRLVPRYRLQLLGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRMMGEVVSA
SQ  LDGKIRVPTVVDYKDVLLTLVPMAPRTQHLCSFLCELSLLHTSLAAYAPAHLAAAALLLARLTHGQTQPWTTQLWDLTGF
SQ  SCEDLIPCVLSLHQKCFHDDAPKDYRQVSLTAVKQRFEDKRYEEISLEEVLSYGQLCAALGVKQESLEPAPFLSAGDIHA
SQ  FLSSPSARRTKRKRENSLQEDRGSFVTTPTAELSSQEETLLGSFLDWSLDYCSGYEGDQESEGEKEGDVTAPSGVLDVTV
SQ  VYLSPEEHCCQESSDEEACPEEACGAQDTQALVPGHQALRTPGPEPPLCSRWGLGKDVTTSGYSSVNSASPTDSGRTSGG
SQ  PPRSTSELPTGSSLNTQPCHHHARKSCLQCRPPSPPESCAPQQQVKRKNLSAHSEEEEEDMNLGFLKL
//
ID  Q6NYX6;
PN  Cyclin-F;
GN  ccnf;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P41002}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41002}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P41002}. Note=Localization in the centrosome is rare in S phase cells and increases in G2 cells, Localizes on both the mother and daughter centrioles. Localizes to the nucleus in G2 phase. {ECO:0000250|UniProtKB:P41002}.
DR  UNIPROT: Q6NYX6;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  Pfam: PF12937;
DR  PROSITE: PS00292;
DR  PROSITE: PS50181;
DE  Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). The SCF(CCNF) E3 ubiquitin-protein ligase complex is an integral component of the ubiquitin proteasome system (UPS) and links proteasome degradation to the cell cycle (By similarity). Mediates the substrate recognition and the proteasomal degradation of various target proteins during G2 phase involved in the regulation of cell cycle progression and in the maintenance of genome stability (By similarity). May play a role in motor neuron development and axonal outgrowth (PubMed:28444311). {ECO:0000250|UniProtKB:P41002, ECO:0000269|PubMed:28444311}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0016538;
GO  GO:0051301;
GO  GO:0044772;
GO  GO:0010826;
GO  GO:0016567;
GO  GO:0000079;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKAGALHCRCAKCFSLPVRKRVRKRASAVSLLSLPEELLVFVLQCLSAEDLLSVRAVHSHLCDIIDTNASIWARVSFKDR
SQ  WPAPDTVWLFERAAEKGNFEAAVKLGIAYLYNEGPLLSEEGRADLCGRMASRYLSLSESLRSPQAEPFIWLFIRPPWSVS
SQ  GSCCKAVVFDRLQAECQTSPGRKGTLLYCLARVLQLFDDEEKRDEAELMLKESSRCGSLQSSYLLWAISRASSTADPGRY
SQ  LQCMRTLRDYAARGCWEAQLAFVKSCGSANPLGLEPRACSELVSQFFQTGPSALRYQPHLQGQDITTKRYILVDWLVEVT
SQ  TTKDFSSQVLHVTISCVDRYLHLRSVPKAQLQLLGIACMVICTRFISKEILTIREAVWLTDNTYQYEDLVHMMGEVISVL
SQ  DGKIRTPTVLDYGEVLLSLLPVERRTAHLFSYICELSLLCSPATVPGPARLASAILLLTRALHNYVPVWPVQLEENTGFS
SQ  KQDLVSCALTLYIKCFGQDVPKDYRHVSLTGVKQRFEDDSYQQISKDTVMGFKELCHVLEVPEVEPQVEVSSTSGQITEM
SQ  HTFLSSPTSSSKRRRADSMQAHRGAFVATPTAELSNQEETLLGDFLDWSLDTSCSGYEGDRESEGEKDGEISTMEVQMEL
SQ  PLDCADRQTHCCLLSSDDTSLCEEDEQEPPTGGSKPWTRHLSSSSTSSSSSSCGFCTDRHSSGYSSIQSFPSPTGSSALV
SQ  SPQNPPGVPSQRIRRQVKRKNTAAHSAGEAEQEDDAANLAFLSF
//
ID  P41002;
PN  Cyclin-F;
GN  CCNF;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10716937, ECO:0000269|PubMed:22632967, ECO:0000269|PubMed:26818844, ECO:0000269|PubMed:7813445}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:7813445}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:20596027}. Note=Localization to the centrosome is rare in S phase cells and increases in G2 cells. Localizes to both the mother and daughter centrioles. Localization to centrosomes is not dependent on CP110. Localizes to the nucleus in G2 phase. {ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:26818844}.
DR  UNIPROT: P41002;
DR  UNIPROT: B2R8H3;
DR  UNIPROT: Q96EG9;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  Pfam: PF00646;
DR  PROSITE: PS00292;
DR  PROSITE: PS50181;
DR  OMIM: 600227;
DR  OMIM: 619141;
DR  DisGeNET: 899;
DE  Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:20596027, PubMed:22632967, PubMed:27653696, PubMed:26818844, PubMed:27080313, PubMed:28852778). The SCF(CCNF) E3 ubiquitin-protein ligase complex is an integral component of the ubiquitin proteasome system (UPS) and links proteasome degradation to the cell cycle (PubMed:8706131, PubMed:20596027, PubMed:27653696, PubMed:26818844). Mediates the substrate recognition and the proteasomal degradation of various target proteins involved in the regulation of cell cycle progression and in the maintenance of genome stability (PubMed:20596027, PubMed:22632967, PubMed:27653696, PubMed:26818844). Mediates the ubiquitination and proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication (PubMed:20596027). In G2, mediates the ubiquitination and subsequent degradation of ribonucleotide reductase RRM2, thereby maintaining a balanced pool of dNTPs and genome integrity (PubMed:22632967). In G2, mediates the ubiquitination and proteasomal degradation of CDC6, thereby suppressing DNA re-replication and preventing genome instability (PubMed:26818844). Involved in the ubiquitination and degradation of the substrate adapter CDH1 of the anaphase-promoting complex (APC/C), thereby acting as an antagonist of APC/C in regulating G1 progression and S phase entry (PubMed:27653696). May play a role in the G2 cell cycle checkpoint control after DNA damage, possibly by promoting the ubiquitination of MYBL2/BMYB (PubMed:25557911). {ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:22632967, ECO:0000269|PubMed:25557911, ECO:0000269|PubMed:26818844, ECO:0000269|PubMed:27080313, ECO:0000269|PubMed:27653696, ECO:0000269|PubMed:28852778, ECO:0000269|PubMed:8706131}.
DE  Disease: Frontotemporal dementia and/or amyotrophic lateral sclerosis 5 (FTDALS5) [MIM:619141]: A neurodegenerative disorder characterized by frontotemporal dementia and/or amyotrophic lateral sclerosis in affected individuals. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. FTDALS5 is an autosomal dominant form with age- dependent penetrance. Penetrance is estimated to be 50% by age 56 and 100% by age 61. {ECO:0000269|PubMed:27080313, ECO:0000269|PubMed:28852778}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P52286; IntAct: EBI-907638; Score: 0.40
DE  Interaction: Q8D0D4; IntAct: EBI-2848359; Score: 0.00
DE  Interaction: P63208; IntAct: EBI-15862670; Score: 0.64
DE  Interaction: P31350; IntAct: EBI-6162528; Score: 0.63
DE  Interaction: Q13616; IntAct: EBI-6162332; Score: 0.66
DE  Interaction: O43303; IntAct: EBI-6163027; Score: 0.79
GO  GO:0030054;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0010997;
GO  GO:0016538;
GO  GO:0051301;
GO  GO:0044772;
GO  GO:0010826;
GO  GO:0001890;
GO  GO:0016567;
GO  GO:0000320;
GO  GO:0051726;
GO  GO:0000079;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGSGGVVHCRCAKCFCYPTKRRIRRRPRNLTILSLPEDVLFHILKWLSVEDILAVRAVHSQLKDLVDNHASVWACASFQE
SQ  LWPSPGNLKLFERAAEKGNFEAAVKLGIAYLYNEGLSVSDEARAEVNGLKASRFFSLAERLNVGAAPFIWLFIRPPWSVS
SQ  GSCCKAVVHESLRAECQLQRTHKASILHCLGRVLSLFEDEEKQQQAHDLFEEAAHQGCLTSSYLLWESDRRTDVSDPGRC
SQ  LHSFRKLRDYAAKGCWEAQLSLAKACANANQLGLEVRASSEIVCQLFQASQAVSKQQVFSVQKGLNDTMRYILIDWLVEV
SQ  ATMKDFTSLCLHLTVECVDRYLRRRLVPRYRLQLLGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRMMGEIVSA
SQ  LEGKIRVPTVVDYKEVLLTLVPVELRTQHLCSFLCELSLLHTSLSAYAPARLAAAALLLARLTHGQTQPWTTQLWDLTGF
SQ  SYEDLIPCVLSLHKKCFHDDAPKDYRQVSLTAVKQRFEDKRYGEISQEEVLSYSQLCAALGVTQDSPDPPTFLSTGEIHA
SQ  FLSSPSGRRTKRKRENSLQEDRGSFVTTPTAELSSQEETLLGSFLDWSLDCCSGYEGDQESEGEKEGDVTAPSGILDVTV
SQ  VYLNPEQHCCQESSDEEACPEDKGPQDPQALALDTQIPATPGPKPLVRTSREPGKDVTTSGYSSVSTASPTSSVDGGLGA
SQ  LPQPTSVLSLDSDSHTQPCHHQARKSCLQCRPPSPPESSVPQQQVKRINLCIHSEEEDMNLGLVRL
//
ID  P51944;
PN  Cyclin-F;
GN  Ccnf;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P41002}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41002}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P41002}. Note=Localization in the centrosome is rare in S phase cells and increases in G2 cells, Localizes on both the mother and daughter centrioles. Localization to centrosomes is not dependent on CP110. Localizes to the nucleus in G2 phase. {ECO:0000250|UniProtKB:P41002}.
DR  UNIPROT: P51944;
DR  UNIPROT: Q3TF73;
DR  UNIPROT: Q60797;
DR  UNIPROT: Q60799;
DR  UNIPROT: Q8BSX9;
DR  UNIPROT: Q8C4D9;
DR  UNIPROT: Q8CI26;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  Pfam: PF00646;
DR  PROSITE: PS00292;
DR  PROSITE: PS50181;
DE  Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). The SCF(CCNF) E3 ubiquitin-protein ligase complex is an integral component of the ubiquitin proteasome system (UPS) and links proteasome degradation to the cell cycle (By similarity). Mediates the substrate recognition and the proteasomal degradation of various target proteins involved in the regulation of cell cycle progression and in the maintenance of genome stability (By similarity). Mediates the ubiquitination and subsequent proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication (By similarity). In G2, mediates the ubiquitination and proteasomal degradation of CDC6, thereby suppressing DNA re-replication and preventing genome instability (By similarity). Involved in the ubiquitination and degradation of the substrate adapter CDH1 of the anaphase-promoting complex (APC/C), thereby acting as an antagonist of APC/C in regulating G1 progression and S phase entry (By similarity). May play a role in the G2 cell cycle checkpoint control after DNA damage, possibly by promoting the ubiquitination of MYBL2/BMYB (By similarity). {ECO:0000250|UniProtKB:P41002}.
DE  Reference Proteome: Yes;
GO  GO:0030054;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0010997;
GO  GO:0016538;
GO  GO:0051301;
GO  GO:0044772;
GO  GO:0010826;
GO  GO:0001890;
GO  GO:0016567;
GO  GO:0000320;
GO  GO:0051726;
GO  GO:0000079;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGSGGVIHCRCAKCFCYPTKRRIKRRPRNLTILSLPEDVLFHILKWLSVGDILAVRAVHSHLKYLVDNHASVWASASFQE
SQ  LWPSPQNLKLFERAAEKGNFEAAVKLGIAYLYNEGLSVSDEACAEVNGLKASRFFSMAERLNTGSEPFIWLFIRPPWSVS
SQ  GSCCKAVVHDSLRAECQLQRSHKASILHCLGRVLNLFEDEEKRKQARSLLEESSRQGCLISSYLLWESDRKVDMSDPGRC
SQ  LHSFRKLRDYAAKGCWEAQLALAKACAGGSQLGLEGKACSESVCQLFQASQAVNKQQIFSVQKGLSDTMRYILIDWLVEV
SQ  ATMKDFTSLCLHLTVECVDRYLRRRLVPRYKLQLLGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRVMGEIISA
SQ  LEGKIRIPTVVDYKEVLLTLVPVAPRTQHLCSFLCELTLLHTSLSIYAPARLASAALLLARLMHGQTQPWTTHLWDLTGF
SQ  SYSDLVPCVLSLHKKCFHDDAPKDYRQVSLTAVKQRFEDKCYEEISREEVLSYADLCSTIGVKQESPEPPSFPSSGEIHT
SQ  FLSSPSGRRSKRKRENSLQEDRGSFVTTPTAELSNQEETLLGSLLDWSLECCSGYEGDQESEGEKEGDVTAPSRLLDVTV
SQ  VYLNPEEHCCQESSDEEAWPEDKIHPAPGTQAPPASAPRPLLCNRGDRAKDITTSGYSSVSSSSPISSLDGGMGGSPQST
SQ  SVLSVGSHSSTKPCHHQAKKSCLQCRPPNSPESGVHQQPVKRQNLSVHSDKDMHLAS
//
ID  Q8K4F8;
PN  Cyclin-F;
GN  Ccnf;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P41002}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41002}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P41002}. Note=Localization in the centrosome is rare in S phase cells and increases in G2 cells, Localizes on both the mother and daughter centrioles. Localization to centrosomes is not dependent on CP110. Localizes to the nucleus in G2 phase. {ECO:0000250|UniProtKB:P41002}.
DR  UNIPROT: Q8K4F8;
DR  UNIPROT: D3ZCW7;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  Pfam: PF00646;
DR  PROSITE: PS00292;
DR  PROSITE: PS50181;
DE  Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). The SCF(CCNF) E3 ubiquitin-protein ligase complex is an integral component of the ubiquitin proteasome system (UPS) and links proteasome degradation to the cell cycle (By similarity). Mediates the substrate recognition and the proteasomal degradation of various target proteins involved in the regulation of cell cycle progression and in the maintenance of genome stability (By similarity). Mediates the ubiquitination and subsequent proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication (By similarity). In G2, mediates the ubiquitination and proteasomal degradation of CDC6, thereby suppressing DNA re-replication and preventing genome instability (By similarity). Involved in the ubiquitination and degradation of the substrate adapter CDH1 of the anaphase-promoting complex (APC/C), thereby acting as an antagonist of APC/C in regulating G1 progression and S phase entry (By similarity). May play a role in the G2 cell cycle checkpoint control after DNA damage, possibly by promoting the ubiquitination of MYBL2/BMYB (By similarity). {ECO:0000250|UniProtKB:P41002}.
DE  Reference Proteome: Yes;
GO  GO:0030054;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0010997;
GO  GO:0016538;
GO  GO:0019901;
GO  GO:0051301;
GO  GO:0044772;
GO  GO:0010826;
GO  GO:0001890;
GO  GO:0016567;
GO  GO:0000320;
GO  GO:0051726;
GO  GO:0000079;
GO  GO:0010033;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGSGGVIHCRCAKCFCYPTKRRIKRRPRNLTILSLPEDVLFHILKWLSVGDILAVRAVHSHLKYLVDNHASVWASASFQE
SQ  LWPSPQNLKLFERAAEKGNFEAAVKLGIAYLYNEGLSVSDEACAEVNGLKASRFFSMAERLNTGSDPFIWLFIRPPWSVS
SQ  GSCCKAVVHDSLRAECQLQRSHKASILHCLGRVLNLFEDEEKRKQAHNLFEESAHQGCLASSYLLWESDRKVDMSDPGRC
SQ  LHSFRKLRDYAAKGCWEAQLALAKACAGGSQLGLEGKACSESVCQLFQASQAVNKQQIFSVQKGLSDTMRYILIDWLVEV
SQ  ATMKDFTSLCLHLTVECVDRYLRRRLVPRYKLQLLGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRVMGEIISA
SQ  LEGKIRIPTVVDYKEVLLTLVPVAPRTQHLCSFLCELTLLHTSLSVYAPARLASAALLLARLMHGHTQPWTTQLWDLTGF
SQ  SYSDLTPCVLSLHKKCFHDDAPKDYRQVSLTAVKQRFEDKCYEEISQEEVLSYAELCSALGVKQESPEPPSFPSSGEIHT
SQ  FLSSPSGRRSKRKRENSLQEDRGSFVTTPTAELSNQEETLLGSLLDWSLDCCSGYEGDQESEGEKEGDVTAPSGLLDVTV
SQ  VYLNPEEHCCQESSDEEVWPEDKSHPTPGTQAPPASAPWPLPCNRGDPGKDVTTSGYSSVSSSSPISSLDGGMVGSPRST
SQ  SVLSVGSHSSTKPCYHQAKKSCLQCRPPNPPESGAHQQPVKRQNLSVHSDEDTNLGFLKL
//
ID  Q7T0L6;
PN  Cyclin-F;
GN  ccnf;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P41002}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41002}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P41002}. Note=Localization in the centrosome is rare in S phase cells and increases in G2 cells, Localizes on both the mother and daughter centrioles. Localizes to the nucleus in G2 phase. {ECO:0000250|UniProtKB:P41002}.
DR  UNIPROT: Q7T0L6;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  Pfam: PF00646;
DR  PROSITE: PS00292;
DR  PROSITE: PS50181;
DE  Function: Substrate recognition component of the SCF(CCNF) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). The SCF(CCNF) E3 ubiquitin-protein ligase complex is an integral component of the ubiquitin proteasome system (UPS) and links proteasome degradation to the cell cycle (By similarity). Mediates the substrate recognition and the proteasomal degradation of various target proteins during G2 phase involved in the regulation of cell cycle progression and in the maintenance of genome stability (By similarity). {ECO:0000250|UniProtKB:P41002}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0010826;
GO  GO:0016567;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKGGGLHCRCSKCFAAPPRRRIKRRPRVLTLLSLPEDVLLYVLECLPAVDILSMREVHPHLRSLVDSHSSVWARASFQDV
SQ  WPSSENLNLFERAAECGNFEACVKLGIAYLYNEGLSVSDDGRAEVNGLKASRFFSLTERLNAGADPFVWLFIRPPWSSSG
SQ  SCCKAVVFDSLNEECGTVTSGEGATGALKGSIQYCLAKVLSLFEDDDKKREALGMLESSASNGCLHSAYLLWETKQKAAL
SQ  SDPGRYLQSFRQLRDYAARGCWDAQISLAKACGHKNPLNQEQRSAGELVNQVFQSSLPINKSSIFTTQKGMNDTMRYILI
SQ  DWLVEVATMKDFSSLCLHMTVGLVDRYLKLRSVPRAKLQLVGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRMM
SQ  GEIISALEGKIRMPTVVDYKDVLSHLIPLDRNTLHLCSYISELSLLYTELSMYSPAQLAAGALLLARILHRQARPWPAQL
SQ  AETTGFTLEHLTPCVVLLHKKCFHDDAPRDYRQVSLTAVKQRFQDDLYDQISKEKVMDHTHLCELLGVPCHDSESPATCP
SQ  NAADFHQFLCSPSGNKTKRRREESIQEDRGSFVTTPTAELSNQEEDLLGDFLDWSLETSCSGYEGDRESEGEREGEVTAP
SQ  SGVLDLSLLLTEHPQCQDSTTDDDSITLHPIPLLSKAENGTDSIEGCVEKSSGYSSVSSGGSPTSSSSPGLPFTPTPGLN
SQ  HSKLTPIPFPQPCSPLLKASRRQVKRKNQAQHSEDNLSDEL
//
ID  Q5XGG5;
PN  Cyclin-F;
GN  ccnf;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P41002}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41002}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P41002}. Note=Localization in the centrosome is rare in S phase cells and increases in G2 cells, Localizes on both the mother and daughter centrioles. Localizes to the nucleus in G2 phase. {ECO:0000250|UniProtKB:P41002}.
DR  UNIPROT: Q5XGG5;
DR  Pfam: PF02984;
DR  Pfam: PF00134;
DR  Pfam: PF00646;
DR  PROSITE: PS00292;
DR  PROSITE: PS50181;
DE  Function: Substrate recognition component of the SCF(CCNF) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). The SCF(CCNF) E3 ubiquitin-protein ligase complex is an integral component of the ubiquitin proteasome system (UPS) and links proteasome degradation to the cell cycle (By similarity). Mediates the substrate recognition and the proteasomal degradation of various target proteins during G2 phase involved in the regulation of cell cycle progression and in the maintenance of genome stability (By similarity). {ECO:0000250|UniProtKB:P41002}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0016538;
GO  GO:0051301;
GO  GO:0044772;
GO  GO:0010826;
GO  GO:0016567;
GO  GO:0000079;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKGGALHCRCSKCFAAPPKRRVKRRPRVLTLLSLPEDVLLYVLECLPAVDILSMREVHPHLRSLVDSHSSVWARASFQDV
SQ  WPSPENLNLFERAAECGNFEACVKLGIAYLYNEGLSLSDDGRAEVNGLKASRFFSLTERLNSGADPFVWLFIRPPWSSSG
SQ  SCCKAVVFDSLKEECGTVTSEEGATGALKGSIQYCLAKVLSLFEDDDKKREALGMLESSASHGCLHSSYLLWETKQKTAL
SQ  SDPGRYLQSFRQLRDYAARGCWDAQISLAKACGHKNQLSQEQRSASELVNQVFQSSLPINKTSIFTTQKGMNDTMRYILI
SQ  DWLVEVATMKDFSSLCLHMTVGLVDRYLKLRSVPRAKLQLVGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRMM
SQ  GEIISALEGKIRMPTVVDYKDVLSHLIPLDRSTLHLCSYISELSLLYTELSTYSPAQLAAGALLLARILHKQARPWPAQL
SQ  AETTGFTLEHLTPCVVLLHKKCFHDDAPKDYRQVSLTAVKQRFQDDLYDQISKEKVMDHSHLCELLGVPCRDSESPASCP
SQ  NAADFHQFLCSPSGSKTKRRREDSIQEDRGSFVTTPTAELSNQEEDLLGDFLDWSLETSCSGYEGDRESEGEREGEVTAP
SQ  SGVLDLSLLITEHQQCQDTTSDDDSLVPLHPIPLLSKLENGTHSTEGCAEKSSGYSSVSSGGSPTSSSSPPGLPFTPTPG
SQ  LNHSKLMPIPFPQPCSPLFKASRRQVKRKNQAQHSEDNLSDEL
//
ID  Q14094;
PN  Cyclin-I;
GN  CCNI;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:28860486}.
DR  UNIPROT: Q14094;
DR  UNIPROT: B2R6M0;
DR  UNIPROT: B7Z6X4;
DR  Pfam: PF00134;
DR  OMIM: 618783;
DR  DisGeNET: 10983;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P05783; IntAct: EBI-3915486; Score: 0.37
DE  Interaction: Q96MT8; IntAct: EBI-1105510; Score: 0.00
DE  Interaction: P40127; IntAct: EBI-2873918; Score: 0.00
DE  Interaction: P30304; IntAct: EBI-3907148; Score: 0.37
DE  Interaction: Q9NPH3; IntAct: EBI-3915476; Score: 0.37
DE  Interaction: P31749; IntAct: EBI-9063688; Score: 0.37
DE  Interaction: Q00535; IntAct: EBI-10103156; Score: 0.67
DE  Interaction: Q00536; IntAct: EBI-11615332; Score: 0.37
DE  Interaction: Q00534; IntAct: EBI-24620488; Score: 0.56
DE  Interaction: Q00526; IntAct: EBI-23812995; Score: 0.56
DE  Interaction: Q96E35; IntAct: EBI-24558458; Score: 0.56
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0016538;
GO  GO:0044772;
GO  GO:0000079;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKFPGPLENQRLSFLLEKAITREAQMWKVNVRKMPSNQNVSPSQRDEVIQWLAKLKYQFNLYPETFALASSLLDRFLATV
SQ  KAHPKYLSCIAISCFFLAAKTVEEDERIPVLKVLARDSFCGCSSSEILRMERIILDKLNWDLHTATPLDFLHIFHAIAVS
SQ  TRPQLLFSLPKLSPSQHLAVLTKQLLHCMACNQLLQFRGSMLALAMVSLEMEKLIPDWLSLTIELLQKAQMDSSQLIHCR
SQ  ELVAHHLSTLQSSLPLNSVYVYRPLKHTLVTCDKGVFRLHPSSVPGPDFSKDNSKPEVPVRGTAAFYHHLPAASGCKQTS
SQ  TKRKVEEMEVDDFYDGIKRLYNEDNVSENVGSVCGTDLSRQEGHASPCPPLQPVSVM
//
ID  O60583;
PN  Cyclin-T2;
GN  CCNT2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TQK0}. Nucleus {ECO:0000250|UniProtKB:Q7TQK0}. Note=Nucleus in differentiating cells. {ECO:0000250|UniProtKB:Q7TQK0}.
DR  UNIPROT: O60583;
DR  UNIPROT: A8KA48;
DR  UNIPROT: D3DP73;
DR  UNIPROT: D3DP74;
DR  UNIPROT: O60582;
DR  UNIPROT: Q29R66;
DR  UNIPROT: Q53SR4;
DR  UNIPROT: Q5I1Y0;
DR  PDB: 2IVX;
DR  Pfam: PF00134;
DR  OMIM: 603862;
DR  DisGeNET: 905;
DE  Function: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy- terminal domain) of the large subunit of RNA polymerase II (RNAP II) (PubMed:9499409, PubMed:15563843). The activity of this complex is regulated by binding with 7SK snRNA (PubMed:11713533). Plays a role during muscle differentiation; P-TEFB complex interacts with MYOD1; this tripartite complex promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation and binds the chromatin of promoters and enhancers of muscle-specific genes; this event correlates with hyperphosphorylation of the CTD domain of RNA pol II (By similarity). In addition, enhances MYOD1-dependent transcription through interaction with PKN1 (PubMed:16331689). Involved in early embryo development (By similarity). {ECO:0000250|UniProtKB:Q7TQK0, ECO:0000269|PubMed:11713533, ECO:0000269|PubMed:15563843, ECO:0000269|PubMed:16331689, ECO:0000269|PubMed:9499409}. (Microbial infection) Promotes transcriptional activation of early and late herpes simplex virus 1/HHV-1 promoters. {ECO:0000269|PubMed:21509660}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A3Q0PRD7; IntAct: EBI-2836754; Score: 0.00
DE  Interaction: O95402; IntAct: EBI-4324040; Score: 0.35
DE  Interaction: Q9UHB7; IntAct: EBI-4324092; Score: 0.35
DE  Interaction: O00472; IntAct: EBI-4324079; Score: 0.35
DE  Interaction: P42568; IntAct: EBI-4324106; Score: 0.35
DE  Interaction: P50750; IntAct: EBI-4324121; Score: 0.85
DE  Interaction: O60885; IntAct: EBI-9077135; Score: 0.35
DE  Interaction: Q6NYC1; IntAct: EBI-9077105; Score: 0.40
DE  Interaction: Q16659; IntAct: EBI-12502733; Score: 0.35
DE  Interaction: A3KMF4; IntAct: EBI-11085933; Score: 0.35
DE  Interaction: Q9ERL0; IntAct: EBI-11086053; Score: 0.35
DE  Interaction: Q9HB65; IntAct: EBI-21631556; Score: 0.35
DE  Interaction: Q9P0M6; IntAct: EBI-21731516; Score: 0.35
DE  Interaction: Q96MH2; IntAct: EBI-21764590; Score: 0.35
DE  Interaction: O94992; IntAct: EBI-21776048; Score: 0.35
DE  Interaction: Q00534; IntAct: EBI-21776141; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q12802; IntAct: EBI-25409729; Score: 0.35
DE  Interaction: Q07139; IntAct: EBI-25410964; Score: 0.35
DE  Interaction: P83105; IntAct: EBI-25745135; Score: 0.35
DE  Interaction: O60583; IntAct: EBI-25684887; Score: 0.35
DE  Interaction: A0A0F6B063; IntAct: EBI-27033283; Score: 0.35
DE  Interaction: D0ZRB2; IntAct: EBI-27033344; Score: 0.35
GO  GO:0008024;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0097322;
GO  GO:0003682;
GO  GO:0061575;
GO  GO:0016538;
GO  GO:0019901;
GO  GO:0070063;
GO  GO:0001223;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0019085;
GO  GO:0019086;
GO  GO:0032786;
GO  GO:0045944;
GO  GO:0032968;
GO  GO:0006468;
GO  GO:0000079;
GO  GO:0051147;
GO  GO:0006357;
GO  GO:0007519;
GO  GO:0006366;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASGRGASSRWFFTREQLENTPSRRCGVEADKELSCRQQAANLIQEMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNKN
SQ  IISSTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVILETIMLQTLGFEITIEHPHTDVVKCT
SQ  QLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEF
SQ  LQILEKTPNRLKKIRNWRANQAARKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNI
SQ  SVQDSHTSDNLSMLATGMPSTSYGLSSHQEWPQHQDSARTEQLYSQKQETSLSGSQYNINFQQGPSISLHSGLHHRPDKI
SQ  SDHSSVKQEYTHKAGSSKHHGPISTTPGIIPQKMSLDKYREKRKLETLDLDVRDHYIAAQVEQQHKQGQSQAASSSSVTS
SQ  PIKMKIPIANTEKYMADKKEKSGSLKLRIPIPPTDKSASKEELKMKIKVSSSERHSSSDEGSGKSKHSSPHISRDHKEKH
SQ  KEHPSSRHHTSSHKHSHSHSGSSSGGSKHSADGIPPTVLRSPVGLSSDGISSSSSSSRKRLHVNDASHNHHSKMSKSSKS
SQ  SGSSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVETNGPDANHEYSTSSQHMDYKDTFDMLD
SQ  SLLSAQGMNM
//
ID  Q7TQK0;
PN  Cyclin-T2;
GN  Ccnt2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:23060074}. Nucleus {ECO:0000269|PubMed:23060074}. Note=Nucleus in differentiating cells. {ECO:0000269|PubMed:23060074}.
DR  UNIPROT: Q7TQK0;
DR  UNIPROT: K4N0L9;
DR  UNIPROT: K4N2S3;
DR  Pfam: PF00134;
DE  Function: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy- terminal domain) of the large subunit of RNA polymerase II (RNAP II). The activity of this complex is regulated by binding with 7SK snRNA (By similarity). Plays a role during muscle differentiation; P-TEFB complex interacts with MYOD1; this tripartite complex promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation and binds the chromatin of promoters and enhancers of muscle-specific genes; this event correlates with hyperphosphorylation of the CTD domain of RNA pol II (PubMed:16245309, PubMed:23060074, PubMed:12037670). In addition, enhances MYOD1-dependent transcription through interaction with PKN1 (By similarity). Involved in early embryo development (PubMed:19364821). {ECO:0000250|UniProtKB:O60583, ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:16245309, ECO:0000269|PubMed:19364821, ECO:0000269|PubMed:23060074}.
DE  Reference Proteome: Yes;
DE  Interaction: Q99J95; IntAct: EBI-6260872; Score: 0.35
GO  GO:0008024;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0097322;
GO  GO:0003682;
GO  GO:0061575;
GO  GO:0016538;
GO  GO:0019901;
GO  GO:0070063;
GO  GO:0001223;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0006351;
GO  GO:0019085;
GO  GO:0019086;
GO  GO:1903655;
GO  GO:1903654;
GO  GO:0032786;
GO  GO:0045944;
GO  GO:0032968;
GO  GO:0006468;
GO  GO:0051147;
GO  GO:0006357;
GO  GO:0007519;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASGRGASSRWFFTREQLENTPSRRCGVEADEELSHRQQAANLIQDMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNRN
SQ  IISPTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVLLETIMLQTLGFEITIEHPHTDVVKCT
SQ  QLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEF
SQ  LQILEKTPSRLKRIRNWRAMAKKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPANPSFQKPSTSTFPAPIPLNSGSTSV
SQ  QDSRASDNLSVLAAGMPSTSYSLSSHQEWPQHPDSARTDPVYTQKQEATLSGSQYISFQQGPSMALHSGLHHRPDKVADH
SQ  SSAKQEYTHKAGSSKHHGPIPATPGMLPQKMSLDKYREKRKLETLDVDTRDHYLAAHAEQQHKHGPAQAVTGTSVTSPIK
SQ  MKLPLTNSDRPEKHVAEKKERSGSLKLRIPIPPPDKGPSKEELKMKIKVASSERHSSSDEGSGKSKHSSPHISRDHKEKH
SQ  KEHPANRHHSSHKYLHMHSGGSKHTADGMPPTVLRSPVGLGPEGVSSASSARKKLHSSEASHNHHSKMSKSSKSAGSSSS
SQ  SSSVKQYLSSHSSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVEPHGPEANHEYSTSSQHMDYKDTFDMLDSLLSAQG
SQ  MNM
//
ID  P46892;
PN  Cyclin-dependent kinase 11B;
GN  Cdk11b;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Cytoplasm, perinuclear region.
DR  UNIPROT: P46892;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Plays multiple roles in cell cycle progression, cytokinesis and apoptosis. Involved in pre-mRNA splicing in a kinase activity- dependent manner. May act as a negative regulator of normal cell cycle progression. {ECO:0000250|UniProtKB:P21127}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004693;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0001824;
GO  GO:0007049;
GO  GO:2001234;
GO  GO:0006468;
GO  GO:0001558;
GO  GO:0007346;
GO  GO:0007088;
GO  GO:0050684;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MKSEKSRTTSWLFQSHEVTEILGRVKKNRKKLVKGLHRAGPPPEKNYLPDSPALSPIELKQELPKYLPALQGCRSVEEFQ
SQ  CLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPLTSIREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYV
SQ  EHDLKSLMETMKQPFLPGEVKTLMIQLLSGVKHLHDNWILHRDLKTSNLLLTHAGILKVGDFGLAREYGSPLKAYTPVVV
SQ  TLWYRAPELLLGAKEYSTACDMWSVGCIFGELLTQKPLFPGKSDIDQINKIFKDIGTPSEKIWPGYSELPAVKKMTFSEL
SQ  PYNNLRKRFGALLSDQGFDLMNKFLTYYPGRRINAEDGLKHEYFRETPLPIDPSMFPTWPAKSEQQCVKRGTSPKPPEGG
SQ  LGYSQLGDDDLKETGFHLTTTNDGAVSCRPWCSLLF
//
ID  Q28199;
PN  Cyclin-dependent kinase 5 activator 1, p25;
GN  CDK5R1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: [Cyclin-dependent kinase 5 activator 1, p35]: Cell membrane {ECO:0000250|UniProtKB:Q15078}; Lipid-anchor {ECO:0000250|UniProtKB:Q15078}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15078}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q15078}. Note=In the primary cortical neurons, p35 is present in the peripheries and nerve terminals. {ECO:0000250|UniProtKB:Q15078}. [Cyclin-dependent kinase 5 activator 1, p25]: Nucleus {ECO:0000250|UniProtKB:Q15078}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15078}. Perikaryon {ECO:0000250|UniProtKB:Q15078}. Note=The conversion of p35 to p25 relocalizes the protein from the cell periphery to the cytoplasm, in nuclear and perinuclear regions. In the primary cortical neurons, p25 is primarily concentrated in the cell soma and is largely absent from neurites. {ECO:0000250|UniProtKB:Q15078}.
DR  UNIPROT: Q28199;
DR  UNIPROT: Q0II69;
DR  UNIPROT: Q28865;
DR  UNIPROT: Q29462;
DR  Pfam: PF03261;
DE  Function: p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000250|UniProtKB:Q15078}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9JLH6; IntAct: EBI-307828; Score: 0.48
DE  Interaction: Q9JLH5; IntAct: EBI-307840; Score: 0.48
DE  Interaction: Q9JLH7; IntAct: EBI-307855; Score: 0.48
DE  Interaction: P15882; IntAct: EBI-7146023; Score: 0.54
GO  GO:0030424;
GO  GO:0043292;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0030426;
GO  GO:0016020;
GO  GO:0031594;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0016533;
GO  GO:0051015;
GO  GO:0043014;
GO  GO:0048487;
GO  GO:0045296;
GO  GO:0005509;
GO  GO:0061575;
GO  GO:0035255;
GO  GO:0016301;
GO  GO:0002020;
GO  GO:0019901;
GO  GO:0043539;
GO  GO:0007411;
GO  GO:0007413;
GO  GO:0007420;
GO  GO:0021549;
GO  GO:0009792;
GO  GO:0048013;
GO  GO:0007213;
GO  GO:0070315;
GO  GO:0021766;
GO  GO:0035235;
GO  GO:0021819;
GO  GO:0045892;
GO  GO:0007158;
GO  GO:0030182;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0018107;
GO  GO:0031116;
GO  GO:0043525;
GO  GO:0090314;
GO  GO:0032956;
GO  GO:0061001;
GO  GO:0048511;
GO  GO:0042501;
GO  GO:0021722;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKVQPNSSYQNNITH
SQ  LNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGVSSSVKKAPHPAVSSAGTPKRVIVQASTSELLRCLGEFLC
SQ  RRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNE
SQ  ISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR
//
ID  Q15078;
PN  Cyclin-dependent kinase 5 activator 1, p25;
GN  CDK5R1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Cyclin-dependent kinase 5 activator 1, p35]: Cell membrane {ECO:0000305|PubMed:17671990}; Lipid-anchor {ECO:0000269|PubMed:18507738}; Cytoplasmic side {ECO:0000305}. Cell projection, neuron projection {ECO:0000269|PubMed:10604467}. Note=In the primary cortical neurons, p35 is present in the peripheries and nerve terminals. {ECO:0000269|PubMed:10604467}. [Cyclin-dependent kinase 5 activator 1, p25]: Nucleus {ECO:0000269|PubMed:18507738}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10604467}. Perikaryon {ECO:0000269|PubMed:10604467}. Note=The conversion of p35 to p25 relocalizes the protein from the cell periphery to the cytoplasm, in nuclear and perinuclear regions (PubMed:18507738). In the primary cortical neurons, p25 is primarily concentrated in the cell soma and is largely absent from neurites (PubMed:18507738). {ECO:0000269|PubMed:18507738}.
DR  UNIPROT: Q15078;
DR  UNIPROT: E1P664;
DR  UNIPROT: Q5U0G3;
DR  PDB: 1H4L;
DR  PDB: 1UNG;
DR  PDB: 1UNH;
DR  PDB: 1UNL;
DR  PDB: 3O0G;
DR  PDB: 6LDP;
DR  PDB: 7CNG;
DR  PDB: 7VDP;
DR  PDB: 7VDQ;
DR  PDB: 7VDR;
DR  PDB: 7VDS;
DR  Pfam: PF03261;
DR  OMIM: 603460;
DR  DisGeNET: 8851;
DE  Function: p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000269|PubMed:24235147}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y3Q8; IntAct: EBI-754939; Score: 0.37
DE  Interaction: Q00535; IntAct: EBI-1041602; Score: 0.93
DE  Interaction: P46527; IntAct: EBI-1226546; Score: 0.40
DE  Interaction: P38936; IntAct: EBI-1226667; Score: 0.40
DE  Interaction: Q6ZMQ8; IntAct: EBI-2008413; Score: 0.59
DE  Interaction: Q9HAV2; IntAct: EBI-9370611; Score: 0.40
DE  Interaction: Q53FC7; IntAct: EBI-9370589; Score: 0.40
DE  Interaction: Q96BE0; IntAct: EBI-9370633; Score: 0.40
DE  Interaction: Q01097; IntAct: EBI-9634890; Score: 0.35
DE  Interaction: P11798; IntAct: EBI-9634890; Score: 0.35
DE  Interaction: P49615; IntAct: EBI-9634890; Score: 0.35
DE  Interaction: O35350; IntAct: EBI-9634890; Score: 0.35
DE  Interaction: Q5JR59; IntAct: EBI-10235827; Score: 0.56
DE  Interaction: O89053; IntAct: EBI-11600074; Score: 0.44
DE  Interaction: Q96EY8; IntAct: EBI-21756327; Score: 0.35
DE  Interaction: Q9NPD8; IntAct: EBI-21756327; Score: 0.35
DE  Interaction: Q96EY5; IntAct: EBI-21756327; Score: 0.35
DE  Interaction: Q96DX4; IntAct: EBI-21756327; Score: 0.35
DE  Interaction: Q04323; IntAct: EBI-21756327; Score: 0.35
DE  Interaction: Q01581; IntAct: EBI-21756327; Score: 0.35
DE  Interaction: P24941; IntAct: EBI-21756327; Score: 0.35
DE  Interaction: P07951; IntAct: EBI-21756327; Score: 0.35
DE  Interaction: O94903; IntAct: EBI-21756327; Score: 0.35
DE  Interaction: O43583; IntAct: EBI-21756327; Score: 0.35
DE  Interaction: Q7Z3S9; IntAct: EBI-22139521; Score: 0.37
DE  Interaction: A2RUH7; IntAct: EBI-25906782; Score: 0.56
DE  Interaction: Q8NCR3; IntAct: EBI-25906774; Score: 0.56
DE  Interaction: Q96E17; IntAct: EBI-25906766; Score: 0.56
DE  Interaction: Q96QH2; IntAct: EBI-25906758; Score: 0.56
DE  Interaction: Q9BT49; IntAct: EBI-25906750; Score: 0.56
DE  Interaction: Q6UXH1; IntAct: EBI-25906742; Score: 0.56
DE  Interaction: Q9NPC7; IntAct: EBI-25906734; Score: 0.56
DE  Interaction: Q8N2W9; IntAct: EBI-25906724; Score: 0.56
DE  Interaction: Q9BQ29; IntAct: EBI-25906716; Score: 0.56
DE  Interaction: O94983; IntAct: EBI-25906706; Score: 0.56
DE  Interaction: Q9ULW0; IntAct: EBI-25906698; Score: 0.56
DE  Interaction: Q9HC98; IntAct: EBI-25906688; Score: 0.56
DE  Interaction: Q02978; IntAct: EBI-25906680; Score: 0.56
DE  Interaction: P43356; IntAct: EBI-25906672; Score: 0.56
DE  Interaction: P16422; IntAct: EBI-25906664; Score: 0.56
DE  Interaction: P26715; IntAct: EBI-25906656; Score: 0.56
DE  Interaction: P49184; IntAct: EBI-25906648; Score: 0.56
GO  GO:0030424;
GO  GO:0043292;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0030426;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031594;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098793;
GO  GO:0016533;
GO  GO:0051015;
GO  GO:0043014;
GO  GO:0048487;
GO  GO:0045296;
GO  GO:0005509;
GO  GO:0061575;
GO  GO:0046875;
GO  GO:0035255;
GO  GO:0016301;
GO  GO:0002020;
GO  GO:0030295;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0043539;
GO  GO:0007411;
GO  GO:0007413;
GO  GO:0007420;
GO  GO:0021549;
GO  GO:0009792;
GO  GO:0048013;
GO  GO:0007213;
GO  GO:0070315;
GO  GO:0021766;
GO  GO:0035235;
GO  GO:0021819;
GO  GO:0000226;
GO  GO:0045892;
GO  GO:0007158;
GO  GO:0030182;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0045348;
GO  GO:0031116;
GO  GO:0043525;
GO  GO:0090314;
GO  GO:2000273;
GO  GO:0032956;
GO  GO:0000079;
GO  GO:0061001;
GO  GO:0016241;
GO  GO:0045664;
GO  GO:0098693;
GO  GO:0048511;
GO  GO:0042501;
GO  GO:0021722;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:20213681};
SQ  MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKVQPNSSYQNNITH
SQ  LNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGGSSSVKKAPHPAVTSAGTPKRVIVQASTSELLRCLGEFLC
SQ  RRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNE
SQ  ISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR
//
ID  P61809;
PN  Cyclin-dependent kinase 5 activator 1, p25;
GN  Cdk5r1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: [Cyclin-dependent kinase 5 activator 1, p35]: Cell membrane {ECO:0000250|UniProtKB:Q15078}; Lipid-anchor {ECO:0000250|UniProtKB:Q15078}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15078}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q15078}. Note=In the primary cortical neurons, p35 is present in the peripheries and nerve terminals. {ECO:0000250|UniProtKB:Q15078}. [Cyclin-dependent kinase 5 activator 1, p25]: Nucleus {ECO:0000250|UniProtKB:Q15078}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15078}. Perikaryon {ECO:0000250|UniProtKB:Q15078}. Note=The conversion of p35 to p25 relocalizes the protein from the cell periphery to the cytoplasm, in nuclear and perinuclear regions. In the primary cortical neurons, p25 is primarily concentrated in the cell soma and is largely absent from neurites. {ECO:0000250|UniProtKB:Q15078}.
DR  UNIPROT: P61809;
DR  UNIPROT: Q62938;
DR  Pfam: PF03261;
DE  Function: p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:24235147}.
DE  Reference Proteome: Yes;
DE  Interaction: P15209; IntAct: EBI-15624695; Score: 0.35
DE  Interaction: P09803; IntAct: EBI-7840493; Score: 0.40
DE  Interaction: P49615; IntAct: EBI-7840587; Score: 0.56
DE  Interaction: Q8CFH6; IntAct: EBI-16094166; Score: 0.54
DE  Interaction: O43164; IntAct: EBI-16094147; Score: 0.40
DE  Interaction: P62991; IntAct: EBI-16094258; Score: 0.40
DE  Interaction: Q80U04; IntAct: EBI-16094239; Score: 0.52
GO  GO:0030424;
GO  GO:0043292;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0030426;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031594;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098793;
GO  GO:0016533;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0045296;
GO  GO:0005509;
GO  GO:0061575;
GO  GO:0008092;
GO  GO:0046875;
GO  GO:0051879;
GO  GO:0035255;
GO  GO:0016301;
GO  GO:0002020;
GO  GO:0019901;
GO  GO:0043539;
GO  GO:0007411;
GO  GO:0007413;
GO  GO:0007420;
GO  GO:0021549;
GO  GO:0021799;
GO  GO:0009792;
GO  GO:0048013;
GO  GO:0007213;
GO  GO:0070315;
GO  GO:0021766;
GO  GO:0035235;
GO  GO:0021819;
GO  GO:0045892;
GO  GO:0007158;
GO  GO:0030182;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0045348;
GO  GO:0043525;
GO  GO:0045860;
GO  GO:0090314;
GO  GO:2000273;
GO  GO:0032956;
GO  GO:0061001;
GO  GO:0070507;
GO  GO:0098693;
GO  GO:0048511;
GO  GO:0042501;
GO  GO:0021722;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKAQPNSSYQSNIAH
SQ  LNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGVSSSVKKAPHPAITSAGTPKRVIVQASTSELLRCLGEFLC
SQ  RRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNE
SQ  ISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR
//
ID  P61810;
PN  Cyclin-dependent kinase 5 activator 1, p25;
GN  Cdk5r1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: [Cyclin-dependent kinase 5 activator 1, p35]: Cell membrane {ECO:0000250|UniProtKB:Q15078}; Lipid-anchor {ECO:0000250|UniProtKB:Q15078}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15078}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q15078}. Note=In the primary cortical neurons, p35 is present in the peripheries and nerve terminals. {ECO:0000250|UniProtKB:Q15078}. [Cyclin-dependent kinase 5 activator 1, p25]: Nucleus {ECO:0000250|UniProtKB:Q15078}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15078}. Perikaryon {ECO:0000250|UniProtKB:Q15078}. Note=The conversion of p35 to p25 relocalizes the protein from the cell periphery to the cytoplasm, in nuclear and perinuclear regions. In the primary cortical neurons, p25 is primarily concentrated in the cell soma and is largely absent from neurites. {ECO:0000250|UniProtKB:Q15078}.
DR  UNIPROT: P61810;
DR  UNIPROT: Q62938;
DR  Pfam: PF03261;
DE  Function: p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000250|UniProtKB:Q15078}.
DE  Reference Proteome: Yes;
DE  Interaction: Q03114; IntAct: EBI-7038493; Score: 0.56
DE  Interaction: P21263; IntAct: EBI-7038472; Score: 0.46
DE  Interaction: P62989; IntAct: EBI-7038532; Score: 0.40
DE  Interaction: Q6ZMQ8; IntAct: EBI-2008524; Score: 0.40
DE  Interaction: B1WCA1; IntAct: EBI-8078736; Score: 0.54
DE  Interaction: Q63604; IntAct: EBI-15624622; Score: 0.35
DE  Interaction: Q03351; IntAct: EBI-15624585; Score: 0.35
DE  Interaction: P35739; IntAct: EBI-15624585; Score: 0.35
GO  GO:0030424;
GO  GO:0043292;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0030426;
GO  GO:0016020;
GO  GO:0031594;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098793;
GO  GO:0016533;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0045296;
GO  GO:0005509;
GO  GO:0061575;
GO  GO:0046875;
GO  GO:0035255;
GO  GO:0016301;
GO  GO:0002020;
GO  GO:0019901;
GO  GO:0043539;
GO  GO:0048675;
GO  GO:0007411;
GO  GO:0007413;
GO  GO:0007420;
GO  GO:0021549;
GO  GO:0021799;
GO  GO:0009792;
GO  GO:0048013;
GO  GO:0007213;
GO  GO:0070315;
GO  GO:0021766;
GO  GO:0035235;
GO  GO:0021819;
GO  GO:0030517;
GO  GO:0045892;
GO  GO:0007158;
GO  GO:0030182;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0043525;
GO  GO:0045860;
GO  GO:0090314;
GO  GO:2000273;
GO  GO:0032956;
GO  GO:0061001;
GO  GO:0070507;
GO  GO:0098693;
GO  GO:0048511;
GO  GO:0042501;
GO  GO:0021722;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKAQPNSSYQSNIAH
SQ  LNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGVSSSVKKAPHPAITSAGTPKRVIVQASTSELLRCLGEFLC
SQ  RRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNE
SQ  ISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR
//
ID  Q4KYY2;
PN  Cyclin-dependent kinase 5 activator 1, p25;
GN  CDK5R1;
OS  9997;
SL  Nucleus Position: SL-0198;
SL  Comments: [Cyclin-dependent kinase 5 activator 1, p35]: Cell membrane {ECO:0000250|UniProtKB:Q15078}; Lipid-anchor {ECO:0000250|UniProtKB:Q15078}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15078}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q15078}. Note=In the primary cortical neurons, p35 is present in the peripheries and nerve terminals. {ECO:0000250|UniProtKB:Q15078}. [Cyclin-dependent kinase 5 activator 1, p25]: Nucleus {ECO:0000250|UniProtKB:Q15078}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15078}. Perikaryon {ECO:0000250|UniProtKB:Q15078}. Note=The conversion of p35 to p25 relocalizes the protein from the cell periphery to the cytoplasm, in nuclear and perinuclear regions. In the primary cortical neurons, p25 is primarily concentrated in the cell soma and is largely absent from neurites. {ECO:0000250|UniProtKB:Q15078}.
DR  UNIPROT: Q4KYY2;
DR  Pfam: PF03261;
DE  Function: p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000250|UniProtKB:Q15078}.
DE  Reference Proteome: No;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0016533;
GO  GO:0061575;
GO  GO:0048013;
GO  GO:0061001;
GO  GO:0048511;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q15078};
SQ  MGTGLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKGQPNSSYQNNITH
SQ  LNNENLKKSLSCANLSTFAQPPPAQPPAPPANQLSGSQTGVSSSVKKAPHPSVTSAGTPKRVIVQASTSELLRCLGEFLC
SQ  RRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYVGNE
SQ  ISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQAFSDLKNESGQEDKKRLLLGLDR
//
ID  P06704;
PN  Cell division control protein 31;
GN  CDC31;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:10684247}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:8188750}. Note=Spindle pole body, SPB half- bridge (PubMed:8188750). Interacts with the nuclear pore complex (NPCs) at the nucleus envelope (PubMed:10684247). {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:8188750}.
DR  UNIPROT: P06704;
DR  UNIPROT: D6W2V8;
DR  PDB: 2DOQ;
DR  PDB: 2GV5;
DR  PDB: 3FWB;
DR  PDB: 3FWC;
DR  PDB: 4MBE;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Functions as a component of the spindle pole body (SPB) half- bridge (PubMed:10684247, PubMed:11156974, PubMed:12486115, PubMed:14504268, PubMed:8070654). At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication (PubMed:11156974, PubMed:12486115, PubMed:14504268, PubMed:8070654). Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity (PubMed:9813095). May play a role in vesicle-mediated transport, in a VPS13-dependent manner (PubMed:28122955). {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11156974, ECO:0000269|PubMed:12486115, ECO:0000269|PubMed:14504268, ECO:0000269|PubMed:28122955, ECO:0000269|PubMed:8070654, ECO:0000269|PubMed:9813095}.
DE  Reference Proteome: Yes;
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q99181; IntAct: EBI-857104; Score: 0.00
DE  Interaction: P00927; IntAct: EBI-7366294; Score: 0.40
DE  Interaction: P41940; IntAct: EBI-7560454; Score: 0.44
DE  Interaction: P47116; IntAct: EBI-7562977; Score: 0.44
DE  Interaction: P10659; IntAct: EBI-7668648; Score: 0.40
DE  Interaction: P34730; IntAct: EBI-7930447; Score: 0.40
DE  Interaction: O94742; IntAct: EBI-7945620; Score: 0.40
DE  Interaction: P46674; IntAct: EBI-7945717; Score: 0.77
DE  Interaction: P39015; IntAct: EBI-7945762; Score: 0.40
DE  Interaction: P11353; IntAct: EBI-8031674; Score: 0.40
DE  Interaction: Q02959; IntAct: EBI-8051544; Score: 0.59
DE  Interaction: P53164; IntAct: EBI-8463661; Score: 0.40
DE  Interaction: P53030; IntAct: EBI-8221748; Score: 0.22
DE  Interaction: Q6WNK7; IntAct: EBI-1370393; Score: 0.76
DE  Interaction: Q02336; IntAct: EBI-1370467; Score: 0.35
DE  Interaction: P53040; IntAct: EBI-1370499; Score: 0.35
DE  Interaction: Q08231; IntAct: EBI-1370592; Score: 0.76
DE  Interaction: P11927; IntAct: EBI-2212825; Score: 0.40
DE  Interaction: P47069; IntAct: EBI-2212835; Score: 0.59
DE  Interaction: P40457; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: Q12369; IntAct: EBI-2213075; Score: 0.56
DE  Interaction: P06704; IntAct: EBI-2213075; Score: 0.52
DE  Interaction: P54199; IntAct: EBI-2612619; Score: 0.35
DE  Interaction: P38590; IntAct: EBI-2612691; Score: 0.35
DE  Interaction: P32944; IntAct: EBI-2613930; Score: 0.35
DE  Interaction: Q08921; IntAct: EBI-2613976; Score: 0.35
DE  Interaction: P32447; IntAct: EBI-2881789; Score: 0.00
DE  Interaction: Q07457; IntAct: EBI-2882228; Score: 0.00
DE  Interaction: P26448; IntAct: EBI-2882390; Score: 0.00
DE  Interaction: Q00684; IntAct: EBI-2882792; Score: 0.00
DE  Interaction: P14832; IntAct: EBI-2882919; Score: 0.00
DE  Interaction: P32472; IntAct: EBI-2883301; Score: 0.00
DE  Interaction: P02293; IntAct: EBI-2884858; Score: 0.00
DE  Interaction: Q02796; IntAct: EBI-2885546; Score: 0.00
DE  Interaction: Q02206; IntAct: EBI-2886536; Score: 0.00
DE  Interaction: P38890; IntAct: EBI-2887466; Score: 0.00
DE  Interaction: P39723; IntAct: EBI-2887969; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P46675; IntAct: EBI-2888241; Score: 0.00
DE  Interaction: P25302; IntAct: EBI-2888465; Score: 0.00
DE  Interaction: Q06677; IntAct: EBI-3651969; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3668305; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3686264; Score: 0.35
DE  Interaction: P38915; IntAct: EBI-4375569; Score: 0.35
DE  Interaction: Q12060; IntAct: EBI-4376704; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-4380099; Score: 0.35
GO  GO:0005737;
GO  GO:0005825;
GO  GO:0005815;
GO  GO:0044732;
GO  GO:0005635;
GO  GO:0070390;
GO  GO:0005509;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0051301;
GO  GO:0048193;
GO  GO:0006406;
GO  GO:0045944;
GO  GO:0043161;
GO  GO:0043549;
GO  GO:0030474;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKREILDLIDEYDSEGRHLMKYDD
SQ  FYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTD
SQ  S
//
ID  Q9BWU1;
PN  Cyclin-dependent kinase 19;
GN  CDK19;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:32330417}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32330417}. Nucleus {ECO:0000269|PubMed:32330417}.
DR  UNIPROT: Q9BWU1;
DR  UNIPROT: Q5JQZ7;
DR  UNIPROT: Q5JR00;
DR  UNIPROT: Q8TC78;
DR  UNIPROT: Q9UPX2;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 614720;
DR  OMIM: 618916;
DR  DisGeNET: 23097;
DE  Function: 
DE  Disease: Developmental and epileptic encephalopathy 87 (DEE87) [MIM:618916]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE87 inheritance is autosomal dominant. {ECO:0000269|PubMed:32330417, ECO:0000269|PubMed:33134521, ECO:0000269|PubMed:33495529}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P10909; IntAct: EBI-6381327; Score: 0.35
DE  Interaction: P50613; IntAct: EBI-15560892; Score: 0.44
DE  Interaction: A0JLT2; IntAct: EBI-394580; Score: 0.62
DE  Interaction: Q9BTT4; IntAct: EBI-394793; Score: 0.62
DE  Interaction: Q9NWA0; IntAct: EBI-394834; Score: 0.71
DE  Interaction: Q9NX70; IntAct: EBI-394875; Score: 0.71
DE  Interaction: Q920D3; IntAct: EBI-394916; Score: 0.35
DE  Interaction: O95402; IntAct: EBI-394957; Score: 0.71
DE  Interaction: P49336; IntAct: EBI-395095; Score: 0.40
DE  Interaction: Q71F56; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q9P086; IntAct: EBI-395095; Score: 0.56
DE  Interaction: Q93074; IntAct: EBI-395095; Score: 0.85
DE  Interaction: Q9UHV7; IntAct: EBI-395095; Score: 0.74
DE  Interaction: O60244; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q96RN5; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q9Y2X0; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q9NVC6; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q9BUE0; IntAct: EBI-395095; Score: 0.56
DE  Interaction: Q15648; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q9H944; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q13503; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q15528; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q9ULK4; IntAct: EBI-395095; Score: 0.67
DE  Interaction: O75448; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q6P2C8; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q9H204; IntAct: EBI-395095; Score: 0.56
DE  Interaction: Q96HR3; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q9Y3C7; IntAct: EBI-395095; Score: 0.74
DE  Interaction: Q9NPJ6; IntAct: EBI-395095; Score: 0.67
DE  Interaction: O75586; IntAct: EBI-395095; Score: 0.67
DE  Interaction: O43513; IntAct: EBI-395095; Score: 0.74
DE  Interaction: Q96G25; IntAct: EBI-395095; Score: 0.67
DE  Interaction: Q8TDY2; IntAct: EBI-1068461; Score: 0.00
DE  Interaction: Q8TBZ2; IntAct: EBI-1074027; Score: 0.00
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P05090; IntAct: EBI-6381327; Score: 0.35
DE  Interaction: P12273; IntAct: EBI-6381327; Score: 0.35
DE  Interaction: P25311; IntAct: EBI-6381327; Score: 0.35
DE  Interaction: Q8IUD2; IntAct: EBI-6381327; Score: 0.53
DE  Interaction: P24863; IntAct: EBI-6381327; Score: 0.80
DE  Interaction: P50750; IntAct: EBI-8765229; Score: 0.35
DE  Interaction: Q12888; IntAct: EBI-20207896; Score: 0.27
DE  Interaction: Q83B01; IntAct: EBI-21286333; Score: 0.37
DE  Interaction: Q96DY7; IntAct: EBI-28945018; Score: 0.35
DE  Interaction: Q8ND56; IntAct: EBI-28945018; Score: 0.35
DE  Interaction: Q86YW9; IntAct: EBI-28945018; Score: 0.35
DE  Interaction: Q71SY5; IntAct: EBI-28945018; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-28945018; Score: 0.35
DE  Interaction: Q15021; IntAct: EBI-28945018; Score: 0.35
DE  Interaction: P49736; IntAct: EBI-28945018; Score: 0.35
DE  Interaction: P45983; IntAct: EBI-28945018; Score: 0.35
DE  Interaction: P33991; IntAct: EBI-28945018; Score: 0.35
DE  Interaction: P25205; IntAct: EBI-28945018; Score: 0.35
DE  Interaction: Q99816; IntAct: EBI-30840175; Score: 0.44
GO  GO:0005829;
GO  GO:0016592;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004693;
GO  GO:0106310;
GO  GO:0008353;
GO  GO:0071222;
GO  GO:0043065;
GO  GO:0050729;
GO  GO:0006468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDYDFKAKLAAERERVEDLFEYEGCKVGRGTYGHVYKARRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIA
SQ  LQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVM
SQ  GEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQED
SQ  IKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKHKVKPDSKVFLLLQKLLTMDP
SQ  TKRITSEQALQDPYFQEDPLPTLDVFAGCQIPYPKREFLNEDDPEEKGDKNQQQQQNQHQQPTAPPQQAAAPPQAPPPQQ
SQ  NSTQTNGTAGGAGAGVGGTGAGLQHSQDSSLNQVPPNKKPRLGPSGANSGGPVMPSDYQHSSSRLNYQSSVQGSSQSQST
SQ  LGYSSSSQQSSQYHPSHQAHRY
//
ID  Q8BWD8;
PN  Cyclin-dependent kinase 19;
GN  Cdk19;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9BWU1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9BWU1}. Nucleus {ECO:0000250|UniProtKB:Q9BWU1}.
DR  UNIPROT: Q8BWD8;
DR  UNIPROT: Q80TM1;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q83FA5; IntAct: EBI-21286775; Score: 0.37
GO  GO:0005829;
GO  GO:0016592;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004693;
GO  GO:0106310;
GO  GO:0008353;
GO  GO:0071222;
GO  GO:0043065;
GO  GO:0050729;
GO  GO:0006468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDYDFKAKLAAERERVEDLFEYEGCKVGRGTYGHVYKARRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIA
SQ  LQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVM
SQ  GEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQED
SQ  IKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKHKVKPDSKVFLLLQKLLTMDP
SQ  TKRITSEQALQDPYFQEDPLPTLDVFAGCQIPYPKREFLNEDEPEEKGDKNQPQQQNPHQQPAAPAQQTAAPPQAPPPQQ
SQ  SSAQTNGTAGGATAGGGGAGAGLQHSQDPGLNQVPPNKKPRIGPSGANSGGPVMPSDYQHSSSRLNYQSSVQGSSQSQST
SQ  LGYSSSQQSTQYHSSHQTHRY
//
ID  Q32KY4;
PN  Cyclin-dependent kinase 4;
GN  CDK4;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P11802}. Nucleus {ECO:0000250|UniProtKB:P11802}. Nucleus membrane {ECO:0000250|UniProtKB:P11802}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250|UniProtKB:P11802}.
DR  UNIPROT: Q32KY4;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250|UniProtKB:P11802}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016592;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005524;
GO  GO:0004693;
GO  GO:0106310;
GO  GO:0008353;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0010971;
GO  GO:0006468;
GO  GO:0051726;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCAT
SQ  ARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFG
SQ  LARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPR
SQ  DVSLPRGAFSPRGPRPVQSVVPELEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGDAE
//
ID  P11802;
PN  Cyclin-dependent kinase 4;
GN  CDK4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:18827403}. Nucleus {ECO:0000269|PubMed:18827403, ECO:0000269|PubMed:20399237, ECO:0000269|PubMed:9106657}. Nucleus membrane {ECO:0000269|PubMed:18827403}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus. {ECO:0000269|PubMed:18827403}.
DR  UNIPROT: P11802;
DR  UNIPROT: B2R9A0;
DR  UNIPROT: B4DNF9;
DR  UNIPROT: O00576;
DR  UNIPROT: Q6FG61;
DR  PDB: 2W96;
DR  PDB: 2W99;
DR  PDB: 2W9F;
DR  PDB: 2W9Z;
DR  PDB: 3G33;
DR  PDB: 5FWK;
DR  PDB: 5FWL;
DR  PDB: 5FWM;
DR  PDB: 5FWP;
DR  PDB: 6P8E;
DR  PDB: 6P8F;
DR  PDB: 6P8G;
DR  PDB: 6P8H;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 123829;
DR  OMIM: 609048;
DR  DisGeNET: 1019;
DE  Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. {ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:18827403, ECO:0000269|PubMed:9003781}.
DE  Disease: Melanoma, cutaneous malignant 3 (CMM3) [MIM:609048]: A malignant neoplasm of melanocytes, arising de novo or from a pre- existing benign nevus, which occurs most often in the skin but may also involve other sites. {ECO:0000269|PubMed:7652577, ECO:0000269|PubMed:8528263, ECO:0000269|PubMed:9311594, ECO:0000269|PubMed:9425228}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O75694; IntAct: EBI-1065754; Score: 0.00
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P07948; IntAct: EBI-1063758; Score: 0.00
DE  Interaction: P0DTD1; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q24158; IntAct: EBI-8620418; Score: 0.37
DE  Interaction: Q16543; IntAct: EBI-295633; Score: 0.93
DE  Interaction: P42771; IntAct: EBI-375269; Score: 0.96
DE  Interaction: P30281; IntAct: EBI-375326; Score: 0.98
DE  Interaction: P49736; IntAct: EBI-375329; Score: 0.44
DE  Interaction: P24385; IntAct: EBI-375341; Score: 0.98
DE  Interaction: P38936; IntAct: EBI-375404; Score: 0.92
DE  Interaction: O00311; IntAct: EBI-375437; Score: 0.44
DE  Interaction: P49918; IntAct: EBI-519276; Score: 0.40
DE  Interaction: P46527; IntAct: EBI-519297; Score: 0.93
DE  Interaction: Q8N720; IntAct: EBI-625679; Score: 0.71
DE  Interaction: P42772; IntAct: EBI-760282; Score: 0.97
DE  Interaction: P04632; IntAct: EBI-728826; Score: 0.00
DE  Interaction: P46379; IntAct: EBI-729744; Score: 0.00
DE  Interaction: Q15047; IntAct: EBI-7118776; Score: 0.55
DE  Interaction: Q9UGY1; IntAct: EBI-737135; Score: 0.00
DE  Interaction: P55273; IntAct: EBI-754729; Score: 0.96
DE  Interaction: Q9NP79; IntAct: EBI-758428; Score: 0.37
DE  Interaction: P30279; IntAct: EBI-768365; Score: 0.93
DE  Interaction: Q1EHW4; IntAct: EBI-922367; Score: 0.35
DE  Interaction: Q9UJU6; IntAct: EBI-1063375; Score: 0.00
DE  Interaction: Q9NS64; IntAct: EBI-1063663; Score: 0.00
DE  Interaction: Q8IZT6; IntAct: EBI-11132267; Score: 0.56
DE  Interaction: P23508; IntAct: EBI-1065583; Score: 0.00
DE  Interaction: Q12996; IntAct: EBI-1066306; Score: 0.00
DE  Interaction: P42773; IntAct: EBI-3906668; Score: 0.97
DE  Interaction: Q04323; IntAct: EBI-1068290; Score: 0.00
DE  Interaction: P57678; IntAct: EBI-1068996; Score: 0.00
DE  Interaction: Q96T76; IntAct: EBI-1069744; Score: 0.00
DE  Interaction: Q9UQE7; IntAct: EBI-1071705; Score: 0.00
DE  Interaction: P35606; IntAct: EBI-1072884; Score: 0.00
DE  Interaction: Q14683; IntAct: EBI-1073208; Score: 0.00
DE  Interaction: Q9UDX5; IntAct: EBI-1074355; Score: 0.00
DE  Interaction: Q9P1U1; IntAct: EBI-1075412; Score: 0.00
DE  Interaction: P62136; IntAct: EBI-1206902; Score: 0.00
DE  Interaction: P36873; IntAct: EBI-1207334; Score: 0.00
DE  Interaction: P30154; IntAct: EBI-1266474; Score: 0.35
DE  Interaction: P30153; IntAct: EBI-1266485; Score: 0.35
DE  Interaction: P32121; IntAct: EBI-1642843; Score: 0.35
DE  Interaction: Q9BQA1; IntAct: EBI-2940933; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-3906703; Score: 0.59
DE  Interaction: Q99956; IntAct: EBI-3906683; Score: 0.37
DE  Interaction: Q13261; IntAct: EBI-3906693; Score: 0.37
DE  Interaction: P63208; IntAct: EBI-3906713; Score: 0.37
DE  Interaction: Q99828; IntAct: EBI-3914485; Score: 0.37
DE  Interaction: Q15555; IntAct: EBI-3914495; Score: 0.37
DE  Interaction: P52209; IntAct: EBI-3927622; Score: 0.37
DE  Interaction: P20073; IntAct: EBI-7096705; Score: 0.37
DE  Interaction: P51693; IntAct: EBI-7117963; Score: 0.37
DE  Interaction: P06576; IntAct: EBI-7118041; Score: 0.37
DE  Interaction: O95865; IntAct: EBI-7118309; Score: 0.37
DE  Interaction: Q12766; IntAct: EBI-7118436; Score: 0.37
DE  Interaction: Q9Y383; IntAct: EBI-7118499; Score: 0.37
DE  Interaction: P14618; IntAct: EBI-7118577; Score: 0.37
DE  Interaction: P47897; IntAct: EBI-7118684; Score: 0.37
DE  Interaction: Q8IZ69; IntAct: EBI-7118859; Score: 0.37
DE  Interaction: Q05516; IntAct: EBI-7118939; Score: 0.37
DE  Interaction: Q15038; IntAct: EBI-7139218; Score: 0.37
DE  Interaction: P37840; IntAct: EBI-7391065; Score: 0.37
DE  Interaction: P04183; IntAct: EBI-7396108; Score: 0.37
DE  Interaction: Q8IZC7; IntAct: EBI-5283871; Score: 0.44
DE  Interaction: Q9H165; IntAct: EBI-5283535; Score: 0.44
DE  Interaction: Q08050; IntAct: EBI-5283631; Score: 0.44
DE  Interaction: P32243; IntAct: EBI-5278204; Score: 0.44
DE  Interaction: P28698; IntAct: EBI-5283775; Score: 0.44
DE  Interaction: O60902; IntAct: EBI-5282940; Score: 0.44
DE  Interaction: Q9P2Y4; IntAct: EBI-5282927; Score: 0.44
DE  Interaction: Q99741; IntAct: EBI-5283967; Score: 0.44
DE  Interaction: P28749; IntAct: EBI-5278658; Score: 0.44
DE  Interaction: Q14493; IntAct: EBI-5284015; Score: 0.44
DE  Interaction: Q9H4L4; IntAct: EBI-5283823; Score: 0.44
DE  Interaction: Q08999; IntAct: EBI-5283583; Score: 0.44
DE  Interaction: Q9H4Z2; IntAct: EBI-5284063; Score: 0.44
DE  Interaction: Q6UB98; IntAct: EBI-5283727; Score: 0.44
DE  Interaction: Q9C0J8; IntAct: EBI-5282970; Score: 0.44
DE  Interaction: P08151; IntAct: EBI-5282953; Score: 0.44
DE  Interaction: Q96PU4; IntAct: EBI-6051398; Score: 0.40
DE  Interaction: Q02556; IntAct: EBI-6115692; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-6255377; Score: 0.78
DE  Interaction: P07900; IntAct: EBI-6255377; Score: 0.53
DE  Interaction: Q00534; IntAct: EBI-6255377; Score: 0.35
DE  Interaction: Q12931; IntAct: EBI-6255377; Score: 0.35
DE  Interaction: Q14004; IntAct: EBI-6380178; Score: 0.53
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-21327757; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P84022; IntAct: EBI-6593176; Score: 0.27
DE  Interaction: Q77Q36; IntAct: EBI-9082540; Score: 0.40
DE  Interaction: Q13451; IntAct: EBI-9393873; Score: 0.64
DE  Interaction: Q9UJC3; IntAct: EBI-10197685; Score: 0.86
DE  Interaction: P53671; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P03129; IntAct: EBI-11721568; Score: 0.35
DE  Interaction: Q9BX66; IntAct: EBI-11132267; Score: 0.35
DE  Interaction: P53814; IntAct: EBI-11132267; Score: 0.35
DE  Interaction: Q9P2E3; IntAct: EBI-11132267; Score: 0.35
DE  Interaction: Q6PJT7; IntAct: EBI-11132267; Score: 0.35
DE  Interaction: Q9H061; IntAct: EBI-11132267; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-11132267; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-11132927; Score: 0.35
DE  Interaction: Q66GS9; IntAct: EBI-11386281; Score: 0.27
DE  Interaction: Q8N448; IntAct: EBI-11766518; Score: 0.49
DE  Interaction: Q16254; IntAct: EBI-12449950; Score: 0.53
DE  Interaction: P49815; IntAct: EBI-11687060; Score: 0.40
DE  Interaction: Q9UKT9; IntAct: EBI-24394070; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-24622275; Score: 0.56
DE  Interaction: Q9ULD0; IntAct: EBI-24764997; Score: 0.56
DE  Interaction: Q8WXX5; IntAct: EBI-11925475; Score: 0.00
DE  Interaction: Q8IVT5; IntAct: EBI-14035152; Score: 0.35
DE  Interaction: P04004; IntAct: EBI-21709311; Score: 0.35
DE  Interaction: Q9UKA8; IntAct: EBI-21786597; Score: 0.35
DE  Interaction: Q58FG0; IntAct: EBI-21835664; Score: 0.35
DE  Interaction: Q5TC84; IntAct: EBI-21835664; Score: 0.35
DE  Interaction: Q58FF7; IntAct: EBI-21835664; Score: 0.35
DE  Interaction: Q58FF6; IntAct: EBI-21835664; Score: 0.35
DE  Interaction: P55789; IntAct: EBI-21835664; Score: 0.35
DE  Interaction: P52333; IntAct: EBI-21835664; Score: 0.35
DE  Interaction: P08236; IntAct: EBI-21835664; Score: 0.35
DE  Interaction: Q9NZT2; IntAct: EBI-21848776; Score: 0.40
DE  Interaction: P50613; IntAct: EBI-15560841; Score: 0.44
DE  Interaction: P46414; IntAct: EBI-15763467; Score: 0.40
DE  Interaction: Q92830; IntAct: EBI-16107564; Score: 0.40
DE  Interaction: Q9JHD2; IntAct: EBI-16107581; Score: 0.40
DE  Interaction: Q9Y6K9; IntAct: EBI-20737021; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9UH17; IntAct: EBI-25296426; Score: 0.64
DE  Interaction: P82930; IntAct: EBI-25477405; Score: 0.35
DE  Interaction: P53007; IntAct: EBI-25477405; Score: 0.35
DE  Interaction: P43307; IntAct: EBI-25477405; Score: 0.35
DE  Interaction: P28482; IntAct: EBI-25477405; Score: 0.35
DE  Interaction: P54819; IntAct: EBI-25477405; Score: 0.35
DE  Interaction: Q8TB24; IntAct: EBI-26518569; Score: 0.35
DE  Interaction: Q9H9E1; IntAct: EBI-26656693; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: P09936; IntAct: EBI-27121923; Score: 0.59
DE  Interaction: P00441; IntAct: EBI-28996885; Score: 0.40
DE  Interaction: Q13619; IntAct: EBI-30863570; Score: 0.35
GO  GO:0005923;
GO  GO:0000785;
GO  GO:0097128;
GO  GO:0097129;
GO  GO:0097130;
GO  GO:0000307;
GO  GO:0005829;
GO  GO:0016592;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005667;
GO  GO:0005524;
GO  GO:0030332;
GO  GO:0004693;
GO  GO:0016538;
GO  GO:0106310;
GO  GO:0008353;
GO  GO:0060612;
GO  GO:0051301;
GO  GO:0032869;
GO  GO:0071353;
GO  GO:1904637;
GO  GO:0071222;
GO  GO:1904628;
GO  GO:0000082;
GO  GO:0008284;
GO  GO:0048146;
GO  GO:0010971;
GO  GO:0006468;
GO  GO:0051726;
GO  GO:0010468;
GO  GO:0046626;
GO  GO:0046890;
GO  GO:0050994;
GO  GO:0040014;
GO  GO:0060260;
GO  GO:0061469;
GO  GO:0009410;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCAT
SQ  SRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFG
SQ  LARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPR
SQ  DVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE
//
ID  P30285;
PN  Cyclin-dependent kinase 4;
GN  Cdk4;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P11802}. Nucleus {ECO:0000250|UniProtKB:P11802}. Nucleus membrane {ECO:0000250|UniProtKB:P11802}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250|UniProtKB:P11802}.
DR  UNIPROT: P30285;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P24385; IntAct: EBI-6988572; Score: 0.40
DE  Interaction: P25322; IntAct: EBI-1005778; Score: 0.94
DE  Interaction: P30280; IntAct: EBI-1005844; Score: 0.53
DE  Interaction: P46414; IntAct: EBI-1005778; Score: 0.56
DE  Interaction: P30282; IntAct: EBI-1005844; Score: 0.53
DE  Interaction: P06400; IntAct: EBI-1182824; Score: 0.62
DE  Interaction: P63087; IntAct: EBI-1202851; Score: 0.00
DE  Interaction: Q01105; IntAct: EBI-1371868; Score: 0.35
DE  Interaction: Q8CIG8; IntAct: EBI-2941146; Score: 0.50
DE  Interaction: Q99J09; IntAct: EBI-3401852; Score: 0.35
DE  Interaction: O15211; IntAct: EBI-3956301; Score: 0.40
DE  Interaction: P46527; IntAct: EBI-12737659; Score: 0.35
DE  Interaction: P51480; IntAct: EBI-15653801; Score: 0.35
DE  Interaction: Q60772; IntAct: EBI-15653801; Score: 0.35
DE  Interaction: P55271; IntAct: EBI-15653855; Score: 0.35
DE  Interaction: P09936; IntAct: EBI-27097896; Score: 0.40
DE  Interaction: Q9R0P9; IntAct: EBI-27121708; Score: 0.35
GO  GO:0005923;
GO  GO:0000785;
GO  GO:0097128;
GO  GO:0097129;
GO  GO:0097130;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016592;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0005667;
GO  GO:0005524;
GO  GO:0030332;
GO  GO:0004693;
GO  GO:0016301;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0044877;
GO  GO:0008353;
GO  GO:0060612;
GO  GO:0051301;
GO  GO:0032869;
GO  GO:0071353;
GO  GO:1904637;
GO  GO:0071222;
GO  GO:1904628;
GO  GO:0000082;
GO  GO:0043065;
GO  GO:0008284;
GO  GO:0045793;
GO  GO:0050679;
GO  GO:0048146;
GO  GO:0010971;
GO  GO:0045727;
GO  GO:0006468;
GO  GO:0051726;
GO  GO:0010468;
GO  GO:0046626;
GO  GO:0046890;
GO  GO:0050994;
GO  GO:0040014;
GO  GO:0061469;
GO  GO:0010288;
GO  GO:0010033;
GO  GO:0033574;
GO  GO:0009410;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAATRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGAAGGGLPVSTVREVALLRRLEAFEHPNVVRLMDVCAT
SQ  SRTDRDIKVTLVFEHIDQDLRTYLDKAPPPGLPVETIKDLMRQFLSGLDFLHANCIVHRDLKPENILVTSNGTVKLADFG
SQ  LARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPR
SQ  EVSLPRGAFAPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKEESDAE
//
ID  P79432;
PN  Cyclin-dependent kinase 4;
GN  CDK4;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P11802}. Nucleus {ECO:0000250|UniProtKB:P11802}. Nucleus membrane {ECO:0000250|UniProtKB:P11802}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250|UniProtKB:P11802}.
DR  UNIPROT: P79432;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250|UniProtKB:P11802}.
DE  Reference Proteome: Yes;
GO  GO:0005923;
GO  GO:0000785;
GO  GO:0097128;
GO  GO:0097129;
GO  GO:0097130;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016592;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005667;
GO  GO:0005524;
GO  GO:0030332;
GO  GO:0004693;
GO  GO:0106310;
GO  GO:0008353;
GO  GO:0060612;
GO  GO:0051301;
GO  GO:0032869;
GO  GO:0071353;
GO  GO:1904637;
GO  GO:0071222;
GO  GO:1904628;
GO  GO:0000082;
GO  GO:0048146;
GO  GO:0010971;
GO  GO:0006468;
GO  GO:0051726;
GO  GO:0010468;
GO  GO:0046626;
GO  GO:0046890;
GO  GO:0050994;
GO  GO:0040014;
GO  GO:0061469;
GO  GO:0009410;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCAT
SQ  ARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFG
SQ  LARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPR
SQ  DVSLPRGAFSPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGNPE
//
ID  P35426;
PN  Cyclin-dependent kinase 4;
GN  Cdk4;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P11802}. Nucleus {ECO:0000250|UniProtKB:P11802}. Nucleus membrane {ECO:0000250|UniProtKB:P11802}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250|UniProtKB:P11802}.
DR  UNIPROT: P35426;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250|UniProtKB:P11802}.
DE  Reference Proteome: Yes;
GO  GO:0005923;
GO  GO:0000785;
GO  GO:0097128;
GO  GO:0097129;
GO  GO:0097130;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0016592;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0005667;
GO  GO:0005524;
GO  GO:0030332;
GO  GO:0004693;
GO  GO:0016301;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0044877;
GO  GO:0008353;
GO  GO:0060612;
GO  GO:0031100;
GO  GO:0051301;
GO  GO:0032869;
GO  GO:0071353;
GO  GO:1904637;
GO  GO:0071222;
GO  GO:1904628;
GO  GO:1904584;
GO  GO:0007623;
GO  GO:0000082;
GO  GO:0002088;
GO  GO:0043065;
GO  GO:0008284;
GO  GO:0045793;
GO  GO:0050679;
GO  GO:0048146;
GO  GO:0010971;
GO  GO:0045727;
GO  GO:0006468;
GO  GO:0051726;
GO  GO:0042127;
GO  GO:0010468;
GO  GO:0046626;
GO  GO:0046890;
GO  GO:0050994;
GO  GO:0040014;
GO  GO:0061469;
GO  GO:0055093;
GO  GO:0010288;
GO  GO:0010033;
GO  GO:0033574;
GO  GO:0009636;
GO  GO:0009410;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATTRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGAAGGGLPVSTVREVALLRRLEAFEHPNVVRLMDVCAT
SQ  SRTDRDIKVTLVFEHIDQDLRTYLDKAPPPGLPVETIKDLMRQFLSGLDFLHANCIVHRDLKPENILVTSNGTVKLADFG
SQ  LARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPR
SQ  EVSLPRGAFSPRGPRPVQSVVPEMEESGAQLLLEMLTFNPLKRISAFRALQHSYLHKEESDPE
//
ID  B2MVY4;
PN  Cyclin-dependent kinase 4;
GN  CDK4;
OS  9940;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P11802}. Nucleus {ECO:0000250|UniProtKB:P11802}. Nucleus membrane {ECO:0000250|UniProtKB:P11802}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250|UniProtKB:P11802}.
DR  UNIPROT: B2MVY4;
DR  UNIPROT: B2CL06;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005923;
GO  GO:0000785;
GO  GO:0097128;
GO  GO:0097129;
GO  GO:0097130;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005667;
GO  GO:0005524;
GO  GO:0030332;
GO  GO:0004693;
GO  GO:0106310;
GO  GO:0060612;
GO  GO:0051301;
GO  GO:0032869;
GO  GO:0071353;
GO  GO:1904637;
GO  GO:0071222;
GO  GO:1904628;
GO  GO:0000082;
GO  GO:0048146;
GO  GO:0010971;
GO  GO:0006468;
GO  GO:0010468;
GO  GO:0046626;
GO  GO:0046890;
GO  GO:0050994;
GO  GO:0040014;
GO  GO:0061469;
GO  GO:0009410;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCAT
SQ  ARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFG
SQ  LARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPR
SQ  DVSLPRGAFSPRGPRPVQSVVPELEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGDAE
//
ID  P50613;
PN  Cyclin-dependent kinase 7;
GN  CDK7;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10958787, ECO:0000269|PubMed:15695176, ECO:0000269|PubMed:19071173}. Cytoplasm {ECO:0000269|PubMed:15695176}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19071173}. Note=Colocalizes with PRKCI in the cytoplasm and nucleus (PubMed:15695176). Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides (PubMed:19071173). {ECO:0000269|PubMed:15695176, ECO:0000269|PubMed:19071173}.
DR  UNIPROT: P50613;
DR  UNIPROT: Q9BS60;
DR  UNIPROT: Q9UE19;
DR  PDB: 1UA2;
DR  PDB: 6O9L;
DR  PDB: 6XBZ;
DR  PDB: 6XD3;
DR  PDB: 7B5O;
DR  PDB: 7B5Q;
DR  PDB: 7EGB;
DR  PDB: 7EGC;
DR  PDB: 7ENA;
DR  PDB: 7ENC;
DR  PDB: 7LBM;
DR  PDB: 7NVR;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 601955;
DR  DisGeNET: 1022;
DE  Function: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C- terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts (PubMed:9852112). Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:16327805, ECO:0000269|PubMed:17373709, ECO:0000269|PubMed:17386261, ECO:0000269|PubMed:17901130, ECO:0000269|PubMed:19015234, ECO:0000269|PubMed:19071173, ECO:0000269|PubMed:19136461, ECO:0000269|PubMed:19450536, ECO:0000269|PubMed:19667075, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:9372954, ECO:0000269|PubMed:9840937, ECO:0000269|PubMed:9852112}.
DE  Reference Proteome: Yes;
DE  Interaction: O15027; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: P11802; IntAct: EBI-15560841; Score: 0.44
DE  Interaction: P12270; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: P51948; IntAct: EBI-1245984; Score: 0.82
DE  Interaction: P51946; IntAct: EBI-1245984; Score: 0.93
DE  Interaction: P32121; IntAct: EBI-1642567; Score: 0.35
DE  Interaction: A0A380PKN3; IntAct: EBI-2873645; Score: 0.00
DE  Interaction: P31016; IntAct: EBI-7960638; Score: 0.44
DE  Interaction: P51659; IntAct: EBI-3906748; Score: 0.37
DE  Interaction: P01909; IntAct: EBI-3906738; Score: 0.37
DE  Interaction: P24941; IntAct: EBI-6255891; Score: 0.71
DE  Interaction: P01023; IntAct: EBI-6380434; Score: 0.35
DE  Interaction: P32780; IntAct: EBI-6380434; Score: 0.76
DE  Interaction: P48740; IntAct: EBI-6380434; Score: 0.35
DE  Interaction: P19447; IntAct: EBI-6380434; Score: 0.74
DE  Interaction: P18074; IntAct: EBI-6380434; Score: 0.74
DE  Interaction: Q92759; IntAct: EBI-6380434; Score: 0.67
DE  Interaction: Q13888; IntAct: EBI-6380434; Score: 0.67
DE  Interaction: P23634; IntAct: EBI-6380434; Score: 0.35
DE  Interaction: P28715; IntAct: EBI-6380434; Score: 0.67
DE  Interaction: Q13889; IntAct: EBI-6380434; Score: 0.67
DE  Interaction: Q6ZYL4; IntAct: EBI-6380434; Score: 0.74
DE  Interaction: P78362; IntAct: EBI-6657590; Score: 0.59
DE  Interaction: Q96SB4; IntAct: EBI-6659767; Score: 0.59
DE  Interaction: P08238; IntAct: EBI-6424069; Score: 0.56
DE  Interaction: Q01094; IntAct: EBI-6599707; Score: 0.27
DE  Interaction: Q6P1K8; IntAct: EBI-21622006; Score: 0.53
DE  Interaction: O96006; IntAct: EBI-21692488; Score: 0.35
DE  Interaction: P14635; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: Q58FG0; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: Q9UBF8; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: Q96NH3; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: Q8IZL9; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: Q58FG1; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: Q58FF7; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: Q58FF6; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: Q13451; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: Q13137; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: P46527; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: P24864; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: P20248; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-15560801; Score: 0.44
DE  Interaction: P24928; IntAct: EBI-15560781; Score: 0.44
DE  Interaction: Q6IAW3; IntAct: EBI-15560872; Score: 0.44
DE  Interaction: Q9BWU1; IntAct: EBI-15560892; Score: 0.44
DE  Interaction: O00267; IntAct: EBI-15560912; Score: 0.44
DE  Interaction: P21127; IntAct: EBI-15560932; Score: 0.44
DE  Interaction: Q9NXF1; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q96PZ0; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q8WUA4; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q7Z4V5; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: O15355; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q13042; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q8N1G0; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P30260; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q96ME7; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q8TDI0; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q7Z5K2; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9NW82; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9Y3C7; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9Y2R4; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9UK58; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9NY93; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9NX58; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9NW13; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9NVC6; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9H0A0; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9BZE4; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q96S94; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q92621; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q8TF01; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q8IY81; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q8IX01; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q6PD62; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q16543; IntAct: EBI-16789709; Score: 0.42
DE  Interaction: Q14684; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q14241; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q13823; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q13610; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q13011; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P55199; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P46013; IntAct: EBI-16789709; Score: 0.48
DE  Interaction: P29083; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: O75683; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: O00541; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9Y5Q9; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9Y5Q8; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9Y4W2; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9Y2X9; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9Y2G7; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9H9Y6; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9H9B1; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9BYE7; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q9BTC8; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q8IWI9; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q6P1X5; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q5UIP0; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q15542; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q13206; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: Q12789; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P62891; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P49848; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P49642; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P38432; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P29084; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P21675; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: O95602; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: O00268; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P15927; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: P56270; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: P0DMV8; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: Q7Z739; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: Q709F0; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: P62633; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: O15235; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: Q02539; IntAct: EBI-20913302; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9Y2W1; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: Q9UPE1; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: Q9NYF8; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: Q96SB3; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: Q8ND56; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: Q8IUD2; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: Q86X55; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: Q16891; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: Q01082; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: P54886; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: P11388; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: P0C0S5; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-28935791; Score: 0.35
DE  Interaction: O00763; IntAct: EBI-28935791; Score: 0.35
GO  GO:0070516;
GO  GO:0019907;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0001650;
GO  GO:0001673;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0000439;
GO  GO:0005675;
GO  GO:0070985;
GO  GO:0005524;
GO  GO:0008094;
GO  GO:0004693;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0008353;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0006281;
GO  GO:0070816;
GO  GO:0045944;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:0051726;
GO  GO:0000079;
GO  GO:2000045;
GO  GO:0042795;
GO  GO:0006366;
GO  GO:0006367;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDA
SQ  FGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAK
SQ  SFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDM
SQ  CSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSNRPGPTPGCQLPRPNCPVETLKEQ
SQ  SNPALAIKRKRTEALEQGGLPKKLIF
//
ID  Q03147;
PN  Cyclin-dependent kinase 7;
GN  Cdk7;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P50613}. Cytoplasm {ECO:0000250|UniProtKB:P50613}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50613}. Note=Colocalizes with PRKCI in the cytoplasm and nucleus. Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides (By similarity). {ECO:0000250|UniProtKB:P50613}.
DR  UNIPROT: Q03147;
DR  UNIPROT: Q99KK3;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C- terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition.
DE  Reference Proteome: Yes;
DE  Interaction: Q99J95; IntAct: EBI-6260872; Score: 0.35
GO  GO:0070516;
GO  GO:0019907;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0001650;
GO  GO:0001673;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0000439;
GO  GO:0005675;
GO  GO:0070985;
GO  GO:0005524;
GO  GO:0008094;
GO  GO:0004693;
GO  GO:0016301;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0044877;
GO  GO:0008353;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0006281;
GO  GO:0070816;
GO  GO:0045944;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:2000045;
GO  GO:0006366;
GO  GO:0006367;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDA
SQ  FGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAK
SQ  SFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDM
SQ  CSLPDYVTFKSFPGVPLQHIFIAAGDDLLELIQGLFLFNPCTRTTASQALKTKYFSNRPGPTPGCQLPRPNCPVEALKEP
SQ  ANPTVATKRKRAEALEQGILPKKLIF
//
ID  P51952;
PN  Cyclin-dependent kinase 7;
GN  Cdk7;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P50613}. Cytoplasm {ECO:0000250|UniProtKB:P50613}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50613}. Note=Colocalizes with PRKCI in the cytoplasm and nucleus. Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides (By similarity). {ECO:0000250|UniProtKB:P50613}.
DR  UNIPROT: P51952;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C- terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0070516;
GO  GO:0019907;
GO  GO:0000307;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0001673;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000439;
GO  GO:0005675;
GO  GO:0070985;
GO  GO:0005524;
GO  GO:0008094;
GO  GO:0004693;
GO  GO:0016301;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0044877;
GO  GO:0008353;
GO  GO:0051301;
GO  GO:0006281;
GO  GO:0051321;
GO  GO:0070816;
GO  GO:0045944;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:2000045;
GO  GO:0006366;
GO  GO:0006367;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  ANRNEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNIS
SQ  LVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNWA
SQ  YTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVT
SQ  FKSFPGIPLQHIFIAAGDDLLELIQGLFLFNPCTRITASQALRTKYFSNRPGPTPGCQLPRPNCPVEALKEQSNPAMATK
SQ  RKRAEALEQ
//
ID  Q16667;
PN  Cyclin-dependent kinase inhibitor 3;
GN  CDKN3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10669749}.
DR  UNIPROT: Q16667;
DR  UNIPROT: Q53ZU6;
DR  UNIPROT: Q5U0M4;
DR  UNIPROT: Q6P1N8;
DR  UNIPROT: Q99585;
DR  UNIPROT: Q9BPW7;
DR  UNIPROT: Q9BY36;
DR  UNIPROT: Q9C042;
DR  UNIPROT: Q9C046;
DR  UNIPROT: Q9C047;
DR  UNIPROT: Q9C049;
DR  UNIPROT: Q9C051;
DR  UNIPROT: Q9C053;
DR  PDB: 1FPZ;
DR  PDB: 1FQ1;
DR  Pfam: PF05706;
DR  PROSITE: PS50056;
DR  PROSITE: PS50054;
DR  OMIM: 114550;
DR  OMIM: 123832;
DR  DisGeNET: 1033;
DE  Function: May play a role in cell cycle regulation. Dual specificity CC phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues (PubMed:8127873, PubMed:8242750). Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner (PubMed:7569954). {ECO:0000269|PubMed:7569954, ECO:0000269|PubMed:8127873, ECO:0000269|PubMed:8242750}.
DE  Disease: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes. {ECO:0000269|PubMed:10987270}. Note=The gene represented in this entry may be involved in disease pathogenesis.
DE  Reference Proteome: Yes;
DE  Interaction: Q00526; IntAct: EBI-8650121; Score: 0.55
DE  Interaction: P00546; IntAct: EBI-8650104; Score: 0.37
DE  Interaction: P24941; IntAct: EBI-8650171; Score: 0.89
DE  Interaction: P06493; IntAct: EBI-8650137; Score: 0.55
DE  Interaction: Q86YZ3; IntAct: EBI-14026618; Score: 0.35
DE  Interaction: P16949; IntAct: EBI-14026618; Score: 0.35
DE  Interaction: Q66LE6; IntAct: EBI-14026618; Score: 0.35
DE  Interaction: P54829; IntAct: EBI-14026618; Score: 0.35
DE  Interaction: P50747; IntAct: EBI-14026618; Score: 0.35
DE  Interaction: P38646; IntAct: EBI-20906264; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0017018;
GO  GO:0004722;
GO  GO:0004725;
GO  GO:0008138;
GO  GO:0000082;
GO  GO:0008285;
GO  GO:0006470;
GO  GO:0051726;
GO  GO:0000079;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCT
SQ  RGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSD
SQ  TISPEQAIDSLRDLRGSGAIQTIKQYNYLHEFRDKLAAHLSSRDSQSRSVSR
//
ID  Q810P3;
PN  Cyclin-dependent kinase inhibitor 3;
GN  Cdkn3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q16667}.
DR  UNIPROT: Q810P3;
DR  UNIPROT: Q9CWS3;
DR  Pfam: PF05706;
DR  PROSITE: PS50056;
DR  PROSITE: PS50054;
DE  Function: May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q16667}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0017018;
GO  GO:0004722;
GO  GO:0004725;
GO  GO:0008138;
GO  GO:0007049;
GO  GO:0006974;
GO  GO:0006470;
GO  GO:0051726;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCT
SQ  RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLAACLLLYLSDS
SQ  ISPQQAIDSLRDVRGSGAIQTIKQYNYLHEFRDKLAAYLSSRDSLSRSVSR
//
ID  Q9MYN5;
PN  Cyclin-dependent kinase inhibitor 3;
GN  CDKN3;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q16667}.
DR  UNIPROT: Q9MYN5;
DR  Pfam: PF05706;
DR  PROSITE: PS50056;
DR  PROSITE: PS50054;
DE  Function: May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q16667}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0017018;
GO  GO:0004725;
GO  GO:0008138;
GO  GO:0007049;
GO  GO:0006470;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPPSSIQTSEFDSSDEEPIEDEQTPIQISWLPLSRVNYSQFLGLCALPGCKFKDVRRNIQKDTEELKSCGIQDVFVFCT
SQ  RGELSKYRVPNLLDLYHQYGIITHHHPIPDGGAPDIASCCEIMEELEICLQNNRKTLIHCYGGLGRSCLVAACLLLYLSD
SQ  TVSPQQAIDSLRDLRGSGAIQTIKQYNYLHEFRDKLAAHLSSRESLSRSVSR
//
ID  B2RZ50;
PN  Cyclin-dependent kinase inhibitor 3;
GN  Cdkn3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q16667}.
DR  UNIPROT: B2RZ50;
DR  Pfam: PF05706;
DR  PROSITE: PS50056;
DR  PROSITE: PS50054;
DE  Function: May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q16667}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0017018;
GO  GO:0004722;
GO  GO:0004725;
GO  GO:0008138;
GO  GO:0007049;
GO  GO:0006470;
GO  GO:0051726;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPPISIQASEFDSSDEEPADDEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSSGIQDVFVFCT
SQ  RGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLVAACLLLYLSD
SQ  SISPQQAIDSLRDVRGSGAIQTIKQYNYLHEFRDKLAAYLSSRDSLSRSVSR
//
ID  Q19972;
PN  Chromo domain-containing protein cec-4;
GN  cec;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:26607792}. Membrane {ECO:0000305|PubMed:26607792}; Peripheral membrane protein {ECO:0000305|PubMed:26607792}.
DR  UNIPROT: Q19972;
DR  Pfam: PF00385;
DR  PROSITE: PS50013;
DE  Function: Chromatin anchor protein which binds to methylated lysine residues on histone H3, thereby recruiting heterochromatin to the nuclear periphery, especially in embryonic cells, with a lesser role in differentiated cells (PubMed:26607792, PubMed:31118512). May be required for the correct positioning of chromatin and nucleoli in embryos (PubMed:26607792). {ECO:0000269|PubMed:26607792, ECO:0000269|PubMed:31118512}.
DE  Reference Proteome: Yes;
GO  GO:0000793;
GO  GO:0005637;
GO  GO:0003682;
GO  GO:0035064;
GO  GO:0097240;
GO  GO:0045595;
GO  GO:0010468;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:26607792};
SQ  MAKKTVEGEHGTPKTNFTKKETSKNHDDFKKIIGHKVVEEHYVEYEVELTSGKTITATEFDFKGDDSLLSTYKKKVTKQS
SQ  DDSSGEYAVERVLAHRKVKGSPLYLVQWKGYPHPVWNSEMWEEDLDNCKDLLAAYKKHQEDLKIAQTPKKTPSKTPKKTP
SQ  KSLKRRALTPSDDEEEAGPIAPEPKKTPKQSTKKLKRTTSPETNLVEKSKKKAIPDLENHTLDQEKNDVIERVEEIQEDE
SQ  DDDDEQREEVVTTAPVETKSRWGFGSWKWF
//
ID  P42573;
PN  Cell death protein 3 subunit p13;
GN  ced;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:27723735}. Perikaryon {ECO:0000269|PubMed:26074078}. Synapse {ECO:0000269|PubMed:26074078}. Mitochondrion {ECO:0000269|PubMed:26074078}. Cytoplasm {ECO:0000269|PubMed:27723735}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27723735}. Note=Colocalizes with nucleoporin npp-14 to the perinuclear region in germ cells (PubMed:27723735). Becomes diffused in the cytoplasm in apoptotic germ cells (PubMed:27723735). Localizes to axonal mitochondria and synapses of DD motor neurons (PubMed:26074078). Synaptic localization is dependent on axonal mitochondria (PubMed:26074078). {ECO:0000269|PubMed:26074078, ECO:0000269|PubMed:27723735}.
DR  UNIPROT: P42573;
DR  UNIPROT: P45435;
DR  UNIPROT: Q9GQQ4;
DR  UNIPROT: Q9NAQ8;
DR  PDB: 4M9R;
DR  PDB: 4M9S;
DR  PDB: 4M9X;
DR  PDB: 4M9Y;
DR  PDB: 4M9Z;
DR  Pfam: PF00619;
DR  PROSITE: PS50209;
DR  PROSITE: PS01122;
DR  PROSITE: PS01121;
DR  PROSITE: PS50207;
DR  PROSITE: PS50208;
DE  Function: Acts as a cysteine protease in controlling programmed cell death (apoptosis) by proteolytically activating or inactivating a wide range of substrates (PubMed:8654923, PubMed:3955651, PubMed:18722182, PubMed:26074078, PubMed:27723735). Component of the egl-1, ced-9, ced-4 and ced-3 apoptotic signaling cascade required for the initiation of programmed cell death in cells fated to die during embryonic and postembryonic development (PubMed:3955651, PubMed:17329362, PubMed:25432023, PubMed:27723735). During oogenesis, required for germline apoptosis downstream of ced-9 and ced-4 but independently of egl-1 (PubMed:9927601). By cleaving and activating ced-8, promotes phosphatidylserine exposure on the surface of apoptotic cells; phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment (PubMed:24225442). By cleaving and converting dcr-1 into a deoxyribonuclease (DNase), promotes apoptotic chromosomal DNA fragmentation (PubMed:20223951). By cleaving mitochondrial fission protein drp-1, may regulate the removal of mitochondria during apoptosis (PubMed:18722182). During germline apoptosis, cleaves translation initiation factor ifg-1 (isoform p170) promoting cap- independent translation (PubMed:21909434). During male tail morphogenesis, promotes apoptosis of the tail-spike cell downstream of ced-4 but independently of egl-1 and ced-9 (PubMed:17329362). By cleaving cnt-1, prevents the activation of the prosurvival akt-1/2 signaling pathway and thus promotes apoptosis (PubMed:25383666). Downstream of ced-4, may play a role in sex-specific cell apoptosis by cleaving sex-determining protein fem-1 (PubMed:10764728). May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway (PubMed:21901106). Cleaves ced-9 in vitro (PubMed:17371877, PubMed:18776901, PubMed:19575016, PubMed:25432023, PubMed:27723735). Cleaves csp-2 isoform b resulting in the removal of the propeptide and the generation of csp-2 subunit p31 in vitro (PubMed:9857046). Independently of its apoptotic role has additional functions. Probably by cleaving and thereby activating actin-severing protein gsnl-1, required for the elimination of transient presynaptic components during larval development downstream of egl-1, ced-9 and ced-4 pathway (PubMed:26074078). Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), regulates temporal cell fate patterning during larval development (PubMed:25432023). In complex with ubr-1, which is E3 ubiquitin-protein ligase and component of the N-end rule pathway, acts in seam cell fate patterning during larval development by cleaving the heterochronic protein lin-28, and promoting its degradation (PubMed:25432023, PubMed:28602583). Also cleaves heterochronic protein lin-14 and exonuclease disl-2 in vitro (PubMed:25432023). Downstream of calreticulin crt-1 and ced-4 and independently of egl-1 and ced-9, plays a role in the initial steps of axonal regrowth following axotomy (PubMed:22629231). Cleaves 14-3-3- like protein ftt-2, tubulin tbb-2 and calreticulin crt-1 in vitro (PubMed:17371877). Also plays a role in resistance to S.typhimurium- mediated infection (PubMed:11226309). {ECO:0000269|PubMed:10764728, ECO:0000269|PubMed:11226309, ECO:0000269|PubMed:17329362, ECO:0000269|PubMed:17371877, ECO:0000269|PubMed:18722182, ECO:0000269|PubMed:18776901, ECO:0000269|PubMed:19575016, ECO:0000269|PubMed:20223951, ECO:0000269|PubMed:21901106, ECO:0000269|PubMed:21909434, ECO:0000269|PubMed:22629231, ECO:0000269|PubMed:24225442, ECO:0000269|PubMed:25383666, ECO:0000269|PubMed:25432023, ECO:0000269|PubMed:26074078, ECO:0000269|PubMed:27723735, ECO:0000269|PubMed:28602583, ECO:0000269|PubMed:3955651, ECO:0000269|PubMed:8654923, ECO:0000269|PubMed:9857046, ECO:0000269|PubMed:9927601}.
DE  Reference Proteome: Yes;
DE  Interaction: P30429; IntAct: EBI-494268; Score: 0.86
DE  Interaction: Q8STE5; IntAct: EBI-8001700; Score: 0.37
DE  Interaction: P41958; IntAct: EBI-494631; Score: 0.70
DE  Interaction: P42573; IntAct: EBI-2655158; Score: 0.75
DE  Interaction: G5ECW5; IntAct: EBI-15727540; Score: 0.60
DE  Interaction: Q9XXH8; IntAct: EBI-16127213; Score: 0.44
DE  Interaction: Q9NAG4; IntAct: EBI-16587378; Score: 0.35
GO  GO:0070161;
GO  GO:0008303;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0031965;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0098793;
GO  GO:0008656;
GO  GO:0004197;
GO  GO:0097153;
GO  GO:0097199;
GO  GO:0097200;
GO  GO:0004175;
GO  GO:0042802;
GO  GO:0030042;
GO  GO:0097202;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:1902742;
GO  GO:0050829;
GO  GO:0009792;
GO  GO:0097194;
GO  GO:0046716;
GO  GO:1905803;
GO  GO:1900118;
GO  GO:1904747;
GO  GO:1905845;
GO  GO:0043525;
GO  GO:1901046;
GO  GO:0010954;
GO  GO:1905808;
GO  GO:0012501;
GO  GO:0016540;
GO  GO:0030163;
GO  GO:0006508;
GO  GO:0030155;
GO  GO:0042659;
GO  GO:0040034;
GO  GO:0040012;
GO  GO:0031647;
GO  GO:0050807;
GO  GO:0040028;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMRQDRRSLLERNIMMFSSHLKVDEILEVLIAKQVLNSDNGDMINSCGTVREKRREIVKAVQRRGDVAFDAFYDALRSTG
SQ  HEGLAEVLEPLARSVDSNAVEFECPMSPASHRRSRALSPAGYTSPTRVHRDSVSSVSSFTSYQDIYSRARSRSRSRALHS
SQ  SDRHNYSSPPVNAFPSQPSSANSSFTGCSSLGYSSSRNRSFSKASGPTQYIFHEEDMNFVDAPTISRVFDEKTMYRNFSS
SQ  PRGMCLIINNEHFEQMPTRNGTKADKDNLTNLFRCMGYTVICKDNLTGRGMLLTIRDFAKHESHGDSAILVILSHGEENV
SQ  IIGVDDIPISTHEIYDLLNAANAPRLANKPKIVFVQACRGERRDNGFPVLDSVDGVPAFLRRGWDNRDGPLFNFLGCVRP
SQ  QVQQVWRKKPSQADILIAYATTAQYVSWRNSARGSWFIQAVCEVFSTHAKDMDVVELLTEVNKKVACGFQTSQGSNILKQ
SQ  MPEMTSRLLKKFYFWPEARNSAV
//
ID  P45436;
PN  Cell death protein 3 subunit p13;
GN  ced;
OS  31234;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P42573}. Perikaryon {ECO:0000250|UniProtKB:P42573}. Synapse {ECO:0000250|UniProtKB:P42573}. Mitochondrion {ECO:0000250|UniProtKB:P42573}. Cytoplasm {ECO:0000250|UniProtKB:P42573}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P42573}. Note=Colocalizes with nucleoporin npp- 14 to the perinuclear region in germ cells. Becomes diffused in the cytoplasm in apoptotic germ cells. Localizes to axonal mitochondria and synapses of DD motor neurons. Synaptic localization is dependent on axonal mitochondria. {ECO:0000250|UniProtKB:P42573}.
DR  UNIPROT: P45436;
DR  UNIPROT: E3M6B9;
DR  Pfam: PF00619;
DR  PROSITE: PS50209;
DR  PROSITE: PS01122;
DR  PROSITE: PS01121;
DR  PROSITE: PS50207;
DR  PROSITE: PS50208;
DE  Function: Acts as a cysteine protease in controlling programmed cell death (apoptosis) by proteolytically activating or inactivating a wide range of substrates. Component of the egl-1, ced-9, ced-4 and ced-3 apoptotic signaling cascade required for the initiation of programmed cell death in cells fated to die during embryonic and postembryonic development. During oogenesis, required for germline apoptosis downstream of ced-9 and ced-4 but independently of egl-1. By cleaving and activating ced-8, promotes phosphatidylserine exposure on the surface of apoptotic cells; phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment. By cleaving and converting dcr-1 into a deoxyribonuclease (DNase), promotes apoptotic chromosomal DNA fragmentation. By cleaving mitochondrial fission protein drp-1, may regulate the removal of mitochondria during apoptosis. During germline apoptosis, cleaves translation initiation factor ifg-1 (isoform p170) promoting cap-independent translation. During male tail morphogenesis, promotes apoptosis of the tail-spike cell downstream of ced-4 but independently of egl-1 and ced-9. By cleaving cnt-1, prevents the activation of the prosurvival akt-1/2 signaling pathway and thus promotes apoptosis. Downstream of ced-4, may play a role in sex- specific cell apoptosis by cleaving sex-determining protein fem-1. May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway. Cleaves ced-9 in vitro. Cleaves csp-2 isoform b resulting in the removal of the propeptide and the generation of csp-2 subunit p31 in vitro. Independently of its apoptotic role has additional functions. Probably by cleaving and thereby activating actin-severing protein gsnl-1, required for the elimination of transient presynaptic components during larval development downstream of egl-1, ced-9 and ced-4 pathway. Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), regulates temporal cell fate patterning during larval development. Acts in cell fate patterning by cleaving heterochronic protein lin-28, likely promoting its degradation. Also cleaves heterochronic protein lin-14 and exonuclease disl-2 in vitro. Downstream of calreticulin crt- 1 and ced-4 and independently of egl-1 and ced-9, plays a role in the initial steps of axonal regrowth following axotomy. Cleaves 14-3-3-like protein ftt-2, tubulin tbb-2 and calreticulin crt-1 in vitro. Plays also a role in resistance to S.typhimurium-mediated infection. {ECO:0000250|UniProtKB:P42573}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0008303;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0098793;
GO  GO:0008656;
GO  GO:0097200;
GO  GO:0042802;
GO  GO:0030042;
GO  GO:0097202;
GO  GO:1902742;
GO  GO:0050829;
GO  GO:0009792;
GO  GO:0046716;
GO  GO:1905803;
GO  GO:1900118;
GO  GO:1904747;
GO  GO:1905845;
GO  GO:0043525;
GO  GO:1901046;
GO  GO:0010954;
GO  GO:1905808;
GO  GO:0016540;
GO  GO:0030163;
GO  GO:0030155;
GO  GO:0042659;
GO  GO:0040034;
GO  GO:0040012;
GO  GO:0031647;
GO  GO:0040028;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMRQDRRNLLERNILVFSNKLQSEQILEVLIAKQILNADNGDVINSCRTERDKRKEIVKAVQRRGDVAFDAFYDALRDTG
SQ  HHELAAVLEPLARTIDFITPRDLECPMSPASHRRSRALSPSTFSSPTRVHRDSVSSVSSFTSTYQDVYTRARSTSRSSRP
SQ  LHASDRHNYVSPSNSFQSQPSSANSSFTGCSSLGYSSSRTRSYSKASAHSQYIFHEEDMNYVDAPTIHRVFDEKTMYRNF
SQ  STPRGLCLIINNEHFEQMPTRNGTKADKDNISNLFRCMGYIVHCKDNLTGRAMMLTIRDFAKNETHGDSAILVILSHGEE
SQ  NVIIGVDDVSVNVHEIYDLLNAANAPRLANKPKLVFVQACRGERRDNGFPVLDSVDGVPALIRPRGWDKGDGPLFNFLGC
SQ  VRPQAQQVWRKKPSQADILIAYATTAQYVSWRNSARGSWFIQAVCEVFSLHAKDMDVVELLTEVNKKVACGFQTSQGANI
SQ  LKQMPELTSRLLKKFYFWPEDRNRSSAV
//
ID  Q60Z52;
PN  Cell death protein 4;
GN  ced;
OS  6238;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion {ECO:0000250|UniProtKB:P30429}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P30429}. Note=In non cell death induced cells, ced-9 is required for mitochondrial localization. Perinuclear in cell death induced cells. {ECO:0000250|UniProtKB:P30429}.
DR  UNIPROT: Q60Z52;
DR  UNIPROT: A8XSP2;
DR  Pfam: PF00619;
DR  Pfam: PF00931;
DE  Function: Plays a major role in programmed cell death (PCD, apoptosis). egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to induce caspase ced-3 autoproteolytic cleavage and activation. Also forms an holoenzyme with processed ced-3 enhancing ced-3 activity. Component of the egl-1, ced-9, ced-4 and ced- 3 apoptotic signaling cascade required for the initiation of programmed cell death in cells fated to die during embryonic and postembryonic development. During oogenesis, required for germline apoptosis downstream of ced-9 and upstream of ced-3 but independently of egl-1. May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway. Regulates CEP neuron apoptosis in response to high Al(3+) levels. During male tail morphogenesis, promotes apoptosis of the tail-spike cell. During larval development, required for the elimination of transient presynaptic components downstream of egl-1 and ced-9 and upstream of ced-3 apoptotic pathway. Together with ain-1, a component of the miRNA- induced-silencing complex (miRISC), and probably upstream of ced-3, regulates temporal cell fate patterning during larval development. May play a role in resistance to S.typhimurium-mediated infection. {ECO:0000250|UniProtKB:P30429}.
DE  Reference Proteome: Yes;
GO  GO:0008303;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0051432;
GO  GO:0051434;
GO  GO:0089720;
GO  GO:0008656;
GO  GO:0061133;
GO  GO:0042802;
GO  GO:0000287;
GO  GO:0030042;
GO  GO:0097202;
GO  GO:0006915;
GO  GO:1902742;
GO  GO:0050829;
GO  GO:0009792;
GO  GO:0048598;
GO  GO:0046716;
GO  GO:0043066;
GO  GO:1900118;
GO  GO:0043065;
GO  GO:1904747;
GO  GO:0010954;
GO  GO:1905808;
GO  GO:0030155;
GO  GO:0008361;
GO  GO:0040034;
GO  GO:0031647;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLCEIECRALNAAHTMLIQDFEPRDALTYLEGEKIFTEDHSDLISNMPTRLERIANFLRAYRRQASELAPLIDFFEYNNQ
SQ  NHLKDFLDEYLWFATHQPDKLRPVVLVPKFSRQMLDRKLLLGNVPKQMNCFSREFHVDRVIEKLDEMCDLESFFLFLHGR
SQ  SGSGKSVIASQALSKSDQLIGINYDSVVWLKDSGTTPKATFDLFTDLLLMLKRARVVSDTDDSHNMPDFINRVLSRSEDD
SQ  LLNFPSVEHVTSVVLKRMIANALIDRPNTLFVLDDVVQEDTIRWAQELRLRCLITTRDVEISNAASPECEFIEVTPLESY
SQ  ECFELLESYGMPVPAIERDEDILHKTIDLTSGNPAALMMIFKSCEPKTFEKMAQLNSKLETRGLSAIECITPYCYKSLSS
SQ  SLQRCVEVLSDEDRSALAFAVIMPPGIDIPVKIWSCVIPVDICSNEEDQLDDEVADRLKRLSKRGALLSGKRSPVLTYKI
SQ  DHVIHLFLKHVVDVQTIANGISILEQRLHELGNNNTPTPERHMPSKFRRTSAGDMFPKVEDSVIRPEDYSKFMQIHRTFY
SQ  DSLKKFTSQ
//
ID  P30429;
PN  Cell death protein 4;
GN  ced;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}. Note=In non cell death induced cells, ced-9 is required for mitochondrial localization. Perinuclear in cell death induced cells. {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:9027313}.
DR  UNIPROT: P30429;
DR  UNIPROT: Q5BHI5;
DR  PDB: 2A5Y;
DR  PDB: 3LQQ;
DR  PDB: 3LQR;
DR  PDB: 4M9S;
DR  PDB: 4M9X;
DR  PDB: 4M9Y;
DR  PDB: 4M9Z;
DR  Pfam: PF00619;
DR  Pfam: PF00931;
DR  PROSITE: PS50209;
DE  Function: Component of the egl-1, ced-9, ced-4 and ced-3 apoptotic signaling cascade required for the initiation of programmed cell death in cells fated to die during embryonic and postembryonic development (PubMed:3955651). During oogenesis, required for germline apoptosis downstream of ced-9 and upstream of ced-3 but independently of egl-1 (PubMed:9927601). May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway (PubMed:21901106). Regulates CEP neuron apoptosis in response to high Al(3+) levels (PubMed:23106139). During male tail morphogenesis, promotes apoptosis of the tail-spike cell upstream of ced-3 but independently of egl-1 and ced-9 (PubMed:17329362). May play a role in sex-specific cell apoptosis, probably by promoting ced-3-mediated cleavage of sex-determining protein fem-1 (PubMed:10764728). During larval development, required for the elimination of transient presynaptic components downstream of egl-1 and ced-9 and upstream of ced-3 apoptotic pathway (PubMed:26074078). Downstream of calreticulin crt-1 and upstream of ced-3 and independently of egl-1 and ced-9, plays a role in the initial steps of axonal regrowth following axotomy (PubMed:22629231). Together with ain-1, a component of the miRNA- induced-silencing complex (miRISC), and probably upstream of ced-3, regulates temporal cell fate patterning during larval development (PubMed:25432023). May play a role in resistance to S.typhimurium- mediated infection (PubMed:11226309). {ECO:0000269|PubMed:10764728, ECO:0000269|PubMed:11226309, ECO:0000269|PubMed:17329362, ECO:0000269|PubMed:21901106, ECO:0000269|PubMed:22629231, ECO:0000269|PubMed:23106139, ECO:0000269|PubMed:25432023, ECO:0000269|PubMed:26074078, ECO:0000269|PubMed:3955651, ECO:0000269|PubMed:9927601}. [Isoform a]: Plays a major role in programmed cell death (PubMed:1286611, PubMed:8706125). egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to induce caspase ced-3 autoproteolytic cleavage and activation (PubMed:15383288, PubMed:16208361, PubMed:20434985, PubMed:24065769). Also forms a holoenzyme with processed ced-3 enhancing ced-3 activity (PubMed:20434985). {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:1286611, ECO:0000269|PubMed:15383288, ECO:0000269|PubMed:16208361, ECO:0000269|PubMed:20434985, ECO:0000269|PubMed:24065769, ECO:0000269|PubMed:8706125}. [Isoform b]: Prevents programmed cell death. {ECO:0000269|PubMed:8706125}.
DE  Reference Proteome: Yes;
DE  Interaction: P41958; IntAct: EBI-494126; Score: 0.84
DE  Interaction: Q07817; IntAct: EBI-494146; Score: 0.40
DE  Interaction: P42573; IntAct: EBI-494268; Score: 0.86
DE  Interaction: O61667; IntAct: EBI-11688070; Score: 0.35
DE  Interaction: P30429; IntAct: EBI-2655126; Score: 0.44
DE  Interaction: Q20924; IntAct: EBI-15599089; Score: 0.56
DE  Interaction: Q14790; IntAct: EBI-16211709; Score: 0.40
DE  Interaction: Q9NAG4; IntAct: EBI-16587288; Score: 0.57
GO  GO:0008303;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0051432;
GO  GO:0051434;
GO  GO:0089720;
GO  GO:0008656;
GO  GO:0061133;
GO  GO:0042802;
GO  GO:0000287;
GO  GO:0016505;
GO  GO:0030042;
GO  GO:0097202;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:1902742;
GO  GO:0050829;
GO  GO:0009792;
GO  GO:0048598;
GO  GO:0046716;
GO  GO:0043066;
GO  GO:1900118;
GO  GO:0043065;
GO  GO:1904747;
GO  GO:2001056;
GO  GO:0010954;
GO  GO:1905808;
GO  GO:0030155;
GO  GO:0008361;
GO  GO:0043281;
GO  GO:0040034;
GO  GO:0031647;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLCEIECRALSTAHTRLIHDFEPRDALTYLEGKNIFTEDHSELISKMSTRLERIANFLRIYRRQASELGPLIDFFNYNNQ
SQ  SHLADFLEDYIDFAINEPDLLRPVVIAPQFSRQMLDRKLLLGNVPKQMTCYIREYHVDRVIKKLDEMCDLDSFFLFLHGR
SQ  AGSGKSVIASQALSKSDQLIGINYDSIVWLKDSGTAPKSTFDLFTDILLMLARVVSDTDDSHSITDFINRVLSRSEDDLL
SQ  NFPSVEHVTSVVLKRMICNALIDRPNTLFVFDDVVQEETIRWAQELRLRCLVTTRDVEISNAASQTCEFIEVTSLEIDEC
SQ  YDFLEAYGMPMPVGEKEEDVLNKTIELSSGNPATLMMFFKSCEPKTFEKMAQLNNKLESRGLVGVECITPYSYKSLAMAL
SQ  QRCVEVLSDEDRSALAFAVVMPPGVDIPVKLWSCVIPVDICSNEEEQLDDEVADRLKRLSKRGALLSGKRMPVLTFKIDH
SQ  IIHMFLKHVVDAQTIANGISILEQRLLEIGNNNVSVPERHIPSHFQKFRRSSASEMYPKTTEETVIRPEDFPKFMQLHQK
SQ  FYDSLKNFACC
//
ID  P49454;
PN  Centromere protein F;
GN  CENPF;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus matrix. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Relocalizes to the kinetochore/centromere (coronal surface of the outer plate) and the spindle during mitosis. Observed in nucleus during interphase but not in the nucleolus. At metaphase becomes localized to areas including kinetochore and mitotic apparatus as well as cytoplasm. By telophase, is concentrated within the intracellular bridge at either side of the mid-body.
DR  UNIPROT: P49454;
DR  UNIPROT: Q13171;
DR  UNIPROT: Q13246;
DR  UNIPROT: Q5VVM7;
DR  Pfam: PF10490;
DR  Pfam: PF10473;
DR  Pfam: PF10481;
DR  OMIM: 243605;
DR  OMIM: 600236;
DR  DisGeNET: 1063;
DE  Function: Required for kinetochore function and chromosome segregation in mitosis. Required for kinetochore localization of dynein, LIS1, NDE1 and NDEL1. Regulates recycling of the plasma membrane by acting as a link between recycling vesicles and the microtubule network though its association with STX4 and SNAP25. Acts as a potential inhibitor of pocket protein-mediated cellular processes during development by regulating the activity of RB proteins during cell division and proliferation. May play a regulatory or permissive role in the normal embryonic cardiomyocyte cell cycle and in promoting continued mitosis in transformed, abnormally dividing neonatal cardiomyocytes. Interaction with RB directs embryonic stem cells toward a cardiac lineage. Involved in the regulation of DNA synthesis and hence cell cycle progression, via its C-terminus. Has a potential role regulating skeletal myogenesis and in cell differentiation in embryogenesis. Involved in dendritic cell regulation of T-cell immunity against chlamydia. {ECO:0000269|PubMed:12974617, ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:7542657, ECO:0000269|PubMed:7651420}.
DE  Disease: Stromme syndrome (STROMS) [MIM:243605]: An autosomal recessive congenital disorder characterized by intestinal atresia, ocular anomalies, microcephaly, and renal and cardiac abnormalities in some patients. The disease has features of a ciliopathy, and lethality in early childhood is observed in severe cases. {ECO:0000269|PubMed:25564561, ECO:0000269|PubMed:26820108}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: P43034; IntAct: EBI-2298103; Score: 0.35
DE  Interaction: Q15714; IntAct: EBI-1083967; Score: 0.00
DE  Interaction: Q9GZM8; IntAct: EBI-2295215; Score: 0.75
DE  Interaction: Q8WUM0; IntAct: EBI-7328986; Score: 0.48
DE  Interaction: P57740; IntAct: EBI-7329356; Score: 0.35
DE  Interaction: Q02224; IntAct: EBI-1375056; Score: 0.37
DE  Interaction: P32121; IntAct: EBI-1642843; Score: 0.35
DE  Interaction: Q9NXR1; IntAct: EBI-2298075; Score: 0.40
DE  Interaction: A2AUM9; IntAct: EBI-2563733; Score: 0.40
DE  Interaction: O46385; IntAct: EBI-7872444; Score: 0.37
DE  Interaction: O00257; IntAct: EBI-3951698; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6515052; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q7TSY8; IntAct: EBI-11011396; Score: 0.35
DE  Interaction: Q8BZQ7; IntAct: EBI-11026803; Score: 0.35
DE  Interaction: Q96FF9; IntAct: EBI-11027063; Score: 0.35
DE  Interaction: P63005; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: P70399; IntAct: EBI-11051507; Score: 0.35
DE  Interaction: Q9QYY8; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q99PT9; IntAct: EBI-11092405; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-11105437; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-11106283; Score: 0.35
DE  Interaction: Q08AG7; IntAct: EBI-11108327; Score: 0.35
DE  Interaction: Q8CI51; IntAct: EBI-11124806; Score: 0.35
DE  Interaction: P25963; IntAct: EBI-11133856; Score: 0.35
DE  Interaction: Q9Y253; IntAct: EBI-11141689; Score: 0.35
DE  Interaction: Q71F23; IntAct: EBI-11156542; Score: 0.35
DE  Interaction: Q9UQN3; IntAct: EBI-11510767; Score: 0.37
DE  Interaction: P49356; IntAct: EBI-21502393; Score: 0.35
DE  Interaction: Q96KS9; IntAct: EBI-21503766; Score: 0.35
DE  Interaction: Q8TDR4; IntAct: EBI-21617027; Score: 0.35
DE  Interaction: Q96A37; IntAct: EBI-21627270; Score: 0.35
DE  Interaction: Q9Y2V7; IntAct: EBI-21673529; Score: 0.35
DE  Interaction: Q8N5R6; IntAct: EBI-21699069; Score: 0.35
DE  Interaction: Q9H2F9; IntAct: EBI-21702403; Score: 0.35
DE  Interaction: Q9Y6K9; IntAct: EBI-21708976; Score: 0.35
DE  Interaction: Q9HD26; IntAct: EBI-21720201; Score: 0.35
DE  Interaction: Q96T17; IntAct: EBI-21796065; Score: 0.35
DE  Interaction: Q9UKA1; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q96EY4; IntAct: EBI-21806027; Score: 0.35
DE  Interaction: Q96AP7; IntAct: EBI-21848470; Score: 0.35
DE  Interaction: Q9UPY6; IntAct: EBI-21852540; Score: 0.35
DE  Interaction: Q96JN8; IntAct: EBI-16814395; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: P30040; IntAct: EBI-20902848; Score: 0.40
DE  Interaction: Q9BYW2; IntAct: EBI-20911906; Score: 0.40
DE  Interaction: Q02539; IntAct: EBI-20938636; Score: 0.40
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21370473; Score: 0.00
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: Q8N612; IntAct: EBI-34574737; Score: 0.27
GO  GO:0005930;
GO  GO:0005813;
GO  GO:0000775;
GO  GO:0036064;
GO  GO:0097539;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0016363;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000940;
GO  GO:0048471;
GO  GO:0045120;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0003682;
GO  GO:0140297;
GO  GO:0070840;
GO  GO:0008017;
GO  GO:0008022;
GO  GO:0042803;
GO  GO:0030154;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0071897;
GO  GO:0001822;
GO  GO:0051382;
GO  GO:0051310;
GO  GO:0000278;
GO  GO:0007094;
GO  GO:0007517;
GO  GO:0045892;
GO  GO:0015031;
GO  GO:0010389;
GO  GO:0016202;
GO  GO:0009410;
GO  GO:0021591;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10852915};
SQ  MSWALEEWKEGLPTRALQKIQELEGQLDKLKKEKQQRQFQLDSLEAALQKQKQKVENEKTEGTNLKRENQRLMEICESLE
SQ  KTKQKISHELQVKESQVNFQEGQLNSGKKQIEKLEQELKRCKSELERSQQAAQSADVSLNPCNTPQKIFTTPLTPSQYYS
SQ  GSKYEDLKEKYNKEVEERKRLEAEVKALQAKKASQTLPQATMNHRDIARHQASSSVFSWQQEKTPSHLSSNSQRTPIRRD
SQ  FSASYFSGEQEVTPSRSTLQIGKRDANSSFFDNSSSPHLLDQLKAQNQELRNKINELELRLQGHEKEMKGQVNKFQELQL
SQ  QLEKAKVELIEKEKVLNKCRDELVRTTAQYDQASTKYTALEQKLKKLTEDLSCQRQNAESARCSLEQKIKEKEKEFQEEL
SQ  SRQQRSFQTLDQECIQMKARLTQELQQAKNMHNVLQAELDKLTSVKQQLENNLEEFKQKLCRAEQAFQASQIKENELRRS
SQ  MEEMKKENNLLKSHSEQKAREVCHLEAELKNIKQCLNQSQNFAEEMKAKNTSQETMLRDLQEKINQQENSLTLEKLKLAV
SQ  ADLEKQRDCSQDLLKKREHHIEQLNDKLSKTEKESKALLSALELKKKEYEELKEEKTLFSCWKSENEKLLTQMESEKENL
SQ  QSKINHLETCLKTQQIKSHEYNERVRTLEMDRENLSVEIRNLHNVLDSKSVEVETQKLAYMELQQKAEFSDQKHQKEIEN
SQ  MCLKTSQLTGQVEDLEHKLQLLSNEIMDKDRCYQDLHAEYESLRDLLKSKDASLVTNEDHQRSLLAFDQQPAMHHSFANI
SQ  IGEQGSMPSERSECRLEADQSPKNSAILQNRVDSLEFSLESQKQMNSDLQKQCEELVQIKGEIEENLMKAEQMHQSFVAE
SQ  TSQRISKLQEDTSAHQNVVAETLSALENKEKELQLLNDKVETEQAEIQELKKSNHLLEDSLKELQLLSETLSLEKKEMSS
SQ  IISLNKREIEELTQENGTLKEINASLNQEKMNLIQKSESFANYIDEREKSISELSDQYKQEKLILLQRCEETGNAYEDLS
SQ  QKYKAAQEKNSKLECLLNECTSLCENRKNELEQLKEAFAKEHQEFLTKLAFAEERNQNLMLELETVQQALRSEMTDNQNN
SQ  SKSEAGGLKQEIMTLKEEQNKMQKEVNDLLQENEQLMKVMKTKHECQNLESEPIRNSVKERESERNQCNFKPQMDLEVKE
SQ  ISLDSYNAQLVQLEAMLRNKELKLQESEKEKECLQHELQTIRGDLETSNLQDMQSQEISGLKDCEIDAEEKYISGPHELS
SQ  TSQNDNAHLQCSLQTTMNKLNELEKICEILQAEKYELVTELNDSRSECITATRKMAEEVGKLLNEVKILNDDSGLLHGEL
SQ  VEDIPGGEFGEQPNEQHPVSLAPLDESNSYEHLTLSDKEVQMHFAELQEKFLSLQSEHKILHDQHCQMSSKMSELQTYVD
SQ  SLKAENLVLSTNLRNFQGDLVKEMQLGLEEGLVPSLSSSCVPDSSSLSSLGDSSFYRALLEQTGDMSLLSNLEGAVSANQ
SQ  CSVDEVFCSSLQEENLTRKETPSAPAKGVEELESLCEVYRQSLEKLEEKMESQGIMKNKEIQELEQLLSSERQELDCLRK
SQ  QYLSENEQWQQKLTSVTLEMESKLAAEKKQTEQLSLELEVARLQLQGLDLSSRSLLGIDTEDAIQGRNESCDISKEHTSE
SQ  TTERTPKHDVHQICDKDAQQDLNLDIEKITETGAVKPTGECSGEQSPDTNYEPPGEDKTQGSSECISELSFSGPNALVPM
SQ  DFLGNQEDIHNLQLRVKETSNENLRLLHVIEDRDRKVESLLNEMKELDSKLHLQEVQLMTKIEACIELEKIVGELKKENS
SQ  DLSEKLEYFSCDHQELLQRVETSEGLNSDLEMHADKSSREDIGDNVAKVNDSWKERFLDVENELSRIRSEKASIEHEALY
SQ  LEADLEVVQTEKLCLEKDNENKQKVIVCLEEELSVVTSERNQLRGELDTMSKKTTALDQLSEKMKEKTQELESHQSECLH
SQ  CIQVAEAEVKEKTELLQTLSSDVSELLKDKTHLQEKLQSLEKDSQALSLTKCELENQIAQLNKEKELLVKESESLQARLS
SQ  ESDYEKLNVSKALEAALVEKGEFALRLSSTQEEVHQLRRGIEKLRVRIEADEKKQLHIAEKLKERERENDSLKDKVENLE
SQ  RELQMSEENQELVILDAENSKAEVETLKTQIEEMARSLKVFELDLVTLRSEKENLTKQIQEKQGQLSELDKLLSSFKSLL
SQ  EEKEQAEIQIKEESKTAVEMLQNQLKELNEAVAALCGDQEIMKATEQSLDPPIEEEHQLRNSIEKLRARLEADEKKQLCV
SQ  LQQLKESEHHADLLKGRVENLERELEIARTNQEHAALEAENSKGEVETLKAKIEGMTQSLRGLELDVVTIRSEKENLTNE
SQ  LQKEQERISELEIINSSFENILQEKEQEKVQMKEKSSTAMEMLQTQLKELNERVAALHNDQEACKAKEQNLSSQVECLEL
SQ  EKAQLLQGLDEAKNNYIVLQSSVNGLIQEVEDGKQKLEKKDEEISRLKNQIQDQEQLVSKLSQVEGEHQLWKEQNLELRN
SQ  LTVELEQKIQVLQSKNASLQDTLEVLQSSYKNLENELELTKMDKMSFVEKVNKMTAKETELQREMHEMAQKTAELQEELS
SQ  GEKNRLAGELQLLLEEIKSSKDQLKELTLENSELKKSLDCMHKDQVEKEGKVREEIAEYQLRLHEAEKKHQALLLDTNKQ
SQ  YEVEIQTYREKLTSKEECLSSQKLEIDLLKSSKEELNNSLKATTQILEELKKTKMDNLKYVNQLKKENERAQGKMKLLIK
SQ  SCKQLEEEKEILQKELSQLQAAQEKQKTGTVMDTKVDELTTEIKELKETLEEKTKEADEYLDKYCSLLISHEKLEKAKEM
SQ  LETQVAHLCSQQSKQDSRGSPLLGPVVPGPSPIPSVTEKRLSSGQNKASGKRQRSSGIWENGRGPTPATPESFSKKSKKA
SQ  VMSGIHPAEDTEGTEFEPEGLPEVVKKGFADIPTGKTSPYILRRTTMATRTSPRLAAQKLALSPLSLGKENLAESSKPTA
SQ  GGSRSQKVKVAQRSPVDSGTILREPTTKSVPVNNLPERSPTDSPREGLRVKRGRLVPSPKAGLESNGSENCKVQ
//
ID  Q5ZKD1;
PN  Choline/ethanolaminephosphotransferase 1;
GN  CEPT1;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y6K0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y6K0}.
DR  UNIPROT: Q5ZKD1;
DR  Pfam: PF01066;
DR  PROSITE: PS00379;
DE  Function: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity. {ECO:0000250|UniProtKB:Q9Y6K0}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0047359;
GO  GO:0004142;
GO  GO:0004307;
GO  GO:0046872;
GO  GO:0006646;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGHRNLKRRCGESHLESPAGCAHGPAAACVLSKLVQLPTPPLSKHQLKRLEEHKYQSAGRSLLEPLMQGYWEWLVGKVP
SQ  AWIAPNLITIIGLLINIFTTLLLVYYCPTATEQAPPWAYIACACGLFIYQSLDTIDGKQARRTNSSTPLGELFDHGCDSL
SQ  STVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSLIP
SQ  ILNIQVKIFPALCTVAGTIFSCTNYFGVIFTGGVGKNGSTIAGTSVLSPFLHIGSVIALAAMIYKKSAVQLFEKHPCLYI
SQ  LTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALIFSLFDLLRYCVSVCNQIAAHLH
SQ  IHVFRIKSSSTHSNHH
//
ID  Q9Y6K0;
PN  Choline/ethanolaminephosphotransferase 1;
GN  CEPT1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein {ECO:0000269|PubMed:12221122}. Nucleus membrane {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein {ECO:0000269|PubMed:12221122}.
DR  UNIPROT: Q9Y6K0;
DR  UNIPROT: Q69YJ9;
DR  UNIPROT: Q9P0Y8;
DR  Pfam: PF01066;
DR  PROSITE: PS00379;
DR  OMIM: 616751;
DR  DisGeNET: 10390;
DE  Function: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity. {ECO:0000269|PubMed:10191259, ECO:0000269|PubMed:10893425, ECO:0000269|PubMed:12216837}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q6ZRP7; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q921T2; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.35
DE  Interaction: A0A384KHP8; IntAct: EBI-2873575; Score: 0.00
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: Q16659; IntAct: EBI-12502733; Score: 0.35
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: P60953; IntAct: EBI-11002356; Score: 0.35
DE  Interaction: P19784; IntAct: EBI-11002671; Score: 0.35
DE  Interaction: Q99JP4; IntAct: EBI-11005491; Score: 0.35
DE  Interaction: Q96SB8; IntAct: EBI-11007096; Score: 0.35
DE  Interaction: Q14807; IntAct: EBI-11033337; Score: 0.35
DE  Interaction: Q7Z406; IntAct: EBI-11033498; Score: 0.35
DE  Interaction: O88441; IntAct: EBI-11096794; Score: 0.35
DE  Interaction: O96008; IntAct: EBI-11113522; Score: 0.35
DE  Interaction: Q9D7F7; IntAct: EBI-11116442; Score: 0.35
DE  Interaction: Q6NZB1; IntAct: EBI-11119708; Score: 0.35
DE  Interaction: P62191; IntAct: EBI-11123102; Score: 0.35
DE  Interaction: P54368; IntAct: EBI-11123446; Score: 0.35
DE  Interaction: Q7LFX5; IntAct: EBI-11123526; Score: 0.35
DE  Interaction: P70335; IntAct: EBI-11124658; Score: 0.35
DE  Interaction: O43379; IntAct: EBI-11127003; Score: 0.35
DE  Interaction: Q969M3; IntAct: EBI-11127233; Score: 0.35
DE  Interaction: Q9NYU2; IntAct: EBI-11127729; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-11132927; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135399; Score: 0.35
DE  Interaction: Q9NZD8; IntAct: EBI-24511333; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-25231884; Score: 0.56
DE  Interaction: Q8N6H7; IntAct: EBI-21875078; Score: 0.35
DE  Interaction: P78332; IntAct: EBI-21875078; Score: 0.35
DE  Interaction: P55196; IntAct: EBI-21875078; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P19419; IntAct: EBI-25378580; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27049069; Score: 0.27
DE  Interaction: Q9H5K3; IntAct: EBI-28948637; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-32719716; Score: 0.35
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0047359;
GO  GO:0004142;
GO  GO:0004307;
GO  GO:0046872;
GO  GO:0006629;
GO  GO:0006646;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVRRVP
SQ  SWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSL
SQ  STVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIP
SQ  VLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAAMIYKKSAVQLFEKHPCLYI
SQ  LTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLH
SQ  IHVFRIKVSTAHSNHH
//
ID  Q8BGS7;
PN  Choline/ethanolaminephosphotransferase 1;
GN  Cept1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y6K0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y6K0}.
DR  UNIPROT: Q8BGS7;
DR  UNIPROT: Q8VC64;
DR  Pfam: PF01066;
DR  PROSITE: PS00379;
DE  Function: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity. {ECO:0000250|UniProtKB:Q9Y6K0}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0047359;
GO  GO:0004142;
GO  GO:0004307;
GO  GO:0046872;
GO  GO:0016780;
GO  GO:0006656;
GO  GO:0006646;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVGRVP
SQ  SWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSL
SQ  STVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIP
SQ  VLNIQMKLLPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAVMIYKKSAVQLFEKHPCLYI
SQ  LTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALIFSFFDLIRYCVSVCNQIASHLH
SQ  IHVFRIKASTAHSNHH
//
ID  Q6AXM5;
PN  Choline/ethanolaminephosphotransferase 1;
GN  Cept1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y6K0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y6K0}.
DR  UNIPROT: Q6AXM5;
DR  Pfam: PF01066;
DR  PROSITE: PS00379;
DE  Function: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity. {ECO:0000250|UniProtKB:Q9Y6K0}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0047359;
GO  GO:0004142;
GO  GO:0004307;
GO  GO:0046872;
GO  GO:0016780;
GO  GO:0006656;
GO  GO:0006646;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGHRSTRKRCGDSHPESPVGFGHMSTTGCILNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVGRVP
SQ  SWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSL
SQ  STVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIP
SQ  VLNIQMKLFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAVMIYKKSAVQLFEKHPCLYI
SQ  LTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLH
SQ  IHVFRIKTSTAHSNHH
//
ID  Q7ZYQ3;
PN  Choline/ethanolaminephosphotransferase 1;
GN  cept1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y6K0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y6K0}.
DR  UNIPROT: Q7ZYQ3;
DR  Pfam: PF01066;
DR  PROSITE: PS00379;
DE  Function: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity. {ECO:0000250|UniProtKB:Q9Y6K0}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0047359;
GO  GO:0004142;
GO  GO:0004307;
GO  GO:0046872;
GO  GO:0006646;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAQRAAKRRTGDFHSEFPSSCGNPYQTACLLSKFIELPNPPLSRHQLKRLEEHRYQSCGKSLLEPLMQGFWEWLVIQVP
SQ  QWIAPNLITIIGLLINIVTTVVLIYYCPTATEKAPTWTYLSCAIGLFMYQSLDAIDGKQARRTNSSTPLGELFDHGCDSL
SQ  STVFVVLGTCIAVQLGTNPDWMFFCCFAGMFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAAIGGPTLWLSMIP
SQ  VLNVPMKLFPALCTVAGTVFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPMLHIGSVIVLATMIYKKSSVQLFEKHPCLYI
SQ  LTFGFVSAKVTNKLVVAHMTKSEMHLHDSAFIGPALLFLNQYFNSFIDEYLVLWIALVLSLIDLIRYSVSVCNQIASHLH
SQ  IEVFRIKTKMARFNHH
//
ID  Q28H54;
PN  Choline/ethanolaminephosphotransferase 1;
GN  cept1;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y6K0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y6K0}.
DR  UNIPROT: Q28H54;
DR  Pfam: PF01066;
DR  PROSITE: PS00379;
DE  Function: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity. {ECO:0000250|UniProtKB:Q9Y6K0}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0047359;
GO  GO:0004142;
GO  GO:0004307;
GO  GO:0046872;
GO  GO:0006646;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGQRAAKRRTGDLHTEFPTSCGNPYQTACLLSKFIELPTPPLTRHQLKRLEEHRYQSCGKSLLEPIMQGFWEWLVEQVP
SQ  QWIAPNLITIIGLLINIITTVVLVYYCPTATEKAPTWTYLSCAIGLFIYQSLDAIDGKQARRTNSSTPLGELFDHGCDSL
SQ  STVFVVLGTCIAVQLGTNPDWMFFCCFAGMFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAAIGGPTLWLSMIP
SQ  VLNVPMKLFPALCTVAGTVFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPMLHIGSVIVLATMIYKKSSVQLFEKHPCLYI
SQ  LTFGFVSAKVTNKLVVAHMTKSEMHLHDSAFIGPALLFLNQYFNSFIDEHLVLWIALVLSFIDLIRYSVSICNQIASHLH
SQ  IEVFRIKTKVARFNHH
//
ID  Q2TBN3;
PN  Centrin-2;
GN  CETN2;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P41208}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P41208}. Nucleus {ECO:0000250|UniProtKB:P41208}. Nucleus envelope {ECO:0000250|UniProtKB:P41208}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P41208}.
DR  UNIPROT: Q2TBN3;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110 (By similarity). {ECO:0000250}. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer (By similarity). {ECO:0000250}. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (By similarity). {ECO:0000250}. As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. {ECO:0000250|UniProtKB:P41208}.
DE  Reference Proteome: Yes;
GO  GO:0097729;
GO  GO:0045177;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0044615;
GO  GO:0032391;
GO  GO:0070390;
GO  GO:0071942;
GO  GO:0005509;
GO  GO:0031683;
GO  GO:0032795;
GO  GO:0008017;
GO  GO:0051301;
GO  GO:0007099;
GO  GO:0000278;
GO  GO:0051028;
GO  GO:0006289;
GO  GO:0015031;
GO  GO:0032465;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASNFKKANMASTTQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEG
SQ  TGKMNFSDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLSDEELQEMIDEADRDGDGEVNEQ
SQ  EFLRIMKKTSLY
//
ID  P41208;
PN  Centrin-2;
GN  CETN2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23591820}. Nucleus envelope {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Nucleus {ECO:0000305}.
DR  UNIPROT: P41208;
DR  UNIPROT: B2R4T4;
DR  UNIPROT: Q53XW1;
DR  PDB: 1M39;
DR  PDB: 1ZMZ;
DR  PDB: 2A4J;
DR  PDB: 2GGM;
DR  PDB: 2K2I;
DR  PDB: 2OBH;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 300006;
DR  DisGeNET: 1069;
DE  Function: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. {ECO:0000269|PubMed:22307388, ECO:0000305|PubMed:23591820}.
DE  Reference Proteome: Yes;
DE  Interaction: O43303; IntAct: EBI-1789852; Score: 0.52
DE  Interaction: Q70CQ1; IntAct: EBI-2512828; Score: 0.40
DE  Interaction: Q9H0E7; IntAct: EBI-2513724; Score: 0.59
DE  Interaction: Q9R1K9; IntAct: EBI-2561097; Score: 0.40
DE  Interaction: A8K8P3; IntAct: EBI-2659498; Score: 0.65
DE  Interaction: P15289; IntAct: EBI-3904577; Score: 0.37
DE  Interaction: Q96LA8; IntAct: EBI-3915269; Score: 0.37
DE  Interaction: P54727; IntAct: EBI-4567671; Score: 0.57
DE  Interaction: Q01831; IntAct: EBI-4567671; Score: 0.78
DE  Interaction: Q2NKQ1; IntAct: EBI-10208385; Score: 0.72
DE  Interaction: Q8NA72; IntAct: EBI-10208397; Score: 0.80
DE  Interaction: Q96PV4; IntAct: EBI-10208407; Score: 0.56
DE  Interaction: Q6P5D4; IntAct: EBI-10991106; Score: 0.35
DE  Interaction: P52732; IntAct: EBI-11007621; Score: 0.35
DE  Interaction: Q6PD62; IntAct: EBI-11013551; Score: 0.35
DE  Interaction: Q99598; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P48754; IntAct: EBI-11097282; Score: 0.35
DE  Interaction: O88286; IntAct: EBI-11104133; Score: 0.35
DE  Interaction: Q3V6T2; IntAct: EBI-11141559; Score: 0.35
DE  Interaction: P29341; IntAct: EBI-11149873; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-11152836; Score: 0.35
DE  Interaction: O14640; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: Q8N0X7; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: P53680; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: P50991; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: P49368; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: P20290; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: Q99832; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: Q9UNY4; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: Q16513; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: Q9BYS8; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: P78371; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: P48643; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: P17987; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: Q8WUY9; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: Q9NYP9; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: P40227; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: P35606; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: O14737; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: Q8WU90; IntAct: EBI-11382084; Score: 0.27
DE  Interaction: P56945; IntAct: EBI-15099687; Score: 0.35
DE  Interaction: Q12798; IntAct: EBI-21576600; Score: 0.35
DE  Interaction: P16104; IntAct: EBI-21578956; Score: 0.35
DE  Interaction: Q96A08; IntAct: EBI-21579454; Score: 0.35
DE  Interaction: O14874; IntAct: EBI-21725538; Score: 0.53
DE  Interaction: Q5VW00; IntAct: EBI-21725806; Score: 0.35
DE  Interaction: P08887; IntAct: EBI-21731028; Score: 0.35
DE  Interaction: Q8IW19; IntAct: EBI-21791365; Score: 0.35
DE  Interaction: Q6ZNE5; IntAct: EBI-21819923; Score: 0.35
DE  Interaction: Q9BQ69; IntAct: EBI-21827171; Score: 0.35
DE  Interaction: Q96DD0; IntAct: EBI-21832541; Score: 0.35
DE  Interaction: Q9NTX7; IntAct: EBI-21839807; Score: 0.35
DE  Interaction: P15927; IntAct: EBI-21839521; Score: 0.35
DE  Interaction: Q0VDD8; IntAct: EBI-21849985; Score: 0.35
DE  Interaction: Q8NEE6; IntAct: EBI-21867658; Score: 0.40
DE  Interaction: P42858; IntAct: EBI-21132926; Score: 0.67
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q16526; IntAct: EBI-21981854; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
GO  GO:0097729;
GO  GO:0045177;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005829;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0032391;
GO  GO:0070390;
GO  GO:0071942;
GO  GO:0005509;
GO  GO:0031683;
GO  GO:0032795;
GO  GO:0008017;
GO  GO:0051301;
GO  GO:0007099;
GO  GO:0000278;
GO  GO:0051028;
GO  GO:0006289;
GO  GO:0015031;
GO  GO:0032465;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASNFKKANMASSSQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEG
SQ  TGKMNFGDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVSEQ
SQ  EFLRIMKKTSLY
//
ID  Q9R1K9;
PN  Centrin-2;
GN  Cetn2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P41208}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:11250075}. Nucleus {ECO:0000250|UniProtKB:P41208}. Nucleus envelope {ECO:0000250|UniProtKB:P41208}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P41208}.
DR  UNIPROT: Q9R1K9;
DR  UNIPROT: B1AUQ6;
DR  UNIPROT: B1AUQ8;
DR  UNIPROT: Q3UBB4;
DR  UNIPROT: Q9CWM0;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110 (By similarity). {ECO:0000250}. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with Rad23b appears to stabilize Xpc. In vitro, stimulates DNA binding of the Xpc:Rad23b dimer (By similarity). {ECO:0000250}. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, Xpa, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (By similarity). {ECO:0000250}. As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. {ECO:0000250|UniProtKB:P41208}.
DE  Reference Proteome: Yes;
DE  Interaction: O15182; IntAct: EBI-2561097; Score: 0.40
DE  Interaction: O60318; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: P41208; IntAct: EBI-2561097; Score: 0.40
DE  Interaction: Q14974; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: Q8NA72; IntAct: EBI-2561097; Score: 0.56
DE  Interaction: P54727; IntAct: EBI-2561097; Score: 0.40
DE  Interaction: Q01831; IntAct: EBI-2561097; Score: 0.56
DE  Interaction: P54728; IntAct: EBI-4567934; Score: 0.35
DE  Interaction: P20263; IntAct: EBI-5240764; Score: 0.35
DE  Interaction: Q92738; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: Q15154; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: P20226; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: P35221; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: O75340; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: Q9UPN4; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: E5RK82; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: P28289; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: Q6P597; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: P30044; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: F5H4F1; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: A8K8P3; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: O60879; IntAct: EBI-11112667; Score: 0.35
DE  Interaction: Q92917; IntAct: EBI-11112667; Score: 0.35
DE  Interaction: Q8IXQ4; IntAct: EBI-11112667; Score: 0.35
DE  Interaction: O75923; IntAct: EBI-11112667; Score: 0.35
DE  Interaction: Q3V6T2; IntAct: EBI-11112667; Score: 0.35
DE  Interaction: Q04837; IntAct: EBI-11112667; Score: 0.35
DE  Interaction: Q9BYT8; IntAct: EBI-11112667; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-11112667; Score: 0.35
DE  Interaction: Q8IWJ2; IntAct: EBI-11112667; Score: 0.35
DE  Interaction: Q08AD1; IntAct: EBI-11112667; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26473140; Score: 0.35
GO  GO:0097729;
GO  GO:0045177;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005929;
GO  GO:0005737;
GO  GO:0044615;
GO  GO:0032391;
GO  GO:0070390;
GO  GO:0071942;
GO  GO:0005509;
GO  GO:0031683;
GO  GO:0032795;
GO  GO:0008017;
GO  GO:0051301;
GO  GO:0007099;
GO  GO:0000278;
GO  GO:0051028;
GO  GO:0006289;
GO  GO:0015031;
GO  GO:0032465;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASNFKKTTMASSAQRKRMSPKPELTEDQKQEIREAFDLFDADGTGTIDIKELKVAMRALGFEPKKEEIKKMISEIDKEG
SQ  TGKMNFSDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVNEQ
SQ  EFLRIMKKTSLY
//
ID  O15182;
PN  Centrin-3;
GN  CETN3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:9256449}. Nucleus, nucleolus {ECO:0000303|PubMed:22307388}. Nucleus envelope {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:26337392}. Note=Centrosome of interphase and mitotic cells (PubMed:9256449). Localizes to centriole distal lumen (PubMed:26337392). Localization at the nuclear pore complex requires NUP153 and TPR (PubMed:23591820). {ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:26337392, ECO:0000269|PubMed:9256449}.
DR  UNIPROT: O15182;
DR  UNIPROT: Q53YD2;
DR  UNIPROT: Q9BS23;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 602907;
DR  DisGeNET: 1070;
DE  Function: Plays a fundamental role in microtubule-organizing center structure and function. As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. {ECO:0000269|PubMed:22307388, ECO:0000305|PubMed:23591820}.
DE  Reference Proteome: Yes;
DE  Interaction: O43924; IntAct: EBI-729774; Score: 0.00
DE  Interaction: Q5UIP0; IntAct: EBI-729777; Score: 0.00
DE  Interaction: Q13432; IntAct: EBI-729780; Score: 0.00
DE  Interaction: O95229; IntAct: EBI-1001131; Score: 0.35
DE  Interaction: Q6UVJ0; IntAct: EBI-1570168; Score: 0.27
DE  Interaction: Q70CQ1; IntAct: EBI-2512828; Score: 0.40
DE  Interaction: Q9R1K9; IntAct: EBI-2561097; Score: 0.40
DE  Interaction: Q9H0K1; IntAct: EBI-2910196; Score: 0.27
DE  Interaction: Q9Y6K9; IntAct: EBI-5772724; Score: 0.00
DE  Interaction: P04792; IntAct: EBI-6872539; Score: 0.37
DE  Interaction: Q2NKQ1; IntAct: EBI-10182468; Score: 0.72
DE  Interaction: Q8NA72; IntAct: EBI-10182480; Score: 0.80
DE  Interaction: Q15293; IntAct: EBI-24265783; Score: 0.56
DE  Interaction: O95994; IntAct: EBI-24269242; Score: 0.56
DE  Interaction: P19237; IntAct: EBI-24271146; Score: 0.56
DE  Interaction: P17540; IntAct: EBI-24678114; Score: 0.56
DE  Interaction: O00141; IntAct: EBI-24728013; Score: 0.56
DE  Interaction: O43679; IntAct: EBI-24793336; Score: 0.56
DE  Interaction: Q12798; IntAct: EBI-21576600; Score: 0.35
DE  Interaction: Q8N490; IntAct: EBI-21596986; Score: 0.35
DE  Interaction: Q96EV8; IntAct: EBI-21651992; Score: 0.35
DE  Interaction: O00212; IntAct: EBI-21717184; Score: 0.35
DE  Interaction: O14874; IntAct: EBI-21725538; Score: 0.53
DE  Interaction: O95976; IntAct: EBI-21725569; Score: 0.35
DE  Interaction: Q01831; IntAct: EBI-21725721; Score: 0.53
DE  Interaction: P18509; IntAct: EBI-21725612; Score: 0.35
DE  Interaction: Q5VW00; IntAct: EBI-21725806; Score: 0.35
DE  Interaction: O15273; IntAct: EBI-21729416; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-20587935; Score: 0.44
DE  Interaction: Q9Y4C4; IntAct: EBI-20589725; Score: 0.44
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: Q9UQ80; IntAct: EBI-20904872; Score: 0.40
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: P13473; IntAct: EBI-25872710; Score: 0.56
DE  Interaction: Q9Y371; IntAct: EBI-25921828; Score: 0.56
DE  Interaction: P0C6X7; IntAct: EBI-26376977; Score: 0.35
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005815;
GO  GO:0044615;
GO  GO:0005730;
GO  GO:0032391;
GO  GO:0070390;
GO  GO:0005509;
GO  GO:0031683;
GO  GO:0008017;
GO  GO:0051301;
GO  GO:0007098;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGK
SQ  ITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFI
SQ  AIMTGDI
//
ID  O35648;
PN  Centrin-3;
GN  Cetn3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O15182}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O15182}. Nucleus envelope {ECO:0000250|UniProtKB:O15182}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15182}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O15182}. Note=Centrosome of interphase and mitotic cells. Localizes to centriole distal lumen (By similarity). Localization at the nuclear pore complex requires NUP153 and TPR (By similarity). {ECO:0000250|UniProtKB:O15182}.
DR  UNIPROT: O35648;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Plays a fundamental role in microtubule-organizing center structure and function. As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. {ECO:0000250|UniProtKB:O15182}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0035869;
GO  GO:0005737;
GO  GO:0005815;
GO  GO:0044615;
GO  GO:0005730;
GO  GO:0032391;
GO  GO:0070390;
GO  GO:0005509;
GO  GO:0031683;
GO  GO:0008017;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLALRGELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDQAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGK
SQ  ITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFI
SQ  AIMTGDI
//
ID  P30922;
PN  Chitinase-3-like protein 1;
GN  CHI3L1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: P30922;
DR  UNIPROT: O18949;
DR  UNIPROT: Q58CW2;
DR  UNIPROT: Q7YSE8;
DR  PDB: 1OWQ;
DR  PDB: 2ESC;
DR  Pfam: PF00704;
DR  PROSITE: PS51910;
DE  Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung (By similarity). {ECO:0000250, ECO:0000269|PubMed:16929095}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0030246;
GO  GO:0008061;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0005975;
GO  GO:0071356;
GO  GO:0006032;
GO  GO:0006954;
GO  GO:0030324;
GO  GO:0045766;
GO  GO:0070374;
GO  GO:0032757;
GO  GO:0010800;
GO  GO:0051897;
GO  GO:0070555;
GO  GO:0070741;
GO  GO:0009612;
GO  GO:0034612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGLRAAHTGFVVLVLLQSCAAYKLICYYTSWSQYREGDGSCFPDAIDPFLCTHVIYSFANISNNEIDTWEWNDVTLYDTL
SQ  NTLKNRNPNLKTLLSVGGWNFGSQRFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGWRDKRHLTTLVKEMKAE
SQ  FVREAQAGTEQLLLSAAVPAGKIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFRGQEDASSDRFSNADYA
SQ  VSYMLRLGAPANKLVMGIPTFGRSYTLASSKTDVGAPISGPGIPGQFTKEKGILAYYEICDFLHGATTHRFRDQQVPYAT
SQ  KGNQWVAYDDQESVKNKARYLKNRQLAGAMVWALDLDDFRGTFCGQNLTFPLTSAIKDVLARV
//
ID  Q7YS85;
PN  Chitinase-3-like protein 1;
GN  CHI3L1;
OS  89462;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q7YS85;
DR  UNIPROT: I6YIV5;
DR  PDB: 1TFV;
DR  PDB: 2O9O;
DR  PDB: 2QF8;
DR  PDB: 4MAV;
DR  PDB: 4ML4;
DR  PDB: 4MPK;
DR  PDB: 4MTV;
DR  PDB: 4NSB;
DR  PDB: 4Q7N;
DR  PDB: 5Z05;
DR  PDB: 5Z3S;
DR  PDB: 5Z4W;
DR  Pfam: PF00704;
DR  PROSITE: PS51910;
DE  Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0030246;
GO  GO:0008061;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0005975;
GO  GO:0071356;
GO  GO:0006954;
GO  GO:0030324;
GO  GO:0045766;
GO  GO:0070374;
GO  GO:0032757;
GO  GO:0010800;
GO  GO:0051897;
GO  GO:0070555;
GO  GO:0070741;
GO  GO:0009612;
GO  GO:0034612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGLRVAQTGFVVLVLLQSCAAYKLICYYTSWSQYREGDGSCFPDAIDPFLCTHVIYSFANISNNEIDTWEWNDVTLYDTL
SQ  NTLKNRNPKLKTLLSVGGWNFGSQRFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGWRDKRHLTTLVKEMKAE
SQ  FVREAQAGTEQLLLSAAVPAGKIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFRGQEDASSDRFSNADYA
SQ  VSYMLRLGAPANKLVMGIPTFGKSYTLASSKTDVGAPISGPGIPGQFTKEKGILAYYEICDFLHGATTHRFRDQQVPYAT
SQ  KGNQWVAYDDQESVKNKARYLKNRQLAGAMVWALDLDDFRGTFCGQNLAFPLTNAIKDVLAGV
//
ID  Q8SPQ0;
PN  Chitinase-3-like protein 1;
GN  CHI3L1;
OS  9925;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q8SPQ0;
DR  PDB: 1LJY;
DR  PDB: 1SYT;
DR  PDB: 1ZBV;
DR  PDB: 1ZBW;
DR  PDB: 1ZU8;
DR  PDB: 2AOS;
DR  PDB: 2B31;
DR  PDB: 2DSZ;
DR  PDB: 2DT0;
DR  PDB: 2DT1;
DR  PDB: 2DT2;
DR  PDB: 2DT3;
DR  PDB: 2O92;
DR  PDB: 2OLH;
DR  Pfam: PF00704;
DR  PROSITE: PS51910;
DE  Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0030246;
GO  GO:0008061;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0005975;
GO  GO:0071356;
GO  GO:0006954;
GO  GO:0030324;
GO  GO:0045766;
GO  GO:0070374;
GO  GO:0032757;
GO  GO:0010800;
GO  GO:0051897;
GO  GO:0070555;
GO  GO:0070741;
GO  GO:0009612;
GO  GO:0034612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGLRASGTGFVVLVLLQSCAAYKLICYYTSWSQYREGDGSCFPDAIDPFLCTHIIYSFANISNNEIDTWEWNDVTLYDTL
SQ  NTLKNRNPKLKTLLSVGGWNFGPERFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKRHLTGLVKEMKAE
SQ  FAREAQAGTERLLLSAAVSAGKIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFRGQEDASSDRFSNADYA
SQ  VSYMLRLGAPANKLVMGIPTFGRSFTLASSKTDVGAPISGPGIPGRFTKEKGILAYYEICDFLHGATTHRFRDQQVPYAT
SQ  KGNQWVAYDDQESVKNKARYLKNRQLAGAMVWALDLDDFRGTFCGQNLTFPLTSAVKDVLAEV
//
ID  P36222;
PN  Chitinase-3-like protein 1;
GN  CHI3L1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space {ECO:0000269|PubMed:9492324}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: P36222;
DR  UNIPROT: B2R7B0;
DR  UNIPROT: P30923;
DR  UNIPROT: Q8IVA4;
DR  UNIPROT: Q96HI7;
DR  PDB: 1HJV;
DR  PDB: 1HJW;
DR  PDB: 1HJX;
DR  PDB: 1NWR;
DR  PDB: 1NWS;
DR  PDB: 1NWT;
DR  PDB: 1NWU;
DR  PDB: 7CJ2;
DR  Pfam: PF00704;
DR  PROSITE: PS51910;
DR  OMIM: 181500;
DR  OMIM: 601525;
DR  OMIM: 611960;
DR  DisGeNET: 1116;
DE  Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung. {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:9492324}.
DE  Disease: Asthma-related traits 7 (ASRT7) [MIM:611960]: Asthma-related traits include clinical symptoms of asthma, such as coughing, wheezing, dyspnea, bronchial hyperresponsiveness as assessed by methacholine challenge test, serum IgE levels, atopy and atopic dermatitis. {ECO:0000269|PubMed:18403759}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. {ECO:0000269|PubMed:17160890, ECO:0000269|PubMed:20051317}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q14627; IntAct: EBI-15187745; Score: 0.80
DE  Interaction: P27797; IntAct: EBI-21846148; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-21846148; Score: 0.35
DE  Interaction: Q9NXR7; IntAct: EBI-21865463; Score: 0.35
DE  Interaction: O94830; IntAct: EBI-21866416; Score: 0.35
DE  Interaction: P08174; IntAct: EBI-21866441; Score: 0.40
DE  Interaction: Q9UGC7; IntAct: EBI-21866460; Score: 0.35
DE  Interaction: P17931; IntAct: EBI-20260956; Score: 0.52
DE  Interaction: Q86XT9; IntAct: EBI-20559520; Score: 0.40
DE  Interaction: O88786; IntAct: EBI-21257604; Score: 0.35
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0070062;
GO  GO:0031012;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0035580;
GO  GO:0030246;
GO  GO:0008061;
GO  GO:0005201;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0005975;
GO  GO:0051216;
GO  GO:0071356;
GO  GO:0006032;
GO  GO:0006954;
GO  GO:0030324;
GO  GO:0045766;
GO  GO:0070374;
GO  GO:0032757;
GO  GO:0010800;
GO  GO:0051897;
GO  GO:0070555;
GO  GO:0070741;
GO  GO:0009612;
GO  GO:0034612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGVKASQTGFVVLVLLQCCSAYKLVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANISNDHIDTWEWNDVTLYGML
SQ  NTLKNRNPNLKTLLSVGGWNFGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKQHFTTLIKEMKAE
SQ  FIKEAQPGKKQLLLSAALSAGKVTIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSPLFRGQEDASPDRFSNTDYA
SQ  VGYMLRLGAPASKLVMGIPTFGRSFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICDFLRGATVHRILGQQVPYAT
SQ  KGNQWVGYDDQESVKSKVQYLKDRQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALAAT
//
ID  Q29411;
PN  Chitinase-3-like protein 1;
GN  CHI3L1;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space {ECO:0000269|PubMed:3086326, ECO:0000269|PubMed:7768902}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q29411;
DR  UNIPROT: Q5UC99;
DR  PDB: 1XHG;
DR  PDB: 1XRV;
DR  PDB: 1ZB5;
DR  PDB: 1ZBC;
DR  Pfam: PF00704;
DR  PROSITE: PS51910;
DE  Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung (By similarity). Stimulates migration and adhesion of cultured vascular smooth muscle cells. {ECO:0000250, ECO:0000269|PubMed:12799184}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0030246;
GO  GO:0008061;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0005975;
GO  GO:0071356;
GO  GO:0006032;
GO  GO:0006954;
GO  GO:0030324;
GO  GO:0045766;
GO  GO:0070374;
GO  GO:0032757;
GO  GO:0010800;
GO  GO:0051897;
GO  GO:0070555;
GO  GO:0070741;
GO  GO:0009612;
GO  GO:0034612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGLRVAQTGFVALVLLQSCAAYKLVCYYTSWSQYREGDGSCFPDAIDPFLCTHIIYSFANISNNEIDTWEWNDVTLYDTL
SQ  NTLKNRNPNLKTLLSVGGWNFGSQRFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKRHLTTLVKEMKAE
SQ  FIREAQAGTEQLLLSAAVSAGKVAIDRGYDIAQISQHLDFISLLTYDFHGAWRQTTGHHSPLFRGQEDASSDRFSNADYA
SQ  VSYVLRLGAPANKLVMGIPTFGRSFTLASSKTDVGAPVSGPGIPGRFTKEKGILAYYEICDFLQGATTHRFRDQQVPYAT
SQ  KGNQWVGYDDQESVKNKAKYLKSRQLAGAMVWALDLDDFRGNFCGQNLRFPLTSAIKDVLAAA
//
ID  Q5RBP6;
PN  Chitinase-3-like protein 1;
GN  CHI3L1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q5RBP6;
DR  Pfam: PF00704;
DR  PROSITE: PS51910;
DE  Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0030246;
GO  GO:0008061;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0005975;
GO  GO:0071356;
GO  GO:0006954;
GO  GO:0030324;
GO  GO:0045766;
GO  GO:0070374;
GO  GO:0032757;
GO  GO:0010800;
GO  GO:0051897;
GO  GO:0070555;
GO  GO:0070741;
GO  GO:0009612;
GO  GO:0034612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGVKAAQTGIWASQGQSIRVVGFQAQTAHRAICLLGFVVLVLLQCCSAYKLVCYYTSWSQYREGDGSCFPDAIDRFLCTH
SQ  IIYSFANISNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNFGSQRFSNIASNTQSRRTFIKSVPPFLRTHGFD
SQ  GLDLAWLYPGQRDKQHFTTLIKEMRAEFIKEAQPGKKQLLLSAAVSAGKVTIDSSYDIAKISQHLDFISIMTYDFHGAWR
SQ  GTTGHHSPLFRGQEDASPDRFSNTDYAVGYMLRLEAPASKLVMGIPTFGRSFTLASSETGVGAPISGPGIPGRFTKEAGT
SQ  LAYYEICDFLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKERQLAGAMVWALDLDDFQGSFCGQDLRFPLT
SQ  NAIKDALAAT
//
ID  Q9WTV1;
PN  Chitinase-3-like protein 1;
GN  Chi3l1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q9WTV1;
DR  UNIPROT: Q5BJR6;
DR  Pfam: PF00704;
DR  PROSITE: PS51910;
DE  Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0030246;
GO  GO:0008061;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0005975;
GO  GO:0071347;
GO  GO:0071356;
GO  GO:0006032;
GO  GO:0006954;
GO  GO:0030324;
GO  GO:0045766;
GO  GO:0070374;
GO  GO:0032757;
GO  GO:0010800;
GO  GO:0051897;
GO  GO:0070555;
GO  GO:0070741;
GO  GO:0009612;
GO  GO:0034612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTLQLPGFAVLMLLQSCSAYKLVCYYTNWSQYREGNGSCFPDALDHSLCTHIIYSFANISNNKLSTSEWNDVTLYGMLNT
SQ  LKTRNPRLKTLLSVGGWSFGSERFSRIVSNAKSRKTFVQSVAPFLRTYGFDGLDLAWLYPGPKDKQHFTTLIKELKAEFT
SQ  KEVQPGTEKLLLSAAVSAGKVTLDSGYDVAQIAQHLDFINLMTYDFHGTWRHTTGHHSPLFRGQQDTGPDRFSNVDYGVG
SQ  YMLRLGAPTNKLVMGIPTFGKSFTLASSENQVGAPITGSGLPGRYTKEKGTLAYYEICDFLRGAEVHRILGQQVPFATKG
SQ  NQWVGYDDPESVKNKVKYLKNKQLAGAMVWAVDLDDFRGSFCGHNVHFPLTNAIKEALAVA
//
ID  Q6TMG6;
PN  Chitinase-3-like protein 1;
GN  CHI3L1;
OS  9940;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space {ECO:0000269|PubMed:17188513}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q6TMG6;
DR  PDB: 1SR0;
DR  PDB: 1ZBK;
DR  PDB: 1ZL1;
DR  PDB: 2DPE;
DR  PDB: 2DSU;
DR  PDB: 2DSV;
DR  PDB: 2DSW;
DR  PDB: 2FDM;
DR  PDB: 2G41;
DR  PDB: 2G8Z;
DR  PDB: 2PI6;
DR  PDB: 5Z4V;
DR  Pfam: PF00704;
DR  PROSITE: PS51910;
DE  Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia- induced injury, inflammation and epithelial apoptosis in lung (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005615;
GO  GO:0048471;
GO  GO:0030246;
GO  GO:0008061;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0005975;
GO  GO:0071356;
GO  GO:0006954;
GO  GO:0030324;
GO  GO:0045766;
GO  GO:0070374;
GO  GO:0032757;
GO  GO:0010800;
GO  GO:0051897;
GO  GO:0070555;
GO  GO:0070741;
GO  GO:0009612;
GO  GO:0034612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  YKLICYYTSWSQYREGDGSCFPDAIDPFLCTHVIYSFANISNNEIDTWEWNDVTLYDTLNTLKNRNPKLKTLLSVGGWNF
SQ  GPERFSAIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKRHLTTLVKEMKAEFIREAQAGTEQLLLSAAVSAG
SQ  KIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFAGNEDASSRFSNADYAVSYMLRLGAPANKLVMGIPTFG
SQ  RSFTLASSKTDVGAPVSGPGVPGRFTKEKGILAYYEICDFLHGATTHRFRDQQVPYATKGNQWVAYDDQESVKNKARYLK
SQ  NRQLAGAMVWALDLDDFRGTFCGQNLTFPLTSAVKDVLAEV
//
ID  Q8IWX8;
PN  Calcium homeostasis endoplasmic reticulum protein;
GN  CHERP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Endoplasmic reticulum {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Note=Distributed throughout the cytoplasm and also localizes to the perinuclear region of both human erythroleukemia (HEL) cells and Jurkat cells. Colocalizes with ITPR1. {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}.
DR  UNIPROT: Q8IWX8;
DR  UNIPROT: O00302;
DR  UNIPROT: Q4G0Y5;
DR  UNIPROT: Q8WU30;
DR  UNIPROT: Q99492;
DR  Pfam: PF04818;
DR  Pfam: PF01585;
DR  Pfam: PF01805;
DR  PROSITE: PS51391;
DR  PROSITE: PS50174;
DR  PROSITE: PS50128;
DR  OMIM: 618539;
DR  DisGeNET: 10523;
DE  Function: Involved in calcium homeostasis, growth and proliferation. {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674}.
DE  Reference Proteome: Yes;
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O75716; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: P07948; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: P63244; IntAct: EBI-7723227; Score: 0.37
DE  Interaction: O75554; IntAct: EBI-7722318; Score: 0.40
DE  Interaction: Q8K4Z5; IntAct: EBI-2555364; Score: 0.40
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: P31016; IntAct: EBI-7958999; Score: 0.44
DE  Interaction: Q01844; IntAct: EBI-3935753; Score: 0.37
DE  Interaction: P26368; IntAct: EBI-7704096; Score: 0.51
DE  Interaction: Q14562; IntAct: EBI-7704116; Score: 0.51
DE  Interaction: Q8WVK2; IntAct: EBI-7704173; Score: 0.51
DE  Interaction: Q70Z53; IntAct: EBI-7704153; Score: 0.51
DE  Interaction: Q9NQ29; IntAct: EBI-7704193; Score: 0.51
DE  Interaction: P08621; IntAct: EBI-7708765; Score: 0.37
DE  Interaction: O75400; IntAct: EBI-7711561; Score: 0.37
DE  Interaction: Q15427; IntAct: EBI-7716078; Score: 0.37
DE  Interaction: Q01081; IntAct: EBI-7719282; Score: 0.37
DE  Interaction: Q8IX12; IntAct: EBI-7721515; Score: 0.37
DE  Interaction: Q86U06; IntAct: EBI-7721614; Score: 0.37
DE  Interaction: Q14498; IntAct: EBI-7721713; Score: 0.37
DE  Interaction: O43290; IntAct: EBI-7721793; Score: 0.37
DE  Interaction: Q8NAV1; IntAct: EBI-7721925; Score: 0.37
DE  Interaction: Q8TAD8; IntAct: EBI-7722081; Score: 0.37
DE  Interaction: Q15287; IntAct: EBI-7722240; Score: 0.37
DE  Interaction: Q9Y580; IntAct: EBI-7722477; Score: 0.37
DE  Interaction: Q9NWB6; IntAct: EBI-7722538; Score: 0.37
DE  Interaction: Q8N302; IntAct: EBI-7722635; Score: 0.37
DE  Interaction: Q8WUA2; IntAct: EBI-7722733; Score: 0.37
DE  Interaction: P31942; IntAct: EBI-7722992; Score: 0.37
DE  Interaction: Q96N46; IntAct: EBI-7723120; Score: 0.37
DE  Interaction: P78362; IntAct: EBI-6658253; Score: 0.44
DE  Interaction: Q96SB4; IntAct: EBI-6660503; Score: 0.44
DE  Interaction: O43143; IntAct: EBI-9246997; Score: 0.53
DE  Interaction: Q5S007; IntAct: EBI-9660150; Score: 0.44
DE  Interaction: Q15637; IntAct: EBI-11297492; Score: 0.58
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: O00159; IntAct: EBI-11030803; Score: 0.35
DE  Interaction: Q9ULU4; IntAct: EBI-11059997; Score: 0.35
DE  Interaction: P09450; IntAct: EBI-11127973; Score: 0.35
DE  Interaction: Q15006; IntAct: EBI-11130215; Score: 0.35
DE  Interaction: Q12899; IntAct: EBI-11135299; Score: 0.35
DE  Interaction: P16070; IntAct: EBI-11137406; Score: 0.35
DE  Interaction: Q9UJV9; IntAct: EBI-11473486; Score: 0.35
DE  Interaction: Q5HY92; IntAct: EBI-24281098; Score: 0.56
DE  Interaction: Q14847; IntAct: EBI-24325847; Score: 0.56
DE  Interaction: Q04726; IntAct: EBI-24332621; Score: 0.56
DE  Interaction: Q8IYX7; IntAct: EBI-24335366; Score: 0.56
DE  Interaction: Q6P1W5; IntAct: EBI-24340482; Score: 0.56
DE  Interaction: Q6UY14; IntAct: EBI-24343283; Score: 0.56
DE  Interaction: O43251; IntAct: EBI-24345250; Score: 0.56
DE  Interaction: Q8IUC1; IntAct: EBI-24616416; Score: 0.56
DE  Interaction: Q9Y5V3; IntAct: EBI-24375990; Score: 0.56
DE  Interaction: O60504; IntAct: EBI-24405530; Score: 0.56
DE  Interaction: Q70EL1; IntAct: EBI-25260374; Score: 0.56
DE  Interaction: Q14296; IntAct: EBI-24435404; Score: 0.56
DE  Interaction: P49761; IntAct: EBI-25179685; Score: 0.56
DE  Interaction: P36817; IntAct: EBI-26508164; Score: 0.37
DE  Interaction: P06423; IntAct: EBI-16046574; Score: 0.49
DE  Interaction: P06921; IntAct: EBI-16047171; Score: 0.00
DE  Interaction: P06422; IntAct: EBI-16048319; Score: 0.00
DE  Interaction: P36780; IntAct: EBI-16049196; Score: 0.00
DE  Interaction: P62136; IntAct: EBI-14025896; Score: 0.42
DE  Interaction: P22492; IntAct: EBI-21580683; Score: 0.35
DE  Interaction: Q02809; IntAct: EBI-21585081; Score: 0.35
DE  Interaction: Q96P53; IntAct: EBI-21607501; Score: 0.35
DE  Interaction: P55075; IntAct: EBI-21635166; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-21677299; Score: 0.35
DE  Interaction: P62304; IntAct: EBI-21697668; Score: 0.35
DE  Interaction: P21802; IntAct: EBI-21718282; Score: 0.35
DE  Interaction: Q15696; IntAct: EBI-21718626; Score: 0.35
DE  Interaction: Q6NYC1; IntAct: EBI-21718825; Score: 0.35
DE  Interaction: Q96I25; IntAct: EBI-21719204; Score: 0.35
DE  Interaction: P62241; IntAct: EBI-21741627; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: O15042; IntAct: EBI-20925834; Score: 0.40
DE  Interaction: P07947; IntAct: EBI-25390545; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-26396507; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-26396827; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-26398473; Score: 0.35
DE  Interaction: P14240; IntAct: EBI-26968430; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27046166; Score: 0.35
DE  Interaction: P27361; IntAct: EBI-28934804; Score: 0.35
DE  Interaction: Q15208; IntAct: EBI-28941263; Score: 0.35
DE  Interaction: Q96BR1; IntAct: EBI-28944277; Score: 0.35
DE  Interaction: Q9Y2H9; IntAct: EBI-28948459; Score: 0.35
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0033017;
GO  GO:0003723;
GO  GO:0044325;
GO  GO:0006874;
GO  GO:0008285;
GO  GO:0007399;
GO  GO:0070886;
GO  GO:0051209;
GO  GO:0006396;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEMPLPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKLALEQQQLICKQQTPELEPAA
SQ  TMPPLPQPPLAPAAPIPPAQGAPSMDELIQQSQWNLQQQEQHLLALRQEQVTAAVAHAVEQQMQKLLEETQLDMNEFDNL
SQ  LQPIIDTCTKDAISAGKNWMFSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKV
SQ  VVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYSSVVQPVQLAFQQQIQTLKTQ
SQ  HEEFVTSLAQQQQQQQQQQQQLQMPQMEAEVKATPPPPAPPPAPAPAPAIPPTTQPDDSKPPIQMPGSSEYEAPGGVQDP
SQ  AAAGPRGPGPHDQIPPNKPPWFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPGWNGQRDAPW
SQ  NNQPDAAWNSQFEGPWNSQHEQPPWGGGQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPHPHNFNRFPPRFMQDDFPPRH
SQ  PFERPPYPHRFDYPQGDFPAEMGPPHHHPGHRMPHPGINEHPPWAGPQHPDFGPPPHGFNGQPPHMRRQGPPHINHDDPS
SQ  LVPNVPYFDLPAGLMAPLVKLEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQNGLYEFFRAK
SQ  MRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSNSRSSKSSGSYSRSRSRSCSRSYSRSRSRSRSRSRSSRSRSRSQSRS
SQ  RSKSYSPGRRRRSRSRSPTPPSSAGLGSNSAPPIPDSRLGEENKGHQMLVKMGWSGSGGLGAKEQGIQDPIKGGDVRDKW
SQ  DQYKGVGVALDDPYENYRRNKSYSFIARMKARDECK
//
ID  Q8CGZ0;
PN  Calcium homeostasis endoplasmic reticulum protein;
GN  Cherp;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8IWX8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWX8}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IWX8}. Note=Distributed throughout the cytoplasm and also localizes to the perinuclear region. Colocalizes with ITPR1 (By similarity). {ECO:0000250|UniProtKB:Q8IWX8}.
DR  UNIPROT: Q8CGZ0;
DR  UNIPROT: Q8K291;
DR  UNIPROT: Q8VCD2;
DR  Pfam: PF04818;
DR  Pfam: PF01585;
DR  Pfam: PF01805;
DR  PROSITE: PS51391;
DR  PROSITE: PS50174;
DR  PROSITE: PS50128;
DE  Function: Involved in calcium homeostasis, growth and proliferation. {ECO:0000250|UniProtKB:Q8IWX8}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13131; IntAct: EBI-2362860; Score: 0.37
DE  Interaction: Q15637; IntAct: EBI-11298622; Score: 0.00
DE  Interaction: Q3UL36; IntAct: EBI-26888124; Score: 0.35
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0033017;
GO  GO:0003723;
GO  GO:0044325;
GO  GO:0006874;
GO  GO:0008285;
GO  GO:0070886;
GO  GO:0051209;
GO  GO:0006396;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEMPMPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKLALEQQQLICKQQAPELEPTS
SQ  AMPPLPQPPLAPTASLTPAQGTPSMDELIQQSQWSLQQQEQHLLALRQEQVTTAVAHAVEQQMQKLLEETQLDMSEFDNL
SQ  LQPIIDTCTKDAISAGKNWMFSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKV
SQ  VVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYSSVVQPVQLAFQQQIQSLKTQ
SQ  HEEFVSSLAQQQQQQQQQQQQQPQPQPQPQIQLPQMEADVKATPPPPAPPPASAPAPTIPPTTQPDDNKPPIQMPGSSEY
SQ  DTSAGVQDPAAAGPRGPGPHEQIPPNKPPWFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPG
SQ  WNGQRDAPWNNQPDPNWNNQFEGPWNNQHEPPPWGGAQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPHPHNFNRFPPRF
SQ  MQDDFPPRHPFERPPYPHRFDYPQGDFPADMGPPHHHPGHRMPHPGINEHPPWAGPQHPDFGPPPHGFNGQPPHMRRQGP
SQ  PHINHDDPSLVPNVPYFDLPAGLMAPLVKLEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQN
SQ  GLYEFFRAKMRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSSSRSSKSSRSSSRSHSRSRSRSSSRSRSRSRSRSRSSR
SQ  SRSRSRSRSRSKSYSPGRRRRSRSRSPTPPSAAGLGSNSAPPIPDSRLGEENKGHQMLVKMGWSGSGGLGAKEQGIQDPI
SQ  KGGDVRDKWDQYKGVGVALDDPYENYRRNKSYSFIARMKARDEFSTFGTRKEEKED
//
ID  O35744;
PN  Chitinase-like protein 3;
GN  Chil3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted. Rough endoplasmic reticulum lumen. Nucleus envelope. Cytoplasm. Cytoplasmic granule. Note=Predominantly localizes to the lumen of rough endoplasmic reticulum (rER) and nuclear envelope in alveolar macrophages. Localizes to the dilated lumen of rER in immature neutrophils in spleen and in cytoplasmic granules in peritoneal neutrophils. Detected in needle-shaped crystals present in the cytoplasm of bone marrow macrophages.
DR  UNIPROT: O35744;
DR  UNIPROT: P70201;
DR  UNIPROT: Q3U462;
DR  UNIPROT: Q3UV87;
DR  UNIPROT: Q61201;
DR  PDB: 1E9L;
DR  PDB: 1VF8;
DR  Pfam: PF00704;
DR  PROSITE: PS51910;
DE  Function: Lectin that binds saccharides with a free amino group, such as glucosamine or galactosamine. Binding to oligomeric saccharides is much stronger than binding to mono- or disaccharides. Also binds chitin and heparin. Has weak hexosaminidase activity but no chitinase activity. Has chemotactic activity for T-lymphocytes, bone marrow cells and eosinophils. May play a role in inflammation and allergy. {ECO:0000269|PubMed:10625674, ECO:0000269|PubMed:11297523, ECO:0000269|PubMed:11733538}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005635;
GO  GO:0048237;
GO  GO:0004563;
GO  GO:0030246;
GO  GO:0008061;
GO  GO:0019900;
GO  GO:0102148;
GO  GO:0006032;
GO  GO:0006954;
GO  GO:0000272;
GO  GO:0032722;
GO  GO:0002532;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAKLILVTGLAILLNVQLGSSYQLMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQNNEITYTHEQDLRDYEAL
SQ  NGLKDKNTELKTLLAIGGWKFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVK
SQ  EMRKAFEEESVEKDIPRLLLTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSAD
SQ  LNVDSIISYWKDHGAASEKLIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDA
SQ  PQEVPYAYQGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDDFSGSFCHQRHFPLTSTLKGDLNIHSASCKGPY
//
ID  Q9N3Z3;
PN  Serine/threonine-protein kinase chk-1;
GN  chk;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:26073019}. Nucleus {ECO:0000250|UniProtKB:O61661}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26073019}. Note=The Ser-344 phosphorylated form colocalizes with P granules in a perinuclear manner in embryonic germline precursor cells and in Z2/Z3 primordial germ cells in L1 stage larvae. {ECO:0000269|PubMed:26073019}.
DR  UNIPROT: Q9N3Z3;
DR  UNIPROT: Q17375;
DR  UNIPROT: Q86FM7;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed:15326393). May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed:15326393). Required for checkpoint mediated cell cycle arrest in response to DNA damage in germline cells (PubMed:15326393, PubMed:27956467). Delays cell-cycle reentry of the Z2 and Z3 primordial germ cells in response to transcription-induced DNA damage as they emerge from cell cycle arrest in L1 larvae (PubMed:26073019). Essential for embryogenesis (PubMed:15326393). {ECO:0000269|PubMed:15326393, ECO:0000269|PubMed:26073019, ECO:0000269|PubMed:27956467}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9XTY9; IntAct: EBI-344141; Score: 0.37
DE  Interaction: Q9N4A9; IntAct: EBI-344144; Score: 0.37
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0000077;
GO  GO:0009792;
GO  GO:0035556;
GO  GO:0033314;
GO  GO:0006468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAASTTSTPAAAAVAPQQPESLYRVVQTLGEGAFGEVLLIVNTKNPEVAAAMKKINIANKSKDFIDNIRKEYLLQKRVS
SQ  AVGHDNVIRMIGMRNDPQFYYLFLEYADGGELFDKIEPDCGMSPVFAQFYFKQLICGLKFIHDNDVVHRDIKPENLLLTG
SQ  THVLKISDFGMATLYRNKGEERLLDLSCGTIPYAAPELCAGKKYRGPPVDVWSSGIVLIAMLTGELPWDRASDASQSYMG
SQ  WISNTSLDERPWKKIDVRALCMLRKIVTDKTDKRATIEQIQADPWYQHNFGQVETPNGRPLKRARNNDENITCTQQAECS
SQ  AKRRHLETPNEKSTLAERQNASFSQPTKTEDLLLTQHIDMSQTNSNLLQRMVCRMTRFCVVTDIRSTYQKVARASEHAGF
SQ  GVRETDDYRLLVTWREVSMMVSLYTMGDIPDKPRVMVDFRRSRGDGIQFKKMFMDVRNRMHEWICTDGNNWLANLGYVPR
SQ  NPQIVNGGGVNVEHSASSINVDV
//
ID  O43633;
PN  Charged multivesicular body protein 2a;
GN  CHMP2A;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Late endosome membrane {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Peripheral membrane protein {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Cytoplasmic side {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}. Nucleus envelope {ECO:0000269|PubMed:28242692}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase (PubMed:28242692). {ECO:0000269|PubMed:28242692}.
DR  UNIPROT: O43633;
DR  UNIPROT: B2R4W6;
DR  UNIPROT: Q3ZTT0;
DR  Pfam: PF03357;
DR  OMIM: 610893;
DR  DisGeNET: 27243;
DE  Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis (PubMed:21310966). Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (PubMed:28242692). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. {ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692, ECO:0000305}. (Microbial infection) The ESCRT machinery functions in topologically equivalent membrane fission events, such as the budding of enveloped viruses (HIV-1 and other lentiviruses). Involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844}.
DE  Reference Proteome: Yes;
DE  Interaction: P40818; IntAct: EBI-8601078; Score: 0.44
DE  Interaction: Q70EL1; IntAct: EBI-8601283; Score: 0.44
DE  Interaction: P61457; IntAct: EBI-2692786; Score: 0.00
DE  Interaction: Q16254; IntAct: EBI-3916764; Score: 0.37
DE  Interaction: P10600; IntAct: EBI-3918280; Score: 0.37
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q8NF50; IntAct: EBI-10184717; Score: 0.56
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P35278; IntAct: EBI-11012136; Score: 0.35
DE  Interaction: Q8BT07; IntAct: EBI-11014656; Score: 0.35
DE  Interaction: Q92734; IntAct: EBI-11029015; Score: 0.35
DE  Interaction: Q9JLQ0; IntAct: EBI-11033702; Score: 0.35
DE  Interaction: O75787; IntAct: EBI-11037152; Score: 0.35
DE  Interaction: P51148; IntAct: EBI-11046231; Score: 0.35
DE  Interaction: P51149; IntAct: EBI-11050319; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: Q9QYY8; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q6PB44; IntAct: EBI-11097749; Score: 0.35
DE  Interaction: P46467; IntAct: EBI-11115954; Score: 0.35
DE  Interaction: P61019; IntAct: EBI-11127113; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-11148324; Score: 0.59
DE  Interaction: O35730; IntAct: EBI-11162936; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9Y3E7; IntAct: EBI-11509057; Score: 0.67
DE  Interaction: Q9UN37; IntAct: EBI-11510032; Score: 0.37
DE  Interaction: O43633; IntAct: EBI-11510376; Score: 0.37
DE  Interaction: Q13144; IntAct: EBI-11510746; Score: 0.37
DE  Interaction: Q8WV92; IntAct: EBI-11510750; Score: 0.73
DE  Interaction: O94818; IntAct: EBI-11511236; Score: 0.37
DE  Interaction: O95630; IntAct: EBI-11511994; Score: 0.55
DE  Interaction: P62491; IntAct: EBI-11512003; Score: 0.37
DE  Interaction: Q9Y5L0; IntAct: EBI-11512013; Score: 0.37
DE  Interaction: Q8TEL6; IntAct: EBI-11512033; Score: 0.37
DE  Interaction: Q6DKK2; IntAct: EBI-11512041; Score: 0.37
DE  Interaction: Q92882; IntAct: EBI-21519358; Score: 0.35
DE  Interaction: Q9NPC8; IntAct: EBI-21617697; Score: 0.35
DE  Interaction: O00161; IntAct: EBI-21756983; Score: 0.40
DE  Interaction: Q8IWF9; IntAct: EBI-21757002; Score: 0.35
DE  Interaction: Q9UBP0; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q9UPQ4; IntAct: EBI-21888198; Score: 0.35
DE  Interaction: Q9NZZ3; IntAct: EBI-21888198; Score: 0.35
DE  Interaction: Q9NP79; IntAct: EBI-21888198; Score: 0.35
DE  Interaction: Q16698; IntAct: EBI-21888198; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: O14979; IntAct: EBI-20937156; Score: 0.40
DE  Interaction: P0DTD2; IntAct: EBI-25491493; Score: 0.53
DE  Interaction: P42858; IntAct: EBI-25958665; Score: 0.56
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
GO  GO:1904930;
GO  GO:0000421;
GO  GO:0005829;
GO  GO:0000815;
GO  GO:0070062;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0005765;
GO  GO:0016020;
GO  GO:0030117;
GO  GO:0030496;
GO  GO:0005771;
GO  GO:0032585;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005886;
GO  GO:0031210;
GO  GO:0019904;
GO  GO:0097352;
GO  GO:0006914;
GO  GO:0032509;
GO  GO:1904903;
GO  GO:0045184;
GO  GO:0010458;
GO  GO:1902774;
GO  GO:0045324;
GO  GO:0016236;
GO  GO:0090148;
GO  GO:0010324;
GO  GO:0061952;
GO  GO:0007080;
GO  GO:0036258;
GO  GO:0071985;
GO  GO:0061763;
GO  GO:0060548;
GO  GO:1903723;
GO  GO:0031468;
GO  GO:0006997;
GO  GO:0001778;
GO  GO:1903543;
GO  GO:0051260;
GO  GO:0051258;
GO  GO:0015031;
GO  GO:0010824;
GO  GO:1901673;
GO  GO:0043162;
GO  GO:0051469;
GO  GO:0046761;
GO  GO:0039702;
GO  GO:0019076;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMR
SQ  ANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEES
SQ  DAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEAAASALADADADLEERLKNLRRD
//
ID  Q9DB34;
PN  Charged multivesicular body protein 2a;
GN  Chmp2a;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Late endosome membrane {ECO:0000250|UniProtKB:O43633}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43633}; Cytoplasmic side {ECO:0000250|UniProtKB:O43633}. Cytoplasm {ECO:0000269|PubMed:15173323}. Nucleus envelope {ECO:0000250|UniProtKB:O43633}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase (By similarity). {ECO:0000250|UniProtKB:O43633}.
DR  UNIPROT: Q9DB34;
DR  Pfam: PF03357;
DE  Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (By similarity). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. {ECO:0000250|UniProtKB:O43633}.
DE  Reference Proteome: Yes;
DE  Interaction: P10909; IntAct: EBI-11115096; Score: 0.35
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: Q9Y3E7; IntAct: EBI-11090637; Score: 0.35
DE  Interaction: Q9HD42; IntAct: EBI-11090637; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-11090637; Score: 0.35
DE  Interaction: O60684; IntAct: EBI-11115096; Score: 0.35
DE  Interaction: Q5T8P6; IntAct: EBI-11115096; Score: 0.35
DE  Interaction: O00255; IntAct: EBI-11115096; Score: 0.35
DE  Interaction: P48681; IntAct: EBI-11115096; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26473528; Score: 0.35
GO  GO:1904930;
GO  GO:0000421;
GO  GO:0000785;
GO  GO:0005829;
GO  GO:0000815;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0005765;
GO  GO:0030117;
GO  GO:0030496;
GO  GO:0005771;
GO  GO:0032585;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005886;
GO  GO:0031210;
GO  GO:0019904;
GO  GO:0097352;
GO  GO:0006914;
GO  GO:0032509;
GO  GO:0045184;
GO  GO:0010458;
GO  GO:1902774;
GO  GO:0045324;
GO  GO:0090148;
GO  GO:0010324;
GO  GO:0061952;
GO  GO:0007080;
GO  GO:0036258;
GO  GO:0071985;
GO  GO:0061763;
GO  GO:0060548;
GO  GO:1903723;
GO  GO:0031468;
GO  GO:0006997;
GO  GO:0001778;
GO  GO:1903543;
GO  GO:0051260;
GO  GO:0051258;
GO  GO:0015031;
GO  GO:0010824;
GO  GO:1901673;
GO  GO:0043162;
GO  GO:0051469;
GO  GO:0046761;
GO  GO:0039702;
GO  GO:0019076;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O43633};
SQ  MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMR
SQ  ANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEES
SQ  DAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEATASALADADADLEERLKNLRRD
//
ID  Q9H444;
PN  Charged multivesicular body protein 4b;
GN  CHMP4B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:15511219}. Late endosome membrane {ECO:0000269|PubMed:15511219, ECO:0000305|PubMed:12860994}; Peripheral membrane protein {ECO:0000305}. Midbody {ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:22422861}. Nucleus envelope {ECO:0000269|PubMed:26040712}. Note=Recruited to the nuclear envelope by CHMP7 during late anaphase (PubMed:26040712). Localizes transiently to the midbody arms immediately before abscission (PubMed:22422861). {ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:26040712}.
DR  UNIPROT: Q9H444;
DR  UNIPROT: E1P5N4;
DR  UNIPROT: Q53ZD6;
DR  PDB: 3C3Q;
DR  PDB: 3UM3;
DR  PDB: 4ABM;
DR  PDB: 5MK2;
DR  Pfam: PF03357;
DR  OMIM: 605387;
DR  OMIM: 610897;
DR  DisGeNET: 128866;
DE  Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released (PubMed:12860994, PubMed:18209100). The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis (PubMed:21310966). Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:18209100, ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:26040712}. (Microbial infection) The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the budding of enveloped viruses (HIV-1 and other lentiviruses). Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:22422861}.
DE  Disease: Cataract 31, multiple types (CTRCT31) [MIM:605387]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT31 includes posterior polar, progressive posterior subcapsular, nuclear, and anterior subcapsular cataracts. {ECO:0000269|PubMed:17701905}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O43633; IntAct: EBI-11148324; Score: 0.59
DE  Interaction: P02545; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: P19525; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: P53990; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-757456; Score: 0.55
DE  Interaction: Q8WUX9; IntAct: EBI-11513083; Score: 0.54
DE  Interaction: Q9DB34; IntAct: EBI-11090637; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: O95630; IntAct: EBI-2118145; Score: 0.55
DE  Interaction: P40818; IntAct: EBI-8601147; Score: 0.44
DE  Interaction: Q70EL1; IntAct: EBI-8601371; Score: 0.44
DE  Interaction: Q9CQ10; IntAct: EBI-2563199; Score: 0.40
DE  Interaction: P10644; IntAct: EBI-2691105; Score: 0.00
DE  Interaction: P38606; IntAct: EBI-4324466; Score: 0.53
DE  Interaction: Q9H3S7; IntAct: EBI-7178748; Score: 0.66
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-9052823; Score: 0.67
DE  Interaction: O14862; IntAct: EBI-9995694; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: Q8BT07; IntAct: EBI-11014656; Score: 0.35
DE  Interaction: Q9QWF0; IntAct: EBI-11015136; Score: 0.35
DE  Interaction: A2AUY4; IntAct: EBI-11016281; Score: 0.35
DE  Interaction: P60122; IntAct: EBI-11023741; Score: 0.35
DE  Interaction: Q92734; IntAct: EBI-11029015; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: Q9JLQ0; IntAct: EBI-11033702; Score: 0.35
DE  Interaction: P21333; IntAct: EBI-11038784; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: P51148; IntAct: EBI-11046231; Score: 0.35
DE  Interaction: P51149; IntAct: EBI-11050319; Score: 0.35
DE  Interaction: Q9JHJ0; IntAct: EBI-11063313; Score: 0.35
DE  Interaction: P58771; IntAct: EBI-11063826; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: Q6ZQ29; IntAct: EBI-11075869; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: P55072; IntAct: EBI-11084314; Score: 0.35
DE  Interaction: Q8R5L1; IntAct: EBI-11085290; Score: 0.35
DE  Interaction: Q9UER7; IntAct: EBI-11088574; Score: 0.35
DE  Interaction: Q9QYY8; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q61187; IntAct: EBI-11090666; Score: 0.35
DE  Interaction: Q6PB44; IntAct: EBI-11097749; Score: 0.35
DE  Interaction: P46467; IntAct: EBI-11115954; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: Q9UQE7; IntAct: EBI-11147323; Score: 0.35
DE  Interaction: Q9Y3E7; IntAct: EBI-11148324; Score: 0.69
DE  Interaction: Q6P1N0; IntAct: EBI-11148324; Score: 0.55
DE  Interaction: Q5T0F9; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q99816; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q96SN8; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: O95714; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q6ZS30; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: O60684; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q13395; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q02878; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q93050; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: P11717; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: P51608; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q9Y2X9; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q8N6N3; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: H0Y9L7; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q9ULT0; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q641Q3; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q9NZZ3; IntAct: EBI-11148324; Score: 0.55
DE  Interaction: P21281; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: P49711; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: O60447; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q5SVZ6; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q86Y56; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q8WV92; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q96K19; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: P26641; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q9Y4G6; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q96SU4; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q6NUK1; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: E9PSI1; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q9NVX2; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q7LBR1; IntAct: EBI-11151252; Score: 0.55
DE  Interaction: Q9H773; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q9UKT4; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q8WUM4; IntAct: EBI-11151252; Score: 0.86
DE  Interaction: Q9Y6W3; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q9UQN3; IntAct: EBI-11151252; Score: 0.59
DE  Interaction: Q14254; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q9Y2B5; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q10589; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q9NQS3; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q96BY9; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q9UBP0; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q9HD42; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: P61421; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q96EY5; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q16739; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: E5RHG8; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: O75955; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q7LBC6; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q96QD8; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: P36543; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q9BY43; IntAct: EBI-24635622; Score: 0.56
DE  Interaction: Q9H444; IntAct: EBI-11510097; Score: 0.64
DE  Interaction: Q96FZ7; IntAct: EBI-11510183; Score: 0.37
DE  Interaction: Q9UN37; IntAct: EBI-11510230; Score: 0.37
DE  Interaction: Q96CF2; IntAct: EBI-11510324; Score: 0.37
DE  Interaction: O75928; IntAct: EBI-11510785; Score: 0.37
DE  Interaction: Q06265; IntAct: EBI-11510789; Score: 0.37
DE  Interaction: Q9H2X6; IntAct: EBI-11510793; Score: 0.37
DE  Interaction: Q12873; IntAct: EBI-11511252; Score: 0.37
DE  Interaction: O60664; IntAct: EBI-24515780; Score: 0.56
DE  Interaction: Q7KZS0; IntAct: EBI-25218607; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q9WU78; IntAct: EBI-15788562; Score: 0.52
DE  Interaction: Q5VW32; IntAct: EBI-15979635; Score: 0.61
DE  Interaction: Q96H96; IntAct: EBI-20304156; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-20307233; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-20307902; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-20821761; Score: 0.35
DE  Interaction: P62807; IntAct: EBI-25471348; Score: 0.27
DE  Interaction: P55040; IntAct: EBI-21260056; Score: 0.35
DE  Interaction: P14316; IntAct: EBI-21260627; Score: 0.35
DE  Interaction: P54920; IntAct: EBI-21261831; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q8TEA7; IntAct: EBI-28943849; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-29373058; Score: 0.35
DE  Interaction: P31314; IntAct: EBI-29607649; Score: 0.35
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
GO  GO:1904930;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0009898;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0000815;
GO  GO:0070062;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0005765;
GO  GO:0030117;
GO  GO:0030496;
GO  GO:0005771;
GO  GO:0032585;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0031982;
GO  GO:0045296;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0097352;
GO  GO:0006914;
GO  GO:0010458;
GO  GO:1902774;
GO  GO:0032511;
GO  GO:0016236;
GO  GO:0036438;
GO  GO:0090148;
GO  GO:0061952;
GO  GO:0000281;
GO  GO:0007080;
GO  GO:0036258;
GO  GO:0071985;
GO  GO:0061763;
GO  GO:1902902;
GO  GO:0060548;
GO  GO:1901215;
GO  GO:0031468;
GO  GO:0006997;
GO  GO:0001778;
GO  GO:0006620;
GO  GO:0051258;
GO  GO:0010824;
GO  GO:1901673;
GO  GO:0043162;
GO  GO:0090611;
GO  GO:0006900;
GO  GO:0051469;
GO  GO:0046755;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLA
SQ  QIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFD
SQ  EDELMAELEELEQEELDKNLLEISGPETVPLPNVPSIALPSKPAKKKEEEDDDMKELENWAGSM
//
ID  Q9D8B3;
PN  Charged multivesicular body protein 4b;
GN  Chmp4b;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9H444}. Late endosome membrane {ECO:0000250|UniProtKB:Q9H444}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H444}. Midbody {ECO:0000250|UniProtKB:Q9H444}. Nucleus envelope {ECO:0000250|UniProtKB:Q9H444}. Note=Recruited to the nuclear envelope by CHMP7 during late anaphase. Localizes transiently to the midbody arms immediately before abscission. {ECO:0000250|UniProtKB:Q9H444}.
DR  UNIPROT: Q9D8B3;
DR  UNIPROT: A2AVM1;
DR  UNIPROT: Q3TXM7;
DR  UNIPROT: Q91VM7;
DR  UNIPROT: Q922P1;
DR  Pfam: PF03357;
DE  Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan. {ECO:0000250|UniProtKB:Q9H444}.
DE  Reference Proteome: Yes;
DE  Interaction: O43633; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P53990; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q07065; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q14244; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q14764; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q6P5Z2; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q6P9B9; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: Q7LBR1; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9Y3E7; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q6P1N0; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q53TN4; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q10589; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9NZZ3; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9BY43; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9UI12; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P28288; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9Y5K6; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: O75477; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9UJZ1; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9UNQ0; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9UHR4; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P21281; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9NRL2; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9H0H5; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: O00560; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q969G5; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q8WUM4; IntAct: EBI-11052854; Score: 0.56
DE  Interaction: P02786; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P14923; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q13111; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q96NT0; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q4KMQ1; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9UIF8; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: O75351; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9HD42; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P08754; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9UKS6; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P40818; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9UBH6; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P61421; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q96EY5; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q86UP2; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q14126; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q15904; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: B4E2V5; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q6NZI2; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P36543; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9UQN3; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9H3S7; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: O75955; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q03135; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q8WV92; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P14384; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q96QD8; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q5T0F9; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: E9PSI1; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q13112; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q9ULH0; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q8NFJ5; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q14254; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q96CM3; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q86TX2; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q9Y573; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: J3QR07; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q96QC4; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q13838; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q5VTR2; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q9BTV6; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q16222; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q7Z6E9; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: A6H8Y1; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q9H3P2; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q8NI27; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q9NU22; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: H0YBU6; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: G3V4T2; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q7Z2Z2; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q5SYE7; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: O75340; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q9BY77; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q5VST9; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q6UUV7; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q8TEU7; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-15613912; Score: 0.40
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
GO  GO:1904930;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0009898;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0000815;
GO  GO:0098978;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0005765;
GO  GO:0016020;
GO  GO:0030117;
GO  GO:0030496;
GO  GO:0005771;
GO  GO:0032585;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0031982;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0097352;
GO  GO:0006914;
GO  GO:0010458;
GO  GO:1902774;
GO  GO:0032511;
GO  GO:0036438;
GO  GO:0090148;
GO  GO:0061952;
GO  GO:0000281;
GO  GO:0007080;
GO  GO:0036258;
GO  GO:0071985;
GO  GO:0061763;
GO  GO:1902902;
GO  GO:0060548;
GO  GO:1901215;
GO  GO:0031468;
GO  GO:0006997;
GO  GO:0001778;
GO  GO:0006620;
GO  GO:0051258;
GO  GO:0010506;
GO  GO:0010824;
GO  GO:1901673;
GO  GO:0043162;
GO  GO:0090611;
GO  GO:0006900;
GO  GO:0051469;
GO  GO:0046755;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9H444};
SQ  MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLA
SQ  QIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFD
SQ  EDELMAELEELEQEELDKNLLEISGPETVPLPNVPSVALPSKPAKKKEEEDDDMKELENWAGSM
//
ID  Q5ZJB7;
PN  Charged multivesicular body protein 7;
GN  CHMP7;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}.
DR  UNIPROT: Q5ZJB7;
DR  Pfam: PF03357;
DE  Function: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope (NE) during late anaphase (By similarity). Together with SPAST, the ESCRT-III complex promotes NE sealing and mitotic spindle disassembly during late anaphase (By similarity). Recruited to the reforming NE during anaphase by LEMD2 (By similarity). Plays a role in the endosomal sorting pathway (By similarity). {ECO:0000250|UniProtKB:Q8WUX9}.
DE  Reference Proteome: Yes;
GO  GO:0000815;
GO  GO:0005771;
GO  GO:0005635;
GO  GO:0010458;
GO  GO:0045324;
GO  GO:0032511;
GO  GO:0031468;
GO  GO:0015031;
GO  GO:0006900;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCSPGRAPPGPAPAGDLPPEWETDDERMAFLFSAFKQSREVNSTEWDSKMAFWVGLVLARGRRRGVVRTCLRELQNGFER
SQ  RGSVPLGLGTVLRELLRRGKMQRESDFMASVDSSWISWGVGVFILKPLKWTLSSVLGDSKVPEEEEVLIYVELLQEKAEE
SQ  VYRLYQNSVLSSHPVVALSELRSLCAGVCPDERTFYLLLLQLQKEKKVTILEQNGEKIVKFARGLHAKVSPMNDVDIGVY
SQ  QLMQSEQLLSQKVESLSQEAEKCKDDARSACRAGKKQLALRCLKSKRRTERRIEELHSKLDAVQGILDRIYASQTDQMVF
SQ  NAYQAGVGALKLSMKDVTVEKAENLVDQIQELCDTQDEVAQTLAGAGVNGLEMDSEELEKELDSLLQDSAKEPVHLHPVP
SQ  QKDSGFAGAISDAELEAELEKLSVCDGDLAQKTPSASSEPQTALGLNL
//
ID  Q6PBQ2;
PN  Charged multivesicular body protein 7;
GN  chmp7;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the nucleus envelope during late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}.
DR  UNIPROT: Q6PBQ2;
DR  UNIPROT: Q6NYA6;
DR  Pfam: PF03357;
DE  Function: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope during late anaphase. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. {ECO:0000250|UniProtKB:Q8WUX9}.
DE  Reference Proteome: Yes;
GO  GO:0000815;
GO  GO:0005771;
GO  GO:0005635;
GO  GO:0010458;
GO  GO:0045324;
GO  GO:0032511;
GO  GO:0031468;
GO  GO:0015031;
GO  GO:0006900;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSVSVEKRSAWFPPDWDDDERMSFLFSAFKENRDVDCTDWDGKIDFWSPLIIEHCRRCGSVCVNLQDLNENFRRKGSVPL
SQ  GLSTVIQSMIRSGKVQKESDFAANVDSGWLSWGVGLLLVRPLKWTLSALLGSGRVPLEESFVVIELVKEKAAELLAAYRG
SQ  SALSARSLLSFQELRSLSSHICPDESTLCMALLQLQREKHVTVSLHEGEKLVKFSQAGQGRVSPVSEVDLGIYQLQCSEK
SQ  LLEERVEALGHEAEKCKQQAKSLLKEGKKSQALRCLRGSKRVEKKADRLFAQLETVKGILDRIANSQTDRLVMQAYQAGV
SQ  AALRISLKGVTVERAENLVDQIQELCDTQDEVNQTLASGAPDAGEDSEDLEEELKSLMEKSVPENDLFPAVPTHPITPPR
SQ  KTDLPDAAFVQFLPSVPNPGMNITDEELDRELRRLTVSDKGLPRESVSPQRRLEPAQ
//
ID  Q8WUX9;
PN  Charged multivesicular body protein 7;
GN  CHMP7;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16856878}. Nucleus envelope {ECO:0000269|PubMed:26040712}. Nucleus envelope {ECO:0000269|PubMed:28242692}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area (PubMed:16856878). Localizes to the reforming nuclear envelope on chromatin disks during late anaphase (PubMed:26040712, PubMed:28242692). {ECO:0000269|PubMed:16856878, ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}.
DR  UNIPROT: Q8WUX9;
DR  UNIPROT: B2RDT3;
DR  UNIPROT: B4DKJ6;
DR  UNIPROT: D3DSS1;
DR  UNIPROT: Q8NDM1;
DR  UNIPROT: Q9BT50;
DR  Pfam: PF03357;
DR  OMIM: 611130;
DE  Function: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope (NE) during late anaphase (PubMed:26040712). Together with SPAST, the ESCRT-III complex promotes NE sealing and mitotic spindle disassembly during late anaphase (PubMed:28242692, PubMed:26040712). Recruited to the reforming NE during anaphase by LEMD2 (PubMed:28242692). Plays a role in the endosomal sorting pathway (PubMed:16856878). {ECO:0000269|PubMed:16856878, ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-25869447; Score: 0.66
DE  Interaction: P62826; IntAct: EBI-25890253; Score: 0.56
DE  Interaction: Q15102; IntAct: EBI-757165; Score: 0.55
DE  Interaction: Q96GX1; IntAct: EBI-11394923; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-11513083; Score: 0.54
DE  Interaction: Q9BY43; IntAct: EBI-11513112; Score: 0.37
DE  Interaction: Q96CF2; IntAct: EBI-11513134; Score: 0.37
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q9BYV6; IntAct: EBI-22022524; Score: 0.00
DE  Interaction: P55212; IntAct: EBI-25835897; Score: 0.56
DE  Interaction: P06307; IntAct: EBI-25837149; Score: 0.56
DE  Interaction: P28329; IntAct: EBI-25838258; Score: 0.56
DE  Interaction: G5E9A7; IntAct: EBI-25843392; Score: 0.56
DE  Interaction: P22607; IntAct: EBI-25855156; Score: 0.56
DE  Interaction: Q0VDC6; IntAct: EBI-25856156; Score: 0.56
DE  Interaction: Q14957; IntAct: EBI-25863073; Score: 0.56
DE  Interaction: P06396; IntAct: EBI-25864746; Score: 0.56
DE  Interaction: P54652; IntAct: EBI-25870109; Score: 0.56
DE  Interaction: P13473; IntAct: EBI-25874252; Score: 0.56
DE  Interaction: D3DTS7; IntAct: EBI-25883702; Score: 0.56
DE  Interaction: O14645; IntAct: EBI-25903256; Score: 0.56
DE  Interaction: O14901; IntAct: EBI-25906055; Score: 0.56
DE  Interaction: Q9BVL2; IntAct: EBI-25908519; Score: 0.56
DE  Interaction: Q9UMX0; IntAct: EBI-25921437; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25933071; Score: 0.56
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
GO  GO:1904930;
GO  GO:0000421;
GO  GO:0005829;
GO  GO:0000815;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0005765;
GO  GO:0030496;
GO  GO:0005771;
GO  GO:0032585;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005886;
GO  GO:0097352;
GO  GO:0006914;
GO  GO:1904903;
GO  GO:0010458;
GO  GO:1902774;
GO  GO:0045324;
GO  GO:0032511;
GO  GO:0090148;
GO  GO:0061952;
GO  GO:0007080;
GO  GO:0036258;
GO  GO:0071985;
GO  GO:0061763;
GO  GO:0060548;
GO  GO:0031468;
GO  GO:0006997;
GO  GO:0001778;
GO  GO:0071168;
GO  GO:0015031;
GO  GO:1901673;
GO  GO:0043162;
GO  GO:0006900;
GO  GO:0051469;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWSPEREAEAPAGGDPAGLLPPEWEEDEERMSFLFSAFKRSREVNSTDWDSKMGFWAPLVLSHSRRQGVVRLRLRDLQEA
SQ  FQRKGSVPLGLATVLQDLLRRGELQRESDFMASVDSSWISWGVGVFLLKPLKWTLSNMLGDNKVPAEEVLVAVELLKEKA
SQ  EEVYRLYQNSPLSSHPVVALSELSTLCANSCPDERTFYLVLLQLQKEKRVTVLEQNGEKIVKFARGPRAKVSPVNDVDVG
SQ  VYQLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQM
SQ  VFNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKEPLDLPD
SQ  NPRNRHFTNSVPNPRISDAELEAELEKLSLSEGGLVPSSKSPKRQLEPTLKPL
//
ID  Q8R1T1;
PN  Charged multivesicular body protein 7;
GN  Chmp7;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}.
DR  UNIPROT: Q8R1T1;
DR  UNIPROT: Q8CFW4;
DR  Pfam: PF03357;
DE  Function: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope (NE) during late anaphase (By similarity). Together with SPAST, the ESCRT-III complex promotes NE sealing and mitotic spindle disassembly during late anaphase (By similarity). Recruited to the reforming NE during anaphase by LEMD2 (By similarity). Plays a role in the endosomal sorting pathway (By similarity). {ECO:0000250|UniProtKB:Q8WUX9}.
DE  Reference Proteome: Yes;
GO  GO:1904930;
GO  GO:0000421;
GO  GO:0000785;
GO  GO:0005829;
GO  GO:0000815;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0005765;
GO  GO:0030496;
GO  GO:0005771;
GO  GO:0032585;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005886;
GO  GO:0097352;
GO  GO:0006914;
GO  GO:0010458;
GO  GO:1902774;
GO  GO:0045324;
GO  GO:0032511;
GO  GO:0090148;
GO  GO:0061952;
GO  GO:0007080;
GO  GO:0036258;
GO  GO:0071985;
GO  GO:0061763;
GO  GO:0060548;
GO  GO:0031468;
GO  GO:0006997;
GO  GO:0001778;
GO  GO:0071168;
GO  GO:0015031;
GO  GO:1901673;
GO  GO:0043162;
GO  GO:0006900;
GO  GO:0051469;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWSPEREAQAPTGGDPAGLLPPEWEEDEERMSFLFSAFKRSREVNSTDWDSKMGFWAPLVLSHSRRQGVVRLRLRDLQEA
SQ  FQRKGSVPLGLATVLQDLLRRGELQRESDFMASVDSSWISWGVGVFLLKPLKWTLSNMLGDHKVPAEEVLVAVELLKEKA
SQ  EEVYRLYQNSPLSSHPVVALSELSALCANSCPDERTFYLVLLQLQKEKRVTVLEQNGEKIVKFARGPHAKVSPVNDVDVG
SQ  VYQLMQSEQLLSRKVESLSQESERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQM
SQ  VFNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTTEPLSLLE
SQ  TPQETTLYTNSVPKPRILDAELEAELEKLSLSEGGLIPSSKSPKRQLEPTL
//
ID  Q5R812;
PN  Charged multivesicular body protein 7;
GN  CHMP7;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}.
DR  UNIPROT: Q5R812;
DR  Pfam: PF03357;
DE  Function: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope (NE) during late anaphase (By similarity). Together with SPAST, the ESCRT-III complex promotes NE sealing and mitotic spindle disassembly during late anaphase (By similarity). Recruited to the reforming NE during anaphase by LEMD2 (By similarity). Plays a role in the endosomal sorting pathway (By similarity). {ECO:0000250|UniProtKB:Q8WUX9}.
DE  Reference Proteome: Yes;
GO  GO:1904930;
GO  GO:0000815;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0005765;
GO  GO:0030496;
GO  GO:0032585;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0097352;
GO  GO:0010458;
GO  GO:1902774;
GO  GO:0045324;
GO  GO:0061952;
GO  GO:0007080;
GO  GO:0071985;
GO  GO:0060548;
GO  GO:0031468;
GO  GO:0001778;
GO  GO:0015031;
GO  GO:1901673;
GO  GO:0043162;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWSPEREAEAPAGGDPAGLLPPEWEEDEERMSFLFSAFKRSREVNSTDWDSKMGFWAPLVLSHSRRQGVVRLRLRDLQEA
SQ  FQRKGSVPLGLATVLQDLLRRGELQRESDFMASVDSSWISWGVGVFLLKPLKWTLSNMLGDNKVPAEEVLVAVELLKEKA
SQ  EEVYRLYQSSPLSSHPVVALSELSTLCANSCPDERTFYLVLLQLQKEKRVTVLEQNGEKIVKFARGPHAKVSPVNDVDVG
SQ  VYQLMQSEQLLSRKVESLSQEAERCKEEARRACRAGKKQLALRSLKAKQRTEKRIEALHAKLDTVQGILDRIYASQTDQM
SQ  VFNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVTNGLDFDSEELEKELDILLQDTTKEPLDLPD
SQ  NPRDRHFTNSVPNPRISDAGLEAELEKLSLSEGGLVPSGKSPKRQLEPTLKPL
//
ID  Q7T0X5;
PN  Charged multivesicular body protein 7;
GN  chmp7;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the nucleus envelope during late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}.
DR  UNIPROT: Q7T0X5;
DR  Pfam: PF03357;
DE  Function: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope during late anaphase. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. {ECO:0000250|UniProtKB:Q8WUX9}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6P5F9; IntAct: EBI-11606853; Score: 0.35
GO  GO:0000815;
GO  GO:0005635;
GO  GO:0010458;
GO  GO:0045324;
GO  GO:0031468;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPLSCNPPEWEDDERMSFLFSAFKRTRDVNTCDWDGKMKFWIPLILTHARAQGLLSITLSQLENDFRRKGCAPMGLRTV
SQ  IQEMIRQGTLRKETDFVSGVSSGWLSWGMRQLVIRPLRWTIGTMLGSQVGPDEPLVIPEVIKERAALVLQRYQSSTFRSF
SQ  PLLCEEEVHTLCAEICPNPSALNLVLLQLQGDKKICVLERAGQKLVKFVRVSVGQVEPISESDLGIYQLQQGEKLLSERL
SQ  QSAGEESNRLTEEARTYNRAGNKNQALRCLRKRKLVERRITELQNKQDNIQGILERISAAETDRKVVSAYQMGVSALKQA
SQ  LKDVTLEKAESIVDQIQEYCDLQDDLSQTLSSVTDADVDSDDLERELNEILQNEEMIIDLPDVPSGPVIISPKRPTEWKM
SQ  DQAAHSPADGSFLRSVPEPMLQ
//
ID  Q5FW14;
PN  Charged multivesicular body protein 7;
GN  chmp7;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the nucleus envelope during late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}.
DR  UNIPROT: Q5FW14;
DR  Pfam: PF03357;
DE  Function: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope during late anaphase. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. {ECO:0000250|UniProtKB:Q8WUX9}.
DE  Reference Proteome: Yes;
GO  GO:0000815;
GO  GO:0005771;
GO  GO:0005635;
GO  GO:0010458;
GO  GO:0045324;
GO  GO:0032511;
GO  GO:0031468;
GO  GO:0015031;
GO  GO:0006900;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALSCYPPEWDDDERMSFLFSAFKQTRDVNTSDWDGKMKFWIPLILKHARAQGLLSISLSQLERDFRRKGFAPLGLRIV
SQ  IQEMMRQGTLRKESDYVSNVSSGWLSWGMRQLVIRPLRWTIGTVLGSQMGPDEPLVIPEIIKERAALVLQRYQSSPLRAL
SQ  PLLSEEEVRTLCAEICPNPSALNLVLLQLQGDKKICVLERAGKKLVKFVRVSVGQVDPISESDLGIYELQQSEKLLSERL
SQ  QSAGEESDRLTEEARTYNRAGNKHQALRCLRKRKLLERRITELQNKQDTVQGILERIAAAETDRKVVSAYQMGVSALKLA
SQ  LKDVTMEKAESIVDQIQEYCDLQDDLSQTLASVSDADIDSEDLEKELNDILQNKEMIVDLPDVPSGPVVISPQRPTEWET
SQ  DQDIDSEDLEKELNDILQKEEMIVDLPDVPSGPVVISPQRPTEWKTDQASRSPADGSFSRSVPEPVLQ
//
ID  Q96LT7;
PN  Guanine nucleotide exchange factor C9orf72;
GN  C9orf72;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:21944779, ECO:0000269|PubMed:27037575}. Cytoplasm {ECO:0000269|PubMed:21944778, ECO:0000269|PubMed:27037575, ECO:0000269|PubMed:27193190}. Cytoplasm, P-body {ECO:0000269|PubMed:27037575}. Cytoplasm, Stress granule {ECO:0000269|PubMed:27037575}. Endosome {ECO:0000269|PubMed:24549040}. Lysosome {ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:27559131}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24549040}. Secreted {ECO:0000269|PubMed:24549040}. Cell projection, axon {ECO:0000269|PubMed:27723745}. Cell projection, growth cone {ECO:0000269|PubMed:27723745}. Perikaryon {ECO:0000250|UniProtKB:Q6DFW0}. Note=Detected in the cytoplasm of neurons from brain tissue (PubMed:21944778). Detected in the nucleus in fibroblasts (PubMed:21944779). During corticogenesis, transitions from being predominantly cytoplasmic to a more even nucleocytoplasmic distribution (By similarity). {ECO:0000250|UniProtKB:Q6DFW0, ECO:0000269|PubMed:21944778, ECO:0000269|PubMed:21944779, ECO:0000269|PubMed:27037575}. [Isoform 1]: Perikaryon {ECO:0000269|PubMed:26174152}. Cell projection, dendrite {ECO:0000269|PubMed:26174152}. Presynapse {ECO:0000250|UniProtKB:Q6DFW0}. Postsynapse {ECO:0000250|UniProtKB:Q6DFW0}. Note=Expressed diffusely throughout the cytoplasm and dendritic processes of cerebellar Purkinje cells. Also expressed diffusely throughout the cytoplasm of spinal motor neurons. {ECO:0000269|PubMed:26174152}. [Isoform 2]: Nucleus membrane {ECO:0000269|PubMed:26174152}; Peripheral membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:26174152}. Note=Detected at the nuclear membrane of cerebellar Purkinje cells and spinal motor neurons. Also shows diffuse nuclear expression in spinal motor neurons. {ECO:0000269|PubMed:26174152}.
DR  UNIPROT: Q96LT7;
DR  UNIPROT: A8K5W0;
DR  UNIPROT: D3DRK6;
DR  UNIPROT: G8I0B6;
DR  UNIPROT: Q6NUS9;
DR  PDB: 6LT0;
DR  PDB: 6V4U;
DR  PDB: 7MGE;
DR  PDB: 7O2W;
DR  Pfam: PF15019;
DR  PROSITE: PS51835;
DR  OMIM: 105550;
DR  OMIM: 614260;
DR  DisGeNET: 203228;
DE  Function: Component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy (PubMed:27193190, PubMed:27103069, PubMed:27617292, PubMed:28195531, PubMed:32303654). In the complex, C9orf72 and SMCR8 probably constitute the catalytic subunits that promote the exchange of GDP to GTP, converting inactive GDP-bound RAB8A and RAB39B into their active GTP-bound form, thereby promoting autophagosome maturation (PubMed:27103069). The C9orf72-SMCR8 complex also acts as a regulator of autophagy initiation by interacting with the ULK1/ATG1 kinase complex and modulating its protein kinase activity (PubMed:27617292). As part of the C9orf72-SMCR8 complex, stimulates RAB8A and RAB11A GTPase activity in vitro (PubMed:32303654). Positively regulates initiation of autophagy by regulating the RAB1A-dependent trafficking of the ULK1/ATG1 kinase complex to the phagophore which leads to autophagosome formation (PubMed:27334615). Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates (PubMed:27559131). Plays a role in endosomal trafficking (PubMed:24549040). May be involved in regulating the maturation of phagosomes to lysosomes (By similarity). Promotes the lysosomal localization and lysosome-mediated degradation of CARM1 which leads to inhibition of starvation-induced lipid metabolism (By similarity). Regulates actin dynamics in motor neurons by inhibiting the GTP-binding activity of ARF6, leading to ARF6 inactivation (PubMed:27723745). This reduces the activity of the LIMK1 and LIMK2 kinases which are responsible for phosphorylation and inactivation of cofilin, leading to CFL1/cofilin activation (PubMed:27723745). Positively regulates axon extension and axon growth cone size in spinal motor neurons (PubMed:27723745). Required for SMCR8 protein expression and localization at pre- and post-synaptic compartments in the forebrain, also regulates protein abundance of RAB3A and GRIA1/GLUR1 in post- synaptic compartments in the forebrain and hippocampus (By similarity). Plays a role within the hematopoietic system in restricting inflammation and the development of autoimmunity (By similarity). {ECO:0000250|UniProtKB:Q6DFW0, ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:27103069, ECO:0000269|PubMed:27193190, ECO:0000269|PubMed:27334615, ECO:0000269|PubMed:27559131, ECO:0000269|PubMed:27617292, ECO:0000269|PubMed:27723745, ECO:0000269|PubMed:28195531, ECO:0000269|PubMed:32303654}. [Isoform 1]: Regulates stress granule assembly in response to cellular stress. {ECO:0000269|PubMed:27037575}. [Isoform 2]: Does not play a role in regulation of stress granule assembly in response to cellular stress. {ECO:0000269|PubMed:27037575}.
DE  Disease: Frontotemporal dementia and/or amyotrophic lateral sclerosis 1 (FTDALS1) [MIM:105550]: An autosomal dominant neurodegenerative disorder characterized by adult onset of frontotemporal dementia and/or amyotrophic lateral sclerosis in an affected individual. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. {ECO:0000269|PubMed:21944778, ECO:0000269|PubMed:21944779, ECO:0000269|PubMed:22936364, ECO:0000269|PubMed:30366907}. Note=The disease is caused by variants affecting the gene represented in this entry. In the first intron of the gene, the expansion of a GGGGCC hexanucleotide that can vary from 10 to thousands of repeats, represents the most common genetic cause of both familial and sporadic FTDALS. The hexanucleotide repeat expansion (HRE) is structurally polymorphic and during transcription, is responsible for the formation of RNA and DNA G-quadruplexes resulting in the production of aborted transcripts at the expense of functional transcripts. The accumulation of those aborted transcripts may cause nucleolar stress and indirectly cell death (PubMed:24598541). The expanded GGGGCC repeats are bidirectionally transcribed into repetitive RNA, which forms sense and antisense RNA foci. Remarkably, despite being within a non-coding region, these repetitive RNAs can be translated in every reading frame to form five different dipeptide repeat proteins (DPRs) -- poly-GA, poly-GP, poly-GR, poly-PA and poly-PR -- via a non-canonical mechanism known as repeat-associated non-ATG (RAN) translation. These dipeptide repeat proteins (DPRs) co-aggregate in the characteristic SQSTM1- positive TARDBP negative inclusions found in FTLD/ALS patients with C9orf72 repeat expansion (PubMed:24132570). {ECO:0000269|PubMed:24132570, ECO:0000269|PubMed:24598541}.
DE  Reference Proteome: Yes;
DE  Interaction: O08788; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q8TDY2; IntAct: EBI-16693641; Score: 0.71
DE  Interaction: P49770; IntAct: EBI-8634732; Score: 0.67
DE  Interaction: Q96SB4; IntAct: EBI-6660776; Score: 0.44
DE  Interaction: O43186; IntAct: EBI-10290948; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-10290958; Score: 0.56
DE  Interaction: Q13287; IntAct: EBI-10290968; Score: 0.56
DE  Interaction: Q53XC2; IntAct: EBI-10290978; Score: 0.56
DE  Interaction: Q9BPX4; IntAct: EBI-10290998; Score: 0.56
DE  Interaction: Q61539; IntAct: EBI-11143365; Score: 0.35
DE  Interaction: Q8TEV9; IntAct: EBI-11773551; Score: 0.81
DE  Interaction: P38432; IntAct: EBI-24341833; Score: 0.56
DE  Interaction: Q9H8Y1; IntAct: EBI-24620575; Score: 0.60
DE  Interaction: Q9NP66; IntAct: EBI-23775639; Score: 0.56
DE  Interaction: Q86UV6; IntAct: EBI-24752111; Score: 0.56
DE  Interaction: O75817; IntAct: EBI-23856758; Score: 0.56
DE  Interaction: Q17R54; IntAct: EBI-24600914; Score: 0.56
DE  Interaction: O75385; IntAct: EBI-16693788; Score: 0.67
DE  Interaction: O75143; IntAct: EBI-16693805; Score: 0.69
DE  Interaction: P62820; IntAct: EBI-16697556; Score: 0.58
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: Q9HAD4; IntAct: EBI-26618111; Score: 0.56
DE  Interaction: Q86VY4; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q8WXF1; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q9BSF8; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: O15015; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q13610; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P20290; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: O15235; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q9P086; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P62891; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: O75935; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P62314; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q9BWH6; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q9H6T0; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P26038; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q14137; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q9BPZ7; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q9Y4Y9; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P31942; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: O14647; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q06455; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P62273; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q8N184; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q96RE9; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q9P0L1; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P09496; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P05388; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P62987; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: P35637; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q9Y446; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q8IWZ3; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q9Y2P7; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: Q9Z2X2; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q5EG47; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: O08547; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q6P8X1; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: P46467; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q6PA06; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q8BGH2; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q8R5A6; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q91YL2; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9R1P0; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: O35963; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9ESK9; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q8BHC1; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q921F2; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q64337; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: A2AH22; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9JKF1; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: P07901; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9JHU4; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: P63017; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q7TMY8; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q8BND3; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9JIS5; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q8CFD4; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9WTV7; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q99KJ8; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: O35226; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: P35279; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9WUN2; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9D0I4; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q504M8; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9CX56; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q920Q4; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q8K4Q0; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: P55258; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9WUD1; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: P46460; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q3UDP0; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q3UMB5; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: Q9JLV1; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: A2AN08; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: P52332; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: A2AKX3; IntAct: EBI-26613562; Score: 0.35
DE  Interaction: P61006; IntAct: EBI-26618111; Score: 0.44
DE  Interaction: Q96DA2; IntAct: EBI-26618130; Score: 0.44
DE  Interaction: Q9UHD2; IntAct: EBI-26618650; Score: 0.44
DE  Interaction: Q86YD7; IntAct: EBI-28997307; Score: 0.35
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
GO  GO:0070161;
GO  GO:0005776;
GO  GO:0044295;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005768;
GO  GO:0005615;
GO  GO:0090543;
GO  GO:0032045;
GO  GO:0043231;
GO  GO:0005764;
GO  GO:0044304;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0043204;
GO  GO:0098794;
GO  GO:0098793;
GO  GO:0005085;
GO  GO:0031267;
GO  GO:0006914;
GO  GO:0048675;
GO  GO:0006897;
GO  GO:1902774;
GO  GO:0045920;
GO  GO:1904425;
GO  GO:0050777;
GO  GO:0001933;
GO  GO:0043547;
GO  GO:0016239;
GO  GO:0110053;
GO  GO:2000785;
GO  GO:0010506;
GO  GO:0032880;
GO  GO:1903432;
GO  GO:0034063;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSTLCPPPSPAVAKTEIALSGKSPLLAATFAYWDNILGPRVRHIWAPKTEQVLLSDGEITFLANHTLNGEILRNAESGAI
SQ  DVKFFVLSEKGVIIVSLIFDGNWNGDRSTYGLSIILPQTELSFYLPLHRVCVDRLTHIIRKGRIWMHKERQENVQKIILE
SQ  GTERMEDQGQSIIPMLTGEVIPVMELLSSMKSHSVPEEIDIADTVLNDDDIGDSCHEGFLLNAISSHLQTCGCSVVVGSS
SQ  AEKVNKIVRTLCLFLTPAERKCSRLCEAESSFKYESGLFVQGLLKDSTGSFVLPFRQVMYAPYPTTHIDVDVNTVKQMPP
SQ  CHEHIYNQRRYMRSELTAFWRATSEEDMAQDTIIYTDESFTPDLNIFQDVLHRDTLVKAFLDQVFQLKPGLSLRSTFLAQ
SQ  FLLVLHRKALTLIKYIEDDTQKGKKPFKSLRNLKIDLDLTAEGDLNIIMALAEKIKPGLHSFIFGRPFYTSVQERDVLMT
SQ  F
//
ID  Q17QE5;
PN  Calcium and integrin-binding protein 1;
GN  CIB1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q99828}; Lipid- anchor {ECO:0000250|UniProtKB:Q99828}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q99828}. Cell membrane {ECO:0000250|UniProtKB:Q99828}. Apical cell membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:Q99828}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99828}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q99828}. Cytoplasm {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99828}. Nucleus {ECO:0000250|UniProtKB:Q99828}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q99828}. Perikaryon {ECO:0000250|UniProtKB:Q99828}. Note=Colocalized with PPP3R1 at the cell membrane of cardiomyocytes in the hypertrophic heart (By similarity). Colocalized with NBR1 to the perinuclear region. Colocalizes with TAS1R2 in apical regions of taste receptor cells. Colocalized with RAC3 in the perinuclear area and at the cell periphery. Colocalized with PAK1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Redistributed to the cytoskeleton upon platelet aggregation. Translocates from the cytosol to the plasma membrane in a calcium-dependent manner. Colocalized with PLK3 at centrosomes in ductal breast carcinoma cells. {ECO:0000250}.
DR  UNIPROT: Q17QE5;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin- mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation- dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0030424;
GO  GO:0071944;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0032433;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0005509;
GO  GO:0000287;
GO  GO:0043495;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0007155;
GO  GO:0051301;
GO  GO:0071363;
GO  GO:1990090;
GO  GO:0071356;
GO  GO:0031122;
GO  GO:0007113;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0045653;
GO  GO:0007026;
GO  GO:0010977;
GO  GO:0051898;
GO  GO:0001933;
GO  GO:0030220;
GO  GO:0070886;
GO  GO:0043085;
GO  GO:0033630;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0090050;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:0070374;
GO  GO:2000256;
GO  GO:0051092;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0071902;
GO  GO:0090314;
GO  GO:1900026;
GO  GO:0051302;
GO  GO:0042127;
GO  GO:0002931;
GO  GO:0007286;
GO  GO:0038163;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEHRSVEESLQARVSLEQILSLPELKANPFKERICKVFSTS
SQ  PSRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSQLVNCLTGESEDTRLSASEMKQLIDNILEES
SQ  DIDRDGTINLSEFQHVISRSPDFASSFKIVL
//
ID  Q99828;
PN  Calcium and integrin-binding protein 1;
GN  CIB1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane; Lipid-anchor. Cell membrane, sarcolemma. Cell membrane. Apical cell membrane. Cell projection, ruffle membrane. Cell projection, filopodium tip. Cell projection, growth cone {ECO:0000269|PubMed:21215777}. Cell projection, lamellipodium {ECO:0000269|PubMed:21215777}. Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Nucleus {ECO:0000269|PubMed:30068544}. Cell projection, neuron projection {ECO:0000269|PubMed:21215777}. Perikaryon {ECO:0000269|PubMed:21215777}. Note=Colocalized with PPP3R1 at the cell membrane of cardiomyocytes in the hypertrophic heart (By similarity). Colocalized with NBR1 to the perinuclear region. Colocalizes with TAS1R2 in apical regions of taste receptor cells. Colocalized with RAC3 in the perinuclear area and at the cell periphery. Colocalized with PAK1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Redistributed to the cytoskeleton upon platelet aggregation. Translocates from the cytosol to the plasma membrane in a calcium-dependent manner. Colocalized with PLK3 at centrosomes in ductal breast carcinoma cells. {ECO:0000250}. [Isoform 2]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:23503467}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:23503467}.
DR  UNIPROT: Q99828;
DR  UNIPROT: B5BU40;
DR  UNIPROT: H6WJF3;
DR  UNIPROT: O00693;
DR  UNIPROT: O00735;
DR  UNIPROT: Q6IB49;
DR  UNIPROT: Q96J54;
DR  UNIPROT: Q99971;
DR  PDB: 1DGU;
DR  PDB: 1DGV;
DR  PDB: 1XO5;
DR  PDB: 1Y1A;
DR  PDB: 2L4H;
DR  PDB: 2L4I;
DR  PDB: 2LM5;
DR  PDB: 6OCX;
DR  PDB: 6OD0;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 602293;
DR  OMIM: 618267;
DR  DisGeNET: 10519;
DE  Function: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin- mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation- dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells. [Isoform 2]: Plays a regulatory role in angiogenesis and tumor growth by mediating PKD/PRKD2-induced vascular endothelial growth factor A (VEGFA) secretion. {ECO:0000269|PubMed:23503467}. (Microbial infection) Involved in keratinocyte-intrinsic immunity to human beta-papillomaviruses (HPVs). {ECO:0000269|PubMed:30068544}.
DE  Disease: Epidermodysplasia verruciformis 3 (EV3) [MIM:618267]: A form of epidermodysplasia verruciformis, a rare genodermatosis associated with a high risk of skin carcinoma that results from an abnormal susceptibility to infection by specific human papillomaviruses, including the oncogenic HPV5. Infection leads to the early development of disseminated flat wart-like and pityriasis versicolor-like skin lesions. Cutaneous Bowen's carcinomas in situ and invasive squamous cell carcinomas develop in about half of the patients, mainly on sun- exposed skin areas. EV3 inheritance is autosomal recessive. {ECO:0000269|PubMed:30068544}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P11802; IntAct: EBI-3914485; Score: 0.37
DE  Interaction: Q92993; IntAct: EBI-25912340; Score: 0.56
DE  Interaction: P49810; IntAct: EBI-7017541; Score: 0.56
DE  Interaction: Q01780; IntAct: EBI-373746; Score: 0.00
DE  Interaction: O00401; IntAct: EBI-8290175; Score: 0.63
DE  Interaction: P17301; IntAct: EBI-8290662; Score: 0.40
DE  Interaction: Q5NHQ1; IntAct: EBI-2799151; Score: 0.00
DE  Interaction: A0A6L8PDF7; IntAct: EBI-2810599; Score: 0.00
DE  Interaction: Q81Y46; IntAct: EBI-2813274; Score: 0.00
DE  Interaction: A0A6H3ACH2; IntAct: EBI-2817511; Score: 0.00
DE  Interaction: A0A6L7HLB1; IntAct: EBI-2817492; Score: 0.00
DE  Interaction: A0A6L8PAR8; IntAct: EBI-2817518; Score: 0.00
DE  Interaction: Q74RZ6; IntAct: EBI-2843481; Score: 0.00
DE  Interaction: A0A0H2W7X9; IntAct: EBI-2848345; Score: 0.00
DE  Interaction: Q96GD4; IntAct: EBI-3935743; Score: 0.37
DE  Interaction: Q13153; IntAct: EBI-9074151; Score: 0.40
DE  Interaction: Q8IUH5; IntAct: EBI-9091611; Score: 0.37
DE  Interaction: Q04637; IntAct: EBI-24338171; Score: 0.56
DE  Interaction: Q3KNT9; IntAct: EBI-24519662; Score: 0.56
DE  Interaction: P40199; IntAct: EBI-25265860; Score: 0.56
DE  Interaction: P10092; IntAct: EBI-24613829; Score: 0.56
DE  Interaction: O43639; IntAct: EBI-23674636; Score: 0.56
DE  Interaction: Q8NEA6; IntAct: EBI-24536125; Score: 0.56
DE  Interaction: P26842; IntAct: EBI-24432861; Score: 0.56
DE  Interaction: Q9H7N4; IntAct: EBI-24557755; Score: 0.56
DE  Interaction: Q3SY00; IntAct: EBI-24793494; Score: 0.56
DE  Interaction: O00746; IntAct: EBI-24538334; Score: 0.56
DE  Interaction: O60422; IntAct: EBI-24540023; Score: 0.56
DE  Interaction: P48449; IntAct: EBI-24540975; Score: 0.56
DE  Interaction: P23759; IntAct: EBI-24553159; Score: 0.56
DE  Interaction: Q7RTT5; IntAct: EBI-24583715; Score: 0.56
DE  Interaction: Q6ZSB9; IntAct: EBI-24594105; Score: 0.56
DE  Interaction: Q6UXG2; IntAct: EBI-24635958; Score: 0.56
DE  Interaction: P04066; IntAct: EBI-24638052; Score: 0.56
DE  Interaction: O00322; IntAct: EBI-21504674; Score: 0.35
DE  Interaction: Q7Z402; IntAct: EBI-21657108; Score: 0.35
DE  Interaction: Q99683; IntAct: EBI-15804106; Score: 0.66
DE  Interaction: P05362; IntAct: EBI-25872248; Score: 0.56
DE  Interaction: P61981; IntAct: EBI-25902198; Score: 0.56
DE  Interaction: Q15047; IntAct: EBI-25909149; Score: 0.56
DE  Interaction: Q8TAP4; IntAct: EBI-25926078; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25931600; Score: 0.56
GO  GO:0016324;
GO  GO:0030424;
GO  GO:0071944;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0070062;
GO  GO:0032433;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0031982;
GO  GO:0005509;
GO  GO:0008427;
GO  GO:0000287;
GO  GO:0030291;
GO  GO:0043495;
GO  GO:0031267;
GO  GO:0044325;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0007155;
GO  GO:0051301;
GO  GO:0006974;
GO  GO:0071363;
GO  GO:1990090;
GO  GO:0071356;
GO  GO:0031122;
GO  GO:0006302;
GO  GO:0007113;
GO  GO:0097191;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0045653;
GO  GO:0007026;
GO  GO:0010977;
GO  GO:0051898;
GO  GO:0001933;
GO  GO:0030220;
GO  GO:0070886;
GO  GO:0043085;
GO  GO:0033630;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0090050;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:0070374;
GO  GO:2000256;
GO  GO:0051092;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0071902;
GO  GO:0090314;
GO  GO:1900026;
GO  GO:0051302;
GO  GO:0042127;
GO  GO:0002931;
GO  GO:0007286;
GO  GO:0038163;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10366599};
SQ  MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEQRSVESSLRAQVPFEQILSLPELKANPFKERICRVFSTS
SQ  PAKDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSRLVNCLTGEGEDTRLSASEMKQLIDNILEES
SQ  DIDRDGTINLSEFQHVISRSPDFASSFKIVL
//
ID  Q9Z0F4;
PN  Calcium and integrin-binding protein 1;
GN  Cib1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q99828}; Lipid- anchor {ECO:0000250|UniProtKB:Q99828}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q99828}. Cell membrane {ECO:0000250|UniProtKB:Q99828}. Apical cell membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:Q99828}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99828}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q99828}. Cytoplasm {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99828}. Nucleus {ECO:0000250|UniProtKB:Q99828}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q99828}. Perikaryon {ECO:0000250|UniProtKB:Q99828}. Note=Colocalized with PPP3R1 at the cell membrane of cardiomyocytes in the hypertrophic heart (By similarity). Colocalized with NBR1 to the perinuclear region. Colocalizes with TAS1R2 in apical regions of taste receptor cells. Colocalized with RAC3 in the perinuclear area and at the cell periphery. Colocalized with PAK1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Redistributed to the cytoskeleton upon platelet aggregation. Translocates from the cytosol to the plasma membrane in a calcium-dependent manner. Colocalized with PLK3 at centrosomes in ductal breast carcinoma cells. {ECO:0000250}.
DR  UNIPROT: Q9Z0F4;
DR  UNIPROT: Q3TN80;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin- mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation- dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells. {ECO:0000269|PubMed:16982698, ECO:0000269|PubMed:17975111, ECO:0000269|PubMed:19691476, ECO:0000269|PubMed:20804551, ECO:0000269|PubMed:22128142}.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0030424;
GO  GO:0071944;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0005783;
GO  GO:0032433;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0005509;
GO  GO:0008427;
GO  GO:0000287;
GO  GO:0008022;
GO  GO:0019901;
GO  GO:0030291;
GO  GO:0043495;
GO  GO:0031267;
GO  GO:0044325;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0007155;
GO  GO:0051301;
GO  GO:0006974;
GO  GO:0071363;
GO  GO:1990090;
GO  GO:0071356;
GO  GO:0031122;
GO  GO:0007113;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0045653;
GO  GO:0007026;
GO  GO:0010977;
GO  GO:0051898;
GO  GO:0001933;
GO  GO:0030220;
GO  GO:0070886;
GO  GO:0043085;
GO  GO:0033630;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0090050;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:0070374;
GO  GO:2000256;
GO  GO:0051092;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0071902;
GO  GO:0090314;
GO  GO:1900026;
GO  GO:0051302;
GO  GO:0042127;
GO  GO:0002931;
GO  GO:0007286;
GO  GO:0038163;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPPEQRTVEESLHTRVSFEQILSLPELKANPFKERICMVFSTS
SQ  PTRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLDREDLSQLVNCLTGEGEDTRLSASEMKQLIDNILEES
SQ  DIDRDGTINLSEFQHVISRSPDFASSFKIVL
//
ID  Q9R010;
PN  Calcium and integrin-binding protein 1;
GN  Cib1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q99828}; Lipid- anchor {ECO:0000250|UniProtKB:Q99828}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q99828}. Cell membrane {ECO:0000250|UniProtKB:Q99828}. Apical cell membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:Q99828}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99828}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q99828}. Cytoplasm {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99828}. Nucleus {ECO:0000250|UniProtKB:Q99828}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q99828}. Perikaryon {ECO:0000250|UniProtKB:Q99828}. Note=Colocalized with PPP3R1 at the cell membrane of cardiomyocytes in the hypertrophic heart (By similarity). Colocalized with NBR1 to the perinuclear region. Colocalizes with TAS1R2 in apical regions of taste receptor cells. Colocalized with RAC3 in the perinuclear area and at the cell periphery. Colocalized with PAK1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Redistributed to the cytoskeleton upon platelet aggregation. Translocates from the cytosol to the plasma membrane in a calcium-dependent manner. Colocalized with PLK3 at centrosomes in ductal breast carcinoma cells. {ECO:0000250}.
DR  UNIPROT: Q9R010;
DR  UNIPROT: Q5BKA8;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin- mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation- dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:18627437}.
DE  Reference Proteome: Yes;
DE  Interaction: P35465; IntAct: EBI-9230038; Score: 0.40
GO  GO:0016324;
GO  GO:0030424;
GO  GO:0071944;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0005783;
GO  GO:0032433;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0005509;
GO  GO:0008427;
GO  GO:0000287;
GO  GO:0008022;
GO  GO:0019901;
GO  GO:0030291;
GO  GO:0043495;
GO  GO:0031267;
GO  GO:0044325;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0007155;
GO  GO:0051301;
GO  GO:0006974;
GO  GO:0071363;
GO  GO:1990090;
GO  GO:0071356;
GO  GO:0031122;
GO  GO:0007113;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0045653;
GO  GO:0007026;
GO  GO:0010977;
GO  GO:0051898;
GO  GO:0001933;
GO  GO:0030220;
GO  GO:0070886;
GO  GO:0043085;
GO  GO:0033630;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0090050;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:0070374;
GO  GO:2000256;
GO  GO:0051092;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0071902;
GO  GO:0090314;
GO  GO:1900026;
GO  GO:0051302;
GO  GO:0042127;
GO  GO:0002931;
GO  GO:0007286;
GO  GO:0038163;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:18627437};
SQ  MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPPEHRTVEESLHTRVSFEQILSLPELKANPFKERICMVFSTS
SQ  PTRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLDREDLSRLVNCLTGEGEDTRLSASEMKQLIDNILEES
SQ  DIDRDGTINLSEFQHVISRSPDFASSFKIVL
//
ID  B1A8Z2;
PN  Calcium and integrin-binding protein 1;
GN  CIB1;
OS  9940;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q99828}; Lipid- anchor {ECO:0000250|UniProtKB:Q99828}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q99828}. Cell membrane {ECO:0000250|UniProtKB:Q99828}. Apical cell membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q99828}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:Q99828}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99828}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q99828}. Cytoplasm {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99828}. Nucleus {ECO:0000250|UniProtKB:Q99828}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q99828}. Perikaryon {ECO:0000250|UniProtKB:Q99828}. Note=Colocalized with PPP3R1 at the cell membrane of cardiomyocytes in the hypertrophic heart (By similarity). Colocalized with NBR1 to the perinuclear region. Colocalizes with TAS1R2 in apical regions of taste receptor cells. Colocalized with RAC3 in the perinuclear area and at the cell periphery. Colocalized with PAK1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Redistributed to the cytoskeleton upon platelet aggregation. Translocates from the cytosol to the plasma membrane in a calcium-dependent manner. Colocalized with PLK3 at centrosomes in ductal breast carcinoma cells. {ECO:0000250}.
DR  UNIPROT: B1A8Z2;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin- mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation- dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0005813;
GO  GO:0005783;
GO  GO:0032433;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0005654;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0005509;
GO  GO:0008427;
GO  GO:0030291;
GO  GO:0043495;
GO  GO:0031267;
GO  GO:0044325;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0007155;
GO  GO:0051301;
GO  GO:0006974;
GO  GO:1990090;
GO  GO:0071356;
GO  GO:0031122;
GO  GO:0007113;
GO  GO:0007229;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0045653;
GO  GO:0007026;
GO  GO:0010977;
GO  GO:0051898;
GO  GO:0001933;
GO  GO:0030220;
GO  GO:0070886;
GO  GO:0033630;
GO  GO:0030307;
GO  GO:0090050;
GO  GO:0001954;
GO  GO:0070374;
GO  GO:2000256;
GO  GO:0051092;
GO  GO:1903078;
GO  GO:0071902;
GO  GO:0090314;
GO  GO:1900026;
GO  GO:0051302;
GO  GO:0002931;
GO  GO:0007286;
GO  GO:0038163;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGGSGSRLSKELLAEYQDLTFLTKQEILLAHRRFCELLPQEHRSVEESLQARVSLEQILSLPELKANPFKERICKVFSTS
SQ  PSRDSLSFEDFLDLLSVFSDTATPDIKSHYAFRIFDFDDDGTLNREDLSQLVNCLTGESEDTRLSASEMKQLIDNILEES
SQ  DIDRDGTINLSEFQHVISRSPDFASSFKIVL
//
ID  Q15642;
PN  Cdc42-interacting protein 4;
GN  TRIP10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Golgi apparatus. Cell membrane. Cell projection, phagocytic cup. Note=Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ (By similarity). Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9. {ECO:0000250}. [Isoform 5]: Cytoplasm, perinuclear region.
DR  UNIPROT: Q15642;
DR  UNIPROT: B2R8A6;
DR  UNIPROT: B7WP22;
DR  UNIPROT: D6W645;
DR  UNIPROT: O15184;
DR  UNIPROT: Q53G22;
DR  UNIPROT: Q5TZN1;
DR  UNIPROT: Q6FI24;
DR  UNIPROT: Q8NFL1;
DR  UNIPROT: Q8TCY1;
DR  UNIPROT: Q8TDX3;
DR  UNIPROT: Q96RJ1;
DR  PDB: 2CT4;
DR  PDB: 2EFK;
DR  PDB: 2KE4;
DR  Pfam: PF00611;
DR  Pfam: PF00018;
DR  PROSITE: PS51741;
DR  PROSITE: PS51860;
DR  PROSITE: PS50002;
DR  OMIM: 604504;
DR  DisGeNET: 9322;
DE  Function: Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5- bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte- derived cells. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269|PubMed:11069762, ECO:0000269|PubMed:16318909, ECO:0000269|PubMed:16326391}.
DE  Reference Proteome: Yes;
DE  Interaction: P07948; IntAct: EBI-8565817; Score: 0.51
DE  Interaction: Q14974; IntAct: EBI-30827298; Score: 0.44
DE  Interaction: P60953; IntAct: EBI-7213336; Score: 0.61
DE  Interaction: Q9Y2W2; IntAct: EBI-752548; Score: 0.37
DE  Interaction: Q15642; IntAct: EBI-1268134; Score: 0.74
DE  Interaction: Q96RU3; IntAct: EBI-1647547; Score: 0.27
DE  Interaction: P48023; IntAct: EBI-7908855; Score: 0.59
DE  Interaction: A0A384KSJ5; IntAct: EBI-2817480; Score: 0.00
DE  Interaction: A0A5P8YEZ8; IntAct: EBI-2873377; Score: 0.00
DE  Interaction: Q9Y4D1; IntAct: EBI-6550032; Score: 0.52
DE  Interaction: Q9Z207; IntAct: EBI-6550121; Score: 0.40
DE  Interaction: O08808; IntAct: EBI-6550199; Score: 0.40
DE  Interaction: O00401; IntAct: EBI-24407610; Score: 0.56
DE  Interaction: Q8IUH5; IntAct: EBI-9090827; Score: 0.37
DE  Interaction: Q92558; IntAct: EBI-10236688; Score: 0.56
DE  Interaction: Q17R89; IntAct: EBI-10238339; Score: 0.56
DE  Interaction: Q1RLN5; IntAct: EBI-10239195; Score: 0.56
DE  Interaction: Q68EM7; IntAct: EBI-10249175; Score: 0.56
DE  Interaction: Q969G3; IntAct: EBI-10280647; Score: 0.56
DE  Interaction: Q9H4E5; IntAct: EBI-10306633; Score: 0.56
DE  Interaction: Q9Y3L3; IntAct: EBI-10327866; Score: 0.56
DE  Interaction: P46379; IntAct: EBI-11154173; Score: 0.35
DE  Interaction: Q6SPF0; IntAct: EBI-11160311; Score: 0.35
DE  Interaction: P54274; IntAct: EBI-11308271; Score: 0.37
DE  Interaction: Q9BSI4; IntAct: EBI-11308281; Score: 0.51
DE  Interaction: Q9NUX5; IntAct: EBI-11308291; Score: 0.37
DE  Interaction: P53933; IntAct: EBI-11533915; Score: 0.56
DE  Interaction: O15156; IntAct: EBI-24294257; Score: 0.56
DE  Interaction: Q8IZP0; IntAct: EBI-24302596; Score: 0.56
DE  Interaction: P26367; IntAct: EBI-24333764; Score: 0.56
DE  Interaction: Q8IWW6; IntAct: EBI-24337375; Score: 0.56
DE  Interaction: P50221; IntAct: EBI-25244628; Score: 0.56
DE  Interaction: P42684; IntAct: EBI-25250506; Score: 0.56
DE  Interaction: Q13671; IntAct: EBI-24484923; Score: 0.56
DE  Interaction: Q15428; IntAct: EBI-24624817; Score: 0.56
DE  Interaction: O75564; IntAct: EBI-24780027; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24376152; Score: 0.56
DE  Interaction: Q5T230; IntAct: EBI-24395781; Score: 0.56
DE  Interaction: Q9NVV9; IntAct: EBI-24455319; Score: 0.56
DE  Interaction: O43248; IntAct: EBI-24560095; Score: 0.56
DE  Interaction: Q8N9I9; IntAct: EBI-25196090; Score: 0.56
DE  Interaction: P52952; IntAct: EBI-24792337; Score: 0.56
DE  Interaction: P81408; IntAct: EBI-21535449; Score: 0.35
DE  Interaction: O15389; IntAct: EBI-21881508; Score: 0.35
DE  Interaction: Q6UY01; IntAct: EBI-21887518; Score: 0.40
DE  Interaction: Q6IN36; IntAct: EBI-16191410; Score: 0.35
DE  Interaction: Q5BJU7; IntAct: EBI-16191410; Score: 0.35
DE  Interaction: P97573; IntAct: EBI-16191410; Score: 0.50
DE  Interaction: E9PT20; IntAct: EBI-16191410; Score: 0.35
DE  Interaction: O08816; IntAct: EBI-16191410; Score: 0.35
DE  Interaction: P39052; IntAct: EBI-16191410; Score: 0.35
DE  Interaction: P18484; IntAct: EBI-16191410; Score: 0.35
DE  Interaction: P17096; IntAct: EBI-20935428; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P78325; IntAct: EBI-21225631; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25944092; Score: 0.56
DE  Interaction: Q9BYB0; IntAct: EBI-26515065; Score: 0.37
GO  GO:0005938;
GO  GO:0042995;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0005764;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0001891;
GO  GO:0042802;
GO  GO:0008289;
GO  GO:0030036;
GO  GO:0007154;
GO  GO:0006897;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEV
SQ  NDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQ
SQ  DINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELE
SQ  VVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKR
SQ  WPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQR
SQ  KRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRG
SQ  DSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTIS
SQ  MAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN
//
ID  Q07065;
PN  Cytoskeleton-associated protein 4;
GN  CKAP4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18296695, ECO:0000269|PubMed:19144824}; Single-pass type II membrane protein. Cell membrane {ECO:0000269|PubMed:18296695, ECO:0000269|PubMed:19144824}; Single-pass type II membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Note=Translocates to the perinuclear region upon APF-stimulation.
DR  UNIPROT: Q07065;
DR  UNIPROT: Q504S5;
DR  UNIPROT: Q53ES6;
DR  OMIM: 618595;
DR  DisGeNET: 10970;
DE  Function: Mediates the anchoring of the endoplasmic reticulum to microtubules. {ECO:0000269|PubMed:15703217}. High-affinity epithelial cell surface receptor for the FZD8- related low molecular weight sialoglycopeptide APF/antiproliferative factor. Mediates the APF antiproliferative signaling within cells. {ECO:0000269|PubMed:17030514, ECO:0000269|PubMed:19144824}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O76050; IntAct: EBI-20901648; Score: 0.40
DE  Interaction: P00519; IntAct: EBI-10101379; Score: 0.35
DE  Interaction: P00533; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9H1I8; IntAct: EBI-733925; Score: 0.00
DE  Interaction: P49407; IntAct: EBI-1642094; Score: 0.35
DE  Interaction: Q70EL3; IntAct: EBI-2512984; Score: 0.40
DE  Interaction: P40692; IntAct: EBI-2932395; Score: 0.37
DE  Interaction: Q8IYT8; IntAct: EBI-2984710; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-3893169; Score: 0.35
DE  Interaction: P18848; IntAct: EBI-3927782; Score: 0.37
DE  Interaction: P17568; IntAct: EBI-3936336; Score: 0.37
DE  Interaction: Q99598; IntAct: EBI-3936346; Score: 0.37
DE  Interaction: Q14764; IntAct: EBI-3936356; Score: 0.37
DE  Interaction: Q07065; IntAct: EBI-3942157; Score: 0.37
DE  Interaction: Q9Y3C0; IntAct: EBI-3942167; Score: 0.37
DE  Interaction: P81172; IntAct: EBI-3942177; Score: 0.37
DE  Interaction: Q6I9Y2; IntAct: EBI-3942193; Score: 0.37
DE  Interaction: P04578; IntAct: EBI-6174316; Score: 0.46
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-8835658; Score: 0.35
DE  Interaction: O75807; IntAct: EBI-9976880; Score: 0.35
DE  Interaction: O60307; IntAct: EBI-10103761; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: P35278; IntAct: EBI-11012136; Score: 0.35
DE  Interaction: Q3UJU9; IntAct: EBI-11021410; Score: 0.35
DE  Interaction: O75787; IntAct: EBI-11037152; Score: 0.35
DE  Interaction: P51148; IntAct: EBI-11046231; Score: 0.35
DE  Interaction: P51149; IntAct: EBI-11050319; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q16513; IntAct: EBI-11070511; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104527; Score: 0.35
DE  Interaction: Q9R0Q3; IntAct: EBI-11111571; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P09450; IntAct: EBI-11127973; Score: 0.35
DE  Interaction: Q15006; IntAct: EBI-11130215; Score: 0.35
DE  Interaction: Q8N4V1; IntAct: EBI-11130635; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135399; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-11155257; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q2MV58; IntAct: EBI-11366929; Score: 0.27
DE  Interaction: Q5HYA8; IntAct: EBI-11367583; Score: 0.27
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11372136; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q96Q45; IntAct: EBI-11377173; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q99IB8; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q13503; IntAct: EBI-21501670; Score: 0.35
DE  Interaction: P30825; IntAct: EBI-21505748; Score: 0.35
DE  Interaction: Q92633; IntAct: EBI-21508694; Score: 0.35
DE  Interaction: Q9H8X2; IntAct: EBI-21509881; Score: 0.35
DE  Interaction: Q16581; IntAct: EBI-21515265; Score: 0.35
DE  Interaction: Q6P5W5; IntAct: EBI-21515976; Score: 0.35
DE  Interaction: Q9UGM1; IntAct: EBI-21517134; Score: 0.35
DE  Interaction: A2A2Y4; IntAct: EBI-21527504; Score: 0.35
DE  Interaction: O75326; IntAct: EBI-21558128; Score: 0.35
DE  Interaction: O95274; IntAct: EBI-21607810; Score: 0.35
DE  Interaction: Q99689; IntAct: EBI-21638763; Score: 0.35
DE  Interaction: O94766; IntAct: EBI-21668731; Score: 0.35
DE  Interaction: Q99871; IntAct: EBI-21670231; Score: 0.35
DE  Interaction: Q9NVF7; IntAct: EBI-21671334; Score: 0.35
DE  Interaction: Q7LGA3; IntAct: EBI-21675787; Score: 0.35
DE  Interaction: Q16322; IntAct: EBI-21690666; Score: 0.35
DE  Interaction: P49796; IntAct: EBI-21716735; Score: 0.35
DE  Interaction: Q86Y78; IntAct: EBI-21717654; Score: 0.35
DE  Interaction: O14763; IntAct: EBI-21722795; Score: 0.35
DE  Interaction: Q8WWF3; IntAct: EBI-21811588; Score: 0.35
DE  Interaction: P08842; IntAct: EBI-21852400; Score: 0.35
DE  Interaction: P51888; IntAct: EBI-21852864; Score: 0.35
DE  Interaction: Q9Y6Z7; IntAct: EBI-21859525; Score: 0.35
DE  Interaction: Q9BZR6; IntAct: EBI-21865956; Score: 0.35
DE  Interaction: Q5BJH7; IntAct: EBI-21881931; Score: 0.35
DE  Interaction: P50876; IntAct: EBI-21881918; Score: 0.40
DE  Interaction: O60858; IntAct: EBI-21881893; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.42
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: P13073; IntAct: EBI-16791533; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800982; Score: 0.42
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-20306992; Score: 0.35
DE  Interaction: Q9UKU6; IntAct: EBI-20901800; Score: 0.40
DE  Interaction: Q8WXX0; IntAct: EBI-20901792; Score: 0.40
DE  Interaction: P04275; IntAct: EBI-20903352; Score: 0.40
DE  Interaction: P29475; IntAct: EBI-20905832; Score: 0.40
DE  Interaction: Q6NUK1; IntAct: EBI-20909712; Score: 0.40
DE  Interaction: Q8IVJ8; IntAct: EBI-20910272; Score: 0.40
DE  Interaction: Q96NB3; IntAct: EBI-20910632; Score: 0.40
DE  Interaction: P21675; IntAct: EBI-20917908; Score: 0.40
DE  Interaction: P16403; IntAct: EBI-20926338; Score: 0.40
DE  Interaction: A6NNW6; IntAct: EBI-20932560; Score: 0.40
DE  Interaction: Q9ULG1; IntAct: EBI-20935724; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P62079; IntAct: EBI-20977847; Score: 0.35
DE  Interaction: O95858; IntAct: EBI-20977902; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P25100; IntAct: EBI-21277437; Score: 0.35
DE  Interaction: Q00059; IntAct: EBI-21980665; Score: 0.35
DE  Interaction: O84793; IntAct: EBI-22302936; Score: 0.35
DE  Interaction: Q640N3; IntAct: EBI-25409042; Score: 0.35
DE  Interaction: Q5FWK3; IntAct: EBI-25409394; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P23497; IntAct: EBI-25485215; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
DE  Interaction: P02452; IntAct: EBI-26366205; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-26396827; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-26398473; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610886; Score: 0.35
DE  Interaction: Q8NDZ4; IntAct: EBI-26597064; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NG92; IntAct: EBI-27055968; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q8NCK7; IntAct: EBI-27105115; Score: 0.35
DE  Interaction: P56180; IntAct: EBI-27116883; Score: 0.27
DE  Interaction: P0DTC4; IntAct: EBI-28955127; Score: 0.35
DE  Interaction: P08069; IntAct: EBI-32718669; Score: 0.35
DE  Interaction: P08922; IntAct: EBI-32719572; Score: 0.35
DE  Interaction: Q5JZY3; IntAct: EBI-32720634; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P54760; IntAct: EBI-32721396; Score: 0.27
DE  Interaction: P21860; IntAct: EBI-32721529; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: P14616; IntAct: EBI-32723232; Score: 0.27
DE  Interaction: O15146; IntAct: EBI-32724025; Score: 0.27
DE  Interaction: P04629; IntAct: EBI-32724282; Score: 0.27
DE  Interaction: P16234; IntAct: EBI-32724889; Score: 0.27
DE  Interaction: P09619; IntAct: EBI-32724964; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
DE  Interaction: Q04912; IntAct: EBI-32725158; Score: 0.27
DE  Interaction: Q6J9G0; IntAct: EBI-32731895; Score: 0.27
DE  Interaction: Q8TCJ2; IntAct: EBI-32732289; Score: 0.27
GO  GO:0035577;
GO  GO:0005856;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0042599;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005791;
GO  GO:0035579;
GO  GO:0003723;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSAKQRGSKGGHGAASPSEKGAHPSGGADDVAKKPPPAPQQPPPPPAPHPQQHPQQHPQNQAHGKGGHRGGGGGGGKSS
SQ  SSSSASAAAAAAAASSSASCSRRLGRALNFLFYLALVAAAAFSGWCVHHVLEEVQQVRRSHQDFSRQREELGQGLQGVEQ
SQ  KVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEER
SQ  LTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASLEESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESD
SQ  IYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKSDSHGPKEDGGFRHSEAFE
SQ  ALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQRLAALQGRLEGLGSSEADQDGLASTVRSLGETQL
SQ  VLYGDVEELKRSVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPPQDFLDRLSSLDNLKASVSQVEADLKMLRTAVDSL
SQ  VAYSVKIETNENNLESAKGLLDDLRNDLDRLFVKVEKIHEKV
//
ID  Q8BMK4;
PN  Cytoskeleton-associated protein 4;
GN  Ckap4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:32075961}; Single-pass type II membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q07065}; Single- pass type II membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Note=Translocates to the perinuclear region upon APF-stimulation. {ECO:0000250}.
DR  UNIPROT: Q8BMK4;
DR  UNIPROT: B2RRB4;
DR  UNIPROT: Q8BTK8;
DR  UNIPROT: Q8R3F2;
DE  Function: High-affinity epithelial cell surface receptor for APF. {ECO:0000250}. Mediates the anchoring of the endoplasmic reticulum to microtubules. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: P14094; IntAct: EBI-20566937; Score: 0.35
DE  Interaction: Q8BRE0; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P07602; IntAct: EBI-21347829; Score: 0.35
GO  GO:0009986;
GO  GO:0005856;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005791;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSAKQRGSKGGHGAASPSDKGAHPSGGADDVAKKPPAAPQQPQPPAPHPPQHPQNQAHRGGHRGRSSAATANASSASCS
SQ  RRLGRVLNFLFYLSLVAAAAFSGWYVHHVLEEVQQVRRGHQDFSRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQH
SQ  KQDLTEKAVKEGESELNRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSINDNIAIFTDVQKR
SQ  SQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQ
SQ  AADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEGAVFKDSKALEELQRQIEGLGARLQYVEDGV
SQ  YSMQVASARHTESLESLLSKSQEYEQRLAMLQEHVGNLGSSSDLASTVRSLGETQLALSSDLKELKQSLGELPGTVESLQ
SQ  EQVLSLLSQDQAQAEGLPPQDFLDRLSSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNLESAKGLLDDLRND
SQ  LDRLFLKVEKIHEKI
//
ID  Q9LEX1;
PN  Calcium-dependent lipid-binding protein;
GN  CLB;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:21252258}; Single-pass membrane protein {ECO:0000255}. Note=Localized in the nucleus membrane of root tips cells. {ECO:0000269|PubMed:21252258}.
DR  UNIPROT: Q9LEX1;
DR  UNIPROT: P92940;
DR  Pfam: PF00168;
DR  Pfam: PF17047;
DR  PROSITE: PS50004;
DR  PROSITE: PS51847;
DE  Function: May be involved in membrane trafficking (By similarity). Acts as a repressor of abiotic stress (e.g. drought and salt) responses by binding specifically to the promoter of THAS1 to regulate its transcription (PubMed:21252258). Binds to membrane lipid ceramides (PubMed:21252258). {ECO:0000250|UniProtKB:B6ETT4, ECO:0000269|PubMed:21252258}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0097001;
GO  GO:0008289;
GO  GO:0046872;
GO  GO:0043565;
GO  GO:0006869;
GO  GO:0045892;
GO  GO:0009958;
GO  GO:0009651;
GO  GO:0009414;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLISGILFGIIFGVALMAGWSRMMTHRSSKRVAKAVDMKLLGSLSRDDLKKICGDNFPQWISFPAFEQVKWLNKLLSKM
SQ  WPYIAEAATMVIRDSVEPLLEDYRPPGITSLKFSKLTLGNVAPKIEGIRVQSFKEGQVTMDVDLRWGGDPNIVLGVTALV
SQ  ASIPIQLKDLQVFTVARVIFQLADEIPCISAVVVALLAEPKPRIDYTLKAVGGSLTAIPGLSDMIDDTVDTIVKDMLQWP
SQ  HRIVVPIGGIPVDLSDLELKPQGKLIVTVVKATNLKNKELIGKSDPYATIYIRPVFKYKTKAIENNLNPVWDQTFELIAE
SQ  DKETQSLTVEVFDKDVGQDERLGLVKLPLSSLEAGVTKELELNLLSSLDTLKVKDKKDRGSITLKVHYHEFNKEEQMAAL
SQ  EDEKKIMEERKRLKEAGVIGSTMDAVGMVGSGLGAGVGMVGTGIGTGVGLVGSGVSSGVGMVGSGFGAVGSGLSKAGRFM
SQ  GRTITGQSSKRSGSSTPVNTVPENDGAKQQ
//
ID  Q1LZF8;
PN  Chloride channel CLIC-like protein 1;
GN  CLCC1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. {ECO:0000250|UniProtKB:Q96S66}.
DR  UNIPROT: Q1LZF8;
DR  Pfam: PF05934;
DE  Function: Seems to act as a chloride ion channel (By similarity). Plays a role in retina development (By similarity). {ECO:0000250|UniProtKB:Q99LI2, ECO:0000250|UniProtKB:Q9WU61}.
DE  Reference Proteome: Yes;
GO  GO:0034707;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0044233;
GO  GO:0031965;
GO  GO:0005254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLYSLLLCECLWLITAYAHDDEWIDPTDMLNYDAASGRMRKSQVKYGISEKEEVNPDLSCANELSECYNRLDSLTYKIDE
SQ  CEKQKRKDYESQSNPVFRRYLNKILIETKKLGLPDENKHDMHYDAEIILKRQTLLEIQKFLSGEDWKPGALDDALSDILI
SQ  NFKFHDFETWKWRFEEFFGVDPYNVFMVLLCLLCIVALVATELWTYVRWYTQLKRVFFISFLISLGWNWMYLYKLAFAQH
SQ  QAEVAKMEPLNNVCAEKMNWSGSLWEWLRSSWTYKDDPCQKYYELLLVNPIWLVPPTKALAVTFTNFVTEPLKHVGKGAG
SQ  EFIKALMKEIPVLLHIPVLIIMALAVLSFCYGAGKSVNMLRHVGGPEREAPQALQAGERRRQQKIDYRPHGGAGDADFYY
SQ  RGQISPIEQGPNDNTYEGRRDVLRERDVGLRFQTGNKSPEVLRPFDLQEAEAREHPKVVPGLKSPNLESKPREMGEIPGE
SQ  STPTESSTESSQPAKPVSGQKVSEGVEGCPAVEKAQLRTDAAGGPEEGSTCSPASTAVEVCG
//
ID  A0A2R8Q3S9;
PN  Chloride channel CLIC-like protein 1;
GN  clcc1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. {ECO:0000250|UniProtKB:Q96S66}.
DR  UNIPROT: A0A2R8Q3S9;
DR  Pfam: PF05934;
DE  Function: Seems to act as a chloride ion channel (By similarity). Plays a role in retina development (PubMed:30157172). {ECO:0000250|UniProtKB:Q9WU61, ECO:0000269|PubMed:30157172}.
DE  Reference Proteome: Yes;
GO  GO:0034707;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0031965;
GO  GO:0005254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKLSSSSSFGLCILVVFFCFVVIESAKIRIDGYNDEAWIDPYDMLNYDPTTKRMRKSTESESYQNVPTKRREFNSESCDV
SQ  PKCPDEHECIKKLHILQKEFDEQKSKSTATLSKPVCLPVFKRFLSKLLKETSKLGLPDDGITAMHYDAEVKLSKQSLAEI
SQ  QKLLNDEDGWTTGAMDEALSQILVQFKLHDYEAWKWRFEDTFHVDVDTVLKVSLIVLIIVAIICTQLWSVVSWFVQFRRM
SQ  FAVSFFISLIWNWFHLYMLAFAEHKKNIVQVESFNAKCTGLKQLNWQDSLSEWYRRTWTLQDDPCKKYYEVLVVNPILLV
SQ  PPTKAITITITNFITDPLKHIGEGISEFLRALLKDLPVTLQIPVLIIIILAILIFVYGSAQAAIHQVARFPRLGWRQEQP
SQ  PPAVGQRQNPQLRAHEEPWEGGDARQPLPMRQDNRGNHVGNRGDQGFRDANAPENREEDRSMDIRQEFSTKRTPVETLQA
SQ  TGNTFPDDETDSQQRTQELDSGANVEEEVKVEEKEKKESFSVDNKEQKETKSPDRSEPITSEPPSSIDVKTVGADQGNEH
SQ  LMCTKRKWAAQNGFKLQVILCEINSEASADLPEEEECFSFKHPVQETQS
//
ID  Q96S66;
PN  Chloride channel CLIC-like protein 1;
GN  CLCC1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30157172, ECO:0000269|PubMed:31653868}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi- pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. {ECO:0000269|PubMed:31653868}.
DR  UNIPROT: Q96S66;
DR  UNIPROT: O94861;
DR  UNIPROT: Q8WYP8;
DR  UNIPROT: Q8WYP9;
DR  UNIPROT: Q9BU25;
DR  Pfam: PF05934;
DR  OMIM: 609913;
DR  OMIM: 617539;
DR  DisGeNET: 23155;
DE  Function: Seems to act as a chloride ion channel (PubMed:30157172). Plays a role in retina development (PubMed:30157172). {ECO:0000269|PubMed:30157172}.
DE  Disease: Retinitis pigmentosa 32 (RP32) [MIM:609913]: A form of retinitis pigmentosa, a retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. RP32 inheritance is autosomal recessive. {ECO:0000269|PubMed:16189710, ECO:0000269|PubMed:30157172}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-21724762; Score: 0.35
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P04626; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: A0A6H3AJ02; IntAct: EBI-2836117; Score: 0.00
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06927; IntAct: EBI-11724813; Score: 0.35
DE  Interaction: Q99JN2; IntAct: EBI-11026090; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q2MV58; IntAct: EBI-11384104; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11389870; Score: 0.27
DE  Interaction: O75326; IntAct: EBI-21558128; Score: 0.35
DE  Interaction: O95858; IntAct: EBI-21724762; Score: 0.35
DE  Interaction: Q96IK5; IntAct: EBI-21724762; Score: 0.35
DE  Interaction: Q8IWV7; IntAct: EBI-21724762; Score: 0.35
DE  Interaction: Q15813; IntAct: EBI-21724762; Score: 0.35
DE  Interaction: Q15038; IntAct: EBI-21724762; Score: 0.35
DE  Interaction: P55061; IntAct: EBI-21724762; Score: 0.35
DE  Interaction: P23470; IntAct: EBI-21724762; Score: 0.35
DE  Interaction: Q6ZMD2; IntAct: EBI-21898749; Score: 0.40
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-20307902; Score: 0.35
DE  Interaction: P13693; IntAct: EBI-20992046; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: Q9UKW4; IntAct: EBI-25410543; Score: 0.35
DE  Interaction: Q92888; IntAct: EBI-25411420; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25491278; Score: 0.84
DE  Interaction: P19739; IntAct: EBI-25685423; Score: 0.35
DE  Interaction: P59632; IntAct: EBI-25688265; Score: 0.53
DE  Interaction: K9N7D2; IntAct: EBI-26375184; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: A0A0B4J2F0; IntAct: EBI-26657494; Score: 0.63
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0H3NG92; IntAct: EBI-27055968; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: Q86YV6; IntAct: EBI-28942265; Score: 0.35
DE  Interaction: Q92932; IntAct: EBI-27116679; Score: 0.27
DE  Interaction: P56180; IntAct: EBI-27116883; Score: 0.27
DE  Interaction: P08922; IntAct: EBI-32719572; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P54756; IntAct: EBI-32720907; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: P14616; IntAct: EBI-32723232; Score: 0.27
DE  Interaction: O15146; IntAct: EBI-32724025; Score: 0.27
DE  Interaction: P04629; IntAct: EBI-32724282; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: P16234; IntAct: EBI-32724889; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
DE  Interaction: Q01974; IntAct: EBI-32725367; Score: 0.27
DE  Interaction: Q6J9G0; IntAct: EBI-32731895; Score: 0.27
DE  Interaction: Q8TCJ2; IntAct: EBI-32732289; Score: 0.27
GO  GO:0034707;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0044233;
GO  GO:0031965;
GO  GO:0005254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLCSLLLCECLLLVAGYAHDDDWIDPTDMLNYDAASGTMRKSQAKYGISGEKDVSPDLSCADEISECYHKLDSLTYKIDE
SQ  CEKKKREDYESQSNPVFRRYLNKILIEAGKLGLPDENKGDMHYDAEIILKRETLLEIQKFLNGEDWKPGALDDALSDILI
SQ  NFKFHDFETWKWRFEDSFGVDPYNVLMVLLCLLCIVVLVATELWTYVRWYTQLRRVLIISFLFSLGWNWMYLYKLAFAQH
SQ  QAEVAKMEPLNNVCAKKMDWTGSIWEWFRSSWTYKDDPCQKYYELLLVNPIWLVPPTKALAVTFTTFVTEPLKHIGKGTG
SQ  EFIKALMKEIPALLHLPVLIIMALAILSFCYGAGKSVHVLRHIGGPESEPPQALRPRDRRRQEEIDYRPDGGAGDADFHY
SQ  RGQMGPTEQGPYAKTYEGRREILRERDVDLRFQTGNKSPEVLRAFDVPDAEAREHPTVVPSHKSPVLDTKPKETGGILGE
SQ  GTPKESSTESSQSAKPVSGQDTSGNTEGSPAAEKAQLKSEAAGSPDQGSTYSPARGVAGPRGQDPVSSPCG
//
ID  Q99LI2;
PN  Chloride channel CLIC-like protein 1;
GN  Clcc1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. {ECO:0000250|UniProtKB:Q96S66}.
DR  UNIPROT: Q99LI2;
DR  UNIPROT: A2AEK9;
DR  Pfam: PF05934;
DE  Function: Seems to act as a chloride ion channel (By similarity). Plays a role in retina development (PubMed:30157172). {ECO:0000250|UniProtKB:Q9WU61, ECO:0000269|PubMed:30157172}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9CZE3; IntAct: EBI-11570876; Score: 0.35
DE  Interaction: Q9D0P8; IntAct: EBI-11571153; Score: 0.35
DE  Interaction: Q8BIZ1; IntAct: EBI-26595802; Score: 0.35
GO  GO:0034707;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0044233;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005254;
GO  GO:0006821;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLCRLLLCECLLLITGYAHDDDWIDPTDMLNYDAASGTMRKSQVRSGTSEKKEVSPDSSEAEELSDCLHRLDSLTHKVDS
SQ  CEKKKMKDYESQSNPVFRRYLNKILIEAGKLGLPDENKVEMRYDAEILLSRQTLLEIQKFLSGEEWKPGALDDALSDILI
SQ  NFKCHDSEAWKWQFEDYFGVDPYNVFMVLLCLLCLVVLVATELWTYVRWYTQMKRIFIISFLLSLAWNWIYLYKMAFAQH
SQ  QANIAGMEPFDNLCAKKMDWTGSLWEWFTSSWTYKDDPCQKYYELLIVNPIWLVPPTKALAITFTNFVTEPLKHIGKGAG
SQ  EFIKALMKEIPVLLQIPVLAILALAVLSFCYGAGRSVPMLRHFGGPDREPPRALEPDDRRRQKGLDYRLHGGAGDADFSY
SQ  RGPAGSIEQGPYDKMHASKRDALRQRFHSGNKSPEVLRAFDLPDTEAQEHPEVVPSHKSPIMNTNLETGELPGESTPTEY
SQ  SQSAKDVSGQVPSAGKSSPTVDKAQLKTDSECSPPGGCPPSKEAAVAAHGTEPVSSPCG
//
ID  Q9WU61;
PN  Chloride channel CLIC-like protein 1;
GN  Clcc1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11279057}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:11279057}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:11279057}; Multi-pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. {ECO:0000250|UniProtKB:Q96S66}.
DR  UNIPROT: Q9WU61;
DR  UNIPROT: Q66HQ5;
DR  UNIPROT: Q8VIE8;
DR  UNIPROT: Q8VIE9;
DR  UNIPROT: Q8VIF0;
DR  UNIPROT: Q8VIF1;
DR  Pfam: PF05934;
DE  Function: Seems to act as a chloride ion channel (PubMed:11279057). Plays a role in retina development (By similarity). {ECO:0000250|UniProtKB:Q99LI2, ECO:0000269|PubMed:11279057}.
DE  Reference Proteome: Yes;
GO  GO:0034707;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0044233;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005254;
GO  GO:0006821;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLCSLLLCGCLLLITGYAHDDDWIDPTDMLNYDAASGTMRKSQAKYGTSEKKEVNPGLSDAQELSDCLQRLDSLTHKVDD
SQ  CEKKKMKDYESQSNPVFRRYLNKILIEAGKLGLPDEDRVDVRYDAEILLTRQTLLEIQKFLSGEEWKPGALDDALSDILT
SQ  NFKSHDAEAWKWQFEDYFGVDPYNVFMVLLCLLCIVALVATELWTYVRWHTQLKRVCIISFLVSLGWNWIYLYKVAFAQH
SQ  QANVAKMAPLNDVCAKKMDWTENLWEWFRISWTYKDDPCQKYYELLIVNPIWLVPPTKALAVTFTNFVTEPLKYIGKGTG
SQ  EFIKALMKEIPVLLQIPVLVILALAVLGFCYGAGQSVPMLRHFRGPEREPPRALEPDDRRRQKELDYRFHGGAGDADFSY
SQ  RGPAGSIEQGPYDKMHVCERDVLRQRQVNMRFPSGNKSPEVLRAFDLPDTEAQEHPEVVPSHKPSIVNTSLKETSELPRE
SQ  STLAECSQCAKDGSGQVPSTAESSPIVEKAQLKTDSECRPHSTEAAAAAARGTDPVSSPCG
//
ID  Q91892;
PN  Chloride channel CLIC-like protein 1;
GN  clcc1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. {ECO:0000250|UniProtKB:Q96S66}.
DR  UNIPROT: Q91892;
DR  Pfam: PF05934;
DE  Function: Seems to act as a chloride ion channel (By similarity). Plays a role in retina development (By similarity). {ECO:0000250|UniProtKB:Q99LI2, ECO:0000250|UniProtKB:Q9WU61}.
DE  Reference Proteome: Yes;
GO  GO:0034707;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0044233;
GO  GO:0031965;
GO  GO:0005254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRLFLLVALYLSPVYGDYTDEWIDPSDMLNYDAASGKMKNKPQVESTQSYYSVENTVSQDATQQPAQKANELHQNPDMTC
SQ  SAEYQEYKTKLENLKGQLEETKRMEKSKSKSQAIFKRYLNKILIEAGRIGLPDESYPKAHYDAEVVFTMEMLQEIQSFLN
SQ  NGDWNVGALDDALSSTLVQFKHHNEEEWKWKFEDSFGVDVYTLFMLILCVLCLVKLIATEIWTHIGWFTQLKRLLILSTV
SQ  ISFGWNWMYLYKVAFAERQAELAKLQDFDKCSQKISWSESLFDWMKGAATFQNDPCEDYFKALIVSPTLMVPPTKALALT
SQ  FTNFITEPLKHIGKGIGEFLNALLSEIPLFFQVPVLIFIAVLLLAFFYGAGTAVMNPVNLYRRLTGPEREKPLPVEPTRS
SQ  NRKRFIEDVRVPPALGQLPRDNDVVNIPKQQPLDDIDGSNNPPVTAPADPSDTGQVKSNNTGEPLVQEDHSIKKSIKESR
SQ  NDERPNTESPEAKPQRPEEPVVETLRST
//
ID  Q5E9B7;
PN  Chloride intracellular channel protein 1;
GN  CLIC1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5E9B7;
DR  Pfam: PF13409;
DR  PROSITE: PS50405;
DE  Function: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0034707;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005254;
GO  GO:0005244;
GO  GO:0006821;
GO  GO:0045669;
GO  GO:0051726;
GO  GO:0034765;
GO  GO:0051881;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKI
SQ  EEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPDEVDETSAEDE
SQ  GISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFSIPDVFRGVHRYLRNAYAREEFASTCPDDEEIELAYEQVAKAL
SQ  K
//
ID  O00299;
PN  Chloride intracellular channel protein 1;
GN  CLIC1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:9139710}. Nucleus membrane {ECO:0000269|PubMed:9139710}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10793131, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:9139710, ECO:0000305|PubMed:11978800, ECO:0000305|PubMed:14613939}. Cell membrane {ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:14613939, ECO:0000305|PubMed:11978800}; Single-pass membrane protein {ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:14613939}. Note=Mostly in the nucleus including in the nuclear membrane (PubMed:9139710, PubMed:12681486). Small amount in the cytoplasm and the plasma membrane (PubMed:9139710). Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (PubMed:11940526, PubMed:11551966, PubMed:14613939). {ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}.
DR  UNIPROT: O00299;
DR  UNIPROT: Q15089;
DR  UNIPROT: Q502X1;
DR  PDB: 1K0M;
DR  PDB: 1K0N;
DR  PDB: 1K0O;
DR  PDB: 1RK4;
DR  PDB: 3O3T;
DR  PDB: 3P8W;
DR  PDB: 3P90;
DR  PDB: 3QR6;
DR  PDB: 3SWL;
DR  PDB: 3TGZ;
DR  PDB: 3UVH;
DR  PDB: 4IQA;
DR  PDB: 4JZQ;
DR  PDB: 4K0G;
DR  PDB: 4K0N;
DR  PDB: 7F8R;
DR  Pfam: PF13409;
DR  PROSITE: PS50405;
DR  OMIM: 602872;
DR  DisGeNET: 1192;
DE  Function: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle. {ECO:0000269|PubMed:10834939, ECO:0000269|PubMed:11195932, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:11978800, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}.
DE  Reference Proteome: Yes;
DE  Interaction: O15116; IntAct: EBI-23757154; Score: 0.67
DE  Interaction: P23508; IntAct: EBI-1063923; Score: 0.00
DE  Interaction: P62330; IntAct: EBI-1068310; Score: 0.00
DE  Interaction: P11171; IntAct: EBI-1078375; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1081273; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1083332; Score: 0.00
DE  Interaction: P32121; IntAct: EBI-1642567; Score: 0.35
DE  Interaction: Q5NID2; IntAct: EBI-2799144; Score: 0.00
DE  Interaction: A0A3P1U0S6; IntAct: EBI-2811954; Score: 0.00
DE  Interaction: Q81U22; IntAct: EBI-2836081; Score: 0.00
DE  Interaction: A0A6L8P1I7; IntAct: EBI-2836088; Score: 0.00
DE  Interaction: A0A0F7REA8; IntAct: EBI-2836074; Score: 0.00
DE  Interaction: Q8CZM8; IntAct: EBI-2848306; Score: 0.00
DE  Interaction: A0A3N4BEU0; IntAct: EBI-2873204; Score: 0.00
DE  Interaction: P40692; IntAct: EBI-2932395; Score: 0.37
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: P20292; IntAct: EBI-3904626; Score: 0.37
DE  Interaction: P24539; IntAct: EBI-3904636; Score: 0.37
DE  Interaction: P27449; IntAct: EBI-3904646; Score: 0.37
DE  Interaction: Q93050; IntAct: EBI-3904656; Score: 0.37
DE  Interaction: P34130; IntAct: EBI-3907454; Score: 0.37
DE  Interaction: P50416; IntAct: EBI-3907444; Score: 0.37
DE  Interaction: Q99676; IntAct: EBI-3907496; Score: 0.37
DE  Interaction: P05386; IntAct: EBI-3907469; Score: 0.37
DE  Interaction: P10827; IntAct: EBI-3907479; Score: 0.37
DE  Interaction: Q9Y6K9; IntAct: EBI-3907506; Score: 0.37
DE  Interaction: P37198; IntAct: EBI-3916132; Score: 0.37
DE  Interaction: Q9NR11; IntAct: EBI-3916149; Score: 0.37
DE  Interaction: Q13162; IntAct: EBI-3935813; Score: 0.37
DE  Interaction: P15336; IntAct: EBI-5529812; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q9NQW6; IntAct: EBI-11009421; Score: 0.35
DE  Interaction: Q61879; IntAct: EBI-11041929; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062262; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: Q9NQX4; IntAct: EBI-11100755; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-11128681; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-11132927; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135399; Score: 0.35
DE  Interaction: H9XIJ5; IntAct: EBI-11514200; Score: 0.37
DE  Interaction: Q6FHY5; IntAct: EBI-24478573; Score: 0.56
DE  Interaction: Q4KMQ1; IntAct: EBI-24491483; Score: 0.67
DE  Interaction: Q5HYW2; IntAct: EBI-25156542; Score: 0.56
DE  Interaction: P56945; IntAct: EBI-15099538; Score: 0.35
DE  Interaction: Q9HCN8; IntAct: EBI-21660533; Score: 0.35
DE  Interaction: Q86WR7; IntAct: EBI-21889242; Score: 0.35
DE  Interaction: O75832; IntAct: EBI-16718696; Score: 0.65
DE  Interaction: Q9Y2H1; IntAct: EBI-20624829; Score: 0.27
DE  Interaction: Q83D60; IntAct: EBI-21285616; Score: 0.37
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P04156; IntAct: EBI-21014477; Score: 0.35
DE  Interaction: Q9Y251; IntAct: EBI-21260107; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.53
DE  Interaction: Q8N5H7; IntAct: EBI-25387159; Score: 0.35
DE  Interaction: Q15139; IntAct: EBI-25395029; Score: 0.35
DE  Interaction: Q01995; IntAct: EBI-26878675; Score: 0.35
DE  Interaction: P05154; IntAct: EBI-27038496; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: O43318; IntAct: EBI-28931001; Score: 0.35
DE  Interaction: Q96Q04; IntAct: EBI-32723651; Score: 0.27
GO  GO:0072562;
GO  GO:0005903;
GO  GO:0034707;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0005615;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031982;
GO  GO:0045296;
GO  GO:0005254;
GO  GO:0005244;
GO  GO:0006821;
GO  GO:0070527;
GO  GO:0045669;
GO  GO:0051726;
GO  GO:0034765;
GO  GO:0051881;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKI
SQ  EEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDE
SQ  GVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKAL
SQ  K
//
ID  Q9Z1Q5;
PN  Chloride intracellular channel protein 1;
GN  Clic1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9Z1Q5;
DR  Pfam: PF13409;
DR  PROSITE: PS50405;
DE  Function: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P70181; IntAct: EBI-653938; Score: 0.37
GO  GO:0034707;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005254;
GO  GO:0005244;
GO  GO:0006821;
GO  GO:0045669;
GO  GO:0051726;
GO  GO:0034765;
GO  GO:0051881;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKI
SQ  EEFLEAMLCPPRYPKLAALNPESNTSGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDE
SQ  GISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVARAL
SQ  K
//
ID  Q29238;
PN  Chloride intracellular channel protein 1;
GN  CLIC1;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250}.
DR  UNIPROT: Q29238;
DR  Pfam: PF13409;
DE  Function: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0034707;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005254;
GO  GO:0005244;
GO  GO:0006821;
GO  GO:0051726;
GO  GO:0034765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKI
SQ  EEFLEAVLCPPRYPKLAALNPESNTAGLDI
//
ID  Q95MF9;
PN  Chloride intracellular channel protein 1;
GN  CLIC1;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250}.
DR  UNIPROT: Q95MF9;
DR  Pfam: PF13409;
DR  PROSITE: PS50405;
DE  Function: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0034707;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005254;
GO  GO:0005244;
GO  GO:0051726;
GO  GO:0034765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVHKLCPGGQLPFLLYGTEVHTDTNKI
SQ  EEFLEAVLCPPRYPKLAALNPESNTAGVDIFAKFSAYIKNSNPALNDNLEKGLLKALKILDNYLTSPLPEEVDETSAEDE
SQ  GISQRKFLDGNELTLADCNLLPKLHIVQVVCKKNRGFTIPEVFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKAL
SQ  K
//
ID  Q6MG61;
PN  Chloride intracellular channel protein 1;
GN  Clic1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O00299}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:O00299}. Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250}.
DR  UNIPROT: Q6MG61;
DR  Pfam: PF13409;
DR  PROSITE: PS50405;
DE  Function: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0034707;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005254;
GO  GO:0005247;
GO  GO:0006821;
GO  GO:0045669;
GO  GO:0051726;
GO  GO:0034765;
GO  GO:0051881;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKI
SQ  EEFLEAVLCPPRYPKLAALNPESNTSGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDE
SQ  GISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVARAL
SQ  K
//
ID  P17697;
PN  Clusterin alpha chain;
GN  CLU;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P10909}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10909}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q9XSC5}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
DR  UNIPROT: P17697;
DR  UNIPROT: A5D983;
DR  UNIPROT: Q148K1;
DR  Pfam: PF01093;
DR  PROSITE: PS00492;
DR  PROSITE: PS00493;
DE  Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:P10909, ECO:0000250|UniProtKB:Q06890}.
DE  Reference Proteome: Yes;
GO  GO:0042583;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0048471;
GO  GO:0034366;
GO  GO:0051787;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0061077;
GO  GO:0002434;
GO  GO:0097193;
GO  GO:1905907;
GO  GO:1902230;
GO  GO:0031333;
GO  GO:0043065;
GO  GO:2001244;
GO  GO:0051092;
GO  GO:0032436;
GO  GO:0048260;
GO  GO:2000060;
GO  GO:0050821;
GO  GO:0042981;
GO  GO:0042127;
GO  GO:0051788;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P10909};
SQ  MKTLLLLMGLLLSWESGWAISDKELQEMSTEGSKYVNKEIKNALKEVKQIKTQIEQTNEERKLLLSSLEEAKKKKEDALN
SQ  DTRDSENKLKASQGVCNETMTALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWINGDRIDSLMEND
SQ  REQSHVMDVMEDSFTRASSIMDELFQDRFFLRRPQDTQYYSPFSSFPRGSLFFNPKSRFARNVMPFPLLEPFNFHDVFQP
SQ  FYDMIHQAQQAMDAHLQRTPYHFPTMEFTENNDRTVCKEIRHNSTGCLRMKDQCEKCQEILEVDCSASNPTQTLLRQQLN
SQ  ASLQLAEKFSRLYDQLLQSYQQKMLNTSALLKQLNEQFTWVSQLANLTQSDDQHYLQVFTVNSHNSDPSIPSGLTKVIVK
SQ  LFNSFPITVTVPQEVSSPNFMENVAEKALQQYRRKSQEE
//
ID  P25473;
PN  Clusterin alpha chain;
GN  CLU;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P10909}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10909}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q9XSC5}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
DR  UNIPROT: P25473;
DR  Pfam: PF01093;
DR  PROSITE: PS00492;
DR  PROSITE: PS00493;
DE  Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself (By similarity). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:11697889). When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin- protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX- mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:P10909, ECO:0000250|UniProtKB:Q06890, ECO:0000269|PubMed:11697889}.
DE  Reference Proteome: Yes;
GO  GO:0042583;
GO  GO:0005829;
GO  GO:0005788;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0048471;
GO  GO:0034366;
GO  GO:0051087;
GO  GO:0051787;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0061077;
GO  GO:0002434;
GO  GO:0097193;
GO  GO:1905907;
GO  GO:1902230;
GO  GO:0031333;
GO  GO:0043065;
GO  GO:2001244;
GO  GO:0051092;
GO  GO:0032436;
GO  GO:0048260;
GO  GO:2000060;
GO  GO:0050821;
GO  GO:0042981;
GO  GO:0042127;
GO  GO:0051788;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P10909};
SQ  MMKTLLLLVGLLLTWDNGRVLGDQAVSDTELQEMSTEGSKYINKEIKNALKGVKQIKTLIEQTNEERKSLLSNLEEAKKK
SQ  KEDALNDTKDSETKLKASQGVCNDTMMALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWMNGDRID
SQ  SLLENDRQQTHALDVMQDSFNRASSIMDELFQDRFFTREPQDTYHYSPFSLFQRRPFFNPKFRIARNIIPFPRFQPLNFH
SQ  DMFQPFFDMIHQAQQAMDVNLHRIPYHFPIEFPEEDNRTVCKEIRHNSTGCLKMKDQCEKCQEILSVDCSSNNPAQVQLR
SQ  QELSNSLQIAEKFTKLYDELLQSYQEKMFNTSSLLKQLNEQFSWVSQLANLTQSEDPFYLQVTTVGSQTSDSNVPVGFTK
SQ  VVVKLFDSDPITVMIPEAVSRNNPKFMETVAEKALQEYRQKHREE
//
ID  Q29482;
PN  Clusterin alpha chain;
GN  CLU;
OS  9796;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P10909}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10909}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q9XSC5}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
DR  UNIPROT: Q29482;
DR  Pfam: PF01093;
DR  PROSITE: PS00492;
DR  PROSITE: PS00493;
DE  Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:P10909, ECO:0000250|UniProtKB:Q06890}.
DE  Reference Proteome: Yes;
GO  GO:0042583;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0048471;
GO  GO:0034366;
GO  GO:0051787;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0061077;
GO  GO:0002434;
GO  GO:0097193;
GO  GO:1905907;
GO  GO:1902230;
GO  GO:0031333;
GO  GO:0043065;
GO  GO:2001244;
GO  GO:0051092;
GO  GO:0032436;
GO  GO:0048260;
GO  GO:2000060;
GO  GO:0050821;
GO  GO:0042981;
GO  GO:0042127;
GO  GO:0051788;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P10909};
SQ  MKTLLLLVGLLLTLENGQVLGDKAVSDRELQEMSTQGSNYINKEIKNALKGVKQIKNLIEQTNEERKSLLGTLEEAKKKK
SQ  EGALNDTKDSEMKLKESQGVCNETMTALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWINGDRIDS
SQ  LLENDRQQTHVLDVMQDSFDRASSIMDELFQDRFFTREPQDTYYYSPFSSPHRRSSLLFNPKSRFARNIMHFPMYRHLNF
SQ  NDMFQPFFDMIHQAQQAMNLHLHRLPDQLPMTEFSEGDNHDRTVCKEIRHNSTGCLKMKDQCEKCQEILSVDCSTNNPSQ
SQ  MQLRQELNNSLQLAEKFTKLYDELLQSYQEKMLNTSSLLKQLNEQFSWVSQLANLTQGEDQYYLQVTTVSSHNSDSEVPS
SQ  GLTRVVVKLFDSYPITVTVPEVVSRNNPKFMETVAEKALQEYRQKNREE
//
ID  P10909;
PN  Clusterin alpha chain;
GN  CLU;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Secreted {ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:17451556, ECO:0000269|PubMed:2387851, ECO:0000269|PubMed:24073260, ECO:0000269|PubMed:2780565, ECO:0000269|PubMed:3154963, ECO:0000269|PubMed:8292612, ECO:0000269|PubMed:8328966}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. {ECO:0000269|PubMed:17451556}. [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:24073260}. Note=Keeps cytoplasmic localization in stressed and unstressed cell. {ECO:0000269|PubMed:24073260}. [Isoform 6]: Cytoplasm {ECO:0000269|PubMed:24073260}. Note=Keeps cytoplasmic localization in stressed and unstressed cell. {ECO:0000269|PubMed:24073260}. Nucleus {ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:19137541}. Cytoplasm {ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:17689225, ECO:0000269|PubMed:19137541, ECO:0000269|PubMed:20068069, ECO:0000269|PubMed:22689054, ECO:0000269|PubMed:24073260}. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:17689225}. Cytoplasm, cytosol {ECO:0000269|PubMed:17451556, ECO:0000269|PubMed:22689054, ECO:0000269|PubMed:24073260}. Microsome {ECO:0000269|PubMed:22689054}. Endoplasmic reticulum {ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:22689054}. Mitochondrion {ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:22689054}. Mitochondrion membrane {ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:17689225}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250}. Note=Secreted isoforms can retrotranslocate from the secretory compartments to the cytosol upon cellular stress (PubMed:17451556). Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (PubMed:20068069). Detected at the mitochondrion membrane upon induction of apoptosis (PubMed:17689225). Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction (PubMed:22689054). ER stress reduces secretion (PubMed:22689054). Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm (PubMed:24073260, PubMed:22689054, PubMed:17451556). Non-secreted forms emerge mainly from failed translocation, alternative splicing or non-canonical initiation start codon (PubMed:24073260, PubMed:12551933). {ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:17451556, ECO:0000269|PubMed:17689225, ECO:0000269|PubMed:20068069, ECO:0000269|PubMed:22689054, ECO:0000269|PubMed:24073260}.
DR  UNIPROT: P10909;
DR  UNIPROT: B2R9Q1;
DR  UNIPROT: B3KSE6;
DR  UNIPROT: P11380;
DR  UNIPROT: P11381;
DR  UNIPROT: Q2TU75;
DR  UNIPROT: Q5HYC1;
DR  UNIPROT: Q7Z5B9;
DR  Pfam: PF01093;
DR  PROSITE: PS00492;
DR  PROSITE: PS00493;
DR  OMIM: 185430;
DR  DisGeNET: 1191;
DE  Function: [Isoform 1]: Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed:11123922, PubMed:19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed:11123922, PubMed:12176985, PubMed:17260971, PubMed:19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:12047389, PubMed:17412999, PubMed:17407782). Does not require ATP (PubMed:11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed:11123922). Does not refold proteins by itself (PubMed:11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:21505792). Protects cells against apoptosis and against cytolysis by complement (PubMed:2780565). Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed:20068069). Modulates NF-kappa-B transcriptional activity (PubMed:12882985). A mitochondrial form suppresses BAX- dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed:16113678, PubMed:17689225). Plays a role in the regulation of cell proliferation (PubMed:19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed:22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:Q06890, ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:12047389, ECO:0000269|PubMed:12176985, ECO:0000269|PubMed:12882985, ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17407782, ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:17689225, ECO:0000269|PubMed:19137541, ECO:0000269|PubMed:19535339, ECO:0000269|PubMed:19996109, ECO:0000269|PubMed:20068069, ECO:0000269|PubMed:21505792, ECO:0000269|PubMed:22689054, ECO:0000269|PubMed:24073260, ECO:0000269|PubMed:2780565}. [Isoform 6]: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. {ECO:0000269|PubMed:24073260}. [Isoform 4]: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Promotes cell death through interaction with BCL2L1 that releases and activates BAX (PubMed:21567405). {ECO:0000269|PubMed:21567405, ECO:0000269|PubMed:24073260}.
DE  Reference Proteome: Yes;
DE  Interaction: O14656; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-1105564; Score: 0.00
DE  Interaction: Q9UKE5; IntAct: EBI-1105584; Score: 0.00
DE  Interaction: P30101; IntAct: EBI-7172377; Score: 0.59
DE  Interaction: P02647; IntAct: EBI-1220621; Score: 0.35
DE  Interaction: P01876; IntAct: EBI-1221175; Score: 0.35
DE  Interaction: P01857; IntAct: EBI-1222317; Score: 0.35
DE  Interaction: P62993; IntAct: EBI-2115936; Score: 0.00
DE  Interaction: O35638; IntAct: EBI-2559549; Score: 0.40
DE  Interaction: P16104; IntAct: EBI-2564373; Score: 0.35
DE  Interaction: P22736; IntAct: EBI-2681480; Score: 0.00
DE  Interaction: P01100; IntAct: EBI-2694247; Score: 0.52
DE  Interaction: Q00987; IntAct: EBI-2682977; Score: 0.00
DE  Interaction: P04150; IntAct: EBI-2684198; Score: 0.00
DE  Interaction: P37231; IntAct: EBI-2793955; Score: 0.52
DE  Interaction: P17028; IntAct: EBI-2691450; Score: 0.00
DE  Interaction: A0A6L7HEE9; IntAct: EBI-2836046; Score: 0.00
DE  Interaction: P02866; IntAct: EBI-2906001; Score: 0.35
DE  Interaction: O15160; IntAct: EBI-3907424; Score: 0.37
DE  Interaction: P05181; IntAct: EBI-3907394; Score: 0.37
DE  Interaction: Q99708; IntAct: EBI-3907404; Score: 0.37
DE  Interaction: O14901; IntAct: EBI-3907414; Score: 0.37
DE  Interaction: Q14145; IntAct: EBI-3907434; Score: 0.37
DE  Interaction: Q9Y3Q8; IntAct: EBI-3916122; Score: 0.37
DE  Interaction: P45984; IntAct: EBI-3927894; Score: 0.37
DE  Interaction: P62829; IntAct: EBI-3927914; Score: 0.37
DE  Interaction: P46379; IntAct: EBI-3927904; Score: 0.37
DE  Interaction: Q07817; IntAct: EBI-4322676; Score: 0.61
DE  Interaction: Q9BWU1; IntAct: EBI-6381327; Score: 0.35
DE  Interaction: P18509; IntAct: EBI-10129061; Score: 0.54
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: Q8AZK7; IntAct: EBI-11734159; Score: 0.35
DE  Interaction: Q6P5D4; IntAct: EBI-10991106; Score: 0.35
DE  Interaction: A2APR8; IntAct: EBI-11001201; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-11044830; Score: 0.35
DE  Interaction: Q9Z0X1; IntAct: EBI-11065573; Score: 0.35
DE  Interaction: Q9D3R3; IntAct: EBI-11075393; Score: 0.35
DE  Interaction: Q6ZQ29; IntAct: EBI-11075869; Score: 0.35
DE  Interaction: Q6NXE6; IntAct: EBI-11080193; Score: 0.35
DE  Interaction: Q96RT8; IntAct: EBI-11083232; Score: 0.35
DE  Interaction: Q9DB34; IntAct: EBI-11115096; Score: 0.35
DE  Interaction: P51114; IntAct: EBI-11117520; Score: 0.35
DE  Interaction: Q96HP0; IntAct: EBI-11117520; Score: 0.35
DE  Interaction: Q7Z333; IntAct: EBI-11117520; Score: 0.35
DE  Interaction: Q5VW52; IntAct: EBI-11117520; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-11117520; Score: 0.35
DE  Interaction: P16234; IntAct: EBI-11134723; Score: 0.35
DE  Interaction: P03428; IntAct: EBI-12580574; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: P20036; IntAct: EBI-21511890; Score: 0.35
DE  Interaction: Q01814; IntAct: EBI-21599092; Score: 0.35
DE  Interaction: Q9H8H2; IntAct: EBI-21616235; Score: 0.35
DE  Interaction: Q8NI29; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q6P9B9; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q9UHG3; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q9UBQ6; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q9P273; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q9NYQ6; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q9NX40; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q9H0V9; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q9BV94; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q8NFZ4; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q8NBM8; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q6V0I7; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q6PKC3; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q5SRI9; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q5JTY5; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q58EX2; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q13332; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: P62879; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: P53708; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: P41273; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: P33908; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: P10586; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: O60476; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q6ZRI8; IntAct: EBI-21744920; Score: 0.35
DE  Interaction: O15063; IntAct: EBI-21830964; Score: 0.35
DE  Interaction: Q6P158; IntAct: EBI-21831097; Score: 0.35
DE  Interaction: Q96AT9; IntAct: EBI-21831245; Score: 0.35
DE  Interaction: Q96QG7; IntAct: EBI-21831285; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-15960333; Score: 0.68
DE  Interaction: Q9H4B6; IntAct: EBI-16425156; Score: 0.37
DE  Interaction: Q96RS6; IntAct: EBI-20723339; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: Q9NZV6; IntAct: EBI-20976398; Score: 0.67
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9NRD1; IntAct: EBI-21259874; Score: 0.35
DE  Interaction: Q14108; IntAct: EBI-21264396; Score: 0.35
DE  Interaction: Q9Y275; IntAct: EBI-21266480; Score: 0.35
DE  Interaction: Q16799; IntAct: EBI-21368794; Score: 0.37
DE  Interaction: Q9Y6D5; IntAct: EBI-21370252; Score: 0.00
DE  Interaction: Q15185; IntAct: EBI-21370704; Score: 0.00
DE  Interaction: Q9UBU8; IntAct: EBI-21370901; Score: 0.00
DE  Interaction: Q96PY5; IntAct: EBI-21371604; Score: 0.00
DE  Interaction: Q06787; IntAct: EBI-21371844; Score: 0.00
DE  Interaction: P10909; IntAct: EBI-21371813; Score: 0.00
DE  Interaction: P11766; IntAct: EBI-21372154; Score: 0.00
DE  Interaction: Q7Z699; IntAct: EBI-21372907; Score: 0.00
DE  Interaction: P14868; IntAct: EBI-21372879; Score: 0.00
DE  Interaction: P36957; IntAct: EBI-21373212; Score: 0.00
DE  Interaction: Q7Z698; IntAct: EBI-21373545; Score: 0.00
DE  Interaction: Q9UL68; IntAct: EBI-21374623; Score: 0.00
DE  Interaction: O75592; IntAct: EBI-21374795; Score: 0.00
DE  Interaction: Q86TG7; IntAct: EBI-21374847; Score: 0.00
DE  Interaction: P02794; IntAct: EBI-21376448; Score: 0.00
DE  Interaction: Q6AI39; IntAct: EBI-21376290; Score: 0.00
DE  Interaction: Q6GYQ0; IntAct: EBI-21376644; Score: 0.00
DE  Interaction: Q96EK5; IntAct: EBI-21377229; Score: 0.00
DE  Interaction: Q00994; IntAct: EBI-21377480; Score: 0.00
DE  Interaction: F8VWT9; IntAct: EBI-21378210; Score: 0.00
DE  Interaction: Q13439; IntAct: EBI-21378008; Score: 0.00
DE  Interaction: P08238; IntAct: EBI-21379316; Score: 0.00
DE  Interaction: P07900; IntAct: EBI-21379300; Score: 0.00
DE  Interaction: Q6ZMI3; IntAct: EBI-21379522; Score: 0.00
DE  Interaction: Q5SZL2; IntAct: EBI-21380088; Score: 0.00
DE  Interaction: P26367; IntAct: EBI-21381283; Score: 0.00
DE  Interaction: Q9NR80; IntAct: EBI-21381216; Score: 0.00
DE  Interaction: Q9UBW8; IntAct: EBI-21381443; Score: 0.00
DE  Interaction: Q9Y575; IntAct: EBI-21381570; Score: 0.00
DE  Interaction: P48426; IntAct: EBI-21382180; Score: 0.00
DE  Interaction: Q9BZ95; IntAct: EBI-21382818; Score: 0.00
DE  Interaction: Q9NVR2; IntAct: EBI-21383211; Score: 0.00
DE  Interaction: Q9NWB6; IntAct: EBI-21383120; Score: 0.00
DE  Interaction: Q5VTB9; IntAct: EBI-21383239; Score: 0.00
DE  Interaction: P53041; IntAct: EBI-21383361; Score: 0.00
DE  Interaction: P31321; IntAct: EBI-21383806; Score: 0.00
DE  Interaction: Q9NPF5; IntAct: EBI-21384190; Score: 0.00
DE  Interaction: Q58WW2; IntAct: EBI-21383966; Score: 0.00
DE  Interaction: Q6NUQ1; IntAct: EBI-21385792; Score: 0.00
DE  Interaction: Q9BXM7; IntAct: EBI-21386538; Score: 0.00
DE  Interaction: Q07890; IntAct: EBI-21387074; Score: 0.00
DE  Interaction: Q99615; IntAct: EBI-21387981; Score: 0.00
DE  Interaction: P26640; IntAct: EBI-21388258; Score: 0.00
DE  Interaction: Q15059; IntAct: EBI-21389314; Score: 0.00
DE  Interaction: Q9C093; IntAct: EBI-21389142; Score: 0.00
DE  Interaction: Q9H974; IntAct: EBI-21389084; Score: 0.00
DE  Interaction: Q96MT8; IntAct: EBI-21389423; Score: 0.00
DE  Interaction: Q14515; IntAct: EBI-21390086; Score: 0.00
DE  Interaction: Q96K75; IntAct: EBI-21390447; Score: 0.00
DE  Interaction: Q92610; IntAct: EBI-21392680; Score: 0.00
DE  Interaction: Q9Y2B5; IntAct: EBI-21392543; Score: 0.00
DE  Interaction: P27918; IntAct: EBI-21995211; Score: 0.35
DE  Interaction: P37840; IntAct: EBI-25295611; Score: 0.66
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: O96028; IntAct: EBI-25486814; Score: 0.35
DE  Interaction: Q9BY14; IntAct: EBI-25505396; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25686340; Score: 0.35
DE  Interaction: P0DTC8; IntAct: EBI-25687968; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25773054; Score: 0.35
DE  Interaction: Q15672; IntAct: EBI-25824698; Score: 0.37
DE  Interaction: P78352; IntAct: EBI-26509146; Score: 0.37
DE  Interaction: Q9BYB0; IntAct: EBI-26513929; Score: 0.37
DE  Interaction: Q8N488; IntAct: EBI-27111302; Score: 0.35
DE  Interaction: P20794; IntAct: EBI-28934658; Score: 0.35
DE  Interaction: Q8NI60; IntAct: EBI-28943519; Score: 0.35
DE  Interaction: Q9H5K3; IntAct: EBI-28948637; Score: 0.35
DE  Interaction: Q16832; IntAct: EBI-32717626; Score: 0.42
DE  Interaction: P11362; IntAct: EBI-32718427; Score: 0.35
DE  Interaction: Q16288; IntAct: EBI-32719212; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-32719373; Score: 0.35
DE  Interaction: P07949; IntAct: EBI-32719411; Score: 0.35
DE  Interaction: P34925; IntAct: EBI-32719634; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-32719716; Score: 0.35
GO  GO:0097440;
GO  GO:0072562;
GO  GO:0009986;
GO  GO:0042583;
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0097418;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0048471;
GO  GO:0031093;
GO  GO:0032991;
GO  GO:0034366;
GO  GO:0045202;
GO  GO:0001540;
GO  GO:0051087;
GO  GO:0050750;
GO  GO:0051787;
GO  GO:0140597;
GO  GO:0046982;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0048156;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0000902;
GO  GO:0032286;
GO  GO:0051131;
GO  GO:0061077;
GO  GO:0006956;
GO  GO:0006958;
GO  GO:0002434;
GO  GO:0045087;
GO  GO:0097193;
GO  GO:0006629;
GO  GO:0001774;
GO  GO:0061518;
GO  GO:1905907;
GO  GO:1902430;
GO  GO:0060548;
GO  GO:1905892;
GO  GO:1905895;
GO  GO:1902230;
GO  GO:0031333;
GO  GO:0090201;
GO  GO:1903573;
GO  GO:1905908;
GO  GO:1902004;
GO  GO:0043065;
GO  GO:0010628;
GO  GO:2001244;
GO  GO:1902998;
GO  GO:1901216;
GO  GO:0051092;
GO  GO:0045429;
GO  GO:0032436;
GO  GO:0031334;
GO  GO:0048260;
GO  GO:1902949;
GO  GO:0032760;
GO  GO:2000060;
GO  GO:0017038;
GO  GO:0050821;
GO  GO:0061740;
GO  GO:1900221;
GO  GO:0042981;
GO  GO:0042127;
GO  GO:1901214;
GO  GO:1902847;
GO  GO:0001836;
GO  GO:0051788;
GO  GO:0009615;
GO  GO:0043691;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKK
SQ  KEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRID
SQ  SLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNF
SQ  HAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQ
SQ  AKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPS
SQ  GVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE
//
ID  P14683;
PN  Clusterin alpha chain;
GN  CLU;
OS  10036;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P10909}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10909}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q9XSC5}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
DR  UNIPROT: P14683;
DR  Pfam: PF01093;
DR  PROSITE: PS00493;
DE  Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:P10909, ECO:0000250|UniProtKB:Q06890}.
DE  Reference Proteome: Yes;
GO  GO:0042583;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005576;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0051082;
GO  GO:0030154;
GO  GO:0002434;
GO  GO:1905907;
GO  GO:0043065;
GO  GO:0048260;
GO  GO:0050821;
GO  GO:0042127;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P10909};
SQ  NRRPHFLYPKSRLIRSLLPPPHYGPLSFHDMFQPFLEMIHQAQQAMDVQFHSPAFQFPDMDLLREGEDDRAVCKEIRHNS
SQ  TGCLKMKGQCEKCQEILSVDCSANNPAQAHLRQELNDSLQVAERLTQRYNELLHSLQTKMLNTSSLLEQLNEQFNWVSQL
SQ  ANLTQGEDQYYLRVSTVTTHSSDSEVPSRVT
//
ID  Q06890;
PN  Clusterin alpha chain;
GN  Clu;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted {ECO:0000269|PubMed:12551933}. Nucleus {ECO:0000269|PubMed:12551933}. Cytoplasm {ECO:0000269|PubMed:12551933}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000269|PubMed:12551933}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:P10909}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
DR  UNIPROT: Q06890;
DR  Pfam: PF01093;
DR  PROSITE: PS00492;
DR  PROSITE: PS00493;
DE  Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins (By similarity). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:14741101). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (PubMed:12551933). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. Following ER stress, suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. When secreted, does not affect caspase or BAX- mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). When secreted, acts as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (PubMed:11865066). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:P10909, ECO:0000269|PubMed:11865066, ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:14741101}.
DE  Reference Proteome: Yes;
DE  Interaction: P04925; IntAct: EBI-7188678; Score: 0.40
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.53
DE  Interaction: Q80YT7; IntAct: EBI-16732484; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
DE  Interaction: Q9JLC3; IntAct: EBI-20976809; Score: 0.40
DE  Interaction: P16056; IntAct: EBI-27112678; Score: 0.35
GO  GO:0016235;
GO  GO:0097440;
GO  GO:0071944;
GO  GO:0009986;
GO  GO:0042583;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0030426;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0097418;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0034366;
GO  GO:0045202;
GO  GO:0001540;
GO  GO:0050750;
GO  GO:0051787;
GO  GO:0140597;
GO  GO:0047485;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0048156;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0000902;
GO  GO:0032286;
GO  GO:0051131;
GO  GO:0061077;
GO  GO:0031018;
GO  GO:0002434;
GO  GO:0097193;
GO  GO:0001774;
GO  GO:0061518;
GO  GO:1905907;
GO  GO:1902430;
GO  GO:0043066;
GO  GO:0060548;
GO  GO:1905892;
GO  GO:1905895;
GO  GO:1902230;
GO  GO:0031333;
GO  GO:1903573;
GO  GO:0048812;
GO  GO:1902004;
GO  GO:0043065;
GO  GO:0045597;
GO  GO:0008284;
GO  GO:0010628;
GO  GO:2001244;
GO  GO:1902998;
GO  GO:1901216;
GO  GO:0051092;
GO  GO:0045429;
GO  GO:0032436;
GO  GO:0031334;
GO  GO:0048260;
GO  GO:1902949;
GO  GO:0032760;
GO  GO:2000060;
GO  GO:0017038;
GO  GO:0050821;
GO  GO:0061740;
GO  GO:1900221;
GO  GO:0042981;
GO  GO:0042127;
GO  GO:1901214;
GO  GO:1902847;
GO  GO:0051788;
GO  GO:0009615;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P10909};
SQ  MKILLLCVALLLIWDNGMVLGEQEVSDNELQELSTQGSRYINKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKK
SQ  EDALEDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGQQLEEFLNQSSPFYFWMNGDRIDS
SQ  LLESDRQQSQVLDAMQDSFARASGIIDTLFQDRFFARELHDPHYFSPIGFPHKRPHFLYPKSRLVRSLMSPSHYGPPSFH
SQ  NMFQPFFEMIHQAQQAMDVQLHSPAFQFPDVDFLREGEDDRTVCKEIRRNSTGCLKMKGQCEKCQEILSVDCSTNNPAQA
SQ  NLRQELNDSLQVAERLTEQYKELLQSFQSKMLNTSSLLEQLNDQFNWVSQLANLTQGEDKYYLRVSTVTTHSSDSEVPSR
SQ  VTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRAE
//
ID  Q29549;
PN  Clusterin alpha chain;
GN  CLU;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P10909}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10909}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q9XSC5}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
DR  UNIPROT: Q29549;
DR  Pfam: PF01093;
DR  PROSITE: PS00492;
DR  PROSITE: PS00493;
DE  Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:P10909, ECO:0000250|UniProtKB:Q06890}.
DE  Reference Proteome: Yes;
DE  Interaction: F0QRW4; IntAct: EBI-13630150; Score: 0.37
GO  GO:0042583;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0048471;
GO  GO:0034366;
GO  GO:0051787;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0061077;
GO  GO:0002434;
GO  GO:0097193;
GO  GO:1905907;
GO  GO:1902230;
GO  GO:0031333;
GO  GO:0043065;
GO  GO:2001244;
GO  GO:0051092;
GO  GO:0032436;
GO  GO:0048260;
GO  GO:2000060;
GO  GO:0050821;
GO  GO:0042981;
GO  GO:0042127;
GO  GO:0051788;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P10909};
SQ  MKTLLLLVGLLLTWENGPWVLGDKAISDKELQEMSTEGSKYVNKEIKNALKEVKQIKTLIEQSNEERKSLLSSLEEAKKK
SQ  KEDALNDTRDTETKLKGSQGLCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGHQLEEFLNQSSPFYFWINGDRID
SQ  SLMENDRQQSHVMDIMEDSFNRASNIMDELFQDRFFNREPFDTQFFSPFGSSHRGSLFFNPKSRFARNIMPFPLFTDLNY
SQ  HDMFQPFFDMIHQAQQAMDAHLHRIPYHFPEAGVPENSNDRAVCKEIRHNSTGCLRMKDQCEKCREILSVDCSASNSSQM
SQ  QLRQELYTSLQMAEKFSKLYDQLLQSYQQKMLNTSSLLKQLNEQFSWVSQLANLTQNDDRYYLQVTTVNSHGSDPSVPSG
SQ  LTKVVVKLFDSYPITLIIPQEVSDPKFMETVAEEALQQYRQRSREE
//
ID  Q9XSC5;
PN  Clusterin alpha chain;
GN  CLU;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P10909}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10909}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre- secreted form retrotranslocates from the endoplasmic reticulum (ER)- Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
DR  UNIPROT: Q9XSC5;
DR  Pfam: PF01093;
DR  PROSITE: PS00492;
DE  Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:P10909, ECO:0000250|UniProtKB:Q06890}.
DE  Reference Proteome: Yes;
GO  GO:0042583;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0048471;
GO  GO:0034366;
GO  GO:0051787;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0061077;
GO  GO:0002434;
GO  GO:0097193;
GO  GO:1905907;
GO  GO:1902230;
GO  GO:0031333;
GO  GO:0043065;
GO  GO:2001244;
GO  GO:0051092;
GO  GO:0032436;
GO  GO:0048260;
GO  GO:2000060;
GO  GO:0050821;
GO  GO:0042127;
GO  GO:0051788;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P10909};
SQ  MKTLLLCVGLLLSWERGQVLGDQLVSDNELQEMSTQGSKYIDREIQNAVKGVQEIKTLIEKTNEERKTLLSVLEEAKKNK
SQ  EDALNETRDSETKLKAFPEVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWINGDRIDS
SQ  LLENDRQQSHVLDVMQDSFNRATGIMDELFQDRFFTHKPQDTFYHSPFSYFRRPPLHYAKSRLVRNIMPLSLYGPLNFQD
SQ  MFQPFFEMIHQAQQAMDVHLHSPAYQTPNVEFITGGPDDRAVCKEIRHNSTGCLRMKDQCAKCQEILSVDCSANNPSQNQ
SQ  LRQELNDSLRLAEELTKRYNELLQSYQWKMLNTSSLLDQPNEQFNWVSQLANLTQGPDQYYLRVSTVTSHTSESEAPSRV
SQ  TEVVVKLFDSDPITITIPEEVSRDNPKFMETVAEKALQEYRKKKRVE
//
ID  P05371;
PN  Clusterin alpha chain;
GN  Clu;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted {ECO:0000269|PubMed:3415696, ECO:0000269|PubMed:3651384}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000269|PubMed:16038898}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16038898}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre- secreted form retrotranslocates from the endoplasmic reticulum (ER)- Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
DR  UNIPROT: P05371;
DR  Pfam: PF01093;
DR  PROSITE: PS00492;
DR  PROSITE: PS00493;
DE  Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (PubMed:16038898). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P10909, ECO:0000250|UniProtKB:Q06890, ECO:0000269|PubMed:16038898}.
DE  Reference Proteome: Yes;
DE  Interaction: P21708; IntAct: EBI-7618770; Score: 0.35
GO  GO:0016235;
GO  GO:0097440;
GO  GO:0009986;
GO  GO:0042583;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0030426;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0097418;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0034366;
GO  GO:0045202;
GO  GO:0001540;
GO  GO:0050750;
GO  GO:0051787;
GO  GO:0140597;
GO  GO:0047485;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0048156;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0007568;
GO  GO:0000902;
GO  GO:0071363;
GO  GO:0032286;
GO  GO:0051131;
GO  GO:0061077;
GO  GO:0031018;
GO  GO:0044849;
GO  GO:0002434;
GO  GO:0097193;
GO  GO:0001774;
GO  GO:0061518;
GO  GO:1905907;
GO  GO:1902430;
GO  GO:0043066;
GO  GO:0060548;
GO  GO:1905892;
GO  GO:1905895;
GO  GO:1902230;
GO  GO:0031333;
GO  GO:1903573;
GO  GO:0048812;
GO  GO:1902004;
GO  GO:0043065;
GO  GO:0045597;
GO  GO:0008284;
GO  GO:0010628;
GO  GO:2001244;
GO  GO:1902998;
GO  GO:1901216;
GO  GO:0051092;
GO  GO:0045429;
GO  GO:0032436;
GO  GO:0031334;
GO  GO:0048260;
GO  GO:1902949;
GO  GO:0032760;
GO  GO:2000060;
GO  GO:0017038;
GO  GO:0050821;
GO  GO:0061740;
GO  GO:1900221;
GO  GO:0042981;
GO  GO:0042127;
GO  GO:1901214;
GO  GO:1902847;
GO  GO:0009416;
GO  GO:0051788;
GO  GO:0035864;
GO  GO:0009615;
GO  GO:0009611;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P10909};
SQ  MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKK
SQ  EGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDS
SQ  LLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFH
SQ  NMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQA
SQ  NLRQELNDSLQVAERLTQQYNELLHSLQSKMLNTSSLLEQLNDQFTWVSQLANLTQGDDQYLRVSTVTTHSSDSEVPSRV
SQ  TEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME
//
ID  P17698;
PN  Clusterin alpha chain;
GN  CLU;
OS  9940;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P10909}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P10909}. Microsome {ECO:0000250|UniProtKB:P10909}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P10909}. Mitochondrion {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05371}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q9XSC5}. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm. {ECO:0000250|UniProtKB:P10909}.
DR  UNIPROT: P17698;
DR  Pfam: PF01093;
DE  Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). {ECO:0000250|UniProtKB:P05371, ECO:0000250|UniProtKB:P10909, ECO:0000250|UniProtKB:Q06890}.
DE  Reference Proteome: Yes;
GO  GO:0042583;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005576;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0099020;
GO  GO:0051082;
GO  GO:0002434;
GO  GO:1905907;
GO  GO:0043065;
GO  GO:0048260;
GO  GO:0050821;
GO  GO:0042127;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P10909};
SQ  ISGKELQEMSTEGSKYVNKEIKNALKEVLQIKLVMEQGREQSSVMNVMPFPLLEPLNFHDVFQPFY
//
ID  Q8N3K9;
PN  Cardiomyopathy-associated protein 5;
GN  CMYA5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:A0A286XF80}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm {ECO:0000250|UniProtKB:Q70KF4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:20634290}. Note=Found predominantly at the periphery of the nucleus but also throughout the cell. Localized in lysosomes (By similarity). In skeletal muscles, localizes along myofiber periphery, at costameres (By similarity). Predominantly flanks Z-disks (By similarity). Occasionally present at the M-band level. Colocalized with RYR2 in the sarcoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:A0A286XF80}.
DR  UNIPROT: Q8N3K9;
DR  UNIPROT: A0PJB7;
DR  UNIPROT: Q05CT4;
DR  UNIPROT: Q2NKX1;
DR  UNIPROT: Q2T9G9;
DR  UNIPROT: Q69YQ8;
DR  UNIPROT: Q69YQ9;
DR  UNIPROT: Q6P517;
DR  UNIPROT: Q6P5U3;
DR  UNIPROT: Q7Z4I1;
DR  UNIPROT: Q86T34;
DR  UNIPROT: Q86T49;
DR  UNIPROT: Q8N3S4;
DR  UNIPROT: Q8N3S7;
DR  UNIPROT: Q8NAG8;
DR  UNIPROT: Q9UK88;
DR  Pfam: PF00041;
DR  PROSITE: PS50188;
DR  PROSITE: PS50853;
DR  OMIM: 612193;
DR  DisGeNET: 202333;
DE  Function: May serve as an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) via binding to PRKAR2A (By similarity). May function as a repressor of calcineurin- mediated transcriptional activity. May attenuate calcineurin ability to induce slow-fiber gene program in muscle and may negatively modulate skeletal muscle regeneration (By similarity). Plays a role in the assembly of ryanodine receptor (RYR2) clusters in striated muscle (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q70KF4}.
DE  Reference Proteome: Yes;
DE  Interaction: O95295; IntAct: EBI-5664244; Score: 0.00
DE  Interaction: P43686; IntAct: EBI-1060801; Score: 0.00
DE  Interaction: Q7L1Q6; IntAct: EBI-1074757; Score: 0.00
DE  Interaction: Q96EB6; IntAct: EBI-2321764; Score: 0.40
DE  Interaction: Q9NTG7; IntAct: EBI-2322825; Score: 0.40
DE  Interaction: O75923; IntAct: EBI-5357119; Score: 0.50
DE  Interaction: P20807; IntAct: EBI-5655093; Score: 0.00
DE  Interaction: Q8N3C7; IntAct: EBI-5655585; Score: 0.00
DE  Interaction: P40189; IntAct: EBI-5655920; Score: 0.00
DE  Interaction: Q8N3K9; IntAct: EBI-5655903; Score: 0.00
DE  Interaction: Q14324; IntAct: EBI-5660911; Score: 0.00
DE  Interaction: Q96CV9; IntAct: EBI-5662034; Score: 0.00
DE  Interaction: Q16082; IntAct: EBI-15487490; Score: 0.37
DE  Interaction: Q01968; IntAct: EBI-16412116; Score: 0.35
DE  Interaction: Q02539; IntAct: EBI-20922246; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21024514; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0031430;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASRDSNHAGESFLGSDGDEEATRELETEEESEGEEDETAAESEEEPDSRLSDQDEEGKIKQEYIISDPSFSMVTVQRED
SQ  SGITWETNSSRSSTPWASEESQTSGVCSREGSTVNSPPGNVSFIVDEVKKVRKRTHKSKHGSPSLRRKGNRKRNSFESQD
SQ  VPTNKKGSPLTSASQVLTTEKEKSYTGIYDKARKKKTTSNTPPITGAIYKEHKPLVLRPVYIGTVQYKIKMFNSVKEELI
SQ  PLQFYGTLPKGYVIKEIHYRKGKDASISLEPDLDNSGSNTVSKTRKLVAQSIEDKVKEVFPPWRGALSKGSESLTLMFSH
SQ  EDQKKIYADSPLNATSALEHTVPSYSSSGRAEQGIQLRHSQSVPQQPEDEAKPHEVEPPSVTPDTPATMFLRTTKEECEL
SQ  ASPGTAASENDSSVSPSFANEVKKEDVYSAHHSISLEAASPGLAASTQDGLDPDQEQPDLTSIERAEPVSAKLTPTHPSV
SQ  KGEKEENMLEPSISLSEPLMLEEPEKEEIETSLPIAITPEPEDSNLVEEEIVELDYPESPLVSEKPFPPHMSPEVEHKEE
SQ  ELILPLLAASSPEHVALSEEEREEIASVSTGSAFVSEYSVPQDLNHELQEQEGEPVPPSNVEAIAEHAVLSEEENEEFEA
SQ  YSPAAAPTSESSLSPSTTEKTSENQSPLFSTVTPEYMVLSGDEASESGCYTPDSTSASEYSVPSLATKESLKKTIDRKSP
SQ  LILKGVSEYMIPSEEKEDTGSFTPAVAPASEPSLSPSTTEKTSECQSPLPSTATSEHVVPSEGEDLGSERFTPDSKLISK
SQ  YAAPLNATQESQKKIINEASQFKPKGISEHTVLSVDGKEVIGPSSPDLVVASEHSFPPHTTEMTSECQAPPLSATPSEYV
SQ  VLSDEEAVELERYTPSSTSASEFSVPPYATPEAQEEEIVHRSLNLKGASSPMNLSEEDQEDIGPFSPDSAFVSEFSFPPY
SQ  ATQEAEKREFECDSPICLTSPSEHTILSDEDTEEAELFSPDSASQVSIPPFRISETEKNELEPDSLLTAVSASGYSCFSE
SQ  ADEEDIGSTAATPVSEQFSSSQKQKAETFPLMSPLEDLSLPPSTDKSEKAEIKPEIPTTSTSVSEYLILAQKQKTQAYLE
SQ  PESEDLIPSHLTSEVEKGEREASSSVAAIPAALPAQSSIVKEETKPASPHSVLPDSVPAIKKEQEPTAALTLKAADEQMA
SQ  LSKVRKEEIVPDSQEATAHVSQDQKMEPQPPNVPESEMKYSVLPDMVDEPKKGVKPKLVLNVTSELEQRKLSKNEPEVIK
SQ  PYSPLKETSLSGPEALSAVKMEMKHDSKITTTPIVLHSASSGVEKQVEHGPPALAFSALSEEIKKEIEPSSSTTTASVTK
SQ  LDSNLTRAVKEEIPTDSSLITPVDRPVLTKVGKGELGSGLPPLVTSADEHSVLAEEDKVAIKGASPIETSSKHLAWSEAE
SQ  KEIKFDSLPSVSSIAEHSVLSEVEAKEVKAGLPVIKTSSSQHSDKSEEARVEDKQDLLFSTVCDSERLVSSQKKSLMSTS
SQ  EVLEPEHELPLSLWGEIKKKETELPSSQNVSPASKHIIPKGKDEETASSSPELENLASGLAPTLLLLSDDKNKPAVEVSS
SQ  TAQGDFPSEKQDVALAELSLEPEKKDKPHQPLELPNAGSEFSSDLGRQSGSIGTKQAKSPITETEDSVLEKGPAELRSRE
SQ  GKEENRELCASSTMPAISELSSLLREESQNEEIKPFSPKIISLESKEPPASVAEGGNPEEFQPFTFSLKGLSEEVSHPAD
SQ  FKKGGNQEIGPLPPTGNLKAQVMGDILDKLSEETGHPNSSQVLQSITEPSKIAPSDLLVEQKKTEKALHSDQTVKLPDVS
SQ  TSSEDKQDLGIKQFSLMRENLPLEQSKSFMTTKPADVKETKMEEFFISPKDENWMLGKPENVASQHEQRIAGSVQLDSSS
SQ  SNELRPGQLKAAVSSKDHTCEVRKQVLPHSAEESHLSSQEAVSALDTSSGNTETLSSKSYSSEEVKLAEEPKSLVLAGNV
SQ  ERNIAEGKEIHSLMESESLLLEKANTELSWPSKEDSQEKIKLPPERFFQKPVSGLSVEQVKSETISSSVKTAHFPAEGVE
SQ  PALGNEKEAHRSTPPFPEEKPLEESKMVQSKVIDDADEGKKPSPEVKIPTQRKPISSIHAREPQSPESPEVTQNPPTQPK
SQ  VAKPDLPEEKGKKGISSFKSWMSSLFFGSSTPDNKVAEQEDLETQPSPSVEKAVTVIDPEGTIPTNFNVAEKPADHSLSE
SQ  VKLKTADEPRGTLVKSGDGQNVKEKSMILSNVEDLQQPKFISEVSREDYGKKEISGDSEEMNINSVVTSADGENLEIQSY
SQ  SLIGEKLVMEEAKTIVPPHVTDSKRVQKPAIAPPSKWNISIFKEEPRSDQKQKSLLSFDVVDKVPQQPKSASSNFASKNI
SQ  TKESEKPESIILPVEESKGSLIDFSEDRLKKEMQNPTSLKISEEETKLRSVSPTEKKDNLENRSYTLAEKKVLAEKQNSV
SQ  APLELRDSNEIGKTQITLGSRSTELKESKADAMPQHFYQNEDYNERPKIIVGSEKEKGEEKENQVYVLSEGKKQQEHQPY
SQ  SVNVAESMSRESDISLGHSLGETQSFSLVKATSVTEKSEAMLAEAHPEIREAKAVGTQPHPLEESKVLVEKTKTFLPVAL
SQ  SCRDEIENHSLSQEGNLVLEKSSRDMPDHSEEKEQFRESELSKGGSVDITKETVKQGFQEKAVGTQPRPLEESKVLVEKT
SQ  KTFLPVVLSCHDEIENHSLSQEGNLVLEKSSRDMPDHSEEKEQFKESELWKGGSVDITKESMKEGFPSKESERTLARPFD
SQ  ETKSSETPPYLLSPVKPQTLASGASPEINAVKKKEMPRSELTPERHTVHTIQTSKDDTSDVPKQSVLVSKHHLEAAEDTR
SQ  VKEPLSSAKSNYAQFISNTSASNADKMVSNKEMPKEPEDTYAKGEDFTVTSKPAGLSEDQKTAFSIISEGCEILNIHAPA
SQ  FISSIDQEESEQMQDKLEYLEEKASFKTIPLPDDSETVACHKTLKSRLEDEKVTPLKENKQKETHKTKEEISTDSETDLS
SQ  FIQPTIPSEEDYFEKYTLIDYNISPDPEKQKAPQKLNVEEKLSKEVTEETISFPVSSVESALEHEYDLVKLDESFYGPEK
SQ  GHNILSHPETQSQNSADRNVSKDTKRDVDSKSPGMPLFEAEEGVLSRTQIFPTTIKVIDPEFLEEPPALAFLYKDLYEEA
SQ  VGEKKKEEETASEGDSVNSEASFPSRNSDTDDGTGIYFEKYILKDDILHDTSLTQKDQGQGLEEKRVGKDDSYQPIAAEG
SQ  EIWGKFGTICREKSLEEQKGVYGEGESVDHVETVGNVAMQKKAPITEDVRVATQKISYAVPFEDTHHVLERADEAGSHGN
SQ  EVGNASPEVNLNVPVQVSFPEEEFASGATHVQETSLEEPKILVPPEPSEERLRNSPVQDEYEFTESLHNEVVPQDILSEE
SQ  LSSESTPEDVLSQGKESFEHISENEFASEAEQSTPAEQKELGSERKEEDQLSSEVVTEKAQKELKKSQIDTYCYTCKCPI
SQ  SATDKVFGTHKDHEVSTLDTAISAVKVQLAEFLENLQEKSLRIEAFVSEIESFFNTIEENCSKNEKRLEEQNEEMMKKVL
SQ  AQYDEKAQSFEEVKKKKMEFLHEQMVHFLQSMDTAKDTLETIVREAEELDEAVFLTSFEEINERLLSAMESTASLEKMPA
SQ  AFSLFEHYDDSSARSDQMLKQVAVPQPPRLEPQEPNSATSTTIAVYWSMNKEDVIDSFQVYCMEEPQDDQEVNELVEEYR
SQ  LTVKESYCIFEDLEPDRCYQVWVMAVNFTGCSLPSERAIFRTAPSTPVIRAEDCTVCWNTATIRWRPTTPEATETYTLEY
SQ  CRQHSPEGEGLRSFSGIKGLQLKVNLQPNDNYFFYVRAINAFGTSEQSEAALISTRGTRFLLLRETAHPALHISSSGTVI
SQ  SFGERRRLTEIPSVLGEELPSCGQHYWETTVTDCPAYRLGICSSSAVQAGALGQGETSWYMHCSEPQRYTFFYSGIVSDV
SQ  HVTERPARVGILLDYNNQRLIFINAESEQLLFIIRHRFNEGVHPAFALEKPGKCTLHLGIEPPDSVRHK
//
ID  Q70KF4;
PN  Cardiomyopathy-associated protein 5;
GN  Cmya5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm, myofibril, sarcomere, M line. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:A0A286XF80}. Note=Found predominantly at the periphery of the nucleus but also throughout the cell. Localized in lysosomes. In skeletal muscles, localizes along myofiber periphery, at costameres. Predominantly flanks Z-disks (By similarity). Occasionally present at the M-band level. In the mdx mouse model for Duchenne muscular dystrophy, exhibits a discontinuous localization at the myofiber periphery with extensive regions devoid of CMYA5. This highly irregular pattern is associated with an increased cytoplasmic localization, particularly in discrete foci within myofibers. Colocalized with RYR2 in the sarcoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:A0A286XF80}.
DR  UNIPROT: Q70KF4;
DR  UNIPROT: Q70X91;
DR  UNIPROT: Q9CV01;
DR  UNIPROT: Q9CV02;
DR  UNIPROT: Q9ER93;
DR  UNIPROT: Q9ER96;
DR  Pfam: PF00041;
DR  PROSITE: PS50188;
DR  PROSITE: PS50853;
DE  Function: May serve as an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) via binding to PRKAR2A. May attenuate calcineurin ability to induce slow-fiber gene program in muscle and may negatively modulate skeletal muscle regeneration. Plays a role in the assembly of ryanodine receptor (RYR2) clusters in striated muscle. {ECO:0000269|PubMed:17499862, ECO:0000269|PubMed:18252718, ECO:0000269|PubMed:21427212, ECO:0000269|PubMed:28740084}.
DE  Reference Proteome: Yes;
DE  Interaction: Q91WZ8; IntAct: EBI-782286; Score: 0.59
DE  Interaction: Q70KF4; IntAct: EBI-782304; Score: 0.37
DE  Interaction: O88609; IntAct: EBI-13951518; Score: 0.35
GO  GO:0043034;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0031430;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016529;
GO  GO:0042802;
GO  GO:0070885;
GO  GO:0032515;
GO  GO:0014733;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESGDSGLAAQGFLGWGADEEVAQELETEEESEGEGEETAAESEEEPDARLSDEDEEGKTKQECIVSDPSFSMVAVQRED
SQ  SGITWETNSSRSSTPWASGESQTSGICSLEGSALTSPPGSVSFIMDEVKRTRKRTQKSKRGSPSLRRKGSKKRNSLESQD
SQ  VLTNQEDGPSISESPVLNIENEKSSIGTYDKTRRKKTASNTPPITGAIYKEHKPLVLKPVYIGTVQYKIKMFNSVKEELI
SQ  PLQFYGTLPKGYVIKEIHYRRGKDSSISLEPDLSNGGSNIVPQRKLAQSPEEDKVRELAPPWRGALSKGSRTSLFSHEEQ
SQ  KKTYADSNLNVPSSTEHAFPSSARNDTADQEENLSLPQMMPQQPADESKTHRMEPPSIPATMVLERAKEELEQNAQGKES
SQ  SEDDASVLTGSADDVQQEGLVSVNHSMPWEAEKESLETGPPRPAPAIQEKFEPDMEGLEPISTEKTEQASEYVTSSEPIV
SQ  HREEEHAPEPIVHREEEHAPEPIVHREEEHAPEPESIVHREEEHAPESIVHREEEHAPEPVPIVHREEEHAPEPESIVHR
SQ  EEEHAPEPIVHRDKGHALEPIVHREEEHAPEPIVHRDEGHAPEPIVHREEEHVPEPESIVRKGEEHAPEPIVHREEEQVP
SQ  EPESIVHREEEHAPEPIVHREEEQVPEPESIVHREEEHAPEPMVLREEHAPEPIVRREEEHAPEPIVHREEEHAPEPMVH
SQ  RKAQQLERGVETSTPITDITEPEDSSLEEEIIELDYPESPLASKETSPSPLSPEVEHRKEPILPTQMTFTPERITLSEEE
SQ  REENESVSTDSAFVSEYSVLQDLNHTPEKLEVEAVSVSDVKSSNEPAVFSEDDEERESYSPAMTSVSEQSLSPSTTEKTS
SQ  AIQSPLFSTVSPVLSGDEASENVCHSPESESAAEYSVPAHAQELLLKTGDHKLPLKSQRVSEPIIQAEDEKEDIGLLPPA
SQ  ALSQAVLSEDESLGSGSFASDSKLPFKPSVSQNATRESPQKTIDDMPQFKPRGLSDPATLLEEEKEAIGVGLSSSNEVSA
SQ  VECALPPQTTELLSESHAPPPWAISSEQVVQSEEGSRDQQRGSFSSTPELGHTSLLLKGASSPTGLSEQGQEEDNIGPLS
SQ  PDSAFASEFSFSPYPTQELEKRELGRDSPLCLTSPSEQTVLSEEDTEEADLFSPDSASQVSIPPYRIAETEQNKVEPDEL
SQ  LPTRSAPDYPYFSEADEEEAGSSVVTLVPEHSEPSQEREESSPCRPVFEDLSLPPSADKTGQAETMSDVPTISTSVSEYL
SQ  ILARQAKTQASLEPEAEDLVPPPTSGWEKRDAKSSLPAVTIAASSSALSSVVKEETTSVLPTSQPSVSPESTCVLKPEQE
SQ  PTAPLTLTSADEQMALPRVGREKAVLDSQEATAHKSQDQTPEPRLPNVPGSGMKYSVLSDLGDEPKADVKLNLAPTVTSE
SQ  LEQRMLSKNEPEVAKPHSPPEETSISGPKVLSAVKTEVKQESKITRELPAASSGRERGAEHSPPVPPALPALTEETGKDT
SQ  EASSSATTVPVTKLDSNSTKLGRDEVLTDPSLASPVEHPGLKGIGKSELGSGLPLPSMSASEVLRPEPKLPVNSGVEVER
SQ  EDNEPPPLQVSPTSKPTVPNDKHEEITRSPDSENLVSDDLAPTLLAFRHEMNRQAEETSSPVPGSFLSGEQELIKLPPEP
SQ  EKHKQLSEVPTAGSELIDSRDRDRSLGIEPVKPIGTEPGPSILEKGPAELQRRGKEQEENRKLPVPASAPLETASFDLPI
SQ  EQKEPKRTLHEGQAVEVPDESSSSADKPELGVKQLAEKKENLEQPKPFVTTERASVTGSKVKESLISPKDNIWMLEKPDG
SQ  LVNQHEDRKPGTGQLESSESTDLMSEKLGAASLDTDHTSETRNQETSKAPVSGEKLSQEPRRVQSKAVDDSEEGRKLASG
SQ  NVEVLTQSKSVPAVKAKATPQPPETPEVTQKPSEKSLVTEQGLPAEKGKKGISSFKSWMSSLLFGSSIPDSKVSDNEDLE
SQ  TRPGPSVEKAVPAIEPKGTVPAEVNIAEKPAVHSLPEVTVKLAEEPKGVSVKSSISQDLKEKLTFLSNEDVLKQPKSNSE
SQ  NYGQKELPGFSEGMGESLATSVGDKHPGIHPCSPMGEKVGMEEAQNMAPLHITESQRRQKPEVSPPSMWNISARKEEPSS
SQ  DHKETWLSSSDVVDRMPQKPKSAQSAFTRMNSEEPASMILPVESKGSLSDLGEDRLRQEMPKPTSLEHCEEEVERPTEEK
SQ  DGWETRSFSLAGKRGLAEKQEIMAPLELRENEAVGELQRMPESRPFKLEESKAAERLEQRISPTEKLMEKPSKTLALDRR
SQ  EKEVQEWVFSEGEKQEYPPAAMPVPGASAVSLDKAQPHLLAKPTPVVEKPEHIVTEVYPEIRERKAAETQPHPQEEGKTL
SQ  VEKTKVSRVESPHGEETDGHSLTQEGNLELEKSGESRVDLKEERRRFVMPELPLGASVAAEDGSVQPRPLSKDAARASDM
SQ  TDETKHLGTPPTQPSAVEPQTLVLGTSVEHAVKKQETWSDRPTVHTFQTSKDDTEEMLKQSVLISKHHLEAVEDVHRNEP
SQ  PSSAASNYAQFMLSASEISADGVPPMGGTAQEPEGTSVKDEEFSVTSKPAGLSEDQKSAFSIISEGCEILNIHAPAFIPS
SQ  VDQEESEQMQDKLQYLEEKASFKSISVHDEKKAAASHKTQKSKLEVPDRKITSLKENKTKETHKTKEEIATDSGMGDFTP
SQ  IQPTVSGEEDYFEKYTLIDYNLSPGSGKQKSTVEESSEEATKTLTSFPESSAEQALDHEYNLVKLDESFYGPEKDDSKLS
SQ  HAEMQKSLAIQKPDDRNAPKGISRDVDSRSPGMPLFDVEEGVLSKRQIFPTTPKAVNPELLEEPPALSFFYKDLYEGACG
SQ  EKNEGETASEGDSVDSETSFPRRHSDTDDGPGMYFEKYILKDDILHDESVTQEDQGQGLEEKPVGEEDSQQLRVAEREIR
SQ  RKPETSFWEKNLEEQHKVVGREGEPTGHMETLDEAAMQQKAPITEQVRAVTQKMSYAVPFQDTRCVLESEPSSQGNEAGN
SQ  ASPDVNLNVPVQVSFPEEESAAGATYAPEVLQERLVPSVSREERLHNTPVQDEYDFVGSLNQEAASQAILPEEPGSESSP
SQ  KEVLSQGSESFEHIREQELTSEGEPRMSASQEVWDRTEDQSARESVTAKTQKEPKKTQAESYCYTCKSLVSEMDKALDIH
SQ  KDHEVSALDTAISAVKVQLGEFLENLQEKSLRIEAFVSEIESFFNTIEEKCSKNEKRLEMQNEEMMKRVLAQYDEKAQSF
SQ  EEVKKKKMEFLHDQMVHFLQSMDTAKDTLETIVREAEELDETVFLASFEEINERLLSAMESTASLENMPAAFSLFEHYDD
SQ  SSARSDQMLKQVAVPQPPRLEPQEPSSATSTTIAVYWSVNKEDVVDSFQVYCVEEPQDDQEINELVEEYRLTVKESCCIF
SQ  EDLEPDRCYQVWVMAVNFTGCSLPSERAIFRTAPSTPVIHVEDCTVCWNTATVRWRPANPEATETYTLEYCRQHSPEGEG
SQ  LRSFSGIKGHQLKVNLPPNDNYFFYVRATNASGTSEQSEAALISTRGTRFLLLRETAHPALQISANGTVISFSERRRLTE
SQ  IPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGETSWYMHCSEPQRYTFFYSGIVSEVHATERPARVG
SQ  ILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFALEKPGRCTLHLGLEPPDSVRHK
//
ID  G7IBJ4;
PN  Protein CNGC15a;
GN  CNGC15A;
OS  3880;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: G7IBJ4;
DR  Pfam: PF00027;
DR  Pfam: PF00520;
DR  PROSITE: PS50042;
DE  Function: Cyclic nucleotide-gated channel involved in the establishment of both rhizobial and mycorrhizal associations (PubMed:27230377). Required for full activation of nuclear-localized Ca(2+) oscillations by Nod and Myc factors (PubMed:27230377). Simultaneous activation of the K(+)-permeable channel DMI1 and the Ca(2+) channel CNGC15 can give rise to sustained Ca(2+) oscillations (PubMed:27230377). May function during fertilization in both female and male gametophytic Ca(2+) signaling (PubMed:27230377). {ECO:0000269|PubMed:27230377}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005262;
GO  GO:0044325;
GO  GO:0005249;
GO  GO:0036377;
GO  GO:0009877;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASVISRAVRFHDDLEKEKLQEGEESHMEMRAYEMSSEYKHGKDAINKPSSNGRGLSRVFSEDYDAGEILVFDPRGPRIN
SQ  LWNKIFLAACLISLFVDPLFFYLPVAKKEKCIDMSIGLEVSLTIIRTFVDAFYIIHIYIRFQTAYIAPSSRVSGRGELII
SQ  DSSKIASNYMKKELWSDLVAALPLPQVLIWAVIPNIKGSEMIASRHVVRLVSIFQYLLRLYLIYPLSSKITKASGVMMEK
SQ  AWAGAAYYLTLYMLASHVLGSTWYLLSIERQDECWKKACTLQYPHCQYHYLDCQSLSDPNRNAWLKSSNLSGLCDQNSHF
SQ  FQFGIFDDAVTLEITSSNFLTKYYYCLWWGLRNLSSSGENLLTSTHVAEINFAVIVAILGLVLFALLIGNMQTYLQSTTI
SQ  RLEEWRIRRTDTERWMHHRQLPHYLKENVRRHDQFRWVATRGVDEEAILRDLPVDLRRDIKRHLCLNLVRQVPLFDQMDD
SQ  RMLDAICERLKPTLCTPGTCIVREGDPVDEMLFIVRGRLDSCTTNGGRTGFFNTCRIGSGDFCGEELLPWALDPRPTAVL
SQ  PSSTRTVRAITEVEAFALIAEDLKFVAAQFRRLHSKQLRQTFRFYSHQWRTWAACFIQAAWFRYKRMKETNEVKEKENLM
SQ  MMSNVKYYGNDDSQYFSAPLQVPKGSSYSMYSGKLVGSLRRGRSMRYGSELDMLGTLRKPIEPDFNDDGD
//
ID  G7JND3;
PN  Protein CNGC15b;
GN  CNGC15B;
OS  3880;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: G7JND3;
DR  UNIPROT: A0A0C3WX45;
DR  Pfam: PF00027;
DR  Pfam: PF00520;
DR  PROSITE: PS50042;
DE  Function: Cyclic nucleotide-gated channel involved in the establishment of both rhizobial and mycorrhizal associations (PubMed:27230377). Required for full activation of nuclear-localized Ca(2+) oscillations by Nod and Myc factors (PubMed:27230377). Simultaneous activation of the K(+)-permeable channel DMI1 and the Ca(2+) channel CNGC15 can give rise to sustained Ca(2+) oscillations (PubMed:27230377). May function during fertilization in both female and male gametophytic Ca(2+) signaling (PubMed:27230377). {ECO:0000269|PubMed:27230377}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005262;
GO  GO:0044325;
GO  GO:0005249;
GO  GO:0036377;
GO  GO:0009877;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVTPKFMSDLFEGDHLELAKLTSPNGDNGIKFNEKHVAPRVLSRVFSEDYKRVKRRRRIFDPRGQTIHQWNKIFLVACLI
SQ  SLFVDPLFFYLPIVQDEVCIDIGIAVEVFLIIIRSIADVFYVIHIFMRFHTAYVAPSSRVFGRGELVIDSSKIASRYLHK
SQ  GFFLDFIAALPLPQVLIWIVIPNLGGSTIANTKNVLRFIIIIQYLPRLFLIFPLSSQIVKATGVVTETAWAGAAYNLMLY
SQ  MLASHVLGACWYLLSIERQEACWKSVCKLEESSCQFDFFDCNMVKDSLRVSWFVTSNVTNLCSPNSLFYQFGIYGDAVTS
SQ  KVTTSAFFNKYFFCLWWGLRNLSSLGQGLLTSTFVGEIMFAIVIATLGLVLFALLIGNMQTYLQSTTVRLEEWRVKRTDT
SQ  EQWMHHRQLPQELRQSVRKYDQYKWIATRGVDEESLLRGLPLDLRRDIKRHLCLELVRRVPLFDAMDERMLDAICERLKP
SQ  ALCTENTYLVREGDPVNEMLFIIRGNLDSYTTDGGRTGFFNSCRIGPGDFCGEELLTWALDPRPTMVIPSSTRTVKAISE
SQ  VEAFALIAEDLKFVASQFRRLHSKQLRNKLRFHSHQWRTWAACFIQVAWRRTIQEKKGSC
//
ID  A0A072VMJ3;
PN  Protein CNGC15c;
GN  CNGC15C;
OS  3880;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: A0A072VMJ3;
DR  Pfam: PF00520;
DR  PROSITE: PS50042;
DR  PROSITE: PS50096;
DE  Function: Cyclic nucleotide-gated channel involved in the establishment of both rhizobial and mycorrhizal associations (PubMed:27230377). Required for full activation of nuclear-localized Ca(2+) oscillations by Nod and Myc factors (PubMed:27230377). Simultaneous activation of the K(+)-permeable channel DMI1 and the Ca(2+) channel CNGC15 can give rise to sustained Ca(2+) oscillations (PubMed:27230377). May function during fertilization in both female and male gametophytic Ca(2+) signaling (PubMed:27230377). {ECO:0000269|PubMed:27230377}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0044325;
GO  GO:0005249;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGFDNPRSERFEDDPEISKIPTTSGVKVKYHIDGTQIPEQSSKKSRKNETRNKFLKTRVLSRVFSEDYERVKKRVLVLDP
SQ  RGQLIHRWNKIFLVACLVSLFVDPLFFYLPVVREEVCIDIGKTLEVILTVVRSFGDLFYIVQICMKFRTAYVAPSSKVFG
SQ  RGELVLTYSKIALRYFSKGFWLDFIAALPLPQVLIWIIIPTLRGSTMANTKNVLRFFIIFQYIPRLYLIFPLSSQIVKAT
SQ  GVVTETAWAGAAYNLMLYMLASHILGACWYLLSIERQEACWKSVCNMEKSNCQYGFFNCHSIKDAPRVAWFIASNVTNLC
SQ  SPNAGFYPFGIYADAMTSKVTSSPFFNKYFYCLWWGLRNLSSLGQGLLTSTFIGEIMVAIVVATLGLVLFALLIGNMQTY
SQ  LQSITVRLEEWRVKRTDTEQWMHHRQLPPELRESIRKYNQYKWVATRGVEEEDLLKGLPLDLRREIKRHLCLELVRGVPL
SQ  FDQMDERMLDAICERLKPALCTEGTYLVREGDPVNEMLFIIRGHLDSYTTNGGRDGFFNSCRIGPGDFCGEELLTWALDP
SQ  RPSVILPSSTRTVKAFSEVEAFALIAEDLKFVASQFRRLHSKQLRHKFRFYSHQWRTWAACFIQAAWRRHKKRKEAAELR
SQ  AKENLVAASEAENEIAKKYGKGFVVYGTRVARSTRKGVNMHSGTNSGVVSSLQKPTEPDFSDE
//
ID  Q1RMV9;
PN  CTD nuclear envelope phosphatase 1;
GN  CTDNEP1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q1RMV9;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0017018;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0060070;
GO  GO:0007276;
GO  GO:0007498;
GO  GO:0006998;
GO  GO:0090263;
GO  GO:0010867;
GO  GO:0006470;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPVSRNRLSQVKRKILVLDLDETLIHSHHDGV
SQ  LRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQH
SQ  CTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQ
SQ  HRLW
//
ID  Q20432;
PN  CTD nuclear envelope phosphatase 1 homolog;
GN  cnep;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:32271860}.
DR  UNIPROT: Q20432;
DR  UNIPROT: H1ZUW4;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Serine/threonine protein phosphatase that may dephosphorylate and activate lipin-like phosphatases (PubMed:22134922). Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels (PubMed:22134922). May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics (PubMed:22134922). Contributes to closure of nuclear envelope (NE) holes and prevents excess nuclear membranes after meiosis and mitosis, possibly through spatial regulation of lipin (PubMed:32271860). May limit the production of endoplasmic reticulum (ER) sheets proximal to the NE to prevent the ER membranes that feed into NE openings from invading the nuclear interior and thereby restrict nuclear transport to nuclear pore complexes (NPCs) (PubMed:32271860). May also indirectly regulate the production of lipid droplets and triacylglycerol (PubMed:22134922). {ECO:0000269|PubMed:22134922, ECO:0000269|PubMed:32271860}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0017018;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0006998;
GO  GO:0031468;
GO  GO:0010867;
GO  GO:0006470;
GO  GO:0051783;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTTIAQSVFCFLAGFFNFFLLYFRKTSRAYCKYQVVKYHSNIPMSPLTTHRLLTVKRKILVLDLDETLIHSHHDGVLRQT
SQ  VKPGTPSDFTIRVVIDRHPVKFSVHERPHVDYFLSVVSQWYELVVFTASMEVYGTSVADRLDRGRGILKRRYFRQHCTME
SQ  VGGYTKDLSAIHPDLSSICILDNSPGAYRKFPHNAIPIPSWFSDPNDTCLLNLLPFLDALRFTSDVRSVLSRNMQALPET
SQ  QSVQYY
//
ID  O95476;
PN  CTD nuclear envelope phosphatase 1;
GN  CTDNEP1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.
DR  UNIPROT: O95476;
DR  UNIPROT: D3DTN7;
DR  UNIPROT: Q96GQ9;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DR  OMIM: 610684;
DR  DisGeNET: 23399;
DE  Function: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling. {ECO:0000269|PubMed:17420445, ECO:0000269|PubMed:22134922}.
DE  Reference Proteome: Yes;
DE  Interaction: O00165; IntAct: EBI-27113178; Score: 0.35
DE  Interaction: O15173; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: O94901; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q8N9A8; IntAct: EBI-5323532; Score: 0.46
DE  Interaction: Q91ZP3; IntAct: EBI-5323701; Score: 0.27
DE  Interaction: Q9WH76; IntAct: EBI-10823914; Score: 0.58
DE  Interaction: P08563; IntAct: EBI-11478420; Score: 0.40
DE  Interaction: Q9UHD9; IntAct: EBI-24288048; Score: 0.56
DE  Interaction: P81408; IntAct: EBI-21535449; Score: 0.35
DE  Interaction: O95897; IntAct: EBI-21570405; Score: 0.35
DE  Interaction: Q6UX71; IntAct: EBI-21588922; Score: 0.35
DE  Interaction: P58658; IntAct: EBI-21588759; Score: 0.35
DE  Interaction: Q9Y5M8; IntAct: EBI-21633655; Score: 0.35
DE  Interaction: O00624; IntAct: EBI-21654627; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-21694943; Score: 0.35
DE  Interaction: Q8WV48; IntAct: EBI-21710200; Score: 0.35
DE  Interaction: O60602; IntAct: EBI-21773313; Score: 0.35
DE  Interaction: P01911; IntAct: EBI-21815688; Score: 0.35
DE  Interaction: A2ICZ0; IntAct: EBI-25685386; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
DE  Interaction: Q9BUF5; IntAct: EBI-27113178; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-27113178; Score: 0.35
DE  Interaction: Q96A33; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q8N766; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P18031; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P51648; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q9BTX1; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q8NEN9; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q96CP6; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q9NRG9; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q9HBM0; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q9NXE4; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q9P0I2; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q15904; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q8WXH0; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q9NX40; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q86Y07; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P28288; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: O60858; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q9HC62; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q9Y2U8; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q9UH99; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q96RL7; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q14573; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P16435; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q14571; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q14643; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q5T8D3; IntAct: EBI-27115722; Score: 0.27
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0017018;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0060070;
GO  GO:0007276;
GO  GO:0007498;
GO  GO:0007077;
GO  GO:0006998;
GO  GO:0090263;
GO  GO:0010867;
GO  GO:0006470;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPVSRNRLAQVKRKILVLDLDETLIHSHHDGV
SQ  LRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQH
SQ  CTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQ
SQ  HRLW
//
ID  Q3TP92;
PN  CTD nuclear envelope phosphatase 1;
GN  Ctdnep1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q3TP92;
DR  UNIPROT: Q5NCW4;
DR  UNIPROT: Q8VEL4;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0017018;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0060070;
GO  GO:0007276;
GO  GO:0007498;
GO  GO:0006998;
GO  GO:0090263;
GO  GO:0010867;
GO  GO:0006470;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPLSRNRLAQVKRKILVLDLDETLIHSHHDGV
SQ  LRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQH
SQ  CTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQ
SQ  HRLW
//
ID  Q3B7T6;
PN  CTD nuclear envelope phosphatase 1;
GN  Ctdnep1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q3B7T6;
DR  UNIPROT: Q5M952;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0017018;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0060070;
GO  GO:0007276;
GO  GO:0007498;
GO  GO:0006998;
GO  GO:0090263;
GO  GO:0010867;
GO  GO:0006470;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPLSRNRLAQVKRKILVLDLDETLIHSHHDGV
SQ  LRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQH
SQ  CTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQ
SQ  HRLW
//
ID  Q8JIL9;
PN  CTD nuclear envelope phosphatase 1;
GN  ctdnep1;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17141153}.
DR  UNIPROT: Q8JIL9;
DR  UNIPROT: Q640I6;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Serine/threonine protein phosphatase that may dephosphorylate and activate lipins. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol (By similarity). Induces neuronal differentiation by antagonizing BMP signaling. Acts both by dephosphorylating BMPR1A and by promoting BMPR2 proteasomal degradation. {ECO:0000250, ECO:0000269|PubMed:12083771, ECO:0000269|PubMed:17141153}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0017018;
GO  GO:0004722;
GO  GO:0030154;
GO  GO:0007399;
GO  GO:0006998;
GO  GO:0010867;
GO  GO:0006470;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMRTPGLLGLRGFVAFAAKLWSFVLYLLRRQFRTIIQYQTVRYDVLPLSPASRNRLSQVKRKVLVLDLDETLIHSHHDGV
SQ  LRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNNKGVLRRRFYRQH
SQ  CTLELGSYIKDLSVVHSDLSSVVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQ
SQ  HRLW
//
ID  Q28HW9;
PN  CTD nuclear envelope phosphatase 1;
GN  ctdnep1;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q28HW9;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Serine/threonine protein phosphatase that may dephosphorylate and activate lipins. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. Induces neuronal differentiation by antagonizing BMP signaling. Acts both by dephosphorylating BMPR1A and by promoting BMPR2 proteasomal degradation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0017018;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0030154;
GO  GO:0007399;
GO  GO:0006998;
GO  GO:0010867;
GO  GO:0006470;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMRTPGLLGLRGFVAFAAKLWSFVLYLLRRQVRTIIQYQTVRYDVLPLSPASRNRLSQVKRKVLVLDLDETLIHSHHDGV
SQ  LRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNNRGVLRRRFYRQH
SQ  CTLELGSYIKDLSVVHSDLSSVVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQ
SQ  HRLW
//
ID  Q5U395;
PN  CTD nuclear envelope phosphatase 1A;
GN  ctdnep1a;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q5U395;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Serine/threonine protein phosphatase that may dephosphorylate and activate lipins. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0017018;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0006998;
GO  GO:0010867;
GO  GO:0006470;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLKTRQCLLGIRTFLGVTSRIWSFFLYILRKHLRTIIQYQTVRYDILPLSPISRNRLNAVKRKILVLDLDETLIHSHHDG
SQ  VLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNNRGILKRRYYRQ
SQ  HCTLDLGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTSDVRSVLSRNLH
SQ  QHRLW
//
ID  Q5U3T3;
PN  CTD nuclear envelope phosphatase 1B;
GN  ctdnep1b;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q5U3T3;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Serine/threonine protein phosphatase that may dephosphorylate and activate lipins. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0017018;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0060322;
GO  GO:0006998;
GO  GO:0010867;
GO  GO:0006470;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLKTRQCLLGVRTFHGVTSRIWSFFLYILRKHIRTIIQYQTVRYDILSLSPISRNRLNNVKRKILVLDLDETLIHSHHDG
SQ  VLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNNKAILKRRYYRQ
SQ  HCTLDSGSYIKDLSVVHDDLSSVVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFPADVRSVLSRNLH
SQ  QHRLW
//
ID  Q9BV73;
PN  Centrosome-associated protein CEP250;
GN  CEP250;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9647649}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26337392, ECO:0000269|PubMed:30404835, ECO:0000269|PubMed:9647649}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:31974111}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:9647649}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q60952}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q60952}. Note=Component of the core centrosome. In interphase cells, it specifically associates with the proximal ends of both mother and daughter centrioles. Associates with the centrosome in interphase cells. In mitotic cells, it dissociates from the mitotic spindle poles. At the end of cell division, it reaccumulates at centrosomes.
DR  UNIPROT: Q9BV73;
DR  UNIPROT: E1P5Q3;
DR  UNIPROT: O14812;
DR  UNIPROT: O60588;
DR  UNIPROT: Q9H450;
DR  PDB: 6OQA;
DR  OMIM: 609689;
DR  OMIM: 618358;
DR  DisGeNET: 11190;
DE  Function: May be involved in ciliogenesis (PubMed:28005958). Probably plays an important role in centrosome cohesion during interphase. Recruits CCDC102B to the proximal ends of centrioles (PubMed:30404835). {ECO:0000269|PubMed:28005958, ECO:0000269|PubMed:30404835}.
DE  Disease: Cone-rod dystrophy and hearing loss 2 (CRDHL2) [MIM:618358]: An autosomal recessive disease defined by the association of progressive cone-rod dystrophy with sensorineural hearing loss. Cone- rod dystrophy is characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa, due to cone photoreceptors degenerating at a higher rate than rod photoreceptors. {ECO:0000269|PubMed:24780881, ECO:0000269|PubMed:29718797, ECO:0000269|PubMed:30459346, ECO:0000269|PubMed:30998843}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626135; Score: 0.35
DE  Interaction: K9N7C7; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: O08788; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: P0C6X7; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-26950012; Score: 0.56
DE  Interaction: Q7Z3B4; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: Q91B85; IntAct: EBI-11422888; Score: 0.37
DE  Interaction: Q96CV9; IntAct: EBI-25910879; Score: 0.56
DE  Interaction: Q6VMQ6; IntAct: EBI-7244323; Score: 0.37
DE  Interaction: Q15008; IntAct: EBI-1066651; Score: 0.00
DE  Interaction: Q6UVJ0; IntAct: EBI-1570162; Score: 0.27
DE  Interaction: Q04917; IntAct: EBI-1644092; Score: 0.35
DE  Interaction: O88566; IntAct: EBI-7866996; Score: 0.46
DE  Interaction: P63104; IntAct: EBI-8063698; Score: 0.35
DE  Interaction: Q8ZGW9; IntAct: EBI-2872616; Score: 0.00
DE  Interaction: Q9H0K1; IntAct: EBI-2909672; Score: 0.62
DE  Interaction: Q9HAU0; IntAct: EBI-3447325; Score: 0.00
DE  Interaction: Q9WMX2; IntAct: EBI-9082134; Score: 0.37
DE  Interaction: P35579; IntAct: EBI-11144042; Score: 0.35
DE  Interaction: Q9E7P0; IntAct: EBI-11422880; Score: 0.37
DE  Interaction: Q96KS9; IntAct: EBI-21503766; Score: 0.35
DE  Interaction: Q5SW79; IntAct: EBI-21644990; Score: 0.35
DE  Interaction: Q9NV56; IntAct: EBI-21683633; Score: 0.35
DE  Interaction: Q9H7C4; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q96ES7; IntAct: EBI-21781962; Score: 0.35
DE  Interaction: Q96GS4; IntAct: EBI-21795617; Score: 0.35
DE  Interaction: Q15311; IntAct: EBI-21818654; Score: 0.35
DE  Interaction: Q96JB2; IntAct: EBI-21879136; Score: 0.35
DE  Interaction: Q9NQ48; IntAct: EBI-21889038; Score: 0.35
DE  Interaction: O94986; IntAct: EBI-16171575; Score: 0.35
DE  Interaction: P06576; IntAct: EBI-20904592; Score: 0.40
DE  Interaction: P27824; IntAct: EBI-20908048; Score: 0.40
DE  Interaction: Q9UII2; IntAct: EBI-20933940; Score: 0.40
DE  Interaction: P0DTC6; IntAct: EBI-26495724; Score: 0.35
DE  Interaction: Q13547; IntAct: EBI-26367383; Score: 0.35
DE  Interaction: P53355; IntAct: EBI-28938354; Score: 0.35
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005815;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0032991;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0010457;
GO  GO:0060271;
GO  GO:0050908;
GO  GO:0000278;
GO  GO:1905515;
GO  GO:1904781;
GO  GO:0008104;
GO  GO:0071539;
GO  GO:0033365;
GO  GO:0030997;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METRSPGLNNMKPQSLQLVLEEQVLALQQQMAENQAASWRKLKNSQEAQQRQATLVRKLQAKVLQYRSWCQELEKRLEAT
SQ  GGPIPQRWENVEEPNLDELLVRLEEEQQRCESLAEVNTQLRLHMEKADVVNKALREDVEKLTVDWSRARDELMRKESQWQ
SQ  MEQEFFKGYLKGEHGRLLSLWREVVTFRRHFLEMKSATDRDLMELKAEHVRLSGSLLTCCLRLTVGAQSREPNGSGRMDG
SQ  REPAQLLLLLAKTQELEKEAHERSQELIQLKSQGDLEKAELQDRVTELSALLTQSQKQNEDYEKMIKALRETVEILETNH
SQ  TELMEHEASLSRNAQEEKLSLQQVIKDITQVMVEEGDNIAQGSGHENSLELDSSIFSQFDYQDADKALTLVRSVLTRRRQ
SQ  AVQDLRQQLAGCQEAVNLLQQQHDQWEEEGKALRQRLQKLTGERDTLAGQTVDLQGEVDSLSKERELLQKAREELRQQLE
SQ  VLEQEAWRLRRVNVELQLQGDSAQGQKEEQQEELHLAVRERERLQEMLMGLEAKQSESLSELITLREALESSHLEGELLR
SQ  QEQTEVTAALARAEQSIAELSSSENTLKTEVADLRAAAVKLSALNEALALDKVGLNQQLLQLEEENQSVCSRMEAAEQAR
SQ  NALQVDLAEAEKRREALWEKNTHLEAQLQKAEEAGAELQADLRDIQEEKEEIQKKLSESRHQQEAATTQLEQLHQEAKRQ
SQ  EEVLARAVQEKEALVREKAALEVRLQAVERDRQDLAEQLQGLSSAKELLESSLFEAQQQNSVIEVTKGQLEVQIQTVTQA
SQ  KEVIQGEVRCLKLELDTERSQAEQERDAAARQLAQAEQEGKTALEQQKAAHEKEVNQLREKWEKERSWHQQELAKALESL
SQ  EREKMELEMRLKEQQTEMEAIQAQREEERTQAESALCQMQLETEKERVSLLETLLQTQKELADASQQLERLRQDMKVQKL
SQ  KEQETTGILQTQLQEAQRELKEAARQHRDDLAALQEESSSLLQDKMDLQKQVEDLKSQLVAQDDSQRLVEQEVQEKLRET
SQ  QEYNRIQKELEREKASLTLSLMEKEQRLLVLQEADSIRQQELSALRQDMQEAQGEQKELSAQMELLRQEVKEKEADFLAQ
SQ  EAQLLEELEASHITEQQLRASLWAQEAKAAQLQLRLRSTESQLEALAAEQQPGNQAQAQAQLASLYSALQQALGSVCESR
SQ  PELSGGGDSAPSVWGLEPDQNGARSLFKRGPLLTALSAEAVASALHKLHQDLWKTQQTRDVLRDQVQKLEERLTDTEAEK
SQ  SQVHTELQDLQRQLSQNQEEKSKWEGKQNSLESELMELHETMASLQSRLRRAELQRMEAQGERELLQAAKENLTAQVEHL
SQ  QAAVVEARAQASAAGILEEDLRTARSALKLKNEEVESERERAQALQEQGELKVAQGKALQENLALLTQTLAEREEEVETL
SQ  RGQIQELEKQREMQKAALELLSLDLKKRNQEVDLQQEQIQELEKCRSVLEHLPMAVQEREQKLTVQREQIRELEKDRETQ
SQ  RNVLEHQLLELEKKDQMIESQRGQVQDLKKQLVTLECLALELEENHHKMECQQKLIKELEGQRETQRVALTHLTLDLEER
SQ  SQELQAQSSQIHDLESHSTVLARELQERDQEVKSQREQIEELQRQKEHLTQDLERRDQELMLQKERIQVLEDQRTRQTKI
SQ  LEEDLEQIKLSLRERGRELTTQRQLMQERAEEGKGPSKAQRGSLEHMKLILRDKEKEVECQQEHIHELQELKDQLEQQLQ
SQ  GLHRKVGETSLLLSQREQEIVVLQQQLQEAREQGELKEQSLQSQLDEAQRALAQRDQELEALQQEQQQAQGQEERVKEKA
SQ  DALQGALEQAHMTLKERHGELQDHKEQARRLEEELAVEGRRVQALEEVLGDLRAESREQEKALLALQQQCAEQAQEHEVE
SQ  TRALQDSWLQAQAVLKERDQELEALRAESQSSRHQEEAARARAEALQEALGKAHAALQGKEQHLLEQAELSRSLEASTAT
SQ  LQASLDACQAHSRQLEEALRIQEGEIQDQDLRYQEDVQQLQQALAQRDEELRHQQEREQLLEKSLAQRVQENMIQEKQNL
SQ  GQEREEEEIRGLHQSVRELQLTLAQKEQEILELRETQQRNNLEALPHSHKTSPMEEQSLKLDSLEPRLQRELERLQAALR
SQ  QTEAREIEWREKAQDLALSLAQTKASVSSLQEVAMFLQASVLERDSEQQRLQDELELTRRALEKERLHSPGATSTAELGS
SQ  RGEQGVQLGEVSGVEAEPSPDGMEKQSWRQRLEHLQQAVARLEIDRSRLQRHNVQLRSTLEQVERERRKLKREAMRAAQA
SQ  GSLEISKATASSPTQQDGRGQKNSDAKCVAELQKEVVLLQAQLTLERKQKQDYITRSAQTSRELAGLHHSLSHSLLAVAQ
SQ  APEATVLEAETRRLDESLTQSLTSPGPVLLHPSPSTTQAASR
//
ID  Q60952;
PN  Centrosome-associated protein CEP250;
GN  Cep250;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16339073}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:16339073}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:16339073, ECO:0000269|PubMed:30998843}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:28005958}. Photoreceptor inner segment {ECO:0000269|PubMed:30998843}. Note=Component of the core centrosome where it is found at the proximal ends of centrioles.
DR  UNIPROT: Q60952;
DR  UNIPROT: E9QMB2;
DR  UNIPROT: Q2I8G3;
DR  UNIPROT: Q3UTR4;
DR  UNIPROT: Q6PFF6;
DR  UNIPROT: Q8BLC6;
DE  Function: May be involved in ciliogenesis. Probably plays an important role in centrosome cohesion during interphase. {ECO:0000250|UniProtKB:Q9BV73}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8BH43; IntAct: EBI-651063; Score: 0.37
DE  Interaction: Q9P2X0; IntAct: EBI-11075169; Score: 0.35
DE  Interaction: Q8NFH4; IntAct: EBI-11075169; Score: 0.35
DE  Interaction: Q5JTD0; IntAct: EBI-11075169; Score: 0.35
DE  Interaction: P53618; IntAct: EBI-11075169; Score: 0.35
DE  Interaction: P13861; IntAct: EBI-11075169; Score: 0.35
DE  Interaction: Q8IYS2; IntAct: EBI-11075169; Score: 0.35
DE  Interaction: Q8BHC1; IntAct: EBI-11568621; Score: 0.35
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0032991;
GO  GO:0031616;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0010457;
GO  GO:0060271;
GO  GO:0050908;
GO  GO:0000278;
GO  GO:1905515;
GO  GO:1904781;
GO  GO:0008104;
GO  GO:0033365;
GO  GO:0030997;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METGSPGLNMKPQSLQLVLEGQVLALQQQMAENQAASWRKLKNSQEAQKRQATLVRKLQAKVLQYRSWCQDLEKRLEATG
SQ  GLIPQRWESVEEPNLEQLLIRLEEEQQRCESLVEVNTELRLHMEKADVVNKALQEDVEKLTVDWSRARDELVRKESQWRM
SQ  EQEFFKGYLRGEHGRLLNLWREVVTFRRHFLKMKSATDRDLTELKAEHARLSGSLLTCCLRLTLRAQSRESSGSGRTEES
SQ  EPARLLLLVAKTQALEKEAHEKSQELMQLKSHGDLEKAELQDRVTELSALLTQSQKQNEDYEKMVKALRETMEILETNHA
SQ  ELMEHEASLSRNAQEEKLSLQQVIKAITQALASVEEEDTVTQSSGHEDSLQSDCNGLSQFDPQDPDRALTLVQSVLTRRQ
SQ  QAVQDLRQQLSGCQEAMSFLQQQHDQWEEEGRALREKLQKLTGERDALAGQTVGLQGEVDSLSRERELLQKARGELQQQL
SQ  EVLEQEAWRLRRMNMELQLQGDSAQGEKLEQQEELHLAVRERERLQETLVGLEAKQSESLSELLTLREALESSRLEGELL
SQ  KQERVEVAAALARAEQSIVELSGSENSLKAEVADLRAAAVKLGALNEALALDKVELNQQLLQLEQENQSLCSRVEAAEQL
SQ  RSALQVDLAEAERRREALWEKKTQLETQLQKAEEAGAELQAELRGTREEKEELKDKLSEAHHQQETATAHLEQLHQDAER
SQ  QEETLARAVQEKEALVRERAALEVRLQAVERDRQDLTEHVLGLRSAKEQLESNLFEAQQQNSVIQVTKGQLEVQIQTIIQ
SQ  AKEVIQGEVKCLKLELDAERTRAEQEWDAVARQLAQAEQEGQASLERQKVAHEEEVNRLQEKWEKERSWLQQELDKTLET
SQ  LERERAELETKLREQQTEMEAIRAQREEERSQADSALYQMQLETEKERVSLLETLLRTQKELADASQQLERLRQDMKIQK
SQ  LKEQETTGMLQAQLQETQQELKEAAQQHRDDLAAFQKDKLDLQKQVEDLMSQLVAHDDSQRLVKEEIEEKVKVAQECSRI
SQ  QKELEKENASLALSLVEKEKRLLILQEADSVRQQELSSLRQDIQEAQEGQRELGVQVELLRQEVKEKEADFVAREAQLLE
SQ  ELEASRVAEQQLRASLWAQEAKATQLQLQLRSTESQLEALVAEQQPENQAQAQLASLCSVLQQALGSACESRPELRGGGD
SQ  SAPTLWGPDPDQNGASRLFKRWSLPTALSPEAVALALQKLHQDVWKARQARDDLRDQVQKLVQRLTDTEAQKSQVHSELQ
SQ  DLQRQLSQSQEEKSKWEGRQNSLESELRDLHETAASLQSRLRQAELQKMEAQNDRELLQASKEKLSAQVEHLQACVAEAQ
SQ  AQADAAAVLEEDLRTARSALKLKNEELESERERAQALQEQGELKVAQGKALQENLALLAQTLSNREREVETLQAEVQELE
SQ  KQREMQKAALELLSLDLKKRSREVDLQQEQIQELEQCRSVLEHLPMAVQEREQKLSVQRDQIRELENDREAQRSVLEHQL
SQ  LDLEQKAQVIESQRGQIQDLKKQLGTLECLALELEESHHKVESQQKMITELEGQREMQRVALTHLTLDLEERSQELQAQS
SQ  SQLHELENHSTHLAKELQERDQEVTSQRQQIDELQKQQEQLAQALERKGQELVLQKERIQVLEDQRTLQTKILEEDLEQI
SQ  KHSLRERSQELASQWQLVHERADDGKSPSKGQRGSLEHLKLILRDKEKEVECQQERIQELQGHMGQLEQQLQGLHRKVGE
SQ  TSLLLTHREQETATLQQHLQEAKEQGELREQVLQGQLEEAQRDLAQRDHELETLRQEKQQTQDQEESMKLKTSALQAALE
SQ  QAHATLKERQGELEEHREQVRRLQEELEVEGRQVRALEEVLGDLRAESREHEKAVLALQQRCAEQAQEHEAEARTLQDSW
SQ  LQAQATLTEQEQELAALRAENQYSRRQEEAAVSQAEALQEALSKAQAALQEKEQSLLEQAELSHTLEASTAALQATLDTC
SQ  QASARQLEEALRIREGEIQAQALQHHEVTQHLQQELCQKKEELRQLLEKAGARRSQENGIQEKQSLEQERQEETRRLLES
SQ  LKELQLTVAQREEEILMLREASSPRHRALPAEKPALQPLPAQQELERLQTALRQTEAREIEWREKAQDLALSLAQSKASI
SQ  SSLQEITMFLQASVLERESEQQRLQEELVLSRQALEEQQSGGPHSTSRADQGPKVGQGSQSGEVETEPSPGVEEKERLTQ
SQ  RLERLQQAVAELEVDRSKLQCHNAQLRTALEQVERERRKLKRDSVRASRAGSLEARETMTSSPTQQDGRGSQRGSSDSVL
SQ  VVELQREVALLRAQLALERKQRQDYIARSVQTSRELAGLHHSLSHSLLTVAQAPEATVLEAETRKLDESLNQSLTSPGPC
SQ  LLHPSLDTTQNTHR
//
ID  Q7SXN4;
PN  Cytoplasmic polyadenylation element-binding protein 4;
GN  cpeb4;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q7TN98}. Postsynaptic density {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, axon {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q7TN98}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q7TN98}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TN98}.
DR  UNIPROT: Q7SXN4;
DR  Pfam: PF16366;
DR  Pfam: PF16367;
DR  PROSITE: PS50102;
DE  Function: Sequence-specific RNA-binding protein that binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism. {ECO:0000250|UniProtKB:Q17RY0}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005783;
GO  GO:0030426;
GO  GO:1990124;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0045202;
GO  GO:0003730;
GO  GO:0000900;
GO  GO:0043022;
GO  GO:0008135;
GO  GO:0071230;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0035235;
GO  GO:2000766;
GO  GO:0043524;
GO  GO:0002931;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQDDILESEMSKAPQLQQESQEGQDKQTLSPPGHQEPPGIISELDNALPEENQLEKGTMENANGKETLRLESPVLSGFDY
SQ  QETTGIGTLAQSSSSSSSSLTGFSSWSTAMPPNPSTLIEEVGFFNQAATTNNAPPPLLFQSFSHHTSTGFGGNFSHQIGP
SQ  LSQHHPSPHPHFQHPHNQHRRSSASPHPPPFSHRSAAFNQLPHLGNNLSKPPSPWGSYQSPSSTPSSTSWSPGGGYGGWG
SQ  SSQGREYRRGGVNPLNSISPLKKSFPNNQTQTQKYPRNNSGFNTKPWVEDTINRNESIFPFQERSRSFDGFSMHSLENSL
SQ  IDIMRAEQDSLKGHSSLFPMEDERSYGEDERSDQSLSGLGSPHSFPHQNGERIERYSRKVFVGGLPPDIDEDEITASFRR
SQ  FGHLFVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACMEEDGKLYLCVSSPTIKDKPVQIRPWNLNDSDFVMDGSQ
SQ  PLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKR
SQ  VEVKPYVLDDQLCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN
//
ID  Q17RY0;
PN  Cytoplasmic polyadenylation element-binding protein 4;
GN  CPEB4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q7TN98}. Postsynaptic density {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, axon {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q7TN98}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q7TN98}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TN98}.
DR  UNIPROT: Q17RY0;
DR  UNIPROT: B7ZLQ7;
DR  UNIPROT: Q7Z310;
DR  UNIPROT: Q8N405;
DR  UNIPROT: Q9C0J0;
DR  PDB: 2MKI;
DR  PDB: 2MKJ;
DR  PDB: 5DIF;
DR  Pfam: PF16366;
DR  Pfam: PF16367;
DR  PROSITE: PS50102;
DR  OMIM: 610607;
DR  DisGeNET: 80315;
DE  Function: Sequence-specific RNA-binding protein that binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR (PubMed:24990967). RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism (PubMed:24990967). Regulates activation of unfolded protein response (UPR) in the process of adaptation to ER stress in liver, by maintaining translation of CPE- regulated mRNAs in conditions in which global protein synthesis is inhibited (By similarity). Required for cell cycle progression, specifically for cytokinesis and chromosomal segregation (PubMed:26398195). Plays a role as an oncogene promoting tumor growth and progression by positively regulating translation of t-plasminogen activator/PLAT (PubMed:22138752). Stimulates proliferation of melanocytes (PubMed:27857118). In contrast to CPEB1 and CPEB3, does not play role in synaptic plasticity, learning and memory (By similarity). {ECO:0000250|UniProtKB:Q7TN98, ECO:0000269|PubMed:22138752, ECO:0000269|PubMed:24990967, ECO:0000269|PubMed:26398195, ECO:0000269|PubMed:27857118}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8D052; IntAct: EBI-2848200; Score: 0.00
DE  Interaction: P50616; IntAct: EBI-8596337; Score: 0.54
DE  Interaction: Q9H4B6; IntAct: EBI-8799416; Score: 0.27
DE  Interaction: Q9H6Z9; IntAct: EBI-12503146; Score: 0.35
DE  Interaction: Q61474; IntAct: EBI-11474493; Score: 0.40
DE  Interaction: Q17RY0; IntAct: EBI-11474906; Score: 0.40
DE  Interaction: Q9BZB8; IntAct: EBI-11474918; Score: 0.40
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568044; Score: 0.35
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005783;
GO  GO:0030426;
GO  GO:1990124;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0045202;
GO  GO:0046872;
GO  GO:0003730;
GO  GO:0000900;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0008135;
GO  GO:0071230;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0035235;
GO  GO:2000766;
GO  GO:0043524;
GO  GO:0002931;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPSPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKA
SQ  KSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKSEENQGDNSSENGNGKEKIRIESPVLTGFDYQEATGLGTSTQPLTS
SQ  SASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPAASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQ
SQ  HHHSQHQQQRRSPASPHPPPFTHRNAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGGSQGRDHRRG
SQ  LNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPDRPRTFDMHSLESSLIDIMRAENDT
SQ  IKGRLNYSYPGSDSSLLINARTYGRRRGQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFSHQNGERVERYSRKVFVGGLP
SQ  PDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRP
SQ  WNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAIS
SQ  ARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDR
SQ  PRHISFRWN
//
ID  Q7TN98;
PN  Cytoplasmic polyadenylation element-binding protein 4;
GN  Cpeb4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:27381259}. Cell projection, dendrite {ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:24386439}. Cell projection, dendritic spine {ECO:0000269|PubMed:24386439}. Postsynaptic density {ECO:0000269|PubMed:17024188}. Cell projection, axon {ECO:0000269|PubMed:27381259}. Cell projection, growth cone {ECO:0000269|PubMed:27381259}. Endoplasmic reticulum {ECO:0000269|PubMed:28092655}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:28092655}.
DR  UNIPROT: Q7TN98;
DR  UNIPROT: A6H6G0;
DR  UNIPROT: Q69ZD7;
DR  Pfam: PF16366;
DR  Pfam: PF16367;
DR  PROSITE: PS50102;
DE  Function: Sequence-specific RNA-binding protein that binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR (PubMed:17024188). RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism (By similarity). Regulates activation of unfolded protein response (UPR) in the process of adaptation to ER stress in liver, by maintaining translation of CPE- regulated mRNAs in conditions in which global protein synthesis is inhibited (PubMed:28092655). Required for cell cycle progression, specifically for cytokinesis and chromosomal segregation (By similarity). Plays a role as an oncogene promoting tumor growth and progression by positively regulating translation of t-plasminogen activator/PLAT (PubMed:22138752). Stimulates proliferation of melanocytes (By similarity). In contrast to CPEB1 and CPEB3, does not play role in synaptic plasticity, learning and memory (PubMed:24386439). {ECO:0000250|UniProtKB:Q17RY0, ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:22138752, ECO:0000269|PubMed:24386439, ECO:0000269|PubMed:28092655}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005783;
GO  GO:0030426;
GO  GO:1990124;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0045202;
GO  GO:0046872;
GO  GO:0003730;
GO  GO:0000900;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0008135;
GO  GO:0071230;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0035235;
GO  GO:2000766;
GO  GO:0043524;
GO  GO:0002931;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPNPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKA
SQ  KSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKAEENPGDSSSENSNGKEKLRIESPVLTGFDYQEATGLGTSTQPLTS
SQ  SASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPGASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQ
SQ  HHHSQHQQQRRSPASPHPPPFTHRSAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGASQGRDHRRG
SQ  LNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPERPRTFDMHSLESSLIDIMRAENDS
SQ  IKGRLNYSYPGSDSSLLINARTYGRRRGQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFTHQNGERVERYSRKVFVGGLP
SQ  PDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRP
SQ  WNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAIS
SQ  ARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDR
SQ  PRHISFRWN
//
ID  Q9LV85;
PN  Protein CPR-5;
GN  CPR5;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:21875893, ECO:0000269|PubMed:25455564}.
DR  UNIPROT: Q9LV85;
DR  UNIPROT: Q8W3U8;
DE  Function: May play a role in transcriptional processes (PubMed:21875893). Regulates negatively the senescence and chlorotic lesions induced by biotic (e.g. pathogens) and abiotic (e.g. sugars, darkness) agents, probably by controlling programmed cell death (pcd) (PubMed:11846876,PubMed:9338960, Ref.6, PubMed:11728314). Negative regulator of plant programmed cell death (PCD) and effector-triggered immunity (ETI) (PubMed:25455564). Promotes cell division and endoreduplication (e.g. in trichomes) (PubMed:11728314). {ECO:0000269|PubMed:11728314, ECO:0000269|PubMed:11846876, ECO:0000269|PubMed:25455564, ECO:0000269|PubMed:9338960, ECO:0000269|Ref.6, ECO:0000305|PubMed:21875893}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0007568;
GO  GO:0006952;
GO  GO:0010150;
GO  GO:0048573;
GO  GO:0009723;
GO  GO:0010182;
GO  GO:0009627;
GO  GO:0010090;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEALLLPPSPEPQNQITNPANSKPNHQSGDVHKDETMMMKKKKDTNPSNLEKRKLKGKKKEIMDNDEASSSYCSTSSTSN
SQ  SNSTKRVTRVVHRLRNPMRLGMARRSVGERQAEKLAKPLGFSLAAFANMVIARKNAAGQNVYVDDLVEIFATLVEESLAN
SQ  VYGNKLGSFATNFEQTFSSTLKILKLTNECANPHQSNNNDGGSCNLDRSTIDGCSDTELFERETSSATSAYEVMQGSATA
SQ  TSLMNELALFEETLQLSCVPPRSSAMALTTDERFLKEQTRANDLKTVEIGLQIRELRCKETALGLKFESNNLGKAALELD
SQ  VSKAAFRAEKFKTELEDTRKEEMVTRIMDWLLVSVFSMLASMVLGVYNFSIKRIEDATSVCDQSEEKSSSWWVPKQVSSI
SQ  NSGFNTFICRVRVWVQIFFGVLMIIVFTYFLNKRSSGTKQTMPISFIVLFLGIFCGVSGKLCVDTLGGDGKLWLIVWEVF
SQ  CLLQFVANVFTLALYGLMFGPINVTQETRSNRCNSMFPYWARRSVVYVVILFVLPVINGLLPFATFGEWRDFAMYHLHGG
SQ  SDYA
//
ID  Q0VCQ0;
PN  Ceramide-1-phosphate transfer protein;
GN  CPTP;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5TA50}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Cell membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5TA50}. Endosome membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}.
DR  UNIPROT: Q0VCQ0;
DR  Pfam: PF08718;
DE  Function: Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1- phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles. Regulates autophagy, inflammasome mediated IL1B and IL18 processing, and pyroptosis, but not apoptosis. {ECO:0000250|UniProtKB:Q5TA50}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:1902387;
GO  GO:1902388;
GO  GO:0005543;
GO  GO:1902389;
GO  GO:0035627;
GO  GO:0120009;
GO  GO:0010507;
GO  GO:0032691;
GO  GO:1900226;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5TA50};
SQ  MDDLESEFNLKVVLVSFKQCLNEKEEVLLEYYLAGWRGLVRFLNSLGTIFSFISKDVVTKLQIMDQLRSGPQQEHYSSLQ
SQ  AMVAYEVGNQLVDLERRSRHPDSGCRTVLRLHRALRWLQLFLEGVRTSPEDARTSVLCTDSYNASLATYHPWIIRRAVTV
SQ  AFCALPTRKVFLESMNVGSSEQAVEMLNEALPFIERVYNISQKLYAEHALLDLP
//
ID  Q6DBQ8;
PN  Ceramide-1-phosphate transfer protein;
GN  cptp;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5TA50}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Cell membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5TA50}. Endosome membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}.
DR  UNIPROT: Q6DBQ8;
DR  Pfam: PF08718;
DE  Function: Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1- phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles. Regulates autophagy and pyroptosis, but not apoptosis. {ECO:0000250|UniProtKB:Q5TA50}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:1902387;
GO  GO:1902388;
GO  GO:0005543;
GO  GO:1902389;
GO  GO:0035627;
GO  GO:0120009;
GO  GO:0010507;
GO  GO:0032691;
GO  GO:1900226;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5TA50};
SQ  MADAFSLQRVLETFRSSLSENKEVYIKYYIAGWQELVSFMNSLGNVFSFISKDVVSKIQILENFLSGENGSNYVTIQSMV
SQ  KYELENDLVDLTKRGSHPESGCRTLLRLHRALRWLELFLERLRTSTEDSKTSVMCSDAYNESLANHHPWLIRKAVGVAFC
SQ  ALPGRETFFDVMNAGDHTQVVALLGESLPLIAEVYQITEDLYAKNNLLELP
//
ID  Q5TA50;
PN  Ceramide-1-phosphate transfer protein;
GN  CPTP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:23863933}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23863933}; Peripheral membrane protein {ECO:0000269|PubMed:23863933}. Cell membrane {ECO:0000269|PubMed:23863933}; Peripheral membrane protein {ECO:0000269|PubMed:23863933}; Cytoplasmic side {ECO:0000269|PubMed:23863933}. Endosome membrane {ECO:0000269|PubMed:23863933}; Peripheral membrane protein {ECO:0000269|PubMed:23863933}. Nucleus outer membrane {ECO:0000269|PubMed:23863933}; Peripheral membrane protein {ECO:0000269|PubMed:23863933}.
DR  UNIPROT: Q5TA50;
DR  UNIPROT: Q4G0E6;
DR  UNIPROT: Q7L5A4;
DR  PDB: 4K80;
DR  PDB: 4K84;
DR  PDB: 4K85;
DR  PDB: 4K8N;
DR  PDB: 4KBS;
DR  PDB: 4KF6;
DR  Pfam: PF08718;
DR  OMIM: 615467;
DR  DisGeNET: 80772;
DE  Function: Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1- phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles (PubMed:28011644). Regulates autophagy, inflammasome mediated IL1B and IL18 processing, and pyroptosis, but not apoptosis (PubMed:29164996). {ECO:0000269|PubMed:23863933, ECO:0000269|PubMed:28011644, ECO:0000269|PubMed:29164996}.
DE  Reference Proteome: Yes;
DE  Interaction: P09564; IntAct: EBI-3913933; Score: 0.37
DE  Interaction: Q16610; IntAct: EBI-3916784; Score: 0.37
DE  Interaction: P84022; IntAct: EBI-3919182; Score: 0.37
DE  Interaction: Q15369; IntAct: EBI-3921421; Score: 0.37
DE  Interaction: Q9Y4E5; IntAct: EBI-3924080; Score: 0.37
DE  Interaction: Q9BT40; IntAct: EBI-3924709; Score: 0.37
DE  Interaction: Q86YI8; IntAct: EBI-3925466; Score: 0.37
DE  Interaction: Q5S007; IntAct: EBI-9660046; Score: 0.44
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:1902387;
GO  GO:1902388;
GO  GO:0005543;
GO  GO:1902389;
GO  GO:0035627;
GO  GO:0006687;
GO  GO:0120009;
GO  GO:0010507;
GO  GO:0032691;
GO  GO:1900226;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:23863933};
SQ  MDDSETGFNLKVVLVSFKQCLDEKEEVLLDPYIASWKGLVRFLNSLGTIFSFISKDVVSKLRIMERLRGGPQSEHYRSLQ
SQ  AMVAHELSNRLVDLERRSHHPESGCRTVLRLHRALHWLQLFLEGLRTSPEDARTSALCADSYNASLAAYHPWVVRRAVTV
SQ  AFCTLPTREVFLEAMNVGPPEQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
//
ID  Q8BS40;
PN  Ceramide-1-phosphate transfer protein;
GN  Cptp;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5TA50}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Cell membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5TA50}. Endosome membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}.
DR  UNIPROT: Q8BS40;
DR  UNIPROT: A2ADA2;
DR  UNIPROT: Q99LU9;
DR  PDB: 4KBR;
DR  Pfam: PF08718;
DE  Function: Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1- phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles (By similarity). Regulates autophagy, inflammasome mediated IL1B and IL18 processing, and pyroptosis, but not apoptosis (PubMed:29164996). {ECO:0000250|UniProtKB:Q5TA50, ECO:0000269|PubMed:29164996}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:1902387;
GO  GO:1902388;
GO  GO:0005543;
GO  GO:1902389;
GO  GO:0035627;
GO  GO:0120009;
GO  GO:0010507;
GO  GO:0032691;
GO  GO:1900226;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5TA50};
SQ  MDDSEKDFNLKVVLVSFKQCLTDKGEVLLDHYIAGWKGLVRFLNSLGAVFSFISKDVVAKLQIMERLRSSPQSEHYASLQ
SQ  SMVAYEVSNKLVDMDHRSHPRHPHSGCRTVLRLHRALHWLQLFLDGLRTSSEDARTSTLCSEAYNATLANYHSWIVRQAV
SQ  TVAFCALPSRKVFLEAMNMESTEQAVEMLGEALPFIEHVYDISQKLYAEHSLLDLP
//
ID  Q5XIS2;
PN  Ceramide-1-phosphate transfer protein;
GN  Cptp;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5TA50}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Cell membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5TA50}. Endosome membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}.
DR  UNIPROT: Q5XIS2;
DR  Pfam: PF08718;
DE  Function: Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1- phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles. Regulates autophagy, inflammasome mediated IL1B and IL18 processing, and pyroptosis, but not apoptosis. {ECO:0000250|UniProtKB:Q5TA50}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:1902387;
GO  GO:1902388;
GO  GO:0005543;
GO  GO:1902389;
GO  GO:0035627;
GO  GO:0120009;
GO  GO:0010507;
GO  GO:0032691;
GO  GO:1900226;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5TA50};
SQ  MDGPERDFNLKVVLISFKKCLTDKGEVLLDHYTASWKGLVRFLNSLGAVFSFISKDVVSKLQIMEHLRSGPQSEHYISLQ
SQ  SMVAYEVSNKLVDRDSRSRPRHPNSGCRTVLRLHRALHWLQLFLEGLRTSSEDARTSTLCSEAYNATLAAYHSWIVRQAV
SQ  NVAFHALPPRKVFLEAMNMGSSEQAVEMLGEALPFIEQVYDISQKLYAEHSLLDLP
//
ID  Q5HZ92;
PN  Ceramide-1-phosphate transfer protein;
GN  cptp;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5TA50}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Cell membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5TA50}. Endosome membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}.
DR  UNIPROT: Q5HZ92;
DR  Pfam: PF08718;
DE  Function: Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1- phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles. Regulates autophagy and pyroptosis, but not apoptosis. {ECO:0000250|UniProtKB:Q5TA50}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:1902387;
GO  GO:1902388;
GO  GO:0005543;
GO  GO:1902389;
GO  GO:0010507;
GO  GO:0032691;
GO  GO:1900226;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5TA50};
SQ  MSSTEEKFSLKEVLVSFKACLIDDDKDVILEHYVNGWKGLVRFMSSLGTIFSFVSKDAVSKIQIMESYLAGPNGERYRTL
SQ  QSMVEYELSSDLVDLTKRSDHTDSGCRTLLRLHRALRWLQLFLEKLRVSNEDSKTSTLCTEAYNDSLANFHPWIVRKAAT
SQ  VSFIALPYRNTFFEIMNVGTTEEVVAMLGESMPYVTKVYDFTQEVYSQHNLLELP
//
ID  Q66JG2;
PN  Ceramide-1-phosphate transfer protein;
GN  cptp;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5TA50}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Cell membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5TA50}. Endosome membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5TA50}.
DR  UNIPROT: Q66JG2;
DR  Pfam: PF08718;
DE  Function: Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1- phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles. Regulates autophagy and pyroptosis, but not apoptosis. {ECO:0000250|UniProtKB:Q5TA50}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:1902387;
GO  GO:1902388;
GO  GO:0005543;
GO  GO:1902389;
GO  GO:0035627;
GO  GO:0120009;
GO  GO:0010507;
GO  GO:0032691;
GO  GO:1900226;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5TA50};
SQ  MSSTEEKFSLKEVLVSFKSCLVDDDQDIIVEQYLNGWKGLVRFMNSLGTIFSFVSKDAVTKIQIMENYLAGTNGERYRTL
SQ  QSMVEHELSSDLVDLTKRCNNPDSGCRTILRLHRALRWLQLFLEKLRTSNEDSKTSTLCTEAYNDSLANFHPWIIRKTAT
SQ  VAFLALPTRNTFFEVMNVGTTEEVVAMLGESMPYVTKVYDFTHEIYSQHNLLELP
//
ID  F4HRT5;
PN  Protein CROWDED NUCLEI 1;
GN  CRWN1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}; Peripheral membrane protein {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:24667841}. Nucleus lamina {ECO:0000269|PubMed:23396599}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (PubMed:24667841). Mostly localized at the nuclear periphery and, to a lesser extent, in the nucleoplasm (PubMed:17873096). Localized on the condensing chromatin during prometaphase to anaphase, but transferred from the decondensing chromatin to the reassembling nuclear envelope during early telophase. Relocalized to the nuclear periphery during late telophase (PubMed:23396599). {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}.
DR  UNIPROT: F4HRT5;
DR  UNIPROT: Q0WKV7;
DR  UNIPROT: Q8GZ88;
DR  UNIPROT: Q9FYH0;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape) (PubMed:17873096, PubMed:24308514, PubMed:23396599, PubMed:24824484). {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514, ECO:0000269|PubMed:24824484}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0006997;
GO  GO:0097298;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSTPLKVWQRWSTPTKATNPDSNGSSHGTGLDMVTPVSGRVSEIQFDDPRILPEKISELEKELFEYQHSMGLLLIEKKEW
SQ  SSQYEALQQAFEEVNECLKQERNAHLIAIADVEKREEGLRKALGIEKQCALDLEKALKELRAENAEIKFTADSKLTEANA
SQ  LVRSVEEKSLEVEAKLRAVDAKLAEVSRKSSDVERKAKEVEARESSLQRERFSYIAEREADEATLSKQREDLREWERKLQ
SQ  EGEERVAKSQMIVKQREDRANESDKIIKQKGKELEEAQKKIDAANLAVKKLEDDVSSRIKDLALREQETDVLKKSIETKA
SQ  RELQALQEKLEAREKMAVQQLVDEHQAKLDSTQREFELEMEQKRKSIDDSLKSKVAEVEKREAEWKHMEEKVAKREQALD
SQ  RKLEKHKEKENDFDLRLKGISGREKALKSEEKALETEKKKLLEDKEIILNLKALVEKVSGENQAQLSEINKEKDELRVTE
SQ  EERSEYLRLQTELKEQIEKCRSQQELLQKEAEDLKAQRESFEKEWEELDERKAKIGNELKNITDQKEKLERHIHLEEERL
SQ  KKEKQAANENMERELETLEVAKASFAETMEYERSMLSKKAESERSQLLHDIEMRKRKLESDMQTILEEKERELQAKKKLF
SQ  EEEREKELSNINYLRDVARREMMDMQNERQRIEKEKLEVDSSKNHLEEQQTEIRKDVDDLVALTKKLKEQREQFISERSR
SQ  FLSSMESNRNCSRCGELLSELVLPEIDNLEMPNMSKLANILDNEAPRQEMRDISPTAAGLGLPVTGGKVSWFRKCTSKML
SQ  KLSPIKMTEPSVTWNLADQEPQSTEQANVGGPSTTVQAATTYSFDVQKAESETGTKEVEVTNVNSDGDQSDINSKAQEVA
SQ  ADSLSNLDVDGQSRMKGKGKARTRRTRSVKDVVDDAKALYGESINLYEPNDSTENVDDSTKASTGETGRSDKAISKNGRK
SQ  RGRVGSLRTCTTEQDGNESDGKSDSVTGGAHQRKRRQKVASEQQGEVVGQRYNLRRPRRVTGEPALSKKNEDIGGVQQEE
SQ  GIHCTQATATASVGVAVSDNGVSTNVVQHEATADSEDTDAGSPKRTDESEAMSEDVNKTPLRADSDGEDDESDAEHPGKV
SQ  SIGKKLWTFLTT
//
ID  Q9SAF6;
PN  Protein CROWDED NUCLEI 2;
GN  CRWN2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:17873096}; Peripheral membrane protein {ECO:0000269|PubMed:17873096}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599}. Cytoplasm {ECO:0000269|PubMed:23396599}. Nucleus lamina {ECO:0000250|UniProtKB:F4HRT5}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (By similarity). Mostly localized in the nucleoplasm and, to a lesser extent, at the nuclear periphery (PubMed:17873096). During prometaphase to anaphase, localized diffusely in the cytoplasm. A small population is later transferred from the cytoplasm to the chromatin surface. Relocalized to the nuclear periphery during late telophase (PubMed:23396599). {ECO:0000250|UniProtKB:F4HRT5, ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599}.
DR  UNIPROT: Q9SAF6;
DR  UNIPROT: F4HP35;
DR  UNIPROT: Q0WQM6;
DR  UNIPROT: Q94AW6;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape) (PubMed:17873096, PubMed:24308514, PubMed:23396599). {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005654;
GO  GO:0006997;
GO  GO:0097298;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17873096};
SQ  MTPRSETHKIGGVTNPRNADRKGKAVAFSDDLVIPTLPPPPIGTLTGQGVSRGHTDDMDMGDWRRFREVGLLNEASMEKK
SQ  DQEALLEKISTLEKELYGYQHNMGLLLMENKELVSKHEQLNQAFQEAQEILKREQSSHLYALTTVEQREENLRKALGLEK
SQ  QCVQELEKALREIQEENSKIRLSSEAKLVEANALVASVNGRSSDVENKIYSAESKLAEATRKSSELKLRLKEVETRESVL
SQ  QQERLSFTKERESYEGTFQKQREYLNEWEKKLQGKEESITEQKRNLNQREEKVNEIEKKLKLKEKELEEWNRKVDLSMSK
SQ  SKETEEDITKRLEELTTKEKEAHTLQITLLAKENELRAFEEKLIAREGTEIQKLIDDQKEVLGSKMLEFELECEEIRKSL
SQ  DKELQRKIEELERQKVEIDHSEEKLEKRNQAMNKKFDRVNEKEMDLEAKLKTIKEREKIIQAEEKRLSLEKQQLLSDKES
SQ  LEDLQQEIEKIRAEMTKKEEMIEEECKSLEIKKEEREEYLRLQSELKSQIEKSRVHEEFLSKEVENLKQEKERFEKEWEI
SQ  LDEKQAVYNKERIRISEEKEKFERFQLLEGERLKKEESALRVQIMQELDDIRLQRESFEANMEHERSALQEKVKLEQSKV
SQ  IDDLEMMRRNLEIELQERKEQDEKDLLDRMAQFEDKRMAELSDINHQKQALNREMEEMMSKRSALQKESEEIAKHKDKLK
SQ  EQQVEMHNDISELSTLSINLKKRREVFGRERSRFLAFVQKLKDCGSCGQLVNDFVLSDLQLPSNDEVAILPPIGVLNDLP
SQ  GSSNASDSCNIKKSLDGDASGSGGSRRPSMSILQKCTSIIFSPSKRVEHGIDTGKPEQRLSSSVAVGMETKGEKPLPVDL
SQ  RLRPSSSSIPEEDEEYTDSRVQETSEGSQLSEFQSSRRGRGRPRKAKPALNPTSSVKHASLEESSKDELSGHVSVTSKKT
SQ  TGGGGRKRQHIDDTATGGKRRRQQTVAVLPQTPGQRHYNLRRKKTVDQVPADVEDNAAAGEDDADIAASAPSKDTVEETV
SQ  VETLRARRIETNADVVSAENNGDVPVANVEPTVNEDTNEDGDEEEDEAQDDDNEENQDDDDDDDGDDDGSPRPGEGSIRK
SQ  KLWTFLTT
//
ID  Q9CA42;
PN  Protein CROWDED NUCLEI 3;
GN  CRWN3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:F4HRT5}; Peripheral membrane protein {ECO:0000250|UniProtKB:F4HRT5}. Nucleus, nucleoplasm {ECO:0000269|PubMed:23396599}. Cytoplasm {ECO:0000269|PubMed:23396599}. Nucleus lamina {ECO:0000250|UniProtKB:F4HRT5}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (By similarity). Punctate or bundle-like structures are detected, especially in trichomes where bundle-shape localization pattern along the long axis of the nucleus is observed. During prometaphase to anaphase, localized diffusely in the cytoplasm. Later transferred from the cytoplasm to the chromatin surface, preferentially assembling to the distal surface of the chromatin. Relocalized to the nuclear periphery during late telophase (PubMed:23396599). {ECO:0000250|UniProtKB:F4HRT5, ECO:0000269|PubMed:23396599}.
DR  UNIPROT: Q9CA42;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape) (PubMed:24308514, PubMed:23396599). {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9SB04; IntAct: EBI-1999431; Score: 0.37
DE  Interaction: Q9ZWS7; IntAct: EBI-1999571; Score: 0.37
GO  GO:0005737;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0009506;
GO  GO:0006997;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:F4HRT5};
SQ  MFTPQRNRWPETDRKGKAIAFSDEIITPPPQRVLLREDDDWQKFKEVGLLDEASLERKDRDALIEKILKLEKELFDYQHN
SQ  MGLLLIEKKQWTSTNNELQQAYDEAMEMLKREKTSNAITLNEADKREENLRKALIDEKQFVAELENDLKYWQREHSVVKS
SQ  TSEAKLEEANALVIGMKEKALEVDRERAIAEEKFSVMNRKSSELERKLKEVETREKVHQREHLSLVTEREAHEAVFYKQR
SQ  EDLQEWEKKLTLEEDRLSEVKRSINHREERVMENERTIEKKEKILENLQQKISVAKSELTEKEESIKIKLNDISLKEKDF
SQ  EAMKAKVDIKEKELHEFEENLIEREQMEIGKLLDDQKAVLDSRRREFEMELEQMRRSLDEELEGKKAEIEQLQVEISHKE
SQ  EKLAKREAALEKKEEGVKKKEKDLDARLKTVKEKEKALKAEEKKLHMENERLLEDKECLRKLKDEIEEIGTETTKQESRI
SQ  REEHESLRITKEERVEFLRLQSELKQQIDKVKQEEELLLKEREELKQDKERFEKEWEALDKKRANITREQNEVAEENEKL
SQ  RNLQISEKHRLKREEMTSRDNLKRELDGVKMQKESFEADMEDLEMQKRNLDMEFQRQEEAGERDFNERARTYEKRSQEEL
SQ  DNINYTKKLAQREMEEMQYEKLALEREREQISVRKKLLKEQEAEMHKDITELDVLRSSLKEKRKEFICERERFLVFLEKL
SQ  KSCSSCGEITENFVLSDLRLPDVEDGDKRFGKQKLKAEEALNISPSAENSKRTSLLGKIASKLLSISPIGKTDKVTDLGI
SQ  TVKLPESSQPDDSLDRVSGEDHEPSATEQSFTDSRIQEGPEGSLQSEMKSDKPRRGRGRGRGRGKSVRGRSQATKAVSRD
SQ  SKPSDGETPRKRQREQTSRITESEQAAGDSDEGVDSITTGGRRKKRQIAVPVSQTPGQTRYQLRRHRNVGTEEDKAQASK
SQ  GATEKQERVNDDIRKVPSPKETRTPPEGENRENGKAEVLVETVTHEEIVTVETETVFKVNNTGKNPVEDPQLEVGGSGEI
SQ  REHGEEDDENISMIEEENEGEEEEETERQGNDASIGKKIWVFFTT
//
ID  Q9FLH0;
PN  Protein CROWDED NUCLEI 4;
GN  CRWN4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:23396599}; Peripheral membrane protein {ECO:0000269|PubMed:23396599}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:F4HRT5}. Nucleus lamina {ECO:0000269|PubMed:23396599}. Cytoplasm {ECO:0000269|PubMed:23396599}. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (By similarity). Localized frequently to the nuclear periphery as punctate structures of different sizes. During prometaphase to anaphase, localized diffusely in the cytoplasm. Later assembled into punctate structures in the cytoplasm and then to the chromatin surface. Relocalized in part to the nuclear periphery during late telophase, the other part is still localized on the punctate structures (PubMed:23396599). {ECO:0000250|UniProtKB:F4HRT5, ECO:0000269|PubMed:23396599}.
DR  UNIPROT: Q9FLH0;
DR  UNIPROT: F4JXK1;
DR  UNIPROT: O49539;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape) (PubMed:24308514, PubMed:23396599). Involved in the maintenance of interphase chromocenter integrity and organization (PubMed:24308514). {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514}.
DE  Reference Proteome: Yes;
GO  GO:0010369;
GO  GO:0005737;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005654;
GO  GO:0006974;
GO  GO:0006997;
GO  GO:0097298;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:23396599};
SQ  MATSSRSERFPITPSTAATNRLTITPNSRVLKSPLTEEIMWKRLKDAGFDEQSIKNRDKAALIAYIAKLESEVYDYQHNM
SQ  GLLLLEKNELSSQYEEIKASVDESDLTHMREKSAYVSALAEAKKREESLKKDVGIAKECISSLEKTLHEMRAECAETKVS
SQ  AGSTMSEAHVMIEDALKKLADAEAKMRAAEALQAEANRYHRIAERKLKEVESREDDLTRRLASFKSECETKENEMVIERQ
SQ  TLNERRKSLQQEHERLLDAQVSLNQREDHIFARSQELAELEKGLDTAKTTFEEERKAFEDKKSNLEIALALCAKREEAVS
SQ  ERESSLLKKEQELLVAEEKIASKESELIQNVLANQEVILRKRKSDVEAELECKSKSVEVEIESKRRAWELREVDIKQRED
SQ  LVGEKEHDLEVQSRALAEKEKDITEKSFNLDEKEKNLVATEEDINRKTTMLEDEKERLRKLDLELQQSLTSLEDKRKRVD
SQ  SATQKLEALKSETSELSTLEMKLKEELDDLRAQKLEMLAEADRLKVEKAKFEAEWEHIDVKREELRKEAEYITRQREAFS
SQ  MYLKDERDNIKEERDALRNQHKNDVESLNREREEFMNKMVEEHSEWLSKIQRERADFLLGIEMQKRELEYCIENKREELE
SQ  NSSRDREKAFEQEKKLEEERIQSLKEMAEKELEHVQVELKRLDAERLEIKLDRERREREWAELKDSVEELKVQREKLETQ
SQ  RHMLRAERDEIRHEIEELKKLENLKVALDDMSMAKMQLSNLERSWEKVSALKQKVVSRDDELDLQNGVSTVSNSEDGYNS
SQ  SMERQNGLTPSSATPFSWIKRCTNLIFKTSPEKSTLMHHYEEEGGVPSEKLKLESSRREEKAYTEGLSIAVERLEAGRKR
SQ  RGNTSGDETSEPSNNKKRKHDVTQKYSDEADTQSVISSPQNVPEDKHELPSSQTQTPSGMVVISETVKITRVTCETEVTN
SQ  KVTTLDCSESPSEAGRKMGEETEDGDCNQTGINASETVIHNEAATEDICT
//
ID  Q17DK5;
PN  Cryptochrome-1;
GN  cry;
OS  7159;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O77059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O77059}. Nucleus {ECO:0000250|UniProtKB:O77059}. Note=Nuclear translocation initiates after the perception of a light signal. {ECO:0000250}.
DR  UNIPROT: Q17DK5;
DR  Pfam: PF00875;
DR  Pfam: PF03441;
DR  PROSITE: PS00394;
DR  PROSITE: PS51645;
DE  Function: Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0009882;
GO  GO:0050660;
GO  GO:0045892;
GO  GO:0006139;
GO  GO:0042752;
GO  GO:0006950;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVNNILWFRHGLRLHDNPSLLEALRNDGTGSESVRLYPIFIFDGESAGTKLVGFNRMKFLLESLADLDRQLREIGGQLY
SQ  VFKGNAVNVMRRLFEELNIRKLCFEQDCEPIWKARDDAIQNLCRMMDVKCVEKVSHTLWDPQQIIRTNGGIPPLTYQMFL
SQ  HTVDIIGKPPRPVAAPSFEFVEFGSIPSILAQEVKLQQVRNLSPEDFGIYYEGNPDISHQQWMGGETKALECLGHRLKQE
SQ  EEAFLGGYFLPTQAKPEFLVPPTSMSAALRFGCLSVRMFYWCVHDLYEKVQANNQYRNPGGQHITGQLIWREYFYTMSVH
SQ  NPHYAEMEANPICLNIPWYEPKDDSLDRWKEGRTGFPMIDAAMRQLLAEGWLHHILRNITATFLTRGALWISWEAGVQHF
SQ  LKYLLDADWSVCAGNWMWVSSSAFEKLLDSSSCTSPIALARRLDPKGEYVRRYLPELKNLPTLYVHEPWKAPLDVQKECG
SQ  CIVGRDYPAPMIDLAAASRANANTMNSIRQKLMERGGSTPPHCRPSDVEEIRNFFWLPEDVVADC
//
ID  Q7PYI7;
PN  Cryptochrome-1;
GN  Cry1;
OS  7165;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O77059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O77059}. Nucleus {ECO:0000250|UniProtKB:O77059}. Note=Nuclear translocation initiates after the perception of a light signal. {ECO:0000250}.
DR  UNIPROT: Q7PYI7;
DR  UNIPROT: Q0QW08;
DR  Pfam: PF00875;
DR  Pfam: PF03441;
DR  PROSITE: PS00394;
DR  PROSITE: PS51645;
DE  Function: Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0009882;
GO  GO:0003677;
GO  GO:0071949;
GO  GO:0050660;
GO  GO:0032922;
GO  GO:0043153;
GO  GO:0045892;
GO  GO:0006139;
GO  GO:0042752;
GO  GO:0006950;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTINNILWFRHGLRLHDNPSLLEALKSDCVNQSSEAVKLFPIFIFDGESAGTRIVGYNRMKFLLESLADLDRQFRDLGGQ
SQ  LLVFRGDSVTVLRRLFEELNIKKLCYEQDCEPIWKERDDAVAKLCRTMDVRCVENVSHTLWNPIEVIQTNGDIPPLTYQM
SQ  FLHTVNIIGDPPRPVGAPNFEYVEFGRVPALLASELKLCQQMPAPDDFGIHYDGNARIAFQKWIGGETRALEALGARLKQ
SQ  EEEAFREGYYLPTQAKPEILGPATSMSAALRFGCLSVRMFYWCVHDLFAKVQSNSQFKYPGGHHITGQLIWREYFYTMSV
SQ  QNPHYGEMERNPICLNIPWYKPEDDSLTRWKEGRTGFPMIDAAMRQLLAEGWLHHILRNITATFLTRGGLWLSWEEGLQH
SQ  FLKYLLDADWSVCAGNWMWVSSSAFERLLDSSKCTCPIALARRLDPKGDYVKRYLPELANYPAQFVHEPWKASREQQIEY
SQ  GCVIGEKYPAPMVDLAIVSKRNAHTMASLREKLVDGGSTPPHCRPSDIEEIRQFFWLADDAATEA
//
ID  B0WRR9;
PN  Cryptochrome-1;
GN  cry;
OS  7176;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O77059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O77059}. Nucleus {ECO:0000250|UniProtKB:O77059}. Note=Nuclear translocation initiates after the perception of a light signal. {ECO:0000250}.
DR  UNIPROT: B0WRR9;
DR  Pfam: PF03441;
DR  PROSITE: PS00394;
DE  Function: Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0009882;
GO  GO:0050660;
GO  GO:0045892;
GO  GO:0006139;
GO  GO:0042752;
GO  GO:0006950;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTDKVRNRVQCWPALAQESSCVDFIPARQGATCGSTVVFIPCCGLTRGRRVLCQWFPCLSGGCCSQESSCVDFIPARQGA
SQ  TCGSTVVFIPCCGLTRGRRVLCQWFPCLSGGCCSQHTVNIIGEPPRPVGAPSFEFVEFGRLPSILSTELKLFQRAPVPED
SQ  FGIYYEGNADIARQRWTGGEAKALELLGRRLKQEEEAFREGYYLPTQARPDFLAPPSSMSAALRFGCLSVRMFYWCVHDL
SQ  FARVQANNQLKHPGGHHITGQLIWREYFYTMSVHNPHYAVMELNPICLNIPWYEAKDDSLDRWKEGRTGFPLIDAAMRQL
SQ  MAEGWLHHILRNITATFLTRGGLWISWEAGVQHFLKYLLDADWSVCAGNWMWVSSSAFEKLLDSSSCTSPVALARRLDPK
SQ  GEYVKRYLPELEKFPALYVHEPWKAPPELQEQYGCVIGKDYPAPMVNLAEVNKCNANKMNAIRQKLLDQGGSTPAHCRPS
SQ  DMDEVRQFFWLPEDVAAES
//
ID  O77059;
PN  Cryptochrome-1;
GN  cry;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Nucleus {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}. Note=Nuclear translocation initiates after the perception of a light signal. Accumulates in the perinuclear region about one hour before translocation into the nucleus. Translocation occurs through interaction with other Clock proteins such as tim and per. {ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:15258584}.
DR  UNIPROT: O77059;
DR  UNIPROT: Q9TYA0;
DR  PDB: 4GU5;
DR  PDB: 4JZY;
DR  PDB: 4K03;
DR  PDB: 6WTB;
DR  Pfam: PF00875;
DR  Pfam: PF03441;
DR  PROSITE: PS51645;
DE  Function: Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry. Necessary for light-dependent magnetosensitivity, an intact circadian system is not required for the magnetoreception mechanism to operate. Required for both the naive and trained responses to magnetic field, consistent with the notion that cry is in the input pathway of magnetic sensing. {ECO:0000269|PubMed:10063806, ECO:0000269|PubMed:10233998, ECO:0000269|PubMed:10417378, ECO:0000269|PubMed:16527739, ECO:0000269|PubMed:17298948, ECO:0000269|PubMed:18597555, ECO:0000269|PubMed:18641630, ECO:0000269|PubMed:9845369, ECO:0000269|PubMed:9845370}.
DE  Reference Proteome: Yes;
DE  Interaction: P49021; IntAct: EBI-872146; Score: 0.27
DE  Interaction: P07663; IntAct: EBI-872150; Score: 0.27
DE  Interaction: P18431; IntAct: EBI-1248163; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0009882;
GO  GO:0003677;
GO  GO:0071949;
GO  GO:0050660;
GO  GO:0008020;
GO  GO:0009881;
GO  GO:0009785;
GO  GO:0071482;
GO  GO:0048512;
GO  GO:0032922;
GO  GO:0007623;
GO  GO:0050980;
GO  GO:0009649;
GO  GO:0043153;
GO  GO:0042332;
GO  GO:0045475;
GO  GO:0050958;
GO  GO:0045892;
GO  GO:0007602;
GO  GO:0042752;
GO  GO:0045187;
GO  GO:0009637;
GO  GO:0009416;
GO  GO:0071000;
GO  GO:0009588;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATRGANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAATDGRGR
SQ  LLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVEKVSHTLWDPQLVIETNGGIPPLTYQM
SQ  FLHTVQIIGLPPRPTADARLEDATFVELDPEFCRSLKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKV
SQ  EQHAFERGFYLPNQALPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGVQMTGGAHITGQLIWREYFYT
SQ  MSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEHG
SQ  LQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQ
SQ  EQYECLIGVHYPERIIDLSMAVKRNMLAMKSLRNSLITPPPHCRPSNEEEVRQFFWLADVVV
//
ID  Q293P8;
PN  Cryptochrome-1;
GN  cry;
OS  46245;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O77059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O77059}. Nucleus {ECO:0000250|UniProtKB:O77059}. Note=Nuclear translocation initiates after the perception of a light signal. Accumulates in the perinuclear region about one hour before translocation into the nucleus. Translocation occurs through interaction with other Clock proteins such as tim and per (By similarity). {ECO:0000250|UniProtKB:O77059}.
DR  UNIPROT: Q293P8;
DR  Pfam: PF00875;
DR  Pfam: PF03441;
DR  PROSITE: PS51645;
DE  Function: Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Light induces the degradation of cry, likely due to conformational change in the photoreceptor leading to targeting to the proteasome. Under circadian regulation, expression is influenced by the clock pacemaker genes period, timeless, Clock and cycle. Binding to tim irreversibly commits tim to proteasomal degradation. Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry. Necessary for light-dependent magnetosensitivity, an intact circadian system is not required for the magnetoreception mechanism to operate. Required for both the naive and trained responses to magnetic field, consistent with the notion that Cry is in the input pathway of magnetic sensing (By similarity). {ECO:0000250|UniProtKB:O77059}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0009882;
GO  GO:0071949;
GO  GO:0050660;
GO  GO:0032922;
GO  GO:0050980;
GO  GO:0043153;
GO  GO:0042332;
GO  GO:0045475;
GO  GO:0045892;
GO  GO:0007602;
GO  GO:0042752;
GO  GO:0045187;
GO  GO:0071000;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVPRGANVLWFRHGLRLHDNPALLAALEEKDQGIPLIPVFIFDGESAGTKSVGYNRMRFLLDSLQDLDEQLQSATEGRGR
SQ  LFVFEGEPTLIFRRLHEQVRLHKICAELDCEPIWNERDESARLLCRELGIEYVEKVSHTLWDPRLVIETNGGIPPLTYQM
SQ  FLHTVQIIGVPPRPAIDAHINDATFIQLAPELRQHLGCFDQVPNPEHFNIYSDNMGFLAKINWRGGETQALALLEERLKV
SQ  ERNAFERGYYLPNQANPNIQEAPKSMSAHLRFGCLSVRRFYWSVHDLFENVQLAACVRGVQIEGGAHITGQLIWREYFYT
SQ  MSVNNPNYDRMEGNEICLTIPWAKPDENLLQRWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEPG
SQ  LKHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPEGVYIRRYVPELKNLPKEYIHEPWRLSAEQQ
SQ  VKFECLIGVHYPERIIDLSKAVKRNMMAMTALRNSLITPPPHCRPSNEEEVRQFFWLANY
//
ID  O13671;
PN  Importin-alpha re-exporter;
GN  kap109;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O13671;
DR  UNIPROT: Q9USC9;
DR  Pfam: PF03378;
DR  Pfam: PF08506;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Export receptor for importin alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates have been released into the nucleoplasm (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005525;
GO  GO:0005049;
GO  GO:0031267;
GO  GO:0006611;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDIPTLLARTLNPTTSKSAEEALKVWELQDSSFALKLLNIVAEDTVDINIKLAASLYFKNYIKKHWDSEEGASIRISDE
SQ  VAELIKREIINLMLKSTTIIQVQLGEVIGYIANFDFPDRWDTLLPDLISKLSAVDMNTNIAVLSTAHAIFKRWRPLFRSD
SQ  ALFLEIKYVLDRFCEPFLALFVQTNNLLRNGPQDAESLNSLFQVILLECKLFYDLNCQDIPEFFEDHMSEFMTAFLNYFT
SQ  YTNPSLEGDEGETNVLIKVKASICEIVELYTLRYEEVFTMLYDFVNVTWTLLTTLTPDEKYDGLVGKAMAFLTSVIRIRK
SQ  HAEFFQQDQVLQQFIELVVLPNICLRESDEELFEDDPLEYVRRDLEGSNSDSRARSAIVLVRGLLDHFDQKITSVVSTHI
SQ  NANLQQFSTNPSLEWNKKYVALQLFSAIAIKGQSTRLGVTSINLMVDVVAFFENNIKPDLLQPAGVIHPMVLAEDIKYVF
SQ  TFRNQLNSQQLIDIFPTILRFLEMPSFVVYTYAAIALDQLLTVRHNHVHIFTSLLIAPHILPALNQLFLIVESASTPQKL
SQ  AENDYLMKAVMRIIIMSQEAILPAASLLLQHLTKITEEVSKNPSNPKFNHYLFESIGALIRSLSKSGPQTVSQLENALLP
SQ  VFQNVLIEDVTEFIPYVLQLLSQLVEASGNEPLPDFVVNLIQPCLSPALWDSKGNIPALVRLLRAMIFRGPQIFISNKFV
SQ  EPVLGIFQKLISSKVNDHFGFDLLDRVFTVFNANILAPYINHIFFLLLSRLKNSRTERFVLRCTIFFFFVASEQTGTCGP
SQ  DNLIQGVDAVQSGVFGQLMTSIILPQAQKLALPLDRKISALGLLRLLTCDLVLAPDAIYENLIIPLLTCILKLFEMPIEQ
SQ  AQTDADEELFMDEIDADSMSFQASFSRLATTGGKRVDPFPQITDLKQYCATEMNLANRNMGGRLSQIISTHLPGDGQSVL
SQ  QSYGYVI
//
ID  Q08955;
PN  Chromosome segregation in meiosis protein 4;
GN  CSM4;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12514182}; Single-pass membrane protein {ECO:0000269|PubMed:12514182}. Nucleus membrane {ECO:0000305|PubMed:12514182}; Single-pass membrane protein {ECO:0000305|PubMed:12514182}.
DR  UNIPROT: Q08955;
DR  UNIPROT: D6W3G9;
DE  Function: Involved in chromosome segregation during meiosis. Involved in meiotic telomere clustering (bouquet formation) and telomere-led rapid prophase movements. {ECO:0000269|PubMed:11470404, ECO:0000269|PubMed:18585352}.
DE  Reference Proteome: Yes;
DE  Interaction: P47069; IntAct: EBI-1795681; Score: 0.50
GO  GO:0000781;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0005640;
GO  GO:0140444;
GO  GO:0007129;
GO  GO:0045132;
GO  GO:0045141;
GO  GO:0010520;
GO  GO:0030435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMDGSITRKVTSTLSNQLATWKWKLQLSLLERKLATINNDYFLLQWELLFITNEVMKWKEMIAFLESQLFCTTQNFVAQE
SQ  THDRETFQSLVDDYNKQLSENNLIISVLKSRPQLSSFPIYLSDEVCSHLKFVIAELNSLIIVFFISLVFLWVSIEV
//
ID  Q6PC30;
PN  COP9 signalosome complex subunit 5;
GN  cops5;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92905}. Nucleus {ECO:0000250|UniProtKB:Q92905}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92905}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q92905}.
DR  UNIPROT: Q6PC30;
DR  Pfam: PF18323;
DR  Pfam: PF01398;
DR  PROSITE: PS50249;
DE  Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligase complexes, leading to modify the Ubl ligase activity. In the complex, it probably acts as the catalytic center that mediates the cleavage of nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. {ECO:0000250|UniProtKB:Q92905}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0008180;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0008021;
GO  GO:0019784;
GO  GO:0046872;
GO  GO:0004222;
GO  GO:0008237;
GO  GO:0043066;
GO  GO:0051091;
GO  GO:0000338;
GO  GO:0060118;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGSSIAMKTWELSNSMQEVQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKLSALALLKMVMHARSGGNLEVMGLML
SQ  GKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQ
SQ  EPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLW
SQ  NKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQAEAQLGRGSFMLGLDTHDRKSEDKLAKATRDSCKTTIEAIHGLMSQV
SQ  IKDKLFNQVNTSAN
//
ID  Q92905;
PN  COP9 signalosome complex subunit 5;
GN  COPS5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20978819, ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:9535219}. Nucleus {ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20978819, ECO:0000269|PubMed:22609399}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9535219}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:21102408}. Note=Nuclear localization is diminished in the presence of IFIT3. {ECO:0000269|PubMed:17050680}.
DR  UNIPROT: Q92905;
DR  UNIPROT: O15386;
DR  UNIPROT: Q6AW95;
DR  UNIPROT: Q86WQ4;
DR  UNIPROT: Q9BQ17;
DR  PDB: 4D10;
DR  PDB: 4D18;
DR  PDB: 4F7O;
DR  PDB: 4WSN;
DR  PDB: 5JOG;
DR  PDB: 5JOH;
DR  PDB: 5M5Q;
DR  PDB: 6R6H;
DR  PDB: 6R7F;
DR  PDB: 6R7H;
DR  PDB: 6R7I;
DR  Pfam: PF18323;
DR  Pfam: PF01398;
DR  PROSITE: PS50249;
DR  OMIM: 604850;
DR  DisGeNET: 10987;
DE  Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. Promotes the proteasomal degradation of BRSK2. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:20978819, ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:9535219}.
DE  Reference Proteome: Yes;
DE  Interaction: O15504; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O75694; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O95831; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O95999; IntAct: EBI-7006208; Score: 0.35
DE  Interaction: P04406; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P11802; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P31689; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P63244; IntAct: EBI-21325777; Score: 0.55
DE  Interaction: P63279; IntAct: EBI-3454145; Score: 0.00
DE  Interaction: Q07065; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q3TLR7; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: Q5JTH9; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-2510150; Score: 0.91
DE  Interaction: Q8IWQ3; IntAct: EBI-30872909; Score: 0.64
DE  Interaction: Q8N114; IntAct: EBI-2115585; Score: 0.00
DE  Interaction: Q8NE71; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8NI35; IntAct: EBI-2659663; Score: 0.35
DE  Interaction: Q8TEL6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92900; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P55789; IntAct: EBI-7286464; Score: 0.60
DE  Interaction: P14174; IntAct: EBI-7522890; Score: 0.59
DE  Interaction: P10599; IntAct: EBI-594678; Score: 0.74
DE  Interaction: P46527; IntAct: EBI-594810; Score: 0.60
DE  Interaction: Q15796; IntAct: EBI-7224786; Score: 0.37
DE  Interaction: Q5VTD9; IntAct: EBI-956654; Score: 0.00
DE  Interaction: P09936; IntAct: EBI-1181897; Score: 0.54
DE  Interaction: P22087; IntAct: EBI-1182007; Score: 0.49
DE  Interaction: O95273; IntAct: EBI-1385474; Score: 0.54
DE  Interaction: P40337; IntAct: EBI-1551755; Score: 0.40
DE  Interaction: O75882; IntAct: EBI-2115511; Score: 0.00
DE  Interaction: P36507; IntAct: EBI-2115525; Score: 0.00
DE  Interaction: Q9HB07; IntAct: EBI-2115530; Score: 0.00
DE  Interaction: Q9NZF1; IntAct: EBI-2115546; Score: 0.00
DE  Interaction: P50336; IntAct: EBI-2115551; Score: 0.00
DE  Interaction: P54578; IntAct: EBI-2115609; Score: 0.00
DE  Interaction: P04004; IntAct: EBI-2115614; Score: 0.00
DE  Interaction: Q16539; IntAct: EBI-2116848; Score: 0.00
DE  Interaction: P62256; IntAct: EBI-2339626; Score: 0.37
DE  Interaction: Q9UDY8; IntAct: EBI-7006117; Score: 0.35
DE  Interaction: Q9BXL7; IntAct: EBI-7006135; Score: 0.46
DE  Interaction: Q13098; IntAct: EBI-7006270; Score: 0.93
DE  Interaction: Q5VTR2; IntAct: EBI-8566847; Score: 0.50
DE  Interaction: Q15018; IntAct: EBI-8566862; Score: 0.35
DE  Interaction: P0CG48; IntAct: EBI-8566988; Score: 0.40
DE  Interaction: P61201; IntAct: EBI-2510150; Score: 0.88
DE  Interaction: Q86XK2; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q9BX70; IntAct: EBI-2510150; Score: 0.67
DE  Interaction: Q13620; IntAct: EBI-2510150; Score: 0.85
DE  Interaction: Q9H496; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q96EF6; IntAct: EBI-2510150; Score: 0.67
DE  Interaction: Q96M94; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q9BT78; IntAct: EBI-2510150; Score: 0.85
DE  Interaction: Q92466; IntAct: EBI-2510150; Score: 0.80
DE  Interaction: Q9P2J3; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q9UBW8; IntAct: EBI-2510150; Score: 0.85
DE  Interaction: P15374; IntAct: EBI-2510150; Score: 0.40
DE  Interaction: Q13616; IntAct: EBI-2510150; Score: 0.74
DE  Interaction: Q99627; IntAct: EBI-2510150; Score: 0.90
DE  Interaction: Q8NEZ5; IntAct: EBI-2510150; Score: 0.40
DE  Interaction: Q6TFL4; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q9H9Q2; IntAct: EBI-2510150; Score: 0.85
DE  Interaction: Q8TEB1; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q13619; IntAct: EBI-2510150; Score: 0.74
DE  Interaction: Q13309; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q15843; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q13618; IntAct: EBI-2510150; Score: 0.67
DE  Interaction: Q15048; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q9Y4B6; IntAct: EBI-2510150; Score: 0.67
DE  Interaction: Q9P2N7; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q13617; IntAct: EBI-2510150; Score: 0.67
DE  Interaction: Q96L50; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q53GT1; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: Q9UNS2; IntAct: EBI-2510150; Score: 0.92
DE  Interaction: Q13216; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: O94889; IntAct: EBI-2510150; Score: 0.56
DE  Interaction: B4DN30; IntAct: EBI-2510150; Score: 0.40
DE  Interaction: Q3U1J4; IntAct: EBI-2559059; Score: 0.40
DE  Interaction: P53355; IntAct: EBI-2659621; Score: 0.35
DE  Interaction: Q96N67; IntAct: EBI-2659621; Score: 0.35
DE  Interaction: P08107; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: P25705; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: Q9NZQ3; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: P80723; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: Q9NNW5; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: P34931; IntAct: EBI-2659628; Score: 0.53
DE  Interaction: O43491; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: Q4VCS5; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: P48741; IntAct: EBI-2659628; Score: 0.53
DE  Interaction: Q8IY63; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-2659628; Score: 0.53
DE  Interaction: P17066; IntAct: EBI-2659628; Score: 0.53
DE  Interaction: P63167; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: P28289; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: O75955; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: Q9UJZ1; IntAct: EBI-2659628; Score: 0.35
DE  Interaction: O75970; IntAct: EBI-2659663; Score: 0.35
DE  Interaction: P62877; IntAct: EBI-2659663; Score: 0.35
DE  Interaction: Q6PJ61; IntAct: EBI-2659663; Score: 0.53
DE  Interaction: Q9NUP9; IntAct: EBI-2659663; Score: 0.35
DE  Interaction: O14974; IntAct: EBI-2659663; Score: 0.35
DE  Interaction: P35580; IntAct: EBI-2659663; Score: 0.35
DE  Interaction: Q5VUJ6; IntAct: EBI-2659663; Score: 0.53
DE  Interaction: Q8N3R9; IntAct: EBI-2659663; Score: 0.35
DE  Interaction: O15085; IntAct: EBI-2659663; Score: 0.35
DE  Interaction: Q16531; IntAct: EBI-2659663; Score: 0.53
DE  Interaction: Q9P2K6; IntAct: EBI-2659663; Score: 0.53
DE  Interaction: Q9Y2D5; IntAct: EBI-2659663; Score: 0.35
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q16584; IntAct: EBI-3442917; Score: 0.00
DE  Interaction: Q99759; IntAct: EBI-3443070; Score: 0.00
DE  Interaction: O43318; IntAct: EBI-3443260; Score: 0.00
DE  Interaction: Q8IVH8; IntAct: EBI-3443337; Score: 0.00
DE  Interaction: Q9Y4K4; IntAct: EBI-3443648; Score: 0.00
DE  Interaction: P61244; IntAct: EBI-3444880; Score: 0.00
DE  Interaction: Q06413; IntAct: EBI-3445247; Score: 0.00
DE  Interaction: Q14814; IntAct: EBI-3445506; Score: 0.00
DE  Interaction: Q12772; IntAct: EBI-3451285; Score: 0.00
DE  Interaction: P61981; IntAct: EBI-3453135; Score: 0.00
DE  Interaction: Q9H4A3; IntAct: EBI-3453687; Score: 0.00
DE  Interaction: O15105; IntAct: EBI-3861684; Score: 0.64
DE  Interaction: Q13485; IntAct: EBI-3862454; Score: 0.40
DE  Interaction: P02743; IntAct: EBI-3907158; Score: 0.37
DE  Interaction: Q99489; IntAct: EBI-3915505; Score: 0.37
DE  Interaction: Q9NPY3; IntAct: EBI-3922558; Score: 0.37
DE  Interaction: Q9P0P8; IntAct: EBI-3922568; Score: 0.37
DE  Interaction: Q8N6T3; IntAct: EBI-3922578; Score: 0.37
DE  Interaction: P19838; IntAct: EBI-3936417; Score: 0.55
DE  Interaction: P32119; IntAct: EBI-3936427; Score: 0.37
DE  Interaction: Q9BYB0; IntAct: EBI-3942223; Score: 0.37
DE  Interaction: P55085; IntAct: EBI-4303187; Score: 0.64
DE  Interaction: P36873; IntAct: EBI-4311588; Score: 0.37
DE  Interaction: Q9H8M7; IntAct: EBI-4422753; Score: 0.54
DE  Interaction: Q02556; IntAct: EBI-6115692; Score: 0.35
DE  Interaction: P12520; IntAct: EBI-6177205; Score: 0.35
DE  Interaction: Q96GG9; IntAct: EBI-21325177; Score: 0.35
DE  Interaction: Q9C0D3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96FX7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P09012; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P35250; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UKV8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UL18; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14011; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8N726; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P54132; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O94844; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q86YV6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8N4N3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UK96; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96ME1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8N1E6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96FN4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NWX5; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q86TJ5; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NR11; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O15231; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96KR1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q5TAX3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q7Z2W4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9H6S0; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P67809; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9H0D6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P12956; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y4P8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9GZS3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P61964; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q5TAQ9; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q5T6F0; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q3SXM0; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8WV16; IntAct: EBI-21325777; Score: 0.53
DE  Interaction: P08670; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P55072; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q93009; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y4E8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P10746; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BZI7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14157; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P22314; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P26368; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P49411; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P68371; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9H4B7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P68366; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8WZ42; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6IQ55; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13263; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62995; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13595; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P11387; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UPQ9; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8TDI8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q01085; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P31483; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q86V81; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92734; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q00059; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P17987; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15370; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15369; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y4P3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92804; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96SI9; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y3F4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NUL3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q08945; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P51571; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q04837; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P05455; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UQ35; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96SB4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P37108; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O15042; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q01082; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13813; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92673; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y5X1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62308; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62306; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62304; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62318; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62316; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P09234; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P14678; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P08621; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O75643; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UQE7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q12824; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P51532; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6IEE8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P12236; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P12235; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8TBC3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q16629; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13247; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13243; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P84103; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q01130; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q07955; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P23246; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15427; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15393; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O75533; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q12874; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P48594; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P29508; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9GZR1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P21912; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14151; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P06702; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P05109; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y265; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O76021; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y3B9; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P23921; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P46781; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62241; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62081; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62701; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P61247; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P23396; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P42677; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62851; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62847; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62266; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P63220; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P60866; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P39019; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P08708; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62249; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62244; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62841; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62263; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62277; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62280; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P46783; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P04843; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P05387; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P05386; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P05388; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P32969; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62917; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62424; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q02878; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P46777; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P36578; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P63173; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P61513; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P42766; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62899; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62888; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P39023; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P46779; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P46776; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P61353; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UNX3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P83731; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62750; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62829; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P35268; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P84098; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q02543; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q07020; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P61313; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P50914; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P26373; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P30050; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62913; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96L21; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62906; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15287; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O43148; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P13489; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8WVD3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P78509; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8NDN9; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O75526; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P52756; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BTD8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BWF3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14498; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P98179; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q16769; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P09417; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13610; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UHX1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P26599; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14997; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O14818; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O60256; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14558; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P21108; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O75400; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q86UA1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8WWY3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UMS4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P78527; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P30048; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q06830; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O75807; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62937; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q99575; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P19388; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P19387; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8WVV4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q02809; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P53350; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P14618; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9P1Y6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O00264; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P00558; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96HS1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q01813; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O00764; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15084; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P29803; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O43924; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6L8Q7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P22061; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15366; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15365; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P61457; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P09874; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q86U42; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13310; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P11940; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q7Z417; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BRJ7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P36639; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q08J23; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P16083; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P46087; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y3C1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15233; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O15226; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P49821; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P19338; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P55209; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NP98; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NPC7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8WXC6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BQG0; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6UB35; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92552; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P82663; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y3D9; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P82650; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P82914; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P82912; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13405; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8N983; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P49406; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y3B7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9HCE1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P50219; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P40926; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P33993; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P25205; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P43243; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P31153; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P49137; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92918; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UNF1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NX58; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y383; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q3MHD2; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8N1G4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6ZN17; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q08380; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P07195; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92615; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6PKG0; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P35527; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6KB66; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8N1N4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q01546; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O95678; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q3SY84; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P48668; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P04259; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P02538; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P13647; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P12035; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q2M2I5; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P35908; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q04695; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P08779; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P02533; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P13646; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P13645; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P04264; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P52294; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9P2G9; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q53HC5; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8NBE8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UJP4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q53G59; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8N163; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9C0C6; IntAct: EBI-21325777; Score: 0.53
DE  Interaction: Q92945; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P50053; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8NC69; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y597; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6PI47; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9H3F6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q86V97; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NVX7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15046; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P14923; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P17535; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96A47; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P61371; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O14654; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P12268; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q12906; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q12905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O00425; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NZI8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P41252; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P38646; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P34932; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q58FF8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14568; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q99714; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q7Z5J1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q86YZ3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P31260; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O14979; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q1KMD3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BUJ2; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O43390; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P52272; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P14866; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P61978; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P31942; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P31943; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P52597; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O60812; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P07910; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q99729; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P51991; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P09651; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13151; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q16778; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P16403; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q00341; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O14929; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P13807; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q7Z2Y8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BZE4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O00178; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P09211; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BQ67; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BVP2; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92820; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8IUC8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8TAE8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P51114; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P35637; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96I24; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96AE4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8IY81; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q5D862; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6UN15; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q5HY92; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96JP0; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UK73; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P22830; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q5XUX1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UKB1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UK97; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y3I1; IntAct: EBI-21325777; Score: 0.53
DE  Interaction: Q9H4M3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q5XUX0; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UK99; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O94952; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UKA1; IntAct: EBI-21325777; Score: 0.53
DE  Interaction: A6NHQ2; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62861; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q52LJ0; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8NCA5; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6ZRV2; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NRY5; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BTL3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q06265; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q01844; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P07814; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P06733; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15717; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BQ52; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P63241; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P05198; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8NDI1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15029; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8IYU8; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P13639; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P26641; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q05639; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P68104; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q19T08; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q99848; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14204; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BVJ7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NZJ0; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P15924; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q02413; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92785; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O00429; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8WXX5; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8IXB1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O60884; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9P225; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P10515; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q08211; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6P158; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9H2U1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q7L2E3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q7Z478; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O43143; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P35659; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9H1M4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P26196; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y2R4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P17844; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O00571; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NY93; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UHI6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UMR2; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NVP1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92841; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q92499; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BW61; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6V1P9; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P81605; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96EP5; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O95886; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P19875; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q93034; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P17812; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P35221; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O75534; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P16989; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O95232; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96SW2; IntAct: EBI-21325777; Score: 0.53
DE  Interaction: Q9UBL6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8IWV2; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P53675; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P09496; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P61024; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O14757; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q00526; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P24941; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q12834; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P78371; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9ULG6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P20248; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P78396; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96A33; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6YP21; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P16152; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q86X55; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q14444; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8NCB2; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NZT1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q05682; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BRJ6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NRH1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NXF7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8N2C7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y3I0; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q7Z2T5; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q07021; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9Y224; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9BRQ4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q5SWW7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13895; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O43684; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96Q07; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9H0C5; IntAct: EBI-21325777; Score: 0.53
DE  Interaction: Q9NSI6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13867; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O95429; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P18846; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P08243; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P05089; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q10567; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6UB98; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UJX3; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9UJX6; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P23109; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9C0C7; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P09972; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: O43823; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q12904; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P23526; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P35573; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P61163; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q562R1; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P60709; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P62736; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q5FVE4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P24666; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8N961; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q8WWZ4; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P35372; IntAct: EBI-6918514; Score: 0.58
DE  Interaction: P89884; IntAct: EBI-9639873; Score: 0.37
DE  Interaction: O41946; IntAct: EBI-9640254; Score: 0.37
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: O43172; IntAct: EBI-11043099; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-11084972; Score: 0.35
DE  Interaction: B2BTY8; IntAct: EBI-11510494; Score: 0.40
DE  Interaction: H9XIJ5; IntAct: EBI-11514210; Score: 0.37
DE  Interaction: B4URF7; IntAct: EBI-11514901; Score: 0.40
DE  Interaction: O60885; IntAct: EBI-11773406; Score: 0.49
DE  Interaction: Q969Y2; IntAct: EBI-24773699; Score: 0.56
DE  Interaction: P06929; IntAct: EBI-26501685; Score: 0.37
DE  Interaction: P36799; IntAct: EBI-26502049; Score: 0.37
DE  Interaction: P24830; IntAct: EBI-16046619; Score: 0.37
DE  Interaction: P06423; IntAct: EBI-16046569; Score: 0.37
DE  Interaction: P06790; IntAct: EBI-16046534; Score: 0.37
DE  Interaction: P36780; IntAct: EBI-16049148; Score: 0.00
DE  Interaction: Q8IWL3; IntAct: EBI-15104984; Score: 0.37
DE  Interaction: O95704; IntAct: EBI-21591300; Score: 0.35
DE  Interaction: O43399; IntAct: EBI-21732177; Score: 0.35
DE  Interaction: Q6JEL2; IntAct: EBI-21755575; Score: 0.35
DE  Interaction: O43583; IntAct: EBI-21785701; Score: 0.35
DE  Interaction: P61081; IntAct: EBI-21805700; Score: 0.35
DE  Interaction: Q7L5Y6; IntAct: EBI-21846729; Score: 0.35
DE  Interaction: O14775; IntAct: EBI-21871177; Score: 0.35
DE  Interaction: Q8TF40; IntAct: EBI-21875885; Score: 0.35
DE  Interaction: O14879; IntAct: EBI-15606624; Score: 0.59
DE  Interaction: Q9NRI5; IntAct: EBI-21371075; Score: 0.00
DE  Interaction: Q92879; IntAct: EBI-21371061; Score: 0.00
DE  Interaction: P05067; IntAct: EBI-21371087; Score: 0.00
DE  Interaction: P10636; IntAct: EBI-21371101; Score: 0.00
DE  Interaction: O84326; IntAct: EBI-22302779; Score: 0.40
DE  Interaction: Q15831; IntAct: EBI-34582140; Score: 0.35
GO  GO:0070161;
GO  GO:0008180;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005852;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0008021;
GO  GO:0019784;
GO  GO:0019899;
GO  GO:0035718;
GO  GO:0046872;
GO  GO:0140492;
GO  GO:0004222;
GO  GO:0008237;
GO  GO:0003713;
GO  GO:0003743;
GO  GO:1990182;
GO  GO:0043066;
GO  GO:0051091;
GO  GO:0045944;
GO  GO:0043687;
GO  GO:0000338;
GO  GO:0016579;
GO  GO:0045116;
GO  GO:0051726;
GO  GO:1903894;
GO  GO:0046328;
GO  GO:2000434;
GO  GO:0006412;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGL
SQ  MLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQ
SQ  FQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLEL
SQ  LWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMS
SQ  QVIKDKLFNQINIS
//
ID  O35864;
PN  COP9 signalosome complex subunit 5;
GN  Cops5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:10721695}. Nucleus {ECO:0000269|PubMed:10721695}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92905}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q92905}. Note=Nuclear localization is diminished in the presence of IFIT3. {ECO:0000250|UniProtKB:Q92905}.
DR  UNIPROT: O35864;
DR  UNIPROT: Q3UA70;
DR  UNIPROT: Q8C1S1;
DR  Pfam: PF18323;
DR  Pfam: PF01398;
DR  PROSITE: PS50249;
DE  Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Promotes the proteasomal degradation of BRSK2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. {ECO:0000250|UniProtKB:Q92905}.
DE  Reference Proteome: Yes;
DE  Interaction: Q99LD4; IntAct: EBI-8482462; Score: 0.35
GO  GO:0070161;
GO  GO:0000785;
GO  GO:0008180;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0008021;
GO  GO:0005667;
GO  GO:0019784;
GO  GO:0019899;
GO  GO:0035718;
GO  GO:0046872;
GO  GO:0140492;
GO  GO:0004222;
GO  GO:0008237;
GO  GO:0003713;
GO  GO:1990182;
GO  GO:0043066;
GO  GO:0051091;
GO  GO:0045944;
GO  GO:0000338;
GO  GO:0016579;
GO  GO:0051726;
GO  GO:0006355;
GO  GO:1903894;
GO  GO:0046328;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGL
SQ  MLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQ
SQ  FQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLEL
SQ  LWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMS
SQ  QVIKDKLFNQINVA
//
ID  Q6GLM9;
PN  COP9 signalosome complex subunit 5;
GN  cops5;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92905}. Nucleus {ECO:0000250|UniProtKB:Q92905}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92905}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q92905}.
DR  UNIPROT: Q6GLM9;
DR  Pfam: PF18323;
DR  Pfam: PF01398;
DR  PROSITE: PS50249;
DE  Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligase complexes, leading to modify the Ubl ligase activity. In the complex, it probably acts as the catalytic center that mediates the cleavage of nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. {ECO:0000250|UniProtKB:Q92905}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0008180;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0008021;
GO  GO:0046872;
GO  GO:0004222;
GO  GO:0043066;
GO  GO:0051091;
GO  GO:0006508;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGSSVAQKTWELSNNMQEVQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKVSALALLKMVMHARSGGNLEVMGLML
SQ  GKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQ
SQ  EPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVTYFKSSLDRKLLELLW
SQ  NKYWVNTLSSSSLLTNAEYTTGQVFDLSEKLEQSEAQLGRGSFMLGLESHDRKSEDKLAKATRDSCKTTIEAIHGLMSQV
SQ  IKDKLFNQINTF
//
ID  Q6P635;
PN  COP9 signalosome complex subunit 5;
GN  cops5;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92905}. Nucleus {ECO:0000250|UniProtKB:Q92905}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92905}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q92905}.
DR  UNIPROT: Q6P635;
DR  UNIPROT: Q28HI7;
DR  Pfam: PF18323;
DR  Pfam: PF01398;
DR  PROSITE: PS50249;
DE  Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligase complexes, leading to modify the Ubl ligase activity. In the complex, it probably acts as the catalytic center that mediates the cleavage of nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. {ECO:0000250|UniProtKB:Q92905}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0008180;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0008021;
GO  GO:0019784;
GO  GO:0046872;
GO  GO:0004222;
GO  GO:0008237;
GO  GO:0043066;
GO  GO:0051091;
GO  GO:0000338;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMAGSSVAQKTWELSNNMQEVQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKVSALALLKMVMHARSGGNLEVMGL
SQ  MLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQ
SQ  FQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVTYFKSSLDRKLLEL
SQ  LWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMS
SQ  QVIKDKLFNQINTA
//
ID  Q7L5N1;
PN  COP9 signalosome complex subunit 6;
GN  COPS6;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:9535219}. Cytoplasm {ECO:0000269|PubMed:9535219}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9520381}. Note=(Microbial infection) The interaction with HIV-1 Vpr protein possibly leads its translocation to a perinuclear region. {ECO:0000269|PubMed:9520381}.
DR  UNIPROT: Q7L5N1;
DR  UNIPROT: A4D2A3;
DR  UNIPROT: O15387;
DR  PDB: 4D10;
DR  PDB: 4D18;
DR  PDB: 4QFT;
DR  PDB: 4R14;
DR  PDB: 4WSN;
DR  PDB: 6R6H;
DR  PDB: 6R7F;
DR  PDB: 6R7H;
DR  PDB: 6R7I;
DR  Pfam: PF01398;
DR  Pfam: PF13012;
DR  PROSITE: PS50249;
DR  OMIM: 614729;
DR  DisGeNET: 10980;
DE  Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF- type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Has some glucocorticoid receptor-responsive activity. Stabilizes COP1 through reducing COP1 auto-ubiquitination and decelerating COP1 turnover rate, hence regulates the ubiquitination of COP1 targets. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:21625211, ECO:0000269|PubMed:9535219}.
DE  Reference Proteome: Yes;
DE  Interaction: O75569; IntAct: EBI-730597; Score: 0.00
DE  Interaction: P04406; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P11802; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P49454; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-731797; Score: 0.00
DE  Interaction: P78406; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q3TLR7; IntAct: EBI-2562304; Score: 0.40
DE  Interaction: Q5JTH9; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P40425; IntAct: EBI-348673; Score: 0.00
DE  Interaction: P08670; IntAct: EBI-475271; Score: 0.37
DE  Interaction: P14174; IntAct: EBI-7523063; Score: 0.40
DE  Interaction: Q9BX70; IntAct: EBI-2510262; Score: 0.75
DE  Interaction: Q96RU7; IntAct: EBI-729666; Score: 0.00
DE  Interaction: Q96HD1; IntAct: EBI-729816; Score: 0.00
DE  Interaction: O43261; IntAct: EBI-729873; Score: 0.00
DE  Interaction: Q3KQU3; IntAct: EBI-729987; Score: 0.00
DE  Interaction: Q9GZN7; IntAct: EBI-730002; Score: 0.00
DE  Interaction: Q16363; IntAct: EBI-730249; Score: 0.00
DE  Interaction: Q15102; IntAct: EBI-730441; Score: 0.00
DE  Interaction: Q6P1K2; IntAct: EBI-730531; Score: 0.00
DE  Interaction: O00231; IntAct: EBI-730615; Score: 0.00
DE  Interaction: P40937; IntAct: EBI-730663; Score: 0.00
DE  Interaction: P15927; IntAct: EBI-730690; Score: 0.00
DE  Interaction: P21673; IntAct: EBI-730750; Score: 0.00
DE  Interaction: P50453; IntAct: EBI-730786; Score: 0.00
DE  Interaction: P62308; IntAct: EBI-730870; Score: 0.00
DE  Interaction: P04183; IntAct: EBI-7396449; Score: 0.55
DE  Interaction: P17028; IntAct: EBI-731131; Score: 0.00
DE  Interaction: Q96SN7; IntAct: EBI-731467; Score: 0.00
DE  Interaction: Q9Y6N8; IntAct: EBI-731527; Score: 0.00
DE  Interaction: P42773; IntAct: EBI-731554; Score: 0.00
DE  Interaction: Q14061; IntAct: EBI-731602; Score: 0.00
DE  Interaction: P20674; IntAct: EBI-731608; Score: 0.00
DE  Interaction: Q53FE4; IntAct: EBI-731683; Score: 0.00
DE  Interaction: O14717; IntAct: EBI-731731; Score: 0.00
DE  Interaction: P05305; IntAct: EBI-731764; Score: 0.00
DE  Interaction: Q09472; IntAct: EBI-731824; Score: 0.00
DE  Interaction: P84090; IntAct: EBI-731839; Score: 0.00
DE  Interaction: Q9NY59; IntAct: EBI-731947; Score: 0.00
DE  Interaction: P30519; IntAct: EBI-732133; Score: 0.00
DE  Interaction: Q9BWC9; IntAct: EBI-732208; Score: 0.00
DE  Interaction: P06858; IntAct: EBI-732383; Score: 0.00
DE  Interaction: Q13113; IntAct: EBI-732452; Score: 0.00
DE  Interaction: Q8IYB7; IntAct: EBI-732497; Score: 0.00
DE  Interaction: Q8N2I9; IntAct: EBI-732509; Score: 0.00
DE  Interaction: P51948; IntAct: EBI-732533; Score: 0.00
DE  Interaction: Q99417; IntAct: EBI-732572; Score: 0.00
DE  Interaction: P09466; IntAct: EBI-732710; Score: 0.00
DE  Interaction: P17858; IntAct: EBI-732806; Score: 0.00
DE  Interaction: Q92561; IntAct: EBI-732833; Score: 0.00
DE  Interaction: P07602; IntAct: EBI-732965; Score: 0.00
DE  Interaction: P60484; IntAct: EBI-733013; Score: 0.00
DE  Interaction: Q9BXR0; IntAct: EBI-733043; Score: 0.00
DE  Interaction: P51159; IntAct: EBI-733067; Score: 0.00
DE  Interaction: P11166; IntAct: EBI-733325; Score: 0.00
DE  Interaction: Q16637; IntAct: EBI-7388742; Score: 0.55
DE  Interaction: Q13190; IntAct: EBI-733412; Score: 0.00
DE  Interaction: P49888; IntAct: EBI-733421; Score: 0.00
DE  Interaction: P13385; IntAct: EBI-733511; Score: 0.00
DE  Interaction: O60315; IntAct: EBI-733740; Score: 0.00
DE  Interaction: Q9Y4P8; IntAct: EBI-734305; Score: 0.00
DE  Interaction: P62861; IntAct: EBI-734475; Score: 0.00
DE  Interaction: Q8IYL3; IntAct: EBI-734959; Score: 0.00
DE  Interaction: P61313; IntAct: EBI-21328549; Score: 0.55
DE  Interaction: P60903; IntAct: EBI-735711; Score: 0.00
DE  Interaction: P05154; IntAct: EBI-735763; Score: 0.00
DE  Interaction: P11230; IntAct: EBI-736505; Score: 0.00
DE  Interaction: P23508; IntAct: EBI-1064987; Score: 0.00
DE  Interaction: Q99816; IntAct: EBI-2339285; Score: 0.37
DE  Interaction: Q15018; IntAct: EBI-8566862; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-2510150; Score: 0.91
DE  Interaction: Q9C0D3; IntAct: EBI-2510262; Score: 0.40
DE  Interaction: Q6TFL4; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q96SW2; IntAct: EBI-2510262; Score: 0.67
DE  Interaction: Q9UNS2; IntAct: EBI-2510262; Score: 0.88
DE  Interaction: Q96Q07; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q15048; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q96EF6; IntAct: EBI-2510262; Score: 0.67
DE  Interaction: Q13618; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q96M94; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q8WXC6; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: P15374; IntAct: EBI-2510262; Score: 0.40
DE  Interaction: Q13616; IntAct: EBI-2510262; Score: 0.62
DE  Interaction: Q9UBW8; IntAct: EBI-2510262; Score: 0.74
DE  Interaction: Q99627; IntAct: EBI-2510262; Score: 0.85
DE  Interaction: Q8NEZ5; IntAct: EBI-2510262; Score: 0.40
DE  Interaction: Q9P2J3; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q13619; IntAct: EBI-2510262; Score: 0.74
DE  Interaction: Q9H078; IntAct: EBI-2510262; Score: 0.40
DE  Interaction: Q9H4M3; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q9Y3I1; IntAct: EBI-2510262; Score: 0.67
DE  Interaction: Q13620; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q13617; IntAct: EBI-2510262; Score: 0.67
DE  Interaction: Q15369; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q53GT1; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q9UK73; IntAct: EBI-2510262; Score: 0.67
DE  Interaction: B4DN30; IntAct: EBI-2510262; Score: 0.40
DE  Interaction: Q8TBC3; IntAct: EBI-2510262; Score: 0.40
DE  Interaction: Q9H496; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q8TEB1; IntAct: EBI-2510262; Score: 0.67
DE  Interaction: Q13309; IntAct: EBI-2510262; Score: 0.67
DE  Interaction: Q9P2K6; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q13216; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q9NZJ0; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q86XK2; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q92466; IntAct: EBI-2510262; Score: 0.67
DE  Interaction: Q9BW61; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q9BT78; IntAct: EBI-2510262; Score: 0.88
DE  Interaction: Q647K1; IntAct: EBI-2510262; Score: 0.40
DE  Interaction: Q9P2G9; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q9Y597; IntAct: EBI-2510262; Score: 0.40
DE  Interaction: Q9H9Q2; IntAct: EBI-2510262; Score: 0.74
DE  Interaction: P61201; IntAct: EBI-2510262; Score: 0.81
DE  Interaction: Q9Y2M5; IntAct: EBI-2510262; Score: 0.40
DE  Interaction: Q96L50; IntAct: EBI-2510262; Score: 0.67
DE  Interaction: Q13098; IntAct: EBI-2510262; Score: 0.86
DE  Interaction: Q9Y4B6; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q9H0C5; IntAct: EBI-2510262; Score: 0.67
DE  Interaction: P61024; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q5XUX1; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q15843; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q9P2N7; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q93034; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: P24386; IntAct: EBI-2515120; Score: 0.40
DE  Interaction: Q3U1J4; IntAct: EBI-2559059; Score: 0.40
DE  Interaction: A0A6L8PK65; IntAct: EBI-2835415; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q9H3D4; IntAct: EBI-3936407; Score: 0.37
DE  Interaction: P04083; IntAct: EBI-7095166; Score: 0.37
DE  Interaction: P20073; IntAct: EBI-7097023; Score: 0.37
DE  Interaction: P38936; IntAct: EBI-7121191; Score: 0.37
DE  Interaction: Q16659; IntAct: EBI-7206027; Score: 0.37
DE  Interaction: Q16644; IntAct: EBI-7242276; Score: 0.37
DE  Interaction: P31947; IntAct: EBI-5279534; Score: 0.65
DE  Interaction: Q8NHY2; IntAct: EBI-5280877; Score: 0.52
DE  Interaction: Q9UBL3; IntAct: EBI-5654425; Score: 0.00
DE  Interaction: Q02556; IntAct: EBI-6115692; Score: 0.35
DE  Interaction: P12520; IntAct: EBI-6177205; Score: 0.35
DE  Interaction: Q96GG9; IntAct: EBI-21325177; Score: 0.35
DE  Interaction: Q5VW00; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O15061; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q96ME1; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q12951; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9H469; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O94844; IntAct: EBI-21328549; Score: 0.53
DE  Interaction: Q8N1E6; IntAct: EBI-21328549; Score: 0.53
DE  Interaction: P10599; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9H4B7; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P68366; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q01085; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P09234; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P08621; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P60866; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P62244; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P62263; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P05386; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P62917; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q02878; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P36578; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P62899; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P83731; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P62829; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q07020; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q06830; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P13647; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q14568; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O14979; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q99729; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P13639; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P53675; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q07021; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P60709; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q92804; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P62316; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P62701; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P05387; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P62424; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P62913; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q13610; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P11940; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P19338; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O95678; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P38646; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P48741; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P52597; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q05639; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P17844; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O00571; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P61962; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P68371; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9Y3Z3; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P63173; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P36639; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P34931; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9BUJ2; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P31942; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P31943; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P62280; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P61626; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q01546; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q2M2I5; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P12268; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P35637; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P35527; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q01844; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9UQE7; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q71RC2; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q92734; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q6P5R6; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9BRP1; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9H3F6; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P35908; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P04264; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P61081; IntAct: EBI-21328549; Score: 0.53
DE  Interaction: P13645; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q8N1G4; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q96MP8; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q6PI47; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9NXK8; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q53G59; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P22830; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O95219; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q96T23; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P49642; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O60237; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q8NDI1; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9UGM3; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q6P3S6; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q96NC0; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P13521; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q92834; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9H4K1; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q05BQ5; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q8WXI2; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P01042; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9NXE8; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q6IMN6; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9GZY4; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9BYV9; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O75110; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9Y2J4; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q10570; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q15370; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q92673; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q00526; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P78396; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q9NXF7; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q3SXM0; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q8WVD3; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q16531; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O94889; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: O94952; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q5T6F0; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q92624; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q8WV16; IntAct: EBI-21328549; Score: 0.53
DE  Interaction: P24941; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: P20248; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q7Z7A1; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q8N5D0; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q5TAQ9; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q5QP82; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q96JK2; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q8TEL6; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q58WW2; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q9C0C7; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q53HC5; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: P57775; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q9Y297; IntAct: EBI-21332205; Score: 0.56
DE  Interaction: Q9UKB1; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q9UK99; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q8NBE8; IntAct: EBI-21332942; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: P28482; IntAct: EBI-11477267; Score: 0.54
DE  Interaction: Q6UXH8; IntAct: EBI-25277037; Score: 0.56
DE  Interaction: Q8N6Y0; IntAct: EBI-25280965; Score: 0.56
DE  Interaction: Q13515; IntAct: EBI-24539227; Score: 0.56
DE  Interaction: Q15911; IntAct: EBI-24561815; Score: 0.56
DE  Interaction: Q92529; IntAct: EBI-24585832; Score: 0.56
DE  Interaction: O95704; IntAct: EBI-21591300; Score: 0.35
DE  Interaction: Q9BQ90; IntAct: EBI-21622599; Score: 0.35
DE  Interaction: A1L190; IntAct: EBI-21724977; Score: 0.35
DE  Interaction: Q6JEL2; IntAct: EBI-21755575; Score: 0.35
DE  Interaction: O43583; IntAct: EBI-21785701; Score: 0.35
DE  Interaction: Q9UKA1; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q7L5Y6; IntAct: EBI-21846729; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P04156; IntAct: EBI-21014477; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21371036; Score: 0.00
DE  Interaction: P06241; IntAct: EBI-21371020; Score: 0.00
DE  Interaction: Q9BYB0; IntAct: EBI-26513938; Score: 0.37
DE  Interaction: Q15831; IntAct: EBI-28941407; Score: 0.53
GO  GO:0008180;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000338;
GO  GO:0045116;
GO  GO:2000434;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAAAAAAATNGTGGSSGMEVDAAVVPSVMACGVTGSVSVALHPLVILNISDHWIRMRSQEGRPVQVIGALIGKQEGRN
SQ  IEVMNSFELLSHTVEEKIIIDKEYYYTKEEQFKQVFKELEFLGWYTTGGPPDPSDIHVHKQVCEIIESPLFLKLNPMTKH
SQ  TDLPVSVFESVIDIINGEATMLFAELTYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVKLILE
SQ  YVKASEAGEVPFNHEILREAYALCHCLPVLSTDKFKTDFYDQCNDVGLMAYLGTITKTCNTMNQFVNKFNVLYDRQGIGR
SQ  RMRGLFF
//
ID  Q58CQ0;
PN  Protein CUSTOS;
GN  CUSTOS;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}.
DR  UNIPROT: Q58CQ0;
DR  UNIPROT: Q58CS2;
DE  Function: Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0030178;
GO  GO:0060061;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDLESSSSSSSDEEELERCREAALPAWGLEQRPRGPEKPGVDATNAKLPANQPSLMHKVDEHEQDGNELQTTPEFRAHV
SQ  AKKLGALLDSSITISEIVKEPRKSEVQQGALEDDGFRLFFTSIPGGPEKEAAPQPCRKRLPSSSSSDDGDEELRRCREAA
SQ  VSASDILQESAIHGHVSVEKKKKRKLKKKAKKEDSADVAATATSKAEVGRQEKESAQLNGDQAPPGTKKKKRKKKTKKAS
SQ  EASLSPPTKSAAAVPSN
//
ID  A9C3N6;
PN  Protein CUSTOS;
GN  custos;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:P0DPK0}.
DR  UNIPROT: A9C3N6;
DR  UNIPROT: A3KNH5;
DR  UNIPROT: A8WGJ3;
DE  Function: Essential for Spemann-Mangold organizer formation and subsequent anterior head development in the embryo. Inhibits canonical Wnt signaling pathway by antagonizing nuclear import of beta-catenin (ctnnb1) during embryogenesis. {ECO:0000269|PubMed:25157132}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0097065;
GO  GO:0030178;
GO  GO:0060061;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSESSSEDENTARLKEAVWSFKPEDVKINGKENNGRQSHRADVSKHEHDGNELGTTPEFRSHVAKKLGTYLDGCISEVCS
SQ  DTVEPAQSENREDEEGFRLFSSSTPGKWMEQSPPPPPKRRPVPSSSDSDSEMEMRFREAAVSLSDILGPVAQNLSEKTEE
SQ  KSTKEETEDTVTKMKKKKKRKTSSEESQDKVNHQTEKQSNVEGNQEQTTAGERLKKKKKKKKKKRKKLEKDIKKDE
//
ID  Q96C57;
PN  Protein CUSTOS;
GN  CUSTOS;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}.
DR  UNIPROT: Q96C57;
DR  UNIPROT: Q53HF0;
DR  UNIPROT: Q9H9Z7;
DR  DisGeNET: 64897;
DE  Function: Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}.
DE  Reference Proteome: Yes;
DE  Interaction: P0DTD1; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: P59595; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P54274; IntAct: EBI-11305569; Score: 0.51
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: P48426; IntAct: EBI-21630443; Score: 0.35
DE  Interaction: Q9HBM1; IntAct: EBI-21702723; Score: 0.35
DE  Interaction: Q8N128; IntAct: EBI-21714042; Score: 0.35
DE  Interaction: O95619; IntAct: EBI-21747731; Score: 0.35
DE  Interaction: Q9UQB9; IntAct: EBI-21807494; Score: 0.35
DE  Interaction: Q00537; IntAct: EBI-21871053; Score: 0.35
DE  Interaction: Q6NXT4; IntAct: EBI-21889655; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-27129711; Score: 0.35
DE  Interaction: P15130; IntAct: EBI-27131516; Score: 0.35
DE  Interaction: Q0ZME3; IntAct: EBI-27131755; Score: 0.35
DE  Interaction: Q6Q1R8; IntAct: EBI-27132003; Score: 0.35
DE  Interaction: K9N4V7; IntAct: EBI-27132270; Score: 0.35
DE  Interaction: P33469; IntAct: EBI-27132272; Score: 0.35
GO  GO:0005635;
GO  GO:0030178;
GO  GO:0060061;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAPSGTVSDSESSNSSSDAEELERCREAAMPAWGLEQRPHVAGKPRAGAANSQLSTSQPSLRHKVNEHEQDGNELQTTP
SQ  EFRAHVAKKLGALLDSFITISEAAKEPAKAKVQKVALEDDGFRLFFTSVPGGREKEESPQPRRKRQPSSSSEDSDEEWRR
SQ  CREAAVSASDILQESAIHSPGTVEKEAKKKRKLKKKAKKVASVDSAVAATTPTSMATVQKQKSGELNGDQVSLGTKKKKK
SQ  AKKASETSPFPPAKSATAIPAN
//
ID  Q3UY34;
PN  Protein CUSTOS;
GN  Custos;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}.
DR  UNIPROT: Q3UY34;
DR  UNIPROT: Q3TX98;
DR  UNIPROT: Q8K0K9;
DR  UNIPROT: Q9CVB7;
DE  Function: Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0030178;
GO  GO:0060061;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVAPSGAMSDSENSSSSSSDAEELARCREAATPAWGLEQRPGAAERPEAGAADKQAPTPQPSRRHEVNQHEEDGNDLRTT
SQ  PEFRAHVAKKLGALLDSSIAIAEVWKKSQKAKMQQVAKEEDGFRLFFTSIPGGHKKEASPRPCRKRQPPSSSEDSDEELQ
SQ  RCREAAVSASDILQESAIHCPAKAEEKKKLKKKAKKKVDNADLAAAPGLEQVKEAGVVNGDPVSLGIQKKRKKKAKKSRE
SQ  APLCPPAECAAAKPEN
//
ID  Q5I034;
PN  Protein CUSTOS;
GN  Custos;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}.
DR  UNIPROT: Q5I034;
DE  Function: Plays a role in the regulation of Wnt signaling pathway during early development. {ECO:0000250|UniProtKB:A9C3N6}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0030178;
GO  GO:0060061;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVAPSGAMSDSESSSSDSSDAEELARCREAATPAWGLEQRPREAERPAAGTADTQAPAPQPSRRREVNQHDEDGNELQTT
SQ  PEFRAYVAKKLGALLDSSIAIAEVWKKTQQARLQQEAKEQQEAKEQQAAKEEQAAKKEEDGFRLFFTSVPGGHEKEASPR
SQ  PCRKRQPPSSSEDSDEELQRCREAAVSASDILQESAIHCPAKVEKEAEKKKLKKKAKKKADADLAAATGLEQVKEAGSVN
SQ  GDPVLSGTKKKKKKKAKKAREASLCPPAECAAAEPKN
//
ID  P0DPK0;
PN  Protein CUSTOS;
GN  custos;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:25157132}.
DR  UNIPROT: P0DPK0;
DE  Function: Essential for Spemann-Mangold organizer formation and subsequent anterior head development in the embryo. Inhibits canonical Wnt signaling pathway by antagonizing nuclear import of beta-catenin (ctnnb1) during embryogenesis. {ECO:0000269|PubMed:25157132}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0030178;
GO  GO:0060061;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAPRRGTQKSDSDSSDEDLDRFREAAWVPPGAHQKVSDEQNEKIALPSLRVRPDCHEHDGNELQTTPEFRSHVAKKLAA
SQ  ILDSSIREVSQNEAVHISKAGNGDSEDEGFRLFRTSLPGEAGIVTSTIPRRKLASSSSEDSEEEQQRCREAAVSACDILR
SQ  HSTLQQEPQSTPSNVCDNQPPKKKRKKKKKDRGDTSQINSVEETMHIEPGKNELQAKRKKKKKQKLEMAHCDELGNE
//
ID  O43310;
PN  CBP80/20-dependent translation initiation factor;
GN  CTIF;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19648179}.
DR  UNIPROT: O43310;
DR  UNIPROT: B3KTR8;
DR  UNIPROT: Q8IVD5;
DR  Pfam: PF02854;
DR  OMIM: 613178;
DR  DisGeNET: 9811;
DE  Function: Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subunit of the ribosome via eIF3. In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD). {ECO:0000269|PubMed:19648179}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A2U2H131; IntAct: EBI-2866199; Score: 0.00
DE  Interaction: Q86VS8; IntAct: EBI-24326289; Score: 0.56
DE  Interaction: Q9NZD8; IntAct: EBI-24333116; Score: 0.56
DE  Interaction: Q96MH2; IntAct: EBI-24352467; Score: 0.56
DE  Interaction: Q6P9E2; IntAct: EBI-24373771; Score: 0.56
DE  Interaction: Q9NUU7; IntAct: EBI-24377593; Score: 0.67
DE  Interaction: A9UHW6; IntAct: EBI-24392534; Score: 0.56
DE  Interaction: Q8N5M1; IntAct: EBI-24400192; Score: 0.56
DE  Interaction: Q9UMR2; IntAct: EBI-25260673; Score: 0.56
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0008494;
GO  GO:0000184;
GO  GO:0006446;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENSSAASASSEAGSSRSQEIEELERFIDSYVLEYQVQGLLADKTEGDGESERTQSHISQWTADCSEPLDSSCSFSRGRA
SQ  PPQQNGSKDNSLDMLGTDIWAANTFDSFSGATWDLQPEKLDFTQFHRKVRHTPKQPLPHIDREGCGKGKLEDGDGINLND
SQ  IEKVLPAWQGYHPMPHEVEIAHTKKLFRRRRNDRRRQQRPPGGNKPQQHGDHQPGSAKHNRDHQKSYQGGSAPHPSGRPT
SQ  HHGYSQNRRWHHGNMKHPPGDKGEAGAHRNAKETMTIENPKLEDTAGDTGHSSLEAPRSPDTLAPVASERLPPQQSGGPE
SQ  VETKRKDSILPERIGERPKITLLQSSKDRLRRRLKEKDEVAVETTTPQQNKMDKLIEILNSMRNNSSDVDTKLTTFMEEA
SQ  QNSTNSEEMLGEIVRTIYQKAVSDRSFAFTAAKLCDKMALFMVEGTKFRSLLLNMLQKDFTVREELQQQDVERWLGFITF
SQ  LCEVFGTMRSSTGEPFRVLVCPIYTCLRELLQSQDVKEDAVLCCSMELQSTGRLLEEQLPEMMTELLASARDKMLCPSES
SQ  MLTRSLLLEVIELHANSWNPLTPPITQYYNRTIQKLTA
//
ID  Q6PEE2;
PN  CBP80/20-dependent translation initiation factor;
GN  Ctif;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q6PEE2;
DR  UNIPROT: Q6A069;
DR  Pfam: PF02854;
DE  Function: Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subunit of the ribosome via eIF3. In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0008494;
GO  GO:0000184;
GO  GO:0006446;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENSSAASASSEAGSSRSQEIEELERFIDSYVLEYQVQGLLTDKTEGDGESQRTQSHISQWTADCREQLDGSCSFSRGRA
SQ  PPQQNGNKDNSLDMLGTDIWAANTFDSFSGATWDLQPEKLDFTQFHRKVRHTPKQPLPHIDREGCGKGKLEDGDGISLND
SQ  IEKVLPTWQGYHPMPHEAEIAHTKKLFRRRRNDRRRQQRPPGGNKPQQHGDHQPGSAKHNRDHQKSYQGGSGPHPSGRPT
SQ  HHGYSQNRRWHHGNMKHPPGDKGEAGSHRNAKETVTVENPKLEDGPGDTGHSGLEPPCSPDTLTPAASERPTPQLPGGPE
SQ  AEIKHKDTVLPERLRERPKITLLQSSKDRLRRRLKEKDRDEVAVETSSPQPSKMDRLMEILNIMRNNSSDVDAKLTSFME
SQ  EAQNSTNSEEMLGEIVRTIYQKAVSDRSFAFTAAKLCDKMALFMVEGTKFRSLLLNMLQKDFTVREELQQQDVERWLGFI
SQ  TFLCEVFGTMRSSTGEPFRVLVCPIYTCLRELLQSQDVKEDAVLCCSMELQSTGRLLEEQLPEMMTELLASARDKMLCPS
SQ  ESMLTRSLLLEVIELHANSWNPLTPPITQYYNRTIQKLTA
//
ID  Q0V9S3;
PN  CBP80/20-dependent translation initiation factor;
GN  ctif;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q0V9S3;
DR  Pfam: PF02854;
DE  Function: Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0008494;
GO  GO:0000184;
GO  GO:0006446;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESSSVASASSEAGSSRSLEIEELERFIDSYVLEYQVQGLLTDKTEGDGESDKTQSNVSQWTVECTERLEENRTSPRNRE
SQ  PTYSQNGNKEGPLDMLGTDIWAASTVESISGATWDLQPEKLDFTQLQLRQRNSPKHPPPQIDRDGFGKGKRVEGDDINLN
SQ  DIEKVLPTWQGYSPLPHEADIAQTKKLFRRKRNDRRKQQKPQGGNKQPPSQQNDHQPATAKHNSREHQRQYHGNPPPPHP
SQ  SGKQGHHGYSQNRRWHHNQKHLPNDLQRNAKETDTLKIEDASVCTVHIPLDIHSNTDSTERHCPPANDSEAKRKESIQSR
SQ  DRPKISLLQSSKDRLRRRLKEKEDVAVESTNPQKTKMDKLIEILNSMRNNSSDVDYKLTTFMAEAQNSANSEEMLGEIVK
SQ  TIYQKAVTDRSFAHTAAKLCDRMALFMVEGTKFRSLLLNMLQKDFSIREEMHRSDVERWLGFITFLCEVFGTMRSNMAEP
SQ  FRVLVCPIYTCLRELLQSEDVKEDAVLCCSMELQSAGRLLEDQLPEMMSELLATARDKMLCPSESMLTRSLLLEVIELHA
SQ  NSWNPLTPTITQYYNKTIQKLTG
//
ID  Q14999;
PN  Cullin-7;
GN  CUL7;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Golgi apparatus. Note=Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. During mitosis, localizes to the mitotic apparatus (PubMed:24793695). CCDC8 is required for centrosomal location (PubMed:24793695). {ECO:0000269|PubMed:24793695}.
DR  UNIPROT: Q14999;
DR  UNIPROT: B4DYZ0;
DR  UNIPROT: F5H0L1;
DR  UNIPROT: Q5T654;
DR  PDB: 2JNG;
DR  Pfam: PF03256;
DR  Pfam: PF11515;
DR  Pfam: PF00888;
DR  PROSITE: PS50069;
DR  PROSITE: PS51284;
DR  OMIM: 273750;
DR  OMIM: 609577;
DR  DisGeNET: 9820;
DE  Function: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695). Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5 (PubMed:24793696). Core component of a Cul7-RING ubiquitin-protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1 (PubMed:21572988, PubMed:24362026). Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) (PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation (PubMed:24362026). Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development (PubMed:20139075). Does not promote polyubiquitination and proteasomal degradation of p53/TP53 (PubMed:16547496, PubMed:17332328). While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions. {ECO:0000269|PubMed:16547496, ECO:0000269|PubMed:17332328, ECO:0000269|PubMed:18498745, ECO:0000269|PubMed:20139075, ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24362026, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.
DE  Disease: 3M syndrome 1 (3M1) [MIM:273750]: An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies. {ECO:0000269|PubMed:16142236, ECO:0000269|PubMed:17675530, ECO:0000269|PubMed:23018678}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: O75147; IntAct: EBI-15927148; Score: 0.54
DE  Interaction: P00519; IntAct: EBI-1958704; Score: 0.40
DE  Interaction: P0C6X4; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P0C6X5; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P0C6X6; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: P29991; IntAct: EBI-8826732; Score: 0.37
DE  Interaction: Q9ULL4; IntAct: EBI-311651; Score: 0.37
DE  Interaction: Q96KG7; IntAct: EBI-308874; Score: 0.37
DE  Interaction: P04637; IntAct: EBI-1781603; Score: 0.83
DE  Interaction: P07939; IntAct: EBI-6159787; Score: 0.35
DE  Interaction: Q16539; IntAct: EBI-6256566; Score: 0.35
DE  Interaction: Q15759; IntAct: EBI-6381006; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21331736; Score: 0.35
DE  Interaction: Q99IB8; IntAct: EBI-6928202; Score: 0.37
DE  Interaction: Q7TSJ6; IntAct: EBI-8797641; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-8835658; Score: 0.35
DE  Interaction: P48039; IntAct: EBI-11576948; Score: 0.00
DE  Interaction: B4URF7; IntAct: EBI-12589250; Score: 0.35
DE  Interaction: Q12798; IntAct: EBI-21576600; Score: 0.35
DE  Interaction: O14958; IntAct: EBI-21622768; Score: 0.35
DE  Interaction: Q08380; IntAct: EBI-21628119; Score: 0.35
DE  Interaction: O60293; IntAct: EBI-21634559; Score: 0.35
DE  Interaction: Q9UBZ4; IntAct: EBI-21640250; Score: 0.35
DE  Interaction: Q9H9D4; IntAct: EBI-21642543; Score: 0.35
DE  Interaction: D6R9G5; IntAct: EBI-21662389; Score: 0.35
DE  Interaction: P04004; IntAct: EBI-21709311; Score: 0.35
DE  Interaction: O14978; IntAct: EBI-21712468; Score: 0.35
DE  Interaction: Q16385; IntAct: EBI-21766591; Score: 0.35
DE  Interaction: Q96BR6; IntAct: EBI-21784034; Score: 0.35
DE  Interaction: Q9NXS3; IntAct: EBI-21857519; Score: 0.35
DE  Interaction: Q92990; IntAct: EBI-21884908; Score: 0.35
DE  Interaction: Q8N3Y1; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: Q13557; IntAct: EBI-16812871; Score: 0.35
DE  Interaction: Q13322; IntAct: EBI-25382050; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574619; Score: 0.35
DE  Interaction: Q9H9E1; IntAct: EBI-26656693; Score: 0.35
DE  Interaction: Q9UNH5; IntAct: EBI-27113106; Score: 0.40
DE  Interaction: Q15375; IntAct: EBI-32718158; Score: 0.42
GO  GO:1990393;
GO  GO:0005680;
GO  GO:0005813;
GO  GO:0031467;
GO  GO:0031461;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0031625;
GO  GO:0001837;
GO  GO:0007030;
GO  GO:0000226;
GO  GO:0000281;
GO  GO:0001890;
GO  GO:0050775;
GO  GO:0016567;
GO  GO:0006508;
GO  GO:0007088;
GO  GO:0006511;
GO  GO:0001570;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVGELRYREFRVPLGPGLHAYPDELIRQRVGHDGHPEYQIRWLILRRGDEGDGGSGQVDCKAEHILLWMSKDEIYANCHK
SQ  MLGEDGQVIGPSQESAGEVGALDKSVLEEMETDVKSLIQRALRQLEECVGTIPPAPLLHTVHVLSAYASIEPLTGVFKDP
SQ  RVLDLLMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLSEHPMSFEGI
SQ  QLPQVPGRVLFSLVKRYLHVTSLLDQLNDSAAEPGAQNTSAPEELSGERGQLELEFSMAMGTLISELVQAMRWDQASDRP
SQ  RSSARSPGSIFQPQLADVSPGLPAAQAQPSFRRSRRFRPRSEFASGNTYALYVRDTLQPGMRVRMLDDYEEISAGDEGEF
SQ  RQSNNGVPPVQVFWESTGRTYWVHWHMLEILGFEEDIEDMVEADEYQGAVASRVLGRALPAWRWRPMTELYAVPYVLPED
SQ  EDTEECEHLTLAEWWELLFFIKKLDGPDHQEVLQILQENLDGEILDDEILAELAVPIELAQDLLLTLPQRLNDSALRDLI
SQ  NCHVYKKYGPEALAGNQAYPSLLEAQEDVLLLDAQAQAKDSEDAAKVEAKEPPSQSPNTPLQRLVEGYGPAGKILLDLEQ
SQ  ALSSEGTQENKVKPLLLQLQRQPQPFLALMQSLDTPETNRTLHLTVLRILKQLVDFPEALLLPWHEAVDACMACLRSPNT
SQ  DREVLQELIFFLHRLTSVSRDYAVVLNQLGARDAISKALEKHLGKLELAQELRDMVFKCEKHAHLYRKLITNILGGCIQM
SQ  VLGQIEDHRRTHQPINIPFFDVFLRYLCQGSSVEVKEDKCWEKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHM
SQ  RRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHTELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTR
SQ  IRGLEILGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDMAEDRRSLLHLSSRLNGALRQEQNFADRFLPDDEAAQALGK
SQ  TCWEALVSPVVQNITSPDEDGISPLGWLLDQYLECQEAVFNPQSRGPAFFSRVRRLTHLLVHVEPCEAPPPVVATPRPKG
SQ  RNRSHDWSSLATRGLPSSIMRNLTRCWRAVVEKQVNNFLTSSWRDDDFVPRYCEHFNILQNSSSELFGPRAAFLLALQNG
SQ  CAGALLKLPFLKAAHVSEQFARHIDQQIQGSRIGGAQEMERLAQLQQCLQAVLIFSGLEIATTFEHYYQHYMADRLLGVV
SQ  SSWLEGAVLEQIGPCFPNRLPQQMLQSLSTSKELQRQFHVYQLQQLDQELLKLEDTEKKIQVGLGASGKEHKSEKEEEAG
SQ  AAAVVDVAEGEEEEEENEDLYYEGAMPEVSVLVLSRHSWPVASICHTLNPRTCLPSYLRGTLNRYSNFYNKSQSHPALER
SQ  GSQRRLQWTWLGWAELQFGNQTLHVSTVQMWLLLYLNDLKAVSVESLLAFSGLSADMLNQAIGPLTSSRGPLDLHEQKDI
SQ  PGGVLKIRDGSKEPRSRWDIVRLIPPQTYLQAEGEDGQNLEKRRNLLNCLIVRILKAHGDEGLHIDQLVCLVLEAWQKGP
SQ  CPPRGLVSSLGKGSACSSTDVLSCILHLLGKGTLRRHDDRPQVLSYAVPVTVMEPHTESLNPGSSGPNPPLTFHTLQIRS
SQ  RGVPYASCTATQSFSTFR
//
ID  Q8VE73;
PN  Cullin-7;
GN  Cul7;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. During mitosis, localizes to the mitotic apparatus. CCDC8 is required for centrosomal location (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8VE73;
DR  UNIPROT: Q3UHY3;
DR  UNIPROT: Q497I2;
DR  UNIPROT: Q6A0D6;
DR  UNIPROT: Q6PB63;
DR  UNIPROT: Q8R3W4;
DR  UNIPROT: Q9CVD5;
DR  Pfam: PF03256;
DR  Pfam: PF11515;
DR  Pfam: PF00888;
DR  PROSITE: PS01256;
DR  PROSITE: PS50069;
DR  PROSITE: PS51284;
DE  Function: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5. Core component of a Cul7-RING ubiquitin- protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1. Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain. Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Acts as a regulator in trophoblast cell epithelial- mesenchymal transition and placental development. Does not promote polyubiquitination and proteasomal degradation of p53/TP53. While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions (By similarity). Probably plays a role in the degradation of proteins involved in endothelial proliferation and/or differentiation. {ECO:0000250, ECO:0000269|PubMed:12904573}.
DE  Reference Proteome: Yes;
GO  GO:1990393;
GO  GO:0005813;
GO  GO:0031467;
GO  GO:0031461;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0031625;
GO  GO:0001837;
GO  GO:0007030;
GO  GO:0000226;
GO  GO:0000281;
GO  GO:0001890;
GO  GO:0050775;
GO  GO:0016567;
GO  GO:0045601;
GO  GO:0007088;
GO  GO:0006511;
GO  GO:0001570;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVGELRYREFRVPLGPGLHAYPDELIRQRVGHNGHPEYQIRWLILRRGDDGDRDSTVDCKAEHILLWMSDDEIYANCHKM
SQ  LGENGQVIAPSRESTEAGALDKSVLGEMETDVKSLIQRALRQLEECVGTVPPAPLLHTVHVLSAYASIEPLTGIFKDRRV
SQ  VNLLMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLTEHPMSFEGVQL
SQ  PQVPGRLLFSLVKRYLHVTFLLDRLNGDAGDQGAQNNFIPEELNVGRGRLELEFSMAMGTLISELVQAMRWDGASSRPES
SQ  SSSSTFQPRPAQFRPYTQRFRRSRRFRPRASFASFNTYALYVRDTLRPGMRVRMLENYEEIAAGDEGQFRQSNDGVPPAQ
SQ  VLWDSTGHTYWVHWHMLEILGFEEDIEDVIDIEELQELGANGALSIVPPSQRWKPITQLFAEPYVVPEEEDREESENLTQ
SQ  AEWWELLFFIRQLSEAERLHIVDLLQDHLEEERVLDYDMLPELTVPVDLAQDLLLSLPQQLEDSALRDLFSCSVYRKYGP
SQ  EVLVGHLSYPFVPGAQPNLFGANEESEAKDPPLQSASPALQRLVESLGPEGEVLVELEQALGSEAPQETEVKSCLLQLQE
SQ  QPQPFLALMRSLDTSASNKTLHLTVLRILMQLVNFPEALLLPWHEAMDACVTCLRSPNTDREVLQELIFFLHRLTTTSRD
SQ  YAVILNQLGARDAISKVLEKHRGKLELAQELRDMVSKCEKHAHLYRKLTTNILGGCIQMVLGQIEDHRRTHRPIQIPFFD
SQ  VFLRYLCQGSSEEMKKNRYWEKVEVSSNPQRASRLTDRNPKTYWESSGRAGSHFITLHMRPGVIIRQLTLLVAGEDSSYM
SQ  PAWVVVCGGNSIKSVNKELNTVNVMPSASRVTLLENLTRFWPIIQIRIKRCQQGGINTRIRGLEVLGPKPTFWPVFREQL
SQ  CRHTRLFYMVRAQAWSQDIAEDRRSLLHLSSRLNGALRHEQNFAERFLPDMEAAQALSKTCWEALVSPLVQNITSPDEDS
SQ  TSSLGWLLDQYLGCREAAYNPQSRAAAFSSRVRRLTHLLVHVEPREAAPPVVAIPRSKGRNRIHDWSYLITRGLPSSIMK
SQ  NLTRCWRSVVEEQMNKFLTASWKDDDFVPRYCERYYVLQKSSSELFGPRAAFLLAMRNGCADAVLRLPFLRAAHVSEQFA
SQ  RHIDQRIQGSRMGGARGMEMLAQLQRCLESVLIFSPLEIATTFEHYYQHYMADRLLSVGSSWLEGAVLEQIGPCFPSRLP
SQ  QQMLQSLNVSEELQRQFHVYQLQQLDQELLKLEDTEKKIQVAHEDSGREDKSKKEEAIGEAAAVAMAEEEDQGKKEEGEE
SQ  EGEGEDEEEERYYKGTMPEVCVLVVTPRFWPVASVCQMLNPATCLPAYLRGTINHYTNFYSKSQSRSSLEKEPQRRLQWT
SQ  WQGRAEVQFGGQILHVSTVQMWLLLHLNNQKEVSVESLQAISELPPDVLHRAIGPLTSSRGPLDLQEQKNVPGGVLKIRD
SQ  DSEEPRPRRGNVWLIPPQTYLQAEAEEGRNMEKRRNLLNCLVVRILKAHGDEGLHVDRLVYLVLEAWEKGPCPARGLVSS
SQ  LGRGATCRSSDVLSCILHLLVKGTLRRHDDRPQVLYYAVPVTVMEPHMESLNPGSAGPNPPLTFHTLQIRSRGVPYASCT
SQ  DNHTFSTFR
//
ID  Q5RCJ3;
PN  Cullin-7;
GN  CUL7;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. During mitosis, localizes to the mitotic apparatus. CCDC8 is required for centrosomal location (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5RCJ3;
DR  Pfam: PF03256;
DR  Pfam: PF11515;
DR  Pfam: PF00888;
DR  PROSITE: PS50069;
DR  PROSITE: PS51284;
DE  Function: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5. Core component of a Cul7-RING ubiquitin- protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1. Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain. Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Acts as a regulator in trophoblast cell epithelial- mesenchymal transition and placental development. Does not promote polyubiquitination and proteasomal degradation of p53/TP53. While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:1990393;
GO  GO:0005813;
GO  GO:0031467;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0031625;
GO  GO:0001837;
GO  GO:0007030;
GO  GO:0000226;
GO  GO:0000281;
GO  GO:0001890;
GO  GO:0050775;
GO  GO:0016567;
GO  GO:0007088;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVGELRYREFRVPLGPGLHAYPDELIRQRVGHDGHPEYQIRWLILRRGDEGDGGSGQVDCKAEHILLWMSKDEIYANCHK
SQ  MLGEDGQVIGPSQESTGEVGALDKSVLEEMETDVKSLIQRALRQLEECVGTIPPAPLLHTVHVLSAYASIEPLTGVFKDP
SQ  RVLDLLMHMLSSPDYQIRWSAGRMIQALSSHDAGEGQCGEEGKAGEELGRLRDSQDTVAGASDLIRTRTQILLSLSQQEA
SQ  IEKHLDFDSRCALLALFAQATLSEHPMSFEGIQLPQVPGRVLFSLVKRYLHVTSLLDQLNDSAAEPGAQNTSAPEEWSGE
SQ  RGQLELEFSMAMGTLISELVQAIRWDQASDRPRSSARSPGSIFQPQLADVSPGLPATQAQPSFRRSRHFRPRSEFASGNT
SQ  YALYVRDTLQPGMRVRMLDEYEEISAGDEGEFRQSNNGVPPVQVLWESTGRTYWVHWHMLEILGFEEDIEDMVEADEYQG
SQ  AVASRVLGRALPAWRWRPMTELYAVPYVLPEDEDSEECEHLTLAEWWELLFFIKKLDGPDHQEVLQILQENLDGEILDDE
SQ  ILAELAVPIELAQDLLLTLPQRLNDSALRDLINCHVYKKYGPEALAGNPAYPSLLEAQEDVLLEAQAQAKDSEDAAKVEA
SQ  KEPPSQSPNTPLQRLVEGYGPAGKILLDLEQALSSEGTQENKVKPLLLQLQRQPQPFLALMQSLDTPETNRTLHLTVLRI
SQ  LKQLVDFPEALLLPWHEAVDACMACLRSPNTDREVLQELIFFLHRLTSVSRDYAVVLNQLGARDAISKALEKHLGKLELA
SQ  QELRDMVFKCEKHAHLYRELITNILGGCIQMVLGQIEDHRRTHRPINIPFFDVFLRYLCQGSSVEVKEDKCWEKVEVSSN
SQ  PHRASKLTDRNPKTYWESNGSAGSRYITLHMRQGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHTELNSVNVMPSA
SQ  SRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLETLGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDMAEDRRSLLH
SQ  LSSRLNGALRQEQNFADRFLPDNEAAQALGKTCWEALVSPVVQNITSPDEDGISPLGWLLDQYLECQEAVFNPQSRGPAF
SQ  FSRVRRLTHLLVHVEPCEAPPPVVATPRPKGRNRSHDWSSLATRGLPSSIMRNLTRCRRAVVEKQVNNFLTSSWRDDDFV
SQ  PRYCEHFNILQNSSSELFGPRAAFLLALQNGCAGALLKLPFLKAAHVSEQFARHIDQQIQGSRIGGAQEMERLAQLQQCL
SQ  QAVLIFSGLEIATTFEHYYQHYMADRLLGVVSSWLEGAVLEQIGPCFPNRLPQQMLQSLSTSKELQRQFHVYQLQQLDQE
SQ  LLKLEDTEKKIQVGHGASGKEHKSEKEEEAGAAAAVDVAEGEEEEEENEDLYYEGAMPEVSVLVLSRHCWPVASICHTLN
SQ  PRTCLPSYLRGTLNRYSNFYNKSQSHPALERGSQRRLQWTWLGWAELQFGNQTLHVSTVQMWLLLYLNDLKAVSVESLLA
SQ  LSGLSADMLNQAIGPLTSSRGPLDLHEQKDIPGGVLKIRDGSKEPRSRWDIVRLIPPQTYLQAEGEEGRNLEKRRNLLNC
SQ  LIVRILKAHGDEGLHIDQLVCLVLEAWQKGPCPPRGLVSSLGKGSACSSTDVLSCILHLLGKGTLRRHDDRPQVLSYAVP
SQ  VTVMEPHTESLNPGSSGPNPPLTFHTVQIRSRGVPYASCTATQSFSTFR
//
ID  D3ZEF4;
PN  Cullin-7;
GN  Cul7;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:21572988}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21572988}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=During mitosis, localizes to the mitotic apparatus. CCDC8 is required for centrosomal location (By similarity). Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. {ECO:0000250}.
DR  UNIPROT: D3ZEF4;
DR  Pfam: PF03256;
DR  Pfam: PF11515;
DR  Pfam: PF00888;
DR  PROSITE: PS50069;
DR  PROSITE: PS51284;
DE  Function: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5. Core component of a Cul7-RING ubiquitin- protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1. Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development. Does not promote polyubiquitination and proteasomal degradation of p53/TP53. While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions (By similarity). {ECO:0000250, ECO:0000269|PubMed:21572988}.
DE  Reference Proteome: Yes;
DE  Interaction: P0DL28; IntAct: EBI-15927289; Score: 0.40
DE  Interaction: Q9BYV6; IntAct: EBI-21998606; Score: 0.35
GO  GO:1990393;
GO  GO:0005813;
GO  GO:0031467;
GO  GO:0031461;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0031625;
GO  GO:0001837;
GO  GO:0007030;
GO  GO:0000226;
GO  GO:0000281;
GO  GO:0001890;
GO  GO:0050775;
GO  GO:0016567;
GO  GO:0007088;
GO  GO:0006511;
GO  GO:0001570;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVGELRYREFRVPLGPGLHAYPDELIRQRVGHNGHPEYQIRWLILRRGDDGDSSQVDCKAEHILLWMTDDEIYANCHKML
SQ  GEDGQVIRPSQESAEAGALDKSVLGEMETDVKSLIQRALRQLEECVGAVPPAPLLHTVHVLSAYASIEPLTGVFKDRRVL
SQ  DLVMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLTEHPMSFEGVQLP
SQ  QVPGRLLFSLVKRYLCVTFLLDRLNGNAEDQDAQNNFIPEELNAGRGRVELEFSMAMGTLISELVQAMRWDWASSRSESS
SQ  SPIFQPPPTEFFRPRAQRFRRSRRFRPRTAFASVNTYALYVRDTLRPGMRVRMLEDFEEISAGDEGQFRQSNDGMPPVQV
SQ  LWDSTGHTYWVHWHMLEILGFEEDIEDVVDIDDQGAMVHGGLGVAPPFQHWKPIAQLFAEPYVVPEEEDREEREHLTQAE
SQ  WWELFFFIKKLNAEERQHVVELLQEFLEGEHVLDFEILPELTVPVELAQDLMLSLPQQLDDSALRDLFNCYVYRKYGPEV
SQ  LVGKRNRPFVLDDQLNLFRIETDSEAQDPPSQSASPALRQLVEGLGPSGKLLVDLERALSSEAPQENEVKPCLLQLQEEP
SQ  QPFLTLMRSLDTPASNKALHLTALRILMQLVNFPEALLLPWHEAMDACMTCLRSPNTDREVLQELIFFLHRLTSTSRDYA
SQ  VILNQLGARDAISKVLEKHRGKLELAQELRDMVFKCEKHAHLYRKLTTNILGGCIQMVLGQIEDHRRTHRPIQIPFFDVF
SQ  LRYLCQGSSAEVKKNKYWEKVEVSSNPHRASRLTDRNAKTYWESNGTAGSHFITVHMRPGVLIRQLTLLVAGEDSSYMPA
SQ  WVVVCGGDSISSVNTELNAVNVMPHASRVILLENLTRFWPIVQIRIKRCQQGGINTRIRGLEVLGPKPTFWPVFREQLCR
SQ  HTRLFYMVRAQAWSQDIAEDRRSLLHLSSRLNGALRQEQNFADRFLPDEEAALALSKTCWEALVSPLVQNITSPDEDSTS
SQ  SLGWLLNQYLECREAAYNPQSRAAAFSSRVRHLTHLLVHVEPCEAAPPVVAISQSKGRNRSHDWSSLTTRGLPSSIMRNL
SQ  TRCWRSVVEEQVNKFLTSSWKDDDFVPRYCERYYILQKSSSELFGPRAAFLLAMRNGCADALLRLPFLRAAHVSEQFARH
SQ  IDQRIQGSRMGGARGMEMLAQLQRCLESVLILSPLEIATTFEHYYQHYMADRLLSVGSSWLEGAVLEQIGPCFPGRLPQQ
SQ  MLQTLNISEELQRRFHVYQLQQLDQELLKLEDTEKKIQVAHEDSGKEHKSKKEDAAGETAAVAMADEEEEEGKKEEGEEE
SQ  EGEGEEELEEEEERYYEGTMPEVCVLVLSPRFWPVASVCHMLNPTTCLPSYLRGTINHYSNFYSKSQSHSGLEKESPRQL
SQ  QWTWQGRAEVQFGDQILHVSTVQMWLLLHLNHLKAVSVESLQALSELPPEVLNKAIGPLTSSRGPLDLQEQKNIPGGVLK
SQ  IRDDSEEPRPRRGNVWLIPPQTYLKAEDEEGRNLEKRRNLLNCLVVRILKAHGDEGLHIDQLVHLVLEAWEKGPCPPRGL
SQ  VSSLGRGAACRSSDVLSCILHLLGKGTLRRHDDRPQMLFYAVPITVMEPHTESLNPGSSGPNPPLTFHTLQIRSRGVPYA
SQ  SCTGTQTFSTFR
//
ID  P38937;
PN  Tethering factor for nuclear proteasome cut8;
GN  cut8;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:11084332, ECO:0000269|PubMed:28974540}.
DR  UNIPROT: P38937;
DR  PDB: 3Q5W;
DR  PDB: 3Q5X;
DR  Pfam: PF08559;
DE  Function: Together with nucleoporin alm1, tethers the proteasome to the nuclear envelope (PubMed:28974540, PubMed:11084332, PubMed:16096059). Involved in ubiquitin-mediated protein degradation and facilitates the degradation of nuclear proteins like mitotic cyclin and cut2 (PubMed:11084332, PubMed:16096059). Required for normal progression of anaphase (PubMed:8065367, PubMed:11084332). {ECO:0000269|PubMed:11084332, ECO:0000269|PubMed:16096059, ECO:0000269|PubMed:28974540, ECO:0000269|PubMed:8065367}.
DE  Reference Proteome: Yes;
DE  Interaction: P50524; IntAct: EBI-1152618; Score: 0.52
DE  Interaction: P41878; IntAct: EBI-1152637; Score: 0.40
DE  Interaction: P87048; IntAct: EBI-1152745; Score: 0.54
DE  Interaction: P40303; IntAct: EBI-1152891; Score: 0.40
DE  Interaction: P23566; IntAct: EBI-1153015; Score: 0.43
DE  Interaction: P38937; IntAct: EBI-15946480; Score: 0.62
GO  GO:0000785;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005634;
GO  GO:0042802;
GO  GO:0032934;
GO  GO:0034080;
GO  GO:0071630;
GO  GO:0031144;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METLSYSQIKKRKADFDEDISKRARQLPVGEQLPLSRLLQYSDKQQLFTILLQCVEKHPDLARDIRGILPAPSMDTCVET
SQ  LRKLLINLNDSFPYGGDKRGDYAFNRIREKYMAVLHALNDMVPCYLPPYSTCFEKNITFLDAATNVVHELPEFHNPNHNV
SQ  YKSQAYYELTGAWLVVLRQLEDRPVVPLLPLEELEEHNKTSQNRMEEALNYLKQLQKNEPLVHERSHTFQQTNPQNNFHR
SQ  HTNSMNIGNDNGMGWHSMHQYI
//
ID  P85091;
PN  Cytoplasmic FMR1-interacting protein 1;
GN  CYFIP1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q7TMB8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TMB8}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q7TMB8}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q7TMB8}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q7TMB8}. Note=Highly expressed in the perinuclear region (By similarity). Enriched in synaptosomes (By similarity). Also enriched in membrane ruffles and at the tips of lamellipodia (By similarity). {ECO:0000250|UniProtKB:Q7TMB8}.
DR  UNIPROT: P85091;
DE  Function: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E- FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA (By similarity). Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q7L576, ECO:0000250|UniProtKB:Q7TMB8}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030027;
GO  GO:0005845;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0001726;
GO  GO:0045202;
GO  GO:0051015;
GO  GO:0031267;
GO  GO:0048675;
GO  GO:0030032;
GO  GO:0008360;
GO  GO:0031529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYLTPSEKRINLSKVHPTDKLADQIFAYYKEGERDGKDEIIKNVPLKRIRK
//
ID  Q90YM8;
PN  Cytoplasmic FMR1-interacting protein 1 homolog;
GN  cyfip1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q7TMB8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TMB8}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q7TMB8}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q7TMB8}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q7TMB8}. Note=Highly expressed in the perinuclear region (By similarity). Enriched in synaptosomes (By similarity). Also enriched in membrane ruffles and at the tips of lamellipodia (By similarity). {ECO:0000250|UniProtKB:Q7TMB8}.
DR  UNIPROT: Q90YM8;
DR  UNIPROT: Q58ES3;
DR  Pfam: PF07159;
DR  Pfam: PF05994;
DE  Function: Involved in formation of membrane ruffles and lamellipodia protrusions and in axon outgrowth. Binds to F-actin but not to RNA (By similarity). {ECO:0000250|UniProtKB:Q7L576, ECO:0000250|UniProtKB:Q7TMB8}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0030027;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0001726;
GO  GO:0031209;
GO  GO:0045202;
GO  GO:0051015;
GO  GO:0000340;
GO  GO:0031267;
GO  GO:0048675;
GO  GO:0007411;
GO  GO:0000902;
GO  GO:0030031;
GO  GO:0030032;
GO  GO:0099563;
GO  GO:0030833;
GO  GO:0008360;
GO  GO:0006417;
GO  GO:0031529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASTVTLEDALSNVDLLEELPLPDQQPCIEPLPSSLIYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNDMLEEGQQYA
SQ  VMLYTWRCCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVNKLMNFMYFQRTAIDRFCGEVRRLCHAERRKDFVSEAYLLT
SQ  LGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMSEPSSIQESQNLSMFLANHNKITQSLQQQLEVINGYDELLAD
SQ  IVNLCVDYYENKMYLTPSERHMLLKVMGFGLYLMDGSNSNIYKLEAKKRINLTKIDKFFKQLQVVPLFGDMQIELARYIK
SQ  TSAHYEENKSRWSCTSTGSSPQYNVCEQMIQIREGHMRFISELARYSNSEVVTGSGRQDAQKTDSEYRKLFDLALQGLQL
SQ  LSQWSAQIMEVYSWKLVHPTDKYSNKECPDNAEEYERATRYNYTSEEKFALVEVLAMIKGLQVLMGRMESVFNHAIRHTI
SQ  YSALQDFAQVTLREPLRQAIKKKKNVVQSVLQAIRKTVCDWETGREPHNDPALRGEKDPKGGFDIKVPRRAVGPSSTQLY
SQ  MVRTMLESLVADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLLNFSETLQQCCDLSQLWFREFFLELTMGRRIQFPI
SQ  EMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVIAGS
SQ  LLLDKRLRAECKNQGANISWPSSNRYETLLKQRHVQLLGRSIDLNRLITQRVSSALYKSLELAISRFESEDLTSIMELEG
SQ  LLDINRMTHKLLSKYLTLDSIDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTILPFSQEFQRDKP
SQ  PNAQPQYLYGSKALNLAYSSIYSLYRNFVGPPHIKAICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKIC
SQ  RLPRHEYGSPGILEFFHHQLKDIVEYAELKSVCFQNLREVGNALLFCLLTEQSLSQEEVCDLLHAAPFQNILPRVHVKEG
SQ  ERLDAKMKRLEAKYTALHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSIFEVILTRVRAYLDDPIWRGPLPSNGVMH
SQ  VDECVEFHRLWSAMQFVYCIPVGAHEFTVEQCFGDGLNWAGCMIITLLGQHRRFDILDFSYHLLKVQKHDGKDEIIKSVP
SQ  LKKMVDRIRKFQILNDEIFAILNKYLKSGDGENMPVEHVRCFQPPIHQSLASN
//
ID  Q7L576;
PN  Cytoplasmic FMR1-interacting protein 1;
GN  CYFIP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q7TMB8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TMB8}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q7TMB8}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q7TMB8}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q7TMB8}. Note=Highly expressed in the perinuclear region (By similarity). Enriched in synaptosomes (By similarity). Also enriched in membrane ruffles and at the tips of lamellipodia (By similarity). {ECO:0000250|UniProtKB:Q7TMB8}.
DR  UNIPROT: Q7L576;
DR  UNIPROT: A8K6D9;
DR  UNIPROT: Q14467;
DR  UNIPROT: Q5IED0;
DR  UNIPROT: Q6ZSX1;
DR  UNIPROT: Q9BSD9;
DR  UNIPROT: Q9BVC7;
DR  PDB: 3P8C;
DR  PDB: 4N78;
DR  Pfam: PF07159;
DR  Pfam: PF05994;
DR  OMIM: 606322;
DR  DisGeNET: 23191;
DE  Function: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E- FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA (By similarity). Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). May act as an invasion suppressor in cancers. {ECO:0000250|UniProtKB:Q7TMB8, ECO:0000269|PubMed:16260607, ECO:0000269|PubMed:19524508, ECO:0000269|PubMed:21107423, ECO:0000269|PubMed:9417078}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q06787; IntAct: EBI-3649503; Score: 0.49
DE  Interaction: Q5SQX6; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: Q8IZP0; IntAct: EBI-7160735; Score: 0.74
DE  Interaction: Q04917; IntAct: EBI-307271; Score: 0.35
DE  Interaction: Q96L34; IntAct: EBI-354787; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-2433948; Score: 0.35
DE  Interaction: O60861; IntAct: EBI-7721151; Score: 0.40
DE  Interaction: P61981; IntAct: EBI-1067488; Score: 0.00
DE  Interaction: Q5S2C4; IntAct: EBI-1548622; Score: 0.37
DE  Interaction: Q9Y2A7; IntAct: EBI-1548644; Score: 0.81
DE  Interaction: Q38919; IntAct: EBI-1548679; Score: 0.37
DE  Interaction: P06730; IntAct: EBI-2000653; Score: 0.44
DE  Interaction: P63073; IntAct: EBI-2000573; Score: 0.52
DE  Interaction: Q5NFJ2; IntAct: EBI-2807484; Score: 0.00
DE  Interaction: Q96F07; IntAct: EBI-3649667; Score: 0.27
DE  Interaction: P62873; IntAct: EBI-3917485; Score: 0.37
DE  Interaction: P47872; IntAct: EBI-3917502; Score: 0.37
DE  Interaction: Q15029; IntAct: EBI-3917512; Score: 0.37
DE  Interaction: Q8HWS3; IntAct: EBI-3925636; Score: 0.37
DE  Interaction: P36873; IntAct: EBI-4311602; Score: 0.37
DE  Interaction: Q8BM65; IntAct: EBI-7447792; Score: 0.40
DE  Interaction: Q6PFX7; IntAct: EBI-7447775; Score: 0.40
DE  Interaction: Q9Y6X6; IntAct: EBI-7447809; Score: 0.40
DE  Interaction: Q92558; IntAct: EBI-7448569; Score: 0.35
DE  Interaction: Q9NYB9; IntAct: EBI-9206143; Score: 0.83
DE  Interaction: Q8WUW1; IntAct: EBI-9208427; Score: 0.35
DE  Interaction: Q9P2E7; IntAct: EBI-9206479; Score: 0.40
DE  Interaction: Q13200; IntAct: EBI-9378392; Score: 0.40
DE  Interaction: Q8K2C9; IntAct: EBI-9378349; Score: 0.40
DE  Interaction: Q15773; IntAct: EBI-9378370; Score: 0.40
DE  Interaction: Q9UIM3; IntAct: EBI-9378414; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.53
DE  Interaction: P50221; IntAct: EBI-21248543; Score: 0.37
DE  Interaction: Q5JST6; IntAct: EBI-21248535; Score: 0.37
DE  Interaction: Q9Z1B5; IntAct: EBI-10996176; Score: 0.35
DE  Interaction: Q921T2; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-11027413; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: Q99PT9; IntAct: EBI-11092405; Score: 0.35
DE  Interaction: Q9D902; IntAct: EBI-11096128; Score: 0.35
DE  Interaction: Q8CAF4; IntAct: EBI-11096313; Score: 0.35
DE  Interaction: Q96QS3; IntAct: EBI-11107478; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-11109663; Score: 0.35
DE  Interaction: Q9UQB8; IntAct: EBI-11135710; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q9H251; IntAct: EBI-12449357; Score: 0.35
DE  Interaction: Q9BSM1; IntAct: EBI-12553841; Score: 0.35
DE  Interaction: O43639; IntAct: EBI-21521290; Score: 0.35
DE  Interaction: Q3ZCQ8; IntAct: EBI-21581953; Score: 0.35
DE  Interaction: Q96EV8; IntAct: EBI-21651992; Score: 0.35
DE  Interaction: Q9ULV8; IntAct: EBI-21715242; Score: 0.35
DE  Interaction: Q5HYW2; IntAct: EBI-21762959; Score: 0.35
DE  Interaction: Q400G9; IntAct: EBI-21768785; Score: 0.35
DE  Interaction: Q6NT52; IntAct: EBI-21804311; Score: 0.35
DE  Interaction: Q70UQ0; IntAct: EBI-21813594; Score: 0.35
DE  Interaction: Q9UPY6; IntAct: EBI-21852540; Score: 0.35
DE  Interaction: Q8NB15; IntAct: EBI-21893201; Score: 0.35
DE  Interaction: P63000; IntAct: EBI-15768401; Score: 0.53
DE  Interaction: Q9Y6W5; IntAct: EBI-15894678; Score: 0.35
DE  Interaction: P15311; IntAct: EBI-16791848; Score: 0.27
DE  Interaction: P11142; IntAct: EBI-16794528; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800982; Score: 0.35
DE  Interaction: Q13557; IntAct: EBI-16812871; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q8IWW6; IntAct: EBI-25410934; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: P01023; IntAct: EBI-25830152; Score: 0.56
DE  Interaction: P51608; IntAct: EBI-25875938; Score: 0.56
DE  Interaction: P07196; IntAct: EBI-25877581; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25898349; Score: 0.56
DE  Interaction: O14901; IntAct: EBI-25905196; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25915439; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25931793; Score: 0.56
DE  Interaction: A0A0H3NJM6; IntAct: EBI-27055677; Score: 0.35
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: P13569; IntAct: EBI-27084109; Score: 0.35
DE  Interaction: Q15375; IntAct: EBI-32721052; Score: 0.27
DE  Interaction: P29323; IntAct: EBI-32721290; Score: 0.27
GO  GO:0044295;
GO  GO:0090724;
GO  GO:0005829;
GO  GO:0044294;
GO  GO:0043197;
GO  GO:0060076;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0032433;
GO  GO:0005925;
GO  GO:0030027;
GO  GO:0005845;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0090725;
GO  GO:0001726;
GO  GO:0031209;
GO  GO:0034774;
GO  GO:0035580;
GO  GO:0045202;
GO  GO:0043195;
GO  GO:1904724;
GO  GO:0051015;
GO  GO:0000340;
GO  GO:0031267;
GO  GO:0045182;
GO  GO:0048675;
GO  GO:0007411;
GO  GO:0000902;
GO  GO:0030031;
GO  GO:0032869;
GO  GO:0050890;
GO  GO:0097484;
GO  GO:0030032;
GO  GO:0099563;
GO  GO:1903422;
GO  GO:2000601;
GO  GO:0045773;
GO  GO:1900006;
GO  GO:0010592;
GO  GO:0051388;
GO  GO:1900029;
GO  GO:0016601;
GO  GO:0030833;
GO  GO:0008360;
GO  GO:1905274;
GO  GO:0031641;
GO  GO:0006417;
GO  GO:0099578;
GO  GO:0051602;
GO  GO:0031529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQVTLEDALSNVDLLEELPLPDQQPCIEPPPSSLLYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGQEYA
SQ  VMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMNFMYFQRNAIERFCGEVRRLCHAERRKDFVSEAYLIT
SQ  LGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNKITQSLQQQLEVISGYEELLAD
SQ  IVNLCVDYYENRMYLTPSEKHMLLKVMGFGLYLMDGSVSNIYKLDAKKRINLSKIDKYFKQLQVVPLFGDMQIELARYIK
SQ  TSAHYEENKSRWTCTSSGSSPQYNICEQMIQIREDHMRFISELARYSNSEVVTGSGRQEAQKTDAEYRKLFDLALQGLQL
SQ  LSQWSAHVMEVYSWKLVHPTDKYSNKDCPDSAEEYERATRYNYTSEEKFALVEVIAMIKGLQVLMGRMESVFNHAIRHTV
SQ  YAALQDFSQVTLREPLRQAIKKKKNVIQSVLQAIRKTVCDWETGHEPFNDPALRGEKDPKSGFDIKVPRRAVGPSSTQLY
SQ  MVRTMLESLIADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLINFSETLQQCCDLSQLWFREFFLELTMGRRIQFPI
SQ  EMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTRFNKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVMAGS
SQ  LLLDKRLRSECKNQGATIHLPPSNRYETLLKQRHVQLLGRSIDLNRLITQRVSAAMYKSLELAIGRFESEDLTSIVELDG
SQ  LLEINRMTHKLLSRYLTLDGFDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTVLPFSQEFQRDKQ
SQ  PNAQPQYLHGSKALNLAYSSIYGSYRNFVGPPHFQVICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKIC
SQ  RLPRHEYGSPGILEFFHHQLKDIVEYAELKTVCFQNLREVGNAILFCLLIEQSLSLEEVCDLLHAAPFQNILPRVHVKEG
SQ  ERLDAKMKRLESKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSFLDDPIWRGPLPSNGVMH
SQ  VDECVEFHRLWSAMQFVYCIPVGTHEFTVEQCFGDGLHWAGCMIIVLLGQQRRFAVLDFCYHLLKVQKHDGKDEIIKNVP
SQ  LKKMVERIRKFQILNDEIITILDKYLKSGDGEGTPVEHVRCFQPPIHQSLASS
//
ID  Q7TMB8;
PN  Cytoplasmic FMR1-interacting protein 1;
GN  Cyfip1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:14765121}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11438699}. Cell projection, lamellipodium {ECO:0000269|PubMed:14765121}. Cell projection, ruffle {ECO:0000269|PubMed:14765121}. Synapse, synaptosome {ECO:0000269|PubMed:11438699}. Note=Highly expressed in the perinuclear region (PubMed:11438699). Enriched in synaptosomes (PubMed:11438699). Also enriched in membrane ruffles and at the tips of lamellipodia (PubMed:14765121). {ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:14765121}.
DR  UNIPROT: Q7TMB8;
DR  UNIPROT: O88558;
DR  UNIPROT: Q3U7Q7;
DR  UNIPROT: Q5DU50;
DR  UNIPROT: Q7TSZ5;
DR  UNIPROT: Q80VN6;
DR  UNIPROT: Q8CE85;
DR  UNIPROT: Q99LY1;
DR  Pfam: PF07159;
DR  Pfam: PF05994;
DE  Function: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E- FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA (By similarity). Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis. May act as an invasion suppressor in cancers. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (PubMed:27605705). {ECO:0000250|UniProtKB:Q7L576, ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:14765121, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19524508, ECO:0000269|PubMed:27605705}.
DE  Reference Proteome: Yes;
DE  Interaction: O08788; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P15209; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P16054; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P35922; IntAct: EBI-2000004; Score: 0.58
DE  Interaction: P61205; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P63318; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q06787; IntAct: EBI-3649150; Score: 0.37
DE  Interaction: Q5SQX6; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q6ZPE2; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P62158; IntAct: EBI-911456; Score: 0.35
DE  Interaction: P63073; IntAct: EBI-2000004; Score: 0.63
DE  Interaction: O55135; IntAct: EBI-2000004; Score: 0.40
DE  Interaction: P62754; IntAct: EBI-2000004; Score: 0.40
DE  Interaction: Q8BM65; IntAct: EBI-7448021; Score: 0.35
DE  Interaction: P26450; IntAct: EBI-7448114; Score: 0.46
DE  Interaction: Q8R5H6; IntAct: EBI-7448095; Score: 0.53
DE  Interaction: Q5DU14; IntAct: EBI-7448718; Score: 0.35
DE  Interaction: Q80TE2; IntAct: EBI-9214306; Score: 0.35
DE  Interaction: Q6ZPJ3; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8C7R4; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9QUQ5; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9CQE1; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P61358; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q62159; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q921J2; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8CHG7; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: O35239; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P48437; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8C167; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q80U63; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q03717; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8VI75; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P24547; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9R0I7; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9R1R2; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: O55013; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9CYZ2; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: B2RWJ3; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8CC35; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: F6SEU4; IntAct: EBI-16727444; Score: 0.53
DE  Interaction: Q68FG2; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q62261; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P16546; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q61548; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8JZR6; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: D3YZU1; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8VD37; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8K0T0; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8BSK8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P63001; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P68404; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P63087; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q7M6Y3; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: E9Q3L2; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q2M3X8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: O89084; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9WU78; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: O88643; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9Z1M0; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P58281; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: O08919; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P46460; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q11011; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P08553; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P08551; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P19246; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P28660; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9Z0E0; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P55066; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q99104; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8K310; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9QXZ0; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8BHA1; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P28740; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8R0S2; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P35436; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q921M4; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P15105; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8K1B8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: F8VPU2; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8BWY3; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q6PH08; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9WV92; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9Z2H5; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P62631; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9JHU4; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9R0P5; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: O35098; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: O08553; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8BZ98; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P39054; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8K1M6; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P39053; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q80TZ3; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q91XM9; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9JLM8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9QXS6; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9JLV5; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P97427; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: O54991; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P80318; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P47754; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q3UHL1; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P28652; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P11798; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8BKX1; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P59999; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q60875; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9DBG3; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P17426; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P61967; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: O35643; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q99NH0; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8C8R3; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16727444; Score: 0.53
DE  Interaction: P60710; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q8CBW3; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q3UHJ0; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9WV60; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q9QYS2; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
DE  Interaction: Q9EP53; IntAct: EBI-16734894; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
GO  GO:0070161;
GO  GO:0044295;
GO  GO:0090724;
GO  GO:0005737;
GO  GO:0044294;
GO  GO:0043197;
GO  GO:0060076;
GO  GO:0032433;
GO  GO:0030027;
GO  GO:0005845;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0090725;
GO  GO:0098794;
GO  GO:0001726;
GO  GO:0031209;
GO  GO:0045202;
GO  GO:0043195;
GO  GO:0051015;
GO  GO:0005522;
GO  GO:0000340;
GO  GO:0031267;
GO  GO:0045182;
GO  GO:0048675;
GO  GO:0007411;
GO  GO:0000902;
GO  GO:0030031;
GO  GO:0032869;
GO  GO:0050890;
GO  GO:0097484;
GO  GO:0030032;
GO  GO:0099563;
GO  GO:1903422;
GO  GO:0031175;
GO  GO:2000601;
GO  GO:0045773;
GO  GO:0050772;
GO  GO:1900006;
GO  GO:0010592;
GO  GO:0051388;
GO  GO:1900029;
GO  GO:0016601;
GO  GO:0030833;
GO  GO:0008360;
GO  GO:1905274;
GO  GO:0031641;
GO  GO:0006417;
GO  GO:0099578;
GO  GO:0051602;
GO  GO:0031529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQVTLEDALSNVDLLEELPLPDQQPCIEPPPSSLLYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGQEYA
SQ  VMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMNFMYFQRNAIERFCGEVRRLCHAERRKDFVSEAYLIT
SQ  LGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNKITQSLQQQLEVISGYEELLAD
SQ  IVNLCVDYYENRMYLTPSEKHMLLKVMGFGLYLMDGSVSNIYKLDAKKRINLSKIDKYFKQLQVVPLFGDMQIELARYIK
SQ  TSAHYEENKSRWTCASSSSSPQYNICEQMIQIREDHMRFISELARYSNSEVVTGSGRQEAQKTDAEYRKLFDLALQGLQL
SQ  LSQWSAHVMEVYSWKLVHPTDKYSNKDCPDNAEEYERATRYNYTTEEKFALVEVIAMIKGLQVLMGRMESVFNHAIRHTV
SQ  YAALQDFSQVTLREPLRQAIKKKKNVIQSVLQAIRKTVCDWETGHEPFNDPALRGEKDPKSGFDIKVPRRAVGPSSTQLY
SQ  MVRTMLESLIADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLINFSETLQQCCDLSQLWFREFFLELTMGRRIQFPI
SQ  EMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTKFNKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVMAGS
SQ  LLLDKRLRSECKNQGATIHLPPSNRYETLLKQRHVQLLGRSIDLNRLITQRVSAAMYKSLELAIGRFESEDLTSVVELDG
SQ  LLEINRMTHKLLSRYLTLDSFDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTVLPFSQEFQRDKQ
SQ  PNAQPQYLHGSKALNLAYSSIYGSYRNFVGPPHFQVICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKIC
SQ  RLPRHEYGSPGILEFFHHQLKDIVEYAELKTVCFQNLREVGNAVLFCLLIEQSLSLEEVCDLLHAAPFQNILPRIHVKEG
SQ  ERVDAKMKRLESKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRTFLDDPIWRGPLPSNGVMH
SQ  VDECVEFHRLWSAMQFVYCIPVGTHEFTVEQCFGDGLHWAGCMIIVLLGQQRRFAVLDFCYHLLKVQKHDGKDEIIKNVP
SQ  LKKMVERIRKFQILNDEIITILDKYLKSGDGESTPVEHVRCFQPPIHQSLASS
//
ID  Q96F07;
PN  Cytoplasmic FMR1-interacting protein 2;
GN  CYFIP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10449408, ECO:0000269|PubMed:17245118}. Nucleus {ECO:0000269|PubMed:17245118}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5SQX6}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q5SQX6}. Note=Highly expressed in the perinuclear regionand enriched in synaptosomes (By similarity). Treatment with leptomycin-B triggers translocation to the nucleus (PubMed:17245118). {ECO:0000250|UniProtKB:Q5SQX6, ECO:0000269|PubMed:17245118}.
DR  UNIPROT: Q96F07;
DR  UNIPROT: A6NLT2;
DR  UNIPROT: D3DQJ3;
DR  UNIPROT: Q53EN5;
DR  UNIPROT: Q9NTK4;
DR  UNIPROT: Q9ULQ2;
DR  UNIPROT: Q9UN29;
DR  Pfam: PF07159;
DR  Pfam: PF05994;
DR  OMIM: 606323;
DR  OMIM: 618008;
DR  DisGeNET: 26999;
DE  Function: Involved in T-cell adhesion and p53/TP53-dependent induction of apoptosis. Does not bind RNA. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q5SQX6, ECO:0000269|PubMed:10449408, ECO:0000269|PubMed:15048733, ECO:0000269|PubMed:17245118}.
DE  Disease: Developmental and epileptic encephalopathy 65 (DEE65) [MIM:618008]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE65 is an autosomal dominant form characterized by onset of intractable seizures usually in the first 6 months of life and severe to profound psychomotor developmental delay. {ECO:0000269|PubMed:29534297}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q06787; IntAct: EBI-3649591; Score: 0.53
DE  Interaction: Q7L576; IntAct: EBI-3649667; Score: 0.27
DE  Interaction: Q9Y2A7; IntAct: EBI-7160508; Score: 0.32
DE  Interaction: Q8IZP0; IntAct: EBI-7160598; Score: 0.56
DE  Interaction: Q9Y6W5; IntAct: EBI-7160648; Score: 0.40
DE  Interaction: Q04917; IntAct: EBI-307271; Score: 0.53
DE  Interaction: P63104; IntAct: EBI-2433948; Score: 0.35
DE  Interaction: O60861; IntAct: EBI-7721256; Score: 0.40
DE  Interaction: Q9P2A4; IntAct: EBI-7087991; Score: 0.40
DE  Interaction: A0A6L7HB35; IntAct: EBI-2817304; Score: 0.00
DE  Interaction: P51116; IntAct: EBI-3650359; Score: 0.37
DE  Interaction: P51114; IntAct: EBI-3650316; Score: 0.37
DE  Interaction: Q13485; IntAct: EBI-3918179; Score: 0.49
DE  Interaction: Q13489; IntAct: EBI-3929935; Score: 0.37
DE  Interaction: P00747; IntAct: EBI-3938582; Score: 0.37
DE  Interaction: Q5D1E8; IntAct: EBI-3943196; Score: 0.37
DE  Interaction: P31946; IntAct: EBI-8796749; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.35
DE  Interaction: P15884; IntAct: EBI-11322276; Score: 0.35
DE  Interaction: O43639; IntAct: EBI-21521290; Score: 0.35
DE  Interaction: Q3ZCQ8; IntAct: EBI-21581953; Score: 0.35
DE  Interaction: Q9NSC5; IntAct: EBI-21639932; Score: 0.35
DE  Interaction: Q96EV8; IntAct: EBI-21651992; Score: 0.35
DE  Interaction: Q9ULV8; IntAct: EBI-21715242; Score: 0.35
DE  Interaction: Q969G2; IntAct: EBI-21754639; Score: 0.35
DE  Interaction: Q5HYW2; IntAct: EBI-21762959; Score: 0.35
DE  Interaction: Q400G9; IntAct: EBI-21768785; Score: 0.35
DE  Interaction: Q9NYB9; IntAct: EBI-21786440; Score: 0.35
DE  Interaction: Q9BQS6; IntAct: EBI-21789770; Score: 0.35
DE  Interaction: Q6NT52; IntAct: EBI-21804311; Score: 0.35
DE  Interaction: O60826; IntAct: EBI-21812182; Score: 0.35
DE  Interaction: Q70UQ0; IntAct: EBI-21813594; Score: 0.35
DE  Interaction: Q9UPY6; IntAct: EBI-21852540; Score: 0.35
DE  Interaction: Q8NB15; IntAct: EBI-21893201; Score: 0.35
DE  Interaction: Q8N3R9; IntAct: EBI-21912043; Score: 0.35
DE  Interaction: P03950; IntAct: EBI-16363232; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P15311; IntAct: EBI-16791848; Score: 0.27
DE  Interaction: P11142; IntAct: EBI-16794405; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q13557; IntAct: EBI-16812871; Score: 0.35
DE  Interaction: P30559; IntAct: EBI-20811004; Score: 0.37
DE  Interaction: P03372; IntAct: EBI-21302175; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21377438; Score: 0.00
DE  Interaction: Q8TB24; IntAct: EBI-26518569; Score: 0.35
DE  Interaction: O14733; IntAct: EBI-28930089; Score: 0.35
DE  Interaction: O43283; IntAct: EBI-28930960; Score: 0.35
DE  Interaction: O60566; IntAct: EBI-28931243; Score: 0.35
DE  Interaction: P23469; IntAct: EBI-27116439; Score: 0.27
DE  Interaction: P21709; IntAct: EBI-32720516; Score: 0.27
DE  Interaction: P54764; IntAct: EBI-32720816; Score: 0.27
DE  Interaction: Q15375; IntAct: EBI-32721052; Score: 0.27
DE  Interaction: P29323; IntAct: EBI-32721290; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: Q01974; IntAct: EBI-32725367; Score: 0.27
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0031209;
GO  GO:0045202;
GO  GO:0031267;
GO  GO:0097202;
GO  GO:0006915;
GO  GO:0000902;
GO  GO:0098609;
GO  GO:0097484;
GO  GO:0051388;
GO  GO:0045862;
GO  GO:0030833;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHEYA
SQ  VMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLT
SQ  LGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLAD
SQ  IVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKQLQVVPLFGDMQIELARYIK
SQ  TSAHYEENKSKWTCTQSSISPQYNICEQMVQIRDDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLL
SQ  SKWSAHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFAFVEVIAMIKGLQVLMGRMESVFNQAIRNTIY
SQ  AALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGGREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQACQ
SQ  WSPRALFHPTGGTQGRRGCRSLLYMVRTMLESLIADKSGSKKTLRSSLDGPIVLAIEDFHKQSFFFTHLLNISEALQQCC
SQ  DLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEPSMMEYVLYPLDLYNDSAYYALTKFKKQFLYDEIEAEVN
SQ  LCFDQFVYKLADQIFAYYKAMAGSVLLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRISAAM
SQ  YKSLDQAISRFESEDLTSIVELEWLLEINRLTHRLLCKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYC
SQ  YNGSTNRFVRTAIPFTQEPQRDKPANVQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKI
SQ  VKSLLQGTILQYVKTLIEVMPKICRLPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAILFCLLIEQALSQ
SQ  EEVCDLLHAAPFQNILPRVYIKEGERLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVI
SQ  LTRIRSYLQDPIWRGPPPTNGVMHVDECVEFHRLWSAMQFVYCIPVGTNEFTAEQCFGDGLNWAGCSIIVLLGQQRRFDL
SQ  FDFCYHLLKVQRQDGKDEIIKNVPLKKMADRIRKYQILNNEVFAILNKYMKSVETDSSTVEHVRCFQPPIHQSLATTC
//
ID  Q5SQX6;
PN  Cytoplasmic FMR1-interacting protein 2;
GN  Cyfip2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11438699}. Nucleus {ECO:0000250|UniProtKB:Q96F07}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11438699}. Synapse, synaptosome {ECO:0000269|PubMed:11438699}. Note=Highly expressed in the perinuclear region and enriched in synaptosomes (PubMed:11438699). {ECO:0000269|PubMed:11438699}.
DR  UNIPROT: Q5SQX6;
DR  UNIPROT: Q3UH21;
DR  UNIPROT: Q3UHS8;
DR  UNIPROT: Q8BSW0;
DR  UNIPROT: Q8CHA9;
DR  UNIPROT: Q924D3;
DR  UNIPROT: Q9R181;
DR  Pfam: PF07159;
DR  Pfam: PF05994;
DE  Function: Part of the WAVE1 complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). Involved in T-cell adhesion and p53-dependent induction of apoptosis (By similarity). Does not bind RNA. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (PubMed:27605705). {ECO:0000250|UniProtKB:Q96F07, ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:27605705}.
DE  Reference Proteome: Yes;
DE  Interaction: P05783; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: P35922; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q03001; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-2307988; Score: 0.53
DE  Interaction: Q8CBW3; IntAct: EBI-2642480; Score: 0.53
DE  Interaction: P50516; IntAct: EBI-6272793; Score: 0.35
DE  Interaction: Q8BPN8; IntAct: EBI-6272767; Score: 0.35
DE  Interaction: Q9Y2A7; IntAct: EBI-16086775; Score: 0.35
DE  Interaction: Q8WUW1; IntAct: EBI-16086775; Score: 0.35
DE  Interaction: Q9NYB9; IntAct: EBI-16086775; Score: 0.35
DE  Interaction: Q92558; IntAct: EBI-16086775; Score: 0.35
DE  Interaction: Q5SYE7; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: Q3ZCQ8; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: O14735; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: P13796; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: O00443; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: P05787; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: Q9Y6W5; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: Q9UPY6; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: P08727; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: Q7L576; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: Q7TMB8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q64514; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16727864; Score: 0.50
DE  Interaction: D3YZU1; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q8BYM5; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P17426; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q8R5H6; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q812A2; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q68FG2; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q62261; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P16546; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: A2AQ25; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q8C437; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: B1AXH1; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q8K1R7; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P28660; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q99104; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: O35099; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q08460; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P46660; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q8VDC1; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P39053; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: B9EJA2; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q02248; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: O54991; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P15116; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P70408; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q6P9K8; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P28652; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P11798; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q8K3H0; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: P62484; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q9EP53; IntAct: EBI-16734894; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16736255; Score: 0.35
DE  Interaction: F6SEU4; IntAct: EBI-16737600; Score: 0.35
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0031209;
GO  GO:0045202;
GO  GO:0031267;
GO  GO:0097202;
GO  GO:0006915;
GO  GO:0000902;
GO  GO:0098609;
GO  GO:0097484;
GO  GO:0031175;
GO  GO:0051388;
GO  GO:0045862;
GO  GO:0030833;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHDYA
SQ  VMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLT
SQ  LGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLAD
SQ  IVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKQLQVVPLFGDMQIELARYIK
SQ  TSAHYEENKSKWTCTQSSISPQYNICEQMVQIRDDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLL
SQ  SKWSAHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFAFVEVIAMIKGLQVLMGRMESVFNQAIRNTIY
SQ  AALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGGREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQLYM
SQ  VRTMLESLIADKSGSKKTLRSSLDGPIVLAIEDFHKQSFFFTHLLNISEALQQCCDLSQLWFREFFLELTMGRRIQFPIE
SQ  MSMPWILTDHILETKEPSMMEYVLYPLDLYNDSAYYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKAMAGSV
SQ  LLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRISAAMYKSLDQAISRFESEDLTSIVELEWL
SQ  LEINRLTHRLLCKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYCYNGSTNRFVRTAIPFTQEPQRDKPA
SQ  NVQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKIVKSLLQGTILQYVKTLIEVMPKICR
SQ  LPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAILFCLLIEQALSQEEVCDLLHAAPFQNILPRVYIKEGE
SQ  RLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSYLQDPIWRGPPPTNGVMHV
SQ  DECVEFHRLWSAMQFVYCIPVGTNEFTAEQCFGDGLNWAGCSIIVLLGQQRRFDLFDFCYHLLKVQRQDGKDEIIKNVPL
SQ  KKMADRIRKYQILNNEVFAILNKYMKSVETDSSTVEHVRCFQPPIHQSLATTC
//
ID  Q5R414;
PN  Cytoplasmic FMR1-interacting protein 2;
GN  CYFIP2;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q96F07}. Nucleus {ECO:0000250|UniProtKB:Q96F07}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5SQX6}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q5SQX6}. Note=Highly expressed in the perinuclear regionand enriched in synaptosomes (By similarity). {ECO:0000250|UniProtKB:Q5SQX6}.
DR  UNIPROT: Q5R414;
DR  UNIPROT: Q5R6T9;
DR  Pfam: PF07159;
DR  Pfam: PF05994;
DE  Function: Involved in T-cell adhesion and p53-dependent induction of apoptosis. Does not bind RNA (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q5SQX6, ECO:0000250|UniProtKB:Q96F07}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0031267;
GO  GO:0006915;
GO  GO:0098609;
GO  GO:0030833;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHEYA
SQ  VMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLT
SQ  LGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLAD
SQ  IVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKQLQVVPLFGDMQIELARYIE
SQ  TSAHYEENKSKWTCTQSSISPQYNICEQMVQIRDDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLL
SQ  SKWSAHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFAFVEVIAMIKGLQVLMGRMESVFNQAIRNTIY
SQ  AALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGGREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQLYM
SQ  VRTMLESLIADKSGSKKTLRSSLDGPIVLAIEDFHKQSFFFTHLLNISEALQQCCDLSQLWFREFFLELTMGRRIQFPIE
SQ  MSMPWILTDHILETKEPSMMEYVLYPLDLYNDSAYYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKAMAGSV
SQ  LLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRISAAMYKSLDQAISRFESEDLTSIVELEWL
SQ  LEINRLTHRLLCKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYCYNGSTNRFVRTAIPFTQEPQRDKPA
SQ  NIQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKIVESLLQGTILQYVKTLIEVMPKICR
SQ  LPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAILFCLLIEQALSQEEVCDLLHAAPFQNILPRVYIKEGE
SQ  RLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSYLQDPIWRGPPPTNGVMHV
SQ  DECVEFHRLWSAMQFVYCIPVGTNEFTAEQCFGDGLNWAGCSIIVLLGQQRRFDLFDFCYHLLKVQRQDGKDEIIKNVPL
SQ  KKMADRIRKYQILNNEVFAILNKYMKSVETDSSTVEHVRCFQPPIHQSLATTC
//
ID  Q1RMU2;
PN  Ubiquitin carboxyl-terminal hydrolase CYLD;
GN  CYLD;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250|UniProtKB:Q9NQC7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NQC7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q80TQ2}. Note=Detected at the microtubule cytoskeleton during interphase (By similarity). Detected at the midbody during telophase (By similarity). During metaphase, it remains localized to the centrosome but is also present along the spindle (By similarity). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000250|UniProtKB:Q9NQC7}.
DR  UNIPROT: Q1RMU2;
DR  Pfam: PF01302;
DR  Pfam: PF00443;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DR  PROSITE: PS00972;
DR  PROSITE: PS50235;
DE  Function: Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis. Negatively regulates NF- kappa-B activation by deubiquitinating upstream signaling factors. Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation. Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules. Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis. Required for normal cell cycle progress and normal cytokinesis. Inhibits nuclear translocation of NF-kappa-B. Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (By similarity). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis. Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins. Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (By similarity). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome (By similarity). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (By similarity). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000250|UniProtKB:Q9NQC7}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0097542;
GO  GO:0005881;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0004843;
GO  GO:0061578;
GO  GO:0070064;
GO  GO:0019901;
GO  GO:0008270;
GO  GO:0045087;
GO  GO:0070266;
GO  GO:0090090;
GO  GO:0050728;
GO  GO:2000493;
GO  GO:0046329;
GO  GO:0032088;
GO  GO:1901223;
GO  GO:1903753;
GO  GO:2001238;
GO  GO:0016579;
GO  GO:0070536;
GO  GO:1990108;
GO  GO:1902017;
GO  GO:0050727;
GO  GO:2001242;
GO  GO:0070507;
GO  GO:0007346;
GO  GO:0060544;
GO  GO:0010803;
GO  GO:0006511;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9NQC7};
SQ  MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQNIQDRSVGLSRIPSAKGKKNQIGLKILEQPHA
SQ  VLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSG
SQ  IFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDTGLESDYAGPVDTMQVELPPLEINSRVSLKL
SQ  GETIESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTILLHINDIIPESVTQERRPPKLAFMS
SQ  RGVGDKGSFSHNKPKATGSTSDPGTRNRSELFYTLNGSSVDSQPQSKSKNSWYIDEVAEDPAKSLTEIPPDFGHASPPLQ
SQ  PPSMNSLSSENRFHSLPFSLTKMPNTNGSISHSPLSLSVQSVMGELNNAPVQESPPLAVSSGNSHGLEVGSLAEVKENPP
SQ  FYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAF
SQ  GGYLSEVVEENTPPKMEKEGFEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELLRTE
SQ  IVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFMEKNE
SQ  KVGVPTIQQLLECSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECY
SQ  DDPDISAGKIKQFCKTCNAQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDS
SQ  AWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLDDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK
//
ID  Q9NQC7;
PN  Ubiquitin carboxyl-terminal hydrolase CYLD;
GN  CYLD;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:18313383, ECO:0000269|PubMed:32185393}. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25134987}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25134987}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q80TQ2}. Note=Detected at the microtubule cytoskeleton during interphase. Detected at the midbody during telophase. During metaphase, it remains localized to the centrosome but is also present along the spindle (PubMed:25134987). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000269|PubMed:25134987}.
DR  UNIPROT: Q9NQC7;
DR  UNIPROT: O94934;
DR  UNIPROT: Q7L3N6;
DR  UNIPROT: Q96EH0;
DR  UNIPROT: Q9NZX9;
DR  PDB: 1IXD;
DR  PDB: 1WHL;
DR  PDB: 1WHM;
DR  PDB: 2VHF;
DR  PDB: 7OWD;
DR  Pfam: PF01302;
DR  Pfam: PF00443;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DR  PROSITE: PS00972;
DR  PROSITE: PS50235;
DR  OMIM: 132700;
DR  OMIM: 601606;
DR  OMIM: 605018;
DR  OMIM: 605041;
DR  OMIM: 619132;
DR  DisGeNET: 1540;
DE  Function: Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis (PubMed:18636086, PubMed:26670046, PubMed:27458237, PubMed:26997266, PubMed:27591049, PubMed:29291351, PubMed:18313383, PubMed:32185393). Negatively regulates NF-kappa-B activation by deubiquitinating upstream signaling factors (PubMed:12917689, PubMed:12917691, PubMed:32185393). Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation (PubMed:12917690). Negative regulator of Wnt signaling (PubMed:20227366). Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules (PubMed:19893491). Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis (PubMed:18222923, PubMed:20194890). Required for normal cell cycle progress and normal cytokinesis (PubMed:17495026, PubMed:19893491). Inhibits nuclear translocation of NF-kappa-B (PubMed:18636086). Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF- kappa-B activation (PubMed:18636086). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells (By similarity). Negatively regulates TNFRSF11A signaling and osteoclastogenesis (By similarity). Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins (PubMed:26997266, PubMed:26670046, PubMed:27458237, PubMed:27591049). Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (PubMed:26997266). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome (By similarity). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (PubMed:29291351). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000269|PubMed:12917689, ECO:0000269|PubMed:12917690, ECO:0000269|PubMed:12917691, ECO:0000269|PubMed:17495026, ECO:0000269|PubMed:18222923, ECO:0000269|PubMed:18313383, ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:20194890, ECO:0000269|PubMed:20227366, ECO:0000269|PubMed:26670046, ECO:0000269|PubMed:26997266, ECO:0000269|PubMed:27458237, ECO:0000269|PubMed:27591049, ECO:0000269|PubMed:29291351, ECO:0000269|PubMed:32185393}.
DE  Disease: Cylindromatosis, familial (FCYL) [MIM:132700]: A disorder characterized by multiple skin tumors that develop from skin appendages, such as hair follicles and sweat glands. Affected individuals typically develop large numbers of tumors called cylindromas that arise predominantly in hairy parts of the body with approximately 90% on the head and neck. In severely affected individuals, cylindromas may combine into a confluent mass which may ulcerate or become infected (turban tumor syndrome). Individuals with familial cylindromatosis occasionally develop other types of tumors including spiradenomas that begin in sweat glands, and trichoepitheliomas arising from hair follicles. {ECO:0000269|PubMed:12190880, ECO:0000269|PubMed:16922728}. Note=The disease is caused by variants affecting the gene represented in this entry. Multiple familial trichoepithelioma 1 (MFT1) [MIM:601606]: Autosomal dominant dermatosis characterized by the presence of many skin tumors predominantly on the face. Since histologic examination shows dermal aggregates of basaloid cells with connection to or differentiation toward hair follicles, this disorder has been thought to represent a benign hamartoma of the pilosebaceous apparatus. Trichoepitheliomas can degenerate into basal cell carcinoma. {ECO:0000269|PubMed:14632188, ECO:0000269|PubMed:16307661, ECO:0000269|PubMed:16922728}. Note=The disease is caused by variants affecting the gene represented in this entry. Brooke-Spiegler syndrome (BRSS) [MIM:605041]: An autosomal dominant disorder characterized by the appearance of multiple skin appendage tumors such as cylindroma, trichoepithelioma, and spiradenoma. These tumors are typically located in the head and neck region, appear in early adulthood, and gradually increase in size and number throughout life. {ECO:0000269|PubMed:12190880, ECO:0000269|PubMed:12950348, ECO:0000269|PubMed:14632188, ECO:0000269|PubMed:15854031}. Note=The disease is caused by variants affecting the gene represented in this entry. Frontotemporal dementia and/or amyotrophic lateral sclerosis 8 (FTDALS8) [MIM:619132]: A neurodegenerative disorder characterized by frontotemporal dementia and/or amyotrophic lateral sclerosis in affected individuals. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. FTDALS8 is an autosomal dominant form. {ECO:0000269|PubMed:23338750, ECO:0000269|PubMed:32185393, ECO:0000269|PubMed:32666117}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: P0DTD1; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q6ZMQ8; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P06463; IntAct: EBI-2117974; Score: 0.35
DE  Interaction: P03126; IntAct: EBI-2118003; Score: 0.35
DE  Interaction: O95786; IntAct: EBI-8021116; Score: 0.52
DE  Interaction: Q7Z434; IntAct: EBI-8021151; Score: 0.40
DE  Interaction: Q14164; IntAct: EBI-8021199; Score: 0.40
DE  Interaction: Q9UHD2; IntAct: EBI-8021169; Score: 0.40
DE  Interaction: P0CG48; IntAct: EBI-6965887; Score: 0.44
DE  Interaction: Q8TEP8; IntAct: EBI-2510419; Score: 0.40
DE  Interaction: Q9UM54; IntAct: EBI-2510419; Score: 0.40
DE  Interaction: Q8IUW3; IntAct: EBI-2510419; Score: 0.40
DE  Interaction: Q13557; IntAct: EBI-2510419; Score: 0.40
DE  Interaction: Q9UM82; IntAct: EBI-2510419; Score: 0.59
DE  Interaction: O60502; IntAct: EBI-2510419; Score: 0.40
DE  Interaction: Q92995; IntAct: EBI-2511562; Score: 0.40
DE  Interaction: Q71U36; IntAct: EBI-7572503; Score: 0.58
DE  Interaction: Q9UBN7; IntAct: EBI-7572848; Score: 0.58
DE  Interaction: A0A3N4B3K9; IntAct: EBI-2848127; Score: 0.00
DE  Interaction: Q9Y6K9; IntAct: EBI-3928546; Score: 0.55
DE  Interaction: Q96J02; IntAct: EBI-5326486; Score: 0.40
DE  Interaction: P31946; IntAct: EBI-8796749; Score: 0.35
DE  Interaction: Q7TSJ6; IntAct: EBI-8798662; Score: 0.27
DE  Interaction: P04083; IntAct: EBI-9028892; Score: 0.35
DE  Interaction: Q5BJF6; IntAct: EBI-11367291; Score: 0.27
DE  Interaction: Q6ZU80; IntAct: EBI-11370150; Score: 0.27
DE  Interaction: Q66GS9; IntAct: EBI-11386281; Score: 0.27
DE  Interaction: Q8N137; IntAct: EBI-11392655; Score: 0.27
DE  Interaction: Q9Y2I6; IntAct: EBI-11399685; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: P62993; IntAct: EBI-21557652; Score: 0.35
DE  Interaction: Q14314; IntAct: EBI-21816328; Score: 0.35
DE  Interaction: Q9NYA1; IntAct: EBI-21871146; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: P15311; IntAct: EBI-16791848; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q9NPJ6; IntAct: EBI-25472202; Score: 0.27
DE  Interaction: Q68FS2; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: Q80W92; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: Q9WUD9; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: Q5XIA5; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: P09875; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: A0A0G2K064; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: B0BNB9; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: P0C0A2; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: B0BN56; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: P15651; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: D3ZYG0; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: P36972; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: B5DFA5; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: D3Z9C0; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: P14604; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: G3V8S2; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: M0R7K1; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: D3ZT90; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: D3ZIL6; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: P15650; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: P63252; IntAct: EBI-27067929; Score: 0.27
DE  Interaction: P41212; IntAct: EBI-29015445; Score: 0.27
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: Q96ED9; IntAct: EBI-34575530; Score: 0.27
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0097542;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0004843;
GO  GO:0061578;
GO  GO:0070064;
GO  GO:0019901;
GO  GO:0008270;
GO  GO:0007049;
GO  GO:0045087;
GO  GO:0070266;
GO  GO:0090090;
GO  GO:0050728;
GO  GO:2000493;
GO  GO:0046329;
GO  GO:0032088;
GO  GO:1901223;
GO  GO:1903753;
GO  GO:0032480;
GO  GO:0070423;
GO  GO:2001238;
GO  GO:0016579;
GO  GO:0070536;
GO  GO:1990108;
GO  GO:1902017;
GO  GO:0050727;
GO  GO:2001242;
GO  GO:0070507;
GO  GO:0007346;
GO  GO:0060544;
GO  GO:0010803;
GO  GO:0006511;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRIPSAKGKKNQIGLKILEQPHA
SQ  VLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSG
SQ  IFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDTALESDYAGPGDTMQVELPPLEINSRVSLKV
SQ  GETIESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFACVESTILLHINDIIPALSESVTQERRPPKLA
SQ  FMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAKSLTEISTDFDRSSP
SQ  PLQPPPVNSLTTENRFHSLPFSLTKMPNTNGSIGHSPLSLSAQSVMEELNTAPVQESPPLAMPPGNSHGLEVGSLAEVKE
SQ  NPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNS
SQ  LAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELL
SQ  RTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFME
SQ  KNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECR
SQ  ECYDDPDISAGKIKQFCKTCNTQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQNMELFAVLCIETSHYVAFVKYGK
SQ  DDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK
//
ID  Q80TQ2;
PN  Ubiquitin carboxyl-terminal hydrolase CYLD;
GN  Cyld;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250|UniProtKB:Q9NQC7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NQC7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25134987}. Note=Detected at the microtubule cytoskeleton during interphase (By similarity). Detected at the midbody during telophase (By similarity). During metaphase, it remains localized to the centrosome but is also present along the spindle (By similarity). {ECO:0000250|UniProtKB:Q9NQC7, ECO:0000269|PubMed:25134987}.
DR  UNIPROT: Q80TQ2;
DR  UNIPROT: Q80VB3;
DR  UNIPROT: Q8BXZ3;
DR  UNIPROT: Q8BYL9;
DR  UNIPROT: Q8CGB0;
DR  Pfam: PF01302;
DR  Pfam: PF00443;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DR  PROSITE: PS00972;
DR  PROSITE: PS50235;
DE  Function: Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis (PubMed:17548520, PubMed:28701375, PubMed:29291351, PubMed:32185393, PubMed:32424362). Negatively regulates NF-kappa-B activation by deubiquitinating upstream signaling factors (PubMed:16713561). Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF- kappa-B activation (PubMed:16713561). Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha- tubulin and stabilization of microtubules (PubMed:19893491). Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis (PubMed:16713561, PubMed:20194890, PubMed:19893491). Required for normal cell cycle progress and normal cytokinesis (PubMed:19893491). Inhibits nuclear translocation of NF- kappa-B (By similarity). Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (By similarity). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells (PubMed:16501569, PubMed:18643924). Negatively regulates TNFRSF11A signaling and osteoclastogenesis (PubMed:18382763). Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (PubMed:25134987). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins (PubMed:28701375). Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (By similarity). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (PubMed:28701375). Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome (PubMed:32424362). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (PubMed:17548520, PubMed:29291351). {ECO:0000250|UniProtKB:Q9NQC7, ECO:0000269|PubMed:16501569, ECO:0000269|PubMed:16713561, ECO:0000269|PubMed:17548520, ECO:0000269|PubMed:18382763, ECO:0000269|PubMed:18643924, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:20194890, ECO:0000269|PubMed:25134987, ECO:0000269|PubMed:28701375, ECO:0000269|PubMed:29291351, ECO:0000269|PubMed:32185393, ECO:0000269|PubMed:32424362}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Z2F6; IntAct: EBI-943890; Score: 0.67
DE  Interaction: P68369; IntAct: EBI-7572707; Score: 0.56
DE  Interaction: Q9Z2V5; IntAct: EBI-7572735; Score: 0.50
DE  Interaction: Q8C863; IntAct: EBI-5326509; Score: 0.40
DE  Interaction: P01375; IntAct: EBI-16186378; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16726570; Score: 0.35
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0097542;
GO  GO:0005881;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0004843;
GO  GO:1990380;
GO  GO:0061578;
GO  GO:0070064;
GO  GO:0019901;
GO  GO:0008270;
GO  GO:0043369;
GO  GO:0048872;
GO  GO:0045087;
GO  GO:0070266;
GO  GO:0090090;
GO  GO:0050728;
GO  GO:2000493;
GO  GO:0046329;
GO  GO:0032088;
GO  GO:1901223;
GO  GO:1903753;
GO  GO:2001238;
GO  GO:1903829;
GO  GO:0045582;
GO  GO:0050862;
GO  GO:0016579;
GO  GO:0070536;
GO  GO:1990108;
GO  GO:0045577;
GO  GO:1902017;
GO  GO:0050727;
GO  GO:2001242;
GO  GO:0070507;
GO  GO:0007346;
GO  GO:0060544;
GO  GO:0043393;
GO  GO:0050856;
GO  GO:0010803;
GO  GO:1901026;
GO  GO:0006511;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9NQC7};
SQ  MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRVPSTKGKKNQIGLKILEQPHA
SQ  VLFVDEKDVVEINEKFTELLLAITNCEERLSLFRNRLRLSKGLQVDVGSPVKVQLRSGEEKFPGVVRFRGPLLAERTVSG
SQ  IFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDNGLESDFAGPGDTMQVEPPPLEINSRVSLKV
SQ  GESTESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTILLHINDIIPDSVTQERRPPKLAFMS
SQ  RGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQQSKSKNPWYIDEVAEDPAKSLTEMSSDFGHSSPPPQP
SQ  PSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPLPISSGNAHGLEVGSLAEVKENPPF
SQ  YGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFG
SQ  GYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSALDTVLLRPKEKNDIEYYSETQELLRTEI
SQ  VNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNEK
SQ  VGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYD
SQ  DPDISAGKIKQFCKTCSTQVHLHPRRLNHSYHPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSA
SQ  WLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK
//
ID  Q5RED8;
PN  Ubiquitin carboxyl-terminal hydrolase CYLD;
GN  CYLD;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250|UniProtKB:Q9NQC7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NQC7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q80TQ2}. Note=Detected at the microtubule cytoskeleton during interphase (By similarity). Detected at the midbody during telophase (By similarity). During metaphase, it remains localized to the centrosome but is also present along the spindle (By similarity). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000250|UniProtKB:Q9NQC7}.
DR  UNIPROT: Q5RED8;
DR  Pfam: PF01302;
DR  Pfam: PF00443;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DR  PROSITE: PS00972;
DR  PROSITE: PS50235;
DE  Function: Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis. Negatively regulates NF- kappa-B activation by deubiquitinating upstream signaling factors. Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation. Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules. Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis. Required for normal cell cycle progress and normal cytokinesis. Inhibits nuclear translocation of NF-kappa-B. Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (By similarity). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis. Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins. Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (By similarity). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome (By similarity). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (By similarity). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000250|UniProtKB:Q9NQC7}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0097542;
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0004843;
GO  GO:0061578;
GO  GO:0008270;
GO  GO:0045087;
GO  GO:0090090;
GO  GO:0050728;
GO  GO:2000493;
GO  GO:0046329;
GO  GO:0032088;
GO  GO:1901223;
GO  GO:1903753;
GO  GO:0016579;
GO  GO:0070536;
GO  GO:1990108;
GO  GO:1902017;
GO  GO:0050727;
GO  GO:0010803;
GO  GO:0006511;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9NQC7};
SQ  MSSGLWSQDKVTSPYWEERVFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRIPSAKGKKNRIGLKILEQPHA
SQ  VLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSG
SQ  IFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDTALESDYAGPGDTMQVELPPLEINSRVSLKV
SQ  GETIESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFACVESTILLHINDIIPALSESVTQERRPPKLA
SQ  FMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAKSLTEISTDFDRSSP
SQ  PLQPPPVNSLSTENRFHSLPFSLTKMPNTNGSIGHSPLSLSAQSVMEELNTAPVQESPPLAMPPGNSHGLEVGSLAEVKE
SQ  NPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNS
SQ  LAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELL
SQ  RTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFME
SQ  KNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECR
SQ  ECYDDPDISAGKIKQFCKTCNTQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQNMELFAVLCIETSHYVAFVKYGK
SQ  DDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK
//
ID  Q66H62;
PN  Ubiquitin carboxyl-terminal hydrolase CYLD;
GN  Cyld;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250|UniProtKB:Q9NQC7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NQC7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q80TQ2}. Note=Detected at the microtubule cytoskeleton during interphase (By similarity). Detected at the midbody during telophase (By similarity). During metaphase, it remains localized to the centrosome but is also present along the spindle (By similarity). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000250|UniProtKB:Q9NQC7}.
DR  UNIPROT: Q66H62;
DR  Pfam: PF01302;
DR  Pfam: PF00443;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DR  PROSITE: PS00972;
DR  PROSITE: PS50235;
DE  Function: Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis. Negatively regulates NF- kappa-B activation by deubiquitinating upstream signaling factors. Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation. Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules. Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis. Required for normal cell cycle progress and normal cytokinesis. Inhibits nuclear translocation of NF-kappa-B. Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (By similarity). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis. Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins. Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (By similarity). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome (By similarity). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (By similarity). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000250|UniProtKB:Q9NQC7}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0097542;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0004843;
GO  GO:1990380;
GO  GO:0061578;
GO  GO:0070064;
GO  GO:0019901;
GO  GO:0008270;
GO  GO:0043369;
GO  GO:0048872;
GO  GO:0045087;
GO  GO:0070266;
GO  GO:0090090;
GO  GO:0050728;
GO  GO:2000493;
GO  GO:0046329;
GO  GO:0032088;
GO  GO:1901223;
GO  GO:1903753;
GO  GO:2001238;
GO  GO:1903829;
GO  GO:0045582;
GO  GO:0050862;
GO  GO:0016579;
GO  GO:0070536;
GO  GO:1990108;
GO  GO:0045577;
GO  GO:1902017;
GO  GO:0050727;
GO  GO:2001242;
GO  GO:0070507;
GO  GO:0007346;
GO  GO:0060544;
GO  GO:0043393;
GO  GO:0010803;
GO  GO:1901026;
GO  GO:0006511;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9NQC7};
SQ  MSSGLWNQEKVTSPYWEERLFYLLLQECSVTDKQTQKLLRVPKGSIGQYIQDRSVGHSRVPSAKGKKNQIGLKILEQPHA
SQ  VLFVDEKDVVEINEKFTELLLAITNCEERLSLFRNRIRLSKGLQVDVGSPVRVQLRSGEEKFPGVVRFRGPLLAERTVSG
SQ  IFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDNGLESDFAGPGDTVQVEPPPLEINSRVSLKV
SQ  GESTESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTVLLHINDIIPDSVTQERRPPKLAFMS
SQ  RGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQQQSKSKNPWYIDEVAEDPAKSLTEMSSDFGHSSPPPQ
SQ  PPSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPMPSSSGNAHGLEVGSLAEVKENPP
SQ  FYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAF
SQ  GGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSALDTVLLRPKEKNDVEYYSETQELLRTE
SQ  IVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNE
SQ  KVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECY
SQ  DDPDISAGKIKQFCKTCSTQVHLHPRRLNHTYHPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDS
SQ  AWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK
//
ID  Q6NUT2;
PN  Probable C-mannosyltransferase DPY19L2;
GN  DPY19L2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:P0CW70}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with DPY19L2 at the inner nuclear membrane. {ECO:0000250|UniProtKB:P0CW70}.
DR  UNIPROT: Q6NUT2;
DR  UNIPROT: A4FVC1;
DR  UNIPROT: B4E191;
DR  UNIPROT: Q3ZCX2;
DR  UNIPROT: Q6UWG8;
DR  UNIPROT: Q96LZ9;
DR  Pfam: PF10034;
DR  OMIM: 613893;
DR  OMIM: 613958;
DR  DisGeNET: 283417;
DE  Function: Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins. {ECO:0000250|UniProtKB:P34413}. Required during spermatogenesis for sperm head elongation and acrosome formation (PubMed:21397063, PubMed:21397064). Also plays a role in acrosome attachment to the nuclear envelope (By similarity). {ECO:0000250|UniProtKB:P0CW70, ECO:0000269|PubMed:21397063, ECO:0000269|PubMed:21397064}.
DE  Disease: Spermatogenic failure 9 (SPGF9) [MIM:613958]: An infertility disorder caused by spermatogenesis defects. The most prominent feature is the malformation of the acrosome, which can be totally absent in most severe cases. Additional features are an abnormal nuclear shape and abnormal arrangement of the mitochondria of the spermatozoon. {ECO:0000269|PubMed:21397063, ECO:0000269|PubMed:21397064}. Note=The disease is caused by variants affecting the gene represented in this entry. Deletions in DPY19L2 are probably the major cause of SPGF9.
DE  Reference Proteome: Yes;
DE  Interaction: P0DTC7; IntAct: EBI-26495729; Score: 0.35
DE  Interaction: Q16774; IntAct: EBI-21888393; Score: 0.40
DE  Interaction: P19739; IntAct: EBI-25685423; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0000030;
GO  GO:0018406;
GO  GO:0007286;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRKQGVSSKRLQSSGRSQSKGRRGASLAREPEVEEEMEKSALGGGKLPRGSWRSSPGRIQSLKERKGLELEVVAKTFLLG
SQ  PFQFVRNSLAQLREKVQELQARRFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTI
SQ  IEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGD
SQ  PACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTS
SQ  SNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSS
SQ  SLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPE
SQ  FDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFL
SQ  TPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGA
SQ  MPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCVVRTKPGCSMLEIWDV
SQ  EDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRVLKVN
//
ID  P0CW70;
PN  Probable C-mannosyltransferase DPY19L2;
GN  Dpy19l2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:22764053, ECO:0000269|PubMed:34471926}; Multi-pass membrane protein {ECO:0000305}. Note=Restricted to the inner nuclear membrane facing the acrosomal vesicle. The N- and C-termini are oriented towards the nucleoplasm (PubMed:22764053). Colocalizes with FAM209 at the inner nuclear membrane (PubMed:34471926). {ECO:0000269|PubMed:22764053, ECO:0000269|PubMed:34471926}.
DR  UNIPROT: P0CW70;
DR  Pfam: PF10034;
DE  Function: Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins. {ECO:0000250|UniProtKB:P34413}. Required during spermatogenesis for sperm head elongation and acrosome formation. Also plays a role in acrosome attachment to the nuclear envelope. {ECO:0000269|PubMed:22764053, ECO:0000269|PubMed:34471926}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0000030;
GO  GO:0018406;
GO  GO:0007286;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVGPTRSKLREGSSDRPQSSCTGQARRRWSAATMEPQQERSAPQERTKWSLLQHFLLGGRKLPSGARNYAARRIQSLNAQ
SQ  NYFQLEEVAKLLLLNRFQFLFTLLDHFREKVQALQMHRFSHRTLFGLAIFVGILHWLHLITLFENDHHFSHLSSLEREMT
SQ  FRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLVINTVKRFHLYPEVVIAYWYRTIIGIMNLFGIETKTCWNVTR
SQ  MEPLNEVQSCEGLGDPACFYIGVIFILNGLMMGLFFIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPF
SQ  LVLQMYILTIILRTSTVHKKHYMALCFSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFI
SQ  LMFGNSMYLSSYYSSCLLVTWAIMQKKSKIQKLGGTELQFWLIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARIL
SQ  RYTDFDTLIYTCAPEFDFMEQATPLRYIKTLLLPLILVITYLIFKKIVRDIMCVLYTNTYVRKQLLDNAELIFHTLQLLA
SQ  FTGLAILIMRLKLFLTPHMCIMASLICSQRLFGWLFCRIHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIH
SQ  WIKHSTRPDAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCV
SQ  VRTKPGCSMLEIWDVEDPSNAANPPLCSILLKDSRPYFTTVFQNSMYRVLKIN
//
ID  A6RC50;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  2059318;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A6RC50;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MATETPAGGPLEARISRAEPKTDASATSEPATGDTTETPAATKPSAADGQTDGASEGFGGSQLQEPEYSVNVKLSDLQAD
SQ  PNNPLYSIKSFEELGLHPSILQGLHSMSFRRPSKIQEKALPLLLNNPPANMIGQSQSGTGKTAAFVLNILSRLDLSPQME
SQ  LAPQALVLAPSRELARQIVGVIQVMGSYVDKLKVATAVPMESNRNQKVEAPVVVGTPGTVMDLIRKRLFNPQHLKVIVLD
SQ  EADNMLDQQGLGDQCIRVKGLLPKNIQVVLFSATFPDHVVRYANKFAPNANQITLKHEELTVEGIKQLYLDCDSDEHKFD
SQ  ILVKFYGLLTIGSSIIFVKTRASAVEIERRMVAEGHTVVSLTGGVEGQKRDEIIDKFRQGDAKVLITTNVLARGIDVQTV
SQ  SMVINYDIPELHAPKATKRIADAQTYLHRIGRTGRFGRVGVAVSFVASKEEWQMLQDIKTYFNTEIQRVNTQDWDEVEEV
SQ  VKTIIRSSRAGSNFQRS
//
ID  Q75C39;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q75C39;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSGNAQKPDASEMLADLDLNKKTKETTLEAGSAESAPSAPAENQAKSDSNLINSEYEVKVRLADIQADPNSPLYSVKSFE
SQ  ELGLAPELLKGLYAMKFQKPSKIQERALPLLLHNPPRNMIAQSQSGTGKTAAFSLTMLSRVDVAVPATQAICLAPSRELA
SQ  RQTLEVIQEMGKFTKIASQLIVPDSYEKNKAINAHIIVGTPGTVLDLMRRKMIQLGKVKTFVLDEADNMLDKQGLGDQCI
SQ  RVKKFLPKDTQLVLFSATFDDSVREYARRVVPNANSLELQRNEVNVSAIKQLFMDCNDERHKFTVLCDLYGLLTIGSSII
SQ  FVQTKQTANMLYTELKREGHQVSILHGDLQSADRDRLIGDFREGRSKVLITTNVLARGIDIPTVSMVVNYDLPMTANGQP
SQ  DPSTYVHRIGRTGRFGRTGVAISFIHDKKSYETLAAIQSYFGDIQITKVPTDDMDEMEKIVKKVLK
//
ID  A1CFV3;
PN  ATP-dependent RNA helicase dbp5;
GN  dbp5;
OS  344612;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A1CFV3;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MASEQPVEAAPLGGSLSDRISKPDEPTASETPEQTSDQADGASAPLGGSDLREPEYNVEVKLSDLQADPNNPLYSVKNFE
SQ  DLGLDPRILKGLSAMNFRKPSKIQERALPLLLGNPPKNLVGQSQSGTGKTAAFVLNALSRVDLSTEQMQKTPQALILAPT
SQ  RELARQIVGVVSVMGQFLDGLIIGTAVPADINNRPKRLECSIAVGTPGTVMDMIKRRIMVPNKLKVLVLDEADNMLDQQG
SQ  LGDQCIRVKALLPRDIQVVLFSATFPDHVHAYAAKFAPNANELTLQHEELTVEGIKQLYLDCSDEEDKYKTLVQLYGLLT
SQ  VGSSIIFVQTRTSASEIEKRMVAEGHTVASLTGGIDVTKRDEIIDKFRSGEAKVLITTNVLARGIDVSTVSMVINYDIPE
SQ  LHRPGVPERQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWDMLNQIQRYFNTEIQRVDTKDWDEVEDIIKKTIKNTRA
SQ  NAQFGKQ
//
ID  Q4WIN6;
PN  ATP-dependent RNA helicase dbp5;
GN  dbp5;
OS  330879;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q4WIN6;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MASEQPVEAAPTGGSLADRITKPDESNTSETPAPIGDQTDGAPAQLGGSDLHEPEYNVEVKLSDLQADPNNPLYSVKNFE
SQ  DLGLDPRILKGLSSMNFRKPSKIQERALPLLLNNPPKNLVGQSQSGTGKTAAFVLNALSRVDLSTEQMQKTPQALILAPT
SQ  RELARQILGVVQVMGQFVDGLIIGAAVPTDRDSRPKRLECSIVVGTPGTVGDMIKRRTFIPNKLKVLVLDEADNMLDQQG
SQ  LGDQCIRVKALLPRDIQVVLFSATFPEHVHQYASKFAPNANEITLQHEELTVEGIKQLYLDCADGEDKYRTLVQLYGLLT
SQ  VGSSIIFVQTRAAAQEIERRMTAEGHTVVSLTGERDPSVRDAIIDQFRRGEAKVLIATNVLARGIDVSTVSMVINYDIPE
SQ  LHQPNVPGRQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWEMLNQIQTYFNCEIQRVDTKDWDEVEDIIKKTIKNSRA
SQ  NPKFAGGKD
//
ID  A2QUY7;
PN  ATP-dependent RNA helicase dbp5;
GN  dbp5;
OS  425011;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A2QUY7;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MASEQPEAGSLADRITKPEEPAPAEAPEQTEDIPQTDGAAAQQGGSDLHEPDYTVEVKLSDLQADPNNPLFSVKNFEDLG
SQ  LDPRILQGLSAMNFRKPSKIQERALPLLLGNPAKNLVGQSQSGTGKTAAFVLNILSRLDLSSEQLQKTPQALILAPTREL
SQ  ARQIVGVIQVMGQFLDGLVIGTAVPADTGARPAKMECSVVVGTPGTVMDMIKRRIMIANKLRVLVLDEADNMLDQQGLGD
SQ  QCIRVKALLPRDIQVVLFSATFPAHVHEYASKFAPQANEITLQHEELTVEGIKQLYLDCSNDEDKYQTLVNLYGLLTVGS
SQ  SIIFVKTRASAQEIEKRMVAEGHTVASLTGGIEGSQRDAVIDQFRAGHAKVLITTNVLARGIDVSTVSMVINYDIPEIHQ
SQ  PGARQRQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWEMLNQIQRYFNTNIQRIDTKDWDEVEEIIKKTIKSSRAQLG
SQ  FR
//
ID  Q2U8K6;
PN  ATP-dependent RNA helicase dbp5;
GN  dbp5;
OS  510516;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q2U8K6;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSAEQPAETASAGNPLADRITTADGSKPEGTTETTDNEQADGAAAQLGGSELNEPDYTVEVKLSDLQADPNNPLYSVKSF
SQ  EDLGLDPRILQGLSAMNFRKPSKIQERALPLLLNNPPKNLVGQSQSGTGKTAAFVLNALSRLDLSTEQAQKTPQALILAP
SQ  TRELARQIVGVIQCMGQFLDGLNVSTAVPADTNSRHSKIESSVVVGTPGTVMDMIRKRVMVANKLKVLVLDEADNMLDQQ
SQ  GLGDQCIRVKALLPKDIQVVLFSATFPTHVHQYASKFAPQANELTLQHEELTVEGIKQLYLDCSDEEDKYKTLVQLYGLL
SQ  TVASSIIFVKTRASAAEIEKRMVAEGHTVASLTGGIEGSQRDAVIDQFRAGQAKVLITTNVLARGIDVSTVSMVINYDIP
SQ  ELHQPGAPERQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWNMLNQIQQYFNCTIQRVDTKDWDEVEDIIKKTIKNTR
SQ  AQAQFGR
//
ID  Q0CDT1;
PN  ATP-dependent RNA helicase dbp5;
GN  dbp5;
OS  341663;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q0CDT1;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSEQPTEAPAGGSLADRISKPEESKPADSTQQPTDNGQTDGAPAQLGGSELHEPEYNVEVKLSDLQADPNNPLFSVKNF
SQ  EDLGLDPRILQGLSAMNFRKPSKIQERALPLLLSNPPKNLVGQSQSGTGKTAAFVLNILSRLDLSTEQMQKTPQALILAP
SQ  TRELARQIVGVIQVMGQFLDNLIIGTAVPADTNNRPARMEASVVVGTPGTVMDMIKKRIMVPAKLQVLVLDEADNMLDQQ
SQ  GLGDQCIRVKALLPRTIQVVLFSATFPTHVHQYASKFAPQANELTLQHEELTVEGIKQLYLDCSDEEDKYRTLVSLYGLL
SQ  TVGSSIIFVKTRQSAMEIEKRMVAEGHTVASLTGGIEGSQRDAVIDQFRAGAAKVLITTNVLARGIDVSTVSMVINYDIP
SQ  ELHLPPNQPRQADFQTYLHRIGRTGRFGRVGVSISFVSNRDEWNMLNQIQKYFNTSIQRIDTKDWDEVEDIIKKTIKNPR
SQ  SQATFGK
//
ID  A6SBT4;
PN  ATP-dependent RNA helicase dbp5;
GN  dbp5;
OS  332648;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A6SBT4;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAESKSTSWADEVASPTIEKNEGNPLEEAQLDGATEPLGGGTLQDGQYEVEVKLSDIQGDETSPLYSVETFEQLGIDASI
SQ  LKGLYAMNFKKPSKIQEKALPLLLRNPPTNMIAQSQSGTGKTAAFVITILSRLDFSKPTTPQALCLAPSRELARQIEGVI
SQ  RSIGQFVDGLTVQAAIPGAVERNAKVNAMVVVGTPGTVMDLIKRRSIDASQMKILCLDEADNMLDQQGLGDQCMRVKSMI
SQ  RVEQILLFSATFPDEVYGFAQDFSPRANEIKLKRDELTVSGIKQMFMDCPNEVGKYEILVKLYGLMTIGSSIIFVKRRDT
SQ  ASNIAERLTKEGHKVAAVHGAFEGSERDQVLEDFRQGKAKVLITTNVLARGIDVQSVSMVINYDVPMKGRSDSDPPPETY
SQ  LHRIGRTGRFGRVGVSISFVFDRKSYDALNQIANHYNIDLIKLNQDDWDETEEIVKKVIKSSRAGTNLQS
//
ID  Q5AJD0;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  237561;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q5AJD0;
DR  UNIPROT: A0A1D8PJB3;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSEKVKRVEADATDLLASLSIDKSGEKLEEIKKGSTPDPSDLLGGLSLKEGDSKKPEEKKEVVEEPENKEINDDKKDED
SQ  KKDESKDEVKDGDGAKEETKEEVKEESKEEPKEPKEPKEPATNLIKSSYEVKVKLADIQADPNSPLYSVKSFEELGLSPE
SQ  LLKGLYAMKFNKPSKIQEKALPLLLSNPPRNMIGQSQSGTGKTAAFSLTMLSRVDPTIKMPQCLCLSPTRELARQTLEVI
SQ  TTMGKFTNITTQLVVPNAIPRGSSVNAQVLVGTPGIAIDLIRRRQLNLSKMKVFVLDEADNMLEAQGLGDQAIRVKKALP
SQ  RGVQLVLFSATFPTEVREYAERLVPDANSLELKQEELNVDGIKQLYMDCRSEQHKFEVLCELYGLLTIGSSIIFVEKKET
SQ  ADVLYGKMKKEGHTVSVLHGGLDNTDRDRLIDDFREGRSKVLITTNVLARGIDIASVSMVVNYDMPTDKYGKPDPSTYLH
SQ  RIGRTGRFGRVGVSISFIHDRRSYDILMAIKAYFGNVEMTRVPTDDWDEVEKIVKKVIKS
//
ID  Q6FKN8;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q6FKN8;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSATEDKKDPASMLAELKLDKDEGNKTPETKTPESNSAETKTTEEVKELKNPFTQKKEDVENDAAEEKTNEVNKDDAKDE
SQ  RENKDTNLIKSEYEVKVNLADLQADPNSPLYSVKSFDELGLSPELLKGIYAMKFQKPSKIQERALPLLLSNPPRNMIAQS
SQ  QSGTGKTAAFSLTMLSRVDETQNVPQAICLAPSRELARQTLEVIQEMGKYTKITTQLIVPDSFEKNTKINANVVVGTPGT
SQ  LLDLIRRKLIQLQNVKIFVLDEADNMLDKQGLGDQCIRVKKFLPKDTQLVLFSATFADAVKAYAQKVIPNANTLELQRNE
SQ  VNVKAIKQLYMDCNDEAHKYEVLCELYGLLTIGSSIIFVAKKDTANLLYGKLKHEGHQVSILHSDLRTDERDRLIDDFRE
SQ  GRSKVLITTNVLARGIDIPSVSMVVNYDLPTLPNGMPDYATYVHRIGRTGRFGRTGVAISFVHDKKSFKILSAIQDYFKD
SQ  IELTRVPTDDWDEVEDIVKKVLKQ
//
ID  Q2HGF7;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  306901;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q2HGF7;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADLASRITKPSDEPVDAVAPAPTATTGEGNGTEEPVDDGVNKGLVETTYDVEVKLSGLQADDESLLYSGVASFEELGLA
SQ  KSINDGLLAMNFKKPSKIQEKALPLMLSNPPRNMIAQSQSGTGKTAAFVLTVLSRVDLTKPTQPQALLLAPSRELARQIQ
SQ  SVIQTIGQFCENLNVEAAIPGSISRETGVRANVVVGTPGTVMDLIRRRQFDVSQLKIMVIDEADNMLDQQGMGDQCVRVK
SQ  GMLPKDIQTLLFSATFPEKVMIFARKYATNAHEIKLRHTDLTVKGISQMYMDCPDESKKYDILCKLYGLMTIGSSVIFVR
SQ  TRESASEIQRRMEADGHKVSALHGAHEGQNRDALLDDFRSGRSKVLITTNVLARGIDVSSVSMVINYDIPMKGPGDKEPD
SQ  METYLHRIGRTGRFGRVGVSISFVYDRKSYDALSKIADHYGLDLVQLAPDDWDATETKVQEVIKSSRARPDYVPNAGDK
//
ID  Q1EB85;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  246410;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q1EB85;
DR  UNIPROT: J3KGE1;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MASENTTETPSVPAGGPLAARISRPEGDANPPSTEAEKPAAEDDSGKGPSIPQVDGASEDQRGSELQDSEFDVNVKLSDL
SQ  QADPNNPLYSIKSFEELGLAEPIQMGLSKMNFRRPSKIQERALPLLMANPPTNMIAQSQSGTGKTAAFVLNILSRLELTP
SQ  EKQKSPQALVLAPSRELARQIVGVIQAMGTFVEGLFVATAVPMEMNRNQRVEASIVVGTPGTVQDLIKKRLFNTQHLRVL
SQ  VLDEADNMLDQQGLGDQCIRVKSLLPRTIQVVLFSATFPDFVVRYAHKFAPNSNQLTLKHEELTVEGIKQLYLDCESDEH
SQ  KYEILVKFYGLLTIGSSIIFVKTRASAAEIERRMVAEGHTVVSLTGGIEGQKRDEIIDRFRNGTAKVLITTNVLARGIDV
SQ  STVSMVINYDIPELHLPGAARRMADAQTYLHRIGRTGRFGRVGVAVSFVSNQEEWQMLQDIQKYFSTNIERVDTRDWDDV
SQ  EKKVKKIIKPSAVAR
//
ID  P0CQ87;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  283643;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: P0CQ87;
DR  UNIPROT: Q55NB1;
DR  UNIPROT: Q5KBP4;
DR  UNIPROT: Q5KBP5;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSDAQAPPASTSWADMVDEDEKQKQEQNMSNQNDGWGETATETSAPAPPPASAPVSSSNNDGWGEPAPSAPADNGWADAG
SQ  ASNGGSGANNNDGWFDAPVPPSSQPPKKEASDIQLQDDTEGLITNTFQVEVKLADLQGDPNSPLYSVQSFKELNLHEDLM
SQ  KGIIAAGFQKPSKIQEKALPLLLSNPPRNLIGQSQSGTGKTAAFTLNMLSRVDPTIPTPQAICIAPSRELARQIQEVVDQ
SQ  IGQFTQVGTFLAIPGSWSRNSRIDKQILIGTPGTLVDMLMRGSRILDPRMIRVLVLDEADELIAQQGLGEQTFRIKQLLP
SQ  PNVQNVLFSATFNDDVQEFADRFAPEANKIFLRKEDITVDAIRQLYLECDSEDQKYEALSALYDCLVIGQSIVFCKRKVT
SQ  ADHIAERLISEGHAVASLHGDKLSQERDAILDGFRNGETKVLITTNVIARGIDIPAVNMVVNYDVPDLGPGGNGPDIETY
SQ  IHRIGRTGRFGRKGCSVIFTHDYRSKSDVERIMNTLGKPMKKIDARSTTDIEQLEKALKLAMKGPA
//
ID  P0CQ86;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  214684;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: P0CQ86;
DR  UNIPROT: Q55NB1;
DR  UNIPROT: Q5KBP4;
DR  UNIPROT: Q5KBP5;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSDAQAPPASTSWADMVDEDEKQKQEQNMSNQNDGWGETATETSAPAPPPASAPVSSSNNDGWGEPAPSAPADNGWADAG
SQ  ASNGGSGANNNDGWFDAPVPPSSQPPKKEASDIQLQDDTEGLITNTFQVEVKLADLQGDPNSPLYSVQSFKELNLHEDLM
SQ  KGIIAAGFQKPSKIQEKALPLLLSNPPRNLIGQSQSGTGKTAAFTLNMLSRVDPTIPTPQAICIAPSRELARQIQEVIDQ
SQ  IGQFTQVGTFLAIPGSWSRNSRIDKQILIGTPGTLVDMLMRGSRILDPRMIRVLVLDEADELIAQQGLGEQTFRIKQLLP
SQ  PNVQNVLFSATFNDDVQEFADRFAPEANKIFLRKEDITVDAIRQLYLECDSEDQKYEALSALYDCLVIGQSIVFCKRKVT
SQ  ADHIAERLISEGHAVASLHGDKLSQERDAILDGFRNGETKVLITTNVIARGIDIPAVNMVVNYDVPDLGPGGNGPDIETY
SQ  IHRIGRTGRFGRKGCSVIFTHDYRSKSDVERIMNTLGKPMKKIDARSTTDIEQLEKALKLAMKGPA
//
ID  Q6BRE4;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  284592;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q6BRE4;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSKEDTRVESDAAELLSSLSLDKKEQTEATVPKVDAKEDKSNDESKQTIKPASTEESKPADVKDATKSEEQEAESNLIKS
SQ  SYEVKVKLADLQADPNSPLYSVKSFEELGLSSELLKGLYAMKFNKPSKIQEKALPLLISNPPKNMIGQSQSGTGKTAAFS
SQ  LTMLSRVDESDPNTQCICLAPARELARQTLEVITTMSKFTKITSQLIVPDAMQRGQSTCAHVLVGTPGTLLDLIRRKLIN
SQ  TSKVKVFVLDEADNMLESQGLGDQCVRVKRTLPKATQLVLFSATFPDEVRKYAEKFVPNANSLELKQEELNVEGIKQLYM
SQ  DCDSANHKFEVLSELYGLLTIGSSIIFVKTKDTANILYAKMKKEGHKCSILHAGLETSERDRLIDDFREGRSKVLITTNV
SQ  LARGIDIASVSMVVNYDLPVDQKGAPDPSTYLHRIGRTGRFGRVGVSISFVHDQKSYQDLMAIRSYFGNIEMTRVPTDDW
SQ  DEVEKIVKKVIKN
//
ID  Q5AVM1;
PN  ATP-dependent RNA helicase dbp5;
GN  dbp5;
OS  227321;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q5AVM1;
DR  UNIPROT: C8VC14;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MASDAPTGGSLADRISNPAETTEPVADKAQLDGAASNQGGSDLAEPEYNVEVKLSDLQADPNNPLYSVKNFEDLGLDPRI
SQ  LQGLSAMNFRKPSKIQERALPLLMGNPPKNLVGQSQSGTGKTAAFVLNILSRLDLSSEQAQKTPQALILAPTRELARQIV
SQ  GVIQVMGKFLDGLHIGTAVPADTNARPTRMEASVVVGTPGTVMDMIKKRIMVAAKLKVIVLDEADNMLDQQGLGDQCIRV
SQ  KALLPRDIQVVLFSATFPAHVHQYASKFAPAANELTLQHEELTVEGIKQLYLDCASEEDKYRTLVQLYGLLTVGSSIIFV
SQ  KTRASAVEIERRMVAEGHTVASLTGGIEGSQRDQIIDQFRAGHAKVLITTNVLARGIDVSTVSMVINYDIPELHQPPNRP
SQ  RQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWEMLNQIQKYFNTDIQRIDTKDWDEVEDIIKKTIKNTRAQAGFR
//
ID  Q4HY71;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  229533;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q4HY71;
DR  UNIPROT: A0A0E0RW04;
DR  UNIPROT: V6RQB4;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADLASRITKPDEVAAETPAETPAETAPAASGELGQADGNIEDLGGSGLQEPEWDVEVSLSELQNNEATPFHSATTWQDL
SQ  GLREDLLKGLLSLNFLKPSKVQGKSLPLMLSDPPRNMLAQSQSGTGKTAAFVTAILSRVDFSKPDQPQALALAPSRELAR
SQ  QIEGVINAIGRFVENKKVAAAIPGVLPRGEPVRASVIVGTPGTVMDIIRRRQLDISQLRVLVLDEADNMLDQQGLGDQCL
SQ  KVKNMLPKEIQVLLFSATFPENVMKYAGKFAPNAHSLKLQRSELTVKGISQMFIDCPDDNMKYDILCKLYGLMTIGQSVI
SQ  FVKTRDSASEIERRMVADGHKVSALHAAFDGAERDNLLTKFRQGENKVLITTNVLARGIDVSSVSMVINYDIPMKGRGDT
SQ  EPDAETYLHRIGRTGRFGRVGVSISFVYDKKSFDALSKIAEMYGIDLVKLDTEDWDEAEERVKEVIKKNRAQASYAPSAT
SQ  EPKAAAGA
//
ID  Q6CJU1;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q6CJU1;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAQLSKEASDLMARLNIKEPAKKASEDNDTTSETKVEKEDAKETKAEEPANKVINSEYEVKVNLADLQADANSPLYSVKS
SQ  FEELGLSEELLKGLYAMKFQKPSKIQEKALPLLIRDPPHNMIAQSQSGTGKTAAFSLTMLTRVDPNVNSTQAICLSPARE
SQ  LARQTLEVIQEMGKFTKTSSQLVVPDSFERNKPITANIVVGTPGTVLDLIRRKMLNLGSIKVFVLDEADNMLDKQGLGDQ
SQ  CIRVKKFLPKTCQLVLFSATFDDGVRQYAKKIIPTAVSLELQKNEVNVSAIKQLFMDCDNEEHKYTILSELYGLLTIGSS
SQ  IIFVKTKQTANLLYAKLKKEGHQVSILHGDLQSQDRDRLIDDFREGRSKVLITTNVLARGIDIPSVSMVVNYDLPTLPNG
SQ  QADPSTYVHRIGRTGRFGRTGVAISFIHDKKSFEVLSAIQKYFGDIEITKVPTDDLDEMETIVKKALKA
//
ID  A5DZX2;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  379508;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A5DZX2;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSNTKDVDADASNLLASLSVSKEKKEDTSNILAGLSLNGDESNKKEGSGVKDTESDKQKGNGKVEKVEKDENKDKSQSEA
SQ  KDDSKRETNLIENRYEVEVKLDDIQADPNSPLYSVKSFEELGLKPELLKGLYAMKFNKPSKIQERALPLLISNPPKNMIG
SQ  QSQSGTGKTAAFSLTMLSRVDESIKAPQCICLAPTRELARQTLEVVETMGKYSNITYQLVVPDSVPRGQAISAQVLVGTP
SQ  GIVHDLINRKAINVAKVKVFVLDEADNMLDAQGLADTCLRVKKRLPRDCQLVLFSATFPTEVRKYAEKFVPNANSLALKQ
SQ  EELNVKGIKQLYMDCKNQEHKFEVLCELYGLLTIGSSIIFVEQKATADSLYLRMKEEGHTVSILHGGLEVADRDRLIDDF
SQ  REGRSKVLITTNVLARGIDIATVSMVVNYDLPRTKEGRPDPSTYLHRIGRTGRFGRVGVSVSFVANEKDYQTLKYIAEYF
SQ  GIEDQMTVVPTDDWDEVEKIVTRVIKEKKMT
//
ID  A4RIF1;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  242507;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A4RIF1;
DR  UNIPROT: G4MVD6;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSDLASRITAPAAATPATETDAPAAASSTLAVPDGAADGANSSGLQESNYDVEVQLGDPDTDSPLSSISSFSELGLPQGI
SQ  IDGLLAMNFKKPSKIQARALPLMLSNPPRNMIAQSQSGTGKTGAFVVTILSRVDFNQPNQPQALALAPSRELARQIQSVI
SQ  QSIGQFCTGLVVDAAIPGAISRETGVKANVVVGTPGTVMDLIRRRQFDVSQLKLLVVDEADNMLDQQGLGEQCVRVKNML
SQ  PKTIQTLLFSATFPDHVKSYAEKFAPQANQMKLRQQELTVKGISQMYMDCPSLKEKYEVLCKLYGLMTIGSSVIFVKTRE
SQ  SADEIQRRMEADGHKVSALHGAFQGQERDQLLDDFRSGKSKVLITTNVLARGIDVSSVSMVINYDIPMKGPGDQSPDAET
SQ  YLHRIGRTGRFGRVGVSISFVHDRKSFTALSSIAEHYGIDLIQLSPDDWDDTEVKVQDVIKSSRAKPDYAPTQEKAA
//
ID  A1CYG5;
PN  ATP-dependent RNA helicase dbp5;
GN  dbp5;
OS  331117;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A1CYG5;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MASEQPVEAAPTGGSLADRITKPDESNTSETPAPAADQTDGAPAQLGGSDLHEPEYNVEVKLSDLQADPNNPLYSVKNFE
SQ  DLGLDPRILKGLSNMNFRKPSKIQERALPLLLNNPPKNLVGQSQSGTGKTAAFVLNALSRVDLSTEQMQKTPQALILAPT
SQ  RELARQILGVVQVMGQFVDGLIIGAAVPTDRDSRPKRLECSIVVGTPGTVGDMIKRRTFIPNKLKVLVLDEADNMLDQQG
SQ  LGDQCIRVKALLPRDIQVVLFSATFPEHVHQYASKFAPNANEITLQHEELTVEGIKQLYLDCADGEDKYKTLVQLYGLLT
SQ  VGSSIIFVQTRAAAQEIEKRMTAEGHTVVSLTGERDPSVRDAIIDQFRRGEAKVLIATNVLARGIDVSTVSMVINYDIPE
SQ  LHQPSVPGRQADFQTYLHRIGRTGRFGRVGVSISFVSNREEWEMLNQIQTYFNCEIQRVDTKDWDEVEDIIKKTIKNSRA
SQ  NPKFAGGKE
//
ID  Q8X0X2;
PN  ATP-dependent RNA helicase dbp-5;
GN  dbp;
OS  367110;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q8X0X2;
DR  UNIPROT: Q1K870;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADLASRITKPDEAPAAAPEAAPVSAPASEEPKAPENETSIEESQSNLVKNEYEVEIKLSDLQNDTESPLYSVSSFDELG
SQ  LPEAVNRGLLAINFKKPSKVQEKCLPLMLSDPPRNMIAQSQSGTGKTAAFVLTVLSRIDLSKPHQPQALLLAPSRELARQ
SQ  IQTVVQTIGQFCENLIVEAAIPGAISRETGVRGSVVVGTPGTVMDLVKRRQFDISQLKVLVIDEADNMLDQQGLGDQCVR
SQ  VKNMLPKTIQILLFSATFPDKVLRFAERFAPNANQMKLKHKELTVKGISQMFMDCPTEKDKYDILCKLYGLMTIGSSVIF
SQ  VRTRETANEIQKRMEADGHKVSALHGAYEGQSRDVLLDEFRSGRSKVLITTNVLARGIDVSSVSMVINYDIPMKGPGERE
SQ  PDAETYLHRIGRTGRFGRVGVSISFVHDRRSFEALSQIAQFYGIDLIQLNPNDLDDTERKVQEVIKSSRAQAEYVPSATD
SQ  SAV
//
ID  Q0UCB9;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  321614;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q0UCB9;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSATEPTKEPAKEEVAEQSTVAQAQVDGSGEPANGSPLTETEYKVEVKLADMQADPNNPLYSAQSFEELQLSEELLKGVR
SQ  NMNFRKPSKIQEKALPLLLMNPPTNMIAQSQSGTGKTAAFSLNILSRIDLSRNEPQAIALAPSRELARQILGVITHMGQF
SQ  MEGLKTMAAIPDPTKRNQRLDAHVLVGTPGTVQEQLKRRLIKSDSIKILVLDEADNMLDQQGMGDQCTRVKSLLPKNIQT
SQ  VLFSATFPPAVINYANKFAPNSNVLTLAHEELTIEGIKQLYIDIDKDQDKYSTLLKFYGLMTQASSIIFVRTRRTAEELE
SQ  RRMVAEGHKVAQLSGALEGQDRDRVIDQFRSGEAKVLITTNVLARGIDVESVTMVINYDVPTMADGREADPETYLHRIGR
SQ  TGRFGRVGVALTFVHDKASWQQLHDIASYFKTDLHPIDTSDWDNVEEMIQKIIKSSRAGKSTKEMTEMITS
//
ID  A5DBI5;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  294746;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A5DBI5;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MPEEPVDSDASKLLESLSINKQGDSAPIKDEKPVVESENKVSDEQNSEPTKEPETKTETENNDSNLISSSYEVQVKLADL
SQ  QADPNSPLYSVKSFEELGLSPELLKGLYAMKFNKPSKIQEKALPLLISNPPKNMIGQSQSGTGKTAAFSLTMLSRVDVND
SQ  PNTQCICLSPTRELARQTLEVITTMGKFTKVTTQLVVPQAMEKNQGTQAHIVVGTPGTLLDMIKRKLLRTGKVKVFVLDE
SQ  ADNMLDGQGLAAQCIRVKKVLPTSCQLVLFSATFPTEVRKYAEKFVPNANSLELKQEELNVDAIKQLYMDCDSEKHKAEV
SQ  LSELYGLLTIGSSIIFVKTKATANYLYAKMKSEGHACSILHSDLDNSERDKLIDDFREGRSKVLITTNVLARGIDIASVS
SQ  MVVNYDIPVDKDDKPDPSTYLHRIGRTGRFGRVGVAVSFVHDKKSYEDLEQIRSYFNDIEMTRVPTDDWDEVEKIVKKVL
SQ  KK
//
ID  A3GH91;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  322104;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A3GH91;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSAEKRVEADAAELLSSLSLGESPAEKKDEKTEEVKKEEAKSEELNKVVEKTEEKVKEANAEDAKPEELKEVGKEENEEP
SQ  KTNLIQSTYEVKVKLADIQADPNSPLFSVKSFEELGLTPELLKGLYAMKFNKPSKIQEKALPLLISNPPRNMIGQSQSGT
SQ  GKTAAFSLTMLSRVDPKVPSTQCLCLAPTRELARQTLEVISTMGKFTNITTQLIVPDALPRGSSTNAHIIVGTPGIVMDL
SQ  IRRKQINVNGVKVFVLDEADNMLDAQGLGDQCVRVKRTLPKTTQLVLFSATFPTKVRQYAEKFVPNANSLELKQEELNVD
SQ  GIKQLYMDCDSEKHKFEVLCELYGLLTIGSSIIFVERKDTANLLYAKMKAEGHACSILHGGLETSERDRLIDDFREGRSK
SQ  VLITTNVLARGIDIASVSMVVNYDLPTDKDGNADPSTYLHRIGRTGRFGRVGVSISFIYDKRSYEILMKIKDYFGNVEMT
SQ  RVPTDDWDEVEKIVKKVIKS
//
ID  Q09747;
PN  ATP-dependent RNA helicase dbp5;
GN  dbp5;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q09747;
DR  PDB: 3FHO;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0002184;
GO  GO:0016973;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSTTLGQESKTDWASLDSDEEVQRISDKVNQLNTSENKNEDQKATNLSDRLGPKITENVDAKSEQDKATNTIAEDANTKQ
SQ  SENDESNLIPNKNEVRVKLADLQADPNSPLFSVKSFEELELKPELLKGIYSMKFQKPSKIQEKALPLLLSNPPRNMIGQS
SQ  QSGTGKTAAFALTMLSRVDASVPKPQAICLAPSRELARQIMDVVTEMGKYTEVKTAFGIKDSVPKGAKIDAQIVIGTPGT
SQ  VMDLMKRRQLDARDIKVFVLDEADNMLDQQGLGDQSMRIKHLLPRNTQIVLFSATFSERVEKYAERFAPNANEIRLKTEE
SQ  LSVEGIKQLYMDCQSEEHKYNVLVELYGLLTIGQSIIFCKKKDTAEEIARRMTADGHTVACLTGNLEGAQRDAIMDSFRV
SQ  GTSKVLVTTNVIARGIDVSQVNLVVNYDMPLDQAGRPDPQTYLHRIGRTGRFGRVGVSINFVHDKKSWEEMNAIQEYFQR
SQ  PITRVPTDDYEELEKVVKNALKM
//
ID  A7EY76;
PN  ATP-dependent RNA helicase dbp5;
GN  dbp5;
OS  665079;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A7EY76;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSESKSTSWADEVASPSTEKNEESSLEDAQVDGATEPLGGGTLQDGQYEVEVKLSDIQGDQTSPLYSVDTFEQLGIDASI
SQ  LKGLYAMNFKKPSKIQEKALPLLLGNPPTNMIAQSQSGTGKTAAFVITILSRLDFSKPTTPQALCLAPSRELARQIEGVV
SQ  RSIGQFVEGLSVQAAIPGAVERNARVNAMVIVGTPGTVMDLIKRKSIDASQMKVLCLDEADNMLDQQGLGDQCLRVKSMI
SQ  KVEQILLFSATFPDEVYGFAQQFSPRANEIKLKRDELTVSGIKQMFMDCPNEVGKYEILVKLYGLMTIGSSIIFVKRRDT
SQ  ASHIAERLTAEGHKVAAIHGAFEGAERDTVLEDFRQGKAKVLITTNVLARGIDVQSVSMVINYDIPMKGRSDFEPDPETY
SQ  LHRIGRTGRFGRVGVSISFVFDRKSYDALNKIAHHYNIDLIKLNQDDWDETEEIVKKVIKSSRAGTNLRA
//
ID  Q4P7Z8;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  237631;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q4P7Z8;
DR  UNIPROT: A0A0D1E0C9;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSESKDKTTAPAADSNVNEIASGISGLLSSKDVAESNLRESSHEVQVTLADQQADPNSPLYSAKSFEALGLHENLLKGIY
SQ  AMKYQKPSKIQEKALPLLLQNPPKNMIGQSQSGTGKTAAFILTMLSRIDYDLQKPQAIALAPSRELARQIMDVARTMSKF
SQ  TNVTTCLCLPDEVKRGEKITAQLIIGTPGKTFDMIKSKGIDTAAIKVFVLDEADNMLDQQSLGEQSIRVKNTMPKSCQLV
SQ  LFSATFPTNVYDFAVRIAPGANEIRLKQEELSVEGIKQFYMDCKDEDHKYEVLVELYNLLTIGQSIIFCAKRETADRIAQ
SQ  KMTQEGHKVDSLHGRLETADRDRTIDAFRDGKSKVLISTNVIARGIDIQQVTLVINYDMPLTQTGEADAETYLHRIGRTG
SQ  RFGRKGVSINFVHDQQSWSYMDQIEKALKCQITRVATNDLEEMEYTIKEALKQIGK
//
ID  Q6C3X7;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  284591;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: Q6C3X7;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005934;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0000822;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSDQVSDMLEKLELQKEKNQAAATEAKVEEVKEDDKKDVKEELNEDDKKVAKEDDKKEDAKEESKEDAEENNLIQTEYEV
SQ  RVKLADLQADPNSPLYSAKRFEDLGLDENLLKGLYAMKFNKPSKIQEKALPLLLSDPPHNMIGQSQSGTGKTGAFSLTML
SQ  SRVDPNLKAVQCICLAPSRELARQTLDVVDEMKKFTDITTHLIVPESTERGQKVTSQILVGTPGSVAGLLQKKQIDAKHV
SQ  KVFVLDEADNMVDSSMGSTCARIKKYLPSSTQVVLFSATFPESVLDLAGKMCPNPNEIRLKANELNVDAITQLYMDCEDG
SQ  EEKFKMLEELYSMLTIASSVIFVAQRSTANALYQRMSKNGHKVSLLHSDLSVDERDRLMDDFRFGRSKVLISTNVIARGI
SQ  DIATVSMVVNYDLPTDKNGKPDPETYLHRIGRTGRFGRSGVSISFVHDEASFEVLDSIQQSLGMTLTQVPTDDIDEVEEI
SQ  IKKAIKGK
//
ID  A6ZNQ1;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
DR  UNIPROT: A6ZNQ1;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0034641;
GO  GO:0043170;
GO  GO:0051028;
GO  GO:0044238;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSDTKRDPADLLASLKIDNEKEDTSEVSTKETVKSQPEKTADSIKPAEKLVPKVEEKKTKQEDSNLISSEYEVKVKLADI
SQ  QADPNSPLYSAKSFDELGLAPELLKGIYAMKFQKPSKIQERALPLLLHNPPRNMIAQSQSGTGKTAAFSLTMLTRVNPED
SQ  ASPQAICLAPSRELARQTLEVVQEMGKFTKITSQLIVPDSFEKNKQINAQVIVGTPGTVLDLMRRKLMQLQKIKIFVLDE
SQ  ADNMLDQQGLGDQCIRVKRFLPKDTQLVLFSATFADAVRQYAKKIVPNANTLELQTNEVNVDAIKQLYMDCKNEADKFDV
SQ  LTELYGLMTIGSSIIFVATKKTANVLYGKLKSEGHEVSILHGDLQTQERDRLIDDFREGRSKVLITTNVLARGIDIPTVS
SQ  MVVNYDLPTLANGQADPATYIHRIGRTGRFGRKGVAISFVHDKNSFNILSAIQKYFGDIEMTRVPTDDWDEVEKIVKKVL
SQ  KD
//
ID  P20449;
PN  ATP-dependent RNA helicase DBP5;
GN  DBP5;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm. Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Nuclear pore complex cytoplasmic fibrils. Accumulates in the nucleus rapidly and reversibly in response to ethanol stress.
DR  UNIPROT: P20449;
DR  UNIPROT: D6W2B2;
DR  PDB: 2KBE;
DR  PDB: 2KBF;
DR  PDB: 3GFP;
DR  PDB: 3PEU;
DR  PDB: 3PEV;
DR  PDB: 3PEW;
DR  PDB: 3PEY;
DR  PDB: 3RRM;
DR  PDB: 3RRN;
DR  PDB: 5ELX;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. Contributes to the blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May also be involved in early transcription. {ECO:0000269|PubMed:10428971, ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:11350039, ECO:0000269|PubMed:12192043, ECO:0000269|PubMed:12686617, ECO:0000269|PubMed:15280434, ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:15619606, ECO:0000269|PubMed:9564047, ECO:0000269|PubMed:9564048}.
DE  Reference Proteome: Yes;
DE  Interaction: Q02159; IntAct: EBI-860380; Score: 0.00
DE  Interaction: P40477; IntAct: EBI-7266119; Score: 0.66
DE  Interaction: Q04839; IntAct: EBI-7998113; Score: 0.66
DE  Interaction: P50111; IntAct: EBI-2132816; Score: 0.51
DE  Interaction: P32491; IntAct: EBI-2617619; Score: 0.35
DE  Interaction: P40484; IntAct: EBI-2617649; Score: 0.35
DE  Interaction: Q12529; IntAct: EBI-2887496; Score: 0.00
DE  Interaction: P40564; IntAct: EBI-3656740; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3744163; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3778915; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3787386; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-7082780; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-15806702; Score: 0.76
GO  GO:0005934;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0008186;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006415;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSDTKRDPADLLASLKIDNEKEDTSEVSTKETVKSQPEKTADSIKPAEKLVPKVEEKKTKQEDSNLISSEYEVKVKLADI
SQ  QADPNSPLYSAKSFDELGLAPELLKGIYAMKFQKPSKIQERALPLLLHNPPRNMIAQSQSGTGKTAAFSLTMLTRVNPED
SQ  ASPQAICLAPSRELARQTLEVVQEMGKFTKITSQLIVPDSFEKNKQINAQVIVGTPGTVLDLMRRKLMQLQKIKIFVLDE
SQ  ADNMLDQQGLGDQCIRVKRFLPKDTQLVLFSATFADAVRQYAKKIVPNANTLELQTNEVNVDAIKQLYMDCKNEADKFDV
SQ  LTELYGLMTIGSSIIFVATKKTANVLYGKLKSEGHEVSILHGDLQTQERDRLIDDFREGRSKVLITTNVLARGIDIPTVS
SQ  MVVNYDLPTLANGQADPATYIHRIGRTGRFGRKGVAISFVHDKNSFNILSAIQKYFGDIEMTRVPTDDWDEVEKIVKKVL
SQ  KD
//
ID  Q5E9V1;
PN  DCN1-like protein 3;
GN  DCUN1D3;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm {ECO:0000250|UniProtKB:Q8IWE4}. Nucleus {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWE4}. Note=After UVC treatment, the protein enters to the nucleus gradually. Cell membrane localization is essential for CUL3 neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
DR  UNIPROT: Q5E9V1;
DR  Pfam: PF03556;
DR  PROSITE: PS51229;
DE  Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and may play a role in the cell cycle progression by regulating the SCF ubiquitin E3 ligase complex, after UV damage. At the cell membrane, can promote and as well inhibit cullins neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0000151;
GO  GO:0097602;
GO  GO:0031624;
GO  GO:0032182;
GO  GO:0030308;
GO  GO:2000134;
GO  GO:2000435;
GO  GO:0043065;
GO  GO:2000436;
GO  GO:0051443;
GO  GO:0045116;
GO  GO:0010564;
GO  GO:2000434;
GO  GO:0010332;
GO  GO:0010225;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8IWE4,};
SQ  MGQCVTKCKNPSSTLGSKNGDRDPSSKSHGRRSASHREEQLPTCGKPGGDILVNGTKKAEAAPEACQLPTSSGDAGREPK
SQ  SNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSID
SQ  GICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISR
SQ  DTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT
//
ID  Q8IWE4;
PN  DCN1-like protein 3;
GN  DCUN1D3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416}. Cytoplasm {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:26906416}. Nucleus {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:26906416}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18823379}. Note=After UVC treatment, the protein enters to the nucleus gradually (PubMed:18823379). Cell membrane localization is essential for CUL3 neddylation (PubMed:19617556). {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:19617556}.
DR  UNIPROT: Q8IWE4;
DR  UNIPROT: B3KVY4;
DR  PDB: 4GBA;
DR  Pfam: PF03556;
DR  PROSITE: PS51229;
DR  OMIM: 616167;
DR  DisGeNET: 123879;
DE  Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and may play a role in the cell cycle progression by regulating the SCF ubiquitin E3 ligase complex, after UV damage (PubMed:23201271, PubMed:19617556, PubMed:27542266, PubMed:18823379). At the cell membrane, can promote and as well inhibit cullins neddylation (PubMed:19617556, PubMed:26906416, PubMed:25349211). {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:27542266}.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q96Q27; IntAct: EBI-21879621; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-15794277; Score: 0.58
DE  Interaction: Q13617; IntAct: EBI-15794136; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-15794136; Score: 0.35
DE  Interaction: P61081; IntAct: EBI-15794345; Score: 0.44
DE  Interaction: Q16695; IntAct: EBI-20937612; Score: 0.40
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0000151;
GO  GO:0097602;
GO  GO:0031624;
GO  GO:0032182;
GO  GO:0030308;
GO  GO:2000134;
GO  GO:2000435;
GO  GO:0043065;
GO  GO:2000436;
GO  GO:0051443;
GO  GO:0045116;
GO  GO:0010564;
GO  GO:2000434;
GO  GO:0010332;
GO  GO:0010225;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis;
SQ  MGQCVTKCKNPSSTLGSKNGDREPSNKSHSRRGAGHREEQVPPCGKPGGDILVNGTKKAEAATEACQLPTSSGDAGRESK
SQ  SNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSID
SQ  GICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISR
SQ  DTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT
//
ID  Q8K0V2;
PN  DCN1-like protein 3;
GN  Dcun1d3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm {ECO:0000250|UniProtKB:Q8IWE4}. Nucleus {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWE4}. Note=After UVC treatment, the protein enters to the nucleus gradually. Cell membrane localization is essential for CUL3 neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
DR  UNIPROT: Q8K0V2;
DR  Pfam: PF03556;
DR  PROSITE: PS51229;
DE  Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and may play a role in the cell cycle progression by regulating the SCF ubiquitin E3 ligase complex, after UV damage. At the cell membrane, can promote and as well inhibit cullins neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0000151;
GO  GO:0097602;
GO  GO:0031624;
GO  GO:0032182;
GO  GO:0030308;
GO  GO:2000134;
GO  GO:2000435;
GO  GO:0043065;
GO  GO:2000436;
GO  GO:0051443;
GO  GO:0045116;
GO  GO:0010564;
GO  GO:2000434;
GO  GO:0010332;
GO  GO:0010225;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8IWE4,};
SQ  MGQCVTKCKNPSSTLGSKNGDRDPSNKSHSRRGASHREEQVPPCGKPAGDILVNGTKKAEAATEACQLPTSSGDAGRESK
SQ  TNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSID
SQ  GICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISR
SQ  DTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREVEGRGTLSSGQEGLCPEEQT
//
ID  Q5R9G1;
PN  DCN1-like protein 3;
GN  DCUN1D3;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm {ECO:0000250|UniProtKB:Q8IWE4}. Nucleus {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWE4}. Note=After UVC treatment, the protein enters to the nucleus gradually. Cell membrane localization is essential for CUL3 neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
DR  UNIPROT: Q5R9G1;
DR  Pfam: PF03556;
DR  PROSITE: PS51229;
DE  Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and may play a role in the cell cycle progression by regulating the SCF ubiquitin E3 ligase complex, after UV damage. At the cell membrane, can promote and as well inhibit cullins neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0097602;
GO  GO:0030308;
GO  GO:2000134;
GO  GO:2000435;
GO  GO:0043065;
GO  GO:2000436;
GO  GO:0010564;
GO  GO:2000434;
GO  GO:0010332;
GO  GO:0010225;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8IWE4,};
SQ  MGQCVTKCKNPSSTLGSKNGDRDPSNKSHSRRGAGHREEQVPPCGKPGGDILVNGTKKAEAATEACQLPTSSGDAGRESK
SQ  SNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSID
SQ  GICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISR
SQ  DTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT
//
ID  Q4V8B2;
PN  DCN1-like protein 3;
GN  Dcun1d3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm {ECO:0000250|UniProtKB:Q8IWE4}. Nucleus {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWE4}. Note=After UVC treatment, the protein enters to the nucleus gradually. Cell membrane localization is essential for CUL3 neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
DR  UNIPROT: Q4V8B2;
DR  Pfam: PF03556;
DR  PROSITE: PS51229;
DE  Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and may play a role in the cell cycle progression by regulating the SCF ubiquitin E3 ligase complex, after UV damage. At the cell membrane, can promote and as well inhibit cullins neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0000151;
GO  GO:0097602;
GO  GO:0031624;
GO  GO:0032182;
GO  GO:0030308;
GO  GO:2000134;
GO  GO:2000435;
GO  GO:0043065;
GO  GO:2000436;
GO  GO:0051443;
GO  GO:0045116;
GO  GO:0010564;
GO  GO:2000434;
GO  GO:0010332;
GO  GO:0010225;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8IWE4,};
SQ  MGQCVTKCKNPSSTLGSKNGDRDPSSKSHSRRGASHREEQVPPCGKPAGDILVNGTKKAEAATEACQLPTSSGDAGRESK
SQ  TNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSID
SQ  GICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISR
SQ  DTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREVEGRGALSSGPEGLCPEEQT
//
ID  Q6DFA1;
PN  DCN1-like protein 3;
GN  dcun1d3;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm {ECO:0000250|UniProtKB:Q8IWE4}. Nucleus {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWE4}.
DR  UNIPROT: Q6DFA1;
DR  Pfam: PF03556;
DR  PROSITE: PS51229;
DE  Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes. At the cell membrane, can promote and as well inhibit cullins neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0097602;
GO  GO:2000435;
GO  GO:2000436;
GO  GO:0010564;
GO  GO:2000434;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8IWE4,};
SQ  MGQCVTKCKNPSSTLGSKNGERESSKPHKRSSSHKEEHMSICGKASGEILVNGTKKGDASLEASQPLAVGVDTKKKEQGV
SQ  GAELSSLQRIEELFRRYKDEREDAILEEGMERFCDDLCVDPTEFRVLVLAWKFQAATMCKFTRREFFEGCKSINADGIES
SQ  ICSQFPGLLNEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNKPLILDQWLEFLTENPSGIKGISRD
SQ  TWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKSEEKTDCIPCLGTDHQSRDEQT
//
ID  A4IHK8;
PN  DCN1-like protein 3;
GN  dcun1d3;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm {ECO:0000250|UniProtKB:Q8IWE4}. Nucleus {ECO:0000250|UniProtKB:Q8IWE4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWE4}.
DR  UNIPROT: A4IHK8;
DR  Pfam: PF03556;
DR  PROSITE: PS51229;
DE  Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes. At the cell membrane, can promote and as well inhibit cullins neddylation. {ECO:0000250|UniProtKB:Q8IWE4}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0000151;
GO  GO:0097602;
GO  GO:0031624;
GO  GO:0032182;
GO  GO:2000435;
GO  GO:2000436;
GO  GO:0051443;
GO  GO:0045116;
GO  GO:0010564;
GO  GO:2000434;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8IWE4,};
SQ  MGQCVTKCKNPSSTLGSKNGERESSKPHKRSSSHKDEHLSICGKASREILVNGTKKGDVSLEASQPLAAGGDTKKKEQGT
SQ  GAELSSVQRIEELFWRYKDEREDAILEEGMERFCNDLYVDPTEFRVLVLAWKFQAATMCKFTRREFFEGCKAINADGIEG
SQ  ICARFPSLLNEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNKPLILDQWLDFLTENPSGIKGISRD
SQ  TWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKNEEETKCIPCSGTDDQSTEGQT
//
ID  O62255;
PN  m7GpppN-mRNA hydrolase dcap-2;
GN  dcap;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic granule {ECO:0000269|PubMed:18439994}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18439994}. Note=Localizes to perinuclear puncta in pachytene-stage germ cells (PubMed:18439994). Diffusely localized to cytoplasmic puncta in maturing oocytes (PubMed:18439994). {ECO:0000269|PubMed:18439994}.
DR  UNIPROT: O62255;
DR  UNIPROT: A0A061ACN4;
DR  UNIPROT: A0A061ADX7;
DR  UNIPROT: B3VKU3;
DR  UNIPROT: O62257;
DR  UNIPROT: Q2YS49;
DR  UNIPROT: Q2YS50;
DR  UNIPROT: Q45F95;
DR  Pfam: PF05026;
DR  Pfam: PF00293;
DR  PROSITE: PS51462;
DR  PROSITE: PS00893;
DE  Function: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs (PubMed:16199859). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:16199859). RNA-decapping enzyme although it does not bind the RNA cap (PubMed:16199859). May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs (PubMed:16199859). In oocytes, may play a role in the response to stress induced by heat shock, osmotic stress and anoxia (PubMed:18439994). Required for the developmental axon guidance and regrowth of PLM touch receptor neurons (PubMed:31983639). Early in embryogenesis, plays a role in ciliary shape formation in sensory neurons (PubMed:28887031). Promotes survival at high temperatures (PubMed:25061667). {ECO:0000269|PubMed:16199859, ECO:0000269|PubMed:18439994, ECO:0000269|PubMed:25061667, ECO:0000269|PubMed:28887031, ECO:0000269|PubMed:31983639}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0043186;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0050072;
GO  GO:0030145;
GO  GO:0003723;
GO  GO:0000290;
GO  GO:0008340;
GO  GO:0006397;
GO  GO:0002119;
GO  GO:0000184;
GO  GO:0040012;
GO  GO:0000003;
GO  GO:0009408;
GO  GO:0006979;
GO  GO:0009411;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEISTENWCKKPKNRSIFSKNISFQKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQPSTSKPKKNEKRKKAVAQAPASA
SQ  PAPGPEEKKKQPKRASVGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGPRIPTDILDELEFR
SQ  FISNMVECEINDNIRVCFHLELAHWYYIDHMVEDDKISGCPNVGSRDFNFQMCQHCRVLRKYAHRADEVLAKFREYKSTV
SQ  PTYGAILVDPEMDHVVLVQSYFAKGKNWGFPKGKINQAEPPRDAAIRETFEETGFDFGIYSEKEKKFQRFINDGMVRLYL
SQ  VKNVPKDFNFQPQTRKEIRKIEWFKIDDLPTDKTDELPAYLQGNKFYMVMPFVKDIQIYVQKEKEKLRRRKAEAVQSTPS
SQ  SSIFSQLFPAQPPPPVPEDATPTRPMYKRLTSEELFSAFKNPPAGEVARPTLPDMSPAVNGLDTLAVLGICTPLKPGASL
SQ  NEFSGAPQNCPMISEEAGSPADPSAEIGFAMPMDLKQPVVTSDHPWQHHKISDSSAPPQTLESHQGWLDTQLVNTIMHSP
SQ  NHPLPPTSNSPATPTAVLGHLIGKPIQPQAILPQAATPTALGSAEKPKSSRISLSDNSAFKAISSTQKQSIPKATAAPPS
SQ  TEKTRSASLSGSSQVVGKPARNLFNSVVSPVSSGIQSIQGDGGAWEDVWFREQLAATTTAGTSISSLAASNQELAMINRE
SQ  ETPIEDPYFKQQAYQKAQKAQSLIPACSQWTNSIKLDIDYVVGPLSFWMQQFSTKSPVSGTGPQLP
//
ID  Q06151;
PN  m7GpppX diphosphatase;
GN  DCS1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body. Note=Predominantly cytoplasmic.
DR  UNIPROT: Q06151;
DR  UNIPROT: D6VYR7;
DR  UNIPROT: Q6Q5L1;
DR  PDB: 5BV3;
DR  PDB: 6TRQ;
DR  Pfam: PF05652;
DR  PROSITE: PS00892;
DE  Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7- methylguanosine monophosphate (m7GMP) or tri-methyl guanosine nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and m3(2,2,7)GMP, respectively (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. May also regulate the 5'->3' exoribonucleolytic mRNA decay pathway in a cap-independent manner. Negatively regulates trehalase activity. {ECO:0000269|PubMed:12198172, ECO:0000269|PubMed:14523240, ECO:0000269|PubMed:15240832, ECO:0000269|PubMed:15273322, ECO:0000269|PubMed:16260594, ECO:0000269|PubMed:16963086, ECO:0000269|PubMed:22985415}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-3764256; Score: 0.35
DE  Interaction: P32356; IntAct: EBI-390849; Score: 0.67
DE  Interaction: Q12123; IntAct: EBI-786407; Score: 0.87
DE  Interaction: Q12179; IntAct: EBI-7885875; Score: 0.44
DE  Interaction: P28240; IntAct: EBI-7998723; Score: 0.40
DE  Interaction: P38009; IntAct: EBI-6344412; Score: 0.00
DE  Interaction: P25303; IntAct: EBI-3659022; Score: 0.35
DE  Interaction: P53940; IntAct: EBI-3768133; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3797766; Score: 0.35
DE  Interaction: P48363; IntAct: EBI-3817134; Score: 0.35
DE  Interaction: Q06151; IntAct: EBI-15484526; Score: 0.75
DE  Interaction: P14680; IntAct: EBI-16286565; Score: 0.35
GO  GO:0005737;
GO  GO:0106095;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0044692;
GO  GO:0016818;
GO  GO:0042802;
GO  GO:0050072;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0000340;
GO  GO:0009267;
GO  GO:0000290;
GO  GO:0000956;
GO  GO:0000288;
GO  GO:0031086;
GO  GO:1901919;
GO  GO:1903398;
GO  GO:0009408;
GO  GO:0007584;
GO  GO:0006970;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQLPTDFASLIKRFQFVSVLDSNPQTKVMSLLGTIDNKDAIITAEKTHFLFDETVRRPSQDGRSTPVLYNCENEYSCIN
SQ  GIQELKEITSNDIYYWGLSVIKQDMESNPTAKLNLIWPATPIHIKKYEQQNFHLVRETPEMYKRIVQPYIEEMCNNGRLK
SQ  WVNNILYEGAESERVVYKDFSEENKDDGFLILPDMKWDGMNLDSLYLVAIVYRTDIKTIRDLRYSDRQWLINLNNKIRSI
SQ  VPGCYNYAVHPDELRILVHYQPSYYHFHIHIVNIKHPGLGNSIAAGKAILLEDIIEMLNYLGPEGYMNKTITYAIGENHD
SQ  LWKRGLEEELTKQLERDGIPKIPKIVNGFK
//
ID  Q12123;
PN  Inactive diphosphatase DCS2;
GN  DCS2;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body. Note=Predominantly cytoplasmic. Localizes close to the perinuclear space before the diauxic growth shift. Recruited to the P-body after the post-diauxic growth shift. Colocalizes with the decapping activator protein LSM1 at P-body.
DR  UNIPROT: Q12123;
DR  UNIPROT: D6W2M9;
DR  Pfam: PF05652;
DR  PROSITE: PS00892;
DE  Function: Plays a role in the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Stress-induced regulatory protein that modulates the m7GpppX diphosphatase activity of DCS1. {ECO:0000269|PubMed:15240832, ECO:0000269|PubMed:16963086}.
DE  Reference Proteome: Yes;
DE  Interaction: Q06151; IntAct: EBI-786407; Score: 0.87
DE  Interaction: P37366; IntAct: EBI-791370; Score: 0.53
DE  Interaction: Q06218; IntAct: EBI-816740; Score: 0.27
DE  Interaction: P40024; IntAct: EBI-817974; Score: 0.27
DE  Interaction: Q08004; IntAct: EBI-819653; Score: 0.27
DE  Interaction: P07245; IntAct: EBI-821183; Score: 0.27
DE  Interaction: P38829; IntAct: EBI-855499; Score: 0.00
DE  Interaction: Q12179; IntAct: EBI-7886118; Score: 0.40
DE  Interaction: P47035; IntAct: EBI-7998776; Score: 0.40
DE  Interaction: P11484; IntAct: EBI-3687179; Score: 0.35
DE  Interaction: P14680; IntAct: EBI-16286565; Score: 0.35
DE  Interaction: Q12123; IntAct: EBI-21322203; Score: 0.37
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0004857;
GO  GO:0050072;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0000340;
GO  GO:0031670;
GO  GO:0009267;
GO  GO:0000290;
GO  GO:0000956;
GO  GO:0000184;
GO  GO:1903398;
GO  GO:0009408;
GO  GO:0007584;
GO  GO:0006970;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGSQDLASLIGRFKYVRVLDSNPHTKVISLLGSIDGKDAVLTAEKTHFIFDETVRRPSQSGRSTPIFFHREIDEYSFLNG
SQ  ITDLKELTSNDIYYWGLSVLKQHILHNPTAKVNLIWPASQFHIKGYDQQDLHVVRETPDMYRNIVVPFIQEMCTSERMKW
SQ  VNNILYEGAEDDRVVYKEYSSRNKEDGFVILPDMKWDGINIDSLYLVAIVYRDDIKSLRDLNPNHRDWLIRLNKKIKTII
SQ  PQHYDYNVNPDELRVFIHYQPSYYHFHVHIVNIRHPGVGEERGSGMTILLEDVIEALGFLGPEGYMKKTLTYVIGENHDL
SQ  WKKGFKEEVEKQLKHDGIATSPEKGSGFNTNLG
//
ID  Q14203;
PN  Dynactin subunit 1;
GN  DCTN1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17828277}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17828277, ECO:0000269|PubMed:22777741, ECO:0000269|PubMed:25774020, ECO:0000269|PubMed:26972003}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:23985322, ECO:0000269|PubMed:25774020}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:25774020}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25774020}. Nucleus envelope {ECO:0000269|PubMed:20679239}. Cytoplasm, cell cortex {ECO:0000269|PubMed:22327364}. Note=Localizes to microtubule plus ends (PubMed:17828277, PubMed:22777741, PubMed:25774020). Localizes preferentially to the ends of tyrosinated microtubules (PubMed:26972003). Localization at centrosome is regulated by SLK- dependent phosphorylation (PubMed:23985322). Localizes to centrosome in a PARKDA-dependent manner (PubMed:20719959). Localizes to the subdistal appendage region of the centriole in a KIF3A-dependent manner (PubMed:23386061). PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope (PubMed:20679239). {ECO:0000269|PubMed:17828277, ECO:0000269|PubMed:20679239, ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:22777741, ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:23985322, ECO:0000269|PubMed:25774020, ECO:0000269|PubMed:26972003}.
DR  UNIPROT: Q14203;
DR  UNIPROT: A8MY36;
DR  UNIPROT: B4DM45;
DR  UNIPROT: E9PFS5;
DR  UNIPROT: E9PGE1;
DR  UNIPROT: G5E9H4;
DR  UNIPROT: O95296;
DR  UNIPROT: Q6IQ37;
DR  UNIPROT: Q9BRM9;
DR  UNIPROT: Q9UIU1;
DR  UNIPROT: Q9UIU2;
DR  PDB: 1TXQ;
DR  PDB: 2COY;
DR  PDB: 2HKN;
DR  PDB: 2HKQ;
DR  PDB: 2HL3;
DR  PDB: 2HL5;
DR  PDB: 2HQH;
DR  PDB: 3E2U;
DR  PDB: 3TQ7;
DR  Pfam: PF01302;
DR  Pfam: PF12455;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DR  OMIM: 105400;
DR  OMIM: 168605;
DR  OMIM: 601143;
DR  OMIM: 607641;
DR  DisGeNET: 1639;
DE  Function: Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule (PubMed:25185702). Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon (PubMed:23874158). Plays a role in metaphase spindle orientation (PubMed:22327364). Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole (PubMed:23386061). Plays a role in primary cilia formation (PubMed:25774020). {ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:23874158, ECO:0000269|PubMed:25185702, ECO:0000269|PubMed:25774020}.
DE  Disease: Neuronopathy, distal hereditary motor, 7B (HMN7B) [MIM:607641]: A neuromuscular disorder. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:12627231, ECO:0000269|PubMed:16505168, ECO:0000269|PubMed:19136952, ECO:0000269|PubMed:19279216, ECO:0000269|PubMed:22777741}. Note=The disease is caused by variants affecting the gene represented in this entry. Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:15326253, ECO:0000269|PubMed:16240349}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Perry syndrome (PERRYS) [MIM:168605]: A neuropsychiatric disorder characterized by mental depression not responsive to antidepressant drugs or electroconvulsive therapy, sleep disturbances, exhaustion and marked weight loss. Parkinsonism develops later and respiratory failure occurred terminally. {ECO:0000269|PubMed:19136952, ECO:0000269|PubMed:23874158, ECO:0000269|PubMed:24676999, ECO:0000269|PubMed:24881494, ECO:0000269|PubMed:25185702, ECO:0000269|PubMed:26972003}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O00423; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: O08788; IntAct: EBI-2561198; Score: 0.56
DE  Interaction: O15027; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P29991; IntAct: EBI-8829140; Score: 0.37
DE  Interaction: P43034; IntAct: EBI-11382201; Score: 0.48
DE  Interaction: P58546; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9UBN7; IntAct: EBI-25840647; Score: 0.56
DE  Interaction: P42025; IntAct: EBI-367597; Score: 0.54
DE  Interaction: Q96KM6; IntAct: EBI-7216721; Score: 0.37
DE  Interaction: P18669; IntAct: EBI-736541; Score: 0.00
DE  Interaction: P30622; IntAct: EBI-15657003; Score: 0.76
DE  Interaction: P20340; IntAct: EBI-8604645; Score: 0.40
DE  Interaction: P49662; IntAct: EBI-1063339; Score: 0.00
DE  Interaction: P43360; IntAct: EBI-25840462; Score: 0.56
DE  Interaction: Q9H8T0; IntAct: EBI-1070932; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-1072184; Score: 0.00
DE  Interaction: P62330; IntAct: EBI-1073142; Score: 0.00
DE  Interaction: P40337; IntAct: EBI-1073742; Score: 0.00
DE  Interaction: O14593; IntAct: EBI-1079448; Score: 0.00
DE  Interaction: Q9Y2Q3; IntAct: EBI-1080223; Score: 0.00
DE  Interaction: Q7L1Q6; IntAct: EBI-1082566; Score: 0.00
DE  Interaction: O76071; IntAct: EBI-1083392; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-1105616; Score: 0.00
DE  Interaction: Q96G01; IntAct: EBI-7141949; Score: 0.43
DE  Interaction: P10636; IntAct: EBI-7637855; Score: 0.70
DE  Interaction: Q8NFJ9; IntAct: EBI-25840415; Score: 0.56
DE  Interaction: Q96RK4; IntAct: EBI-1805881; Score: 0.63
DE  Interaction: P54256; IntAct: EBI-8013384; Score: 0.65
DE  Interaction: P61164; IntAct: EBI-2559425; Score: 0.40
DE  Interaction: Q99KJ8; IntAct: EBI-2559460; Score: 0.56
DE  Interaction: Q9Z0Y1; IntAct: EBI-2560063; Score: 0.56
DE  Interaction: P47753; IntAct: EBI-2563793; Score: 0.40
DE  Interaction: Q0VEJ0; IntAct: EBI-2563897; Score: 0.40
DE  Interaction: Q99551; IntAct: EBI-2690077; Score: 0.00
DE  Interaction: A0JNT9; IntAct: EBI-7894392; Score: 0.43
DE  Interaction: Q921C5; IntAct: EBI-7894652; Score: 0.35
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q9JK25; IntAct: EBI-8098108; Score: 0.46
DE  Interaction: O14777; IntAct: EBI-8098382; Score: 0.45
DE  Interaction: P42224; IntAct: EBI-3451713; Score: 0.00
DE  Interaction: Q8TCX1; IntAct: EBI-8568044; Score: 0.46
DE  Interaction: O95817; IntAct: EBI-8568339; Score: 0.35
DE  Interaction: P31749; IntAct: EBI-7094924; Score: 0.37
DE  Interaction: Q16543; IntAct: EBI-7112856; Score: 0.37
DE  Interaction: Q6ZU52; IntAct: EBI-7140179; Score: 0.37
DE  Interaction: O14576; IntAct: EBI-25840452; Score: 0.56
DE  Interaction: P51955; IntAct: EBI-7257818; Score: 0.37
DE  Interaction: O60925; IntAct: EBI-7284860; Score: 0.37
DE  Interaction: P13929; IntAct: EBI-5658334; Score: 0.00
DE  Interaction: Q96S44; IntAct: EBI-5665262; Score: 0.00
DE  Interaction: P62136; IntAct: EBI-5564400; Score: 0.37
DE  Interaction: O75381; IntAct: EBI-5911953; Score: 0.35
DE  Interaction: P10209; IntAct: EBI-6509331; Score: 0.37
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q9Y496; IntAct: EBI-8847255; Score: 0.27
DE  Interaction: P28741; IntAct: EBI-8847318; Score: 0.40
DE  Interaction: P88996; IntAct: EBI-9641406; Score: 0.37
DE  Interaction: O41964; IntAct: EBI-9641478; Score: 0.37
DE  Interaction: Q14980; IntAct: EBI-10039064; Score: 0.27
DE  Interaction: Q14653; IntAct: EBI-11321946; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: E9QKK1; IntAct: EBI-10995761; Score: 0.35
DE  Interaction: Q8R1Q8; IntAct: EBI-11000601; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-11027413; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: P62627; IntAct: EBI-11032607; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: Q8R5C5; IntAct: EBI-11073047; Score: 0.35
DE  Interaction: Q8CBY8; IntAct: EBI-11074062; Score: 0.35
DE  Interaction: Q9QZB9; IntAct: EBI-11074142; Score: 0.35
DE  Interaction: Q15691; IntAct: EBI-11091481; Score: 0.86
DE  Interaction: Q9WTI7; IntAct: EBI-11093786; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.48
DE  Interaction: Q14134; IntAct: EBI-11137164; Score: 0.35
DE  Interaction: Q14204; IntAct: EBI-11148090; Score: 0.48
DE  Interaction: P14635; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q96T17; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9BT25; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P31930; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q3KQU3; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: O00139; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9P0I2; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9NQ86; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P36776; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q99643; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q96GD4; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9HAU0; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P61019; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q08AD1; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q96R06; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q01130; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q96P70; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9Y5Y2; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q15555; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q8WWK9; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: O75330; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9BRR8; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q8WVK7; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9NZ32; IntAct: EBI-11366138; Score: 0.62
DE  Interaction: P11137; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q8IWC1; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9NYZ3; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q7Z460; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9UJW0; IntAct: EBI-11366138; Score: 0.62
DE  Interaction: Q9UPY8; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q5SW79; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: O00487; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q8WU90; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q969S3; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q14847; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P43897; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9Y4F5; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P50570; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9ULD2; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: O95373; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q8N2U0; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q8IX90; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: O15075; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q15286; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P51665; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q53H12; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9H3G5; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q99733; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q86V48; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P61163; IntAct: EBI-11366138; Score: 0.62
DE  Interaction: Q96K17; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9HC35; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: O00399; IntAct: EBI-11366138; Score: 0.62
DE  Interaction: Q9Y4L1; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q49MG5; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q00610; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q8IYA6; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9GZQ8; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q99848; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q66K74; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P20290; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q13561; IntAct: EBI-11366138; Score: 0.62
DE  Interaction: O75935; IntAct: EBI-11366138; Score: 0.62
DE  Interaction: P61006; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q13423; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9Y6M1; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q14244; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: O94905; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P30419; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P22570; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: P55209; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q9Y448; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q5JU00; IntAct: EBI-11367780; Score: 0.27
DE  Interaction: Q8N4C6; IntAct: EBI-11374469; Score: 0.27
DE  Interaction: Q8NBT2; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q6P1N0; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: P07203; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q99661; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9BXJ9; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9P1F3; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q5EBL8; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9P289; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q92900; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9Y5B9; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q96CT7; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q7Z4H7; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9BX40; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q13409; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9Y5A9; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: O76041; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q96GY0; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: P41227; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q7KZI7; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9H6D7; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: O75122; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: O14640; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q8TAT6; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: P33981; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q5QJ74; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: P04083; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9H4H8; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: O43663; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q2NL82; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9H6S0; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q8N568; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q96BD8; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9BYV8; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9C0F1; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q5T5Y3; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q16718; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: E9PAV3; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9NX55; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9UHG0; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9UNY4; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9H7E2; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: P49458; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9BWT3; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9BYJ9; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q15058; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q96GA3; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q92974; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q15398; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q8NHV4; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9Y3Y2; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9P2B7; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q99871; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9P270; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q86XJ1; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q9BTE1; IntAct: EBI-21619572; Score: 0.35
DE  Interaction: H9XIJ5; IntAct: EBI-11514215; Score: 0.37
DE  Interaction: P47756; IntAct: EBI-12449631; Score: 0.51
DE  Interaction: P52907; IntAct: EBI-12449631; Score: 0.51
DE  Interaction: Q9Y2I6; IntAct: EBI-12451292; Score: 0.35
DE  Interaction: G3G960; IntAct: EBI-11688985; Score: 0.40
DE  Interaction: Q9UQM7; IntAct: EBI-11913229; Score: 0.00
DE  Interaction: Q8N157; IntAct: EBI-11922091; Score: 0.00
DE  Interaction: Q16082; IntAct: EBI-15187599; Score: 0.37
DE  Interaction: P02511; IntAct: EBI-15187643; Score: 0.37
DE  Interaction: Q3KP66; IntAct: EBI-21617875; Score: 0.35
DE  Interaction: Q99797; IntAct: EBI-21619572; Score: 0.35
DE  Interaction: Q6XUX3; IntAct: EBI-21619572; Score: 0.35
DE  Interaction: P62736; IntAct: EBI-21619572; Score: 0.35
DE  Interaction: D6R9G5; IntAct: EBI-21619572; Score: 0.35
DE  Interaction: Q96MC5; IntAct: EBI-21663233; Score: 0.35
DE  Interaction: Q86WX3; IntAct: EBI-21663135; Score: 0.35
DE  Interaction: Q9NPQ8; IntAct: EBI-21663468; Score: 0.35
DE  Interaction: Q9GZP0; IntAct: EBI-21663347; Score: 0.35
DE  Interaction: Q13748; IntAct: EBI-15642149; Score: 0.44
DE  Interaction: Q9UNH7; IntAct: EBI-16042701; Score: 0.50
DE  Interaction: O95219; IntAct: EBI-16042750; Score: 0.35
DE  Interaction: Q08345; IntAct: EBI-22227061; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21024514; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9NQ75; IntAct: EBI-21373041; Score: 0.00
DE  Interaction: Q9Y5K6; IntAct: EBI-21373015; Score: 0.00
DE  Interaction: Q9UKE5; IntAct: EBI-21373000; Score: 0.00
DE  Interaction: O84166; IntAct: EBI-22302598; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC6; IntAct: EBI-26495724; Score: 0.35
DE  Interaction: P18847; IntAct: EBI-25840405; Score: 0.56
DE  Interaction: O15392; IntAct: EBI-25840395; Score: 0.56
DE  Interaction: P63010; IntAct: EBI-25840385; Score: 0.56
DE  Interaction: O60479; IntAct: EBI-25840435; Score: 0.56
DE  Interaction: P42574; IntAct: EBI-25840425; Score: 0.56
DE  Interaction: Q9ULX5; IntAct: EBI-25840575; Score: 0.56
DE  Interaction: Q8WUW1; IntAct: EBI-25840565; Score: 0.56
DE  Interaction: P62987; IntAct: EBI-25840555; Score: 0.56
DE  Interaction: Q15554; IntAct: EBI-25840542; Score: 0.56
DE  Interaction: P19474; IntAct: EBI-25840525; Score: 0.56
DE  Interaction: Q92834; IntAct: EBI-25840515; Score: 0.56
DE  Interaction: P17980; IntAct: EBI-25840505; Score: 0.56
DE  Interaction: Q9BR81; IntAct: EBI-25840495; Score: 0.56
DE  Interaction: O15381; IntAct: EBI-25840483; Score: 0.56
DE  Interaction: Q6NXG1; IntAct: EBI-25840813; Score: 0.56
DE  Interaction: Q9H0E2; IntAct: EBI-25840803; Score: 0.56
DE  Interaction: P57075; IntAct: EBI-25840793; Score: 0.56
DE  Interaction: Q96RL1; IntAct: EBI-25840783; Score: 0.56
DE  Interaction: O95777; IntAct: EBI-25840771; Score: 0.56
DE  Interaction: Q04323; IntAct: EBI-25840761; Score: 0.56
DE  Interaction: Q9UJ41; IntAct: EBI-25840749; Score: 0.56
DE  Interaction: Q9Y2M5; IntAct: EBI-25840739; Score: 0.56
DE  Interaction: Q99932; IntAct: EBI-25840729; Score: 0.56
DE  Interaction: Q96EK5; IntAct: EBI-25840719; Score: 0.56
DE  Interaction: Q8N488; IntAct: EBI-25840708; Score: 0.56
DE  Interaction: O00308; IntAct: EBI-25840688; Score: 0.56
DE  Interaction: Q15436; IntAct: EBI-25840677; Score: 0.56
DE  Interaction: Q9BSL1; IntAct: EBI-25840667; Score: 0.56
DE  Interaction: O75886; IntAct: EBI-25840657; Score: 0.56
DE  Interaction: Q6DN90; IntAct: EBI-25840625; Score: 0.56
DE  Interaction: Q9UHY8; IntAct: EBI-25840615; Score: 0.56
DE  Interaction: O95671; IntAct: EBI-25840605; Score: 0.56
DE  Interaction: Q9UNS2; IntAct: EBI-25840595; Score: 0.56
DE  Interaction: P46379; IntAct: EBI-25840585; Score: 0.56
DE  Interaction: Q6ZTN6; IntAct: EBI-25840998; Score: 0.56
DE  Interaction: Q8NBM4; IntAct: EBI-25840983; Score: 0.56
DE  Interaction: Q8TC29; IntAct: EBI-25840966; Score: 0.56
DE  Interaction: Q8IYW5; IntAct: EBI-25840956; Score: 0.56
DE  Interaction: Q96D59; IntAct: EBI-25840946; Score: 0.56
DE  Interaction: Q8WVJ9; IntAct: EBI-25840936; Score: 0.56
DE  Interaction: Q9BYZ2; IntAct: EBI-25840926; Score: 0.56
DE  Interaction: Q8IY31; IntAct: EBI-25840916; Score: 0.56
DE  Interaction: Q8N594; IntAct: EBI-25840906; Score: 0.56
DE  Interaction: Q96JM7; IntAct: EBI-25840896; Score: 0.56
DE  Interaction: Q9GZS3; IntAct: EBI-25840886; Score: 0.56
DE  Interaction: Q71RG4; IntAct: EBI-25840876; Score: 0.56
DE  Interaction: A4FUJ8; IntAct: EBI-25840866; Score: 0.56
DE  Interaction: Q9HCE7; IntAct: EBI-25840856; Score: 0.56
DE  Interaction: Q6GQQ9; IntAct: EBI-25840844; Score: 0.56
DE  Interaction: Q96FW1; IntAct: EBI-25840833; Score: 0.56
DE  Interaction: Q9NV79; IntAct: EBI-25840823; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25938504; Score: 0.56
DE  Interaction: P51114; IntAct: EBI-26510253; Score: 0.37
DE  Interaction: P49639; IntAct: EBI-26512419; Score: 0.37
DE  Interaction: P13569; IntAct: EBI-27087549; Score: 0.35
DE  Interaction: Q12792; IntAct: EBI-28939213; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q6ZMQ8; IntAct: EBI-32723474; Score: 0.27
GO  GO:0030424;
GO  GO:0005938;
GO  GO:0099738;
GO  GO:0031252;
GO  GO:0120103;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030286;
GO  GO:0045171;
GO  GO:0000776;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0015630;
GO  GO:0035371;
GO  GO:0072686;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0019901;
GO  GO:0048156;
GO  GO:0015631;
GO  GO:0051301;
GO  GO:0010457;
GO  GO:0031122;
GO  GO:0000132;
GO  GO:0099558;
GO  GO:0032402;
GO  GO:0034454;
GO  GO:0000278;
GO  GO:0061744;
GO  GO:0007399;
GO  GO:0007528;
GO  GO:0050905;
GO  GO:0070050;
GO  GO:1990535;
GO  GO:1905515;
GO  GO:0051081;
GO  GO:0007097;
GO  GO:0090063;
GO  GO:0031116;
GO  GO:1904398;
GO  GO:0060236;
GO  GO:0042147;
GO  GO:0021517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFT
SQ  CDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGV
SQ  AGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAE
SQ  DKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAES
SQ  LQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQ
SQ  ELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARE
SQ  TELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFA
SQ  ETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFELSENCSERP
SQ  GLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPL
SQ  TKAIKYYQHLYSIHLAEQPEDCTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKK
SQ  IRRRMPGTDAPGIPAALAFGPQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLLVAALEELAFKASEQIYGT
SQ  PSSSPYECLRQSCNILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLK
SQ  IKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQ
SQ  SKRTIEGLRGPPPSGIATLVSGIAGEEQQRGAIPGQAPGSVPGPGLVKDSPLLLQQISAMRLHISQLQHENSILKGAQMK
SQ  ASLASLPPLHVAKLSHEGPGSELPAGALYRKTSQLLETLNQLSTHTHVVDITRTSPAAKSPSAQLMEQVAQLKSLSDTVE
SQ  KLKDEVLKETVSQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGFGQRHRLVLTQEQLHQLHSRLIS
//
ID  O08788;
PN  Dynactin subunit 1;
GN  Dctn1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14203}. Nucleus envelope {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules (PubMed:16954346). Localization at centrosome is regulated by SLK- dependent phosphorylation. Localizes to centrosome in a PARKDA- dependent manner. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope (By similarity). Localizes to the subdistal appendage region of the centriole in a KIF3A-dependent manner (PubMed:23386061). {ECO:0000250|UniProtKB:Q14203, ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:23386061}.
DR  UNIPROT: O08788;
DR  UNIPROT: E9QLJ1;
DR  UNIPROT: Q3TZG7;
DR  Pfam: PF01302;
DR  Pfam: PF12455;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DE  Function: Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation. {ECO:0000250|UniProtKB:Q14203}.
DE  Reference Proteome: Yes;
DE  Interaction: Q64368; IntAct: EBI-6946418; Score: 0.40
DE  Interaction: P33175; IntAct: EBI-8013466; Score: 0.40
DE  Interaction: P06493; IntAct: EBI-2561198; Score: 0.40
DE  Interaction: Q9UJW0; IntAct: EBI-2561198; Score: 0.56
DE  Interaction: P61163; IntAct: EBI-2561198; Score: 0.56
DE  Interaction: Q9NZ32; IntAct: EBI-2561198; Score: 0.56
DE  Interaction: Q9BTE1; IntAct: EBI-2561198; Score: 0.56
DE  Interaction: Q14203; IntAct: EBI-2561198; Score: 0.56
DE  Interaction: O00399; IntAct: EBI-2561198; Score: 0.56
DE  Interaction: P47755; IntAct: EBI-2561198; Score: 0.56
DE  Interaction: A8K8J9; IntAct: EBI-2561198; Score: 0.40
DE  Interaction: O75935; IntAct: EBI-2561198; Score: 0.40
DE  Interaction: P42025; IntAct: EBI-2561198; Score: 0.56
DE  Interaction: O35685; IntAct: EBI-7691158; Score: 0.35
DE  Interaction: Q61768; IntAct: EBI-7691193; Score: 0.35
DE  Interaction: A0JNT9; IntAct: EBI-7894187; Score: 0.27
DE  Interaction: Q8CG73; IntAct: EBI-4284701; Score: 0.35
DE  Interaction: Q13561; IntAct: EBI-6857116; Score: 0.53
DE  Interaction: P28741; IntAct: EBI-8847308; Score: 0.46
DE  Interaction: Q8BKC8; IntAct: EBI-9085471; Score: 0.35
DE  Interaction: P48651; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: Q9Y592; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: Q9NP97; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: P47756; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: P52907; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: O14949; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: Q86XL3; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: O15235; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: Q9BV73; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: Q15643; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: B4E1G1; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: Q9Y6G9; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: Q96L93; IntAct: EBI-11066549; Score: 0.35
DE  Interaction: Q80VJ8; IntAct: EBI-11666413; Score: 0.35
DE  Interaction: Q6A078; IntAct: EBI-11784184; Score: 0.50
DE  Interaction: O88485; IntAct: EBI-15640911; Score: 0.35
DE  Interaction: Q7TMB8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16726570; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
DE  Interaction: Q96LT7; IntAct: EBI-26613562; Score: 0.35
GO  GO:0030424;
GO  GO:0005938;
GO  GO:0099738;
GO  GO:0031252;
GO  GO:0120103;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0005829;
GO  GO:0045171;
GO  GO:0000776;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0015630;
GO  GO:0035371;
GO  GO:0072686;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0030904;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0019901;
GO  GO:0015631;
GO  GO:0051301;
GO  GO:0010457;
GO  GO:0031122;
GO  GO:0000132;
GO  GO:0032402;
GO  GO:0034454;
GO  GO:0061744;
GO  GO:0007528;
GO  GO:0050905;
GO  GO:0070050;
GO  GO:1990535;
GO  GO:1905515;
GO  GO:0051081;
GO  GO:0007097;
GO  GO:0090316;
GO  GO:0090063;
GO  GO:0031116;
GO  GO:1904398;
GO  GO:0060236;
GO  GO:0042147;
GO  GO:0021517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQSRRHMSSRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFT
SQ  CDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGV
SQ  AGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSE
SQ  DKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAES
SQ  LQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQ
SQ  ELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARE
SQ  TELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFA
SQ  ETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERP
SQ  GLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPL
SQ  TKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMGVEVGRLRAFLQGGQEATDIALLLRDLETSCSDTRQFCKK
SQ  IRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGS
SQ  PSSSPYECLRQSCTILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLK
SQ  IKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQ
SQ  SKRTIEGLRGPPPSGIATLVSGIAGEEPQRGGAPGQAPGALPGPGLVKDSPLLLQQISAMRLHISQLQHENSILRGAQMK
SQ  ASLAALPPLHVAKLSLPPHEGPGGNLVAGALYRKTSQLLEKLNQLSTHTHVVDITRSSPAAKSPSAQLMEQVAQLKSLSD
SQ  TIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHSRLI
SQ  S
//
ID  P28023;
PN  Dynactin subunit 1;
GN  Dctn1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14203}. Nucleus envelope {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules. Localization at centrosome is regulated by SLK-dependent phosphorylation. Localizes to centrosome in a PARKDA-dependent manner. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope. Localizes to the subdistal appendage region of the centriole in a KIF3A-dependent manner. {ECO:0000250|UniProtKB:O08788, ECO:0000250|UniProtKB:Q14203}.
DR  UNIPROT: P28023;
DR  PDB: 2M02;
DR  PDB: 2MPX;
DR  Pfam: PF01302;
DR  Pfam: PF12455;
DR  PROSITE: PS00845;
DR  PROSITE: PS50245;
DE  Function: Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation. {ECO:0000250|UniProtKB:Q14203}.
DE  Reference Proteome: Yes;
DE  Interaction: A0JNT9; IntAct: EBI-7894963; Score: 0.27
DE  Interaction: P54256; IntAct: EBI-9639028; Score: 0.49
DE  Interaction: P54645; IntAct: EBI-16399805; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16400563; Score: 0.35
DE  Interaction: P28023; IntAct: EBI-16128725; Score: 0.56
DE  Interaction: Q969Q1; IntAct: EBI-21997483; Score: 0.35
DE  Interaction: P19332; IntAct: EBI-26374040; Score: 0.35
GO  GO:0030424;
GO  GO:0005938;
GO  GO:0099738;
GO  GO:0031252;
GO  GO:0120103;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0035371;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0060090;
GO  GO:0019901;
GO  GO:0015631;
GO  GO:0051301;
GO  GO:0010457;
GO  GO:0031122;
GO  GO:0000132;
GO  GO:0032402;
GO  GO:0034454;
GO  GO:0061744;
GO  GO:0007528;
GO  GO:0050905;
GO  GO:0070050;
GO  GO:1990535;
GO  GO:1905515;
GO  GO:0051081;
GO  GO:0007097;
GO  GO:0090316;
GO  GO:0090063;
GO  GO:0031116;
GO  GO:1904398;
GO  GO:0060236;
GO  GO:0042147;
GO  GO:0021517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQSKRHMYNRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFT
SQ  CDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKILKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGV
SQ  AGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRDQVRDLEEKLETLRLKRSE
SQ  DKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEAKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESL
SQ  QQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQE
SQ  LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARET
SQ  ELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAE
SQ  TKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPG
SQ  LRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLT
SQ  KAIKYYQHLYSIHLAEQPEESTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKI
SQ  RRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSP
SQ  SSSPYECLRQSCSILISTMNKLATAMQEGEYDAERPPSKPPPVEPWPAALRAEITDAEGLGLKLEDRETVIKELKKSLKI
SQ  KGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQTLLRKKEKEFEETMDALQADIDQLEAEKTELKQRLNSQS
SQ  KRTIEGLRGPPPSGIATLVSGIAGEEQQRGGTPGQAPGALPGPGPVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKA
SQ  SLAALPPLHVAKFSLPPHEGPGGNLLSGALYRKTSQLLEKLNQLSTYTHVVDITRSSPACKSPSAQLMEQVAQLKSLSDT
SQ  IEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHGRLIS
//
ID  Q5W5U4;
PN  Probable ATP-dependent RNA helicase DDX4;
GN  DDX4;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q61496}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}. Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q61496}.
DR  UNIPROT: Q5W5U4;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs. {ECO:0000250|UniProtKB:Q61496}.
DE  Reference Proteome: Yes;
GO  GO:0033391;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0071546;
GO  GO:0071547;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003676;
GO  GO:0003724;
GO  GO:0030154;
GO  GO:0043046;
GO  GO:0031047;
GO  GO:0007141;
GO  GO:0007140;
GO  GO:0010529;
GO  GO:1990511;
GO  GO:0034587;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDEDWEAEIIKPHISSYVPVFEKDRYSSGANGDTFNRTPASSSEMGDGSSRRDHFMRSGFASGRSLGNRDPGESNKREN
SQ  TSTVGGFGVGKSFGNRGFSNNKFEEGDSSGFWRESSIDCEDNQTRNRGFSKRGGYQDGNDSEALGSSRRGGRGSFRGCRG
SQ  GFGRGSPNSDYEQDEGTQRSGGIFGSRRSALSGAGNGDTFQSRSGGGSGRGGYKGLNEEVITGSGKNSWKSEAEGGESGD
SQ  TQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDPPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYS
SQ  IPIIQGGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVV
SQ  IYGGTQLGHSIRQIVQGCNILCATPGRLMDVIGKEKIGLRQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTL
SQ  MFSATFPEEIQRLAGEFLKSNYLFVAVGQVGGACRDVQQTILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIAT
SQ  FLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTG
SQ  RAISFFDLESDSQLAQPLVKVLSDAQQDVPAWLEEIAFSTYGPGFSGNARGNVFASVDTRKNYPGKSSLNTAGFSSTQAP
SQ  NPVDDESWD
//
ID  Q9NQI0;
PN  Probable ATP-dependent RNA helicase DDX4;
GN  DDX4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q61496}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}. Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q61496}.
DR  UNIPROT: Q9NQI0;
DR  UNIPROT: A8K8Q2;
DR  UNIPROT: B3KSF4;
DR  UNIPROT: D6RDK4;
DR  UNIPROT: E9PCD8;
DR  UNIPROT: Q5M7Z3;
DR  UNIPROT: Q86VX0;
DR  UNIPROT: Q9NT92;
DR  UNIPROT: Q9NYB1;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DR  OMIM: 605281;
DR  DisGeNET: 54514;
DE  Function: ATP-dependent RNA helicase required during spermatogenesis (PubMed:10920202, PubMed:21034600). Required to repress transposable elements and preventing their mobilization, which is essential for the germline integrity (By similarity). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (By similarity). Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle (By similarity). Required for PIWIL2 slicing- triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs (By similarity). {ECO:0000250|UniProtKB:Q61496, ECO:0000269|PubMed:10920202, ECO:0000269|PubMed:21034600}.
DE  Reference Proteome: Yes;
DE  Interaction: P12931; IntAct: EBI-7609853; Score: 0.40
DE  Interaction: Q8JPQ9; IntAct: EBI-6159460; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q96GG9; IntAct: EBI-21325177; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q9NZ43; IntAct: EBI-10887976; Score: 0.35
DE  Interaction: Q9Y2H1; IntAct: EBI-20624829; Score: 0.27
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0071546;
GO  GO:0071547;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0140693;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0030154;
GO  GO:0043046;
GO  GO:0030317;
GO  GO:0007276;
GO  GO:0031047;
GO  GO:0007141;
GO  GO:0007140;
GO  GO:0010529;
GO  GO:1990511;
GO  GO:0034587;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDEDWEAEINPHMSSYVPIFEKDRYSGENGDNFNRTPASSSEMDDGPSRRDHFMKSGFASGRNFGNRDAGECNKRDNTS
SQ  TMGGFGVGKSFGNRGFSNSRFEDGDSSGFWRESSNDCEDNPTRNRGFSKRGGYRDGNNSEASGPYRRGGRGSFRGCRGGF
SQ  GLGSPNNDLDPDECMQRTGGLFGSRRPVLSGTGNGDTSQSRSGSGSERGGYKGLNEEVITGSGKNSWKSEAEGGESSDTQ
SQ  GPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIP
SQ  IILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIY
SQ  GGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMF
SQ  SATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQTVLQVGQFSKREKLVEILRNIGDERTMVFVETKKKADFIATFL
SQ  CQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRA
SQ  ISFFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSTLNTAGFSSSQAPNPVDD
SQ  ESWD
//
ID  Q4R5S7;
PN  Probable ATP-dependent RNA helicase DDX4;
GN  DDX4;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q61496}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}. Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q61496}.
DR  UNIPROT: Q4R5S7;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs. {ECO:0000250|UniProtKB:Q61496}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0071546;
GO  GO:0071547;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003676;
GO  GO:0003724;
GO  GO:0030154;
GO  GO:0043046;
GO  GO:0031047;
GO  GO:0007141;
GO  GO:0007140;
GO  GO:0010529;
GO  GO:1990511;
GO  GO:0034587;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDEDWEAEINPHMSSYVPIFEKDRYSSGENGDNFNRTPTSSSEMDDGPSRRDHFMKSGFASGRNFGNRDAGESNKRDNT
SQ  STMGGFGVGKSFGNRGFSNSKFEDGDSSGFWRESSNDCEDNPTRNRGFSKRGGYRDGNNSEASGPSRRGGRSSFRGCRGG
SQ  FGLGSPNNDLDPDECMQRTGGLFGSRRPALSGTGNGDTSQSRSGSGSERGGYKGLNEEVITGSGKNSWKSEAEGGESSDT
SQ  QGPKVTYIPPPPPEDEDSIFAHYQTGISFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSI
SQ  PIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASCFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVI
SQ  YGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLM
SQ  FSATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQTVLQVGQFSKREKLVEILRNIGDERTMVFVETKKKADFIATF
SQ  LCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGR
SQ  AISFFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSSLNTAGFSSSQAPNPVD
SQ  DESWD
//
ID  Q61496;
PN  ATP-dependent RNA helicase DDX4;
GN  Ddx4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:20439430, ECO:0000269|PubMed:22900038}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22900038}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000269|PubMed:20439430}.
DR  UNIPROT: Q61496;
DR  UNIPROT: Q9D5X7;
DR  PDB: 5JIU;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:20439430, PubMed:28633017). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (PubMed:20439430, PubMed:28633017). Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle (PubMed:20439430, PubMed:28633017). Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs (PubMed:28633017). {ECO:0000269|PubMed:20439430, ECO:0000269|PubMed:28633017}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UPY3; IntAct: EBI-15569634; Score: 0.54
GO  GO:0033391;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0071546;
GO  GO:0071547;
GO  GO:1990904;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0030154;
GO  GO:0043046;
GO  GO:0030317;
GO  GO:0007276;
GO  GO:0031047;
GO  GO:0007141;
GO  GO:0007140;
GO  GO:0010529;
GO  GO:1990511;
GO  GO:0034587;
GO  GO:0032880;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDEDWEAEILKPHVSSYVPVFEKDKYSSGANGDTFNRTSASSDIGESSKKENTSTTGGFGRGKGFGNRGFLNNKFEEGD
SQ  SSGFWKESNNDCEDNQTRSRGFSKRGGCQDGNDSEASGPFRRGGRGSFRGCRGGFGLGRPNSESDQDQGTQRGGGLFGSR
SQ  KPAASDSGNGDTYQSRSGSGRGGYKGLNEEVVTGSGKNSWKSETEGGESSDSQGPKVTYIPPPPPEDEDSIFAHYQTGIN
SQ  FDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL
SQ  AHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSVRQIVQGCNILCATPGRLM
SQ  DIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGDFLKSSYLFVAVGQ
SQ  VGGACRDVQQTILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFR
SQ  CGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDTDSDNHLAQPLVKVLSDAQQDV
SQ  PAWLEEIAFSTYVPPSFSSSTRGGAVFASVDTRKNYQGKHTLNTAGISSSQAPNPVDDESWD
//
ID  Q6GWX0;
PN  Probable ATP-dependent RNA helicase DDX4;
GN  DDX4;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q61496}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}. Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q61496}.
DR  UNIPROT: Q6GWX0;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs. {ECO:0000250|UniProtKB:Q61496}.
DE  Reference Proteome: Yes;
GO  GO:0033391;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0071546;
GO  GO:0071547;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0030154;
GO  GO:0043046;
GO  GO:0007276;
GO  GO:0031047;
GO  GO:0007141;
GO  GO:0007140;
GO  GO:0010529;
GO  GO:1990511;
GO  GO:0034587;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDEDWEAEINPHVSSYVPIFEKDGYSGENGDKFNRTTASSSEMDDGPSGRDHFMKSGFTSGRSYGKRDAGESNKRENTS
SQ  TTGGFGVGKSFGNRGFSNNRFEDGDSSGFWRESTNDCEDNTTRNRGFSKRGGSRDGNKSEASGPFRRGGRGSFRGCRGGF
SQ  GLGSQNSELDPDQGMQRGGGLFGSGRPAASDTGNGDTYQSRSGRGRGGYKGLNEEVVTGSGKNSWKSEAEGGESSDTQGP
SQ  KVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPII
SQ  LAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGG
SQ  TQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSA
SQ  TFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQADLQVGQYSKREKLLEILRNIGDERTMVFVETKKKADFIATFLCQ
SQ  EKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAIS
SQ  FFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSTLNTAGFSSSQAPNPVDDES
SQ  WD
//
ID  Q64060;
PN  Probable ATP-dependent RNA helicase DDX4;
GN  Ddx4;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q61496}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}. Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q61496}.
DR  UNIPROT: Q64060;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs. {ECO:0000250|UniProtKB:Q61496}.
DE  Reference Proteome: Yes;
GO  GO:0033391;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0071546;
GO  GO:0071547;
GO  GO:1990904;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0030154;
GO  GO:0043046;
GO  GO:0030317;
GO  GO:0007276;
GO  GO:0031047;
GO  GO:0007141;
GO  GO:0007140;
GO  GO:0010529;
GO  GO:1990511;
GO  GO:0034587;
GO  GO:0032880;
GO  GO:0080021;
GO  GO:0032526;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDEDWEAEILKPHVSSYVPVFEKDKYSSGANGDTFNRTSASSSEMEDGPSGRDHFMRSGFSSGRNLGNRDIGESSKRET
SQ  TSTTGGFGRGKGFGNRGFLNNKFEEGDSSGFWKESTNDCEDTQTRSRGFSKRGGYPDGNDSEASGPFRRGGRDSEYDQDQ
SQ  GSQRGGGLFGSRKPAASDSGSGDTFQSRSGNARGAYKGLNEEVVTGSGKNSWKSEAEGGESSDIQGPKVTYIPPPPPEDE
SQ  DSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTG
SQ  SGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQFGHSIRQIVQG
SQ  CNILCATPGRLMDIIGKEKIGLKQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLLFSATFPEEIQRLAGEF
SQ  LKSNYLFVAVGQVGGACRDVQQSILQVGPVFKKRKLVEILRNIGDERPMVFVETKKKADFIATFLCQEKISTTSIHGDRE
SQ  QREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFNLPSTIDEYVHRIGRTGRCGNTGRAISFFDTESDNHLAQP
SQ  LVKVLSDAQQDVPAWLEEIAFSSYAPPSFSNSTRGAVFASFDTRKNFQGKNTLNTAGISSAQAPNPVDDESWD
//
ID  Q9H4E7;
PN  Differentially expressed in FDCP 6 homolog;
GN  DEF6;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15023524}. Cell membrane {ECO:0000269|PubMed:15023524, ECO:0000305|PubMed:12651066}. Nucleus {ECO:0000269|PubMed:15023524}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15023524}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15023524}. Cell projection, filopodium {ECO:0000269|PubMed:15023524}. Note=Recruited to the plasma membrane upon binding phosphatidylinositol 3,4,5-trisphosphate (PubMed:15023524). Binds to actin filaments (PubMed:15023524). {ECO:0000269|PubMed:15023524}.
DR  UNIPROT: Q9H4E7;
DR  UNIPROT: Q86VF4;
DR  Pfam: PF00169;
DR  PROSITE: PS50003;
DR  OMIM: 610094;
DR  OMIM: 619573;
DR  DisGeNET: 50619;
DE  Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which plays a role in the activation of Rho GTPases RAC1, RhoA and CDC42 (PubMed:12651066, PubMed:15023524). Can regulate cell morphology in cooperation with activated RAC1 (By similarity). Involved in immune homeostasis by ensuring proper trafficking and availability of T-cell regulator CTLA-4 at T-cell surface (PubMed:31308374). Plays a role in Th2 (T helper cells) development and/or activation, perhaps by interfering with ZAP70 signaling (By similarity). {ECO:0000250|UniProtKB:Q8C2K1, ECO:0000269|PubMed:12651066, ECO:0000269|PubMed:15023524, ECO:0000269|PubMed:31308374}.
DE  Disease: Immunodeficiency 87 and autoimmunity (IMD87) [MIM:619573]: An autosomal recessive disorder with onset in infancy or early childhood. It is characterized by increased susceptibility to infections, often Epstein-Barr virus, as well as lymphadenopathy or autoimmune manifestations, predominantly hemolytic anemia. The disorder results primarily from defects in T-cell function. {ECO:0000269|PubMed:31308374, ECO:0000269|PubMed:32562707}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-10306705; Score: 0.56
DE  Interaction: Q9H0H0; IntAct: EBI-24620161; Score: 0.56
DE  Interaction: Q9BUH8; IntAct: EBI-754471; Score: 0.37
DE  Interaction: Q61738; IntAct: EBI-1786346; Score: 0.37
DE  Interaction: Q8ZAR2; IntAct: EBI-2871608; Score: 0.00
DE  Interaction: Q8D0E1; IntAct: EBI-2871601; Score: 0.00
DE  Interaction: I6L996; IntAct: EBI-10306695; Score: 0.72
DE  Interaction: Q8IX15; IntAct: EBI-10306735; Score: 0.56
DE  Interaction: P15884; IntAct: EBI-10306715; Score: 0.67
DE  Interaction: Q00587; IntAct: EBI-10306725; Score: 0.56
DE  Interaction: Q96AQ6; IntAct: EBI-10306747; Score: 0.56
DE  Interaction: Q9NRA8; IntAct: EBI-10306757; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-24304101; Score: 0.56
DE  Interaction: Q96JM7; IntAct: EBI-24305175; Score: 0.56
DE  Interaction: Q86T90; IntAct: EBI-24326579; Score: 0.56
DE  Interaction: A6NC98; IntAct: EBI-24344394; Score: 0.56
DE  Interaction: P25786; IntAct: EBI-24699153; Score: 0.56
DE  Interaction: Q96N21; IntAct: EBI-24729596; Score: 0.56
DE  Interaction: O95391; IntAct: EBI-24748905; Score: 0.56
DE  Interaction: O00422; IntAct: EBI-24753175; Score: 0.56
DE  Interaction: Q8WZA2; IntAct: EBI-23888902; Score: 0.56
DE  Interaction: Q86YV0; IntAct: EBI-24370130; Score: 0.56
DE  Interaction: Q9NYA3; IntAct: EBI-24382536; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-24401680; Score: 0.56
DE  Interaction: Q15323; IntAct: EBI-24408384; Score: 0.56
DE  Interaction: Q7Z5H3; IntAct: EBI-25263076; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-24580521; Score: 0.56
DE  Interaction: P0C7X2; IntAct: EBI-24745278; Score: 0.56
DE  Interaction: Q9ULK0; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q9P258; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q9NXR7; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q9NXF7; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q9NWV8; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q9HCJ0; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q96JM3; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q92625; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q8N6N3; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q8IUH3; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q7Z4W1; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q15018; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q04759; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: Q00653; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: P46736; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: P35612; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: P28370; IntAct: EBI-21558763; Score: 0.35
DE  Interaction: A6NI28; IntAct: EBI-21558763; Score: 0.35
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0030175;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005085;
GO  GO:0051056;
GO  GO:0098876;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALRKELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLHIPHDPVALEEHFRDDDDGPVSSQGYMPYLNKYILDKV
SQ  EEGAFVKEHFDELCWTLTAKKNYRADSNGNSMLSNQDAFRLWCLFNFLSEDKYPLIMVPDEVEYLLKKVLSSMSLEVSLG
SQ  ELEELLAQEAQVAQTTGGLSVWQFLELFNSGRCLRGVGRDTLSMAIHEVYQELIQDVLKQGYLWKRGHLRRNWAERWFQL
SQ  QPSCLCYFGSEECKEKRGIIPLDAHCCVEVLPDRDGKRCMFCVKTANRTYEMSASDTRQRQEWTAAIQMAIRLQAEGKTS
SQ  LHKDLKQKRREQREQRERRRAAKEEELLRLQQLQEEKERKLQELELLQEAQRQAERLLQEEEERRRSQHRELQQALEGQL
SQ  REAEQARASMQAEMELKEEEAARQRQRIKELEEMQQRLQEALQLEVKARRDEESVRIAQTRLLEEEEEKLKQLMQLKEEQ
SQ  ERYIERAQQEKEELQQEMAQQSRSLQQAQQQLEEVRQNRQRADEDVEAAQRKLRQASTNVKHWNVQMNRLMHPIEPGDKR
SQ  PVTSSSFSGFQPPLLAHRDSSLKRLTRWGSQGNRTPSPNSNEQQKSLNGGDEAPAPASTPQEDKLDPAPEN
//
ID  Q8C2K1;
PN  Differentially expressed in FDCP 6;
GN  Def6;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12648457}. Cell membrane {ECO:0000269|PubMed:12648457}. Nucleus {ECO:0000250|UniProtKB:Q9H4E7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9H4E7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H4E7}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9H4E7}. Note=Recruited to the plasma membrane upon binding phosphatidylinositol 3,4,5-trisphosphate. Binds to actin filaments. {ECO:0000250|UniProtKB:Q9H4E7}.
DR  UNIPROT: Q8C2K1;
DR  UNIPROT: A1KXF9;
DR  UNIPROT: B2KF17;
DR  UNIPROT: Q0VBU6;
DR  UNIPROT: Q3V3M7;
DR  UNIPROT: Q80XA9;
DR  UNIPROT: Q9CRJ2;
DR  Pfam: PF00169;
DR  PROSITE: PS50003;
DE  Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which plays a role in the activation of Rho GTPases RAC1, RhoA and CDC42 (PubMed:12648457, PubMed:12923183). Can regulate cell morphology in cooperation with activated RAC1 (PubMed:12648457, PubMed:12923183). Involved in immune homeostasis by ensuring proper trafficking and availability of T-cell regulator CTLA-4 at T-cell surface (By similarity). Plays a role in Th2 (T helper cells) development and/or activation, perhaps by interfering with ZAP70 signaling. Required for optimal T-cell effector function, lymphocyte homeostasis and the prevention of systemic autoimmunity (By similarity). {ECO:0000250|UniProtKB:Q9H4E7, ECO:0000269|PubMed:12648457, ECO:0000269|PubMed:12923183}.
DE  Disease: Note=Defects in Def6 results in spontaneous development of a lupus-like syndrome in aging female mice. It is characterized by the accumulation of effector/memory T-cells and IgG B-cells, profound hypergammaglobulinemia, autoantibody production, and glomerulonephritis. {ECO:0000269|PubMed:12923183}.
DE  Reference Proteome: Yes;
DE  Interaction: Q61738; IntAct: EBI-1786373; Score: 0.54
DE  Interaction: Q3U1F9; IntAct: EBI-12603117; Score: 0.40
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0030175;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098876;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALRKELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLNIPHDPVALEEHFRDDDDGPVSSQGYMPYLNKYILDKV
SQ  EEGAFVKEHFDELCWTLTAKKNYRADGIGSSPLSNQDAFRLWCLFNFLSEDKYPLIMVPDEVEYLLKKLLGSLSLEMGLG
SQ  ELEELLAQDAQSAQTAVGLSVWQFLELFNSGRCLRGVGRDSLSMAIQEVYQELIQDVLKQGYLWKRGHLRRNWAERWFQL
SQ  QPSSLCYFGSEECKEKRGTIPLDAHCCVEVLPDREGKRCMFCVKTASRTYEMSASDTRQRQEWTAAIQTAIRLQAEGKTS
SQ  LHKDLKQKRREQREQRERRRAAKEEELLRLQQLQEEKERKLQELELLQEAQRQAERLLQEEEERRRSQHKELQQALEGQL
SQ  REAEQARASMQAEMELKKEEAARQRQRIAELEEMQERLQEALQLEVKARRDEEAVRLAQTRLLEEEEEKLKQLMHLKEEQ
SQ  ERYIERAQQEKQELQQEMALQSRSLQHAQQQLEEVRQNRQRADEDVEAAQRKLRQASTNVKHWNVQMNRLMHPIEPGDKR
SQ  PTTSSSFTGFQPPPLARRDSSLKRLTRWGSQGNRTLSVNSSEQKSLNGGDETPILALASQEEKLDPAPGN
//
ID  Q08DM1;
PN  Dematin;
GN  DMTN;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000250}. Endomembrane system {ECO:0000250}. Cell projection {ECO:0000250}. Note=Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane (By similarity). {ECO:0000250}.
DR  UNIPROT: Q08DM1;
DR  Pfam: PF16182;
DR  Pfam: PF02209;
DR  PROSITE: PS51089;
DE  Function: Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Also plays a role as a modulator of actin dynamics in fibroblasts; acts as negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0031253;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031095;
GO  GO:0014731;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0043621;
GO  GO:0005102;
GO  GO:0030507;
GO  GO:0030036;
GO  GO:0051017;
GO  GO:0051693;
GO  GO:0090527;
GO  GO:0035585;
GO  GO:0035584;
GO  GO:0071277;
GO  GO:0071320;
GO  GO:0048821;
GO  GO:0030032;
GO  GO:0010812;
GO  GO:0051895;
GO  GO:0033137;
GO  GO:0010801;
GO  GO:0050732;
GO  GO:0090315;
GO  GO:1900025;
GO  GO:0030194;
GO  GO:0010763;
GO  GO:2001046;
GO  GO:1901731;
GO  GO:1900026;
GO  GO:0090303;
GO  GO:0070560;
GO  GO:0065003;
GO  GO:0032956;
GO  GO:0008360;
GO  GO:0051489;
GO  GO:0010591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERLQKQPLTSPGSVSSSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPR
SQ  SRERSLSPKSTSPPPSPEVWAESRSPGTISQASAPRTAGTPRTSLPHFHHPETTRPDSNIYKKPPIYKQRAESTGGSPQS
SQ  KHPIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQRE
SQ  ELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHAGTSKSSSLPAYGRTTLSRLQSTDFSPSGSEAESPGLQ
SQ  NGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNRGRTKLPPGVDRMRLERHLSAEDFSRVFSMSPEEFGKLALWKRNELK
SQ  KKASLF
//
ID  Q08495;
PN  Dematin;
GN  DMTN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, cytosol. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton. Cell membrane. Membrane {ECO:0000250}. Endomembrane system. Cell projection {ECO:0000250}. Note=Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane. Detected at the cell membrane and at the parasitophorous vacuole in malaria-infected erythrocytes at late stages of plasmodium berghei or falciparum development.
DR  UNIPROT: Q08495;
DR  UNIPROT: A8K0T5;
DR  UNIPROT: B3KP70;
DR  UNIPROT: B3KRH3;
DR  UNIPROT: B4DI75;
DR  UNIPROT: E9PEJ0;
DR  UNIPROT: Q13215;
DR  UNIPROT: Q9BRE3;
DR  PDB: 1QZP;
DR  PDB: 1ZV6;
DR  Pfam: PF16182;
DR  Pfam: PF02209;
DR  PROSITE: PS51089;
DR  OMIM: 125305;
DR  DisGeNET: 2039;
DE  Function: Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Also plays a role as a modulator of actin dynamics in fibroblasts; acts as a negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation. {ECO:0000269|PubMed:10565303, ECO:0000269|PubMed:11856323, ECO:0000269|PubMed:18347014, ECO:0000269|PubMed:19241372, ECO:0000269|PubMed:22927433, ECO:0000269|PubMed:23355471}.
DE  Reference Proteome: Yes;
DE  Interaction: O43237; IntAct: EBI-731827; Score: 0.00
DE  Interaction: Q9UNN8; IntAct: EBI-734445; Score: 0.00
DE  Interaction: Q86YD1; IntAct: EBI-735504; Score: 0.00
DE  Interaction: P62316; IntAct: EBI-736673; Score: 0.00
DE  Interaction: P31946; IntAct: EBI-8796749; Score: 0.35
DE  Interaction: P14618; IntAct: EBI-9355736; Score: 0.44
DE  Interaction: Q08379; IntAct: EBI-10225555; Score: 0.56
DE  Interaction: Q8TAP6; IntAct: EBI-24382670; Score: 0.56
DE  Interaction: Q8IYF3; IntAct: EBI-24387259; Score: 0.56
DE  Interaction: Q12933; IntAct: EBI-24472525; Score: 0.56
DE  Interaction: Q8IWV7; IntAct: EBI-21864310; Score: 0.35
DE  Interaction: Q86TI2; IntAct: EBI-21864310; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-21864310; Score: 0.35
DE  Interaction: P62258; IntAct: EBI-21864310; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21864310; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21907689; Score: 0.35
DE  Interaction: P50552; IntAct: EBI-30845230; Score: 0.44
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0031253;
GO  GO:0030863;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031095;
GO  GO:0014069;
GO  GO:0014731;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0043621;
GO  GO:0005102;
GO  GO:0030507;
GO  GO:0030036;
GO  GO:0051017;
GO  GO:0051693;
GO  GO:0090527;
GO  GO:0035585;
GO  GO:0035584;
GO  GO:0071277;
GO  GO:0071320;
GO  GO:0007010;
GO  GO:0048821;
GO  GO:0030032;
GO  GO:0010812;
GO  GO:0051895;
GO  GO:0033137;
GO  GO:0010801;
GO  GO:0050732;
GO  GO:0090315;
GO  GO:1900025;
GO  GO:0030194;
GO  GO:0010763;
GO  GO:2001046;
GO  GO:1901731;
GO  GO:1900026;
GO  GO:0090303;
GO  GO:0070560;
GO  GO:0065003;
GO  GO:0032956;
GO  GO:0008360;
GO  GO:0051489;
GO  GO:0010591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERLQKQPLTSPGSVSPSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPR
SQ  SRERSLSPKSTSPPPSPEVWADSRSPGIISQASAPRTTGTPRTSLPHFHHPETSRPDSNIYKKPPIYKQRESVGGSPQTK
SQ  HLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREE
SQ  LSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHQGTSKSSSLPAYGRTTLSRLQSTEFSPSGSETGSPGLQN
SQ  GEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKK
SQ  KASLF
//
ID  Q9WV69;
PN  Dematin;
GN  Dmtn;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:18505823}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18505823}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000269|PubMed:18505823}. Endomembrane system {ECO:0000250}. Cell projection {ECO:0000269|PubMed:18505823}. Note=Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9WV69;
DR  UNIPROT: F8WIF9;
DR  UNIPROT: Q3TYC5;
DR  UNIPROT: Q8JZV5;
DR  UNIPROT: Q9WVM2;
DR  Pfam: PF16182;
DR  Pfam: PF02209;
DR  PROSITE: PS51089;
DE  Function: Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Also plays a role as a modulator of actin dynamics in fibroblasts; acts as negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation. {ECO:0000269|PubMed:12011427, ECO:0000269|PubMed:18505823, ECO:0000269|PubMed:23060452}.
DE  Reference Proteome: Yes;
DE  Interaction: P63104; IntAct: EBI-6271507; Score: 0.35
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0031253;
GO  GO:0030863;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031095;
GO  GO:0014069;
GO  GO:0014731;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0043621;
GO  GO:0005102;
GO  GO:0030507;
GO  GO:0030036;
GO  GO:0051017;
GO  GO:0051693;
GO  GO:0090527;
GO  GO:0035585;
GO  GO:0035584;
GO  GO:0071277;
GO  GO:0071320;
GO  GO:0048821;
GO  GO:0030032;
GO  GO:0010812;
GO  GO:0051895;
GO  GO:0033137;
GO  GO:0010801;
GO  GO:0050732;
GO  GO:0090315;
GO  GO:1900025;
GO  GO:0030194;
GO  GO:0010763;
GO  GO:2001046;
GO  GO:1901731;
GO  GO:1900026;
GO  GO:0090303;
GO  GO:0070560;
GO  GO:0065003;
GO  GO:0032956;
GO  GO:0008360;
GO  GO:0051489;
GO  GO:0010591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERLQKQPLTSPGSVSSSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPR
SQ  SRECSLSPKSTSPPPSPEVWAESRTLGIISQASTPRTTGTPRTSLPHFHHPETTRPDSNIYKKPPIYKQRESVGGSPQSK
SQ  HLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRKGAEEEEEEEDDDSEEEIKAIRERQKEE
SQ  LSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHSGTSKSSSLPSYGRTTLSRLQSTEFSPSGSEAGSPGLQN
SQ  GEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKK
SQ  KASLF
//
ID  Q5R4B6;
PN  Dematin;
GN  DMTN;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000250}. Endomembrane system {ECO:0000250}. Cell projection {ECO:0000250}. Note=Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5R4B6;
DR  Pfam: PF16182;
DR  Pfam: PF02209;
DR  PROSITE: PS51089;
DE  Function: Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Also plays a role as a modulator of actin dynamics in fibroblasts; acts as negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005884;
GO  GO:0031253;
GO  GO:0030863;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031095;
GO  GO:0014069;
GO  GO:0014731;
GO  GO:0003779;
GO  GO:0043621;
GO  GO:0005102;
GO  GO:0030507;
GO  GO:0030036;
GO  GO:0051017;
GO  GO:0051693;
GO  GO:0090527;
GO  GO:0035585;
GO  GO:0035584;
GO  GO:0071277;
GO  GO:0071320;
GO  GO:0048821;
GO  GO:0010812;
GO  GO:0051895;
GO  GO:0033137;
GO  GO:0010801;
GO  GO:0050732;
GO  GO:0090315;
GO  GO:1900025;
GO  GO:0030194;
GO  GO:0010763;
GO  GO:2001046;
GO  GO:1901731;
GO  GO:1900026;
GO  GO:0090303;
GO  GO:0070560;
GO  GO:0065003;
GO  GO:0032956;
GO  GO:0008360;
GO  GO:0051489;
GO  GO:0010591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERLQKQPLTSPGSVSPSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPR
SQ  SRERSLSPKSTSPPPSPEVWADSRSPGIISQASAPRTTGTPRTSLPHFHHPETSRPDSNIYKKPPIYKQRESVGGSPQTK
SQ  HLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREE
SQ  LSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHQGTSKSSSLPAYGRTTLSRLQSTEFSPSGSETGSPGLQN
SQ  GEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKK
SQ  KASLF
//
ID  O75140;
PN  GATOR complex protein DEPDC5;
GN  DEPDC5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61460}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P61460}. Lysosome membrane {ECO:0000269|PubMed:28199306}. Note=Localization to lysosomes is amino acid-independent. {ECO:0000269|PubMed:28199306}.
DR  UNIPROT: O75140;
DR  UNIPROT: A6H8V6;
DR  UNIPROT: A8MPX9;
DR  UNIPROT: B4DH93;
DR  UNIPROT: B9EGN9;
DR  UNIPROT: Q5K3V5;
DR  UNIPROT: Q5THY9;
DR  UNIPROT: Q5THZ0;
DR  UNIPROT: Q5THZ1;
DR  UNIPROT: Q5THZ3;
DR  UNIPROT: Q68DR1;
DR  UNIPROT: Q6MZX3;
DR  UNIPROT: Q6PEZ1;
DR  UNIPROT: Q9UGV8;
DR  UNIPROT: Q9UH13;
DR  PDB: 6CES;
DR  PDB: 6CET;
DR  PDB: 7T3A;
DR  PDB: 7T3B;
DR  PDB: 7T3C;
DR  Pfam: PF00610;
DR  Pfam: PF19418;
DR  Pfam: PF12257;
DR  PROSITE: PS50186;
DR  OMIM: 604364;
DR  OMIM: 614191;
DR  DisGeNET: 9681;
DE  Function: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway. {ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:29769719}.
DE  Disease: Epilepsy, familial focal, with variable foci 1 (FFEVF1) [MIM:604364]: An autosomal dominant form of epilepsy characterized by focal seizures arising from different cortical regions in different family members. Many patients have an aura and show automatisms during the seizures, whereas others may have nocturnal seizures. There is often secondary generalization. Some patients show abnormal interictal EEG, and some patients may have intellectual disability or autism spectrum disorders. Seizure onset usually occurs in the first or second decades, although later onset has been reported, and there is phenotypic variability within families. Penetrance of the disorder is incomplete. {ECO:0000269|PubMed:23542697, ECO:0000269|PubMed:23542701, ECO:0000269|PubMed:24283814, ECO:0000269|PubMed:24591017, ECO:0000269|PubMed:25366275, ECO:0000269|PubMed:26505888, ECO:0000269|PubMed:27173016}. Note=The disease is caused by variants affecting the gene represented in this entry. Note=Inactivating mutations and truncating deletions in the genes encoding GATOR1 proteins, including DEPDC5, are detected in glioblastoma and ovarian tumors and are associated with loss of heterozygosity events. Inactivation of GATOR1 proteins promotes constitutive localization of mTORC1 to the lysosomal membrane and blocks mTORC1 inactivation following amino acid withdrawal (PubMed:23723238). {ECO:0000269|PubMed:23723238}.
DE  Reference Proteome: Yes;
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: P58043; IntAct: EBI-11102804; Score: 0.35
DE  Interaction: Q6W0C5; IntAct: EBI-24665620; Score: 0.56
DE  Interaction: O75604; IntAct: EBI-24681385; Score: 0.56
DE  Interaction: Q13257; IntAct: EBI-24703582; Score: 0.56
DE  Interaction: P49368; IntAct: EBI-24741275; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24434236; Score: 0.56
DE  Interaction: Q9BSW7; IntAct: EBI-24642109; Score: 0.56
DE  Interaction: Q96QG7; IntAct: EBI-24656502; Score: 0.56
DE  Interaction: Q9UI95; IntAct: EBI-24775208; Score: 0.56
DE  Interaction: Q1RMZ1; IntAct: EBI-21587773; Score: 0.35
DE  Interaction: Q8WTW4; IntAct: EBI-21720164; Score: 0.53
DE  Interaction: Q9Y664; IntAct: EBI-21890520; Score: 0.35
DE  Interaction: Q96MD2; IntAct: EBI-21890520; Score: 0.35
DE  Interaction: Q969R8; IntAct: EBI-21890520; Score: 0.35
DE  Interaction: Q5T011; IntAct: EBI-21890520; Score: 0.35
DE  Interaction: Q12980; IntAct: EBI-16126226; Score: 0.35
DE  Interaction: Q9HB90; IntAct: EBI-16126252; Score: 0.35
DE  Interaction: Q7L523; IntAct: EBI-16126252; Score: 0.35
DE  Interaction: Q5VZM2; IntAct: EBI-16752640; Score: 0.35
DE  Interaction: Q96S15; IntAct: EBI-16752640; Score: 0.35
DE  Interaction: Q9NXC5; IntAct: EBI-16752640; Score: 0.35
DE  Interaction: Q93079; IntAct: EBI-20935716; Score: 0.40
DE  Interaction: Q99459; IntAct: EBI-21392827; Score: 0.00
DE  Interaction: P63010; IntAct: EBI-30815544; Score: 0.44
GO  GO:0005829;
GO  GO:1990130;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0048471;
GO  GO:0005096;
GO  GO:0044877;
GO  GO:0034198;
GO  GO:0035556;
GO  GO:0032007;
GO  GO:1904262;
GO  GO:0010508;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRTTKVYKLVIHKKGFGGSDDELVVNPKVFPHIKLGDIVEIAHPNDEYSPLLLQVKSLKEDLQKETISVDQTVTQVFRLR
SQ  PYQDVYVNVVDPKDVTLDLVELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAGIRAQAGELWVKNEKVMCGYISEDT
SQ  RVVFRSTSAMVYIFIQMSCEMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSVDEFPEINRA
SQ  SIRQDHKGRFYEDFYKVVVQNERREEWTSLLVTIKKLFIQYPVLVRLEQAEGFPQGDNSTSAQGNYLEAINLSFNVFDKH
SQ  YINRNFDRTGQMSVVITPGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFKLHNRSAPRDSRLGDDYNIP
SQ  HWINHSFYTSKSQLFCNSFTPRIKLAGKKPASEKAKNGRDTSLGSPKESENALPIQVDYDAYDAQVFRLPGPSRAQCLTT
SQ  CRSVRERESHSRKSASSCDVSSSPSLPSRTLPTEEVRSQASDDSSLGKSANILMIPHPHLHQYEVSSSLGYTSTRDVLEN
SQ  MMEPPQRDSSAPGRFHVGSAESMLHVRPGGYTPQRALINPFAPSRMPMKLTSNRRRWMHTFPVGPSGEAIQIHHQTRQNM
SQ  AELQGSGQRDPTHSSAELLELAYHEAAGRHSNSRQPGDGMSFLNFSGTEELSVGLLSNSGAGMNPRTQNKDSLEDSVSTS
SQ  PDPILTLSAPPVVPGFCCTVGVDWKSLTTPACLPLTTDYFPDRQGLQNDYTEGCYDLLPEADIDRRDEDGVQMTAQQVFE
SQ  EFICQRLMQGYQIIVQPKTQKPNPAVPPPLSSSPLYSRGLVSRNRPEEEDQYWLSMGRTFHKVTLKDKMITVTRYLPKYP
SQ  YESAQIHYTYSLCPSHSDSEFVSCWVEFSHERLEEYKWNYLDQYICSAGSEDFSLIESLKFWRTRFLLLPACVTATKRIT
SQ  EGEAHCDIYGDRPRADEDEWQLLDGFVRFVEGLNRIRRRHRSDRMMRKGTAMKGLQMTGPISTHSLESTAPPVGKKGTSA
SQ  LSALLEMEASQKCLGEQQAAVHGGKSSAQSAESSSVAMTPTYMDSPRKDGAFFMEFVRSPRTASSAFYPQVSVDQTATPM
SQ  LDGTSLGICTGQSMDRGNSQTFGNSQNIGEQGYSSTNSSDSSSQQLVASSLTSSSTLTEILEAMKHPSTGVQLLSEQKGL
SQ  SPYCFISAEVVHWLVNHVEGIQTQAMAIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVTDKEPDRVAMQQPATTWHT
SQ  AGVDDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASYASRHSSFSRSFGGRSQAAALLAATVPEQRTVTLDVDV
SQ  NNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTAAVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRAQLF
SQ  IPLNISCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSASAFNFPAENKPQYIHVTGTVFLQLPYSKRKF
SQ  SGQQRRRRNSTSSTNQNMFCEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDNRLVTFWTSCLEKMHA
SQ  SAP
//
ID  P61460;
PN  GATOR complex protein DEPDC5;
GN  Depdc5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:23542697}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23542697}. Lysosome membrane {ECO:0000250|UniProtKB:O75140}. Note=Localization to lysosomes is amino acid-independent. {ECO:0000250|UniProtKB:O75140}.
DR  UNIPROT: P61460;
DR  UNIPROT: E9Q5J2;
DR  UNIPROT: E9Q5Y0;
DR  Pfam: PF00610;
DR  Pfam: PF19418;
DR  Pfam: PF12257;
DR  PROSITE: PS50186;
DE  Function: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway. {ECO:0000250|UniProtKB:O75140}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9R1S0; IntAct: EBI-11784907; Score: 0.35
GO  GO:0031463;
GO  GO:0005829;
GO  GO:1990130;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0048471;
GO  GO:0005096;
GO  GO:0044877;
GO  GO:0034198;
GO  GO:0035556;
GO  GO:0032007;
GO  GO:1904262;
GO  GO:0010508;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRTTKVYKLVIHKKGFGGSDDELVVNPKVFPHIKLGDIVEIAHPNDEYSPLLLQVKSLKEDLQKETISVDQTVTQVFRLR
SQ  PYQDVYVNVVDPKDVTLDLVELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAGIRAQAGELWVKNEKVMCGYISEET
SQ  RVVFRSTSAMVYIFIQMSCEMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSIDEFPEINRA
SQ  SIQEDHKGRFYEDFYKVVVQNERREEWTSLLVTIKKLFIQYPVLVRLEQAGGFPQGDNSTSAQGNYLEAINLSFNVFDKH
SQ  YINRNFDRTGQMSVVITPGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFKLHNRSVPRDSRLGDDYNIP
SQ  HWINHSFYTSKSQLFCNSFTPRIKLAGKKSASEKTKNGRDTSLGTPKESENTLPIQVDYDAYDAQVFRLPGPSRAQRLAT
SQ  CRSVREQENHSRKSASSCDVSSSPSLPSRALPTEEVRSQASDDSSLGKSTNILMIPNPHLHQYEVSSSLGYTSTRDVLEN
SQ  MIEPPQRDSSAPGRFHVGSAESMLHVRPGGYTPQRALINPFAPSRMPMKLTSNRRRWMHTFPVGPSGEAIQIHHQTRQNM
SQ  AELQGSRQRDPTHSSAELLELAYHEAAGRHSTSRQPGDSMSLNFSGTEELSVSLLSNSSTGVNPRTQNKDSLEDSVSTSP
SQ  DPMPGFCCTVGVDWKSLTTPACLPLTTDYFPDRQGLQNDYTEGCYDLLPEADMDRRDEEGVQMTAQQVFEEFICQRLMQG
SQ  YQIIVQPKTQKPNTTVPPPLSSSPLYSRGLVSRNRPEEEGQYWLSMGRTFHKVTLKDKMITVTRYLPKYPYESAQIHYTY
SQ  SLCPSHSDSEFVSCWVDFCHERLEEYKWNYLDQYICSAGSEDFSLIESLKFWRTRFLLLPACVTATKRITEGEVHCDIYG
SQ  DKPRADEDEWQLLDGFIRFVEGLNRIRRRHRSDRMIRKGTAMKGLQMTGPISAHSLEAAGPPVGKKGTSALSALLEMEAS
SQ  QKSLGEQQTTVHGKSSTQPAENSSVAMTPTYVDSPRKDGAFFMEFVRSPRTASSAFYPQASVDQTAPLVLDSTSLGVSTG
SQ  QPMDRGNNQTFGNSQNIEQAFPSANSGDYSSQQHVASSLTSSSTLVEILEAMKHPSTGVQLLSEQKGLSPCCFISAEVVH
SQ  WLMNNVEGVQTQAMGIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVMDKEPERVAMQQPSAPWYTAGADDFASFQRK
SQ  WFEVAFVAEELVHSEIPAFLLPWLPSRPASYASRHSSFSRSFGGRSQAAALLAATVPEQRTVTLDVDVNNRTDRLEWCSC
SQ  YYHGNFSLNAAFEIKLHWMAVTATVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRAQLFIPLNLSCLLKEG
SQ  SEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSVSAFNFPAENKPQYIHVTGTVFLQLPYSKRKFSGQQRRRRNSTS
SQ  STNQNMFCEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDNRLVTFWTNCLEKMHASAP
//
ID  Q9N303;
PN  P-granule-associated protein deps-1;
GN  deps;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic granule {ECO:0000269|PubMed:18234720, ECO:0000269|PubMed:32843637}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32843637}. Note=Localizes to P-granules in germ cells at all stages of development (PubMed:18234720). Co-localizes with prg-1 at peri-nuclear P-granules in the proliferative zone and transition zone, at pachytene, in oocytes and in embryos (PubMed:32843637). In the distal loop, a higher proportion of deps-1 than prg-1 dissociates from the perinuclear region (PubMed:32843637). In the adult germline, co-localizes with znfx-1 at P-granules and with pgl-1 at P-granules in the pachytene region (PubMed:32843637). {ECO:0000269|PubMed:18234720, ECO:0000269|PubMed:32843637}.
DR  UNIPROT: Q9N303;
DR  UNIPROT: V6CLC9;
DE  Function: Component of P-granules which is required for P-granule formation and integrity in adult germ cells (PubMed:18234720). Promotes the accumulation of glh-1 mRNA and localization of pgl-1 to P-granules (PubMed:18234720). Involved in RNA-mediated gene silencing (RNAi) in the germline (PubMed:18234720, PubMed:32843637). In particular, it is required for piwi-interacting RNA (piRNA) gene silencing and positively regulates the formation of secondary 22G-RNAs, which are RNA-dependent RNA polymerase-derived endo-siRNAs, typically 22 nucleotides in length with a 5'guanosine residue (PubMed:32843637). Its role in RNAi may also be through positively regulating the expression of the dsRNA-binding protein rde-4 (PubMed:18234720). Plays a role in small RNA-directed transgenerational epigenetic inheritance (PubMed:27015309, PubMed:29769721). {ECO:0000269|PubMed:18234720, ECO:0000269|PubMed:27015309, ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:32843637}.
DE  Reference Proteome: Yes;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0031047;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSERQSKYFDYQGIVISSTGQDNQDSETDLVYLIQAHGKAAPKNIMYGVSKCAFVPTNLERNFDNIEEAKNLERRSKIPL
SQ  KFGEVILWNESDCDHDKRIILHIKREKPIYEASSSRNGLILKVGGVIQPTSTTSFWTPLCTVTMPETEATRAEPDVWLYA
SQ  WIRFETTMKSGLDPFNMTATFESFDSCDPSDQARVCEAPWNAGSPDSKFGVWRPDPKPADSDDEIDIEPREGWHLPEDKW
SQ  AEVIKMQLGLYVGERLLICKELSQFDFIIPLQKPFSRGTDKTLIYPAVGEYFHFSAIWSMQHNGFLIYELQPVPLLRQHV
SQ  TSVNGNLLTRVVPASIRGLFVDKEGTLGLIDDPHHLLSFFEFHPAGYEFLKAMAEVRAVRTSENKSVRYRIVRTSGMSIF
SQ  ENWLRDTQFVVGPVKGIRINEDTVICAKHPNVYFKIPNNLKEGIPIGGGVQFVGKRQAGVDSEIMITECSPCPAFTCKNY
SQ  SVSGDTRLFQVYLKPNCDHEQLAESDSMGFVDFRELETPCRGKFLAWVRESITVNDCRRAATIMEVCSTAICPPLIAMSA
SQ  NSSRATSARTTPAGSSIGSRSSIQSRASAATSVSSNRFVGPSSRRTPSGTPQSSTSSRV
//
ID  Q70VZ8;
PN  Diacylglycerol O-acyltransferase 2;
GN  DGAT2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}.
DR  UNIPROT: Q70VZ8;
DR  UNIPROT: A5D9B3;
DR  UNIPROT: Q6B852;
DR  UNIPROT: Q6PP93;
DR  UNIPROT: Q6PP94;
DR  UNIPROT: Q6PP95;
DR  UNIPROT: Q6PP96;
DR  Pfam: PF03982;
DE  Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides (By similarity). Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides (By similarity). Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1- monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By similarity). {ECO:0000250|UniProtKB:Q96PD7, ECO:0000250|UniProtKB:Q9DCV3}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:1990578;
GO  GO:0048471;
GO  GO:0003846;
GO  GO:0004144;
GO  GO:0050252;
GO  GO:0071400;
GO  GO:0035356;
GO  GO:0042632;
GO  GO:0006651;
GO  GO:0046339;
GO  GO:0060613;
GO  GO:0055089;
GO  GO:0006071;
GO  GO:0006629;
GO  GO:0019915;
GO  GO:0035336;
GO  GO:0034383;
GO  GO:0006640;
GO  GO:0097006;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKTLIAAYSGVLRGTGSSILSALQDLFSVTWLNRAKVEKQLQVISVLQWVLSFLVLGVACSVILMYTFCTDCWLIAVLYF
SQ  TWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTSRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPG
SQ  IRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLAL
SQ  RHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPRL
SQ  ERPTQQDIDLYHAMYVQALVKLFDQHKTKFGLPETEVLEVN
//
ID  Q4V9F0;
PN  Diacylglycerol O-acyltransferase 2;
GN  dgat2;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}.
DR  UNIPROT: Q4V9F0;
DR  Pfam: PF03982;
DE  Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation (By similarity). {ECO:0000250|UniProtKB:Q96PD7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:1990578;
GO  GO:0004144;
GO  GO:0050252;
GO  GO:0006651;
GO  GO:0006071;
GO  GO:0055088;
GO  GO:0006629;
GO  GO:1905897;
GO  GO:0061959;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKTILAAYSGVKKGSGSSILSALHDLPTVPWLTRSKMVKHLQVISVLQFIMTFLTMGIACSLLLMYMFCTDFWVISVLYV
SQ  AWLIYDWNTPGQGGRRSTWVRDWTVWKYMRDYFPIRLIKTHNLLPSRNYIFGYHPHGILCFGAFCNFGTEATGFTKVFPG
SQ  IKPSLATLAGNFRLPMFREYLMCGGICPVNRNSIDYLLSSNGTGNAVVIVIGGAAESLDCAPGRNSVMLKKRKGFVKLAL
SQ  KQGADLVPVYSFGENEVYKQLIFEEGSWWRTIQRKLQKFLGFAPCLFHGCGLFFPESWGLVPYCKPITTVVGEPITVPKI
SQ  EEPTQDVIDMYHAMYIRSLKSLFDNYKTRFGLNESDTLIIH
//
ID  Q96PD7;
PN  Diacylglycerol O-acyltransferase 2;
GN  DGAT2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14521909, ECO:0000269|PubMed:27184406}; Multi-pass membrane protein {ECO:0000269|PubMed:14521909}. Lipid droplet {ECO:0000269|PubMed:27184406}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27184406}.
DR  UNIPROT: Q96PD7;
DR  UNIPROT: A6ND76;
DR  UNIPROT: Q5U810;
DR  UNIPROT: Q68CL3;
DR  UNIPROT: Q68DJ0;
DR  UNIPROT: Q8NDB7;
DR  UNIPROT: Q96BS0;
DR  UNIPROT: Q9BYE5;
DR  Pfam: PF03982;
DR  OMIM: 606983;
DR  DisGeNET: 84649;
DE  Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides (PubMed:27184406). Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides (By similarity). Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1- monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705). {ECO:0000250|UniProtKB:Q9DCV3, ECO:0000269|PubMed:27184406, ECO:0000269|PubMed:28420705}.
DE  Reference Proteome: Yes;
DE  Interaction: P55072; IntAct: EBI-9519939; Score: 0.40
DE  Interaction: Q9UKV5; IntAct: EBI-9520083; Score: 0.40
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005811;
GO  GO:0005739;
GO  GO:1990578;
GO  GO:0048471;
GO  GO:0003846;
GO  GO:0004144;
GO  GO:0042803;
GO  GO:0050252;
GO  GO:0038183;
GO  GO:0071400;
GO  GO:0035356;
GO  GO:0042632;
GO  GO:0006651;
GO  GO:0046339;
GO  GO:0060613;
GO  GO:0055089;
GO  GO:0006071;
GO  GO:0006629;
GO  GO:0019915;
GO  GO:0035336;
GO  GO:0034383;
GO  GO:0006640;
GO  GO:0046322;
GO  GO:0045722;
GO  GO:0010867;
GO  GO:0090181;
GO  GO:0050746;
GO  GO:0097006;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLNRSKVEKQLQVISVLQWVLSF
SQ  LVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGY
SQ  HPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGG
SQ  AAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLF
SQ  SSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHTMYMEALVKLFDKHKTKFGLPETEVLEVN
//
ID  Q9DCV3;
PN  Diacylglycerol O-acyltransferase 2;
GN  Dgat2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}.
DR  UNIPROT: Q9DCV3;
DR  Pfam: PF03982;
DE  Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides. Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By similarity). {ECO:0000250|UniProtKB:Q96PD7, ECO:0000269|PubMed:11481335, ECO:0000269|PubMed:15797871, ECO:0000269|PubMed:21680734, ECO:0000269|PubMed:22493088}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:1990578;
GO  GO:0048471;
GO  GO:0003846;
GO  GO:0004144;
GO  GO:0042803;
GO  GO:0050252;
GO  GO:0038183;
GO  GO:0071400;
GO  GO:0035356;
GO  GO:0042632;
GO  GO:0006651;
GO  GO:0046339;
GO  GO:0060613;
GO  GO:0055089;
GO  GO:0006071;
GO  GO:0006629;
GO  GO:0019915;
GO  GO:0035336;
GO  GO:0034383;
GO  GO:0006640;
GO  GO:0046322;
GO  GO:0045722;
GO  GO:0010867;
GO  GO:0090181;
GO  GO:0050746;
GO  GO:0097006;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKTLIAAYSGVLRGERRAEAARSENKNKGSALSREGSGRWGTGSSILSALQDIFSVTWLNRSKVEKQLQVISVLQWVLSF
SQ  LVLGVACSVILMYTFCTDCWLIAVLYFTWLAFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGY
SQ  HPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIIIVVGG
SQ  AAESLSSMPGKNAVTLKNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLF
SQ  SSDTWGLVPYSKPITTVVGEPITVPKLEHPTQKDIDLYHAMYMEALVKLFDNHKTKFGLPETEVLEVN
//
ID  Q5FVP8;
PN  Diacylglycerol O-acyltransferase 2;
GN  Dgat2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}.
DR  UNIPROT: Q5FVP8;
DR  UNIPROT: Q8K4Y4;
DR  Pfam: PF03982;
DE  Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides (By similarity). Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides (By similarity). Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1- monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By similarity). {ECO:0000250|UniProtKB:Q96PD7, ECO:0000250|UniProtKB:Q9DCV3}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:1990578;
GO  GO:0048471;
GO  GO:0003846;
GO  GO:0004144;
GO  GO:0042803;
GO  GO:0050252;
GO  GO:0038183;
GO  GO:0071400;
GO  GO:0035356;
GO  GO:0042632;
GO  GO:0006651;
GO  GO:0046339;
GO  GO:0060613;
GO  GO:0055089;
GO  GO:0006071;
GO  GO:0006629;
GO  GO:0019915;
GO  GO:0035336;
GO  GO:0034383;
GO  GO:0006640;
GO  GO:0046322;
GO  GO:0045722;
GO  GO:0010867;
GO  GO:0090181;
GO  GO:0050746;
GO  GO:0097006;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKTLIAAYSGVLRGERRAEAARSENKNKGSALSREGSGRWGTGSSILSALQDIFSVTWLNRSKVEKHLQVISVLQWVLSF
SQ  LVLGVACSVILMYTFCTDCWLIAALYFTWLAFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGY
SQ  HPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIVIVVGG
SQ  AAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLF
SQ  SSDTWGLVPYSKPITTVVGEPITVPKLEHPTQKDIDLYHTMYMEALVKLFDNHKTKFGLPETEVLEVN
//
ID  Q6PAZ3;
PN  Diacylglycerol O-acyltransferase 2;
GN  dgat2;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}.
DR  UNIPROT: Q6PAZ3;
DR  Pfam: PF03982;
DE  Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation (By similarity). {ECO:0000250|UniProtKB:Q96PD7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:1990578;
GO  GO:0004144;
GO  GO:0050252;
GO  GO:0006651;
GO  GO:0006071;
GO  GO:0006640;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKTIIAAYSGVLRGTGSSLLSAVHDLPSIPWLSKSSVVRHLQIISVLQWVLSFLILGVACTAVLVYIFCTDLWLIAALYF
SQ  TWMVLDWNTPYKGGRRSSWVRNWAVWRYFRDYFPVKLVKTHNLLPSRNYIFGYHPHGIMCLGAFCNFGTEATGVSKKFPG
SQ  IKCHLATLAGNFRMPVLREYLMSGGICPVNRDTINYILSKNGTGNAVVIAVGGAAESLNCRPGKNTVTLLHRKGFVKVAL
SQ  QHGADLVPIYSFGENETYKQVVFEEGSWGRWIQQKFQKYVGFAPCLFHGCSFFSSNSWGLVPYANPITTVVGEPITVPKI
SQ  EQPTQKDVELYHSMYLSSLHRLFDKYKTKLGLPDSETLEFI
//
ID  Q6P342;
PN  Diacylglycerol O-acyltransferase 2;
GN  dgat2;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}.
DR  UNIPROT: Q6P342;
DR  Pfam: PF03982;
DE  Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation (By similarity). {ECO:0000250|UniProtKB:Q96PD7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:1990578;
GO  GO:0004144;
GO  GO:0050252;
GO  GO:0006651;
GO  GO:0046339;
GO  GO:0006071;
GO  GO:0006629;
GO  GO:0006640;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKTIIAAYSGVLRGTGSSLLSAVHDLPNIPWLSKSSVVRHLQIISVLQWVLSFLILGVACTAVLVYIFCTDLWLIAALYL
SQ  TWMVLDWNTPYKGGRRSSWVRNWAVWRYFRDYFPIKLVKTHNLLPSRNYIFGYHPHGIMCLGAFCNFGTEATGVSKKFPG
SQ  IKCHLATLAGNFRMPVLREYLMSGGICPVARDTIDYILSKNGTGNAVVIAVGGAAESLNCRPGKNTVTLKQRKGFVKVAL
SQ  QHGADLVPVYSFGENEAYKQVVFEEGSWGRWIQKKFQKYVGFAPCLFHGCSFFSSNSWGLVPYANPITTVVGEPITVPKI
SQ  EQPTQKDVELYHAMYVTSLQRLFDKYKTKLGLHDSEMLEIV
//
ID  Q753I3;
PN  CTP-dependent diacylglycerol kinase 1;
GN  DGK1;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12382}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12382}. Nucleus membrane {ECO:0000250|UniProtKB:Q12382}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12382}.
DR  UNIPROT: Q753I3;
DE  Function: CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus. {ECO:0000250|UniProtKB:Q12382}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0004143;
GO  GO:0006654;
GO  GO:0016310;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MANEEELQTAESAFVTGARRYSNDYSESESSSKHSGCSTPVEGTPAEAATTIGARASGGSTTWQRLRQLLMERGSDVHLP
SQ  VTEIHLKSQEWFGDFITKHEVPRKVFHSSIGFFTLALYVRDVDYRNVRLPLIVGFVHVLLLDVIRLHWPAFNTLYCQVTG
SQ  LLMRKKEVHTYNGVLWYLLGLIFAFSFFSKDVALVSLFLLSWCDTAASTVGRLYGHLTPRISRNKSLAGSLAAFVVGVIS
SQ  CAVFYGYFVPAYSHVNHPGEIMWNPETSRLSLVQLSLLGGFVASLSEGIDLFNWDDNFTIPVLSAIFMHTIIAFSQR
//
ID  P87170;
PN  CTP-dependent diacylglycerol kinase 1;
GN  ptp4;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:26990381}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:26990381}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: P87170;
DE  Function: CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of PA phosphatase ned1. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus (By similarity). Involved in pre-tRNA splicing (PubMed:11955632). {ECO:0000250|UniProtKB:Q12382, ECO:0000269|PubMed:11955632}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0097038;
GO  GO:0004143;
GO  GO:0006654;
GO  GO:0016310;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSTKLTWSQWSKKHEIPRKALHTSIGFFALLLQGCGYHAAQIIPVIEIGFIPAFTGDVIRFNWPAFSRLYNRVIGPLMRE
SQ  SEKNAWNGVIFYMIGVWIVLKVFPEEIAVMSVLLLSWCDTTASTVGRKWGKYTPKIAKNKSLAGSLGAFVCGVFCCYVYW
SQ  GLFRTGPDSLAAQSRIPFPWLCLINGFIGAFAEAMDVWGLDDNLVIPVVSACLLYLIM
//
ID  Q12382;
PN  CTP-dependent diacylglycerol kinase 1;
GN  DGK1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11481671, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18458075}; Multi-pass membrane protein {ECO:0000305|PubMed:11481671, ECO:0000305|PubMed:18458075}. Nucleus membrane {ECO:0000269|PubMed:18458075}; Multi-pass membrane protein {ECO:0000305|PubMed:18458075}.
DR  UNIPROT: Q12382;
DR  UNIPROT: D6W310;
DE  Function: CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of PA phosphatase PAH1/SMP2, controlling the levels of PA and DAG for the synthesis of triacylglycerol and membrane phospholipids (PubMed:18458075, PubMed:27834677). May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus (PubMed:11481671). Required to convert triacylglycerol-derived DAG to PA for phospholipid synthesis during growth resumption from stationary phase in the absence of de novo fatty acid synthesis (PubMed:21071438). Involved in the resistance to nickel chloride and nalidixic acid (PubMed:10407277). {ECO:0000269|PubMed:10407277, ECO:0000269|PubMed:11481671, ECO:0000269|PubMed:18458075, ECO:0000269|PubMed:21071438, ECO:0000269|PubMed:27834677}.
DE  Reference Proteome: Yes;
DE  Interaction: P11484; IntAct: EBI-3689295; Score: 0.35
DE  Interaction: Q96BA8; IntAct: EBI-11537340; Score: 0.56
DE  Interaction: Q8N6L0; IntAct: EBI-11537331; Score: 0.56
DE  Interaction: P50112; IntAct: EBI-16254616; Score: 0.00
GO  GO:0005783;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0004143;
GO  GO:0006654;
GO  GO:0016310;
GO  GO:2001210;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGTEDAIALPNSTLEPRTEAKQRLSSKSHQVSAKVTIPAKEEISSSDDDAHVPVTEIHLKSHEWFGDFITKHEIPRKVFH
SQ  SSIGFITLYLYTQGINYKNVLWPLIYAFIILFILDLIRLNWPFFNMLYCRTVGALMRKKEIHTYNGVLWYILGLIFSFNF
SQ  FSKDVTLISLFLLSWSDTAAATIGRKYGHLTPKVARNKSLAGSIAAFTVGVITCWVFYGYFVPAYSYVNKPGEIQWSPET
SQ  SRLSLNMLSLLGGVVAALSEGIDLFNWDDNFTIPVLSSLFMNAVIKTFKK
//
ID  Q86CZ2;
PN  Hybrid signal transduction histidine kinase K;
GN  dhkK;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q86CZ2;
DR  UNIPROT: Q54Y10;
DR  UNIPROT: Q95PH2;
DR  Pfam: PF02518;
DR  Pfam: PF00512;
DR  Pfam: PF00072;
DR  PROSITE: PS50109;
DR  PROSITE: PS50110;
DE  Function: Involved in a signal transduction pathway that regulates morphogenesis and controls entry into the culmination stage. May act via the regA pathway, being activated by a morphogenesis-stimulated ligand, reducing phosphodiesterase regA levels and allowing cAMP level to rise to promote the culmination stage. This protein probably undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0000155;
GO  GO:0140582;
GO  GO:0031154;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIELNNHSKINKNENNTNTRNNSSNNNNNNNNINKTNTNKYFEYNQNSIIYSSIPNSFLSHHPNSVGSQCLSLNSFLPPK
SQ  PPILLSIFNSDTIGNNNNNNYSSSSSRNNSSGCSSSNNNNNNNNNNNNNNNNNNNNNNNNCNIEQYKNNQKQPKQQQQQK
SQ  DQTIATQHRISLSSSSSSSSLSSSSSSSSVKQSFQIVKRLFGSLSEYMFPQKDEILYETDPYYLYQDDTQSNDSNEFYDD
SQ  TDIGSDIDEANLNNTYNIQNCNKTLYNKQQQQAHFVNMNKNVNSNNGTGNSNQSNNVNKNQQNNNNNNNNNSHNNNNGNQ
SQ  NSSSSSSNSGASGSGGNGNNNNNNNNNNNNNNNNNNNSNSNSNNNSKSNNNNKKEGKDGATMNGSHPLIPFRKKPAQVPS
SQ  PCFRMNSPNSDNDQYLDQLALENSSKKSLVVYNTDNLDQWKHSHLNENFDILQNDLIDIQQQQQQQQQQDNTLQYSSPIN
SQ  KRQEQEQQHIPFQFTTEQQQQLQQQQQQQQQNKTKQHPILLQRQQQQKQKQQQQQQIQQEQIGNNNSNNNNNINNNNNIN
SQ  NNYNNVNDLMNKFEIDQKQHDSQQNLVEEKRTPSFHEHNIIFNSFNFICSIVLDGSNIKSTEKYKAKLIIGFCFTILSFI
SQ  PSWIIFFWLSGINKPAVMAIIAMPMSISSLVILKRTGSIHYPCHILCFTLCFALTINSYYTGGHQSTIRLLMSTVPIISA
SQ  LVLGRKASIQWSLMVLSIYLLFFVANLYGHEYVQGIPSIIIRSHMNFIIDVTIIIMTLIFTLCYQYFIDEAHRETKLKNA
SQ  QLTIAKDAAIEAYQARQEFLATMSHEIRTPLNGLIGMATLLRDSHNLPPEEKTMAKAVKSCGDILLRLVNDILDLSKLEA
SQ  NQMGLEHIPFRMRELTQQICHVLSGQANEKNIHLSCEVSDKIPSILLGDSGRILQILMNLTGNALKFTQSGYVKIIIDLI
SQ  EEESELVSLKKGEYNISFRVKDTGIGVPVESHQKIFEAFVQADPSDSRKYGGSGLGLYLCAKLVRLMKGEIGVYNNPDCD
SQ  GSTFWFILPLEEGTDQSMQQMNNGARHKAFPQDCVKVLIAEDNIINQRVAVKFLEKIGIKAEVAGNGNEVLEILERQHYD
SQ  LIFMDFQMPILDGLRCSKTIREFEQNHKWNRICPSIFICGLTANTMSTDKKRCFDHGMNHFISKPFQLEQLRSAIEMAIE
SQ  HKQRNLMNLNIRN
//
ID  Q8IY37;
PN  Probable ATP-dependent RNA helicase DHX37;
GN  DHX37;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleolus {ECO:0000269|PubMed:30582406, ECO:0000269|PubMed:31337883}. Cytoplasm {ECO:0000269|PubMed:31337883}. Nucleus membrane {ECO:0000269|PubMed:31337883}.
DR  UNIPROT: Q8IY37;
DR  UNIPROT: Q9BUI7;
DR  UNIPROT: Q9P211;
DR  PDB: 7MQA;
DR  Pfam: PF00270;
DR  Pfam: PF04408;
DR  Pfam: PF00271;
DR  Pfam: PF07717;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  OMIM: 273250;
DR  OMIM: 617362;
DR  OMIM: 618731;
DR  DisGeNET: 57647;
DE  Function: ATP-binding RNA helicase that plays a role in maturation of the small ribosomal subunit in ribosome biogenesis (PubMed:30582406). Required for the release of the U3 snoRNP from pre-ribosomal particles (PubMed:30582406). Plays a role in early testis development (PubMed:31287541, PubMed:31337883). Probably also plays a role in brain development (PubMed:31256877). {ECO:0000269|PubMed:30582406, ECO:0000269|PubMed:31256877, ECO:0000269|PubMed:31287541, ECO:0000269|PubMed:31337883}.
DE  Disease: Neurodevelopmental disorder with brain anomalies and with or without vertebral or cardiac anomalies (NEDBAVC) [MIM:618731]: An autosomal recessive neurodevelopmental disorder characterized by severe developmental delay, impaired intellectual development, hypotonia, brain anomalies including cortical volume loss, corpus callosum dysgenesis and cerebellar hypoplasia, and variable dysmorphic features. Patients may have platyspondyly, scoliosis, and cardiac anomalies. {ECO:0000269|PubMed:26539891, ECO:0000269|PubMed:31256877}. Note=The disease may be caused by variants affecting the gene represented in this entry. 46,XY sex reversal 11 (SRXY11) [MIM:273250]: An autosomal dominant disorder of sex development. Affected individuals have a 46,XY karyotype and a genital phenotype that may range from predominantly female to predominantly male, including marked sex ambiguity. Approximately half of patients present with micropenis and bilateral or unilateral cryptorchidism, and half present with female-appearing or ambiguous external genitalia. {ECO:0000269|PubMed:31287541, ECO:0000269|PubMed:31337883}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P0C6X7; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: O75051; IntAct: EBI-308790; Score: 0.37
DE  Interaction: P01106; IntAct: EBI-1069119; Score: 0.00
DE  Interaction: Q9NY93; IntAct: EBI-1075155; Score: 0.00
DE  Interaction: P54253; IntAct: EBI-6450099; Score: 0.37
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q6PGB6; IntAct: EBI-11027782; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-11069711; Score: 0.35
DE  Interaction: Q5VWQ0; IntAct: EBI-21719701; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-16786806; Score: 0.27
DE  Interaction: Q96GD4; IntAct: EBI-16787973; Score: 0.27
DE  Interaction: P22087; IntAct: EBI-16792282; Score: 0.27
DE  Interaction: P68431; IntAct: EBI-16793336; Score: 0.27
DE  Interaction: P62753; IntAct: EBI-16798663; Score: 0.27
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
DE  Interaction: Q9UGL1; IntAct: EBI-25480242; Score: 0.35
DE  Interaction: K9N4V0; IntAct: EBI-26375098; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-27102259; Score: 0.53
DE  Interaction: Q9BXK1; IntAct: EBI-29018137; Score: 0.27
DE  Interaction: O43763; IntAct: EBI-29786140; Score: 0.27
DE  Interaction: P54760; IntAct: EBI-32721396; Score: 0.27
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0034511;
GO  GO:0007420;
GO  GO:0000462;
GO  GO:2000020;
GO  GO:0042255;
GO  GO:0042254;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGKLRRRYNIKGRQQAGPGPSKGPPEPPPVQLELEDKDTLKGVDASNALVLPGKKKKKTKAPPLSKKEKKPLTKKEKKVL
SQ  QKILEQKEKKSQRAEMLQKLSEVQASEAEMRLFYTTSKLGTGNRMYHTKEKADEVVAPGQEKISSLSGAHRKRRRWPSAE
SQ  EEEEEEEESESELEEESELDEDPAAEPAEAGVGTTVAPLPPAPAPSSQPVPAGMTVPPPPAAAPPLPRALAKPAVFIPVN
SQ  RSPEMQEERLKLPILSEEQVIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGFSSEDSIIGVTEPRRVAAVAMSQRVAK
SQ  EMNLSQRVVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLRYKVVIIDEAHERSVYTDILIGLLSRIVTLRAKRNL
SQ  PLKLLIMSATLRVEDFTQNPRLFAKPPPVIKVESRQFPVTVHFNKRTPLEDYSGECFRKVCKIHRMLPAGGILVFLTGQA
SQ  EVHALCRRLRKAFPPSRARPQEKDDDQKDSVEEMRKFKKSRARAKKARAEVLPQINLDHYSVLPAGEGDEDREAEVDEEE
SQ  GALDSDLDLDLGDGGQDGGEQPDASLPLHVLPLYSLLAPEKQAQVFKPPPEGTRLCVVATNVAETSLTIPGIKYVVDCGK
SQ  VKKRYYDRVTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALNVEKV
SQ  INFPFPTPPSVEALLAAEELLIALGALQPPQKAERVKQLQENRLSCPITALGRTMATFPVAPRYAKMLALSRQHGCLPYA
SQ  ITIVASMTVRELFEELDRPAASDEELTRLKSKRARVAQMKRTWAGQGASLKLGDLMVLLGAVGACEYASCTPQFCEANGL
SQ  RYKAMMEIRRLRGQLTTAVNAVCPEAELFVDPKMQPPTESQVTYLRQIVTAGLGDHLARRVQSEEMLEDKWRNAYKTPLL
SQ  DDPVFIHPSSVLFKELPEFVVYQEIVETTKMYMKGVSSVEVQWIPALLPSYCQFDKPLEEPAPTYCPERGRVLCHRASVF
SQ  YRVGWPLPAIEVDFPEGIDRYKHFARFLLEGQVFRKLASYRSCLLSSPGTMLKTWARLQPRTESLLRALVAEKADCHEAL
SQ  LAAWKKNPKYLLAEYCEWLPQAMHPDIEKAWPPTTVH
//
ID  Q8VXU6;
PN  Protein DEHYDRATION-INDUCED 19 homolog 4;
GN  DI19;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16786289}. Note=May be part of the endoplasmic reticulum.
DR  UNIPROT: Q8VXU6;
DR  UNIPROT: Q9M7Y2;
DR  Pfam: PF14571;
DR  Pfam: PF05605;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDSNWINCPSVFSSSSSSSRRCQSRSDLYLGGGYEDLEGEDDLKAEFICPFCAEDFDIVGLCCHIDEEHPVEAKNGVCPV
SQ  CTKRVGLDIVGHITTQHANFFKVQRRRRLRRGGYSSTYLALKKELREANLQSLLGGSSSFTSSTNIDSDPLLSSFMFNSP
SQ  SVNQSANKSATPVTVGNAATKVSIKESLKRDIQEAPLSGEDQEKAKKSEFVRGLLLSTMLEDDF
//
ID  Q9UPY3;
PN  Endoribonuclease Dicer;
GN  DICER1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16424907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19022417}.
DR  UNIPROT: Q9UPY3;
DR  UNIPROT: A7E2D3;
DR  UNIPROT: B3KRG4;
DR  UNIPROT: E0AD28;
DR  UNIPROT: O95943;
DR  UNIPROT: Q9UQ02;
DR  PDB: 2EB1;
DR  PDB: 4NGB;
DR  PDB: 4NGC;
DR  PDB: 4NGD;
DR  PDB: 4NGF;
DR  PDB: 4NGG;
DR  PDB: 4NH3;
DR  PDB: 4NH5;
DR  PDB: 4NH6;
DR  PDB: 4NHA;
DR  PDB: 4WYQ;
DR  PDB: 5ZAK;
DR  PDB: 5ZAL;
DR  PDB: 5ZAM;
DR  Pfam: PF00271;
DR  Pfam: PF02170;
DR  Pfam: PF04851;
DR  Pfam: PF00636;
DR  PROSITE: PS51327;
DR  PROSITE: PS50137;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50821;
DR  PROSITE: PS00517;
DR  PROSITE: PS50142;
DR  OMIM: 138800;
DR  OMIM: 180295;
DR  OMIM: 601200;
DR  OMIM: 606241;
DR  OMIM: 618272;
DR  DisGeNET: 23405;
DE  Function: Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes. {ECO:0000269|PubMed:15242644, ECO:0000269|PubMed:15973356, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:18178619}.
DE  Disease: Pleuropulmonary blastoma (PPB) [MIM:601200]: A rare pediatric intrathoracic neoplasm. The tumor arises from the lung, pleura, or both, and appears to be purely mesenchymal in phenotype. It lacks malignant epithelial elements, a feature that distinguishes it from the classic adult-type pulmonary blastoma. It arises during fetal lung development and is often part of an inherited cancer syndrome. The tumor contain both epithelial and mesenchymal cells. Early in tumorigenesis, cysts form in lung airspaces, and these cysts are lined with benign-appearing epithelium. Mesenchymal cells susceptible to malignant transformation reside within the cyst walls and form a dense layer beneath the epithelial lining. In a subset of patients, overgrowth of the mesenchymal cells produces a sarcoma, a transition that is associated with a poorer prognosis. Some patients have multilocular cystic nephroma, a benign kidney tumor. {ECO:0000269|PubMed:19556464}. Note=The disease is caused by variants affecting the gene represented in this entry. Goiter multinodular 1, with or without Sertoli-Leydig cell tumors (MNG1) [MIM:138800]: A common disorder characterized by nodular overgrowth of the thyroid gland. Some individuals may also develop Sertoli-Leydig cell tumors, usually of the ovary. {ECO:0000269|PubMed:21205968}. Note=The disease is caused by variants affecting the gene represented in this entry. Rhabdomyosarcoma, embryonal, 2 (RMSE2) [MIM:180295]: A form of rhabdomyosarcoma, a highly malignant tumor of striated muscle derived from primitive mesenchymal cells and exhibiting differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently occurring soft tissue sarcomas and the most common in children. It occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal rhabdomyosarcomas. {ECO:0000269|PubMed:21882293}. Note=The disease is caused by variants affecting the gene represented in this entry. Global developmental delay, lung cysts, overgrowth, and Wilms tumor (GLOW) [MIM:618272]: A disease characterized by the association of congenital nephromegaly, bilateral Wilms tumor, somatic overgrowth, developmental delay, macrocephaly, and bilateral lung cysts. {ECO:0000269|PubMed:24676357}. Note=The disease is caused by variants affecting the gene represented in this entry. Note=DICER1 mutations have been found in uterine cervix embryonal rhabdomyosarcoma, primitive neuroectodermal tumor, Wilms tumor, pulmonary sequestration and juvenile intestinal polyp (PubMed:21882293). Somatic missense mutations affecting the RNase IIIb domain of DICER1 are common in non-epithelial ovarian tumors. These mutations do not abolish DICER1 function but alter it in specific cell types, a novel mechanism through which perturbation of microRNA processing may be oncogenic (PubMed:22187960). {ECO:0000269|PubMed:21882293, ECO:0000269|PubMed:22187960}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: K9N7C7; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: O15027; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: O15234; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: O75569; IntAct: EBI-8031519; Score: 0.74
DE  Interaction: P0C6X1; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P0C6X4; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P0C6X5; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P0C6X6; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: P19525; IntAct: EBI-6116026; Score: 0.50
DE  Interaction: P27958; IntAct: EBI-9392140; Score: 0.40
DE  Interaction: P35658; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-20621330; Score: 0.50
DE  Interaction: P52948; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q06787; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-20621330; Score: 0.35
DE  Interaction: Q15633; IntAct: EBI-8031567; Score: 0.96
DE  Interaction: Q61496; IntAct: EBI-15569634; Score: 0.54
DE  Interaction: Q8TB72; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q92900; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q99523; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9H6S0; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9NZI8; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9NWA0; IntAct: EBI-394834; Score: 0.35
DE  Interaction: Q9NX70; IntAct: EBI-394875; Score: 0.35
DE  Interaction: Q96J94; IntAct: EBI-527373; Score: 0.50
DE  Interaction: Q9UKV8; IntAct: EBI-527585; Score: 0.94
DE  Interaction: Q7Z3Z4; IntAct: EBI-528620; Score: 0.37
DE  Interaction: Q9UL18; IntAct: EBI-528294; Score: 0.72
DE  Interaction: Q8CJG0; IntAct: EBI-528561; Score: 0.52
DE  Interaction: P02768; IntAct: EBI-1222961; Score: 0.35
DE  Interaction: Q70CQ1; IntAct: EBI-2512828; Score: 0.40
DE  Interaction: P0C205; IntAct: EBI-8332957; Score: 0.61
DE  Interaction: O43741; IntAct: EBI-3937984; Score: 0.37
DE  Interaction: Q96C10; IntAct: EBI-6115711; Score: 0.50
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.46
DE  Interaction: Q9UHI6; IntAct: EBI-6598911; Score: 0.35
DE  Interaction: P57678; IntAct: EBI-6598937; Score: 0.35
DE  Interaction: P55265; IntAct: EBI-6913036; Score: 0.65
DE  Interaction: Q14686; IntAct: EBI-8756175; Score: 0.44
DE  Interaction: P16150; IntAct: EBI-10049049; Score: 0.35
DE  Interaction: Q9UI95; IntAct: EBI-11059438; Score: 0.35
DE  Interaction: Q9H9G7; IntAct: EBI-11090247; Score: 0.35
DE  Interaction: Q9Y5L4; IntAct: EBI-11125620; Score: 0.35
DE  Interaction: Q96EQ0; IntAct: EBI-11152414; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-11152836; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-11153302; Score: 0.53
DE  Interaction: P22415; IntAct: EBI-11158458; Score: 0.35
DE  Interaction: Q9H9F9; IntAct: EBI-11160007; Score: 0.35
DE  Interaction: P61224; IntAct: EBI-11160765; Score: 0.35
DE  Interaction: Q96LK0; IntAct: EBI-11376319; Score: 0.27
DE  Interaction: Q9Y6A4; IntAct: EBI-12449464; Score: 0.51
DE  Interaction: C5E524; IntAct: EBI-12584280; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: A2AM67; IntAct: EBI-15101712; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q9H0B3; IntAct: EBI-21526575; Score: 0.35
DE  Interaction: P13727; IntAct: EBI-21570605; Score: 0.35
DE  Interaction: Q8N490; IntAct: EBI-21596986; Score: 0.35
DE  Interaction: Q8IZ69; IntAct: EBI-21636338; Score: 0.35
DE  Interaction: Q8WV44; IntAct: EBI-21636495; Score: 0.35
DE  Interaction: O14965; IntAct: EBI-21639587; Score: 0.53
DE  Interaction: O75173; IntAct: EBI-21640424; Score: 0.35
DE  Interaction: P61313; IntAct: EBI-21697528; Score: 0.35
DE  Interaction: Q3SYB3; IntAct: EBI-21720692; Score: 0.35
DE  Interaction: Q8N4T0; IntAct: EBI-21731449; Score: 0.35
DE  Interaction: Q96SI9; IntAct: EBI-21752787; Score: 0.35
DE  Interaction: Q8N1E6; IntAct: EBI-21820146; Score: 0.35
DE  Interaction: Q92945; IntAct: EBI-15781931; Score: 0.40
DE  Interaction: O14980; IntAct: EBI-15819105; Score: 0.35
DE  Interaction: P04156; IntAct: EBI-15979960; Score: 0.35
DE  Interaction: P24928; IntAct: EBI-16106916; Score: 0.50
DE  Interaction: P35637; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P23396; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P62917; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P62701; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P61247; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P12236; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P07910; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q15365; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q8IU99; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P09651; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P38159; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q96I24; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9Y5A9; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: O00425; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q7Z739; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9Y6M1; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q4G0J3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q96AE4; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q01844; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P17844; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q96PK6; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P51114; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P11940; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q13310; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: O43390; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q92841; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P38646; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P51116; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: O75746; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P23246; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P52272; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q14444; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q92499; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: O43143; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P43243; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9Y2W1; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q8WWM7; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q14157; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q5T6F2; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q99700; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9NZB2; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q14671; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q7L2E3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q08211; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q6Y7W6; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q6P158; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9BY12; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q04637; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9UPQ9; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P48634; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: Q9NQB0; IntAct: EBI-21265942; Score: 0.35
DE  Interaction: O43508; IntAct: EBI-21195246; Score: 0.54
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: A0A0H3LBU6; IntAct: EBI-25402078; Score: 0.35
DE  Interaction: P59633; IntAct: EBI-25688366; Score: 0.35
DE  Interaction: Q9IK90; IntAct: EBI-25747350; Score: 0.50
DE  Interaction: K9N4V0; IntAct: EBI-26375098; Score: 0.35
DE  Interaction: P98179; IntAct: EBI-26967387; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: P53350; IntAct: EBI-28938281; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0005524;
GO  GO:0004530;
GO  GO:0003677;
GO  GO:0003725;
GO  GO:0004521;
GO  GO:0004386;
GO  GO:0046872;
GO  GO:0070883;
GO  GO:0019904;
GO  GO:0004525;
GO  GO:0003723;
GO  GO:0035197;
GO  GO:0006309;
GO  GO:0098795;
GO  GO:0010586;
GO  GO:0035196;
GO  GO:0010629;
GO  GO:0010626;
GO  GO:0000122;
GO  GO:0032720;
GO  GO:0021675;
GO  GO:0048812;
GO  GO:0038061;
GO  GO:0032290;
GO  GO:0031643;
GO  GO:0014040;
GO  GO:0031054;
GO  GO:0070922;
GO  GO:0090501;
GO  GO:0090502;
GO  GO:0030422;
GO  GO:0016078;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKE
SQ  LSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWNQEFTKHQVLIMTCYVALNVLK
SQ  NGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDL
SQ  VVLDRYTSQPCEIVVDCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADK
SQ  VAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFVTPKVIKLLEILRKYKPYERQQFESVEW
SQ  YNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFIT
SQ  GHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNY
SQ  IMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDIDPVMDDDDVFPPYVLRPDDGGPRVTINTAIGHINRYCAR
SQ  LPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETV
SQ  KYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRDSYPRPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTR
SQ  CFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFMLSLQMLELITRLHQYIFSHILRLEKPALEFKPTDADSAYCVLP
SQ  LNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKF
SQ  PSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAI
SQ  HPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPNLDFGWKKSIDSKSFISISNSSSAENDN
SQ  YCKHSTIVPENAAHQGANRTSSLENHDQMSVNCRTLLSESPGKLHVEVSADLTAINGLSYNQNLANGSYDLANRDFCQGN
SQ  QLNYYKQEIPVQPTTSYSIQNLYSYENQPQPSDECTLLSNKYLDGNANKSTSDGSPVMAVMPGTTDTIQVLKGRMDSEQS
SQ  PSIGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLG
SQ  KKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNTDKWEKDEMTKDCMLANGKLDEDYEEEDEEEESLMWRAPKEEADYED
SQ  DFLEYDQEHIRFIDNMLMGSGAFVKKISLSPFSTTDSAYEWKMPKKSSLGSMPFSSDFEDFDYSSWDAMCYLDPSKAVEE
SQ  DDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTDRE
SQ  KALCPTRENFNSQQKNLSVSCAAASVASSRSSVLKDSEYGCLKIPPRCMFDHPDADKTLNHLISGFENFEKKINYRFKNK
SQ  AYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKA
SQ  VSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLETVWQVYYPMMRP
SQ  LIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVP
SQ  NS
//
ID  B9U3F2;
PN  Protein dispatched homolog 3;
GN  DISP3;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:19179482}; Multi- pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Note=Predominantly localized to cholesterol-enriched domains within membranes (PubMed:19179482). Localizes to cytoplasmic punctate vesicular structures (PubMed:19179482). {ECO:0000269|PubMed:19179482}.
DR  UNIPROT: B9U3F2;
DR  UNIPROT: F1NH44;
DR  Pfam: PF02460;
DR  PROSITE: PS50156;
DE  Function: Plays a role in neuronal proliferation and differentiation (By similarity). Plays a role in the accumulation of cellular cholesterol (PubMed:19179482). Involved in intracellular lipid droplet formation (PubMed:19179482). May contribute to cholesterol homeostasis in neuronal cells (PubMed:19179482). {ECO:0000250|UniProtKB:Q9P2K9, ECO:0000269|PubMed:19179482}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030154;
GO  GO:0042632;
GO  GO:0008203;
GO  GO:0045665;
GO  GO:0045834;
GO  GO:2000179;
GO  GO:0009725;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDTEDDPLLQDAWLDEEDEEVAFSSRKRREGALLCGKSSCRVRPLRVTLPVSGFWNIVGWIFTNPYCAGFILFLGCAIPA
SQ  VLAVVMFLHYPALDIDISYNAFEIRNHESSQRFDALALALKSQFGSWGRNRRDLADFTSETLQRLIFEQLQQLHLNASHL
SQ  QVSTRAKRSAPQGRTSSPEPRAHPHPGNETSRVTRGAPRWDYSNTYISANTQTHAHWRIELIFLARGDSENNIFTTERLV
SQ  TIHEVERKIMDHPRFREFCWKPHEVLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIQGSLELAMTHPE
SQ  FYWYVDEGLSAENKKSSLLRSEILFGAPLPNYYSVEDRWEEQRHKFQNFVVTYVAMLAKQSTSKVQVLYGGTDLFDYEVR
SQ  RTFNNDMLLAFISSSCIAVLVYILTSCSVFLSFFGIASIGLSCLVALFLYHVVFGIQYLGILNGVAAFVIVGIGVDDVFV
SQ  FINTYRQATHLKDLRLRMIHTIQTAGKATFFTSLTTAAAYAANIFSQIPAVHDFGLFMSLIVSCCWVAVLFTMPAALGIW
SQ  TLYVSPLESSCQNSCSQKCTKKSTLHLAEDLFVASEGTSRAGRETLPYLDDDIPLLSVEEEPVSLEMGDVPLVSVMPENL
SQ  QLPVEKSNRGHLIAHLQELLEHWVLWSAVKSRWVIVGLFLLVLLLSIFFASRLRPASRAPVLFRPDTNIQVLLDLKYNLS
SQ  AEGISCITCSGLFQEKPHSLQNNFRTSLEKKKRGSASPWGSKGSISDTGQQDLQGTVYISKSRSKGRPAIYRFSLNASIP
SQ  APWQMVSPGDGEVPSFQVYRVPFGNFTRKLTACVSTVGLLKQTSPRKWMMTTLSCDSKRGWKFDFSFYVAAKEQQRTRKL
SQ  YFAQSHKPPYHGRVCVAPPGCLLSSSPDGPTKGILYVPSEKAAPKARLSATSGFNPCMNMGCGKPAVRPLVDTGAMVFVV
SQ  FGIRGVNRTKNSDNHVIGDMGSVIYDDSFDLFKEIGNLCRLCKAIASNTELVKPGGAQCLPSGYSISSFLQMLHPECKNI
SQ  PEPNLLPGQLSHGAVGVKDGKVQWISMAFESTTYKGKSSFQTYADYLKWETFLQQQLQLFPEGSALRHGFQTCEHWKQIF
SQ  MEIIGVQSALYGLILSLVICVAAVAVFTTHILLLLPVLLSILGVVCLVVTIMYWSGWEMGAVEAISLSILVGSSVDYCVH
SQ  LVEGYLLAGENLPLHHAEDPTACRQWRTIEAIRHVGVAIVSSAVTTVIATVPLFFCIIAPFAKFGKIVALNTGVSILYTL
SQ  TVSTALLSIMGPGTFTRSRTSCLKAVAGVLLAGLLGLCICLALLKGGFKIPLPNGTAL
//
ID  Q9P2K9;
PN  Protein dispatched homolog 3;
GN  DISP3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:19179482}; Multi- pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:B9U3F2}; Multi-pass membrane protein {ECO:0000305}. Note=Predominantly localized to cholesterol-enriched domains within the membrane (PubMed:19179482). Localizes to cytoplasmic punctate vesicular structures (By similarity). {ECO:0000250|UniProtKB:B9U3F2, ECO:0000269|PubMed:19179482}.
DR  UNIPROT: Q9P2K9;
DR  UNIPROT: Q5VTU9;
DR  UNIPROT: Q9UJD6;
DR  Pfam: PF02460;
DR  PROSITE: PS50156;
DR  OMIM: 611251;
DR  DisGeNET: 57540;
DE  Function: Plays a role in neuronal proliferation and differentiation (PubMed:25281927). Plays a role in the accumulation of cellular cholesterol (By similarity). Involved in intracellular lipid droplet formation (PubMed:25281927). May contribute to cholesterol homeostasis in neuronal cells (By similarity). {ECO:0000250|UniProtKB:B9U3F2, ECO:0000269|PubMed:25281927}.
DE  Reference Proteome: Yes;
DE  Interaction: Q99417; IntAct: EBI-735190; Score: 0.00
DE  Interaction: Q7LDG7; IntAct: EBI-735584; Score: 0.00
DE  Interaction: P00918; IntAct: EBI-736439; Score: 0.00
DE  Interaction: P49286; IntAct: EBI-11576414; Score: 0.37
DE  Interaction: P62263; IntAct: EBI-20908096; Score: 0.40
DE  Interaction: Q9NR30; IntAct: EBI-20930416; Score: 0.40
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030154;
GO  GO:0042632;
GO  GO:0008203;
GO  GO:0045665;
GO  GO:0045834;
GO  GO:2000179;
GO  GO:0032368;
GO  GO:0007224;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDTEDDPLLQDVWLEEEQEEEEATGETFLGAQKPGPQPGAGGQCCWRHWPLASRPPASGFWSTLGWAFTNPCCAGLVLFL
SQ  GCSIPMALSAFMFLYYPPLDIDISYNAFEIRNHEASQRFDALTLALKSQFGSWGRNRRDLADFTSETLQRLISEQLQQLH
SQ  LGNRSRQASRAPRVIPAASLGGPGPYRDTSAAQKPTANRSGRLRRETPPLEDLAANQSEDPRNQRLSKNGRYQPSIPPHA
SQ  AVAANQSRARRGASRWDYSRAYVSANTQTHAHWRIELIFLARGDAERNIFTSERLVTIHEIERKIMDHPGFREFCWKPHE
SQ  VLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIRGSLELAMTHPEFYWYVDEGLSADNLKSSLLRSEIL
SQ  FGAPLPNYYSVDDRWEEQRAKFQSFVVTYVAMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYIL
SQ  TSCSVFLSFFGIASIGLSCLVALFLYHVVFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATHLEDPQLRMIHTVQT
SQ  AGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVSCCWLAVLVTMPAALGLWSLYLAPLESSCQTSCHQNCSRKTS
SQ  LHFPGDVFAAPEQVGGSPAQGPIPYLDDDIPLLEVEEEPVSLELGDVSLVSVSPEGLQPASNTGSRGHLIVQLQELLHHW
SQ  VLWSAVKSRWVIVGLFVSILILSLVFASRLRPASRAPLLFRPDTNIQVLLDLKYNLSAEGISCITCSGLFQEKPHSLQNN
SQ  IRTSLEKKRRGSGVPWASRPEATLQDFPGTVYISKVKSQGHPAVYRLSLNASLPAPWQAVSPGDGEVPSFQVYRAPFGNF
SQ  TKKLTACMSTVGLLQAASPSRKWMLTTLACDAKRGWKFDFSFYVATKEQQHTRKLYFAQSHKPPFHGRVCMAPPGCLLSS
SQ  SPDGPTKGFFFVPSEKVPKARLSATFGFNPCVNTGCGKPAVRPLVDTGAMVFVVFGIIGVNRTRQVDNHVIGDPGSVVYD
SQ  SSFDLFKEIGHLCHLCKAIAANSELVKPGGAQCLPSGYSISSFLQMLHPECKELPEPNLLPGQLSHGAVGVREGRVQWIS
SQ  MAFESTTYKGKSSFQTYSDYLRWESFLQQQLQALPEGSVLRRGFQTCEHWKQIFMEIVGVQSALCGLVLSLLICVAAVAV
SQ  FTTHILLLLPVLLSILGIVCLVVTIMYWSGWEMGAVEAISLSILVGSSVDYCVHLVEGYLLAGENLPPHQAEDARTQRQW
SQ  RTLEAVRHVGVAIVSSALTTVIATVPLFFCIIAPFAKFGKIVALNTGVSILYTLTVSTALLGIMAPSSFTRTRTSFLKAL
SQ  GAVLLAGALGLGACLVLLQSGYKIPLPAGASL
//
ID  A3KFU9;
PN  Protein dispatched homolog 3;
GN  Disp3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9P2K9}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:Q9P2K9}; Multi- pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:B9U3F2}; Multi-pass membrane protein {ECO:0000305}. Note=Predominantly localized to cholesterol-enriched domains within the membrane (By similarity). Localizes to cytoplasmic punctate vesicular structures (By similarity). {ECO:0000250|UniProtKB:B9U3F2, ECO:0000250|UniProtKB:Q9P2K9}.
DR  UNIPROT: A3KFU9;
DR  UNIPROT: Q0EEE3;
DR  UNIPROT: Q69ZL6;
DR  UNIPROT: Q6GQX3;
DR  UNIPROT: Q6NS63;
DR  Pfam: PF02460;
DR  PROSITE: PS50156;
DE  Function: Plays a role in neuronal proliferation and differentiation. Plays a role in the accumulation of cellular cholesterol. Involved in intracellular lipid droplet formation. May contribute to cholesterol homeostasis in neuronal cells. {ECO:0000250|UniProtKB:B9U3F2, ECO:0000250|UniProtKB:Q9P2K9}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030154;
GO  GO:0008203;
GO  GO:0045665;
GO  GO:0045834;
GO  GO:2000179;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDSEDDPLLQDVWLEEEQPEDEACRGIPGPGLQSGAQGCWRRWTLPSRPPTLGFWSTLGWAFTNPCCAGLVLFLGCSIPM
SQ  VLSAFMFLYYPPLDIDISYNAFEIRNHEASQRFDALALALKSQFGSWGRNRRDLADFTSETLQRLISEQLQQLHLGNHSR
SQ  PASRAPRSAPRDTVATQTSAANSSERRRREAPSPEGQVTNQSRARRGASRWDYSRTYVSANTQTHAHWRIELIFLARGDA
SQ  ERNIFTSERLVTIHEIERKIMDHPGFREFCWKPHEVLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIR
SQ  GSLELAMTHPEFYWYVDEGLSVDNLKSSLLRSEILFGAPLPNYYSVDDRWEEQRAKFQSFVVTYVAMLAKQSTSKVQVLY
SQ  GGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSCLVALFLYHVVFGIQYLGILNGVAAFV
SQ  IVGIGVDDVFVFINTYRQATHLEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVTCCWLAV
SQ  LFTMPAALGLWSLYMAPLESSCQNSCHQKCGRKSSLHFPGDLFTAPERAGGGPAQGPLPYLDDDIPLLNVEDEPASLELG
SQ  DVSLVSVHCEGLQPTPDANSRGQLLAQLQELLHHWVLWAAVKSRWVIVGLFASILILSLVFASRLRPASRAPLLFRPDTN
SQ  IQVLLDLKYNLSAEGISCITCSGLFQEKPHSLQNNVRTSLEKKKRGSGVSWASRTETTAQESMSTVYISKVKSKGHPAVY
SQ  RLSLNASLPAPWQAVSPGDGEVPSFQVYRAPFGDFTKKLTACMSTVGLLQAASPSRKWMVTALACDARRGWKFDFSFYVA
SQ  TKEQQHTRKLYFAQSHKPPFHGRLCVAPPGCLLSSSPDGPTKGFFYVPSDKVPKARISATFGFNPCVNTGCGKPAVRPLV
SQ  DTGAMVFVVFGIIGLNRTQQMDNHVIGDPGSVIYDSSFDLFKEIGHLCRLCKAIAGNSELVKPGGAQCLPSGYSISSFLQ
SQ  MLHPECKELPEPNLLPGQLSHGAVGVKEGRVQWISMAFESTTYKGKSSFQTYSDYLRWESFLRQQLQTFPEGSALHRGFQ
SQ  TCEHWKQIFMEIIGVQSALYGLVLSLLICVAAVAVFTTHVLLLLPVLLSILGIVCLVVTIMYWSGWEMGAVEAISLSILV
SQ  GSSVDYCVHLVEGYLLAGENLPPQLSQDPSSQRQWRTLEAVRHVGVAIVSSALTTVIATVPLFFCIIAPFAKFGKIVALN
SQ  TGVSILYTLTVSTALLGIMAPGSFTRTRTSFLKALGAVLLAGALGLGACLVLLRSGYKIPLPSGATL
//
ID  Q58DR2;
PN  DnaJ homolog subfamily B member 12;
GN  DNAJB12;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NXW2}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9NXW2}; Single- pass membrane protein {ECO:0000250|UniProtKB:Q9NXW2}. Note=Localizes to the endoplasmic reticulum membrane. When overexpressed, forms membranous structures in the nucleus. {ECO:0000250|UniProtKB:Q9NXW2}.
DR  UNIPROT: Q58DR2;
DR  Pfam: PF00226;
DR  Pfam: PF09320;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear. {ECO:0000250|UniProtKB:Q9NXW2}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0030544;
GO  GO:0071218;
GO  GO:0051085;
GO  GO:0036503;
GO  GO:0065003;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESNKDEAERCISIALKAIQSNQPDRALRFLEKAQRLYPTPRVHALIESLNQKPQPAGDQPQPTEATHTTHRKAAGANTA
SQ  SANGEAGGESTKGYTAEQVAAVKRVKQCKDYYEILGVSRGASDEDLKKAYRKLALKFHPDKNHAPGATEAFKAIGTAYAV
SQ  LSNPEKRKQYDQFGDDKGQAARHGHGHGDFHRGFEADISPEDLFNMFFGGGFPSSNVHVYSNGRMRYTYHQRQDRRENQG
SQ  DGGLGVFVQLMPILILILVSALSQLMVSSPPYSLSLRPSVGHVHKRVTDHLNVVYYVADTFSQEYTGSSLKMVERNVEDD
SQ  YIANLRNNCWKEKQQKEGLLYRARYFGDADMYNKAQKDGAPQAVTDCQRL
//
ID  Q9NXW2;
PN  DnaJ homolog subfamily B member 12;
GN  DNAJB12;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:24732912}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to the endoplasmic reticulum membrane (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). When overexpressed, forms membranous structures in the nucleus (PubMed:24732912). {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}.
DR  UNIPROT: Q9NXW2;
DR  UNIPROT: B7Z7I3;
DR  UNIPROT: Q9H6H0;
DR  PDB: 2CTP;
DR  Pfam: PF00226;
DR  Pfam: PF09320;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  OMIM: 608376;
DR  DisGeNET: 54788;
DE  Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway (PubMed:21150129, PubMed:21148293). Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities (PubMed:21148293). Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers (PubMed:27916661). While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70 (PubMed:27916661). When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear (PubMed:24732912). {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}. (Microbial infection) In case of infection by polyomavirus, involved in the virus endoplasmic reticulum membrane penetration and infection (PubMed:21673190, PubMed:24675744). {ECO:0000269|PubMed:21673190, ECO:0000269|PubMed:24675744}.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P19438; IntAct: EBI-364378; Score: 0.00
DE  Interaction: P08473; IntAct: EBI-1389788; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-3893169; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: O95429; IntAct: EBI-9393134; Score: 0.35
DE  Interaction: Q96BE0; IntAct: EBI-9394503; Score: 0.35
DE  Interaction: O43765; IntAct: EBI-9395484; Score: 0.35
DE  Interaction: Q16659; IntAct: EBI-12502733; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-12579142; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12588098; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12588729; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q13011; IntAct: EBI-16813992; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P04233; IntAct: EBI-21258980; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21132574; Score: 0.35
DE  Interaction: P49768; IntAct: EBI-21132675; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P17813; IntAct: EBI-22197897; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-28935882; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32717464; Score: 0.35
DE  Interaction: Q5JZY3; IntAct: EBI-32717780; Score: 0.35
DE  Interaction: P08069; IntAct: EBI-32718669; Score: 0.35
DE  Interaction: P04629; IntAct: EBI-32719115; Score: 0.35
DE  Interaction: Q16288; IntAct: EBI-32719212; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0030544;
GO  GO:0071218;
GO  GO:0051085;
GO  GO:0036503;
GO  GO:0065003;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESNKDEAERCISIALKAIQSNQPDRALRFLEKAQRLYPTPRVRALIESLNQKPQTAGDQPPPTDTTHATHRKAGGTDAP
SQ  SANGEAGGESTKGYTAEQVAAVKRVKQCKDYYEILGVSRGASDEDLKKAYRRLALKFHPDKNHAPGATEAFKAIGTAYAV
SQ  LSNPEKRKQYDQFGDDKSQAARHGHGHGDFHRGFEADISPEDLFNMFFGGGFPSSNVHVYSNGRMRYTYQQRQDRRDNQG
SQ  DGGLGVFVQLMPILILILVSALSQLMVSSPPYSLSPRPSVGHIHRRVTDHLGVVYYVGDTFSEEYTGSSLKTVERNVEDD
SQ  YIANLRNNCWKEKQQKEGLLYRARYFGDTDMYHRAQKMGTPSCSRLSEVQASLHG
//
ID  Q9QYI4;
PN  DnaJ homolog subfamily B member 12;
GN  Dnajb12;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NXW2}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9NXW2}; Single- pass membrane protein {ECO:0000250|UniProtKB:Q9NXW2}. Note=Localizes to the endoplasmic reticulum membrane. When overexpressed, forms membranous structures in the nucleus. {ECO:0000250|UniProtKB:Q9NXW2}.
DR  UNIPROT: Q9QYI4;
DR  UNIPROT: Q8K037;
DR  Pfam: PF00226;
DR  Pfam: PF09320;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear. {ECO:0000250|UniProtKB:Q9NXW2}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0031965;
GO  GO:0030544;
GO  GO:0071218;
GO  GO:0051085;
GO  GO:0036503;
GO  GO:0065003;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESNKDEAERCISIALKAIQSNQPERALRFLEKAQRLYPTPRVSALIESLNQKPQSTGDHPQPTDTTHTTTKKAGGTETP
SQ  SANGEAGGGESAKGYTSEQVAAVKRVKQCKDYYEILGVSRSASDEDLKKAYRKLALKFHPDKNHAPGATEAFKAIGTAYA
SQ  VLSNPEKRKQYDQFGDDKSQAARHGHSHGDFHRGFEADISPEDLFNMFFGGGFPSSNVHVYSNGRMRYTYQQRQDRRDNQ
SQ  GDGGLGVFVQLMPILILILVSALSQLMVSSPPYSLSPRPSVGHIHKRVTDHLNVAYYVADTFSEEYTGSSLKTVERNVED
SQ  DYIANLRNNCWKEKQQKEGLLYRARYFGDTDMYHRAQKMGTPSCNRLSEVQASLHG
//
ID  Q0IIE8;
PN  DnaJ homolog subfamily B member 14;
GN  DNAJB14;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single- pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic reticulum membrane. When overexpressed, forms membranous structures in the nucleus. {ECO:0000250|UniProtKB:Q8TBM8}.
DR  UNIPROT: Q0IIE8;
DR  Pfam: PF00226;
DR  Pfam: PF09320;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear. {ECO:0000250|UniProtKB:Q8TBM8}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030544;
GO  GO:0071218;
GO  GO:0051085;
GO  GO:0065003;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGGGDQSKPNCTKD
SQ  SSSGSGESGKGYTKDQVDGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLS
SQ  NPEKRKQYDLTGNEEQACNQQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSNQHQHRHSGHEREE
SQ  ERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGSGQTIKMQTENLGVIYYVNKDFKNEYKGMLLQKVEKSV
SQ  EEDYVTNIRNNCWKERQQKTDMQYAAKVYHDERLRRKAEALSMDNCKELERLTSIYKGG
//
ID  Q8TBM8;
PN  DnaJ homolog subfamily B member 14;
GN  DNAJB14;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:24732912}; Single- pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic reticulum membrane (PubMed:23018488, PubMed:24732912, PubMed:27916661). When overexpressed, forms membranous structures in the nucleus (PubMed:24732912). {ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}.
DR  UNIPROT: Q8TBM8;
DR  UNIPROT: Q6UXN1;
DR  UNIPROT: Q7Z3P0;
DR  UNIPROT: Q86TA7;
DR  UNIPROT: Q86TM0;
DR  UNIPROT: Q9GZU9;
DR  Pfam: PF00226;
DR  Pfam: PF09320;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  OMIM: 617487;
DR  DisGeNET: 79982;
DE  Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway (PubMed:24732912). Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities (PubMed:24732912). Can also act independently of HSPA8/Hsc70: together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers (PubMed:27916661). While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70 (PubMed:27916661). When overexpressed, forms membranous structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear (PubMed:24732912). {ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}. (Microbial infection) In case of infection by polyomavirus, involved in the virus endoplasmic reticulum membrane penetration and infection (PubMed:21673190, PubMed:24675744). {ECO:0000269|PubMed:21673190, ECO:0000269|PubMed:24675744}.
DE  Reference Proteome: Yes;
DE  Interaction: P28702; IntAct: EBI-2689805; Score: 0.00
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: P06461; IntAct: EBI-11723785; Score: 0.35
DE  Interaction: P50053; IntAct: EBI-21871951; Score: 0.40
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0030544;
GO  GO:0071218;
GO  GO:0051085;
GO  GO:0065003;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGSGDQSKPNCTKD
SQ  STSGSGEGGKGYTKDQVDGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLS
SQ  NPEKRKQYDLTGNEEQACNHQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSQQHQHRHSGHEREE
SQ  ERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGTGQTIKMQTENLGVVYYVNKDFKNEYKGMLLQKVEKSV
SQ  EEDYVTNIRNNCWKERQQKTDMQYAAKVYRDDRLRRKADALSMDNCKELERLTSLYKGG
//
ID  Q149L6;
PN  DnaJ homolog subfamily B member 14;
GN  Dnajb14;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single- pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic reticulum membrane. When overexpressed, forms membranous structures in the nucleus. {ECO:0000250|UniProtKB:Q8TBM8}.
DR  UNIPROT: Q149L6;
DR  UNIPROT: Q3TU54;
DR  UNIPROT: Q3UTE5;
DR  Pfam: PF00226;
DR  Pfam: PF09320;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear. {ECO:0000250|UniProtKB:Q8TBM8}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030544;
GO  GO:0071218;
GO  GO:0051085;
GO  GO:0065003;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGNRDEAEKCVQIAREALSAGNRDKAQRFLQKAEKLYPLPAARALLEIIMKNGSTAGSSTHCRKPPGSSDQSKPSCGKD
SQ  GTSGAGEGGKVYTKDQVEGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLS
SQ  NPEKRKQYDLTGSEEQACNHQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAAYSHQHQHRHSGHEREE
SQ  ERADGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGSGQTIKMQTENLGVVYYVSKDFKSEYKGTLLQKVEKSV
SQ  EEDYVTNIRNNCWKERQQKTDMQYAAKVYRDEQLRRKADALSMENCKELERLTSLYKGG
//
ID  Q5R6H3;
PN  DnaJ homolog subfamily B member 14;
GN  DNAJB14;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single- pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic reticulum membrane. When overexpressed, forms membranous structures in the nucleus. {ECO:0000250|UniProtKB:Q8TBM8}.
DR  UNIPROT: Q5R6H3;
DR  Pfam: PF00226;
DR  Pfam: PF09320;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear. {ECO:0000250|UniProtKB:Q8TBM8}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0051085;
GO  GO:0065003;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGSGDQSKPNCTKD
SQ  STSGSGEGGKGYTKDQVDGVLSINKCKNCYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLS
SQ  NPEKRKQYDLTGNEEQACNHQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSQQHQHRHSGHEREE
SQ  ERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGTGQTIKMQTENLGVVYYVNKDFKNEYKGMLLQKVEKSV
SQ  EEDYVTNIRNNCWKERQQKTDMQYAAKVYRDDRLRRKADALSMDNCKELERLTSLYKGG
//
ID  Q6RHR6;
PN  Ion channel DMI1;
GN  DMI1;
OS  3880;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:17173544, ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000269|PubMed:17173544}.
DR  UNIPROT: Q6RHR6;
DR  UNIPROT: Q1SKV5;
DR  Pfam: PF06241;
DE  Function: Required for early signal transduction events leading to endosymbiosis. Acts early in a signal transduction chain leading from the perception of Nod factor to the activation of calcium spiking. Also involved in mycorrhizal symbiosis. May be involved in the regulation of the calcium channel responsible for calcium spiking by mobilizing another cation, and thereby altering the membrane potential. {ECO:0000269|PubMed:17631529}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006811;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKSNEESSNLNVMNKPPLKKTKTLPSLNLRVSVTPPNPNDNNGIGGTSTTKTDFSEQQWNYPSFLGIGSTSRKRRQPPP
SQ  PPSKPPVNLIPPHPRPLSVNDHNKTTSSLLPQPSSSSITKQQQQHSTSSPIFYLLVICCIILVPYSAYLQYKLAKLKDMK
SQ  LQLCGQIDFCSRNGKTSIQEEVDDDDNADSRTIALYIVLFTLILPFVLYKYLDYLPQIINFLRRTESNKEDVPLKKRVAY
SQ  MVDVFFSIYPYAKLLALLCATLFLIAFGGLALYAVTGGSMAEALWHSWTYVADAGNHAETEGTGQRIVSVSISAGGMLIF
SQ  AMMLGLVSDAISEKVDSLRKGKSEVIERNHVLILGWSDKLGSLLKQLAIANKSVGGGVIVVLAEKEKEEMEMDIAKLEFD
SQ  FMGTSVICRSGSPLILADLKKVSVSKARAIIVLAADENADQSDARALRVVLSLAGVKEGLRGHVVVEMSDLDNEPLVKLV
SQ  GGELIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIKRWPELDDLLFKDILISFPDAIPCGVKVAADGGKIV
SQ  INPDDNYVLRDGDEVLVIAEDDDTYAPGPLPEVRKGYFPRIRDPPKYPEKILFCGWRRDIDDMIMVLEAFLAPGSELWMF
SQ  NEVPEKERERKLAAGELDVFGLENIKLVHREGNAVIRRHLESLPLETFDSILILADESVEDSVAHSDSRSLATLLLIRDI
SQ  QSRRLPYRDTKSTSLRLSGFSHNSWIREMQQASDKSIIISEILDSRTRNLVSVSRISDYVLSNELVSMALAMVAEDKQIN
SQ  RVLEELFAEEGNEMCIKPAEFYLFDQEELCFYDIMIRGRTRKEIVIGYRLANQERAIINPSEKSVPRKWSLDDVFVVLAS
SQ  GE
//
ID  Q09013;
PN  Myotonin-protein kinase;
GN  DMPK;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Mitochondrion outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Sarcoplasmic reticulum membrane {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Localizes to sarcoplasmic reticulum membranes of cardiomyocytes. {ECO:0000250}. [Isoform 1]: Mitochondrion membrane. [Isoform 3]: Mitochondrion membrane.
DR  UNIPROT: Q09013;
DR  UNIPROT: E5KR08;
DR  UNIPROT: Q16205;
DR  UNIPROT: Q6P5Z6;
DR  PDB: 1WT6;
DR  PDB: 2VD5;
DR  Pfam: PF08826;
DR  Pfam: PF00069;
DR  PROSITE: PS51285;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 160900;
DR  OMIM: 605377;
DR  DisGeNET: 1760;
DE  Function: Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity. {ECO:0000269|PubMed:10811636, ECO:0000269|PubMed:10913253, ECO:0000269|PubMed:11287000, ECO:0000269|PubMed:15598648, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:21949239}.
DE  Disease: Dystrophia myotonica 1 (DM1) [MIM:160900]: A muscular disorder characterized by myotonia, muscle wasting in the distal extremities, cataract, hypogonadism, defective endocrine functions, male baldness and cardiac arrhythmias. {ECO:0000269|PubMed:1302022, ECO:0000269|PubMed:1310900, ECO:0000269|PubMed:1546326, ECO:0000269|PubMed:19514047}. Note=The disease is caused by variants affecting the gene represented in this entry. The causative mutation is a CTG expansion in the 3'-UTR of the DMPK gene. A length exceeding 50 CTG repeats is pathogenic, while normal individuals have 5 to 37 repeats. Intermediate alleles with 35-49 triplets are not disease- causing but show instability in intergenerational transmissions. Disease severity varies with the number of repeats: mildly affected persons have 50 to 150 repeats, patients with classic DM have 100 to 1,000 repeats, and those with congenital onset can have more than 2,000 repeats. {ECO:0000269|PubMed:1310900, ECO:0000269|PubMed:19514047}.
DE  Reference Proteome: Yes;
DE  Interaction: P54259; IntAct: EBI-951106; Score: 0.00
DE  Interaction: O14974; IntAct: EBI-7816696; Score: 0.57
DE  Interaction: P26678; IntAct: EBI-692834; Score: 0.56
DE  Interaction: O95166; IntAct: EBI-736628; Score: 0.00
DE  Interaction: Q9NRR5; IntAct: EBI-950164; Score: 0.00
DE  Interaction: P54253; IntAct: EBI-25979988; Score: 0.67
DE  Interaction: A0A380PIN1; IntAct: EBI-2871448; Score: 0.00
DE  Interaction: A0A5P8YAW1; IntAct: EBI-2871441; Score: 0.00
DE  Interaction: P57678; IntAct: EBI-3937335; Score: 0.37
DE  Interaction: P20073; IntAct: EBI-7097427; Score: 0.37
DE  Interaction: Q13526; IntAct: EBI-7301228; Score: 0.37
DE  Interaction: P46783; IntAct: EBI-7366739; Score: 0.37
DE  Interaction: Q16637; IntAct: EBI-7388858; Score: 0.37
DE  Interaction: P04183; IntAct: EBI-7397010; Score: 0.37
DE  Interaction: P08238; IntAct: EBI-6422924; Score: 0.40
DE  Interaction: O43364; IntAct: EBI-21249174; Score: 0.37
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0031307;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:0033017;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0017020;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0006874;
GO  GO:0035556;
GO  GO:0010657;
GO  GO:0006998;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0014853;
GO  GO:0008016;
GO  GO:0010830;
GO  GO:0014722;
GO  GO:0002028;
GO  GO:0051823;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRG
SQ  AFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLL
SQ  SKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSP
SQ  EILQAVGGGPGTGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCP
SQ  PETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPF
SQ  VGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVL
SQ  TRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATDPPSHLDGPPAVAVGQ
SQ  CPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP
//
ID  P54265;
PN  Myotonin-protein kinase;
GN  Dmpk;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Sarcoplasmic reticulum membrane. Cell membrane. Note=Localizes to sarcoplasmic reticulum membranes of cardiomyocytes. [Isoform 1]: Endoplasmic reticulum membrane; Single-pass type IV membrane protein; Cytoplasmic side. Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side. [Isoform 8]: Mitochondrion outer membrane; Single-pass type IV membrane protein. [Isoform 5]: Cytoplasm, cytosol.
DR  UNIPROT: P54265;
DR  Pfam: PF08826;
DR  Pfam: PF00069;
DR  PROSITE: PS51285;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity. {ECO:0000269|PubMed:12612014, ECO:0000269|PubMed:15598648, ECO:0000269|PubMed:18729234, ECO:0000269|PubMed:21949239, ECO:0000269|PubMed:9294109}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0031307;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:0033017;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0017020;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0006874;
GO  GO:0035556;
GO  GO:0010657;
GO  GO:0006998;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0014853;
GO  GO:0008016;
GO  GO:0010830;
GO  GO:0014722;
GO  GO:0002028;
GO  GO:0051823;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAEVRLRQLQQLVLDPGFLGLEPLLDLLLGVHQELGASHLAQDKYVADFLQWVEPIAARLKEVRLQRDDFEILKVIGRG
SQ  AFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVKGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLL
SQ  SKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLQPDGMVRSLVAVGTPDYLSP
SQ  EILQAVGGGPGAGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYAKIVHYREHLSLPLADTVVPEEAQDLIRGLLCP
SQ  AEIRLGRGGAGDFQKHPFFFGLDWEGLRDSVPPFTPDFEGATDTCNFDVVEDRLTAMVSGGGETLSDMQEDMPLGVRLPF
SQ  VGYSYCCMAFRDNQVPDPTPMELEALQLPVSDLQGLDLQPPVSPPDQVAEEADLVAVPAPVAEAETTVTLQQLQEALEEE
SQ  VLTRQSLSRELEAIRTANQNFSSQLQEAEVRNRDLEAHVRQLQERMEMLQAPGAAAITGVPSPRATDPPSHLDGPPAVAV
SQ  GQCPLVGPGPMHRRHLLLPARIPRPGLSEARCLLLFAAALAAAATLGCTGLVAYTGGLTPVWCFPGATFAP
//
ID  Q95JF4;
PN  DnaJ homolog subfamily A member 1;
GN  DNAJA1;
OS  9534;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity). {ECO:0000250}.
DR  UNIPROT: Q95JF4;
DR  Pfam: PF00226;
DR  Pfam: PF01556;
DR  Pfam: PF00684;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51188;
DE  Function: Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). {ECO:0000250, ECO:0000269|PubMed:11874471}.
DE  Reference Proteome: No;
GO  GO:0005783;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0001671;
GO  GO:0051087;
GO  GO:0030544;
GO  GO:0046872;
GO  GO:0051082;
GO  GO:0043066;
GO  GO:0043508;
GO  GO:0043065;
GO  GO:0006457;
GO  GO:0070585;
GO  GO:0051223;
GO  GO:0009408;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGG
SQ  FGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQI
SQ  RIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDII
SQ  IVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRL
SQ  IIEFKINFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
//
ID  P00639;
PN  Deoxyribonuclease-1;
GN  DNASE1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000269|PubMed:4734471}. Zymogen granule {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: P00639;
DR  UNIPROT: A5PK44;
DR  UNIPROT: Q8MJ27;
DR  PDB: 1ATN;
DR  PDB: 1DNK;
DR  PDB: 2A3Z;
DR  PDB: 2A40;
DR  PDB: 2A41;
DR  PDB: 2A42;
DR  PDB: 2D1K;
DR  PDB: 2DNJ;
DR  PDB: 3CJC;
DR  PDB: 3DNI;
DR  PDB: 3W3D;
DR  PDB: 7NXV;
DR  PDB: 7NZM;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:4976790, PubMed:5166750, PubMed:3352748, PubMed:2395459). Expressed by non- hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (PubMed:2395459). Binds specifically to G-actin and blocks actin polymerization (PubMed:2395459). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P49183, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:3352748, ECO:0000269|PubMed:4976790, ECO:0000269|PubMed:5166750}.
DE  Reference Proteome: Yes;
DE  Interaction: P68133; IntAct: EBI-8545980; Score: 0.44
DE  Interaction: P68135; IntAct: EBI-15622376; Score: 0.72
DE  Interaction: P60010; IntAct: EBI-15635389; Score: 0.44
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0042588;
GO  GO:0003779;
GO  GO:0004530;
GO  GO:0003677;
GO  GO:0006915;
GO  GO:0006308;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRGTRLMGLLLALAGLLQLGLSLKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQD
SQ  DPNTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPS
SQ  DAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAG
SQ  SLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTLT
//
ID  Q767J3;
PN  Deoxyribonuclease-1;
GN  DNASE1;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: Q767J3;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:14688237). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (PubMed:14688237). Binds specifically to G- actin and blocks actin polymerization (PubMed:14688237). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P49183, ECO:0000269|PubMed:14688237}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0042588;
GO  GO:0003779;
GO  GO:0004530;
GO  GO:0003677;
GO  GO:0006915;
GO  GO:0006308;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRGARLMGALLALAGLLQGALALRMAAFNIRTFGETKMSNATLSKYIVQILSRYDVAVVQEVRDSHLTAVGKLLDTLNQD
SQ  DPNAYHYVVSEPLGRSSYKERYLFLFRPDRVSVLDSYQYDDGCEPCGNDTFSREPAIVRFHSPLTEVKEFAVVPLHAAPL
SQ  DAVAEIDALYDVYLDVQHKWDLEDIVLMGDFNAGCSYVAASQWSSIRLRTNPAFQWLIPDTADTTSTSTHCAYDRIVVAG
SQ  SQLQHAVVPESAAPFNFQVAYGLSSQLAQAISDHYPVEVTLKRA
//
ID  Q9YGI5;
PN  Deoxyribonuclease-1;
GN  DNASE1;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: Q9YGI5;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:12739897). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (By similarity). Binds specifically to G-actin and blocks actin polymerization (By similarity). {ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P24855, ECO:0000269|PubMed:12739897}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0042588;
GO  GO:0003779;
GO  GO:0004530;
GO  GO:0006915;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MARLVLELLAAALLLRVAATLRISAFNIRTFGDSKMSNQTVAGFIVSILVQYDITLVQEVRDADLSSVKKLVSQLNSASS
SQ  YPYSFLSSIPLGRNSYKEQYVFIYRSDIVSVLESYYYDDGCESCGTDIFSREPFIVKFSSPTTQLDEFVIVPLHAEPSSA
SQ  PAEINALTDVYTDVINKWETNNIFFMGDFNADCSYVTAEQWPSIRLRSLSSCEWLIPDSADTTVTSTDCAYDRIVACGSA
SQ  LRQAVEYGSATVNNFQETLRIQNKDALAISDHFPVEVTLKAR
//
ID  Q4AEE3;
PN  Deoxyribonuclease-1;
GN  DNASE1;
OS  9796;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: Q4AEE3;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (By similarity). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA. Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P00639, ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P24855, ECO:0000250|UniProtKB:P49183}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0042588;
GO  GO:0003779;
GO  GO:0004530;
GO  GO:0003677;
GO  GO:0006915;
GO  GO:0006308;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRGARLTGALLALAGLLQVALSLRIAAFNIRTFGETKMSNDTLSNYIVQILNRYDIALIQEVRDSHLTAVGKLLDRLNQD
SQ  DPNTYHFVVSEPLGRNNYKERYLFVFRPDQVSLLDSYQYNDGCEPCGNDTFSREPAIVKFSSPFTQVKEFAIVPLHAAPS
SQ  DALAEIDSLYDVYLDVQQKWDMEDIMLMGDFNAGCSYVTSSQWPSIRLRRNPAFWWLIPDTADTTVKSTHCAYDRIVVAG
SQ  TLLQEAVVPDSAVPFDFQAAYGLNDQTAEAISDHYPVEVTLM
//
ID  P24855;
PN  Deoxyribonuclease-1;
GN  DNASE1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000269|PubMed:2277032}. Zymogen granule {ECO:0000305}. Nucleus envelope. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope.
DR  UNIPROT: P24855;
DR  UNIPROT: B4DV35;
DR  UNIPROT: Q14UU9;
DR  UNIPROT: Q14UV0;
DR  PDB: 4AWN;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DR  OMIM: 125505;
DR  OMIM: 152700;
DR  DisGeNET: 1773;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:2251263, PubMed:11241278, PubMed:2277032). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (PubMed:11241278). Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P00639, ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P49183, ECO:0000269|PubMed:11241278, ECO:0000269|PubMed:2251263, ECO:0000269|PubMed:2277032}.
DE  Disease: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:11479590, ECO:0000269|PubMed:20439745}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Neutrophil extracellular traps (NETs) are impaired in patients suffering from SLE (PubMed:20439745). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (PubMed:20439745). {ECO:0000269|PubMed:20439745}.
DE  Reference Proteome: Yes;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0042588;
GO  GO:0003779;
GO  GO:0004530;
GO  GO:0003677;
GO  GO:0006915;
GO  GO:0006308;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRGMKLLGALLALAALLQGAVSLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQD
SQ  APDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPG
SQ  DAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAG
SQ  MLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK
//
ID  P49183;
PN  Deoxyribonuclease-1;
GN  Dnase1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: P49183;
DR  UNIPROT: O70532;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:29191910). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA. Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (PubMed:29191910). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (PubMed:29191910). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (PubMed:29191910). {ECO:0000250|UniProtKB:P00639, ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P24855, ECO:0000269|PubMed:29191910}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9WVE0; IntAct: EBI-3870545; Score: 0.35
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0042588;
GO  GO:0003779;
GO  GO:0004536;
GO  GO:0004530;
GO  GO:0003677;
GO  GO:0006915;
GO  GO:0006308;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRYTGLMGTLLTLVNLLQLAGTLRIAAFNIRTFGETKMSNATLSVYFVKILSRYDIAVIQEVRDSHLVAVGKLLDELNRD
SQ  KPDTYRYVVSEPLGRKSYKEQYLFVYRPDQVSILDSYQYDDGCEPCGNDTFSREPAIVKFFSPYTEVQEFAIVPLHAAPT
SQ  EAVSEIDALYDVYLDVWQKWGLEDIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTVTSTHCAYDRIVVAG
SQ  ALLQAAVVPNSAVPFDFQAEYGLSNQLAEAISDHYPVEVTLRKI
//
ID  O42446;
PN  Deoxyribonuclease-1;
GN  dnase1;
OS  8127;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: O42446;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:9395327). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (By similarity). Binds specifically to G-actin and blocks actin polymerization. Preferentially attacks double-stranded DNA and produces oligonucleotides with 5'-phospho and 3'-hydroxy termini (PubMed:9395327). {ECO:0000250|UniProtKB:P21704, ECO:0000269|PubMed:9395327}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0042588;
GO  GO:0004530;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQTYRSRMHLVCSLGLFLTLLHLSNSLLLGAFNIKSFGDTKASNATLMNIITKIVKRYDVILIQEVRDSDLSATQTLMNY
SQ  VNKDSPQYKYIVSEPLGASTYKERYLFLYREALVSVVKSYTYDDGPEETGQDTFSREPFVVMFSSKNTAVRDFTLIPQHT
SQ  SPDLAVRELNALYDVVLDVRARWNTNDIVLLGDFNAGCSYVSGSAWQQIRIFTDKTFHWLITDAADTTVSQTVCPYDRIV
SQ  VTTDMMRGVVQNSAKVYNYMTDLNLKQDLALAVSDHFPVEVKLS
//
ID  P11936;
PN  Deoxyribonuclease-1;
GN  DNASE1;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: P11936;
DR  UNIPROT: Q95KK2;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:3782104). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (PubMed:3782104). Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P49183, ECO:0000269|PubMed:3782104}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0042588;
GO  GO:0003779;
GO  GO:0004530;
GO  GO:0003677;
GO  GO:0006915;
GO  GO:0006308;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRAARLMGALLALAGLLQLALSLRIAAFNIRTFGETKMSNATLSNYIVRILSRYDIALIQEVRDSHLTAVGKLLNELNQD
SQ  DPNNYHHVVSEPLGRSTYKERYLFVFRPDQVSVLDSYLYDDGCEPCGNDTFNREPSVVKFSSPSTQVKEFAIVPLHAAPS
SQ  DAAAEIDSLYDVYLNVRQKWDLEDIMLMGDFNAGCSYVTTSHWSSIRLRESPPFQWLIPDTADTTVSSTHCAYDRIVVAG
SQ  PLLQRAVVPDSAAPFDFQAAFGLSEQTALAISDHYPVEVTLKRA
//
ID  O18998;
PN  Deoxyribonuclease-1;
GN  DNASE1;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: O18998;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:9230129). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (PubMed:9230129). Preferentially attacks double-stranded DNA and produces oligonucleotides with 5'-phospho and 3'-hydroxy termini (PubMed:9230129). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P49183, ECO:0000269|PubMed:9230129}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0042588;
GO  GO:0003779;
GO  GO:0004530;
GO  GO:0006915;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRSEMLTALLTLAVLLQVAGSLKIAAFNIRSFGETKMSNATLTSYIVRILQRYDIALIQEVRDSHLTAVGKLLDKLNEKA
SQ  ADTYRFVASEPLGRRTYKERYLFVYRPDQVSVLDSYYYDDGCEPCGTDTFSREPAVVRFSSPSTKVREFAIVPLHSAPED
SQ  AVAEIDALYDVYLDVQKKWGLQDVMLMGDFNADYSYVTSSQWSSIRLRTNPAFKWLIPDTADTTATSTNCAYDRIVVAGP
SQ  LLQDAVVPNSAAPFNFQAAYGLSNQLAQAISDHYPVEVTLA
//
ID  P21704;
PN  Deoxyribonuclease-1;
GN  Dnase1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: P21704;
DR  UNIPROT: Q5FVU6;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:8428592, PubMed:15796714). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (PubMed:15796714). Among other functions, seems to be involved in cell death by apoptosis (PubMed:8428592, PubMed:15796714). Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P00639, ECO:0000250|UniProtKB:P49183, ECO:0000269|PubMed:15796714, ECO:0000269|PubMed:8428592}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0042588;
GO  GO:0003779;
GO  GO:0004536;
GO  GO:0004530;
GO  GO:0003677;
GO  GO:0006915;
GO  GO:0006308;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRYTGLMGILLTLVNLLQLAATLRIAAFNIRTFGDTKMSNATLSSYIVKILSRYDIAVVQEVRDTHLVAVGKLLDELNRD
SQ  IPDNYRYIISEPLGRKSYKEQYLFVYRPSQVSVLDSYHYDDGCEPCGNDTFSREPAIVKFFSPYTEVREFAIVPLHSAPT
SQ  EAVSEIDALYDVYLDVRQKWGLEDIMFMGDFNAGCSYVTSSQWSSIRLRTSPIFQWLIPDSADTTATSTHCAYDRIVVAG
SQ  ALLQAAVVPSSAVPFDFQAEYRLTNQMAEAISDHYPVEVTLRKT
//
ID  P11937;
PN  Deoxyribonuclease-1;
GN  DNASE1;
OS  9940;
SL  Nucleus Position: SL-0178;
SL  Comments: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
DR  UNIPROT: P11937;
DR  Pfam: PF03372;
DR  PROSITE: PS00919;
DR  PROSITE: PS00918;
DE  Function: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (By similarity). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA. Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P00639, ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P24855, ECO:0000250|UniProtKB:P49183}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0042588;
GO  GO:0003779;
GO  GO:0004530;
GO  GO:0006915;
GO  GO:0000737;
GO  GO:0002283;
GO  GO:0002673;
GO  GO:0070948;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  LKIAAFNIRTFGETKMSNATLSSYIVRILRRYDIALIEQVRDSHLVAVGKLLDDLNQDDPNSYHYVVSEPLGRNSYKERY
SQ  LFVFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSSPSTKVKAFAIVPLHSAPSDAVAEINSLYDVYLDVQQKWDL
SQ  NDIMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVGPSAVPFDFQAAYG
SQ  LSNEMALAISDHYPVEVTLT
//
ID  Q5FWN8;
PN  DnaJ homolog subfamily B member 6-A;
GN  dnajb6;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}.
DR  UNIPROT: Q5FWN8;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Plays an indispensable role in the organization of krt8/krt18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6P5F9; IntAct: EBI-11606853; Score: 0.35
GO  GO:0005634;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVEYYEVLGVQRNASADDIKKAYRRLALKWHPDKNPDNKDEAERRFKEVAEAYEVLSDSKKRDIYDKYGKEGLTNRGGGS
SQ  HFDEAPFQFGFTFRSPDDVFRDFFGGRDPFSFDLFADDPFDDFFGRSRHRANRSRPAGGGGGPFLSTFGGFPAFGPSFSP
SQ  FDSGFSSSFGSFGGHGGHGGFTSFSSSSFGGSEMGNFRSVSTSTKVVNGRRVTTKRIVENGQERVEVEEDGQLKSLTVNG
SQ  KEQLLRLDNK
//
ID  Q5XGU5;
PN  DnaJ homolog subfamily B member 6-B;
GN  dnajb6;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}.
DR  UNIPROT: Q5XGU5;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Plays an indispensable role in the organization of krt8/krt18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVEYYDVLGVQRNSSPDDIKKAYRRLALKWHPDKNPDNKEEAERRFKEVAEAYEVLSDSKKRDIYDKYGKEGLAGGGGGG
SQ  GSHYDVPFQFGFTFRSPDDVFREFFGGRDPFSFDLFAEDPFDDFFGRRGHRGNRSRPGGGSFLSTFGGFPAFGPSFSPFD
SQ  SGFSSSFGSFGGHGGFTSFSSSSFGGSGMGNVRSVSTSTKIVNGRRVTTKRIVENGQERVEVEEDGQLKSLTINGKEQLL
SQ  RLDNK
//
ID  Q5E954;
PN  DnaJ homolog subfamily A member 1;
GN  DNAJA1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5E954;
DR  UNIPROT: Q3SZU2;
DR  Pfam: PF00226;
DR  Pfam: PF01556;
DR  Pfam: PF00684;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51188;
DE  Function: Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0001671;
GO  GO:0051087;
GO  GO:0030544;
GO  GO:0050750;
GO  GO:0046872;
GO  GO:0051082;
GO  GO:0030521;
GO  GO:0030317;
GO  GO:0043066;
GO  GO:0043508;
GO  GO:0043065;
GO  GO:0070585;
GO  GO:0042026;
GO  GO:0051223;
GO  GO:0009408;
GO  GO:0007283;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGG
SQ  FGSPMDIFDMFFGGGGRMQRERRGKNVVHQLTVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQI
SQ  RIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDII
SQ  IVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRL
SQ  IIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
//
ID  Q54ED3;
PN  DnaJ homolog subfamily A member 1 homolog;
GN  dnaja1;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity). {ECO:0000250}.
DR  UNIPROT: Q54ED3;
DR  Pfam: PF00226;
DR  Pfam: PF01556;
DR  Pfam: PF00684;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51188;
DE  Function: Co-chaperone for Hsp70 family members. Plays a role in protein transport into mitochondria and in the regulation of apoptosis via its role as co-chaperone (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0051087;
GO  GO:0030544;
GO  GO:0046872;
GO  GO:0051082;
GO  GO:0042026;
GO  GO:0009408;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVKEKEYYERLGVKPDCTEDELKKAYRKMAVKYHPDKNQGPGKDAAEAKFKDISEAYEVLSDPEKRKMYDSYGSEGMKES
SQ  GFHASSAEDLFSHFFGAGGGGGGFSFGGGGGDDFGGFSFGNMGGMGGMGGMGGGHKKRRKGEDIEHEMNRSLEELYNGKL
SQ  VKISISRDEVCKTCKGSGSNKPGVTTTCPTCNGSRYVFQKKQVGPGMIQQVQTACHTCHGTGEKIKEEDKCKECKGKRVI
SQ  QGKKIVQFQVEKGTRDGERIMLQGQGSEYPGVPPGDVIITIREKPNVNFKRNGDNLIYTKRLKLLDSIAGSQFIINTLDQ
SQ  RKLWVNHEKGDIIKQGDMRYIENEGMPIKGTSRKGKLIIAFDIEYPSNLTNDDIEKLSKILPKAATPSVSKSDCKSVGLS
SQ  KVNFNTNEQSSHGGAGGAYQQHGGAYGHQKQQQQGFNPADFGAQFGGGGPQQAQQCQQQ
//
ID  P31689;
PN  DnaJ homolog subfamily A member 1;
GN  DNAJA1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305|PubMed:10816573}; Lipid- anchor {ECO:0000305|PubMed:10816573}. Cytoplasm {ECO:0000269|PubMed:10816573}. Microsome {ECO:0000250}. Nucleus {ECO:0000269|PubMed:10816573}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10816573}. Mitochondrion {ECO:0000250}. Note=Primarily associated with microsomes. A minor proportion is associated with mitochondria (By similarity). Primarily cytoplasmic. A minor proportion is associated with nuclei. {ECO:0000250}.
DR  UNIPROT: P31689;
DR  UNIPROT: Q5T7Q0;
DR  UNIPROT: Q86TL9;
DR  PDB: 2LO1;
DR  PDB: 2M6Y;
DR  PDB: 6E8M;
DR  Pfam: PF00226;
DR  Pfam: PF01556;
DR  Pfam: PF00684;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51188;
DR  OMIM: 602837;
DR  DisGeNET: 3301;
DE  Function: Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co- chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202). {ECO:0000269|PubMed:10816573, ECO:0000269|PubMed:14752510, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24512202, ECO:0000269|PubMed:9192730}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O95831; IntAct: EBI-16786283; Score: 0.27
DE  Interaction: P00533; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: P05129; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: Q9Y333; IntAct: EBI-348751; Score: 0.00
DE  Interaction: Q13233; IntAct: EBI-361839; Score: 0.00
DE  Interaction: Q99759; IntAct: EBI-362154; Score: 0.00
DE  Interaction: Q00653; IntAct: EBI-362743; Score: 0.00
DE  Interaction: Q99558; IntAct: EBI-362977; Score: 0.00
DE  Interaction: Q04206; IntAct: EBI-363259; Score: 0.00
DE  Interaction: Q13546; IntAct: EBI-363616; Score: 0.00
DE  Interaction: Q9Y572; IntAct: EBI-363772; Score: 0.00
DE  Interaction: Q15750; IntAct: EBI-363982; Score: 0.00
DE  Interaction: Q9NYJ8; IntAct: EBI-364051; Score: 0.00
DE  Interaction: O43318; IntAct: EBI-364144; Score: 0.00
DE  Interaction: P19438; IntAct: EBI-364369; Score: 0.00
DE  Interaction: P20333; IntAct: EBI-364603; Score: 0.00
DE  Interaction: Q15628; IntAct: EBI-364837; Score: 0.00
DE  Interaction: Q13077; IntAct: EBI-364942; Score: 0.00
DE  Interaction: Q12933; IntAct: EBI-365035; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-365134; Score: 0.00
DE  Interaction: A0JLT2; IntAct: EBI-394580; Score: 0.35
DE  Interaction: Q9NX70; IntAct: EBI-394875; Score: 0.35
DE  Interaction: Q8IXH7; IntAct: EBI-733541; Score: 0.00
DE  Interaction: P49703; IntAct: EBI-733840; Score: 0.00
DE  Interaction: P19256; IntAct: EBI-734132; Score: 0.00
DE  Interaction: P30408; IntAct: EBI-736034; Score: 0.00
DE  Interaction: Q9UM11; IntAct: EBI-736796; Score: 0.00
DE  Interaction: Q9NPF4; IntAct: EBI-1062592; Score: 0.00
DE  Interaction: O75365; IntAct: EBI-1068254; Score: 0.00
DE  Interaction: O00422; IntAct: EBI-1076324; Score: 0.00
DE  Interaction: P31930; IntAct: EBI-1078266; Score: 0.00
DE  Interaction: Q9Y2Q3; IntAct: EBI-1081237; Score: 0.00
DE  Interaction: Q92956; IntAct: EBI-1082988; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1083927; Score: 0.00
DE  Interaction: P13569; IntAct: EBI-1171566; Score: 0.64
DE  Interaction: Q9H9G7; IntAct: EBI-2267899; Score: 0.35
DE  Interaction: Q9HCK5; IntAct: EBI-2269711; Score: 0.35
DE  Interaction: P99024; IntAct: EBI-2555184; Score: 0.40
DE  Interaction: P05213; IntAct: EBI-2558640; Score: 0.40
DE  Interaction: Q9Z1B5; IntAct: EBI-2560653; Score: 0.40
DE  Interaction: P83887; IntAct: EBI-2561869; Score: 0.40
DE  Interaction: P68372; IntAct: EBI-2562208; Score: 0.40
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-3050465; Score: 0.35
DE  Interaction: P15822; IntAct: EBI-3930535; Score: 0.37
DE  Interaction: Q13042; IntAct: EBI-3930976; Score: 0.37
DE  Interaction: Q15051; IntAct: EBI-4286917; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-4310841; Score: 0.35
DE  Interaction: Q9Y276; IntAct: EBI-7104167; Score: 0.37
DE  Interaction: P51636; IntAct: EBI-7110722; Score: 0.37
DE  Interaction: P35914; IntAct: EBI-7174982; Score: 0.37
DE  Interaction: O95989; IntAct: EBI-7273627; Score: 0.37
DE  Interaction: Q9GZX7; IntAct: EBI-7553697; Score: 0.50
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: Q8JPQ9; IntAct: EBI-6159460; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-21327757; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q93034; IntAct: EBI-21331078; Score: 0.35
DE  Interaction: Q92769; IntAct: EBI-6597828; Score: 0.35
DE  Interaction: Q9UBN7; IntAct: EBI-6597993; Score: 0.53
DE  Interaction: Q969S8; IntAct: EBI-6598258; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: Q7Z6J6; IntAct: EBI-6911571; Score: 0.35
DE  Interaction: Q15334; IntAct: EBI-6911667; Score: 0.35
DE  Interaction: P35240; IntAct: EBI-6911783; Score: 0.35
DE  Interaction: P21860; IntAct: EBI-8770321; Score: 0.35
DE  Interaction: P34969; IntAct: EBI-9027817; Score: 0.35
DE  Interaction: Q8WW22; IntAct: EBI-9393722; Score: 0.35
DE  Interaction: Q96BE0; IntAct: EBI-9394503; Score: 0.35
DE  Interaction: Q9Y266; IntAct: EBI-9395024; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.53
DE  Interaction: Q16659; IntAct: EBI-12502733; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: Q13043; IntAct: EBI-10049645; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-9996267; Score: 0.35
DE  Interaction: Q6ZMQ8; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: P10398; IntAct: EBI-10101587; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-10103376; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-10103481; Score: 0.53
DE  Interaction: P53671; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-10104226; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770028; Score: 0.35
DE  Interaction: P03179; IntAct: EBI-11721697; Score: 0.35
DE  Interaction: P03220; IntAct: EBI-11722152; Score: 0.35
DE  Interaction: P03225; IntAct: EBI-11722220; Score: 0.35
DE  Interaction: P06463; IntAct: EBI-11724048; Score: 0.35
DE  Interaction: P0CK49; IntAct: EBI-11725356; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: P0CK58; IntAct: EBI-11732874; Score: 0.35
DE  Interaction: P30119; IntAct: EBI-11733103; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: Q2MG95; IntAct: EBI-11733653; Score: 0.35
DE  Interaction: Q69117; IntAct: EBI-11733954; Score: 0.35
DE  Interaction: P05214; IntAct: EBI-10992821; Score: 0.35
DE  Interaction: P35550; IntAct: EBI-11044604; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-11139064; Score: 0.35
DE  Interaction: O75665; IntAct: EBI-11365691; Score: 0.27
DE  Interaction: Q15468; IntAct: EBI-11383475; Score: 0.27
DE  Interaction: Q92834; IntAct: EBI-11394826; Score: 0.27
DE  Interaction: Q9C0F1; IntAct: EBI-11397104; Score: 0.27
DE  Interaction: Q9NXB0; IntAct: EBI-11397893; Score: 0.27
DE  Interaction: Q14CZ7; IntAct: EBI-11426979; Score: 0.35
DE  Interaction: Q9WMX2; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q13509; IntAct: EBI-11897134; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-11897791; Score: 0.57
DE  Interaction: P56945; IntAct: EBI-15099384; Score: 0.35
DE  Interaction: O14829; IntAct: EBI-14024386; Score: 0.35
DE  Interaction: Q9Y2T4; IntAct: EBI-14027932; Score: 0.42
DE  Interaction: Q8IVT5; IntAct: EBI-14035664; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q05322; IntAct: EBI-15481401; Score: 0.35
DE  Interaction: Q9BXB4; IntAct: EBI-21817602; Score: 0.35
DE  Interaction: Q96SU4; IntAct: EBI-21817602; Score: 0.35
DE  Interaction: Q14249; IntAct: EBI-21817602; Score: 0.35
DE  Interaction: O95714; IntAct: EBI-21817602; Score: 0.35
DE  Interaction: P54645; IntAct: EBI-16361875; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16362252; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: Q9H9B4; IntAct: EBI-16799442; Score: 0.27
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: O00429; IntAct: EBI-20305770; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: Q86U44; IntAct: EBI-20594935; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20799058; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q9Y251; IntAct: EBI-21260107; Score: 0.35
DE  Interaction: Q9HC29; IntAct: EBI-21262102; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: P03427; IntAct: EBI-21268420; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21132308; Score: 0.35
DE  Interaction: P49768; IntAct: EBI-21132675; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-21132926; Score: 0.67
DE  Interaction: Q16526; IntAct: EBI-21981854; Score: 0.35
DE  Interaction: O15524; IntAct: EBI-25373793; Score: 0.35
DE  Interaction: Q13163; IntAct: EBI-25374437; Score: 0.35
DE  Interaction: Q13164; IntAct: EBI-25374538; Score: 0.35
DE  Interaction: P41240; IntAct: EBI-25376544; Score: 0.35
DE  Interaction: P46734; IntAct: EBI-25377403; Score: 0.35
DE  Interaction: Q02156; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P19419; IntAct: EBI-25378580; Score: 0.35
DE  Interaction: Q13153; IntAct: EBI-25379067; Score: 0.35
DE  Interaction: Q05513; IntAct: EBI-25380056; Score: 0.35
DE  Interaction: P41743; IntAct: EBI-25380638; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-25383128; Score: 0.35
DE  Interaction: Q13882; IntAct: EBI-25385709; Score: 0.35
DE  Interaction: P15498; IntAct: EBI-25385501; Score: 0.35
DE  Interaction: P36507; IntAct: EBI-25391779; Score: 0.35
DE  Interaction: Q9H1R3; IntAct: EBI-25392649; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-25394264; Score: 0.35
DE  Interaction: P06239; IntAct: EBI-25394571; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P83110; IntAct: EBI-25471693; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25510118; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25510237; Score: 0.35
DE  Interaction: P0DTC8; IntAct: EBI-25510273; Score: 0.35
DE  Interaction: Q96CS3; IntAct: EBI-25770166; Score: 0.35
DE  Interaction: O60260; IntAct: EBI-25879547; Score: 0.56
DE  Interaction: Q6PB30; IntAct: EBI-26354359; Score: 0.35
DE  Interaction: Q9Y5P2; IntAct: EBI-26354638; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-26399642; Score: 0.35
DE  Interaction: Q8TB24; IntAct: EBI-26518569; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574478; Score: 0.35
DE  Interaction: O60303; IntAct: EBI-26582514; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610886; Score: 0.35
DE  Interaction: A0A0H3NJM6; IntAct: EBI-27055978; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: P22612; IntAct: EBI-28934688; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: A4FU01; IntAct: EBI-27113520; Score: 0.35
DE  Interaction: A6NLX3; IntAct: EBI-28997370; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-29628346; Score: 0.35
DE  Interaction: P11362; IntAct: EBI-32718427; Score: 0.42
DE  Interaction: P08069; IntAct: EBI-32718669; Score: 0.35
DE  Interaction: P06213; IntAct: EBI-32718777; Score: 0.35
DE  Interaction: P04629; IntAct: EBI-32719115; Score: 0.42
DE  Interaction: Q16288; IntAct: EBI-32719212; Score: 0.35
DE  Interaction: Q01974; IntAct: EBI-32719482; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-32719716; Score: 0.35
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
GO  GO:0005737;
GO  GO:0098554;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0001671;
GO  GO:0055131;
GO  GO:0051087;
GO  GO:0001664;
GO  GO:0030544;
GO  GO:0050750;
GO  GO:0046872;
GO  GO:0030957;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0030521;
GO  GO:0030317;
GO  GO:0043066;
GO  GO:1903748;
GO  GO:0043508;
GO  GO:1905259;
GO  GO:0031397;
GO  GO:0043065;
GO  GO:0006457;
GO  GO:0070585;
GO  GO:0042026;
GO  GO:0051223;
GO  GO:0009408;
GO  GO:0006986;
GO  GO:0007283;
GO  GO:1901998;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:14752510,};
SQ  MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGG
SQ  FGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQI
SQ  RIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDII
SQ  IVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRL
SQ  IIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
//
ID  P63037;
PN  DnaJ homolog subfamily A member 1;
GN  Dnaja1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity). {ECO:0000250}.
DR  UNIPROT: P63037;
DR  UNIPROT: P54102;
DR  Pfam: PF00226;
DR  Pfam: PF01556;
DR  Pfam: PF00684;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51188;
DE  Function: Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. {ECO:0000250, ECO:0000269|PubMed:14752510}.
DE  Reference Proteome: Yes;
DE  Interaction: P03332; IntAct: EBI-8484283; Score: 0.37
DE  Interaction: P20263; IntAct: EBI-3043810; Score: 0.35
DE  Interaction: Q8BP00; IntAct: EBI-4283417; Score: 0.35
DE  Interaction: Q8CG73; IntAct: EBI-4284701; Score: 0.35
DE  Interaction: O55222; IntAct: EBI-6914965; Score: 0.35
DE  Interaction: Q80Z64; IntAct: EBI-8820601; Score: 0.35
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q15637; IntAct: EBI-11298350; Score: 0.00
DE  Interaction: O54957; IntAct: EBI-12602113; Score: 0.35
DE  Interaction: A0A0F6AZL3; IntAct: EBI-13950507; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-15753536; Score: 0.35
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: Q9EP53; IntAct: EBI-16734894; Score: 0.35
DE  Interaction: Q9EPK7; IntAct: EBI-17171503; Score: 0.35
DE  Interaction: Q83B01; IntAct: EBI-21287663; Score: 0.49
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0001671;
GO  GO:0055131;
GO  GO:0051087;
GO  GO:0001664;
GO  GO:0030544;
GO  GO:0050750;
GO  GO:0046872;
GO  GO:0030957;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0030521;
GO  GO:0030317;
GO  GO:0043066;
GO  GO:1903748;
GO  GO:0043508;
GO  GO:1905259;
GO  GO:0031397;
GO  GO:0043065;
GO  GO:0070585;
GO  GO:0042026;
GO  GO:0051223;
GO  GO:0009408;
GO  GO:0007283;
GO  GO:1901998;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLADSKKRELYDKGGEQAIKEGGAGGG
SQ  FGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQI
SQ  RIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDII
SQ  IVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRL
SQ  IIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
//
ID  Q5NVI9;
PN  DnaJ homolog subfamily A member 1;
GN  DNAJA1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5NVI9;
DR  Pfam: PF00226;
DR  Pfam: PF01556;
DR  Pfam: PF00684;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51188;
DE  Function: Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0001671;
GO  GO:0051087;
GO  GO:0030544;
GO  GO:0046872;
GO  GO:0051082;
GO  GO:0043066;
GO  GO:0043508;
GO  GO:0043065;
GO  GO:0006457;
GO  GO:0070585;
GO  GO:0051223;
GO  GO:0009408;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGG
SQ  FGSPMDIFDMFFGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIR
SQ  IHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIII
SQ  VLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLI
SQ  IEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
//
ID  P63036;
PN  DnaJ homolog subfamily A member 1;
GN  Dnaja1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:10816573}. Microsome {ECO:0000269|PubMed:10816573}. Mitochondrion {ECO:0000269|PubMed:10816573}. Nucleus {ECO:0000269|PubMed:10816573}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria.
DR  UNIPROT: P63036;
DR  UNIPROT: P54102;
DR  Pfam: PF00226;
DR  Pfam: PF01556;
DR  Pfam: PF00684;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51188;
DE  Function: Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone (PubMed:10816573). {ECO:0000250, ECO:0000269|PubMed:10816573, ECO:0000269|PubMed:9605323}.
DE  Reference Proteome: Yes;
DE  Interaction: P06536; IntAct: EBI-1187343; Score: 0.35
DE  Interaction: P54645; IntAct: EBI-16399805; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0001671;
GO  GO:0055131;
GO  GO:0051087;
GO  GO:0001664;
GO  GO:0030544;
GO  GO:0050750;
GO  GO:0046872;
GO  GO:0030957;
GO  GO:0031625;
GO  GO:0051082;
GO  GO:0030521;
GO  GO:0030317;
GO  GO:0043066;
GO  GO:1903748;
GO  GO:0043508;
GO  GO:1905259;
GO  GO:0031397;
GO  GO:0043065;
GO  GO:0070585;
GO  GO:0042026;
GO  GO:0051223;
GO  GO:0009408;
GO  GO:0007283;
GO  GO:1901998;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLADSKKRELYDKGGEQAIKEGGAGGG
SQ  FGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQI
SQ  RIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDII
SQ  IVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRL
SQ  IIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
//
ID  Q0III6;
PN  DnaJ homolog subfamily B member 6;
GN  DNAJB6;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
DR  UNIPROT: Q0III6;
DR  UNIPROT: Q8WN90;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:11896048}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0051087;
GO  GO:0044183;
GO  GO:0051082;
GO  GO:0061077;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDRYGKEGLNGGGGGG
SQ  SHFDSPFEFGFTFRNPEDVFREFFGGRDPFSFDFFEDPFEDFFGHRRGPRGSRSRGTGSFFSTFSGFPSFGGAFPSFDAG
SQ  FSSFGSLGHGGLTAFSSSSAFGGSGMGNYKSISTSTKVVNGRKITTKRIVENGQERVEVEEDGQLKSLTINGKEQLLRLD
SQ  NK
//
ID  Q5F3Z5;
PN  DnaJ homolog subfamily B member 6;
GN  DNAJB6;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
DR  UNIPROT: Q5F3Z5;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0051087;
GO  GO:0044183;
GO  GO:0051082;
GO  GO:0061077;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYYEVLGVQKHASAEDIKKAYRKLALKWHPDKNPENKEEAEQQFKQVAEAYEVLSDAKKRDIYDRFGKEGLINGGGGG
SQ  SHHDNPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGGRRGPRGSRSRAGGSFLSAFGGFPAFGNAFPSFDTG
SQ  FTSFGSLGHGGLTSFSSTSFGGSGMGNFKSVSTSTKIVNGRKITTKRIVENGQERVEVEEDGQLRSLTINGEANEEAFAE
SQ  ECRRRGQHALPFQPTNTRLLKPHKPASSPRYAYHYNSDEVEEQEKSRVASSLETPFYLSGYKEGSKRRKQKQREEQKKKK
SQ  STKGSY
//
ID  O75190;
PN  DnaJ homolog subfamily B member 6;
GN  DNAJB6;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10954706}. Nucleus {ECO:0000269|PubMed:10954706}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22366786}.
DR  UNIPROT: O75190;
DR  UNIPROT: A4D232;
DR  UNIPROT: A8K7D8;
DR  UNIPROT: A8KAG0;
DR  UNIPROT: B4DN73;
DR  UNIPROT: E9PCZ2;
DR  UNIPROT: O95806;
DR  UNIPROT: Q53EN8;
DR  UNIPROT: Q59EF2;
DR  UNIPROT: Q6FIC8;
DR  UNIPROT: Q75MA2;
DR  UNIPROT: Q9UIK6;
DR  PDB: 6U3R;
DR  PDB: 6U3S;
DR  PDB: 7JSQ;
DR  PDB: 7QBY;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  OMIM: 603511;
DR  OMIM: 611332;
DR  DisGeNET: 10049;
DE  Function: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity. {ECO:0000269|PubMed:10954706, ECO:0000269|PubMed:11896048, ECO:0000269|PubMed:20159555, ECO:0000269|PubMed:22366786, ECO:0000269|PubMed:28233300}.
DE  Disease: Muscular dystrophy, limb-girdle, autosomal dominant 1 (LGMDD1) [MIM:603511]: An autosomal dominant myopathy characterized by adult onset of proximal muscle weakness, beginning in the hip girdle region and later progressing to the shoulder girdle region. {ECO:0000269|PubMed:22334415, ECO:0000269|PubMed:22366786}. Note=The disease is caused by variants affecting the gene represented in this entry. There is evidence that LGMDD1 is caused by dysfunction of isoform B (PubMed:22366786). {ECO:0000269|PubMed:22366786}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y5J5; IntAct: EBI-1073616; Score: 0.00
DE  Interaction: Q15714; IntAct: EBI-1082393; Score: 0.00
DE  Interaction: P01241; IntAct: EBI-1084628; Score: 0.00
DE  Interaction: Q9HCU9; IntAct: EBI-1199948; Score: 0.51
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.35
DE  Interaction: P05783; IntAct: EBI-1255173; Score: 0.62
DE  Interaction: P05787; IntAct: EBI-1255584; Score: 0.40
DE  Interaction: P11142; IntAct: EBI-1255642; Score: 0.48
DE  Interaction: Q8AZK7; IntAct: EBI-9632715; Score: 0.53
DE  Interaction: P42336; IntAct: EBI-2116670; Score: 0.00
DE  Interaction: Q8IY92; IntAct: EBI-2371263; Score: 0.35
DE  Interaction: P0DPB6; IntAct: EBI-3941479; Score: 0.37
DE  Interaction: O75923; IntAct: EBI-5357236; Score: 0.45
DE  Interaction: Q13326; IntAct: EBI-5357396; Score: 0.45
DE  Interaction: Q9ULH1; IntAct: EBI-5656165; Score: 0.00
DE  Interaction: Q15327; IntAct: EBI-5656148; Score: 0.00
DE  Interaction: P58340; IntAct: EBI-9360287; Score: 0.57
DE  Interaction: O75155; IntAct: EBI-5656188; Score: 0.00
DE  Interaction: Q15773; IntAct: EBI-9360330; Score: 0.63
DE  Interaction: Q9UKD2; IntAct: EBI-5656239; Score: 0.00
DE  Interaction: Q00872; IntAct: EBI-5656274; Score: 0.00
DE  Interaction: P52179; IntAct: EBI-5656292; Score: 0.00
DE  Interaction: P36871; IntAct: EBI-5656311; Score: 0.00
DE  Interaction: O75563; IntAct: EBI-5656329; Score: 0.00
DE  Interaction: Q7KZ85; IntAct: EBI-5656346; Score: 0.00
DE  Interaction: Q8WZ42; IntAct: EBI-5656363; Score: 0.00
DE  Interaction: Q96CW5; IntAct: EBI-5656400; Score: 0.00
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q9Y468; IntAct: EBI-8833199; Score: 0.53
DE  Interaction: Q13398; IntAct: EBI-8837070; Score: 0.35
DE  Interaction: Q8K2C9; IntAct: EBI-9360309; Score: 0.40
DE  Interaction: Q13200; IntAct: EBI-9360352; Score: 0.40
DE  Interaction: Q9BTE6; IntAct: EBI-9360374; Score: 0.40
DE  Interaction: Q99933; IntAct: EBI-9392988; Score: 0.35
DE  Interaction: O95816; IntAct: EBI-9393030; Score: 0.35
DE  Interaction: O95817; IntAct: EBI-9393075; Score: 0.35
DE  Interaction: O95429; IntAct: EBI-9393134; Score: 0.35
DE  Interaction: Q13451; IntAct: EBI-9393873; Score: 0.35
DE  Interaction: Q96BE0; IntAct: EBI-9394503; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-9395526; Score: 0.35
DE  Interaction: Q9UNE7; IntAct: EBI-9395575; Score: 0.35
DE  Interaction: Q62925; IntAct: EBI-9971410; Score: 0.00
DE  Interaction: Q13404; IntAct: EBI-9971410; Score: 0.00
DE  Interaction: P22314; IntAct: EBI-9971410; Score: 0.00
DE  Interaction: P61088; IntAct: EBI-9971410; Score: 0.00
DE  Interaction: Q9NWT6; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q16659; IntAct: EBI-12502733; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: E9Q2H1; IntAct: EBI-11033563; Score: 0.35
DE  Interaction: Q91YN9; IntAct: EBI-11052510; Score: 0.35
DE  Interaction: P43243; IntAct: EBI-11071398; Score: 0.35
DE  Interaction: O55187; IntAct: EBI-11125708; Score: 0.35
DE  Interaction: P26447; IntAct: EBI-11158347; Score: 0.35
DE  Interaction: Q5JU00; IntAct: EBI-11367780; Score: 0.27
DE  Interaction: Q9UPV0; IntAct: EBI-11379107; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9BW83; IntAct: EBI-12453281; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-11897791; Score: 0.53
DE  Interaction: P03452; IntAct: EBI-12577240; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-12579142; Score: 0.35
DE  Interaction: P03428; IntAct: EBI-12579909; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581764; Score: 0.35
DE  Interaction: Q5EP37; IntAct: EBI-12582596; Score: 0.35
DE  Interaction: C5E527; IntAct: EBI-12585514; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12588098; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12588729; Score: 0.35
DE  Interaction: O75190; IntAct: EBI-12593128; Score: 0.40
DE  Interaction: Q9BY84; IntAct: EBI-14027455; Score: 0.35
DE  Interaction: Q8N5I9; IntAct: EBI-21859350; Score: 0.35
DE  Interaction: P25686; IntAct: EBI-21859350; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: Q86U44; IntAct: EBI-20594935; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20799058; Score: 0.35
DE  Interaction: Q8TED1; IntAct: EBI-20902320; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P54253; IntAct: EBI-21132804; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-25945964; Score: 0.56
DE  Interaction: Q5S007; IntAct: EBI-22228108; Score: 0.40
DE  Interaction: Q5JSP0; IntAct: EBI-25409226; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: O95072; IntAct: EBI-25483697; Score: 0.35
DE  Interaction: Q9IK92; IntAct: EBI-25747216; Score: 0.35
DE  Interaction: O43572; IntAct: EBI-26451580; Score: 0.35
DE  Interaction: P15313; IntAct: EBI-25909736; Score: 0.56
DE  Interaction: O94778; IntAct: EBI-25909728; Score: 0.56
DE  Interaction: P09525; IntAct: EBI-25909720; Score: 0.56
DE  Interaction: Q9NP70; IntAct: EBI-25909712; Score: 0.56
DE  Interaction: P54687; IntAct: EBI-25909745; Score: 0.56
DE  Interaction: Q8TD91; IntAct: EBI-25910153; Score: 0.56
DE  Interaction: P06276; IntAct: EBI-25909753; Score: 0.56
DE  Interaction: Q96QF0; IntAct: EBI-25910137; Score: 0.56
DE  Interaction: Q96CS2; IntAct: EBI-25910129; Score: 0.56
DE  Interaction: Q9UII2; IntAct: EBI-25910121; Score: 0.56
DE  Interaction: Q9Y605; IntAct: EBI-25910113; Score: 0.56
DE  Interaction: Q86TI2; IntAct: EBI-25910103; Score: 0.56
DE  Interaction: Q8WTV1; IntAct: EBI-25910095; Score: 0.56
DE  Interaction: Q8NHS9; IntAct: EBI-25910087; Score: 0.56
DE  Interaction: Q9BRX9; IntAct: EBI-25910079; Score: 0.56
DE  Interaction: Q96JB6; IntAct: EBI-25910069; Score: 0.56
DE  Interaction: Q9BQS8; IntAct: EBI-25910059; Score: 0.56
DE  Interaction: Q9BRX5; IntAct: EBI-25910051; Score: 0.56
DE  Interaction: Q9H270; IntAct: EBI-25910033; Score: 0.56
DE  Interaction: Q96LR2; IntAct: EBI-25910025; Score: 0.56
DE  Interaction: Q96FW1; IntAct: EBI-25910017; Score: 0.56
DE  Interaction: Q96EN9; IntAct: EBI-25910001; Score: 0.56
DE  Interaction: Q9BUL9; IntAct: EBI-25909993; Score: 0.56
DE  Interaction: Q9BY12; IntAct: EBI-25909975; Score: 0.56
DE  Interaction: Q9NNX6; IntAct: EBI-25909967; Score: 0.56
DE  Interaction: Q9H0W9; IntAct: EBI-25909959; Score: 0.56
DE  Interaction: Q9UBP4; IntAct: EBI-25909951; Score: 0.56
DE  Interaction: Q9UH77; IntAct: EBI-25909941; Score: 0.56
DE  Interaction: Q6PID6; IntAct: EBI-25909933; Score: 0.56
DE  Interaction: Q96H20; IntAct: EBI-25909925; Score: 0.56
DE  Interaction: Q99871; IntAct: EBI-25909915; Score: 0.56
DE  Interaction: Q8IXS7; IntAct: EBI-25909907; Score: 0.56
DE  Interaction: Q9UJX2; IntAct: EBI-25909897; Score: 0.56
DE  Interaction: Q14457; IntAct: EBI-25909889; Score: 0.56
DE  Interaction: O75558; IntAct: EBI-25909881; Score: 0.56
DE  Interaction: O15273; IntAct: EBI-25909873; Score: 0.56
DE  Interaction: Q99598; IntAct: EBI-25909865; Score: 0.56
DE  Interaction: Q12888; IntAct: EBI-25909857; Score: 0.56
DE  Interaction: Q15293; IntAct: EBI-25909849; Score: 0.56
DE  Interaction: P30154; IntAct: EBI-25909841; Score: 0.56
DE  Interaction: I6L9F6; IntAct: EBI-25909833; Score: 0.56
DE  Interaction: Q13123; IntAct: EBI-25909817; Score: 0.56
DE  Interaction: P80217; IntAct: EBI-25909809; Score: 0.56
DE  Interaction: H3BUJ7; IntAct: EBI-25909801; Score: 0.56
DE  Interaction: A0A024RCP2; IntAct: EBI-25909793; Score: 0.56
DE  Interaction: P53672; IntAct: EBI-25909785; Score: 0.56
DE  Interaction: P24310; IntAct: EBI-25909777; Score: 0.56
DE  Interaction: Q13191; IntAct: EBI-25909769; Score: 0.56
DE  Interaction: Q13887; IntAct: EBI-25909761; Score: 0.56
DE  Interaction: Q6XD76; IntAct: EBI-25910145; Score: 0.56
DE  Interaction: Q6ZTN6; IntAct: EBI-25910219; Score: 0.56
DE  Interaction: Q494V2; IntAct: EBI-25910227; Score: 0.56
DE  Interaction: Q8NBB4; IntAct: EBI-25910203; Score: 0.56
DE  Interaction: Q6PJW8; IntAct: EBI-25910195; Score: 0.56
DE  Interaction: Q8N6F8; IntAct: EBI-25910187; Score: 0.56
DE  Interaction: Q8NA54; IntAct: EBI-25910179; Score: 0.56
DE  Interaction: Q6P1L5; IntAct: EBI-25910169; Score: 0.56
DE  Interaction: Q6P597; IntAct: EBI-25910161; Score: 0.56
DE  Interaction: Q6NXT2; IntAct: EBI-25910261; Score: 0.56
DE  Interaction: Q3KNS6; IntAct: EBI-25910243; Score: 0.56
DE  Interaction: Q7Z6I5; IntAct: EBI-25910235; Score: 0.56
DE  Interaction: Q8IV33; IntAct: EBI-25910211; Score: 0.56
DE  Interaction: P48431; IntAct: EBI-26574478; Score: 0.35
DE  Interaction: O60303; IntAct: EBI-26582514; Score: 0.35
DE  Interaction: Q9Y224; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-28931531; Score: 0.35
DE  Interaction: P22612; IntAct: EBI-28934688; Score: 0.35
DE  Interaction: P80192; IntAct: EBI-28938802; Score: 0.35
DE  Interaction: Q8IY84; IntAct: EBI-28942464; Score: 0.35
DE  Interaction: Q8IWB6; IntAct: EBI-28942423; Score: 0.35
DE  Interaction: Q8NFD2; IntAct: EBI-28943481; Score: 0.35
DE  Interaction: Q96D53; IntAct: EBI-28944341; Score: 0.35
DE  Interaction: Q99558; IntAct: EBI-28944828; Score: 0.35
DE  Interaction: Q9NR20; IntAct: EBI-28946409; Score: 0.35
DE  Interaction: Q9NSY0; IntAct: EBI-28946547; Score: 0.35
DE  Interaction: Q9UGI9; IntAct: EBI-28946731; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q05DH4; IntAct: EBI-34574576; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0001671;
GO  GO:0051087;
GO  GO:0003677;
GO  GO:0031072;
GO  GO:0042802;
GO  GO:0044183;
GO  GO:0051082;
GO  GO:0030036;
GO  GO:0061077;
GO  GO:0060710;
GO  GO:0060717;
GO  GO:0030198;
GO  GO:0045109;
GO  GO:0043154;
GO  GO:0045892;
GO  GO:0090084;
GO  GO:0006457;
GO  GO:0034504;
GO  GO:1900034;
GO  GO:0032880;
GO  GO:0060715;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGG
SQ  SHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFGSGFSSFDTG
SQ  FTSFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKMVNGRKITTKRIVENGQERVEVEEDGQLKSLTINGVADDDALAE
SQ  ERMRRGQNALPAQPAGLRPPKPPRPASLLRHAPHCLSEEEGEQDRPRAPGPWDPLASAAGLKEGGKRKKQKQREESKKKK
SQ  STKGNH
//
ID  Q4R7Y5;
PN  DnaJ homolog subfamily B member 6;
GN  DNAJB6;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
DR  UNIPROT: Q4R7Y5;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030018;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGG
SQ  SHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFEFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFGSGFSSFDTG
SQ  FTSFGSLGHGGLTSFSSTSFGGGGMGNFKSISTSTKMVNGRKITTKRIVENGQERVEVEEDGQLKSLTINGKEQLLRLDN
SQ  K
//
ID  O54946;
PN  DnaJ homolog subfamily B member 6;
GN  Dnajb6;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
DR  UNIPROT: O54946;
DR  UNIPROT: Q3TE94;
DR  UNIPROT: Q3U6L0;
DR  UNIPROT: Q3UNJ5;
DR  UNIPROT: Q3UYT7;
DR  UNIPROT: Q99LA5;
DR  UNIPROT: Q9QYI9;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8BWG8; IntAct: EBI-649852; Score: 0.37
DE  Interaction: Q8CG73; IntAct: EBI-4284701; Score: 0.35
DE  Interaction: Q13686; IntAct: EBI-13941029; Score: 0.37
DE  Interaction: P0CB42; IntAct: EBI-13941082; Score: 0.40
DE  Interaction: P56524; IntAct: EBI-13941106; Score: 0.40
DE  Interaction: Q6P1J9; IntAct: EBI-20729673; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0001671;
GO  GO:0051087;
GO  GO:0003677;
GO  GO:0031072;
GO  GO:0042802;
GO  GO:0044183;
GO  GO:0051082;
GO  GO:0030036;
GO  GO:0061077;
GO  GO:0060710;
GO  GO:0060717;
GO  GO:0030198;
GO  GO:0045109;
GO  GO:0043154;
GO  GO:0045892;
GO  GO:0090084;
GO  GO:0006457;
GO  GO:0034504;
GO  GO:0032880;
GO  GO:0060715;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGG
SQ  GIHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGNRSRGAGSFFSTFSGFPSFGSGFPAFDT
SQ  GFTPFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALA
SQ  EECQRRGQPTPALAPGPAPAPVRVPSQARPLAPTPAPTPAPTPAPAPAQTPAPSVSTRPQKPPRPAPTAKLGSKSNWEDD
SQ  EQDRQRVPGNWDAPMTSAGLKEGGKRKKQKQKEDLKKKKSTKGNH
//
ID  Q5R8H0;
PN  DnaJ homolog subfamily B member 6;
GN  DNAJB6;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
DR  UNIPROT: Q5R8H0;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030018;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGG
SQ  SHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFGSGFSSFDTG
SQ  FTSFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKMVNGRKITTKRIVENGQERVEVGEDGQLKSLTINGVADDDALAE
SQ  ERMRRGQNALPAQPAGLRPPKPPRPASLLRHAPHCLSEEEGEQDRPRAPGPWDPLASAAGLKEGGKRKKQKQREESKKKK
SQ  STKGNH
//
ID  Q6AYU3;
PN  DnaJ homolog subfamily B member 6;
GN  Dnajb6;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
DR  UNIPROT: Q6AYU3;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9EPX0; IntAct: EBI-12593062; Score: 0.27
DE  Interaction: Q5U2U8; IntAct: EBI-12593066; Score: 0.27
DE  Interaction: D4A4T0; IntAct: EBI-12593095; Score: 0.27
DE  Interaction: P63018; IntAct: EBI-12593099; Score: 0.27
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0001671;
GO  GO:0051087;
GO  GO:0003677;
GO  GO:0031072;
GO  GO:0044183;
GO  GO:0051082;
GO  GO:0030036;
GO  GO:0061077;
GO  GO:0060710;
GO  GO:0060717;
GO  GO:0030198;
GO  GO:0045109;
GO  GO:0043154;
GO  GO:0045892;
GO  GO:0090084;
GO  GO:0006457;
GO  GO:0034504;
GO  GO:0032880;
GO  GO:0060715;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGG
SQ  GSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGSRSRGAGSFFSAFSGFPSFGSGFPAFDT
SQ  GFTPFGSLGHGGLTSFSSASFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALA
SQ  EECRRRGQPTPALAPGPAPAPARVPSQARPPTPAPTPAPAQTPAPSVSTRPQKPPRPAPTAKLVSKSNWEDEEQDRQRVP
SQ  GNCDAPMTSAGLKEGGKRKKQKQKEDSKKKKSTKGNH
//
ID  Q6P642;
PN  DnaJ homolog subfamily B member 6;
GN  dnajb6;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}.
DR  UNIPROT: Q6P642;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Plays an indispensable role in the organization of krt8/krt18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051087;
GO  GO:0044183;
GO  GO:0051082;
GO  GO:0061077;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVEYYDVLGVQRNASPEDIKKAYRKLALKWHPDKNPDNKDEAERRFKEVAEAYEVLSDSKKRDIYDKYGKEGLTGGGGGS
SQ  HFDNPYEFGFTFRSPDDVFRDFFGGRDPFSFDLFADDPFDDFFGRRGHRANRSRPGGSFLSTFGGFPAFGPTFSPFDSGF
SQ  SSSFGSFGGHGGFSSFSSSSFGGSGMGNFRSVSTSTKVVNGRRVTTKRIVENGQERIEVEEDGQLKSLTINGKEQLLRLD
SQ  NK
//
ID  P82539;
PN  DnaJ homolog subfamily C member 1;
GN  DNAJC1;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12065409}; Single-pass type I membrane protein {ECO:0000269|PubMed:12065409}. Nucleus membrane {ECO:0000250}; Single- pass type I membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
DR  UNIPROT: P82539;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  WESGDLELFDLVEEVXLNFY
//
ID  Q96KC8;
PN  DnaJ homolog subfamily C member 1;
GN  DNAJC1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane; Single-pass type I membrane protein. Microsome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
DR  UNIPROT: Q96KC8;
DR  UNIPROT: B0YIZ8;
DR  UNIPROT: Q5VX89;
DR  UNIPROT: Q9H6B8;
DR  PDB: 2CQQ;
DR  PDB: 2CQR;
DR  Pfam: PF00226;
DR  Pfam: PF00249;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51293;
DR  OMIM: 611207;
DR  DisGeNET: 64215;
DE  Function: May modulate protein synthesis. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P03246; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P0C6X7; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q5SNT2; IntAct: EBI-24662993; Score: 0.56
DE  Interaction: P80294; IntAct: EBI-296562; Score: 0.37
DE  Interaction: P01011; IntAct: EBI-296913; Score: 0.58
DE  Interaction: O95870; IntAct: EBI-348775; Score: 0.00
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q04941; IntAct: EBI-24673775; Score: 0.56
DE  Interaction: P78329; IntAct: EBI-24723472; Score: 0.56
DE  Interaction: P27449; IntAct: EBI-24645899; Score: 0.56
DE  Interaction: Q96FZ5; IntAct: EBI-25186763; Score: 0.56
DE  Interaction: Q6RW13; IntAct: EBI-24762587; Score: 0.56
DE  Interaction: O14798; IntAct: EBI-24762712; Score: 0.56
DE  Interaction: Q13296; IntAct: EBI-21513670; Score: 0.35
DE  Interaction: Q9UHP7; IntAct: EBI-21517465; Score: 0.35
DE  Interaction: P58658; IntAct: EBI-21588759; Score: 0.35
DE  Interaction: Q15884; IntAct: EBI-21620222; Score: 0.35
DE  Interaction: P15498; IntAct: EBI-21631629; Score: 0.35
DE  Interaction: Q5QGZ9; IntAct: EBI-21633112; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-21650356; Score: 0.35
DE  Interaction: Q8NBR6; IntAct: EBI-21714170; Score: 0.35
DE  Interaction: Q9NWS8; IntAct: EBI-21842948; Score: 0.35
DE  Interaction: P31146; IntAct: EBI-21842948; Score: 0.35
DE  Interaction: P10321; IntAct: EBI-21842948; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q14409; IntAct: EBI-20900375; Score: 0.40
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P13473; IntAct: EBI-25873928; Score: 0.56
DE  Interaction: Q9Y371; IntAct: EBI-25922422; Score: 0.56
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0001671;
GO  GO:0051087;
GO  GO:0003677;
GO  GO:0045861;
GO  GO:0006457;
GO  GO:0050708;
GO  GO:0006417;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTAPCSQPAQLPGRRQLGLVPFPPPPPRTPLLWLLLLLLAAVAPARGWESGDLELFDLVEEVQLNFYQFLGVQQDASSAD
SQ  IRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDILINGLPDWRQPVFYYRRVRKMSNAELALLLFI
SQ  ILTVGHYAVVWSIYLEKQLDELLSRKKREKKKKTGSKSVDVSKLGASEKNERLLMKPQWHDLLPCKLGIWFCLTLKALPH
SQ  LIQDAGQFYAKYKETRLKEKEDALTRTELETLQKQKKVKKPKPEFPVYTPLETTYIQSYDHGTSIEEIEEQMDDWLENRN
SQ  RTQKKQAPEWTEEDLSQLTRSMVKFPGGTPGRWEKIAHELGRSVTDVTTKAKQLKDSVTCSPGMVRLSELKSTVQNSRPI
SQ  KTATTLPDDMITQREDAEGVAAEEEQEGDSGEQETGATDARPRRRKPARLLEATAKPEPEEKSRAKRQKDFDIAEQNESS
SQ  DEESLRKERARSAEEPWTQNQQKLLELALQQYPRGSSDRWDKIARCVPSKSKEDCIARYKLLVELVQKKKQAKS
//
ID  Q61712;
PN  DnaJ homolog subfamily C member 1;
GN  Dnajc1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Microsome membrane; Single-pass type I membrane protein.
DR  UNIPROT: Q61712;
DR  Pfam: PF00226;
DR  Pfam: PF00249;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51293;
DE  Function: May modulate protein synthesis. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P70168; IntAct: EBI-15558601; Score: 0.44
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0051087;
GO  GO:0003677;
GO  GO:0043022;
GO  GO:0006457;
GO  GO:0050708;
GO  GO:0006417;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MWVPGFGSARLPQRRRSGLESSSVRPLWLLLLFLLAAVRPVRAWESGDLELFDLVEEVQLNFYEFLGVQQDASSADIRKA
SQ  YRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDVLINGLPDWRQPVFYYRRVRKMSNAELALLLFIILTV
SQ  GHYAVVWSIYLEKQLDELLGRKKRERKKKTGSKSVDAAKLGASEKNERLLIKPQWHDLLPCKLGIWFCLTLKALPHLIQD
SQ  AGQFYAKYKETKLKEKEDALARIEIETLQKQKKVKVKKPKPEFPVYMPLENTYIQSYDHGTSIEEIEEQMDDWLENRKRT
SQ  QKRQAPEWTEEDLSQLTRSMVKFPGGTPGRWDKIAHELGRSVTDVTTKAKELKDSVTSSPGMTRLSELKSNGQNSRPIKI
SQ  ATALPDDIITQREDSAGAMEDEEHEAAEGEQESATTEARPRRRKSARAAEAVTRVEPEEKLRGKRQKDFDISEQNDSSDE
SQ  EKQRKERTRAAEEAWTQSQQKLLELALQQYPKGASDRWDKIAKCVPSKSKEDCIARYKLLVELVQKKKQAKS
//
ID  P40318;
PN  ERAD-associated E3 ubiquitin-protein ligase DOA10;
GN  SSM4;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:17051211}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:17051211}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: P40318;
DR  UNIPROT: D6VVQ1;
DR  PDB: 2M6M;
DR  Pfam: PF12906;
DR  PROSITE: PS51292;
DE  Function: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Mediates the degradation of a broad range of substrates, including endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC) (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains (PubMed:16873066). ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1 (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Also recognizes the N-terminally acetylated residue of proteins as degradation signal (degron) (PubMed:20110468). N-terminally acetylated target proteins include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8 (PubMed:20110468). Catalyzes ubiquitination of mislocalized tail-anchored proteins that are extracted from the mitochondrion membrane by MSP1: following extraction, mistargeted proteins are transferred to the endoplasmic reticulum, where they are ubiquitinated by DOA10 and degraded by the proteasome (PubMed:31445887). {ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:16179952, ECO:0000269|PubMed:16437165, ECO:0000269|PubMed:16873066, ECO:0000269|PubMed:17051211, ECO:0000269|PubMed:18812321, ECO:0000269|PubMed:20110468, ECO:0000269|PubMed:31445887}.
DE  Reference Proteome: Yes;
DE  Interaction: P39015; IntAct: EBI-939185; Score: 0.44
DE  Interaction: Q04121; IntAct: EBI-7756909; Score: 0.37
DE  Interaction: P47137; IntAct: EBI-939093; Score: 0.44
DE  Interaction: P40513; IntAct: EBI-939098; Score: 0.44
DE  Interaction: P06738; IntAct: EBI-939105; Score: 0.44
DE  Interaction: Q12007; IntAct: EBI-939110; Score: 0.44
DE  Interaction: P38758; IntAct: EBI-939115; Score: 0.44
DE  Interaction: P39683; IntAct: EBI-939120; Score: 0.44
DE  Interaction: P16467; IntAct: EBI-939125; Score: 0.44
DE  Interaction: P11154; IntAct: EBI-939130; Score: 0.44
DE  Interaction: P33399; IntAct: EBI-939135; Score: 0.44
DE  Interaction: P25617; IntAct: EBI-939140; Score: 0.44
DE  Interaction: P32288; IntAct: EBI-939145; Score: 0.44
DE  Interaction: P53982; IntAct: EBI-939150; Score: 0.44
DE  Interaction: P10963; IntAct: EBI-939155; Score: 0.44
DE  Interaction: P00925; IntAct: EBI-939160; Score: 0.44
DE  Interaction: P40825; IntAct: EBI-939165; Score: 0.44
DE  Interaction: P30952; IntAct: EBI-939170; Score: 0.44
DE  Interaction: Q04697; IntAct: EBI-939175; Score: 0.44
DE  Interaction: P32835; IntAct: EBI-939180; Score: 0.44
DE  Interaction: P23542; IntAct: EBI-939190; Score: 0.44
DE  Interaction: P38998; IntAct: EBI-939195; Score: 0.44
DE  Interaction: P38720; IntAct: EBI-939200; Score: 0.44
DE  Interaction: P35202; IntAct: EBI-939205; Score: 0.44
DE  Interaction: P80210; IntAct: EBI-939210; Score: 0.44
DE  Interaction: P40217; IntAct: EBI-939215; Score: 0.44
DE  Interaction: P38009; IntAct: EBI-939220; Score: 0.44
DE  Interaction: Q04458; IntAct: EBI-939225; Score: 0.44
DE  Interaction: P40959; IntAct: EBI-939230; Score: 0.44
DE  Interaction: Q05979; IntAct: EBI-939235; Score: 0.44
DE  Interaction: P40892; IntAct: EBI-939240; Score: 0.44
DE  Interaction: P08524; IntAct: EBI-939245; Score: 0.44
DE  Interaction: P25561; IntAct: EBI-939250; Score: 0.44
DE  Interaction: P38787; IntAct: EBI-939255; Score: 0.44
DE  Interaction: P46655; IntAct: EBI-939260; Score: 0.44
DE  Interaction: P38158; IntAct: EBI-939265; Score: 0.44
DE  Interaction: P38081; IntAct: EBI-939270; Score: 0.44
DE  Interaction: Q01454; IntAct: EBI-939275; Score: 0.44
DE  Interaction: Q08968; IntAct: EBI-939280; Score: 0.44
DE  Interaction: P41816; IntAct: EBI-939285; Score: 0.44
DE  Interaction: P46151; IntAct: EBI-939290; Score: 0.44
DE  Interaction: P54885; IntAct: EBI-939295; Score: 0.44
DE  Interaction: Q08686; IntAct: EBI-939300; Score: 0.44
DE  Interaction: Q08444; IntAct: EBI-939305; Score: 0.44
DE  Interaction: P50278; IntAct: EBI-939310; Score: 0.44
DE  Interaction: P37254; IntAct: EBI-939315; Score: 0.44
DE  Interaction: Q10740; IntAct: EBI-939320; Score: 0.44
DE  Interaction: P50101; IntAct: EBI-939325; Score: 0.44
DE  Interaction: P00331; IntAct: EBI-939330; Score: 0.44
DE  Interaction: P16862; IntAct: EBI-939335; Score: 0.44
DE  Interaction: P46680; IntAct: EBI-939340; Score: 0.44
DE  Interaction: Q04212; IntAct: EBI-939345; Score: 0.44
DE  Interaction: P15274; IntAct: EBI-939350; Score: 0.44
DE  Interaction: P54007; IntAct: EBI-939355; Score: 0.44
DE  Interaction: Q99260; IntAct: EBI-939360; Score: 0.44
DE  Interaction: Q04491; IntAct: EBI-939365; Score: 0.44
DE  Interaction: P31539; IntAct: EBI-939370; Score: 0.44
DE  Interaction: P10592; IntAct: EBI-939375; Score: 0.44
DE  Interaction: P41903; IntAct: EBI-939380; Score: 0.44
DE  Interaction: P38716; IntAct: EBI-939385; Score: 0.44
DE  Interaction: P17076; IntAct: EBI-939390; Score: 0.44
DE  Interaction: P53051; IntAct: EBI-939395; Score: 0.44
DE  Interaction: P53265; IntAct: EBI-939400; Score: 0.44
DE  Interaction: P53101; IntAct: EBI-939405; Score: 0.44
DE  Interaction: P53183; IntAct: EBI-939410; Score: 0.44
DE  Interaction: P10356; IntAct: EBI-939415; Score: 0.44
DE  Interaction: P21524; IntAct: EBI-939420; Score: 0.44
DE  Interaction: P25044; IntAct: EBI-939425; Score: 0.44
DE  Interaction: Q07505; IntAct: EBI-939430; Score: 0.44
DE  Interaction: P16120; IntAct: EBI-939435; Score: 0.44
DE  Interaction: P25576; IntAct: EBI-939440; Score: 0.44
DE  Interaction: P17967; IntAct: EBI-939445; Score: 0.44
DE  Interaction: P00817; IntAct: EBI-939450; Score: 0.44
DE  Interaction: Q04228; IntAct: EBI-982121; Score: 0.71
DE  Interaction: P38428; IntAct: EBI-982234; Score: 0.56
DE  Interaction: P38911; IntAct: EBI-982234; Score: 0.35
DE  Interaction: P25694; IntAct: EBI-982234; Score: 0.71
DE  Interaction: P33296; IntAct: EBI-1102319; Score: 0.40
DE  Interaction: Q02159; IntAct: EBI-1102333; Score: 0.40
DE  Interaction: P53044; IntAct: EBI-1008654; Score: 0.46
DE  Interaction: P12866; IntAct: EBI-1637277; Score: 0.64
DE  Interaction: P32589; IntAct: EBI-3807868; Score: 0.35
DE  Interaction: P38360; IntAct: EBI-15787591; Score: 0.40
DE  Interaction: P53756; IntAct: EBI-20814404; Score: 0.37
GO  GO:0000837;
GO  GO:0005783;
GO  GO:0030176;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0008270;
GO  GO:0071712;
GO  GO:0030970;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVDSDVNVSRLRDELHKVANEETDTATFNDDAPSGATCRICRGEATEDNPLFHPCKCRGSIKYMHESCLLEWVASKNID
SQ  ISKPGADVKCDICHYPIQFKTIYAENMPEKIPFSLLLSKSILTFFEKARLALTIGLAAVLYIIGVPLVWNMFGKLYTMML
SQ  DGSSPYPGDFLKSLIYGYDQSATPELTTRAIFYQLLQNHSFTSLQFIMIVILHIALYFQYDMIVREDVFSKMVFHKIGPR
SQ  LSPKDLKSRLKERFPMMDDRMVEYLAREMRAHDENRQEQGHDRLNMPAAAADNNNNVINPRNDNVPPQDPNDHRNFENLR
SQ  HVDELDHDEATEEHENNDSDNSLPSGDDSSRILPGSSSDNEEDEEAEGQQQQQQPEEEADYRDHIEPNPIDMWANRRAQN
SQ  EFDDLIAAQQNAINRPNAPVFIPPPAQNRAGNVDQDEQDFGAAVGVPPAQANPDDQGQGPLVINLKLKLLNVIAYFIIAV
SQ  VFTAIYLAISYLFPTFIGFGLLKIYFGIFKVILRGLCHLYYLSGAHIAYNGLTKLVPKVDVAMSWISDHLIHDIIYLYNG
SQ  YTENTMKHSIFIRALPALTTYLTSVSIVCASSNLVSRGYGRENGMSNPTRRLIFQILFALKCTFKVFTLFFIELAGFPIL
SQ  AGVMLDFSLFCPILASNSRMLWVPSICAIWPPFSLFVYWTIGTLYMYWFAKYIGMIRKNIIRPGVLFFIRSPEDPNIKIL
SQ  HDSLIHPMSIQLSRLCLSMFIYAIFIVLGFGFHTRIFFPFMLKSNLLSVPEAYKPTSIISWKFNTILLTLYFTKRILESS
SQ  SYVKPLLERYWKTIFKLCSRKLRLSSFILGKDTPTERGHIVYRNLFYKYIAAKNAEWSNQELFTKPKTLEQAEELFGQVR
SQ  DVHAYFVPDGVLMRVPSSDIVSRNYVQTMFVPVTKDDKLLKPLDLERIKERNKRAAGEFGYLDEQNTEYDQYYIVYVPPD
SQ  FRLRYMTLLGLVWLFASILMLGVTFISQALINFVCSFGFLPVVKLLLGERNKVYVAWKELSDISYSYLNIYYVCVGSVCL
SQ  SKIAKDILHFTEGQNTLDEHAVDENEVEEVEHDIPERDINNAPVNNINNVEEGQGIFMAIFNSIFDSMLVKYNLMVFIAI
SQ  MIAVIRTMVSWVVLTDGILACYNYLTIRVFGNSSYTIGNSKWFKYDESLLFVVWIISSMVNFGTGYKSLKLFFRNRNTSK
SQ  LNFLKTMALELFKQGFLHMVIYVLPIIILSLVFLRDVSTKQIIDISHGSRSFTLSLNESFPTWTRMQDIYFGLLIALESF
SQ  TFFFQATVLFIQWFKSTVQNVKDEVYTKGRALENLPDES
//
ID  Q96HP0;
PN  Dedicator of cytokinesis protein 6;
GN  DOCK6;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17196961}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17196961}. Note=Mainly located near the cell surface.
DR  UNIPROT: Q96HP0;
DR  UNIPROT: A6H8X5;
DR  UNIPROT: Q7Z7P4;
DR  UNIPROT: Q9P2F2;
DR  Pfam: PF06920;
DR  Pfam: PF14429;
DR  Pfam: PF11878;
DR  PROSITE: PS51650;
DR  PROSITE: PS51651;
DR  OMIM: 614194;
DR  OMIM: 614219;
DR  DisGeNET: 57572;
DE  Function: Acts as guanine nucleotide exchange factor (GEF) for CDC42 and RAC1 small GTPases. Through its activation of CDC42 and RAC1, may regulate neurite outgrowth (By similarity). {ECO:0000250, ECO:0000269|PubMed:17196961}.
DE  Disease: Adams-Oliver syndrome 2 (AOS2) [MIM:614219]: A disorder characterized by the congenital absence of skin (aplasia cutis congenita) in combination with transverse limb defects. Aplasia cutis congenita can be located anywhere on the body, but in the vast majority of the cases, it is present on the posterior parietal region where it is often associated with an underlying defect of the parietal bones. Limb abnormalities are typically limb truncation defects affecting the distal phalanges or entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal limb structures are also affected. Apart from transverse limb defects, syndactyly, most commonly of second and third toes, can also be observed. The clinical features are highly variable and can also include cardiovascular malformations, brain abnormalities and vascular defects such as cutis marmorata and dilated scalp veins. {ECO:0000269|PubMed:21820096}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95271; IntAct: EBI-30838480; Score: 0.44
DE  Interaction: P0DTD1; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: P10909; IntAct: EBI-11117520; Score: 0.35
DE  Interaction: Q8IUI8; IntAct: EBI-8795913; Score: 0.35
DE  Interaction: Q8NF50; IntAct: EBI-8795967; Score: 0.53
DE  Interaction: Q96II8; IntAct: EBI-8796001; Score: 0.53
DE  Interaction: Q9H8S9; IntAct: EBI-8796143; Score: 0.42
DE  Interaction: Q7L9L4; IntAct: EBI-8796201; Score: 0.42
DE  Interaction: Q96N67; IntAct: EBI-8797541; Score: 0.35
DE  Interaction: Q6P5D4; IntAct: EBI-10991106; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: P13533; IntAct: EBI-11004546; Score: 0.35
DE  Interaction: P26041; IntAct: EBI-11010611; Score: 0.35
DE  Interaction: Q8BUN5; IntAct: EBI-11016066; Score: 0.35
DE  Interaction: Q2M1P5; IntAct: EBI-11100577; Score: 0.35
DE  Interaction: O75792; IntAct: EBI-11115131; Score: 0.35
DE  Interaction: Q13637; IntAct: EBI-11116348; Score: 0.35
DE  Interaction: Q14114; IntAct: EBI-11117560; Score: 0.35
DE  Interaction: Q00765; IntAct: EBI-11120162; Score: 0.35
DE  Interaction: P70335; IntAct: EBI-11124658; Score: 0.35
DE  Interaction: P61019; IntAct: EBI-11127113; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135399; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: A8K8V0; IntAct: EBI-21612043; Score: 0.35
DE  Interaction: Q9NQX6; IntAct: EBI-21675860; Score: 0.35
DE  Interaction: Q14315; IntAct: EBI-20912382; Score: 0.40
DE  Interaction: Q32P51; IntAct: EBI-20922858; Score: 0.40
DE  Interaction: O15371; IntAct: EBI-25408957; Score: 0.35
DE  Interaction: O00232; IntAct: EBI-25408957; Score: 0.35
DE  Interaction: O75427; IntAct: EBI-25408957; Score: 0.50
DE  Interaction: Q9Y2L9; IntAct: EBI-25408957; Score: 0.35
DE  Interaction: Q9Y6G9; IntAct: EBI-25408957; Score: 0.35
DE  Interaction: P10515; IntAct: EBI-25408957; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005085;
GO  GO:0043547;
GO  GO:0007264;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASERRAFAHKINRTVAAEVRKQVSRERSGSPHSSRRCSSSLGVPLTEVVEPLDFEDVLLSRPPDAEPGPLRDLVEFPA
SQ  DDLELLLQPRECRTTEPGIPKDEKLDAQVRAAVEMYIEDWVIVHRRYQYLSAAYSPVTTDTQRERQKGLPRQVFEQDASG
SQ  DERSGPEDSNDSRRGSGSPEDTPRSSGASSIFDLRNLAADSLLPSLLERAAPEDVDRRNETLRRQHRPPALLTLYPAPDE
SQ  DEAVERCSRPEPPREHFGQRILVKCLSLKFEIEIEPIFGILALYDVREKKKISENFYFDLNSDSMKGLLRAHGTHPAIST
SQ  LARSAIFSVTYPSPDIFLVIKLEKVLQQGDISECCEPYMVLKEVDTAKNKEKLEKLRLAAEQFCTRLGRYRMPFAWTAVH
SQ  LANIVSSAGQLDRDSDSEGERRPAWTDRRRRGPQDRASSGDDACSFSGFRPATLTVTNFFKQEAERLSDEDLFKFLADMR
SQ  RPSSLLRRLRPVTAQLKIDISPAPENPHFCLSPELLHIKPYPDPRGRPTKEILEFPAREVYAPHTSYRNLLYVYPHSLNF
SQ  SSRQGSVRNLAVRVQYMTGEDPSQALPVIFGKSSCSEFTREAFTPVVYHNKSPEFYEEFKLHLPACVTENHHLLFTFYHV
SQ  SCQPRPGTALETPVGFTWIPLLQHGRLRTGPFCLPVSVDQPPPSYSVLTPDVALPGMRWVDGHKGVFSVELTAVSSVHPQ
SQ  DPYLDKFFTLVHVLEEGAFPFRLKDTVLSEGNVEQELRASLAALRLASPEPLVAFSHHVLDKLVRLVIRPPIISGQIVNL
SQ  GRGAFEAMAHVVSLVHRSLEAAQDARGHCPQLAAYVHYAFRLPGTEPSLPDGAPPVTVQAATLARGSGRPASLYLARSKS
SQ  ISSSNPDLAVAPGSVDDEVSRILASKLLHEELALQWVVSSSAVREAILQHAWFFFQLMVKSMALHLLLGQRLDTPRKLRF
SQ  PGRFLDDITALVGSVGLEVITRVHKDVELAEHLNASLAFFLSDLLSLVDRGFVFSLVRAHYKQVATRLQSSPNPAALLTL
SQ  RMEFTRILCSHEHYVTLNLPCCPLSPPASPSPSVSSTTSQSSTFSSQAPDPKVTSMFELSGPFRQQHFLAGLLLTELALA
SQ  LEPEAEGAFLLHKKAISAVHSLLCGHDTDPRYAEATVKARVAELYLPLLSIARDTLPRLHDFAEGPGQRSRLASMLDSDT
SQ  EGEGDIAGTINPSVAMAIAGGPLAPGSRASISQGPPTASRAGCALSAESSRTLLACVLWVLKNTEPALLQRWATDLTLPQ
SQ  LGRLLDLLYLCLAAFEYKGKKAFERINSLTFKKSLDMKARLEEAILGTIGARQEMVRRSRERSPFGNPENVRWRKSVTHW
SQ  KQTSDRVDKTKDEMEHEALVEGNLATEASLVVLDTLEIIVQTVMLSEARESVLGAVLKVVLYSLGSAQSALFLQHGLATQ
SQ  RALVSKFPELLFEEDTELCADLCLRLLRHCGSRISTIRTHASASLYLLMRQNFEIGHNFARVKMQVTMSLSSLVGTTQNF
SQ  SEEHLRRSLKTILTYAEEDMGLRDSTFAEQVQDLMFNLHMILTDTVKMKEHQEDPEMLIDLMYRIARGYQGSPDLRLTWL
SQ  QNMAGKHAELGNHAEAAQCMVHAAALVAEYLALLEDHRHLPVGCVSFQNISSNVLEESAISDDILSPDEEGFCSGKHFTE
SQ  LGLVGLLEQAAGYFTMGGLYEAVNEVYKNLIPILEAHRDYKKLAAVHGKLQEAFTKIMHQSSGWERVFGTYFRVGFYGAH
SQ  FGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDDVVEIIKDSNPVDKSKLDSQKAYIQITYVEPYFDTYELKDRVTY
SQ  FDRNYGLRTFLFCTPFTPDGRAHGELPEQHKRKTLLSTDHAFPYIKTRIRVCHREETVLTPVEVAIEDMQKKTRELAFAT
SQ  EQDPPDAKMLQMVLQGSVGPTVNQGPLEVAQVFLAEIPEDPKLFRHHNKLRLCFKDFCKKCEDALRKNKALIGPDQKEYH
SQ  RELERNYCRLREALQPLLTQRLPQLMAPTPPGLRNSLNRASFRKADL
//
ID  Q8VDR9;
PN  Dedicator of cytokinesis protein 6;
GN  Dock6;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Mainly located near the cell surface. {ECO:0000250}.
DR  UNIPROT: Q8VDR9;
DR  UNIPROT: E9QKQ0;
DR  UNIPROT: Q3UM59;
DR  UNIPROT: Q6PFY0;
DR  UNIPROT: Q8BJS1;
DR  UNIPROT: Q9D461;
DR  Pfam: PF06920;
DR  Pfam: PF14429;
DR  Pfam: PF11878;
DR  PROSITE: PS51650;
DR  PROSITE: PS51651;
DE  Function: Acts as guanine nucleotide exchange factor (GEF) for CDC42 and RAC1 small GTPases (By similarity). Through its activation of CDC42 and RAC1, regulates neurite outgrowth in an vitro differentiation system. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005085;
GO  GO:0043547;
GO  GO:0007264;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASERRAFAHKINRTVAAEVRKQVSRERSGSPHSSRRSSSSLGVPLTEVIEPLDFEDVLLSRPPEVEPGPLRDLIEFPV
SQ  DDLELLKQPRECRTTESGVPEDGQLDAQVRAAVEMYSEDWVIVRRRYQHLSTAYSPITTETQREWQKGLTCQVFEQDTPG
SQ  DERTGPEDVDDPQHCSGSPEDTPRSSGASGIFSLRNLAADSLLPTLLEQAAPEDVDRRNEALRRQHRAPTLLTLYPAPDE
SQ  DEAVERCSRPEPPREHFGQRILVKCLSLKFEIEIEPIFGTLALYDVREKKKISENFYFDLNSDSVKGLLRAHGTHPAIST
SQ  LARSAIFSVTYPSPDIFLVVKLEKVLQQGDISECCEPYMVMKEADTAKNKEKLEKLRLAAEQFCTRLGRYRMPFAWTAVH
SQ  LANIVSRPQDRDSDSEGERRPTWAERRRRGPQDRGYSGDDACSFSSFRPATLTVTNFFKQEAERLSDEDLFKFLADMRRP
SQ  SSLLRRLRPVTAQLKLDISPAPENLHFCLSPDLLHVKPYPDPRGRPTKEILEFPAREVYAPHSCYRNLLFVYPHSLNFSS
SQ  RQGSVRNLAVRIQYMAGEDQSQALPVIFGKSSCSEFTREAFTPVVYHNKSPEFYEEFKLRLPACVTENHHLFFTFYHVSC
SQ  QPRPGTALETPVGFTWIPLLQHGRLRTGPFCLPVSVDQPPPSYSVLTPDVALPGMRWVDGHKGVFSVELTAVSSVHPQDP
SQ  HLDKFFTLVHVLEEGIFPFRLKETVLSEGTMEQELRASLAALRLASPEPLVAFSHLVLDKLVRLVVRPPIICGQMVNLGR
SQ  GAFEAMAHVASLVHRNLEAVQDSRGHCPLLASYVHYAFRLPGGDLSLPGEAPPATVQAATLARGSGRPASLYLARSKSIS
SQ  SSNPDLAVVPGSVDDEVSRILASKGVDRSHSWVNSAYAPGGSKAVLRRVPPYCGADPRQLLHEELALQWVVSGSAVRELV
SQ  LQHAWFFFQLMVKSMELHLLLGQRLDTPRKLRFPGRFLDDIAALVASVGLEVITRVHKDMKLAERLNASLAFFLSDLLSI
SQ  ADRGYIFSLVRAHYKQVATRLQSAPNPTALLTLRMDFTRILCSHEHYVTLNLPCCPLSPPASPSPSVSSTTSQSSTFSSQ
SQ  APDPKVTSMFELSGPFRQQHFLSGLLLTELALALDPEAEGASLLHKKAISAVHSLLCSHDVDSRYAEATVKAKVAELYLP
SQ  LLSLARDTLPQLHGFAEGSGQRSRLASMLDSDTEGEGDIGSTINPSVAMAIAGGPLAPGSRTSISQGPSTAARSGCPLSA
SQ  ESSRTLLVCVLWVLKNAEPTLLQRWAADLALPQLGRLLDLLYLCLAAFEYKGKKAFERINSLTFKKSLDMKARLEEAILG
SQ  TIGARQEMVRRSRERSPFGNQENVRWRKSATHWRQTSDRVDKTKDEMEHEALVDGNLATEASLVVLDTLETIVQTVMLSE
SQ  ARESILSAVLKVVLYSLGSAQSALFLQHGLATQRALVSKFPELLFEEDTELCADLCLRLLRHCGSRISTIRMHASASLYL
SQ  LMRQNFEIGHNFARVKMLVTMSLSSLVGTTQNFSEEHLRKSLKTILTYAEEDIGLRDSTFAEQVQDLMFNLHMILTDTVK
SQ  MKEHQEDPEMLMDLMYRIARGYQGSPDLRLTWLQNMAGKHAELGNHAEAAQCMVHAAALVAEYLALLEDSRHLPVGCVSF
SQ  QNVSSNVLEESAISDDILSPDEEGFCSGKNFTELGLVGLLEQAAGYFTMGGLYEAVNEVYKNLIPILEAHRDYKKLAAVH
SQ  GKLQEAFTKIMHQSSGWERVFGTYFRVGFYGTRFGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDDVVEIIKDSNP
SQ  VDKSKLDPQKAYIQITYVEPHFDTYELKDRVTYFDRNYGLRAFLFCTPFTPDGRAHGELAEQHKRKTLLSTEHAFPYIKT
SQ  RIRVCHREETVLTPVEVAIEDMQKKTRELAFATEQDPPDAKMLQMVLQGSVGPTVNQGPLEVAQVFLSEIPEDPKLFRHH
SQ  NKLRLCFKDFCKKCEDALRKNKALIGPDQKEYHRELERHYSRLREALQPLLTQRLPQLLAPSSTSLRSSMNRSSFRKADL
//
ID  Q99704;
PN  Docking protein 1;
GN  DOK1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Cytoplasm. Nucleus. [Isoform 3]: Cytoplasm, perinuclear region.
DR  UNIPROT: Q99704;
DR  UNIPROT: O43204;
DR  UNIPROT: Q53TY2;
DR  UNIPROT: Q9UHG6;
DR  PDB: 2V76;
DR  Pfam: PF02174;
DR  Pfam: PF00169;
DR  PROSITE: PS51064;
DR  OMIM: 602919;
DR  DisGeNET: 1796;
DE  Function: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3. {ECO:0000269|PubMed:18156175}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-9688841; Score: 0.55
DE  Interaction: P04626; IntAct: EBI-7878971; Score: 0.44
DE  Interaction: O60880; IntAct: EBI-7298602; Score: 0.46
DE  Interaction: Q06124; IntAct: EBI-7380741; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-3045543; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: P31016; IntAct: EBI-7969766; Score: 0.44
DE  Interaction: Q9Q2G4; IntAct: EBI-6176962; Score: 0.50
DE  Interaction: Q9JIY2; IntAct: EBI-7645406; Score: 0.52
DE  Interaction: Q9H3Y6; IntAct: EBI-8541291; Score: 0.64
DE  Interaction: Q7L591; IntAct: EBI-10694731; Score: 0.49
DE  Interaction: P46109; IntAct: EBI-10695513; Score: 0.49
DE  Interaction: O43639; IntAct: EBI-21521290; Score: 0.35
DE  Interaction: Q8IYK4; IntAct: EBI-21827478; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: Q06884; IntAct: EBI-22253692; Score: 0.35
DE  Interaction: Q9JJ31; IntAct: EBI-22253692; Score: 0.35
DE  Interaction: G3V8S2; IntAct: EBI-22253692; Score: 0.35
DE  Interaction: Q2LC84; IntAct: EBI-22253796; Score: 0.35
DE  Interaction: F1LRI5; IntAct: EBI-22253796; Score: 0.35
DE  Interaction: O08776; IntAct: EBI-22253796; Score: 0.35
DE  Interaction: A0A0G2JV77; IntAct: EBI-22253796; Score: 0.35
DE  Interaction: F1LMZ8; IntAct: EBI-22253796; Score: 0.35
DE  Interaction: A0A0G2K064; IntAct: EBI-22253796; Score: 0.35
DE  Interaction: B5DFA5; IntAct: EBI-22253796; Score: 0.35
DE  Interaction: P62845; IntAct: EBI-22253796; Score: 0.35
DE  Interaction: P09875; IntAct: EBI-22253796; Score: 0.35
DE  Interaction: D3ZZM3; IntAct: EBI-22253796; Score: 0.35
DE  Interaction: G3V619; IntAct: EBI-22253796; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0007166;
GO  GO:0038145;
GO  GO:0007265;
GO  GO:0007165;
GO  GO:0007169;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDGAVMEGPLFLQSQRFGTKRWRKTWAVLYPASPHGVARLEFFDHKGSSSGGGRGSSRRLDCKVIRLAECVSVAPVTVET
SQ  PPEPGATAFRLDTAQRSHLLAADAPSSAAWVQTLCRNAFPKGSWTLAPTDNPPKLSALEMLENSLYSPTWEGSQFWVTVQ
SQ  RTEAAERCGLHGSYVLRVEAERLTLLTVGAQSQILEPLLSWPYTLLRRYGRDKVMFSFEAGRRCPSGPGTFTFQTAQGND
SQ  IFQAVETAIHRQKAQGKAGQGHDVLRADSHEGEVAEGKLPSPPGPQELLDSPPALYAEPLDSLRIAPCPSQDSLYSDPLD
SQ  STSAQAGEGVQRKKPLYWDLYEHAQQQLLKAKLTDPKEDPIYDEPEGLAPVPPQGLYDLPREPKDAWWCQARVKEEGYEL
SQ  PYNPATDDYAVPPPRSTKPLLAPKPQGPAFPEPGTATGSGIKSHNSALYSQVQKSGASGSWDCGLSRVGTDKTGVKSEGS
SQ  T
//
ID  Q9NZJ0;
PN  Denticleless protein homolog;
GN  DTL;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:26431207}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome. Note=Nuclear matrix-associated protein. Translocates from the interphase nucleus to the metaphase cytoplasm during mitosis.
DR  UNIPROT: Q9NZJ0;
DR  UNIPROT: A8K8H8;
DR  UNIPROT: D3DT98;
DR  UNIPROT: Q5VT77;
DR  UNIPROT: Q96SN0;
DR  UNIPROT: Q9NW03;
DR  UNIPROT: Q9NW34;
DR  UNIPROT: Q9NWM5;
DR  PDB: 6QC0;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 610617;
DR  DisGeNET: 51514;
DE  Function: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2 (PubMed:16861906, PubMed:16949367, PubMed:16964240, PubMed:17085480, PubMed:18703516, PubMed:18794347, PubMed:18794348, PubMed:19332548, PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613, PubMed:27906959). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication (PubMed:16861906, PubMed:16949367, PubMed:17085480). CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing (PubMed:18794348, PubMed:19332548). KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration (PubMed:23478445). Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA- dependent translesion DNA synthesis (PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). {ECO:0000269|PubMed:16861906, ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:17085480, ECO:0000269|PubMed:18703516, ECO:0000269|PubMed:18794347, ECO:0000269|PubMed:18794348, ECO:0000269|PubMed:19332548, ECO:0000269|PubMed:20129063, ECO:0000269|PubMed:23478441, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:23677613, ECO:0000269|PubMed:26431207, ECO:0000269|PubMed:27906959}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3TLR7; IntAct: EBI-2562304; Score: 0.40
DE  Interaction: Q7L5N1; IntAct: EBI-2510262; Score: 0.56
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-1176116; Score: 0.53
DE  Interaction: Q13619; IntAct: EBI-1176157; Score: 0.53
DE  Interaction: P61964; IntAct: EBI-1176605; Score: 0.40
DE  Interaction: Q16531; IntAct: EBI-1176630; Score: 0.56
DE  Interaction: Q9BQ67; IntAct: EBI-1176630; Score: 0.35
DE  Interaction: Q3U1J4; IntAct: EBI-2559059; Score: 0.40
DE  Interaction: O60232; IntAct: EBI-21543889; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-21594461; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-21594293; Score: 0.35
DE  Interaction: Q8NB37; IntAct: EBI-21611026; Score: 0.35
DE  Interaction: Q9UHV9; IntAct: EBI-21645427; Score: 0.35
DE  Interaction: Q6ZN54; IntAct: EBI-21689078; Score: 0.35
DE  Interaction: Q15170; IntAct: EBI-21699650; Score: 0.35
DE  Interaction: Q13557; IntAct: EBI-21719478; Score: 0.35
DE  Interaction: Q8N4J0; IntAct: EBI-21736494; Score: 0.35
DE  Interaction: Q99627; IntAct: EBI-21875970; Score: 0.35
DE  Interaction: Q92990; IntAct: EBI-21884908; Score: 0.35
DE  Interaction: P97784; IntAct: EBI-21991345; Score: 0.40
DE  Interaction: P40337; IntAct: EBI-25895784; Score: 0.56
GO  GO:0005813;
GO  GO:0005694;
GO  GO:0080008;
GO  GO:0031464;
GO  GO:0031465;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0030674;
GO  GO:0006974;
GO  GO:0006260;
GO  GO:0007095;
GO  GO:0010971;
GO  GO:0045732;
GO  GO:0043161;
GO  GO:0006513;
GO  GO:0000209;
GO  GO:0051726;
GO  GO:0009411;
GO  GO:0048511;
GO  GO:0019985;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MLFNSVLRQPQLGVLRNGWSSQYPLQSLLTGYQCSGNDEHTSYGETGVPVPPFGCTFSSAPNMEHVLAVANEEGFVRLYN
SQ  TESQSFRKKCFKEWMAHWNAVFDLAWVPGELKLVTAAGDQTAKFWDVKAGELIGTCKGHQCSLKSVAFSKFEKAVFCTGG
SQ  RDGNIMVWDTRCNKKDGFYRQVNQISGAHNTSDKQTPSKPKKKQNSKGLAPSVDFQQSVTVVLFQDENTLVSAGAVDGII
SQ  KVWDLRKNYTAYRQEPIASKSFLYPGSSTRKLGYSSLILDSTGSTLFANCTDDNIYMFNMTGLKTSPVAIFNGHQNSTFY
SQ  VKSSLSPDDQFLVSGSSDEAAYIWKVSTPWQPPTVLLGHSQEVTSVCWCPSDFTKIATCSDDNTLKIWRLNRGLEEKPGG
SQ  DKLSTVGWASQKKKESRPGLVTVTSSQSTPAKAPRAKCNPSNSSPSSAACAPSCAGDLPLPSNTPTFSIKTSPAKARSPI
SQ  NRRGSVSSVSPKPPSSFKMSIRNWVTRTPSSSPPITPPASETKIMSPRKALIPVSQKSSQAEACSESRNRVKRRLDSSCL
SQ  ESVKQKCVKSCNCVTELDGQVENLHLDLCCLAGNQEDLSKDSLGPTKSSKIEGAGTSISEPPSPISPYASESCGTLPLPL
SQ  RPCGEGSEMVGKENSSPENKNWLLAMAAKRKAENPSPRSPSSQTPNSRRQSGKKLPSPVTITPSSMRKICTYFHRKSQED
SQ  FCGPEHSTEL
//
ID  Q3TLR7;
PN  Denticleless protein homolog;
GN  Dtl;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9NZJ0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9NZJ0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZJ0}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9NZJ0}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NZJ0}. Chromosome {ECO:0000250|UniProtKB:Q9NZJ0}. Note=Nuclear matrix- associated protein. Translocates from the interphase nucleus to the metaphase cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:Q9NZJ0}.
DR  UNIPROT: Q3TLR7;
DR  UNIPROT: Q3TTE9;
DR  UNIPROT: Q6PAN1;
DR  UNIPROT: Q80WY1;
DR  UNIPROT: Q80WY2;
DR  UNIPROT: Q8BW38;
DR  UNIPROT: Q9CZ76;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2. CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication. CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing. KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration. Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis. The DDB1- CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (By similarity). {ECO:0000250|UniProtKB:Q9NZJ0}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13620; IntAct: EBI-2562304; Score: 0.40
DE  Interaction: P61201; IntAct: EBI-2562304; Score: 0.56
DE  Interaction: Q9NZJ0; IntAct: EBI-2562304; Score: 0.40
DE  Interaction: Q9BT78; IntAct: EBI-2562304; Score: 0.56
DE  Interaction: Q16531; IntAct: EBI-2562304; Score: 0.56
DE  Interaction: Q13619; IntAct: EBI-2562304; Score: 0.56
DE  Interaction: Q7L5N1; IntAct: EBI-2562304; Score: 0.40
DE  Interaction: O15078; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: Q9NP92; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: Q9BW61; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: Q9UNS2; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: P17987; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: Q9UBW8; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: O75150; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: P62877; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: A1L170; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: E9PGT6; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: C9JFE4; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: Q9C0J8; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: E7EM64; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: P78371; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: B4DSW0; IntAct: EBI-11019947; Score: 0.35
DE  Interaction: Q96EB6; IntAct: EBI-11019947; Score: 0.35
GO  GO:0005813;
GO  GO:0005694;
GO  GO:0080008;
GO  GO:0031464;
GO  GO:0031465;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0030674;
GO  GO:0004842;
GO  GO:0006974;
GO  GO:0006260;
GO  GO:0007095;
GO  GO:0010971;
GO  GO:0045732;
GO  GO:0043161;
GO  GO:0006513;
GO  GO:0000209;
GO  GO:0051726;
GO  GO:0009411;
GO  GO:0048511;
GO  GO:0019985;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9NZJ0};
SQ  MLFNSVLRQPQLGVLRNGWSSHYPLQSLLSGYQCNCNDEHTSYGETGVPVPPFGCTFCTAPSMEHILAVANEEGFVRLYN
SQ  TESQTSKKTCFKEWMAHWNAVFDLAWVPGELKLVTAAGDQTAKFWDVRAGELMGTCKGHQCSLKSVAFPKFQKAVFSTGG
SQ  RDGNIMIWDTRCNKKDGFYRQVNQISGAHNTADKQTPSKPKKKQNSKGLAPAVDSQQSVTVVLFQDENTLVSAGAVDGII
SQ  KVWDLRKNYTAYRQEPIASKSFLYPGTSTRKLGYSSLVLDSTGSTLFANCTDDNIYMFNMTGLKTSPVAVFNGHQNSTFY
SQ  VKSSLSPDDQFLISGSSDEAAYIWKVSMPWHPPTVLLGHSQEVTSVCWCPSDFTKIATCSDDNTLKIWRLNRGLEEKPGD
SQ  KHSIVGWTSQKKKEVKACPVTVPSSQSTPAKAPRAKSSPSISSPSSAACTPSCAGDLPLPSSTPTFSVKTTPATTRSSVS
SQ  RRGSISSVSPKPLSSFKMSLRNWVTRTPSSSPPVTPPASETKISSPRKALIPVSQKSSQADACSESRNRVKRRLDSSCLE
SQ  SVKQKCVKSCNCVTELDGQAESLRLDLCCLSGTQEVLSQDSEGPTKSSKTEGAGTSISEPPSPVSPYASEGCGPLPLPLR
SQ  PCGEGSEMVGKENSSPENKNWLLAIAAKRKAENSSPRSPSSQTPSSRRQSGKTSPGPVTITPSSMRKICTYFRRKTQDDF
SQ  CSPEHSTEL
//
ID  Q24246;
PN  Cytoplasmic dynein 1 intermediate chain;
GN  sw;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9774695}. [Isoform 2c]: Lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around lysosomes. [Isoform 2a]: Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around the nucleus. [Isoform 2b]: Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm around the nucleus.
DR  UNIPROT: Q24246;
DR  UNIPROT: O96508;
DR  UNIPROT: O96510;
DR  UNIPROT: O96511;
DR  UNIPROT: O96512;
DR  UNIPROT: O96513;
DR  UNIPROT: O96514;
DR  UNIPROT: O96515;
DR  UNIPROT: O96516;
DR  UNIPROT: Q5U0Z1;
DR  UNIPROT: Q86BQ5;
DR  UNIPROT: Q9NG49;
DR  UNIPROT: Q9TZR7;
DR  UNIPROT: Q9TZR8;
DR  UNIPROT: Q9TZR9;
DR  UNIPROT: Q9TZS0;
DR  UNIPROT: Q9VR78;
DR  PDB: 2P2T;
DR  PDB: 3FM7;
DR  PDB: 3L9K;
DR  Pfam: PF11540;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the help dynein bind to dynactin 150 kDa component (By similarity). {ECO:0000250, ECO:0000269|PubMed:11071907}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8T0I9; IntAct: EBI-213466; Score: 0.00
DE  Interaction: Q4V5A7; IntAct: EBI-253285; Score: 0.00
DE  Interaction: Q9XZ56; IntAct: EBI-9919028; Score: 0.46
DE  Interaction: O61307; IntAct: EBI-9921261; Score: 0.35
DE  Interaction: P18431; IntAct: EBI-9925534; Score: 0.35
DE  Interaction: Q9VLS7; IntAct: EBI-9929131; Score: 0.35
DE  Interaction: Q24568; IntAct: EBI-9944837; Score: 0.35
GO  GO:0005868;
GO  GO:0005765;
GO  GO:0005874;
GO  GO:0043005;
GO  GO:0031965;
GO  GO:0032991;
GO  GO:0034452;
GO  GO:0045504;
GO  GO:0045503;
GO  GO:0060090;
GO  GO:0008088;
GO  GO:0007349;
GO  GO:0051642;
GO  GO:0001754;
GO  GO:0000226;
GO  GO:0007018;
GO  GO:0034501;
GO  GO:0007291;
GO  GO:0007051;
GO  GO:0010970;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MDRKAELERKKAKLAALREEKDRRRREKEIKDMEEAAGRIGGGAGIDKDQRKDLDEMLSSLGVAPVSEVLSSLSSVNSMT
SQ  SDNSNTQTPDASLQATVNGQSGGKKQPLNLSVYNVQATNIPPKETLVYTKQTQTTSTGGGNGDVLSCHSSPLSGYMEDWW
SQ  RPRKAHATDYYDEYNLNPGLEWEDEFTDDEESSLQNLGNGFTSKLPPGYLTHGLPTVKDVAPAITPLEIKKETEVKKEVN
SQ  ELSEEQKQMIILSENFQRFVVRAGRVIERALSENVDIYTDYIGGGDSEEANDERSHARLSLNRVFYDERWSKNRCITSMD
SQ  WSTHFPELVVGSYHNNEESPNEPDGVVMVWNTKFKKSTPEDVFHCQSAVMSTCFAKFNPNLILGGTYSGQIVLWDNRVQK
SQ  RTPIQRTPLSAAAHTHPVYCLQMVGTQNAHNVISISSDGKLCSWSLDMLSQPQDTLELQQRQSKAIAITSMAFPANEINS
SQ  LVMGSEDGYVYSASRHGLRSGVNEVYERHLGPITGISTHYNQLSPDFGHLFLTSSIDWTIKLWSLKDTKPLYSFEDNSDY
SQ  VMDVAWSPVHPALFAAVDGSGRLDLWNLNQDTEVPTASIVVAGAPALNRVSWTPSGLHVCIGDEAGKLYVYDVAENLAQP
SQ  SRDEWSRFNTHLSEIKMNQSDEV
//
ID  Q759T0;
PN  Dynein light chain 1, cytoplasmic;
GN  DYN2;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}.
DR  UNIPROT: Q759T0;
DR  Pfam: PF01221;
DR  PROSITE: PS01239;
DE  Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q02647}.
DE  Reference Proteome: Yes;
GO  GO:0005868;
GO  GO:0005881;
GO  GO:0005643;
GO  GO:1990429;
GO  GO:0005777;
GO  GO:0045505;
GO  GO:0008574;
GO  GO:0044877;
GO  GO:0040001;
GO  GO:0051028;
GO  GO:0030473;
GO  GO:0051292;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKPAILKASDITDELRDEIFGISVQAVEQFQLEREVAAYIKKELDSKHGQTWHVIVGKNFGSYVTHEKGHFIYFYIGPL
SQ  AFLVFKTA
//
ID  Q22799;
PN  Dynein light chain 1, cytoplasmic;
GN  dlc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P63170}. Nucleus envelope {ECO:0000269|PubMed:27864381, ECO:0000305|PubMed:20005871}. Cytoplasmic granule {ECO:0000269|PubMed:27864381}. Note=Probably recruited to the nuclear envelope by unc-83 (PubMed:20005871). Localizes to perinuclear patches in the transition zone (PubMed:27864381). Localizes to P- granules in the mitotic region and transition zone (PubMed:27864381). {ECO:0000269|PubMed:27864381, ECO:0000305|PubMed:20005871}.
DR  UNIPROT: Q22799;
DR  Pfam: PF01221;
DR  PROSITE: PS01239;
DE  Function: Acts as a non-catalytic accessory component of a dynein complex (By similarity). Part of a complex with bicd-1 and egal-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migrations in hypodermal precursor cells (PubMed:20005871). Probably within a dynein motor complex, plays a role in the cell fate specification of the germline and oogenesis (PubMed:19752194, PubMed:27864381). In particular, it inhibits germ cell proliferation (PubMed:19752194). Regulates the function and localization of the RNA-binding protein fbf- 2 in the germline (PubMed:27864381). Plays a role in mitotic and meiotic processes (PubMed:19752194, PubMed:26483555). Involved in the pairing of homologous chromosomes (PubMed:26483555). Independently of its dynein-mediated functions, plays a role in germ cell apoptosis (PubMed:24030151). {ECO:0000250|UniProtKB:Q24117, ECO:0000269|PubMed:19752194, ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:24030151, ECO:0000269|PubMed:26483555, ECO:0000269|PubMed:27864381}.
DE  Reference Proteome: Yes;
DE  Interaction: O02101; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q17902; IntAct: EBI-2413132; Score: 0.75
DE  Interaction: G5EBV6; IntAct: EBI-342182; Score: 0.00
DE  Interaction: Q18192; IntAct: EBI-342185; Score: 0.00
DE  Interaction: O16474; IntAct: EBI-342197; Score: 0.00
DE  Interaction: O17641; IntAct: EBI-342188; Score: 0.00
DE  Interaction: P34766; IntAct: EBI-342191; Score: 0.00
DE  Interaction: Q18529; IntAct: EBI-6456071; Score: 0.55
DE  Interaction: P91249; IntAct: EBI-342206; Score: 0.00
DE  Interaction: O45335; IntAct: EBI-342200; Score: 0.00
DE  Interaction: G5EG76; IntAct: EBI-342203; Score: 0.00
DE  Interaction: Q19816; IntAct: EBI-6456097; Score: 0.55
DE  Interaction: Q9XVX4; IntAct: EBI-342209; Score: 0.00
DE  Interaction: Q93572; IntAct: EBI-342212; Score: 0.00
DE  Interaction: P48150; IntAct: EBI-342224; Score: 0.00
DE  Interaction: O45436; IntAct: EBI-342218; Score: 0.00
DE  Interaction: Q19988; IntAct: EBI-342221; Score: 0.00
DE  Interaction: G5ECT7; IntAct: EBI-2418552; Score: 0.62
DE  Interaction: Q20805; IntAct: EBI-342227; Score: 0.00
DE  Interaction: P48154; IntAct: EBI-342230; Score: 0.00
DE  Interaction: G5EBX2; IntAct: EBI-342239; Score: 0.00
DE  Interaction: P55853; IntAct: EBI-342236; Score: 0.00
DE  Interaction: C6KRN1; IntAct: EBI-2420006; Score: 0.71
DE  Interaction: P34574; IntAct: EBI-342248; Score: 0.00
DE  Interaction: Q22696; IntAct: EBI-342251; Score: 0.00
DE  Interaction: G5EDQ5; IntAct: EBI-342245; Score: 0.00
DE  Interaction: Q9U2M6; IntAct: EBI-342260; Score: 0.00
DE  Interaction: P55954; IntAct: EBI-342254; Score: 0.00
DE  Interaction: Q9N432; IntAct: EBI-342257; Score: 0.00
DE  Interaction: H2L0C9; IntAct: EBI-342263; Score: 0.00
DE  Interaction: Q9XUM8; IntAct: EBI-2420748; Score: 0.49
DE  Interaction: Q23064; IntAct: EBI-2905315; Score: 0.53
DE  Interaction: Q7K714; IntAct: EBI-6455746; Score: 0.37
DE  Interaction: O45599; IntAct: EBI-6456841; Score: 0.37
DE  Interaction: P30642; IntAct: EBI-6456967; Score: 0.37
DE  Interaction: Q18194; IntAct: EBI-6456947; Score: 0.37
DE  Interaction: P46502; IntAct: EBI-6456957; Score: 0.37
DE  Interaction: Q22799; IntAct: EBI-6456977; Score: 0.37
DE  Interaction: G5EFV3; IntAct: EBI-6456987; Score: 0.37
DE  Interaction: Q19207; IntAct: EBI-6457073; Score: 0.37
DE  Interaction: O45087; IntAct: EBI-6458000; Score: 0.37
DE  Interaction: G5EBL8; IntAct: EBI-6458325; Score: 0.37
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0005635;
GO  GO:0045505;
GO  GO:0006915;
GO  GO:0051301;
GO  GO:0051321;
GO  GO:0030473;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDRKAVIKNADMSDDMQQDAIDCATQALEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQ
SQ  VAILLFKSG
//
ID  Q6FUJ0;
PN  Dynein light chain 1, cytoplasmic;
GN  DYN2;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}.
DR  UNIPROT: Q6FUJ0;
DR  Pfam: PF01221;
DR  PROSITE: PS01239;
DE  Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q02647}.
DE  Reference Proteome: Yes;
GO  GO:0005868;
GO  GO:0005881;
GO  GO:0005643;
GO  GO:1990429;
GO  GO:0005777;
GO  GO:0008574;
GO  GO:0044877;
GO  GO:0040001;
GO  GO:0051028;
GO  GO:0030473;
GO  GO:0051292;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDQVIVKASDMGDEMQQEVFRIAEEAMREHTLEREIASVIKKEMDSRYGHTWHVIVGRSFGSYVTHEKGKFVYFYVGPLA
SQ  LLVFKT
//
ID  Q6BZF8;
PN  Dynein light chain 1, cytoplasmic;
GN  DYN2;
OS  284592;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}.
DR  UNIPROT: Q6BZF8;
DR  Pfam: PF01221;
DR  PROSITE: PS01239;
DE  Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q02647}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0030286;
GO  GO:0005874;
GO  GO:0005643;
GO  GO:0007017;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSEKEQEPILKASDLPEEMQTRIFELSNEAVSNYKIEKDIATYLKKELDQLYGATWHVIVGKSFGSYVTHEQGFFTYFYI
SQ  GQLAFLIFKSG
//
ID  O94111;
PN  Dynein light chain, cytoplasmic;
GN  nudG;
OS  227321;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}.
DR  UNIPROT: O94111;
DR  UNIPROT: C8VTG5;
DR  UNIPROT: Q547D6;
DR  UNIPROT: Q5BGB0;
DR  Pfam: PF01221;
DR  PROSITE: PS01239;
DE  Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q02647}.
DE  Reference Proteome: Yes;
GO  GO:0005868;
GO  GO:0005881;
GO  GO:0005643;
GO  GO:1990429;
GO  GO:0005777;
GO  GO:0045505;
GO  GO:0008574;
GO  GO:0044877;
GO  GO:0048315;
GO  GO:0040001;
GO  GO:0051028;
GO  GO:0030473;
GO  GO:0051292;
GO  GO:0015031;
GO  GO:0043935;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASEKKDKLEPQIKSVDMSEDMQQEAVEVAIEAMEKYHIEKDIAQYIKREFDSRKGATWHCVVGRNFGSFVTHETKHFIY
SQ  FYLGHCAILLFKTQ
//
ID  Q6CWX4;
PN  Dynein light chain 1, cytoplasmic;
GN  DYN2;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}.
DR  UNIPROT: Q6CWX4;
DR  Pfam: PF01221;
DR  PROSITE: PS01239;
DE  Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q02647}.
DE  Reference Proteome: Yes;
GO  GO:0005868;
GO  GO:0005881;
GO  GO:0005643;
GO  GO:1990429;
GO  GO:0005777;
GO  GO:0008574;
GO  GO:0044877;
GO  GO:0040001;
GO  GO:0051028;
GO  GO:0030473;
GO  GO:0051292;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKPVLKASDITDELRDEIFELSSNATANYKLEREIAAYIKKQLDVSQGETWHVIVGKNFGSYVTHEKGYFVYFYIGPLA
SQ  FLVFKTA
//
ID  Q9UR05;
PN  Dynein light chain 1, cytoplasmic;
GN  dlc2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02647}.
DR  UNIPROT: Q9UR05;
DR  Pfam: PF01221;
DR  PROSITE: PS01239;
DE  Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q02647}.
DE  Reference Proteome: Yes;
GO  GO:0005868;
GO  GO:0005829;
GO  GO:0035974;
GO  GO:0005874;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0045505;
GO  GO:0030437;
GO  GO:0030989;
GO  GO:0051028;
GO  GO:0000743;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVIKAVDMSEKMQQEAIHAAVQAMEKFTIEKDIAAFIKREFDKKFSPTWHCIVGRNFGSFVTHESRHFIYFYLGTVAFL
SQ  LFKSG
//
ID  Q02647;
PN  Dynein light chain 1, cytoplasmic;
GN  DYN2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytoskeleton. Nucleus, nuclear pore complex {ECO:0000269|PubMed:17546040, ECO:0000269|PubMed:23223634, ECO:0000269|PubMed:25646085}.
DR  UNIPROT: Q02647;
DR  UNIPROT: D6VT54;
DR  PDB: 4DS1;
DR  PDB: 4HT6;
DR  PDB: 7N9F;
DR  Pfam: PF01221;
DR  PROSITE: PS01239;
DE  Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). Also a component of the nuclear pore complex where it may contribute to the stable association of the Nup82 subcomplex with the NPC (PubMed:17546040, PubMed:23223634, PubMed:25646085). {ECO:0000250, ECO:0000269|PubMed:17546040, ECO:0000269|PubMed:23223634, ECO:0000269|PubMed:25646085}.
DE  Reference Proteome: Yes;
DE  Interaction: P36161; IntAct: EBI-8466751; Score: 0.40
DE  Interaction: P40960; IntAct: EBI-8480342; Score: 0.81
DE  Interaction: P40494; IntAct: EBI-2613029; Score: 0.35
DE  Interaction: P24869; IntAct: EBI-2617071; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3724582; Score: 0.35
DE  Interaction: Q8IYA8; IntAct: EBI-11534278; Score: 0.56
DE  Interaction: O96015; IntAct: EBI-11534269; Score: 0.56
DE  Interaction: Q02647; IntAct: EBI-15483402; Score: 0.44
DE  Interaction: P36022; IntAct: EBI-15483422; Score: 0.43
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0005881;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:1990429;
GO  GO:0045505;
GO  GO:0044877;
GO  GO:0040001;
GO  GO:0000132;
GO  GO:0051028;
GO  GO:0030473;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDENKSTPIVKASDITDKLKEDILTISKDALDKYQLERDIAGTVKKQLDVKYGNTWHVIVGKNFGSYVTHEKGHFVYFY
SQ  IGPLAFLVFKTA
//
ID  Q03001;
PN  Dystonin;
GN  DST;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11751855, ECO:0000269|PubMed:19932097}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q91ZU6}. Cell projection, axon {ECO:0000250|UniProtKB:Q91ZU6}. Note=Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells (By similarity). Associated at the growing distal tip of microtubules. {ECO:0000250|UniProtKB:Q91ZU6}. [Isoform 1]: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, sarcomere, H zone {ECO:0000250}. Note=Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. {ECO:0000250}. [Isoform 2]: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes both cortical and cytoplasmic actin filaments. {ECO:0000250}. [Isoform 3]: Cytoplasm, cytoskeleton. Cell junction, hemidesmosome. Note=Localizes to actin and intermediate filaments cytoskeletons (By similarity). Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes. {ECO:0000250}. [Isoform 6]: Nucleus {ECO:0000250|UniProtKB:Q91ZU6}. Nucleus envelope {ECO:0000269|PubMed:10428034}. Membrane {ECO:0000269|PubMed:10428034}; Single-pass membrane protein {ECO:0000269|PubMed:10428034}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q91ZU6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q91ZU6}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10428034}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q91ZU6}. Note=Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. {ECO:0000250|UniProtKB:Q91ZU6}. [Isoform 7]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10428034}. Cell projection, axon {ECO:0000269|PubMed:10428034}. Membrane {ECO:0000269|PubMed:10428034}. Note=Associates with axonal microtubules and intermediate filaments, but not with actin cytoskeleton, in sensory neurons. [Isoform 8]: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
DR  UNIPROT: Q03001;
DR  UNIPROT: B7Z3H1;
DR  UNIPROT: E7ERU0;
DR  UNIPROT: O94833;
DR  UNIPROT: Q12825;
DR  UNIPROT: Q13266;
DR  UNIPROT: Q13267;
DR  UNIPROT: Q13775;
DR  UNIPROT: Q5TBT0;
DR  UNIPROT: Q5TBT2;
DR  UNIPROT: Q5TF23;
DR  UNIPROT: Q5TF24;
DR  UNIPROT: Q8N1T8;
DR  UNIPROT: Q8N8J3;
DR  UNIPROT: Q8WXK8;
DR  UNIPROT: Q8WXK9;
DR  UNIPROT: Q96AK9;
DR  UNIPROT: Q96DQ5;
DR  UNIPROT: Q96J76;
DR  UNIPROT: Q96QT5;
DR  UNIPROT: Q9H555;
DR  UNIPROT: Q9UGD7;
DR  UNIPROT: Q9UGD8;
DR  UNIPROT: Q9UN10;
DR  PDB: 3GJO;
DR  Pfam: PF00307;
DR  Pfam: PF13499;
DR  Pfam: PF02187;
DR  Pfam: PF00681;
DR  Pfam: PF17902;
DR  Pfam: PF00435;
DR  Pfam: PF18373;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51460;
DR  PROSITE: PS50002;
DR  OMIM: 113810;
DR  OMIM: 614653;
DR  OMIM: 615425;
DR  DisGeNET: 667;
DE  Function: Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1 (By similarity). {ECO:0000250|UniProtKB:Q91ZU6}. [Isoform 3]: Plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity. [Isoform 6]: Required for bundling actin filaments around the nucleus. {ECO:0000250, ECO:0000269|PubMed:10428034, ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692}. [Isoform 7]: Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport.
DE  Disease: Neuropathy, hereditary sensory and autonomic, 6 (HSAN6) [MIM:614653]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN6 is a severe autosomal recessive disorder characterized by neonatal hypotonia, respiratory and feeding difficulties, lack of psychomotor development, and autonomic abnormalities including labile cardiovascular function, lack of corneal reflexes leading to corneal scarring, areflexia, and absent axonal flare response after intradermal histamine injection. {ECO:0000269|PubMed:22522446}. Note=The disease is caused by variants affecting the gene represented in this entry. Epidermolysis bullosa simplex 3, localized or generalized intermediate, with BP230 deficiency (EBS3) [MIM:615425]: A form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. EBS3 is an autosomal recessive disorder characterized by skin blistering mainly occurring on the feet and ankles. Ultrastructural analysis of skin biopsy shows abnormal hemidesmosomes with poorly formed inner plaques. {ECO:0000269|PubMed:20164846, ECO:0000269|PubMed:22113475}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95295; IntAct: EBI-5664296; Score: 0.00
DE  Interaction: P04626; IntAct: EBI-25367963; Score: 0.37
DE  Interaction: P29991; IntAct: EBI-8828450; Score: 0.37
DE  Interaction: Q9NYQ7; IntAct: EBI-311579; Score: 0.37
DE  Interaction: Q9HCM3; IntAct: EBI-311727; Score: 0.37
DE  Interaction: P62993; IntAct: EBI-350217; Score: 0.35
DE  Interaction: Q9BZL6; IntAct: EBI-7235479; Score: 0.37
DE  Interaction: O15198; IntAct: EBI-7263646; Score: 0.37
DE  Interaction: Q15287; IntAct: EBI-1065372; Score: 0.00
DE  Interaction: P15121; IntAct: EBI-1067054; Score: 0.00
DE  Interaction: Q9UHX1; IntAct: EBI-1077592; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-1105693; Score: 0.00
DE  Interaction: Q9NV70; IntAct: EBI-1105725; Score: 0.00
DE  Interaction: Q9UKE5; IntAct: EBI-1105730; Score: 0.00
DE  Interaction: Q8TDR0; IntAct: EBI-1105735; Score: 0.00
DE  Interaction: Q15691; IntAct: EBI-2409886; Score: 0.73
DE  Interaction: P19838; IntAct: EBI-2680933; Score: 0.00
DE  Interaction: Q13951; IntAct: EBI-2691963; Score: 0.00
DE  Interaction: P25054; IntAct: EBI-3436852; Score: 0.00
DE  Interaction: Q16659; IntAct: EBI-3444390; Score: 0.00
DE  Interaction: Q13952; IntAct: EBI-3446173; Score: 0.00
DE  Interaction: Q13177; IntAct: EBI-3446930; Score: 0.00
DE  Interaction: Q96CV9; IntAct: EBI-5357450; Score: 0.45
DE  Interaction: Q9UKG1; IntAct: EBI-5357625; Score: 0.45
DE  Interaction: Q8IZP0; IntAct: EBI-5652673; Score: 0.00
DE  Interaction: Q15327; IntAct: EBI-5653401; Score: 0.00
DE  Interaction: P0C862; IntAct: EBI-5654717; Score: 0.00
DE  Interaction: Q8N3C7; IntAct: EBI-5655638; Score: 0.00
DE  Interaction: Q14324; IntAct: EBI-5660966; Score: 0.00
DE  Interaction: O75386; IntAct: EBI-5666780; Score: 0.00
DE  Interaction: Q13188; IntAct: EBI-6256382; Score: 0.35
DE  Interaction: Q61166; IntAct: EBI-8062428; Score: 0.70
DE  Interaction: Q99IB8; IntAct: EBI-6928217; Score: 0.37
DE  Interaction: Q9H8S9; IntAct: EBI-8798967; Score: 0.27
DE  Interaction: Q7L9L4; IntAct: EBI-8799069; Score: 0.27
DE  Interaction: O00161; IntAct: EBI-11294079; Score: 0.37
DE  Interaction: O41952; IntAct: EBI-9640619; Score: 0.37
DE  Interaction: P88986; IntAct: EBI-9640971; Score: 0.37
DE  Interaction: O41970; IntAct: EBI-9641577; Score: 0.37
DE  Interaction: Q9NQW6; IntAct: EBI-11009421; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062262; Score: 0.35
DE  Interaction: Q3UH45; IntAct: EBI-11090763; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11144042; Score: 0.35
DE  Interaction: Q5JU00; IntAct: EBI-11367780; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11390509; Score: 0.27
DE  Interaction: P49286; IntAct: EBI-11577533; Score: 0.00
DE  Interaction: Q67020; IntAct: EBI-11514491; Score: 0.37
DE  Interaction: P43355; IntAct: EBI-21634905; Score: 0.35
DE  Interaction: Q9H9Q2; IntAct: EBI-21739689; Score: 0.35
DE  Interaction: Q5SQX6; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P15311; IntAct: EBI-16791848; Score: 0.27
DE  Interaction: P49841; IntAct: EBI-16793176; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: P35408; IntAct: EBI-20811489; Score: 0.37
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: P05455; IntAct: EBI-20900824; Score: 0.40
DE  Interaction: Q02878; IntAct: EBI-20907504; Score: 0.40
DE  Interaction: O76021; IntAct: EBI-20920060; Score: 0.40
DE  Interaction: P50993; IntAct: EBI-20925034; Score: 0.40
DE  Interaction: Q12996; IntAct: EBI-20929904; Score: 0.40
DE  Interaction: Q9NPJ6; IntAct: EBI-25472202; Score: 0.27
DE  Interaction: Q14108; IntAct: EBI-21264396; Score: 0.35
DE  Interaction: Q96GC9; IntAct: EBI-21267986; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21302175; Score: 0.35
DE  Interaction: Q96AC1; IntAct: EBI-21387090; Score: 0.00
DE  Interaction: Q99459; IntAct: EBI-21387226; Score: 0.00
DE  Interaction: O60239; IntAct: EBI-21387213; Score: 0.00
DE  Interaction: Q96MT8; IntAct: EBI-21387200; Score: 0.00
DE  Interaction: P61764; IntAct: EBI-21387187; Score: 0.00
DE  Interaction: Q96BS2; IntAct: EBI-21387161; Score: 0.00
DE  Interaction: Q9BY11; IntAct: EBI-21387148; Score: 0.00
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
DE  Interaction: Q9Y5P2; IntAct: EBI-26354638; Score: 0.35
DE  Interaction: P06702; IntAct: EBI-27037935; Score: 0.37
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: P63252; IntAct: EBI-28956270; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q93009; IntAct: EBI-30842049; Score: 0.44
DE  Interaction: Q9NZR4; IntAct: EBI-29000642; Score: 0.35
DE  Interaction: P21709; IntAct: EBI-32720516; Score: 0.27
DE  Interaction: P29317; IntAct: EBI-32720711; Score: 0.27
DE  Interaction: P29320; IntAct: EBI-32720767; Score: 0.27
DE  Interaction: P21802; IntAct: EBI-32721907; Score: 0.27
DE  Interaction: Q06124; IntAct: EBI-32723738; Score: 0.27
DE  Interaction: P04629; IntAct: EBI-32724282; Score: 0.27
DE  Interaction: Q16620; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P16234; IntAct: EBI-32724889; Score: 0.27
DE  Interaction: P09619; IntAct: EBI-32724964; Score: 0.27
DE  Interaction: P34925; IntAct: EBI-32731802; Score: 0.27
DE  Interaction: Q6J9G0; IntAct: EBI-32731895; Score: 0.27
DE  Interaction: P38398; IntAct: EBI-34581773; Score: 0.35
GO  GO:0015629;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0009925;
GO  GO:0005604;
GO  GO:0005938;
GO  GO:0031252;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005925;
GO  GO:0031673;
GO  GO:0030056;
GO  GO:0016021;
GO  GO:0005882;
GO  GO:0045111;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0035371;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0005509;
GO  GO:0005178;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0008022;
GO  GO:0042803;
GO  GO:0005198;
GO  GO:0007155;
GO  GO:0048870;
GO  GO:0031122;
GO  GO:0007010;
GO  GO:0031581;
GO  GO:0007229;
GO  GO:0045104;
GO  GO:0030011;
GO  GO:0000226;
GO  GO:0009611;
GO  GO:0008090;
GO  GO:0042060;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDT
SQ  LPREKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLW
SQ  TQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDE
SQ  KSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIRHHVTTMSERTFPNNPVELKALYNQYLQFKETE
SQ  IPPKETEKSKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVERLEMLQQIANRVQRDSVIC
SQ  EDKLILAGNALQSDSKRLESGVQFQNEAEIAGYILECENLLRQHVIDVQILIDGKYYQADQLVQRVAKLRDEIMALRNEC
SQ  SSVYSKGRILTTEQTKLMISGITQSLNSGFAQTLHPSLTSGLTQSLTPSLTSSSMTSGLSSGMTSRLTPSVTPAYTPGFP
SQ  SGLVPNFSSGVEPNSLQTLKLMQIRKPLLKSSLLDQNLTEEEINMKFVQDLLNWVDEMQVQLDRTEWGSDLPSVESHLEN
SQ  HKNVHRAIEEFESSLKEAKISEIQMTAPLKLTYAEKLHRLESQYAKLLNTSRNQERHLDTLHNFVSRATNELIWLNEKEE
SQ  EEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYRAAMQTQWSWILQLCQCVEQH
SQ  IKENTAYFEFFNDAKEATDYLRNLKDAIQRKYSCDRSSSIHKLEDLVQESMEEKEELLQYKSTIANLMGKAKTIIQLKPR
SQ  NSDCPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVPPPNKEAVDLANRIEQQYQ
SQ  NVLTLWHESHINMKSVVSWHYLINEIDRIRASNVASIKTMLPGEHQQVLSNLQSRFEDFLEDSQESQVFSGSDITQLEKE
SQ  VNVCKQYYQELLKSAEREEQEESVYNLYISEVRNIRLRLENCEDRLIRQIRTPLERDDLHESVFRITEQEKLKKELERLK
SQ  DDLGTITNKCEEFFSQAAASSSVPTLRSELNVVLQNMNQVYSMSSTYIDKLKTVNLVLKNTQAAEALVKLYETKLCEEEA
SQ  VIADKNNIENLISTLKQWRSEVDEKRQVFHALEDELQKAKAISDEMFKTYKERDLDFDWHKEKADQLVERWQNVHVQIDN
SQ  RLRDLEGIGKSLKYYRDTYHPLDDWIQQVETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQKYAEQYSA
SQ  TVKDYELQTMTYRAMVDSQQKSPVKRRRMQSSADLIIQEFMDLRTRYTALVTLMTQYIKFAGDSLKRLEEEEKSLEEEKK
SQ  EHVEKAKELQKWVSNISKTLKDAEKAGKPPFSKQKISSEEISTKKEQLSEALQTIQLFLAKHGDKMTDEERNELEKQVKT
SQ  LQESYNLLFSESLKQLQESQTSGDVKVEEKLDKVIAGTIDQTTGEVLSVFQAVLRGLIDYDTGIRLLETQLMISGLISPE
SQ  LRKCFDLKDAKSHGLIDEQILCQLKELSKAKEIISAASPTTIPVLDALAQSMITESMAIKVLEILLSTGSLVIPATGEQL
SQ  TLQKAFQQNLVSSALFSKVLERQNMCKDLIDPCTSEKVSLIDMVQRSTLQENTGMWLLPVRPQEGGRITLKCGRNISILR
SQ  AAHEGLIDRETMFRLLSAQLLSGGLINSNSGQRMTVEEAVREGVIDRDTASSILTYQVQTGGIIQSNPAKRLTVDEAVQC
SQ  DLITSSSALLVLEAQRGYVGLIWPHSGEIFPTSSSLQQELITNELAYKILNGRQKIAALYIPESSQVIGLDAAKQLGIID
SQ  NNTASILKNITLPDKMPDLGDLEACKNARRWLSFCKFQPSTVHDYRQEEDVFDGEEPVTTQTSEETKKLFLSYLMINSYM
SQ  DANTGQRLLLYDGDLDEAVGMLLEGCHAEFDGNTAIKECLDVLSSSGVFLNNASGREKDECTATPSSFNKCHCGEPEHEE
SQ  TPENRKCAIDEEFNEMRNTVINSEFSQSGKLASTISIDPKVNSSPSVCVPSLISYLTQTELADISMLRSDSENILTNYEN
SQ  QSRVETNERANECSHSKNIQNFPSDLIENPIMKSKMSKFCGVNETENEDNTNRDSPIFDYSPRLSALLSHDKLMHSQGSF
SQ  NDTHTPESNGNKCEAPALSFSDKTMLSGQRIGEKFQDQFLGIAAINISLPGEQYGQKSLNMISSNPQVQYHNDKYISNTS
SQ  GEDEKTHPGFQQMPEDKEDESEIEEYSCAVTPGGDTDNAIVSLTCATPLLDETISASDYETSLLNDQQNNTGTDTDSDDD
SQ  FYDTPLFEDDDHDSLLLDGDDRDCLHPEDYDTLQEENDETASPADVFYDVSKENENSMVPQGAPVGSLSVKNKAHCLQDF
SQ  LMDVEKDELDSGEKIHLNPVGSDKVNGQSLETGSERECTNILEGDESDSLTDYDIVGGKESFTASLKFDDSGSWRGRKEE
SQ  YVTGQEFHSDTDHLDSMQSEESYGDYIYDSNDQDDDDDDGIDEEGGGIRDENGKPRCQNVAEDMDIQLCASILNENSDEN
SQ  ENINTMILLDKMHSCSSLEKQQRVNVVQLASPSENNLVTEKSNLPEYTTEIAGKSKENLLNHEMVLKDVLPPIIKDTESE
SQ  KTFGPASISHDNNNISSTSELGTDLANTKVKLIQGSELPELTDSVKGKDEYFKNMTPKVDSSLDHIICTEPDLIGKPAEE
SQ  SHLSLIASVTDKDPQGNGSDLIKGRDGKSDILIEDETSIQKMYLGEGEVLVEGLVEEENRHLKLLPGKNTRDSFKLINSQ
SQ  FPFPQITNNEELNQKGSLKKATVTLKDEPNNLQIIVSKSPVQFENLEEIFDTSVSKEISDDITSDITSWEGNTHFEESFT
SQ  DGPEKELDLFTYLKHCAKNIKAKDVAKPNEDVPSHVLITAPPMKEHLQLGVNNTKEKSTSTQKDSPLNDMIQSNDLCSKE
SQ  SISGGGTEISQFTPESIEATLSILSRKHVEDVGKNDFLQSERCANGLGNDNSSNTLNTDYSFLEINNKKERIEQQLPKEQ
SQ  ALSPRSQEKEVQIPELSQVFVEDVKDILKSRLKEGHMNPQEVEEPSACADTKILIQNLIKRITTSQLVNEASTVPSDSQM
SQ  SDSSGVSPMTNSSELKPESRDDPFCIGNLKSELLLNILKQDQHSQKITGVFELMRELTHMEYDLEKRGITSKVLPLQLEN
SQ  IFYKLLADGYSEKIEHVGDFNQKACSTSEMMEEKPHILGDIKSKEGNYYSPNLETVKEIGLESSTVWASTLPRDEKLKDL
SQ  CNDFPSHLECTSGSKEMASGDSSTEQFSSELQQCLQHTEKMHEYLTLLQDMKPPLDNQESLDNNLEALKNQLRQLETFEL
SQ  GLAPIAVILRKDMKLAEEFLKSLPSDFPRGHVEELSISHQSLKTAFSSLSNVSSERTKQIMLAIDSEMSKLAVSHEEFLH
SQ  KLKSFSDWVSEKSKSVKDIEIVNVQDSEYVKKRLEFLKNVLKDLGHTKMQLETTAFDVQFFISEYAQDLSPNQSKQLLRL
SQ  LNTTQKCFLDVQESVTTQVERLETQLHLEQDLDDQKIVAERQQEYKEKLQGICDLLTQTENRLIGHQEAFMIGDGTVELK
SQ  KYQSKQEELQKDMQGSAQALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKKELDKVVTTAIK
SQ  EETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDEVNGNLLETDVDGQVG
SQ  TTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLSPEEKEKLQKNMKELKVHYETALAESEKKMKLTHS
SQ  LQEELEKFDADYTEFEHWLQQSEQELENLEAGADDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRVLEAAKSCSKR
SQ  DGGKVDTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCGLLAGLQACEATASKHLSEPIAVDPK
SQ  NLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVNERNEKLQITLTRSL
SQ  SVQDGLDEMLDWMGNVESSLKEQGQVPLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMETTDPSTASSLQAKM
SQ  KDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQTFLETKTQALTEVDVPGKDVTELSQYMQESTSEFLEHKKHL
SQ  EVLHSLLKEISSHGLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVPIVQP
SQ  SFGAEDLGKSLEDTKKLQEKWSLKTPEIQKVNNSGISLCNLISAVTTPAKAIAAVKSGGAVLNGEGTATNTEEFWANKGL
SQ  TSIKKDMTDISHGYEDLGLLLKDKIAELNTKLSKLQKAQEESSAMMQWLQKMNKTATKWQQTPAPTDTEAVKTQVEQNKS
SQ  FEAELKQNVNKVQELKDKLTELLEENPDTPEAPRWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEAQLKQW
SQ  LVEKELMVSVLGPLSIDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSLRGIVKEQLAAVTQKWDSL
SQ  TGQLSDRCDWIDQAIVKSTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALC
SQ  EDLSALVKEEYLKAELSRQLEGILKSFKDVEQKAENHVQHLQSACASSHQFQQMSRDFQAWLDTKKEEQNKSHPISAKLD
SQ  VLESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESLEKALKY
SQ  KEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDENKSLI
SQ  QKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQALKHQVDL
SQ  AKRLAQDLVVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLETKLQGIGHFQNTIREMFSQFAEFDDELDSMAPV
SQ  GRDAETLQKQKETIKAFLKKLEALMASNDNANKTCKMMLATEETSPDLVGIKRDLEALSKQCNKLLDRAQAREEQVEGTI
SQ  KRLEEFYSKLKEFSILLQKAEEHEESQGPVGMETETINQQLNMFKVFQKEEIEPLQGKQQDVNWLGQGLIQSAAKSTSTQ
SQ  GLEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALESLLSWMVDTEELVANQKPPSAEFKVVKAQIQEQKLLQR
SQ  LLDDRKSTVEVIKREGEKIATTAEPADKVKILKQLSLLDSRWEALLNKAETRNRQLEGISVVAQQFHETLEPLNEWLTTI
SQ  EKRLVNCEPIGTQASKLEEQIAQHKALEDDIINHNKHLHQAVSIGQSLKVLSSREDKDMVQSKLDFSQVWYIEIQEKSHS
SQ  RSELLQQALCNAKIFGEDEVELMNWLNEVHDKLSKLSVQDYSTEGLWKQQSELRVLQEDILLRKQNVDQALLNGLELLKQ
SQ  TTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQALQLARRLHSTHEELCTWLDKVEVELLSYETQVLKGEEASQAQM
SQ  RPKELKKEAKNNKALLDSLNEVSSALLELVPWRAREGLEKMVAEDNERYRLVSDTITQKVEEIDAAILRSQQFDQAADAE
SQ  LSWITETEKKLMSLGDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEEKQSMKKKLDKVLKNYDT
SQ  ICQINSERYLQLERAQSLVNQFWETYEELWPWLTETQSIISQLPAPALEYETLRQQQEEHRQLRELIAEHKPHIDKMNKT
SQ  GPQLLELSPGEGFSIQEKYVAADTLYSQIKEDVKKRAVALDEAISQSTQFHDKIDQILESLERIVERLRQPPSISAEVEK
SQ  IKEQISENKNVSVDMEKLQPLYETLKQRGEEMIARSGGTDKDISAKAVQDKLDQMVFIWENIHTLVEEREAKLLDVMELA
SQ  EKFWCDHMSLIVTIKDTQDFIRDLEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAACGEPDKPIVKKS
SQ  IDELNSAWDSLNKAWKDRIDKLEEAMQAAVQYQDGLQAVFDWVDIAGGKLASMSPIGTDLETVKQQIEELKQFKSEAYQQ
SQ  QIEMERLNHQAELLLKKVTEESDKHTVQDPLMELKLIWDSLEERIINRQHKLEGALLALGQFQHALDELLAWLTHTEGLL
SQ  SEQKPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSAGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQ
SQ  LDGALRQAKGFHGEIEDLQQWLTDTERHLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKS
SQ  AETNIDQDINNLKEKWESVETKLNERKTKLEEALNLAMEFHNSLQDFINWLTQAEQTLNVASRPSLILDTVLFQIDEHKV
SQ  FANEVNSHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDDARKRAKQFHEAWSKLMEWL
SQ  EESEKSLDSELEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEKTSLADDNLKLDDMLSELRDKWDTICG
SQ  KSVERQNKLEEALLFSGQFTDALQALIDWLYRVEPQLAEDQPVHGDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARE
SQ  LIEGSRDDSSWVKVQMQELSTRWETVCALSISKQTRLEAALRQAEEFHSVVHALLEWLAEAEQTLRFHGVLPDDEDALRT
SQ  LIDQHKEFMKKLEEKRAELNKATTMGDTVLAICHPDSITTIKHWITIIRARFEEVLAWAKQHQQRLASALAGLIAKQELL
SQ  EALLAWLQWAETTLTDKDKEVIPQEIEEVKALIAEHQTFMEEMTRKQPDVDKVTKTYKRRAADPSSLQSHIPVLDKGRAG
SQ  RKRFPASSLYPSGSQTQIETKNPRVNLLVSKWQQVWLLALERRRKLNDALDRLEELREFANFDFDIWRKKYMRWMNHKKS
SQ  RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAYKPITDADKIED
SQ  EVTRQVAKCKCAKRFQVEQIGDNKYRFFLGNQFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRVHHHGSKML
SQ  RSESNSSITTTQPTIAKGRTNMELREKFILADGASQGMAAFRPRGRRSRPSSRGASPNRSTSVSSQAAQAASPQVPATTT
SQ  PKGTPIQGSKLRLPGYLSGKGFHSGEDSGLITTAAARVRTQFADSKKTPSRPGSRAGSKAGSRASSRRGSDASDFDISEI
SQ  QSVCSDVETVPQTHRPTPRAGSRPSTAKPSKIPTPQRKSPASKLDKSSKR
//
ID  Q91ZU6;
PN  Dystonin;
GN  Dst;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber. Cell projection, axon {ECO:0000269|PubMed:17287360}. Note=Associates with axonal microtubules at the growing distal tip and intermediate filaments, but not with actin cytoskeleton, in sensory neurons (By similarity). Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells. {ECO:0000250, ECO:0000269|PubMed:14576348}. [Isoform 1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19932097}. Note=Colocalizes both cortical and cytoplasmic actin filaments (PubMed:19932097). Localizes to vesicule- like structures associated with microtubules (PubMed:14581450, PubMed:17287360). {ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:19932097}. [Isoform 2]: Cell membrane, sarcolemma. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, sarcomere, H zone. Cytoplasm, cytoskeleton. Note=Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. [Isoform 5]: Cytoplasm, cytoskeleton. Cell junction, hemidesmosome. Note=Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes (By similarity). Localizes to actin and intermediate filaments cytoskeletons. {ECO:0000250}. [Isoform 6]: Nucleus. Nucleus envelope. Membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single- pass membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:14576348}. Note=Associates with actin cytoskeleton in sensory neurons (By similarity). Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus. {ECO:0000250}. [Isoform 7]: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Cell membrane; Lipid-anchor.
DR  UNIPROT: Q91ZU6;
DR  UNIPROT: E9PXE5;
DR  UNIPROT: E9QL23;
DR  UNIPROT: Q1KP04;
DR  UNIPROT: Q3I6J6;
DR  UNIPROT: Q60824;
DR  UNIPROT: Q60845;
DR  UNIPROT: Q8K5D4;
DR  UNIPROT: Q91ZU7;
DR  UNIPROT: Q91ZU8;
DR  UNIPROT: Q9WU50;
DR  UNIPROT: S4R1U5;
DR  PDB: 2IAK;
DR  Pfam: PF00307;
DR  Pfam: PF13499;
DR  Pfam: PF02187;
DR  Pfam: PF00681;
DR  Pfam: PF17902;
DR  Pfam: PF00435;
DR  Pfam: PF18373;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51460;
DR  PROSITE: PS50002;
DE  Function: Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1. {ECO:0000269|PubMed:17287360}. [Isoform 5]: Plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity. [Isoform 6]: Required for bundling actin filaments around the nucleus.
DE  Reference Proteome: Yes;
DE  Interaction: P21807; IntAct: EBI-446225; Score: 0.54
DE  Interaction: P19527; IntAct: EBI-446339; Score: 0.37
DE  Interaction: P16884; IntAct: EBI-446356; Score: 0.37
DE  Interaction: O70589; IntAct: EBI-3647717; Score: 0.35
DE  Interaction: P35279; IntAct: EBI-11566531; Score: 0.35
DE  Interaction: Q4U2R1; IntAct: EBI-16730475; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0015629;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005938;
GO  GO:0031252;
GO  GO:0005737;
GO  GO:0009898;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005925;
GO  GO:0031673;
GO  GO:0030056;
GO  GO:0016021;
GO  GO:0014704;
GO  GO:0005882;
GO  GO:0045111;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0035371;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0097038;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0042383;
GO  GO:0001725;
GO  GO:0045098;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0005509;
GO  GO:0005178;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0008022;
GO  GO:0042803;
GO  GO:0005198;
GO  GO:0007409;
GO  GO:0007155;
GO  GO:0048870;
GO  GO:0031122;
GO  GO:0007010;
GO  GO:0031581;
GO  GO:0045104;
GO  GO:0046907;
GO  GO:0030011;
GO  GO:0000226;
GO  GO:0009611;
GO  GO:0008090;
GO  GO:0042060;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis;
SQ  MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDT
SQ  LPREKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLW
SQ  TQQATEGYAGVRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDE
SQ  KSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIRHHVVTMSERTFPNNPLELKALYNQYLQFKEKE
SQ  IPPKEMEKSKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVERLDMLQQIATRVQRDSVSC
SQ  EDKLILARNALQSDSKRLESGVQFQNEAEIAGYILECENLLRQHVIDVQILIDGKYYQADQLVQRVAKLRDEIMALRNEC
SQ  SSVYSKGRMLTTEQTKLMISGITQSLNSGFAQTLHPSLNSGLTQSLTPSLTSSSVTSGLSSGMTSRLTPSVTPVYAPGFP
SQ  SVVAPNFSLGVEPNSLQTLKLMQIRKPLLKSSLLDQNLTEEEVNMKFVQDLLNWVDEMQVQLDRTEWGSDLPSVESHLEN
SQ  HKNVHRAIEEFESSLKEAKISEIQMTAPLKLSYTDKLHRLESQYAKLLNTSRNQERHLDTLHNFVTRATNELIWLNEKEE
SQ  SEVAYDWSERNSSVARKKSYHAELMRELEQKEESIKAVQEIAEQLLLENHPARLTIEAYRAAMQTQWSWILQLCQCVEQH
SQ  IQENSAYFEFFNDAKEATDYLRNLKDAIQRKYSCDRSSSIHKLEDLVQESMEKEELLQYRSVVAGLMGRAKTVVQLKPRN
SQ  PDNPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVPPPNKEAVDFANRIEQQYQS
SQ  VLTLWHESHINMKSVVSWHYLVNEIDRIRASNVASIKTMLPGEHQQVLSNLQSRLEDFLEDSQESQIFSGSDISQLEKEV
SQ  SVCRKYYQELLKSAEREEQEESVYNLYISEVRNIRLRLESCEDRLIRQIRTPLERDDLHESMLRITEQEKLKKELDRLKD
SQ  DLGTITNKCEEFFSQAADSPSVPALRSELSVVIQSLSQIYSMSSTYIEKLKTVNLVLKNTQAAEALVKLYETKLCEEEAV
SQ  IADKNNIENLMSTLKQWRSEVDEKREVFHALEDELQKAKAISDEMFKTHKERDLDFDWHKEKADQLVERWQSVHVQIDNR
SQ  LRDLEGIGKSLKHYRDSYHPLDDWIQHIETTQRKIQENQPENSKALALQLNQQKMLVSEIEVKQSKMDECQKYSEQYSAA
SQ  VKDYELQTMTYRAMVESQQKSPVKRRRIQSSADLVIQEFMDLRTRYTALVTLMTQYIKFAGDSLKRLEEEEKSLDEEKKQ
SQ  HIEKAKELQKWVSNISKTLGDGEKAGKPLFSKQQMSSKEISTKKEQFSEALQTTQIFLAKHGDKLTEEERSDLEKQVKTL
SQ  QEGYNLLFSESLKQQELQPSGESKVPEKPDKVIAGTINQTTGEVLSVFQAVLRGLIDYETGIRLLEAQLVITGLISPELR
SQ  KCFDLRDAESHGLIDEQVLRQLKELNRAKQLISTASPTSIPVLDSLAQGMVSESMAIRVLEILLSAGPLLVPATGEHLTL
SQ  QQAFQQNLISSALFSKVLERQDTCKDLIDPCTSEKVSLTDMVQRSILQENTRMWLLPVRPQEAGRITLKCGRSVSILRAA
SQ  HEGLIDRETMFRLLGAQLLSGGLIDCNSGQKMTVEEAVAEGVIDRDTASSILTYQVQTGGIVHSNPAKRLTVDEAVQCEL
SQ  ITSSSALLVLEAQRGYVGLIWPHSGEIFPTSSSLQQELITNELASKILNGRQKIAALYIPESSQVIGLDAAKQLGIIDNN
SQ  TASVLKSVTLPDKMPDLGDLEDCKNAKRWLSFCKLQPSTVHDYRQEEGGSDGEEPVTAQSSEQTKKLFLSYLMVNSYMDA
SQ  HTGQRLLLYDGDLDEAVGMLLESCGTELGADTSTRESLSVLTIPDAFPDCALSEEKHECSAAAAGPDKCHYSHPGHKESL
SQ  ENAKWDMNEAFCKMGNNDSNGELPRPENLADTTVVQKGSESPSRVRVPKPTSSSTQPEGSVLRPESGSILKGCKSQSEPV
SQ  TKKYPDGANHSHFLTSETSRPCDSNEREDEENIQKGPSVFDYSPRLSALLSHDELRQSQGRFSDTSTPQNTGYLCEASTL
SQ  SPSDQRVLADQSTREKFQDQFLGIAAISVSLQGAPCGQKPVDTECSSSQVHYHSEESMSDASAESGATRQTDESEKTGSK
SQ  VEDNSCTMVPGGGSRNDNTSDCGPLSHKGAIDAGDYETSLLAGQQSDTATDSDSDDYFYDTPLFEDEDHDSLILQGDDRD
SQ  CLQPEDYDTSLQEENDRTPPPDDIFYDVMKEKENPEFPHGGMDESLGVENKVCCPQGFPVGIEKPELYLAGEKEFNSGGS
SQ  EQLVESVSESENPPGLWDSESDSLTEGEIIGRKERLGASLTPDGHWRGDREECDTSRESQSDTDGVGSIQSSESYRPYMS
SQ  DGSDLDEEDNGGRSSEDSGDGRGGQGVADEGGEPQYQADPTQLYTAIRKEHGGETQNVSDMIPLDKTHSYSPLETQHGAG
SQ  VFQPESAGRGGWDTERSSHPELTTEADEEDEASLSTHMATKGVSLSNAEGTASEEIRLVQGPDSTGILKAEDLENVSPEI
SQ  SPSSDNIVRSEAELGGGASEDGHLSFTGSDRDQQGPGRGLVKGRDGQSDKLVDETSIREMGFQKEGVLMSSPEEGGEEER
SQ  DLEPFPNGSATESLNMGKSQVPPLLTHTEELSHRGAPHTTTMTTTMTLEGEAKNVQTGLTESPVLLETLAEIFDTPASKV
SQ  TRADLTSAVTASEMKSQVKEDSLTGGPEKETGPCTSLGHCDKCIHVDMLEPNEHTPSCALVAPPTVKDNLCSVNNAGEKS
SQ  VRPQEDWPPAAEVRLSDACVEESISEGKAGILQFTPENSDSTLSRLPHQSVAGWGKSADSVQARLPVSGVRHTSADTLDV
SQ  GCPQLESSREKASAEEEPHRERALSLKPQEREHHMLGFVEDGRSILKSSLDKVHMNLQEVGDPSAGTGTKISIQNLIRRA
SQ  ILSELPNEVSNVPSHGISPISNSSEVRAESGGDPFCITSFLHLLKQNQPPQETPGISELAKVLTQMDCDPEQRGLGSELL
SQ  PPQLKNAFYKLLFDGYATEKDQAEALGQTSCAVPKMAEEKPHVCSDLRNKEGHHCPLNPQAVGEAEVEPFSVHIAALPGG
SQ  EKLGELCSEPPEHSESTSGSKERSSDSSSKEKCSNGLQQCLQHTEKMHEYLVLLQDMKPPLDNQASVESSLEALKSQLKQ
SQ  LEAFELGLAPIAVFLRKDLKLAEEFLKSFPSDLPRRHHEELSKSHQRLQNAFSSLSSVSSERMKLIKLAINSEMSKLAVR
SQ  HEDFLHKLTSYSDWVSEKSRSVKAIQTVNVQDTELVKNSVKFLKNVLADLSHTKMQLETTAFDVQSFISDYAQDLSPSQS
SQ  RQLLRLLNTTQKGFLDLQELVTTEADRLEALLQLEQELGHQKVVAERQQEYREKLQGLCDLLTQTENRLISNQEAFVIGD
SQ  GTVELQKYQSKQEELQRDMQGSTQAMEEIVRNTELFLKESGDELSQADRALIEQKLNEVKMKCAQLNLKAEQSRKELDKA
SQ  VTTALKEETEKVAAVRQLEESKTKIENLLNWLSNVEEDSEGVWTKHTQPMEQNGTYLHEGDSKLGAGEEDEVNGNLLETD
SQ  AEGHSEATKGNLNQQYEKVKAQHGKIMAQHQAVLLATQSAQVLLEKQGHYLSPEEKEKLQKNTQELKVHYEKVLAECEKK
SQ  VKLTHSLQEELEKFDTDYSEFEHWLQQSEQELANLEAGADDLSGLMDKLTRQKSFSEDVISHKGDLRYITISGNRVIDAA
SQ  KSCSKRDSDRIGKDSVETSATHREVQTKLDQVTDRFRSLYSKCSVLGNNLKDLVDQYQQYEDASCGLLSGLQACEAKASK
SQ  HLREPIALDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDAKGSLLPAKNDIQKTLDDIVGRYDDLSKCVNERN
SQ  EKLQITLTRSLSVQDALDEMLDWMGSVESSLVKPGQVPLNSTALQDLISKDTMLEQDITGRQSSINAMNEKVKTFIETTD
SQ  PSTASSLQAKMKDLSARFSEASQKHKEKLAKMVELKAKVEQFEKLSDKLQTFLETQSQALTEVAMPGKDVPELSQHMQES
SQ  TAKFLEHRKDLEALHSLLKEISSHGLPGDKALVFEKTNNLSRKFKEMEDTIQEKKDALSSCQEQLSAFQTLAQSLKTWIK
SQ  ETTKQVPVVKPSLGTEDLRKSLEETKKLQEKWNLKAPEIHKANNSGVSLCNLLSALISPAKAIAAAKSGGVILNGEGTDT
SQ  NTQDFLANKGLTSIKKDMTDISHSYEDLGLLLKDKIVELNTKLSKLQKAQEESSAMMQWLEKMNKTASRWRQTPTPADTE
SQ  SVKLQVEQNKSFEAELKQNVNKVQELKDKLSELLEENPEAPEAQSWKQALAEMDTKWQELNQLTMDRQQKLEESSNNLTQ
SQ  FQTTEAQLKQWLMEKELMVSVLGPLSIDPNMLNTQKQQVQILLQEFDTRKPQYEQLTAAGQGILSRPGEDPSLHGIVNEQ
SQ  LEAVTQKWDNLTGQLRDRCDWIDQAIVKSTQYQSLLRSLSGTLTELDDKLSSGLTSGALPDAVNQQLEAAQRLKQEIEQQ
SQ  APKIKEAQEVCEDLSALVKEEYLKAELSRQLEGILKSFKDIEQKTENHVQHLQSACASSHQFQQMSKDFQAWLDAKKEEQ
SQ  RDSPPISAKLDVLESLLNSQKDFGKTFTEQSNIYEKTISEGENLLLKTQGAEKAALQLQLNTMKTDWDRFRKQVKEREEK
SQ  LKDSLEKALKYREQVETLRPWIDRCQHSLDGVTFSLDPTESESSIAELKSLQKEMDHHFGMLELLNNTANSLLSVCEVDK
SQ  EAVTEENQSLMEKVNRVTEQLQSKTVSLENMAQKFKEFQEVSRDTQRQLQDTKEQLEVHHSLGPQAYSNKHLSVLQAQQK
SQ  SLQTLKQQVDEAKRLAQDLVVEAADSKGTSDVLLQAETLAEEHSELSQQVDEKCSFLETKLQGLGHFQNTIREMFSQFTE
SQ  CDDELDGMAPVGRDAETLRKQKACMQTFLKKLEALMASNDSANRTCKMMLATEETSPDLIGVKRDLEALSKQCNKLLDRA
SQ  KTREEQVDGATEKLEEFHRKLEEFSTLLQKAEEHEESQGPVGTETETINQQLDVFKVFQKEEIEPLQVKQQDVNWLGQGL
SQ  IQSAAANTCTQGLEHDLDSVNSRWKTLNKKVAQRTSQLQEALLHCGRFQDALESLLSWMADTEELVANQKPPSAEFKVVK
SQ  AQIQEQKLLQRLLEDRKSTVEVIKREGEKIAASAEPADRVKLTRQLSLLDSRWEALLSRAEARNRQLEGISVVAQEFHET
SQ  LEPLNEWLTAVEKKLANSEPIGTQAPKLEEQISQHKALQEDILLRKQSVDQALLNGLELLKQTTGDEVLIIQDKLEAIKA
SQ  RYKDITKLSADVAKTLEHALQLAGQLQSMHKELCNWLDKVEVELLSYETQGLKGEAASQVQERQKELKNEVRSNKALVDS
SQ  LNEVSSALLELVPWRAREGLEKTIAEDNERYRLVSDTITQKVEEIDAAILRSQQFEQAADAELSWITETQKKLMSLGDIR
SQ  LEQDQTSAQLQVQKAFTMDILRHKDIIDELVTSGHKIMTTSSEEEKQSMKKKLDKVLKKYDAVCQINSERHLQLERAQSL
SQ  VSQFWETYEELWPWLTETQRIISQLPAPALEYETLRRQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPKEGIYIQEK
SQ  YVAADTLYSQIKEDVKKRAVVLDEAISQSTQFHDKIDQILESLERIAERLRQPPSISAEVEKIKEQIGENKSVSVDMEKL
SQ  QPLYETLRQRGEEMIARSEGTEKDVSARAVQDKLDQMVFIWGSIHTLVEEREAKLLDVMELAEKFWCDHMSLVVTIKDTQ
SQ  DFIRDLEDPGIDPSVVKQQQEAAEAIREEIDGLQEELDMVITLGSELIAACGEPDKPIVKKSIDELNSAWDSLNKAWKDR
SQ  VDRLEEAMQAAVQYQDGLQGIFDWVDIAGNKLATMSPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKV
SQ  TEEADKHTVQDPLMELKLIWDSLDERIVSRQHKLEGALLALGQFQHALDELLAWLTHTKGLLSEQKPVGGDPKAIEIELA
SQ  KHHVLQNDVLAHQSTVEAVNKAGNDLIESSEGEEASNLQYKLRILNQRWQDILEKTDQRKQQLDSALRQAKGFHGEIEDL
SQ  QQWLTDTERHLLASKPLGGLPETAKEQLNAHMEVCTAFAIKEETYKSLMLRGQQMLARCPRSAETNIDQDITNLKEKWES
SQ  VKSKLNEKKTKLEEALHLAMNFHNSLQDFINWLTQAEQTLNVASRPSLILDTILFQIDEHKVFANEVNSHREQIIELDKT
SQ  GTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDEARKRAKQFHEAWSKLMEWLEESEKSLDSELEIANDPD
SQ  KIKAQLVQHKEFQKSLGGKHSVYDTTNRTGRSLKEKTSLADDNLKLDNMLSELRDKWDTICGKSVERQNKLEEALLFSGQ
SQ  FTDALQALIDWLYRVEPQLAEDQPVHGDIDLVMNLIDNHKVFQKELGKRTSSVQALKRSARELIEGSRDDSSWVRVQMQE
SQ  LSTRWETVCALSISKQTRLESALQQAEEFHSVVHTLLEWLAEAEQTLRFHGALPDDEDALRTLIEQHKEFMKRLEEKRAE
SQ  LSKATGMGDALLAVCHPDSITTIKHWITIIQARFEEVLAWAKQHQQRLAGALAGLIAKQELLETLLAWLQWAETTLTEKD
SQ  KEVIPQEIEEVKTLIAEHQTFMEEMTRKQPDVDKVTKTYKRRATDPPSLQSHIPVLDKGRAGRKRFPASGFYPSGSQTQI
SQ  ETKNPRVNLLVSKWQQVWLLALERRRKLNDALDRLEELREFANFDFDIWRKKYMRWMNHKKSRVMDFFRRIDKDQDGKIT
SQ  RQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAYKPITDADKIEDEVTRQVAKCKCAKRFQVE
SQ  QIGDNKYRFFLGNQFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRVHHHGSKMLRSESNSSITATQPTLAKG
SQ  RTNMELREKFILADGASQGMAAFRPRGRRSRPSSRGASPNRSTSASSHACQAASPPVPAAASTPKGTPIQGSKLRLPGYL
SQ  SGKGFHSGEDSALITTAAARVRTQFAESRKTPSRPGSRAGSKAGSRASSRRGSDASDFDISEIQSVCSDVETVPQTHRPV
SQ  PRAGSRPSTAKPSKIPTPQRRSPASKLDKSSKR
//
ID  P03247;
PN  E1B protein, small T-antigen;
GN  E1B;
OS  10515;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0416;
SL  Comments: Host cell membrane {ECO:0000250}. Host nucleus envelope {ECO:0000250}. Host nucleus lamina {ECO:0000250}. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. {ECO:0000250}.
DR  UNIPROT: P03247;
DR  Pfam: PF01691;
DR  PROSITE: PS50062;
DE  Function: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: O60238; IntAct: EBI-849900; Score: 0.65
DE  Interaction: P02545; IntAct: EBI-849870; Score: 0.37
DE  Interaction: Q16611; IntAct: EBI-849884; Score: 0.37
DE  Interaction: Q12982; IntAct: EBI-849887; Score: 0.37
DE  Interaction: Q12983; IntAct: EBI-849890; Score: 0.49
GO  GO:0044165;
GO  GO:0044199;
GO  GO:0044203;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEAWECLEDFSAVRNLLEQSSNSTSWFWRFLWGSSQAKLVCRIKEDYKWEFEELLKSCGELFDSLNLGHQALFQEKVIKT
SQ  LDFSTPGRAAAAVAFLSFIKDKWSEETHLSGGYLLDFLAMHLWRAVVRHKNRLLLLSSVRPAIIPTEEQQQEEARRRRRQ
SQ  EQSPWNPRAGLDPRE
//
ID  P10406;
PN  E1B protein, small T-antigen;
GN  E1BS;
OS  28280;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0416;
SL  Comments: Host cell membrane {ECO:0000250}. Host nucleus envelope {ECO:0000250}. Host nucleus lamina {ECO:0000250}. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. {ECO:0000250}.
DR  UNIPROT: P10406;
DR  Pfam: PF01691;
DR  PROSITE: PS50062;
DE  Function: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044203;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEIWTVLEDFHKTRQLLENASNGVSHLWRFCFGGDLAKLVYRAKQDYREQFEDILRECPSLFDALNLGHQSHFNQRISRA
SQ  LDFTTPGRTTAAVAFFAFIFDKWSQETHFSRDYQLDFLAVALWRTWKCQRLNAIPATCRYSR
//
ID  P03246;
PN  E1B protein, small T-antigen;
GN  E1BS;
OS  28285;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0416;
SL  Comments: Host cell membrane. Host nucleus envelope. Host nucleus lamina. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina.
DR  UNIPROT: P03246;
DR  Pfam: PF01691;
DR  PROSITE: PS50062;
DE  Function: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates.
DE  Reference Proteome: No;
DE  Interaction: O15173; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9H2V7; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P62834; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P35813; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9NZM1; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: O95297; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P50281; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: O75695; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9Y6C9; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9BQB6; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q96IX5; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: O14773; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q96JJ7; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P42166; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q8N4L2; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9BTV4; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9NV96; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9HC07; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: O15533; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P46977; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q13586; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9Y5M8; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P08240; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9Y6N5; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q99523; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q15599; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P11166; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P60468; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: O75396; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q14108; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q969E2; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9NTJ5; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P06703; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9NQC3; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q14699; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9HBH5; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P51148; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9BZG1; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9NP72; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P53801; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q13308; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9HCU5; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: O60831; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: O75688; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: O00264; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P50479; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q96AQ6; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9Y639; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: O00483; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q6PIU2; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9BRK3; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q13724; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q14165; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q96N66; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P29966; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q6IAA8; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P05556; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P26006; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q16891; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q70UQ0; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P11717; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q8TED1; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P59768; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P62873; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9H4G4; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P48060; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P17302; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P25445; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: A0FGR8; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q969X5; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P17813; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: A4FU69; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q96KC8; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: O00273; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P39656; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q16527; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q1MSJ5; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q6UVK1; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P09543; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9H5V8; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P16070; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9BWT7; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P35613; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q07812; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q16611; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q8IZ07; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q8N2K0; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P80404; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q13323; IntAct: EBI-11735775; Score: 0.37
GO  GO:0044203;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEAWECLEDFSAVRNLLEQSSNSTSWFWRFLWGSSQAKLVCRIKEDYKWEFEELLKSCGELFDSLNLGHQALFQEKVIKT
SQ  LDFSTPGRAAAAVAFLSFIKDKWSEETHLSGGYLLDFLAMHLWRAVVRHKNRLLLLSSVRPAIIPTEEQQQQQEEARRRR
SQ  QEQSPWNPRAGLDPRE
//
ID  P03248;
PN  E1B protein, small T-antigen;
GN  E1BS;
OS  10519;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0416;
SL  Comments: Host cell membrane {ECO:0000250}. Host nucleus envelope {ECO:0000250}. Host nucleus lamina {ECO:0000250}. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. {ECO:0000250}.
DR  UNIPROT: P03248;
DR  Pfam: PF01691;
DR  PROSITE: PS50062;
DE  Function: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044203;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEVWAILEDLRQTRLLLENASDGVSGLWRFWFGGDLARLVFRIKQDYREEFEKLLDDIPGLFEALNLGHQAHFKEKVLSV
SQ  LDFSTPGRTAAAVAFLTFILDKWIRQTHFSKGYVLDFIAAALWRTWKARRMRTILDYWPVQPLGVAGILRHPPTMPAVLQ
SQ  EEQQEDNPRAGLDPPVEE
//
ID  P04492;
PN  E1B protein, small T-antigen;
GN  E1BS;
OS  28282;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0416;
SL  Comments: Host cell membrane {ECO:0000250}. Host nucleus envelope {ECO:0000250}. Host nucleus lamina {ECO:0000250}. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. {ECO:0000250}.
DR  UNIPROT: P04492;
DR  Pfam: PF01691;
DR  PROSITE: PS50062;
DE  Function: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044203;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELETVLQSFQSVRQLLQYTSKNTSGFWRYLFGSTLSKVVNRVKEDYREEFENILADCPGLLASLDLCYHLVFQEKVVRS
SQ  LDFSSVGRTVASIAFLATILDKWSEKSHLSWDYMLDYMSMQLWRAWLKRRVCIYSLARPLTMPPLPTLQEEKEEERNPAV
SQ  VEK
//
ID  P10543;
PN  E1B protein, small T-antigen;
GN  E1BS;
OS  28284;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0416;
SL  Comments: Host cell membrane {ECO:0000250}. Host nucleus envelope {ECO:0000250}. Host nucleus lamina {ECO:0000250}. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. {ECO:0000250}.
DR  UNIPROT: P10543;
DR  Pfam: PF01691;
DR  PROSITE: PS50062;
DE  Function: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044203;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELWSELQSYQNLRRLLELASARTSSCWRILFGSTLTNVIYRAKEEYSSRFADLLSHNPGIFASLNLGHHSFFQEIVIRN
SQ  LDFSSPGRTVSGLAFICFILDQWSAQTHLSQGYTLDYMAMALWRTLLRRKRVLGCLPAQRPHGLDPVQEEEEEEENLRAG
SQ  LDPSTEL
//
ID  P10544;
PN  E1B protein, small T-antigen;
GN  E1BS;
OS  10524;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0416;
SL  Comments: Host cell membrane {ECO:0000250}. Host nucleus envelope {ECO:0000250}. Host nucleus lamina {ECO:0000250}. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. {ECO:0000250}.
DR  UNIPROT: P10544;
DR  Pfam: PF01691;
DR  PROSITE: PS50062;
DE  Function: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044203;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0019050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEFWSELQSYQSLRRLLELASARTSSCWRFIFGSTLTNVIYRAKEDYSSRFAELLSFNPGIFASLNLGHHSFFQEIVIKN
SQ  LDFSSPGRTVSGLAFICFILDQWSAQTHLSEGYTLDYMTMALWRTLLRRKRVLGCSPAQPPHGLDPVREEEEEEEEEENL
SQ  RAGLDPQTEL
//
ID  P12827;
PN  Protein E26;
GN  DA26;
OS  46015;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000269|PubMed:17169392, ECO:0000269|PubMed:9448690}. Virion {ECO:0000269|PubMed:9448690}. Host cytoplasm {ECO:0000269|PubMed:17169392, ECO:0000269|PubMed:9448690}. Host nucleus {ECO:0000269|PubMed:17169392}. Note=Early in infection, localizes both in the host nucleus and cytoplasm while later in infection localizes in viral-induced microvesicles within the host nucleus. {ECO:0000269|PubMed:17169392}.
DR  UNIPROT: P12827;
DR  Pfam: PF11050;
DE  Function: Plays a role in the sorting of ODV envelope proteins to the host inner nuclear membrane. May facilitate the fusion and release of nucleocapsids into the cytoplasm. Modulates the expression levels of IE0 and IE1. {ECO:0000269|PubMed:17169392, ECO:0000269|PubMed:19019955, ECO:0000269|PubMed:19150105}.
DE  Reference Proteome: Yes;
GO  GO:0030430;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0044423;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESVQTRLCASSNQFAPFKKRQLAVPVGSVNSLTHTITSTTVTSVIPKNYQEKRQKICHIISSLRNTHLNFNKIQSVHKK
SQ  KLRHLQNLLRKKNEIIAELVRKLESAQKKTTHRNISKPAHWKYFGVVRCDNTIRTIIGNEKFVRRRLAELCTLYNAEYVF
SQ  CQARADGDKDRQALASLLTAAFGSRVIVYENSRRFEFINPDEIASGKRLIIKHLQDESQSDINAY
//
ID  P19525;
PN  Interferon-induced, double-stranded RNA-activated protein kinase;
GN  EIF2AK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:21029237, ECO:0000269|PubMed:22214662}. Nucleus {ECO:0000269|PubMed:21029237, ECO:0000269|PubMed:21072047}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15121867}. Note=Nuclear localization is elevated in acute leukemia, myelodysplastic syndrome (MDS), melanoma, breast, colon, prostate and lung cancer patient samples or cell lines as well as neurocytes from advanced Creutzfeldt- Jakob disease patients. {ECO:0000269|PubMed:21072047}.
DR  UNIPROT: P19525;
DR  UNIPROT: A8K3P0;
DR  UNIPROT: D6W584;
DR  UNIPROT: E9PC80;
DR  UNIPROT: Q52M43;
DR  UNIPROT: Q7Z6F6;
DR  UNIPROT: Q9UIR4;
DR  PDB: 1QU6;
DR  PDB: 2A19;
DR  PDB: 2A1A;
DR  PDB: 3UIU;
DR  PDB: 6D3K;
DR  PDB: 6D3L;
DR  Pfam: PF00035;
DR  Pfam: PF00069;
DR  PROSITE: PS50137;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 176871;
DR  OMIM: 618877;
DR  OMIM: 619687;
DR  DisGeNET: 5610;
DE  Function: IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (PubMed:18835251, PubMed:19507191, PubMed:19189853, PubMed:21123651, PubMed:21072047, PubMed:22948139, PubMed:23229543, PubMed:22381929). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2- alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (PubMed:19189853, PubMed:21123651, PubMed:22948139, PubMed:23229543). Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1) (PubMed:11836380, PubMed:19189853, PubMed:20171114, PubMed:19840259, PubMed:21710204, PubMed:23115276, PubMed:23399035). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11 (PubMed:11836380, PubMed:22214662, PubMed:19229320). In addition to serine/threonine- protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation (PubMed:20395957). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (PubMed:22948139, PubMed:23084476, PubMed:23372823). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (PubMed:10848580, PubMed:15121867, PubMed:15229216). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (PubMed:20685959). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (PubMed:20685959). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (PubMed:22801494). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (By similarity). {ECO:0000250|UniProtKB:Q03963, ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:11836380, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15229216, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:19189853, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19507191, ECO:0000269|PubMed:19840259, ECO:0000269|PubMed:20171114, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20685959, ECO:0000269|PubMed:21072047, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21710204, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:22381929, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948139, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:23115276, ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:23372823, ECO:0000269|PubMed:23399035, ECO:0000269|PubMed:32197074}.
DE  Disease: Leukoencephalopathy, developmental delay, and episodic neurologic regression syndrome (LEUDEN) [MIM:618877]: An autosomal dominant disorder characterized by global developmental delay apparent in early childhood, cognitive impairment, ataxia, poor or absent speech with dysarthria, hypotonia, hypertonia, extrapyramidal signs, tremor, and abnormal involuntary movements. Affected individuals also exhibit neurological regression in the setting of febrile illness or infection. Many patients have seizures. Brain imaging shows diffuse white matter abnormalities with poor myelination. {ECO:0000269|PubMed:32197074}. Note=The disease may be caused by variants affecting the gene represented in this entry. Dystonia 33 (DYT33) [MIM:619687]: A form of dystonia, a disorder defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYT33 is a slowly progressive form characterized by onset of focal or generalized dystonia in the first decades of life. Disease manifestations are variable. Some patients show ambulation difficulties, dysarthria, or dysphagia. Some affected individuals may manifest motor delay, lower limb spasticity, and mild developmental delay with intellectual disability. DYT33 penetrance is incomplete. Inheritance can be autosomal dominant or recessive. {ECO:0000269|PubMed:33236446, ECO:0000269|PubMed:33866603, ECO:0000269|PubMed:35146068}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O75569; IntAct: EBI-6116026; Score: 0.80
DE  Interaction: O92972; IntAct: EBI-6918687; Score: 0.40
DE  Interaction: P60953; IntAct: EBI-8612632; Score: 0.44
DE  Interaction: P62999; IntAct: EBI-8612643; Score: 0.44
DE  Interaction: Q27968; IntAct: EBI-640789; Score: 0.59
DE  Interaction: P06748; IntAct: EBI-6958371; Score: 0.46
DE  Interaction: Q9UJU6; IntAct: EBI-1080906; Score: 0.00
DE  Interaction: P05198; IntAct: EBI-1226418; Score: 0.78
DE  Interaction: P20639; IntAct: EBI-8674959; Score: 0.67
DE  Interaction: P35570; IntAct: EBI-2603511; Score: 0.44
DE  Interaction: P06493; IntAct: EBI-7909622; Score: 0.44
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: Q96C10; IntAct: EBI-6115711; Score: 0.50
DE  Interaction: Q8IY81; IntAct: EBI-6116026; Score: 0.62
DE  Interaction: P05455; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: P46087; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q9HCE1; IntAct: EBI-6116026; Score: 0.62
DE  Interaction: O00458; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q99848; IntAct: EBI-6116026; Score: 0.53
DE  Interaction: P07910; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: P56537; IntAct: EBI-6116026; Score: 0.50
DE  Interaction: Q13310; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q9NUL3; IntAct: EBI-6116026; Score: 0.62
DE  Interaction: Q9NZM5; IntAct: EBI-6116026; Score: 0.53
DE  Interaction: Q9BZE4; IntAct: EBI-6116026; Score: 0.53
DE  Interaction: Q9H0E2; IntAct: EBI-6116026; Score: 0.50
DE  Interaction: Q7L2E3; IntAct: EBI-6116026; Score: 0.71
DE  Interaction: Q9H0D6; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: P20248; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q9NSD9; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: O95793; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: O60812; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q8WTT2; IntAct: EBI-6116026; Score: 0.53
DE  Interaction: Q9UPY3; IntAct: EBI-6116026; Score: 0.50
DE  Interaction: Q9NX58; IntAct: EBI-6116026; Score: 0.53
DE  Interaction: Q8N5Z5; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q96CT7; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q00577; IntAct: EBI-6116026; Score: 0.53
DE  Interaction: P36873; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q15633; IntAct: EBI-6116026; Score: 0.50
DE  Interaction: Q6P2E9; IntAct: EBI-6116026; Score: 0.50
DE  Interaction: Q9Y285; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q9UL40; IntAct: EBI-6116026; Score: 0.62
DE  Interaction: P16403; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q00526; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: P11387; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q9BVP2; IntAct: EBI-6116026; Score: 0.35
DE  Interaction: Q08211; IntAct: EBI-6116026; Score: 0.50
DE  Interaction: P04591; IntAct: EBI-6178285; Score: 0.40
DE  Interaction: O00425; IntAct: EBI-6255714; Score: 0.35
DE  Interaction: Q9Y6M1; IntAct: EBI-6255714; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-6424177; Score: 0.40
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P04487; IntAct: EBI-6880922; Score: 0.59
DE  Interaction: P27958; IntAct: EBI-8765629; Score: 0.70
DE  Interaction: Q16543; IntAct: EBI-8770673; Score: 0.35
DE  Interaction: Q2HR71; IntAct: EBI-8876191; Score: 0.40
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q96FF9; IntAct: EBI-11027063; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: Q14108; IntAct: EBI-11072280; Score: 0.35
DE  Interaction: Q6PFD6; IntAct: EBI-11093571; Score: 0.35
DE  Interaction: Q6PJG2; IntAct: EBI-11106137; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: P78563; IntAct: EBI-25249266; Score: 0.56
DE  Interaction: P51608; IntAct: EBI-21532962; Score: 0.35
DE  Interaction: Q96SL4; IntAct: EBI-21714987; Score: 0.35
DE  Interaction: Q8N6M8; IntAct: EBI-21771054; Score: 0.35
DE  Interaction: P04798; IntAct: EBI-21774067; Score: 0.35
DE  Interaction: Q60803; IntAct: EBI-15560282; Score: 0.40
DE  Interaction: P53235; IntAct: EBI-15561786; Score: 0.44
DE  Interaction: P19525; IntAct: EBI-15561809; Score: 0.56
DE  Interaction: Q96P20; IntAct: EBI-15999105; Score: 0.60
DE  Interaction: O14862; IntAct: EBI-15999033; Score: 0.40
DE  Interaction: Q9C000; IntAct: EBI-15999201; Score: 0.40
DE  Interaction: Q9NPP4; IntAct: EBI-15999262; Score: 0.40
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.53
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: Q15628; IntAct: EBI-20936084; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-26877955; Score: 0.40
DE  Interaction: Q13283; IntAct: EBI-26877944; Score: 0.53
DE  Interaction: P0DTC9; IntAct: EBI-26948583; Score: 0.82
DE  Interaction: P59595; IntAct: EBI-26984718; Score: 0.40
DE  Interaction: K9N4V7; IntAct: EBI-26984727; Score: 0.40
DE  Interaction: Q9BY44; IntAct: EBI-26989881; Score: 0.40
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q9Y4W2; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9Y3T9; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9Y3C1; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9Y3B9; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9UKM9; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9UKD2; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9NW13; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9NVP1; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9NQ55; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9H7B2; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9H0A0; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9GZR7; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9BYG3; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9BU76; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q9BRT6; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q96SI9; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q96SB4; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q96KR1; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q96GQ7; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q96B26; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q8WTW3; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q8TDD1; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q8N9T8; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q8IZL8; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q1KMD3; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q15024; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q14690; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q14146; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q14137; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q13823; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q13523; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q12906; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q03701; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: Q01780; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: P55265; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: P51116; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: P30048; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: O95478; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: O75683; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: O60832; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: O60287; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: O43159; IntAct: EBI-28934478; Score: 0.35
DE  Interaction: O15226; IntAct: EBI-28934478; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005840;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0004694;
GO  GO:0042802;
GO  GO:0004715;
GO  GO:0004672;
GO  GO:0019888;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0003723;
GO  GO:0034198;
GO  GO:0051607;
GO  GO:0030968;
GO  GO:0045087;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0033689;
GO  GO:0017148;
GO  GO:0045071;
GO  GO:0032722;
GO  GO:0001819;
GO  GO:0043410;
GO  GO:0051092;
GO  GO:1901224;
GO  GO:0032874;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:1901532;
GO  GO:1902036;
GO  GO:1902033;
GO  GO:1900225;
GO  GO:0035455;
GO  GO:0009615;
GO  GO:0006412;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKK
SQ  AVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKL
SQ  AYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAK
SQ  RSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNI
SQ  VHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITK
SQ  GVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAE
SQ  LLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC
//
ID  Q03963;
PN  Interferon-induced, double-stranded RNA-activated protein kinase;
GN  Eif2ak2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P19525}. Nucleus {ECO:0000250|UniProtKB:P19525}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P19525}.
DR  UNIPROT: Q03963;
DR  UNIPROT: Q61742;
DR  UNIPROT: Q62026;
DR  PDB: 1X48;
DR  PDB: 1X49;
DR  Pfam: PF00035;
DR  Pfam: PF00069;
DR  PROSITE: PS50137;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (PubMed:20038207, PubMed:20478537, PubMed:21123651). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (PubMed:21123651, PubMed:20631127). Exerts its antiviral activity on a wide range of DNA and RNA viruses including west nile virus (WNV), sindbis virus (SV), foot-and-mouth virus (FMDV), semliki Forest virus (SFV) and lymphocytic choriomeningitis virus (LCMV) (PubMed:19264662, PubMed:20585572, PubMed:20631127, PubMed:21994357). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, and IRS1 (PubMed:19229320, PubMed:23403623). In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation (By similarity). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF- kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (PubMed:22948222, PubMed:23392680). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (By similarity). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (By similarity). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (By similarity). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (PubMed:22801494, PubMed:23401008). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (PubMed:22633459). {ECO:0000250|UniProtKB:P19525, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19264662, ECO:0000269|PubMed:20038207, ECO:0000269|PubMed:20478537, ECO:0000269|PubMed:20585572, ECO:0000269|PubMed:20631127, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21994357, ECO:0000269|PubMed:22633459, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948222, ECO:0000269|PubMed:23392680, ECO:0000269|PubMed:23401008, ECO:0000269|PubMed:23403623}.
DE  Reference Proteome: Yes;
DE  Interaction: P35569; IntAct: EBI-2603482; Score: 0.40
DE  Interaction: P35570; IntAct: EBI-2603524; Score: 0.44
DE  Interaction: Q8R4B8; IntAct: EBI-15999088; Score: 0.52
DE  Interaction: Q9EPB4; IntAct: EBI-15999182; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0004694;
GO  GO:0042802;
GO  GO:0004715;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0034198;
GO  GO:0051607;
GO  GO:0030968;
GO  GO:0045087;
GO  GO:0043066;
GO  GO:0033689;
GO  GO:0017148;
GO  GO:0045071;
GO  GO:0043065;
GO  GO:0032722;
GO  GO:0001819;
GO  GO:0043410;
GO  GO:0051092;
GO  GO:1901224;
GO  GO:0032874;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:1901532;
GO  GO:1902036;
GO  GO:1902033;
GO  GO:1900225;
GO  GO:0035455;
GO  GO:0032496;
GO  GO:0009636;
GO  GO:0009615;
GO  GO:0033197;
GO  GO:0006412;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASDTPGFYMDKLNKYRQMHGVAITYKELSTSGPPHDRRFTFQVLIDEKEFPEAKGRSKQEARNAAAKLAVDILDNENKV
SQ  DCHTSASEQGLFVGNYIGLVNSFAQKKKLSVNYEQCEPNSELPQRFICKCKIGQTMYGTGSGVTKQEAKQLAAKEAYQKL
SQ  LKSPPKTAGTSSSVVTSTFSGFSSSSSMTSNGVSQSAPGSFSSENVFTNGLGENKRKSGVKVSPDDVQRNKYTLDARFNS
SQ  DFEDIEEIGLGGFGQVFKAKHRIDGKRYAIKRVKYNTEKAEHEVQALAELNHVNIVQYHSCWEGVDYDPEHSMSDTSRYK
SQ  TRCLFIQMEFCDKGTLEQWMRNRNQSKVDKALILDLYEQIVTGVEYIHSKGLIHRDLKPGNIFLVDERHIKIGDFGLATA
SQ  LENDGKSRTRRTGTLQYMSPEQLFLKHYGKEVDIFALGLILAELLHTCFTESEKIKFFESLRKGDFSNDIFDNKEKSLLK
SQ  KLLSEKPKDRPETSEILKTLAEWRNISEKKKRNTC
//
ID  Q63184;
PN  Interferon-induced, double-stranded RNA-activated protein kinase;
GN  Eif2ak2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P19525}. Nucleus {ECO:0000250|UniProtKB:P19525}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P19525}.
DR  UNIPROT: Q63184;
DR  Pfam: PF00035;
DR  Pfam: PF00069;
DR  PROSITE: PS50137;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (By similarity). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF- 2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (By similarity). Exerts its antiviral activity on a wide range of DNA and RNA viruses (By similarity). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3 and IRS1 (By similarity). In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation (By similarity). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (By similarity). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (By similarity). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (By similarity). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (By similarity). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (By similarity). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (By similarity). {ECO:0000250|UniProtKB:P19525, ECO:0000250|UniProtKB:Q03963}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0004694;
GO  GO:0042802;
GO  GO:0004715;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0034198;
GO  GO:0051607;
GO  GO:0030968;
GO  GO:0045087;
GO  GO:0043066;
GO  GO:0033689;
GO  GO:0017148;
GO  GO:0045071;
GO  GO:0043065;
GO  GO:0032722;
GO  GO:0001819;
GO  GO:0043410;
GO  GO:0051092;
GO  GO:1901224;
GO  GO:0032874;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:1901532;
GO  GO:1902036;
GO  GO:1902033;
GO  GO:1900225;
GO  GO:0043330;
GO  GO:0035455;
GO  GO:0032496;
GO  GO:0009612;
GO  GO:0010033;
GO  GO:0009636;
GO  GO:0009615;
GO  GO:0033197;
GO  GO:0006412;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASDTPGFYVDKLNKYSQIHKVKIIYKEISVTGPPHDRRFTFQVIIEEREFPEGEGRSKQEAKNNAAKLAVEILDNENKV
SQ  DSHTDASEQGLIEGNYIGLVNSFAQKENLPVNFELCDPDSQLPHRFICKCKIGQTTYGTGFGANKKEAKQLAAKNAYQKL
SQ  SEKSPSKTGFVTSLSSDFSSSSSITSNSASQSASGRDFEDIFMNGLREKRKSGVKVPSDDVLRNKYTLDDRFSKDFEDIE
SQ  EIGSGGFGQVFKAKHRIDGKTYAIKRITYNTKKAKREVQALAELNHANIVQYRVCWEGEDYDYDPENSTNGDTSRYKTRC
SQ  LFIQMEFCDKGTLQQWLEKRNRSQEDKALVLELFEQIVTGVDYIHSKGLIHRDLKPGNIFLVDEKHIKIGDFGLATALEN
SQ  DGNPRTKYTGTPQYMSPEQKSSLVEYGKEVDIFALGLILAELLHICKTDSEKIEFFQLLRNGIFSDDIFDNKEKSLLQKL
SQ  LSSKPRERPNTSEILKTLAEWKNISEKKKRNTC
//
ID  P11317;
PN  Early E3 9.0 kDa glycoprotein;
GN  E311;
OS  45659;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: P11317;
DE  Function: 
DE  Reference Proteome: No;
GO  GO:0044200;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MILFQSNTTTSYAYTNIQPKYAMQLEITILIVIGILILSVILYFIFCRQIPNVHRNSKRRPIYSPMISRPHMALNEI
//
ID  P17590;
PN  Early E3A 10.5 kDa glycoprotein;
GN  E311;
OS  28285;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host nucleus membrane; Single-pass membrane protein.
DR  UNIPROT: P17590;
DR  Pfam: PF05393;
DE  Function: 
DE  Reference Proteome: No;
GO  GO:0044200;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTNTTNAAAATGLTSTTNTPQVSAFVNNWDNLGMWWFSIALMFVCLIIMWLICCLKRKRARPPIYSPIIVLHPNNDGIHR
SQ  LDGLKHMFFSLTV
//
ID  O55653;
PN  Early E3A 11.6 kDa glycoprotein;
GN  E311;
OS  10534;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host nucleus membrane; Single-pass membrane protein.
DR  UNIPROT: O55653;
DR  Pfam: PF05393;
DE  Function: 
DE  Reference Proteome: No;
GO  GO:0044200;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTGSTIAPTTDYRNTTATGLKSALNLPQVHAFVNDWASLGMWWFSIALMFVCLIIMWLICCLKRRRARPPIYRPIIVLNP
SQ  HNEKIHRLDGLKPCSLLLQYD
//
ID  P17592;
PN  Early E3 7.7 kDa protein;
GN  E311;
OS  10519;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Host nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: P17592;
DE  Function: 
DE  Reference Proteome: No;
GO  GO:0044200;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MILFQSNTTNTINVQTTLNHDMENHTTSYAYINIQPKYAMHLKITILIVIGILILSVILYFLFSYD
//
ID  Q60490;
PN  3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase;
GN  EBP;
OS  10141;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:7961902}; Multi-pass membrane protein {ECO:0000305|PubMed:7961902}. Nucleus envelope {ECO:0000250|UniProtKB:Q15125}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q15125}. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q15125}.
DR  UNIPROT: Q60490;
DR  UNIPROT: Q9QV23;
DR  PROSITE: PS51751;
DE  Function: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000250|UniProtKB:Q15125}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0000247;
GO  GO:0047750;
GO  GO:0042802;
GO  GO:0004769;
GO  GO:0006695;
GO  GO:0030097;
GO  GO:0043931;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATTSTGPLHPYWPRHLRLDHFVPNDLSAWYIVTVLFTVFGALVVTMWLLSSRASVVPLGTWRRLSVCWFAVCAFVHLVI
SQ  EGWFVLYQKAILGDQAFLSQLWKEYAKGDSRYIIEDNFIICMESITVVLWGPLSLWAVIAFLRQHPSRYVLQFVISLGQI
SQ  YGDLLYFLTEYRDGFQHGEMGHPIYFWFYFFFMNVLWLVIPGVLFFDSVKQFYGAQNALDTKVMKSKGK
//
ID  Q15125;
PN  3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase;
GN  EBP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10406945}; Multi-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:10406945}. Cytoplasmic vesicle {ECO:0000269|PubMed:10406945}. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles. {ECO:0000269|PubMed:10406945}.
DR  UNIPROT: Q15125;
DR  UNIPROT: Q6FGL3;
DR  UNIPROT: Q6IBI9;
DR  PDB: 6OHT;
DR  PDB: 6OHU;
DR  PROSITE: PS51751;
DR  OMIM: 300205;
DR  OMIM: 300960;
DR  OMIM: 302960;
DR  DisGeNET: 10682;
DE  Function: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000269|PubMed:12760743, ECO:0000269|PubMed:8798407, ECO:0000269|PubMed:9894009}.
DE  Disease: Chondrodysplasia punctata 2, X-linked dominant (CDPX2) [MIM:302960]: A clinically and genetically heterogeneous disorder characterized by punctiform calcification of the bones. The key clinical features of CDPX2 are chondrodysplasia punctata, linear ichthyosis, cataracts and short stature. CDPX2 is a rare disorder of defective cholesterol biosynthesis, biochemically characterized by an increased amount of 8-dehydrocholesterol and cholest-8(9)-en-3-beta-ol in the plasma and tissues. {ECO:0000269|PubMed:10391218, ECO:0000269|PubMed:10391219, ECO:0000269|PubMed:10942423, ECO:0000269|PubMed:11493318, ECO:0000269|PubMed:18176751, ECO:0000269|PubMed:25814754}. Note=The disease is caused by variants affecting the gene represented in this entry. MEND syndrome (MEND) [MIM:300960]: An X-linked recessive disorder associated with a defect in sterol biosynthesis. Disease manifestations and severity are highly variable. Clinical features include intellectual disability, short stature, scoliosis, digital abnormalities, cataracts, and dermatologic abnormalities. {ECO:0000269|PubMed:12503101, ECO:0000269|PubMed:20949533, ECO:0000269|PubMed:24459067, ECO:0000269|PubMed:24700572}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: A0PK00; IntAct: EBI-24669908; Score: 0.56
DE  Interaction: P0DTD1; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q05397; IntAct: EBI-20903608; Score: 0.40
DE  Interaction: O75030; IntAct: EBI-3915259; Score: 0.37
DE  Interaction: Q9WMX2; IntAct: EBI-9083439; Score: 0.37
DE  Interaction: Q9Z1B5; IntAct: EBI-10996176; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-11044830; Score: 0.35
DE  Interaction: Q92542; IntAct: EBI-11046886; Score: 0.35
DE  Interaction: O75446; IntAct: EBI-11060854; Score: 0.35
DE  Interaction: Q8BGH2; IntAct: EBI-11097023; Score: 0.35
DE  Interaction: Q9R0Q3; IntAct: EBI-11111571; Score: 0.35
DE  Interaction: Q8K1S6; IntAct: EBI-11147685; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: P49286; IntAct: EBI-11576336; Score: 0.37
DE  Interaction: P27105; IntAct: EBI-12452286; Score: 0.51
DE  Interaction: Q5T700; IntAct: EBI-24310594; Score: 0.56
DE  Interaction: Q8WWP7; IntAct: EBI-24268159; Score: 0.56
DE  Interaction: P02724; IntAct: EBI-22752401; Score: 0.56
DE  Interaction: Q8IXM6; IntAct: EBI-22753239; Score: 0.56
DE  Interaction: Q9BXJ8; IntAct: EBI-22754310; Score: 0.56
DE  Interaction: Q8IWU4; IntAct: EBI-22754620; Score: 0.56
DE  Interaction: Q9BWM7; IntAct: EBI-22754569; Score: 0.56
DE  Interaction: Q6UX98; IntAct: EBI-24270634; Score: 0.56
DE  Interaction: O95167; IntAct: EBI-24271223; Score: 0.56
DE  Interaction: P23141; IntAct: EBI-22757994; Score: 0.56
DE  Interaction: Q08426; IntAct: EBI-22758661; Score: 0.56
DE  Interaction: Q9NVC3; IntAct: EBI-22759787; Score: 0.56
DE  Interaction: Q6P1K1; IntAct: EBI-22760233; Score: 0.56
DE  Interaction: Q9H2L4; IntAct: EBI-24272883; Score: 0.56
DE  Interaction: Q96G79; IntAct: EBI-22760053; Score: 0.56
DE  Interaction: Q96BA8; IntAct: EBI-24631155; Score: 0.56
DE  Interaction: Q96GQ5; IntAct: EBI-24659828; Score: 0.56
DE  Interaction: Q9NRX6; IntAct: EBI-24660186; Score: 0.56
DE  Interaction: Q3SXY8; IntAct: EBI-23669642; Score: 0.56
DE  Interaction: Q9BU79; IntAct: EBI-24661627; Score: 0.56
DE  Interaction: Q9NZG7; IntAct: EBI-24663072; Score: 0.56
DE  Interaction: P23763; IntAct: EBI-24664214; Score: 0.56
DE  Interaction: P63027; IntAct: EBI-24667622; Score: 0.56
DE  Interaction: Q9Y385; IntAct: EBI-24670704; Score: 0.56
DE  Interaction: P01031; IntAct: EBI-23688881; Score: 0.56
DE  Interaction: A5PKU2; IntAct: EBI-24671905; Score: 0.56
DE  Interaction: Q13190; IntAct: EBI-24673341; Score: 0.56
DE  Interaction: Q96CP7; IntAct: EBI-24673683; Score: 0.56
DE  Interaction: O75396; IntAct: EBI-24674462; Score: 0.56
DE  Interaction: B2RUZ4; IntAct: EBI-24675325; Score: 0.56
DE  Interaction: O43759; IntAct: EBI-24676164; Score: 0.56
DE  Interaction: P81534; IntAct: EBI-24677503; Score: 0.56
DE  Interaction: Q8TBM7; IntAct: EBI-24681654; Score: 0.56
DE  Interaction: O14653; IntAct: EBI-24684144; Score: 0.56
DE  Interaction: P07204; IntAct: EBI-24684847; Score: 0.56
DE  Interaction: Q8N2H4; IntAct: EBI-24685442; Score: 0.56
DE  Interaction: Q9Y342; IntAct: EBI-24686559; Score: 0.56
DE  Interaction: Q7Z4F1; IntAct: EBI-23718808; Score: 0.56
DE  Interaction: P43378; IntAct: EBI-24688841; Score: 0.56
DE  Interaction: P17152; IntAct: EBI-24690030; Score: 0.56
DE  Interaction: O95870; IntAct: EBI-24690968; Score: 0.56
DE  Interaction: Q8N6S5; IntAct: EBI-24694418; Score: 0.56
DE  Interaction: Q9NV29; IntAct: EBI-24695294; Score: 0.56
DE  Interaction: Q16873; IntAct: EBI-23732251; Score: 0.56
DE  Interaction: Q96BZ9; IntAct: EBI-24696326; Score: 0.56
DE  Interaction: P30519; IntAct: EBI-23733774; Score: 0.56
DE  Interaction: Q9NW97; IntAct: EBI-24698352; Score: 0.56
DE  Interaction: Q9Y6X1; IntAct: EBI-24698993; Score: 0.56
DE  Interaction: Q96LL9; IntAct: EBI-24699507; Score: 0.56
DE  Interaction: Q86Y82; IntAct: EBI-24702845; Score: 0.56
DE  Interaction: Q92982; IntAct: EBI-24703744; Score: 0.56
DE  Interaction: P49447; IntAct: EBI-24704221; Score: 0.56
DE  Interaction: Q8N2M4; IntAct: EBI-24706015; Score: 0.56
DE  Interaction: Q8N8N0; IntAct: EBI-24705925; Score: 0.56
DE  Interaction: Q8NBD8; IntAct: EBI-24706316; Score: 0.56
DE  Interaction: Q8TD22; IntAct: EBI-24707774; Score: 0.56
DE  Interaction: Q9UGM5; IntAct: EBI-24708280; Score: 0.56
DE  Interaction: O75379; IntAct: EBI-24711580; Score: 0.56
DE  Interaction: Q9HD20; IntAct: EBI-24716721; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-24716697; Score: 0.56
DE  Interaction: Q969S6; IntAct: EBI-24716998; Score: 0.56
DE  Interaction: O95452; IntAct: EBI-24717966; Score: 0.56
DE  Interaction: Q6ZSS7; IntAct: EBI-24719764; Score: 0.56
DE  Interaction: Q96F15; IntAct: EBI-23774914; Score: 0.56
DE  Interaction: Q9Y282; IntAct: EBI-24721575; Score: 0.56
DE  Interaction: Q969E2; IntAct: EBI-24722338; Score: 0.56
DE  Interaction: Q9BZL3; IntAct: EBI-24722570; Score: 0.56
DE  Interaction: Q15125; IntAct: EBI-24723056; Score: 0.56
DE  Interaction: Q9Y5Z9; IntAct: EBI-24725377; Score: 0.56
DE  Interaction: O15400; IntAct: EBI-23784204; Score: 0.56
DE  Interaction: O43169; IntAct: EBI-23784333; Score: 0.56
DE  Interaction: O14925; IntAct: EBI-24728082; Score: 0.56
DE  Interaction: Q12983; IntAct: EBI-24729517; Score: 0.56
DE  Interaction: Q15836; IntAct: EBI-24730650; Score: 0.56
DE  Interaction: P50281; IntAct: EBI-24732670; Score: 0.56
DE  Interaction: Q9BSR8; IntAct: EBI-24732968; Score: 0.56
DE  Interaction: Q9UNK0; IntAct: EBI-24732900; Score: 0.56
DE  Interaction: Q9P0L0; IntAct: EBI-24733627; Score: 0.56
DE  Interaction: Q8N661; IntAct: EBI-24733842; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-23803453; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-24740093; Score: 0.56
DE  Interaction: Q5BJF2; IntAct: EBI-24740501; Score: 0.56
DE  Interaction: Q9NV12; IntAct: EBI-24747854; Score: 0.56
DE  Interaction: Q7Z5P4; IntAct: EBI-23821019; Score: 0.56
DE  Interaction: Q9NRQ5; IntAct: EBI-24750511; Score: 0.56
DE  Interaction: Q96EC8; IntAct: EBI-24751251; Score: 0.56
DE  Interaction: Q6PI78; IntAct: EBI-24752570; Score: 0.56
DE  Interaction: Q7L5A8; IntAct: EBI-24753438; Score: 0.56
DE  Interaction: Q8NHS1; IntAct: EBI-24753392; Score: 0.56
DE  Interaction: Q9NWH2; IntAct: EBI-24756813; Score: 0.56
DE  Interaction: Q9NX14; IntAct: EBI-24756945; Score: 0.56
DE  Interaction: Q9BTX3; IntAct: EBI-24763251; Score: 0.56
DE  Interaction: P60033; IntAct: EBI-24764608; Score: 0.56
DE  Interaction: Q9BVK8; IntAct: EBI-24764734; Score: 0.56
DE  Interaction: Q9H1M4; IntAct: EBI-24765471; Score: 0.56
DE  Interaction: Q9UHE5; IntAct: EBI-24765482; Score: 0.56
DE  Interaction: Q9P0S3; IntAct: EBI-24766077; Score: 0.56
DE  Interaction: Q9UKR5; IntAct: EBI-24767459; Score: 0.56
DE  Interaction: A2RU14; IntAct: EBI-24768914; Score: 0.56
DE  Interaction: Q68G75; IntAct: EBI-24769184; Score: 0.56
DE  Interaction: Q86W74; IntAct: EBI-24769830; Score: 0.56
DE  Interaction: Q9H2C2; IntAct: EBI-24779387; Score: 0.56
DE  Interaction: Q04941; IntAct: EBI-24781694; Score: 0.56
DE  Interaction: Q9H1C4; IntAct: EBI-24782065; Score: 0.56
DE  Interaction: O95393; IntAct: EBI-24782166; Score: 0.56
DE  Interaction: Q9Y5U4; IntAct: EBI-24782454; Score: 0.56
DE  Interaction: Q9H0R3; IntAct: EBI-24783086; Score: 0.56
DE  Interaction: O14523; IntAct: EBI-24783925; Score: 0.56
DE  Interaction: Q9NTJ5; IntAct: EBI-24784958; Score: 0.56
DE  Interaction: Q16617; IntAct: EBI-24785619; Score: 0.56
DE  Interaction: Q8WW34; IntAct: EBI-24786375; Score: 0.56
DE  Interaction: P61266; IntAct: EBI-24787698; Score: 0.56
DE  Interaction: Q9P0B6; IntAct: EBI-24795437; Score: 0.56
DE  Interaction: Q14318; IntAct: EBI-24797367; Score: 0.56
DE  Interaction: Q96IV6; IntAct: EBI-24797582; Score: 0.56
DE  Interaction: P25942; IntAct: EBI-23911966; Score: 0.56
DE  Interaction: Q2M3R5; IntAct: EBI-25279560; Score: 0.56
DE  Interaction: Q9BV81; IntAct: EBI-25282644; Score: 0.56
DE  Interaction: P08195; IntAct: EBI-25283560; Score: 0.56
DE  Interaction: Q9Y548; IntAct: EBI-25283492; Score: 0.56
DE  Interaction: Q53HI1; IntAct: EBI-23922913; Score: 0.56
DE  Interaction: Q9BWH2; IntAct: EBI-25286529; Score: 0.56
DE  Interaction: Q96AG4; IntAct: EBI-24548327; Score: 0.56
DE  Interaction: Q07108; IntAct: EBI-24594671; Score: 0.56
DE  Interaction: Q8N138; IntAct: EBI-24641145; Score: 0.56
DE  Interaction: Q8N511; IntAct: EBI-25145474; Score: 0.56
DE  Interaction: Q53FV1; IntAct: EBI-24641826; Score: 0.56
DE  Interaction: Q8NHW4; IntAct: EBI-24642201; Score: 0.56
DE  Interaction: P15151; IntAct: EBI-24644197; Score: 0.56
DE  Interaction: Q8WVV5; IntAct: EBI-24646926; Score: 0.56
DE  Interaction: P54849; IntAct: EBI-24647331; Score: 0.56
DE  Interaction: Q8IY26; IntAct: EBI-24647840; Score: 0.56
DE  Interaction: Q9NSU2; IntAct: EBI-24652174; Score: 0.56
DE  Interaction: Q99519; IntAct: EBI-24652828; Score: 0.56
DE  Interaction: Q01453; IntAct: EBI-24654227; Score: 0.56
DE  Interaction: P55061; IntAct: EBI-24654827; Score: 0.56
DE  Interaction: Q8WVX3; IntAct: EBI-24654804; Score: 0.56
DE  Interaction: Q9Y5U9; IntAct: EBI-24656328; Score: 0.56
DE  Interaction: Q6UX34; IntAct: EBI-24657064; Score: 0.56
DE  Interaction: P57105; IntAct: EBI-24659444; Score: 0.56
DE  Interaction: Q96JW4; IntAct: EBI-24746616; Score: 0.56
DE  Interaction: Q5JX71; IntAct: EBI-24758742; Score: 0.56
DE  Interaction: Q5TGU0; IntAct: EBI-24762253; Score: 0.56
DE  Interaction: Q14802; IntAct: EBI-24774166; Score: 0.56
DE  Interaction: A0AVG3; IntAct: EBI-24776609; Score: 0.56
DE  Interaction: Q9NZ43; IntAct: EBI-24789687; Score: 0.56
DE  Interaction: Q7L5N7; IntAct: EBI-24790934; Score: 0.56
DE  Interaction: Q0VAQ4; IntAct: EBI-24790824; Score: 0.56
DE  Interaction: Q96MV1; IntAct: EBI-25203477; Score: 0.56
DE  Interaction: Q5J8X5; IntAct: EBI-24791226; Score: 0.56
DE  Interaction: Q8N6R1; IntAct: EBI-25205775; Score: 0.56
DE  Interaction: O95070; IntAct: EBI-24799738; Score: 0.56
DE  Interaction: P54315; IntAct: EBI-24800746; Score: 0.56
DE  Interaction: Q69YG0; IntAct: EBI-24801451; Score: 0.56
DE  Interaction: P29033; IntAct: EBI-24803571; Score: 0.56
DE  Interaction: Q9P0S9; IntAct: EBI-25216661; Score: 0.56
DE  Interaction: Q6UWT4; IntAct: EBI-24806821; Score: 0.56
DE  Interaction: O95292; IntAct: EBI-24808346; Score: 0.56
DE  Interaction: Q2M2E3; IntAct: EBI-25223826; Score: 0.56
DE  Interaction: O14735; IntAct: EBI-24810822; Score: 0.56
DE  Interaction: Q9H9P2; IntAct: EBI-24810960; Score: 0.56
DE  Interaction: P06681; IntAct: EBI-25266575; Score: 0.56
DE  Interaction: O43752; IntAct: EBI-25266516; Score: 0.56
DE  Interaction: Q5QGT7; IntAct: EBI-25268527; Score: 0.56
DE  Interaction: P78329; IntAct: EBI-25269159; Score: 0.56
DE  Interaction: Q8N5M9; IntAct: EBI-25270965; Score: 0.56
DE  Interaction: Q9H0Q3; IntAct: EBI-25273560; Score: 0.56
DE  Interaction: O95159; IntAct: EBI-25273227; Score: 0.56
DE  Interaction: Q9Y3D6; IntAct: EBI-25274191; Score: 0.56
DE  Interaction: Q7RTS5; IntAct: EBI-25274864; Score: 0.56
DE  Interaction: O43889; IntAct: EBI-12701192; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-14035152; Score: 0.35
DE  Interaction: Q99679; IntAct: EBI-21516430; Score: 0.35
DE  Interaction: P06028; IntAct: EBI-21557067; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-21559824; Score: 0.35
DE  Interaction: Q8TD20; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P41587; IntAct: EBI-21567910; Score: 0.35
DE  Interaction: Q8NHX9; IntAct: EBI-21578009; Score: 0.35
DE  Interaction: O95274; IntAct: EBI-21607810; Score: 0.35
DE  Interaction: P32241; IntAct: EBI-21613594; Score: 0.35
DE  Interaction: Q9H244; IntAct: EBI-21614520; Score: 0.35
DE  Interaction: Q9H2J7; IntAct: EBI-21614809; Score: 0.35
DE  Interaction: Q9ULW2; IntAct: EBI-21704037; Score: 0.35
DE  Interaction: Q00765; IntAct: EBI-21723128; Score: 0.35
DE  Interaction: P46098; IntAct: EBI-21749232; Score: 0.35
DE  Interaction: Q96G97; IntAct: EBI-21755399; Score: 0.35
DE  Interaction: P25101; IntAct: EBI-21755472; Score: 0.35
DE  Interaction: Q9Y2T5; IntAct: EBI-21760939; Score: 0.35
DE  Interaction: Q53R12; IntAct: EBI-21829296; Score: 0.35
DE  Interaction: P04899; IntAct: EBI-21830586; Score: 0.40
DE  Interaction: Q8NHS3; IntAct: EBI-21887118; Score: 0.35
DE  Interaction: P05161; IntAct: EBI-16720078; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-20769256; Score: 0.37
DE  Interaction: Q12816; IntAct: EBI-20904848; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: Q5T9L3; IntAct: EBI-22085230; Score: 0.49
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0005635;
GO  GO:0000247;
GO  GO:0047750;
GO  GO:0042802;
GO  GO:0004769;
GO  GO:0006695;
GO  GO:0033489;
GO  GO:0033490;
GO  GO:0008203;
GO  GO:0030097;
GO  GO:0043931;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIE
SQ  GWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIY
SQ  GDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN
//
ID  P70245;
PN  3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase;
GN  Ebp;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15125}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15125}. Nucleus envelope {ECO:0000250|UniProtKB:Q15125}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q15125}. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q15125}.
DR  UNIPROT: P70245;
DR  UNIPROT: Q9CSP4;
DR  PROSITE: PS51751;
DE  Function: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000269|PubMed:8798407}.
DE  Disease: Note=Defects in Ebp are a cause of 'Tattered' (Td) which is an X-linked, semidominant mouse mutation associated with prenatal male lethality. Heterozygous females are small and at 4 to 5 days of age develop patches of hyperkeratotic skin where no hair grows, resulting in a striping of the coat in adults. Craniofacial anomalies and twisted toes have also been observed in some affected females.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0000247;
GO  GO:0047750;
GO  GO:0042802;
GO  GO:0004769;
GO  GO:0006695;
GO  GO:0008203;
GO  GO:0030097;
GO  GO:0043931;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTTNTVPLHPYWPRHLKLDNFVPNDLPTSHILVGLFSISGGLIVITWLLSSRASVVPLGAGRRLALCWFAVCTFIHLVIE
SQ  GWFSLYNGILLEDQAFLSQLWKEYSKGDSRYILSDSFVVCMETVTACLWGPLSLWVVIAFLRQQPFRFVLQLVVSMGQIY
SQ  GDVLYFLTELHEGLQHGEIGHPVYFWFYFVFLNAVWLVIPSILVLDAIKHLTSAQSVLDSKVMKIKSKHN
//
ID  Q9JJ46;
PN  3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase;
GN  Ebp;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15125}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15125}. Nucleus envelope {ECO:0000250|UniProtKB:Q15125}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q15125}. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q15125}.
DR  UNIPROT: Q9JJ46;
DR  UNIPROT: Q548M8;
DR  PROSITE: PS51751;
DE  Function: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers. {ECO:0000269|PubMed:11171067}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0000247;
GO  GO:0047750;
GO  GO:0042802;
GO  GO:0004769;
GO  GO:0006695;
GO  GO:0008203;
GO  GO:0030097;
GO  GO:0043931;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTTNMLPLHPYWPRHLRLDNFVPNDLPTWHILVGLFSFSGVLIVITWLLSSRVSVVPLGTGRRLALCWFAVCTFIHLVIE
SQ  GWFSFYHEILLEDQAFLSQLWKEYSKGDSRYILSDGFIVCMESVTACLWGPLSLWVVIAFLRHQPFRFVLQLVVSVGQIY
SQ  GDVLYFLTELRDGFQHGELGHPLYFWFYFVIMNAIWLVIPGILVFDAIKHLTNAQSMLDNKVMKIKSKHN
//
ID  Q8GTY0;
PN  Elongation factor 1-alpha 4;
GN  A4;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:21245040}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21245040}.
DR  UNIPROT: Q8GTY0;
DR  UNIPROT: P13905;
DR  UNIPROT: Q0WSD5;
DR  UNIPROT: Q39093;
DR  UNIPROT: Q9C5L4;
DR  Pfam: PF00009;
DR  Pfam: PF03144;
DR  Pfam: PF03143;
DR  PROSITE: PS00301;
DR  PROSITE: PS51722;
DE  Function: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
DE  Reference Proteome: Yes;
DE  Interaction: Q03250; IntAct: EBI-8801785; Score: 0.35
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000325;
GO  GO:0005886;
GO  GO:0009506;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0003729;
GO  GO:0003746;
GO  GO:0006412;
GO  GO:0006414;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF
SQ  ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP
SQ  KYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD
SQ  VYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSKDD
SQ  PAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVV
SQ  ETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKDPTGAKVTKAAVKKGAK
//
ID  Q17902;
PN  Egalitarian protein homolog;
GN  egal;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000305|PubMed:20005871}. Note=Probably recruited to the nuclear envelope by unc-83. {ECO:0000305|PubMed:20005871}.
DR  UNIPROT: Q17902;
DR  UNIPROT: Q65ZH5;
DR  Pfam: PF01612;
DE  Function: Part of a complex with bicd-1 and dlc-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migration in hypodermal precursor cells. {ECO:0000269|PubMed:20005871}.
DE  Reference Proteome: Yes;
DE  Interaction: Q22799; IntAct: EBI-2413132; Score: 0.75
DE  Interaction: V6CJ04; IntAct: EBI-2903351; Score: 0.51
GO  GO:0005875;
GO  GO:0005635;
GO  GO:1990923;
GO  GO:0008408;
GO  GO:0003676;
GO  GO:0031047;
GO  GO:0030473;
GO  GO:0034587;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEAKNMALLFFMDHLMQKNGRRTIHDLSCQFGARGFSEEMRNAVGTTQEGLTEFLQGHPSLFTVEGDQVILNGHNDLNA
SQ  KNNPLLQSGIRSRNYEKEAVDFFVTKLTKFGPELQIKSLLGHRSQAAPEVRLVSGRHLKEFCEFLQSQVDYFVVEGDRVR
SQ  LKNMPEPDENAIEMDDEGRPLAGVKAKQAAVEYLKSVLEQNEDQPIPLDQFYQNFCQRFSHTIRQDVATNPKELLQFLKL
SQ  NRGLFFIRSNKVSLVKNRLNEDGSENGSDEGEETNNNGMFPLDQSALTRIHFVKALKPAQDLISRLWQDINNMEKKVVGL
SQ  DLKTVTVGVDGEIFLSLGVIATTSQIGIFDLASSDVIILESGFKGILESEKVVKVIHDARRVASLLAHKYAVHMRNVFDT
SQ  QVAHSLLQHEKFNKSLNEMRPISFINLQRVYYPQSIMLSDVTPRKMSMCPNWGVRPITEEFQLTIVEEAHCLLSALYQSL
SQ  SNLIPVHLRGVFEDKCIEVNHPEVLLASPNRPPPQPFISSPYRASTRRDVRNGGSIMQSFSPAPYAAAPRPQMSDACTQT
SQ  FSTGDIEVLNVFYE
//
ID  P13387;
PN  Epidermal growth factor receptor;
GN  EGFR;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:3260329}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endosome {ECO:0000250|UniProtKB:P00533}. Endosome membrane. Nucleus {ECO:0000250|UniProtKB:P00533}. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand (By similarity). {ECO:0000250|UniProtKB:P00533}.
DR  UNIPROT: P13387;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF01030;
DE  Function: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:3260329). Known ligands include EGF and TGFA/TGF-alpha (PubMed:3260329). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues (By similarity). The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades (By similarity). Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (By similarity). May also activate the NF-kappa-B signaling cascade (By similarity). {ECO:0000250|UniProtKB:P00533, ECO:0000269|PubMed:3260329}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0010008;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0004713;
GO  GO:0004714;
GO  GO:0071364;
GO  GO:0007173;
GO  GO:0007611;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGVRSPLSASGPRGAAVLVLLLLGVALCSAVEEKKVCQGTNNKLTQLGHVEDHFTSLQRMYNNCEVVLSNLEITYVEHNR
SQ  DLTFLKTIQEVAGYVLIALNMVDVIPLENLQIIRGNVLYDNSFALAVLSNYHMNKTQGLRELPMKRLSEILNGGVKISNN
SQ  PKLCNMDTVLWNDIIDTSRKPLTVLDFASNLSSCPKCHPNCTEDHCWGAGEQNCQTLTKVICAQQCSGRCRGKVPSDCCH
SQ  NQCAAGCTGPRESDCLACRKFRDDATCKDTCPPLVLYNPTTYQMDVNPEGKYSFGATCVRECPHNYVVTDHGSCVRSCNT
SQ  DTYEVEENGVRKCKKCDGLCSKVCNGIGIGELKGILSINATNIDSFKNCTKINGDVSILPVAFLGDAFTKTLPLDPKKLD
SQ  VFRTVKEISGFLLIQAWPDNATDLYAFENLEIIRGRTKQHGQYSLAVVNLKIQSLGLRSLKEISDGDIAIMKNKNLCYAD
SQ  TMNWRSLFATQSQKTKIIQNRNKNDCTADRHVCDPLCSDVGCWGPGPFHCFSCRFFSRQKECVKQCNILQGEPREFERDS
SQ  KCLPCHSECLVQNSTAYNTTCSGPGPDHCMKCAHFIDGPHCVKACPAGVLGENDTLVWKYADANAVCQLCHPNCTRGCKG
SQ  PGLEGCPNGSKTPSIAAGVVGGLLCLVVVGLGIGLYLRRRHIVRKRTLRRLLQERELVEPLTP
//
ID  P00533;
PN  Epidermal growth factor receptor;
GN  EGFR;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:23589287, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960}; Single-pass type I membrane protein {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27153536}; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Endosome {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:27153536}. Endosome membrane. Nucleus {ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:20551055, ECO:0000269|PubMed:20674546}. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER (PubMed:20674546, PubMed:17909029). Endocytosed upon activation by ligand (PubMed:2790960, PubMed:17182860, PubMed:27153536, PubMed:17909029). Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) (PubMed:20551055). {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:20674546, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960}. [Isoform 2]: Secreted.
DR  UNIPROT: P00533;
DR  UNIPROT: O00688;
DR  UNIPROT: O00732;
DR  UNIPROT: P06268;
DR  UNIPROT: Q14225;
DR  UNIPROT: Q68GS5;
DR  UNIPROT: Q92795;
DR  UNIPROT: Q9BZS2;
DR  UNIPROT: Q9GZX1;
DR  UNIPROT: Q9H2C9;
DR  UNIPROT: Q9H3C9;
DR  UNIPROT: Q9UMD7;
DR  UNIPROT: Q9UMD8;
DR  UNIPROT: Q9UMG5;
DR  PDB: 1IVO;
DR  PDB: 1M14;
DR  PDB: 1M17;
DR  PDB: 1MOX;
DR  PDB: 1NQL;
DR  PDB: 1XKK;
DR  PDB: 1YY9;
DR  PDB: 1Z9I;
DR  PDB: 2EB2;
DR  PDB: 2EB3;
DR  PDB: 2GS2;
DR  PDB: 2GS6;
DR  PDB: 2GS7;
DR  PDB: 2ITN;
DR  PDB: 2ITO;
DR  PDB: 2ITP;
DR  PDB: 2ITQ;
DR  PDB: 2ITT;
DR  PDB: 2ITU;
DR  PDB: 2ITV;
DR  PDB: 2ITW;
DR  PDB: 2ITX;
DR  PDB: 2ITY;
DR  PDB: 2ITZ;
DR  PDB: 2J5E;
DR  PDB: 2J5F;
DR  PDB: 2J6M;
DR  PDB: 2JIT;
DR  PDB: 2JIU;
DR  PDB: 2JIV;
DR  PDB: 2KS1;
DR  PDB: 2M0B;
DR  PDB: 2M20;
DR  PDB: 2N5S;
DR  PDB: 2RF9;
DR  PDB: 2RFD;
DR  PDB: 2RFE;
DR  PDB: 2RGP;
DR  PDB: 3B2U;
DR  PDB: 3B2V;
DR  PDB: 3BEL;
DR  PDB: 3BUO;
DR  PDB: 3C09;
DR  PDB: 3G5V;
DR  PDB: 3G5Y;
DR  PDB: 3GOP;
DR  PDB: 3GT8;
DR  PDB: 3IKA;
DR  PDB: 3LZB;
DR  PDB: 3NJP;
DR  PDB: 3OB2;
DR  PDB: 3OP0;
DR  PDB: 3P0Y;
DR  PDB: 3PFV;
DR  PDB: 3POZ;
DR  PDB: 3QWQ;
DR  PDB: 3UG1;
DR  PDB: 3UG2;
DR  PDB: 3VJN;
DR  PDB: 3VJO;
DR  PDB: 3VRP;
DR  PDB: 3VRR;
DR  PDB: 3W2O;
DR  PDB: 3W2P;
DR  PDB: 3W2Q;
DR  PDB: 3W2R;
DR  PDB: 3W2S;
DR  PDB: 3W32;
DR  PDB: 3W33;
DR  PDB: 4G5J;
DR  PDB: 4G5P;
DR  PDB: 4HJO;
DR  PDB: 4I1Z;
DR  PDB: 4I20;
DR  PDB: 4I21;
DR  PDB: 4I22;
DR  PDB: 4I23;
DR  PDB: 4I24;
DR  PDB: 4JQ7;
DR  PDB: 4JQ8;
DR  PDB: 4JR3;
DR  PDB: 4JRV;
DR  PDB: 4KRL;
DR  PDB: 4KRM;
DR  PDB: 4KRO;
DR  PDB: 4KRP;
DR  PDB: 4LI5;
DR  PDB: 4LL0;
DR  PDB: 4LQM;
DR  PDB: 4LRM;
DR  PDB: 4R3P;
DR  PDB: 4R3R;
DR  PDB: 4R5S;
DR  PDB: 4RIW;
DR  PDB: 4RIX;
DR  PDB: 4RIY;
DR  PDB: 4RJ4;
DR  PDB: 4RJ5;
DR  PDB: 4RJ6;
DR  PDB: 4RJ7;
DR  PDB: 4RJ8;
DR  PDB: 4TKS;
DR  PDB: 4UIP;
DR  PDB: 4UV7;
DR  PDB: 4WD5;
DR  PDB: 4WKQ;
DR  PDB: 4WRG;
DR  PDB: 4ZAU;
DR  PDB: 4ZJV;
DR  PDB: 4ZSE;
DR  PDB: 5C8K;
DR  PDB: 5C8M;
DR  PDB: 5C8N;
DR  PDB: 5CAL;
DR  PDB: 5CAN;
DR  PDB: 5CAO;
DR  PDB: 5CAP;
DR  PDB: 5CAQ;
DR  PDB: 5CAS;
DR  PDB: 5CAU;
DR  PDB: 5CAV;
DR  PDB: 5CNN;
DR  PDB: 5CNO;
DR  PDB: 5CZH;
DR  PDB: 5CZI;
DR  PDB: 5D41;
DR  PDB: 5EDP;
DR  PDB: 5EDQ;
DR  PDB: 5EDR;
DR  PDB: 5EM5;
DR  PDB: 5EM6;
DR  PDB: 5EM7;
DR  PDB: 5EM8;
DR  PDB: 5FED;
DR  PDB: 5FEE;
DR  PDB: 5FEQ;
DR  PDB: 5GMP;
DR  PDB: 5GNK;
DR  PDB: 5GTY;
DR  PDB: 5GTZ;
DR  PDB: 5HCX;
DR  PDB: 5HCY;
DR  PDB: 5HCZ;
DR  PDB: 5HG5;
DR  PDB: 5HG7;
DR  PDB: 5HG8;
DR  PDB: 5HG9;
DR  PDB: 5HIB;
DR  PDB: 5HIC;
DR  PDB: 5J9Y;
DR  PDB: 5J9Z;
DR  PDB: 5JEB;
DR  PDB: 5LV6;
DR  PDB: 5SX4;
DR  PDB: 5SX5;
DR  PDB: 5U8L;
DR  PDB: 5UG8;
DR  PDB: 5UG9;
DR  PDB: 5UGA;
DR  PDB: 5UGB;
DR  PDB: 5UGC;
DR  PDB: 5UWD;
DR  PDB: 5WB7;
DR  PDB: 5WB8;
DR  PDB: 5X26;
DR  PDB: 5X27;
DR  PDB: 5X28;
DR  PDB: 5X2A;
DR  PDB: 5X2C;
DR  PDB: 5X2F;
DR  PDB: 5X2K;
DR  PDB: 5XDK;
DR  PDB: 5XDL;
DR  PDB: 5XGM;
DR  PDB: 5XGN;
DR  PDB: 5XWD;
DR  PDB: 5Y25;
DR  PDB: 5Y9T;
DR  PDB: 5YU9;
DR  PDB: 5ZTO;
DR  PDB: 5ZWJ;
DR  PDB: 6ARU;
DR  PDB: 6B3S;
DR  PDB: 6D8E;
DR  PDB: 6DUK;
DR  PDB: 6JRJ;
DR  PDB: 6JRK;
DR  PDB: 6JRX;
DR  PDB: 6JWL;
DR  PDB: 6JX0;
DR  PDB: 6JX4;
DR  PDB: 6JXT;
DR  PDB: 6JZ0;
DR  PDB: 6LUB;
DR  PDB: 6LUD;
DR  PDB: 6P1D;
DR  PDB: 6P1L;
DR  PDB: 6P8Q;
DR  PDB: 6S89;
DR  PDB: 6S8A;
DR  PDB: 6S9B;
DR  PDB: 6S9C;
DR  PDB: 6S9D;
DR  PDB: 6TFU;
DR  PDB: 6TFV;
DR  PDB: 6TFW;
DR  PDB: 6TFY;
DR  PDB: 6TFZ;
DR  PDB: 6TG0;
DR  PDB: 6TG1;
DR  PDB: 6V5N;
DR  PDB: 6V5P;
DR  PDB: 6V66;
DR  PDB: 6V6K;
DR  PDB: 6V6O;
DR  PDB: 6VH4;
DR  PDB: 6VHN;
DR  PDB: 6VHP;
DR  PDB: 6WA2;
DR  PDB: 6WAK;
DR  PDB: 6WXN;
DR  PDB: 6XL4;
DR  PDB: 6Z4B;
DR  PDB: 6Z4D;
DR  PDB: 7A2A;
DR  PDB: 7A6I;
DR  PDB: 7A6J;
DR  PDB: 7A6K;
DR  PDB: 7AEI;
DR  PDB: 7AEM;
DR  PDB: 7B85;
DR  PDB: 7JXI;
DR  PDB: 7JXK;
DR  PDB: 7JXL;
DR  PDB: 7JXM;
DR  PDB: 7JXP;
DR  PDB: 7JXQ;
DR  PDB: 7JXW;
DR  PDB: 7K1H;
DR  PDB: 7K1I;
DR  PDB: 7KXZ;
DR  PDB: 7KY0;
DR  PDB: 7LEN;
DR  PDB: 7LFR;
DR  PDB: 7LFS;
DR  PDB: 7LG8;
DR  PDB: 7LGS;
DR  PDB: 7LTX;
DR  PDB: 7OM4;
DR  PDB: 7OXB;
DR  PDB: 7SYD;
DR  PDB: 7SYE;
DR  PDB: 7SZ0;
DR  PDB: 7SZ1;
DR  PDB: 7SZ5;
DR  PDB: 7SZ7;
DR  PDB: 7TVD;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF07714;
DR  Pfam: PF01030;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  OMIM: 131550;
DR  OMIM: 211980;
DR  OMIM: 616069;
DR  DisGeNET: 1956;
DE  Function: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:2790960, PubMed:10805725, PubMed:27153536). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin- binding EGF (PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975, PubMed:15611079, PubMed:12297049, PubMed:27153536, PubMed:20837704, PubMed:17909029). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Plays a role in enhancing learning and memory performance (By similarity). {ECO:0000250|UniProtKB:Q01279, ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11116146, ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:11602604, ECO:0000269|PubMed:12297049, ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15374980, ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:15611079, ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:19560417, ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:20837704, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960, ECO:0000269|PubMed:7679104, ECO:0000269|PubMed:8144591, ECO:0000269|PubMed:9419975}. Isoform 2 may act as an antagonist of EGF action. (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins. {ECO:0000269|PubMed:21516087}.
DE  Disease: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. {ECO:0000269|PubMed:15118125, ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:16672372}. Note=The gene represented in this entry is involved in disease pathogenesis. Inflammatory skin and bowel disease, neonatal, 2 (NISBD2) [MIM:616069]: A disorder characterized by inflammatory features with neonatal onset, involving the skin, hair, and gut. The skin lesions involve perioral and perianal erythema, psoriasiform erythroderma, with flares of erythema, scaling, and widespread pustules. Gastrointestinal symptoms include malabsorptive diarrhea that is exacerbated by intercurrent gastrointestinal infections. The hair is short or broken, and the eyelashes and eyebrows are wiry and disorganized. {ECO:0000269|PubMed:24691054}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: D4A631; IntAct: EBI-22084260; Score: 0.35
DE  Interaction: O43707; IntAct: EBI-9689686; Score: 0.55
DE  Interaction: O60645; IntAct: EBI-10764491; Score: 0.40
DE  Interaction: O75694; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O94875; IntAct: EBI-4397010; Score: 0.55
DE  Interaction: O96018; IntAct: EBI-7877395; Score: 0.44
DE  Interaction: P00519; IntAct: EBI-7887814; Score: 0.69
DE  Interaction: P22681; IntAct: EBI-8682709; Score: 0.96
DE  Interaction: P29353; IntAct: EBI-8682733; Score: 0.98
DE  Interaction: P27986; IntAct: EBI-8682765; Score: 0.81
DE  Interaction: P16333; IntAct: EBI-8682777; Score: 0.82
DE  Interaction: P62994; IntAct: EBI-8682799; Score: 0.56
DE  Interaction: P15941; IntAct: EBI-7913778; Score: 0.82
DE  Interaction: Q99962; IntAct: EBI-8173591; Score: 0.68
DE  Interaction: Q96B97; IntAct: EBI-8173605; Score: 0.69
DE  Interaction: Q13322; IntAct: EBI-8679878; Score: 0.73
DE  Interaction: P62993; IntAct: EBI-297464; Score: 0.98
DE  Interaction: P68431; IntAct: EBI-298046; Score: 0.27
DE  Interaction: P13987; IntAct: EBI-298103; Score: 0.44
DE  Interaction: P98083; IntAct: EBI-370958; Score: 0.40
DE  Interaction: P63104; IntAct: EBI-446460; Score: 0.77
DE  Interaction: Q17R13; IntAct: EBI-457635; Score: 0.35
DE  Interaction: P04083; IntAct: EBI-7411482; Score: 0.77
DE  Interaction: P25098; IntAct: EBI-7436130; Score: 0.46
DE  Interaction: Q06124; IntAct: EBI-8533094; Score: 0.82
DE  Interaction: O75368; IntAct: EBI-8533072; Score: 0.68
DE  Interaction: P51692; IntAct: EBI-8533286; Score: 0.40
DE  Interaction: P46109; IntAct: EBI-8533556; Score: 0.75
DE  Interaction: P41240; IntAct: EBI-8533610; Score: 0.68
DE  Interaction: P01133; IntAct: EBI-640874; Score: 0.97
DE  Interaction: P22682; IntAct: EBI-640915; Score: 0.50
DE  Interaction: O00750; IntAct: EBI-641139; Score: 0.81
DE  Interaction: O00443; IntAct: EBI-641139; Score: 0.35
DE  Interaction: O43147; IntAct: EBI-733199; Score: 0.00
DE  Interaction: P36542; IntAct: EBI-733962; Score: 0.00
DE  Interaction: Q8WUM4; IntAct: EBI-7397470; Score: 0.68
DE  Interaction: P02533; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q03135; IntAct: EBI-702075; Score: 0.81
DE  Interaction: P10809; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P31689; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P68104; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-702075; Score: 0.89
DE  Interaction: Q99959; IntAct: EBI-702075; Score: 0.48
DE  Interaction: P38646; IntAct: EBI-702075; Score: 0.75
DE  Interaction: Q04695; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-702075; Score: 0.53
DE  Interaction: P13647; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P10412; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P31943; IntAct: EBI-702075; Score: 0.53
DE  Interaction: P11142; IntAct: EBI-702075; Score: 0.80
DE  Interaction: Q14289; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P29317; IntAct: EBI-702075; Score: 0.48
DE  Interaction: Q9NR50; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q96EY1; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P40855; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P61978; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q05397; IntAct: EBI-702075; Score: 0.75
DE  Interaction: Q71U36; IntAct: EBI-702075; Score: 0.75
DE  Interaction: P02538; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P10599; IntAct: EBI-702075; Score: 0.79
DE  Interaction: P49023; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P62807; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P52597; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P04264; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P98172; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q13191; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-702075; Score: 0.67
DE  Interaction: P16615; IntAct: EBI-702075; Score: 0.64
DE  Interaction: P35221; IntAct: EBI-702075; Score: 0.68
DE  Interaction: P40763; IntAct: EBI-702075; Score: 0.92
DE  Interaction: P04792; IntAct: EBI-702075; Score: 0.61
DE  Interaction: P62258; IntAct: EBI-702075; Score: 0.35
DE  Interaction: O60716; IntAct: EBI-702075; Score: 0.75
DE  Interaction: P27348; IntAct: EBI-702075; Score: 0.85
DE  Interaction: Q14192; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-702075; Score: 0.95
DE  Interaction: P31947; IntAct: EBI-702075; Score: 0.83
DE  Interaction: P31949; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P07947; IntAct: EBI-702075; Score: 0.56
DE  Interaction: Q07065; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q9UBB4; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q14134; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P08195; IntAct: EBI-702075; Score: 0.64
DE  Interaction: Q96AG4; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q9H5V8; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q07912; IntAct: EBI-702075; Score: 0.35
DE  Interaction: O75815; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q969Z0; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P06576; IntAct: EBI-702075; Score: 0.35
DE  Interaction: O43592; IntAct: EBI-702075; Score: 0.53
DE  Interaction: P54760; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P0CG47; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P08107; IntAct: EBI-702075; Score: 0.80
DE  Interaction: O60884; IntAct: EBI-702075; Score: 0.53
DE  Interaction: Q00325; IntAct: EBI-702075; Score: 0.53
DE  Interaction: P55060; IntAct: EBI-702075; Score: 0.53
DE  Interaction: P56945; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-702075; Score: 0.35
DE  Interaction: Q8IZV2; IntAct: EBI-7868933; Score: 0.56
DE  Interaction: P42684; IntAct: EBI-7874891; Score: 0.69
DE  Interaction: Q96D37; IntAct: EBI-7875378; Score: 0.44
DE  Interaction: Q9Y490; IntAct: EBI-7875422; Score: 0.44
DE  Interaction: P43405; IntAct: EBI-7875448; Score: 0.44
DE  Interaction: Q92529; IntAct: EBI-7875536; Score: 0.44
DE  Interaction: P20936; IntAct: EBI-7875605; Score: 0.44
DE  Interaction: P19174; IntAct: EBI-7875736; Score: 0.85
DE  Interaction: Q92569; IntAct: EBI-7875764; Score: 0.76
DE  Interaction: O00459; IntAct: EBI-7875895; Score: 0.76
DE  Interaction: P49757; IntAct: EBI-7876086; Score: 0.57
DE  Interaction: Q13387; IntAct: EBI-7876156; Score: 0.69
DE  Interaction: Q9UQF2; IntAct: EBI-7876199; Score: 0.44
DE  Interaction: O60674; IntAct: EBI-7876243; Score: 0.44
DE  Interaction: O14654; IntAct: EBI-7876269; Score: 0.44
DE  Interaction: Q7Z6G8; IntAct: EBI-7876386; Score: 0.44
DE  Interaction: P98077; IntAct: EBI-7876430; Score: 0.44
DE  Interaction: Q6PKX4; IntAct: EBI-7876474; Score: 0.44
DE  Interaction: Q9P104; IntAct: EBI-7876593; Score: 0.44
DE  Interaction: Q8TEW6; IntAct: EBI-7876742; Score: 0.44
DE  Interaction: Q8IZW8; IntAct: EBI-7876785; Score: 0.44
DE  Interaction: P46108; IntAct: EBI-7876865; Score: 0.69
DE  Interaction: Q9UKG1; IntAct: EBI-7876909; Score: 0.57
DE  Interaction: O95704; IntAct: EBI-7877048; Score: 0.44
DE  Interaction: Q92870; IntAct: EBI-7877108; Score: 0.74
DE  Interaction: Q92625; IntAct: EBI-7877154; Score: 0.79
DE  Interaction: O00213; IntAct: EBI-7877304; Score: 0.44
DE  Interaction: Q9NP31; IntAct: EBI-7879463; Score: 0.44
DE  Interaction: O60880; IntAct: EBI-7879502; Score: 0.44
DE  Interaction: Q9NRF2; IntAct: EBI-7879524; Score: 0.77
DE  Interaction: Q13882; IntAct: EBI-7879563; Score: 0.44
DE  Interaction: P16885; IntAct: EBI-7879602; Score: 0.79
DE  Interaction: Q7Z7G1; IntAct: EBI-7879641; Score: 0.44
DE  Interaction: Q9UQQ2; IntAct: EBI-7879742; Score: 0.44
DE  Interaction: P51451; IntAct: EBI-7883080; Score: 0.69
DE  Interaction: Q13239; IntAct: EBI-7887945; Score: 0.69
DE  Interaction: Q8WYP3; IntAct: EBI-7888049; Score: 0.44
DE  Interaction: Q9Y6R0; IntAct: EBI-7888501; Score: 0.57
DE  Interaction: P35568; IntAct: EBI-7888870; Score: 0.44
DE  Interaction: P07332; IntAct: EBI-7888914; Score: 0.44
DE  Interaction: Q9NSE2; IntAct: EBI-7889043; Score: 0.74
DE  Interaction: P43403; IntAct: EBI-7889327; Score: 0.69
DE  Interaction: P51813; IntAct: EBI-7890778; Score: 0.44
DE  Interaction: P21860; IntAct: EBI-875451; Score: 0.91
DE  Interaction: Q15303; IntAct: EBI-875456; Score: 0.56
DE  Interaction: P42566; IntAct: EBI-921718; Score: 0.35
DE  Interaction: Q9UJ41; IntAct: EBI-921718; Score: 0.60
DE  Interaction: P00533; IntAct: EBI-970714; Score: 0.98
DE  Interaction: Q9UQC2; IntAct: EBI-975219; Score: 0.67
DE  Interaction: P01135; IntAct: EBI-1034394; Score: 0.78
DE  Interaction: O60603; IntAct: EBI-7127435; Score: 0.68
DE  Interaction: O00206; IntAct: EBI-7127511; Score: 0.40
DE  Interaction: P09496; IntAct: EBI-1188138; Score: 0.35
DE  Interaction: P05026; IntAct: EBI-1188138; Score: 0.35
DE  Interaction: P68366; IntAct: EBI-1188138; Score: 0.53
DE  Interaction: P53675; IntAct: EBI-1188138; Score: 0.35
DE  Interaction: Q13740; IntAct: EBI-1188138; Score: 0.35
DE  Interaction: P04406; IntAct: EBI-1188138; Score: 0.79
DE  Interaction: Q9NYD6; IntAct: EBI-1188138; Score: 0.35
DE  Interaction: P51636; IntAct: EBI-1188138; Score: 0.67
DE  Interaction: P05362; IntAct: EBI-1188138; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-1188138; Score: 0.35
DE  Interaction: P06702; IntAct: EBI-1188138; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-1188138; Score: 0.35
DE  Interaction: P07948; IntAct: EBI-1188138; Score: 0.82
DE  Interaction: P62158; IntAct: EBI-1188138; Score: 0.83
DE  Interaction: P0A0I7; IntAct: EBI-7213556; Score: 0.46
DE  Interaction: P62157; IntAct: EBI-1256868; Score: 0.40
DE  Interaction: Q29376; IntAct: EBI-1256888; Score: 0.44
DE  Interaction: P62161; IntAct: EBI-1256912; Score: 0.52
DE  Interaction: P62204; IntAct: EBI-1256994; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-4309290; Score: 0.52
DE  Interaction: P12931; IntAct: EBI-7248693; Score: 0.90
DE  Interaction: Q62245; IntAct: EBI-8661857; Score: 0.40
DE  Interaction: Q60631; IntAct: EBI-8664380; Score: 0.35
DE  Interaction: P13866; IntAct: EBI-1772419; Score: 0.52
DE  Interaction: P20417; IntAct: EBI-8608593; Score: 0.80
DE  Interaction: P18031; IntAct: EBI-8629259; Score: 0.90
DE  Interaction: O75886; IntAct: EBI-2119941; Score: 0.58
DE  Interaction: Q13671; IntAct: EBI-2119957; Score: 0.46
DE  Interaction: P08575; IntAct: EBI-25369712; Score: 0.59
DE  Interaction: P23467; IntAct: EBI-20976986; Score: 0.69
DE  Interaction: Q12913; IntAct: EBI-2264953; Score: 0.00
DE  Interaction: Q8K424; IntAct: EBI-2650756; Score: 0.40
DE  Interaction: Q5NEB4; IntAct: EBI-2807083; Score: 0.00
DE  Interaction: A0A6L7H280; IntAct: EBI-2834648; Score: 0.00
DE  Interaction: Q8ZE20; IntAct: EBI-2870787; Score: 0.00
DE  Interaction: O75674; IntAct: EBI-7270434; Score: 0.56
DE  Interaction: P52294; IntAct: EBI-8109298; Score: 0.40
DE  Interaction: P08581; IntAct: EBI-2927740; Score: 0.80
DE  Interaction: P42224; IntAct: EBI-8478938; Score: 0.77
DE  Interaction: P06240; IntAct: EBI-8638762; Score: 0.35
DE  Interaction: P52735; IntAct: EBI-8565016; Score: 0.35
DE  Interaction: P29350; IntAct: EBI-8683880; Score: 0.55
DE  Interaction: O75165; IntAct: EBI-8631408; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-8631521; Score: 0.43
DE  Interaction: Q00944; IntAct: EBI-3953289; Score: 0.44
DE  Interaction: Q05209; IntAct: EBI-3952087; Score: 0.81
DE  Interaction: P17931; IntAct: EBI-3989365; Score: 0.40
DE  Interaction: P13693; IntAct: EBI-4303426; Score: 0.40
DE  Interaction: Q13480; IntAct: EBI-4303473; Score: 0.74
DE  Interaction: P06396; IntAct: EBI-5235004; Score: 0.55
DE  Interaction: O15511; IntAct: EBI-5234978; Score: 0.55
DE  Interaction: Q9H299; IntAct: EBI-5234886; Score: 0.55
DE  Interaction: Q15819; IntAct: EBI-4397413; Score: 0.55
DE  Interaction: Q15005; IntAct: EBI-4397397; Score: 0.55
DE  Interaction: Q14204; IntAct: EBI-4397381; Score: 0.55
DE  Interaction: Q12852; IntAct: EBI-4397329; Score: 0.62
DE  Interaction: Q06830; IntAct: EBI-4397313; Score: 0.55
DE  Interaction: Q02952; IntAct: EBI-4397297; Score: 0.63
DE  Interaction: Q02790; IntAct: EBI-4397289; Score: 0.55
DE  Interaction: Q02246; IntAct: EBI-4397281; Score: 0.55
DE  Interaction: P60520; IntAct: EBI-4397232; Score: 0.63
DE  Interaction: P60174; IntAct: EBI-4397224; Score: 0.55
DE  Interaction: P54368; IntAct: EBI-4397208; Score: 0.55
DE  Interaction: P43243; IntAct: EBI-4397192; Score: 0.55
DE  Interaction: P40925; IntAct: EBI-4397176; Score: 0.55
DE  Interaction: P34932; IntAct: EBI-4397168; Score: 0.67
DE  Interaction: P31948; IntAct: EBI-4397160; Score: 0.63
DE  Interaction: P31939; IntAct: EBI-4397152; Score: 0.55
DE  Interaction: P26641; IntAct: EBI-4397136; Score: 0.55
DE  Interaction: P23528; IntAct: EBI-4397128; Score: 0.67
DE  Interaction: P20336; IntAct: EBI-4397112; Score: 0.55
DE  Interaction: P17174; IntAct: EBI-4397104; Score: 0.55
DE  Interaction: P16930; IntAct: EBI-4397074; Score: 0.55
DE  Interaction: P14625; IntAct: EBI-4397058; Score: 0.55
DE  Interaction: P06132; IntAct: EBI-4397042; Score: 0.55
DE  Interaction: P04075; IntAct: EBI-4397034; Score: 0.55
DE  Interaction: O95433; IntAct: EBI-4397026; Score: 0.55
DE  Interaction: O94992; IntAct: EBI-4397018; Score: 0.55
DE  Interaction: O00170; IntAct: EBI-5324173; Score: 0.55
DE  Interaction: Q9Y2H9; IntAct: EBI-4397860; Score: 0.63
DE  Interaction: Q9UNE7; IntAct: EBI-4397844; Score: 0.72
DE  Interaction: Q9P0L0; IntAct: EBI-4397828; Score: 0.71
DE  Interaction: Q99784; IntAct: EBI-4397783; Score: 0.55
DE  Interaction: Q96CW1; IntAct: EBI-4397767; Score: 0.77
DE  Interaction: Q92733; IntAct: EBI-4397759; Score: 0.55
DE  Interaction: Q8N4S1; IntAct: EBI-4397712; Score: 0.37
DE  Interaction: Q8N111; IntAct: EBI-4397696; Score: 0.55
DE  Interaction: A4FU49; IntAct: EBI-4397659; Score: 0.55
DE  Interaction: P17600; IntAct: EBI-4397603; Score: 0.55
DE  Interaction: Q59GR8; IntAct: EBI-4397580; Score: 0.55
DE  Interaction: Q6UWJ1; IntAct: EBI-4397688; Score: 0.55
DE  Interaction: Q59EJ3; IntAct: EBI-4397553; Score: 0.55
DE  Interaction: P53041; IntAct: EBI-4397535; Score: 0.55
DE  Interaction: Q16186; IntAct: EBI-4397421; Score: 0.55
DE  Interaction: Q15120; IntAct: EBI-4397405; Score: 0.55
DE  Interaction: Q14318; IntAct: EBI-4397389; Score: 0.68
DE  Interaction: Q14050; IntAct: EBI-4397373; Score: 0.55
DE  Interaction: Q13561; IntAct: EBI-4397365; Score: 0.55
DE  Interaction: Q13491; IntAct: EBI-4397337; Score: 0.55
DE  Interaction: Q09666; IntAct: EBI-4397321; Score: 0.67
DE  Interaction: P62330; IntAct: EBI-4397240; Score: 0.55
DE  Interaction: P55036; IntAct: EBI-4397216; Score: 0.55
DE  Interaction: P49908; IntAct: EBI-4397200; Score: 0.55
DE  Interaction: P41222; IntAct: EBI-4397184; Score: 0.55
DE  Interaction: P31321; IntAct: EBI-4397144; Score: 0.55
DE  Interaction: P16152; IntAct: EBI-4397066; Score: 0.55
DE  Interaction: P21291; IntAct: EBI-4397120; Score: 0.55
DE  Interaction: P09936; IntAct: EBI-4397050; Score: 0.63
DE  Interaction: O14818; IntAct: EBI-4396992; Score: 0.55
DE  Interaction: O75095; IntAct: EBI-4397001; Score: 0.55
DE  Interaction: Q9Y3A3; IntAct: EBI-4397868; Score: 0.55
DE  Interaction: Q9Y237; IntAct: EBI-4397852; Score: 0.55
DE  Interaction: Q9UBN7; IntAct: EBI-4397836; Score: 0.81
DE  Interaction: Q96AD5; IntAct: EBI-4397820; Score: 0.55
DE  Interaction: Q9NNZ3; IntAct: EBI-4397812; Score: 0.55
DE  Interaction: Q99608; IntAct: EBI-4397775; Score: 0.55
DE  Interaction: Q8TDB4; IntAct: EBI-4397733; Score: 0.55
DE  Interaction: Q8N2Y8; IntAct: EBI-4397704; Score: 0.55
DE  Interaction: Q7L273; IntAct: EBI-4397611; Score: 0.55
DE  Interaction: P07900; IntAct: EBI-4397595; Score: 0.78
DE  Interaction: Q59G22; IntAct: EBI-4397572; Score: 0.55
DE  Interaction: Q53GZ6; IntAct: EBI-4397527; Score: 0.55
DE  Interaction: P60880; IntAct: EBI-4397510; Score: 0.55
DE  Interaction: P52306; IntAct: EBI-4397490; Score: 0.55
DE  Interaction: Q4KWH8; IntAct: EBI-4397437; Score: 0.55
DE  Interaction: O95782; IntAct: EBI-4397884; Score: 0.67
DE  Interaction: P02751; IntAct: EBI-4398148; Score: 0.40
DE  Interaction: P46940; IntAct: EBI-5465302; Score: 0.63
DE  Interaction: Q01973; IntAct: EBI-6082648; Score: 0.58
DE  Interaction: Q9H267; IntAct: EBI-7913457; Score: 0.27
DE  Interaction: Q15075; IntAct: EBI-8051513; Score: 0.43
DE  Interaction: P12830; IntAct: EBI-6592813; Score: 0.74
DE  Interaction: P01100; IntAct: EBI-6593803; Score: 0.27
DE  Interaction: P08631; IntAct: EBI-6599779; Score: 0.65
DE  Interaction: Q16539; IntAct: EBI-6600298; Score: 0.27
DE  Interaction: P33992; IntAct: EBI-6870068; Score: 0.35
DE  Interaction: P33993; IntAct: EBI-6870068; Score: 0.35
DE  Interaction: P50281; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-8769968; Score: 0.57
DE  Interaction: Q8TF42; IntAct: EBI-8769968; Score: 0.60
DE  Interaction: Q9UBS4; IntAct: EBI-8769968; Score: 0.57
DE  Interaction: O75223; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: P62701; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: P62269; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: P34931; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: P54652; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: P01040; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: P62805; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: Q75V66; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: O95155; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: Q01469; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: Q92832; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: Q6UWL2; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: P25705; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: Q8N163; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: Q13098; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: Q9UJM3; IntAct: EBI-8769968; Score: 0.87
DE  Interaction: P49411; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: Q8WV24; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P10586; IntAct: EBI-8770081; Score: 0.55
DE  Interaction: Q9BYJ9; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: Q92522; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P53680; IntAct: EBI-8770081; Score: 0.57
DE  Interaction: P62841; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: Q96JX3; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P30711; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P48594; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: Q96QV6; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P23634; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: Q01650; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P35321; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P18621; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P23246; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P01892; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: Q5JNZ5; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: Q10567; IntAct: EBI-8770081; Score: 0.65
DE  Interaction: P26232; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: O94973; IntAct: EBI-8770081; Score: 0.57
DE  Interaction: Q9H0D6; IntAct: EBI-8770081; Score: 0.53
DE  Interaction: P23468; IntAct: EBI-8770081; Score: 0.55
DE  Interaction: Q9UMD9; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: Q8IUR7; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P04114; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: O95470; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: Q9UQB8; IntAct: EBI-8770081; Score: 0.74
DE  Interaction: Q96RL7; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P49756; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: Q9UK59; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P16144; IntAct: EBI-8770081; Score: 0.35
DE  Interaction: P35222; IntAct: EBI-8770081; Score: 0.48
DE  Interaction: P43307; IntAct: EBI-8770271; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-8770271; Score: 0.79
DE  Interaction: O95573; IntAct: EBI-8770773; Score: 0.35
DE  Interaction: Q8NFI3; IntAct: EBI-8770773; Score: 0.35
DE  Interaction: O00483; IntAct: EBI-8770773; Score: 0.53
DE  Interaction: A1L0T0; IntAct: EBI-8770773; Score: 0.35
DE  Interaction: P16083; IntAct: EBI-8770773; Score: 0.35
DE  Interaction: Q14457; IntAct: EBI-8849553; Score: 0.63
DE  Interaction: Q92622; IntAct: EBI-8847331; Score: 0.56
DE  Interaction: Q9BU70; IntAct: EBI-8997522; Score: 0.37
DE  Interaction: Q8N6M6; IntAct: EBI-8997535; Score: 0.37
DE  Interaction: Q5T7W7; IntAct: EBI-8997548; Score: 0.37
DE  Interaction: Q00597; IntAct: EBI-8997574; Score: 0.37
DE  Interaction: Q14093; IntAct: EBI-8997561; Score: 0.37
DE  Interaction: O75474; IntAct: EBI-8997587; Score: 0.37
DE  Interaction: Q16644; IntAct: EBI-8997613; Score: 0.37
DE  Interaction: Q9BXL5; IntAct: EBI-8997600; Score: 0.37
DE  Interaction: Q9NR45; IntAct: EBI-8997626; Score: 0.37
DE  Interaction: P62714; IntAct: EBI-8997639; Score: 0.37
DE  Interaction: P01137; IntAct: EBI-8997665; Score: 0.37
DE  Interaction: P56962; IntAct: EBI-8997652; Score: 0.37
DE  Interaction: Q9Y2H8; IntAct: EBI-8997678; Score: 0.37
DE  Interaction: Q9NWQ8; IntAct: EBI-9072824; Score: 0.40
DE  Interaction: P63244; IntAct: EBI-9072870; Score: 0.40
DE  Interaction: Q70E73; IntAct: EBI-9160561; Score: 0.40
DE  Interaction: Q6PK50; IntAct: EBI-9356626; Score: 0.40
DE  Interaction: Q96BE0; IntAct: EBI-9356689; Score: 0.40
DE  Interaction: Q8K2C9; IntAct: EBI-9356718; Score: 0.40
DE  Interaction: Q53FC7; IntAct: EBI-9356746; Score: 0.40
DE  Interaction: Q9BPW0; IntAct: EBI-9356782; Score: 0.40
DE  Interaction: Q13451; IntAct: EBI-9356807; Score: 0.56
DE  Interaction: Q8IVD9; IntAct: EBI-9356902; Score: 0.40
DE  Interaction: P14618; IntAct: EBI-9353748; Score: 0.44
DE  Interaction: P97313; IntAct: EBI-9544664; Score: 0.52
DE  Interaction: P78527; IntAct: EBI-9545994; Score: 0.48
DE  Interaction: P17936; IntAct: EBI-9546000; Score: 0.54
DE  Interaction: Q9Y6W3; IntAct: EBI-9550636; Score: 0.27
DE  Interaction: O14965; IntAct: EBI-9552223; Score: 0.58
DE  Interaction: Q38SD2; IntAct: EBI-9657355; Score: 0.54
DE  Interaction: P30307; IntAct: EBI-9689039; Score: 0.55
DE  Interaction: P42685; IntAct: EBI-9689033; Score: 0.55
DE  Interaction: P45984; IntAct: EBI-9689021; Score: 0.55
DE  Interaction: Q12929; IntAct: EBI-9688960; Score: 0.71
DE  Interaction: Q07954; IntAct: EBI-9688972; Score: 0.55
DE  Interaction: P32121; IntAct: EBI-9688953; Score: 0.55
DE  Interaction: Q6S5L8; IntAct: EBI-9688947; Score: 0.63
DE  Interaction: P52630; IntAct: EBI-9688785; Score: 0.55
DE  Interaction: O75791; IntAct: EBI-9688773; Score: 0.63
DE  Interaction: O14543; IntAct: EBI-9688761; Score: 0.55
DE  Interaction: O14544; IntAct: EBI-9688767; Score: 0.55
DE  Interaction: Q07890; IntAct: EBI-9688755; Score: 0.55
DE  Interaction: P10636; IntAct: EBI-9689234; Score: 0.55
DE  Interaction: Q8N5H7; IntAct: EBI-9689216; Score: 0.55
DE  Interaction: O00401; IntAct: EBI-9689173; Score: 0.55
DE  Interaction: Q9H6Q3; IntAct: EBI-9689167; Score: 0.55
DE  Interaction: P31946; IntAct: EBI-9689154; Score: 0.55
DE  Interaction: Q99952; IntAct: EBI-9689148; Score: 0.55
DE  Interaction: Q14155; IntAct: EBI-9688935; Score: 0.55
DE  Interaction: Q68CZ2; IntAct: EBI-9688929; Score: 0.68
DE  Interaction: Q13094; IntAct: EBI-9688923; Score: 0.63
DE  Interaction: P05067; IntAct: EBI-9688911; Score: 0.55
DE  Interaction: P49798; IntAct: EBI-9688859; Score: 0.55
DE  Interaction: P49407; IntAct: EBI-9688853; Score: 0.55
DE  Interaction: Q99704; IntAct: EBI-9688841; Score: 0.55
DE  Interaction: P14923; IntAct: EBI-9688829; Score: 0.65
DE  Interaction: P26447; IntAct: EBI-9688823; Score: 0.74
DE  Interaction: P16234; IntAct: EBI-9689130; Score: 0.68
DE  Interaction: Q9BRG2; IntAct: EBI-9689124; Score: 0.63
DE  Interaction: P45983; IntAct: EBI-9689106; Score: 0.55
DE  Interaction: Q9UPY6; IntAct: EBI-9689094; Score: 0.55
DE  Interaction: Q99759; IntAct: EBI-9689082; Score: 0.55
DE  Interaction: Q13153; IntAct: EBI-9689070; Score: 0.55
DE  Interaction: Q8WUI4; IntAct: EBI-9689058; Score: 0.63
DE  Interaction: P15498; IntAct: EBI-9689052; Score: 0.55
DE  Interaction: Q15750; IntAct: EBI-9689415; Score: 0.65
DE  Interaction: Q02156; IntAct: EBI-9689399; Score: 0.55
DE  Interaction: P49069; IntAct: EBI-9689427; Score: 0.63
DE  Interaction: P42229; IntAct: EBI-9689411; Score: 0.63
DE  Interaction: Q02297; IntAct: EBI-9689395; Score: 0.55
DE  Interaction: Q13905; IntAct: EBI-9689457; Score: 0.55
DE  Interaction: Q8TDI0; IntAct: EBI-9689363; Score: 0.55
DE  Interaction: P37840; IntAct: EBI-9689359; Score: 0.55
DE  Interaction: O43639; IntAct: EBI-9689383; Score: 0.55
DE  Interaction: Q9Y5X1; IntAct: EBI-9689379; Score: 0.55
DE  Interaction: Q99963; IntAct: EBI-9689453; Score: 0.55
DE  Interaction: Q92918; IntAct: EBI-9689367; Score: 0.55
DE  Interaction: P19438; IntAct: EBI-9689461; Score: 0.55
DE  Interaction: Q14247; IntAct: EBI-9689626; Score: 0.63
DE  Interaction: Q9Y6K9; IntAct: EBI-9689584; Score: 0.55
DE  Interaction: Q9NZM3; IntAct: EBI-9689760; Score: 0.65
DE  Interaction: Q9Y2R2; IntAct: EBI-9689754; Score: 0.63
DE  Interaction: Q05513; IntAct: EBI-9689736; Score: 0.55
DE  Interaction: P05107; IntAct: EBI-9689742; Score: 0.55
DE  Interaction: P09769; IntAct: EBI-9689730; Score: 0.63
DE  Interaction: Q08881; IntAct: EBI-9689718; Score: 0.55
DE  Interaction: P07949; IntAct: EBI-9689712; Score: 0.55
DE  Interaction: Q12933; IntAct: EBI-9689692; Score: 0.63
DE  Interaction: Q9UGK3; IntAct: EBI-9689680; Score: 0.55
DE  Interaction: P15311; IntAct: EBI-9689656; Score: 0.65
DE  Interaction: Q16620; IntAct: EBI-9689644; Score: 0.55
DE  Interaction: P17252; IntAct: EBI-9689614; Score: 0.63
DE  Interaction: P31749; IntAct: EBI-9689602; Score: 0.55
DE  Interaction: O43561; IntAct: EBI-9689638; Score: 0.63
DE  Interaction: P04049; IntAct: EBI-9689596; Score: 0.55
DE  Interaction: P11309; IntAct: EBI-9689590; Score: 0.55
DE  Interaction: P04150; IntAct: EBI-9689480; Score: 0.63
DE  Interaction: Q92889; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: P19338; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: Q13263; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: P07992; IntAct: EBI-10043997; Score: 0.57
DE  Interaction: Q12906; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: P33991; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: Q12905; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: P11387; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: P35637; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: P09874; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: P27695; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: Q9NXR7; IntAct: EBI-10043963; Score: 0.35
DE  Interaction: Q08211; IntAct: EBI-10043963; Score: 0.35
DE  Interaction: Q14566; IntAct: EBI-10043963; Score: 0.35
DE  Interaction: P39748; IntAct: EBI-10043963; Score: 0.35
DE  Interaction: P25205; IntAct: EBI-10043963; Score: 0.35
DE  Interaction: P18074; IntAct: EBI-10043915; Score: 0.35
DE  Interaction: Q86VI4; IntAct: EBI-10762157; Score: 0.60
DE  Interaction: Q9UPT5; IntAct: EBI-10764463; Score: 0.46
DE  Interaction: Q96A65; IntAct: EBI-10764367; Score: 0.50
DE  Interaction: Q8IYI6; IntAct: EBI-10764512; Score: 0.40
DE  Interaction: Q80U62; IntAct: EBI-10764527; Score: 0.50
DE  Interaction: O54921; IntAct: EBI-10764545; Score: 0.35
DE  Interaction: Q96KP1; IntAct: EBI-10821928; Score: 0.40
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P0CK49; IntAct: EBI-11725356; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: P0CK58; IntAct: EBI-11732874; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: Q8AZJ3; IntAct: EBI-11734105; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-10888004; Score: 0.47
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: Q8NBJ4; IntAct: EBI-12735639; Score: 0.64
DE  Interaction: P62491; IntAct: EBI-12686343; Score: 0.40
DE  Interaction: P15363; IntAct: EBI-13644052; Score: 0.40
DE  Interaction: P07355; IntAct: EBI-13644057; Score: 0.58
DE  Interaction: P60033; IntAct: EBI-20568535; Score: 0.60
DE  Interaction: Q15262; IntAct: EBI-21624743; Score: 0.35
DE  Interaction: P59665; IntAct: EBI-21626698; Score: 0.35
DE  Interaction: Q92187; IntAct: EBI-21641713; Score: 0.35
DE  Interaction: Q9Y5F2; IntAct: EBI-21658599; Score: 0.35
DE  Interaction: Q13635; IntAct: EBI-21717305; Score: 0.35
DE  Interaction: P46098; IntAct: EBI-21749232; Score: 0.35
DE  Interaction: Q15165; IntAct: EBI-21790723; Score: 0.35
DE  Interaction: Q6XE38; IntAct: EBI-21823039; Score: 0.35
DE  Interaction: Q15109; IntAct: EBI-15599395; Score: 0.52
DE  Interaction: Q96FE5; IntAct: EBI-15654884; Score: 0.40
DE  Interaction: P62974; IntAct: EBI-15666144; Score: 0.40
DE  Interaction: P51149; IntAct: EBI-15727368; Score: 0.35
DE  Interaction: Q6NZI2; IntAct: EBI-15727368; Score: 0.35
DE  Interaction: P62991; IntAct: EBI-15794515; Score: 0.40
DE  Interaction: O14964; IntAct: EBI-15844252; Score: 0.54
DE  Interaction: Q9UKV8; IntAct: EBI-16056423; Score: 0.68
DE  Interaction: Q07889; IntAct: EBI-16158038; Score: 0.56
DE  Interaction: P14174; IntAct: EBI-16170998; Score: 0.59
DE  Interaction: Q14956; IntAct: EBI-16191087; Score: 0.54
DE  Interaction: P23470; IntAct: EBI-16824749; Score: 0.57
DE  Interaction: Q9BZP6; IntAct: EBI-16880687; Score: 0.40
DE  Interaction: P46934; IntAct: EBI-20218869; Score: 0.46
DE  Interaction: Q92731; IntAct: EBI-20765014; Score: 0.50
DE  Interaction: P18433; IntAct: EBI-20827451; Score: 0.63
DE  Interaction: Q9HD43; IntAct: EBI-20827459; Score: 0.51
DE  Interaction: O14522; IntAct: EBI-20977004; Score: 0.37
DE  Interaction: P35813; IntAct: EBI-20977309; Score: 0.51
DE  Interaction: Q15256; IntAct: EBI-20980716; Score: 0.37
DE  Interaction: P35236; IntAct: EBI-20980726; Score: 0.37
DE  Interaction: P16298; IntAct: EBI-20980676; Score: 0.37
DE  Interaction: Q8WTR2; IntAct: EBI-20980756; Score: 0.37
DE  Interaction: Q9H0C8; IntAct: EBI-20980706; Score: 0.37
DE  Interaction: O75688; IntAct: EBI-20980696; Score: 0.37
DE  Interaction: Q8WUJ0; IntAct: EBI-20980766; Score: 0.37
DE  Interaction: Q9Y6Q6; IntAct: EBI-20939033; Score: 0.46
DE  Interaction: O95859; IntAct: EBI-21222657; Score: 0.35
DE  Interaction: Q99075; IntAct: EBI-21401577; Score: 0.61
DE  Interaction: O15357; IntAct: EBI-22083895; Score: 0.35
DE  Interaction: Q9UKW4; IntAct: EBI-22083950; Score: 0.35
DE  Interaction: Q63768; IntAct: EBI-22084092; Score: 0.35
DE  Interaction: D3ZYG0; IntAct: EBI-22084092; Score: 0.35
DE  Interaction: P54100; IntAct: EBI-22084092; Score: 0.35
DE  Interaction: Q5U2U2; IntAct: EBI-22084092; Score: 0.35
DE  Interaction: F1LWB1; IntAct: EBI-22084092; Score: 0.35
DE  Interaction: Q62985; IntAct: EBI-22084260; Score: 0.35
DE  Interaction: Q64725; IntAct: EBI-22084260; Score: 0.35
DE  Interaction: Q9WVR3; IntAct: EBI-22084260; Score: 0.35
DE  Interaction: Q5RJK6; IntAct: EBI-22084260; Score: 0.35
DE  Interaction: F1LNG5; IntAct: EBI-22085491; Score: 0.35
DE  Interaction: B2RZ33; IntAct: EBI-22085491; Score: 0.35
DE  Interaction: Q9QZC5; IntAct: EBI-22085491; Score: 0.50
DE  Interaction: P50904; IntAct: EBI-22179932; Score: 0.35
DE  Interaction: P32577; IntAct: EBI-22179950; Score: 0.35
DE  Interaction: P41499; IntAct: EBI-22179950; Score: 0.35
DE  Interaction: Q9WUD9; IntAct: EBI-22179950; Score: 0.35
DE  Interaction: Q8CFN2; IntAct: EBI-22180003; Score: 0.35
DE  Interaction: A0A0G2K3B0; IntAct: EBI-22180003; Score: 0.35
DE  Interaction: A0A0G2JSR4; IntAct: EBI-22180124; Score: 0.35
DE  Interaction: Q5XI26; IntAct: EBI-22180124; Score: 0.35
DE  Interaction: F1M9D6; IntAct: EBI-22180124; Score: 0.35
DE  Interaction: Q8K4S7; IntAct: EBI-22237510; Score: 0.35
DE  Interaction: D3ZY64; IntAct: EBI-22237510; Score: 0.35
DE  Interaction: B2GV15; IntAct: EBI-22237510; Score: 0.35
DE  Interaction: D3ZV15; IntAct: EBI-22237510; Score: 0.35
DE  Interaction: P24135; IntAct: EBI-22237486; Score: 0.35
DE  Interaction: P10686; IntAct: EBI-22237486; Score: 0.35
DE  Interaction: E9PT59; IntAct: EBI-22237831; Score: 0.35
DE  Interaction: D4A3T0; IntAct: EBI-22237831; Score: 0.35
DE  Interaction: P59622; IntAct: EBI-22237831; Score: 0.35
DE  Interaction: Q8R424; IntAct: EBI-22237831; Score: 0.35
DE  Interaction: F1M3E4; IntAct: EBI-22237831; Score: 0.35
DE  Interaction: Q920L0; IntAct: EBI-22237831; Score: 0.35
DE  Interaction: Q4KM68; IntAct: EBI-22237831; Score: 0.35
DE  Interaction: D3ZG10; IntAct: EBI-22237831; Score: 0.35
DE  Interaction: Q9EQH1; IntAct: EBI-22237766; Score: 0.35
DE  Interaction: P97573; IntAct: EBI-22237766; Score: 0.35
DE  Interaction: P85968; IntAct: EBI-22237766; Score: 0.35
DE  Interaction: D4A5Q1; IntAct: EBI-22237766; Score: 0.35
DE  Interaction: P52631; IntAct: EBI-22237766; Score: 0.35
DE  Interaction: Q63788; IntAct: EBI-22237766; Score: 0.35
DE  Interaction: P08461; IntAct: EBI-22238066; Score: 0.35
DE  Interaction: P15651; IntAct: EBI-22238080; Score: 0.35
DE  Interaction: A0A0R4J8U1; IntAct: EBI-22238080; Score: 0.35
DE  Interaction: Q63065; IntAct: EBI-22238008; Score: 0.35
DE  Interaction: Q5M824; IntAct: EBI-22238008; Score: 0.35
DE  Interaction: Q32PX8; IntAct: EBI-22238008; Score: 0.35
DE  Interaction: B5DFI9; IntAct: EBI-22238008; Score: 0.35
DE  Interaction: F1M9C0; IntAct: EBI-22238008; Score: 0.35
DE  Interaction: D3Z8I4; IntAct: EBI-22238008; Score: 0.35
DE  Interaction: Q00972; IntAct: EBI-22238008; Score: 0.35
DE  Interaction: P52632; IntAct: EBI-22238008; Score: 0.35
DE  Interaction: Q5BK11; IntAct: EBI-22238008; Score: 0.35
DE  Interaction: O55156; IntAct: EBI-22238008; Score: 0.35
DE  Interaction: Q6AZ23; IntAct: EBI-22241891; Score: 0.35
DE  Interaction: A0A0G2K064; IntAct: EBI-22241891; Score: 0.35
DE  Interaction: P24155; IntAct: EBI-22241891; Score: 0.35
DE  Interaction: P84083; IntAct: EBI-22241891; Score: 0.35
DE  Interaction: Q7TT49; IntAct: EBI-22241891; Score: 0.35
DE  Interaction: A9CMB8; IntAct: EBI-22241875; Score: 0.35
DE  Interaction: P50116; IntAct: EBI-22241875; Score: 0.35
DE  Interaction: F1MAF2; IntAct: EBI-22266198; Score: 0.35
DE  Interaction: Q6ZWB6; IntAct: EBI-25370031; Score: 0.37
DE  Interaction: Q14515; IntAct: EBI-25370141; Score: 0.37
DE  Interaction: P0DMV8; IntAct: EBI-25370295; Score: 0.37
DE  Interaction: P23469; IntAct: EBI-25370790; Score: 0.37
DE  Interaction: Q58FF7; IntAct: EBI-25380009; Score: 0.35
DE  Interaction: P09651; IntAct: EBI-25380009; Score: 0.35
DE  Interaction: Q32P51; IntAct: EBI-25380009; Score: 0.35
DE  Interaction: P17844; IntAct: EBI-25380009; Score: 0.35
DE  Interaction: P61221; IntAct: EBI-25380009; Score: 0.35
DE  Interaction: Q8IXB1; IntAct: EBI-25380009; Score: 0.48
DE  Interaction: P60709; IntAct: EBI-25391021; Score: 0.35
DE  Interaction: Q15208; IntAct: EBI-25391021; Score: 0.35
DE  Interaction: Q16875; IntAct: EBI-25391021; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-25391021; Score: 0.35
DE  Interaction: Q9ULV4; IntAct: EBI-25391021; Score: 0.35
DE  Interaction: Q9Y383; IntAct: EBI-25391021; Score: 0.35
DE  Interaction: P0DJI4; IntAct: EBI-22303808; Score: 0.35
DE  Interaction: O94898; IntAct: EBI-25414995; Score: 0.46
DE  Interaction: Q96JA1; IntAct: EBI-25467913; Score: 0.74
DE  Interaction: O14944; IntAct: EBI-25434733; Score: 0.62
DE  Interaction: Q6UW88; IntAct: EBI-25434749; Score: 0.62
DE  Interaction: P35070; IntAct: EBI-25434882; Score: 0.44
DE  Interaction: P15514; IntAct: EBI-25434902; Score: 0.44
DE  Interaction: Q9BXH1; IntAct: EBI-25466126; Score: 0.40
DE  Interaction: O43752; IntAct: EBI-25466975; Score: 0.46
DE  Interaction: Q63635; IntAct: EBI-25467027; Score: 0.27
DE  Interaction: P69479; IntAct: EBI-25568044; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.35
DE  Interaction: P0DTC2; IntAct: EBI-26592776; Score: 0.54
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P63252; IntAct: EBI-28956270; Score: 0.27
DE  Interaction: O15194; IntAct: EBI-27115784; Score: 0.27
DE  Interaction: P0DTD8; IntAct: EBI-27127141; Score: 0.35
DE  Interaction: Q96ST3; IntAct: EBI-30836929; Score: 0.44
DE  Interaction: Q13885; IntAct: EBI-32717697; Score: 0.50
DE  Interaction: Q9NVI1; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: O14980; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q14257; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-32717697; Score: 0.42
DE  Interaction: Q9UBV2; IntAct: EBI-32717697; Score: 0.50
DE  Interaction: Q8TEM1; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q7Z3U7; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q9Y4L1; IntAct: EBI-32717697; Score: 0.53
DE  Interaction: Q5SRE5; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q5T9A4; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: P01893; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: P19823; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q00059; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: O94822; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: P51571; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q9BXW9; IntAct: EBI-32717697; Score: 0.50
DE  Interaction: Q13438; IntAct: EBI-32717697; Score: 0.50
DE  Interaction: P52926; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q6ZNB6; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: O75843; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q9BSD7; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: P61619; IntAct: EBI-32717697; Score: 0.50
DE  Interaction: Q9H583; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: O43819; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: P47869; IntAct: EBI-32717697; Score: 0.50
DE  Interaction: Q15653; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q92504; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q8WVX9; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q9NZ01; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: O15438; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: O94933; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: O75155; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q92973; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q2M3M2; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: Q9Y2A7; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q01484; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P52594; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q96RU3; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P09012; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q92738; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8IYB1; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q16625; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q12955; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q15811; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q96RT1; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q7Z2K8; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q12923; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q7L576; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UHD8; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9P0K7; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q14126; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q7Z3T8; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9HAU0; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q92598; IntAct: EBI-32720286; Score: 0.47
DE  Interaction: Q96AC1; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UGP4; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: A8MVW0; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9BSJ8; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O95487; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q96F07; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O95757; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q15334; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9H3P7; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9HB21; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q7Z2W4; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q5T2T1; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O43865; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8NDI1; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q5JSH3; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P35241; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q0JRZ9; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9ULH0; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q15437; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P35612; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q96TA1; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q92599; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O95486; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q86YQ8; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q15654; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q96HN2; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q14141; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UHR4; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9P265; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O95819; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9H4G0; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UKE5; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q15436; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8IY81; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8IZP0; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q01968; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UGI8; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9Y217; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9NNW5; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P35240; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q02487; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q04721; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q13425; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9P0V9; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q6WCQ1; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q7KZI7; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9Y4K4; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8IYB5; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q13492; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q99618; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9NUP9; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O95405; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q5VUB5; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P41743; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q86X29; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O14639; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q96JB5; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O95721; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9NZ52; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8TEW0; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q13642; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9H2D6; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9P2D6; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8WU79; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P51648; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UNF0; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9H2J7; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q15311; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q96S66; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9NYB9; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P61081; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q07960; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q7Z6J0; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q96Q05; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9H425; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9GZT9; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8WUW1; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9Y2I1; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9C0B5; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9NRW7; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9H792; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q96QG7; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O43318; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8NEU8; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P98082; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9H939; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q13586; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q12792; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9HDC5; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O95292; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q92734; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q6WKZ4; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9HD26; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9H8Y8; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O60858; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UH03; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UKD2; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q00013; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9Y4J8; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q13177; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9H1K0; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P48553; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8NI08; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O75116; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P08240; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P61088; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8TAA9; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q14254; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q86WR0; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UQN3; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O60869; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q96KQ4; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q53SF7; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O95208; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q13610; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q6ZVF9; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8WU20; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P15170; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UH65; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O60493; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O43617; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8NBS9; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: C4AMC7; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8TDM6; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q8IXS6; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q5HYI8; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: O60925; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q12774; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q13541; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q5HYK7; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q9UQ80; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: P36776; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: P06733; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: Q9NYU2; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: P36952; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: Q9NSE4; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: P80723; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: Q99798; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: P50995; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: P08865; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: Q9Y696; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: P08758; IntAct: EBI-34582286; Score: 0.35
DE  Interaction: P29144; IntAct: EBI-34582286; Score: 0.35
GO  GO:0009925;
GO  GO:0016323;
GO  GO:0030054;
GO  GO:0009986;
GO  GO:0030669;
GO  GO:0005737;
GO  GO:0031901;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0010008;
GO  GO:0005615;
GO  GO:0005925;
GO  GO:0000139;
GO  GO:0005887;
GO  GO:0097708;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0097489;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0043235;
GO  GO:0032587;
GO  GO:0070435;
GO  GO:0044214;
GO  GO:0051015;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0045296;
GO  GO:0003682;
GO  GO:0003690;
GO  GO:0019899;
GO  GO:0048408;
GO  GO:0005006;
GO  GO:0042802;
GO  GO:0019900;
GO  GO:0004709;
GO  GO:0019903;
GO  GO:0030296;
GO  GO:0004713;
GO  GO:0030297;
GO  GO:0004714;
GO  GO:0004888;
GO  GO:0031625;
GO  GO:0001618;
GO  GO:0007202;
GO  GO:0030154;
GO  GO:0000902;
GO  GO:0007166;
GO  GO:0098609;
GO  GO:0071230;
GO  GO:0071276;
GO  GO:0071364;
GO  GO:0071392;
GO  GO:0034614;
GO  GO:0021795;
GO  GO:0048546;
GO  GO:0001892;
GO  GO:0007173;
GO  GO:0050673;
GO  GO:0038134;
GO  GO:0061029;
GO  GO:0001942;
GO  GO:0007611;
GO  GO:0060571;
GO  GO:0043066;
GO  GO:1905208;
GO  GO:0042059;
GO  GO:0042177;
GO  GO:0001503;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0090263;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0045737;
GO  GO:0045739;
GO  GO:0045740;
GO  GO:0045893;
GO  GO:0050679;
GO  GO:0070374;
GO  GO:0048146;
GO  GO:1900087;
GO  GO:0033674;
GO  GO:0043406;
GO  GO:1903800;
GO  GO:1901224;
GO  GO:0010750;
GO  GO:0033138;
GO  GO:0042327;
GO  GO:0051897;
GO  GO:1900020;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0045944;
GO  GO:0046777;
GO  GO:0051205;
GO  GO:0070372;
GO  GO:0046328;
GO  GO:0050999;
GO  GO:0050730;
GO  GO:0014066;
GO  GO:0070141;
GO  GO:0007435;
GO  GO:0007165;
GO  GO:0007169;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLK
SQ  TIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVE
SQ  SIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC
SQ  TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEE
SQ  DGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKE
SQ  ITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL
SQ  FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHP
SQ  ECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNG
SQ  PKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS
SQ  GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLD
SQ  YVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKW
SQ  MALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK
SQ  FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSA
SQ  TSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPS
SQ  RDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV
SQ  APQSSEFIGA
//
ID  P55245;
PN  Epidermal growth factor receptor;
GN  EGFR;
OS  9544;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00533}; Single- pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Nucleus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endosome {ECO:0000250|UniProtKB:P00533}. Endosome membrane {ECO:0000250|UniProtKB:P00533}. Nucleus {ECO:0000250|UniProtKB:P00533}. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF). {ECO:0000250|UniProtKB:P00533}.
DR  UNIPROT: P55245;
DR  UNIPROT: F6YXS7;
DR  UNIPROT: G7ML99;
DR  UNIPROT: H9FAB2;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF07714;
DR  Pfam: PF01030;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (By similarity). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (By similarity). Plays a role in enhancing learning and memory performance (By similarity). {ECO:0000250|UniProtKB:P00533, ECO:0000250|UniProtKB:Q01279}.
DE  Reference Proteome: Yes;
GO  GO:0009925;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0010008;
GO  GO:0000139;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0043235;
GO  GO:0005524;
GO  GO:0003682;
GO  GO:0048408;
GO  GO:0005006;
GO  GO:0004713;
GO  GO:0004714;
GO  GO:0030154;
GO  GO:0071364;
GO  GO:0071392;
GO  GO:0007173;
GO  GO:0007611;
GO  GO:0043066;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0050679;
GO  GO:0070374;
GO  GO:0033674;
GO  GO:1902966;
GO  GO:0001934;
GO  GO:0045944;
GO  GO:0046777;
GO  GO:0007169;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLK
SQ  TIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVE
SQ  SIQWRDIVSSEFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC
SQ  TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEE
SQ  DGVRKCKKCEGPCRKVCNGIGIGEFKDTLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKE
SQ  ITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL
SQ  FGTSSQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCQNVSRGRECVDKCNVLEGEPREFVENSECIQCHP
SQ  ECLPQVMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCARNG
SQ  PKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS
SQ  GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLD
SQ  YVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKW
SQ  MALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK
SQ  FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSA
SQ  TSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPS
SQ  RDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV
SQ  APQSSEFIGA
//
ID  Q01279;
PN  Epidermal growth factor receptor;
GN  Egfr;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00533}; Single- pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Nucleus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endosome {ECO:0000250|UniProtKB:P00533}. Endosome membrane {ECO:0000250|UniProtKB:P00533}. Nucleus {ECO:0000250|UniProtKB:P00533}. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF). {ECO:0000250|UniProtKB:P00533}.
DR  UNIPROT: Q01279;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF07714;
DR  Pfam: PF01030;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:8404850). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (By similarity). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (By similarity). Plays a role in enhancing learning and memory performance (PubMed:20639532). {ECO:0000250|UniProtKB:P00533, ECO:0000269|PubMed:10953014, ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:8404850}.
DE  Reference Proteome: Yes;
DE  Interaction: P42567; IntAct: EBI-7373206; Score: 0.44
DE  Interaction: O70469; IntAct: EBI-7588761; Score: 0.40
DE  Interaction: O54928; IntAct: EBI-7477248; Score: 0.40
DE  Interaction: P01132; IntAct: EBI-7853849; Score: 0.40
DE  Interaction: P18031; IntAct: EBI-7945363; Score: 0.40
DE  Interaction: P01133; IntAct: EBI-8618729; Score: 0.44
DE  Interaction: P35831; IntAct: EBI-8614373; Score: 0.40
DE  Interaction: P32883; IntAct: EBI-6296299; Score: 0.46
DE  Interaction: P22682; IntAct: EBI-8846800; Score: 0.50
DE  Interaction: Q60631; IntAct: EBI-8846800; Score: 0.35
DE  Interaction: Q15109; IntAct: EBI-15599433; Score: 0.52
DE  Interaction: O54890; IntAct: EBI-15645972; Score: 0.40
DE  Interaction: Q9D1T0; IntAct: EBI-15654918; Score: 0.40
DE  Interaction: P62991; IntAct: EBI-15844305; Score: 0.40
DE  Interaction: Q91XA9; IntAct: EBI-16880617; Score: 0.27
DE  Interaction: P70193; IntAct: EBI-25424163; Score: 0.40
DE  Interaction: Q9JKY5; IntAct: EBI-27088765; Score: 0.40
GO  GO:0016324;
GO  GO:0009925;
GO  GO:0016323;
GO  GO:0030054;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0031901;
GO  GO:0030139;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0010008;
GO  GO:0000139;
GO  GO:0005887;
GO  GO:0097708;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0097489;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0043235;
GO  GO:0032587;
GO  GO:0044214;
GO  GO:0045202;
GO  GO:0051015;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0003682;
GO  GO:0019899;
GO  GO:0048408;
GO  GO:0005006;
GO  GO:0042802;
GO  GO:0005178;
GO  GO:0016301;
GO  GO:0019900;
GO  GO:0030235;
GO  GO:0019901;
GO  GO:0019903;
GO  GO:0030296;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0030297;
GO  GO:0004714;
GO  GO:0004888;
GO  GO:0031625;
GO  GO:0048143;
GO  GO:0030154;
GO  GO:0000902;
GO  GO:0008283;
GO  GO:0007166;
GO  GO:0098609;
GO  GO:0071230;
GO  GO:0071276;
GO  GO:0071549;
GO  GO:0071364;
GO  GO:0071392;
GO  GO:0071363;
GO  GO:0071260;
GO  GO:0034614;
GO  GO:0071466;
GO  GO:0021795;
GO  GO:0007623;
GO  GO:0048546;
GO  GO:0016101;
GO  GO:0001892;
GO  GO:0007173;
GO  GO:0008544;
GO  GO:0050673;
GO  GO:0038134;
GO  GO:0061029;
GO  GO:0001942;
GO  GO:0042743;
GO  GO:0035556;
GO  GO:0007611;
GO  GO:0097421;
GO  GO:0030324;
GO  GO:0010960;
GO  GO:0007494;
GO  GO:0060571;
GO  GO:0043066;
GO  GO:1905208;
GO  GO:0045930;
GO  GO:0042177;
GO  GO:0048812;
GO  GO:0042698;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0045780;
GO  GO:0090263;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0045737;
GO  GO:0045739;
GO  GO:0045740;
GO  GO:0045893;
GO  GO:0050679;
GO  GO:0070374;
GO  GO:0048146;
GO  GO:1900087;
GO  GO:0060252;
GO  GO:0050729;
GO  GO:0033674;
GO  GO:0043406;
GO  GO:0043410;
GO  GO:1903800;
GO  GO:0070257;
GO  GO:1901224;
GO  GO:0010750;
GO  GO:0033138;
GO  GO:0042327;
GO  GO:1902722;
GO  GO:0051897;
GO  GO:1900020;
GO  GO:1902966;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0048661;
GO  GO:0032930;
GO  GO:0051968;
GO  GO:0045944;
GO  GO:0045907;
GO  GO:0046777;
GO  GO:0042127;
GO  GO:0070372;
GO  GO:0046328;
GO  GO:0050999;
GO  GO:0050730;
GO  GO:0014066;
GO  GO:0051592;
GO  GO:0033590;
GO  GO:0033594;
GO  GO:0006970;
GO  GO:0070141;
GO  GO:0007435;
GO  GO:0007165;
GO  GO:0043586;
GO  GO:0006412;
GO  GO:0007169;
GO  GO:0042311;
GO  GO:0042060;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRPSGTARTTLLVLLTALCAAGGALEEKKVCQGTSNRLTQLGTFEDHFLSLQRMYNNCEVVLGNLEITYVQRNYDLSFLK
SQ  TIQEVAGYVLIALNTVERIPLENLQIIRGNALYENTYALAILSNYGTNRTGLRELPMRNLQEILIGAVRFSNNPILCNMD
SQ  TIQWRDIVQNVFMSNMSMDLQSHPSSCPKCDPSCPNGSCWGGGEENCQKLTKIICAQQCSHRCRGRSPSDCCHNQCAAGC
SQ  TGPRESDCLVCQKFQDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGPDYYEVEE
SQ  DGIRKCKKCDGPCRKVCNGIGIGEFKDTLSINATNIKHFKYCTAISGDLHILPVAFKGDSFTRTPPLDPRELEILKTVKE
SQ  ITGFLLIQAWPDNWTDLHAFENLEIIRGRTKQHGQFSLAVVGLNITSLGLRSLKEISDGDVIISGNRNLCYANTINWKKL
SQ  FGTPNQKTKIMNNRAEKDCKAVNHVCNPLCSSEGCWGPEPRDCVSCQNVSRGRECVEKCNILEGEPREFVENSECIQCHP
SQ  ECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGIMGENNTLVWKYADANNVCHLCHANCTYGCAGPGLQGCEVWP
SQ  SGPKIPSIATGIVGGLLFIVVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQAHLRILKETEFKKIKVL
SQ  GSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPYGCL
SQ  LDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPI
SQ  KWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASDISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSR
SQ  PKFRELILEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMEDVVDADEYLIPQQGFFNSPSTSRTPLLSSL
SQ  SATSNNSTVACINRNGSCRVKEDAFLQRYSSDPTGAVTEDNIDDAFLPVPEYVNQSVPKRPAGSVQNPVYHNQPLHPAPG
SQ  RDLHYQNPHSNAVGNPEYLNTAQPTCLSSGFNSPALWIQKGSHQMSLDNPDYQQDFFPKETKPNGIFKGPTAENAEYLRV
SQ  APPSSEFIGA
//
ID  Q18250;
PN  Early growth response factor homolog 1;
GN  egrh;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:20736289}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20736289}. Note=Perinuclear localization only observed in sperm. {ECO:0000269|PubMed:20736289}.
DR  UNIPROT: Q18250;
DR  Pfam: PF00096;
DR  PROSITE: PS00028;
DR  PROSITE: PS50157;
DE  Function: Sequence-specific DNA-binding transcription factor (By similarity). Plays a role in oocyte development, acting cell- autonomously in the somatic gonad (PubMed:20736289). Involved in negative regulation of oocyte MAPK activation and inhibits oocyte maturation and ovulation (PubMed:20736289). {ECO:0000250|UniProtKB:P11161, ECO:0000269|PubMed:20736289}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000981;
GO  GO:0046872;
GO  GO:0000978;
GO  GO:0043407;
GO  GO:1900194;
GO  GO:0060280;
GO  GO:0006357;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALHEPPSKLNRHSHSNLLKPPSLNKPILTFADNDCLKTPTMNDMLKTPTVNSPRHTPMNIDGTPKVNGFSGFTPQTDQK
SQ  FFGEHEPLFNQMHTTTLMPAPSSSYKEPAYSSEQPSSSSDEAKPKELLGSNSFGVPRMTNGNSKQKPEELTLKDIEISST
SQ  GPGGVDSPGLSAAMFQFSPMVEHFLQNLTNKAGLPELVVDSKTAGLNHQEPSDLIKSVQVRRSSIEDQKFSDVLHVPTLP
SQ  RKTSEPSHLGSSLQNEHPQSNSRPSTVIPRVQRTNTSASLTRSMDHSSMSPISAHDDPYSNSASYSSLSTHTSFSDSASL
SQ  AHFEPKTEPMDDYSYNFSDNDFNSFEFSSTSEELKNIGCQKMKSSKMPLQDRPYKCPRDGCDRRFSRSDELTRHIRIHTG
SQ  QKPFQCRICMRAFSRSDHLTTHVRTHTGEKPFSCDICGRKFARSDERKRHTKVHKTSRSGS
//
ID  O14681;
PN  Etoposide-induced protein 2.4 homolog;
GN  EI24;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:21154811}; Multi-pass membrane protein {ECO:0000269|PubMed:21154811}. Cytoplasm {ECO:0000269|PubMed:21154811}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: O14681;
DR  UNIPROT: A8K7D6;
DR  UNIPROT: B4DKL6;
DR  UNIPROT: Q9BUQ1;
DR  OMIM: 605170;
DR  DisGeNET: 9538;
DE  Function: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250}.
DE  Disease: Note=EI24 is on a chromosomal region frequently deleted in solid tumors, and it is thought to play a role in breast and cervical cancer. Particularly, expression analysis of EI24 in cancerous tissues shows that EI24 loss is associated with tumor invasiveness.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626169; Score: 0.35
DE  Interaction: P51668; IntAct: EBI-2339419; Score: 0.37
DE  Interaction: P62837; IntAct: EBI-2339474; Score: 0.37
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q9WMX2; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: P11234; IntAct: EBI-12451925; Score: 0.51
DE  Interaction: P27105; IntAct: EBI-12452286; Score: 0.51
DE  Interaction: Q8N4P2; IntAct: EBI-12452567; Score: 0.51
DE  Interaction: Q9NUH8; IntAct: EBI-24698409; Score: 0.56
DE  Interaction: O15173; IntAct: EBI-24712104; Score: 0.56
DE  Interaction: Q12982; IntAct: EBI-24742623; Score: 0.56
DE  Interaction: Q9UI14; IntAct: EBI-24743382; Score: 0.56
DE  Interaction: Q6PL24; IntAct: EBI-25225021; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: P51685; IntAct: EBI-20804904; Score: 0.37
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9H5K3; IntAct: EBI-28948637; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0061676;
GO  GO:0006915;
GO  GO:0016236;
GO  GO:0030308;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADSVKTFLQDLARGIKDSIWGICTISKLDARIQQKREEQRRRRASSVLAQRRAQSIERKQESEPRIVSRIFQCCAWNGG
SQ  VFWFSLLLFYRVFIPVLQSVTARIIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRK
SQ  PHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWP
SQ  YYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSTS
SQ  AEKFPSPHPSPAKLKATAGH
//
ID  Q61070;
PN  Etoposide-induced protein 2.4;
GN  Ei24;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15781622}; Multi-pass membrane protein {ECO:0000269|PubMed:15781622}.
DR  UNIPROT: Q61070;
DR  UNIPROT: Q3T9X1;
DR  UNIPROT: Q3TVX9;
DR  UNIPROT: Q3UGS7;
DE  Function: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250, ECO:0000269|PubMed:10594026, ECO:0000269|PubMed:15781622}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0061676;
GO  GO:0006914;
GO  GO:0071494;
GO  GO:0008630;
GO  GO:0016236;
GO  GO:0030308;
GO  GO:0042308;
GO  GO:0050885;
GO  GO:2001244;
GO  GO:0009410;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADSVKTFLQDLGRGIKDSIWGICTISKLDARIQQKREEQRRRRASSLLAQRRPQSVERKQESEPRIVSRIFQCCAWNGG
SQ  VFWFSLLLFYRVFIPVLQSVTARIIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRK
SQ  PHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWP
SQ  YYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSSS
SQ  AEKFPSPHPSPAKLKAAAGH
//
ID  Q4KM77;
PN  Etoposide-induced protein 2.4 homolog;
GN  Ei24;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q4KM77;
DE  Function: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy. {ECO:0000269|PubMed:20550938}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0061676;
GO  GO:0006914;
GO  GO:0071494;
GO  GO:0008630;
GO  GO:0016236;
GO  GO:0030308;
GO  GO:0042308;
GO  GO:0050885;
GO  GO:2001244;
GO  GO:0009410;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADSVKTFLQDLGRGIKDSIWGICTISKLDARIQQKREEQRRRRASSLLAQRRAQSVERKQESEPRIVSRIFQCCAWNGG
SQ  VFWFSLLLFYRVFIPVLQSVTARVIGDPSLHGDVWSWLEFFLTSIFSALWVLPLFVLSKVVNAIWFQDIADLAFEVSGRK
SQ  PHPFPSVSKIIADMLFNLLLQALFLIQGMFVSLFPIHLVGQLVSLLHMSLLYSLYCFEYRWFNKGIEMHQRLSNIERNWP
SQ  YYFGFGLPLAFLTAMQSSYIISGCLFSILFPLFIISANEAKTPGKAYLFQLRLFSLVVFLSNRLFHKTVYLQSALSSSSS
SQ  AEKFPSPHPSPAKLKAAAGH
//
ID  Q3ZC12;
PN  Eukaryotic translation initiation factor 3 subunit G;
GN  EIF3G;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03006}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006}. Note=Colocalizes with AIFM1 in the nucleus and perinuclear region. {ECO:0000255|HAMAP- Rule:MF_03006}.
DR  UNIPROT: Q3ZC12;
DR  Pfam: PF12353;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre- initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. This subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006}.
DE  Reference Proteome: Yes;
GO  GO:0016282;
GO  GO:0033290;
GO  GO:0005852;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0003743;
GO  GO:0001732;
GO  GO:0006413;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSLEPELLPGAPLPPPKEVINGNIKTVTEYRIDEDGKKFK
SQ  IVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRIC
SQ  KGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNAT
SQ  IRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN
//
ID  O75821;
PN  Eukaryotic translation initiation factor 3 subunit G;
GN  EIF3G;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Note=Colocalizes with AIFM1 in the nucleus and perinuclear region.
DR  UNIPROT: O75821;
DR  UNIPROT: O14801;
DR  UNIPROT: Q969U5;
DR  PDB: 2CQ0;
DR  PDB: 2MJC;
DR  PDB: 5K0Y;
DR  PDB: 6YBS;
DR  PDB: 6ZMW;
DR  Pfam: PF12353;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DR  OMIM: 603913;
DR  DisGeNET: 8666;
DE  Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF- 2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem- loop binding to exert either translational activation or repression (PubMed:25849773). This subunit can bind 18S rRNA. {ECO:0000255|HAMAP- Rule:MF_03006, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}. (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.
DE  Reference Proteome: Yes;
DE  Interaction: P55884; IntAct: EBI-366642; Score: 0.86
DE  Interaction: O75822; IntAct: EBI-366663; Score: 0.35
DE  Interaction: Q99547; IntAct: EBI-373791; Score: 0.00
DE  Interaction: O60739; IntAct: EBI-1059553; Score: 0.00
DE  Interaction: P62330; IntAct: EBI-1068233; Score: 0.00
DE  Interaction: O95831; IntAct: EBI-7083391; Score: 0.60
DE  Interaction: Q13347; IntAct: EBI-7083418; Score: 0.69
DE  Interaction: O15372; IntAct: EBI-2510472; Score: 0.56
DE  Interaction: Q9Y6I4; IntAct: EBI-2512627; Score: 0.40
DE  Interaction: Q9Z0R6; IntAct: EBI-2557425; Score: 0.40
DE  Interaction: P23116; IntAct: EBI-2559355; Score: 0.56
DE  Interaction: Q5NEC0; IntAct: EBI-2807069; Score: 0.00
DE  Interaction: A0A5P8YFD8; IntAct: EBI-2870697; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q9P2Y5; IntAct: EBI-3622729; Score: 0.35
DE  Interaction: P54619; IntAct: EBI-8638625; Score: 0.37
DE  Interaction: O95257; IntAct: EBI-7156156; Score: 0.37
DE  Interaction: Q13526; IntAct: EBI-7302217; Score: 0.37
DE  Interaction: Q16513; IntAct: EBI-7308665; Score: 0.37
DE  Interaction: Q16637; IntAct: EBI-7388997; Score: 0.37
DE  Interaction: P37840; IntAct: EBI-7391140; Score: 0.37
DE  Interaction: P04183; IntAct: EBI-7397222; Score: 0.37
DE  Interaction: B2BUF1; IntAct: EBI-6110503; Score: 0.35
DE  Interaction: P03366; IntAct: EBI-6174791; Score: 0.46
DE  Interaction: O00571; IntAct: EBI-6261906; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-10189737; Score: 0.56
DE  Interaction: Q8IZU0; IntAct: EBI-10189751; Score: 0.56
DE  Interaction: Q9H074; IntAct: EBI-10766330; Score: 0.35
DE  Interaction: Q99613; IntAct: EBI-10766374; Score: 0.67
DE  Interaction: Q14152; IntAct: EBI-10766374; Score: 0.67
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: E9QNG1; IntAct: EBI-11017017; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: P60229; IntAct: EBI-11148789; Score: 0.35
DE  Interaction: Q9QZD9; IntAct: EBI-11149349; Score: 0.35
DE  Interaction: Q96AP0; IntAct: EBI-11307293; Score: 0.51
DE  Interaction: Q9NUX5; IntAct: EBI-11307303; Score: 0.37
DE  Interaction: P40217; IntAct: EBI-11530486; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24331428; Score: 0.56
DE  Interaction: A9UHW6; IntAct: EBI-25261639; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q9Y262; IntAct: EBI-21660564; Score: 0.35
DE  Interaction: Q7L2H7; IntAct: EBI-21660564; Score: 0.35
DE  Interaction: P60228; IntAct: EBI-21660564; Score: 0.35
DE  Interaction: O15371; IntAct: EBI-21660564; Score: 0.35
DE  Interaction: O00303; IntAct: EBI-21660564; Score: 0.35
DE  Interaction: Q49MI3; IntAct: EBI-21731388; Score: 0.35
DE  Interaction: O95714; IntAct: EBI-16811721; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: Q9BRX2; IntAct: EBI-20567709; Score: 0.65
DE  Interaction: P10636; IntAct: EBI-20799058; Score: 0.35
DE  Interaction: Q9UMQ6; IntAct: EBI-20900672; Score: 0.40
DE  Interaction: P13693; IntAct: EBI-20992046; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-21132926; Score: 0.67
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P20339; IntAct: EBI-25391898; Score: 0.35
DE  Interaction: Q8K337; IntAct: EBI-25409748; Score: 0.35
DE  Interaction: Q6ZR37; IntAct: EBI-25411486; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P06730; IntAct: EBI-25478272; Score: 0.35
DE  Interaction: P0C6X7; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-27102375; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-27128043; Score: 0.27
DE  Interaction: P46108; IntAct: EBI-30819739; Score: 0.44
DE  Interaction: Q9UIH9; IntAct: EBI-29019642; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016282;
GO  GO:0033290;
GO  GO:0005852;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0003743;
GO  GO:0001732;
GO  GO:0006413;
GO  GO:0075525;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSPEPELLPGAPLPPPKEVINGNIKTVTEYKIDEDGKKFK
SQ  IVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRIC
SQ  KGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNAT
SQ  IRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN
//
ID  Q9Z1D1;
PN  Eukaryotic translation initiation factor 3 subunit G;
GN  Eif3g;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03006}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006}. Note=Colocalizes with AIFM1 in the nucleus and perinuclear region. {ECO:0000255|HAMAP- Rule:MF_03006}.
DR  UNIPROT: Q9Z1D1;
DR  UNIPROT: Q9R079;
DR  Pfam: PF12353;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre- initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. This subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17581632}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3TBT3; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9QWV4; IntAct: EBI-767142; Score: 0.37
DE  Interaction: Q9JL25; IntAct: EBI-649611; Score: 0.37
DE  Interaction: P23116; IntAct: EBI-7466744; Score: 0.46
DE  Interaction: Q9H074; IntAct: EBI-10766353; Score: 0.35
DE  Interaction: Q9EPK7; IntAct: EBI-17171503; Score: 0.35
DE  Interaction: P97414; IntAct: EBI-20564572; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016282;
GO  GO:0033290;
GO  GO:0005852;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0003743;
GO  GO:0001732;
GO  GO:0006413;
GO  GO:0075525;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLPTGDTSPEPELLPGDPLPPPKEVINGNIKTVTEYKIEEDGKKFK
SQ  IVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRIC
SQ  KGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQAAQSKTGKYVPPSLRDGASRRGESMQPNRRADDNAT
SQ  IRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN
//
ID  Q5RK09;
PN  Eukaryotic translation initiation factor 3 subunit G;
GN  Eif3g;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03006}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006}. Note=Colocalizes with AIFM1 in the nucleus and perinuclear region. {ECO:0000255|HAMAP- Rule:MF_03006}.
DR  UNIPROT: Q5RK09;
DR  Pfam: PF12353;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre- initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. This subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006}.
DE  Reference Proteome: Yes;
DE  Interaction: P09619; IntAct: EBI-22247316; Score: 0.35
DE  Interaction: Q9H5Y7; IntAct: EBI-22259307; Score: 0.35
GO  GO:0005737;
GO  GO:0016282;
GO  GO:0033290;
GO  GO:0005852;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0003743;
GO  GO:0001732;
GO  GO:0006413;
GO  GO:0075525;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLPTGDTSPEPELLPGDPLPPPKEVINGNIKTVTEYKVEEDGKKFK
SQ  IVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRIC
SQ  KGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQAAQNKTGKYVPPSLRDGASRRGESMQPNRRADDNAT
SQ  IRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN
//
ID  G0S2G1;
PN  Protein ELYS;
GN  ELYS;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8WYP5}.
DR  UNIPROT: G0S2G1;
DR  UNIPROT: G0ZGV2;
DR  Pfam: PF13934;
DE  Function: Required for the assembly of a functional nuclear pore complex (NPC). {ECO:0000250|UniProtKB:Q8WYP5}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S0E7; IntAct: EBI-16069427; Score: 0.62
DE  Interaction: G0S2X1; IntAct: EBI-16069404; Score: 0.56
DE  Interaction: G0SDQ4; IntAct: EBI-16069488; Score: 0.62
DE  Interaction: G0S9A7; IntAct: EBI-16069540; Score: 0.49
DE  Interaction: G0SAK3; IntAct: EBI-16069540; Score: 0.58
DE  Interaction: G0SER9; IntAct: EBI-16069540; Score: 0.49
DE  Interaction: G0SA60; IntAct: EBI-16069540; Score: 0.49
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLDFTHFPEVFPTDGPRPYDQHFVRQTETFRKSLDGVLFIDRVLGALGLPDAAKAYPPRGDAGLRALHQQVCSAKVSAHA
SQ  KLSVLYYLLLDHDEHRGSRSQLADALAEEVGLPANYQILMRGLWHMDRKEFKFALEHLAHPSLPAEFADEIITVLVRDGH
SQ  TTGDYSLPLAYYHAVRPVLQTSSALENLFAALARTSVTDALAFSRTYPDHGARQLLFERLVASVLEEHGSGQVAGRSASR
SQ  AKELVSLPLTGVEEKWLNDYLSTGEGRKSRSAKAVVQMRQVVTGRQKELGAVVGVRAGR
//
ID  Q9VWE6;
PN  Protein ELYS homolog;
GN  Elys;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:28472469}. Chromosome {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:31784359}. Note=Interacts with chromatin. {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:31784359}.
DR  UNIPROT: Q9VWE6;
DR  UNIPROT: Q95TR2;
DR  Pfam: PF13934;
DE  Function: Component of the nuclear pore complex (PubMed:28366641, PubMed:29773558). Binds to transcriptionally active chromatin including regulatory regions (PubMed:28366641, PubMed:31784359). {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:29773558, ECO:0000269|PubMed:31784359}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VHC7; IntAct: EBI-235409; Score: 0.00
DE  Interaction: Q24276; IntAct: EBI-469514; Score: 0.00
DE  Interaction: Q961V9; IntAct: EBI-469517; Score: 0.00
DE  Interaction: Q9V470; IntAct: EBI-471896; Score: 0.00
DE  Interaction: P49657; IntAct: EBI-471899; Score: 0.00
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: Q9VUH7; IntAct: EBI-9961648; Score: 0.35
DE  Interaction: P31007; IntAct: EBI-9965763; Score: 0.35
DE  Interaction: Q9VF82; IntAct: EBI-26819136; Score: 0.49
GO  GO:0005694;
GO  GO:0005643;
GO  GO:0003682;
GO  GO:0031490;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEWHEVELDGSRTIAFPERIVPGFGREPSAHLDAAEYLGGIIRDGQWGWVTWRYGSDATLLVCSMSTGDYLSWHCFWSES
SQ  DDLGPRKSIRCVEELFPGEHERPAMLAICLESWNSGDQRPIDCPLSTQVLIYAIRNSQVLRRFDLHGITCSALTFLDKRI
SQ  YGLTRLRRFKGCLAVATEEGTVLLVDLNSDSLQASTQRRSLCSPSSKDEPSDGNLYFVSSEESKRQLSSKLTHCRSKGAH
SQ  LAVRMDVASIGISCLMGISMAPGYAAGLEDGRILIYDLINFDVTTDLNSPVKRKGVNRAVKRMCLIMPPDDPKPCFYICA
SQ  LYQNIDVLQMMLHSVCYRGSYRDRETHTIRFKDYRSRTVRNRQILDGGICSVIGCATASTFSFAGDNGTLLIVISWHSSA
SQ  DKKNKLVLFDINQWYKDEMPTSVHKNEVPNYMSGYILSGLQTGLALDLRSTTILHFVSLQRYDEHFYPNSLTFDCSLLTP
SQ  TGKRYYAQDGVQHRFLNALRCDRATLFLRPQIYHEDIVRLRLLPQFCELNPNATFSKIAMYELILSVALEHNCGALLNDC
SQ  ARSWMDGSFLCNMIDNTQLSLSTLTNWILKRAGQIKTRCSELCHGIFDYGGYPLDQRERREFQVLSGQLRELVRLQSYIV
SQ  EQGRRRLTSSILDDCRANERALKTVLEYQRVLLWFIDHGLLPEGQHMDNLVPGEQAFVRLQHEYSEKRAQGKILYIDSLG
SQ  KRASFPEPYPPDSLHAYIHLMLSPDIELCHKHALILYLLMDLNQQLVGRFQIAFQLDKDLATSLRCFWYLDHGDYERGVE
SQ  ELYKEPAPAKNLKSWQMRLLIDKLLAEGAVKAAKKVVSRPPGPLSSALHMKVLLANENITEAFQIARLDDDEDGQPLLER
SQ  FFRHCIEIRRFKVLAELYLREPEERLLYSLLRQCRSRQTDCVQLIMLLQKSKFIEAVSFMDEVAAERERDESSNTILPAY
SQ  SATMGPVTQNIAGTYLRIRDTLEPYQKTGPLEPFSCQLVKQNASGQLGGIFQSSAVSAHWATQCESPPKMTPVSIQSKIG
SQ  YTNVPFLRHAQYGHSELPLPRRIVKPVPHQVVEKRQRELEDQRTNLQDQRQLGTERPNKRPCLMVERMVEDVKDYVRSIR
SQ  EKSSNQMEQEEVKQNEATNLLQPPNFLQARQSTTIRQSSSSPQPIPPILKGSGAVDAVKRAPPVATFTALAGPKRFRFVP
SQ  PIPLRTDKSDKSTEMGSEGAAEGEEETDEIIVEIESRSEPRSACSYESDEEDEFLSPLVSANVSLVDPVPSRNSPHYFAP
SQ  PAGPQPRNSLLHGGNGSGSKIGTATGSESSSGFGSFSTVQPAQTSSHSQFVPTVCSSKMGETQSQVFSSGSCGIKISERT
SQ  TICGEMESTDLGAELTAAPSAQWSLPSARPAIQGHHQMMDTTLGMSTYDVASLEQQDTQDVENEEELKLGDTKSLEEQQN
SQ  PQDEQKPEQEQDQDEDQAQEPLATGGQLAFLSNSEGTAQEPLSSPIYSLSSEDSNVSSAGIRNPMLPTLHTDDPMYSIVV
SQ  ESPGSITTSRSVTHTPTSFLPSDTNVSQTSSPQAPHGEDGDGTPISLYRANSLETVDDLDTTKGSLEEEEEYDDDDCVIA
SQ  LDGTEVRGYVARPQQSAASSSAELFAFKDECQEEAAGVPSPFLSLGATVNSDSDVADTIVLDSDEETAKEKDTQPEQRKD
SQ  WPMEEETPSNESVATVEFSEQKQPRADMDIGMEVDAVPDVLEVLEVPEMEPLPVLSDVDIEMAVDEVPNVLEVLEVPELE
SQ  PLPAGQATQSSGLGEIPEEDVDAEAEEQVVVKVEHVADEQPKEGDKTESKEASEEETQHNPEPLLPEEEDSRHSLKLIFS
SQ  GDEDEEEQDVPTRAIHTLRPRRSFTEHQDSPRTLRPRRVSQEHRDSPTPVAGRTMSLRSTDAPTLSPASNPPVSTPKRRG
SQ  LQHKYLLEVIDEHSPSDLSLPRTRSRTRLSVDSEATSSRPGTPTMTKARGKRATSQAPPTASPSVRRSLRGHSEPPAALS
SQ  AQLVRKPKTARAGVRSRKTSSGVQSPVAVSPTPIDAPIDVPDSTAPEEEQPRLRRTARRRISELSDQSANGTGDLRSEAS
SQ  SSRTGSKSNSAASTQNRELRPRLRRTSKSEH
//
ID  Q8WYP5;
PN  Protein ELYS;
GN  AHCTF1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8CJF7}. Nucleus {ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:27341616}. Nucleus envelope {ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:27341616}. Nucleus matrix {ECO:0000269|PubMed:17098863}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:27341616}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17098863}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:17098863}. Note=Localizes to the nuclear pore complex (NPC) throughout interphase. Localizes to the kinetochore from prophase, and this appears to require the Nup107-160 subcomplex of the NPC. Localizes to the periphery of chromatin from late anaphase. {ECO:0000269|PubMed:17098863}.
DR  UNIPROT: Q8WYP5;
DR  UNIPROT: A6NGM0;
DR  UNIPROT: A8MSG9;
DR  UNIPROT: A8MZ86;
DR  UNIPROT: Q7Z4E3;
DR  UNIPROT: Q8IZA4;
DR  UNIPROT: Q96EH9;
DR  UNIPROT: Q9Y4Q6;
DR  Pfam: PF13934;
DR  Pfam: PF16687;
DR  OMIM: 610853;
DE  Function: Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis. {ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:17235358}.
DE  Reference Proteome: Yes;
DE  Interaction: O75694; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P05783; IntAct: EBI-20924394; Score: 0.40
DE  Interaction: P37198; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: P49792; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: P52948; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: P55735; IntAct: EBI-9050503; Score: 0.32
DE  Interaction: P57740; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: Q12769; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: Q5SRE5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: Q6PFD9; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: Q8NFH3; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: Q8NFH4; IntAct: EBI-9050503; Score: 0.62
DE  Interaction: Q8NFH5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: Q8WUM0; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: A0JLT2; IntAct: EBI-394580; Score: 0.35
DE  Interaction: Q80Z64; IntAct: EBI-2312516; Score: 0.35
DE  Interaction: P35222; IntAct: EBI-2686783; Score: 0.00
DE  Interaction: Q8D0N9; IntAct: EBI-2876232; Score: 0.00
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: Q9BW27; IntAct: EBI-9050503; Score: 0.57
DE  Interaction: Q96EE3; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: Q92621; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: Q99567; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: Q96HA1; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: P06748; IntAct: EBI-11145880; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q14627; IntAct: EBI-21561326; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: P08670; IntAct: EBI-20924386; Score: 0.40
DE  Interaction: P05787; IntAct: EBI-20924378; Score: 0.40
DE  Interaction: Q15149; IntAct: EBI-20924370; Score: 0.40
DE  Interaction: Q15651; IntAct: EBI-20928904; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
DE  Interaction: Q02763; IntAct: EBI-32732012; Score: 0.35
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0032465;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRDLRAQVTSGLLPFPEVTLQALGEDEITLESVLRGKFAAGKNGLACLACGPQLEVVNSITGERLSAYRFSGVNEQPPVV
SQ  LAVKEFSWQKRTGLLIGLEETEGSVLCLYDLGISKVVKAVVLPGRVTAIEPIINHGGASASTQHLHPSLRWLFGVAAVVT
SQ  DVGQILLVDLCLDDLSCNQNEVEASDLEVLTGIPAEVPHIRESVMRQGRHLCFQLVSPTGTAVSTLSYISRTNQLAVGFS
SQ  DGYLALWNMKSMKREYYIQLESGQVPVYAVTFQEPENDPRNCCYLWAVQSTQDSEGDVLSLHLLQLAFGNRKCLASGQIL
SQ  YEGLEYCEERYTLDLTGGMFPLRGQTSNTKLLGCQSIEKFRSHGDREEGVNEALSPDTSVSVFTWQVNIYGQGKPSVYLG
SQ  LFDINRWYHAQMPDSLRSGEYLHNCSYFALWSLESVVSRTSPHGILDILVHERSLNRGVPPSYPPPEQFFNPSTYNFDAT
SQ  CLLNSGVVHLTCTGFQKETLTFLKKSGPSLNELIPDGYNRCLVAGLLSPRFVDVQPSSLSQEEQLEAILSAAIQTSSLGL
SQ  LTGYIRRWITEEQPNSATNLRFVLEWTWNKVVLTKEEFDRLCVPLFDGSCHFMDPQTIQSIQQCYLLLSNLNIVLSCFAS
SQ  EAREITERGLIDLSNKFVVSHLICQYAQVVLWFSHSGLLPEGIDDSVQLSRLCYNYPVIQNYYTSRRQKFERLSRGKWNP
SQ  DCLMIDGLVSQLGERIEKLWKRDEGGTGKYPPASLHAVLDMYLLDGVTEAAKHSITIYLLLDIMYSFPNKTDTPIESFPT
SQ  VFAISWGQVKLIQGFWLIDHNDYESGLDLLFHPATAKPLSWQHSKIIQAFMSQGEHRQALRYIQTMKPTVSSGNDVILHL
SQ  TVLLFNRCMVEAWNFLRQHCNRLNIEELLKHMYEVCQEMGLMEDLLKLPFTDTEQECLVKFLQSSASVQNHEFLLVHHLQ
SQ  RANYVPALKLNQTLKINVMNDRDPRLRERSLARNSILDQYGKILPRVHRKLAIERAKPYHLSTSSVFRLVSRPKPLSAVP
SQ  KQVVTGTVLTRSVFINNVLSKIGEVWASKEPINSTTPFNSSKIEEPSPIVYSLPAPELPEAFFGTPISKASQKISRLLDL
SQ  VVQPVPRPSQCSEFIQQSSMKSPLYLVSRSLPSSSQLKGSPQAISRASELHLLETPLVVKKAKSLAMSVTTSGFSEFTPQ
SQ  SILRSTLRSTPLASPSPSPGRSPQRLKETRISFVEEDVHPKWIPGAADDSKLEVFTTPKKCAVPVETEWLKSKDRTTSFF
SQ  LNSPEKEHQEMDEGSQSLEKLDVSKGNSSVSITSDETTLEYQDAPSPEDLEETVFTASKPKSSSTALTTNVTEQTEKDGD
SQ  KDVFASEVTPSDLQKQMGNLEDAETKDLLVAAEAFSELNHLSPVQGTEASLCAPSVYEGKIFTQKSKVPVLDEGLTSVET
SQ  YTPAIRANDNKSMADVLGDGGNSSLTISEGPIVSERRLNQEVALNLKEDHEVEVGVLKESVDLPEEKLPISDSPPDTQEI
SQ  HVIEQEKLEAQDSGEEARNLSFNELYPSGTLKLQYNFDTIDQQFCDLADNKDTAECDIAEVDGELFVAQSNFTLILEGEE
SQ  GEVEPGDFASSDVLPKAANTATEEKLVCSGENDNHGQIANLPSAVTSDQKSQKVDTLPYVPEPIKVAIAENLLDVIKDTR
SQ  SKEITSDTMEQSIHETIPLVSQNIMCPTKLVKSAFKTAQETSTMTMNVSQVDDVVSSKTRTRGQRIQNVNVKSAQQEASA
SQ  DVATPKMPGQSVRKKTRKAKEISEASENIYSDVRGLSQNQQIPQNSVTPRRGRRKKEVNQDILENTSSVEQELQITTGRE
SQ  SKRLKSSQLLEPAVEETTKKEVKVSSVTKRTPRRIKRSVENQESVEIINDLKVSTVTSPSRMIRKLRSTNLDASENTGNK
SQ  QDDKSSDKQLRIKHVRRVRGREVSPSDVREDSNLESSQLTVQAEFDMSAIPRKRGRPRKINPSEDVGSKAVKEERSPKKK
SQ  EAPSIRRRSTRNTPAKSENVDVGKPALGKSILVPNEELSMVMSSKKKLTKKTESQSQKRSLHSVSEERTDEMTHKETNEQ
SQ  EERLLATASFTKSSRSSRTRSSKAILLPDLSEPNNEPLFSPASEVPRKAKAKKIEVPAQLKELVSDLSSQFVISPPALRS
SQ  RQKNTSNKNKLEDELKDDAQSVETLGKPKAKRIRTSKTKQASKNTEKESAWSPPPIEIRLISPLASPADGVKSKPRKTTE
SQ  VTGTGLGRNRKKLSSYPKQILRRKML
//
ID  Q8CJF7;
PN  Protein ELYS;
GN  Ahctf1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11952839}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23499022}. Nucleus matrix {ECO:0000269|PubMed:23499022}. Cytoplasm {ECO:0000269|PubMed:11952839}. Note=Localizes to the nuclear pore complex (NPC) throughout interphase. Localizes to the kinetochore from prophase, and this appears to require the Nup107-160 subcomplex of the NPC. Localizes to the periphery of chromatin from late anaphase (By similarity). {ECO:0000250|UniProtKB:Q8WYP5}.
DR  UNIPROT: Q8CJF7;
DR  UNIPROT: B2RRC8;
DR  UNIPROT: Q8BVJ5;
DR  UNIPROT: Q8VD55;
DR  PDB: 4I0O;
DR  Pfam: PF13934;
DR  Pfam: PF16687;
DE  Function: Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis (By similarity). Has also been proposed to function as a transcription factor which may play a specific role in hematopoietic tissues (PubMed:11952839). {ECO:0000250, ECO:0000269|PubMed:11952839}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0030097;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0032465;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQDLTAQVTSDLLHFPEVTIEALGEDEITLESVLRGKFAAGKNGLACLACGPQLEVVNSLTGERLSAYRFSGVNEQPPVV
SQ  LAVKEFSWHKRTGLLIGLEEADGSVLCLYDLGISRVVKAVVLPGRVTAIEPIINHGGASASTQHLHPSLRWLFGVAAVVT
SQ  DVGQILLIDLCLDDLSCSQNEVEASDLEVITGIPAEVPHIRERVMREGRHLCFQLVSPLGVAISTLSYINRTNQLAVGFS
SQ  DGYLALWNMKSMKREYYTQLEGGRVPVHAVAFQEPENDPRNCCYLWAVQSTQDSEGDVLSLHLLQLAFGDRKCLASGQIL
SQ  YEGLEYCEERYTLDLAGGTFPLRGQTSNTKLLGCQSIERFPSHGDREESMREALSPDTSVSVFTWQVNIYGQGKPSVYLG
SQ  LFDINRWYHAQMPDSLRSGESLHNCSYFALWSLDSVVSRTSPHHILDILVHERSLNRGVPPSYPPPEQFFNPSTFNFDAT
SQ  CLLDSGVIHVTCAGFQKETLTFLKKSGPTLNEVIPDSYNRCLVAGLLSPRLIDIQPSSLSQEEQLEAILSAAIQTSSLGL
SQ  LTGYIRTWIIEEQPNSAANLRFVLEWTWNKVVLTKEEFDRLCVPLFDGSCRFIDPQTIQSIQQCHLLLSNLSTVLSCFAM
SQ  EAQGITERGLVDLSNKHMVTQLLCQYAHMVLWFCHSGLLPEGLDDALQLSRLRYNYPVIQNYYTSRRQKSERSPRGKWNH
SQ  DCLMIDGLVSQLGDEVEKLWKRDEGGTGRYPPASIHALLDIYLLDNITEASKHAITIYLLLDIMYSFPNKTDTPIESFPT
SQ  AFAISWGQVKLVQGFWLLDHNDYENGLDLLFHPVTAKPASWQHSKIIEAFMSQGEHKQALRYLQTMKPTVSSSNEVILHL
SQ  TVLLFNRCMVEAWNLLRQNSNRVNIEELLKHAYEVCQEMGLMEDLLKLPFTNTEQECLVKFLQSSTSVENHEFLLVHHLQ
SQ  RANYISALKLNQILKNNLMSDRDPRLRERSVTRNSILDQYGKILPRVQRKLAVERAKPYHLSTSSVFHEVSRPKPLSAFP
SQ  KKAITGTVLTRSTFISNVLSKIGEVWASHEPRNGVSLFNSPKTEQPSPVVHSFPHPELPEAFVGTPISNTSQRISRLLDL
SQ  VVHPVPQPSQCLEFIQQSPTRSPLCLLSSSLPLSSQFKRPHQNTSRPSELLLLETPLIVKKAKSLALSATSSGFAEFTPP
SQ  SILRSGFRTTPLASPSLSPGRSLTPPFRVKETRISFMEEGMNTHWTDRATDDRNTKAFVSTSFHKCGLPAETEWMKTSDK
SQ  NTYFPLDVPAKGPQKVVAESLATHSGRLEKLDVSKEDSTASTRSDQTSLEYHDAPSPEDLEGAVFVSPKPASSSTELTTN
SQ  STLQTERDNDKDAFKSEGAPSPVKKQIGTGDAAVEAFSELSRLDPVERAEASFAVSSVCEGETSTSNSKTSVLDGIVPIE
SQ  SRTSILTADHKESVANTVADVESSGSTSSKCPVTSERSLGQKLTLNLKEDEIEAHVPKENVGLPEESPRISAAPSDTHEI
SQ  HLIGCENLEVQNSEEEAKNLSFDELYPLGAEKLEYNLSTIEQQFCDLPDDKDSAECDAAEVDGELFVAQSNFTLILEGEE
SQ  GEAEASDSAAPNMLPKATKEKPVCHREPHNQERVTDLPSAVTADQESHKVETLPYVPEPVKVAIAENLLDVIKDTRSKEA
SQ  TPVAAGEAGDEDGAVIVSKAAHSSRLTNSTPKTVKEPHAETVNTSQNDDMVSSRTLTRRQHALSLNVTSEQEPSAVATPK
SQ  KRTRKIKETPESSERTCSDLKVAPENQLTAQSPPAPRRGKKKDVSQGTLPSSGAVEPEPEPQGTPGRLRLRTQPPEPAAE
SQ  ETPSRTKVRLSSVRKGTPRRLKKSVENGQSTEILDDLKGSEAASHDGTVTELRNANLEDTQNMEYKQDEHSDQQLPLKRK
SQ  RVREREVSVSSVTEEPKLDSSQLPLQTGLDVPATPRKRGRPRKVVPLEADGGTTGKEQTSPQKKDVPVVRRSTRNTPARN
SQ  VSTLEKSVLVPNKEAALVVTSKRRPTKKSAEESSKDPSAAVSDLAGGAAHTESADRRDGLLAAAALTPSAQGTRTRSRRT
SQ  MLLTDISEPKTEPLFPPPSVKVPKKKSKAENMEAAAQLKELVSDLSSQFVVSPPALRTRQKSISNTSKLLGELESDPKPL
SQ  EIIEQKPKRSRTVKTRASRNTGKGSSWSPPPVEIKLVSPLASPVDEIKTGKPRKTAEIAGKTLGRGRKKPSSFPKQILRR
SQ  KML
//
ID  Q5U249;
PN  Protein ELYS;
GN  ahctf1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17235358, ECO:0000269|PubMed:18596237}. Cytoplasm {ECO:0000250|UniProtKB:Q8CJF7}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17235358}. Note=Binds to chromatin during mitosis, and chromatin binding increases as nuclei assemble and grows through interphase (PubMed:17235358). Does not localize to the pores of annulate lamellae, which are cytoplasmic stacks of membrane that form in rapidly dividing cells (PubMed:18596237). {ECO:0000269|PubMed:17235358, ECO:0000269|PubMed:18596237}.
DR  UNIPROT: Q5U249;
DR  PDB: 7VCI;
DR  PDB: 7WB4;
DR  Pfam: PF13934;
DR  Pfam: PF16687;
DE  Function: Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex, which may in turn recruit membrane vesicles containing pom121 and tmem48/ndc1. Association with chromatin may require the presence of the mcm2-mcm7 complex, suggesting a mechanism for coordination of nuclear assembly and the inactivation of replication licensing. {ECO:0000269|PubMed:17235358, ECO:0000269|PubMed:17825564, ECO:0000269|PubMed:18596237}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6P5F9; IntAct: EBI-11606853; Score: 0.35
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0003677;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQNLEAQVTGSLVAFPDVTQKALKEDEINLDSVLRGKFSTGRTSLAWLACGPQLEITNSVTGERISAYHFSGLTERPPVV
SQ  VAVKEFTWQKKTGLLVGLVEAEGSVLCLYDIGISKVVKAVVLPGSVTAVEPIINHGGASASTQHLHQSLRWFFGVTAVVT
SQ  DVGHVLLIDLCLDEVSSNQDELDASDLEVMSVIPTKIPKLREAATRERRHLCLQLAAPTGTTVSCLSYISRTNQLAVGYS
SQ  DGYFSLWNMKTLRRDYHVQIEGGRVPVCAVAFQEPENDPRNCCYLWAVQSSESGGDVSLHLLQLAFSDRKCLASGQIMYE
SQ  LLEYCEERYSLDLSGSTLSLRGQSNNTKLLGCQTIEKFRVHGEREDGVHEVTSPDTSVSVFSWQVNTYGQGKPSVYLGVF
SQ  DINRWYQAQMPDSLRSGQFLRNCSYFAFWSLEAVVNITTQDIIFDILVHERSLSRGIPPSYPPPEQFYYPSTYNFDATCL
SQ  LNSGLIHFACTGFQKETLHFLKKSGSSLNEAIPDGYNRCLAAGLLAPKFTDVQASSLSQEEQLQAILAAAVETSSLGLLT
SQ  SCIKRWTAEEQPRSAANLRFVLEWTWKKVTLTKQEFDRLCFRLFDGSCNFIDPHTLQSLQQCHLYFSNLTAVLNCFIAQA
SQ  KEVTQQGAVDLTNKQSVTRLLTLYASVVLWFCRSGMLPDSSDETVQLTRPFYNYQVIQQYYSDQRKKLERLARGKWDTSS
SQ  LMIDGLINQFGDRIQQLWSRDDNGTGKYPPANLHALLDVYLLENADEMSKHAITIYFLLDIMYSFPDKPDSSIESFPTAF
SQ  FVPGSLIKLIQGFWLLDHNDYQNSVDCILNPASSRVMSWQHSQIIENLLCHGDSRQALRYLQVMKPVATTSKEVKLHMTV
SQ  LLANRSILEAWNLQRLHSSRLNVEELLKHMYEMCQEMGLIEELLKLTFTDFEQGYLHKFLQTTGVQNQELLLVHHLQRAN
SQ  YISALQLNQSLKTNHLNDCDRRLRERSGARNAILDQYGKILPRVQRTLASERAKPYSLPSLVWREVARPKPLSTTAKQAA
SQ  PGSIITKANFICNVLSKIKEVSTANEKREEYSPYQSMVSEEPTAPPLQDIDVPDAFFGTPINKSRRVSRLLDSVVHPVLM
SQ  EPTPLTSSDTDNNQTPHKSPLLKTSSPLHSSLRRIAHMRSFAKASEFSLLETPLVVRKAKALAANTASSGYTSITPQSIL
SQ  RSSVRTTPLVSPSVSPGRSLTPPLRPKETKISFMELSFTRHAKAAHSSEGNLLAISPVLRSSPDAVWSVKGKVASFTQNT
SQ  PVKKLDEIDASSSGIQEESQDEMEVSKEISNISVRSEQASLEYHDAPTPEDLENDEISGTTNSQPQVNEVHHQMEDGQLT
SQ  EKPAELALTEMQEEFIDSEEREIEYISAPLNGPNALECMTAVPDIYLEDASQCILETPEGSSVSVTGEQECVSSAKDSES
SQ  VISIHDSDDAHSNLSENDQDSEEIEENNLRVPTTVTRCEEFDLIETKDLEVELEEADSEKTNYKDIYPDATVQLGFTVES
SQ  IEQRYTCELADRRETPSETDEIEGEHFETENNFSLVLEGDVTEEEILEPSSSKTDLELTRPPIAHQKLISENRENIENCE
SQ  TTEKIPANMSPLVDSDHESKTLETLPSEADLSVAEKVLKGTEEKDVPPEVHSEVVLESKLVGNAMMSLDSSESQEVIISQ
SQ  YDNVISIEKLEMTQEKMYGEKTEQINEGQVSPNRDQSTLVKPLTPRRSIRKSSKPADSSTDIIGNITLPTTPKRGLKKAK
SQ  ENVDTLKNSISVVPEEELTLGTRRITRKATLTALDNPEPLQIKEPPSGEDLQVQPSTPTRGRRGKVITSDDLKEPPSGED
SQ  LQVQPSTPTRGRRGRVITSDDLREPPPGEDLQVQPSTPTRGRRGRVITSDDIKESPSVEDLQVQPSTPTRGRRGKVITSD
SQ  DIKEPPSVEDLQVQPSTPTRGRKGKVITSDDIKEPLSGEDLQVQPSTPTRGRKGKVITSDDIKEPLSEEVLQEQPSTPTR
SQ  GRRGRVITSDGKGYECVEEKNALPLTPTRITRSKNILEPEKGISQIEPEKGISQIEPDKGLSQIEDTGETEHEVVTPRRG
SQ  RRGKRVVNELVKHFERNSSQPNIKADTSPPVSPKKVSLRWTRTRSENQRINATEEQASKIQEDLSDTPRKRYKKSSNKMG
SQ  FEETTDTVTEGAIVEDVQESLIISHLGKNPNTSIVRSARKTALPPVTEDHSEQPLLPPESHSKVHSSLAIADEENKTNTR
SQ  TRSGNKSSVDVSAITFEFSTPKARTKKTAKGSAVPTELIPSTQYVFSPPSTRTRRATRANVSEAVIEPQLQFQESCEIAE
SQ  TEVPEVPASKPRGRPPKHKAKAVTRVLKKPSWSTPPVEIKLISPPESPAVSETNTKTDSTEAKGAEKISVRRTRRRIIAK
SQ  PVTRRKMR
//
ID  O00423;
PN  Echinoderm microtubule-associated protein-like 1;
GN  EML1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:25740311}. Note=Detected in cytoplasmic punctae. Co- localizes with microtubules (PubMed:24859200, PubMed:25740311). Enriched in perinuclear regions during interphase and in the region of spindle microtubules during metaphase. Enriched at the midzone during telophase and cytokinesis. Detected at growth cones in neurons (By similarity). {ECO:0000250|UniProtKB:Q05BC3, ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:25740311}.
DR  UNIPROT: O00423;
DR  UNIPROT: Q86U15;
DR  UNIPROT: Q8N536;
DR  UNIPROT: Q8N5C4;
DR  UNIPROT: Q8WWL6;
DR  PDB: 4CI8;
DR  Pfam: PF03451;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 600348;
DR  OMIM: 602033;
DR  DisGeNET: 2009;
DE  Function: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se. {ECO:0000250|UniProtKB:Q05BC3}.
DE  Disease: Band heterotopia (BH) [MIM:600348]: A brain malformation of the lissencephaly spectrum, resulting from disordered neuronal migration and characterized by bands of gray matter interposed in the central white matter. Disease features include severe developmental delay with intellectual disability, enlarged head circumference, periventricular and ribbon-like subcortical heterotopia, polymicrogyria and agenesis of the corpus callosum. {ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:28556411}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9H9L3; IntAct: EBI-759235; Score: 0.62
DE  Interaction: Q96GG9; IntAct: EBI-21325177; Score: 0.35
DE  Interaction: Q9Y266; IntAct: EBI-9482705; Score: 0.40
DE  Interaction: Q14203; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q13509; IntAct: EBI-21665394; Score: 0.35
DE  Interaction: Q9NVF7; IntAct: EBI-21835198; Score: 0.35
DE  Interaction: Q9HC35; IntAct: EBI-21835198; Score: 0.35
DE  Interaction: Q9BVA1; IntAct: EBI-21835198; Score: 0.35
DE  Interaction: Q13885; IntAct: EBI-21835198; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-21835198; Score: 0.35
DE  Interaction: P55212; IntAct: EBI-25834583; Score: 0.56
DE  Interaction: P13473; IntAct: EBI-25872768; Score: 0.56
DE  Interaction: P31948; IntAct: EBI-25913540; Score: 0.56
DE  Interaction: P51114; IntAct: EBI-26508437; Score: 0.51
DE  Interaction: P60484; IntAct: EBI-26513677; Score: 0.37
DE  Interaction: Q05086; IntAct: EBI-26516191; Score: 0.37
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:1990023;
GO  GO:0097431;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0008017;
GO  GO:0015631;
GO  GO:0007420;
GO  GO:0002244;
GO  GO:0000226;
GO  GO:0007052;
GO  GO:0007405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKG
SQ  PTKARPLMQTLPLRTTVNNGTVLPKKPTGSLPSPSGVRKETAVPATKSNIKRTSSSERVSPGGRRESNGDSRGNRNRTGS
SQ  TSSSSSGKKNSESKPKEPVFSAEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYL
SQ  LPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIG
SQ  IGFFDRAVTCIAFSKSNGGTNLCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTL
SQ  EGSSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGK
SQ  DRKLISWSGNYQKLRKTEIPEQFGPIRTVAEGKGDVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKSQFLT
SQ  CGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNF
SQ  LAIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWAT
SQ  YTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYGGHSSHVTNVDFLCEDSHLI
SQ  STGGKDTSIMQWRVI
//
ID  Q05BC3;
PN  Echinoderm microtubule-associated protein-like 1;
GN  Eml1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:24859200}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24859200}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24859200}. Note=Detected in cytoplasmic punctae. Co-localizes with microtubules. Enriched in perinuclear regions during interphase and in the region of spindle microtubules during metaphase. Enriched at the midzone during telophase and cytokinesis. Detected at growth cones in neurons. {ECO:0000269|PubMed:24859200}.
DR  UNIPROT: Q05BC3;
DR  UNIPROT: Q05AF8;
DR  UNIPROT: Q0P5V3;
DR  Pfam: PF03451;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se. {ECO:0000269|PubMed:24859200}.
DE  Disease: Note=Defects in Eml1 are the cause of the neuronal heterotopia observed in HeCo mice. These mice display heterotopic neurons in the rostro-medial part of the neocortex, together with epilepsy and subtle learning deficits in adults. At 17 dpc both Tbr1(+) and Cux1(+) neurons contribute to the heterotopia. Three days after birth, most Tbr1(+) have reached their final destination, but many Cux1(+) neurons remain in the heterotopia and fail to reach cortical layers II to IV, contrary to the situation in wild-type. Besides, progenitor cells continue to proliferate, resulting in large numbers of abnormally positioned actively proliferating cells during both early and late stages of corticogenesis. In HeCo mice, insertion of a retrotransposon into Eml1 leads to the absence of full-length Eml1 transcripts.
DE  Reference Proteome: Yes;
DE  Interaction: P35922; IntAct: EBI-16728828; Score: 0.35
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0048471;
GO  GO:0008017;
GO  GO:0015631;
GO  GO:0007420;
GO  GO:0002244;
GO  GO:0000226;
GO  GO:0007052;
GO  GO:0007405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKG
SQ  PTKARPLGQTLPLRTTVNNGTVLPKKPSASLPAPSGARKEVVVPVTKSINRTSSSERVSPGGRRESSGDSKGSRNRTGST
SQ  SSSSSGKKNSESKPKEPAFSPEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLL
SQ  PTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGI
SQ  GFFDRAVTCIAFSKSNGGGHLCAVDDSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLE
SQ  GNSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKD
SQ  RRLISWNGNYQKLHKAEIPEQFGPIRTVAEGKGNVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKPQFLTC
SQ  GHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFL
SQ  AIGSHDNCIYIYGVTDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATY
SQ  TCTLGFHVFGVWPEGSDGTDINAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRAPSHIYSGHSSHVTNVDFLCEDSHLIS
SQ  TGGKDTSIMQWRVI
//
ID  Q4V8C3;
PN  Echinoderm microtubule-associated protein-like 1;
GN  Eml1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q05BC3}. Note=Detected in cytoplasmic punctae. Co-localizes with microtubules. Enriched in perinuclear regions during interphase and in the region of spindle microtubules during metaphase. Enriched at the midzone during telophase and cytokinesis. Detected at growth cones in neurons. {ECO:0000250|UniProtKB:Q05BC3}.
DR  UNIPROT: Q4V8C3;
DR  Pfam: PF03451;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se. {ECO:0000250|UniProtKB:Q05BC3}.
DE  Reference Proteome: Yes;
DE  Interaction: P54645; IntAct: EBI-16399805; Score: 0.35
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0008017;
GO  GO:0015631;
GO  GO:0007420;
GO  GO:0002244;
GO  GO:0000226;
GO  GO:0007052;
GO  GO:0007405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEISDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKG
SQ  PTKARPLGQTLPLRTTVNNGTVLPKKPSASLPSPSGSRKEMVVPVTKSINRTSSSERVSPGGRRESSGDSKGSRNRTGST
SQ  SSSSSGKKNSESKPKEPTFSPEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLL
SQ  PTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGI
SQ  GFFDRAVTCIAFSKSNGGSHLCAVDDSNDHVLSVWDWQREERLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLE
SQ  GNSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKD
SQ  RRLISWNGNYQKLHKAEIPEQFGPIRTVAEGKGNVILIGTTRNFVLQGTLTGDFTPITQGHTDELWGLAIHASKPQFLTC
SQ  GHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFL
SQ  AIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATY
SQ  TCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYSGHSSHVTNVDFLCEDSHLIS
SQ  TGGKDTSIMQWRVI
//
ID  P50402;
PN  Emerin;
GN  EMD;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:19167377}; Single-pass membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus.
DR  UNIPROT: P50402;
DR  UNIPROT: Q6FI02;
DR  PDB: 1JEI;
DR  PDB: 2ODC;
DR  PDB: 2ODG;
DR  PDB: 6GHD;
DR  PDB: 6RPR;
DR  PDB: 7NDY;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DR  OMIM: 300384;
DR  OMIM: 310300;
DR  DisGeNET: 2010;
DE  Function: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta- catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1- dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non- farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. {ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:17785515, ECO:0000269|PubMed:19323649, ECO:0000269|PubMed:32923640}.
DE  Disease: Emery-Dreifuss muscular dystrophy 1, X-linked (EDMD1) [MIM:310300]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:10323252, ECO:0000269|PubMed:11587540, ECO:0000269|PubMed:15009215, ECO:0000269|PubMed:15328537}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A1L3G9; IntAct: EBI-12595918; Score: 0.40
DE  Interaction: O75531; IntAct: EBI-10759397; Score: 0.94
DE  Interaction: O94901; IntAct: EBI-22057164; Score: 0.46
DE  Interaction: P00533; IntAct: EBI-32717697; Score: 0.42
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.80
DE  Interaction: P03246; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P0DTC7; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P13285; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P35240; IntAct: EBI-23824818; Score: 0.56
DE  Interaction: Q9NYF8; IntAct: EBI-489904; Score: 0.59
DE  Interaction: Q7L5N1; IntAct: EBI-731797; Score: 0.00
DE  Interaction: Q7L190; IntAct: EBI-731800; Score: 0.00
DE  Interaction: Q99962; IntAct: EBI-710249; Score: 0.51
DE  Interaction: Q99963; IntAct: EBI-731806; Score: 0.00
DE  Interaction: Q969F0; IntAct: EBI-753397; Score: 0.85
DE  Interaction: O43889; IntAct: EBI-12701204; Score: 0.56
DE  Interaction: Q8N7W2; IntAct: EBI-10211848; Score: 0.81
DE  Interaction: P35222; IntAct: EBI-8577506; Score: 0.59
DE  Interaction: P13569; IntAct: EBI-1171716; Score: 0.53
DE  Interaction: Q9UKV8; IntAct: EBI-7642406; Score: 0.35
DE  Interaction: P04296; IntAct: EBI-9631489; Score: 0.35
DE  Interaction: Q9HCK5; IntAct: EBI-2269711; Score: 0.35
DE  Interaction: O70126; IntAct: EBI-2557780; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-2877710; Score: 0.35
DE  Interaction: Q9BQS8; IntAct: EBI-3242919; Score: 0.35
DE  Interaction: Q15051; IntAct: EBI-4286917; Score: 0.35
DE  Interaction: P51858; IntAct: EBI-4409719; Score: 0.35
DE  Interaction: Q16659; IntAct: EBI-7207761; Score: 0.37
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6191076; Score: 0.53
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P22893; IntAct: EBI-6506418; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6515609; Score: 0.53
DE  Interaction: Q9UH99; IntAct: EBI-6753091; Score: 0.64
DE  Interaction: Q9D666; IntAct: EBI-6752609; Score: 0.52
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: Q8IWZ5; IntAct: EBI-10211808; Score: 0.72
DE  Interaction: Q53Z40; IntAct: EBI-10211828; Score: 0.56
DE  Interaction: Q5JST6; IntAct: EBI-10211838; Score: 0.56
DE  Interaction: Q8NEC5; IntAct: EBI-10211860; Score: 0.81
DE  Interaction: Q9P286; IntAct: EBI-10211880; Score: 0.56
DE  Interaction: Q8NHQ1; IntAct: EBI-10211870; Score: 0.72
DE  Interaction: Q9P127; IntAct: EBI-10211900; Score: 0.81
DE  Interaction: Q9UNY5; IntAct: EBI-10211910; Score: 0.56
DE  Interaction: Q9Y228; IntAct: EBI-10211920; Score: 0.81
DE  Interaction: Q13895; IntAct: EBI-10230959; Score: 0.72
DE  Interaction: Q8N8X9; IntAct: EBI-10268015; Score: 0.56
DE  Interaction: Q8WTP8; IntAct: EBI-10275770; Score: 0.56
DE  Interaction: Q9ULW3; IntAct: EBI-10323933; Score: 0.72
DE  Interaction: P50402; IntAct: EBI-10484783; Score: 0.37
DE  Interaction: O14862; IntAct: EBI-9995694; Score: 0.35
DE  Interaction: P10398; IntAct: EBI-10101587; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-10103376; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-10103481; Score: 0.53
DE  Interaction: O60674; IntAct: EBI-10103554; Score: 0.35
DE  Interaction: P53671; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-10104226; Score: 0.53
DE  Interaction: Q9H0K1; IntAct: EBI-10104403; Score: 0.35
DE  Interaction: Q8NF91; IntAct: EBI-10759458; Score: 0.52
DE  Interaction: Q8WXH0; IntAct: EBI-10760372; Score: 0.58
DE  Interaction: P03177; IntAct: EBI-11721652; Score: 0.35
DE  Interaction: P03179; IntAct: EBI-11721697; Score: 0.35
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P03225; IntAct: EBI-11722220; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06461; IntAct: EBI-11723785; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P06927; IntAct: EBI-11724813; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: P0CK58; IntAct: EBI-11732874; Score: 0.35
DE  Interaction: P30119; IntAct: EBI-11733103; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: Q2MG95; IntAct: EBI-11733653; Score: 0.35
DE  Interaction: Q2MG96; IntAct: EBI-11733890; Score: 0.35
DE  Interaction: Q8AZK7; IntAct: EBI-11734159; Score: 0.35
DE  Interaction: Q8AZJ3; IntAct: EBI-11734105; Score: 0.35
DE  Interaction: E9QKK1; IntAct: EBI-10995761; Score: 0.35
DE  Interaction: Q9Z1B5; IntAct: EBI-10996176; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: P31150; IntAct: EBI-11035437; Score: 0.35
DE  Interaction: Q9Z2X1; IntAct: EBI-11066678; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104527; Score: 0.35
DE  Interaction: Q6ZNC8; IntAct: EBI-11121915; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-11155257; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11372136; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q96Q45; IntAct: EBI-11396533; Score: 0.27
DE  Interaction: P48039; IntAct: EBI-11575834; Score: 0.37
DE  Interaction: Q8N6L0; IntAct: EBI-11774371; Score: 0.79
DE  Interaction: Q71U36; IntAct: EBI-11897791; Score: 0.53
DE  Interaction: Q6FHY5; IntAct: EBI-24279203; Score: 0.56
DE  Interaction: Q9BYN7; IntAct: EBI-24339377; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-24344788; Score: 0.56
DE  Interaction: Q16623; IntAct: EBI-24487831; Score: 0.56
DE  Interaction: Q6P2D0; IntAct: EBI-24525478; Score: 0.56
DE  Interaction: P20138; IntAct: EBI-24662714; Score: 0.56
DE  Interaction: Q5JRM2; IntAct: EBI-23676624; Score: 0.56
DE  Interaction: Q8N5K1; IntAct: EBI-23679672; Score: 0.56
DE  Interaction: Q96HE8; IntAct: EBI-24667793; Score: 0.56
DE  Interaction: Q6NX45; IntAct: EBI-24670601; Score: 0.56
DE  Interaction: B7U540; IntAct: EBI-24672111; Score: 0.56
DE  Interaction: A6NEL2; IntAct: EBI-23696046; Score: 0.56
DE  Interaction: Q15842; IntAct: EBI-24689183; Score: 0.56
DE  Interaction: Q9NQX5; IntAct: EBI-24699630; Score: 0.56
DE  Interaction: Q8N4V1; IntAct: EBI-24709706; Score: 0.56
DE  Interaction: Q7RTU1; IntAct: EBI-23756438; Score: 0.56
DE  Interaction: O60930; IntAct: EBI-23758332; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-24717955; Score: 0.56
DE  Interaction: Q7Z6M4; IntAct: EBI-23772605; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-23795943; Score: 0.56
DE  Interaction: P16157; IntAct: EBI-24733419; Score: 0.56
DE  Interaction: Q9HA82; IntAct: EBI-23800001; Score: 0.56
DE  Interaction: P43628; IntAct: EBI-24742152; Score: 0.56
DE  Interaction: Q9BSJ6; IntAct: EBI-24763001; Score: 0.56
DE  Interaction: Q5JX71; IntAct: EBI-24763501; Score: 0.56
DE  Interaction: Q6IBW4; IntAct: EBI-23853144; Score: 0.56
DE  Interaction: Q86VY9; IntAct: EBI-24778276; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-25275476; Score: 0.56
DE  Interaction: Q5T7V8; IntAct: EBI-23923221; Score: 0.56
DE  Interaction: Q8IUY3; IntAct: EBI-24390287; Score: 0.56
DE  Interaction: P50221; IntAct: EBI-24397223; Score: 0.56
DE  Interaction: O75031; IntAct: EBI-24417083; Score: 0.56
DE  Interaction: Q9HAQ2; IntAct: EBI-24439983; Score: 0.56
DE  Interaction: Q8TD17; IntAct: EBI-24447341; Score: 0.56
DE  Interaction: Q5SNT2; IntAct: EBI-24476865; Score: 0.68
DE  Interaction: Q96S94; IntAct: EBI-24556880; Score: 0.56
DE  Interaction: Q6P9A3; IntAct: EBI-24557406; Score: 0.56
DE  Interaction: Q9NU63; IntAct: EBI-24580547; Score: 0.56
DE  Interaction: Q5T686; IntAct: EBI-24599743; Score: 0.56
DE  Interaction: P21964; IntAct: EBI-24641360; Score: 0.56
DE  Interaction: Q86UD4; IntAct: EBI-24646904; Score: 0.56
DE  Interaction: Q96PL5; IntAct: EBI-25169259; Score: 0.56
DE  Interaction: Q4KMG9; IntAct: EBI-24747207; Score: 0.56
DE  Interaction: Q68DC2; IntAct: EBI-25195191; Score: 0.56
DE  Interaction: Q9BRJ2; IntAct: EBI-24789200; Score: 0.56
DE  Interaction: Q14500; IntAct: EBI-24790299; Score: 0.56
DE  Interaction: Q7Z7G2; IntAct: EBI-25207978; Score: 0.56
DE  Interaction: Q9H400; IntAct: EBI-24799476; Score: 0.56
DE  Interaction: Q8WWF3; IntAct: EBI-24800633; Score: 0.56
DE  Interaction: Q9UGI6; IntAct: EBI-24807534; Score: 0.56
DE  Interaction: Q86T13; IntAct: EBI-25224374; Score: 0.56
DE  Interaction: Q8WUU8; IntAct: EBI-25273036; Score: 0.56
DE  Interaction: P49910; IntAct: EBI-12696914; Score: 0.56
DE  Interaction: O95292; IntAct: EBI-12698321; Score: 0.56
DE  Interaction: Q9NTW7; IntAct: EBI-12700590; Score: 0.56
DE  Interaction: Q12846; IntAct: EBI-12702158; Score: 0.56
DE  Interaction: P50222; IntAct: EBI-12702328; Score: 0.56
DE  Interaction: Q8N5R6; IntAct: EBI-12702476; Score: 0.56
DE  Interaction: O14829; IntAct: EBI-14024386; Score: 0.35
DE  Interaction: P56180; IntAct: EBI-14025693; Score: 0.57
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q05322; IntAct: EBI-15481401; Score: 0.35
DE  Interaction: P60709; IntAct: EBI-15531451; Score: 0.52
DE  Interaction: P68135; IntAct: EBI-15531470; Score: 0.60
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: P68431; IntAct: EBI-16793336; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: P62491; IntAct: EBI-16797971; Score: 0.27
DE  Interaction: P20339; IntAct: EBI-16798221; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: P62753; IntAct: EBI-16798663; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.42
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-20307233; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-20307902; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: P14316; IntAct: EBI-21260627; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: Q03518; IntAct: EBI-21265865; Score: 0.35
DE  Interaction: Q9NQB0; IntAct: EBI-21265942; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: Q9BTV4; IntAct: EBI-22085077; Score: 0.54
DE  Interaction: Q13163; IntAct: EBI-25374437; Score: 0.35
DE  Interaction: Q15311; IntAct: EBI-25375541; Score: 0.35
DE  Interaction: Q92934; IntAct: EBI-25378368; Score: 0.35
DE  Interaction: P19419; IntAct: EBI-25378580; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9H9V9; IntAct: EBI-25479633; Score: 0.35
DE  Interaction: Q8N5Y8; IntAct: EBI-25482187; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568044; Score: 0.35
DE  Interaction: P0DTC4; IntAct: EBI-25509966; Score: 0.35
DE  Interaction: P0DTC8; IntAct: EBI-25510273; Score: 0.35
DE  Interaction: P0DTD3; IntAct: EBI-25510342; Score: 0.35
DE  Interaction: Q96CS3; IntAct: EBI-25770166; Score: 0.35
DE  Interaction: Q8IWF2; IntAct: EBI-25770736; Score: 0.35
DE  Interaction: Q8NBM4; IntAct: EBI-25771384; Score: 0.35
DE  Interaction: Q5U458; IntAct: EBI-26450034; Score: 0.35
DE  Interaction: O60303; IntAct: EBI-26582514; Score: 0.35
DE  Interaction: P34972; IntAct: EBI-26880846; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NG92; IntAct: EBI-27055968; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: Q6P5Z2; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q86UX6; IntAct: EBI-28942129; Score: 0.35
DE  Interaction: Q99986; IntAct: EBI-28944934; Score: 0.35
DE  Interaction: Q9UJY1; IntAct: EBI-28946841; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q93009; IntAct: EBI-30841862; Score: 0.44
DE  Interaction: Q05925; IntAct: EBI-29000369; Score: 0.35
DE  Interaction: P23769; IntAct: EBI-29000495; Score: 0.35
DE  Interaction: P23771; IntAct: EBI-29000509; Score: 0.35
DE  Interaction: Q8TDD2; IntAct: EBI-29000537; Score: 0.35
DE  Interaction: P57682; IntAct: EBI-29000670; Score: 0.35
DE  Interaction: P43694; IntAct: EBI-29011567; Score: 0.35
DE  Interaction: Q9UIH9; IntAct: EBI-29019642; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-29373058; Score: 0.35
DE  Interaction: P35712; IntAct: EBI-29384845; Score: 0.35
DE  Interaction: P08047; IntAct: EBI-29385496; Score: 0.35
DE  Interaction: P31314; IntAct: EBI-29607649; Score: 0.35
DE  Interaction: O43763; IntAct: EBI-29612789; Score: 0.35
DE  Interaction: O43711; IntAct: EBI-29624592; Score: 0.35
DE  Interaction: P52952; IntAct: EBI-29653951; Score: 0.35
DE  Interaction: Q9Y4X4; IntAct: EBI-29017631; Score: 0.27
DE  Interaction: P21709; IntAct: EBI-32717758; Score: 0.35
DE  Interaction: P29322; IntAct: EBI-32718189; Score: 0.42
DE  Interaction: P22455; IntAct: EBI-32718547; Score: 0.35
DE  Interaction: P35916; IntAct: EBI-32718614; Score: 0.35
DE  Interaction: P08069; IntAct: EBI-32718669; Score: 0.42
DE  Interaction: P06213; IntAct: EBI-32718777; Score: 0.42
DE  Interaction: P08581; IntAct: EBI-32719056; Score: 0.42
DE  Interaction: P04629; IntAct: EBI-32719115; Score: 0.35
DE  Interaction: Q16288; IntAct: EBI-32719212; Score: 0.35
DE  Interaction: Q01974; IntAct: EBI-32719482; Score: 0.42
DE  Interaction: Q6J9G0; IntAct: EBI-32719662; Score: 0.42
DE  Interaction: Q06418; IntAct: EBI-32719716; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P21860; IntAct: EBI-32721529; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
DE  Interaction: P14616; IntAct: EBI-32723232; Score: 0.27
DE  Interaction: P35968; IntAct: EBI-32723270; Score: 0.27
DE  Interaction: Q8IWU2; IntAct: EBI-32723604; Score: 0.27
DE  Interaction: Q12866; IntAct: EBI-32723870; Score: 0.27
DE  Interaction: O15146; IntAct: EBI-32724025; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
DE  Interaction: P08922; IntAct: EBI-32731758; Score: 0.27
DE  Interaction: Q02763; IntAct: EBI-32732012; Score: 0.35
DE  Interaction: Q8N612; IntAct: EBI-34574737; Score: 0.27
DE  Interaction: Q5W0V3; IntAct: EBI-34574999; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005819;
GO  GO:0003779;
GO  GO:0048487;
GO  GO:0045296;
GO  GO:0071363;
GO  GO:0006936;
GO  GO:0007517;
GO  GO:0090090;
GO  GO:0048147;
GO  GO:0071763;
GO  GO:0046827;
GO  GO:0060828;
GO  GO:0035914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDNYADLSDTELTTLLRRYNIPHGPVVGSTRRLYEKKIFEYETQRRRLSPPSSSAASSYSFSDLNSTRGDADMYDLPKKE
SQ  DALLYQSKGYNDDYYEESYFTTRTYGEPESAGPSRAVRQSVTSFPDADAFHHQVHDDDLLSSSEEECKDRERPMYGRDSA
SQ  YQSITHYRPVSASRSSLDLSYYPTSSSTSFMSSSSSSSSWLTRRAIRPENRAPGAGLGQDRQVPLWGQLLLFLVFVIVLF
SQ  FIYHFMQAEEGNPF
//
ID  O08579;
PN  Emerin;
GN  Emd;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:P50402}; Single-pass membrane protein; Nucleoplasmic side {ECO:0000250|UniProtKB:P50402}. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: O08579;
DR  UNIPROT: Q3TIH6;
DR  UNIPROT: Q3UJP3;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta- catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1- dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non- farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells. {ECO:0000250|UniProtKB:P50402}.
DE  Reference Proteome: Yes;
DE  Interaction: P20263; IntAct: EBI-3043810; Score: 0.35
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q8NF91; IntAct: EBI-10760599; Score: 0.27
DE  Interaction: Q8WXH0; IntAct: EBI-10760623; Score: 0.27
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0032541;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0031616;
GO  GO:0003779;
GO  GO:0048487;
GO  GO:0071363;
GO  GO:0090090;
GO  GO:0048147;
GO  GO:0071763;
GO  GO:0046827;
GO  GO:0060828;
GO  GO:0035914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDDYAVLSDTELAAVLRQYNIPHGPIVGSTRKLYEKKIFEYETQRRRLLPPNSSSSSFSYQFSDLDSAAVDSDMYDLPKK
SQ  EDALLYQSKDYNDDYYEESYLTTKTYGEPESVGMSKSFRQPGTSLVDADTFHHQVRDDIFSSLEEEGKDRERLIYGQDSA
SQ  YQSIAHYRPISNVSRSSLGLSYYPTSSTSSVSSSSSSPSSWLTRRAIRPEKQAPAAALGQDRQVPLWGQLLLFLVFAAFL
SQ  LFVYYSIQAEEGNPFWMDP
//
ID  Q63190;
PN  Emerin;
GN  Emd;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:P50402}; Single-pass membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250|UniProtKB:P50402}. Nucleus outer membrane {ECO:0000250}. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle- attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q63190;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta- catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1- dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non- farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells. {ECO:0000250|UniProtKB:P50402}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0003779;
GO  GO:0048487;
GO  GO:0071363;
GO  GO:0090090;
GO  GO:0048147;
GO  GO:0071763;
GO  GO:0031468;
GO  GO:0046827;
GO  GO:0060828;
GO  GO:0035914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDDYAVLSDTELAAVLRQYNIPHGPILGSTRKLYEKKIFEYETQRRRLSPPSSSSSSFSYRFSDLDSASVDSDMYDLPKK
SQ  EDALLYQSKDYNDDYYEESYLTTRTYGEPESVGMSKSFRRPGTSLVDADDTFHHQVRDDIFSSSEEEGKDRERPIYGRDS
SQ  AYQSIAEYRPISNVSRSSLGLSYYPRSSTSSVSSSSSSPSSWLTRRAIRPEKQAPTAALGQDRQVPLWGQLLLFLAFATF
SQ  LLFVYYSIQAQEGNPFWMDP
//
ID  Q2NKU9;
PN  Epithelial membrane protein 2;
GN  EMP2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:O88662}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Apical cell membrane {ECO:0000250|UniProtKB:O88662}. Membrane raft {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Cytoplasm {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851, ECO:0000250|UniProtKB:Q66HH2}. Nucleus {ECO:0000250|UniProtKB:Q66HH2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88662}. Note=Localizes in cytoplasm, foot processes and cell bodies of podocytes and nucleus of endothelial cells of kidney. Localizes to the apical cell surface in the luminal epithelium and glandular epithelium. Colocalized with ITGB1 and GPI-anchor proteins on plasma membrane. {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:Q66HH2}.
DR  UNIPROT: Q2NKU9;
DR  Pfam: PF00822;
DR  PROSITE: PS01221;
DR  PROSITE: PS01222;
DE  Function: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potentially via mediation of cell surface expression of adhesion markers and lipid raft formation (By similarity). Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (By similarity). Facilitates surface trafficking and the formation of lipid rafts bearing GPI-anchor proteins (By similarity). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T- cell mediated cytotoxicity (By similarity). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5- ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (By similarity). Also regulates many processes through PTK2 (By similarity). Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (By similarity). Regulates cell migration and cell contraction through PTK2 and SRC activation (By similarity). Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2. Positively regulates cell proliferation (By similarity). Plays a role during cell death and cell blebbing (By similarity). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A-dependent pathway (By similarity). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (By similarity). Plays a role in placental angiogenesis and uterine natural killer cell regulation at the maternal-fetal placental interface, however not required in the maternal tissues for a viable pregnancy (By similarity). Involved in the early stages of embryogenic development and cardiogenesis, potentially via regulation of epithelial-mesenchymal transition timing (By similarity). May play a role in glomerular filtration (By similarity). {ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}.
DE  Reference Proteome: Yes;
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0045121;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0019901;
GO  GO:0007015;
GO  GO:0070252;
GO  GO:0032147;
GO  GO:0032060;
GO  GO:0043534;
GO  GO:0007155;
GO  GO:0008219;
GO  GO:0016477;
GO  GO:0007160;
GO  GO:0045022;
GO  GO:0007566;
GO  GO:0060136;
GO  GO:0060914;
GO  GO:0001765;
GO  GO:0001787;
GO  GO:1990266;
GO  GO:0044854;
GO  GO:0045766;
GO  GO:0062043;
GO  GO:0008284;
GO  GO:2001046;
GO  GO:0034394;
GO  GO:0072659;
GO  GO:0045765;
GO  GO:0001952;
GO  GO:0010594;
GO  GO:0003093;
GO  GO:0043549;
GO  GO:2001212;
GO  GO:0001913;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLVLLAFIIVFHITSAALLLVATIDNAWWVGEEFFADIWKVCVNNTNCTELNDSVQDFSTVQAVQATMILSTILCCIAFL
SQ  IFLLQLFRLKQGERFVLTSIIQLMACLCVMIAASIYTDRRKDIHEKNEELYAQTSGGSFGYSFILAWVAFAFTFISGLMY
SQ  LILRKRK
//
ID  F1QIK8;
PN  Epithelial membrane protein 2;
GN  emp2;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:O88662}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Apical cell membrane {ECO:0000250|UniProtKB:O88662}. Membrane raft {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Cytoplasm {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851, ECO:0000250|UniProtKB:Q66HH2}. Nucleus {ECO:0000250|UniProtKB:Q66HH2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88662}.
DR  UNIPROT: F1QIK8;
DR  Pfam: PF00822;
DR  PROSITE: PS01221;
DR  PROSITE: PS01222;
DE  Function: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. May play a role in glomerular filtration (PubMed:24814193). {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851, ECO:0000269|PubMed:24814193}.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0045121;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0008284;
GO  GO:0003093;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLVILAFIILFHITSAILLFIATINNAWRIKGDFSMDLWYNCNTTACYDIPKSATYDAAYLQAVQATMILATILCCVGFF
SQ  VFILQLFRLKQGERFVFTAIIQLLSAFCVMTGASIYTAEGLTFNGQEFKNAEYGYSFVVAWVAFPMTLLSGLMYLVLRKR
SQ  K
//
ID  P54851;
PN  Epithelial membrane protein 2;
GN  EMP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000269|PubMed:18400107}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:12107182, ECO:0000269|PubMed:18400107, ECO:0000269|PubMed:21637765, ECO:0000269|PubMed:28295343}. Apical cell membrane {ECO:0000250|UniProtKB:O88662}. Membrane raft {ECO:0000269|PubMed:21637765}. Cytoplasm {ECO:0000269|PubMed:21637765}. Nucleus {ECO:0000250|UniProtKB:Q66HH2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88662}. Note=Localizes in cytoplasm, foot processes and cell bodies of podocytes and nucleus of endothelial cells of kidney. Localizes to the apical cell surface in the luminal epithelium and glandular epithelium. Colocalized with ITGB1 and GPI- anchor proteins on plasma membrane. {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:Q66HH2}.
DR  UNIPROT: P54851;
DR  UNIPROT: B2R7V6;
DR  UNIPROT: D3DUF8;
DR  Pfam: PF00822;
DR  PROSITE: PS01221;
DR  PROSITE: PS01222;
DR  OMIM: 602334;
DR  OMIM: 615861;
DR  DisGeNET: 2013;
DE  Function: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potentially via mediation of cell surface expression of adhesion markers and lipid raft formation (By similarity). Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (PubMed:24814193). Facilitates surface trafficking and formation of lipid rafts bearing GPI-anchor proteins (By similarity). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T-cell mediated cytotoxicity (By similarity). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5- ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (PubMed:16216233). Also regulates many processes through PTK2. Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (PubMed:23439602). Regulates cell migration and cell contraction through PTK2 and SRC activation (PubMed:21637765, PubMed:22728127). Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (PubMed:19494199). Positively regulates cell proliferation (PubMed:24814193). Plays a role during cell death and cell blebbing (PubMed:12107182). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A- dependent pathway (PubMed:23334331). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (PubMed:16487956). Plays a role in placental angiogenesis and uterine natural killer cell regulation at the maternal-fetal placental interface, however not required in the maternal tissues for a viable pregnancy (By similarity). Involved in the early stages of embryogenic development and cardiogenesis, potentially via regulation of epithelial-mesenchymal transition timing (By similarity). May play a role in glomerular filtration (By similarity). {ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:O88662, ECO:0000269|PubMed:12107182, ECO:0000269|PubMed:16216233, ECO:0000269|PubMed:16487956, ECO:0000269|PubMed:19494199, ECO:0000269|PubMed:21637765, ECO:0000269|PubMed:22728127, ECO:0000269|PubMed:23334331, ECO:0000269|PubMed:23439602, ECO:0000269|PubMed:24814193}.
DE  Disease: Nephrotic syndrome 10 (NPHS10) [MIM:615861]: A form of nephrotic syndrome, a renal disease clinically characterized by focal segmental glomerulosclerosis, progressive renal failure, severe proteinuria, hypoalbuminemia, hyperlipidemia and edema. NPHS10 is a steroid-sensitive form characterized by onset in childhood and remission without end-stage kidney disease. {ECO:0000269|PubMed:24814193}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9WMX2; IntAct: EBI-9083575; Score: 0.37
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0045121;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005178;
GO  GO:0019900;
GO  GO:0019901;
GO  GO:0007015;
GO  GO:0070252;
GO  GO:0032147;
GO  GO:0032060;
GO  GO:0043534;
GO  GO:0007155;
GO  GO:0008219;
GO  GO:0016477;
GO  GO:0007160;
GO  GO:0045022;
GO  GO:0007566;
GO  GO:0060136;
GO  GO:0060914;
GO  GO:0001765;
GO  GO:0001787;
GO  GO:1990266;
GO  GO:0044854;
GO  GO:0045766;
GO  GO:0062043;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:2001046;
GO  GO:0034394;
GO  GO:0072659;
GO  GO:0045765;
GO  GO:0001952;
GO  GO:0010594;
GO  GO:0003093;
GO  GO:0043549;
GO  GO:2001212;
GO  GO:0001913;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLVLLAFIIAFHITSAALLFIATVDNAWWVGDEFFADVWRICTNNTNCTVINDSFQEYSTLQAVQATMILSTILCCIAFF
SQ  IFVLQLFRLKQGERFVLTSIIQLMSCLCVMIAASIYTDRREDIHDKNAKFYPVTREGSYGYSYILAWVAFACTFISGMMY
SQ  LILRKRK
//
ID  O88662;
PN  Epithelial membrane protein 2;
GN  Emp2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000269|PubMed:12189152, ECO:0000269|PubMed:14978215, ECO:0000269|PubMed:16487956, ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:12189152}. Apical cell membrane {ECO:0000269|PubMed:16216233, ECO:0000269|PubMed:18400107}. Membrane raft {ECO:0000269|PubMed:12763482, ECO:0000269|PubMed:14978215}. Cytoplasm {ECO:0000269|PubMed:16216233, ECO:0000269|PubMed:18400107, ECO:0000269|PubMed:28295343}. Nucleus {ECO:0000250|UniProtKB:Q66HH2}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:28295343}. Note=Localizes in cytoplasm, foot processes and cell bodies of podocytes and nucleus of endothelial cells of kidney (By similarity). Localizes to the apical cell surface in the luminal epithelium and glandular epithelium (PubMed:16487956). Colocalized with ITGB1 and GPI-anchor proteins on plasma membrane (PubMed:12189152) (PubMed:14978215). {ECO:0000250|UniProtKB:Q66HH2, ECO:0000269|PubMed:12189152, ECO:0000269|PubMed:14978215, ECO:0000269|PubMed:16487956}.
DR  UNIPROT: O88662;
DR  Pfam: PF00822;
DR  PROSITE: PS01221;
DR  PROSITE: PS01222;
DE  Function: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potentially via mediation of cell surface expression of adhesion markers and lipid raft formation (PubMed:31550239). Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (PubMed:17609206, PubMed:14978215). Facilitates surface trafficking and the formation of lipid rafts bearing GPI-anchor proteins (PubMed:14978215). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T-cell mediated cytotoxicity (PubMed:12763482). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5-ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (PubMed:12189152). Also regulates many processes through PTK2. Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (By similarity). Regulates cell migration and cell contraction through PTK2 and SRC activation (By similarity). Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (By similarity). Positively regulates cell proliferation (By similarity). Plays a role during cell death and cell blebbing (By similarity). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A- dependent pathway (By similarity). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (PubMed:16487956, PubMed:16216233). Plays a role in placental angiogenesis and uterine natural killer cell regulation at the maternal-fetal placental interface, however not required in the maternal tissues for a viable pregnancy (PubMed:28295343). Involved in the early stages of embryogenic development and cardiogenesis, potentially via regulation of epithelial-mesenchymal transition timing (PubMed:30773261). May play a role in glomerular filtration (By similarity). {ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:P54851, ECO:0000269|PubMed:12189152, ECO:0000269|PubMed:12763482, ECO:0000269|PubMed:14978215, ECO:0000269|PubMed:16216233, ECO:0000269|PubMed:16487956, ECO:0000269|PubMed:17609206, ECO:0000269|PubMed:28295343, ECO:0000269|PubMed:30773261, ECO:0000269|PubMed:31550239}.
DE  Reference Proteome: Yes;
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0045121;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005178;
GO  GO:0019900;
GO  GO:0019901;
GO  GO:0007015;
GO  GO:0070252;
GO  GO:0032147;
GO  GO:0032060;
GO  GO:0043534;
GO  GO:0007155;
GO  GO:0008219;
GO  GO:0016477;
GO  GO:0007160;
GO  GO:0045022;
GO  GO:0007566;
GO  GO:0060136;
GO  GO:0060914;
GO  GO:0001765;
GO  GO:0001787;
GO  GO:1990266;
GO  GO:0044854;
GO  GO:0045766;
GO  GO:0062043;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:2001046;
GO  GO:0034394;
GO  GO:0072659;
GO  GO:0045765;
GO  GO:0001952;
GO  GO:0010594;
GO  GO:0003093;
GO  GO:0043549;
GO  GO:2001212;
GO  GO:0001913;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLVILAFIIVFHIVSTALLFISTIDNAWWVGDSFSADLWRVCTNSTNCTEINELTGPEAFEGYSVMQAVQATMILSTILS
SQ  CISFLIFLLQLFRLKQGERFVLTSIIQLMSCLCVMIGASIYTDRRQDLHQQNRKLYYLLQEGSYGYSFILAWVAFAFTFI
SQ  SGLMYMILRKRK
//
ID  A5A6N6;
PN  Epithelial membrane protein 2;
GN  EMP2;
OS  9598;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:O88662}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Apical cell membrane {ECO:0000250|UniProtKB:O88662}. Membrane raft {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Cytoplasm {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851, ECO:0000250|UniProtKB:Q66HH2}. Nucleus {ECO:0000250|UniProtKB:Q66HH2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88662}. Note=Localizes in cytoplasm, foot processes and cell bodies of podocytes and nucleus of endothelial cells of kidney. Localizes to the apical cell surface in the luminal epithelium and glandular epithelium. Colocalized with ITGB1 and GPI-anchor proteins on plasma membrane on plasma membrane. {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:Q66HH2}.
DR  UNIPROT: A5A6N6;
DR  Pfam: PF00822;
DR  PROSITE: PS01221;
DR  PROSITE: PS01222;
DE  Function: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potentially via mediation of cell surface expression of adhesion markers and lipid raft formation (By similarity). Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (By similarity). Facilitates surface trafficking and the formation of lipid rafts bearing GPI-anchor proteins (By similarity). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T- cell mediated cytotoxicity (By similarity). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5- ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (By similarity). Also regulates many processes through PTK2 (By similarity). Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (By similarity). Regulates cell migration and cell contraction through PTK2 and SRC activation. Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (By similarity). Positively regulates cell proliferation (By similarity). Plays a role during cell death and cell blebbing (By similarity). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A-dependent pathway (By similarity). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (By similarity). Plays a role in placental angiogenesis and uterine natural killer cell regulation at the maternal-fetal placental interface, however not required in the maternal tissues for a viable pregnancy (By similarity). Involved in the early stages of embryogenic development and cardiogenesis, potentially via regulation of epithelial-mesenchymal transition timing (By similarity). May play a role in glomerular filtration (By similarity). {ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}.
DE  Reference Proteome: Yes;
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0045121;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005178;
GO  GO:0019901;
GO  GO:0007015;
GO  GO:0070252;
GO  GO:0032147;
GO  GO:0032060;
GO  GO:0043534;
GO  GO:0007155;
GO  GO:0008219;
GO  GO:0016477;
GO  GO:0007160;
GO  GO:0045022;
GO  GO:0007566;
GO  GO:0060136;
GO  GO:0060914;
GO  GO:0001765;
GO  GO:0001787;
GO  GO:1990266;
GO  GO:0044854;
GO  GO:0045766;
GO  GO:0062043;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:2001046;
GO  GO:0034394;
GO  GO:0072659;
GO  GO:0045765;
GO  GO:0001952;
GO  GO:0010594;
GO  GO:0003093;
GO  GO:0043549;
GO  GO:2001212;
GO  GO:0001913;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLVLLAFIIAFHITSAALLFIATIDNAWWVGDEFFADVWRICTNNTNCTVINDSFQEYSTLQAVQATMILSTILCCIAFF
SQ  IFVLQLFRLKQGERFVLTSIIQLMSCLCVMIAASIYTDRREDIHHKNAKFYPVTREGSYGYSYILAWVAFACTFISGMMY
SQ  LILRKRK
//
ID  Q66HH2;
PN  Epithelial membrane protein 2;
GN  Emp2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:O88662}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Apical cell membrane {ECO:0000250|UniProtKB:O88662}. Membrane raft {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Cytoplasm {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851, ECO:0000269|PubMed:24814193}. Nucleus {ECO:0000269|PubMed:24814193}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88662}. Note=Localizes in cytoplasm, foot processes and cell bodies of podocytes and nucleus of endothelial cells of kidney (PubMed:24814193). Localizes to the apical cell surface in the luminal epithelium and glandular epithelium. Colocalized with ITGB1 and GPI-anchor proteins on plasma membrane (By similarity). {ECO:0000250|UniProtKB:O88662, ECO:0000269|PubMed:24814193}.
DR  UNIPROT: Q66HH2;
DR  Pfam: PF00822;
DR  PROSITE: PS01221;
DR  PROSITE: PS01222;
DE  Function: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potentially via mediation of cell surface expression of adhesion markers and lipid raft formation (By similarity). Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (By similarity). Facilitates surface trafficking and the formation of lipid rafts bearing GPI-anchor proteins (By similarity). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T- cell mediated cytotoxicity (By similarity). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5- ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (By similarity). Also regulates many processes through PTK2 (By similarity). Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (By similarity). Regulates cell migration and cell contraction through PTK2 and SRC activation (By similarity). Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (By similarity). Positively regulates cell proliferation (By similarity). Plays a role during cell death and cell blebbing. Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A-dependent pathway (By similarity). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (By similarity). Plays a role in placental angiogenesis and uterine natural killer cell regulation at the maternal-fetal placental interface, however not required in the maternal tissues for a viable pregnancy (By similarity). Involved in the early stages of embryogenic development and cardiogenesis, potentially via regulation of epithelial-mesenchymal transition timing (By similarity). May play a role in glomerular filtration (By similarity). {ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}.
DE  Reference Proteome: Yes;
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0045121;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005178;
GO  GO:0019900;
GO  GO:0019901;
GO  GO:0007015;
GO  GO:0070252;
GO  GO:0032147;
GO  GO:0032060;
GO  GO:0043534;
GO  GO:0007155;
GO  GO:0008219;
GO  GO:0016477;
GO  GO:0007160;
GO  GO:0045022;
GO  GO:0007566;
GO  GO:0060136;
GO  GO:0060914;
GO  GO:0001765;
GO  GO:0001787;
GO  GO:1990266;
GO  GO:0044854;
GO  GO:0045766;
GO  GO:0062043;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:2001046;
GO  GO:0034394;
GO  GO:0072659;
GO  GO:0045765;
GO  GO:0001952;
GO  GO:0010594;
GO  GO:0003093;
GO  GO:0043549;
GO  GO:2001212;
GO  GO:0001913;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLVILAFIIVFHIVSTALLFISTIDNAWWVGDGFSADIWRVCTNSTNCTEINDLSSTEEFSGYSVMQAVQATMILSTILS
SQ  CISFLIFLLQLFRLKQGERFVLTAIIQLMSCLCVMIGASVYTDRRQDLHHQNSQLYYLLQEGSYGYSFILAWVAFAFTFI
SQ  SGLMYMILRKRK
//
ID  O01971;
PN  Emerin homolog 1;
GN  emr;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}; Single-pass membrane protein {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}; Nucleoplasmic side {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}. Nucleus envelope {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:25653391}. Note=Lmn-1 and mel-28 are required for its localization to the nuclear envelope (PubMed:11870211, PubMed:16950114). Remains in the nuclear envelope until mid-late anaphase (PubMed:10982402). Recruited to the reforming nuclear envelope from telophase and throughout interphase (PubMed:25653391). {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:25653391}.
DR  UNIPROT: O01971;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Nuclear lamina-associated inner nuclear membrane protein that is involved in cell division, nuclear structure organization, maintenance of nuclear envelope integrity and nuclear envelope reformation after mitosis (PubMed:11870211, PubMed:12684533, PubMed:22171324). Involved in chromosome segregation and cell division, probably via its interaction with the nuclear intermediate filament protein lmn-1, the main component of nuclear lamina (PubMed:11870211, PubMed:12684533). Required to organize the distribution of lmn-1, nuclear pore complexes (NPCs) and chromatin in mitotically active cells (PubMed:22171324). Together with lem-2, plays a role in baf-1 enrichment at the nuclear envelope in anaphase (PubMed:12684533). Together with lem-2, involved in muscle cell attachment to hypodermal cells, as well as muscle cell location and sarcomere organization (PubMed:22171324). May play a role in radiation-induced DNA damage repair response (PubMed:22383942). May repress binding of transcription factor pha-4 with target sequences in pharyngeal cells. {ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12684533, ECO:0000269|PubMed:20714352, ECO:0000269|PubMed:22171324, ECO:0000269|PubMed:22383942}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9XTB5; IntAct: EBI-6260324; Score: 0.27
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0005521;
GO  GO:0007059;
GO  GO:0000281;
GO  GO:0006998;
GO  GO:0010165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVSQLTDAELRDSLKSHGVSVGPIVATTRKLYEKKLIKLSDGSINNQSNLNDSQFNEDSLIISSSPKKSPPQRVFQNVS
SQ  AATAAATTSPESDSDDCEESMRYLTEEEMAADRASARQAQSNKGGFLGSTITFTILFVFIAVFAYFLIENAEQLKLVAET
SQ  NPEDTI
//
ID  Q9VYX1;
PN  Enhancer of yellow 2 transcription factor;
GN  e;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleoplasm {ECO:0000255|HAMAP- Rule:MF_03046, ECO:0000269|PubMed:17643381, ECO:0000269|PubMed:20048002}. Cytoplasm {ECO:0000255|HAMAP- Rule:MF_03046, ECO:0000269|PubMed:27016737}. Nucleus membrane {ECO:0000269|PubMed:18034162, ECO:0000269|PubMed:20048002, ECO:0000269|PubMed:27016737}; Peripheral membrane protein {ECO:0000269|PubMed:18034162, ECO:0000269|PubMed:20048002, ECO:0000269|PubMed:27016737}. Nucleus {ECO:0000269|Ref.11}. Note=Localizes to nuclear periphery, in contact with the nuclear pore complex (NPC). {ECO:0000269|PubMed:18034162, ECO:0000269|PubMed:20048002}.
DR  UNIPROT: Q9VYX1;
DR  Pfam: PF10163;
DE  Function: Involved in mRNA export coupled transcription activation by association with both the TREX-2/AMEX and the SAGA complexes (PubMed:18034162, PubMed:19947544, PubMed:27016737). The SAGA complex is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination (PubMed:11438676, PubMed:18206972). Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone H2B (PubMed:18206972). The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription (PubMed:18034162, PubMed:19947544). Required for nuclear receptor- mediated transactivation (PubMed:20714859, PubMed:20048002). Involved in transcription elongation by recruiting the THO complex onto nascent mRNA (PubMed:20048002). The TREX-2/AMEX complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket) (PubMed:27016737). TREX-2/AMEX participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (PubMed:17643381, PubMed:27016737). Recruited to the su(Hw) insulators via its interaction with su(Hw) and participates in the barrier activity of such insulators (PubMed:17643381). In contrast, it does not participate in the enhancer-blocking activity of the su(Hw) insulators (PubMed:17643381). {ECO:0000269|PubMed:11438676, ECO:0000269|PubMed:17643381, ECO:0000269|PubMed:18034162, ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:19947544, ECO:0000269|PubMed:20048002, ECO:0000269|PubMed:20714859, ECO:0000269|PubMed:27016737}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7JXF5; IntAct: EBI-2550835; Score: 0.46
DE  Interaction: Q9U3V9; IntAct: EBI-2550885; Score: 0.54
DE  Interaction: Q9U5W9; IntAct: EBI-2550010; Score: 0.35
DE  Interaction: Q8I8U7; IntAct: EBI-2550010; Score: 0.35
DE  Interaction: O76216; IntAct: EBI-2550010; Score: 0.43
DE  Interaction: Q8I8V0; IntAct: EBI-2550010; Score: 0.35
DE  Interaction: Q9VZJ9; IntAct: EBI-15145789; Score: 0.67
DE  Interaction: Q9U6R9; IntAct: EBI-15171898; Score: 0.49
DE  Interaction: Q9VI64; IntAct: EBI-15172342; Score: 0.49
DE  Interaction: Q9VVR6; IntAct: EBI-15172118; Score: 0.49
DE  Interaction: Q9VRY7; IntAct: EBI-15172566; Score: 0.67
DE  Interaction: P98149; IntAct: EBI-26728176; Score: 0.49
DE  Interaction: P49905; IntAct: EBI-26751710; Score: 0.49
DE  Interaction: Q9VGG3; IntAct: EBI-26795784; Score: 0.49
DE  Interaction: Q9VE51; IntAct: EBI-26806623; Score: 0.49
DE  Interaction: Q8IP15; IntAct: EBI-26838266; Score: 0.49
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0071819;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0000124;
GO  GO:0070390;
GO  GO:0070742;
GO  GO:0003682;
GO  GO:0043035;
GO  GO:0030374;
GO  GO:0001094;
GO  GO:0003713;
GO  GO:0033696;
GO  GO:0016578;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0045893;
GO  GO:0045944;
GO  GO:0015031;
GO  GO:0006357;
GO  GO:0006368;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSTSGAVDQYTVLTGDRSKIKDLLCSRLTECGWRDEVRLMCRNILMEKGTNNSFTVEQLIAEVTPKARTLVPDAVKKELL
SQ  MKIRTILTEIEEEPDEPEDES
//
ID  Q9VE34;
PN  Ectopic P granules protein 5 homolog;
GN  Epg5;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HCE0}. Lysosome {ECO:0000250|UniProtKB:Q9HCE0}.
DR  UNIPROT: Q9VE34;
DR  UNIPROT: Q8MT53;
DE  Function: Involved in autophagy. Plays a role in late steps of autophagy. {ECO:0000269|PubMed:26917586}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: O61307; IntAct: EBI-9946542; Score: 0.35
DE  Interaction: M9NFI9; IntAct: EBI-9959939; Score: 0.35
GO  GO:0005737;
GO  GO:0005764;
GO  GO:0048471;
GO  GO:0097352;
GO  GO:0006914;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATLEKPKKEKSKKSRNRVPIEKEEEEPAELSTSEEQRPAENVSLLEEFERVATLASSSSGEAIISHECCISSDVGVTSQ
SQ  EPEGTQEPTETEAQPSAPSAPPSTTVHVVQYPNLQPMQLSNAQVEEHSAKIVYRQAESPTGFALARSHIKLLSTEELRQI
SQ  YDCPELELAKQFELEFLMNSLLETSEADPLYAAVMEYYELQGKITSNLHDVEKLRKGCAESQKQIWVRQPVTRTFSGTCG
SQ  DGNVVQECVTYDVIQVDPIKLEVAKTSLTGLYDLVCHAYTNNSITAKITKVKVDQIINDLLTYPNLDGHSVVSLHHTQSG
SQ  EALQCVSQLRRAISILFSFVRRPSPNANFDKDLKEWLRKLIALQLLLATREDHWFLLFNILRCPNGVGSWAAQFLQLPGT
SQ  RAVRRGSQQNELPLDLNSPELNHCMAVLQILLMPVKKRNEYLKSQAQAHRELSDTPGATDRWIVVDSDGEDSHTPAGECV
SQ  GLKESDLVALLNQMPFEKIFTSALRIEKFLDDYIIEPDMITAQQMLAVVVFFSQLVKTIGEGLLTYNNERYKQLAKRLGR
SQ  LVRHTLQYVFDYNELFINNNLYKSSEMYERIQVELQALLVRACGYIYRTRNLGTWQYFSTLPFGTLDAEVIWHLFYYLNV
SQ  GFPTDLANDLVSNAEAAFQAEDFWRKFDLANADVAPEDMYYLLQTFFEMANERNRSKDGSLVKAICLHIFHIGYIHKSTR
SQ  EICYKTARDMLANLMDEDLFGCVLVQLKMRYGEVDQAAYLFKALPLENWHPSMDTFEVLSNWLLHFDYQSSESQLARLII
SQ  SHLNWGLDCEGRLFLPHNIHVRMAHLVNEALNKYAPEVIGASGISESVRQVSSLIDSTQSSREQFTNWCWRMVSVLRLHL
SQ  MDQGVESVRRTLQHPTEPLLFIPELERMEMIFQGVNENRPLALYVGMLVSLHGHSIPLICQHGFILLQQLLLDHRHAATI
SQ  RCLELIVPLFLETPETLANCESFQRLITTLLNADRTYLKLAKDMVYANSIGPILELLDNMLHHQIISYTSYGLCSPLNLL
SQ  NIWLNCFTTLPGWSQNSNLLYLLDRMLRISYQFPDCRAQAVEFFYNYYKDCTEWKSAPKGSALKAFFGGQSVSRIPLISP
SQ  QNCWLNLVILEIEFRLVDTRIFPELLRQISAQPVEAALKKTISLSKTSAFPASQLVIFKYAQLLASMESTHALFPIVCQK
SQ  FFELYLWRVPTENESLNFSHNFGVSDKFYEYNVPLMKSIKSQLKSAESYYSALATKNANDDAMAHFYRNCCKLMQNCALW
SQ  LEDTQINRFTSDAEHLPAQYNSEKLRELLSGHVNHWTEFLCLASLRKEQRHQADQWGRKVMRLSNQKAPRTPVQPKQRQP
SQ  PAQHIKSLLKSYEKIVENPLHIRVEPIKTPPIDGVIVAQIQKKMTTLNSTANNYHYKTSELNSLDLNYLERVPTLYSMIP
SQ  YEETRRKECTSLLFKRNCTAPAQIKLTPEHIRINDVISRKQAQNRERHDKIIEDILLAMSVESFAQAIEELGVCIGALLV
SQ  APLESSVTQIGVRVFYDIVDNLNEVTMKFQPTHDLYFQVLEKLGVFLEADQAAQGLAILRLALKRPDLLELLAGVFVPSR
SQ  TDVDHFLSMYEFLIDSHLKHCDTQTLFVLFSKFDLLGWMEAYQPKLSEINRLLLLVLQGLEAWSQPDSSLLQDLFRRHLV
SQ  HIFGYDFPQHYGEVMQLVLDRTSDQKLMPVVLLDLLNALFVRSNCAELSLQQSEVRVHELALDFARRQKLFTLKAATDTL
SQ  LLLSRHFQKERLHHGLHGLYPKHKDYCQALVLWFTSFGHTLLASAICSYQELLADQISDIVFGSIVETYSPWLIPYTEET
SQ  VSGVAHWIRQLTPGQSKVLLPWSEQHVSSCKLMIRSFVATIIQVLQYLPSSNKILEHVFAWYVHHFAQSSTTGHVLAPIH
SQ  EGLAQLPWERFLPPAQHVELLYDSLQKFLPESHAMLGHIFIRIEWNNWFAQMPQPVSILSRLFTIFVKIAFEPNIHIHPN
SQ  TSKILEDAIRYPWHLVECSELEQLLKWFVASVEPAIALKIPAESNYADRAVLELLRLACAMLPERSAQDAVVLGTAKRML
SQ  YTRSMVRMQRACGAKHQKLLATKEGERAFSNAFLELLDSIDGAISSCSEHRTMEEQRREALNLMLELVAPTQTQSQEVSN
SQ  IHIKALVWWQQRCSPGNLVMCSTLPAIGHLNTYIASIYSLLEASIENYFRTSPEIASWHAPSWQGLMEALSMSLPKLDLM
SQ  PIMQGSYFFSLHVFVLYKMEEIATDGDKVTFLQDLSQLLENLKTSPQTEPRMALVWGVIIARGCQIAQVNQQVKKPLHML
SQ  ARHLQIASTKAEGWGDGLLGVIGLKSEVITNRRKVLTRCLACVIFSLFPANRDLRIPSEEYESALRELSMLLANKKFTDI
SQ  KPLIVRAVSLLKESTFPDIRAVPHMVCRLISIFYEESYLTTIPEVWDFEFKLMAT
//
ID  Q9HCE0;
PN  Ectopic P granules protein 5 homolog;
GN  EPG5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:29130391}. Lysosome {ECO:0000269|PubMed:29130391}.
DR  UNIPROT: Q9HCE0;
DR  UNIPROT: A2BDF3;
DR  UNIPROT: Q9H8C8;
DR  PDB: 7JHX;
DR  OMIM: 242840;
DR  OMIM: 615068;
DR  DisGeNET: 57724;
DE  Function: Involved in autophagy. May play a role in a late step of autophagy, such as clearance of autophagosomal cargo. Plays a key role in innate and adaptive immune response triggered by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides from pathogens, and mediated by the nucleotide-sensing receptor TLR9. It is necessary for the translocation of CpG dinucleotides from early endosomes to late endosomes and lysosomes, where TLR9 is located (PubMed:29130391). {ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:23222957, ECO:0000269|PubMed:29130391}.
DE  Disease: Vici syndrome (VICIS) [MIM:242840]: A rare congenital multisystem disorder characterized by agenesis of the corpus callosum, cataracts, pigmentary defects, progressive cardiomyopathy, and variable immunodeficiency. Affected individuals also have profound psychomotor retardation and hypotonia due to a myopathy. {ECO:0000269|PubMed:23222957, ECO:0000269|PubMed:25331754, ECO:0000269|PubMed:26917586, ECO:0000269|PubMed:27343256, ECO:0000269|PubMed:28168853, ECO:0000269|PubMed:29130391}. Note=The disease is caused by variants affecting the gene represented in this entry. Affected individuals show homozygosity or compound heterozygosity for truncating mutations, aberrant splicing and/or missense mutations. Parental studies suggest recessive inheritance with no carrier manifestation (PubMed:23222957). {ECO:0000269|PubMed:23222957}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6VMQ6; IntAct: EBI-7244636; Score: 0.37
DE  Interaction: O55234; IntAct: EBI-11049538; Score: 0.35
DE  Interaction: P19739; IntAct: EBI-25685423; Score: 0.35
GO  GO:0005737;
GO  GO:0005764;
GO  GO:0048471;
GO  GO:0097352;
GO  GO:1990786;
GO  GO:0032456;
GO  GO:0008333;
GO  GO:0006862;
GO  GO:0034162;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEAVKPQRRAKAKASRTKTKEKKKYETPQREESSEVSLPKTSREQEIPSLACEFKGDHLKVVTDSQLQDDASGQNESEM
SQ  FDVPLTSLTISNEESLTCNTEPPKEGGEARPCVGDSAVTPKVHPGDNVGTKVETPKNFTEVEENMSVQGGLSESAPQSNF
SQ  SYTQPAMENIQVRETQNSKEDKQGLVCSSEVPQNVGLQSSCPAKHGFQTPRVKKLYPQLPAEIAGEAPALVAVKPLLRSE
SQ  RLYPELPSQLELVPFTKEQLKILEPGSWLENVESYLEEFDSMAHQDRHEFYELLLNYSRCRKQLLLAEAELLTLTSDCQN
SQ  AKSRLWQFKEEQMSVQGICADQVKVFSYHRYQRVEMNENALVELKKLFDAKSEHLHQTLALHSYTSVLSRLQVESYIYAL
SQ  LSSSAVLRSSAIHQQGRASKQTESIPSDLCQLKECISVLFMFTRRVNEDTQFHDDILLWLQKLVSVLQRVGCPGDHLFLL
SQ  NHILRCPAGVSKWAVPFIQIKVLHNPSGVFHFMQSLALLMSPVKNRAEFMCHMKPSERKPSSSGPGSGTWTLVDEGGEED
SQ  EDPETSWILLNEDDLVTILAQFPFHELFQHLLGFKAKGDYLPETTRPQEMMKIFAFANSLVELLAVGLETFNRARYRQFV
SQ  KRIGYMIRMTLGYVSDHWAQYVSHNQGSGLAQQPYSMEKLQVEFDELFLRAVLHVLKAKRLGIWLFMSEMPFGTLSVQML
SQ  WKLFYLMHQVESENLQQLSSSLQPAQCKQQLQDPEHFTNFEKCLSSMNSSEEICLLTTFAQMAQARRTNVDEDFIKIIVL
SQ  EIYEVSYVTLSTRETFSKVGRELLGTITAVHPEIISVLLDRVQETIDQVGMVSLYLFKELPLYLWQPSASEIAVIRDWLL
SQ  NYNLTVVKNKLACVILEGLNWGFAKQATLHLDQAVHAEVALMVLEAYQKYLAQKPYAGILSESMKQVSYLASIVRYGETP
SQ  ETSFNQWAWNLILRLKLHKNDYGIQPNCPAVPFSVTVPDMTESPTFHPLLKAVKAGMPIGCYLALSMTAVGHSIEKFCAE
SQ  GIPLLGILVQSRHLRTVVHVLDKILPLFYPCQYYLLKNEQFLSHLLLFLHLDSGVPQGVTQQVTHKVAQHLTGASHGDNV
SQ  KLLNSMIQAHISVSTQPNEVGPVAVLEFWVQALISQHLWYREQPILFLMDHLCKAAFQLMQEDCIQKLLYQQHKNALGYH
SQ  CDRSLLSSLVSWIVAGNITPSFVEGLATPTQVWFAWTVLNMESIFEEDSQLRRVIEGELVINSAFTPDQALKKAQTQLKL
SQ  PIVPSLQRLLIYRWAHQALVTPSDHPLLPLIWQKFFLLYLHRPGPQYGLPIDGCIGRRFFQSPAHINLLKEMKRRLTEVA
SQ  DFHHAASKALRVPAEGSEGLPESHSGTPGYLTSPELHKELVRLFNVYILWLEDENFQKGDTYIPSLPKHYDIHRLAKVMQ
SQ  NQQDLWMEYLNMERIYHEFQETVGLWTQAKLESHSTPCSLSVQLDFTDPLLAKERVLSNLRKHEAPQPPLALHPTKPPVP
SQ  VISSAVLLSQKDATQLVCTDLNLLQQQARTAALRESQQVALDGELLDTMPKQYVNREEQTTLHLECRGSSGKKCQGAAVV
SQ  TVQFEGMHKNEAISQQLHVLRKEVKQLQAEAAKPPSLNIVEAAVHAENLITALVNAYKLQPTPGIQKVGISLFFTIVDYV
SQ  SDETQRHPPTRQFFTSCIEILGQVFISGIKSECRKVLETILKNSRLCSLLSPFFTPNAAPAEFIQLYEQVVKFLSEDNSD
SQ  MIFMLLTKFDLKQWLSATKPPLSDRTRLLESIHLALTAWGLEPDEDILMPFNLFCKHWTYLLLYQFPDQYSDILRLLMQS
SQ  SAEQLLSPECWKATLRALGCCAPSCQQGAASTEGAVLPSSSDALLSDKQVMETIQWLSDFFYKLRLSKMDFKSFGLFSKW
SQ  SPYMADVKTFLGYLVKRLIDLEMTCLAQDPTASRKTVLKSLHSVIIQLFKPWILVLEDNESSQQRHYPWLESDTVVASSI
SQ  VQLFTDCIDSLHESFKDKLLPGDAGALWLHLMHYCEACTAPKMPEFILYAFHSTYRKLPWKDLHPDQMLMEAFFKVERGS
SQ  PKSCFLFLGSVLCEVNWVSVLSDAWNSSPHPETRSMIVCLLFMMILLAKEVQLVDQTDSPLLSLLGQTSSLSWHLVDIVS
SQ  YQSVLSYFSSHYPPSIILAKESYAELIMKLLKVSAGLSIPTDSQKHLDAVPKCQAFTHQMVQFLSTLEQNGKITLAVLEQ
SQ  EMSKLLDDIIVFNPPDMDSQTRHMALSSLFMEVLMMMNNATIPTAEFLRGSIRTWIGQKMHGLVVLPLLTAACQSLASVR
SQ  HMAETTEACITAYFKESPLNQNSGWGPILVSLQVPELTMEEFLQECLTLGSYLTLYVYLLQCLNSEQTLRNEMKVLLILS
SQ  KWLEQVYPSSVEEEAKLFLWWHQVLQLSLIQTEQNDSVLTESVIRILLLVQSRQNLVAEERLSSGILGAIGFGRKSPLSN
SQ  RFRVVARSMAAFLSVQVPMEDQIRLRPGSELHLTPKAQQALNALESMASSKQYVEYQDQILQATQFIRHPGHCLQDGKSF
SQ  LALLVNCLYPEVHYLDHIR
//
ID  Q80TA9;
PN  Ectopic P granules protein 5 homolog;
GN  Epg5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HCE0}. Lysosome {ECO:0000250|UniProtKB:Q9HCE0}.
DR  UNIPROT: Q80TA9;
DE  Function: Involved in autophagy. May play a role in a late step of autophagy, such as clearance of autophagosomal cargo. Plays a key role in innate and adaptive immune response triggered by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides from pathogens, and mediated by the nucleotide-sensing receptor TLR9. It is necessary for the translocation of CpG dinucleotides from early endosomes to late endosomes and lysosomes, where TLR9 is located. {ECO:0000250|UniProtKB:Q9HCE0}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005764;
GO  GO:0048471;
GO  GO:0097352;
GO  GO:0006914;
GO  GO:1990786;
GO  GO:0032456;
GO  GO:0008333;
GO  GO:0006862;
GO  GO:0034162;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEAVKPRRAKAKASRTKGKEKKKHEALQTCDAGPLPETCREQESPCPASELKGDDLKSSADPQLHSDVCGWNESEMFDI
SQ  PLTSLTIGDEGPPVQDTEDLKERGEVTAGDGDDEMELKVDPGDNVIAKGEPCKNFPEVEDHTLIQCGPPESTLQPDFPCT
SQ  QQAVEGSHAREHPTRKQDEAALGCSKVFQNVSLHSSYEAKEVSQPPRVKKLYPELPAEIAEVPALVAVKPLLRSERLYPE
SQ  LPSQPEVTPFTKEQLKLLEPGSWLENVASYVEEFDNIAHQDRHEFYELLLNYSRCRKQLLLAEAELLTLMSDCHSAKSRL
SQ  WHFKDEQMAVQGICADQVKVYGHHHYQRVEMNENVLGELKKLFDAKSEHLHQTLTLHSYTSVLSRLQVESYIFTLLNSSA
SQ  ALRSLAVYQADQVPKLTESIPSDVCQLKECISVLFMFTRRVSEDAQFHEDILLWLQKLVSVLQRVGCPGDHFFLLNHVLR
SQ  CPAGIRKWAVPFIQIKVLNNPSGVFHFMQSLALLMSPVKNRAEFMCHMKPSEWKPSSSGPASGNWTLVDEAGEEDEDPET
SQ  SWILLNEDDLVTLLSQFPFQELFQHLLGFKAKGDYLPETTRPQEMMKIFAFANSLVELLAVGLDTFNRARYRQFVKRIGY
SQ  LIRMTLGYVSDHWAQYVSHSTGAGLTPQPYSMEKLQVEFDELFLRAVLHVLKAKRLGIWLFMSEMPFGTLSVQMLWKLLY
SQ  LMHQVESGDLQQLCASLQPAECKRRLQDPEHFASFEKCLSSINSSEEICLLTAFAQMARARRTNVDEDFIKIIVLEIYEV
SQ  SYVTLSTRETFSKVGRELLGAIAAVHPEIISVLLDRVQETIDQVGMVSLYLFKELPLYLWRPSAPEIAVIRDWLLNNNLT
SQ  AVKNKLACVILEGLNWGFTEQGTLHLDQALHTEVALLVLEAYQKYLAQKPYTGLISESMKQVSYLASIVRYGETPETSFN
SQ  QWAWNLILRLKLHKNDFGRQNFPVIPFCSTVPDMTESSMFHPLLKAVKSGLPIGCYLALAVTAVGHSLEKFCAEGIPLLG
SQ  VLVQSRHLRAVVHALDKILPVFYPYQCYLLKNEQFLSNLLLFLQLDSGVPQGVTQQVTHRVAQHLTGAVHGDNVKLLSSM
SQ  IQAHICVSTQPDGVGPVAVLEFWVQALISQHLWYREQPILFLMDHLCKTAFHLMQEDCVQKLLYQQHKNALGYHCDRSLL
SQ  SSLVNWIVAGNITPSFVEGLSTSTQVWFAWTVLNMESIFEEDSQLRRVVERELVINAFSPDQALKKAQVQLKLPIVPSLQ
SQ  RLLIYRWAHQALVTPSDHPLLPLIWQKFFLLYLHRPGPQYGLPVDGCIGRRFFQSPSHVNLLKDMKRRLTEVADFHYAAS
SQ  KALRVPAEGSEGTPEGQAGTPGFLTSPELHRELVRLFNVYVLWLEDENFQKGDTYIPSLPKHYDVHRLAKVMQNQQDLWM
SQ  EYVNMERIQHEFQETVALWTQAKLESHAAPCSSSAQLDFTDPLLAKARVLSNLEKHEAPHPPLLLHPVRPPVPLIPSAAL
SQ  LTQKDSTQLMCTDLNLLQQQARSATLRESQQVALDGELLETMPKQYVNREDQATLHLECRGSSGKKCQGAAVVTVQFEGM
SQ  NKNEAVSQQIHVLQKEVRQLQAEAAQPPALNVVEAAVHAENLITALVNTYKLQPTPGVQKLGISLFFTVVDHVSDETQRH
SQ  PPTRQFFTSCIEILGQVFVSGTKSECRKLLQTILKNRRLCSLLAPFFTPNAAPAEFIQLYERVVTCLREDNSDVIFMLLT
SQ  KFDIQQWLNSTKPPLSDRTRLLESIHLALTAWGLEPEEDILMPFNLFCKHWTHLLLYQFPDQYSDVLRLLVQSSAEQLLS
SQ  PECWKATLRALGCYAPSSQQGAASVESSGLHSASRVLLSDKQVMETVQWLSDFFYKLRLSKLDFKSFGLFSKWSPYMADV
SQ  KTFLGYLVKRLTDLEIASLSQDPTASSKEVLRSLHAQIIQLFKPWILVLEDAESSHQRHYPWLESDTAVASSIVQLFSDC
SQ  VGSLHTSFKDRLLPGDEGALRLHLLHYCETCTAPKMPEFILYAFHSAYQRLEWKDLHPDQRLMEAFFKVERGSPKSCFLF
SQ  LGSVLCRVNWVSVLSDAWNPSPLPETQSMAVCLLFMMVLLAKEAQLVDEPDSPLLSLLGQTSSLSWHLVDLVSYQSVLGY
SQ  FSSHYPPSVVLANDCSSELIVKLLKVSAGLSAHADGRKHVDIVPKCQAFTHQMVQFLSALEQTGKITFPALEREISKLLD
SQ  DIIIFNPPDMDSQTRHMALSSFFVEVLMMMNNAAVPTAEFLAVSIRTWIGQRVHGLIVLPLLTAACQSLASVRHMAEITE
SQ  ACIMAYFKESSLDQNLGWGPVLVSLQVPQLTARDFLEECLALGSCLTLYVYLLQCLNSEQTVKNDMKMLLVVSGWLEQVY
SQ  PSSAQEEAKLFLWWHQILQLSLIQLEQNDSVLTESVIRILLMLQSRQSLMAEERLSSGILGAIGLGRRSPLSNRFRVAAR
SQ  SMAAFLLVQVPAEDQIRLKPSSELHLAPKAQQVLTALESMTLSKQYVEYQDQILHALQFIRHPGHCLQNGKSFLALLVNR
SQ  LYPEVHYLDNIR
//
ID  Q9H201;
PN  Epsin-3;
GN  EPN3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11359770}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11359770}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:11359770}. Nucleus {ECO:0000305|PubMed:11359770}. Note=Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the cell periphery. May shuttle to the nucleus.
DR  UNIPROT: Q9H201;
DR  UNIPROT: A8K6J3;
DR  UNIPROT: A8KAB2;
DR  UNIPROT: Q9BVN6;
DR  UNIPROT: Q9NWK2;
DR  Pfam: PF01417;
DR  Pfam: PF02809;
DR  PROSITE: PS50942;
DR  PROSITE: PS50330;
DR  OMIM: 607264;
DR  DisGeNET: 55040;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: O95271; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q9Y3C5; IntAct: EBI-7221338; Score: 0.37
DE  Interaction: Q13571; IntAct: EBI-7265708; Score: 0.37
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q9Y6I3; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q9Y597; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q9Y4X5; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q9UK73; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q9UJV3; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q9HCE7; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q9H3F6; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q9H2K2; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q9H0C5; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q96JC1; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q8TBC3; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q8IWV7; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q86YT6; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: P42575; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: P0CG47; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: O95208; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: O43175; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: O15344; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: E9PJD7; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-20908912; Score: 0.40
DE  Interaction: P62258; IntAct: EBI-25384933; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P42566; IntAct: EBI-30823506; Score: 0.44
GO  GO:0030125;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0005768;
GO  GO:0070062;
GO  GO:0019897;
GO  GO:0043231;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030276;
GO  GO:1990175;
GO  GO:0005543;
GO  GO:0006897;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTL
SQ  LDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGIG
SQ  IGSGQLGFSRRYGEDYSRSRGSPSSYNSSSSSPRYTSDLEQARPQTSGEEELQLQLALAMSREEAEKPVPPASHRDEDLQ
SQ  LQLALRLSRQEHEKEVRSWQGDGSPMANGAGAVVHHQRDREPEREERKEEEKLKTSQSSILDLADIFVPALAPPSTHCSA
SQ  DPWDIPGFRPNTEASGSSWGPSADPWSPIPSGTVLSRSQPWDLTPMLSSSEPWGRTPVLPAGPPTTDPWALNSPHHKLPS
SQ  TGADPWGASLETSDTPGGASTFDPFAKPPESTETKEGLEQALPSGKPSSPVELDLFGDPSPSSKQNGTKEPDALDLGILG
SQ  EALTQPSKEARACRTPESFLGPSASSLVNLDSLVKAPQVAKTRNPFLTGLSAPSPTNPFGAGEPGRPTLNQMRTGSPALG
SQ  LAGGPVGAPLGSMTYSASLPLPLSSVPAGLTLPASVSVFPQAGAFAPQPLLPTPSSAGPRPPPPQTGTNPFL
//
ID  Q91W69;
PN  Epsin-3;
GN  Epn3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the cell periphery. May shuttle to the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q91W69;
DR  UNIPROT: Q9CV55;
DR  Pfam: PF01417;
DR  Pfam: PF02809;
DR  PROSITE: PS50942;
DR  PROSITE: PS50330;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9WVK4; IntAct: EBI-15895272; Score: 0.35
DE  Interaction: P42566; IntAct: EBI-15895302; Score: 0.35
DE  Interaction: Q8BH64; IntAct: EBI-15895326; Score: 0.35
GO  GO:0005938;
GO  GO:0030125;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0005768;
GO  GO:0019897;
GO  GO:0043231;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030276;
GO  GO:1990175;
GO  GO:0005543;
GO  GO:0006897;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFAEVMGMVWRRLNDSGKNWRHVYKALTL
SQ  LDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGMG
SQ  IGSGQLGYSRRSRGSPSSYTSASSSPRYASDLEQARPQTSGEEELQLQLALAMSREEAERPVPPASHRDEDLQLQLALSL
SQ  SRQEHEKGVRSWKGDDSPVANGAEPAGQRRQRDREPEREERKEEEKLKTSQSSILDLADIFAPAPALPSTHCSADPWDIP
SQ  GLRPNTEPSGSSWGPSADPWSPVPSGNALSRSQPWDLLPTLSSSEPWGRTPVLPSGPPIADPWAPSSPTRKLPSTGADPW
SQ  GASMETSDTSALGGASPFDPFAKPLESTEPKESRDSAQALPTGKSPSTVELDPFGDSSPSCKQNGMKEPEALDLGVLGEA
SQ  LPQQPGKEARPCRTPESFLGPSASSLVNLDSLVKAPLAARTRNPFLTGLGVPSPTNPFGAGDQGRPTLNQMRTGSPALGL
SQ  PPGGPVGAPVGSMTYSASLPLPLSSVPVGATLPASVSVFPQAGAFAPPPASLPQPLLPTSGPMGPLPPQAGTNPFL
//
ID  Q4V882;
PN  Epsin-3;
GN  Epn3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Nucleus {ECO:0000250}. Note=Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the cell periphery. May shuttle to the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q4V882;
DR  Pfam: PF01417;
DR  PROSITE: PS50942;
DR  PROSITE: PS50330;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0030125;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0005768;
GO  GO:0019897;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030276;
GO  GO:1990175;
GO  GO:0005543;
GO  GO:0006897;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFAEVMGMVWRRLNDSGKNWRHVYKALTL
SQ  LDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGMG
SQ  IGSGQLGFSRRSRGSPSSYTSASSSPRYASDLEQARPQTSGEEELQLQLALAMSREEAEKGGRSWKGDDFPVANGAEPAG
SQ  QRRRDREPEREERKEEEKLKTSQSSILDLADVFAPAPALPSTHCSADPWDIPGLRPNTEPSGSSWGPSADPWSPVPSGNA
SQ  LSRSQPWDLLPTLSSSEPWGRTPVLPSGPPITDPWAPSSPTPKLPSTGVDPWGASVETSNTSALGGASPFDPFAKPLEST
SQ  EPMESRDSAQALPKGKSPSPVELDPFGDSSPSCKQNGVKETEALDLGVLGEALTQQPGKEARPCRTPESFLGPSASSLVN
SQ  LDSLVKAPLAARTRNPFLTGLSAPSPTNPFGAGEQGRPTLNQMRTGSPALGLPPGGPVGVPLGSMTYSASLPLPLSSVPV
SQ  GATLPASVSVFPQAGAFAPPPASLPQPLLPTSDPVGPLPPQAGTNPFL
//
ID  A7Z035;
PN  Clathrin interactor 1;
GN  CLINT1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00243}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans- Golgi network (By similarity). {ECO:0000250}.
DR  UNIPROT: A7Z035;
DR  Pfam: PF01417;
DR  PROSITE: PS50942;
DE  Function: Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030125;
GO  GO:0005768;
GO  GO:0005798;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005802;
GO  GO:0030276;
GO  GO:0005543;
GO  GO:0006897;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLNMWKVRELVDKATNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVY
SQ  KSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYV
SQ  GVSSDSVGGFRYSERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKA
SQ  RRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSLKTSVPSS
SQ  KSSGDLVDLFDGTSQSTGGSADLFGGFADFGSAAASGNFPSQVTATSGNGDFGDWSAFNQAPSVPVAASGELFGSASQPA
SQ  VELVSSSQPALGPPPAASNSSDLFDLMGSSQATMTSSQSMNFSMMSTNTVGLGLPMSRSQPLQNVSTVLQKPNPLYNQNT
SQ  DMVQKSVSKTLPSTWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPMNMMTQSFGAVNLSSPSNMLPVRPQTN
SQ  PLMGGPMPMSMPNVMTGTMGMAPLGNSPMMNQSMMGMNMNIGMSTTGMGLTGTMGMGMPNLAMTSGTMQPKQDAFANFAN
SQ  FSK
//
ID  Q14677;
PN  Clathrin interactor 1;
GN  CLINT1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Membrane; Peripheral membrane protein. Cytoplasmic vesicle, clathrin- coated vesicle. Note=Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans-Golgi network.
DR  UNIPROT: Q14677;
DR  UNIPROT: B7Z6F8;
DR  UNIPROT: D3DQJ6;
DR  UNIPROT: Q8NAF1;
DR  UNIPROT: Q96E05;
DR  PDB: 1XGW;
DR  PDB: 2QY7;
DR  PDB: 2V8S;
DR  Pfam: PF01417;
DR  PROSITE: PS50942;
DR  OMIM: 607265;
DR  DisGeNET: 9685;
DE  Function: Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. {ECO:0000269|PubMed:12429846, ECO:0000269|PubMed:12538641}.
DE  Reference Proteome: Yes;
DE  Interaction: O14976; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: O15027; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P22892; IntAct: EBI-7071326; Score: 0.54
DE  Interaction: P13569; IntAct: EBI-1171360; Score: 0.35
DE  Interaction: Q68FD5; IntAct: EBI-7071372; Score: 0.40
DE  Interaction: Q96FJ0; IntAct: EBI-2511015; Score: 0.40
DE  Interaction: O95630; IntAct: EBI-2511053; Score: 0.40
DE  Interaction: Q9BXB5; IntAct: EBI-2514827; Score: 0.40
DE  Interaction: Q9JLQ0; IntAct: EBI-2563436; Score: 0.40
DE  Interaction: A0A5P8YCG4; IntAct: EBI-2847836; Score: 0.00
DE  Interaction: A0A5P8YJZ1; IntAct: EBI-2870530; Score: 0.00
DE  Interaction: Q8CKM1; IntAct: EBI-2870523; Score: 0.00
DE  Interaction: Q8ZD27; IntAct: EBI-2870516; Score: 0.00
DE  Interaction: A0A5P8YBI5; IntAct: EBI-2870542; Score: 0.00
DE  Interaction: Q8ZDX4; IntAct: EBI-2870549; Score: 0.00
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-2946896; Score: 0.44
DE  Interaction: Q9H0R8; IntAct: EBI-2947275; Score: 0.52
DE  Interaction: P60520; IntAct: EBI-2947563; Score: 0.44
DE  Interaction: Q9GZQ8; IntAct: EBI-2947914; Score: 0.52
DE  Interaction: Q9BXW4; IntAct: EBI-2948265; Score: 0.44
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q9NQW6; IntAct: EBI-11009421; Score: 0.35
DE  Interaction: Q91X51; IntAct: EBI-11015786; Score: 0.35
DE  Interaction: Q99JI4; IntAct: EBI-11026623; Score: 0.35
DE  Interaction: Q92734; IntAct: EBI-11029015; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-11030093; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: O75787; IntAct: EBI-11037152; Score: 0.35
DE  Interaction: P56377; IntAct: EBI-11037753; Score: 0.35
DE  Interaction: P21333; IntAct: EBI-11038784; Score: 0.35
DE  Interaction: Q61879; IntAct: EBI-11041929; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: P51148; IntAct: EBI-11046231; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-12449761; Score: 0.51
DE  Interaction: Q91YN9; IntAct: EBI-11052510; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062262; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079358; Score: 0.35
DE  Interaction: Q91VZ6; IntAct: EBI-11079957; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: P09497; IntAct: EBI-11081190; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: Q13492; IntAct: EBI-11082344; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: P13541; IntAct: EBI-11092646; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-11092730; Score: 0.35
DE  Interaction: Q9WTI7; IntAct: EBI-11093786; Score: 0.35
DE  Interaction: P12883; IntAct: EBI-11098156; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11098811; Score: 0.35
DE  Interaction: Q96QS3; IntAct: EBI-11107478; Score: 0.35
DE  Interaction: P16333; IntAct: EBI-11108107; Score: 0.35
DE  Interaction: Q9Z1Z0; IntAct: EBI-11110688; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: Q6ZNC8; IntAct: EBI-11121915; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-11132927; Score: 0.35
DE  Interaction: Q99615; IntAct: EBI-11136121; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-11142496; Score: 0.35
DE  Interaction: Q5BJF6; IntAct: EBI-11367291; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11398030; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q8WTR4; IntAct: EBI-16430940; Score: 0.56
DE  Interaction: Q96FJ2; IntAct: EBI-12449804; Score: 0.51
DE  Interaction: P03431; IntAct: EBI-12579531; Score: 0.35
DE  Interaction: P03428; IntAct: EBI-12579909; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581451; Score: 0.35
DE  Interaction: Q5EP37; IntAct: EBI-12582677; Score: 0.35
DE  Interaction: C5E526; IntAct: EBI-12584689; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12588354; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12588729; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q96CW1; IntAct: EBI-21520588; Score: 0.35
DE  Interaction: O75379; IntAct: EBI-21524155; Score: 0.35
DE  Interaction: Q9UEU0; IntAct: EBI-21525256; Score: 0.35
DE  Interaction: Q9UNK0; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: Q9NSY1; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: Q9H0L4; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: Q96D71; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: Q8WXE9; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: Q8WU79; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: Q15311; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: Q10567; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: P53675; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: O95782; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: O94973; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: O00443; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: B9A025; IntAct: EBI-21615189; Score: 0.35
DE  Interaction: Q9UJ41; IntAct: EBI-21644136; Score: 0.35
DE  Interaction: Q96T17; IntAct: EBI-21796065; Score: 0.35
DE  Interaction: Q9UJY4; IntAct: EBI-21886169; Score: 0.35
DE  Interaction: O88384; IntAct: EBI-15671994; Score: 0.65
DE  Interaction: Q01968; IntAct: EBI-16412089; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.42
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: Q9NPJ6; IntAct: EBI-25472202; Score: 0.27
DE  Interaction: Q9Y586; IntAct: EBI-21261050; Score: 0.35
DE  Interaction: G3V2R1; IntAct: EBI-21264254; Score: 0.35
DE  Interaction: O84226; IntAct: EBI-22302652; Score: 0.40
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: O76024; IntAct: EBI-25897869; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25915115; Score: 0.56
DE  Interaction: O43464; IntAct: EBI-27050249; Score: 0.35
DE  Interaction: Q96LU5; IntAct: EBI-27050332; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: P80192; IntAct: EBI-28938802; Score: 0.35
DE  Interaction: Q5TCX8; IntAct: EBI-28941668; Score: 0.35
DE  Interaction: Q9BYP7; IntAct: EBI-28946054; Score: 0.35
DE  Interaction: Q9H3S7; IntAct: EBI-27114830; Score: 0.35
DE  Interaction: Q9Y6R9; IntAct: EBI-27132749; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-30816421; Score: 0.44
DE  Interaction: P54756; IntAct: EBI-32720907; Score: 0.27
DE  Interaction: Q15375; IntAct: EBI-32721052; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P21802; IntAct: EBI-32721907; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
DE  Interaction: P03372; IntAct: EBI-34581889; Score: 0.35
GO  GO:0030125;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045296;
GO  GO:0030276;
GO  GO:0005543;
GO  GO:0006897;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MLNMWKVRELVDKATNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVY
SQ  KSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYV
SQ  GVSSDSVGGFRYSERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKA
SQ  RRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSVKTSVPSS
SQ  KSSGDLVDLFDGTSQSTGGSADLFGGFADFGSAAASGSFPSQVTATSGNGDFGDWSAFNQAPSGPVASSGEFFGSASQPA
SQ  VELVSGSQSALGPPPAASNSSDLFDLMGSSQATMTSSQSMNFSMMSTNTVGLGLPMSRSQNTDMVQKSVSKTLPSTWSDP
SQ  SVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPMNVMTQSFGAVNLSSPSNMLPVRPQTNALIGGPMPMSMPNVMTGT
SQ  MGMAPLGNTPMMNQSMMGMNMNIGMSAAGMGLTGTMGMGMPNIAMTSGTVQPKQDAFANFANFSK
//
ID  Q99KN9;
PN  Clathrin interactor 1;
GN  Clint1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00243}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans- Golgi network (By similarity). {ECO:0000250}.
DR  UNIPROT: Q99KN9;
DR  UNIPROT: Q8CFH4;
DR  Pfam: PF01417;
DR  PROSITE: PS50942;
DE  Function: Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030125;
GO  GO:0030136;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030276;
GO  GO:0005543;
GO  GO:0048268;
GO  GO:0006897;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLIFMYLYVCVCTCTCAFSLCSTNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDN
SQ  KKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKA
SQ  KKNKDKYVGVSSDSVGGFRYNERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCS
SQ  DSDEEKKARRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSS
SQ  AKPSVPSSKSSGDLVDLFDGSSQSAGGSADLFGGFADFGSAAASGNFPSQATSGNGDFGDWSAFNQAPSGPVASGGELFG
SQ  SAPQSAVELISASQPALGPPPAASNSADLFDLMGSSQATMTSSQSMNFSLMSTNTVGLGLPMSRSQNTDMVQKSASKTLP
SQ  STWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPLNVMTQSFGAVNLSSPSNMLPVRPQTNPLLGGPMPMNMP
SQ  GVMTGTMGMAPLGNSAGMSQGMVGMNMNMGMSASGMGLSGTMGMGMPSMAMPSGTVQPKQDAFANFANFSK
//
ID  O18735;
PN  Receptor tyrosine-protein kinase erbB-2;
GN  ERBB2;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Early endosome {ECO:0000250|UniProtKB:P04626}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P04626}. Nucleus {ECO:0000250|UniProtKB:P04626}. Note=Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in endosome-to-TGN retrograde vesicles. Internalized from the cell membrane in response to EGF stimulation. {ECO:0000250|UniProtKB:P04626}.
DR  UNIPROT: O18735;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF07714;
DR  Pfam: PF01030;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). {ECO:0000250}. In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0009925;
GO  GO:0005769;
GO  GO:0005887;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0043235;
GO  GO:0005524;
GO  GO:0001042;
GO  GO:0004714;
GO  GO:0071364;
GO  GO:0071363;
GO  GO:0035556;
GO  GO:0030182;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0033674;
GO  GO:0043410;
GO  GO:0090314;
GO  GO:0045943;
GO  GO:0045727;
GO  GO:0070372;
GO  GO:0032886;
GO  GO:0007169;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELAAWCRWGLLLALLPSGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPANASLSFLQDIQEV
SQ  QGYVLIAHSQVRQIPLQRLRIVRGTQLFEDNYALAVLDNGDPLEGGIPAPGAAQGGLRELQLRSLTEILKGGVLIQRSPQ
SQ  LCHQDTILWKDVFHKNNQLALTLIDTNRFSACPPCSPACKDAHCWGASSGDCQSLTRTVCAGGCARCKGPQPTDCCHEQC
SQ  AAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTSCPYNYLSTDVGSCTLVCPLNNQ
SQ  EVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLRVF
SQ  EALEEITGYLYISAWPDSLPNLSVFQNLRVIRGRVLHDGAYSLTLQGLGISWLGLRSLRELGSGLALIHRNARLCFVHTV
SQ  PWDQLFRNPHQALLHSANRPEEECVGEGLACYPCAHGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVKDRYCL
SQ  PCHSECQPQNGSVTCFGSEADQCVACAHYKDPPFCVARCPSGVKPDLSFMPIWKFADEEGTCQPCPINCTHSCADLDEKG
SQ  CPAEQRASPVTSIIAAVVGILLAVVVGLVLGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELR
SQ  KVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLM
SQ  PYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADG
SQ  GKVPIKWMALESIPPRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMI
SQ  DSECRPRFRELVAEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPEPTPGAGG
SQ  TAHRRHRSSSTRNGGGELTLGLEPSEEEPPKSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPSQDPSPLQRYSEDPTVPLP
SQ  PETDGKVAPLTCSPQPEYVNQPEVWPQPPLALEGPLPPSRPAGATLERPKTLSPKTLSPGKNGVVKDVFAFGSAVENPEY
SQ  LAPRGRAAPQPHPPPAFSPAFDNLYYWDQDPSERGSPPSTFEGTPTAENPEYLGLDVPV
//
ID  P04626;
PN  Receptor tyrosine-protein kinase erbB-2;
GN  ERBB2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:32381043}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000269|PubMed:34380438}; Single-pass type I membrane protein {ECO:0000255}. Note=Internalized from the cell membrane in response to EGF stimulation. {ECO:0000269|PubMed:32381043}. [Isoform 1]: Cell membrane {ECO:0000269|PubMed:31138794, ECO:0000269|PubMed:33497358}; Single-pass type I membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:31138794}. Cytoplasm, perinuclear region. Nucleus. Note=Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in VPS35-positive endosome-to-TGN retrograde vesicles (PubMed:31138794). {ECO:0000269|PubMed:31138794}. [Isoform 2]: Cytoplasm. Nucleus. [Isoform 3]: Cytoplasm. Nucleus.
DR  UNIPROT: P04626;
DR  UNIPROT: B2RZG3;
DR  UNIPROT: B4DHN3;
DR  UNIPROT: Q14256;
DR  UNIPROT: Q6LDV1;
DR  UNIPROT: Q9UMK4;
DR  UNIPROT: X5D2V5;
DR  PDB: 1MFG;
DR  PDB: 1MFL;
DR  PDB: 1MW4;
DR  PDB: 1N8Z;
DR  PDB: 1QR1;
DR  PDB: 1S78;
DR  PDB: 2A91;
DR  PDB: 2JWA;
DR  PDB: 2KS1;
DR  PDB: 2L4K;
DR  PDB: 2N2A;
DR  PDB: 3BE1;
DR  PDB: 3H3B;
DR  PDB: 3MZW;
DR  PDB: 3N85;
DR  PDB: 3PP0;
DR  PDB: 3RCD;
DR  PDB: 3WLW;
DR  PDB: 3WSQ;
DR  PDB: 4GFU;
DR  PDB: 4HRL;
DR  PDB: 4HRM;
DR  PDB: 4HRN;
DR  PDB: 4NND;
DR  PDB: 5K33;
DR  PDB: 5KWG;
DR  PDB: 5MY6;
DR  PDB: 5O4G;
DR  PDB: 5OB4;
DR  PDB: 5TQS;
DR  PDB: 6ATT;
DR  PDB: 6BGT;
DR  PDB: 6J71;
DR  PDB: 6LBX;
DR  PDB: 6OGE;
DR  PDB: 7JXH;
DR  PDB: 7MN5;
DR  PDB: 7MN6;
DR  PDB: 7MN8;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF07714;
DR  Pfam: PF01030;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  OMIM: 137800;
DR  OMIM: 164870;
DR  OMIM: 167000;
DR  OMIM: 211980;
DR  OMIM: 613659;
DR  OMIM: 619465;
DR  DisGeNET: 2064;
DE  Function: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization. {ECO:0000305}. In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth. {ECO:0000269|PubMed:10358079, ECO:0000269|PubMed:15380516, ECO:0000269|PubMed:21555369}.
DE  Disease: Glioma (GLM) [MIM:137800]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. {ECO:0000269|PubMed:15457249}. Note=The gene represented in this entry is involved in disease pathogenesis. Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:15457249, ECO:0000269|PubMed:17344846}. Note=The gene represented in this entry is involved in disease pathogenesis. Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. {ECO:0000269|PubMed:15457249}. Note=The gene represented in this entry is involved in disease pathogenesis. Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. {ECO:0000269|PubMed:15457249, ECO:0000269|PubMed:17344846}. Note=The protein represented in this entry is involved in disease pathogenesis. Note=Chromosomal aberrations involving ERBB2 may be a cause gastric cancer. Deletions within 17q12 region producing fusion transcripts with CDK12, leading to CDK12-ERBB2 fusion leading to truncated CDK12 protein not in-frame with ERBB2. {ECO:0000269|PubMed:21097718}. Visceral neuropathy, familial, 2, autosomal recessive (VSCN2) [MIM:619465]: An autosomal recessive disorder characterized by intestinal dysmotility due to aganglionosis (Hirschsprung disease), hypoganglionosis, and/or chronic intestinal pseudoobstruction. Patients also show peripheral axonal neuropathy, hypotonia, mild developmental delay, unilateral ptosis, and sensorineural hearing loss. {ECO:0000269|PubMed:33497358}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O00165; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: O70248; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: O75190; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: O75694; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P00519; IntAct: EBI-7881352; Score: 0.44
DE  Interaction: P00533; IntAct: EBI-702075; Score: 0.95
DE  Interaction: P04406; IntAct: EBI-9687897; Score: 0.55
DE  Interaction: Q9H299; IntAct: EBI-8533023; Score: 0.40
DE  Interaction: P29353; IntAct: EBI-8533045; Score: 0.82
DE  Interaction: O00459; IntAct: EBI-8533204; Score: 0.70
DE  Interaction: P62993; IntAct: EBI-8533665; Score: 0.92
DE  Interaction: O00443; IntAct: EBI-641125; Score: 0.35
DE  Interaction: O00750; IntAct: EBI-641125; Score: 0.52
DE  Interaction: P23727; IntAct: EBI-7472363; Score: 0.40
DE  Interaction: P43405; IntAct: EBI-7872191; Score: 0.44
DE  Interaction: P20936; IntAct: EBI-7872273; Score: 0.59
DE  Interaction: P19174; IntAct: EBI-7872323; Score: 0.44
DE  Interaction: Q92569; IntAct: EBI-7872366; Score: 0.59
DE  Interaction: P27986; IntAct: EBI-7872561; Score: 0.76
DE  Interaction: P23458; IntAct: EBI-7872614; Score: 0.44
DE  Interaction: Q9Y490; IntAct: EBI-7872742; Score: 0.44
DE  Interaction: Q7KZ85; IntAct: EBI-7872692; Score: 0.44
DE  Interaction: Q63HR2; IntAct: EBI-7872814; Score: 0.44
DE  Interaction: Q9UQF2; IntAct: EBI-7873480; Score: 0.59
DE  Interaction: Q13387; IntAct: EBI-7873391; Score: 0.44
DE  Interaction: P09769; IntAct: EBI-7873560; Score: 0.44
DE  Interaction: O14796; IntAct: EBI-7873641; Score: 0.44
DE  Interaction: P98077; IntAct: EBI-7873711; Score: 0.44
DE  Interaction: Q8TEW6; IntAct: EBI-7873800; Score: 0.44
DE  Interaction: P46109; IntAct: EBI-7873890; Score: 0.44
DE  Interaction: P46108; IntAct: EBI-7873995; Score: 0.44
DE  Interaction: P42684; IntAct: EBI-7874156; Score: 0.44
DE  Interaction: Q9NSE2; IntAct: EBI-7874052; Score: 0.44
DE  Interaction: P42681; IntAct: EBI-7877479; Score: 0.44
DE  Interaction: P42224; IntAct: EBI-7877610; Score: 0.57
DE  Interaction: O15524; IntAct: EBI-7877654; Score: 0.44
DE  Interaction: Q9H6Q3; IntAct: EBI-7877680; Score: 0.44
DE  Interaction: Q13239; IntAct: EBI-7877723; Score: 0.44
DE  Interaction: Q8WYP3; IntAct: EBI-7877809; Score: 0.44
DE  Interaction: Q13671; IntAct: EBI-7877852; Score: 0.44
DE  Interaction: Q7Z7G1; IntAct: EBI-7878187; Score: 0.44
DE  Interaction: Q08881; IntAct: EBI-7878322; Score: 0.44
DE  Interaction: O14654; IntAct: EBI-7878365; Score: 0.44
DE  Interaction: P35568; IntAct: EBI-7878450; Score: 0.44
DE  Interaction: Q14451; IntAct: EBI-7878494; Score: 0.78
DE  Interaction: Q7Z6G8; IntAct: EBI-7878520; Score: 0.44
DE  Interaction: Q6PKX4; IntAct: EBI-7878747; Score: 0.44
DE  Interaction: Q99704; IntAct: EBI-7878971; Score: 0.44
DE  Interaction: Q8WV28; IntAct: EBI-7879040; Score: 0.44
DE  Interaction: P51451; IntAct: EBI-7879084; Score: 0.44
DE  Interaction: O95704; IntAct: EBI-7879155; Score: 0.44
DE  Interaction: O00213; IntAct: EBI-7879203; Score: 0.44
DE  Interaction: Q92625; IntAct: EBI-7879248; Score: 0.44
DE  Interaction: Q9UKW4; IntAct: EBI-7879334; Score: 0.44
DE  Interaction: P52735; IntAct: EBI-7879377; Score: 0.44
DE  Interaction: Q96D37; IntAct: EBI-7879875; Score: 0.44
DE  Interaction: Q68CZ2; IntAct: EBI-7879918; Score: 0.44
DE  Interaction: P78314; IntAct: EBI-7880141; Score: 0.44
DE  Interaction: Q9NP31; IntAct: EBI-7880184; Score: 0.44
DE  Interaction: Q06124; IntAct: EBI-7880270; Score: 0.59
DE  Interaction: P16885; IntAct: EBI-7880409; Score: 0.57
DE  Interaction: O43639; IntAct: EBI-7880962; Score: 0.44
DE  Interaction: O75791; IntAct: EBI-7881093; Score: 0.57
DE  Interaction: O75553; IntAct: EBI-7881180; Score: 0.44
DE  Interaction: P51813; IntAct: EBI-7881223; Score: 0.44
DE  Interaction: O75815; IntAct: EBI-7881266; Score: 0.44
DE  Interaction: P40763; IntAct: EBI-7883743; Score: 0.78
DE  Interaction: Q92529; IntAct: EBI-7883839; Score: 0.44
DE  Interaction: P42679; IntAct: EBI-7884171; Score: 0.59
DE  Interaction: Q9UQQ2; IntAct: EBI-7884193; Score: 0.44
DE  Interaction: P16591; IntAct: EBI-7884310; Score: 0.44
DE  Interaction: Q6ZV89; IntAct: EBI-7884338; Score: 0.44
DE  Interaction: P15882; IntAct: EBI-7884418; Score: 0.44
DE  Interaction: P42680; IntAct: EBI-7891341; Score: 0.44
DE  Interaction: Q9BRG2; IntAct: EBI-7892184; Score: 0.44
DE  Interaction: O14492; IntAct: EBI-7893084; Score: 0.44
DE  Interaction: P21860; IntAct: EBI-875459; Score: 0.97
DE  Interaction: Q15303; IntAct: EBI-875465; Score: 0.82
DE  Interaction: Q80TH2; IntAct: EBI-7806162; Score: 0.37
DE  Interaction: P04626; IntAct: EBI-1000502; Score: 0.93
DE  Interaction: P62157; IntAct: EBI-1257031; Score: 0.40
DE  Interaction: P62161; IntAct: EBI-1257044; Score: 0.44
DE  Interaction: P16070; IntAct: EBI-1774582; Score: 0.35
DE  Interaction: P08575; IntAct: EBI-2256762; Score: 0.00
DE  Interaction: Q15262; IntAct: EBI-2257483; Score: 0.00
DE  Interaction: P23470; IntAct: EBI-2258522; Score: 0.00
DE  Interaction: P23471; IntAct: EBI-2263296; Score: 0.00
DE  Interaction: P23467; IntAct: EBI-2264176; Score: 0.00
DE  Interaction: Q12913; IntAct: EBI-2264587; Score: 0.00
DE  Interaction: Q16827; IntAct: EBI-2265156; Score: 0.00
DE  Interaction: P26045; IntAct: EBI-2266001; Score: 0.00
DE  Interaction: Q05209; IntAct: EBI-3952071; Score: 0.59
DE  Interaction: Q9Y2R2; IntAct: EBI-2266470; Score: 0.00
DE  Interaction: Q02297; IntAct: EBI-2460992; Score: 0.44
DE  Interaction: P12931; IntAct: EBI-8289901; Score: 0.71
DE  Interaction: P41240; IntAct: EBI-8677066; Score: 0.35
DE  Interaction: Q05397; IntAct: EBI-2942138; Score: 0.54
DE  Interaction: O95980; IntAct: EBI-8569595; Score: 0.56
DE  Interaction: Q9Y316; IntAct: EBI-7072663; Score: 0.40
DE  Interaction: Q14974; IntAct: EBI-4373084; Score: 0.57
DE  Interaction: P49792; IntAct: EBI-4373195; Score: 0.46
DE  Interaction: O14980; IntAct: EBI-4373229; Score: 0.56
DE  Interaction: Q00610; IntAct: EBI-4373234; Score: 0.35
DE  Interaction: Q15075; IntAct: EBI-4373273; Score: 0.57
DE  Interaction: P50570; IntAct: EBI-4373368; Score: 0.35
DE  Interaction: P42566; IntAct: EBI-4373373; Score: 0.43
DE  Interaction: P60709; IntAct: EBI-4373715; Score: 0.54
DE  Interaction: O95602; IntAct: EBI-4373923; Score: 0.57
DE  Interaction: Q9UBN7; IntAct: EBI-4398276; Score: 0.55
DE  Interaction: P15309; IntAct: EBI-8681281; Score: 0.47
DE  Interaction: P98172; IntAct: EBI-5451673; Score: 0.46
DE  Interaction: P46940; IntAct: EBI-5458762; Score: 0.60
DE  Interaction: O43157; IntAct: EBI-6092574; Score: 0.40
DE  Interaction: O75367; IntAct: EBI-6249307; Score: 0.56
DE  Interaction: P06401; IntAct: EBI-6255956; Score: 0.35
DE  Interaction: Q96SB4; IntAct: EBI-6659552; Score: 0.44
DE  Interaction: P08238; IntAct: EBI-6424213; Score: 0.79
DE  Interaction: Q14289; IntAct: EBI-6589791; Score: 0.27
DE  Interaction: P35070; IntAct: EBI-6590054; Score: 0.27
DE  Interaction: P14923; IntAct: EBI-6592604; Score: 0.27
DE  Interaction: P01135; IntAct: EBI-6593605; Score: 0.27
DE  Interaction: Q99650; IntAct: EBI-6595538; Score: 0.27
DE  Interaction: Q16543; IntAct: EBI-8770673; Score: 0.69
DE  Interaction: Q03169; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P25686; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P33947; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q9HCY8; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q3ZCQ8; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: P42704; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: P36542; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: P08195; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P07355; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: P07900; IntAct: EBI-8770853; Score: 0.86
DE  Interaction: O60884; IntAct: EBI-8770853; Score: 0.57
DE  Interaction: P15880; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: O00483; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: P02786; IntAct: EBI-8770853; Score: 0.67
DE  Interaction: P27348; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P55795; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: P62714; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q9H254; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-8770853; Score: 0.66
DE  Interaction: P49411; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P61619; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: P30153; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q99959; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P67775; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q9BVV7; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: Q9P035; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q92504; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: Q93084; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q8TF42; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P62879; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q9UJM3; IntAct: EBI-8770853; Score: 0.66
DE  Interaction: O95292; IntAct: EBI-8770853; Score: 0.67
DE  Interaction: Q9HAV0; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P43307; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q8WUY1; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: P35232; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q8NHS0; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q9UBM7; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P53007; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-8770853; Score: 0.57
DE  Interaction: Q9NTG1; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-8770853; Score: 0.64
DE  Interaction: P62873; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-8770853; Score: 0.55
DE  Interaction: P10620; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P16520; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q9GZT3; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: O95470; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P31689; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: Q96FQ6; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P57088; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q8IXB1; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: O95573; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: P16615; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: Q14032; IntAct: EBI-8997691; Score: 0.37
DE  Interaction: Q9BU70; IntAct: EBI-8997704; Score: 0.37
DE  Interaction: P49336; IntAct: EBI-8997717; Score: 0.37
DE  Interaction: Q14093; IntAct: EBI-8997730; Score: 0.37
DE  Interaction: O75474; IntAct: EBI-8997756; Score: 0.37
DE  Interaction: P09467; IntAct: EBI-8997743; Score: 0.37
DE  Interaction: P37058; IntAct: EBI-8997769; Score: 0.37
DE  Interaction: Q9P1Z9; IntAct: EBI-8997782; Score: 0.37
DE  Interaction: Q02750; IntAct: EBI-8997795; Score: 0.37
DE  Interaction: Q6FHJ7; IntAct: EBI-8997821; Score: 0.37
DE  Interaction: Q15797; IntAct: EBI-8997834; Score: 0.37
DE  Interaction: O75820; IntAct: EBI-8997860; Score: 0.37
DE  Interaction: P01137; IntAct: EBI-8997847; Score: 0.37
DE  Interaction: O94812; IntAct: EBI-9064260; Score: 0.37
DE  Interaction: P08133; IntAct: EBI-9064247; Score: 0.37
DE  Interaction: P41252; IntAct: EBI-9064312; Score: 0.37
DE  Interaction: P51797; IntAct: EBI-9064273; Score: 0.37
DE  Interaction: Q9P2T1; IntAct: EBI-9064286; Score: 0.55
DE  Interaction: Q00341; IntAct: EBI-9064299; Score: 0.37
DE  Interaction: Q9BUL5; IntAct: EBI-9064351; Score: 0.37
DE  Interaction: Q8IW90; IntAct: EBI-9064325; Score: 0.37
DE  Interaction: Q96DR8; IntAct: EBI-9064338; Score: 0.37
DE  Interaction: Q9H3H9; IntAct: EBI-9064403; Score: 0.37
DE  Interaction: P49005; IntAct: EBI-9064364; Score: 0.37
DE  Interaction: P07602; IntAct: EBI-9064377; Score: 0.37
DE  Interaction: Q9Y6E0; IntAct: EBI-9064390; Score: 0.37
DE  Interaction: Q9Y5J1; IntAct: EBI-9064442; Score: 0.37
DE  Interaction: Q15904; IntAct: EBI-9064416; Score: 0.37
DE  Interaction: Q8N6N2; IntAct: EBI-9064429; Score: 0.37
DE  Interaction: P05093; IntAct: EBI-9067433; Score: 0.37
DE  Interaction: Q14627; IntAct: EBI-9067472; Score: 0.37
DE  Interaction: O94923; IntAct: EBI-9067459; Score: 0.37
DE  Interaction: Q9Y337; IntAct: EBI-9067485; Score: 0.37
DE  Interaction: O95274; IntAct: EBI-9067498; Score: 0.37
DE  Interaction: P11245; IntAct: EBI-9067511; Score: 0.37
DE  Interaction: Q9P2W1; IntAct: EBI-9067537; Score: 0.37
DE  Interaction: Q9GZV8; IntAct: EBI-9067524; Score: 0.37
DE  Interaction: Q9BYZ6; IntAct: EBI-9067550; Score: 0.37
DE  Interaction: Q92748; IntAct: EBI-9067563; Score: 0.37
DE  Interaction: Q13451; IntAct: EBI-9363176; Score: 0.40
DE  Interaction: Q3UJD6; IntAct: EBI-9363211; Score: 0.40
DE  Interaction: Q6PK50; IntAct: EBI-9363230; Score: 0.40
DE  Interaction: Q9BPW0; IntAct: EBI-9363250; Score: 0.40
DE  Interaction: P58340; IntAct: EBI-9363270; Score: 0.40
DE  Interaction: Q9BTE6; IntAct: EBI-9363294; Score: 0.40
DE  Interaction: Q9Y266; IntAct: EBI-9363318; Score: 0.40
DE  Interaction: Q13200; IntAct: EBI-9363339; Score: 0.40
DE  Interaction: Q8IWX7; IntAct: EBI-9363369; Score: 0.40
DE  Interaction: P31948; IntAct: EBI-9363393; Score: 0.57
DE  Interaction: Q8IVD9; IntAct: EBI-9363414; Score: 0.40
DE  Interaction: B4DYC6; IntAct: EBI-9363439; Score: 0.40
DE  Interaction: Q96BE0; IntAct: EBI-9363465; Score: 0.40
DE  Interaction: Q9HB71; IntAct: EBI-9363493; Score: 0.57
DE  Interaction: Q15773; IntAct: EBI-9363541; Score: 0.40
DE  Interaction: Q53FC7; IntAct: EBI-9363565; Score: 0.40
DE  Interaction: Q13882; IntAct: EBI-9293590; Score: 0.63
DE  Interaction: P14618; IntAct: EBI-9353947; Score: 0.44
DE  Interaction: P06241; IntAct: EBI-9396596; Score: 0.56
DE  Interaction: P15311; IntAct: EBI-9690211; Score: 0.37
DE  Interaction: P06461; IntAct: EBI-11723785; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: P0CK58; IntAct: EBI-11732874; Score: 0.35
DE  Interaction: P48651; IntAct: EBI-11145552; Score: 0.35
DE  Interaction: P26641; IntAct: EBI-11145552; Score: 0.35
DE  Interaction: O15260; IntAct: EBI-11145552; Score: 0.35
DE  Interaction: Q9H9Y6; IntAct: EBI-11145552; Score: 0.35
DE  Interaction: Q92973; IntAct: EBI-11145552; Score: 0.35
DE  Interaction: Q3V6T2; IntAct: EBI-11145552; Score: 0.35
DE  Interaction: P11498; IntAct: EBI-11145552; Score: 0.35
DE  Interaction: Q8ND82; IntAct: EBI-11145552; Score: 0.35
DE  Interaction: Q9Y251; IntAct: EBI-11145552; Score: 0.35
DE  Interaction: Q969S3; IntAct: EBI-11145552; Score: 0.35
DE  Interaction: Q99952; IntAct: EBI-12739796; Score: 0.56
DE  Interaction: P22681; IntAct: EBI-13637258; Score: 0.40
DE  Interaction: P04201; IntAct: EBI-21538834; Score: 0.35
DE  Interaction: Q8TDQ0; IntAct: EBI-21556046; Score: 0.35
DE  Interaction: P43115; IntAct: EBI-21607127; Score: 0.35
DE  Interaction: P37173; IntAct: EBI-21668347; Score: 0.35
DE  Interaction: P40259; IntAct: EBI-21668943; Score: 0.35
DE  Interaction: Q58DX5; IntAct: EBI-21782845; Score: 0.35
DE  Interaction: P24394; IntAct: EBI-21800565; Score: 0.35
DE  Interaction: Q8NBA8; IntAct: EBI-21829890; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-16072470; Score: 0.40
DE  Interaction: Q93034; IntAct: EBI-16247158; Score: 0.40
DE  Interaction: O14522; IntAct: EBI-20977013; Score: 0.37
DE  Interaction: Q92729; IntAct: EBI-20977022; Score: 0.37
DE  Interaction: Q15256; IntAct: EBI-20977323; Score: 0.51
DE  Interaction: Q9H0C8; IntAct: EBI-20980596; Score: 0.37
DE  Interaction: O95147; IntAct: EBI-20980636; Score: 0.37
DE  Interaction: Q8NEJ0; IntAct: EBI-20980646; Score: 0.37
DE  Interaction: Q8WTR2; IntAct: EBI-20980656; Score: 0.37
DE  Interaction: Q8WUJ0; IntAct: EBI-20980666; Score: 0.37
DE  Interaction: P29350; IntAct: EBI-20980616; Score: 0.37
DE  Interaction: P35813; IntAct: EBI-20980576; Score: 0.37
DE  Interaction: P49593; IntAct: EBI-20980586; Score: 0.37
DE  Interaction: Q96LT7; IntAct: EBI-20938756; Score: 0.35
DE  Interaction: B4F779; IntAct: EBI-22242273; Score: 0.35
DE  Interaction: P62078; IntAct: EBI-22242273; Score: 0.35
DE  Interaction: A0A0G2K064; IntAct: EBI-22242273; Score: 0.35
DE  Interaction: Q64537; IntAct: EBI-22242273; Score: 0.35
DE  Interaction: Q6AZ23; IntAct: EBI-22242273; Score: 0.35
DE  Interaction: Q62985; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: P41499; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: F1LM93; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: A0A0G2JVN4; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: P68101; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: M0R6T4; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: Q3KRF2; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: Q5M963; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: D3ZT90; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: Q8K1Q0; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: Q6AYD5; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: Q9QZC5; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: P62083; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: B2GV09; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: B2RZ33; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: D3ZD73; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: M0R7K1; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: P62703; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: G3V8S2; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: Q9Z2M4; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: Q66X93; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: Q9WVK3; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: Q8VID1; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: P10860; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: P15651; IntAct: EBI-22242478; Score: 0.35
DE  Interaction: P24666; IntAct: EBI-25367578; Score: 0.37
DE  Interaction: P25098; IntAct: EBI-25367534; Score: 0.37
DE  Interaction: P26038; IntAct: EBI-25367457; Score: 0.37
DE  Interaction: P63104; IntAct: EBI-25367490; Score: 0.37
DE  Interaction: Q15654; IntAct: EBI-25367468; Score: 0.37
DE  Interaction: Q96NW7; IntAct: EBI-25367523; Score: 0.37
DE  Interaction: P04075; IntAct: EBI-25367688; Score: 0.37
DE  Interaction: O00170; IntAct: EBI-25367666; Score: 0.37
DE  Interaction: Q6ZMQ8; IntAct: EBI-25367655; Score: 0.37
DE  Interaction: P09972; IntAct: EBI-25367699; Score: 0.37
DE  Interaction: Q13367; IntAct: EBI-25367710; Score: 0.37
DE  Interaction: Q02952; IntAct: EBI-25367677; Score: 0.37
DE  Interaction: P84085; IntAct: EBI-25367743; Score: 0.37
DE  Interaction: P84077; IntAct: EBI-25367732; Score: 0.37
DE  Interaction: P51693; IntAct: EBI-25367721; Score: 0.37
DE  Interaction: Q7L266; IntAct: EBI-25367754; Score: 0.37
DE  Interaction: P27449; IntAct: EBI-25367765; Score: 0.37
DE  Interaction: Q12981; IntAct: EBI-25367776; Score: 0.37
DE  Interaction: Q96D05; IntAct: EBI-25367787; Score: 0.37
DE  Interaction: Q9UKR5; IntAct: EBI-25367798; Score: 0.37
DE  Interaction: Q96A57; IntAct: EBI-25367809; Score: 0.37
DE  Interaction: P57076; IntAct: EBI-25367820; Score: 0.37
DE  Interaction: Q8N5G0; IntAct: EBI-25367831; Score: 0.37
DE  Interaction: P16152; IntAct: EBI-25367842; Score: 0.37
DE  Interaction: Q9Y2S6; IntAct: EBI-25367853; Score: 0.37
DE  Interaction: P12277; IntAct: EBI-25367897; Score: 0.37
DE  Interaction: O75122; IntAct: EBI-25367908; Score: 0.37
DE  Interaction: Q14055; IntAct: EBI-25367919; Score: 0.37
DE  Interaction: Q14050; IntAct: EBI-25367930; Score: 0.37
DE  Interaction: P52943; IntAct: EBI-25367941; Score: 0.37
DE  Interaction: O75534; IntAct: EBI-25367952; Score: 0.37
DE  Interaction: P23528; IntAct: EBI-25367886; Score: 0.37
DE  Interaction: Q9NYZ1; IntAct: EBI-25367974; Score: 0.37
DE  Interaction: P62942; IntAct: EBI-25367985; Score: 0.37
DE  Interaction: Q00688; IntAct: EBI-25367996; Score: 0.37
DE  Interaction: P49368; IntAct: EBI-25367864; Score: 0.37
DE  Interaction: Q8N111; IntAct: EBI-25367875; Score: 0.37
DE  Interaction: Q03001; IntAct: EBI-25367963; Score: 0.37
DE  Interaction: P23677; IntAct: EBI-25368128; Score: 0.37
DE  Interaction: Q7Z5L9; IntAct: EBI-25368117; Score: 0.37
DE  Interaction: Q12906; IntAct: EBI-25368106; Score: 0.37
DE  Interaction: P10809; IntAct: EBI-25368095; Score: 0.37
DE  Interaction: P38646; IntAct: EBI-25368084; Score: 0.37
DE  Interaction: P06396; IntAct: EBI-25368073; Score: 0.37
DE  Interaction: Q13491; IntAct: EBI-25368062; Score: 0.37
DE  Interaction: O76003; IntAct: EBI-25368051; Score: 0.37
DE  Interaction: P60520; IntAct: EBI-25368040; Score: 0.37
DE  Interaction: Q9H0R8; IntAct: EBI-25368029; Score: 0.37
DE  Interaction: Q14643; IntAct: EBI-25368139; Score: 0.37
DE  Interaction: O75369; IntAct: EBI-25368018; Score: 0.37
DE  Interaction: Q14318; IntAct: EBI-25368007; Score: 0.55
DE  Interaction: Q9H9V9; IntAct: EBI-25368150; Score: 0.37
DE  Interaction: Q07866; IntAct: EBI-25368172; Score: 0.37
DE  Interaction: Q8NC69; IntAct: EBI-25368161; Score: 0.37
DE  Interaction: Q9BRJ7; IntAct: EBI-25368260; Score: 0.37
DE  Interaction: Q9Y2I6; IntAct: EBI-25368249; Score: 0.37
DE  Interaction: Q643R3; IntAct: EBI-25368194; Score: 0.37
DE  Interaction: B2RTY4; IntAct: EBI-25368227; Score: 0.37
DE  Interaction: Q7L2J0; IntAct: EBI-25368216; Score: 0.37
DE  Interaction: P40925; IntAct: EBI-25368205; Score: 0.37
DE  Interaction: O00214; IntAct: EBI-25368183; Score: 0.37
DE  Interaction: Q14690; IntAct: EBI-25368293; Score: 0.37
DE  Interaction: P11940; IntAct: EBI-25368282; Score: 0.37
DE  Interaction: Q9ULJ1; IntAct: EBI-25368271; Score: 0.37
DE  Interaction: P12036; IntAct: EBI-25368238; Score: 0.37
DE  Interaction: P30086; IntAct: EBI-25368304; Score: 0.37
DE  Interaction: P18669; IntAct: EBI-25368315; Score: 0.37
DE  Interaction: Q9Y237; IntAct: EBI-25368326; Score: 0.37
DE  Interaction: Q14863; IntAct: EBI-25368337; Score: 0.37
DE  Interaction: P30044; IntAct: EBI-25368359; Score: 0.37
DE  Interaction: P25786; IntAct: EBI-25368370; Score: 0.37
DE  Interaction: P17980; IntAct: EBI-25368381; Score: 0.37
DE  Interaction: P51148; IntAct: EBI-25368392; Score: 0.37
DE  Interaction: Q8NDT2; IntAct: EBI-25368403; Score: 0.37
DE  Interaction: Q6NTF9; IntAct: EBI-25368414; Score: 0.37
DE  Interaction: Q8N4K4; IntAct: EBI-25368425; Score: 0.37
DE  Interaction: Q15181; IntAct: EBI-25368348; Score: 0.37
DE  Interaction: P31949; IntAct: EBI-25368447; Score: 0.37
DE  Interaction: Q14151; IntAct: EBI-25368458; Score: 0.37
DE  Interaction: Q9Y6D0; IntAct: EBI-25368469; Score: 0.37
DE  Interaction: O43246; IntAct: EBI-25368480; Score: 0.37
DE  Interaction: Q9NQC3; IntAct: EBI-25368436; Score: 0.37
DE  Interaction: O60641; IntAct: EBI-25368502; Score: 0.37
DE  Interaction: P10451; IntAct: EBI-25368513; Score: 0.37
DE  Interaction: P16949; IntAct: EBI-25368524; Score: 0.37
DE  Interaction: Q93045; IntAct: EBI-25368535; Score: 0.37
DE  Interaction: Q9NXE4; IntAct: EBI-25368491; Score: 0.37
DE  Interaction: Q9HCE3; IntAct: EBI-25368634; Score: 0.37
DE  Interaction: Q9ULU4; IntAct: EBI-25368623; Score: 0.37
DE  Interaction: Q96NC0; IntAct: EBI-25368612; Score: 0.37
DE  Interaction: Q8TCF1; IntAct: EBI-25368601; Score: 0.37
DE  Interaction: P19971; IntAct: EBI-25368590; Score: 0.37
DE  Interaction: P10599; IntAct: EBI-25368579; Score: 0.37
DE  Interaction: Q8WW01; IntAct: EBI-25368568; Score: 0.37
DE  Interaction: Q9H6X4; IntAct: EBI-25368557; Score: 0.37
DE  Interaction: O15061; IntAct: EBI-25368546; Score: 0.37
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q96JA1; IntAct: EBI-25424141; Score: 0.75
DE  Interaction: Q6UXM1; IntAct: EBI-25424266; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.53
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P63252; IntAct: EBI-28956128; Score: 0.27
DE  Interaction: Q9BUF5; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q58FF8; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q01813; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9NNW5; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q53GQ0; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P00367; IntAct: EBI-32718334; Score: 0.42
DE  Interaction: Q5T9A4; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P17858; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: A1L0T0; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q15293; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q96EY1; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9BSD7; IntAct: EBI-32718334; Score: 0.42
DE  Interaction: P13674; IntAct: EBI-32718334; Score: 0.42
DE  Interaction: P13667; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9H936; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P42338; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9UBS4; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9Y6K0; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9Y4W6; IntAct: EBI-32718334; Score: 0.42
DE  Interaction: O14967; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9UBX3; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q5VV42; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9H0U4; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q8IV08; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9UET6; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: O43819; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9Y4L1; IntAct: EBI-32718334; Score: 0.42
DE  Interaction: O94905; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9NXW2; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q5XKP0; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P62158; IntAct: EBI-32718334; Score: 0.42
DE  Interaction: Q9NZ01; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q04837; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q5K4L6; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q15072; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: O15269; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q13308; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P54709; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q9H3P7; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: O95487; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q14141; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q96B97; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: O95757; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: O75410; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P05198; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q15437; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P35241; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q13643; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q92599; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q9NSK0; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: O60282; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P16333; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q12774; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P63244; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q96JB5; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: O95486; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q13586; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P43034; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P18085; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P51648; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q9GZT9; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q9UKD2; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q93008; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P09543; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q96PK6; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q5JRA6; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q8N1F7; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P51659; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: O95433; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q9Y5M8; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q15717; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q96S66; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q9H939; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P61088; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q92974; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q5VUB5; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: O94979; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q9H9A6; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: O14745; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q13541; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q14126; IntAct: EBI-34582386; Score: 0.40
GO  GO:0016324;
GO  GO:0009925;
GO  GO:0016323;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0010008;
GO  GO:0038143;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0043209;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0043235;
GO  GO:0044214;
GO  GO:0005524;
GO  GO:0043125;
GO  GO:0042802;
GO  GO:0008022;
GO  GO:0046982;
GO  GO:0019903;
GO  GO:0004713;
GO  GO:0001042;
GO  GO:0004714;
GO  GO:0004888;
GO  GO:0007166;
GO  GO:0071364;
GO  GO:0071363;
GO  GO:0007167;
GO  GO:0038134;
GO  GO:0038133;
GO  GO:0038135;
GO  GO:0007507;
GO  GO:0033080;
GO  GO:0035556;
GO  GO:0008045;
GO  GO:0042552;
GO  GO:0033088;
GO  GO:0007528;
GO  GO:0030182;
GO  GO:0048709;
GO  GO:0018108;
GO  GO:0007422;
GO  GO:0014065;
GO  GO:0045785;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0050679;
GO  GO:0043547;
GO  GO:0033674;
GO  GO:0043406;
GO  GO:0043410;
GO  GO:0001934;
GO  GO:0090314;
GO  GO:0045943;
GO  GO:0045727;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0045765;
GO  GO:0070372;
GO  GO:0032886;
GO  GO:0007165;
GO  GO:0007169;
GO  GO:0042060;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEV
SQ  QGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQ
SQ  LCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQC
SQ  AAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQ
SQ  EVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVF
SQ  ETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTV
SQ  PWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHC
SQ  LPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDK
SQ  GCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETEL
SQ  RKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQL
SQ  MPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHAD
SQ  GGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWM
SQ  IDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAG
SQ  GMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPL
SQ  PSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQ
SQ  GGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV
//
ID  Q60553;
PN  Receptor tyrosine-protein kinase erbB-2;
GN  ERBB2;
OS  10036;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Early endosome {ECO:0000250|UniProtKB:P04626}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P04626}. Nucleus {ECO:0000250|UniProtKB:P04626}. Note=Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in endosome-to-TGN retrograde vesicles. Internalized from the cell membrane in response to EGF stimulation. {ECO:0000250|UniProtKB:P04626}.
DR  UNIPROT: Q60553;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF07714;
DR  Pfam: PF01030;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). {ECO:0000250}. In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005769;
GO  GO:0016021;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098590;
GO  GO:0005524;
GO  GO:0001042;
GO  GO:0004714;
GO  GO:0048513;
GO  GO:0071364;
GO  GO:0071363;
GO  GO:0007417;
GO  GO:0035556;
GO  GO:0030307;
GO  GO:0090314;
GO  GO:0045943;
GO  GO:0045727;
GO  GO:0042127;
GO  GO:0070372;
GO  GO:0032886;
GO  GO:0007169;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELAAWCGWGLLLALLSPGASGTQVCTGTDMKLRLPASPETHLDIVRHLYQGCQVVQGNLELTYLPANATLSFLQDIQEV
SQ  QGYMLIAHSQVRHVPLQRLRIVRGTQLFEDKYALAVLDNRDPLDNVTTATGRTPEGLRELQLRSLTEILKGGVLIRGNPQ
SQ  LCYQDTVLWKDVFRKNNQLAPVDIDTNRSRACPPCAPACKDNHCWGASPEDCQTLTGTIAPRAVPAARARLPTDCCHEQC
SQ  AAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTTCPYNYLSTEVGSCTLVCPLNNQ
SQ  EVTAEDGTQRCEKCSKSCARVCYGLGMEHLRGARAITSANIQEFAGCKKIFGSLAFLPESFDGNPSSGIAPLTPEQLQVF
SQ  ETLEEITGYLYISAWPDSLHDLSVFQNLRVIRGRVLHDGAYSLALQGLGIRWLGLRSLRELGSGLVLIHRNTHLCFVHTV
SQ  PWDQLFRNPHQALLHSGNPSEEECGLKDFACYPLCAHGHCWGPGPTQCVNCSHFLRGQECVKECRVWKGLPREYVNGKHC
SQ  LPCHPECQPQNSTETCTGSEADQCTACPHYKDSPFCVARCPSGVKPDLSYMPIWKYPDEEGMCQPCPINCTHSCVDLDER
SQ  GCPAEQRASPATSIIATVVGILLFLVIGVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETEL
SQ  RKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGLGSPYVSRLLGICLTSTVQLVTQL
SQ  MPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHAD
SQ  GGKVPIKWIALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWM
SQ  IDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFFPDPAPGAG
SQ  STAHRRHRSSSTRSGGGELTLGMEPSGEEPPRSPLAPSEGAGSDVFEGELGMGATKGPQSISPRDLSPLQRYSEDPTLPL
SQ  PTETDGYVAPLACSPQPEYVNQPEVRPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFTFGGAVENPEYLVPR
SQ  GGSASQPHPPALCPAFDNLYYWDQDPSERGSPPNTFEGTPTAENPEYLGLDVPV
//
ID  P70424;
PN  Receptor tyrosine-protein kinase erbB-2;
GN  Erbb2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Early endosome {ECO:0000250|UniProtKB:P04626}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P04626}. Nucleus {ECO:0000250|UniProtKB:P04626}. Note=Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in endosome-to-TGN retrograde vesicles. Internalized from the cell membrane in response to EGF stimulation. {ECO:0000250|UniProtKB:P04626}.
DR  UNIPROT: P70424;
DR  UNIPROT: Q61525;
DR  UNIPROT: Q6ZPE0;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF07714;
DR  Pfam: PF01030;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). {ECO:0000250}. In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P12931; IntAct: EBI-5451946; Score: 0.40
DE  Interaction: Q80TH2; IntAct: EBI-7320494; Score: 0.67
DE  Interaction: Q61526; IntAct: EBI-2945516; Score: 0.40
DE  Interaction: P98172; IntAct: EBI-5451919; Score: 0.46
DE  Interaction: P42227; IntAct: EBI-6255143; Score: 0.54
DE  Interaction: Q60748; IntAct: EBI-15606164; Score: 0.40
DE  Interaction: P18762; IntAct: EBI-15606183; Score: 0.52
GO  GO:0016324;
GO  GO:0009925;
GO  GO:0016323;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0010008;
GO  GO:0038143;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0043219;
GO  GO:0045121;
GO  GO:0005902;
GO  GO:0043209;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045211;
GO  GO:0043235;
GO  GO:0044214;
GO  GO:0005524;
GO  GO:0043125;
GO  GO:0019838;
GO  GO:0051879;
GO  GO:0042802;
GO  GO:0008022;
GO  GO:0046982;
GO  GO:0019903;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0001042;
GO  GO:0004714;
GO  GO:0004888;
GO  GO:0031625;
GO  GO:0007166;
GO  GO:0071364;
GO  GO:0071363;
GO  GO:0038134;
GO  GO:0038133;
GO  GO:0038135;
GO  GO:0044849;
GO  GO:0010001;
GO  GO:0007507;
GO  GO:0033080;
GO  GO:0035556;
GO  GO:0008045;
GO  GO:0042552;
GO  GO:0043066;
GO  GO:0033088;
GO  GO:0007399;
GO  GO:0007528;
GO  GO:0030182;
GO  GO:0048709;
GO  GO:0018108;
GO  GO:0007422;
GO  GO:0014065;
GO  GO:0045785;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0050679;
GO  GO:0010628;
GO  GO:0043547;
GO  GO:0033674;
GO  GO:0043406;
GO  GO:0043410;
GO  GO:0014068;
GO  GO:0001934;
GO  GO:0090314;
GO  GO:0046579;
GO  GO:0045943;
GO  GO:0045727;
GO  GO:0046777;
GO  GO:0070372;
GO  GO:0032886;
GO  GO:0048678;
GO  GO:0007165;
GO  GO:0048485;
GO  GO:0007169;
GO  GO:0042060;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELAAWCRWGFLLALLSPGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPANASLSFLQDIQEV
SQ  QGYMLIAHNRVKHVPLQRLRIVRGTQLFEDKYALAVLDNRDPLDNVTTAAPGRTPEGLRELQLRSLTEILKGGVLIRGNP
SQ  QLCYQDMVLWKDVLRKNNQLAPVDMDTNRSRACPPCAPTCKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ
SQ  CAAGCTGPKHSDCLACLHFNHSGICELHCPALITYNTDTFESMLNPEGRYTFGASCVTTCPYNYLSTEVGSCTLVCPPNN
SQ  QEVTAEDGTQRCEKCSKPCAGVCYGLGMEHLRGARAITSDNIQEFAGCKKIFGSLAFLPESFDGNPSSGVAPLKPEHLQV
SQ  FETLEEITGYLYISAWPESFQDLSVFQNLRVIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNTHLCFVNT
SQ  VPWDQLFRNPHQALLHSGNRPEEACGLEGLVCNSLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVWKGLPREYVRGKH
SQ  CLPCHPECQPQNSSETCYGSEADQCEACAHYKDSSSCVARCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDE
SQ  RGCPAEQRASPVTFIIATVVGVLLFLIIVVVIGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAVPNQAQMRILKETE
SQ  LRKLKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQ
SQ  LMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHA
SQ  DGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCW
SQ  MIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGELVDAEEYLVPQQGFFSPDPALGT
SQ  GSTAHRRHRSSSARSGGGELTLGLEPSEEEPPRSPLAPSEGAGSDVFDGDLAVGVTKGLQSLSPHDLSPLQRYSEDPTLP
SQ  LPPETDGYVAPLACSPQPEYVNQPEVRPQSPLTPEGPPPPIRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLAP
SQ  RAGTASQPHPSPAFSPAFDNLYYWDQNSSEQGPPPSTFEGTPTAENPEYLGLDVPV
//
ID  P06494;
PN  Receptor tyrosine-protein kinase erbB-2;
GN  Erbb2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Early endosome {ECO:0000250|UniProtKB:P04626}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P04626}. Nucleus {ECO:0000250|UniProtKB:P04626}. Note=Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in endosome-to-TGN retrograde vesicles. Internalized from the cell membrane in response to EGF stimulation. {ECO:0000250|UniProtKB:P04626}.
DR  UNIPROT: P06494;
DR  UNIPROT: Q6P732;
DR  PDB: 1IIJ;
DR  PDB: 1N8Y;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF07714;
DR  Pfam: PF01030;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Interacts (preferentially with the tyrosine phosphorylated form) with CPNE3; this interaction occurs at the cell membrane and is increased in a growth factor heregulin-dependent manner (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04626}. In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0009925;
GO  GO:0016323;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005769;
GO  GO:0010008;
GO  GO:0038143;
GO  GO:0005887;
GO  GO:0043219;
GO  GO:0045121;
GO  GO:0005902;
GO  GO:0043209;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045211;
GO  GO:0043235;
GO  GO:0044214;
GO  GO:0005524;
GO  GO:0060724;
GO  GO:0003677;
GO  GO:0043125;
GO  GO:0051879;
GO  GO:0042802;
GO  GO:0008022;
GO  GO:0046982;
GO  GO:0019903;
GO  GO:0030296;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0001042;
GO  GO:0030297;
GO  GO:0004714;
GO  GO:0004888;
GO  GO:0031625;
GO  GO:0007166;
GO  GO:0071364;
GO  GO:0071363;
GO  GO:0007417;
GO  GO:0038134;
GO  GO:0038133;
GO  GO:0038135;
GO  GO:0044849;
GO  GO:0010001;
GO  GO:0007507;
GO  GO:0033080;
GO  GO:0035556;
GO  GO:0001889;
GO  GO:0060056;
GO  GO:0008045;
GO  GO:0042552;
GO  GO:0043066;
GO  GO:0033088;
GO  GO:0007399;
GO  GO:0007528;
GO  GO:0030182;
GO  GO:0048709;
GO  GO:0018108;
GO  GO:0007422;
GO  GO:0014065;
GO  GO:0045785;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0050679;
GO  GO:0010628;
GO  GO:0043547;
GO  GO:0033674;
GO  GO:0043406;
GO  GO:0043410;
GO  GO:0014068;
GO  GO:0001934;
GO  GO:0090314;
GO  GO:0046579;
GO  GO:0045943;
GO  GO:0045727;
GO  GO:0046777;
GO  GO:0045595;
GO  GO:0042127;
GO  GO:0070372;
GO  GO:0032886;
GO  GO:0048678;
GO  GO:0032570;
GO  GO:0009410;
GO  GO:0007165;
GO  GO:0007519;
GO  GO:0048485;
GO  GO:0043586;
GO  GO:0007169;
GO  GO:0042060;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYVPANASLSFLQDIQEV
SQ  QGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNRDPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNP
SQ  QLCYQDMVLWKDVFRKNNQLAPVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ
SQ  CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTCPYNYLSTEVGSCTLVCPPNN
SQ  QEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSDNVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQV
SQ  FETLEEITGYLYISAWPDSLRDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT
SQ  VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQECVEECRVWKGLPREYVSDK
SQ  RCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVARCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLD
SQ  ERGCPAEQRASPVTFIIATVVGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET
SQ  ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVT
SQ  QLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYH
SQ  ADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC
SQ  WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFSPDPTPG
SQ  TGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPSEGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTL
SQ  PLPPETDGYVAPLACSPQPEYVNQSEVQPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLV
SQ  PREGTASPPHPSPAFSPAFDNLYYWDQNSSEQGPPPSNFEGTPTAENPEYLGLDVPV
//
ID  Q96RT1;
PN  Erbin;
GN  ERBIN;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell junction, hemidesmosome {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:11375975}. Nucleus membrane {ECO:0000250}. Basolateral cell membrane {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which are cell-substrate adhesion complexes in stratified epithelia. In transfected cells, either diffusely distributed over the cytoplasm or concentrated at the basolateral membrane. Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: Q96RT1;
DR  UNIPROT: A0AVR1;
DR  UNIPROT: B4E3F1;
DR  UNIPROT: B7ZLV9;
DR  UNIPROT: E7EQW9;
DR  UNIPROT: E9PCR8;
DR  UNIPROT: Q1RMD0;
DR  UNIPROT: Q86W38;
DR  UNIPROT: Q9NR18;
DR  UNIPROT: Q9NW48;
DR  UNIPROT: Q9ULJ5;
DR  PDB: 1MFG;
DR  PDB: 1MFL;
DR  PDB: 1N7T;
DR  PDB: 2H3L;
DR  PDB: 2QBW;
DR  PDB: 3CH8;
DR  PDB: 6Q0M;
DR  PDB: 6Q0N;
DR  PDB: 6Q0U;
DR  PDB: 6UBH;
DR  PDB: 7LUL;
DR  Pfam: PF13855;
DR  Pfam: PF00595;
DR  PROSITE: PS51450;
DR  PROSITE: PS50106;
DR  OMIM: 606944;
DR  DisGeNET: 55914;
DE  Function: Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion (PubMed:16203728). {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:16203728}.
DE  Reference Proteome: Yes;
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q16620; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q5XI72; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q6AXS5; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: O95405; IntAct: EBI-7255424; Score: 0.37
DE  Interaction: Q99569; IntAct: EBI-8449263; Score: 0.63
DE  Interaction: P35222; IntAct: EBI-8449492; Score: 0.27
DE  Interaction: Q9UQ13; IntAct: EBI-993893; Score: 0.62
DE  Interaction: Q15796; IntAct: EBI-2695978; Score: 0.40
DE  Interaction: P84022; IntAct: EBI-2696171; Score: 0.40
DE  Interaction: Q5NID9; IntAct: EBI-2805400; Score: 0.00
DE  Interaction: Q8CZZ5; IntAct: EBI-2841600; Score: 0.00
DE  Interaction: Q8CZQ2; IntAct: EBI-2865700; Score: 0.00
DE  Interaction: P25054; IntAct: EBI-3436880; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-3893063; Score: 0.35
DE  Interaction: P25791; IntAct: EBI-3939532; Score: 0.37
DE  Interaction: P40763; IntAct: EBI-3940529; Score: 0.37
DE  Interaction: B1AYL1; IntAct: EBI-8068438; Score: 0.44
DE  Interaction: P36873; IntAct: EBI-6911905; Score: 0.57
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: A2AUM9; IntAct: EBI-10994361; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: Q8C767; IntAct: EBI-11064501; Score: 0.35
DE  Interaction: Q5HZK1; IntAct: EBI-11074242; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079358; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: Q8BGH2; IntAct: EBI-11097023; Score: 0.35
DE  Interaction: P53667; IntAct: EBI-11101207; Score: 0.35
DE  Interaction: P09803; IntAct: EBI-11106849; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11390509; Score: 0.27
DE  Interaction: Q9HC29; IntAct: EBI-11420226; Score: 0.66
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-11519918; Score: 0.37
DE  Interaction: Q2PJP0; IntAct: EBI-11520503; Score: 0.37
DE  Interaction: Q6DP93; IntAct: EBI-11520678; Score: 0.37
DE  Interaction: P03508; IntAct: EBI-11520965; Score: 0.37
DE  Interaction: Q20MH4; IntAct: EBI-11521170; Score: 0.37
DE  Interaction: Q9UQB3; IntAct: EBI-11793333; Score: 0.40
DE  Interaction: O00192; IntAct: EBI-11793379; Score: 0.40
DE  Interaction: Q9BY21; IntAct: EBI-11793409; Score: 0.40
DE  Interaction: Q96DL1; IntAct: EBI-11793419; Score: 0.40
DE  Interaction: Q8NHY3; IntAct: EBI-11793429; Score: 0.40
DE  Interaction: A3EX99; IntAct: EBI-11794147; Score: 0.40
DE  Interaction: A3EXD5; IntAct: EBI-11794185; Score: 0.40
DE  Interaction: P06427; IntAct: EBI-11794195; Score: 0.40
DE  Interaction: Q9IDV3; IntAct: EBI-11794220; Score: 0.40
DE  Interaction: Q1A244; IntAct: EBI-11794243; Score: 0.40
DE  Interaction: P03126; IntAct: EBI-11794253; Score: 0.40
DE  Interaction: P50804; IntAct: EBI-11794263; Score: 0.40
DE  Interaction: P0C9G5; IntAct: EBI-11794280; Score: 0.40
DE  Interaction: A3EXD4; IntAct: EBI-11794297; Score: 0.40
DE  Interaction: P89432; IntAct: EBI-11794318; Score: 0.40
DE  Interaction: P0C213; IntAct: EBI-11794328; Score: 0.40
DE  Interaction: Q18LE1; IntAct: EBI-11794586; Score: 0.40
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: P62136; IntAct: EBI-14025896; Score: 0.42
DE  Interaction: Q96H86; IntAct: EBI-21521634; Score: 0.35
DE  Interaction: Q7Z398; IntAct: EBI-21528160; Score: 0.35
DE  Interaction: A8K8V0; IntAct: EBI-21612043; Score: 0.35
DE  Interaction: P09017; IntAct: EBI-21634836; Score: 0.35
DE  Interaction: Q8IZ69; IntAct: EBI-21636338; Score: 0.35
DE  Interaction: Q8WV44; IntAct: EBI-21636495; Score: 0.35
DE  Interaction: Q96IQ9; IntAct: EBI-21636586; Score: 0.35
DE  Interaction: Q9H9D4; IntAct: EBI-21642543; Score: 0.35
DE  Interaction: O43296; IntAct: EBI-21725229; Score: 0.35
DE  Interaction: Q49MI3; IntAct: EBI-21731388; Score: 0.35
DE  Interaction: P43235; IntAct: EBI-21781359; Score: 0.35
DE  Interaction: Q8TA94; IntAct: EBI-21783979; Score: 0.35
DE  Interaction: Q9NY56; IntAct: EBI-21795463; Score: 0.35
DE  Interaction: Q6ZMY9; IntAct: EBI-21818150; Score: 0.35
DE  Interaction: P20160; IntAct: EBI-21867396; Score: 0.35
DE  Interaction: Q14CB8; IntAct: EBI-21871748; Score: 0.35
DE  Interaction: Q9P0T4; IntAct: EBI-21882203; Score: 0.35
DE  Interaction: P15311; IntAct: EBI-16791848; Score: 0.27
DE  Interaction: P49841; IntAct: EBI-16793176; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16795491; Score: 0.27
DE  Interaction: Q9NPJ6; IntAct: EBI-25472202; Score: 0.27
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q2LC84; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q04970; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P60868; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: A0A0G2K8Z9; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: G3V7V7; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: D4A9L2; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: A0A0G2K654; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q27W01; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: B2RYP6; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: G3V6S1; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P62890; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P35427; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q8K1Q0; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: B5DFM8; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q6AYK8; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q4V8C8; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q920F5; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: D4A3K5; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: E9PT65; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P62850; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: G3V9L1; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: M0R6J0; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P62278; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q6IMY8; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q62780; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P24368; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: A0A0G2K719; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q7TT49; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P09875; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P09895; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P62893; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q9R0T3; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: A0A0G2JW88; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: M0R9L3; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q5RK00; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: E9PU01; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q3KRF2; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: F1M124; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: D3ZZT9; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q9JJ31; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q63186; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P17078; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P13471; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: F1MAF2; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q6AYE2; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: D4AD15; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P50904; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: B2GV09; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P05197; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: G3V9N7; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q9Z1W6; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P62961; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: A0A096MK30; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: D4A4R1; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P30009; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q5M7V8; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P47198; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P31000; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P61314; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: D3Z898; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q5U2Q7; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q5XIM5; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P13086; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: Q5M963; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P81795; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: M0R9T2; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P41743; IntAct: EBI-25380638; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: K9N5R3; IntAct: EBI-26973414; Score: 0.40
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: P13569; IntAct: EBI-27087549; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952324; Score: 0.27
DE  Interaction: Q13886; IntAct: EBI-29000705; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-32717503; Score: 0.35
DE  Interaction: P29317; IntAct: EBI-32720711; Score: 0.27
DE  Interaction: P29320; IntAct: EBI-32720767; Score: 0.27
DE  Interaction: P54764; IntAct: EBI-32720816; Score: 0.27
DE  Interaction: P54756; IntAct: EBI-32720907; Score: 0.27
DE  Interaction: Q15375; IntAct: EBI-32721052; Score: 0.27
DE  Interaction: P21802; IntAct: EBI-32721907; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: Q06124; IntAct: EBI-32723738; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: P16234; IntAct: EBI-32724889; Score: 0.27
DE  Interaction: Q01973; IntAct: EBI-32725295; Score: 0.27
DE  Interaction: Q6J9G0; IntAct: EBI-32731895; Score: 0.27
DE  Interaction: P12830; IntAct: EBI-34580821; Score: 0.35
GO  GO:0009925;
GO  GO:0005604;
GO  GO:0016323;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0098978;
GO  GO:0030056;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0005176;
GO  GO:0005102;
GO  GO:0005200;
GO  GO:0045175;
GO  GO:0007155;
GO  GO:0071356;
GO  GO:0007173;
GO  GO:0045197;
GO  GO:0007229;
GO  GO:0045104;
GO  GO:0071638;
GO  GO:0032088;
GO  GO:0070433;
GO  GO:0046579;
GO  GO:0006605;
GO  GO:0099072;
GO  GO:0032496;
GO  GO:0032495;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTKRSLFVRLVPCRCLRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDND
SQ  LTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRL
SQ  TKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLKEFWMDANRLTFIPGFIGSLKQLTYLDVSKN
SQ  NIEMVEEGISTCENLQDLLLSSNSLQQLPETIGSLKNITTLKIDENQLMYLPDSIGGLISVEELDCSFNEVEALPSSIGQ
SQ  LTNLRTFAADHNYLQQLPPEIGSWKNITVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSD
SQ  NQSKPLIPLQKETDSETQKMVLTNYMFPQQPRTEDVMFISDNESFNPSLWEEQRKQRAQVAFECDEDKDEREAPPREGNL
SQ  KRYPTPYPDELKNMVKTVQTIVHRLKDEETNEDSGRDLKPHEDQQDINKDVGVKTSESTTTVKSKVDEREKYMIGNSVQK
SQ  ISEPEAEISPGSLPVTANMKASENLKHIVNHDDVFEESEELSSDEEMKMAEMRPPLIETSINQPKVVALSNNKKDDTKET
SQ  DSLSDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTSLCSPVKQTHIDINSKIRQEDENFNSLLQNGDILNSSTEEKF
SQ  KAHDKKDFNLPEYDLNVEERLVLIEKSVDSTATADDTHKLDHINMNLNKLITNDTFQPEIMERSKTQDIVLGTSFLSINS
SQ  KEETEHLENGNKYPNLESVNKVNGHSEETSQSPNRTEPHDSDCSVDLGISKSTEDLSPQKSGPVGSVVKSHSITNMEIGG
SQ  LKIYDILSDNGPQQPSTTVKITSAVDGKNIVRSKSATLLYDQPLQVFTGSSSSSDLISGTKAIFKFDSNHNPEEPNIIRG
SQ  PTSGPQSAPQIYGPPQYNIQYSSSAAVKDTLWHSKQNPQIDHASFPPQLLPRSESTENQSYAKHSANMNFSNHNNVRANT
SQ  AYHLHQRLGPARHGEMWAISPNDRLIPAVTRSTIQRQSSVSSTASVNLGDPGSTRRAQIPEGDYLSYREFHSAGRTPPMM
SQ  PGSQRPLSARTYSIDGPNASRPQSARPSINEIPERTMSVSDFNYSRTSPSKRPNARVGSEHSLLDPPGKSKVPRDWREQV
SQ  LRHIEAKKLEKKHPQTSSSGDPCQDGIFISGQQNYSSATLSHKDVPPDSLMKMPLSNGQMGQPLRPQANYSQIHHPPQAS
SQ  VARHPSREQLIDYLMLKVAHQPPYTQPHCSPRQGHELAKQEIRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQ
SQ  PEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVREVSS
//
ID  Q80TH2;
PN  Erbin;
GN  Erbin;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell junction, hemidesmosome {ECO:0000250|UniProtKB:Q96RT1}. Nucleus membrane {ECO:0000269|PubMed:18802028}. Basolateral cell membrane {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which are cell-substrate adhesion complexes in stratified epithelia. In transfected cells, either diffusely distributed over the cytoplasm or concentrated at the basolateral membrane (By similarity). Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q96RT1}.
DR  UNIPROT: Q80TH2;
DR  UNIPROT: E9QND6;
DR  UNIPROT: Q8BQ14;
DR  UNIPROT: Q8CE41;
DR  UNIPROT: Q8K171;
DR  UNIPROT: Q99JU3;
DR  UNIPROT: Q9JI47;
DR  Pfam: PF13855;
DR  Pfam: PF00595;
DR  PROSITE: PS51450;
DR  PROSITE: PS50106;
DE  Function: Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated ERBB2 'Tyr-1248' receptor, it may contribute to stabilize this unphosphorylated state (By similarity). Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory cytokine secretion (PubMed:16203728). {ECO:0000250|UniProtKB:Q96RT1, ECO:0000269|PubMed:16203728}.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-7806162; Score: 0.37
DE  Interaction: P70424; IntAct: EBI-7320494; Score: 0.67
DE  Interaction: Q8BUN5; IntAct: EBI-8626978; Score: 0.40
DE  Interaction: Q62432; IntAct: EBI-8627018; Score: 0.44
DE  Interaction: P70340; IntAct: EBI-8627088; Score: 0.44
DE  Interaction: P97471; IntAct: EBI-8627224; Score: 0.44
DE  Interaction: O35253; IntAct: EBI-8627324; Score: 0.44
DE  Interaction: P84022; IntAct: EBI-8627354; Score: 0.37
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0016323;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0098978;
GO  GO:0030056;
GO  GO:0031594;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0099572;
GO  GO:0005176;
GO  GO:0005102;
GO  GO:0071356;
GO  GO:0071638;
GO  GO:0032088;
GO  GO:0070433;
GO  GO:0046579;
GO  GO:0006605;
GO  GO:0099072;
GO  GO:0032496;
GO  GO:0032495;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTKRSLFVRLVPCRCLRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDND
SQ  LTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRL
SQ  TKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLREFWMDGNRLTFIPGFIGSLRQLTYLDVSKN
SQ  NIEMVEEGISTCENLQDFLLSSNSLQQLPETIGSLKNVTTLKIDENQLMYLPDSIGGLRSIEELDCSFNEIEALPSSIGQ
SQ  LTNMRTFAADHNYLQQLPPEIGNWKNITVLFLHCNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSD
SQ  NQSKPLIPLQKETDTETQKMVLTNYMFPQQPRTEDVMFISDNESFNPALWEEQRKQRAQVAFECDEDKDEREAPPREGNL
SQ  KRYPTPYPDELKNMVKTVQTIVHRLKDEETNEESGRDLKQHEDQQVVNKDKCVKTSESTTTKSKLDEREKYMNSVQKMSE
SQ  PEAETNGGNLPVTASMKLSGNLKHIVNHDDVFEESEELSSDEEMKMAEMRPPLIESSINQPKVVALSNNKKDDAKDADSL
SQ  SDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTSLCSPVKQTPVDSNSKVRQEDENFNSLLQNGVNLNNSPEEKFKIN
SQ  DKKDFKLPEYDLNIEEQLVLIEKDIDSKATSDDSRQLDHINMNINKLVTNNIFQPEVMERSKMQDIVLGTGFLSIHPKNE
SQ  AEHIENGAKFPNLESINKVNGLCEDTAPSPGRVEPQKASSSADVGISKSTEDLSPQRSGPTGAVVKSHSITNMETGGLKI
SQ  YDILGDDGPQPPSAAVKIASAVDGKNIVRSKSATLLYDQPLQVFTAASSSSELLSGTKAVFKFDSNHNPEEPDIIRAATV
SQ  SGPQSTPHLYGPPQYNVQYSGSATVKDTLWHPKQNPQIDPVSFPPQRLPRSESAENHSYAKHSANMNFSNHNNVRANTGY
SQ  HLQQRLAPARHGEMWAISPNDRLVPAVTRTTIQRQSSVSSTASVNLGDPTRRTEGDYLSYRELHSMGRTPVMSGSQRPLS
SQ  ARAYSIDGPNTSRPQSARPSINEIPERTMSVSDFNYSRTSPSKRPNTRVGSEHSLLDPPGKSKVPHDWREQVLRHIEAKK
SQ  LEKHPQTSSPGECCQDDRFMSEEQNHPSGALSHRGLPDSLMKMPLSNGQMGQPLRPQAHYSQTHHPPQASVARHPSREQL
SQ  IDYLMLKVAHQPPYTHPHCSPRQGHELAKQEIRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQ
SQ  PGDKIIQANGYSFINIEHGQAVSLLKTFHNAVDLIIVREVSS
//
ID  Q20057;
PN  Enhancer of rudimentary homolog 2;
GN  erh;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Nucleus {ECO:0000269|PubMed:31216475}. Note=Dispersedly distributes throughout the cytoplasm in early embryos (PubMed:31147388). During early embryogenesis, localizes to the nucleus at prophase of cell division, and remains in the cytosol at interphase in 2- and 4-cell embryos (PubMed:31216475). Localizes to puncta in the perinuclear region in the germline syncytium (PubMed:31216475, PubMed:31147388). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
DR  UNIPROT: Q20057;
DR  PDB: 7EJO;
DR  PDB: 7EJS;
DR  PDB: 7O6L;
DR  PDB: 7O6N;
DR  Pfam: PF01133;
DE  Function: Required for chromosome segregation and cell division in early embryos (PubMed:31216475). Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Within the tost-1 variant of the PETISCO complex binds to splice leader SL1 RNA fragments to possibly play a role in their processing (PubMed:31147388). Promotes the biogenesis of 21U-RNAs (PubMed:31216475). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475, ECO:0000305|PubMed:31216475}.
DE  Reference Proteome: Yes;
DE  Interaction: O61955; IntAct: EBI-21449069; Score: 0.35
DE  Interaction: O76616; IntAct: EBI-21449031; Score: 0.48
DE  Interaction: Q09293; IntAct: EBI-21449069; Score: 0.35
DE  Interaction: Q19541; IntAct: EBI-21448974; Score: 0.55
DE  Interaction: Q17698; IntAct: EBI-21449069; Score: 0.35
DE  Interaction: Q8T3B7; IntAct: EBI-21449069; Score: 0.35
DE  Interaction: Q9BL06; IntAct: EBI-21449069; Score: 0.35
DE  Interaction: Q20140; IntAct: EBI-21449069; Score: 0.35
DE  Interaction: Q20848; IntAct: EBI-21449069; Score: 0.35
DE  Interaction: Q22537; IntAct: EBI-21449069; Score: 0.35
DE  Interaction: Q18490; IntAct: EBI-21449069; Score: 0.48
DE  Interaction: Q20057; IntAct: EBI-21449848; Score: 0.37
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0034518;
GO  GO:0034585;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0009792;
GO  GO:0031047;
GO  GO:1990511;
GO  GO:0051781;
GO  GO:0051984;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTSSHTVLLIQTSPRLDSRTWGDYESVTDALDALCKMFEDFLSKKSAAPVTYDVSQVYEFLDKLSDVSMMIFNRETGQY
SQ  IGRTRAWIKQQVYEMMRGRCQHPEGGEKVIVGY
//
ID  Q94F30;
PN  Ubiquitin-like-specific protease ESD4;
GN  ESD4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:14507998, ECO:0000269|PubMed:17513499}; Peripheral membrane protein {ECO:0000269|PubMed:14507998, ECO:0000269|PubMed:17513499}. Note=The nuclear envelope localization is independent of the presence of the nuclear pore anchor NUA.
DR  UNIPROT: Q94F30;
DR  UNIPROT: B9DFG4;
DR  UNIPROT: O23439;
DR  UNIPROT: Q70G10;
DR  UNIPROT: Q7DLT0;
DR  Pfam: PF02902;
DR  PROSITE: PS50600;
DE  Function: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMOs to their mature forms and deconjugation of SUMO from targeted proteins. Cleaves precursors of SUM1 and SUM2, but not of SUM3 or SUM5. Able to release SUM1 and SUM2 from conjugates, but unable to cleave SUM3. Acts predominantly as an isopeptidase, cleaving SUMO-conjugated proteins better than SUMO peptides. Plays an important role in the control of flowering time. {ECO:0000269|PubMed:14507998, ECO:0000269|PubMed:16740136}.
DE  Reference Proteome: Yes;
DE  Interaction: A4GSN8; IntAct: EBI-1545682; Score: 0.37
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0016929;
GO  GO:0019900;
GO  GO:0070139;
GO  GO:0009911;
GO  GO:0016926;
GO  GO:0009909;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MGAVAINRKRSDESFNFINQQSTNPLRNSPYFQASKKRRFSFAMSEDSGKPASSNPTISRISRYPDAKAPLRREIHAPSR
SQ  GILRYGKAKSNDYCEKDANFFVRKYDDAKRSALEALRFVNKGKDFVDLGDEVEKEEVVSDDSSVQAIEVIDCDDDEEKKN
SQ  LQPSFSSGVTDVKKGENFRVEDTSMMLDSLSLDRDVDNDASSLEAYRKLMQSAEKRNSKLEALGFEIVLNEKKLSLLRQS
SQ  RPKTVEKRVEVPREPFIPLTEDEEAEVYRAFSGRNRRKVLATHENSNIDITGEVLQCLTPSAWLNDEVINVYLELLKERE
SQ  TREPKKYLKCHYFNTFFYKKLVSDSGYNFKAVRRWTTQRKLGYALIDCDMIFVPIHRGVHWTLAVINNRESKLLYLDSLN
SQ  GVDPMILNALAKYMGDEANEKSGKKIDANSWDMEFVEDLPQQKNGYDCGMFMLKYIDFFSRGLGLCFSQEHMPYFRLRTA
SQ  KEILRLRAD
//
ID  Q9LTB0;
PN  Exocyst complex component EXO84B;
GN  EXO84B;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:19895414}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19895414}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:20870962}. Secreted, cell wall {ECO:0000269|PubMed:20870962}. Cell membrane {ECO:0000269|PubMed:27803190}. Note=Localized to globular structures in the perinuclear region (PubMed:19895414). During cytokinesis, localizes to the nascent cell plate and later to the cell plate insertion site and along the post-cytokinetic wall (PubMed:20870962). Polarized localization at the outermost side of root epidermal and cap cells, in the outer lateral membrane domain facing the environment (PubMed:27803190). {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:27803190}.
DR  UNIPROT: Q9LTB0;
DR  Pfam: PF16528;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. Probable component of an exocyst subcomplex specifically involved in autophagy-related, Golgi-independent membrane traffic to the vacuole. Regulates autophagosome formation and autophagy-related Golgi- independent import into the vacuole. Mediates ABCG36/PEN3 outer- membrane polarity at the periphery of lateral root cap and root epidermal cells (PubMed:27803190). {ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:23944713, ECO:0000269|PubMed:27803190}.
DE  Reference Proteome: Yes;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0000145;
GO  GO:0005576;
GO  GO:0048471;
GO  GO:0009524;
GO  GO:0005886;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0008104;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAKTARSKATPTKENGVRVEEGLSLFKSDKFDADAYVQSKCSINEKDIKQLCSYLLDLKRASAEEMRRSVYANYPAFIR
SQ  TSKEISDLEGELSSIRNLLSTQATLIHGLADGVNIDDDKVSDESLANGLLNFEDNGLSDLEKWATEFPDHLDALLAERRV
SQ  DEALAAFDEGEILVSQANEKHTLSSSVLSSLQFAIAERKQKLADQLAKAACQPSTRGGELRSAIAALKRLGDGPRAHTVL
SQ  LDAHFQRYQYNMQSLRPSSTSYGGAYTAALSQLVFSAISQASSDSLGIFGKEPAYSSELVTWATKQTEAFSLLVKRHALA
SQ  SSAAAGGLRAAAECAQIALGHCSLLEARGLSLCPVLLKHFKPIVEQALEANLKRIEENTAAMAAADDWVLTSPPAGSRHA
SQ  STAFQNKLTSSAHRFNLMVQDFFEDVGPLLSMQLGSKALEGLFRVFNSYVDVLVRALPGSIEEEDPNFESSCNKIVQMAE
SQ  TEANQLALLANASLLADELLPRAAMKLSLDQTGQRTDDLRRPLDRQNRNPEQREWKRRLLSTVDKLKDAFCRQHALDLIF
SQ  TEEGDSHLSADMYVNIDENGEDVDFFPSLIFQELFAKLNRMASLAADMFVGRERFAISLLMRLTETVILWLSGDQSFWDD
SQ  IEEGPRPLGPLGLRQLYLDMKFVICFASQGRYLSRNLHRGTNEIISKALAAFTATGIDPYSELPEDDWFNDICVDAMERL
SQ  SGKTKGNNGDVHSPTASVSAQSVSSARSHGSY
//
ID  Q9NV70;
PN  Exocyst complex component 1;
GN  EXOC1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Cytoplasm {ECO:0000269|PubMed:16181645, ECO:0000269|PubMed:19889084}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19889084}. Cell membrane {ECO:0000269|PubMed:16181645}. Note=Colocalizes with CNTRL/centriolin at the midbody ring (PubMed:16213214). Localizes in cell membrane in the presence of SLC6A9 (PubMed:16181645). {ECO:0000269|PubMed:16181645, ECO:0000269|PubMed:16213214}.
DR  UNIPROT: Q9NV70;
DR  UNIPROT: Q504V4;
DR  UNIPROT: Q8WUE7;
DR  UNIPROT: Q96T15;
DR  UNIPROT: Q9NZE4;
DR  Pfam: PF15277;
DR  Pfam: PF09763;
DR  OMIM: 607879;
DR  DisGeNET: 55763;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. (Microbial infection) Has an antiviral effect against flaviviruses by affecting viral RNA transcription and translation through the sequestration of elongation factor 1-alpha (EEF1A1). This results in decreased viral RNA synthesis and decreased viral protein translation. {ECO:0000269|PubMed:19889084}.
DE  Reference Proteome: Yes;
DE  Interaction: O60645; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: O95295; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q03001; IntAct: EBI-1105725; Score: 0.00
DE  Interaction: Q12840; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q7Z3B4; IntAct: EBI-24426768; Score: 0.67
DE  Interaction: Q8IX03; IntAct: EBI-15812551; Score: 0.41
DE  Interaction: Q8IYI6; IntAct: EBI-12450194; Score: 0.51
DE  Interaction: Q8NF91; IntAct: EBI-21375821; Score: 0.00
DE  Interaction: Q8TAG9; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: Q8WXH0; IntAct: EBI-21375239; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-1062888; Score: 0.00
DE  Interaction: Q9BZD4; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q5KU26; IntAct: EBI-1105596; Score: 0.00
DE  Interaction: Q9HCM1; IntAct: EBI-1105801; Score: 0.00
DE  Interaction: Q13439; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q9H7U1; IntAct: EBI-1105914; Score: 0.00
DE  Interaction: Q9C0D2; IntAct: EBI-1105940; Score: 0.00
DE  Interaction: Q9UPN3; IntAct: EBI-1106060; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-1106277; Score: 0.00
DE  Interaction: Q96A65; IntAct: EBI-12449995; Score: 0.80
DE  Interaction: O60239; IntAct: EBI-1106308; Score: 0.00
DE  Interaction: Q13813; IntAct: EBI-1106390; Score: 0.00
DE  Interaction: Q9C026; IntAct: EBI-1106505; Score: 0.00
DE  Interaction: O75962; IntAct: EBI-1106525; Score: 0.00
DE  Interaction: Q5NH32; IntAct: EBI-2806981; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q80U62; IntAct: EBI-3506571; Score: 0.40
DE  Interaction: Q8CDJ3; IntAct: EBI-3506695; Score: 0.40
DE  Interaction: Q15051; IntAct: EBI-4286917; Score: 0.64
DE  Interaction: A8K0Z3; IntAct: EBI-9075674; Score: 0.51
DE  Interaction: Q6P5D4; IntAct: EBI-10991106; Score: 0.35
DE  Interaction: P48039; IntAct: EBI-11578238; Score: 0.00
DE  Interaction: Q96KP1; IntAct: EBI-12449995; Score: 0.80
DE  Interaction: O95721; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: Q13445; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: Q9UEU0; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: Q9UPT5; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: Q53HC9; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: Q13049; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: O00471; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: Q9H5N1; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: Q9Y2D4; IntAct: EBI-12450145; Score: 0.51
DE  Interaction: Q8TD31; IntAct: EBI-24359951; Score: 0.56
DE  Interaction: P18848; IntAct: EBI-22734600; Score: 0.56
DE  Interaction: P11234; IntAct: EBI-11934086; Score: 0.00
DE  Interaction: O36551; IntAct: EBI-14062552; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-21559824; Score: 0.35
DE  Interaction: Q96EV8; IntAct: EBI-21651992; Score: 0.35
DE  Interaction: P27930; IntAct: EBI-21662122; Score: 0.35
DE  Interaction: P24530; IntAct: EBI-21672284; Score: 0.35
DE  Interaction: O95229; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q9UJ41; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q9Y2X7; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q9UID3; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q9NUP1; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q9NNX1; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q9BRV8; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q9BQD3; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q96JG6; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q96EK4; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q96BD5; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q8TBA6; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q6S8J3; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q6QNY1; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q6NZI2; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q5VIR6; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q5T1M5; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q5T0U0; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q5R372; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q4V328; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q16204; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q15276; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q15025; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q14161; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q14155; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q13107; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q13033; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: P33176; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: O95613; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: O60282; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: O43815; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: O15516; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: O14777; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q9Y2V7; IntAct: EBI-21673529; Score: 0.35
DE  Interaction: Q9UJT2; IntAct: EBI-21696311; Score: 0.35
DE  Interaction: P28908; IntAct: EBI-21750180; Score: 0.35
DE  Interaction: Q70UQ0; IntAct: EBI-21813594; Score: 0.35
DE  Interaction: Q9BT49; IntAct: EBI-21869056; Score: 0.35
DE  Interaction: Q9NPJ6; IntAct: EBI-25472377; Score: 0.35
DE  Interaction: Q9Y275; IntAct: EBI-21266480; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: Q9UP83; IntAct: EBI-21370112; Score: 0.00
DE  Interaction: O14795; IntAct: EBI-21370190; Score: 0.00
DE  Interaction: Q96RF0; IntAct: EBI-21371429; Score: 0.00
DE  Interaction: Q86XK3; IntAct: EBI-21371888; Score: 0.00
DE  Interaction: Q8TAB5; IntAct: EBI-21372100; Score: 0.00
DE  Interaction: A0AUZ9; IntAct: EBI-21372770; Score: 0.00
DE  Interaction: Q7Z6K1; IntAct: EBI-21373121; Score: 0.00
DE  Interaction: O60341; IntAct: EBI-21374572; Score: 0.00
DE  Interaction: Q9NYJ8; IntAct: EBI-21374944; Score: 0.00
DE  Interaction: Q08AD1; IntAct: EBI-21375463; Score: 0.00
DE  Interaction: O75044; IntAct: EBI-21376088; Score: 0.00
DE  Interaction: O94822; IntAct: EBI-21377108; Score: 0.00
DE  Interaction: Q9UIF3; IntAct: EBI-21377680; Score: 0.00
DE  Interaction: Q96JM3; IntAct: EBI-21378253; Score: 0.00
DE  Interaction: Q8WYA0; IntAct: EBI-21378706; Score: 0.00
DE  Interaction: P28330; IntAct: EBI-21379260; Score: 0.00
DE  Interaction: Q14197; IntAct: EBI-21379436; Score: 0.00
DE  Interaction: Q14571; IntAct: EBI-21379754; Score: 0.00
DE  Interaction: Q6ZTA4; IntAct: EBI-21380545; Score: 0.00
DE  Interaction: O15230; IntAct: EBI-21380204; Score: 0.00
DE  Interaction: Q14980; IntAct: EBI-21380995; Score: 0.00
DE  Interaction: Q9ULH1; IntAct: EBI-21381430; Score: 0.00
DE  Interaction: Q9NR80; IntAct: EBI-21381244; Score: 0.00
DE  Interaction: Q9Y383; IntAct: EBI-21381969; Score: 0.00
DE  Interaction: Q567U6; IntAct: EBI-21382571; Score: 0.00
DE  Interaction: Q5T0N5; IntAct: EBI-21382805; Score: 0.00
DE  Interaction: Q9NX95; IntAct: EBI-21383531; Score: 0.00
DE  Interaction: Q7Z4S6; IntAct: EBI-21383490; Score: 0.00
DE  Interaction: Q3V6T2; IntAct: EBI-21383689; Score: 0.00
DE  Interaction: Q8WXA3; IntAct: EBI-21383580; Score: 0.00
DE  Interaction: Q99459; IntAct: EBI-21383874; Score: 0.00
DE  Interaction: Q8TDR0; IntAct: EBI-21383847; Score: 0.00
DE  Interaction: Q96SN8; IntAct: EBI-21383834; Score: 0.00
DE  Interaction: Q8N2N9; IntAct: EBI-21385250; Score: 0.00
DE  Interaction: Q8IYE0; IntAct: EBI-21385113; Score: 0.00
DE  Interaction: Q7Z6B7; IntAct: EBI-21384976; Score: 0.00
DE  Interaction: Q49A88; IntAct: EBI-21386371; Score: 0.00
DE  Interaction: P53804; IntAct: EBI-21388051; Score: 0.00
DE  Interaction: Q8IYT3; IntAct: EBI-21389251; Score: 0.00
DE  Interaction: P55197; IntAct: EBI-21389515; Score: 0.00
DE  Interaction: Q9H2F5; IntAct: EBI-21389541; Score: 0.00
DE  Interaction: Q9ULU8; IntAct: EBI-21390808; Score: 0.00
DE  Interaction: O43490; IntAct: EBI-21391143; Score: 0.00
DE  Interaction: P35609; IntAct: EBI-21391067; Score: 0.00
DE  Interaction: Q8NEY1; IntAct: EBI-21391441; Score: 0.00
DE  Interaction: O15066; IntAct: EBI-21392232; Score: 0.00
DE  Interaction: Q5NHH2; IntAct: EBI-22298200; Score: 0.37
DE  Interaction: Q5NGE3; IntAct: EBI-22298210; Score: 0.37
DE  Interaction: O84008; IntAct: EBI-22302433; Score: 0.35
GO  GO:0005737;
GO  GO:0098592;
GO  GO:0005829;
GO  GO:0000145;
GO  GO:0090543;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005546;
GO  GO:0051607;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0090148;
GO  GO:0000281;
GO  GO:0048015;
GO  GO:0050714;
GO  GO:0015031;
GO  GO:0016241;
GO  GO:0006904;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTAIKHALQRDIFTPNDERLLSIVNVCKAGKKKKNCFLCATVTTERPVQVKVVKVKKSDKGDFYKRQIAWALRDLAVVDA
SQ  KDAIKENPEFDLHFEKIYKWVASSTAEKNAFISCIWKLNQRYLRKKIDFVNVSSQLLEESVPSGENQSVTGGDEEVVDEY
SQ  QELNAREEQDIEIMMEGCEYAISNAEAFAEKLSRELQVLDGANIQSIMASEKQVNILMKLLDEALKEVDQIELKLSSYEE
SQ  MLQSVKEQMDQISESNHLIHLSNTNNVKLLSEIEFLVNHMDLAKGHIKALQEGDLASSRGIEACTNAADALLQCMNVALR
SQ  PGHDLLLAVKQQQQRFSDLRELFARRLASHLNNVFVQQGHDQSSTLAQHSVELTLPNHHPFHRDLLRYAKLMEWLKSTDY
SQ  GKYEGLTKNYMDYLSRLYEREIKDFFEVAKIKMTGTTKESKKFATLPRKESAVKQETESLHGSSGKLTGSTSSLNKLSVQ
SQ  SSGNRRSQSSSLLDMGNMSASDLDVADRTKFDKIFEQVLSELEPLCLAEQDFISKFFKLQQHQSMPGTMAEAEDLDGGTL
SQ  SRQHNCGTPLPVSSEKDMIRQMMIKIFRCIEPELNNLIALGDKIDSFNSLYMLVKMSHHVWTAQNVDPASFLSTTLGNVL
SQ  VTVKRNFDKCISNQIRQMEEVKISKKSKVGILPFVAEFEEFAGLAESIFKNAERRGDLDKAYTKLIRGVFVNVEKVANES
SQ  QKTPRDVVMMENFHHIFATLSRLKISCLEAEKKEAKQKYTDHLQSYVIYSLGQPLEKLNHFFEGVEARVAQGIREEEVSY
SQ  QLAFNKQELRKVIKEYPGKEVKKGLDNLYKKVDKHLCEEENLLQVVWHSMQDEFIRQYKHFEGLIARCYPGSGVTMEFTI
SQ  QDILDYCSSIAQSH
//
ID  Q8R3S6;
PN  Exocyst complex component 1;
GN  Exoc1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9NV70}. Cytoplasm {ECO:0000250|UniProtKB:Q9NV70}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9NV70}. Cell membrane {ECO:0000250|UniProtKB:Q9NV70}. Note=Colocalizes with CNTRL/centriolin at the midbody ring. Localizes in cell membrane in the presence of SLC6A9. {ECO:0000250|UniProtKB:Q9NV70}.
DR  UNIPROT: Q8R3S6;
DR  UNIPROT: E9QQ24;
DR  Pfam: PF15277;
DR  Pfam: PF09763;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0098592;
GO  GO:0000145;
GO  GO:0090543;
GO  GO:0005886;
GO  GO:0005546;
GO  GO:0007566;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0090148;
GO  GO:0000281;
GO  GO:0048015;
GO  GO:0050714;
GO  GO:0015031;
GO  GO:0006904;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTAIKHALQRDIFTPNDERLLSIVNVCKAGKKKKNCFLCATVTTERPVQVKVVKVKKSDKGDFYKRQIAWALRDLAVVDA
SQ  KDAIKENPEFDLHFEKVYKWVASSTAEKNAFISCIWKLNQRYLRKKIDFVNVSSQLLEESVPSGENQSVAGGDEEAVDEY
SQ  QELNAREEQDIEIMMEGCECAISNAEAFAEKLSRELQVLDGANIQSIMASEKQVNTLMQLLDEALTEVDQIELKLSSYEE
SQ  MLQSVKEQMDQISESNHLIHLSNTNNVKLLSEIEFLVNHMDLAKGHIKALQEGDLVSSRGIEACTNAADALLQCMNVALR
SQ  PGHDMLLAVKQQQQRFSDLREHFARRLASHLNNVFVQQGHDQSSTLAQHSVELTLPNHHPFHRDLLRYAKLMEWLKSTDY
SQ  GKYEGLTKNYMDYLSRLYEREIKDFFEVAKMKMTGTSKESKKFATLPRKESAVKQETESLHGSSGKLTGSTSSLNKLSVQ
SQ  SSGSRRSQSSSLLDMGNMSASDLDVADRTKFDKIFEQVLSELEPLCLAEQDFISKFFKLQQHQNMSASMTEAEDLDGGSL
SQ  LRQHSSGTLLPVSSEKDMIRQMMIKIFRCIEPELNNLIALGDKVDSFNSLYMLVKMSHHVWTAQNVDPASFLSTTLGNVL
SQ  VTVKRNFDKCISNQIRQMEEVKISKKSKVGILPFVAEFEEFAGLAESIFKNAERRGDLDKAYTKLIRGVFINVEKVANES
SQ  QKTPRDVVMMENFHHIFATLSRLKISCLEAEKKEAKQKYTDHLQSYVIYSLGQPLEKLNHFFEGVEARVAQGIREEEVSY
SQ  QLAFNKQELRKVIKEYPGKEVKKGLDNLYKKVDKHLCEEENLLQVVWHSMQDEFIRQYKHFEGLIARCYPGSGVTMEFTI
SQ  QDILDYCSSIAQSH
//
ID  Q0V8C2;
PN  Exocyst complex component 3;
GN  EXOC3;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q62825}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q62825}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q62825}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q62825}. Midbody {ECO:0000250|UniProtKB:O60645}. Golgi apparatus {ECO:0000250|UniProtKB:O60645}. Note=Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (By similarity). During mitosis, early recruitment to the midbody requires RALA, but not RALB, and EXOC2. In late stages of cytokinesis, localization to the midbody is RALB-dependent (By similarity). {ECO:0000250|UniProtKB:O60645, ECO:0000250|UniProtKB:Q62825}.
DR  UNIPROT: Q0V8C2;
DR  Pfam: PF06046;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0000149;
GO  GO:0051601;
GO  GO:0006887;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKETDREAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLA
SQ  DVSKDWRQSINTIESLKDVKDAVVRHSQLAAAVENLKNIFSVPEIVRETQDLIEHGELLQAHRKLMDLECSRDGLMYEQY
SQ  RMDSGNTRDMTLIHSYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGR
SQ  PKNWKEKMFTILDRTVTTRIEGTQADTRESDRMWLVRHLEIIRKYVLDDLIVAKNLLAQCFPPHYEIFRSLLRTYHQALS
SQ  ARMQDLAAEDLEANEIVSLLTWVLNTYTSVEMMGNAELAPEVDVALLEPLLSADVVSALLDTYMSTLTSNIIAWLRKALE
SQ  TDKKDWMKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKEEAQLYRDEHLRDR
SQ  QHPHCYVQYMVAVVNNCQTFKESIVSLKRKYLKHEAEEGVSLSQPSMDGVLDAIAKEGCGSLLEEVFLDLEQHLNELMTK
SQ  KWLLGSNAVDIICVTVEDYFNDFAKIKKPYRKRMIAEAHRRAVQEYLRAVMQKRISFRSAEERKDGAERMVREAEQLRFL
SQ  FRKLASGFGEEMDSYCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLAMRGDASRDMKQTIIETLEQGPA
SQ  QASPDYVPIFKDIVVPSLNVAKLLK
//
ID  Q54BP6;
PN  Exocyst complex component 3;
GN  exoc3;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q62825}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q62825}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q62825}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q62825}. Midbody {ECO:0000250|UniProtKB:O60645}. Golgi apparatus {ECO:0000250|UniProtKB:O60645}.
DR  UNIPROT: Q54BP6;
DR  Pfam: PF06046;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0000149;
GO  GO:0051601;
GO  GO:0006887;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METVSLVPLEGLDDLSAQSAAIKKIEQNFSNIDSLASVTNHKISLIQQKKTIEAQIKNEVHSELEKSKKGLETLYKSYNR
SQ  INRMDESFSDTVELCSETSNLIGHYQLIKKVNTVRVNLINILKEVDRLLTIPEKAAEIEQLLSDDLNLLEIHSKLRELER
SQ  LHQKALKQFESNFEELEAIKEMFSSVPELSHRFENKIWNIVSNSIDIAQIKPAVLVKVAQIIEREKLHEQKQKEKKSQNS
SQ  LISSEGIHDDDDDDDDTEVNLNNSNKQQNNENENSSSNNNNNYDINNEDEGYDRNRSNYGDRFLEVLIQSISGKFEPMFL
SQ  NSHNDLVQTLKDVNKMVDELFIVMDIVQECYPPSYDLFNFYVDQYHTKFYSLFGSFSNLMESSHVNNNYQVVVTKNIPSA
SQ  HILMLVEWVVKNYSRDLSRLGIQDISPPLLDSLDPLIKIYKMHIKQLMREWCDNIINNDNQNKPEVVDGQYCSLAPIQLF
SQ  ESVASQLDIAAATKCQKLVVGVMEEVVSALMYFQVQSITLLQERNHEIKLENVIAYVNNNSKCYDHTQTIVDKVSNILDS
SQ  EHMGYLDFDPVLEGFLNVSKVATQAISSVIFRDLDECIHKFYTVEWYQEDLMQPIINTFEDYVTNDIQKYILENYLKRLA
SQ  LLLLDTLIEQLLAQLIGGKNKFNENTYKILSNDCDKLLDFFKKYLRLSVVTAKVQILEDFKQMITSSIDMVPVYFRSVIN
SQ  FHKDINERVVELVLYQRTDISKSEITEVLGQIKTIVETVHTDPTNPPTGIFSRMNIYQRGWFS
//
ID  O60645;
PN  Exocyst complex component 3;
GN  EXOC3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54921}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54921}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54921}. Midbody {ECO:0000269|PubMed:18756269}. Golgi apparatus {ECO:0000305|PubMed:18756269}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q62825}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). During mitosis, early recruitment to the midbody requires RALA, but not RALB, and EXOC2. In late stages of cytokinesis, localization to the midbody is RALB- dependent (PubMed:18756269). {ECO:0000250|UniProtKB:O54921, ECO:0000269|PubMed:18756269}.
DR  UNIPROT: O60645;
DR  UNIPROT: Q6P2E8;
DR  UNIPROT: Q8TEN6;
DR  UNIPROT: Q8WUW0;
DR  UNIPROT: Q96DI4;
DR  Pfam: PF06046;
DR  OMIM: 608186;
DR  DisGeNET: 11336;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
DE  Reference Proteome: Yes;
DE  Interaction: A1L4K1; IntAct: EBI-25258050; Score: 0.56
DE  Interaction: P01106; IntAct: EBI-1074529; Score: 0.00
DE  Interaction: O88738; IntAct: EBI-1765706; Score: 0.35
DE  Interaction: Q8BHD1; IntAct: EBI-2557128; Score: 0.40
DE  Interaction: A0A2U2H1F8; IntAct: EBI-2870328; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: P40692; IntAct: EBI-2932395; Score: 0.37
DE  Interaction: O43684; IntAct: EBI-3916000; Score: 0.37
DE  Interaction: Q86VI4; IntAct: EBI-10764290; Score: 0.40
DE  Interaction: P00533; IntAct: EBI-10764491; Score: 0.40
DE  Interaction: Q8CAQ8; IntAct: EBI-11096643; Score: 0.35
DE  Interaction: Q9HBH9; IntAct: EBI-11139967; Score: 0.35
DE  Interaction: O00139; IntAct: EBI-11140263; Score: 0.35
DE  Interaction: Q9Z172; IntAct: EBI-11157923; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q9NV70; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: Q96KP1; IntAct: EBI-12450028; Score: 0.64
DE  Interaction: Q9UPT5; IntAct: EBI-12450043; Score: 0.51
DE  Interaction: Q13445; IntAct: EBI-12450043; Score: 0.51
DE  Interaction: Q96A65; IntAct: EBI-12450043; Score: 0.64
DE  Interaction: O00471; IntAct: EBI-12450093; Score: 0.64
DE  Interaction: Q9BZL4; IntAct: EBI-24371831; Score: 0.56
DE  Interaction: Q96IK5; IntAct: EBI-24472724; Score: 0.56
DE  Interaction: Q13049; IntAct: EBI-11902318; Score: 0.00
DE  Interaction: P11234; IntAct: EBI-11902309; Score: 0.00
DE  Interaction: O75386; IntAct: EBI-11902300; Score: 0.00
DE  Interaction: Q9Y2D4; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q8IYI6; IntAct: EBI-21672932; Score: 0.51
DE  Interaction: Q8TAG9; IntAct: EBI-21673041; Score: 0.51
DE  Interaction: P35613; IntAct: EBI-21560440; Score: 0.35
DE  Interaction: P34741; IntAct: EBI-21628438; Score: 0.35
DE  Interaction: Q96EV8; IntAct: EBI-21651992; Score: 0.35
DE  Interaction: P27930; IntAct: EBI-21662122; Score: 0.35
DE  Interaction: Q13563; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q9Y496; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q9H0B6; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q9BQD3; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q9BQ69; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q99666; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q96NL6; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q96JN2; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q8WXW3; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q8IY31; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q8IWJ2; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: P0DJD1; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q2M2Z5; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q15643; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q07866; IntAct: EBI-21672799; Score: 0.35
DE  Interaction: Q32P51; IntAct: EBI-20938684; Score: 0.40
DE  Interaction: P12004; IntAct: EBI-21238234; Score: 0.37
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P18433; IntAct: EBI-27116377; Score: 0.27
DE  Interaction: Q9HD43; IntAct: EBI-27116527; Score: 0.27
GO  GO:0005829;
GO  GO:0000145;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0042734;
GO  GO:0030667;
GO  GO:0045296;
GO  GO:0000149;
GO  GO:0051601;
GO  GO:0006887;
GO  GO:0090148;
GO  GO:0000281;
GO  GO:0015031;
GO  GO:0006904;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKETDREAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLA
SQ  DVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLECSRDGLMYEQY
SQ  RMDSGNTRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGR
SQ  PKNWKEKMFTILERTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLIVAKNLMVQCFPPHYEIFKNLLNMYHQALS
SQ  TRMQDLASEDLEANEIVSLLTWVLNTYTSTEMMRNVELAPEVDVGTLEPLLSPHVVSELLDTYMSTLTSNIIAWLRKALE
SQ  TDKKDWVKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKDEAQLYKEEHLRNR
SQ  QHPHCYVQYMIAIINNCQTFKESIVSLKRKYLKNEVEEGVSPSQPSMDGILDAIAKEGCSGLLEEVFLDLEQHLNELMTK
SQ  KWLLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSPEERKEGAEKMVREAEQLRFL
SQ  FRKLASGFGEDVDGYCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLAVRGDASRDMKQTIMETLEQGPA
SQ  QASPSYVPLFKDIVVPSLNVAKLLK
//
ID  Q6KAR6;
PN  Exocyst complex component 3;
GN  Exoc3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54921}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54921}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54921}. Midbody {ECO:0000250|UniProtKB:O60645}. Golgi apparatus {ECO:0000250|UniProtKB:O60645}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q62825}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). During mitosis, early recruitment to the midbody requires RALA, but not RALB, and EXOC2. In late stages of cytokinesis, localization to the midbody is RALB- dependent (By similarity). {ECO:0000250|UniProtKB:O54921, ECO:0000250|UniProtKB:O60645}.
DR  UNIPROT: Q6KAR6;
DR  Pfam: PF06046;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P25322; IntAct: EBI-3956307; Score: 0.46
DE  Interaction: O35382; IntAct: EBI-8299949; Score: 0.40
DE  Interaction: P23819; IntAct: EBI-8300089; Score: 0.40
DE  Interaction: P35438; IntAct: EBI-8300130; Score: 0.40
DE  Interaction: P11234; IntAct: EBI-3956345; Score: 0.27
GO  GO:0000145;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0042734;
GO  GO:0030667;
GO  GO:0000149;
GO  GO:0051601;
GO  GO:0006887;
GO  GO:0090148;
GO  GO:0000281;
GO  GO:0015031;
GO  GO:0006904;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCKDSACFLTMKETDLEAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALN
SQ  DVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLEC
SQ  SRDGLMCEQYRMDSGNKRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRK
SQ  KQTGFVPPGRPKNWKEKMFAILDRTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLIVAKNLMVQCFPPHYEIFKN
SQ  LLSMYHQALSTRMQDLASEDLEANEIVSLLTWVLNTYTSAEMMGNVELAPEVDVSALEPLLSPNIVSELLDTYMSTLTSN
SQ  IIAWLRKALETDKKDWSKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKDEAQ
SQ  LYKEEHLRNRQHPHCYVQYMIAIINNCQTFKESIISLKRKYLKTEAEEGLCLSQPSMDGILDAIAKEGCSSLLEEVFLDL
SQ  EQHLNELMTKKWLLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSAEERKEGAEKM
SQ  VREAEQLRFLFRKLASGFGEDADGHCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLALRGDASRDMKQT
SQ  IMETLEQGPMQASPNYVPIFKEIVVPSLNVAKLLK
//
ID  Q62825;
PN  Exocyst complex component 3;
GN  Exoc3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12954101}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12954101}. Cell projection, growth cone {ECO:0000269|PubMed:12954101}. Cell projection, neuron projection {ECO:0000269|PubMed:12954101}. Midbody {ECO:0000250|UniProtKB:O60645}. Golgi apparatus {ECO:0000250|UniProtKB:O60645}. Note=Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (PubMed:12954101). During mitosis, early recruitment to the midbody requires RALA, but not RALB, and EXOC2. In late stages of cytokinesis, localization to the midbody is RALB-dependent (By similarity). {ECO:0000250|UniProtKB:O60645, ECO:0000269|PubMed:12954101}.
DR  UNIPROT: Q62825;
DR  UNIPROT: Q4QQU2;
DR  Pfam: PF06046;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
DE  Reference Proteome: Yes;
DE  Interaction: P97879; IntAct: EBI-15885274; Score: 0.35
DE  Interaction: P07949; IntAct: EBI-22248789; Score: 0.35
GO  GO:0000145;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030496;
GO  GO:0048471;
GO  GO:0042734;
GO  GO:0000149;
GO  GO:0051601;
GO  GO:0006887;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCKDSACFSTMKETDLEAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALN
SQ  DVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLEC
SQ  SRDGLMCEQYRMDSGNKRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRK
SQ  KQTGFVPPGRPKNWKEKMFAVLDRTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLVIAKNLLVQCFPPHYDIFKN
SQ  LLSMYHQALSIRMQDLASEDLEANEIVSLLTWVLNTYTSAEMMGNVELAPEVDVNALEPLLSPNVVSELLDTYMSTLTSN
SQ  IIAWLRKALETDKKDWSKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKEEAQ
SQ  LYKEEHLRNRQHPHCYVQYMVAIINNCQTFKESIISLKRKYLKPETEESLCQSQPSMDGILDAIAKEGCSSLLEEVFLDL
SQ  EQHLNELMTKKWMLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSAEERKEGAEKM
SQ  VREAEQLRFLFRKLASGFGEDADGHCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLALRGDASRDMKQT
SQ  IMETLEQGPMQASPNYVPIFQEIVVPSLNVAKLLK
//
ID  E2R766;
PN  Exocyst complex component 6;
GN  EXOC6;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54923}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). {ECO:0000250|UniProtKB:O54923, ECO:0000250|UniProtKB:Q8TAG9}.
DR  UNIPROT: E2R766;
DR  Pfam: PF04091;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane (By similarity). Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. {ECO:0000250, ECO:0000269|PubMed:20890297}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0090543;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0006886;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAENSEGLGTVPEHERILQEIESTDTACVGPTLRSVYDDQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITEL
SQ  LKVRTDAEKLKVQVTDTNRRFQDAGKEVIIQTEDIIRCRIQQRNITTVVENLQYAFPVLEMYSKLKEQMTAKRYYSALKT
SQ  MEQLENVYFPRVSQYRFCQLMIENLPKLREDIKEISMSDLKDFLESIRKHSDKIGETAMKQAQQQKTFSVALQKQNNVKF
SQ  GKNMYINDRIPEERKENELKQGFEEEDENEEEILTVQDLVDFSPVYRCLHIYSVLGDEETFENYYRKQRKKQARLVLQPQ
SQ  SNMHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRAYTDELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLIVIFAD
SQ  TLQGYGFPVNRLFDLLFEIRDQYNETLLKKWAGVFRDIFEEDNYSPIPIVNEEEYKAVISKFPFQDPDFEKQSFPKKFPM
SQ  SQSVPHIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRTLSSCLLNLIRKPHIGLTELVQIIINTTHLEQAC
SQ  KYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMSEPDGRASGYLMDLINFLR
SQ  SIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFIDL
SQ  RQLLDLFMVWDWSTYLADYGQPASKYLRVNPNTALTLLEKMKDTSKKNNIFAQFRKNDRDKQKLIETVVKQLRSLVNGMS
SQ  QHT
//
ID  Q54B27;
PN  Exocyst complex component 6;
GN  exoc6;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}.
DR  UNIPROT: Q54B27;
DR  Pfam: PF04091;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0090543;
GO  GO:0048471;
GO  GO:0031267;
GO  GO:0070177;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0006886;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNKKQKEEINTAGGSVILKTMVRDKDKEQKEEKREKKEKKRLEKKEAENVKKEKKKEKKELKKIGKAGRSGSITSDSST
SQ  HSGAQEFDSYGNDSNGGGGGLSASIDSNGLSSSGQPMQTRHLEKEVGEKQGIYSLSSQDRSSSLPHSSQDDQAKPLITES
SQ  EIFSSESFLIAVSDTDHLGPAIKSVFENNKEKEVIKILNAYIAQKDLDIEKICGENHEGFINSVTAFLGLKGENLDLKQD
SQ  VINLNYELQEIGRKYVTKAEELFAYKQIKDNIKRTKEVLNNCQYAILLGMKVDEYVQQKKYYQAIKNMDQLHNVYLKKLS
SQ  DFQFARNMDYNIPVLKEKIKKLVKDEFNQWMVEIKEKSAVIGKLGMIQTSKKLLKEREINPLKIKTTFGENEQIWDKILD
SQ  IPPIINSSSIGSLALYPTLNSPVTAPIYSPNSGKTPSSFGFNKQINEKDLKEDINQFSPFDESDIQFHPLYQCLFIHASI
SQ  GQLEEFQAYYTLNRLLQFQLVIQPKESGQVWELFLQQILGYFMVESKVIDSTEPFLSKTTINDSWNSALVKVTSVLQELF
SQ  THCVDTQPLIAFKKFVLIFTNTMSFYSYHVQPLYYFLDTMKEKYCQFSIKEAVERFTIILERDSHCSLIIESLEEYKSLI
SQ  LANKLDILERQQLRQLQNSLNNNQFQFGDKNLNNNNNNDDDDDYFDEDENEDDKISKRLPKSFLFSKMVPQFYTLIKKFI
SQ  SEFYEFSDQLTENENFIIRSTDTLIKKINEVLYSYLTQSQAVPQVIQLVINLQHLISGCSFFKDYLNSLILGEDYQKNQS
SQ  IVNETNKVILNSQNLLYTTKSHGEKLIIKLCEQKIEDLMSSAANIEWFPQNAIDDRPRDYIIDVCTFLEVTLPFISPLSQ
SQ  NLKEEFITKAFKNISESLFSLIYDDQLKKLNLQGVKSFDADLKYIETYVKEKANEKERTTTTSRNMVGYFVELRQLTNFL
SQ  LSDNPEDFVDPKIKAKHYNLITNIPQLLNILNKYKEESKGFTTSKEIKDRNKKIADAIKKIKDSL
//
ID  Q8TAG9;
PN  Exocyst complex component 6;
GN  EXOC6;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54923}. Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation. Colocalizes with CNTRL/centriolin at the midbody ring (PubMed:16213214). {ECO:0000250|UniProtKB:O54923, ECO:0000269|PubMed:16213214}.
DR  UNIPROT: Q8TAG9;
DR  UNIPROT: E9PHI3;
DR  UNIPROT: Q5VXH8;
DR  UNIPROT: Q9NZ24;
DR  Pfam: PF04091;
DR  OMIM: 609672;
DR  DisGeNET: 54536;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O60645; IntAct: EBI-21673041; Score: 0.51
DE  Interaction: P0DTD1; IntAct: EBI-26951880; Score: 0.49
DE  Interaction: P50148; IntAct: EBI-21673041; Score: 0.35
DE  Interaction: P62834; IntAct: EBI-21673041; Score: 0.35
DE  Interaction: Q53GS7; IntAct: EBI-25859244; Score: 0.56
DE  Interaction: Q8IYI6; IntAct: EBI-12450124; Score: 0.64
DE  Interaction: P02768; IntAct: EBI-1223494; Score: 0.35
DE  Interaction: Q9BQ95; IntAct: EBI-3385759; Score: 0.37
DE  Interaction: P32119; IntAct: EBI-3385854; Score: 0.37
DE  Interaction: Q96JB6; IntAct: EBI-3385849; Score: 0.37
DE  Interaction: Q92947; IntAct: EBI-3385844; Score: 0.37
DE  Interaction: Q9Y3B2; IntAct: EBI-3385839; Score: 0.37
DE  Interaction: P05067; IntAct: EBI-3385834; Score: 0.37
DE  Interaction: P29474; IntAct: EBI-3385829; Score: 0.37
DE  Interaction: Q8TAG9; IntAct: EBI-3385859; Score: 0.37
DE  Interaction: Q9Y2H9; IntAct: EBI-3385991; Score: 0.37
DE  Interaction: P49810; IntAct: EBI-3386181; Score: 0.37
DE  Interaction: Q96A65; IntAct: EBI-10764425; Score: 0.73
DE  Interaction: P0DOE7; IntAct: EBI-11327042; Score: 0.40
DE  Interaction: Q9NV70; IntAct: EBI-12449995; Score: 0.51
DE  Interaction: O00471; IntAct: EBI-12450093; Score: 0.79
DE  Interaction: P61006; IntAct: EBI-12450124; Score: 0.51
DE  Interaction: Q9UPT5; IntAct: EBI-12450124; Score: 0.51
DE  Interaction: Q96KP1; IntAct: EBI-12450124; Score: 0.64
DE  Interaction: Q16891; IntAct: EBI-12450124; Score: 0.51
DE  Interaction: Q9Y2D4; IntAct: EBI-11923380; Score: 0.00
DE  Interaction: P32970; IntAct: EBI-21512742; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-21559824; Score: 0.35
DE  Interaction: P49146; IntAct: EBI-21569349; Score: 0.35
DE  Interaction: Q8N7X8; IntAct: EBI-21585341; Score: 0.35
DE  Interaction: O75558; IntAct: EBI-21632742; Score: 0.35
DE  Interaction: Q96EV8; IntAct: EBI-21651992; Score: 0.35
DE  Interaction: P27930; IntAct: EBI-21662122; Score: 0.35
DE  Interaction: O60939; IntAct: EBI-21671922; Score: 0.35
DE  Interaction: Q96LW7; IntAct: EBI-21673041; Score: 0.35
DE  Interaction: Q5VIR6; IntAct: EBI-21673041; Score: 0.35
DE  Interaction: Q9H410; IntAct: EBI-21673116; Score: 0.35
DE  Interaction: P08173; IntAct: EBI-21707586; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC5; IntAct: EBI-26495256; Score: 0.35
DE  Interaction: O43572; IntAct: EBI-26451580; Score: 0.35
DE  Interaction: Q7Z699; IntAct: EBI-25932191; Score: 0.56
GO  GO:0005829;
GO  GO:0000145;
GO  GO:0090543;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0006886;
GO  GO:0090148;
GO  GO:0000281;
GO  GO:0006904;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAENSESLGTVPEHERILQEIESTDTACVGPTLRSVYDDQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITEL
SQ  LKVRTDAEKLKVQVTDTNRRFQDAGKEVIVHTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSAKRYYSALKT
SQ  MEQLENVYFPWVSQYRFCQLMIENLPKLREDIKEISMSDLKDFLESIRKHSDKIGETAMKQAQHQKTFSVSLQKQNKMKF
SQ  GKNMYINRDRIPEERNETVLKHSLEEEDENEEEILTVQDLVDFSPVYRCLHIYSVLGDEETFENYYRKQRKKQARLVLQP
SQ  QSNMHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRAYTDELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLTVIFA
SQ  DTLQGYGFPVNRLFDLLFEIRDQYNETLLKKWAGVFRDIFEEDNYSPIPVVNEEEYKIVISKFPFQDPDLEKQSFPKKFP
SQ  MSQSVPHIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRTLSSCLLNLIRKPHIGLTELVQIIINTTHLEQA
SQ  CKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMSEPDGRASGYLMDLINFL
SQ  RSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFID
SQ  LRQLLDLFMVWDWSTYLADYGQPASKYLRVNPNTALTLLEKMKDTSKKNNIFAQFRKNDRDKQKLIETVVKQLRSLVNGM
SQ  SQHM
//
ID  Q8R313;
PN  Exocyst complex component 6;
GN  Exoc6;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54923}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). {ECO:0000250|UniProtKB:O54923, ECO:0000250|UniProtKB:Q8TAG9}.
DR  UNIPROT: Q8R313;
DR  Pfam: PF04091;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q62739; IntAct: EBI-9202177; Score: 0.52
GO  GO:0000145;
GO  GO:0090543;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030218;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0006886;
GO  GO:0090148;
GO  GO:0000281;
GO  GO:0006904;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAESCEALGTVPEHERILQEIESTDTACVGPTLRSVYDDQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITEL
SQ  LKVRADAEKLKVTDTNRRFQDAGKEVIIQTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSMKRYYSALKTME
SQ  QLENVYFPRVSQYRFCQLMMETLPKLREDMMNYCMSDLTYGLESIRKHSDKIGEAAMKQAQQQKSFSVALQKQNNMRFGK
SQ  NMHVNNDRILEEKSDVIPKHALEEEAENDEEVLTVQDLVDFSPVYRCLHIYSALGDEETFENYYRKQRKKQARLVLQPQS
SQ  SVHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRVYTEELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLIVIFADT
SQ  LQGYGFPVNRLFDLLFEIRDQYNETLLKKWAGIFRDIFEEDNYSPIPIGSEEEYKVVISRFPFQDPDLEKQSFPKKFPMS
SQ  QSVPLIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRILSSCLLNLIRKPHIGLTELVQIIINTTHLEQACK
SQ  YLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMAESDGRASGYLMDLINFLRS
SQ  IFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFIDLR
SQ  QLLDLFMVWDWSTYLADYGQPASKYLRVNPHAALTLLEKMKDTSKKNNIFAQFRKNDRDRQKLIETVVRQLRGLVTGMSQ
SQ  HT
//
ID  O54923;
PN  Exocyst complex component 6;
GN  Exoc6;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12954101}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12954101}. Cell projection, growth cone {ECO:0000269|PubMed:12954101}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (PubMed:12954101). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). {ECO:0000250|UniProtKB:Q8TAG9, ECO:0000269|PubMed:12954101}.
DR  UNIPROT: O54923;
DR  Pfam: PF04091;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. {ECO:0000269|PubMed:20890297}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0090543;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0030218;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0006886;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAESGEALGTVPEHERILQEIESTDTACVGPTLRSVYDGQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITEL
SQ  LKVRADAEKLKVQVTDTNRRFQDAGKEVIEQTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSMQRYYSALKT
SQ  MEQLENVYFPRVSQYRFCQLMMDTLPKLREDIKDISMSDLKDFLESIRKHSDKIGETAMKQAQQQKSFSIAVQKQTNMRF
SQ  GKNMHVNNDRTLEEKSDIILKHTLEEEAENDEEVLTVQDLVDFSPVYRCSHIYSALGDEETFENYYRKQRKKQARLVLQP
SQ  QSSVHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRAYTDELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLIVIFA
SQ  DTLQGYGFSVNRLFDLLFEIRDQYNETLLKKWAGIFRDIFEEDNYSPIPIGSEEEYKMVISKFPFQDPDLEKQSFPKKFP
SQ  MSQSVPLIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRILSSCLLNLIRKPHIGLTELVQIIINTTHLEQA
SQ  CKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMAESDGRASGYLMDLINFL
SQ  RSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFID
SQ  LRQLLDLFMVWDWSTYLADYGQPASKYLRVNPHAALTLLEKMKDTSKKNNIFAQFRKNDRDRQKLIETVVKQLRGLVTGM
SQ  SQHM
//
ID  A4IF89;
PN  Exocyst complex component 8;
GN  EXOC8;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}. Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (By similarity). Localizes at the leading edge of migrating cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O54924}.
DR  UNIPROT: A4IF89;
DR  Pfam: PF16528;
DR  PROSITE: PS50003;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0030426;
GO  GO:0005770;
GO  GO:0048471;
GO  GO:0035091;
GO  GO:0031267;
GO  GO:0007032;
GO  GO:0006887;
GO  GO:0022617;
GO  GO:0006893;
GO  GO:0008104;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMAMSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRIQALAEETAQNLKRNVYQNYRQFIETAREISYL
SQ  ESEMYQLSHLLTEQKSSLESIPLTLLPAAAAAGAAAASGGEEGGGGAGGRDQLRGQTGFFPSPGGASRDGSGPGEEGKQR
SQ  TLTTLLEKVEGCRHLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDGLAVVN
SQ  VKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSEKRRREQEEAAAPRGPPQVTPKASNPFEDEDDDEP
SQ  TVPEIEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRARVDERVRQLTEVLVFELSP
SQ  DRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAG
SQ  TDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVRVAKEHCQQLGDIGLDLTFIVHALLVKDIQGALHSYKE
SQ  IIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELH
SQ  MVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLIRVNPES
SQ  TTSVV
//
ID  Q5ZJ43;
PN  Exocyst complex component 8;
GN  EXOC8;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}.
DR  UNIPROT: Q5ZJ43;
DR  Pfam: PF16528;
DR  PROSITE: PS50003;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0008104;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALALGEGGGGSRLRRQLESGGFAAAEYVKQLSQQSDGDRDLQEHRQRIQALQEETAQSLKRNVYQNYRQFIETAREISY
SQ  LESEMYQLSHILTEQKGIMEAVTQALLLQADRDDPALGARRAAAADPFLPLSAKEAAASEEGRQRTLTTLLEKVEGCRDL
SQ  LPESPGKYLVYNGDLLEYDADHMAQIQRVHAFLMNDCLLVATALPNRRGAYRYDALYPLEGLAVVNVKDNPPMKDMFKLL
SQ  MFPESRIFQAENAKIKKEWLEVLEETKRNRALSEKRRLEQEALPRPAPTPPESTNPFEEEEEEEEEPSAEEEAVDLSLEW
SQ  IQELPEDLDVCIAQRDFEGAVDLLDKLNEYLADKPVSQPVKELRAKVDERVRQLTDVLVFELSPDRSLRGGPRATRRAVS
SQ  QLIRLGQSTKACELFLKNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGNNGCYSAFVVWARSSM
SQ  RMFVDAFSKQVFDSKESLSTAAECVKVAKEHCKQLSDIGLDLTFIIHALLVKDIKGALQSYKDIIIEATKHRNSEEMWRR
SQ  MNLMTPEALGKLREEMKSCGVGSFDQYTGDDCWVNLSYTVVAFTKQTMAFLEEALKLYFPELHMVLLESLVEIILVAVQH
SQ  VDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLMRINPESTTSVV
//
ID  Q54VZ8;
PN  Exocyst complex component 8;
GN  exoc8;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}.
DR  UNIPROT: Q54VZ8;
DR  Pfam: PF16528;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0042995;
GO  GO:0000145;
GO  GO:0048471;
GO  GO:0006887;
GO  GO:0006893;
GO  GO:0008104;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKKGVTYPLKIDTNLSTVSSSVNYNDIECVDIKSNGHYIVKFMYREWVGPLNLMTTQKTSIKISIDLKEQTVTCTHTDKK
SQ  KTVYRWGEFPNKKETEQNKKEDNPVQYETFLSSNFNSEKYVNDLFTHKTDQQATVHLQYLENRKLGCIDHLKKDVYKNHL
SQ  IFIGASKEIANSEVDMLDFRNLISDYGNVMSSLQNISISWDHYKVKKSGKIDFEPLSPATEPIQWLTTAPNELSVSIEQR
SQ  EFEVAVGLVEKINKIYESNPKVEIVMQTHPLKDQIENKVKILTDKLMNELRSPLLKANQIKDTISLLVRLSQNDKAKSIF
SQ  LESRSHSINQAIKKIVFSGDLNRFIGELARVIFNSINSTCNDFTNSFPSYMNSGLVSWIIEELVLISDIFNRQVFILDNF
SQ  YSISQAIRIIESHCEMMDQTGLSIGFYWNLLLQPHVEQLIVNYEIKIRDSMLHQLMDEKWNGVSNWDYEVKSQLNSLPSS
SQ  LKNSGTPNSGGSGISNNNSNNNNNYQSPIINNNFNSGGGNKKIGLTFQQMHQDNLNNMEDIDQGRLKLTSSTIFLNTIIQ
SQ  KFAIDICQIITIDLIPVISQSLGSIFKDYMSYLKNEIQKEYLSDTQCLAIISDSVYIVDDLVSRIATRFEDATGEKLNNL
SQ  TQLSSLLYSYFESIRDQYSTRKALELVDNSMNWEEQEYQVEEELDPFPKNFIVLSEALDRLAESIQTNVNVESVLPIASR
SQ  IISEIVNIISNRFESTSNLVFGYGGLQHFILEMKYLATFAGKYPVEDSTFELINTMIRNHKEIYLNNTSDPKPLKTEEYF
SQ  TSIIDNLVYQKAVYN
//
ID  Q8IYI6;
PN  Exocyst complex component 8;
GN  EXOC8;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}. Note=Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Localizes at the leading edge of migrating cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O54924}.
DR  UNIPROT: Q8IYI6;
DR  UNIPROT: B3KU33;
DR  UNIPROT: Q5TE82;
DR  Pfam: PF16528;
DR  PROSITE: PS50003;
DR  OMIM: 615283;
DR  OMIM: 619076;
DR  DisGeNET: 149371;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
DE  Disease: Neurodevelopmental disorder with microcephaly, seizures, and brain atrophy (NEDMISB) [MIM:619076]: An autosomal recessive neurodevelopmental disorder characterized by severe global developmental delay, developmental regression with loss of milestones, severe microcephaly, and brain abnormalities, primarily cerebral atrophy and hypoplasia of the corpus callosum. Affected individuals develop seizures in the first year of life. Death in childhood may occur. {ECO:0000269|PubMed:32103185}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O60645; IntAct: EBI-21672932; Score: 0.51
DE  Interaction: P00533; IntAct: EBI-10764512; Score: 0.40
DE  Interaction: P05783; IntAct: EBI-756712; Score: 0.37
DE  Interaction: Q7Z3B4; IntAct: EBI-24565174; Score: 0.56
DE  Interaction: Q8N6Y0; IntAct: EBI-760525; Score: 0.70
DE  Interaction: P35900; IntAct: EBI-753154; Score: 0.37
DE  Interaction: O75478; IntAct: EBI-753181; Score: 0.37
DE  Interaction: P19012; IntAct: EBI-753475; Score: 0.37
DE  Interaction: O14964; IntAct: EBI-754885; Score: 0.37
DE  Interaction: Q9UL45; IntAct: EBI-756178; Score: 0.67
DE  Interaction: P08727; IntAct: EBI-756208; Score: 0.67
DE  Interaction: Q15154; IntAct: EBI-24482767; Score: 0.56
DE  Interaction: Q15834; IntAct: EBI-758167; Score: 0.37
DE  Interaction: Q8TBN0; IntAct: EBI-2349923; Score: 0.49
DE  Interaction: Q9NS73; IntAct: EBI-10263400; Score: 0.56
DE  Interaction: Q5JST6; IntAct: EBI-2349935; Score: 0.49
DE  Interaction: P46736; IntAct: EBI-2510058; Score: 0.40
DE  Interaction: Q14457; IntAct: EBI-3506822; Score: 0.60
DE  Interaction: Q8CDJ3; IntAct: EBI-3506734; Score: 0.40
DE  Interaction: Q80U62; IntAct: EBI-3506709; Score: 0.40
DE  Interaction: Q96A65; IntAct: EBI-3509957; Score: 0.73
DE  Interaction: Q4R379; IntAct: EBI-3509942; Score: 0.35
DE  Interaction: A8K0Z3; IntAct: EBI-9075672; Score: 0.55
DE  Interaction: Q14247; IntAct: EBI-9075593; Score: 0.27
DE  Interaction: Q8VDD8; IntAct: EBI-9075562; Score: 0.27
DE  Interaction: Q15323; IntAct: EBI-10263378; Score: 0.56
DE  Interaction: Q8IYX8; IntAct: EBI-10263388; Score: 0.56
DE  Interaction: Q9UKT9; IntAct: EBI-10263412; Score: 0.78
DE  Interaction: P06428; IntAct: EBI-11738085; Score: 0.37
DE  Interaction: O00471; IntAct: EBI-12450093; Score: 0.64
DE  Interaction: Q8TAG9; IntAct: EBI-12450124; Score: 0.64
DE  Interaction: Q9Y2D4; IntAct: EBI-12450145; Score: 0.51
DE  Interaction: Q9UPT5; IntAct: EBI-12450194; Score: 0.51
DE  Interaction: Q9NV70; IntAct: EBI-12450194; Score: 0.51
DE  Interaction: P11234; IntAct: EBI-12451925; Score: 0.64
DE  Interaction: P14373; IntAct: EBI-24274457; Score: 0.56
DE  Interaction: Q9UBB9; IntAct: EBI-24277384; Score: 0.56
DE  Interaction: Q9Y250; IntAct: EBI-24282357; Score: 0.56
DE  Interaction: P20807; IntAct: EBI-24310203; Score: 0.56
DE  Interaction: P29084; IntAct: EBI-24320917; Score: 0.56
DE  Interaction: Q8TD31; IntAct: EBI-24326974; Score: 0.56
DE  Interaction: Q9H9H4; IntAct: EBI-24338768; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-24339832; Score: 0.56
DE  Interaction: P15884; IntAct: EBI-24339961; Score: 0.56
DE  Interaction: Q15742; IntAct: EBI-24480518; Score: 0.56
DE  Interaction: Q9H2G9; IntAct: EBI-24488250; Score: 0.56
DE  Interaction: Q99081; IntAct: EBI-24492403; Score: 0.56
DE  Interaction: Q13155; IntAct: EBI-24501654; Score: 0.56
DE  Interaction: P19474; IntAct: EBI-24506936; Score: 0.56
DE  Interaction: Q6AI39; IntAct: EBI-24508160; Score: 0.56
DE  Interaction: Q9H992; IntAct: EBI-24511640; Score: 0.56
DE  Interaction: O76013; IntAct: EBI-24527203; Score: 0.60
DE  Interaction: Q9NU19; IntAct: EBI-24617208; Score: 0.56
DE  Interaction: Q5EBL2; IntAct: EBI-23729583; Score: 0.56
DE  Interaction: Q6GMQ7; IntAct: EBI-23732828; Score: 0.56
DE  Interaction: Q6ZMJ2; IntAct: EBI-24703615; Score: 0.56
DE  Interaction: O00472; IntAct: EBI-24709958; Score: 0.56
DE  Interaction: Q9BRT2; IntAct: EBI-23790765; Score: 0.56
DE  Interaction: Q969W8; IntAct: EBI-23791595; Score: 0.56
DE  Interaction: Q9NTX9; IntAct: EBI-23801072; Score: 0.56
DE  Interaction: Q9BVN2; IntAct: EBI-24739968; Score: 0.56
DE  Interaction: Q9NZ72; IntAct: EBI-24767700; Score: 0.56
DE  Interaction: Q16533; IntAct: EBI-24771824; Score: 0.56
DE  Interaction: Q9NPF5; IntAct: EBI-23881341; Score: 0.56
DE  Interaction: Q8NAM6; IntAct: EBI-23889434; Score: 0.56
DE  Interaction: Q6QNY1; IntAct: EBI-25276513; Score: 0.56
DE  Interaction: Q9ULR0; IntAct: EBI-24803153; Score: 0.56
DE  Interaction: Q9BSW7; IntAct: EBI-23914736; Score: 0.56
DE  Interaction: Q9BYV2; IntAct: EBI-24396533; Score: 0.56
DE  Interaction: Q96GS4; IntAct: EBI-24401384; Score: 0.56
DE  Interaction: Q8IYA8; IntAct: EBI-24409360; Score: 0.56
DE  Interaction: Q5T5P2; IntAct: EBI-24413377; Score: 0.56
DE  Interaction: P0CG20; IntAct: EBI-24420156; Score: 0.56
DE  Interaction: Q9BVG8; IntAct: EBI-24423104; Score: 0.56
DE  Interaction: Q8N0S2; IntAct: EBI-24423729; Score: 0.56
DE  Interaction: Q01546; IntAct: EBI-24425129; Score: 0.56
DE  Interaction: O14777; IntAct: EBI-24431662; Score: 0.56
DE  Interaction: Q8TD10; IntAct: EBI-24438784; Score: 0.56
DE  Interaction: Q70EL1; IntAct: EBI-24446451; Score: 0.56
DE  Interaction: Q14142; IntAct: EBI-24450438; Score: 0.56
DE  Interaction: O76011; IntAct: EBI-24458571; Score: 0.56
DE  Interaction: Q5JR59; IntAct: EBI-24470046; Score: 0.56
DE  Interaction: Q6NUQ1; IntAct: EBI-24477001; Score: 0.56
DE  Interaction: Q9Y6H3; IntAct: EBI-24545393; Score: 0.56
DE  Interaction: Q6IC98; IntAct: EBI-24560187; Score: 0.56
DE  Interaction: Q96GY0; IntAct: EBI-24575784; Score: 0.56
DE  Interaction: A0A1U9X8X8; IntAct: EBI-24595565; Score: 0.56
DE  Interaction: Q8N2N9; IntAct: EBI-24597123; Score: 0.56
DE  Interaction: Q9BYU1; IntAct: EBI-24633510; Score: 0.56
DE  Interaction: Q9BXY8; IntAct: EBI-25154342; Score: 0.56
DE  Interaction: Q8WWY6; IntAct: EBI-24659479; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-25181664; Score: 0.56
DE  Interaction: Q8TDC0; IntAct: EBI-24773710; Score: 0.56
DE  Interaction: P13682; IntAct: EBI-24790242; Score: 0.56
DE  Interaction: Q96DF8; IntAct: EBI-24799511; Score: 0.56
DE  Interaction: Q13360; IntAct: EBI-25211267; Score: 0.56
DE  Interaction: P03427; IntAct: EBI-14405248; Score: 0.35
DE  Interaction: P61006; IntAct: EBI-11909914; Score: 0.00
DE  Interaction: Q96KP1; IntAct: EBI-21672932; Score: 0.51
DE  Interaction: Q8N7X8; IntAct: EBI-21585341; Score: 0.35
DE  Interaction: P21709; IntAct: EBI-21595997; Score: 0.35
DE  Interaction: P27930; IntAct: EBI-21662122; Score: 0.35
DE  Interaction: Q9Y3L3; IntAct: EBI-21672932; Score: 0.35
DE  Interaction: Q9NX40; IntAct: EBI-21672932; Score: 0.35
DE  Interaction: Q9H4M9; IntAct: EBI-21672932; Score: 0.35
DE  Interaction: Q9H223; IntAct: EBI-21672932; Score: 0.35
DE  Interaction: Q15345; IntAct: EBI-21672932; Score: 0.35
DE  Interaction: Q13136; IntAct: EBI-21672932; Score: 0.35
DE  Interaction: Q12981; IntAct: EBI-21672932; Score: 0.35
DE  Interaction: O14975; IntAct: EBI-21672932; Score: 0.35
DE  Interaction: O75131; IntAct: EBI-20901088; Score: 0.40
DE  Interaction: P82914; IntAct: EBI-20903504; Score: 0.40
DE  Interaction: P46781; IntAct: EBI-20932336; Score: 0.40
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P19739; IntAct: EBI-25685423; Score: 0.35
GO  GO:0031252;
GO  GO:0005829;
GO  GO:0000145;
GO  GO:0030426;
GO  GO:0005770;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0035091;
GO  GO:0031267;
GO  GO:0007032;
GO  GO:0006887;
GO  GO:0022617;
GO  GO:0006893;
GO  GO:0090148;
GO  GO:0000281;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:0016241;
GO  GO:0006904;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMAMSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRIQALAEETAQNLKRNVYQNYRQFIETAREISYL
SQ  ESEMYQLSHLLTEQKSSLESIPLTLLPAAAAAGAAAASGGEEGVGGAGGRDHLRGQAGFFSTPGGASRDGSGPGEEGKQR
SQ  TLTTLLEKVEGCRHLLETPGQYLVYNGDLVEYDADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYSLDGLAVVN
SQ  VKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEDTKRALSEKRRREQEEAAAPRGPPQVTSKATNPFEDDEEEEP
SQ  AVPEVEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRAKVEERVRQLTEVLVFELSP
SQ  DRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFEIDFAG
SQ  TDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGDIGLDLTFIIHALLVKDIQGALHSYKE
SQ  IIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELH
SQ  MVLLESLVEIILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVEKRFEEGVGKPAKQLQDLRNASRLIRVNPES
SQ  TTSVV
//
ID  Q6PGF7;
PN  Exocyst complex component 8;
GN  Exoc8;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}. Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (By similarity). Localizes at the leading edge of migrating cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O54924}.
DR  UNIPROT: Q6PGF7;
DR  Pfam: PF16528;
DR  PROSITE: PS50003;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q91VJ1; IntAct: EBI-6253412; Score: 0.27
DE  Interaction: Q9EPB4; IntAct: EBI-6253421; Score: 0.27
GO  GO:0031252;
GO  GO:0000145;
GO  GO:0030426;
GO  GO:0005770;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0035091;
GO  GO:0031267;
GO  GO:0007032;
GO  GO:0006887;
GO  GO:0022617;
GO  GO:0006893;
GO  GO:0090148;
GO  GO:0000281;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:0006904;
GO  GO:0090522;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRVQALAEETAQNLKRNVYQNYRQFIETAREISYLESEM
SQ  YQLSHLLTEQKSSLESIPLALLPAAAAGASAGEDTAGAGPRERGAVQAGFLPGPAGVPREGSGTGEEGKQRTLTTLLEKV
SQ  EGCRDLLETPGQYLVYNGDLVEYDADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKD
SQ  MFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSDKRRREQEEAAAPRAPPPVTSKGSNPFEDEDDEELATPEAEEEK
SQ  VDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPPVKELRAKVDERVRQLTEVLVFELSPDRSLRGGPK
SQ  ATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAF
SQ  VVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGEIGLDLTFIIHALLVKDIQGALHSYKEIIIEATKHR
SQ  NSEEMWRRMNLMTPEALGKLKEEMKSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVE
SQ  IILVAVQHVDYSLRCEQDPEKKAFIRQNASFLYETVLPVVERRFEEGVGKPAKQLQDLRNASRLLRVNPESTTSVV
//
ID  O54924;
PN  Exocyst complex component 8;
GN  Exoc8;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12954101}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12954101}. Cell projection, growth cone {ECO:0000269|PubMed:12954101}. Cell projection {ECO:0000269|PubMed:21658605}. Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (PubMed:12954101). Localizes at the leading edge of migrating cells (PubMed:21658605). {ECO:0000250, ECO:0000269|PubMed:12954101, ECO:0000269|PubMed:21658605}.
DR  UNIPROT: O54924;
DR  PDB: 1ZC3;
DR  PDB: 1ZC4;
DR  Pfam: PF16528;
DR  PROSITE: PS50003;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
DE  Reference Proteome: Yes;
GO  GO:0031252;
GO  GO:0000145;
GO  GO:0030426;
GO  GO:0005770;
GO  GO:0048471;
GO  GO:0035091;
GO  GO:0031267;
GO  GO:0007032;
GO  GO:0006887;
GO  GO:0022617;
GO  GO:0006893;
GO  GO:0008104;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRVQALAEETAQNLKRNVYQNYRQFIETAREISYLESEM
SQ  YQLSHLLTEQKSSLESIPLALLPAAAAGASTGEDTAGAGPRERGAAQAGFLPGPAGVPREGPGTGEEGKQRTLTTLLEKV
SQ  EGCRDLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKD
SQ  MFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSDKRRREQEEAAALRAPPPVTSKGSNPFEDEAEEELATPEAEEEK
SQ  VDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPSVKELRAKVDERVRQLTEVLVFELSPDRSLRGGPK
SQ  ATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAF
SQ  VVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGEIGLDLTFIIHALLVKDIQGALLSYKEIIIEATKHR
SQ  NSEEMWRRMNLMTPEALGKLKEEMRSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVE
SQ  VILVAVQHVDYSLRCEQDPEKKTFIRQNASFLYDTVLPVVERRFEEGVGKPAKQLQDLRNASRLLRVNPESTTSVV
//
ID  Q5U247;
PN  Exocyst complex component 8;
GN  exoc8;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O54924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54924}. Cell projection {ECO:0000250|UniProtKB:O54924}.
DR  UNIPROT: Q5U247;
DR  Pfam: PF16528;
DR  PROSITE: PS50003;
DE  Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000145;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0006887;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEGGGSVQRLRRQLESNSFQAEQYVKLLSQQSDGDRDLQEHRQRIQSLADETAQSLKRNVYQNYRQFIETAKEISYLEG
SQ  EMYQLSHILTEQKSIMESVTQALLYTDRSEAARELQTAFPKEAEEGKVRNLTTLLEKVEGCKNLLETPGRYLVYNGDLTE
SQ  FDVDNMALIQKVHAFLMNDCLLIATSVPNRRGIYKYNALHNLDDLAVVNVKENPPMKDMFKILMFPESRIFQAENAKIKK
SQ  EWLEILEQTKKNKALNEKQKQEETTPQLPVVPEIPANPFIDEDGTFDEVEVDLTIDWIQELPEDLDVCIAQRNFEGAVDL
SQ  LDKLNSYLEDKPLTHPVKELKSKVDERVRQLTDVLVFELSPDRSLRGGPKATRRAVSQLVRLGQSTKACELFLKNQAAAV
SQ  QTAIRQLRIEGATLLYIHKLCNVFFTSLLETAKEFEMDFAENHGCYSAFIVWSRLALKMFVDAFSKQVFDSKESLSTVAE
SQ  CVKVAKEHCKQLSEIGLDLTFILHTLLVKDIKAALQSYKDIVIEATKHRNSEEMWRRMNLMTPEVLGKLREEMRNCGINN
SQ  FDQYTGDDCWVNISYTIVAFTKQTMAFLEEALKLYFPELHMVLLECLMEIILVAIQHVDYSLRCEQESEKKAFIRQNASF
SQ  LYENVLVVVEKRFEEGVGKPAKQLQELRNSSRLVRVNPESTTSVV
//
ID  A8E639;
PN  Myelin-associated neurite-outgrowth inhibitor;
GN  FAM168B;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000250|UniProtKB:Q80XQ8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80XQ8}. Cell projection, axon {ECO:0000250|UniProtKB:Q80XQ8}. Note=Expressed in neuronal cell bodies and axonal fibers. {ECO:0000250|UniProtKB:Q80XQ8}.
DR  UNIPROT: A8E639;
DR  UNIPROT: F1MAZ2;
DR  Pfam: PF14944;
DE  Function: Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27. {ECO:0000250|UniProtKB:D4AEP3}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYPGANPTFQAGYTSGTPYKVSCSPTSGAVPPYSSSPNPY
SQ  QTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPLPPPRGNGVTMGMVAGTTMAMSAGT
SQ  LLTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW
//
ID  Q08BY2;
PN  Myelin-associated neurite-outgrowth inhibitor;
GN  fam168b;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000250|UniProtKB:D4AEP3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D4AEP3}. Cell projection, axon {ECO:0000250|UniProtKB:D4AEP3}.
DR  UNIPROT: Q08BY2;
DR  Pfam: PF14944;
DE  Function: Inhibitor of neuronal axonal outgrowth. {ECO:0000250|UniProtKB:D4AEP3}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNPVYSPASSGVPYANPKGIGYPAGFPVGYAAAAPAYSPSMYPGANPAFPSGYAPGTPFKMSCSPTTGAVPPYSSSPNPY
SQ  PAAVYPVRSPYPQQNPYAQQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPAAMYAPPIPPPRPNGVTMGMVGGTTMAMSAG
SQ  TLLTTHSPTPVAPHPSMPTYRQPATPTYSYVPPQW
//
ID  A1KXE4;
PN  Myelin-associated neurite-outgrowth inhibitor;
GN  FAM168B;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000250|UniProtKB:Q80XQ8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80XQ8}. Cell projection, axon {ECO:0000250|UniProtKB:Q80XQ8}. Note=Expressed in neuronal cell bodies and axonal fibers. {ECO:0000250|UniProtKB:Q80XQ8}.
DR  UNIPROT: A1KXE4;
DR  UNIPROT: Q2TAZ6;
DR  UNIPROT: Q6NZ40;
DR  Pfam: PF14944;
DR  DisGeNET: 130074;
DE  Function: Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27. {ECO:0000250|UniProtKB:D4AEP3}.
DE  Reference Proteome: Yes;
DE  Interaction: P0C762; IntAct: EBI-2622097; Score: 0.37
DE  Interaction: Q9UGN5; IntAct: EBI-7055170; Score: 0.44
DE  Interaction: Q9H6Z9; IntAct: EBI-24622894; Score: 0.56
DE  Interaction: Q96A09; IntAct: EBI-24509722; Score: 0.56
DE  Interaction: Q9BQY4; IntAct: EBI-24509960; Score: 0.56
DE  Interaction: Q15915; IntAct: EBI-24510851; Score: 0.56
DE  Interaction: Q9H0L4; IntAct: EBI-24513225; Score: 0.56
DE  Interaction: O75593; IntAct: EBI-24516068; Score: 0.56
DE  Interaction: Q6PEX3; IntAct: EBI-24517441; Score: 0.56
DE  Interaction: O95231; IntAct: EBI-24517283; Score: 0.56
DE  Interaction: P17482; IntAct: EBI-24518222; Score: 0.56
DE  Interaction: Q96K80; IntAct: EBI-24524781; Score: 0.56
DE  Interaction: Q9BZE0; IntAct: EBI-24526759; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-24528491; Score: 0.56
DE  Interaction: Q71SY5; IntAct: EBI-24532543; Score: 0.56
DE  Interaction: Q13227; IntAct: EBI-24609069; Score: 0.56
DE  Interaction: Q99932; IntAct: EBI-24608889; Score: 0.56
DE  Interaction: Q7Z3H4; IntAct: EBI-24616907; Score: 0.56
DE  Interaction: P78337; IntAct: EBI-24621384; Score: 0.56
DE  Interaction: P32242; IntAct: EBI-24631701; Score: 0.56
DE  Interaction: Q5T6F2; IntAct: EBI-24714983; Score: 0.56
DE  Interaction: Q96HA1; IntAct: EBI-24715141; Score: 0.56
DE  Interaction: P0CG20; IntAct: EBI-24793729; Score: 0.56
DE  Interaction: P33240; IntAct: EBI-25276276; Score: 0.56
DE  Interaction: Q9UQM7; IntAct: EBI-24444859; Score: 0.56
DE  Interaction: P14678; IntAct: EBI-24532872; Score: 0.56
DE  Interaction: A8MV65; IntAct: EBI-24535723; Score: 0.56
DE  Interaction: Q64LD2; IntAct: EBI-24535978; Score: 0.56
DE  Interaction: Q7Z5V6; IntAct: EBI-24537270; Score: 0.56
DE  Interaction: A5D8V6; IntAct: EBI-24543313; Score: 0.56
DE  Interaction: Q14119; IntAct: EBI-24545906; Score: 0.56
DE  Interaction: Q8IXL7; IntAct: EBI-24546845; Score: 0.56
DE  Interaction: Q01085; IntAct: EBI-24552897; Score: 0.56
DE  Interaction: Q14847; IntAct: EBI-24557301; Score: 0.56
DE  Interaction: O43251; IntAct: EBI-24559610; Score: 0.56
DE  Interaction: Q9ULV5; IntAct: EBI-24560739; Score: 0.56
DE  Interaction: Q7Z3K3; IntAct: EBI-24561135; Score: 0.56
DE  Interaction: O43711; IntAct: EBI-24564751; Score: 0.56
DE  Interaction: Q8TDC0; IntAct: EBI-24570617; Score: 0.56
DE  Interaction: Q12951; IntAct: EBI-24571134; Score: 0.56
DE  Interaction: O75909; IntAct: EBI-24574824; Score: 0.56
DE  Interaction: Q9HBE1; IntAct: EBI-24585617; Score: 0.56
DE  Interaction: Q01974; IntAct: EBI-24590730; Score: 0.56
DE  Interaction: Q03989; IntAct: EBI-24595017; Score: 0.56
DE  Interaction: P21549; IntAct: EBI-24595339; Score: 0.56
DE  Interaction: Q9BTL3; IntAct: EBI-24598895; Score: 0.56
DE  Interaction: Q14511; IntAct: EBI-24633779; Score: 0.56
DE  Interaction: Q8WU58; IntAct: EBI-24636945; Score: 0.56
DE  Interaction: Q9NQB0; IntAct: EBI-24637975; Score: 0.56
DE  Interaction: Q92567; IntAct: EBI-24639575; Score: 0.56
DE  Interaction: O95817; IntAct: EBI-24640942; Score: 0.56
DE  Interaction: P09234; IntAct: EBI-24758025; Score: 0.56
DE  Interaction: Q8IVT5; IntAct: EBI-14035664; Score: 0.35
DE  Interaction: Q9BYX4; IntAct: EBI-20206253; Score: 0.35
DE  Interaction: P17813; IntAct: EBI-22197897; Score: 0.35
DE  Interaction: P22607; IntAct: EBI-25855324; Score: 0.56
DE  Interaction: O14901; IntAct: EBI-25906201; Score: 0.56
DE  Interaction: Q9BVL2; IntAct: EBI-25908575; Score: 0.56
GO  GO:0030424;
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYPGANPTFQTGYTPGTPYKVSCSPTSGAVPPYSSSPNPY
SQ  QTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPIPPPRGNGVTMGMVAGTTMAMSAGT
SQ  LLTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW
//
ID  Q80XQ8;
PN  Myelin-associated neurite-outgrowth inhibitor;
GN  Fam168b;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000269|PubMed:20716133}; Multi-pass membrane protein {ECO:0000269|PubMed:20716133}. Cell projection, axon {ECO:0000269|PubMed:20716133}. Note=Expressed in neuronal cell bodies and axonal fibers. {ECO:0000269|PubMed:20716133}.
DR  UNIPROT: Q80XQ8;
DR  UNIPROT: Q3UNC7;
DR  UNIPROT: Q5DTR7;
DR  Pfam: PF14944;
DE  Function: Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27. {ECO:0000269|PubMed:20716133}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNPVYSPGSSGVPYANAKGIGYPAGFPVGYAAAPAYSPNMYPGANPTFQTGYTPGTPYKVSCSPTSGAVPPYSSSPNPYQ
SQ  TAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPIPPPRGSGVTMGMVAGTTMAMSAGTL
SQ  LTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW
//
ID  D4AEP3;
PN  Myelin-associated neurite-outgrowth inhibitor;
GN  Fam168b;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:22771904}. Cell membrane {ECO:0000269|PubMed:22771904}; Multi-pass membrane protein {ECO:0000269|PubMed:22771904}. Cell projection, axon {ECO:0000269|PubMed:22771904}. Note=In cortical neurons, predominantly found at perinuclear regions. Expressed in neuronal cell bodies and axonal fibers. {ECO:0000269|PubMed:22771904}.
DR  UNIPROT: D4AEP3;
DR  Pfam: PF14944;
DE  Function: Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27. {ECO:0000269|PubMed:20716133}.
DE  Reference Proteome: Yes;
DE  Interaction: Q92567; IntAct: EBI-7957948; Score: 0.37
DE  Interaction: Q96QA6; IntAct: EBI-7958149; Score: 0.37
DE  Interaction: Q15038; IntAct: EBI-7958079; Score: 0.37
DE  Interaction: Q8IUR5; IntAct: EBI-7958221; Score: 0.37
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNPVYSPGSSGVPYANAKGIGYPAGFPVGYAAAPAYSPNMYPGANPTFQTGYTPGTPYKVSCSPTSGAVPPYSSSPNPYQ
SQ  TAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPIPPPRGSGVTMGMVAGTTMAMSAGTL
SQ  LTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW
//
ID  Q0IHC4;
PN  Myelin-associated neurite-outgrowth inhibitor;
GN  fam168b;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000250|UniProtKB:D4AEP3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D4AEP3}. Cell projection, axon {ECO:0000250|UniProtKB:D4AEP3}.
DR  UNIPROT: Q0IHC4;
DR  Pfam: PF14944;
DE  Function: Inhibitor of neuronal axonal outgrowth. {ECO:0000250|UniProtKB:D4AEP3}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYAGPNPAFQQELEHPAHVSSGVQMFMFGHAFSVARNGAI
SQ  PSGYTPGTPYKVSCSPTSGTVPPYSSSPNPYQTAVYPVRSAYPQQNPYAQQGAYYTQPFYAAPPHVIHHTTVVQPNGMPA
SQ  TMYPAPIQSPRGNGVAMGMVAGTTMAMSAGTLLTSHYPSPVAPQVTMPTYRPPGTPTYSYVPPQW
//
ID  Q0VFP2;
PN  Myelin-associated neurite-outgrowth inhibitor;
GN  fam168b;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000250|UniProtKB:D4AEP3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D4AEP3}. Cell projection, axon {ECO:0000250|UniProtKB:D4AEP3}.
DR  UNIPROT: Q0VFP2;
DR  Pfam: PF14944;
DE  Function: Inhibitor of neuronal axonal outgrowth. {ECO:0000250|UniProtKB:D4AEP3}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYAGPNPAFQPGYTPGTPYKVSCSPTSGTVPPYSSSPNPY
SQ  QTAVYPVRSAYPQQNPYAQQGAYYTQPLYAAPPHVIHHTTVVQPNGMPATMYPAPIPQPRGNGVAMGMVAGTTMAMSAGT
SQ  LLTSHYPTPVAPHQVTMPTYRPPGTPTYSYVPPQW
//
ID  Q9Y6X4;
PN  Soluble lamin-associated protein of 75 kDa;
GN  FAM169A;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:22412018}. Nucleus inner membrane {ECO:0000269|PubMed:22412018}; Peripheral membrane protein {ECO:0000269|PubMed:22412018}; Nucleoplasmic side {ECO:0000269|PubMed:22412018}. Note=Enriched at the nuclear lamina.
DR  UNIPROT: Q9Y6X4;
DR  UNIPROT: A8K1T9;
DR  UNIPROT: Q6MZT0;
DR  UNIPROT: Q9H989;
DR  OMIM: 615769;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P20700; IntAct: EBI-24534698; Score: 0.56
DE  Interaction: Q96QG7; IntAct: EBI-24348015; Score: 0.56
DE  Interaction: P02647; IntAct: EBI-1220621; Score: 0.35
DE  Interaction: P58166; IntAct: EBI-21648669; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: P62807; IntAct: EBI-25471348; Score: 0.27
GO  GO:0005637;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:22412018};
SQ  MAFPVDMLENCSHEELENSAEDYMSDLRCGDPENPECFSLLNITIPISLSNVGFVPLYGGDQTQKILALFAPEDSLTAVA
SQ  LYLADQWWAIDDIVKTSVPSREGLKQVSTLGERVVLYVLNRIIYRKQEMERNEIPFLCHSSTDYAKILWKKGEAIGFYSV
SQ  KPTGSICASFLTQSYQLPVLDTMFLRKKYRGKDFGLHMLEDFVDSFTEDALGLRYPLSSLMYTACKQYFEKYPGDHELLW
SQ  EVEGVGHWYQRIPVTRALQREALKILALSQNEPKRPMSGEYGPASVPEYEARTEDNQSSEMQLTIDSLKDAFASTSEGHD
SQ  KTSVSTHTRSGNLKRPKIGKRFQDSEFSSSQGEDEKTSQTSLTASINKLESTARPSESSEEFLEEEPEQRGIEFEDESSD
SQ  RDARPALETQPQQEKQDGEKESELEPMNGEIMDDSLKTSLITEEEDSTSEVLDEELKLQPFNSSEDSTNLVPLVVESSKP
SQ  PEVDAPDKTPRIPDSEMLMDEGTSDEKGHMEEKLSLLPRKKAHLGSSDNVATMSNEERSDGGFPNSVIAEFSEEPVSENL
SQ  SPNTTSSLEDQGEEGVSEPQETSTALPQSSLIEVELEDVPFSQNAGQKNQSEEQSEASSEQLDQFTQSAEKAVDSSSEEI
SQ  EVEVPVVDRRNLRRKAKGHKGPAKKKAKLT
//
ID  Q5XG69;
PN  Soluble lamin-associated protein of 75 kDa;
GN  Fam169a;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000250}. Nucleus inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Note=Enriched at the nuclear lamina. {ECO:0000250}.
DR  UNIPROT: Q5XG69;
DR  UNIPROT: E9Q0D7;
DR  UNIPROT: Q69ZW7;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005637;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAFPVDLLDNCTHEELENSSEDYLSSLRCGDPEHPECFSSLNITIPVSLSNVGFVPLYGGNQTQKILALFAPEDSLTAVA
SQ  LYLVGQWWAIDDIVKTSEPSREGLKQVSTLGERVVLYVLNRIIYRKQEMERNEIPFLCHSSTDYAKILWKKGEAVGFYSV
SQ  KPTGSLCASFLTQNYQLPVLDTMFIRKKYRGKDLGLHMLEDFVDSFTEDALGLRYPLSSLMYTASKQYFEKYPGDHELLW
SQ  EVEGVGHWHQRVPVTRALQREAIKATDVSQYEATRPVSGEYGLAAVPEHEPGLDDTQSSELQIHSLKDAFASTSEGPEKT
SQ  PVSTRTRSSHLKRPKIGKHFQDSEFSSSQGEDENVAKTSPTASVNKIEYAARTSESSEEFLEEEPEQGVIDFEDESGDKD
SQ  AQPALETQPRLQKQDGDKDSALEPVNGEVMDAALKPSLTTEDEDSTSEGLEEDLKVPPFNSSGEPGNPVPLVAESSKVPE
SQ  ATLAKTSPDTDSEMLIDQSPSDDKGHTEENLSPVSKKKTLLGSSDNVATVSNIEKSDGNFPNSVVPEFPEEPVSQNLSPN
SQ  TTSSVEDQGEEGAPEAQEPSATQSSLIEVELEDAPFPQNAGQKSQSEEQSEASSEHLEQFTQSAEKAVDSSSEEIEVEVP
SQ  VVDRRNLRRKAKGHKGPGKKKAKLT
//
ID  Q5JX71;
PN  Protein FAM209A;
GN  FAM209A;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:A2APA5}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: Q5JX71;
DR  UNIPROT: Q05C43;
DR  Pfam: PF15206;
DE  Function: May play a role in sperm acrosome biogenesis. {ECO:0000250|UniProtKB:A2APA5}.
DE  Reference Proteome: Yes;
DE  Interaction: P50402; IntAct: EBI-24763501; Score: 0.56
DE  Interaction: Q12982; IntAct: EBI-25279273; Score: 0.56
DE  Interaction: Q15125; IntAct: EBI-24758742; Score: 0.56
DE  Interaction: Q53HI1; IntAct: EBI-24651712; Score: 0.56
DE  Interaction: Q5BJF2; IntAct: EBI-24745243; Score: 0.56
DE  Interaction: P30519; IntAct: EBI-24659762; Score: 0.56
DE  Interaction: Q9BXJ8; IntAct: EBI-24660892; Score: 0.56
DE  Interaction: Q92482; IntAct: EBI-24661914; Score: 0.56
DE  Interaction: P55061; IntAct: EBI-24663858; Score: 0.56
DE  Interaction: Q6UXB4; IntAct: EBI-24665193; Score: 0.56
DE  Interaction: Q96F05; IntAct: EBI-24665171; Score: 0.56
DE  Interaction: P24593; IntAct: EBI-24667567; Score: 0.56
DE  Interaction: Q8NBD8; IntAct: EBI-24669580; Score: 0.56
DE  Interaction: Q7Z2K6; IntAct: EBI-24669534; Score: 0.56
DE  Interaction: B2RUZ4; IntAct: EBI-24670029; Score: 0.56
DE  Interaction: Q14508; IntAct: EBI-24673017; Score: 0.56
DE  Interaction: Q7Z769; IntAct: EBI-24674473; Score: 0.56
DE  Interaction: O14931; IntAct: EBI-24674574; Score: 0.56
DE  Interaction: Q9BQB6; IntAct: EBI-24675452; Score: 0.56
DE  Interaction: Q8NHY0; IntAct: EBI-24675781; Score: 0.56
DE  Interaction: P43628; IntAct: EBI-24677593; Score: 0.56
DE  Interaction: Q8WVV5; IntAct: EBI-24677762; Score: 0.56
DE  Interaction: O60883; IntAct: EBI-24678057; Score: 0.56
DE  Interaction: Q9GZX9; IntAct: EBI-24678373; Score: 0.56
DE  Interaction: P01350; IntAct: EBI-24680641; Score: 0.56
DE  Interaction: Q96FZ5; IntAct: EBI-24681115; Score: 0.56
DE  Interaction: Q8WWP7; IntAct: EBI-24683139; Score: 0.56
DE  Interaction: O75063; IntAct: EBI-24683555; Score: 0.56
DE  Interaction: Q5VZY2; IntAct: EBI-24686702; Score: 0.56
DE  Interaction: Q96LB9; IntAct: EBI-24687412; Score: 0.56
DE  Interaction: Q92520; IntAct: EBI-24688381; Score: 0.56
DE  Interaction: Q96GQ5; IntAct: EBI-24692371; Score: 0.56
DE  Interaction: P23560; IntAct: EBI-23726439; Score: 0.56
DE  Interaction: Q9UPQ8; IntAct: EBI-24693724; Score: 0.56
DE  Interaction: Q8WVX3; IntAct: EBI-24694786; Score: 0.56
DE  Interaction: Q9Y5U4; IntAct: EBI-24696764; Score: 0.56
DE  Interaction: Q9HAB3; IntAct: EBI-24696666; Score: 0.56
DE  Interaction: P57739; IntAct: EBI-24697673; Score: 0.56
DE  Interaction: I3L0A0; IntAct: EBI-24698635; Score: 0.56
DE  Interaction: O14653; IntAct: EBI-24698512; Score: 0.56
DE  Interaction: Q969Y0; IntAct: EBI-24699463; Score: 0.56
DE  Interaction: Q9NV29; IntAct: EBI-24699387; Score: 0.56
DE  Interaction: P02724; IntAct: EBI-24701121; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-24703342; Score: 0.56
DE  Interaction: Q9NPR9; IntAct: EBI-24703316; Score: 0.56
DE  Interaction: P01375; IntAct: EBI-24703711; Score: 0.56
DE  Interaction: P54315; IntAct: EBI-24703665; Score: 0.56
DE  Interaction: Q8IY49; IntAct: EBI-24703604; Score: 0.56
DE  Interaction: Q8TBB6; IntAct: EBI-24704053; Score: 0.56
DE  Interaction: P30536; IntAct: EBI-24704355; Score: 0.56
DE  Interaction: Q8IY26; IntAct: EBI-24705960; Score: 0.56
DE  Interaction: Q9BQJ4; IntAct: EBI-24706026; Score: 0.56
DE  Interaction: Q9Y6D0; IntAct: EBI-24706768; Score: 0.56
DE  Interaction: Q8N2M4; IntAct: EBI-24707299; Score: 0.56
DE  Interaction: Q5BJH2; IntAct: EBI-24708034; Score: 0.56
DE  Interaction: Q8NHS1; IntAct: EBI-24708497; Score: 0.56
DE  Interaction: Q1RMY5; IntAct: EBI-24709934; Score: 0.56
DE  Interaction: Q9Y6X1; IntAct: EBI-24711058; Score: 0.56
DE  Interaction: A5D903; IntAct: EBI-24711648; Score: 0.56
DE  Interaction: Q71RG4; IntAct: EBI-24711927; Score: 0.56
DE  Interaction: P60033; IntAct: EBI-24716011; Score: 0.56
DE  Interaction: O14735; IntAct: EBI-24717599; Score: 0.56
DE  Interaction: P02808; IntAct: EBI-24718795; Score: 0.56
DE  Interaction: Q8TBE7; IntAct: EBI-24719810; Score: 0.56
DE  Interaction: P37268; IntAct: EBI-24720377; Score: 0.56
DE  Interaction: Q8NHW4; IntAct: EBI-24720728; Score: 0.56
DE  Interaction: P41732; IntAct: EBI-24721505; Score: 0.56
DE  Interaction: Q969S6; IntAct: EBI-24723426; Score: 0.56
DE  Interaction: Q8WVQ1; IntAct: EBI-24724764; Score: 0.56
DE  Interaction: Q9C0I4; IntAct: EBI-24726005; Score: 0.56
DE  Interaction: Q04941; IntAct: EBI-24726747; Score: 0.56
DE  Interaction: P29033; IntAct: EBI-24727519; Score: 0.56
DE  Interaction: O75396; IntAct: EBI-24727475; Score: 0.56
DE  Interaction: Q96EC8; IntAct: EBI-24727308; Score: 0.56
DE  Interaction: Q8IXM6; IntAct: EBI-24729136; Score: 0.56
DE  Interaction: Q9NZ01; IntAct: EBI-24728923; Score: 0.56
DE  Interaction: P11836; IntAct: EBI-24729270; Score: 0.56
DE  Interaction: Q96I45; IntAct: EBI-24729879; Score: 0.56
DE  Interaction: Q96IW7; IntAct: EBI-24731532; Score: 0.56
DE  Interaction: Q5W0B7; IntAct: EBI-24732788; Score: 0.56
DE  Interaction: Q9NZG7; IntAct: EBI-24733776; Score: 0.56
DE  Interaction: Q8TBM7; IntAct: EBI-24734476; Score: 0.56
DE  Interaction: Q86WK9; IntAct: EBI-24735695; Score: 0.56
DE  Interaction: P29972; IntAct: EBI-24741655; Score: 0.56
DE  Interaction: P19397; IntAct: EBI-24741916; Score: 0.56
DE  Interaction: O60636; IntAct: EBI-24741870; Score: 0.56
DE  Interaction: Q9UHJ9; IntAct: EBI-24743958; Score: 0.56
DE  Interaction: Q9H2L4; IntAct: EBI-24744254; Score: 0.56
DE  Interaction: Q15848; IntAct: EBI-24744581; Score: 0.56
DE  Interaction: A0A0C4DFN3; IntAct: EBI-24748093; Score: 0.56
DE  Interaction: Q8TAF8; IntAct: EBI-24748474; Score: 0.56
DE  Interaction: Q9UHX3; IntAct: EBI-24750533; Score: 0.56
DE  Interaction: Q69YG0; IntAct: EBI-24750810; Score: 0.56
DE  Interaction: Q9NS64; IntAct: EBI-24755295; Score: 0.56
DE  Interaction: Q6PI78; IntAct: EBI-24755815; Score: 0.56
DE  Interaction: Q9NS71; IntAct: EBI-24755725; Score: 0.56
DE  Interaction: Q7Z7B8; IntAct: EBI-24763350; Score: 0.56
DE  Interaction: Q8N912; IntAct: EBI-24765153; Score: 0.56
DE  Interaction: O95183; IntAct: EBI-24766009; Score: 0.56
DE  Interaction: Q96S97; IntAct: EBI-24767098; Score: 0.56
DE  Interaction: Q4VAQ0; IntAct: EBI-24768660; Score: 0.56
DE  Interaction: Q13635; IntAct: EBI-24769357; Score: 0.56
DE  Interaction: P29034; IntAct: EBI-24770320; Score: 0.56
DE  Interaction: Q5QGT7; IntAct: EBI-24771029; Score: 0.56
DE  Interaction: Q9HCP6; IntAct: EBI-24771241; Score: 0.56
DE  Interaction: O14493; IntAct: EBI-24771780; Score: 0.56
DE  Interaction: P41181; IntAct: EBI-24771883; Score: 0.56
DE  Interaction: Q9H3K2; IntAct: EBI-24773001; Score: 0.56
DE  Interaction: P02656; IntAct: EBI-24778709; Score: 0.56
DE  Interaction: Q9GZY8; IntAct: EBI-24778858; Score: 0.56
DE  Interaction: Q9BVK2; IntAct: EBI-24779310; Score: 0.56
DE  Interaction: Q8IWU4; IntAct: EBI-24780535; Score: 0.56
DE  Interaction: Q92903; IntAct: EBI-24780869; Score: 0.56
DE  Interaction: Q7L5A8; IntAct: EBI-24781569; Score: 0.56
DE  Interaction: O75379; IntAct: EBI-24782054; Score: 0.56
DE  Interaction: Q86W74; IntAct: EBI-24782320; Score: 0.56
DE  Interaction: P05090; IntAct: EBI-24782399; Score: 0.56
DE  Interaction: O14569; IntAct: EBI-24783279; Score: 0.56
DE  Interaction: P26678; IntAct: EBI-24784407; Score: 0.56
DE  Interaction: P02786; IntAct: EBI-24784925; Score: 0.56
DE  Interaction: A6NDP7; IntAct: EBI-24785107; Score: 0.56
DE  Interaction: O95674; IntAct: EBI-24793784; Score: 0.56
DE  Interaction: Q7Z4F1; IntAct: EBI-24793953; Score: 0.56
DE  Interaction: Q15546; IntAct: EBI-24794093; Score: 0.56
DE  Interaction: Q9P0N8; IntAct: EBI-24794270; Score: 0.56
DE  Interaction: Q8N609; IntAct: EBI-24795904; Score: 0.56
DE  Interaction: O95393; IntAct: EBI-24798213; Score: 0.56
DE  Interaction: P13987; IntAct: EBI-25276491; Score: 0.56
DE  Interaction: P40313; IntAct: EBI-25276423; Score: 0.56
DE  Interaction: Q59EV6; IntAct: EBI-25276813; Score: 0.56
DE  Interaction: Q8N6F1; IntAct: EBI-25277574; Score: 0.56
DE  Interaction: Q8N661; IntAct: EBI-25278338; Score: 0.56
DE  Interaction: Q9HDC9; IntAct: EBI-25279172; Score: 0.56
DE  Interaction: P21964; IntAct: EBI-25279786; Score: 0.56
DE  Interaction: P29400; IntAct: EBI-25280159; Score: 0.56
DE  Interaction: P56557; IntAct: EBI-25280653; Score: 0.56
DE  Interaction: Q02094; IntAct: EBI-25281444; Score: 0.56
DE  Interaction: Q9BQS2; IntAct: EBI-25281434; Score: 0.56
DE  Interaction: Q9H2S6; IntAct: EBI-25282993; Score: 0.56
DE  Interaction: O95968; IntAct: EBI-25283181; Score: 0.56
DE  Interaction: Q9NRS4; IntAct: EBI-25283685; Score: 0.56
DE  Interaction: Q8TDV0; IntAct: EBI-25284292; Score: 0.56
DE  Interaction: Q9Y5Z9; IntAct: EBI-25285255; Score: 0.56
DE  Interaction: Q4LDR2; IntAct: EBI-25285389; Score: 0.56
DE  Interaction: Q9Y385; IntAct: EBI-25285367; Score: 0.56
DE  Interaction: Q01453; IntAct: EBI-25286025; Score: 0.56
DE  Interaction: Q9Y3D6; IntAct: EBI-25287586; Score: 0.56
DE  Interaction: P09601; IntAct: EBI-25287799; Score: 0.56
DE  Interaction: Q13190; IntAct: EBI-25288503; Score: 0.56
DE  Interaction: Q86UF1; IntAct: EBI-24641235; Score: 0.56
DE  Interaction: Q9UKR5; IntAct: EBI-24641314; Score: 0.56
DE  Interaction: Q9BTX3; IntAct: EBI-24641793; Score: 0.56
DE  Interaction: Q9BTV4; IntAct: EBI-24641558; Score: 0.56
DE  Interaction: Q5J8X5; IntAct: EBI-24642453; Score: 0.56
DE  Interaction: Q9NRQ5; IntAct: EBI-24642874; Score: 0.56
DE  Interaction: Q96LL9; IntAct: EBI-24643260; Score: 0.56
DE  Interaction: O75355; IntAct: EBI-24643214; Score: 0.56
DE  Interaction: Q9BUP3; IntAct: EBI-24643959; Score: 0.56
DE  Interaction: Q5NDL2; IntAct: EBI-24645284; Score: 0.56
DE  Interaction: Q96G79; IntAct: EBI-24646026; Score: 0.56
DE  Interaction: Q9BT09; IntAct: EBI-24647320; Score: 0.56
DE  Interaction: Q5J5C9; IntAct: EBI-24647994; Score: 0.56
DE  Interaction: Q9HD20; IntAct: EBI-24648696; Score: 0.56
DE  Interaction: Q8N138; IntAct: EBI-24649134; Score: 0.56
DE  Interaction: O43681; IntAct: EBI-24650187; Score: 0.56
DE  Interaction: Q9H0R3; IntAct: EBI-24650534; Score: 0.56
DE  Interaction: Q9H2C2; IntAct: EBI-24650290; Score: 0.56
DE  Interaction: P17152; IntAct: EBI-24650279; Score: 0.56
DE  Interaction: Q13323; IntAct: EBI-24651167; Score: 0.56
DE  Interaction: Q15836; IntAct: EBI-24651889; Score: 0.56
DE  Interaction: P60059; IntAct: EBI-24652003; Score: 0.56
DE  Interaction: Q12983; IntAct: EBI-24652350; Score: 0.56
DE  Interaction: A0PK05; IntAct: EBI-24652273; Score: 0.56
DE  Interaction: Q9BZW4; IntAct: EBI-24653078; Score: 0.56
DE  Interaction: P30301; IntAct: EBI-24653337; Score: 0.56
DE  Interaction: O14798; IntAct: EBI-24653654; Score: 0.56
DE  Interaction: P07306; IntAct: EBI-24655518; Score: 0.56
DE  Interaction: Q6UX40; IntAct: EBI-24656181; Score: 0.56
DE  Interaction: Q6RW13; IntAct: EBI-24657303; Score: 0.56
DE  Interaction: Q5BVD1; IntAct: EBI-24659602; Score: 0.56
DE  Interaction: Q14162; IntAct: EBI-24659536; Score: 0.56
DE  Interaction: Q14802; IntAct: EBI-24744695; Score: 0.56
DE  Interaction: O43169; IntAct: EBI-24745059; Score: 0.56
DE  Interaction: Q9Y6I9; IntAct: EBI-24758880; Score: 0.56
DE  Interaction: Q9BSE2; IntAct: EBI-24759294; Score: 0.56
DE  Interaction: P06681; IntAct: EBI-24759556; Score: 0.56
DE  Interaction: Q9NVC3; IntAct: EBI-24759878; Score: 0.56
DE  Interaction: P43005; IntAct: EBI-24761066; Score: 0.56
DE  Interaction: Q9BQE5; IntAct: EBI-24773951; Score: 0.56
DE  Interaction: A2RU14; IntAct: EBI-24774300; Score: 0.56
DE  Interaction: Q8WWT9; IntAct: EBI-24774991; Score: 0.56
DE  Interaction: Q9NWW5; IntAct: EBI-24775375; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-24776394; Score: 0.56
DE  Interaction: Q9UHE5; IntAct: EBI-24776145; Score: 0.56
DE  Interaction: Q9BQA9; IntAct: EBI-24776598; Score: 0.56
DE  Interaction: Q6UX06; IntAct: EBI-24777357; Score: 0.56
DE  Interaction: Q9Y228; IntAct: EBI-24787867; Score: 0.56
DE  Interaction: Q9BV81; IntAct: EBI-24788001; Score: 0.56
DE  Interaction: Q9NRC9; IntAct: EBI-24788293; Score: 0.56
DE  Interaction: Q13277; IntAct: EBI-24788844; Score: 0.56
DE  Interaction: O43759; IntAct: EBI-24789665; Score: 0.56
DE  Interaction: O95159; IntAct: EBI-24790231; Score: 0.56
DE  Interaction: Q9BU79; IntAct: EBI-24792203; Score: 0.56
DE  Interaction: Q9UBY5; IntAct: EBI-24792539; Score: 0.56
DE  Interaction: O75711; IntAct: EBI-24800001; Score: 0.56
DE  Interaction: P60201; IntAct: EBI-24802443; Score: 0.56
DE  Interaction: Q969F0; IntAct: EBI-24802386; Score: 0.56
DE  Interaction: P11686; IntAct: EBI-24803127; Score: 0.56
DE  Interaction: Q969S0; IntAct: EBI-24803316; Score: 0.56
DE  Interaction: O95406; IntAct: EBI-24804040; Score: 0.56
DE  Interaction: Q9P0S9; IntAct: EBI-24804775; Score: 0.56
DE  Interaction: Q8N5M9; IntAct: EBI-24804922; Score: 0.56
DE  Interaction: O75841; IntAct: EBI-24809719; Score: 0.56
DE  Interaction: Q96GC9; IntAct: EBI-24810789; Score: 0.56
DE  Interaction: Q9NVV5; IntAct: EBI-24810993; Score: 0.56
DE  Interaction: Q86XP6; IntAct: EBI-25266404; Score: 0.56
DE  Interaction: Q6UX34; IntAct: EBI-25267080; Score: 0.56
DE  Interaction: P21145; IntAct: EBI-25267772; Score: 0.56
DE  Interaction: Q9H115; IntAct: EBI-25269370; Score: 0.56
DE  Interaction: P78382; IntAct: EBI-25269850; Score: 0.56
DE  Interaction: O15155; IntAct: EBI-25270807; Score: 0.56
DE  Interaction: Q9NV12; IntAct: EBI-25270546; Score: 0.56
DE  Interaction: P07204; IntAct: EBI-25271156; Score: 0.56
DE  Interaction: Q9UNK0; IntAct: EBI-25271982; Score: 0.56
DE  Interaction: Q6Y1H2; IntAct: EBI-25273339; Score: 0.56
DE  Interaction: P61266; IntAct: EBI-25273755; Score: 0.56
DE  Interaction: Q8TF42; IntAct: EBI-21896717; Score: 0.40
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0030154;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MWTLKSSLVLLLCLTCSYAFMFSSLRQKTSEPQGKVQYGEHFRIRQNLPEHTQGWLGSKWLWLLFVVVPFVILQCQRDSE
SQ  KNKEQSPPGLRGGQLHSPLKKKRNASPNKDCAFNTLMELEVELMKFVSKVRNLKRAMATGSGSNLRLRKSEMPADPYHVT
SQ  ICEIWGEESSS
//
ID  Q5JX69;
PN  Protein FAM209B;
GN  FAM209B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:A2APA5}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: Q5JX69;
DR  UNIPROT: Q3KRB5;
DR  Pfam: PF15206;
DE  Function: May play a role in sperm acrosome biogenesis. {ECO:0000250|UniProtKB:A2APA5}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0030154;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MWTLKSSLVLLLCLTCSYAFMFSSLRQKTSEPQGKVPCGEHFRIRQNLPEHTQGWLGSKWLWLLFAVVPFVILQCQRDSE
SQ  KNKEQSPPGLRGFPFRTPLKKNQNASLYKDCVFNTLNELEVELLKFVSEVQNLKGAMATGSGSNLKLRRSEMPADPYHVT
SQ  ICKIWGEESSS
//
ID  A2APA5;
PN  Protein FAM209;
GN  Fam209;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:34471926}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: A2APA5;
DR  UNIPROT: Q9D9T2;
DR  Pfam: PF15206;
DE  Function: Required for sperm acrosome biogenesis. {ECO:0000269|PubMed:34471926}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0001675;
GO  GO:0007286;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRTLLRWCLFLSLCVSCACAFMFSSMREKTKESPGKVPCGGHFRIRQNLPENAQGWLGNKWLWLFVAIMIYVMLKFRGDG
SQ  ENKEQHPPGLRGCQLRSPPKKAQNISPSKDFTFNTLTQLEMELVKFVSKVRNLKVSMATNSNSRQQVPESPTNLYNNVTI
SQ  YEIWGEEDSE
//
ID  O75844;
PN  CAAX prenyl protease 1 homolog;
GN  ZMPSTE24;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000269|PubMed:23539603}. Nucleus inner membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000269|PubMed:23539603}. Early endosome {ECO:0000269|PubMed:35283811}. Late endosome {ECO:0000269|PubMed:35283811}.
DR  UNIPROT: O75844;
DR  UNIPROT: B3KQI7;
DR  UNIPROT: D3DPU7;
DR  UNIPROT: Q8NDZ8;
DR  UNIPROT: Q9UBQ2;
DR  PDB: 2YPT;
DR  PDB: 4AW6;
DR  PDB: 5SYT;
DR  PDB: 6BH8;
DR  Pfam: PF01435;
DR  Pfam: PF16491;
DR  OMIM: 275210;
DR  OMIM: 606480;
DR  OMIM: 608612;
DR  DisGeNET: 10269;
DE  Function: Transmembrane metalloprotease whose catalytic activity is critical for processing lamin A/LMNA on the inner nuclear membrane and clearing clogged translocons on the endoplasmic reticulum (PubMed:33315887, PubMed:33293369). Proteolytically removes the C- terminal three residues of farnesylated proteins. Plays also an antiviral role independently of its protease activity by restricting enveloped RNA and DNA viruses, including influenza A, Zika, Ebola, Sindbis, vesicular stomatitis, cowpox, and vaccinia (PubMed:28246125). Mechanistically, controls IFITM antiviral pathway to hinder viruses from breaching the endosomal barrier by modulating membrane fluidity (PubMed:35283811). {ECO:0000269|PubMed:28246125, ECO:0000269|PubMed:33293369, ECO:0000269|PubMed:33315887, ECO:0000269|PubMed:35283811}.
DE  Disease: Mandibuloacral dysplasia with type B lipodystrophy (MADB) [MIM:608612]: A form of mandibuloacral dysplasia, a rare progeroid disorder with clinical and genetic heterogeneity, characterized by growth retardation, craniofacial dysmorphic features due to distal bone resorption, musculoskeletal and skin abnormalities associated with lipodystrophy. MADB is a disease characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, joint contractures, and generalized lipodystrophy with loss of subcutaneous fat from the extremities, face, neck and trunk. {ECO:0000269|PubMed:12913070, ECO:0000269|PubMed:17152860, ECO:0000269|PubMed:18435794, ECO:0000269|PubMed:20814950}. Note=The disease is caused by variants affecting the gene represented in this entry. Restrictive dermopathy 1 (RSDM1) [MIM:275210]: An autosomal recessive form of restrictive dermopathy, a genodermatosis mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial dysmorphism, sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. {ECO:0000269|PubMed:15317753}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UET6; IntAct: EBI-1069131; Score: 0.00
DE  Interaction: P08473; IntAct: EBI-1389788; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: Q16666; IntAct: EBI-9995438; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: P06821; IntAct: EBI-12590819; Score: 0.50
DE  Interaction: C5E519; IntAct: EBI-12590830; Score: 0.50
DE  Interaction: Q6DPW5; IntAct: EBI-12590841; Score: 0.40
DE  Interaction: Q20MH8; IntAct: EBI-12590852; Score: 0.50
DE  Interaction: P29084; IntAct: EBI-21499432; Score: 0.35
DE  Interaction: Q13503; IntAct: EBI-21501670; Score: 0.35
DE  Interaction: Q99679; IntAct: EBI-21516430; Score: 0.35
DE  Interaction: Q6PEY0; IntAct: EBI-21551307; Score: 0.35
DE  Interaction: P22732; IntAct: EBI-21554490; Score: 0.35
DE  Interaction: Q8WTR4; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: P54219; IntAct: EBI-21609589; Score: 0.35
DE  Interaction: Q08AM6; IntAct: EBI-21634069; Score: 0.35
DE  Interaction: O00624; IntAct: EBI-21654627; Score: 0.35
DE  Interaction: Q9BVJ7; IntAct: EBI-21667644; Score: 0.35
DE  Interaction: Q02223; IntAct: EBI-21757502; Score: 0.35
DE  Interaction: Q86WS5; IntAct: EBI-21771386; Score: 0.35
DE  Interaction: Q9BY78; IntAct: EBI-21772313; Score: 0.35
DE  Interaction: P04798; IntAct: EBI-21774067; Score: 0.35
DE  Interaction: O15263; IntAct: EBI-21800402; Score: 0.40
DE  Interaction: P14324; IntAct: EBI-21800273; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16043055; Score: 0.56
DE  Interaction: P16401; IntAct: EBI-20900343; Score: 0.40
DE  Interaction: A4D263; IntAct: EBI-20905088; Score: 0.40
DE  Interaction: P47902; IntAct: EBI-20906784; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
GO  GO:0070062;
GO  GO:0030176;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0032991;
GO  GO:0003690;
GO  GO:0046872;
GO  GO:0004222;
GO  GO:0008235;
GO  GO:0007628;
GO  GO:0030282;
GO  GO:0071586;
GO  GO:1990036;
GO  GO:0061762;
GO  GO:0061337;
GO  GO:0055013;
GO  GO:0003231;
GO  GO:0044255;
GO  GO:0071480;
GO  GO:0006325;
GO  GO:0008340;
GO  GO:0006281;
GO  GO:0003417;
GO  GO:0001942;
GO  GO:0003007;
GO  GO:0043979;
GO  GO:0044029;
GO  GO:0006925;
GO  GO:0060993;
GO  GO:0001889;
GO  GO:0043007;
GO  GO:0035264;
GO  GO:1903799;
GO  GO:0050905;
GO  GO:0006998;
GO  GO:0030327;
GO  GO:0006508;
GO  GO:0010506;
GO  GO:0030500;
GO  GO:0008360;
GO  GO:2000772;
GO  GO:0050688;
GO  GO:0043516;
GO  GO:0048145;
GO  GO:0010906;
GO  GO:2000618;
GO  GO:0032350;
GO  GO:0019216;
GO  GO:1903463;
GO  GO:0040014;
GO  GO:1903025;
GO  GO:0070302;
GO  GO:2000730;
GO  GO:0032006;
GO  GO:0060307;
GO  GO:0072423;
GO  GO:0048538;
GO  GO:0003229;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGMWASLDALWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFW
SQ  SGLYSETEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTL
SQ  GFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEV
SQ  MAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEEGNSEEIKAKVKNK
SQ  KQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDSQPTLIGLLIIFQFIFSPYN
SQ  EVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHYSHPPLLERLQALKTMKQH
//
ID  Q80W54;
PN  CAAX prenyl protease 1 homolog;
GN  Zmpste24;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q80W54;
DR  UNIPROT: Q8BJK4;
DR  UNIPROT: Q8K569;
DR  Pfam: PF01435;
DR  Pfam: PF16491;
DE  Function: Transmembrane metalloprotease whose catalytic activity is critical for processing lamin A/LMNA on the inner nuclear membrane and clearing clogged translocons on the endoplasmic reticulum (PubMed:11923874). Proteolytically removes the C-terminal three residues of farnesylated proteins. Plays also an antiviral role independently of its protease activity by restricting enveloped RNA and DNA viruses, including influenza A, Zika, Ebola, Sindbis, vesicular stomatitis, cowpox, and vaccinia (PubMed:28246125). Mechanistically, controls IFITM antiviral pathway to hinder viruses from breaching the endosomal barrier by modulating membrane fluidity (PubMed:28246125). {ECO:0000250|UniProtKB:O75844, ECO:0000269|PubMed:11923874, ECO:0000269|PubMed:28246125}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0032991;
GO  GO:0003690;
GO  GO:0004175;
GO  GO:0046872;
GO  GO:0004222;
GO  GO:0007628;
GO  GO:0030282;
GO  GO:0071586;
GO  GO:1990036;
GO  GO:0061762;
GO  GO:0061337;
GO  GO:0055013;
GO  GO:0003231;
GO  GO:0044255;
GO  GO:0006974;
GO  GO:0071480;
GO  GO:0006325;
GO  GO:0051276;
GO  GO:0008340;
GO  GO:0006281;
GO  GO:0008544;
GO  GO:0003417;
GO  GO:0001942;
GO  GO:0003007;
GO  GO:0043969;
GO  GO:0043979;
GO  GO:0044029;
GO  GO:0006925;
GO  GO:0060993;
GO  GO:0001889;
GO  GO:0043007;
GO  GO:0035264;
GO  GO:0010629;
GO  GO:1903799;
GO  GO:0050905;
GO  GO:0006998;
GO  GO:0006997;
GO  GO:0010628;
GO  GO:0030327;
GO  GO:0016485;
GO  GO:0010506;
GO  GO:1903522;
GO  GO:0030500;
GO  GO:0008360;
GO  GO:2000772;
GO  GO:0050688;
GO  GO:0043516;
GO  GO:0044030;
GO  GO:0006355;
GO  GO:0048145;
GO  GO:0010906;
GO  GO:0008016;
GO  GO:0090239;
GO  GO:2000618;
GO  GO:0032350;
GO  GO:0019216;
GO  GO:0007346;
GO  GO:1903463;
GO  GO:0040014;
GO  GO:1903025;
GO  GO:0070302;
GO  GO:2000730;
GO  GO:0032006;
GO  GO:0060307;
GO  GO:0072423;
GO  GO:0048538;
GO  GO:0003229;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGMWASVDAMWDFPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTRVPAELEQIMDSDTFEKSRLYQLDKSTFSFW
SQ  SGLYSEVEGTFILLFGGIPYLWRLSGQFCSSAGFGPEYEIIQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNHQTL
SQ  EFFMKDAIKKFIVTQCILLPVSALLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKQEIEV
SQ  MAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVPNKDNQEESGMEARNEGEGDSEEVKAKVKNK
SQ  KQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRRELFAAFGFYDSQPTLIGLLIIFQFIFSPYN
SQ  EVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSTWHYSHPPLLERLQALKNAKQD
//
ID  Q00944;
PN  Focal adhesion kinase 1;
GN  PTK2;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, focal adhesion {ECO:0000269|PubMed:8423801}. Cell membrane {ECO:0000269|PubMed:8423801}; Peripheral membrane protein {ECO:0000269|PubMed:8423801}; Cytoplasmic side {ECO:0000269|PubMed:8423801}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8423801}. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O35346}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000269|PubMed:8423801}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q05397}. Cytoplasm {ECO:0000250|UniProtKB:P34152}. Note=Constituent of focal adhesions. Detected at microtubules. {ECO:0000250|UniProtKB:P34152}.
DR  UNIPROT: Q00944;
DR  PDB: 1KTM;
DR  PDB: 1PV3;
DR  PDB: 1QVX;
DR  PDB: 2AEH;
DR  PDB: 2AL6;
DR  PDB: 2J0J;
DR  PDB: 2J0K;
DR  PDB: 2J0L;
DR  PDB: 2J0M;
DR  PDB: 2JKK;
DR  PDB: 2JKM;
DR  PDB: 2JKO;
DR  PDB: 2JKQ;
DR  PDB: 2L6F;
DR  PDB: 2L6G;
DR  PDB: 2L6H;
DR  PDB: 3ZDT;
DR  PDB: 4BRX;
DR  PDB: 4C7T;
DR  PDB: 4CYE;
DR  PDB: 4D4R;
DR  PDB: 4D4S;
DR  PDB: 4D4V;
DR  PDB: 4D4Y;
DR  PDB: 4D55;
DR  PDB: 4D58;
DR  PDB: 4D5H;
DR  PDB: 4D5K;
DR  PDB: 6CB0;
DR  PDB: 6GCR;
DR  PDB: 6GCW;
DR  PDB: 6GCX;
DR  PDB: 6TY3;
DR  PDB: 6TY4;
DR  Pfam: PF00373;
DR  Pfam: PF18038;
DR  Pfam: PF03623;
DR  Pfam: PF07714;
DR  PROSITE: PS00661;
DR  PROSITE: PS50057;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development, embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), ephrin receptors, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Regulates P53/TP53 activity and stability. Phosphorylates SRC; this increases SRC kinase activity. Isoform 2 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. {ECO:0000269|PubMed:15494732, ECO:0000269|PubMed:15494733, ECO:0000269|PubMed:15494734, ECO:0000269|PubMed:20705914, ECO:0000269|PubMed:21852560, ECO:0000269|PubMed:21937583}.
DE  Reference Proteome: Yes;
DE  Interaction: P00523; IntAct: EBI-6861774; Score: 0.59
DE  Interaction: P00533; IntAct: EBI-3953289; Score: 0.44
DE  Interaction: P49024; IntAct: EBI-2896453; Score: 0.61
DE  Interaction: P08581; IntAct: EBI-3894385; Score: 0.60
DE  Interaction: P09619; IntAct: EBI-3953300; Score: 0.44
DE  Interaction: Q00944; IntAct: EBI-4305329; Score: 0.66
DE  Interaction: Q14451; IntAct: EBI-4288386; Score: 0.40
DE  Interaction: P61157; IntAct: EBI-6692630; Score: 0.61
DE  Interaction: A7MB62; IntAct: EBI-6692672; Score: 0.35
DE  Interaction: G3GXX7; IntAct: EBI-6899259; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-6899017; Score: 0.40
DE  Interaction: Q61140; IntAct: EBI-6900257; Score: 0.40
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0043197;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042383;
GO  GO:0005524;
GO  GO:0004198;
GO  GO:0042802;
GO  GO:0005178;
GO  GO:0140677;
GO  GO:0004715;
GO  GO:0002020;
GO  GO:0004713;
GO  GO:0005102;
GO  GO:0007015;
GO  GO:0001525;
GO  GO:0060055;
GO  GO:0030154;
GO  GO:0007173;
GO  GO:0045087;
GO  GO:2000811;
GO  GO:0010812;
GO  GO:0031953;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0051894;
GO  GO:0032092;
GO  GO:0061098;
GO  GO:1904237;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0140650;
GO  GO:0030155;
GO  GO:0035994;
GO  GO:0009268;
GO  GO:0007172;
GO  GO:0007169;
GO  GO:0044319;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8423801};
SQ  MAAAYLDPNLNHTPSSSAKTHLGTGMERSPGAMERVLKVFHYFENSSEPTTWASIIRHGDATDVRGIIQKIVDCHKVKNV
SQ  ACYGLRLSHLQSEEVHWLHLDMGVSNVREKFELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKNDYMLEIA
SQ  DQVDQEIALKLGCLEIRRSYGEMRGNALEKKSNYEVLEKDVGLRRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESI
SQ  LKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGANPTHLADFNQVQTIQYSNSEDKDRKGMLQLKI
SQ  AGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANNEKQGVRSHTVSVSETDDYAEI
SQ  IDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAMAVAIKTCKNCTSDSVREKFLQEALTMRQFDH
SQ  PHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKFSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSATDCV
SQ  KLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGER
SQ  LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKLQQEERMRMESRRQVTVSWDSGGSDEAPPKPSRPGY
SQ  PSPRSSEGFYPSPQHMVQPNHYQVSGYSGSHGIPAMAGSIYPGQASLLDQTDSWNHRPQEVSAWQPNMEDSGTLDVRGMG
SQ  QVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLVMKPDVRLSRGSIEREDGGLQGPAGNQHIYQPVGKPDHAAPPKKPPR
SQ  PGAPHLGSLASLNSPVDSYNEGVKIKPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGL
SQ  ALRTLLATVDESLPVLPASTHREIEMAQKLLNSDLAELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVID
SQ  QARLKMISQSRPH
//
ID  Q05397;
PN  Focal adhesion kinase 1;
GN  PTK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, focal adhesion {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:15855171, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:18256281, ECO:0000269|PubMed:31630787}. Cell membrane {ECO:0000250|UniProtKB:Q00944}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q00944}; Cytoplasmic side {ECO:0000250|UniProtKB:Q00944}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15855171}. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O35346}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000269|PubMed:15855171, ECO:0000269|PubMed:18206965}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:31630787}. Cytoplasm {ECO:0000269|PubMed:15855171, ECO:0000269|PubMed:18078954, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:18256281}. Note=Constituent of focal adhesions. Detected at microtubules. {ECO:0000250|UniProtKB:P34152}.
DR  UNIPROT: Q05397;
DR  UNIPROT: B4E2N6;
DR  UNIPROT: F5H4S4;
DR  UNIPROT: J3QT16;
DR  UNIPROT: Q14291;
DR  UNIPROT: Q8IYN9;
DR  UNIPROT: Q9UD85;
DR  PDB: 1K04;
DR  PDB: 1K05;
DR  PDB: 1MP8;
DR  PDB: 1OW6;
DR  PDB: 1OW7;
DR  PDB: 1OW8;
DR  PDB: 2ETM;
DR  PDB: 2IJM;
DR  PDB: 3B71;
DR  PDB: 3BZ3;
DR  PDB: 3PXK;
DR  PDB: 3S9O;
DR  PDB: 4EBV;
DR  PDB: 4EBW;
DR  PDB: 4GU6;
DR  PDB: 4GU9;
DR  PDB: 4I4E;
DR  PDB: 4I4F;
DR  PDB: 4K8A;
DR  PDB: 4K9Y;
DR  PDB: 4KAB;
DR  PDB: 4KAO;
DR  PDB: 4NY0;
DR  PDB: 4Q9S;
DR  PDB: 6I8Z;
DR  PDB: 6LES;
DR  PDB: 6PW8;
DR  PDB: 6YOJ;
DR  PDB: 6YQ1;
DR  PDB: 6YR9;
DR  PDB: 6YT6;
DR  PDB: 6YVS;
DR  PDB: 6YVY;
DR  PDB: 6YXV;
DR  PDB: 7PI4;
DR  Pfam: PF00373;
DR  Pfam: PF18038;
DR  Pfam: PF03623;
DR  Pfam: PF07714;
DR  PROSITE: PS00661;
DR  PROSITE: PS50057;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  OMIM: 600758;
DR  DisGeNET: 5747;
DE  Function: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (PubMed:9360983). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:11980671, ECO:0000269|PubMed:15166238, ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:15895076, ECO:0000269|PubMed:16919435, ECO:0000269|PubMed:16927379, ECO:0000269|PubMed:17395594, ECO:0000269|PubMed:17431114, ECO:0000269|PubMed:17968709, ECO:0000269|PubMed:18006843, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:18256281, ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:18677107, ECO:0000269|PubMed:19138410, ECO:0000269|PubMed:19147981, ECO:0000269|PubMed:19224453, ECO:0000269|PubMed:20332118, ECO:0000269|PubMed:20495381, ECO:0000269|PubMed:21454698, ECO:0000269|PubMed:9360983}. [Isoform 6]: Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269|PubMed:20109444}.
DE  Disease: Note=Aberrant PTK2/FAK1 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. PTK2/FAK1 overexpression is seen in many types of cancer.
DE  Reference Proteome: Yes;
DE  Interaction: O60711; IntAct: EBI-7326264; Score: 0.55
DE  Interaction: P00533; IntAct: EBI-702075; Score: 0.75
DE  Interaction: P04626; IntAct: EBI-2942138; Score: 0.54
DE  Interaction: P05480; IntAct: EBI-7976544; Score: 0.68
DE  Interaction: P07948; IntAct: EBI-7859736; Score: 0.57
DE  Interaction: P12931; IntAct: EBI-968957; Score: 0.92
DE  Interaction: P37198; IntAct: EBI-30836789; Score: 0.44
DE  Interaction: P56945; IntAct: EBI-8617929; Score: 0.59
DE  Interaction: P78396; IntAct: EBI-6592527; Score: 0.54
DE  Interaction: P04637; IntAct: EBI-1544471; Score: 0.75
DE  Interaction: Q80ZW7; IntAct: EBI-7809276; Score: 0.46
DE  Interaction: P70372; IntAct: EBI-7809400; Score: 0.40
DE  Interaction: Q7L0Q8; IntAct: EBI-1792522; Score: 0.40
DE  Interaction: Q62219; IntAct: EBI-1810942; Score: 0.52
DE  Interaction: P49023; IntAct: EBI-1810961; Score: 0.94
DE  Interaction: O43294; IntAct: EBI-1811097; Score: 0.77
DE  Interaction: Q62884; IntAct: EBI-7505062; Score: 0.44
DE  Interaction: Q68CZ2; IntAct: EBI-2607447; Score: 0.56
DE  Interaction: P54792; IntAct: EBI-7848137; Score: 0.35
DE  Interaction: O14640; IntAct: EBI-7848672; Score: 0.35
DE  Interaction: P43146; IntAct: EBI-2678596; Score: 0.35
DE  Interaction: A0A5P8YHQ6; IntAct: EBI-2870073; Score: 0.00
DE  Interaction: P62993; IntAct: EBI-8590192; Score: 0.66
DE  Interaction: P63000; IntAct: EBI-3449574; Score: 0.00
DE  Interaction: Q9BY76; IntAct: EBI-3843710; Score: 0.35
DE  Interaction: P29317; IntAct: EBI-3843951; Score: 0.49
DE  Interaction: Q9UBE0; IntAct: EBI-3914256; Score: 0.37
DE  Interaction: Q8TAM1; IntAct: EBI-7322989; Score: 0.37
DE  Interaction: O00148; IntAct: EBI-7323069; Score: 0.37
DE  Interaction: P26641; IntAct: EBI-7323654; Score: 0.37
DE  Interaction: Q9H6S3; IntAct: EBI-7323997; Score: 0.37
DE  Interaction: P00488; IntAct: EBI-7324567; Score: 0.37
DE  Interaction: P09467; IntAct: EBI-7325203; Score: 0.37
DE  Interaction: Q14469; IntAct: EBI-7325706; Score: 0.37
DE  Interaction: O15069; IntAct: EBI-7326959; Score: 0.37
DE  Interaction: P49321; IntAct: EBI-7327416; Score: 0.37
DE  Interaction: Q9NQX6; IntAct: EBI-7328100; Score: 0.37
DE  Interaction: Q9H3S7; IntAct: EBI-8423552; Score: 0.64
DE  Interaction: P46108; IntAct: EBI-6181896; Score: 0.63
DE  Interaction: Q9Y3E5; IntAct: EBI-6253054; Score: 0.40
DE  Interaction: P21145; IntAct: EBI-6253719; Score: 0.35
DE  Interaction: O00459; IntAct: EBI-6256910; Score: 0.35
DE  Interaction: P42336; IntAct: EBI-6256910; Score: 0.35
DE  Interaction: Q92569; IntAct: EBI-6256910; Score: 0.63
DE  Interaction: Q96SB4; IntAct: EBI-6659921; Score: 0.59
DE  Interaction: P08238; IntAct: EBI-6423484; Score: 0.40
DE  Interaction: O75925; IntAct: EBI-6591889; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-6592681; Score: 0.27
DE  Interaction: P40763; IntAct: EBI-6593385; Score: 0.27
DE  Interaction: P42224; IntAct: EBI-6593396; Score: 0.54
DE  Interaction: P25054; IntAct: EBI-6594490; Score: 0.27
DE  Interaction: P46109; IntAct: EBI-6599743; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-6599815; Score: 0.27
DE  Interaction: P07947; IntAct: EBI-6599941; Score: 0.57
DE  Interaction: P06756; IntAct: EBI-6600280; Score: 0.27
DE  Interaction: P60484; IntAct: EBI-6600406; Score: 0.27
DE  Interaction: P19174; IntAct: EBI-6600388; Score: 0.27
DE  Interaction: P54939; IntAct: EBI-6620512; Score: 0.40
DE  Interaction: P39052; IntAct: EBI-8699700; Score: 0.40
DE  Interaction: Q05397; IntAct: EBI-9256428; Score: 0.44
DE  Interaction: P14618; IntAct: EBI-9355072; Score: 0.44
DE  Interaction: P29350; IntAct: EBI-10691827; Score: 0.57
DE  Interaction: O60880; IntAct: EBI-10691844; Score: 0.49
DE  Interaction: Q8TEW6; IntAct: EBI-10691810; Score: 0.49
DE  Interaction: Q9NP31; IntAct: EBI-10691878; Score: 0.57
DE  Interaction: Q14451; IntAct: EBI-10691861; Score: 0.57
DE  Interaction: O14796; IntAct: EBI-10697408; Score: 0.37
DE  Interaction: P08631; IntAct: EBI-10697432; Score: 0.51
DE  Interaction: Q9H269; IntAct: EBI-11047581; Score: 0.35
DE  Interaction: Q9QZB9; IntAct: EBI-11074142; Score: 0.35
DE  Interaction: P16144; IntAct: EBI-12599461; Score: 0.52
DE  Interaction: P16671; IntAct: EBI-13940936; Score: 0.35
DE  Interaction: P05120; IntAct: EBI-21713063; Score: 0.35
DE  Interaction: Q13976; IntAct: EBI-21852154; Score: 0.35
DE  Interaction: Q15125; IntAct: EBI-20903608; Score: 0.40
DE  Interaction: P07355; IntAct: EBI-20913238; Score: 0.40
DE  Interaction: Q9NQ75; IntAct: EBI-21384868; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-21384856; Score: 0.00
DE  Interaction: P06241; IntAct: EBI-28938953; Score: 0.55
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: D4A3T0; IntAct: EBI-22240287; Score: 0.35
DE  Interaction: F1M3E4; IntAct: EBI-22240287; Score: 0.35
DE  Interaction: Q920L0; IntAct: EBI-22240287; Score: 0.35
DE  Interaction: Q4KM68; IntAct: EBI-22240287; Score: 0.35
DE  Interaction: P62994; IntAct: EBI-22240287; Score: 0.35
DE  Interaction: D3ZG10; IntAct: EBI-22240287; Score: 0.35
DE  Interaction: P20339; IntAct: EBI-25381246; Score: 0.35
DE  Interaction: O84008; IntAct: EBI-22302433; Score: 0.35
DE  Interaction: Q07889; IntAct: EBI-25438153; Score: 0.35
DE  Interaction: Q06124; IntAct: EBI-25438153; Score: 0.35
DE  Interaction: Q824H6; IntAct: EBI-26494109; Score: 0.54
DE  Interaction: P49024; IntAct: EBI-26498316; Score: 0.37
DE  Interaction: P25105; IntAct: EBI-27099240; Score: 0.40
DE  Interaction: Q00535; IntAct: EBI-28938854; Score: 0.35
DE  Interaction: P35251; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: P35249; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9Y5J1; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9Y3B2; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9UQ35; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9NXZ2; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9NW13; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9NQ55; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9HCM4; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9H7E9; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9GZR7; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9BZE4; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q9BRJ6; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q96B26; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q7L2E3; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q6DKI1; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q5TAQ9; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q2NL82; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q14978; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q14137; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q13868; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q13428; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q01780; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q00577; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: P67870; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: P56182; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: P49458; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: P49354; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: P42696; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: P13674; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: O75683; IntAct: EBI-28938953; Score: 0.35
DE  Interaction: Q3SY52; IntAct: EBI-30836811; Score: 0.44
DE  Interaction: Q504T8; IntAct: EBI-30836822; Score: 0.44
DE  Interaction: O75038; IntAct: EBI-30836778; Score: 0.44
DE  Interaction: Q08378; IntAct: EBI-30836800; Score: 0.44
DE  Interaction: Q7Z478; IntAct: EBI-30836833; Score: 0.44
DE  Interaction: Q8IYE1; IntAct: EBI-30836844; Score: 0.44
DE  Interaction: Q8WZA0; IntAct: EBI-30836855; Score: 0.44
DE  Interaction: Q92859; IntAct: EBI-30836866; Score: 0.44
DE  Interaction: Q96BU1; IntAct: EBI-30836877; Score: 0.44
DE  Interaction: Q9H0J4; IntAct: EBI-30836888; Score: 0.44
GO  GO:0005938;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0043231;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0001725;
GO  GO:0003779;
GO  GO:0005524;
GO  GO:0005178;
GO  GO:0008432;
GO  GO:0140677;
GO  GO:0004715;
GO  GO:0019901;
GO  GO:0019903;
GO  GO:0004713;
GO  GO:0004725;
GO  GO:0042169;
GO  GO:0005102;
GO  GO:0001525;
GO  GO:0007411;
GO  GO:0030154;
GO  GO:0016477;
GO  GO:0048870;
GO  GO:0035995;
GO  GO:0048013;
GO  GO:0007173;
GO  GO:0030010;
GO  GO:0038096;
GO  GO:0060396;
GO  GO:0003007;
GO  GO:0045087;
GO  GO:0007229;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:0022408;
GO  GO:0038007;
GO  GO:0018108;
GO  GO:0001890;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0010634;
GO  GO:0010718;
GO  GO:0010763;
GO  GO:0010759;
GO  GO:0120041;
GO  GO:0043552;
GO  GO:0014068;
GO  GO:0045860;
GO  GO:0051897;
GO  GO:0001934;
GO  GO:2000060;
GO  GO:0090303;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0065008;
GO  GO:0030155;
GO  GO:0033628;
GO  GO:0042127;
GO  GO:0008360;
GO  GO:0051493;
GO  GO:0010594;
GO  GO:0010632;
GO  GO:0051893;
GO  GO:0043087;
GO  GO:0045667;
GO  GO:0001932;
GO  GO:1900024;
GO  GO:0007172;
GO  GO:0007179;
GO  GO:0007169;
GO  GO:0048010;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q00944};
SQ  MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHV
SQ  ACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIA
SQ  DQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESI
SQ  LKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKI
SQ  AGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEI
SQ  IDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDH
SQ  PHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV
SQ  KLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGER
SQ  LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGY
SQ  PSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIG
SQ  QVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPG
SQ  APGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLA
SQ  LRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQ
SQ  ARLKMLGQTRPH
//
ID  P34152;
PN  Focal adhesion kinase 1;
GN  Ptk2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, focal adhesion {ECO:0000269|PubMed:1528852}. Cell membrane {ECO:0000250|UniProtKB:Q00944}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q00944}; Cytoplasmic side {ECO:0000250|UniProtKB:Q00944}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12941275}. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O35346}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus {ECO:0000269|PubMed:18206965}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q05397}. Cytoplasm {ECO:0000269|PubMed:18206965}. Note=Constituent of focal adhesions. Detected at microtubules. {ECO:0000269|PubMed:12941275}.
DR  UNIPROT: P34152;
DR  UNIPROT: O08578;
DR  UNIPROT: Q5DTH7;
DR  UNIPROT: Q8C513;
DR  UNIPROT: Q8CFH7;
DR  UNIPROT: Q8CHM2;
DR  UNIPROT: Q8K2S0;
DR  UNIPROT: Q9DAW3;
DR  PDB: 1K40;
DR  PDB: 5F28;
DR  PDB: 6BZ3;
DR  Pfam: PF00373;
DR  Pfam: PF18038;
DR  Pfam: PF03623;
DR  Pfam: PF07714;
DR  PROSITE: PS00661;
DR  PROSITE: PS50057;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (PubMed:25059660). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. {ECO:0000250|UniProtKB:Q05397, ECO:0000269|PubMed:10373530, ECO:0000269|PubMed:10806474, ECO:0000269|PubMed:11278462, ECO:0000269|PubMed:11369769, ECO:0000269|PubMed:12702722, ECO:0000269|PubMed:12941275, ECO:0000269|PubMed:15967814, ECO:0000269|PubMed:16000375, ECO:0000269|PubMed:16391003, ECO:0000269|PubMed:17093062, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19147981, ECO:0000269|PubMed:19473962, ECO:0000269|PubMed:22056317, ECO:0000269|PubMed:25059660, ECO:0000269|PubMed:7478517, ECO:0000269|PubMed:7997267, ECO:0000269|PubMed:9148935}. [Isoform 9]: Does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription (By similarity). {ECO:0000250|UniProtKB:Q05397}.
DE  Reference Proteome: Yes;
DE  Interaction: P05480; IntAct: EBI-7361479; Score: 0.59
DE  Interaction: P12931; IntAct: EBI-7921275; Score: 0.56
DE  Interaction: Q61140; IntAct: EBI-77098; Score: 0.65
DE  Interaction: Q8VI36; IntAct: EBI-7361489; Score: 0.78
DE  Interaction: P39688; IntAct: EBI-653453; Score: 0.37
DE  Interaction: P54763; IntAct: EBI-983197; Score: 0.46
DE  Interaction: Q60631; IntAct: EBI-983357; Score: 0.51
DE  Interaction: Q03160; IntAct: EBI-7281453; Score: 0.44
DE  Interaction: P18031; IntAct: EBI-8672381; Score: 0.44
DE  Interaction: P97333; IntAct: EBI-7921208; Score: 0.40
DE  Interaction: P11627; IntAct: EBI-7921264; Score: 0.40
DE  Interaction: P35235; IntAct: EBI-7186929; Score: 0.40
DE  Interaction: P54792; IntAct: EBI-7848377; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-8633193; Score: 0.60
DE  Interaction: P56945; IntAct: EBI-6569708; Score: 0.40
DE  Interaction: P49023; IntAct: EBI-6569717; Score: 0.46
DE  Interaction: Q99JY9; IntAct: EBI-6675060; Score: 0.46
DE  Interaction: Q91YD9; IntAct: EBI-6675097; Score: 0.40
DE  Interaction: P39054; IntAct: EBI-8699666; Score: 0.40
DE  Interaction: P39052; IntAct: EBI-8699679; Score: 0.32
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16736255; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26473528; Score: 0.35
GO  GO:0016324;
GO  GO:0016323;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0098978;
GO  GO:0014704;
GO  GO:0043231;
GO  GO:0030027;
GO  GO:0016604;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0042383;
GO  GO:0001725;
GO  GO:0003779;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0005178;
GO  GO:0008432;
GO  GO:0004715;
GO  GO:0019902;
GO  GO:0043548;
GO  GO:0019901;
GO  GO:0019903;
GO  GO:0004713;
GO  GO:0004725;
GO  GO:0044877;
GO  GO:0042169;
GO  GO:0005102;
GO  GO:0001525;
GO  GO:0007409;
GO  GO:0001568;
GO  GO:0030154;
GO  GO:0016477;
GO  GO:0030644;
GO  GO:0071560;
GO  GO:0021955;
GO  GO:0043542;
GO  GO:0048013;
GO  GO:0007173;
GO  GO:0030198;
GO  GO:0060396;
GO  GO:0045087;
GO  GO:0007229;
GO  GO:0007254;
GO  GO:0000165;
GO  GO:0000226;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:0010507;
GO  GO:0050771;
GO  GO:0030336;
GO  GO:0022408;
GO  GO:0046621;
GO  GO:0051964;
GO  GO:0001764;
GO  GO:0007097;
GO  GO:0035265;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0010613;
GO  GO:0045785;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0010763;
GO  GO:0060252;
GO  GO:0010759;
GO  GO:0120041;
GO  GO:0050766;
GO  GO:0014068;
GO  GO:0045860;
GO  GO:0051897;
GO  GO:0001934;
GO  GO:0014911;
GO  GO:0048661;
GO  GO:0050806;
GO  GO:2000060;
GO  GO:0090303;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0030155;
GO  GO:0033628;
GO  GO:0042127;
GO  GO:0008360;
GO  GO:0010632;
GO  GO:0051893;
GO  GO:0045667;
GO  GO:0001932;
GO  GO:1900024;
GO  GO:0007172;
GO  GO:0007179;
GO  GO:0007169;
GO  GO:0001570;
GO  GO:0042311;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q00944};
SQ  MAAAYLDPNLNHTPSSSTKTHLGTGMERSPGAMERVLKVFHYFESSSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHV
SQ  ACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMQEIA
SQ  DQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESI
SQ  LKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKI
SQ  AGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEI
SQ  IDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGVYLSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDH
SQ  PHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV
SQ  KLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGER
SQ  LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKVQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGY
SQ  PSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGIPAMAGSIYQGQASLLDQTELWNHRPQEMSMWQPSVEDSAALDLRGMG
SQ  QVLPPHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSFQGPTGNQHIYQPVGKPDPAAPPKKPPRPG
SQ  APGHLSNLSSISSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLA
SQ  LRTLLATVDETIPALPASTHREIEMAQKLLNSDLGELISKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQ
SQ  ARLKMLGQTRPH
//
ID  O35346;
PN  Focal adhesion kinase 1;
GN  Ptk2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q00944}. Cell membrane {ECO:0000250|UniProtKB:Q00944}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q00944}; Cytoplasmic side {ECO:0000250|UniProtKB:Q00944}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q00944}. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12732587}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000269|PubMed:12732587, ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:16373587}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q05397}. Cytoplasm {ECO:0000269|PubMed:16373587}. Note=Constituent of focal adhesions. Detected at microtubules. {ECO:0000250|UniProtKB:P34152}.
DR  UNIPROT: O35346;
DR  UNIPROT: Q62900;
DR  Pfam: PF00373;
DR  Pfam: PF18038;
DR  Pfam: PF03623;
DR  Pfam: PF07714;
DR  PROSITE: PS00661;
DR  PROSITE: PS50057;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (By similarity). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. {ECO:0000250|UniProtKB:P34152, ECO:0000250|UniProtKB:Q05397, ECO:0000269|PubMed:15494733}. [Isoform 2]: Does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription (By similarity). {ECO:0000250|UniProtKB:Q05397}.
DE  Reference Proteome: Yes;
DE  Interaction: P62140; IntAct: EBI-7935349; Score: 0.40
DE  Interaction: P41239; IntAct: EBI-8594657; Score: 0.40
DE  Interaction: Q9BX66; IntAct: EBI-8536646; Score: 0.35
DE  Interaction: Q5XI86; IntAct: EBI-6253014; Score: 0.46
DE  Interaction: O70161; IntAct: EBI-6614935; Score: 0.27
DE  Interaction: O35346; IntAct: EBI-9256497; Score: 0.72
DE  Interaction: Q8VI36; IntAct: EBI-9256513; Score: 0.38
DE  Interaction: Q6P6T5; IntAct: EBI-15783756; Score: 0.59
DE  Interaction: F1M4A0; IntAct: EBI-15783823; Score: 0.40
GO  GO:0016324;
GO  GO:0016323;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0098978;
GO  GO:0014704;
GO  GO:0030027;
GO  GO:0016604;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0042383;
GO  GO:0001725;
GO  GO:0003779;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0005178;
GO  GO:0008432;
GO  GO:0004715;
GO  GO:0019902;
GO  GO:0043548;
GO  GO:0019901;
GO  GO:0019903;
GO  GO:0004713;
GO  GO:0004725;
GO  GO:0044877;
GO  GO:0042169;
GO  GO:0005102;
GO  GO:0001525;
GO  GO:0007409;
GO  GO:0001568;
GO  GO:0030154;
GO  GO:0016477;
GO  GO:0030644;
GO  GO:0071560;
GO  GO:0021955;
GO  GO:0043542;
GO  GO:0048013;
GO  GO:0007173;
GO  GO:0030198;
GO  GO:0045444;
GO  GO:0060396;
GO  GO:0045087;
GO  GO:0007229;
GO  GO:0007254;
GO  GO:0000165;
GO  GO:0000226;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:0010507;
GO  GO:0050771;
GO  GO:0030336;
GO  GO:0022408;
GO  GO:0046621;
GO  GO:0051964;
GO  GO:0001764;
GO  GO:0007097;
GO  GO:0035265;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0010613;
GO  GO:0045785;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0010763;
GO  GO:0060252;
GO  GO:0010759;
GO  GO:0120041;
GO  GO:0050766;
GO  GO:0014068;
GO  GO:0045860;
GO  GO:0051897;
GO  GO:0001934;
GO  GO:0014911;
GO  GO:0048661;
GO  GO:0050806;
GO  GO:2000060;
GO  GO:0090303;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0030155;
GO  GO:0033628;
GO  GO:0042127;
GO  GO:0008360;
GO  GO:0010632;
GO  GO:0051893;
GO  GO:0045667;
GO  GO:0001932;
GO  GO:1900024;
GO  GO:0046685;
GO  GO:0032355;
GO  GO:0009749;
GO  GO:0009612;
GO  GO:0014070;
GO  GO:0010033;
GO  GO:0010243;
GO  GO:0009410;
GO  GO:0007172;
GO  GO:0007179;
GO  GO:0007169;
GO  GO:0001570;
GO  GO:0042311;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q00944};
SQ  MAAAYLDPNLNHTPSSSTKTHLGTGTERSPGAMERVLKVFHYFESSNEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHV
SQ  ACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIA
SQ  DQVDQDIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESI
SQ  LKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKI
SQ  AGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANNEKQGMRTHAVSVSETDDYAEI
SQ  IDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGVYLSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDH
SQ  PHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV
SQ  KLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGER
SQ  LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKVQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGY
SQ  PSPRSSEGFYPSPQHMVQTNHYQISGYPGSHGIPAMAGSIYPGQASLLDQTELWNHRPQEMSMWQPSVEDSAALDLRGMG
SQ  QVLPPHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSFQGPTGNQHIYQPVGKPDPAAPPKKPPRPG
SQ  APGHLSNLSSISSPAESYNEGVKPWRLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEV
SQ  GLALRTLLATVDETIPILPASTHREIEMAQKLLNSDLGELISKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDV
SQ  IDQARLKMLGQTRPH
//
ID  Q14289;
PN  Protein-tyrosine kinase 2-beta;
GN  PTK2B;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, focal adhesion. Cell projection, lamellipodium. Cytoplasm, cell cortex. Nucleus. Note=Interaction with NPHP1 induces the membrane-association of the kinase. Colocalizes with integrins at the cell periphery.
DR  UNIPROT: Q14289;
DR  UNIPROT: D3DST0;
DR  UNIPROT: Q13475;
DR  UNIPROT: Q14290;
DR  UNIPROT: Q16709;
DR  UNIPROT: Q6PID4;
DR  PDB: 2LK4;
DR  PDB: 3CC6;
DR  PDB: 3ET7;
DR  PDB: 3FZO;
DR  PDB: 3FZP;
DR  PDB: 3FZR;
DR  PDB: 3FZS;
DR  PDB: 3FZT;
DR  PDB: 3GM1;
DR  PDB: 3GM2;
DR  PDB: 3GM3;
DR  PDB: 3H3C;
DR  PDB: 3U3F;
DR  PDB: 4EKU;
DR  PDB: 4H1J;
DR  PDB: 4H1M;
DR  PDB: 4R32;
DR  PDB: 4XEF;
DR  PDB: 4XEK;
DR  PDB: 4XEV;
DR  PDB: 5TO8;
DR  PDB: 5TOB;
DR  PDB: 6LF3;
DR  Pfam: PF00373;
DR  Pfam: PF18038;
DR  Pfam: PF03623;
DR  Pfam: PF07714;
DR  PROSITE: PS50057;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  OMIM: 601212;
DR  DisGeNET: 2185;
DE  Function: Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2. {ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:12771146, ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:15050747, ECO:0000269|PubMed:15166227, ECO:0000269|PubMed:17634955, ECO:0000269|PubMed:18086875, ECO:0000269|PubMed:18339875, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:18765415, ECO:0000269|PubMed:19086031, ECO:0000269|PubMed:19207108, ECO:0000269|PubMed:19244237, ECO:0000269|PubMed:19428251, ECO:0000269|PubMed:19648005, ECO:0000269|PubMed:19880522, ECO:0000269|PubMed:20001213, ECO:0000269|PubMed:20381867, ECO:0000269|PubMed:20521079, ECO:0000269|PubMed:21357692, ECO:0000269|PubMed:21533080, ECO:0000269|PubMed:7544443, ECO:0000269|PubMed:8670418, ECO:0000269|PubMed:8849729}.
DE  Disease: Note=Aberrant PTK2B/PYK2 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. Elevated PTK2B/PYK2 expression is seen in gliomas, hepatocellular carcinoma, lung cancer and breast cancer.
DE  Reference Proteome: Yes;
DE  Interaction: A1A4S6; IntAct: EBI-28941112; Score: 0.35
DE  Interaction: O60711; IntAct: EBI-21392269; Score: 0.00
DE  Interaction: P00533; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-6589791; Score: 0.27
DE  Interaction: P12931; IntAct: EBI-7095687; Score: 0.64
DE  Interaction: Q02156; IntAct: EBI-28938908; Score: 0.35
DE  Interaction: Q9Y6R4; IntAct: EBI-7426200; Score: 0.46
DE  Interaction: Q8WUM4; IntAct: EBI-7397527; Score: 0.40
DE  Interaction: Q00005; IntAct: EBI-2210942; Score: 0.35
DE  Interaction: Q7L0Q8; IntAct: EBI-1792396; Score: 0.58
DE  Interaction: P17778; IntAct: EBI-2870052; Score: 0.00
DE  Interaction: Q8CKM0; IntAct: EBI-2870059; Score: 0.00
DE  Interaction: Q8CKF8; IntAct: EBI-2870066; Score: 0.00
DE  Interaction: P06241; IntAct: EBI-7313404; Score: 0.70
DE  Interaction: P42679; IntAct: EBI-8467868; Score: 0.46
DE  Interaction: P62993; IntAct: EBI-8684794; Score: 0.35
DE  Interaction: Q99836; IntAct: EBI-6390158; Score: 0.40
DE  Interaction: Q8NF50; IntAct: EBI-6390162; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-6423496; Score: 0.40
DE  Interaction: O75161; IntAct: EBI-11790516; Score: 0.40
DE  Interaction: P24830; IntAct: EBI-16046716; Score: 0.37
DE  Interaction: P06921; IntAct: EBI-16046979; Score: 0.00
DE  Interaction: P06422; IntAct: EBI-16048727; Score: 0.00
DE  Interaction: P36780; IntAct: EBI-16050118; Score: 0.00
DE  Interaction: P06790; IntAct: EBI-16051603; Score: 0.00
DE  Interaction: P06423; IntAct: EBI-16052167; Score: 0.00
DE  Interaction: P03118; IntAct: EBI-16053185; Score: 0.00
DE  Interaction: P36778; IntAct: EBI-16054551; Score: 0.00
DE  Interaction: O15259; IntAct: EBI-21257674; Score: 0.40
DE  Interaction: Q00610; IntAct: EBI-21371914; Score: 0.00
DE  Interaction: Q9NQ75; IntAct: EBI-21373824; Score: 0.00
DE  Interaction: O60346; IntAct: EBI-21375347; Score: 0.00
DE  Interaction: Q9Y2D4; IntAct: EBI-21375334; Score: 0.00
DE  Interaction: P43121; IntAct: EBI-21380363; Score: 0.00
DE  Interaction: P26367; IntAct: EBI-21381329; Score: 0.00
DE  Interaction: Q9UQM7; IntAct: EBI-21389795; Score: 0.00
DE  Interaction: O75563; IntAct: EBI-21391374; Score: 0.00
DE  Interaction: Q9BUZ4; IntAct: EBI-21980067; Score: 0.35
DE  Interaction: O43294; IntAct: EBI-21980067; Score: 0.53
DE  Interaction: P14598; IntAct: EBI-21980104; Score: 0.40
DE  Interaction: P49023; IntAct: EBI-25376663; Score: 0.53
DE  Interaction: P05067; IntAct: EBI-25938518; Score: 0.56
DE  Interaction: Q9H3G5; IntAct: EBI-28941112; Score: 0.35
DE  Interaction: Q9C0A1; IntAct: EBI-28941112; Score: 0.35
DE  Interaction: P24752; IntAct: EBI-28941112; Score: 0.35
GO  GO:0097440;
GO  GO:0044297;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0045121;
GO  GO:0043025;
GO  GO:0017146;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0043423;
GO  GO:0005524;
GO  GO:0004683;
GO  GO:0004972;
GO  GO:0004715;
GO  GO:0008022;
GO  GO:0043621;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0031625;
GO  GO:0090630;
GO  GO:0042976;
GO  GO:0002250;
GO  GO:0006915;
GO  GO:0043534;
GO  GO:0045453;
GO  GO:0030154;
GO  GO:0007166;
GO  GO:0006968;
GO  GO:0071498;
GO  GO:0071300;
GO  GO:0070098;
GO  GO:0086100;
GO  GO:0007173;
GO  GO:0048041;
GO  GO:0014009;
GO  GO:0045087;
GO  GO:0007229;
GO  GO:0035235;
GO  GO:0060292;
GO  GO:0060291;
GO  GO:0000165;
GO  GO:0002315;
GO  GO:0043066;
GO  GO:0030502;
GO  GO:0008285;
GO  GO:0010656;
GO  GO:0045638;
GO  GO:0043524;
GO  GO:0043267;
GO  GO:0031175;
GO  GO:0001556;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0030838;
GO  GO:0045766;
GO  GO:2000538;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:0007204;
GO  GO:2000573;
GO  GO:0010595;
GO  GO:0070374;
GO  GO:2000463;
GO  GO:0046330;
GO  GO:0043507;
GO  GO:0010976;
GO  GO:0045429;
GO  GO:0051000;
GO  GO:0050731;
GO  GO:0043552;
GO  GO:0045860;
GO  GO:2000379;
GO  GO:0051968;
GO  GO:0045727;
GO  GO:2000060;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0065003;
GO  GO:2000249;
GO  GO:0050848;
GO  GO:0030155;
GO  GO:0008360;
GO  GO:0010752;
GO  GO:2000114;
GO  GO:0032960;
GO  GO:0010758;
GO  GO:2000310;
GO  GO:0051279;
GO  GO:0048167;
GO  GO:2000058;
GO  GO:0051592;
GO  GO:0051591;
GO  GO:0043157;
GO  GO:0042220;
GO  GO:0045471;
GO  GO:0009749;
GO  GO:0009725;
GO  GO:0042542;
GO  GO:0001666;
GO  GO:0035902;
GO  GO:0002931;
GO  GO:0010226;
GO  GO:0009612;
GO  GO:0009410;
GO  GO:0007172;
GO  GO:0007165;
GO  GO:0002040;
GO  GO:0043149;
GO  GO:0007169;
GO  GO:0033209;
GO  GO:0048010;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSGVSEPLSRVKLGTLRRPEGPAEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIREIITSILLSGRI
SQ  GPNIRLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRN
SQ  DYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYAS
SQ  LREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDAKPTCLAEFKQIRSIRCLPLEEGQAVL
SQ  QLGIEGAPQALSIKTSSLAEAENMADLIDGYCRLQGEHQGSLIIHPRKDGEKRNSLPQIPMLNLEARRSHLSESCSIESD
SQ  IYAEIPDETLRRPGGPQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEAVIMKN
SQ  LDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICKAMAYLESINCVHRDIAVRNILVASP
SQ  ECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEK
SQ  GDRLPKPDLCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAMEQERNARYRTPKILEPTAFQEPPPKPSRP
SQ  KYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIQPSSREEAQQLWEAE
SQ  KVKMRQILDKQQKQMVEDYQWLRQEEKSLDPMVYMNDKSPLTPEKEVGYLEFTGPPQKPPRLGAQSIQPTANLDRTDDLV
SQ  YLNVMELVRAVLELKNELCQLPPEGYVVVVKNVGLTLRKLIGSVDDLLPSLPSSSRTEIEGTQKLLNKDLAELINKMRLA
SQ  QQNAVTSLSEECKRQMLTASHTLAVDAKNLLDAVDQAKVLANLAHPPAE
//
ID  Q9QVP9;
PN  Protein-tyrosine kinase 2-beta;
GN  Ptk2b;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, focal adhesion. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with integrins at the cell periphery (By similarity). Interaction with NPHP1 induces the membrane- association of the kinase. Colocalizes with PXN at the microtubule- organizing center. The tyrosine phosphorylated form is detected at cell-cell contacts. {ECO:0000250}.
DR  UNIPROT: Q9QVP9;
DR  UNIPROT: B2RQ16;
DR  UNIPROT: G3X8V1;
DR  Pfam: PF00373;
DR  Pfam: PF18038;
DR  Pfam: PF03623;
DR  Pfam: PF07714;
DR  PROSITE: PS50057;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376' (By similarity). Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10881171, ECO:0000269|PubMed:11238453, ECO:0000269|PubMed:12960403, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:17537919, ECO:0000269|PubMed:17698736, ECO:0000269|PubMed:17846174, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:19561089, ECO:0000269|PubMed:19880522, ECO:0000269|PubMed:20688918, ECO:0000269|PubMed:21640103}.
DE  Reference Proteome: Yes;
DE  Interaction: P16054; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P35438; IntAct: EBI-396959; Score: 0.46
DE  Interaction: Q9QWY8; IntAct: EBI-8651469; Score: 0.65
DE  Interaction: P59240; IntAct: EBI-11790541; Score: 0.40
DE  Interaction: Q9EPK7; IntAct: EBI-17171503; Score: 0.35
DE  Interaction: Q8BIZ1; IntAct: EBI-26595802; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
GO  GO:0097440;
GO  GO:0030424;
GO  GO:0044297;
GO  GO:0005938;
GO  GO:0042995;
GO  GO:0005856;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0045121;
GO  GO:0043025;
GO  GO:0017146;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0043423;
GO  GO:0005524;
GO  GO:0004683;
GO  GO:0019899;
GO  GO:0004972;
GO  GO:0004715;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0043621;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0031625;
GO  GO:0007015;
GO  GO:0090630;
GO  GO:0042976;
GO  GO:0002250;
GO  GO:0001525;
GO  GO:0043534;
GO  GO:0045453;
GO  GO:0007155;
GO  GO:0030154;
GO  GO:0007166;
GO  GO:0006968;
GO  GO:0071498;
GO  GO:0071300;
GO  GO:0070098;
GO  GO:0086100;
GO  GO:0007173;
GO  GO:0048041;
GO  GO:0014009;
GO  GO:0045087;
GO  GO:0007229;
GO  GO:0035235;
GO  GO:0060292;
GO  GO:0060291;
GO  GO:0000165;
GO  GO:0002315;
GO  GO:0043066;
GO  GO:0030502;
GO  GO:0008285;
GO  GO:0010656;
GO  GO:0045638;
GO  GO:0043524;
GO  GO:0030279;
GO  GO:0043267;
GO  GO:0031175;
GO  GO:0001556;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0030838;
GO  GO:0045766;
GO  GO:2000538;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:0007204;
GO  GO:2000573;
GO  GO:0010595;
GO  GO:0070374;
GO  GO:2000463;
GO  GO:0046330;
GO  GO:0043507;
GO  GO:0010976;
GO  GO:0045429;
GO  GO:0051000;
GO  GO:0050731;
GO  GO:0043552;
GO  GO:0045860;
GO  GO:0051247;
GO  GO:2000379;
GO  GO:0051968;
GO  GO:0045727;
GO  GO:2000060;
GO  GO:0006468;
GO  GO:2000249;
GO  GO:0050848;
GO  GO:0030155;
GO  GO:0008360;
GO  GO:0010752;
GO  GO:2000114;
GO  GO:0032960;
GO  GO:0010758;
GO  GO:0045428;
GO  GO:2000310;
GO  GO:0051279;
GO  GO:2000058;
GO  GO:0051592;
GO  GO:0051591;
GO  GO:0043157;
GO  GO:0042220;
GO  GO:0045471;
GO  GO:0009749;
GO  GO:0009725;
GO  GO:0042542;
GO  GO:0001666;
GO  GO:0035902;
GO  GO:0002931;
GO  GO:0010226;
GO  GO:0009612;
GO  GO:0009410;
GO  GO:0007172;
GO  GO:0002040;
GO  GO:0043149;
GO  GO:0007169;
GO  GO:0033209;
GO  GO:0048010;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSGVSEPLSRVKVGTLRRPEGPPEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIQEIITSILLSGRI
SQ  GPNIQLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRN
SQ  DYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYAS
SQ  LREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDTKPTCLAEFKQIKSIRCLPLEETQAVL
SQ  QLGIEGAPQSLSIKTSSLAEAENMADLIDGYCRLQGEHKGSLIMHAKKDGEKRNSLPQIPTLNLEARRSHLSESCSIESD
SQ  IYAEIPDETLRRPGGPQYGVAREEVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTQDNKEKFMSEAVIMKN
SQ  LDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVPTLVLYTLQICKAMAYLESINCVHRDIAVRNILVASP
SQ  ECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEK
SQ  GDRLPKPELCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDIYQMEKDIAIEQERNARYRPPKILEPTTFQEPPPKPSRP
SQ  KYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIRPSSREEAQQLWEAE
SQ  KIKMKQVLERQQKQMVEDSQWLRREERCLDPMVYMNDKSPLTPEKEAGYTEFTGPPQKPPRLGAQSIQPTANLDRTDDLV
SQ  YHNVMTLVEAVLELKNKLGQLPPEDYVVVVKNVGLNLRKLIGSVDDLLPSLPASSRTEIEGTQKLLNKDLAELINKMKLA
SQ  QQNAVTSLSEDCKRQMLTASHTLAVDAKNLLDAVDQAKVVANLAHPPAE
//
ID  P70600;
PN  Protein-tyrosine kinase 2-beta;
GN  Ptk2b;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:9645946}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:9645946}; Peripheral membrane protein {ECO:0000269|PubMed:9645946}; Cytoplasmic side {ECO:0000269|PubMed:9645946}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with integrins at the cell periphery. Interaction with NPHP1 induces the membrane-association of the kinase. Colocalizes with PXN at the microtubule-organizing center. The tyrosine phosphorylated form is detected at cell-cell contacts (By similarity). {ECO:0000250}. [Isoform 2]: Cell junction, focal adhesion. Note=Localizes to focal adhesions, but not isoform 1 and isoform 3.
DR  UNIPROT: P70600;
DR  UNIPROT: O88489;
DR  UNIPROT: Q3T1H4;
DR  UNIPROT: Q63201;
DR  Pfam: PF00373;
DR  Pfam: PF18038;
DR  Pfam: PF03623;
DR  Pfam: PF07714;
DR  PROSITE: PS50057;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376' (By similarity). Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:7544443}.
DE  Reference Proteome: Yes;
DE  Interaction: Q62848; IntAct: EBI-8651337; Score: 0.40
DE  Interaction: Q9WUD9; IntAct: EBI-16803792; Score: 0.40
GO  GO:0097440;
GO  GO:0030424;
GO  GO:0044297;
GO  GO:0005938;
GO  GO:0042995;
GO  GO:0005856;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0045121;
GO  GO:0043025;
GO  GO:0017146;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0043423;
GO  GO:0005524;
GO  GO:0004683;
GO  GO:0019899;
GO  GO:0004715;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0043621;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0031625;
GO  GO:0007015;
GO  GO:0090630;
GO  GO:0042976;
GO  GO:0002250;
GO  GO:0001525;
GO  GO:0043534;
GO  GO:0045453;
GO  GO:0007155;
GO  GO:0030154;
GO  GO:0007166;
GO  GO:0006968;
GO  GO:0071498;
GO  GO:0071300;
GO  GO:0070098;
GO  GO:0086100;
GO  GO:0007173;
GO  GO:0048041;
GO  GO:0014009;
GO  GO:0045087;
GO  GO:0007229;
GO  GO:0035235;
GO  GO:0060292;
GO  GO:0060291;
GO  GO:0000165;
GO  GO:0002315;
GO  GO:0043066;
GO  GO:0030502;
GO  GO:0008285;
GO  GO:0010656;
GO  GO:0045638;
GO  GO:0043524;
GO  GO:0030279;
GO  GO:0043267;
GO  GO:0031175;
GO  GO:0001556;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0030838;
GO  GO:0045766;
GO  GO:2000538;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0001954;
GO  GO:0007204;
GO  GO:2000573;
GO  GO:0010595;
GO  GO:0070374;
GO  GO:2000463;
GO  GO:0046330;
GO  GO:0043507;
GO  GO:0010976;
GO  GO:0045429;
GO  GO:0051000;
GO  GO:0050731;
GO  GO:0043552;
GO  GO:0045860;
GO  GO:0051247;
GO  GO:2000379;
GO  GO:0051968;
GO  GO:0045727;
GO  GO:2000060;
GO  GO:0006468;
GO  GO:2000249;
GO  GO:0050848;
GO  GO:0030155;
GO  GO:0008360;
GO  GO:0010752;
GO  GO:2000114;
GO  GO:0032960;
GO  GO:0010758;
GO  GO:0045428;
GO  GO:2000310;
GO  GO:0051279;
GO  GO:2000058;
GO  GO:0051592;
GO  GO:0051591;
GO  GO:0043157;
GO  GO:0042220;
GO  GO:0045471;
GO  GO:0009749;
GO  GO:0009725;
GO  GO:0042542;
GO  GO:0001666;
GO  GO:0035902;
GO  GO:0002931;
GO  GO:0010226;
GO  GO:0009612;
GO  GO:0010243;
GO  GO:0006970;
GO  GO:0000302;
GO  GO:0009410;
GO  GO:0007172;
GO  GO:0002040;
GO  GO:0043149;
GO  GO:0007169;
GO  GO:0033209;
GO  GO:0048010;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:9645946};
SQ  MSGVSEPLSRVKVGTLRPPEGPPEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIQEIITSILLSGRI
SQ  GPNIQLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRN
SQ  DYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYAS
SQ  LREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDTKPTCLAEFKQIRSIRCLPLEETQAVL
SQ  QLGIEGAPQSLSIKTSSLAEAENMADLIDGYCRLQGEHKGSLIIHAKKDGEKRNSLPQIPTLNLESRRSHLSESCSIESD
SQ  IYAEIPDETLRRPGGPQYGVAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEAVIMKN
SQ  LDHPHIVKLIGIIEEEPTWIVMELYPYGELGHYLERNKNSLKVPTLVLYALQICKAMAYLESINCVHRDIAVRNILVASP
SQ  ECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEK
SQ  GDRLPKPELCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDIYQMERDIAIEQERNARYRPPKILEPTAFQEPPPKPSRP
SQ  KYKHPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIRPSSREEAQQLWEAE
SQ  KIKMRQVLDRQQKQMVEDSQWLRREERCLDPMVYMNDKSPLTPEKEAGYTEFTGPPQKPPRLGAQSIQPTANLDRTDDLV
SQ  YHNVMTLVEAVLELKNKLSQLPPEEYVVVVKNVGLNLRKLIGSVDDLLPSLPASSRTEIEGTQKLLNKDLAELINKMRLA
SQ  QQNAVTSLSEDCKRQMLTASHTLAVDAKNLLDAVDQAKVVANLAHPPAE
//
ID  A2VE78;
PN  F-box/LRR-repeat protein 5;
GN  FBXL5;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: A2VE78;
DR  Pfam: PF12937;
DR  Pfam: PF01814;
DR  Pfam: PF13516;
DR  PROSITE: PS50181;
DE  Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0005506;
GO  GO:0055072;
GO  GO:0045732;
GO  GO:0016567;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPFPEEVDVFTAPHWRMKQLVGLYCDKLSKTNFSNNNDFRALLQSLYATFKEFKMHEQIENEYIIGLLQQRSQTIYNVH
SQ  SDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTKDFLPHMKEEEEVFQPMLMEYFTYEELKDIKKKVIAQHCS
SQ  QKDTAELLRGLSLWNQAEERQKFFKYSVDEKSDKEAEVSEQSTGITHLPPEVMVSIFSYLNPQELCRCSQVSTKWSQLAK
SQ  TGSLWKHLYPVHWARGDWYSGPAAELDTEPDEEWVKSRRDESRAFQEWDEDADIDESEESGEESIAISIAQMEKRLLHGL
SQ  IHNVLPYVGTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTDISDSAFDSWSWLGCCQSLRHLDLSGCEKITDVA
SQ  LEKISRALGILTTHESGLLKTSTSKVTSTTWKNKDITMQSFKQSACLHDVTNKDIGEEVDNEHPWTKPISSDDFTSPYVW
SQ  MLDAEDLADIEDAVEWRHRNVESLCVMETASNFSCPSSACYSKDIVGLRTSVCWQQHCASPAFAYCGHSYCCTGTALRTM
SQ  SALPESSALCRKAPRTRLLREKDLIYSGSEKSDQETGRVLLFLSLSGCYQITDHGLRVLTLGGGLPYLEHLNLSGCLTVT
SQ  GAGLQDLVSACPSLNDEYFYYCDNINGPHADTASGCQNLQCGFRACCRSGE
//
ID  Q2YDQ5;
PN  F-box/LRR-repeat protein 5;
GN  fbxl5;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q2YDQ5;
DR  Pfam: PF12937;
DR  Pfam: PF01814;
DR  Pfam: PF13516;
DR  PROSITE: PS50181;
DE  Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of ireb2/irp2. Upon high iron and oxygen level, it specifically recognizes and binds ireb2/irp2, promoting its ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0005506;
GO  GO:0055072;
GO  GO:0016567;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPFPDEVDVFTGPHWRMKQLVGLYSEKLSNTNFSNNRDFRSFLQSLLDTFTEFKKHEQIENECIMELLQERSHTVYHVH
SQ  ADNKLSDMLTLFQKGLRSVTSEFEQLNYAQQLKERLEAFTQDFIPHMKEEEEVYQPMLMEYFSYEELKAIKQQVMLQHCS
SQ  SQCQSSCSDTHTLLKGLSLWSHAELQKAFKYSDHEKTGDERVLERVSVSSLPQELLLRIFRFLGPQDLCRCAQVCSVWTQ
SQ  VTRTGSLWRHLYPVRWARGEYYSGPPGDLDLEPDDDWIKSLQDDGRAYQEWDEDADVDESEEASAERSSISALQREKLLL
SQ  NGIIQKLLPAVGSSVRSLSLAYSSTLSSKMVRQMLSLCPNLTHLDLTQTDVSDSAFDSWCALGACGTLQHLDLSGCDKIT
SQ  DRTLKILSVGLGDSSTPSPAHKLLQAPPSPIRIEEPRLQPMGRSCQDLIFKRRPGGRGSGCGPTHIWVLDPVKLADIEDA
SQ  ADWSRRGGVASQEIGCGGISEALSASCCCRRSQRRGFRTGLSSSPWQYGDALCGHSSCCSSDAAAIRTQSDLQATGGSAE
SQ  LRTKCWFEGQSCAEHHNRTDQSGAQRALRFLSLSGCHQITDLGLRCVCLRGGLPLLEHLNLSGCPLITGAGLQEVVSASP
SQ  ALNIEHFYYCDNINGPHADTASGCQNLQCGFRVCCRSGE
//
ID  Q9UKA1;
PN  F-box/LRR-repeat protein 5;
GN  FBXL5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17532294}.
DR  UNIPROT: Q9UKA1;
DR  UNIPROT: A8MSK4;
DR  UNIPROT: B4DIB5;
DR  UNIPROT: Q4W5A8;
DR  UNIPROT: Q8NHP3;
DR  UNIPROT: Q9NXN2;
DR  UNIPROT: Q9P0I0;
DR  UNIPROT: Q9P0X5;
DR  UNIPROT: Q9UJT7;
DR  UNIPROT: Q9UKC8;
DR  PDB: 3U9J;
DR  PDB: 3U9M;
DR  PDB: 3V5X;
DR  PDB: 3V5Y;
DR  PDB: 3V5Z;
DR  PDB: 6VCD;
DR  Pfam: PF12937;
DR  Pfam: PF01814;
DR  Pfam: PF13516;
DR  PROSITE: PS50181;
DR  OMIM: 605655;
DR  DisGeNET: 26234;
DE  Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued. {ECO:0000269|PubMed:17532294, ECO:0000269|PubMed:19762596, ECO:0000269|PubMed:19762597}.
DE  Reference Proteome: Yes;
DE  Interaction: P49454; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.53
DE  Interaction: P10242; IntAct: EBI-2692353; Score: 0.00
DE  Interaction: Q5NID2; IntAct: EBI-2806872; Score: 0.00
DE  Interaction: P63208; IntAct: EBI-8636412; Score: 0.83
DE  Interaction: Q09472; IntAct: EBI-3937381; Score: 0.37
DE  Interaction: O43929; IntAct: EBI-3938477; Score: 0.44
DE  Interaction: P67870; IntAct: EBI-7133308; Score: 0.37
DE  Interaction: P53350; IntAct: EBI-7312743; Score: 0.37
DE  Interaction: Q9Y4X5; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q9Y3D0; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q9UNS2; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q9H2Y7; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q9BQ90; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q96T76; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q96JN8; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q92624; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q8N5M4; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q562R1; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q3KQU3; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: P61201; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: P60709; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: P28676; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: P26232; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: O95714; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: O76071; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: O75521; IntAct: EBI-21796233; Score: 0.35
DE  Interaction: Q13148; IntAct: EBI-25985913; Score: 0.56
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0000151;
GO  GO:0005506;
GO  GO:0004842;
GO  GO:0055072;
GO  GO:0045732;
GO  GO:0016567;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPFPEEVDVFTAPHWRMKQLVGLYCDKLSKTNFSNNNDFRALLQSLYATFKEFKMHEQIENEYIIGLLQQRSQTIYNVH
SQ  SDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTRDFLPHMKEEEEVFQPMLMEYFTYEELKDIKKKVIAQHCS
SQ  QKDTAELLRGLSLWNHAEERQKFFKYSVDEKSDKEAEVSEHSTGITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTK
SQ  TGSLWKHLYPVHWARGDWYSGPATELDTEPDDEWVKNRKDESRAFHEWDEDADIDESEESAEESIAISIAQMEKRLLHGL
SQ  IHNVLPYVGTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTDISDSAFDSWSWLGCCQSLRHLDLSGCEKITDVA
SQ  LEKISRALGILTSHQSGFLKTSTSKITSTAWKNKDITMQSTKQYACLHDLTNKGIGEEIDNEHPWTKPVSSENFTSPYVW
SQ  MLDAEDLADIEDTVEWRHRNVESLCVMETASNFSCSTSGCFSKDIVGLRTSVCWQQHCASPAFAYCGHSFCCTGTALRTM
SQ  SSLPESSAMCRKAARTRLPRGKDLIYFGSEKSDQETGRVLLFLSLSGCYQITDHGLRVLTLGGGLPYLEHLNLSGCLTIT
SQ  GAGLQDLVSACPSLNDEYFYYCDNINGPHADTASGCQNLQCGFRACCRSGE
//
ID  Q8C2S5;
PN  F-box/LRR-repeat protein 5;
GN  Fbxl5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q8C2S5;
DR  UNIPROT: Q14CG1;
DR  UNIPROT: Q3TAK6;
DR  UNIPROT: Q3TWC9;
DR  UNIPROT: Q3UC66;
DR  UNIPROT: Q80XI5;
DR  UNIPROT: Q8BGF5;
DR  UNIPROT: Q8BNL3;
DR  UNIPROT: Q8C3Q8;
DR  Pfam: PF12937;
DR  Pfam: PF01814;
DR  Pfam: PF13516;
DR  PROSITE: PS50181;
DE  Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0005506;
GO  GO:0055072;
GO  GO:0045732;
GO  GO:0030163;
GO  GO:0016567;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPFPDEVDVFTAPHWRMKQLVGRYCDKLSKTNFSNNNDFRALLQSLYATFKEFKMHEQIENEYIIGLLQQRSQTIYNVH
SQ  SDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTRDFLPHMKEEEEVFQPMLMEYFTYEELKDIKKKVIAQHCS
SQ  QKDTAELLRGLSLWNQAEERQKVLKYSVDEKADTEAEVSEHSTGITHLPPEVMLSIFSYLNPQELCRCSQVSTKWSQLAK
SQ  TGSLWKHLYPVHWARGDWYSGPATELDTEPDEEWVRNRKDESRAFQEWDEDADIDESEESAEESVAISIAQMEKRVLHGL
SQ  IHNVLPYVGTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTDISDSAFDSWSWLGCCQSLRHLDLSGCEKITDMA
SQ  LEKISRALGVLTSHQSGFLKSAGKAASTPWTSKDITMPSTTQYACLHNLTDKGIGEEIDNEHSWTEPVSSESLTSPYVWM
SQ  LDAEDLADIEDAVEWRHRNVESLCVMETASNFGCSSSGCYSKDIVGLRTSVCWQQHCASPAFAYCGHSFCCTGTALRTMT
SQ  TLPATSAMCRKALRTTLPRGKDLIYFGSEKSDQETGRVLLFLSLSGCYQITDHGLRALTLGGGLPYLEHLNLSGCLTVTG
SQ  AGLQDLVSACPSLNDEYFYYCDNINGPHADTASGCQNLQCGFRACCRSGE
//
ID  Q5R6E1;
PN  F-box/LRR-repeat protein 5;
GN  FBXL5;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q5R6E1;
DR  Pfam: PF12937;
DR  Pfam: PF01814;
DR  Pfam: PF13516;
DR  PROSITE: PS50181;
DE  Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0005506;
GO  GO:0055072;
GO  GO:0016567;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPFPEEVDVFTAPHWRTKQLVGLYCDKLSKTNFSNNNDFRALLQSLYATFKEFKMHEQIENEYIIGLLQQRSQTIYNVH
SQ  SDNKLSEMLSLFEKGLKNVKNEYEQLNYAKQLKERLEAFTRDFLPHMKEEEEVFQPMLMEYFTYEELKDIKKKVIAQHCS
SQ  QKDTAELLRGLSLWNHAEERQKFFKYSVDEKSDKEAEVSEHSTGITHLPPEVMLSIFSYLNPQELCRCSQVSMKWSQLTK
SQ  TGSLWKHLYPVHWARGDWYSGPATGLDTEPDEEWVKNRKDESRAFHEWDEDADIDESEESVEESIAISIAQMEKRLLHGL
SQ  IHNVLPYVGTSVKTLVLAYSSAVSSKMVRQILELCPNLEHLDLTQTDISDSAFDSWSWLGCCQSLRHLDLSGCEKITDVA
SQ  LEKISRALGILTSHQSGFLKTSTSKITSTTWKNKDVTMQSTKQYAYLHDLTNKGIGEEIDNEHPWTKPVSSENFTSPYLW
SQ  MLDAEDLADIEDTVEWRHRNVESLCVVETASNFSCSTSGCFSKDIVGLRTSVCWQQHCASPAFAYCGHSFCCTGTALRTM
SQ  SALPESSAMCRKASRTRLPRGKDLIYFGSEKSDQETGRVLLFLSLSGCYQITDHGLRVLTLGGGLPYLEHLNLSGCLTIT
SQ  GAGLQDLVSACPSLNDEYFYYCDNINGPHADTASGCQNLQCGFRACCRSGE
//
ID  C0HAC0;
PN  F-box/LRR-repeat protein 5;
GN  fbxl5;
OS  8030;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: C0HAC0;
DR  Pfam: PF12937;
DR  Pfam: PF01814;
DR  Pfam: PF13516;
DR  PROSITE: PS50181;
DE  Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of ireb2/irp2. Upon high iron and oxygen level, it specifically recognizes and binds ireb2/irp2, promoting its ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0005506;
GO  GO:0055072;
GO  GO:0016567;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPFPDEVDVFTGPHWRMKQLVGLYCEKLSQTNFSNNNDFRSFLQSLCATFKEFKMHEQIENEYIIGLLQQRSCNVYNVH
SQ  SDNKLSEMLSLFEKGLRSVKSENEQLNYAQQLKERLEAFTQDFLPHMKEEEEVFQPMLMQYFTYEELKDIKKQVIAQHSS
SQ  QQRWDCAAEVLKGLSLWSQAEELHKAFKYADHEKTDDELEKELCSTHISQLPTEILLCLFRYLGPEDLCHCGQVCSAWSD
SQ  LAKTGSLWRHLYPVRWARGDYYRGPPDDVNQEPDEEWVKSLQDEGKAYQEWDEDADVDESDASCEDSLAISAAQREKKLL
SQ  NGMIQNLLPAVGSSVRSIVLAYSSTVSSKMVRQILSLCPNLTHLDLTQTDVTDSAFDSWSSLWACLSLEHLDLSGCEKLT
SQ  DRTLKKLSLGLGDLASPTCSEKRSDRRAKLLKSPPSPISLLDKRSLRPTGHSRQVLIFKQWPGKLGSAPCSPTRVWVLDA
SQ  SELADIEDAAEWNRRRGVSTPEVRGFVETQPGGLSCCCRRRRGGFRTGFSTSYWQQQYGLGEAGCGHSTCCTGETALRTL
SQ  GGLQYESYTTRGSAGAEFRTKCSSGGQLCLECDNRTDPSDGRRSLRFLSLSGCYQVTDLGLRALSQRGGLPLLEHLNLSG
SQ  CLLITEVGLQELVSACPALNDEHFYYCDNINGPHADTASGCQNLQCGFRVCCRSGE
//
ID  Q6INS1;
PN  F-box/LRR-repeat protein 5;
GN  fbxl5;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q6INS1;
DR  Pfam: PF12937;
DR  Pfam: PF01814;
DR  Pfam: PF13516;
DR  PROSITE: PS50181;
DE  Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of ireb2/irp2. Upon high iron and oxygen level, it specifically recognizes and binds ireb2/irp2, promoting its ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0005506;
GO  GO:0055072;
GO  GO:0016567;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPFPDEVDLFTGPHWRMKQLVGRYCEKLSNTNFSNNNDLLALLQSLYETFKEFKMHEQIENEYIIGLLQQRSHTVYNVH
SQ  SDNKLSEMLVLFEKGMKNVKNEYKQLNYVQQLKERLEAFTSDFLPHMKEEEEVFQPMLMEYFTYDEMKDIKKKVIAQHCS
SQ  QKDTTELLRGLSLWNKAEELQKVLKYSVDEKAERNSKTQKSSSSISSLPPEVMLNIFTYLNPQDLCRCSQVNTEWAQLAK
SQ  TGSLWRHLYPVLWARGDWYSGSHAYLDNEPDEDWISRRKDESRAYQEWDEDADIDESEETGEEEDSSISMAQREKELLNS
SQ  LVHYILPYVGHSVKTLVLAYSSATSSKVIRQMLEYCPNLEHLDLTQTDISDSAFNGWHFGACQTLHHIDLSGCDKITDLT
SQ  LEKLSVALGIPSAHKKRLLKCYRNNRTLKDIRNQMRCSSLAQITGESTIYSDAFWANSDRSQDYTSPPIWILDSGNPGDI
SQ  EDAADWKFRTTDGLCVLEMAPSVTCFSNGCCSRARPGRWTNVGWQEHCKAATVSYCGHTLCGNTLRTIHTLPEASALCNI
SQ  GTRTLHSDITDCFPGSAKSDQQAARALQFLSLSGCHQITDHGLRALTIGGGLPKLEHLNLSGCLNVTGSGLQDLVATCPS
SQ  LNDEHFYYCDNISGPHGATASGCQNLQCGFRMCCRSGE
//
ID  Q5XGI3;
PN  F-box/LRR-repeat protein 5;
GN  fbxl5;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q5XGI3;
DR  Pfam: PF12937;
DR  Pfam: PF01814;
DR  Pfam: PF13516;
DR  PROSITE: PS50181;
DE  Function: Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of ireb2/irp2. Upon high iron and oxygen level, it specifically recognizes and binds ireb2/irp2, promoting its ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0005506;
GO  GO:0055072;
GO  GO:0016567;
GO  GO:0031146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPFPDEVDLFTGPHWRMKQLVGRYCEKLSNTNFSSNTDFLALLQSLYETFKEFKMHEQIENEYIIGLLQQRSQTVFNVH
SQ  SDNKLSEMLVLFEKGMKNNEYEQLNYAQQLKERLEAFTSDFLPHMKEEEEVFQPMLMEYFTYDELKDIKKKVIAQHCSQK
SQ  DTAELLRGFSLWNKAEELQKVFKYSVDEKIERDSKNRKSSASICNLPPEVMLNIFSYLNPQDLCRCSQVNTKWAQLARTG
SQ  SLWRHLYPVLWARGDWYSGPPTHLDNEPDEDWISRRKDESRAYQEWDEDADIDESEETGEDDPSISVAQREKELLNSLVH
SQ  YILPYIGHSVKTLVLAYSSATSNKVIRQILEYCPNMEHLDLTQTDISDSAFNGWCFGACQTLRHIDLSGCEKITDSALEK
SQ  LSVALGMPLAHKKRLLKCYRNNRTVKDIRNQMRCGSLAQITGESGIYSDYSSSQIWILNSGNLGDIEDAADWKFRTTDGL
SQ  GVLEMTPNLTCFSNGCCSRAVPGRWTNVIRQEHCKAAPLNYCGHTLCGNTLRTIQALPGSNIGTKTLQSEIRDICPGSAK
SQ  LDQQVARVLQFLSLSGCHQITDHGLRVLTIGGGLPNLEHLNLSGCLNVTGSGLQDLVSACPSLNDEHFYYCDNISGPHAA
SQ  TASGCQNLQCGFRACCRSGE
//
ID  Q8N3Y1;
PN  F-box/WD repeat-containing protein 8;
GN  FBXW8;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:21572988}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:P0DL28}.
DR  UNIPROT: Q8N3Y1;
DR  UNIPROT: Q9UK95;
DR  Pfam: PF12937;
DR  PROSITE: PS50181;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 609073;
DR  DisGeNET: 26259;
DE  Function: Substrate-recognition component of a Cul7-RING ubiquitin- protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7- RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) (PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation (PubMed:24362026). Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions (PubMed:24793695). {ECO:0000269|PubMed:18498745, ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24362026, ECO:0000269|PubMed:24793695}.
DE  Reference Proteome: Yes;
DE  Interaction: O75147; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: P0C6X4; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P0C6X5; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P0C6X6; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q14999; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-914791; Score: 0.56
DE  Interaction: P01106; IntAct: EBI-1228329; Score: 0.57
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.46
DE  Interaction: Q13620; IntAct: EBI-21332061; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-7902921; Score: 0.64
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q12798; IntAct: EBI-21576600; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-21594461; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-21594293; Score: 0.35
DE  Interaction: Q8NA56; IntAct: EBI-21620988; Score: 0.35
DE  Interaction: O14958; IntAct: EBI-21622768; Score: 0.35
DE  Interaction: O60293; IntAct: EBI-21634559; Score: 0.35
DE  Interaction: Q9H9D4; IntAct: EBI-21642543; Score: 0.35
DE  Interaction: D6R9G5; IntAct: EBI-21662389; Score: 0.35
DE  Interaction: O14978; IntAct: EBI-21712468; Score: 0.35
DE  Interaction: Q16539; IntAct: EBI-21766048; Score: 0.35
DE  Interaction: Q96BR6; IntAct: EBI-21784034; Score: 0.35
DE  Interaction: O14737; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: Q15645; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: P84077; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: Q9H0W5; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: P61758; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: P78371; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: Q99471; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: Q92526; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: B1WBR1; IntAct: EBI-15927171; Score: 0.40
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q13619; IntAct: EBI-30863570; Score: 0.35
DE  Interaction: Q8WV16; IntAct: EBI-30863977; Score: 0.35
GO  GO:0031467;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0008283;
GO  GO:0007030;
GO  GO:0060716;
GO  GO:0050775;
GO  GO:1901485;
GO  GO:0016567;
GO  GO:0060712;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDYSLDEFRRRWQEELAQAQAPKKRRRPEAAERRARRPEVGSGRGEQASGDPALAQRLLEGAGRPPAARATRAEGQDVA
SQ  SRSRSPLAREGAGGGEQLVDQLIRDLNEMNDVPFFDIQLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLC
SQ  QQEGHLPDSSISDYSCWKLIFQECRAKEHMLRTNWKNRKGAVSELEHVPDTVLCDVHSHDGVVIAGYTSGDVRVWDTRTW
SQ  DYVAPFLESEDEEDEPGMQPNVSFVRINSSLAVAAYEDGFLNIWDLRTGKYPVHRFEHDARIQALALSQDDATVATASAF
SQ  DVVMLSPNEEGYWQIAAEFEVPKLVQYLEIVPETRRYPVAVAAAGDLMYLLKAEDSARTLLYAHGPPVTCLDVSANQVAF
SQ  GVQGLGWVYEGSKILVYSLEAGRRLLKLGNVLRDFTCVNLSDSPPNLMVSGNMDGRVRIHDLRSGNIALSLSAHQLRVSA
SQ  VQMDDWKIVSGGEEGLVSVWDYRMNQKLWEVYSGHPVQHISFSSHSLITANVPYQTVMRNADLDSFTTHRRHRGLIRAYE
SQ  FAVDQLAFQSPLPVCRSSCDAMATHYYDLALAFPYNHV
//
ID  Q8BIA4;
PN  F-box/WD repeat-containing protein 8;
GN  Fbxw8;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DL28}. Golgi apparatus {ECO:0000250|UniProtKB:P0DL28}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:P0DL28}.
DR  UNIPROT: Q8BIA4;
DR  UNIPROT: Q8BI62;
DR  UNIPROT: Q8BI75;
DR  UNIPROT: Q8BI76;
DR  UNIPROT: Q8CID8;
DR  UNIPROT: Q921Z1;
DR  Pfam: PF12937;
DR  PROSITE: PS50181;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Substrate-recognition component of a Cul7-RING ubiquitin- protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7- RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions (By similarity). {ECO:0000250|UniProtKB:Q8N3Y1}.
DE  Reference Proteome: Yes;
GO  GO:1990393;
GO  GO:0031467;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0004842;
GO  GO:0008283;
GO  GO:0007030;
GO  GO:0060716;
GO  GO:0050775;
GO  GO:1901485;
GO  GO:0016567;
GO  GO:0060712;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDHNLEEFRRHWQEELAQSQALRRRRRLEAGERRSPRRPEAGARGEPASGYLGLAQGLLEGAGRPPAPRPGRGGDRKDT
SQ  SSRSRSPPDRDATEPEPLVDQLIRDLNELDDVPFFDVRLPYELAINIFQYLNRRELGLCAQVSKTWKVIAEDEVLWYRLC
SQ  RQEGHLPHSRFSDYTCWKLILQECLAKEHTLRANWKNRKGAVSELEHVPDAVLCDVRSHDGVVIAGYTSGDVRVWDTRTW
SQ  DYVAPFLESESEEEDPGMQPYVSFVRINSSLAVAAYEDGILNIWDLRTGRFPIFRFEHDARIQALALSQEKPIVATASAF
SQ  DVVMLYPNEEGHWHVASEFEVQKLVDYLEIVPNTGRYPVAIATAGDLVYLLKADDSARTLHYVYGQPATCLDVSASQVAF
SQ  GVKSLGWVYEGNKILVYSLEAERCLSKLGNALGDFTCVNIRDSPPNLMVSGNMDRRVRIHDLRSDKIALSLSAHQLGVSA
SQ  VQMDDWKVVSGGEEGLVSVWDYRMNQKLWEVHSRHPVRYLSFNSHSLITANVPYEKVLRNSDLDNFACHRRHRGLIHAYE
SQ  FAVDQLAFQSPLPVCRLPRDIMAGYSYDLALSFPHDSI
//
ID  P0DL28;
PN  F-box/WD repeat-containing protein 8;
GN  Fbxw8;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:21572988}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons.
DR  UNIPROT: P0DL28;
DR  Pfam: PF12937;
DR  PROSITE: PS50181;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Substrate-recognition component of a Cul7-RING ubiquitin- protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7- RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions (By similarity). The Cul7-RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. {ECO:0000250|UniProtKB:Q8N3Y1, ECO:0000269|PubMed:21572988}.
DE  Reference Proteome: Yes;
DE  Interaction: D3ZEF4; IntAct: EBI-15927289; Score: 0.40
DE  Interaction: O35254; IntAct: EBI-15927211; Score: 0.40
GO  GO:1990393;
GO  GO:0031467;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0019005;
GO  GO:0004842;
GO  GO:0008283;
GO  GO:0007030;
GO  GO:0060716;
GO  GO:0050775;
GO  GO:1901485;
GO  GO:0016567;
GO  GO:0060712;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDHNLEEFRQRWQEELAHSQVLRRRRRLEAGERRPRRPEAGARGEPASGYLGLAQGLLEGAGRPPAPRPGRTDRKDVSS
SQ  RSRSPPDRDAAEPEPLVDQLIRDLNEMDDVPFFDVHLPYELAINIFQYLNRRELGLCAQVSKTWKVIAEDEVLWYRLCRQ
SQ  EGHLPHSRFSDYTCWKLILQECLAPVHLIRPSWMNRKGAVSELEHVPDAVLCDVRSHDGVVIAGYTSGEVRVWDTRTWDY
SQ  VAPFLESESEEEDPGMQPYVSFVRINSSLAVAAYEDGILNVWDLRTGRFPIFRFEHDARIQALALSQEKPVVATASAFDV
SQ  VMLYPNEEGNWHVASEFEVQKLVDYLEIVPNTGRYPVAIATAGDLVYLLKAEDSARTLHYVYGQPATCLDVSASQVAFGV
SQ  KSLGWVYEGNKILVYSLEAERCLSKLGNALGDFTCVNIRDSPPNLMVSGNMDRRVRLHDLRTDKIALSLSAHQLGVSAVQ
SQ  MDDWKIVSGGEEGLVSVWDYRMNQKLWEVHSRHPVRYISFNSHSLITANVPYEKVLRNSDLDNFACHRRHRGLIHAYEFA
SQ  VDQLAFQSPLPICRLPRDTVAGYSYDLALSFPYDSI
//
ID  A8X181;
PN  Protein adenylyltransferase fic-1;
GN  fic;
OS  6238;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q23544}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q23544}. Nucleus membrane {ECO:0000250|UniProtKB:Q23544}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q23544}. Note=Predominantly localized to the endoplasmic reticulum and to the nucleus. {ECO:0000250|UniProtKB:Q23544}.
DR  UNIPROT: A8X181;
DR  Pfam: PF02661;
DR  PROSITE: PS51459;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Protein that can both mediate the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-273 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Adenylyltransferase that mediates the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins. In vivo target proteins include the heat-shock 70 family proteins hsp-1 and hsp-3 and the translation elongation factors eef-1A, eef-1G and eef-2. Can AMPylate core histone H3 in vitro (By similarity). Can also act as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from target proteins (By similarity). Decreases susceptibility to P.aeruginosa-mediated killing and might therefore play a role in the innate immune response (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q23544, ECO:0000250|UniProtKB:Q8SWV6}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0016787;
GO  GO:0070733;
GO  GO:0050829;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSVRRRTHSDDFSFRLERTRRPSKLDVLRESPTLPVQQGYSLTTVVLVSLVVTLVCQNVAPPAFSYLNQLIKNSPKRKIP
SQ  GQSNRLNIGFISTNSPEKFAPAVQKPTFLVDPIYDEKWKGVHTAVPVMTTEPEEKRDNNHAKVKEAILAAKAASRSRRDG
SQ  NLERAVTIMEHAMALAPNNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTNPLVSAIDRKMLKTVHD
SQ  LRNEFAHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLSK
SQ  EHHEISIDDILEMHRRVLGNADPVEAGKIRTTQVYVGKFTPVAPEYVLEQLADMVDWLNDESTMAMDPIERAAIAHYKLV
SQ  LVHPFTDGNGRTARLLLNLIMMRSGFPPVILPVETRAEYYASLHVANLGDLRPFVRYVAKHSEASIQRYIGAMKTSSGNV
SQ  INGEEPNLTAEESKVSEKIETECRAGS
//
ID  Q23544;
PN  Protein adenylyltransferase fic-1;
GN  fic;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27138431}; Single-pass membrane protein. Nucleus membrane {ECO:0000269|PubMed:27138431}; Single-pass membrane protein. Note=Predominantly localized to the endoplasmic reticulum and to the nucleus. {ECO:0000269|PubMed:27138431}.
DR  UNIPROT: Q23544;
DR  PDB: 5JJ6;
DR  PDB: 5JJ7;
DR  Pfam: PF02661;
DR  PROSITE: PS51459;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Protein that can both mediate the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-274 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Adenylyltransferase that mediates the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (PubMed:27138431). In vivo target proteins include the heat-shock 70 family proteins hsp-1 and hsp-3 and the translation elongation factors eef-1A, eef-1G and eef-2 (PubMed:27138431). Can AMPylate core histone H3 in vitro (PubMed:27138431). Can also act as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from target proteins (By similarity). Decreases susceptibility to P.aeruginosa-mediated killing and might therefore play a role in the innate immune response (PubMed:27138431). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6, ECO:0000269|PubMed:27138431}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0016787;
GO  GO:0070733;
GO  GO:0050829;
GO  GO:0018117;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSVRRRTHSDDFSYLLEKTRRPSKLNVVQEDPKSAPPQGYSLTTVIIISVLVSLICQHFVPYAVSTLHTVIKNSPKQKSS
SQ  PPPSNRLNIGFISGNSPEKYAPAVQKPTFLVDPIYDEKWKGIQTAVPVMSTQTDEKRENDPAKVKEAILAAKAAGRSRKD
SQ  GNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTTPLVSAIDRKMLRSVH
SQ  DLRDEFNHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLS
SQ  KEHDEISIDDILEMHRRVLGNADPVEAGRIRTTQVYVGRFTPVSPEYVMEQLKDIVDWLNDESTLTIDPIERAAIAHYKL
SQ  VLVHPFTDGNGRTARLLLNLIMMRSGFPPVILPVETRAEYYASLHVANLGDLRPFVRYVAKHSEASIQRYIGAMKTSSDN
SQ  ILNSGDSKLTPEESEVSEKIEAECRAGN
//
ID  Q6PIW4;
PN  Fidgetin-like protein 1;
GN  FIGNL1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:23754376}. Cytoplasm {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BPY9}. Note=Together with RAD51 and a subset of H2A histone proteins, redistributed in discrete nuclear DNA damage- induced foci after ionizing radiation (IR) treatment (PubMed:23754376).
DR  UNIPROT: Q6PIW4;
DR  UNIPROT: D3DVM6;
DR  UNIPROT: Q86V18;
DR  UNIPROT: Q8ND59;
DR  UNIPROT: Q9H8P1;
DR  UNIPROT: Q9H917;
DR  PDB: 3D8B;
DR  Pfam: PF00004;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DR  OMIM: 615383;
DR  DisGeNET: 63979;
DE  Function: Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation (PubMed:23754376). May play a role in the control of male meiosis dynamic (By similarity). {ECO:0000250|UniProtKB:Q8BPY9, ECO:0000269|PubMed:23754376}.
DE  Reference Proteome: Yes;
DE  Interaction: Q06609; IntAct: EBI-21840775; Score: 0.35
DE  Interaction: O60341; IntAct: EBI-8468384; Score: 0.37
DE  Interaction: Q9WMX2; IntAct: EBI-9079662; Score: 0.37
DE  Interaction: O14713; IntAct: EBI-10181340; Score: 0.56
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q9QWF0; IntAct: EBI-11015136; Score: 0.35
DE  Interaction: Q99576; IntAct: EBI-11128906; Score: 0.35
DE  Interaction: Q9NSG2; IntAct: EBI-11128906; Score: 0.35
DE  Interaction: Q05682; IntAct: EBI-11128906; Score: 0.35
DE  Interaction: Q9H7E2; IntAct: EBI-11128906; Score: 0.35
DE  Interaction: Q96EK4; IntAct: EBI-11128906; Score: 0.35
DE  Interaction: Q96CN9; IntAct: EBI-24633661; Score: 0.56
DE  Interaction: P29401; IntAct: EBI-21539637; Score: 0.35
DE  Interaction: O75366; IntAct: EBI-21577101; Score: 0.35
DE  Interaction: P00740; IntAct: EBI-21577264; Score: 0.35
DE  Interaction: Q9BQ31; IntAct: EBI-21590203; Score: 0.35
DE  Interaction: Q9BTE6; IntAct: EBI-21593012; Score: 0.35
DE  Interaction: Q6IBW4; IntAct: EBI-21600868; Score: 0.35
DE  Interaction: Q6UWQ5; IntAct: EBI-21641185; Score: 0.35
DE  Interaction: Q86YD3; IntAct: EBI-21644294; Score: 0.35
DE  Interaction: Q7Z4W2; IntAct: EBI-21670934; Score: 0.35
DE  Interaction: O15496; IntAct: EBI-21699277; Score: 0.35
DE  Interaction: Q6ZWK4; IntAct: EBI-21782601; Score: 0.35
DE  Interaction: O14593; IntAct: EBI-21807186; Score: 0.35
DE  Interaction: Q96JH7; IntAct: EBI-21840775; Score: 0.35
DE  Interaction: P0CG38; IntAct: EBI-21840775; Score: 0.35
DE  Interaction: P20160; IntAct: EBI-21867396; Score: 0.35
DE  Interaction: B7ZBD5; IntAct: EBI-21871699; Score: 0.35
DE  Interaction: O94808; IntAct: EBI-21881570; Score: 0.35
DE  Interaction: P22105; IntAct: EBI-21892376; Score: 0.40
DE  Interaction: Q9H910; IntAct: EBI-21892399; Score: 0.35
DE  Interaction: P10412; IntAct: EBI-20924530; Score: 0.40
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P09613; IntAct: EBI-21497303; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: O75874; IntAct: EBI-27039729; Score: 0.37
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0000228;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0016787;
GO  GO:0000287;
GO  GO:0008568;
GO  GO:0046034;
GO  GO:0071479;
GO  GO:0007140;
GO  GO:0043066;
GO  GO:2001243;
GO  GO:0001649;
GO  GO:0033687;
GO  GO:0051726;
GO  GO:0010569;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQTSSSRSVHLSEWQKNYFAITSGICTGPKADAYRAQILRIQYAWANSEISQVCATKLFKKYAEKYSAIIDSDNVESGLN
SQ  NYAENILTLAGSQQTDSDKWQSGLSINNVFKMSSVQKMMQAGKKFKDSLLEPALASVVIHKEATVFDLPKFSVCGSSQES
SQ  DSLPNSAHDRDRTQDFPESNRLKLLQNAQPPMVTNTARTCPTFSAPVGESATAKFHVTPLFGNVKKENHSSAKENIGLNV
SQ  FLSNQSCFPAACENPQRKSFYGSGTIDALSNPILNKACSKTEDNGPKEDSSLPTFKTAKEQLWVDQQKKYHQPQRASGSS
SQ  YGGVKKSLGASRSRGILGKFVPPIPKQDGGEQNGGMQCKPYGAGPTEPAHPVDERLKNLEPKMIELIMNEIMDHGPPVNW
SQ  EDIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEK
SQ  MVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLV
SQ  KRLYIPLPEASARKQIVINLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREASLGPIRSLQTADIATITPDQVRPIA
SQ  YIDFENAFRTVRPSVSPKDLELYENWNKTFGCGK
//
ID  Q8BPY9;
PN  Fidgetin-like protein 1;
GN  Fignl1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000269|PubMed:22110678}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22110678}. Note=Together with RAD51 and a subset of H2A histone proteins, redistributed in discrete nuclear DNA damage- induced foci after ionizing radiation (IR) treatment. {ECO:0000250|UniProtKB:Q6PIW4}.
DR  UNIPROT: Q8BPY9;
DR  UNIPROT: Q3UF48;
DR  UNIPROT: Q8C2I6;
DR  UNIPROT: Q9ERZ5;
DR  Pfam: PF00004;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation (PubMed:17352653). May play a role in the control of male meiosis dynamic (PubMed:22110678). {ECO:0000250|UniProtKB:Q6PIW4, ECO:0000269|PubMed:17352653, ECO:0000269|PubMed:22110678}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000228;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0016787;
GO  GO:0000287;
GO  GO:0008568;
GO  GO:0046034;
GO  GO:0071479;
GO  GO:0007140;
GO  GO:0043066;
GO  GO:2001243;
GO  GO:0001649;
GO  GO:0033687;
GO  GO:0051726;
GO  GO:0010569;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METSSSMSVETTRSVQVDEWQKNYCVVTSSICTPKQKADAYRALLLHIQYAYANSEISQVFATNLFKRYTEKYSAIIDSD
SQ  NVVTGLNNYAESIFALAGSRQADSNKWQSGLSIDNVFKMSCVQEMMQAGKKFEESLLEPADASVVLCKEPTAFEVPQLSV
SQ  CGGSEDADILSSSGHDTDKTQAIPGSSLRCSPFQSARLPKETNTTKTCLTSSTSLGESATAAFHMTPLFGNTEKDTQSFP
SQ  KTSTGLNMFLSNLSCVPSGCENPQERKAFNDSDIIDILSNPTLNKAPSKTEDRGRREDNSLPTFKTAKEQLWVDQKKKGH
SQ  QSQHTSKSSNGVMKKSLGAGRSRGIFGKFVPPVSNKQDGSEQHAKKHKSSRAGSAEPAHLTDDCLKNVEPRMVELIMNEI
SQ  MDHGPPVHWDDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT
SQ  SKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEI
SQ  DEAARRRLVKRLYIPLPEASARKQIVGNLMSKEQCCLSDEETDLVVQQSDGFSGADMTQLCREASLGPIRSLHAADIATI
SQ  SPDQVRPIAYIDFENAFKTVRPTVSPKDLELYENWNETFGCGK
//
ID  Q6GX84;
PN  Fidgetin-like protein 1;
GN  Fignl1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BPY9}. Note=Together with RAD51 and a subset of H2A histone proteins, redistributed in discrete nuclear DNA damage- induced foci after ionizing radiation (IR) treatment. {ECO:0000250|UniProtKB:Q6PIW4}.
DR  UNIPROT: Q6GX84;
DR  Pfam: PF00004;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation (By similarity). May play a role in the control of male meiosis dynamic (By similarity). {ECO:0000250|UniProtKB:Q6PIW4}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000228;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0016787;
GO  GO:0000287;
GO  GO:0008568;
GO  GO:0046034;
GO  GO:0071479;
GO  GO:0007140;
GO  GO:0043066;
GO  GO:2001243;
GO  GO:0001649;
GO  GO:0033687;
GO  GO:0051726;
GO  GO:0010569;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METSSSRSVQVDDWQKNYSVVASSICTPKQKADAYRALLLHIQDAYANSEISQVFATNLFKRYTEKYSAIIDSDNVVTGL
SQ  NNYAESIFALAGSQQADSDKWQSGLSINNVFKMSTVQEMMQAGQKFKESLLEPADASVVMCKEPTIFEVPQLGVCGGSEE
SQ  ADLLSSSVHGTEKTQAIPGNSLRCSPFQSTLFPMATNTKTCLTSSAPSGESTTATFHRTPLFGNTKKEPQSFPKTSTGLN
SQ  MFLSNPSCVPSGCENPRERKAFNDSDTINMLSNPTLNKAPSKTEDSGQREDNSLPTFKTAKEQLWADQKKRSHQSQHTSK
SQ  SFNGAIKKSLGAGRSRGIFGKFVPPVSNKQDGSEQNGNVKPKSSRAGSAEPAHLTDDRLKNVEPRMVELIMNEIMDHGPP
SQ  VHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGE
SQ  GEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARR
SQ  RLVKRLYIPLPEASARKQIVVNLMSKEQCCLTDEETELVVQQSDGFSGADMTQLCREASLGPIRSLHTADIATISPDQVR
SQ  PIAYIDFENAFRTVRPSVSPKDLELYENWNKTFGCGK
//
ID  Q6DDU8;
PN  Fidgetin-like protein 1;
GN  fignl1;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BPY9}.
DR  UNIPROT: Q6DDU8;
DR  Pfam: PF00004;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: May be involved in DNA double-strand break (DBS) repair via homologous recombination (HR). May regulate osteoblast proliferation and differentiation (By similarity). {ECO:0000250|UniProtKB:Q6PIW4}.
DE  Reference Proteome: Yes;
GO  GO:0000228;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0016787;
GO  GO:0000287;
GO  GO:0046034;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQIPETSSVHQNEWQRDVFVLSSGTCLPQQKAEVYRAHLAQIQYAWANSEISEASAVHLFKKYAEKYSAILDSDKLEIGL
SQ  NNYADSILTMAKCQRNESDKWQSSLTTNNVLKLKSVQEMAEAGRRAQLSLLNSTDASVRVGNEIGTSGYSTVLAHNVLRN
SQ  PSHAVPHAASSDCQIPEGSSNFLQNSKVSAFTKANTSSNTLINNSIPINTSLMQRNEVKAPTTFSTQSGPNVFSSTTSVY
SQ  SGKRKACYALGDESTDIQPKPLVQRQLASKEATGDSDFKTAKEQLWVDQQKKHSNQPQRNPGPLYGGGKKSLGAARSRGL
SQ  HGKFIPPLPRQEDVEDSNRKVYGQGNSEMNSTSDEHLKNIEPKMIELIMSEIMDHGPPLNWDDIAGLEFAKTTIKEIVVW
SQ  PMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFTVARCHQPAVIFI
SQ  DEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVVS
SQ  LMSKEHCSLTEQEVEAIVLQADGFSGADMTQLCREAALGPIRSIQLMDISTITAEQVRPIAYIDFQSAFLVVRPSVSQKD
SQ  LELYENWNKTFGCGR
//
ID  A4IHT0;
PN  Fidgetin-like protein 1;
GN  fignl1;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q6PIW4}. Cytoplasm {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BPY9}.
DR  UNIPROT: A4IHT0;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: May be involved in DNA double-strand break (DBS) repair via homologous recombination (HR). May regulate osteoblast proliferation and differentiation (By similarity). {ECO:0000250|UniProtKB:Q6PIW4}.
DE  Reference Proteome: Yes;
GO  GO:0000228;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0016787;
GO  GO:0000287;
GO  GO:0008568;
GO  GO:0030674;
GO  GO:0046034;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQVPESSLAHLSEWQRDAFVLSSGTCLPQQKAEVYRAHLAQIQYAWANSEISEASAVHLFKKYAEKYSAIIDSDKLEIGL
SQ  NNYADSILTLAKCQRNESDKWQSSLTTNNVLKLKSVQDMAVAGRRTQLSKSSADASVRVGNGINTSGYSAGLGNNVLRNS
SQ  GYTVPHAALSDCQMPGGSANFLQKPKISAFTIANTTSVANTSSNTLINNSISMTSSLMQSNEDKDPASFSGHMFLPTTSV
SQ  HSGKRKAYSALGNESSDIKPNPLVQRQLTNKEATCESGFKTAKEQLWVDQQKKYSNQPQRNPSPLYGGAKKSLGAARSRG
SQ  LHGKFVPPVPRQEDVQDSNRKVYGQGNSEMNAPSDERLKNIEPKMIELIMSEIMDHGPPLNWDDIAGLEFAKTTIKEIVV
SQ  WPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFTVARCHQPAVIF
SQ  IDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSDDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVV
SQ  SLMAKEHCSLAEQEVEAIVLQADGFSGADMTQLCREAALGPIRSIQLMDISTITPEQVRPIAYIDFQSAFLVVRPSVSQK
SQ  DLELYENWNKTFGCGR
//
ID  Q9LH52;
PN  Leucine-rich repeat protein FLOR 1;
GN  FLR1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|Ref.7}. Nucleus {ECO:0000269|Ref.7}. Cytoplasm, perinuclear region {ECO:0000269|Ref.7}. Cell membrane {ECO:0000269|Ref.7}. Note=In carpels, observed both in cytoplasm and nucleus, as well as in the perinuclear and cell membrane in a vesicle-like pattern. In style cells, present in cytoplasm as well as in nucleus possibly in the perinuclear membrane. In leaf tissue, observed in the plasma membrane and in the perinuclear membrane. In roots and tapetum cells, restricted to the cytoplasm. {ECO:0000269|Ref.7}.
DR  UNIPROT: Q9LH52;
DR  UNIPROT: Q93ZC1;
DR  UNIPROT: Q9C7D9;
DR  UNIPROT: Q9M7E7;
DR  Pfam: PF00560;
DR  Pfam: PF08263;
DE  Function: Promotes flowering transition in long days (LD). {ECO:0000269|PubMed:22319055}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0048574;
GO  GO:0048510;
GO  GO:0010228;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKLFVHLSIFFSILFITLPSSYSCTENDKNALLQIKKALGNPPLLSSWNPRTDCCTGWTGVECTNRRVTGLSVTSGEVSG
SQ  QISYQIGDLVDLRTLDFSYLPHLTGNIPRTITKLKNLNTLYLKHTSLSGPIPDYISELKSLTFLDLSFNQFTGPIPGSLS
SQ  QMPKLEAIQINDNKLTGSIPNSFGSFVGNVPNLYLSNNKLSGKIPESLSKYDFNAVDLSGNGFEGDAFMFFGRNKTTVRV
SQ  DLSRNMFNFDLVKVKFARSIVSLDLSQNHIYGKIPPALTKLHLEHFNVSDNHLCGKIPSGGLLQTFEPSAFAHNICLCGT
SQ  PLKAC
//
ID  Q9NZU1;
PN  Leucine-rich repeat transmembrane protein FLRT1;
GN  FLRT1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q6RKD8}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q6RKD8}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6RKD8}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q6RKD8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6RKD8}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q6RKD8}. Secreted {ECO:0000250|UniProtKB:Q6RKD8}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q6RKD8}. Cell junction {ECO:0000250|UniProtKB:Q6RKD8}. Note=In addition to its location at the cell membrane, colocalizes with FGFR1 in punctate perinuclear cytoplasmic vesicles. Detected along neurites and at contacts between neurite termini and other cells. Proteolytic cleavage gives rise to a shedded ectodomain. {ECO:0000250|UniProtKB:Q6RKD8}.
DR  UNIPROT: Q9NZU1;
DR  UNIPROT: Q8WVA2;
DR  Pfam: PF13855;
DR  Pfam: PF01462;
DR  PROSITE: PS50853;
DR  PROSITE: PS51450;
DR  OMIM: 604806;
DR  DisGeNET: 23769;
DE  Function: Plays a role in fibroblast growth factor-mediated signaling cascades that lead to the activation of MAP kinases. Promotes neurite outgrowth via FGFR1-mediated activation of downstream MAP kinases. Promotes an increase both in neurite number and in neurite length. May play a role in cell-cell adhesion and cell guidance via its interaction with ADGRL1/LPHN1 and ADGRL3. {ECO:0000250|UniProtKB:Q6RKD8}.
DE  Reference Proteome: Yes;
DE  Interaction: Q70AK3; IntAct: EBI-8042356; Score: 0.40
DE  Interaction: O43155; IntAct: EBI-8042606; Score: 0.27
DE  Interaction: Q9UN70; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: Q9NZU0; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: Q9HAR2; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: Q9H2G9; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: Q96JH8; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: Q92569; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: P42338; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: P42336; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: P27986; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: O95490; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: O94910; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: O60245; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: O14917; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: O00459; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: A6NFQ2; IntAct: EBI-21556493; Score: 0.35
DE  Interaction: Q9HC97; IntAct: EBI-20807418; Score: 0.37
DE  Interaction: P05067; IntAct: EBI-20768351; Score: 0.40
GO  GO:0005911;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0005789;
GO  GO:0031012;
GO  GO:0005615;
GO  GO:0005925;
GO  GO:0005887;
GO  GO:0044306;
GO  GO:0032809;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030674;
GO  GO:0007155;
GO  GO:0016358;
GO  GO:0008543;
GO  GO:1990138;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLRDWLFLCYGLIAFLTEVIDSTTCPSVCRCDNGFIYCNDRGLTSIPADIPDDATTLYLQNNQINNAGIPQDLKTKVNV
SQ  QVIYLYENDLDEFPINLPRSLRELHLQDNNVRTIARDSLARIPLLEKLHLDDNSVSTVSIEEDAFADSKQLKLLFLSRNH
SQ  LSSIPSGLPHTLEELRLDDNRISTIPLHAFKGLNSLRRLVLDGNLLANQRIADDTFSRLQNLTELSLVRNSLAAPPLNLP
SQ  SAHLQKLYLQDNAISHIPYNTLAKMRELERLDLSNNNLTTLPRGLFDDLGNLAQLLLRNNPWFCGCNLMWLRDWVKARAA
SQ  VVNVRGLMCQGPEKVRGMAIKDITSEMDECFETGPQGGVANAAAKTTASNHASATTPQGSLFTLKAKRPGLRLPDSNIDY
SQ  PMATGDGAKTLAIHVKALTADSIRITWKATLPASSFRLSWLRLGHSPAVGSITETLVQGDKTEYLLTALEPKSTYIICMV
SQ  TMETSNAYVADETPVCAKAETADSYGPTTTLNQEQNAGPMASLPLAGIIGGAVALVFLFLVLGAICWYVHQAGELLTRER
SQ  AYNRGSRKKDDYMESGTKKDNSILEIRGPGLQMLPINPYRAKEEYVVHTIFPSNGSSLCKATHTIGYGTTRGYRDGGIPD
SQ  IDYSYT
//
ID  Q6RKD8;
PN  Leucine-rich repeat transmembrane protein FLRT1;
GN  Flrt1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:22405201}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:16872596, ECO:0000305|PubMed:20421966}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cell junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted {ECO:0000269|PubMed:21673655}. Cell projection, neuron projection {ECO:0000269|PubMed:20421966}. Cell junction {ECO:0000269|PubMed:20421966}. Note=In addition to its location at the cell membrane, colocalizes with FGFR1 in punctate perinuclear cytoplasmic vesicles (PubMed:16872596, PubMed:20421966). Detected along neurites and at contacts between neurite termini and other cells (PubMed:20421966). Proteolytic cleavage gives rise to a shedded ectodomain (PubMed:21673655). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:21673655}.
DR  UNIPROT: Q6RKD8;
DR  UNIPROT: Q14DT7;
DR  UNIPROT: Q6RKD9;
DR  Pfam: PF13855;
DR  Pfam: PF01462;
DR  PROSITE: PS50853;
DR  PROSITE: PS51450;
DE  Function: Plays a role in fibroblast growth factor-mediated signaling cascades that lead to the activation of MAP kinases (PubMed:16872596, PubMed:20421966). Promotes neurite outgrowth via FGFR1-mediated activation of downstream MAP kinases. Promotes an increase both in neurite number and in neurite length (PubMed:20421966). May play a role in cell-cell adhesion and cell guidance via its interaction with ADGRL1/LPHN1 and ADGRL3 (PubMed:22405201). {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966, ECO:0000305|PubMed:22405201}.
DE  Reference Proteome: Yes;
GO  GO:0005911;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0005789;
GO  GO:0005615;
GO  GO:0005925;
GO  GO:0005887;
GO  GO:0044306;
GO  GO:0032809;
GO  GO:0048471;
GO  GO:0005104;
GO  GO:0007155;
GO  GO:0016358;
GO  GO:0008543;
GO  GO:1990138;
GO  GO:0051965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLRDWLFLCYGLIAFLTEVIDSTTCPSVCRCDNGFIYCNDRGLTSIPSDIPDDATTLYLQNNQINNAGIPQDLKTKVKV
SQ  QVIYLYENDLDEFPINLPRSLRELHLQDNNVRTIARDSLARIPLLEKLHLDDNSVSTVSIEEDAFADSKQLKLLFLSRNH
SQ  LSSIPSGLPHTLEELRLDDNRISTIPLHAFKGLNSLRRLVLDGNLLANQRIADDTFSRLQNLTELSLVRNSLAAPPLNLP
SQ  SAHLQKLYLQDNAISHIPYNTLAKMRELERLDLSNNNLTTLPRGLFDDLGNLAQLLLRNNPWFCGCNLMWLRDWVRARAA
SQ  VVNVRGLMCQGPEKVRGMAIKDITSEMDECFEAGSQGGAANAAAKTTVSNHASATTPQGSLFTLKAKRPGLRLPDSNIDY
SQ  PMATGDGAKTLVIQVKPLTADSIRITWKAMLPASSFRLSWLRLGHSPAVGSITETLVQGDKTEYLLTALEPKSTYIICMV
SQ  TMETGNTYVADETPVCAKAETADSYGPTTTLNQEQNAGPMAGLPLAGIIGGAVALVFLFLVLGAICWYVHRAGELLTRER
SQ  VYNRGSRRKDDYMESGTKKDNSILEIRGPGLQMLPINPYRSKEEYVVHTIFPSNGSSLCKGAHTIGYGTTRGYREAGIPD
SQ  VDYSYT
//
ID  Q9NZ56;
PN  Formin-2;
GN  FMN2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20082305}. Cytoplasm, cytosol {ECO:0000269|PubMed:20082305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9JL04}. Nucleus {ECO:0000269|PubMed:26287480}. Nucleus, nucleolus {ECO:0000269|PubMed:23375502}. Cell membrane {ECO:0000250|UniProtKB:Q9JL04}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JL04}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9JL04}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9JL04}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JL04}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9JL04}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9JL04}. Note=Colocalizes with the actin cytoskeleton (PubMed:20082305). Recruited to the membranes via its interaction with SPIRE1 (By similarity). Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (By similarity). Accumulates in the nucleus following DNA damage (PubMed:26287480). {ECO:0000250|UniProtKB:Q9JL04, ECO:0000269|PubMed:20082305, ECO:0000269|PubMed:26287480}.
DR  UNIPROT: Q9NZ56;
DR  UNIPROT: B0QZA7;
DR  UNIPROT: B4DP05;
DR  UNIPROT: Q59GF6;
DR  UNIPROT: Q5VU37;
DR  UNIPROT: Q9NZ55;
DR  PDB: 2YLE;
DR  PDB: 3R7G;
DR  Pfam: PF02181;
DR  PROSITE: PS51444;
DR  OMIM: 606373;
DR  OMIM: 616193;
DR  DisGeNET: 56776;
DE  Function: Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization (PubMed:22330775, PubMed:21730168). Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2 (PubMed:22330775, PubMed:21730168). Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (By similarity). Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest (PubMed:23375502). Also acts in the nucleus: together with SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage (PubMed:26287480). Protects cells against apoptosis by protecting CDKN1A against degradation (PubMed:23375502). {ECO:0000250|UniProtKB:Q9JL04, ECO:0000269|PubMed:21730168, ECO:0000269|PubMed:22330775, ECO:0000269|PubMed:23375502, ECO:0000269|PubMed:26287480}.
DE  Disease: Intellectual developmental disorder, autosomal recessive 47 (MRT47) [MIM:616193]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT47 patients show delayed development, with cognition and speech more affected than motor skills. {ECO:0000269|PubMed:25480035}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P43353; IntAct: EBI-21500028; Score: 0.35
DE  Interaction: Q8WUD1; IntAct: EBI-21500361; Score: 0.35
DE  Interaction: Q7KYR7; IntAct: EBI-21541130; Score: 0.35
DE  Interaction: Q9Y664; IntAct: EBI-21597637; Score: 0.35
DE  Interaction: Q8NB37; IntAct: EBI-21611026; Score: 0.35
DE  Interaction: Q9BVQ7; IntAct: EBI-21645803; Score: 0.35
DE  Interaction: Q92870; IntAct: EBI-21653121; Score: 0.35
DE  Interaction: P37173; IntAct: EBI-21668347; Score: 0.35
DE  Interaction: Q12974; IntAct: EBI-21791071; Score: 0.35
DE  Interaction: Q96IK1; IntAct: EBI-21835435; Score: 0.35
DE  Interaction: P29466; IntAct: EBI-21873638; Score: 0.35
DE  Interaction: P55145; IntAct: EBI-20907608; Score: 0.40
DE  Interaction: O15194; IntAct: EBI-27115784; Score: 0.27
DE  Interaction: P07947; IntAct: EBI-30849899; Score: 0.44
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005902;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0003779;
GO  GO:0006974;
GO  GO:0071456;
GO  GO:0051295;
GO  GO:0070649;
GO  GO:0051758;
GO  GO:0035556;
GO  GO:0046907;
GO  GO:0043066;
GO  GO:0042177;
GO  GO:0048477;
GO  GO:0040038;
GO  GO:2000781;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9JL04};
SQ  MGNQDGKLKRSAGDALHEGGGGAEDALGPRDVEATKKGSGGKKALGKHGKGGGGGGGGGESGKKKSKSDSRASVFSNLRI
SQ  RKNLSKGKGAGGSREDVLDSQALQTGELDSAHSLLTKTPDLSLSADEAGLSDTECADPFEVTGPGGPGPAEARVGGRPIA
SQ  EDVETAAGAQDGQRTSSGSDTDIYSFHSATEQEDLLSDIQQAIRLQQQQQQQLQLQLQQQQQQQQLQGAEEPAAPPTAVS
SQ  PQPGAFLGLDRFLLGPSGGAGEAPGSPDTEQALSALSDLPESLAAEPREPQQPPSPGGLPVSEAPSLPAAQPAAKDSPSS
SQ  TAFPFPEAGPGEEAAGAPVRGAGDTDEEGEEDAFEDAPRGSPGEEWAPEVGEDAPQRLGEEPEEEAQGPDAPAAASLPGS
SQ  PAPSQRCFKPYPLITPCYIKTTTRQLSSPNHSPSQSPNQSPRIKRRPEPSLSRGSRTALASVAAPAKKHRADGGLAAGLS
SQ  RSADWTEELGARTPRVGGSAHLLERGVASDSGGGVSPALAAKASGAPAAADGFQNVFTGRTLLEKLFSQQENGPPEEAEK
SQ  FCSRIIAMGLLLPFSDCFREPCNQNAQTNAASFDQDQLYTWAAVSQPTHSLDYSEGQFPRRVPSMGPPSKPPDEEHRLED
SQ  AETESQSAVSETPQKRSDAVQKEVVDMKSEGQATVIQQLEQTIEDLRTKIAELERQYPALDTEVASGHQGLENGVTASGD
SQ  VCLEALRLEEKEVRHHRILEAKSIQTSPTEEGGVLTLPPVDGLPGRPPCPPGAESGPQTKFCSEISLIVSPRRISVQLDS
SQ  HQPTQSISQPPPPPSLLWSAGQGQPGSQPPHSISTEFQTSHEHSVSSAFKNSCNIPSPPPLPCTESSSSMPGLGMVPPPP
SQ  PPLPGMTVPTLPSTAIPQPPPLQGTEMLPPPPPPLPGAGIPPPPPLPGAGILPLPPLPGAGIPPPPPLPGAAIPPPPPLP
SQ  GAGIPLPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAG
SQ  IPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGVGIPPPPPLPGAGIPP
SQ  PPPLPGAGIPPPPPLPGAGIPPPPPLPRVGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGVGIPPPPPLPGVGIPPPPP
SQ  LPGAGIPPPPPLPGMGIPPAPAPPLPPPGTGIPPPPLLPVSGPPLLPQVGSSTLPTPQVCGFLPPPLPSGLFGLGMNQDK
SQ  GSRKQPIEPCRPMKPLYWTRIQLHSKRDSSTSLIWEKIEEPSIDCHEFEELFSKTAVKERKKPISDTISKTKAKQVVKLL
SQ  SNKRSQAVGILMSSLHLDMKDIQHAVVNLDNSVVDLETLQALYENRAQSDELEKIEKHGRSSKDKENAKSLDKPEQFLYE
SQ  LSLIPNFSERVFCILFQSTFSESICSIRRKLELLQKLCETLKNGPGVMQVLGLVLAFGNYMNGGNKTRGQADGFGLDILP
SQ  KLKDVKSSDNSRSLLSYIVSYYLRNFDEDAGKEQCLFPLPEPQDLFQASQMKFEDFQKDLRKLKKDLKACEVEAGKVYQV
SQ  SSKEHMQPFKENMEQFIIQAKIDQEAEENSLTETHKCFLETTAYFFMKPKLGEKEVSPNAFFSIWHEFSSDFKDFWKKEN
SQ  KLLLQERVKEAEEVCRQKKGKSLYKIKPRHDSGIKAKISMKT
//
ID  Q9JL04;
PN  Formin-2;
GN  Fmn2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19062278, ECO:0000269|PubMed:21620703}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NZ56}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21620703}. Nucleus {ECO:0000250|UniProtKB:Q9NZ56}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NZ56}. Cell membrane {ECO:0000269|PubMed:21705804}; Peripheral membrane protein {ECO:0000269|PubMed:21705804}; Cytoplasmic side {ECO:0000269|PubMed:21705804}. Cytoplasm, cell cortex {ECO:0000269|PubMed:21983562}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21983562}; Peripheral membrane protein {ECO:0000269|PubMed:21983562}; Cytoplasmic side {ECO:0000269|PubMed:21983562}. Note=Colocalizes with the actin cytoskeleton (PubMed:21705804). Recruited to the membranes via its interaction with SPIRE1 (PubMed:21705804). Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (PubMed:21620703). Accumulates in the nucleus following DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9NZ56, ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21705804}.
DR  UNIPROT: Q9JL04;
DR  UNIPROT: Q505D3;
DR  Pfam: PF02181;
DR  PROSITE: PS51444;
DE  Function: Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization (PubMed:18848445, PubMed:21620703). Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2 (PubMed:18848445, PubMed:21620703). Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (PubMed:21983562). Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (PubMed:12447394, PubMed:18848445, PubMed:19062278, PubMed:21620703). Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest (By similarity). Also acts in the nucleus: together with SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage (By similarity). Protects cells against apoptosis by protecting CDKN1A against degradation (By similarity). {ECO:0000250|UniProtKB:Q9NZ56, ECO:0000269|PubMed:12447394, ECO:0000269|PubMed:18848445, ECO:0000269|PubMed:19062278, ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}.
DE  Reference Proteome: Yes;
DE  Interaction: P68135; IntAct: EBI-16095077; Score: 0.44
DE  Interaction: Q6NZM9; IntAct: EBI-26473528; Score: 0.35
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005902;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0003779;
GO  GO:0008017;
GO  GO:0051017;
GO  GO:0045010;
GO  GO:0006974;
GO  GO:0071456;
GO  GO:0051295;
GO  GO:0070649;
GO  GO:0051758;
GO  GO:0046907;
GO  GO:0016344;
GO  GO:0043066;
GO  GO:0042177;
GO  GO:0048477;
GO  GO:0040038;
GO  GO:2000781;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:21983562};
SQ  MGNQDGKLKRSAGDASHEGGGAEDAAGPRDAEITKKASGSKKALGKHGKGGGGSGETSKKKSKSDSRASVFSNLRIRKNL
SQ  TKGKGACDSREDVLDSQALPIGELDSAHSIVTKTPDLSLSAEETGLSDTECADPFEVIHPGASRPAEAGVGIQATAEDLE
SQ  TAAGAQDGQRTSSGSDTDIYSFHSATEQEDLLSDIQQAIRLQQQQQQKLLLQDSEEPAAPPTAISPQPGAFLGLDQFLLG
SQ  PRSEAEKDTVQALPVRPDLPETTKSLVPEHPPSSGSHLTSETPGYATAPSAVTDSLSSPAFTFPEAGPGEGAAGVPVAGT
SQ  GDTDEECEEDAFEDAPRGSPGEEWVPEVEEASQRLEKEPEEGMRESITSAVVSLPGSPAPSPRCFKPYPLITPCYIKTTT
SQ  RQLSSPNHSPSQSPNQSPRIKKRPDPSVSRSSRTALASAAAPAKKHRLEGGLTGGLSRSADWTEELGVRTPGAGGSVHLL
SQ  GRGATADDSGGGSPVLAAKAPGAPATADGFQNVFTGRTLLEKLFSQQENGPPEEAEKFCSRIIAMGLLLPFSDCFREPCN
SQ  QNAGSSSAPFDQDQLYTWAAVSQPTHSMDYSEGQFPRREPSMWPSSKLPEEEPSPKDVDTEPKSSILESPKKCSNGVQQE
SQ  VFDVKSEGQATVIQQLEQTIEDLRTKIAELEKQYPALDLEGPRGLSGLENGLTASADVSLDALVLHGKVAQPPRTLEAKS
SQ  IQTSPTEEGRILTLPPPKAPPEGLLGSPAAASGESALLTSPSGPQTKFCSEISLIVSPRRISVQLDAQQIQSASQLPPPP
SQ  PLLGSDSQGQPSQPSLHTESETSHEHSVSSSFGNNCNVPPAPPLPCTESSSFMPGLGMAIPPPPCLSDITVPALPSPTAP
SQ  ALQFSNLQGPEMLPAPPQPPPLPGLGVPPPPPAPPLPGMGIPPPPPLPGMGIPPPPPLPGMGISPLPPLPGMGIPPPPPL
SQ  PGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGV
SQ  GIPPPPPLPGSGIPPPPALPGVAIPPPPPLPGMGVPPPAPPPPGAGIPPPPLLPGSGPPHSSQVGSSTLPAAPQGCGFLF
SQ  PPLPTGLFGLGMNQDRVARKQLIEPCRPMKPLYWTRIQLHSKRDSSPSLIWEKIEEPSIDCHEFEELFSKTAVKERKKPI
SQ  SDTISKTKAKQVVKLLSNKRSQAVGILMSSLHLDMKDIQHAVVNLDNSVVDLETLQALYENRAQSDELEKIEKHSRSSKD
SQ  KENAKSLDKPEQFLYELSLIPNFSERVFCILFQSTFSESICSIRRKLELLQKLCETLKNGPGVMQVLGLVLAFGNYMNAG
SQ  NKTRGQADGFGLDILPKLKDVKSSDNSRSLLSYIVSYYLRNFDEDAGKEQCVFPLAEPQELFQASQMKFEDFQKDLRKLK
SQ  KDLKACEAEAGKVYQVSSAEHMQPFKENMEQFISQAKIDQESQEAALTETHKCFLETTAYYFMKPKLGEKEVSPNVFFSV
SQ  WHEFSSDFKDAWKKENKLILQERVKEAEEVCRQKKGKSLYKVKPRHDSGIKAKISMKT
//
ID  P51113;
PN  Fragile X messenger ribonucleoprotein 1 homolog A;
GN  fmr1;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q06787}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere {ECO:0000250|UniProtKB:P35922}. Chromosome {ECO:0000250|UniProtKB:P35922}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q06787}. Perikaryon {ECO:0000250|UniProtKB:Q06787}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q06787}. Cell projection, axon {ECO:0000250|UniProtKB:P35922}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35922}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P35922}. Synapse, synaptosome {ECO:0000250|UniProtKB:P35922}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q06787}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:P35922}. Synapse {ECO:0000250|UniProtKB:P35922}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Cell membrane {ECO:0000250|UniProtKB:P35922}.
DR  UNIPROT: P51113;
DR  Pfam: PF05641;
DR  Pfam: PF16098;
DR  Pfam: PF12235;
DR  Pfam: PF00013;
DR  Pfam: PF17904;
DR  Pfam: PF18336;
DR  PROSITE: PS51641;
DR  PROSITE: PS50084;
DE  Function: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs (By similarity). Binds poly(G) and poly(U), and to a lower extent poly(A) and poly(C). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:7781595}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0042995;
GO  GO:0010369;
GO  GO:0005694;
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:1902737;
GO  GO:0043197;
GO  GO:0019897;
GO  GO:0032433;
GO  GO:0097386;
GO  GO:0030426;
GO  GO:1990812;
GO  GO:0043005;
GO  GO:0071598;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098793;
GO  GO:0042734;
GO  GO:1990904;
GO  GO:0045202;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0002151;
GO  GO:0035064;
GO  GO:0008017;
GO  GO:0035198;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:0034046;
GO  GO:0008266;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0003723;
GO  GO:0035613;
GO  GO:0033592;
GO  GO:1990825;
GO  GO:0035197;
GO  GO:0030371;
GO  GO:0006281;
GO  GO:0007215;
GO  GO:0006397;
GO  GO:0051028;
GO  GO:2000766;
GO  GO:0010629;
GO  GO:1900453;
GO  GO:2000301;
GO  GO:0017148;
GO  GO:0045947;
GO  GO:1901386;
GO  GO:0007399;
GO  GO:0060999;
GO  GO:0051491;
GO  GO:2000637;
GO  GO:1902416;
GO  GO:1901800;
GO  GO:0002092;
GO  GO:0045727;
GO  GO:0000381;
GO  GO:0060998;
GO  GO:0051489;
GO  GO:0060964;
GO  GO:0043488;
GO  GO:0098908;
GO  GO:0046928;
GO  GO:0008380;
GO  GO:0060538;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELAVEVRGSNGAFYKAFMKDVHEDSITVTFENNWQQERQIPFHDVRFPPPSGYNKDINERDEVEVYSRANEKEPCCWW
SQ  LAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKSSFHKVKLDVPEDLRQMCAKDSAHKDFKKAVGAFSVS
SQ  YDSENYQLVILSVNEVSIKRASMLSDMHFRSLRTKLSLMLRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGAN
SQ  IQQARKVPGVTAIDLDEDTCTFHIYGEDQEAVKKARTYLEFAENVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEA
SQ  ENDKNISQEEGIVPFVFVGTKDSITNATVLLDYHLNYLKEVDQLRLERLQIDEQLRHIGASSRPPPNRPDKEKGYLSEDC
SQ  SGTVRGSRPYSNRGRSRRGTGYASGTNSEASNASETESDHRDELSDWSLAPAEDDRDNYHRRGDGRRRGGTRGQGMRGRG
SQ  GFKGNDDQPRPDNRQRNSRETKARTSDGSLQIRLDCNNERSVHTKTLQNASVDGSRLRTGKDRVQKKEKTDGVDGPQVVV
SQ  NGVP
//
ID  Q2KHP9;
PN  Fragile X messenger ribonucleoprotein 1 homolog B;
GN  fmr1;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q06787}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere {ECO:0000250|UniProtKB:P35922}. Chromosome {ECO:0000250|UniProtKB:P35922}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q06787}. Perikaryon {ECO:0000250|UniProtKB:Q06787}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q06787}. Cell projection, axon {ECO:0000250|UniProtKB:P35922}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35922}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P35922}. Synapse, synaptosome {ECO:0000250|UniProtKB:P35922}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q06787}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:P35922}. Synapse {ECO:0000250|UniProtKB:P35922}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Cell membrane {ECO:0000250|UniProtKB:P35922}.
DR  UNIPROT: Q2KHP9;
DR  Pfam: PF05641;
DR  Pfam: PF16098;
DR  Pfam: PF12235;
DR  Pfam: PF00013;
DR  Pfam: PF17904;
DR  Pfam: PF18336;
DR  PROSITE: PS51641;
DR  PROSITE: PS50084;
DE  Function: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs. Binds poly(G) and poly(U), and to a lower extent poly(A) and poly(C). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:P51113, ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0042995;
GO  GO:0010369;
GO  GO:0005694;
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:1902737;
GO  GO:0043197;
GO  GO:0019897;
GO  GO:0032433;
GO  GO:0097386;
GO  GO:0030426;
GO  GO:1990812;
GO  GO:0043005;
GO  GO:0071598;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098793;
GO  GO:0042734;
GO  GO:1990904;
GO  GO:0045202;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0002151;
GO  GO:0035064;
GO  GO:0008017;
GO  GO:0035198;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:0034046;
GO  GO:0008266;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0003723;
GO  GO:0035613;
GO  GO:0033592;
GO  GO:1990825;
GO  GO:0035197;
GO  GO:0030371;
GO  GO:0006281;
GO  GO:0007215;
GO  GO:0006397;
GO  GO:0051028;
GO  GO:2000766;
GO  GO:0010629;
GO  GO:1900453;
GO  GO:2000301;
GO  GO:0017148;
GO  GO:0045947;
GO  GO:1901386;
GO  GO:0007399;
GO  GO:0060999;
GO  GO:0051491;
GO  GO:2000637;
GO  GO:1902416;
GO  GO:1901800;
GO  GO:0002092;
GO  GO:0045727;
GO  GO:0000381;
GO  GO:0060998;
GO  GO:0051489;
GO  GO:0060964;
GO  GO:0043488;
GO  GO:0098908;
GO  GO:0046928;
GO  GO:0008380;
GO  GO:0060538;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELAVEVRGSNGAFYKAFVKDVHEDSITVTFENNWQQEKQIPFHDVRFPPPSGYNKDINESDEVEVYSRANEKEPCCWW
SQ  LAKVRMIKGEFYVIEYAACDATYNEIVTIDRLRSVNPNKSATKNSFHKVKLDVPEDLRQMCAKDSAHKDFKKAVGAFSVS
SQ  YDSENYQLVILSVNEVTIKRANMLCDMHFRSLRTKLSLMLRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGAN
SQ  IQQARKVPGVTAIDLDEDTCTFHIYGEDQEAVKKARTYLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEA
SQ  ENDKNISQEEGNVPFVFVGTKDSITNATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPSNRPDKEKGYLSEDC
SQ  SGTVRGSRPYNNRGRSRRGTGYASGTNSEASNASETESDHRDELSDWSLAPAEDDRDNYHRRGDGRRRGGMRGQGMRGRG
SQ  GFKGNDDQPRPDNRQRNSRETKARTSDGSLQIRIDCNNERSVHTKTLQNASVEGSRLRTGKDRIQKKEKTDGVDGPQVVV
SQ  NGVP
//
ID  Q06787;
PN  Fragile X messenger ribonucleoprotein 1;
GN  FMR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:18936162}. Nucleus, nucleolus {ECO:0000269|PubMed:12837692, ECO:0000269|PubMed:16407062, ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:24658146}. Chromosome, centromere {ECO:0000250|UniProtKB:P35922}. Chromosome {ECO:0000250|UniProtKB:P35922}. Cytoplasm {ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:12837692, ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:18936162, ECO:0000269|PubMed:7781595, ECO:0000269|PubMed:8401578, ECO:0000269|PubMed:8515814}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24658146}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:14532325, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:9659908}. Perikaryon {ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:18093976}. Cell projection, neuron projection {ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:18093976}. Cell projection, axon {ECO:0000250|UniProtKB:P35922}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35922}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P35922}. Synapse, synaptosome {ECO:0000250|UniProtKB:P35922}. Cell projection, growth cone {ECO:0000269|PubMed:15380484}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:P35922}. Synapse {ECO:0000250|UniProtKB:P35922}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Cell membrane {ECO:0000250|UniProtKB:P35922}. Cytoplasm, Stress granule {ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:18664458}. Note=Colocalizes with H2AX/H2A.x in pericentromeric heterochromatin in response to DNA damaging agents (By similarity). Localizes on meiotic pachytene-stage chromosomes (By similarity). Forms nuclear foci representing sites of ongoing DNA replication in response to DNA damaging agents (By similarity). Shuttles between nucleus and cytoplasm in a XPO1/CRM1-dependent manner (PubMed:10196376). Localizes to cytoplasmic ribonucleoprotein granules, also referred to as messenger ribonucleoprotein particles or mRNPs, along dendrites and dendritic spines (PubMed:9659908, PubMed:14532325). FMR1-containing cytoplasmic granules colocalize to F-actin-rich structures, including filopodium, spines and growth cone during the development of hippocampal neurons (By similarity). FMR1-containing cytoplasmic granules are transported out of the soma along axon and dendrite to synaptic contacts in a microtubule- and kinesin-dependent manner (PubMed:12417734, PubMed:15380484). Colocalizes with CACNA1B in the cytoplasm and at the cell membrane of neurons (By similarity). Colocalizes with CYFIP1, CYFIP2, NXF2 and ribosomes in the perinuclear region (By similarity). Colocalizes with CYFIP1 and EIF4E in dendrites and probably at synapses (By similarity). Colocalizes with FXR1, kinesin, 60S acidic ribosomal protein RPLP0 and SMN in cytoplasmic granules in the soma and neurite cell processes (PubMed:12417734, PubMed:18093976, PubMed:16636078). Colocalizes with FXR1 and FXR2 in discrete granules, called fragile X granules (FXGs), along axon and presynaptic compartments (By similarity). Colocalizes with TDRD3 in cytoplasmic stress granules (SGs) in response to various cellular stress (PubMed:18632687, PubMed:18664458, PubMed:16636078). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:14532325, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:9659908}. [Isoform 6]: Cytoplasm {ECO:0000269|PubMed:24204304, ECO:0000269|PubMed:8789445}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24204304}. [Isoform 9]: Cytoplasm {ECO:0000269|PubMed:24204304, ECO:0000269|PubMed:8789445}. [Isoform 10]: Nucleus {ECO:0000269|PubMed:8789445}. Nucleus, Cajal body {ECO:0000269|PubMed:24204304}. Note=Colocalizes with Colin and SMN in Cajal bodies (PubMed:24204304). [Isoform 11]: Nucleus {ECO:0000269|PubMed:8789445}. Nucleus, Cajal body {ECO:0000269|PubMed:24204304}.
DR  UNIPROT: Q06787;
DR  UNIPROT: A6NNH4;
DR  UNIPROT: D3DWT0;
DR  UNIPROT: D3DWT1;
DR  UNIPROT: D3DWT2;
DR  UNIPROT: G8JL90;
DR  UNIPROT: Q16578;
DR  UNIPROT: Q5PQZ6;
DR  UNIPROT: Q99054;
DR  PDB: 2BKD;
DR  PDB: 2FMR;
DR  PDB: 2LA5;
DR  PDB: 2QND;
DR  PDB: 4OVA;
DR  PDB: 4QVZ;
DR  PDB: 4QW2;
DR  PDB: 5DE5;
DR  PDB: 5DE8;
DR  PDB: 5DEA;
DR  PDB: 5UWJ;
DR  PDB: 5UWO;
DR  Pfam: PF05641;
DR  Pfam: PF16098;
DR  Pfam: PF12235;
DR  Pfam: PF00013;
DR  Pfam: PF17904;
DR  Pfam: PF18336;
DR  PROSITE: PS51641;
DR  PROSITE: PS50084;
DR  OMIM: 300623;
DR  OMIM: 300624;
DR  OMIM: 309550;
DR  OMIM: 311360;
DR  OMIM: 616034;
DR  DisGeNET: 2332;
DE  Function: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs (PubMed:16631377, PubMed:18653529, PubMed:19166269, PubMed:23235829, PubMed:25464849). Plays a role in the alternative splicing of its own mRNA (PubMed:18653529). Plays a role in mRNA nuclear export (By similarity). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (By similarity). Stabilizes the scaffolding postsynaptic density protein DLG4/PSD-95 and the myelin basic protein (MBP) mRNAs in hippocampal neurons and glial cells, respectively; this stabilization is further increased in response to metabotropic glutamate receptor (mGluR) stimulation (By similarity). Plays a role in selective delivery of a subset of dendritic mRNAs to synaptic sites in response to mGluR activation in a kinesin-dependent manner (By similarity). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postsynaptic dendritic spines (PubMed:11532944, PubMed:11157796, PubMed:12594214, PubMed:23235829). Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation (By similarity). Represses mRNA translation by stalling ribosomal translocation during elongation (By similarity). Reports are contradictory with regards to its ability to mediate translation inhibition of MBP mRNA in oligodendrocytes (PubMed:23891804). Also involved in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and hence regulates microRNA (miRNA)-mediated translational repression by AGO2 (PubMed:14703574, PubMed:17057366, PubMed:25464849). Facilitates the assembly of miRNAs on specific target mRNAs (PubMed:17057366). Also plays a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses (PubMed:19097999, PubMed:19166269). In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses (By similarity). Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions (PubMed:7692601, PubMed:11719189, PubMed:11157796, PubMed:12594214, PubMed:17417632, PubMed:23235829, PubMed:24448548). Binds to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated region (UTR) and less frequently at 5'-UTR (PubMed:23235829). Binds to intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of mRNA targets (PubMed:11719189, PubMed:18579868, PubMed:25464849, PubMed:25692235). Binds to G-quadruplex structures in the 3'-UTR of its own mRNA (PubMed:7692601, PubMed:11532944, PubMed:12594214, PubMed:15282548, PubMed:18653529). Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes (PubMed:15805463). Binds mRNAs containing U-rich target sequences (PubMed:12927206). Binds to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR region of superoxide dismutase SOD1 mRNA (PubMed:19166269). Binds to the dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1 target mRNAs at synapses (By similarity). Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner (By similarity). Binds to a subset of miRNAs in the brain (PubMed:14703574, PubMed:17057366). May associate with nascent transcripts in a nuclear protein NXF1-dependent manner (PubMed:18936162). In vitro, binds to RNA homomer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:7688265, PubMed:7781595, PubMed:12950170, PubMed:15381419, PubMed:8156595). Moreover, plays a role in the modulation of the sodium-activated potassium channel KCNT1 gating activity (PubMed:20512134). Negatively regulates the voltage- dependent calcium channel current density in soma and presynaptic terminals of dorsal root ganglion (DRG) neurons, and hence regulates synaptic vesicle exocytosis (By similarity). Modulates the voltage- dependent calcium channel CACNA1B expression at the plasma membrane by targeting the channels for proteosomal degradation (By similarity). Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development (By similarity). Recently, has been shown to play a translation-independent role in the modulation of presynaptic action potential (AP) duration and neurotransmitter release via large- conductance calcium-activated potassium (BK) channels in hippocampal and cortical excitatory neurons (PubMed:25561520). Finally, FMR1 may be involved in the control of DNA damage response (DDR) mechanisms through the regulation of ATR-dependent signaling pathways such as histone H2AX/H2A.x and BRCA1 phosphorylations (PubMed:24813610). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:11157796, ECO:0000269|PubMed:11532944, ECO:0000269|PubMed:11719189, ECO:0000269|PubMed:12594214, ECO:0000269|PubMed:12927206, ECO:0000269|PubMed:12950170, ECO:0000269|PubMed:14703574, ECO:0000269|PubMed:15282548, ECO:0000269|PubMed:15381419, ECO:0000269|PubMed:15805463, ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:17057366, ECO:0000269|PubMed:17417632, ECO:0000269|PubMed:18579868, ECO:0000269|PubMed:18653529, ECO:0000269|PubMed:18936162, ECO:0000269|PubMed:19097999, ECO:0000269|PubMed:19166269, ECO:0000269|PubMed:20512134, ECO:0000269|PubMed:23235829, ECO:0000269|PubMed:23891804, ECO:0000269|PubMed:24448548, ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25464849, ECO:0000269|PubMed:25561520, ECO:0000269|PubMed:25692235, ECO:0000269|PubMed:7688265, ECO:0000269|PubMed:7692601, ECO:0000269|PubMed:7781595, ECO:0000269|PubMed:8156595}. [Isoform 10]: Binds to RNA homomer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:24204304). May bind to RNA in Cajal bodies (PubMed:24204304). {ECO:0000269|PubMed:24204304}. [Isoform 6]: Binds to RNA homomer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:24204304). May bind to RNA in Cajal bodies (PubMed:24204304). {ECO:0000269|PubMed:24204304}. (Microbial infection) Acts as a positive regulator of influenza A virus (IAV) replication. Required for the assembly and nuclear export of the viral ribonucleoprotein (vRNP) components. {ECO:0000269|PubMed:24514761}.
DE  Disease: Fragile X syndrome (FXS) [MIM:300624]: An X-linked dominant disease characterized by moderate to severe intellectual disability, macroorchidism (enlargement of the testicles), large ears, prominent jaw, and high-pitched, jocular speech. The defect in most patients results from an amplification of a CGG repeat region in the FMR1 gene and abnormal methylation. {ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:11157796, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:15805463, ECO:0000269|PubMed:17850748, ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:23235829, ECO:0000269|PubMed:24204304, ECO:0000269|PubMed:24448548, ECO:0000269|PubMed:24514761, ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25561520, ECO:0000269|PubMed:7633450, ECO:0000269|PubMed:7688265, ECO:0000269|PubMed:8156595, ECO:0000269|PubMed:8401578, ECO:0000269|PubMed:8490650, ECO:0000269|PubMed:9659908}. Note=The disease is caused by variants affecting the gene represented in this entry. Fragile X tremor/ataxia syndrome (FXTAS) [MIM:300623]: An X- linked neurodegenerative disorder characterized by late-onset, progressive cerebellar ataxia and intention tremor followed by cognitive decline. {ECO:0000269|PubMed:11445641}. Note=The disease is caused by variants affecting the gene represented in this entry. Premature ovarian failure 1 (POF1) [MIM:311360]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol. {ECO:0000269|PubMed:9719368}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A1L4K1; IntAct: EBI-10224474; Score: 0.56
DE  Interaction: P0DTD1; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P10909; IntAct: EBI-21371844; Score: 0.00
DE  Interaction: P21980; IntAct: EBI-25856705; Score: 0.56
DE  Interaction: P63165; IntAct: EBI-21388180; Score: 0.00
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: O95793; IntAct: EBI-366371; Score: 0.43
DE  Interaction: Q9UL18; IntAct: EBI-7641969; Score: 0.35
DE  Interaction: P63073; IntAct: EBI-2000674; Score: 0.35
DE  Interaction: A0A5P8YGX7; IntAct: EBI-2869681; Score: 0.00
DE  Interaction: P03372; IntAct: EBI-2878124; Score: 0.35
DE  Interaction: Q92731; IntAct: EBI-2880211; Score: 0.46
DE  Interaction: Q13131; IntAct: EBI-3213822; Score: 0.35
DE  Interaction: Q7TMB8; IntAct: EBI-3649150; Score: 0.37
DE  Interaction: Q7L576; IntAct: EBI-3649503; Score: 0.49
DE  Interaction: Q96F07; IntAct: EBI-3649591; Score: 0.53
DE  Interaction: Q06787; IntAct: EBI-8619896; Score: 0.69
DE  Interaction: Q5JVS0; IntAct: EBI-7032254; Score: 0.40
DE  Interaction: Q6QDQ4; IntAct: EBI-5276631; Score: 0.35
DE  Interaction: P48059; IntAct: EBI-5660443; Score: 0.00
DE  Interaction: Q13137; IntAct: EBI-6115370; Score: 0.55
DE  Interaction: A7MCY6; IntAct: EBI-6116450; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-6116602; Score: 0.35
DE  Interaction: Q9JHG6; IntAct: EBI-8013831; Score: 0.40
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P61326; IntAct: EBI-6551517; Score: 0.35
DE  Interaction: P38919; IntAct: EBI-6551387; Score: 0.35
DE  Interaction: Q8NC51; IntAct: EBI-8844408; Score: 0.35
DE  Interaction: Q9NWT6; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P51116; IntAct: EBI-25478814; Score: 0.66
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q9JLI8; IntAct: EBI-11023430; Score: 0.35
DE  Interaction: Q96FV9; IntAct: EBI-11034504; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: D6RFU6; IntAct: EBI-11044384; Score: 0.35
DE  Interaction: P54227; IntAct: EBI-11048628; Score: 0.35
DE  Interaction: Q91YN9; IntAct: EBI-11052510; Score: 0.35
DE  Interaction: Q9NYF8; IntAct: EBI-11086629; Score: 0.35
DE  Interaction: Q61768; IntAct: EBI-11094840; Score: 0.35
DE  Interaction: Q8R5C0; IntAct: EBI-11096914; Score: 0.35
DE  Interaction: A0AVT1; IntAct: EBI-11105405; Score: 0.35
DE  Interaction: Q08AG7; IntAct: EBI-11108327; Score: 0.35
DE  Interaction: Q8BH65; IntAct: EBI-11109889; Score: 0.35
DE  Interaction: P37840; IntAct: EBI-11113842; Score: 0.35
DE  Interaction: P04062; IntAct: EBI-11114072; Score: 0.35
DE  Interaction: P83887; IntAct: EBI-11115300; Score: 0.35
DE  Interaction: Q9Y2D8; IntAct: EBI-11379249; Score: 0.27
DE  Interaction: Q9UJV9; IntAct: EBI-11473486; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q9JIN6; IntAct: EBI-15097151; Score: 0.35
DE  Interaction: Q08460; IntAct: EBI-15097151; Score: 0.35
DE  Interaction: Q6ICG8; IntAct: EBI-21880135; Score: 0.35
DE  Interaction: Q9BQE9; IntAct: EBI-21882089; Score: 0.35
DE  Interaction: Q8IY47; IntAct: EBI-21882089; Score: 0.35
DE  Interaction: Q08380; IntAct: EBI-21882089; Score: 0.35
DE  Interaction: Q7Z417; IntAct: EBI-15562677; Score: 0.44
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: Q12824; IntAct: EBI-20624550; Score: 0.27
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q3KP66; IntAct: EBI-20715953; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20799058; Score: 0.35
DE  Interaction: Q13428; IntAct: EBI-20929176; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P35637; IntAct: EBI-21221307; Score: 0.35
DE  Interaction: Q96S59; IntAct: EBI-21369245; Score: 0.00
DE  Interaction: O95267; IntAct: EBI-21369403; Score: 0.00
DE  Interaction: Q9NP66; IntAct: EBI-21369822; Score: 0.00
DE  Interaction: Q7L5Y9; IntAct: EBI-21369724; Score: 0.00
DE  Interaction: O60884; IntAct: EBI-21369710; Score: 0.00
DE  Interaction: Q9Y6X2; IntAct: EBI-21369904; Score: 0.00
DE  Interaction: Q9BSL1; IntAct: EBI-21369945; Score: 0.00
DE  Interaction: P40123; IntAct: EBI-21370139; Score: 0.00
DE  Interaction: Q99784; IntAct: EBI-21369996; Score: 0.00
DE  Interaction: Q9UQB8; IntAct: EBI-21370061; Score: 0.00
DE  Interaction: Q14919; IntAct: EBI-21370370; Score: 0.00
DE  Interaction: O00471; IntAct: EBI-21370498; Score: 0.00
DE  Interaction: Q14314; IntAct: EBI-21370849; Score: 0.00
DE  Interaction: Q9UBU8; IntAct: EBI-21370917; Score: 0.00
DE  Interaction: Q8N5Y2; IntAct: EBI-21370931; Score: 0.00
DE  Interaction: Q13438; IntAct: EBI-21370945; Score: 0.00
DE  Interaction: O14647; IntAct: EBI-21371152; Score: 0.00
DE  Interaction: P61964; IntAct: EBI-21371193; Score: 0.00
DE  Interaction: Q9UKN5; IntAct: EBI-21371207; Score: 0.00
DE  Interaction: Q9UNN5; IntAct: EBI-21371221; Score: 0.00
DE  Interaction: Q9Y496; IntAct: EBI-21371235; Score: 0.00
DE  Interaction: Q96RF0; IntAct: EBI-21371415; Score: 0.00
DE  Interaction: Q9C026; IntAct: EBI-21371538; Score: 0.00
DE  Interaction: Q96CW1; IntAct: EBI-21371769; Score: 0.00
DE  Interaction: Q96N64; IntAct: EBI-21371660; Score: 0.00
DE  Interaction: Q96PV6; IntAct: EBI-21371646; Score: 0.00
DE  Interaction: Q96PY5; IntAct: EBI-21371620; Score: 0.00
DE  Interaction: Q00610; IntAct: EBI-21371927; Score: 0.00
DE  Interaction: Q8N1A0; IntAct: EBI-21371994; Score: 0.00
DE  Interaction: Q12860; IntAct: EBI-21372035; Score: 0.00
DE  Interaction: Q14194; IntAct: EBI-21372447; Score: 0.00
DE  Interaction: Q96L42; IntAct: EBI-21372275; Score: 0.00
DE  Interaction: Q8N3I7; IntAct: EBI-21372220; Score: 0.00
DE  Interaction: P29400; IntAct: EBI-21372182; Score: 0.00
DE  Interaction: Q8WXF8; IntAct: EBI-21372962; Score: 0.00
DE  Interaction: Q8TF20; IntAct: EBI-21373160; Score: 0.00
DE  Interaction: Q6PEW1; IntAct: EBI-21373134; Score: 0.00
DE  Interaction: Q1L5Z9; IntAct: EBI-21373054; Score: 0.00
DE  Interaction: Q12882; IntAct: EBI-21373320; Score: 0.00
DE  Interaction: Q14204; IntAct: EBI-21373282; Score: 0.00
DE  Interaction: P29692; IntAct: EBI-21373439; Score: 0.00
DE  Interaction: O43491; IntAct: EBI-21373658; Score: 0.00
DE  Interaction: Q9H4G0; IntAct: EBI-21373644; Score: 0.00
DE  Interaction: O60293; IntAct: EBI-21373492; Score: 0.00
DE  Interaction: P33121; IntAct: EBI-21373794; Score: 0.00
DE  Interaction: P42566; IntAct: EBI-21373716; Score: 0.00
DE  Interaction: Q9Y483; IntAct: EBI-21373970; Score: 0.00
DE  Interaction: Q70YC4; IntAct: EBI-21374286; Score: 0.00
DE  Interaction: Q9UPW8; IntAct: EBI-21374527; Score: 0.00
DE  Interaction: Q9UPY8; IntAct: EBI-21374400; Score: 0.00
DE  Interaction: Q96RU3; IntAct: EBI-21374719; Score: 0.00
DE  Interaction: Q9UBB6; IntAct: EBI-21375011; Score: 0.00
DE  Interaction: P21333; IntAct: EBI-21375025; Score: 0.00
DE  Interaction: Q9Y2J2; IntAct: EBI-21374970; Score: 0.00
DE  Interaction: O60333; IntAct: EBI-21374889; Score: 0.00
DE  Interaction: Q9BT88; IntAct: EBI-21375171; Score: 0.00
DE  Interaction: Q9Y5W8; IntAct: EBI-21375052; Score: 0.00
DE  Interaction: O95490; IntAct: EBI-21375435; Score: 0.00
DE  Interaction: Q9UJ04; IntAct: EBI-21375449; Score: 0.00
DE  Interaction: Q9C040; IntAct: EBI-21375699; Score: 0.00
DE  Interaction: O94874; IntAct: EBI-21376033; Score: 0.00
DE  Interaction: Q7Z460; IntAct: EBI-21375713; Score: 0.00
DE  Interaction: Q96JC1; IntAct: EBI-21375752; Score: 0.00
DE  Interaction: O75044; IntAct: EBI-21376062; Score: 0.00
DE  Interaction: Q8N488; IntAct: EBI-21376128; Score: 0.00
DE  Interaction: O75533; IntAct: EBI-21376142; Score: 0.00
DE  Interaction: Q9UPN3; IntAct: EBI-21376184; Score: 0.00
DE  Interaction: Q9ULA0; IntAct: EBI-21376333; Score: 0.00
DE  Interaction: Q6PID6; IntAct: EBI-21376319; Score: 0.00
DE  Interaction: Q8NAP3; IntAct: EBI-21376630; Score: 0.00
DE  Interaction: Q8TF01; IntAct: EBI-21376898; Score: 0.00
DE  Interaction: Q96DZ5; IntAct: EBI-21376912; Score: 0.00
DE  Interaction: O43166; IntAct: EBI-21377092; Score: 0.00
DE  Interaction: Q9Y4E5; IntAct: EBI-21377023; Score: 0.00
DE  Interaction: Q9NUQ6; IntAct: EBI-21376926; Score: 0.00
DE  Interaction: Q9ULX6; IntAct: EBI-21377424; Score: 0.00
DE  Interaction: Q96NJ3; IntAct: EBI-21377397; Score: 0.00
DE  Interaction: Q06210; IntAct: EBI-21377371; Score: 0.00
DE  Interaction: Q9UHB7; IntAct: EBI-21377556; Score: 0.00
DE  Interaction: Q9ULD5; IntAct: EBI-21377623; Score: 0.00
DE  Interaction: Q9UMS4; IntAct: EBI-21377802; Score: 0.00
DE  Interaction: P38159; IntAct: EBI-21377775; Score: 0.00
DE  Interaction: Q86WH2; IntAct: EBI-21378180; Score: 0.00
DE  Interaction: Q9HBT6; IntAct: EBI-21378166; Score: 0.00
DE  Interaction: Q5JPE7; IntAct: EBI-21378278; Score: 0.00
DE  Interaction: Q8N660; IntAct: EBI-21378426; Score: 0.00
DE  Interaction: Q6NZI2; IntAct: EBI-21378344; Score: 0.00
DE  Interaction: P07305; IntAct: EBI-21378914; Score: 0.00
DE  Interaction: Q9BWC9; IntAct: EBI-21378823; Score: 0.00
DE  Interaction: Q00341; IntAct: EBI-21378943; Score: 0.00
DE  Interaction: P61978; IntAct: EBI-21379125; Score: 0.00
DE  Interaction: P11021; IntAct: EBI-21379273; Score: 0.00
DE  Interaction: Q5HYM0; IntAct: EBI-21379476; Score: 0.00
DE  Interaction: P78318; IntAct: EBI-21379562; Score: 0.00
DE  Interaction: Q13123; IntAct: EBI-21379655; Score: 0.00
DE  Interaction: O14782; IntAct: EBI-21379843; Score: 0.00
DE  Interaction: A6QL64; IntAct: EBI-21379817; Score: 0.00
DE  Interaction: O60282; IntAct: EBI-21379969; Score: 0.00
DE  Interaction: P33176; IntAct: EBI-21379927; Score: 0.00
DE  Interaction: Q12840; IntAct: EBI-21379882; Score: 0.00
DE  Interaction: A8MQT2; IntAct: EBI-21380484; Score: 0.00
DE  Interaction: Q15784; IntAct: EBI-21380833; Score: 0.00
DE  Interaction: Q14494; IntAct: EBI-21380847; Score: 0.00
DE  Interaction: Q9UQ80; IntAct: EBI-21381113; Score: 0.00
DE  Interaction: P67809; IntAct: EBI-21380954; Score: 0.00
DE  Interaction: Q16656; IntAct: EBI-21380927; Score: 0.00
DE  Interaction: Q6P4R8; IntAct: EBI-21380889; Score: 0.00
DE  Interaction: P05165; IntAct: EBI-21381471; Score: 0.00
DE  Interaction: Q15154; IntAct: EBI-21381512; Score: 0.00
DE  Interaction: Q9UJX3; IntAct: EBI-21381861; Score: 0.00
DE  Interaction: O95071; IntAct: EBI-21381759; Score: 0.00
DE  Interaction: Q9UBS4; IntAct: EBI-21382031; Score: 0.00
DE  Interaction: Q7LFL8; IntAct: EBI-21381914; Score: 0.00
DE  Interaction: Q99719; IntAct: EBI-21382462; Score: 0.00
DE  Interaction: Q9NZR2; IntAct: EBI-21382344; Score: 0.00
DE  Interaction: Q9H0C5; IntAct: EBI-21382290; Score: 0.00
DE  Interaction: Q00169; IntAct: EBI-21382196; Score: 0.00
DE  Interaction: O43236; IntAct: EBI-21382476; Score: 0.00
DE  Interaction: P46100; IntAct: EBI-21382624; Score: 0.00
DE  Interaction: Q5T0N5; IntAct: EBI-21382791; Score: 0.00
DE  Interaction: Q6ZN54; IntAct: EBI-21382753; Score: 0.00
DE  Interaction: Q8WUP2; IntAct: EBI-21382702; Score: 0.00
DE  Interaction: Q8NDB2; IntAct: EBI-21382915; Score: 0.00
DE  Interaction: Q8TEP8; IntAct: EBI-21383160; Score: 0.00
DE  Interaction: Q8TC92; IntAct: EBI-21382981; Score: 0.00
DE  Interaction: Q8NEU8; IntAct: EBI-21383268; Score: 0.00
DE  Interaction: Q15172; IntAct: EBI-21383310; Score: 0.00
DE  Interaction: Q9P0M6; IntAct: EBI-21383440; Score: 0.00
DE  Interaction: Q6VMQ6; IntAct: EBI-21383754; Score: 0.00
DE  Interaction: Q3V6T2; IntAct: EBI-21383663; Score: 0.00
DE  Interaction: Q96IV0; IntAct: EBI-21383887; Score: 0.00
DE  Interaction: P10644; IntAct: EBI-21383768; Score: 0.00
DE  Interaction: P05771; IntAct: EBI-21383926; Score: 0.00
DE  Interaction: Q9Y5G2; IntAct: EBI-21384294; Score: 0.00
DE  Interaction: Q9UHQ4; IntAct: EBI-21384245; Score: 0.00
DE  Interaction: Q8NFW8; IntAct: EBI-21384164; Score: 0.00
DE  Interaction: Q9NQZ6; IntAct: EBI-21384137; Score: 0.00
DE  Interaction: Q5T6F2; IntAct: EBI-21383995; Score: 0.00
DE  Interaction: Q2TAA8; IntAct: EBI-21383952; Score: 0.00
DE  Interaction: P17980; IntAct: EBI-21384575; Score: 0.00
DE  Interaction: Q9NR46; IntAct: EBI-21384475; Score: 0.00
DE  Interaction: Q9NRA8; IntAct: EBI-21384346; Score: 0.00
DE  Interaction: Q6PEZ3; IntAct: EBI-21384756; Score: 0.00
DE  Interaction: O00231; IntAct: EBI-21384666; Score: 0.00
DE  Interaction: Q8N2N9; IntAct: EBI-21385221; Score: 0.00
DE  Interaction: Q9P246; IntAct: EBI-21385083; Score: 0.00
DE  Interaction: Q9Y2V7; IntAct: EBI-21384947; Score: 0.00
DE  Interaction: Q9NS37; IntAct: EBI-21385397; Score: 0.00
DE  Interaction: P15622; IntAct: EBI-21385411; Score: 0.00
DE  Interaction: Q9UNH7; IntAct: EBI-21385440; Score: 0.00
DE  Interaction: Q53G59; IntAct: EBI-21385611; Score: 0.00
DE  Interaction: Q15424; IntAct: EBI-21385936; Score: 0.00
DE  Interaction: P62979; IntAct: EBI-21385886; Score: 0.00
DE  Interaction: P62750; IntAct: EBI-21385846; Score: 0.00
DE  Interaction: P35268; IntAct: EBI-21385832; Score: 0.00
DE  Interaction: Q9C0C9; IntAct: EBI-21386016; Score: 0.00
DE  Interaction: Q9H2G4; IntAct: EBI-21386093; Score: 0.00
DE  Interaction: P23246; IntAct: EBI-26509668; Score: 0.55
DE  Interaction: Q96BJ3; IntAct: EBI-21386472; Score: 0.00
DE  Interaction: Q2KHR2; IntAct: EBI-21386486; Score: 0.00
DE  Interaction: Q86XZ4; IntAct: EBI-21386554; Score: 0.00
DE  Interaction: P28370; IntAct: EBI-21386642; Score: 0.00
DE  Interaction: P51532; IntAct: EBI-21386670; Score: 0.00
DE  Interaction: Q14527; IntAct: EBI-21386656; Score: 0.00
DE  Interaction: P18583; IntAct: EBI-21387034; Score: 0.00
DE  Interaction: Q13813; IntAct: EBI-21387265; Score: 0.00
DE  Interaction: P21579; IntAct: EBI-21387640; Score: 0.00
DE  Interaction: P21675; IntAct: EBI-21387657; Score: 0.00
DE  Interaction: Q14241; IntAct: EBI-21387697; Score: 0.00
DE  Interaction: Q15906; IntAct: EBI-21387723; Score: 0.00
DE  Interaction: P10600; IntAct: EBI-21387750; Score: 0.00
DE  Interaction: P10828; IntAct: EBI-21387764; Score: 0.00
DE  Interaction: P05452; IntAct: EBI-21387855; Score: 0.00
DE  Interaction: P09936; IntAct: EBI-21388194; Score: 0.00
DE  Interaction: Q15361; IntAct: EBI-21388064; Score: 0.00
DE  Interaction: O96028; IntAct: EBI-21388313; Score: 0.00
DE  Interaction: P52746; IntAct: EBI-21388613; Score: 0.00
DE  Interaction: Q99676; IntAct: EBI-21388653; Score: 0.00
DE  Interaction: P21506; IntAct: EBI-21388441; Score: 0.00
DE  Interaction: Q06732; IntAct: EBI-21388507; Score: 0.00
DE  Interaction: Q06730; IntAct: EBI-21388493; Score: 0.00
DE  Interaction: Q13029; IntAct: EBI-21388784; Score: 0.00
DE  Interaction: Q86XK2; IntAct: EBI-21389330; Score: 0.00
DE  Interaction: Q6ZS17; IntAct: EBI-21388993; Score: 0.00
DE  Interaction: A6NKB5; IntAct: EBI-21389170; Score: 0.00
DE  Interaction: P51114; IntAct: EBI-25478796; Score: 0.75
DE  Interaction: P45974; IntAct: EBI-21389685; Score: 0.00
DE  Interaction: Q8IZ26; IntAct: EBI-21389671; Score: 0.00
DE  Interaction: Q9UQM7; IntAct: EBI-21389808; Score: 0.00
DE  Interaction: Q6PIJ6; IntAct: EBI-21389822; Score: 0.00
DE  Interaction: Q9H7E2; IntAct: EBI-25485785; Score: 0.55
DE  Interaction: Q9BZR9; IntAct: EBI-21389862; Score: 0.00
DE  Interaction: P51784; IntAct: EBI-21389928; Score: 0.00
DE  Interaction: P04632; IntAct: EBI-21389954; Score: 0.00
DE  Interaction: Q2LD37; IntAct: EBI-21390138; Score: 0.00
DE  Interaction: Q9BSF8; IntAct: EBI-21390192; Score: 0.00
DE  Interaction: Q86W92; IntAct: EBI-21390487; Score: 0.00
DE  Interaction: Q5VT25; IntAct: EBI-21390408; Score: 0.00
DE  Interaction: Q96JF6; IntAct: EBI-21390326; Score: 0.00
DE  Interaction: Q5H9K5; IntAct: EBI-21390257; Score: 0.00
DE  Interaction: Q9BR77; IntAct: EBI-21390230; Score: 0.00
DE  Interaction: O75925; IntAct: EBI-21390743; Score: 0.00
DE  Interaction: Q92538; IntAct: EBI-21391002; Score: 0.00
DE  Interaction: P52179; IntAct: EBI-21391016; Score: 0.00
DE  Interaction: P12814; IntAct: EBI-21390951; Score: 0.00
DE  Interaction: O15379; IntAct: EBI-21391129; Score: 0.00
DE  Interaction: O14617; IntAct: EBI-21391403; Score: 0.00
DE  Interaction: O75928; IntAct: EBI-21391700; Score: 0.00
DE  Interaction: O60229; IntAct: EBI-21391481; Score: 0.00
DE  Interaction: Q8WV44; IntAct: EBI-21391773; Score: 0.00
DE  Interaction: P54296; IntAct: EBI-21391903; Score: 0.00
DE  Interaction: Q9NYA4; IntAct: EBI-21391824; Score: 0.00
DE  Interaction: Q13023; IntAct: EBI-21392373; Score: 0.00
DE  Interaction: Q9NRD5; IntAct: EBI-26509641; Score: 0.55
DE  Interaction: Q9UII2; IntAct: EBI-21392257; Score: 0.00
DE  Interaction: O15066; IntAct: EBI-21392218; Score: 0.00
DE  Interaction: O75376; IntAct: EBI-21392586; Score: 0.00
DE  Interaction: Q9Y4A8; IntAct: EBI-21392529; Score: 0.00
DE  Interaction: Q5JY77; IntAct: EBI-21392894; Score: 0.00
DE  Interaction: P50749; IntAct: EBI-21392944; Score: 0.00
DE  Interaction: P43243; IntAct: EBI-21392970; Score: 0.00
DE  Interaction: Q9UKI8; IntAct: EBI-21393215; Score: 0.00
DE  Interaction: Q16181; IntAct: EBI-21393295; Score: 0.00
DE  Interaction: O43295; IntAct: EBI-21393383; Score: 0.00
DE  Interaction: Q8N5U6; IntAct: EBI-21393422; Score: 0.00
DE  Interaction: Q8N7X4; IntAct: EBI-25856749; Score: 0.56
DE  Interaction: Q86TI2; IntAct: EBI-25856739; Score: 0.56
DE  Interaction: Q8TCT7; IntAct: EBI-25856729; Score: 0.56
DE  Interaction: O43257; IntAct: EBI-25856721; Score: 0.56
DE  Interaction: P45880; IntAct: EBI-25856713; Score: 0.56
DE  Interaction: Q15583; IntAct: EBI-25856697; Score: 0.56
DE  Interaction: P49768; IntAct: EBI-25856689; Score: 0.56
DE  Interaction: P62714; IntAct: EBI-25856681; Score: 0.56
DE  Interaction: P08473; IntAct: EBI-25856673; Score: 0.56
DE  Interaction: P19419; IntAct: EBI-25856665; Score: 0.56
DE  Interaction: Q14790; IntAct: EBI-25856657; Score: 0.56
DE  Interaction: Q06481; IntAct: EBI-25856649; Score: 0.56
DE  Interaction: P09972; IntAct: EBI-26509515; Score: 0.37
DE  Interaction: Q9ULU4; IntAct: EBI-26509702; Score: 0.37
DE  Interaction: Q8WW38; IntAct: EBI-26509693; Score: 0.37
DE  Interaction: O95359; IntAct: EBI-26509686; Score: 0.37
DE  Interaction: Q9H0F6; IntAct: EBI-26509677; Score: 0.37
DE  Interaction: P61289; IntAct: EBI-26509659; Score: 0.37
DE  Interaction: Q9BZL4; IntAct: EBI-26509650; Score: 0.37
DE  Interaction: Q7Z6G3; IntAct: EBI-26509632; Score: 0.37
DE  Interaction: Q14764; IntAct: EBI-26509623; Score: 0.37
DE  Interaction: Q5TCQ9; IntAct: EBI-26509614; Score: 0.37
DE  Interaction: Q8N163; IntAct: EBI-26509605; Score: 0.37
DE  Interaction: Q9NSC5; IntAct: EBI-26509596; Score: 0.37
DE  Interaction: Q9C0E4; IntAct: EBI-26509587; Score: 0.37
DE  Interaction: Q16760; IntAct: EBI-26509560; Score: 0.37
DE  Interaction: Q9H773; IntAct: EBI-26509551; Score: 0.37
DE  Interaction: Q13554; IntAct: EBI-26509542; Score: 0.37
DE  Interaction: Q9NWD9; IntAct: EBI-26509524; Score: 0.37
DE  Interaction: P55265; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q7Z7C8; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q04637; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q8TAA9; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q05639; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: O43242; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q9H307; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q9Y5V3; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q15007; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: O43660; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q08211; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q9NZI8; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q9P013; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: P41221; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q9BUF5; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: O00154; IntAct: EBI-26367348; Score: 0.50
DE  Interaction: Q6NT76; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: O00425; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q9ULK5; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: O60832; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q99700; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: P48634; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q14157; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q9Y520; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: P39880; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q8WWM7; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q14444; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q96I24; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q13948; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q9HBM6; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-26397711; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-26877965; Score: 0.35
DE  Interaction: A0A0F6B063; IntAct: EBI-27033283; Score: 0.35
DE  Interaction: D0ZRB2; IntAct: EBI-27033344; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: P43405; IntAct: EBI-28935283; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-28955513; Score: 0.35
DE  Interaction: Q6ZMQ8; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q06124; IntAct: EBI-32723738; Score: 0.27
DE  Interaction: Q86UE4; IntAct: EBI-34580762; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0015030;
GO  GO:0042995;
GO  GO:0010369;
GO  GO:0005694;
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:1902737;
GO  GO:0043197;
GO  GO:0044326;
GO  GO:0019897;
GO  GO:0032433;
GO  GO:0097386;
GO  GO:0030426;
GO  GO:1990812;
GO  GO:0043232;
GO  GO:0016020;
GO  GO:1990124;
GO  GO:0005845;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0071598;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098793;
GO  GO:0042734;
GO  GO:1990904;
GO  GO:0045202;
GO  GO:0003682;
GO  GO:0003677;
GO  GO:0070840;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0035064;
GO  GO:0008017;
GO  GO:0035198;
GO  GO:0140693;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:0034046;
GO  GO:0008266;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0035613;
GO  GO:0033592;
GO  GO:1990825;
GO  GO:0035197;
GO  GO:0031369;
GO  GO:0045182;
GO  GO:0030371;
GO  GO:0044325;
GO  GO:0098586;
GO  GO:0006281;
GO  GO:0031047;
GO  GO:0007215;
GO  GO:0044830;
GO  GO:0006397;
GO  GO:0051028;
GO  GO:2000766;
GO  GO:1900453;
GO  GO:1902373;
GO  GO:2000301;
GO  GO:0017148;
GO  GO:0045947;
GO  GO:1901386;
GO  GO:0007399;
GO  GO:0060999;
GO  GO:0051491;
GO  GO:1901254;
GO  GO:2000637;
GO  GO:1902416;
GO  GO:1901800;
GO  GO:0001934;
GO  GO:0002092;
GO  GO:2001022;
GO  GO:0045727;
GO  GO:0000381;
GO  GO:0060998;
GO  GO:0051489;
GO  GO:0060964;
GO  GO:0043488;
GO  GO:0098908;
GO  GO:0046928;
GO  GO:0008380;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWW
SQ  LAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVT
SQ  YDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGAN
SQ  IQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEA
SQ  ENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVP
SQ  FVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRG
SQ  HGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTD
SQ  NRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP
//
ID  P35922;
PN  Fragile X messenger ribonucleoprotein 1;
GN  Fmr1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:16908410, ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:8895584}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere {ECO:0000269|PubMed:24813610}. Chromosome {ECO:0000269|PubMed:24813610}. Cytoplasm {ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:14570712, ECO:0000269|PubMed:15317853, ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:8895584}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:9285783}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:15312650, ECO:0000269|PubMed:15329415, ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:9285783}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q06787}. Perikaryon {ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:16908410, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19193898}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q06787}. Cell projection, axon {ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:19193898}. Cell projection, dendrite {ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:16908410, ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19193898}. Cell projection, dendritic spine {ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:16631377}. Synapse, synaptosome {ECO:0000269|PubMed:18805096}. Cell projection, filopodium {ECO:0000269|PubMed:16631377}. Cell projection, growth cone {ECO:0000269|PubMed:16631377}. Cell projection, filopodium tip {ECO:0000269|PubMed:16631377}. Synapse {ECO:0000269|PubMed:16631377}. Postsynaptic cell membrane {ECO:0000269|PubMed:19193898}. Presynaptic cell membrane {ECO:0000269|PubMed:19193898}. Cell membrane {ECO:0000269|PubMed:24709664}. Note=Colocalizes with H2AX/H2A.x in pericentromeric heterochromatin in response to DNA damaging agents (PubMed:24813610). Localizes on meiotic pachytene-stage chromosomes (PubMed:24813610). Forms nuclear foci representing sites of ongoing DNA replication in response to DNA damaging agents (PubMed:24813610). Shuttles between nucleus and cytoplasm in a XPO1/CRM1-dependent manner (PubMed:8895584, PubMed:8842725). Localizes to cytoplasmic granules, also referred to as messenger ribonucleoprotein particles or mRNPs, along dendrites and dendritic spines (PubMed:15028757, PubMed:16631377). FMR1-containing cytoplasmic granules colocalize to F- actin-rich structures, including filopodium, spines and growth cone during the development of hippocampal neurons (By similarity). FMR1- containing cytoplasmic granules are transported out of the soma along axon and dendrite to synaptic contacts in a microtubule- and kinesin- dependent manner (PubMed:15312650, PubMed:16098134, PubMed:18539120). Colocalizes with CACNA1B in the cytoplasm and at the cell membrane of neurons (PubMed:24709664). Colocalizes with CYFIP1, CYFIP2, NXF2 and ribosomes in the perinuclear region (PubMed:11438699, PubMed:16790844). Colocalizes with CYFIP1 and EIF4E in dendrites and probably at synapses (PubMed:18805096). Colocalizes with FXR1, kinesin, 60S acidic ribosomal protein RPLP0 and SMN in cytoplasmic granules in the soma and neurite cell processes (By similarity). Colocalizes with FXR1 and FXR2 in discrete granules, called fragile X granules (FXGs), along axon and presynaptic compartments (PubMed:19193898). Colocalizes with TDRD3 in cytoplasmic stress granules (SGs) in response to various cellular stress (By similarity). Interacts with SND1 (By similarity). {ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:15312650, ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19193898, ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:8895584}. [Isoform 4]: Nucleus {ECO:0000269|PubMed:8842725}. Nucleus, nucleoplasm {ECO:0000269|PubMed:8842725}.
DR  UNIPROT: P35922;
DR  Pfam: PF05641;
DR  Pfam: PF16098;
DR  Pfam: PF12235;
DR  Pfam: PF00013;
DR  Pfam: PF17904;
DR  Pfam: PF18336;
DR  PROSITE: PS51641;
DR  PROSITE: PS50084;
DE  Function: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs (PubMed:11438589, PubMed:12032354, PubMed:15475576, PubMed:16631377, PubMed:16790844, PubMed:17417632, PubMed:17548835, PubMed:18539120, PubMed:18653529, PubMed:19640847, PubMed:19166269, PubMed:20159450, PubMed:21784246, PubMed:23235829, PubMed:24813610). Plays a role in the alternative splicing of its own mRNA (PubMed:18653529). Plays a role in mRNA nuclear export (PubMed:16790844). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (PubMed:17548835). Stabilizes the scaffolding postsynaptic density protein DLG4/PSD-95 and the myelin basic protein MBP mRNAs in hippocampal neurons and glial cells, respectively; this stabilization is further increased in response to metabotropic glutamate receptor (mGluR) stimulation (PubMed:17417632). Plays a role in selective delivery of a subset of dendritic mRNAs to synaptic sites in response to mGluR activation in a kinesin-dependent manner (PubMed:18539120). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postsynaptic dendritic spines (PubMed:11376146, PubMed:12581522, PubMed:14570712, PubMed:12927206, PubMed:15475576, PubMed:16908410, PubMed:18805096, PubMed:19640847, PubMed:21784246, PubMed:23235829). Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation (PubMed:18805096). Represses mRNA translation by stalling ribosomal translocation during elongation (PubMed:21784246). Reports are contradictory with regards to its ability to mediate translation inhibition of (MBP) mRNA in oligodendrocytes (PubMed:14613971, PubMed:23891804). Also involved in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and hence regulates microRNA (miRNA)-mediated translational repression by AGO2 (PubMed:20159450, PubMed:25464849). Facilitates the assembly of miRNAs on specific target mRNAs (By similarity). Also plays a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses (PubMed:14614133, PubMed:14613971, PubMed:15548614, PubMed:19640847, PubMed:19166269, PubMed:21490210). In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses (PubMed:16908410, PubMed:17507556, PubMed:19640847). Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions (PubMed:11719188, PubMed:11376146, PubMed:14613971, PubMed:17507556, PubMed:21784246, PubMed:21490210, PubMed:24349419). Binds to 5'- ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated region (UTR) and less frequently at 5'-UTR (By similarity). Binds to intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of mRNA targets (PubMed:25692235). Binds to G-quadruplex structures in the 3'- UTR of its own mRNA (By similarity). Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes (By similarity). Binds mRNAs containing U-rich target sequences (By similarity). Binds to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR region of superoxide dismutase SOD1 mRNA (PubMed:19166269). Binds to the dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1 target mRNAs at synapses (PubMed:12581522, PubMed:18805096). Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner (PubMed:17548835). Binds to a subset of miRNAs in the brain (PubMed:20159450). May associate with nascent transcripts in a nuclear protein NXF1-dependent manner (By similarity). In vitro, binds to RNA homomer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (By similarity). Moreover, plays a role in the modulation of the sodium-activated potassium channel KCNT1 gating activity (PubMed:20512134). Negatively regulates the voltage- dependent calcium channel current density in soma and presynaptic terminals of dorsal root ganglion (DRG) neurons, and hence regulates synaptic vesicle exocytosis (By similarity). Modulates the voltage- dependent calcium channel CACNA1B expression at the plasma membrane by targeting the channels for proteosomal degradation (PubMed:24709664). Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development (PubMed:15475576). Recently, has been shown to play a translation-independent role in the modulation of presynaptic action potential (AP) duration and neurotransmitter release via large- conductance calcium-activated potassium (BK) channels in hippocampal and cortical excitatory neurons (PubMed:25561520). Finally, FMR1 may be involved in the control of DNA damage response (DDR) mechanisms through the regulation of ATR-dependent signaling pathways such as histone H2AX/H2A.x and BRCA1 phosphorylations (PubMed:24813610). {ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:11376146, ECO:0000269|PubMed:11438589, ECO:0000269|PubMed:11719188, ECO:0000269|PubMed:12032354, ECO:0000269|PubMed:12581522, ECO:0000269|PubMed:12927206, ECO:0000269|PubMed:14570712, ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:14614133, ECO:0000269|PubMed:15475576, ECO:0000269|PubMed:15548614, ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:16908410, ECO:0000269|PubMed:17417632, ECO:0000269|PubMed:17507556, ECO:0000269|PubMed:17548835, ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:18653529, ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19166269, ECO:0000269|PubMed:19640847, ECO:0000269|PubMed:20159450, ECO:0000269|PubMed:20512134, ECO:0000269|PubMed:21490210, ECO:0000269|PubMed:21784246, ECO:0000269|PubMed:23235829, ECO:0000269|PubMed:23891804, ECO:0000269|PubMed:24349419, ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25561520, ECO:0000269|PubMed:25692235}.
DE  Reference Proteome: Yes;
DE  Interaction: P33175; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q61584; IntAct: EBI-8598304; Score: 0.56
DE  Interaction: P26323; IntAct: EBI-653886; Score: 0.37
DE  Interaction: Q7TMB8; IntAct: EBI-2000004; Score: 0.58
DE  Interaction: P63073; IntAct: EBI-2000515; Score: 0.43
DE  Interaction: P49452; IntAct: EBI-8573213; Score: 0.35
DE  Interaction: Q9JHG6; IntAct: EBI-8014106; Score: 0.47
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q5SQX6; IntAct: EBI-16727864; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9Z2D8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8CJG0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6PDG5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P62996; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9EPQ8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q80YR5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6RHR9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P97379; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O35218; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9JIY2; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P53995; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8R151; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q7TQJ8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8CGF6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P52479; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q91VX2; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q91W18; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8CHG7; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P80560; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q3V1L4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8R4U7; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6Y7W8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9WVR4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6A0A9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q61701; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q60900; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q60899; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6NZJ6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8C008; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O70305; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q61315; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9Z1D7; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6IQX8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q91VL9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q5I043; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: A2AN08; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P70399; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q569Z6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8BHJ5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q920B9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8C804; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: E1U8D0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P61406; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q3TKT4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q62141; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q80U72; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P46061; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9JIF0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P62137; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9R0L6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P60335; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8BSQ9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q99NH2; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8C015; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: B2RRE7; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: E9Q7G0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q5F2E7; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9D6T0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q80TM9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6KCD5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P46935; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q61026; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P09405; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9EPN1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q69ZK1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P60762; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P97820; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9QYH6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9QXZ0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q3UMG5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q5XJV6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P70168; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9QXL1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: A2AIV2; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6ZQ88; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q99JP6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q4U2R1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P70288; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9QZQ8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9WV60; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q61545; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P84089; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8BMB0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9Z148; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q3UJB9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q60838; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8R1A4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P13864; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q80Y83; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q62167; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O54833; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q60737; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q80TV8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: A2AJK6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6PDQ2; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8K389; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6A068; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8VDP4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P23198; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8K3W3; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q99PV8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9QYE3; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9Z1K7; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q70FJ1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9DBR0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P61164; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: F6SEU4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q5DU25; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q68FF6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6PFD5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q91XM9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q811D0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: A2AGT5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O88737; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P61205; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8BGS3; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O88532; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8BJH1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6VNB8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P70398; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: A2RSJ4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q80X50; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9R1R2; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q62318; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9Z321; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: E9Q0S6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8BKI2; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8BYI9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P39447; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9QXE7; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q60864; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P56873; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O54781; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q62261; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6NZL0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q3UHU5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: A2AQ25; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6P4S6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P58801; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P69566; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P70388; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O35295; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P42669; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q3TLH4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q7TPM1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q7TSC1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q62101; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P63318; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P68404; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q76MZ3; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q68FH0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q922S4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P48725; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O08919; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P46460; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P08551; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9WU42; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q60974; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O09000; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P28660; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8VE19; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: E9PWI3; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8K310; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P63085; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q91ZX7; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q7TME0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8BZL8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O55203; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P70662; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O88447; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P28738; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q61768; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P28740; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q3U0V1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q3UXZ9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6ZPR4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q08460; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8C863; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8R0S2; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P46660; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q60625; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O88895; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q91VW5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: A2A699; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: A2ATK9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8C3F2; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q05BC3; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P70372; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9QXY6; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P63168; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9JHU4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O08553; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P39053; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q3UH60; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O70566; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O54784; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q02248; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q0V8T9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P12960; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6ZQ08; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q80U49; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6A065; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6P9K8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q60865; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8C1B1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q923T9; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6PHZ2; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P28652; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P11798; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8R0S4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8CC27; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8R3Z5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q5RJI5; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: O08539; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9D219; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q60875; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6P9R4; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8C4V1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q6DFV3; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q99NH0; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q8CJG1; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9ESC8; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q9EP53; IntAct: EBI-16734894; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16750831; Score: 0.35
DE  Interaction: Q6UWE0; IntAct: EBI-22050272; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26472902; Score: 0.35
DE  Interaction: D0ZPH9; IntAct: EBI-27035192; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0043679;
GO  GO:0015030;
GO  GO:0044297;
GO  GO:0042995;
GO  GO:0010369;
GO  GO:0005694;
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:1902737;
GO  GO:0043197;
GO  GO:0044327;
GO  GO:0044326;
GO  GO:0019897;
GO  GO:0032433;
GO  GO:0097386;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:1990812;
GO  GO:0098686;
GO  GO:0016020;
GO  GO:1990124;
GO  GO:0015630;
GO  GO:0005845;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0071598;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0098794;
GO  GO:0099524;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098793;
GO  GO:0099523;
GO  GO:0042734;
GO  GO:1990635;
GO  GO:1990904;
GO  GO:0005791;
GO  GO:0098685;
GO  GO:0032797;
GO  GO:0005790;
GO  GO:0097444;
GO  GO:0045202;
GO  GO:0043195;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0035064;
GO  GO:0008017;
GO  GO:0035198;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:0034046;
GO  GO:0008266;
GO  GO:0019904;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0019903;
GO  GO:0043022;
GO  GO:0000340;
GO  GO:0003723;
GO  GO:0035613;
GO  GO:0033592;
GO  GO:1990825;
GO  GO:0035197;
GO  GO:0031369;
GO  GO:0045182;
GO  GO:0030371;
GO  GO:0044325;
GO  GO:0008089;
GO  GO:0098586;
GO  GO:0007417;
GO  GO:0060996;
GO  GO:0006281;
GO  GO:0098976;
GO  GO:0031047;
GO  GO:0007215;
GO  GO:0098977;
GO  GO:0044830;
GO  GO:0006397;
GO  GO:0051028;
GO  GO:2000766;
GO  GO:0010629;
GO  GO:1900453;
GO  GO:1902373;
GO  GO:0043524;
GO  GO:0045665;
GO  GO:0010955;
GO  GO:0002091;
GO  GO:2000301;
GO  GO:0017148;
GO  GO:0045947;
GO  GO:1901386;
GO  GO:0060999;
GO  GO:0051491;
GO  GO:0010628;
GO  GO:1901254;
GO  GO:0048170;
GO  GO:1900454;
GO  GO:1900273;
GO  GO:2000637;
GO  GO:1902416;
GO  GO:1901800;
GO  GO:0001934;
GO  GO:0002092;
GO  GO:2001022;
GO  GO:0050806;
GO  GO:0045727;
GO  GO:0000381;
GO  GO:0060998;
GO  GO:0051489;
GO  GO:0060964;
GO  GO:1905244;
GO  GO:0043488;
GO  GO:0098908;
GO  GO:0046928;
GO  GO:0099578;
GO  GO:0099577;
GO  GO:0097396;
GO  GO:0008380;
GO  GO:0035176;
GO  GO:0019226;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPERQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWW
SQ  LAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLEVPEDLRQMCAKESAHKDFKKAVGAFSVT
SQ  YDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLILRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGAN
SQ  IQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEA
SQ  ENEKSVPQEEEIMPPSSLPSNNSRVGPNSSEEKKHLDTKENTHFSQPNSTKVQRVLVVSSIVAGGPQKPEPKAWQGMVPF
SQ  VFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKGYVTDDGQGMGRGSRPYRNRGH
SQ  GRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRRGGGRGQGGRGRGGGFKGNDDHSRTDN
SQ  RPRNPREAKGRTADGSLQSASSEGSRLRTGKDRNQKKEKPDSVDGLQPLVNGVP
//
ID  Q5R9B4;
PN  Fragile X messenger ribonucleoprotein 1;
GN  FMR1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q06787}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere {ECO:0000250|UniProtKB:P35922}. Chromosome {ECO:0000250|UniProtKB:P35922}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q06787}. Perikaryon {ECO:0000250|UniProtKB:Q06787}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q06787}. Cell projection, axon {ECO:0000250|UniProtKB:P35922}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35922}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P35922}. Synapse, synaptosome {ECO:0000250|UniProtKB:P35922}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q06787}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:P35922}. Synapse {ECO:0000250|UniProtKB:P35922}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Cell membrane {ECO:0000250|UniProtKB:P35922}. Note=Colocalizes with H2AX/H2A.x in pericentromeric heterochromatin in response to DNA damaging agents. Localizes on meiotic pachytene-stage chromosomes. Forms nuclear foci representing sites of ongoing DNA replication in response to DNA damaging agents. Shuttles between nucleus and cytoplasm in a XPO1/CRM1- dependent manner. Localizes to cytoplasmic granules, also referred to as messenger ribonucleoprotein particles or mRNPs, along dendrites and dendritic spines. FMR1-containing cytoplasmic granules colocalize to F- actin-rich structures, including filopodium, spines and growth cone during the development of hippocampal neurons. FMR1-containing cytoplasmic granules are transported out of the soma along axon and dendrite to synaptic contacts in a microtubule- and kinesin-dependent manner. Colocalizes with CACNA1B in the cytoplasm and at the cell membrane of neurons. Colocalizes with CYFIP1, CYFIP2, NXF2 and ribosomes in the perinuclear region. Colocalizes with CYFIP1 and EIF4E in dendrites and probably at synapses. Colocalizes with FXR1, kinesin, 60S acidic ribosomal protein RPLP0 and SMN in cytoplasmic granules in the soma and neurite cell processes. Colocalizes with FXR1 and FXR2 in discrete granules, called fragile X granules (FXGs), along axon and presynaptic compartments. Colocalizes with TDRD3 in cytoplasmic stress granules (SGs) in response to various cellular stress. {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1}.
DR  UNIPROT: Q5R9B4;
DR  Pfam: PF05641;
DR  Pfam: PF16098;
DR  Pfam: PF12235;
DR  Pfam: PF00013;
DR  Pfam: PF17904;
DR  Pfam: PF18336;
DR  PROSITE: PS51641;
DR  PROSITE: PS50084;
DE  Function: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs. Plays a role in the alternative splicing of its own mRNA. Plays a role in mRNA nuclear export. Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons. Stabilizes the scaffolding postsynaptic density protein DLG4/PSD-95 and the myelin basic protein (MBP) mRNAs in hippocampal neurons and glial cells, respectively; this stabilization is further increased in response to metabotropic glutamate receptor (mGluR) stimulation. Plays a role in selective delivery of a subset of dendritic mRNAs to synaptic sites in response to mGluR activation in a kinesin-dependent manner. Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postsynaptic dendritic spines. Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation. Represses mRNA translation by stalling ribosomal translocation during elongation. Reports are contradictory with regards to its ability to mediate translation inhibition of MBP mRNA in oligodendrocytes. Also involved in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and hence regulates microRNA (miRNA)-mediated translational repression by AGO2. Facilitates the assembly of miRNAs on specific target mRNAs. Also plays a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses. In response to mGluR stimulation, FMR1- target mRNAs are rapidly derepressed, allowing for local translation at synapses. Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions. Binds to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated region (UTR) and less frequently at 5'-UTR. Binds to intramolecular G- quadruplex structures in the 5'- or 3'-UTRs of mRNA targets. Binds to G-quadruplex structures in the 3'-UTR of its own mRNA. Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes. Binds mRNAs containing U-rich target sequences. Binds to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR region of superoxide dismutase SOD1 mRNA. Binds to the dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1 target mRNAs at synapses. Associates with export factor NXF1 mRNA- containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner. Binds to a subset of miRNAs in the brain. May associate with nascent transcripts in a nuclear protein NXF1-dependent manner. In vitro, binds to RNA homomer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C). Moreover, plays a role in the modulation of the sodium-activated potassium channel KCNT1 gating activity. Negatively regulates the voltage-dependent calcium channel current density in soma and presynaptic terminals of dorsal root ganglion (DRG) neurons, and hence regulates synaptic vesicle exocytosis. Modulates the voltage-dependent calcium channel CACNA1B expression at the plasma membrane by targeting the channels for proteosomal degradation. Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development. Recently, has been shown to play a translation-independent role in the modulation of presynaptic action potential (AP) duration and neurotransmitter release via large-conductance calcium-activated potassium (BK) channels in hippocampal and cortical excitatory neurons. Finally, FMR1 may be involved in the control of DNA damage response (DDR) mechanisms through the regulation of ATR-dependent signaling pathways such as histone H2AX/H2A.x and BRCA1 phosphorylations. {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0042995;
GO  GO:0010369;
GO  GO:0005694;
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:1902737;
GO  GO:0043197;
GO  GO:0019897;
GO  GO:0032433;
GO  GO:0097386;
GO  GO:0030426;
GO  GO:1990812;
GO  GO:0005845;
GO  GO:0043005;
GO  GO:0071598;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098793;
GO  GO:0042734;
GO  GO:1990904;
GO  GO:0045202;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0002151;
GO  GO:0035064;
GO  GO:0008017;
GO  GO:0035198;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:0034046;
GO  GO:0008266;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0035613;
GO  GO:0033592;
GO  GO:1990825;
GO  GO:0035197;
GO  GO:0030371;
GO  GO:0006281;
GO  GO:0031047;
GO  GO:0007215;
GO  GO:0006397;
GO  GO:0051028;
GO  GO:2000766;
GO  GO:0010629;
GO  GO:1900453;
GO  GO:2000301;
GO  GO:0017148;
GO  GO:0045947;
GO  GO:1901386;
GO  GO:0007399;
GO  GO:0060999;
GO  GO:0051491;
GO  GO:2000637;
GO  GO:1902416;
GO  GO:1901800;
GO  GO:0002092;
GO  GO:0045727;
GO  GO:0000381;
GO  GO:0060998;
GO  GO:0051489;
GO  GO:0060964;
GO  GO:0043488;
GO  GO:0098908;
GO  GO:0046928;
GO  GO:0008380;
GO  GO:0060538;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWW
SQ  LAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKESAHKDFKKAVGAFSVT
SQ  YDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGAN
SQ  IQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEA
SQ  ENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLEIKENSTHFSQPNSTKVQRGMVPFVFVGTKDSIANATVLLDYHL
SQ  NYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASE
SQ  TESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFEGNDDHSRTDNRPRNPREAKGRTTDGSLQNT
SQ  SSEGNRLRTGKDRNRKKEKPDSVDGQQPLVNGVP
//
ID  Q80WE1;
PN  Fragile X messenger ribonucleoprotein 1;
GN  Fmr1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:9030614}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere {ECO:0000250|UniProtKB:P35922}. Chromosome {ECO:0000250|UniProtKB:P35922}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P35922}. Perikaryon {ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:15564573, ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:9030614, ECO:0000269|PubMed:9144248}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:23891804}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q06787}. Cell projection, neuron projection {ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:24709664}. Cell projection, dendrite {ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:15564573, ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:9030614, ECO:0000269|PubMed:9144248}. Cell projection, dendritic spine {ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:9030614, ECO:0000269|PubMed:9144248}. Cell projection, growth cone {ECO:0000269|PubMed:16098134}. Cell projection, filopodium {ECO:0000269|PubMed:16098134}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:P35922}. Cell projection, axon {ECO:0000269|PubMed:9030614}. Synapse {ECO:0000269|PubMed:15028757}. Synapse, synaptosome {ECO:0000269|PubMed:15564573, ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:9030614, ECO:0000269|PubMed:9144248}. Postsynaptic density {ECO:0000269|PubMed:9144248}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Cell membrane {ECO:0000250|UniProtKB:P35922}. Note=Colocalizes with H2AX/H2A.x in pericentromeric heterochromatin in response to DNA damaging agents (By similarity). Localizes on meiotic pachytene-stage chromosomes (By similarity). Forms nuclear foci representing sites of ongoing DNA replication in response to DNA damaging agents (By similarity). Shuttles between nucleus and cytoplasm in a XPO1/CRM1-dependent manner (By similarity). Localizes to cytoplasmic granules, also referred to as messenger ribonucleoprotein particles or mRNPs, along dendrites and dendritic spines (PubMed:15028757, PubMed:23891804). FMR1-containing cytoplasmic granules colocalize to F-actin-rich structures, including filopodium, spines and growth cone during the development of hippocampal neurons (PubMed:16098134). FMR1-containing cytoplasmic granules are transported out of the soma along axon and dendrite to synaptic contacts in a microtubule- and kinesin-dependent manner (PubMed:16098134). Colocalizes with CACNA1B in the cytoplasm and at the cell membrane of neurons (By similarity). Colocalizes with CYFIP1, CYFIP2, NXF2 and ribosomes in the perinuclear region (By similarity). Colocalizes with CYFIP1 and EIF4E in dendrites and probably at synapses (By similarity). Colocalizes with FXR1, kinesin, 60S acidic ribosomal protein RPLP0 and SMN in cytoplasmic granules in the soma and neurite cell processes (By similarity). Colocalizes with FXR1 and FXR2 in discrete granules, called fragile X granules (FXGs), along axon and presynaptic compartments (By similarity). Colocalizes with TDRD3 in cytoplasmic stress granules (SGs) in response to various cellular stress (By similarity). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787, ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:23891804}.
DR  UNIPROT: Q80WE1;
DR  UNIPROT: P70568;
DR  Pfam: PF05641;
DR  Pfam: PF16098;
DR  Pfam: PF12235;
DR  Pfam: PF00013;
DR  Pfam: PF17904;
DR  Pfam: PF18336;
DR  PROSITE: PS51641;
DR  PROSITE: PS50084;
DE  Function: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs (PubMed:9144248). Plays a role in the alternative splicing of its own mRNA (By similarity). Plays a role in mRNA nuclear export (By similarity). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (By similarity). Stabilizes the scaffolding postsynaptic density protein DLG4/PSD-95 and the myelin basic protein MBP mRNAs in hippocampal neurons and glial cells, respectively; this stabilization is further increased in response to metabotropic glutamate receptor (mGluR) stimulation (By similarity). Plays a role in selective delivery of a subset of dendritic mRNAs to synaptic sites in response to mGluR activation in a kinesin-dependent manner (By similarity). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postsynaptic dendritic spines (PubMed:9144248). Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation (By similarity). Represses mRNA translation by stalling ribosomal translocation during elongation (By similarity). Reports are contradictory with regards to its ability to mediate translation inhibition of (MBP) mRNA in oligodendrocytes (By similarity). Also involved in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and hence regulates microRNA (miRNA)-mediated translational repression by AGO2 (By similarity). Facilitates the assembly of miRNAs on specific target mRNAs (By similarity). Also plays a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses (By similarity). In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses (By similarity). Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions (By similarity). Binds to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated region (UTR) and less frequently at 5'-UTR (By similarity). Binds to intramolecular G- quadruplex structures in the 5'- or 3'-UTRs of mRNA targets (By similarity). Binds to G-quadruplex structures in the 3'-UTR of its own mRNA (By similarity). Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes (By similarity). Binds mRNAs containing U-rich target sequences (By similarity). Binds to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR region of superoxide dismutase SOD1 mRNA (By similarity). Binds to the dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1 target mRNAs at synapses (By similarity). Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2- dependent manner (By similarity). Binds to a subset of miRNAs in the brain (By similarity). May associate with nascent transcripts in a nuclear protein NXF1-dependent manner (By similarity). In vitro, binds to RNA homomer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (By similarity). Moreover, plays a role in the modulation of the sodium-activated potassium channel KCNT1 gating activity (By similarity). Negatively regulates the voltage-dependent calcium channel current density in soma and presynaptic terminals of dorsal root ganglion (DRG) neurons, and hence regulates synaptic vesicle exocytosis (PubMed:24709664). Modulates the voltage-dependent calcium channel CACNA1B expression at the plasma membrane by targeting the channels for proteosomal degradation (By similarity). Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development (By similarity). Recently, has been shown to play a translation-independent role in the modulation of presynaptic action potential (AP) duration and neurotransmitter release via large-conductance calcium-activated potassium (BK) channels in hippocampal and cortical excitatory neurons (By similarity). Finally, FMR1 may be involved in the control of DNA damage response (DDR) mechanisms through the regulation of ATR-dependent signaling pathways such as histone H2AX/H2A.x and BRCA1 phosphorylations (By similarity). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787, ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:9144248}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9R0N3; IntAct: EBI-9526900; Score: 0.35
DE  Interaction: F1M0Z1; IntAct: EBI-26961439; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0043679;
GO  GO:0015030;
GO  GO:0044297;
GO  GO:0042995;
GO  GO:0010369;
GO  GO:0005694;
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:1902737;
GO  GO:0043197;
GO  GO:0044327;
GO  GO:0044326;
GO  GO:0019897;
GO  GO:0032433;
GO  GO:0097386;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:1990812;
GO  GO:0098686;
GO  GO:0016020;
GO  GO:1990124;
GO  GO:0015630;
GO  GO:0005845;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0071598;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0098794;
GO  GO:0099524;
GO  GO:0014069;
GO  GO:0098793;
GO  GO:0099523;
GO  GO:0042734;
GO  GO:1990635;
GO  GO:1990904;
GO  GO:0005791;
GO  GO:0098685;
GO  GO:0032797;
GO  GO:0005790;
GO  GO:0097444;
GO  GO:0045202;
GO  GO:0043195;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0035064;
GO  GO:0008017;
GO  GO:0035198;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:0034046;
GO  GO:0008266;
GO  GO:0019904;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0019903;
GO  GO:0043022;
GO  GO:0000340;
GO  GO:0003723;
GO  GO:0035613;
GO  GO:0033592;
GO  GO:1990825;
GO  GO:0035197;
GO  GO:0031369;
GO  GO:0045182;
GO  GO:0030371;
GO  GO:0044325;
GO  GO:0008089;
GO  GO:0006974;
GO  GO:0072711;
GO  GO:1904009;
GO  GO:0035865;
GO  GO:0034644;
GO  GO:0098586;
GO  GO:0007417;
GO  GO:0060996;
GO  GO:0050974;
GO  GO:0006281;
GO  GO:0098976;
GO  GO:0031047;
GO  GO:0007215;
GO  GO:0098977;
GO  GO:0044830;
GO  GO:0006397;
GO  GO:0051028;
GO  GO:2000766;
GO  GO:0010629;
GO  GO:1900453;
GO  GO:1902373;
GO  GO:0043524;
GO  GO:0045665;
GO  GO:0010955;
GO  GO:0002091;
GO  GO:2000301;
GO  GO:0017148;
GO  GO:0045947;
GO  GO:1901386;
GO  GO:0001541;
GO  GO:0060999;
GO  GO:0051491;
GO  GO:0010628;
GO  GO:1901254;
GO  GO:0048170;
GO  GO:1900454;
GO  GO:1900273;
GO  GO:2000637;
GO  GO:1902416;
GO  GO:1901800;
GO  GO:0001934;
GO  GO:0002092;
GO  GO:2001022;
GO  GO:0050806;
GO  GO:0045727;
GO  GO:0000381;
GO  GO:0060998;
GO  GO:0051489;
GO  GO:0060964;
GO  GO:1905244;
GO  GO:0043488;
GO  GO:0098908;
GO  GO:0046928;
GO  GO:0006417;
GO  GO:0099578;
GO  GO:0099577;
GO  GO:0014823;
GO  GO:0042220;
GO  GO:0051602;
GO  GO:0034698;
GO  GO:0070555;
GO  GO:0097396;
GO  GO:0009416;
GO  GO:0008380;
GO  GO:0060538;
GO  GO:0035176;
GO  GO:0019226;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPERQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWW
SQ  LAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLEVPEDLRQMCAKESAHKDFKKAVGAFSVT
SQ  YDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLILRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGAN
SQ  IQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEA
SQ  ENEKSVPQEEENLPPSSLPSNNSRVGSNSSEEKKHLDTKENTHFSQPNSTKVQRGMVPFVFVGTKDSIANATVLLDYHLN
SQ  YLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKGYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASET
SQ  ESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPRETKGRTTDGSLQSTS
SQ  SEGSRLRTGKDRNQKKEKPDSVDGLQPLVNGVP
//
ID  Q6GLC9;
PN  Fragile X messenger ribonucleoprotein 1 homolog;
GN  fmr1;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q06787}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere {ECO:0000250|UniProtKB:P35922}. Chromosome {ECO:0000250|UniProtKB:P35922}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q06787}. Perikaryon {ECO:0000250|UniProtKB:Q06787}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q06787}. Cell projection, axon {ECO:0000250|UniProtKB:P35922}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35922}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P35922}. Synapse, synaptosome {ECO:0000250|UniProtKB:P35922}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q06787}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:P35922}. Synapse {ECO:0000250|UniProtKB:P35922}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Cell membrane {ECO:0000250|UniProtKB:P35922}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q06787}.
DR  UNIPROT: Q6GLC9;
DR  Pfam: PF05641;
DR  Pfam: PF16098;
DR  Pfam: PF12235;
DR  Pfam: PF00013;
DR  Pfam: PF17904;
DR  Pfam: PF18336;
DR  PROSITE: PS51641;
DR  PROSITE: PS50084;
DE  Function: Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs. Binds poly(G) and poly(U), and to a lower extent poly(A) and poly(C). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:P51113, ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0042995;
GO  GO:0010369;
GO  GO:0005694;
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0010494;
GO  GO:0030425;
GO  GO:1902737;
GO  GO:0043197;
GO  GO:0044326;
GO  GO:0019897;
GO  GO:0032433;
GO  GO:0097386;
GO  GO:0030426;
GO  GO:1990812;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0071598;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098793;
GO  GO:0042734;
GO  GO:1990904;
GO  GO:0045202;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0002151;
GO  GO:0035064;
GO  GO:0008017;
GO  GO:0035198;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:0034046;
GO  GO:0008266;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0003723;
GO  GO:0035613;
GO  GO:0033592;
GO  GO:1990825;
GO  GO:0035197;
GO  GO:0045182;
GO  GO:0030371;
GO  GO:0007420;
GO  GO:0048755;
GO  GO:0051216;
GO  GO:0050890;
GO  GO:0006281;
GO  GO:0021905;
GO  GO:0007215;
GO  GO:0006397;
GO  GO:0051028;
GO  GO:2000766;
GO  GO:0010629;
GO  GO:1900453;
GO  GO:2000301;
GO  GO:0017148;
GO  GO:0045947;
GO  GO:1901386;
GO  GO:0014036;
GO  GO:0048812;
GO  GO:0060999;
GO  GO:0051491;
GO  GO:2000637;
GO  GO:1902416;
GO  GO:1901800;
GO  GO:0001934;
GO  GO:0002092;
GO  GO:2001022;
GO  GO:0045727;
GO  GO:0000381;
GO  GO:0060998;
GO  GO:0051489;
GO  GO:0060964;
GO  GO:0090365;
GO  GO:0043488;
GO  GO:0098908;
GO  GO:0046928;
GO  GO:0008380;
GO  GO:0060538;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELAVEVRGSNGAFYKAFVKDVHEDSITVTFENNWQQERQIPFHDVRFPPPSGYNKDINESDEVEVYSRANEKEPCCWW
SQ  LAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKNSFHKVKLDVPEDLRQMCAKDSAHKDFKKAVGAFSVS
SQ  YDSENYQLVILSVNEVTIKRANMLSDMHFRSLRTKLSLMLRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGAN
SQ  IQQARKVPGVTAIDLDEDTCTFHIYGEDQEAVKKARTYLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEA
SQ  ENDKNISPEEGMVPFVFVGTKDSITNATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRPDKEKGYQSEDL
SQ  SGTGRGSRPYNNRGRSRRGTGYASDIRYGDPDYRKTTYPEYPRSQAFWIKGTNSEASNASETESDHRDELSDWSLAPAED
SQ  DRDNYHRRGDGRRRGGPRGQGMRGRGGFKGNDDQPRPDNRQRNSRETKARTSDGSLQIRIDCNNERSVHTKTLQNASVEG
SQ  SRLRTGKDRVQKKEKSEVVDGPQVVVNGIP
//
ID  Q6PIV2;
PN  Forkhead box protein R1;
GN  FOXR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:34723967}. Cytoplasm {ECO:0000269|PubMed:25609838, ECO:0000269|PubMed:34723967}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25609838}. Note=Localizes to the nucleus and cytoplasm with higher levels in the nucleus where it is expressed in a diffuse manner (PubMed:34723967). Located in the cytoplasm of spermatocytes and strongly accumulates at the perinuclear region in elongated spermatids (PubMed:25609838). {ECO:0000269|PubMed:25609838, ECO:0000269|PubMed:34723967}.
DR  UNIPROT: Q6PIV2;
DR  UNIPROT: B0YJ15;
DR  UNIPROT: Q08AS8;
DR  UNIPROT: Q86UT9;
DR  UNIPROT: Q8IXX2;
DR  Pfam: PF00250;
DR  PROSITE: PS50039;
DR  OMIM: 615755;
DR  DisGeNET: 283150;
DE  Function: Transcription factor which acts as both an activator and a repressor (PubMed:34723967). Activates transcription of a number of genes including the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 which are involved in protection against oxidative stress (PubMed:34723967). Required for normal brain development (By similarity). {ECO:0000250|UniProtKB:Q3UTB7, ECO:0000269|PubMed:34723967}.
DE  Disease: Note=Defects in FOXR1 may be the cause of a severe neurological disorder characterized by postnatal microcephaly, progressive brain atrophy and global developmental delay. {ECO:0000269|PubMed:34723967}.
DE  Reference Proteome: Yes;
DE  Interaction: O14656; IntAct: EBI-25847482; Score: 0.56
DE  Interaction: P50222; IntAct: EBI-10253813; Score: 0.56
DE  Interaction: Q53SE7; IntAct: EBI-10253831; Score: 0.56
DE  Interaction: Q8N9N5; IntAct: EBI-10253841; Score: 0.56
DE  Interaction: Q96CD2; IntAct: EBI-10253853; Score: 0.78
DE  Interaction: Q9UBU8; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q969R5; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q9BZS1; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q00532; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q9NSD9; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: P01040; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q9Y4A5; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q96L91; IntAct: EBI-11319459; Score: 0.53
DE  Interaction: O95347; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q969U6; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q52LR7; IntAct: EBI-11319459; Score: 0.53
DE  Interaction: Q9NPF5; IntAct: EBI-11319459; Score: 0.53
DE  Interaction: P01106; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: P31276; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q6PIV2; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q9NXR8; IntAct: EBI-11319459; Score: 0.53
DE  Interaction: O60264; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: O95619; IntAct: EBI-11319459; Score: 0.53
DE  Interaction: Q9H2F5; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: P04198; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: O96019; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q05BQ5; IntAct: EBI-11319459; Score: 0.53
DE  Interaction: Q9NV56; IntAct: EBI-11319459; Score: 0.53
DE  Interaction: Q15014; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: P61244; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q9H0E9; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q92993; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: Q9UBN7; IntAct: EBI-11321774; Score: 0.35
DE  Interaction: Q99523; IntAct: EBI-11321774; Score: 0.35
DE  Interaction: Q96T76; IntAct: EBI-11321774; Score: 0.35
DE  Interaction: Q16720; IntAct: EBI-11321774; Score: 0.35
DE  Interaction: P53621; IntAct: EBI-11321774; Score: 0.35
DE  Interaction: Q96IK5; IntAct: EBI-25252587; Score: 0.56
DE  Interaction: Q96LK0; IntAct: EBI-24531695; Score: 0.56
DE  Interaction: Q7L190; IntAct: EBI-24582359; Score: 0.56
DE  Interaction: Q9HAF1; IntAct: EBI-21816916; Score: 0.35
DE  Interaction: Q15906; IntAct: EBI-21816916; Score: 0.35
DE  Interaction: P50225; IntAct: EBI-21816916; Score: 0.35
DE  Interaction: P01023; IntAct: EBI-25830325; Score: 0.56
DE  Interaction: Q92870; IntAct: EBI-25831871; Score: 0.56
DE  Interaction: G5E9A7; IntAct: EBI-25843815; Score: 0.56
DE  Interaction: P50570; IntAct: EBI-25845425; Score: 0.56
DE  Interaction: P51608; IntAct: EBI-25876038; Score: 0.56
DE  Interaction: D3DTS7; IntAct: EBI-25883900; Score: 0.56
DE  Interaction: Q16637; IntAct: EBI-25891888; Score: 0.56
DE  Interaction: Q86WV8; IntAct: EBI-25893897; Score: 0.56
DE  Interaction: Q8TB36; IntAct: EBI-25923540; Score: 0.56
DE  Interaction: Q7Z412; IntAct: EBI-25925249; Score: 0.56
DE  Interaction: P37840; IntAct: EBI-25941226; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25944360; Score: 0.56
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001228;
GO  GO:0000981;
GO  GO:0001227;
GO  GO:1990837;
GO  GO:0007420;
GO  GO:0045944;
GO  GO:0006357;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGNELFLAFTTSHLPLAEQKLARYKLRIVKPPKLPLEKKPNPDKDGPDYEPNLWMWVNPNIVYPPGKLEVSGRRKREDLT
SQ  STLPSSQPPQKEEDASCSEAAGVESLSQSSSKRSPPRKRFAFSPSTWELTEEEEAEDQEDSSSMALPSPHKRAPLQSRRL
SQ  RQASSQAGRLWSRPPLNYFHLIALALRNSSPCGLNVQQIYSFTRKHFPFFRTAPEGWKNTVRHNLCFRDSFEKVPVSMQG
SQ  GASTRPRSCLWKLTEEGHRRFAEEARALASTRLESIQQCMSQPDVMPFLFDL
//
ID  Q3UTB7;
PN  Forkhead box protein R1;
GN  Foxr1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q6PIV2}. Cytoplasm {ECO:0000269|PubMed:25609838}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25609838}. Note=Localizes to the nucleus and cytoplasm with higher levels in the nucleus where it is expressed in a diffuse manner (PubMed:34723967). Located in the cytoplasm of spermatocytes and strongly accumulates at the perinuclear region in elongated spermatids (PubMed:25609838). {ECO:0000269|PubMed:25609838, ECO:0000269|PubMed:34723967}.
DR  UNIPROT: Q3UTB7;
DR  Pfam: PF00250;
DR  PROSITE: PS50039;
DE  Function: Transcription factor which acts as both an activator and a repressor (By similarity). Activates transcription of a number of genes including the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 which are involved in protection against oxidative stress (By similarity). Required for normal brain development (PubMed:34723967). {ECO:0000250|UniProtKB:Q6PIV2, ECO:0000269|PubMed:34723967}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001228;
GO  GO:0001227;
GO  GO:1990837;
GO  GO:0007420;
GO  GO:0045944;
GO  GO:0006357;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGNECFLTFTTTHLSEAEQKLALYRLQLVEPPKLPLEKKTNPDKDGPDIKPNLWMWVNPNMVYPPGKLEVAVKEEDQSAL
SQ  SAFQPALKEEEDSCSEASEVQQPLPPCRQKRKQRRSTVPLPLAPGRRAPLENPWRLPQAISPEGRLWSRPPLHYFHLIAL
SQ  ALRNSPPCGLSVQQIYSFTREHFPFFRTAPEAWKNTVRHNLSFRDSFEKVPASRQGGASTGPRSCLWKLTEEGHRRFSKE
SQ  ARTLASTQLQSIQQCMSQPGVKPFLFDL
//
ID  H0UZ81;
PN  Fibronectin type III and SPRY domain-containing protein 2;
GN  FSD2;
OS  10141;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:28740084}. Sarcoplasmic reticulum {ECO:0000269|PubMed:28740084}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:28740084}. Note=In skeletal muscles and striated muscles flanks Z-disks (PubMed:28740084). Partially colocalizes with RYR2 in the sarcoplasmic reticulum (PubMed:28740084). {ECO:0000269|PubMed:28740084}.
DR  UNIPROT: H0UZ81;
DR  Pfam: PF00041;
DR  Pfam: PF00622;
DR  PROSITE: PS50188;
DR  PROSITE: PS50853;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEEAGEEPRLDRPTAPKDFHFYNMDLYDSEDRLPLFPEENTRLRRQTIQAEMTYDPKEVGNSFVDEGRMGVPAYPPYGI
SQ  KRREPGWEQRDWRLEGEVETEDQDQDFSQWSMAGQSQALWESYRYTHGRASEEYECYVIPEEEDEEEAADLFCVTCRTPI
SQ  RAVEKDFGEHKEHEVTPLSKALESAKEEIHKNMYKLEQQIIEMENFASHLEEVFITVEENFGRQEQNFESHYNGILETLA
SQ  QKYEEKIQALGEKKKEKLEALYGQLVSCGENLDTCKELMETIEEMCHEEKVDFLKVSNETLGKFLKTKTDVEIAAQPEFE
SQ  DQTLDFSDVEQLMGSMNTILAPSAPVINPQAPNSATGSSVRVCWSLYADDTVESYQLSYRPVRDSLPGKEQAEFTVTVKE
SQ  SYCSVTNLEPNTQYEFWVIAQNRAGPSPSSEHAMYMTAPSPPIIKTEAIRSCEEAALICWESGNLNPVDSYTVELTQVEE
SQ  PAASGVTESVVGIPICESLIQLQPGQSYTICVRALNVGGPSARSTPATVRTTGSYFPLNKATCHPWLTISEDGFTVIRSE
SQ  RKNLTQELQPQQTQFTRCVAIMGNLIPVRGRHYWEIEMDEHLDYTVGVAFEDVPKQEDLGANGFSWCMRHTFASSRHKYE
SQ  FLHNRTTPDIRITVPPKKIGILLDYENSKLSFFNVDIAQHLYTFSCQLQQFVHPCFSLEKPGCLKIHNGISMPMHATFY
//
ID  A1L4K1;
PN  Fibronectin type III and SPRY domain-containing protein 2;
GN  FSD2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:H0UZ81}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:H0UZ81}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:H0UZ81}. Note=In skeletal muscles and striated muscles flanks Z-disks. Partially colocalizes with RYR2 in the sarcoplasmic reticulum. {ECO:0000250|UniProtKB:H0UZ81}.
DR  UNIPROT: A1L4K1;
DR  UNIPROT: B3KVG1;
DR  UNIPROT: B7ZM02;
DR  Pfam: PF00041;
DR  Pfam: PF00622;
DR  PROSITE: PS50188;
DR  PROSITE: PS50853;
DR  DisGeNET: 123722;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q14324; IntAct: EBI-5661041; Score: 0.00
DE  Interaction: Q7Z3I7; IntAct: EBI-10172604; Score: 0.60
DE  Interaction: Q7Z3B3; IntAct: EBI-10178303; Score: 0.56
DE  Interaction: O95990; IntAct: EBI-10192906; Score: 0.56
DE  Interaction: P10768; IntAct: EBI-10197227; Score: 0.78
DE  Interaction: P17024; IntAct: EBI-10199416; Score: 0.56
DE  Interaction: P28070; IntAct: EBI-10204607; Score: 0.56
DE  Interaction: P29972; IntAct: EBI-10204944; Score: 0.56
DE  Interaction: P31146; IntAct: EBI-10205786; Score: 0.78
DE  Interaction: Q00994; IntAct: EBI-10222282; Score: 0.72
DE  Interaction: Q06787; IntAct: EBI-10224474; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-10224779; Score: 0.67
DE  Interaction: Q14738; IntAct: EBI-10233892; Score: 0.56
DE  Interaction: Q15973; IntAct: EBI-10237322; Score: 0.56
DE  Interaction: Q16670; IntAct: EBI-10238175; Score: 0.56
DE  Interaction: Q3B820; IntAct: EBI-10240125; Score: 0.56
DE  Interaction: Q53FD0; IntAct: EBI-10242267; Score: 0.56
DE  Interaction: Q5JS98; IntAct: EBI-10244397; Score: 0.56
DE  Interaction: Q6NYC8; IntAct: EBI-10251682; Score: 0.72
DE  Interaction: Q6P1J9; IntAct: EBI-10252260; Score: 0.78
DE  Interaction: Q6PJG3; IntAct: EBI-10253974; Score: 0.56
DE  Interaction: Q86VK4; IntAct: EBI-10259792; Score: 0.56
DE  Interaction: Q86YD7; IntAct: EBI-10260722; Score: 0.72
DE  Interaction: Q8IY31; IntAct: EBI-10262646; Score: 0.56
DE  Interaction: Q8N381; IntAct: EBI-10265171; Score: 0.56
DE  Interaction: Q8N8B7; IntAct: EBI-10267719; Score: 0.56
DE  Interaction: Q8NEF3; IntAct: EBI-10270620; Score: 0.56
DE  Interaction: Q8TAU3; IntAct: EBI-10272085; Score: 0.72
DE  Interaction: Q8TD31; IntAct: EBI-10274456; Score: 0.72
DE  Interaction: Q96BZ8; IntAct: EBI-10282596; Score: 0.72
DE  Interaction: Q96NC0; IntAct: EBI-10291592; Score: 0.56
DE  Interaction: Q96SQ5; IntAct: EBI-10293466; Score: 0.72
DE  Interaction: Q9BXY8; IntAct: EBI-10301478; Score: 0.56
DE  Interaction: Q9H0A9; IntAct: EBI-10304145; Score: 0.60
DE  Interaction: Q9H0E9; IntAct: EBI-10304359; Score: 0.72
DE  Interaction: Q9H6F0; IntAct: EBI-10307479; Score: 0.56
DE  Interaction: Q9H788; IntAct: EBI-10308323; Score: 0.72
DE  Interaction: Q9HC52; IntAct: EBI-10310314; Score: 0.72
DE  Interaction: Q9P0T4; IntAct: EBI-10317754; Score: 0.72
DE  Interaction: Q9UGP5; IntAct: EBI-10320763; Score: 0.60
DE  Interaction: Q9UIE0; IntAct: EBI-10321904; Score: 0.56
DE  Interaction: Q9Y3B7; IntAct: EBI-10327384; Score: 0.72
DE  Interaction: Q8IXW7; IntAct: EBI-21249370; Score: 0.37
DE  Interaction: Q99608; IntAct: EBI-21251010; Score: 0.37
DE  Interaction: Q9H0I2; IntAct: EBI-24276119; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-24292204; Score: 0.56
DE  Interaction: Q9P1Y5; IntAct: EBI-24292226; Score: 0.56
DE  Interaction: Q9H9D4; IntAct: EBI-24302090; Score: 0.56
DE  Interaction: Q5T619; IntAct: EBI-24309981; Score: 0.56
DE  Interaction: Q96EG3; IntAct: EBI-24311294; Score: 0.56
DE  Interaction: Q96AL5; IntAct: EBI-24314166; Score: 0.56
DE  Interaction: Q8IVT4; IntAct: EBI-24315626; Score: 0.56
DE  Interaction: Q6NX45; IntAct: EBI-24321517; Score: 0.56
DE  Interaction: Q9BT49; IntAct: EBI-24325694; Score: 0.56
DE  Interaction: Q9BWG6; IntAct: EBI-24340348; Score: 0.56
DE  Interaction: Q96HB5; IntAct: EBI-24349830; Score: 0.56
DE  Interaction: Q9UK33; IntAct: EBI-24352123; Score: 0.56
DE  Interaction: P78358; IntAct: EBI-24352383; Score: 0.56
DE  Interaction: Q96EZ8; IntAct: EBI-24352759; Score: 0.56
DE  Interaction: Q8WWY3; IntAct: EBI-24355284; Score: 0.56
DE  Interaction: O76064; IntAct: EBI-24355797; Score: 0.56
DE  Interaction: Q9ULM2; IntAct: EBI-24362843; Score: 0.56
DE  Interaction: Q96HP4; IntAct: EBI-25253734; Score: 0.56
DE  Interaction: O43602; IntAct: EBI-25254540; Score: 0.56
DE  Interaction: P0CB47; IntAct: EBI-25255462; Score: 0.56
DE  Interaction: P56524; IntAct: EBI-25255284; Score: 0.56
DE  Interaction: Q3SY00; IntAct: EBI-25255985; Score: 0.56
DE  Interaction: O60645; IntAct: EBI-25258050; Score: 0.56
DE  Interaction: Q9P2K3; IntAct: EBI-24366860; Score: 0.56
DE  Interaction: P13682; IntAct: EBI-24478087; Score: 0.56
DE  Interaction: Q07002; IntAct: EBI-24478674; Score: 0.56
DE  Interaction: Q969G3; IntAct: EBI-24492471; Score: 0.56
DE  Interaction: O95295; IntAct: EBI-24500672; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-24508217; Score: 0.56
DE  Interaction: O14964; IntAct: EBI-24370108; Score: 0.56
DE  Interaction: Q8TAB5; IntAct: EBI-24382819; Score: 0.56
DE  Interaction: O43482; IntAct: EBI-24385225; Score: 0.56
DE  Interaction: Q14119; IntAct: EBI-24388342; Score: 0.56
DE  Interaction: Q2TBA0; IntAct: EBI-24398616; Score: 0.56
DE  Interaction: Q99633; IntAct: EBI-24401399; Score: 0.56
DE  Interaction: Q5W5X9; IntAct: EBI-25260730; Score: 0.56
DE  Interaction: Q9ULD5; IntAct: EBI-24422254; Score: 0.56
DE  Interaction: Q6ZNE5; IntAct: EBI-24423012; Score: 0.56
DE  Interaction: Q9Y2P0; IntAct: EBI-24424287; Score: 0.56
DE  Interaction: O60941; IntAct: EBI-24426448; Score: 0.56
DE  Interaction: O95363; IntAct: EBI-24427910; Score: 0.56
DE  Interaction: Q96PV4; IntAct: EBI-24432894; Score: 0.56
DE  Interaction: Q9BQ89; IntAct: EBI-24438032; Score: 0.56
DE  Interaction: P36508; IntAct: EBI-24445889; Score: 0.56
DE  Interaction: P53365; IntAct: EBI-24447892; Score: 0.56
DE  Interaction: Q8IYE0; IntAct: EBI-24463350; Score: 0.56
DE  Interaction: Q9UJV3; IntAct: EBI-24468925; Score: 0.56
DE  Interaction: Q9Y247; IntAct: EBI-24470709; Score: 0.56
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: Q9Y394; IntAct: EBI-20903160; Score: 0.40
DE  Interaction: P40426; IntAct: EBI-22133174; Score: 0.37
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEESGEELGLDRSTPKDFHFYHMDLYDSEDRLHLFPEENTRMRKVVQAEMANESRGAGDGKAQRDLQEEVDELVHLYGL
SQ  EDDHELGDEFVDENIPRTGVSEYPPYMMKRRDPAREQRDWRLSGEAAEAEDLGFGGWGSAGQCQDLREAYRYTHGRASEE
SQ  YECYVIPEEEDEEEAADVFCVTCKTPIRAFQKVFDEHKEHEVIPLNEALESAKDEIHKNMYKLEKQIIEMENFANHLEEV
SQ  FITVEENFGKQEQNFESHYNEILETLAQKYEEKIQALGEKKKEKLEALYGQLVSCGENLDTCKELMETIEEMCHEEKVDF
SQ  IKDAVAMADRLGKFLKTKTDVEISAQPEFEDQTLDFSDVEQLMGSINTIPAPSAPVINPQVPNSATGSSVRVCWSLYSDD
SQ  TVESYQLSYRPVQDSSPGTDQAEFTVTVKETYCSVTNLVPNTQYEFWVTAHNRAGPSPSSERAVYMTAPSPPIIKTKEIR
SQ  SCEEAVLICWESGNLNPVDSYTVELTQAESPEASGVTESVVGIPTCESVVQLQPGRSYIIYVRALNMGGPSVRSEPATVH
SQ  TIGSYFRLNKDTCHPWLTISEDGLTAVRSERRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAF
SQ  ADVRKQEDLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHE
SQ  FVHPCFSLEKPGCLKVHNGISMPKHVTFY
//
ID  Q8BZ52;
PN  Fibronectin type III and SPRY domain-containing protein 2;
GN  Fsd2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:H0UZ81}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:H0UZ81}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:H0UZ81}. Note=In skeletal muscles and striated muscles flanks Z-disks. Partially colocalizes with RYR2 in the sarcoplasmic reticulum. {ECO:0000250|UniProtKB:H0UZ81}.
DR  UNIPROT: Q8BZ52;
DR  UNIPROT: A0A140T8J1;
DR  UNIPROT: E9QMV0;
DR  Pfam: PF00041;
DR  Pfam: PF13765;
DR  Pfam: PF00622;
DR  PROSITE: PS50188;
DR  PROSITE: PS50853;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016529;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEEAEEESGLGRSAAPKDFHFYHMDLYDSEDRLQLFPGDSSRIRREVTQAEDDRELGDEFVDEHRLGTLGYPSYGMRRR
SQ  DPGREPRDWGEAAEAEDLGYGGGQGPLDQCQDLREAYRYTHGRASEEYECYVIPEEEDEEEPADVFCITCKTPVRTVEKD
SQ  FDTHKEHEVTPISKALEHAKDEVHKNMCKLEQQIIEMENFASHLEEVFITVEENFGRQEQNFECHYNGILETLAQKYEEK
SQ  IQALGEKKREKLEALYGQLVSCGENLDACRELMETVEEMCHEEKVEFLKDAVAMTDRLGKFLKTKTDVELSAQPEFEDQT
SQ  LDFSDVEQLMDAINTIPAPSAPVINPQAPNSATGSSVRVCWSLYSDDTVESYQLSYRPVQDSSSGKDRAEFTMMVKETYC
SQ  SVTNLEPNTQYEFWVIAQNRTGPSPCSEHAVYMTAPSPPSIKTEAIRSCEEAVLICWESGNLNPVDSYTVELIQAETPEA
SQ  SGVTESVVGIPTCESLIQLQPRHSYTIYVRALNVGGTSARSEPATVHTTGSYFQLNKDTCHPWLTISEDGFTVVRSEKKS
SQ  FRKELPPSKTQFTRCVAVMGNLIPVRGRHYWEVEVAEHLDYTVGVACEDVPKQEDLGANSLSWCMRHTFVSKRHRYEFLH
SQ  NKMTPDIRITVAPRKIGVLLDYENAKLSFFNVDIAQHLYTFSCQLHQFVHPCFSLEKSGCLKICNGISMPKHVTFF
//
ID  P25028;
PN  Mitosis initiation protein fs(1)Ya;
GN  fs;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope. Nucleus, nucleoplasm. Cytoplasm. Note=In the nuclear envelope during interphase to metaphase. And in the nucleoplasm and cytoplasm during anaphase and telophase.
DR  UNIPROT: P25028;
DR  UNIPROT: Q8T057;
DR  UNIPROT: Q9W4W0;
DR  UNIPROT: Q9W4W1;
DR  PROSITE: PS00028;
DE  Function: Cell cycle-dependent nuclear envelope component required for embryonic mitosis.
DE  Reference Proteome: Yes;
DE  Interaction: P08928; IntAct: EBI-872894; Score: 0.27
DE  Interaction: P19889; IntAct: EBI-8296323; Score: 0.40
DE  Interaction: P02283; IntAct: EBI-872898; Score: 0.27
DE  Interaction: O61307; IntAct: EBI-9946542; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0005654;
GO  GO:0051301;
GO  GO:0006325;
GO  GO:0030261;
GO  GO:0006260;
GO  GO:0000278;
GO  GO:0006997;
GO  GO:0007344;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFSNVLIMRQPDEGKCHICKRVFCCGKCRQKHQFKAHAIAVREPLGLRSAGGGIIEHRHQMESGATTIYVFCPICERRP
SQ  LLLREEMHGELLAHIETCHLPLRCRKCQRNYTRVDDLREFSKCVDQQQSCTDVTGATETSKATLKKAANSTAISTQTSPS
SQ  VTPISLINMRWKAKSRVTHEEFISDSVSSIRNLSSFSNSSIRRSIGQLGVNPSETMEKGKVIRSTSTPLHVESVFAKPKE
SQ  PITFNASTGGHVSSIYHEEPSPTPESNPVQQQQQQQQPLQQRAWKMGARNKMSAATPLRQVMSKSIQKAFVEHGGMMVHQ
SQ  PPSAVVQRRVRLDLSEHSSHEAAGSSALDLRLSPAMRRTQSESSASEVNSGSSSSYSTSRNADLCKRQFLLSAQKLTTES
SQ  IIITRTNSSSQKTSSTVYNSCESVEIIRSTSESAEVCHVPAITPIRVTGAGINKKQIKFETPPKSSQQMRSNGEGDETKD
SQ  QFFTPEPGTPEIPERRHRQAIVPRQLSGEFSPKKDKPKEKGLAVMALISPPLQQPRVRPPLRECRQQRVYSGVQDVGEPE
SQ  VVDAEEEDEVFRPTNASTCNDKKLEAPNSGRLWSLMSSMMRLPASLRGEREKDRDRDRDSDKENAGSGSLIRRCASIAGS
SQ  LVRPSARDSSMEDQQCLKRKRTQTLDSQYCSPLSPSSSSKRYRIRPREPIERMRRQ
//
ID  P0C044;
PN  F protein;
GN  F;
OS  11104;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C044;
DR  Pfam: PF01543;
DE  Function: 
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0019028;
GO  GO:0005198;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTNPKPQKKKTNVTPTVAHRTSSSRVAVRSLVEFTCCRAGALDWVCARRERLPSGRNLEVDVSLSPRLVGPRAGPGLSP
SQ  GTLGPSMAMRAAGGRDGSCLPVALGLAGAPQTPGVGRAIWVRSSIPLRAASPTSWGTYRSSAPLLEALPGPWRMASGFWK
SQ  TA
//
ID  P0C045;
PN  F protein;
GN  F;
OS  63746;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm {ECO:0000269|PubMed:12810869}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12810869}.
DR  UNIPROT: P0C045;
DR  Pfam: PF01543;
DE  Function: Contributes to the DDX58/RIG-I-mediated inhibition of type I interferon production. {ECO:0000269|PubMed:27404108}.
DE  Reference Proteome: Yes;
DE  Interaction: Q63HM2; IntAct: EBI-10685725; Score: 0.51
DE  Interaction: P05156; IntAct: EBI-9352054; Score: 0.37
DE  Interaction: O60844; IntAct: EBI-9352018; Score: 0.37
DE  Interaction: P05155; IntAct: EBI-9352014; Score: 0.37
DE  Interaction: P04004; IntAct: EBI-9352010; Score: 0.37
DE  Interaction: P07858; IntAct: EBI-9352006; Score: 0.37
DE  Interaction: P01019; IntAct: EBI-9351994; Score: 0.37
DE  Interaction: P61106; IntAct: EBI-9351990; Score: 0.37
DE  Interaction: P25311; IntAct: EBI-9351982; Score: 0.37
DE  Interaction: O75352; IntAct: EBI-9351986; Score: 0.37
DE  Interaction: P15907; IntAct: EBI-9351998; Score: 0.37
DE  Interaction: P51522; IntAct: EBI-9352002; Score: 0.37
DE  Interaction: Q9UHV9; IntAct: EBI-10685314; Score: 0.54
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0019028;
GO  GO:0001848;
GO  GO:0019899;
GO  GO:0097655;
GO  GO:0031267;
GO  GO:0005198;
GO  GO:0035375;
GO  GO:0051494;
GO  GO:0039540;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTNPKPQRKKPNVTPTVAHRTSSSRVAVRSLVEFTCCRAGALDWVCARRGRLPSGRNLEVDVSLSPRHVGPRAGPGLSP
SQ  GTLGPSMAMRVAGGRDGSCLPVALGLAGAPQTPGVGRAIWVRSSIPLRAASPTSWGTYRSSAPLLEALPGPWRMASGFWK
SQ  TA
//
ID  P04406;
PN  Glyceraldehyde-3-phosphate dehydrogenase;
GN  GAPDH;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:12829261}. Nucleus {ECO:0000250|UniProtKB:P04797}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12829261}. Membrane {ECO:0000269|PubMed:12829261}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (By similarity). Postnuclear and Perinuclear regions (PubMed:12829261). {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:12829261}.
DR  UNIPROT: P04406;
DR  UNIPROT: E7EUT4;
DR  UNIPROT: P00354;
DR  UNIPROT: Q53X65;
DR  PDB: 1U8F;
DR  PDB: 1ZNQ;
DR  PDB: 3GPD;
DR  PDB: 4WNC;
DR  PDB: 4WNI;
DR  PDB: 6ADE;
DR  PDB: 6IQ6;
DR  PDB: 6M61;
DR  PDB: 6YND;
DR  PDB: 6YNE;
DR  PDB: 6YNF;
DR  PDB: 6YNH;
DR  Pfam: PF02800;
DR  Pfam: PF00044;
DR  PROSITE: PS00071;
DR  OMIM: 138400;
DR  DisGeNET: 2597;
DE  Function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:3170585, PubMed:11724794). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D- glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:3170585, PubMed:11724794). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1- dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:23332158, ECO:0000269|PubMed:27387501, ECO:0000269|PubMed:3170585}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-1188138; Score: 0.79
DE  Interaction: Q04864; IntAct: EBI-360834; Score: 0.00
DE  Interaction: Q99759; IntAct: EBI-362433; Score: 0.00
DE  Interaction: Q99558; IntAct: EBI-363130; Score: 0.00
DE  Interaction: O43353; IntAct: EBI-363706; Score: 0.00
DE  Interaction: Q9UHD2; IntAct: EBI-7476716; Score: 0.56
DE  Interaction: P20333; IntAct: EBI-364783; Score: 0.00
DE  Interaction: Q13077; IntAct: EBI-365002; Score: 0.00
DE  Interaction: P60709; IntAct: EBI-353790; Score: 0.40
DE  Interaction: Q13268; IntAct: EBI-354614; Score: 0.40
DE  Interaction: Q92993; IntAct: EBI-25857246; Score: 0.56
DE  Interaction: P15927; IntAct: EBI-707645; Score: 0.51
DE  Interaction: Q9NXU5; IntAct: EBI-728720; Score: 0.00
DE  Interaction: Q9BX70; IntAct: EBI-728775; Score: 0.00
DE  Interaction: Q16363; IntAct: EBI-729012; Score: 0.00
DE  Interaction: Q15102; IntAct: EBI-729096; Score: 0.00
DE  Interaction: Q9UN74; IntAct: EBI-729117; Score: 0.00
DE  Interaction: O00231; IntAct: EBI-729159; Score: 0.00
DE  Interaction: P50453; IntAct: EBI-729279; Score: 0.00
DE  Interaction: P04183; IntAct: EBI-7398156; Score: 0.55
DE  Interaction: O43504; IntAct: EBI-730105; Score: 0.00
DE  Interaction: Q06830; IntAct: EBI-730582; Score: 0.00
DE  Interaction: P08238; IntAct: EBI-709762; Score: 0.35
DE  Interaction: O60861; IntAct: EBI-7720940; Score: 0.40
DE  Interaction: O60739; IntAct: EBI-1072279; Score: 0.00
DE  Interaction: O00141; IntAct: EBI-1075257; Score: 0.00
DE  Interaction: Q9H0J4; IntAct: EBI-1078469; Score: 0.00
DE  Interaction: P10599; IntAct: EBI-25857222; Score: 0.68
DE  Interaction: P63104; IntAct: EBI-7194241; Score: 0.40
DE  Interaction: Q27957; IntAct: EBI-7025783; Score: 0.27
DE  Interaction: P01023; IntAct: EBI-7183126; Score: 0.35
DE  Interaction: Q14653; IntAct: EBI-7476716; Score: 0.35
DE  Interaction: P32121; IntAct: EBI-1642567; Score: 0.35
DE  Interaction: P42771; IntAct: EBI-1641665; Score: 0.35
DE  Interaction: P48637; IntAct: EBI-7830840; Score: 0.40
DE  Interaction: P28482; IntAct: EBI-2115126; Score: 0.00
DE  Interaction: O15264; IntAct: EBI-2255044; Score: 0.35
DE  Interaction: Q07820; IntAct: EBI-7173317; Score: 0.35
DE  Interaction: P00558; IntAct: EBI-7907378; Score: 0.54
DE  Interaction: P04406; IntAct: EBI-7907471; Score: 0.59
DE  Interaction: Q3KSU8; IntAct: EBI-2622922; Score: 0.37
DE  Interaction: P03372; IntAct: EBI-2877710; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-8302829; Score: 0.57
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-3045543; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-3050465; Score: 0.35
DE  Interaction: P49768; IntAct: EBI-3385373; Score: 0.37
DE  Interaction: Q06187; IntAct: EBI-3505275; Score: 0.35
DE  Interaction: P43351; IntAct: EBI-3646827; Score: 0.35
DE  Interaction: Q96Q15; IntAct: EBI-3903995; Score: 0.35
DE  Interaction: Q15051; IntAct: EBI-4286917; Score: 0.35
DE  Interaction: P04083; IntAct: EBI-7095327; Score: 0.37
DE  Interaction: P20073; IntAct: EBI-7098273; Score: 0.37
DE  Interaction: P55957; IntAct: EBI-7104540; Score: 0.37
DE  Interaction: P24522; IntAct: EBI-7152962; Score: 0.37
DE  Interaction: P68032; IntAct: EBI-7157149; Score: 0.37
DE  Interaction: P00505; IntAct: EBI-7157215; Score: 0.37
DE  Interaction: Q14469; IntAct: EBI-7157494; Score: 0.37
DE  Interaction: Q15046; IntAct: EBI-7157574; Score: 0.37
DE  Interaction: Q13952; IntAct: EBI-7157626; Score: 0.37
DE  Interaction: Q99650; IntAct: EBI-7157758; Score: 0.37
DE  Interaction: Q92882; IntAct: EBI-7157808; Score: 0.37
DE  Interaction: P52756; IntAct: EBI-7157858; Score: 0.37
DE  Interaction: P62258; IntAct: EBI-7157955; Score: 0.37
DE  Interaction: P49841; IntAct: EBI-7165309; Score: 0.55
DE  Interaction: Q9Y6H6; IntAct: EBI-7183576; Score: 0.37
DE  Interaction: Q16637; IntAct: EBI-7389132; Score: 0.37
DE  Interaction: P37840; IntAct: EBI-7391160; Score: 0.37
DE  Interaction: P18084; IntAct: EBI-5659917; Score: 0.00
DE  Interaction: P15336; IntAct: EBI-5529812; Score: 0.35
DE  Interaction: P04487; IntAct: EBI-6157560; Score: 0.35
DE  Interaction: P0C1C6; IntAct: EBI-6158469; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-6158649; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q00537; IntAct: EBI-6380868; Score: 0.35
DE  Interaction: Q13164; IntAct: EBI-6380894; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-21327757; Score: 0.53
DE  Interaction: Q15843; IntAct: EBI-21328206; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q9WMX2; IntAct: EBI-9078245; Score: 0.37
DE  Interaction: P42858; IntAct: EBI-9053301; Score: 0.67
DE  Interaction: P48147; IntAct: EBI-9550467; Score: 0.64
DE  Interaction: Q15303; IntAct: EBI-9687710; Score: 0.37
DE  Interaction: P04626; IntAct: EBI-9687897; Score: 0.55
DE  Interaction: Q60823; IntAct: EBI-9702520; Score: 0.42
DE  Interaction: Q13043; IntAct: EBI-10049589; Score: 0.35
DE  Interaction: P51451; IntAct: EBI-10102766; Score: 0.35
DE  Interaction: P05109; IntAct: EBI-10098112; Score: 0.65
DE  Interaction: P35228; IntAct: EBI-10091932; Score: 0.50
DE  Interaction: P06702; IntAct: EBI-10091932; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-10091892; Score: 0.35
DE  Interaction: P62805; IntAct: EBI-10091892; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-11322719; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q13098; IntAct: EBI-10766278; Score: 0.35
DE  Interaction: O35071; IntAct: EBI-10996866; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: Q8N2N9; IntAct: EBI-11053871; Score: 0.35
DE  Interaction: Q96G25; IntAct: EBI-11053871; Score: 0.35
DE  Interaction: Q8NG31; IntAct: EBI-11053871; Score: 0.35
DE  Interaction: P48039; IntAct: EBI-11575898; Score: 0.37
DE  Interaction: P54274; IntAct: EBI-11310274; Score: 0.37
DE  Interaction: Q9BSI4; IntAct: EBI-11310284; Score: 0.51
DE  Interaction: Q96AP0; IntAct: EBI-11310294; Score: 0.37
DE  Interaction: Q9NUX5; IntAct: EBI-11310304; Score: 0.37
DE  Interaction: Q9UBX2; IntAct: EBI-11614356; Score: 0.35
DE  Interaction: P06929; IntAct: EBI-26506766; Score: 0.37
DE  Interaction: P06427; IntAct: EBI-26507442; Score: 0.37
DE  Interaction: P24835; IntAct: EBI-26507526; Score: 0.37
DE  Interaction: P56945; IntAct: EBI-15099384; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q16082; IntAct: EBI-15487660; Score: 0.37
DE  Interaction: Q9BZE9; IntAct: EBI-21690090; Score: 0.35
DE  Interaction: O14556; IntAct: EBI-21690090; Score: 0.35
DE  Interaction: Q15915; IntAct: EBI-21696712; Score: 0.35
DE  Interaction: Q92696; IntAct: EBI-21736347; Score: 0.35
DE  Interaction: Q920M9; IntAct: EBI-15571980; Score: 0.44
DE  Interaction: Q7MWG4; IntAct: EBI-15591000; Score: 0.40
DE  Interaction: P16749; IntAct: EBI-15833083; Score: 0.41
DE  Interaction: P04075; IntAct: EBI-16426431; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20303881; Score: 0.50
DE  Interaction: P25705; IntAct: EBI-21929063; Score: 0.35
DE  Interaction: Q96HJ9; IntAct: EBI-21929593; Score: 0.35
DE  Interaction: Q9Y2Z9; IntAct: EBI-21930056; Score: 0.35
DE  Interaction: O00483; IntAct: EBI-21930681; Score: 0.35
DE  Interaction: O75489; IntAct: EBI-21931040; Score: 0.35
DE  Interaction: Q96FC7; IntAct: EBI-21931532; Score: 0.35
DE  Interaction: Q9H6K4; IntAct: EBI-21931410; Score: 0.35
DE  Interaction: Q3MIX3; IntAct: EBI-21935154; Score: 0.35
DE  Interaction: P0C7P0; IntAct: EBI-21935930; Score: 0.35
DE  Interaction: Q99807; IntAct: EBI-21936186; Score: 0.35
DE  Interaction: Q8TB22; IntAct: EBI-21937705; Score: 0.35
DE  Interaction: Q9NQH7; IntAct: EBI-21937834; Score: 0.35
DE  Interaction: Q9C002; IntAct: EBI-21938261; Score: 0.35
DE  Interaction: Q9HAC7; IntAct: EBI-21938493; Score: 0.35
DE  Interaction: O00746; IntAct: EBI-21940120; Score: 0.35
DE  Interaction: Q8N3Z0; IntAct: EBI-21940471; Score: 0.35
DE  Interaction: Q86U44; IntAct: EBI-20594935; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: Q8TDU9; IntAct: EBI-20807086; Score: 0.37
DE  Interaction: P02730; IntAct: EBI-20795573; Score: 0.40
DE  Interaction: P04920; IntAct: EBI-20795563; Score: 0.40
DE  Interaction: P10636; IntAct: EBI-20799352; Score: 0.35
DE  Interaction: Q8NFJ5; IntAct: EBI-20902056; Score: 0.40
DE  Interaction: Q6A163; IntAct: EBI-20904168; Score: 0.40
DE  Interaction: O76041; IntAct: EBI-20904328; Score: 0.40
DE  Interaction: Q03936; IntAct: EBI-20906200; Score: 0.40
DE  Interaction: P04908; IntAct: EBI-20906576; Score: 0.40
DE  Interaction: Q5TZA2; IntAct: EBI-20909272; Score: 0.40
DE  Interaction: P57740; IntAct: EBI-20910640; Score: 0.40
DE  Interaction: Q99442; IntAct: EBI-20911552; Score: 0.40
DE  Interaction: O75602; IntAct: EBI-20914552; Score: 0.40
DE  Interaction: O95425; IntAct: EBI-20916064; Score: 0.40
DE  Interaction: Q5VST9; IntAct: EBI-20920604; Score: 0.40
DE  Interaction: Q502W7; IntAct: EBI-20925058; Score: 0.40
DE  Interaction: P48751; IntAct: EBI-20926210; Score: 0.40
DE  Interaction: Q00535; IntAct: EBI-20926978; Score: 0.40
DE  Interaction: A1A4G5; IntAct: EBI-20927136; Score: 0.40
DE  Interaction: Q69YH5; IntAct: EBI-20928976; Score: 0.40
DE  Interaction: Q13283; IntAct: EBI-20929856; Score: 0.40
DE  Interaction: Q63HK5; IntAct: EBI-20929960; Score: 0.40
DE  Interaction: Q5T6S3; IntAct: EBI-20931832; Score: 0.40
DE  Interaction: Q6P1J9; IntAct: EBI-20932880; Score: 0.40
DE  Interaction: O95139; IntAct: EBI-20934708; Score: 0.40
DE  Interaction: O15015; IntAct: EBI-20935244; Score: 0.40
DE  Interaction: A8MT65; IntAct: EBI-20937020; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: O96013; IntAct: EBI-26962273; Score: 0.35
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.46
DE  Interaction: P52292; IntAct: EBI-20993846; Score: 0.35
DE  Interaction: Q9H9Z2; IntAct: EBI-20993846; Score: 0.35
DE  Interaction: P13693; IntAct: EBI-20992046; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: O60260; IntAct: EBI-21135687; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: Q16526; IntAct: EBI-21981854; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-21993601; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568044; Score: 0.35
DE  Interaction: Q9BY14; IntAct: EBI-25504841; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25510118; Score: 0.35
DE  Interaction: P0DTD3; IntAct: EBI-25510342; Score: 0.35
DE  Interaction: P17612; IntAct: EBI-25857214; Score: 0.56
DE  Interaction: Q9UIJ7; IntAct: EBI-25857278; Score: 0.56
DE  Interaction: Q8WUY3; IntAct: EBI-25857270; Score: 0.56
DE  Interaction: Q9UHX1; IntAct: EBI-25857262; Score: 0.56
DE  Interaction: O00471; IntAct: EBI-25857254; Score: 0.56
DE  Interaction: Q9BPW9; IntAct: EBI-25857238; Score: 0.56
DE  Interaction: O75344; IntAct: EBI-25857230; Score: 0.56
DE  Interaction: P06241; IntAct: EBI-25857206; Score: 0.56
DE  Interaction: P35222; IntAct: EBI-25857198; Score: 0.56
DE  Interaction: Q14194; IntAct: EBI-25857190; Score: 0.56
DE  Interaction: Q9UQM7; IntAct: EBI-25857182; Score: 0.56
DE  Interaction: Q6UY14; IntAct: EBI-25857286; Score: 0.56
DE  Interaction: Q96GZ6; IntAct: EBI-25857296; Score: 0.56
DE  Interaction: Q8NEA9; IntAct: EBI-25857304; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25936448; Score: 0.56
DE  Interaction: Q7Z417; IntAct: EBI-26513452; Score: 0.37
DE  Interaction: Q9BYB0; IntAct: EBI-26514195; Score: 0.37
DE  Interaction: P51531; IntAct: EBI-26515253; Score: 0.37
DE  Interaction: P49815; IntAct: EBI-26516083; Score: 0.37
DE  Interaction: P52298; IntAct: EBI-26397282; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-26399030; Score: 0.35
DE  Interaction: Q8TB24; IntAct: EBI-26518569; Score: 0.35
DE  Interaction: Q5U458; IntAct: EBI-26450034; Score: 0.35
DE  Interaction: P14240; IntAct: EBI-26968430; Score: 0.35
DE  Interaction: P60880; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: Q99608; IntAct: EBI-26955247; Score: 0.27
DE  Interaction: P06401; IntAct: EBI-26871590; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: P42695; IntAct: EBI-28951349; Score: 0.50
DE  Interaction: P0DTC9; IntAct: EBI-28955760; Score: 0.35
DE  Interaction: Q13619; IntAct: EBI-30863570; Score: 0.35
DE  Interaction: Q8WV16; IntAct: EBI-30863977; Score: 0.35
DE  Interaction: Q05DH4; IntAct: EBI-34574576; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0097452;
GO  GO:0043231;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:1990904;
GO  GO:0031982;
GO  GO:0019828;
GO  GO:0097718;
GO  GO:0004365;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0051287;
GO  GO:0050661;
GO  GO:0035605;
GO  GO:0061844;
GO  GO:0071346;
GO  GO:0050832;
GO  GO:0006006;
GO  GO:0006096;
GO  GO:0051873;
GO  GO:0031640;
GO  GO:0000226;
GO  GO:0010951;
GO  GO:0017148;
GO  GO:0051402;
GO  GO:0035606;
GO  GO:0001819;
GO  GO:0043123;
GO  GO:0032481;
GO  GO:0050821;
GO  GO:0016241;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQER
SQ  DPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPL
SQ  AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV
SQ  SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY
SQ  SNRVVDLMAHMASKE
//
ID  Q9C5H9;
PN  Gamma-tubulin complex component 2;
GN  GCP2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q9BSJ2}. Nucleus envelope. Cytoplasm. Cytoplasm, cell cortex. Note=Associated to motile complexes in the cytosol that transiently stabilized at fixed locations in the cell cortex (e.g. along the outer periclinal edge of newly formed crosswalls) from which microtubules grow away prior to microtubules nucleation. Colocalizes with gamma-tubulin at the nuclear surface where microtubules are nucleated.
DR  UNIPROT: Q9C5H9;
DR  UNIPROT: F4KGZ8;
DR  UNIPROT: Q9LF43;
DR  Pfam: PF04130;
DR  Pfam: PF17681;
DE  Function: Gamma-tubulin complex is necessary for microtubule nucleation at the microtubule organizing centers (MTOCs). Required for the positioning of the gamma-tubulin-containing complex on pre-existing microtubules and for the proper organization of cortical arrays. {ECO:0000269|PubMed:19509058, ECO:0000269|PubMed:20935636}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9LT56; IntAct: EBI-4521088; Score: 0.37
GO  GO:0005938;
GO  GO:0055028;
GO  GO:0005737;
GO  GO:0000923;
GO  GO:0000930;
GO  GO:0008275;
GO  GO:0005635;
GO  GO:0000922;
GO  GO:0043015;
GO  GO:0031122;
GO  GO:0048229;
GO  GO:0033566;
GO  GO:0051321;
GO  GO:0007020;
GO  GO:0000278;
GO  GO:0090063;
GO  GO:0051225;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESMTPISCPTTPRWNQDRPFLTGRFHQETRASSKFADSKRFTLDSSSSGVEQAIGCYDTPVQELIVIDDLLSALVGIEG
SQ  RYISIKRFHGKEDSIAFQVDPSMDLALQELAKRIFPLCEYYLLIDQFVESSSQFKNGLVNHAFAAALRALLLDYQAMVAQ
SQ  LEHQFRLGRLSIQGLWFYCQPMMGSMRALAAVIQQASTKQFVGSGVLNLLQSQAKAMAGDNSVRSLLEKMTECASNAYLS
SQ  ILERWVYEGIIDDPYGEFFIAENRSLKKESLSQDSTAKYWSQRYSLKDTIPGFLANIAATILTTGKYLNVMRECGHNVQV
SQ  PISERSKLTIFGSNHHYLECIKAAHEFASIELVNLIKDKYDLVGRLRSIKHYLLLDQGDFLVHFMDIAREELNKKVHEIS
SQ  VEKLQSLLDLALRTTAAAADPRHEDLTCCVDRASLLTTLGMHKDTDSNSIEDPMSITGLETFSLSYKVQWPLSIVISKKA
SQ  LSKYQLIFRFLFHCKHVERQLCGAWQIHQGIRSMNSKGTAILRSSLLCRSMLKFISSLLHYLTFEVLEPNWHVMHDRLQS
SQ  TRSVDEVIQHHDFFLDKCLRGCLLLLPDVLKKMEKLKSVCLQYAAATQWLISSSIDINSQSHPQKTMIRDTTVTESIFNF
SQ  EREFNSELQSLGPVLSKGSQAEPYLTHLSQWILGVSKE
//
ID  Q9FG37;
PN  Gamma-tubulin complex component 3;
GN  GCP3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q9BSJ2}. Nucleus envelope. Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton, spindle. Note=Associated to motile complexes in the cytosol that transiently stabilized at fixed locations in the cell cortex (e.g. along the outer periclinal edge of newly formed crosswalls) from which microtubules grow away prior to microtubules nucleation. Colocalizes with gamma- tubulin at the nuclear surface where microtubules are nucleated. Localizes to both cortical cytoplasm and mitotic microtubule arrays of the nematode feeding giant cells.
DR  UNIPROT: Q9FG37;
DR  Pfam: PF04130;
DR  Pfam: PF17681;
DE  Function: Gamma-tubulin complex is necessary for microtubule nucleation at the microtubule organizing centers (MTOCs). Required for the positioning of the gamma-tubulin-containing complex on pre-existing microtubules and for the proper organization of cortical arrays. Gamma-tubulin complex is essential for the control of microtubular network remodeling in the course of initiation and development of giant-feeding cells, and for the successful reproduction of nematodes (e.g. Meloidogyne spp.) in their plant hosts.
DE  Reference Proteome: Yes;
DE  Interaction: Q39069; IntAct: EBI-2651346; Score: 0.00
GO  GO:0005938;
GO  GO:0055028;
GO  GO:0005737;
GO  GO:0009898;
GO  GO:0000923;
GO  GO:0000930;
GO  GO:0008275;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0043015;
GO  GO:0015631;
GO  GO:0031122;
GO  GO:0051321;
GO  GO:0007020;
GO  GO:0000278;
GO  GO:0090063;
GO  GO:0009624;
GO  GO:0051225;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDDDQQKAADLVQELVLRLVSQNPQTPNLDPNSPAFLKTLRYAFRILSSRLTPSVLPDATAIAESLKRRLATQGKSSDA
SQ  LAFADLYTKFASKTGPGSVNNKWALVYLLKIVSDDRKSAINGLDSSVLLPNLGIGDTGNGVLSRGEAKKKDWSNGVLLVS
SQ  KDPENLRDIAFREYAILVKEENEVTEEVLVRDVLYASQGIDGKYVKFNSEIDGYAVQESVKVPRATRIMVRMLSELGWLF
SQ  RKVKTFITESMDRFPAEDVGTVGQAFCAALQDELSDYYKLLAVLEAQAMNPIPLVSESASSNNYLSLRRLSVWFAEPMVK
SQ  MRLMAVLVDKCKVLRGGAMAGAIHLHAQHGDPLVHDFMMSLLRCVCSPLFEMVRSWVLEGELEDTFGEFFVVGQPVKVDL
SQ  LWREGYKLHPAMLPSFISPSLAQRILRTGKSINFLRVCCDDHGWADAASEAAAASGTTTRRGGLGYGETDALEHLVTEAA
SQ  KRIDKHLLDVLYKRYKFKEHCLAIKRYLLLGQGDFVQYLMDIVGPKLSEPANNISSFELAGFLEAAIRASNAQYDDRDML
SQ  DRLRVKMMPHGSGDRGWDVFSLEYEARVPLDTVFTESVLSKYLRVFNFLWKLKRVEHALIGIWKTMKPNCITSNSFVKLQ
SQ  SSVKLQLLSALRRCQVLWNEMNHFVTNFQYYIMFEVLEVSWSNFSKEMEAAKDLDDLLAAHEKYLNAIVGKSLLGEQSQT
SQ  IRESLFVLFELILRFRSHADRLYEGIHELQIRSKESGREKNKSQEPGSWISEGRKGLTQRAGEFLQSMSQDMDSIAKEYT
SQ  SSLDGFLSLLPLQQSVDLKFLFFRLDFTEFYSRLHSKG
//
ID  O56860;
PN  p3;
GN  gag;
OS  53182;
SL  Nucleus Position: SL-0382;
SL  Comments: [Gag protein]: Virion {ECO:0000250}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=Nuclear at initial phase, cytoplasmic at assembly. Shortly after infection, Gag protein is targeted to centrosomes. It is then actively transported into the nucleus thanks to its nuclear localization signal (By similarity). In the late phases of infection, Gag proteins assemble in the cytoplasm to form the virion's capsids. {ECO:0000250}. [p3]: Virion. Host cytoplasm, host perinuclear region. Note=Gag proteins assemble in the cytoplasm to form the capsids. {ECO:0000250}.
DR  UNIPROT: O56860;
DR  Pfam: PF03276;
DE  Function: Involved in capsid formation and genome binding. Shortly after infection, interaction between incoming particle-associated Gag proteins and host dynein allows centrosomal targeting of the viral genome (associated to Gag), prior to nucleus translocation and integration into host genome (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044163;
GO  GO:0019013;
GO  GO:0003677;
GO  GO:0003723;
GO  GO:0075521;
GO  GO:0046718;
GO  GO:0019076;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MARELNPLQLQQLYINNGLQPNPGHGDIIAVRFTGGPWGPGDRWARVTIRLQDNTGQPLQVPGYDLEPGIINLREDILIA
SQ  GPYNLIRTAFLDLEPARGPERHGPFGDGRLQPGDGLSEGFQPITDEEIQAEVGTIGAARNEIRLLREALQRLQAGGVGRP
SQ  IPGAVLQPQPVIGPVIPINHLRSVIGNTPPNPRDVALWLGRSTAAIEGVFPIVDQVTRMRVVNALVASHPGLTLTENEAG
SQ  SWNAAISALWRKAHGAAAQHELAGVLSDINKKEGIQTAFNLGMQFTDGNWSLVWGIIRTLLPGQALVTNAQSQFDLMGDD
SQ  IQRAENFPRVINNLYTMLGLNIHGQSIRPRVQTQPLQTRPRNPGRSQQGQLNQPRPQNRANQSYRPPRQQQQHSDVPEQR
SQ  DQRGPSQPPRGSGGGYNFRRNPQQPQRYGQGPPGPNPYRRFGDGGNPQQQGPPPNRGPDQGPRPGGNPRGGGRGQGPRNG
SQ  GGSAAAVHTVKASENETKNGSAEAVDGGKKGGKD
//
ID  O14976;
PN  Cyclin-G-associated kinase;
GN  GAK;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10625686}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:10625686}. Cell junction, focal adhesion {ECO:0000305|PubMed:10625686}. Note=Localizes to the perinuclear area and to the trans-Golgi network. Also seen on the plasma membrane, probably at focal adhesions.
DR  UNIPROT: O14976;
DR  UNIPROT: Q5U4P5;
DR  UNIPROT: Q9BVY6;
DR  PDB: 4C57;
DR  PDB: 4C58;
DR  PDB: 4C59;
DR  PDB: 4O38;
DR  PDB: 4Y8D;
DR  PDB: 5Y7Z;
DR  PDB: 5Y80;
DR  Pfam: PF00069;
DR  Pfam: PF10409;
DR  PROSITE: PS51182;
DR  PROSITE: PS50076;
DR  PROSITE: PS51181;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 602052;
DR  DisGeNET: 2580;
DE  Function: Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1. {ECO:0000269|PubMed:10625686}.
DE  Reference Proteome: Yes;
DE  Interaction: O14966; IntAct: EBI-9247728; Score: 0.35
DE  Interaction: O15169; IntAct: EBI-731365; Score: 0.00
DE  Interaction: O60763; IntAct: EBI-759358; Score: 0.37
DE  Interaction: P10275; IntAct: EBI-1632203; Score: 0.37
DE  Interaction: Q9Q2G4; IntAct: EBI-6174875; Score: 0.35
DE  Interaction: Q9NQ11; IntAct: EBI-6377262; Score: 0.51
DE  Interaction: Q5S007; IntAct: EBI-9247177; Score: 0.79
DE  Interaction: P11142; IntAct: EBI-9655962; Score: 0.69
DE  Interaction: Q9UL15; IntAct: EBI-9655962; Score: 0.35
DE  Interaction: Q38SD2; IntAct: EBI-9659083; Score: 0.44
DE  Interaction: Q76MZ3; IntAct: EBI-10991736; Score: 0.35
DE  Interaction: A2AUM9; IntAct: EBI-10994361; Score: 0.35
DE  Interaction: P63005; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: P10126; IntAct: EBI-11048962; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079358; Score: 0.35
DE  Interaction: P09497; IntAct: EBI-11081190; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: Q13492; IntAct: EBI-11082344; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: O15027; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9Z1Z0; IntAct: EBI-11112182; Score: 0.35
DE  Interaction: P15735; IntAct: EBI-11135895; Score: 0.35
DE  Interaction: P51805; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q07912; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q96CW1; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q9H2Y7; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q5TB80; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q8TEH3; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q8N684; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q9Y496; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q14789; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q2M2I8; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q8N556; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: O43175; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: O75146; IntAct: EBI-11150908; Score: 0.53
DE  Interaction: P47756; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P27482; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P53992; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q14677; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P49757; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q9ULH0; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P42566; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q13813; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q96PK6; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: E9PK67; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q96FJ0; IntAct: EBI-11150908; Score: 0.53
DE  Interaction: Q8IVT2; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P53675; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P09496; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P08047; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q9H0K6; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q8WXE9; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q27J81; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P14384; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P28066; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q3B7T1; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q6ZRV2; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q9UBH6; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: O00159; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q5T0W9; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: O00443; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: H0YEF7; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q9NSY1; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: F5GWT4; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q9UM54; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P62158; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q9UK73; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: O94973; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q13470; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q8TDG2; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: O00291; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: O95782; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: Q9BY43; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P98082; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P29703; IntAct: EBI-11525188; Score: 0.56
DE  Interaction: P56945; IntAct: EBI-15099463; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q8TBP5; IntAct: EBI-21502646; Score: 0.35
DE  Interaction: Q9P296; IntAct: EBI-21519943; Score: 0.35
DE  Interaction: Q8N3R9; IntAct: EBI-21627185; Score: 0.35
DE  Interaction: Q9UJ41; IntAct: EBI-21644136; Score: 0.35
DE  Interaction: O95630; IntAct: EBI-21667922; Score: 0.35
DE  Interaction: Q9NZL4; IntAct: EBI-21711136; Score: 0.35
DE  Interaction: Q09019; IntAct: EBI-21714883; Score: 0.35
DE  Interaction: Q9ULV8; IntAct: EBI-21715242; Score: 0.35
DE  Interaction: Q8N2M8; IntAct: EBI-21714908; Score: 0.35
DE  Interaction: Q96SL4; IntAct: EBI-21714987; Score: 0.35
DE  Interaction: Q9NSE4; IntAct: EBI-21715157; Score: 0.35
DE  Interaction: Q01968; IntAct: EBI-16412116; Score: 0.35
DE  Interaction: Q9Y6W8; IntAct: EBI-16721689; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q9Y4C4; IntAct: EBI-20590176; Score: 0.44
DE  Interaction: Q9Y586; IntAct: EBI-21261050; Score: 0.35
DE  Interaction: P49023; IntAct: EBI-25376663; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-28935882; Score: 0.35
DE  Interaction: Q9BYP7; IntAct: EBI-28946054; Score: 0.35
DE  Interaction: P31947; IntAct: EBI-30814567; Score: 0.44
DE  Interaction: P04637; IntAct: EBI-34581131; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0098793;
GO  GO:0031982;
GO  GO:0005524;
GO  GO:0051087;
GO  GO:0030276;
GO  GO:0030332;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0007049;
GO  GO:0051085;
GO  GO:0072318;
GO  GO:1905224;
GO  GO:0072583;
GO  GO:0007029;
GO  GO:0007030;
GO  GO:0090160;
GO  GO:0010977;
GO  GO:0034067;
GO  GO:0072659;
GO  GO:0006468;
GO  GO:0006898;
GO  GO:0016191;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLLQSALDFLAGPGSLGGASGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDVGSGREYALKRLLSNEEEKNR
SQ  AIIQEVCFMKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQ
SQ  HMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEITRNTTPMYRTPEIIDLYSNFPI
SQ  GEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAAR
SQ  NVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSV
SQ  ANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAP
SQ  HLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYMC
SQ  DMVAEEPITPHSKPILVRAVVMTPVPLFSKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDV
SQ  LIVIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSREAP
SQ  PWENSSMRGLNPKILFSSREEQQDILSKFGKPELPRQPGSTAQYDAGAGSPEAEPTDSDSPPSSSADASRFLHTLDWQEE
SQ  KEAETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQEDG
SQ  VDLLGLHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADP
SQ  FGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAW
SQ  TETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPDPFADLGDLSSGLQGSPAGFPPGGFIPKTATTPKGSSSWQ
SQ  TSRPPAQGASWPPQAKPPPKACTQPRPNYASNFSVIGAREERGVRAPSFAQKPKVSENDFEDLLSNQGFSSRSDKKGPKT
SQ  IAEMRKQDLAKDTDPLKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVGMADLVAPEQVKKHYRRAVLAVHPDKAA
SQ  GQPYEQHAKMIFMELNDAWSEFENQGSRPLF
//
ID  Q99KY4;
PN  Cyclin-G-associated kinase;
GN  Gak;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Localizes to the perinuclear area and to the trans-Golgi network. Also seen on the plasma membrane, probably at focal adhesions (By similarity). {ECO:0000250}.
DR  UNIPROT: Q99KY4;
DR  UNIPROT: Q6P1I8;
DR  UNIPROT: Q6P9S5;
DR  UNIPROT: Q8BM74;
DR  UNIPROT: Q8K0Q4;
DR  Pfam: PF00226;
DR  Pfam: PF00069;
DR  Pfam: PF10409;
DR  PROSITE: PS51182;
DR  PROSITE: PS50076;
DR  PROSITE: PS51181;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P97378; IntAct: EBI-7652953; Score: 0.51
DE  Interaction: Q8CI32; IntAct: EBI-9248889; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0031982;
GO  GO:0005524;
GO  GO:0030276;
GO  GO:0030332;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0007049;
GO  GO:0072318;
GO  GO:1905224;
GO  GO:0072583;
GO  GO:0007029;
GO  GO:0009913;
GO  GO:0002064;
GO  GO:0061436;
GO  GO:0048853;
GO  GO:0007030;
GO  GO:0090160;
GO  GO:0035622;
GO  GO:0030216;
GO  GO:0010977;
GO  GO:0061351;
GO  GO:0060563;
GO  GO:2000179;
GO  GO:2000648;
GO  GO:0034067;
GO  GO:0072659;
GO  GO:0006468;
GO  GO:0006898;
GO  GO:0048863;
GO  GO:0072089;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLLQSALDFLAGPGSLGGAAGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDLGSGREYALKRLLSNEEEKNR
SQ  AIIQEVCFLKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLKRVECKGPLSCDSILKIFYQTCRAVQ
SQ  HMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPI
SQ  GEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRAMLKVNPVERLSIAEVVRQLQEIAAAR
SQ  NVNPKAPITELLEQNGGYGNSGPSRAQPPCGGTVNSSGVLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVAN
SQ  YAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRMFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRAPHL
SQ  HSLYTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYVCDM
SQ  VAEEPITPHSKPMLVKSVVMTPVPLFSKQRNGCRPFCEVYVGEERVTTTSQEYDRMKEFKIEDGKAVIPLGVTVQGDVLI
SQ  IIYHARATLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSREAPPW
SQ  ENTSLRGLNPKILFSNREEQQDILSKFGKPELPRQPGSTAQYDAEAGSPEAEITESDSPQSSSTDTNHFLHTLDWQEEKE
SQ  PETGLDNTSPKESQSVLIADGDGSEVSDEEEASFPSEERKPGAGEDTPRLAAGTKQQDLIFDVGMLAAPQEPVQPEEGVD
SQ  LLGLHSEGDLRPAAPLQACGVPSSNTDLLSCLLEPSDAAQVGPPGDLLGGEAPLLLASPVSPLGLQNNLQGKVPDTVDPF
SQ  DQFLLSSNSDTQPCSKPDLFGEFLNSDSVASSTAFPSTHSAPPPSCSTAFLHLGDLPAEPSKVIASSSHPDLLGGWDTWA
SQ  DTATPGPASIPVPEGTLFSSAGHPAPPGPNPSQTKSQNLDPFADLSDLSSSLQGLPAGLPAGGFVGAPAPTQKSNSPWQA
SQ  NRPTAPGTSWTPQAKPAPRASEQLRSHFSVIGAREERGVRVPSFAQKPKVSENDFEDLLPNQGFSKSDKKGPKTMAEMRK
SQ  QELARDTDPLKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVSMADLVTPEQVKKQYRRAVLVVHPDKATGQPYEQ
SQ  YAKMIFMELNDAWSEFENQGSRPLF
//
ID  P97874;
PN  Cyclin-G-associated kinase;
GN  Gak;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Localizes to the perinuclear area and to the trans-Golgi network. Also seen on the plasma membrane, probably at focal adhesions (By similarity). {ECO:0000250}.
DR  UNIPROT: P97874;
DR  Pfam: PF00226;
DR  Pfam: PF00069;
DR  Pfam: PF10409;
DR  PROSITE: PS51182;
DR  PROSITE: PS50076;
DR  PROSITE: PS51181;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P39052; IntAct: EBI-6947872; Score: 0.38
DE  Interaction: Q5XIE8; IntAct: EBI-26440627; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0031982;
GO  GO:0005524;
GO  GO:0030276;
GO  GO:0030332;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0007049;
GO  GO:0048468;
GO  GO:0072318;
GO  GO:1905224;
GO  GO:0072583;
GO  GO:0007029;
GO  GO:0009913;
GO  GO:0002064;
GO  GO:0061436;
GO  GO:0048853;
GO  GO:0007030;
GO  GO:0090160;
GO  GO:0035622;
GO  GO:0030216;
GO  GO:0010977;
GO  GO:0061351;
GO  GO:0060563;
GO  GO:2000179;
GO  GO:2000648;
GO  GO:0034067;
GO  GO:0072659;
GO  GO:0006468;
GO  GO:0006898;
GO  GO:0048863;
GO  GO:0072089;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLLQSALDFLAGPGSLGGAAGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDLGSGREYALKRLLSNEEEKNR
SQ  AIIQEVCFLKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLRRVECKGPLSCDSILKIFYQTCRAVQ
SQ  HMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPI
SQ  GEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRGMLKVNPEERLSIAEVVRQLQEIAAAR
SQ  NVNPKAPITELLEQNGGYGNSGPSRAQPPSGGPVNSSGVLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVAN
SQ  YAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRAPHL
SQ  HSLYTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYVCDM
SQ  VAEEPITPHSKPMLVKSVVMTPVPLFSKQRNGCRPFCEVYVGEERVTTTSQEYDRMKEFKIEDGKAVIPLGITVQGDVLT
SQ  IIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSRDVPPW
SQ  ENTSLRGLNPKILFSNREEQQDILSKFGKPELPRQPGSTAQYDAEAGSPEAEITESDSPQSSSTDTNHFLHTLDWQEEKD
SQ  PETGVDNTSPKESQSNLIADGDGSEVSDEEEASCPSEERKPGAGEDTPRLAAGTRQQDLIFDVGMLAAPQEPVQPEEGVD
SQ  LLGLHSEGDLRPAAPLQASGVQSSNTDLLSSLLEPSDASQVGPPGDLLGGETPLLLASPVSLLGVQSNLQGKVPDTVDPF
SQ  DQFLLPSSSDTQPCSKPDLFGEFLNSDSVASSTAFPSTHSAPPPSCSTAFLHLGDLPAEPNKVIASSSHPDLLGGWDTWA
SQ  ETALPGPASMPVPEGTLFSSAGHPAPPGPNPSQTKSQNPDPFADLSDLSSSLQGLPAGLPAGSFVGTSATTHKSNSSWQT
SQ  TRPTAPGTSWPPQAKPAPRASEQLRSHFSVIGAREERGVRAPSFAQKPKVSENDFEDLLPNQGFSKSDKKGPKTMAEMRK
SQ  QELARDTDPFKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVSMADLVTPEQVKKQYRRAVLVVHPDKATGQPYEQ
SQ  SAKMIFMELNDAWSEFENQGSRPLF
//
ID  O60318;
PN  Germinal-center associated nuclear protein;
GN  MCM3AP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: [Isoform GANP]: Nucleus envelope {ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:21195085, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:28633435}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20005110}. Chromosome {ECO:0000269|PubMed:23652018}. Note=Predominantly located at the nuclear envelope, facing the nucleus interior (PubMed:20005110, PubMed:21195085, PubMed:23591820). Localization at the nuclear pore complex requires NUP153, TPR and ALYREF/ALY (PubMed:23591820, PubMed:22307388). Also found associated with chromatin (PubMed:23652018). In B-cells, targeted to the immunoglobulin variable region genes (PubMed:23652018). {ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:21195085, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:23652018}. [Isoform MCM3AP]: Cytoplasm {ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:21195085}. Nucleus {ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:21195085}. Note=Translocates into the nucleus in the presence of MCM3 (PubMed:12226073). Associates with chromatin possibly through interaction with MCM3 (PubMed:12226073). {ECO:0000269|PubMed:12226073}.
DR  UNIPROT: O60318;
DR  UNIPROT: C9JL56;
DR  UNIPROT: Q2M3C1;
DR  UNIPROT: Q6PJP6;
DR  UNIPROT: Q9BSY5;
DR  UNIPROT: Q9UMT4;
DR  PDB: 4DHX;
DR  Pfam: PF16766;
DR  Pfam: PF16769;
DR  Pfam: PF16768;
DR  Pfam: PF03399;
DR  PROSITE: PS50250;
DR  OMIM: 603294;
DR  OMIM: 618124;
DR  DisGeNET: 8888;
DE  Function: [Isoform GANP]: As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (PubMed:20005110, PubMed:20384790, PubMed:23591820, PubMed:22307388). Through the acetylation of histones, affects the assembly of nucleosomes at immunoglobulin variable region genes and promotes the recruitment and positioning of transcription complex to favor DNA cytosine deaminase AICDA/AID targeting, hence promoting somatic hypermutations (PubMed:23652018). {ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:20384790, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:23652018}. [Isoform MCM3AP]: Binds to and acetylates the replication protein MCM3. Plays a role in the initiation of DNA replication and participates in controls that ensure that DNA replication initiates only once per cell cycle (PubMed:11258703, PubMed:12226073). Through the acetylation of histones, affects the assembly of nucleosomes at immunoglobulin variable region genes and promotes the recruitment and positioning of transcription complex to favor DNA cytosine deaminase AICDA/AID targeting, hence promoting somatic hypermutations (PubMed:23652018). {ECO:0000269|PubMed:11258703, ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:23652018}.
DE  Disease: Peripheral neuropathy, autosomal recessive, with or without impaired intellectual development (PNRIID) [MIM:618124]: An autosomal recessive disorder characterized by early childhood-onset of peripheral sensorimotor neuropathy, progressive distal muscle weakness, atrophy in hands and feet, and gait difficulties, often with loss of ambulation. Most affected individuals also have impaired intellectual development, although some have normal cognition. Additional features may include eye movement abnormalities, claw hands, foot deformities, and scoliosis. {ECO:0000269|PubMed:24123876, ECO:0000269|PubMed:28633435, ECO:0000269|PubMed:28969388, ECO:0000269|PubMed:29982295}. Note=The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O94985; IntAct: EBI-311611; Score: 0.37
DE  Interaction: Q9NYQ7; IntAct: EBI-308834; Score: 0.37
DE  Interaction: P84022; IntAct: EBI-7232431; Score: 0.37
DE  Interaction: O15198; IntAct: EBI-7261838; Score: 0.37
DE  Interaction: Q9NPA8; IntAct: EBI-734236; Score: 0.00
DE  Interaction: Q9P0N5; IntAct: EBI-735082; Score: 0.00
DE  Interaction: Q9UKK9; IntAct: EBI-735262; Score: 0.00
DE  Interaction: Q14194; IntAct: EBI-737126; Score: 0.00
DE  Interaction: Q5NGE6; IntAct: EBI-2796304; Score: 0.00
DE  Interaction: Q5NIJ3; IntAct: EBI-2804997; Score: 0.00
DE  Interaction: A0A0F7REH3; IntAct: EBI-2816349; Score: 0.00
DE  Interaction: Q81KK8; IntAct: EBI-2829932; Score: 0.00
DE  Interaction: A0A2U2GVV1; IntAct: EBI-2846769; Score: 0.00
DE  Interaction: Q7CIS2; IntAct: EBI-2864681; Score: 0.00
DE  Interaction: Q0WC40; IntAct: EBI-2864674; Score: 0.00
DE  Interaction: P25054; IntAct: EBI-3437195; Score: 0.00
DE  Interaction: P60953; IntAct: EBI-3438542; Score: 0.00
DE  Interaction: P63000; IntAct: EBI-3449487; Score: 0.00
DE  Interaction: P30304; IntAct: EBI-3906561; Score: 0.37
DE  Interaction: P62487; IntAct: EBI-3912322; Score: 0.37
DE  Interaction: Q09472; IntAct: EBI-3929206; Score: 0.37
DE  Interaction: Q6P1J9; IntAct: EBI-7116410; Score: 0.37
DE  Interaction: Q9BPY3; IntAct: EBI-7148250; Score: 0.37
DE  Interaction: Q9H5I1; IntAct: EBI-7393874; Score: 0.37
DE  Interaction: Q9H5J8; IntAct: EBI-7394492; Score: 0.37
DE  Interaction: Q15714; IntAct: EBI-7408152; Score: 0.37
DE  Interaction: Q8BUH2; IntAct: EBI-10991696; Score: 0.35
DE  Interaction: Q9CYN2; IntAct: EBI-11000176; Score: 0.35
DE  Interaction: Q9BVG8; IntAct: EBI-11004364; Score: 0.35
DE  Interaction: Q9NSK0; IntAct: EBI-11004456; Score: 0.35
DE  Interaction: P13533; IntAct: EBI-11004546; Score: 0.35
DE  Interaction: P54132; IntAct: EBI-11057507; Score: 0.35
DE  Interaction: Q9R1K9; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: C5E524; IntAct: EBI-12584088; Score: 0.35
DE  Interaction: Q194T2; IntAct: EBI-12587357; Score: 0.35
DE  Interaction: Q9H0B3; IntAct: EBI-21526575; Score: 0.35
DE  Interaction: Q12798; IntAct: EBI-21576600; Score: 0.35
DE  Interaction: Q9BTL4; IntAct: EBI-21675209; Score: 0.35
DE  Interaction: P60896; IntAct: EBI-15970583; Score: 0.35
DE  Interaction: Q5JVF3; IntAct: EBI-15970583; Score: 0.35
DE  Interaction: Q15149; IntAct: EBI-20929080; Score: 0.40
DE  Interaction: P12004; IntAct: EBI-21256683; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-21391268; Score: 0.00
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC5; IntAct: EBI-25685699; Score: 0.35
DE  Interaction: P07947; IntAct: EBI-30849071; Score: 0.44
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0003682;
GO  GO:0010484;
GO  GO:0004402;
GO  GO:0042393;
GO  GO:0003676;
GO  GO:0006406;
GO  GO:0034728;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0016446;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNPTNPFSGQQPSAFSASSSNVGTLPSKPPFRFGQPSLFGQNSTLSGKSSGFSQVSSFPASSGVSHSSSVQTLGFTQTSS
SQ  VGPFSGLEHTSTFVATSGPSSSSVLGNTGFSFKSPTSVGAFPSTSAFGQEAGEIVNSGFGKTEFSFKPLENAVFKPILGA
SQ  ESEPEKTQSQIASGFFTFSHPISSAPGGLAPFSFPQVTSSSATTSNFTFSKPVSSNNSLSAFTPALSNQNVEEEKRGPKS
SQ  IFGSSNNSFSSFPVSSAVLGEPFQASKAGVRQGCEEAVSQVEPLPSLMKGLKRKEDQDRSPRRHGHEPAEDSDPLSRGDH
SQ  PPDKRPVRLNRPRGGTLFGRTIQDVFKSNKEVGRLGNKEAKKETGFVESAESDHMAIPGGNQSVLAPSRIPGVNKEEETE
SQ  SREKKEDSLRGTPARQSNRSESTDSLGGLSPSEVTAIQCKNIPDYLNDRTILENHFGKIAKVQRIFTRRSKKLAVVHFFD
SQ  HASAALARKKGKSLHKDMAIFWHRKKISPNKKPFSLKEKKPGDGEVSPSTEDAPFQHSPLGKAAGRTGASSLLNKSSPVK
SQ  KPSLLKAHQFEGDSFDSASEGSEGLGPCVLSLSTLIGTVAETSKEKYRLLDQRDRIMRQARVKRTDLDKARTFVGTCLDM
SQ  CPEKERYMRETRSQLSVFEVVPGTDQVDHAAAVKEYSRSSADQEEPLPHELRPLPVLSRTMDYLVTQIMDQKEGSLRDWY
SQ  DFVWNRTRGIRKDITQQHLCDPLTVSLIEKCTRFHIHCAHFMCEEPMSSFDAKINNENMTKCLQSLKEMYQDLRNKGVFC
SQ  ASEAEFQGYNVLLSLNKGDILREVQQFHPAVRNSSEVKFAVQAFAALNSNNFVRFFKLVQSASYLNACLLHCYFSQIRKD
SQ  ALRALNFAYTVSTQRSTIFPLDGVVRMLLFRDCEEATDFLTCHGLTVSDGCVELNRSAFLEPEGLSKTRKSVFITRKLTV
SQ  SVGEIVNGGPLPPVPRHTPVCSFNSQNKYIGESLAAELPVSTQRPGSDTVGGGRGEECGVEPDAPLSSLPQSLPAPAPSP
SQ  VPLPPVLALTPSVAPSLFQLSVQPEPPPPEPVPMYSDEDLAQVVDELIQEALQRDCEEVGSAGAAYAAAALGVSNAAMED
SQ  LLTAATTGILRHIAAEEVSKERERREQERQRAEEERLKQERELVLSELSQGLAVELMERVMMEFVRETCSQELKNAVETD
SQ  QRVRVARCCEDVCAHLVDLFLVEEIFQTAKETLQELQCFCKYLQRWREAVTARKKLRRQMRAFPAAPCCVDVSDRLRALA
SQ  PSAECPIAEENLARGLLDLGHAGRLGISCTRLRRLRNKTAHQMKVQHFYQQLLSDVAWASLDLPSLVAEHLPGRQEHVFW
SQ  KLVLVLPDVEEQSPESCGRILANWLKVKFMGDEGSVDDTSSDAGGIQTLSLFNSLSSKGDQMISVNVCIKVAHGALSDGA
SQ  IDAVETQKDLLGASGLMLLLPPKMKSEDMAEEDVYWLSALLQLKQLLQAKPFQPALPLVVLVPSPGGDAVEKEVEDGLML
SQ  QDLVSAKLISDYTVTEIPDTINDLQGSTKVLQAVQWLVSHCPHSLDLCCQTLIQYVEDGIGHEFSGRFFHDRRERRLGGL
SQ  ASQEPGAIIELFNSVLQFLASVVSSEQLCDLSWPVTEFAEAGGSRLLPHLHWNAPEHLAWLKQAVLGFQLPQMDLPPLGA
SQ  PWLPVCSMVVQYASQIPSSRQTQPVLQSQVENLLHRTYCRWKSKSPSPVHGAGPSVMEIPWDDLIALCINHKLRDWTPPR
SQ  LPVTSEALSEDGQICVYFFKNDLKKYDVPLSWEQARLQTQKELQLREGRLAIKPFHPSANNFPIPLLHMHRNWKRSTECA
SQ  QEGRIPSTEDLMRGASAEELLAQCLSSSLLLEKEENKRFEDQLQQWLSEDSGAFTDLTSLPLYLPQTLVSLSHTIEPVMK
SQ  TSVTTSPQSDMMREQLQLSEATGTCLGERLKHLERLIRSSREEEVASELHLSALLDMVDI
//
ID  Q9WUU9;
PN  Germinal-center associated nuclear protein;
GN  Mcm3ap;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10733502, ECO:0000269|PubMed:20507984}. Nucleus {ECO:0000269|PubMed:10733502, ECO:0000269|PubMed:20507984}. Nucleus envelope {ECO:0000250|UniProtKB:O60318}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O60318}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O60318}. Chromosome {ECO:0000250|UniProtKB:O60318}. Note=In stimulated B-cells, selectively targeted to immunoglobulin gene variable regions (PubMed:20507984). Predominantly located at the nuclear envelope, facing the nucleus interior (By similarity). Localization at the nuclear pore complex requires NUP153, TPR and ALYREF/ALY (By similarity). Also found associated with chromatin (PubMed:23652018). In B-cells, targeted to the immunoglobulin variable region genes (PubMed:20507984, PubMed:23652018). {ECO:0000250|UniProtKB:O60318, ECO:0000269|PubMed:20507984, ECO:0000269|PubMed:23652018}.
DR  UNIPROT: Q9WUU9;
DR  UNIPROT: Q7TS87;
DR  Pfam: PF16766;
DR  Pfam: PF16769;
DR  Pfam: PF16768;
DR  Pfam: PF03399;
DR  PROSITE: PS50250;
DE  Function: As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (By similarity). Through the acetylation of histones, affects the assembly of nucleosomes at immunoglobulin variable region genes and promotes the recruitment and positioning of transcription complex to favor DNA cytosine deaminase AICDA/AID targeting, hence promoting somatic hypermutations (PubMed:23652018). {ECO:0000250|UniProtKB:O60318, ECO:0000269|PubMed:23652018}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Z0S9; IntAct: EBI-20974677; Score: 0.37
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0003682;
GO  GO:0010484;
GO  GO:0004402;
GO  GO:0042393;
GO  GO:0003676;
GO  GO:0006406;
GO  GO:0034728;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0016446;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MHPVNPFGGQQPSAFAVSSSTTGTYQTKSPFRFGQPSLFGQNSTPSKSLAFSQVPSFATPSGGSHSSSLPAFGLTQTSSV
SQ  GLFSSLESTPSFAATSSSSVPGNTAFSFKSTSSVGVFPSGATFGPETGEVAGSGFRKTEFKFKPLENAVFKPIPGPESEP
SQ  EKTQSQISSGFFTFSHPVGSGSGGLTPFSFPQVTNSSVTSSSFIFSKPVTSNTPAFASPLSNQNVEEEKRVSTSAFGSSN
SQ  SSFSTFPTASPGSLGEPFPANKPSLRQGCEEAISQVEPLPTLMKGLKRKEDQDRSPRRHCHEAAEDPDPLSRGDHPPDKR
SQ  PVRLNRPRGGTLFGRTIQEVFKSNKEAGRLGSKESKESGFAEPGESDHAAVPGGSQSTMVPSRLPAVTKEEEESRDEKED
SQ  SLRGKSVRQSKRREEWIYSLGGVSSLELTAIQCKNIPDYLNDRAILEKHFSKIAKVQRVFTRRSKKLAVIHFFDHASAAL
SQ  ARKKGKGLHKDVVIFWHKKKISPSKKLFPLKEKLGESEASQGIEDSPFQHSPLSKPIVRPAAGSLLSKSSPVKKPSLLKM
SQ  HQFEADPFDSGSEGSEGLGSCVSSLSTLIGTVADTSEEKYRLLDQRDRIMRQARVKRTDLDKARAFVGTCPDMCPEKERY
SQ  LRETRSQLSVFEVVPGTDQVDHAAAVKEYSRSSADQEEPLPHELRPSAVLSRTMDYLVTQIMDQKEGSLRDWYDFVWNRT
SQ  RGIRKDITQQHLCDPLTVSLIEKCTRFHIHCAHFMCEEPMSSFDAKINNENMTKCLQSLKEMYQDLRNKGVFCASEAEFQ
SQ  GYNVLLNLNKGDILREVQQFHPDVRNSPEVNFAVQAFAALNSNNFVRFFKLVQSASYLNACLLHCYFNQIRKDALRALNV
SQ  AYTVSTQRSTVFPLDGVVRMLLFRDSEEATNFLNYHGLTVADGCVELNRSAFLEPEGLCKARKSVFIGRKLTVSVGEVVN
SQ  GGPLPPVPRHTPVCSFNSQNKYVGESLATELPISTQRAGGDPAGGGRGEDCEAEVDVPTLAVLPQPPPASSATPALHVQP
SQ  LAPAAAPSLLQASTQPEVLLPKPAPVYSDSDLVQVVDELIQEALQVDCEEVSSAGAAYVAAALGVSNAAVEDLITAATTG
SQ  ILRHVAAEEVSMERQRLEEEKQRAEEERLKQERELMLTQLSEGLAAELTELTVTECVWETCSQELQSAVEIDQKVRVARC
SQ  CEAVCAHLVDLFLAEEIFQTAKETLQELQCFCKYLQRWREAVAARKKFRRQMRAFPAAPCCVDVNDRLQALVPSAECPIT
SQ  EENLAKGLLDLGHAGKVGVSCTRLRRLRNKTAHQIKVQHFHQQLLRNAAWAPLDLPSIVSEHLPMKQKRRFWKLVLVLPD
SQ  VEEQTPESPGRILENWLKVKFTGDDSMVGDIGDNAGDIQTLSVFNTLSSKGDQTVSVNVCIKVAHGTLSDSALDAVETQK
SQ  DLLGTSGLMLLLPPKVKSEEVAEEELSWLSALLQLKQLLQAKPFQPALPLVVLVPSSRGDSAGRAVEDGLMLQDLVSAKL
SQ  ISDYIVVEIPDSVNDLQGTVKVSGAVQWLISRCPQALDLCCQTLVQYVEDGISREFSRRFFHDRRERRLASLPSQEPSTI
SQ  IELFNSVLQFLASVVSSEQLCDISWPVMEFAEVGGSQLLPHLHWNSPEHLAWLKQAVLGFQLPQMDLPPPGAPWLPVCSM
SQ  VIQYTSQIPSSSQTQPVLQSQVENLLCRTYQKWKNKSLSPGQELGPSVAEIPWDDIITLCINHKLRDWTPPRLPVTLEAL
SQ  SEDGQICVYFFKNLLRKYHVPLSWEQARMQTQRELQLSHGRSGMRSIHPPTSTFPTPLLHVHQKGKKKEESGREGSLSTE
SQ  DLLRGASAEELLAQSLSSSLLEEKEENKRFEDQLQQWLSQDSQAFTESTRLPLYLPQTLVSFPDSIKTQTMVKTSTSPQN
SQ  SGTGKQLRFSEASGSSLTEKLKLLERLIQSSRAEEAASELHLSALLEMVDM
//
ID  P11017;
PN  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2;
GN  GNB2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62879}. Cell membrane {ECO:0000250|UniProtKB:P62879}.
DR  UNIPROT: P11017;
DR  UNIPROT: A5D7A9;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005834;
GO  GO:0048471;
GO  GO:0003924;
GO  GO:0051020;
GO  GO:0044877;
GO  GO:0030159;
GO  GO:0007186;
GO  GO:1901379;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLI
SQ  IWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITS
SQ  SGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYA
SQ  FTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGV
SQ  TDDGMAVATGSWDSFLKIWN
//
ID  P62879;
PN  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2;
GN  GNB2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16498633}. Cell membrane {ECO:0000269|PubMed:28219978}.
DR  UNIPROT: P62879;
DR  UNIPROT: B3KPU1;
DR  UNIPROT: P11016;
DR  UNIPROT: P54312;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 139390;
DR  OMIM: 619464;
DR  OMIM: 619503;
DR  DisGeNET: 2783;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
DE  Disease: Neurodevelopmental disorder with hypotonia and dysmorphic facies (NEDHYDF) [MIM:619503]: An autosomal dominant disorder characterized by global developmental delay, hypotonia, and variably impaired intellectual development, often with speech delay and delayed walking. Most patients have dysmorphic facial features. Clinical features are highly variable and may include congenital cardiac defects, non-specific renal anomalies, joint contractures or joint hyperextensibility, dry skin, and cryptorchidism. {ECO:0000269|PubMed:31698099, ECO:0000269|PubMed:33971351, ECO:0000269|PubMed:34183358}. Note=The disease is caused by variants affecting the gene represented in this entry. Sick sinus syndrome 4 (SSS4) [MIM:619464]: The term 'sick sinus syndrome' encompasses a variety of conditions caused by sinus node dysfunction. The most common clinical manifestations are syncope, presyncope, dizziness, and fatigue. Electrocardiogram typically shows sinus bradycardia, sinus arrest, and/or sinoatrial block. Episodes of atrial tachycardias coexisting with sinus bradycardia ('tachycardia- bradycardia syndrome') are also common in this disorder. SSS occurs most often in the elderly associated with underlying heart disease or previous cardiac surgery, but can also occur in the fetus, infant, or child without heart disease or other contributing factors. SSS4 is characterized by early and progressive sinus node and atrioventricular conduction dysfunction. Some affected individuals are asymptomatic. SSS4 inheritance is autosomal dominant. {ECO:0000269|PubMed:28219978}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P0C6X7; IntAct: EBI-25507431; Score: 0.37
DE  Interaction: P10909; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q99759; IntAct: EBI-362076; Score: 0.00
DE  Interaction: Q9Y572; IntAct: EBI-363730; Score: 0.00
DE  Interaction: P04632; IntAct: EBI-732037; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1074963; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-1079942; Score: 0.00
DE  Interaction: P49286; IntAct: EBI-1188355; Score: 0.53
DE  Interaction: Q70EL3; IntAct: EBI-2512984; Score: 0.40
DE  Interaction: P83917; IntAct: EBI-2556579; Score: 0.40
DE  Interaction: P11440; IntAct: EBI-2556914; Score: 0.40
DE  Interaction: Q8BFT2; IntAct: EBI-2558223; Score: 0.40
DE  Interaction: Q9D2X5; IntAct: EBI-2561173; Score: 0.40
DE  Interaction: Q80X56; IntAct: EBI-2561540; Score: 0.40
DE  Interaction: Q8BHX1; IntAct: EBI-2562723; Score: 0.40
DE  Interaction: Q0VEJ0; IntAct: EBI-2563897; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-2878124; Score: 0.35
DE  Interaction: P48729; IntAct: EBI-3907887; Score: 0.37
DE  Interaction: P11177; IntAct: EBI-3909631; Score: 0.37
DE  Interaction: P20073; IntAct: EBI-7098405; Score: 0.37
DE  Interaction: P38936; IntAct: EBI-7123717; Score: 0.37
DE  Interaction: Q9BPY3; IntAct: EBI-7147527; Score: 0.37
DE  Interaction: P24522; IntAct: EBI-7153265; Score: 0.37
DE  Interaction: Q14451; IntAct: EBI-7160608; Score: 0.37
DE  Interaction: P49841; IntAct: EBI-7165519; Score: 0.55
DE  Interaction: P18754; IntAct: EBI-7349763; Score: 0.37
DE  Interaction: P42229; IntAct: EBI-7392908; Score: 0.37
DE  Interaction: Q15714; IntAct: EBI-7407723; Score: 0.37
DE  Interaction: P15336; IntAct: EBI-5529812; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-6156949; Score: 0.35
DE  Interaction: Q9WMX2; IntAct: EBI-9079674; Score: 0.37
DE  Interaction: P42858; IntAct: EBI-9071699; Score: 0.67
DE  Interaction: P05549; IntAct: EBI-9679115; Score: 0.37
DE  Interaction: P35579; IntAct: EBI-11004631; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-11009211; Score: 0.35
DE  Interaction: P80315; IntAct: EBI-11016531; Score: 0.35
DE  Interaction: P80314; IntAct: EBI-11019324; Score: 0.35
DE  Interaction: P80318; IntAct: EBI-11029579; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: P21333; IntAct: EBI-11038784; Score: 0.35
DE  Interaction: Q61879; IntAct: EBI-11041929; Score: 0.35
DE  Interaction: P51149; IntAct: EBI-11050319; Score: 0.35
DE  Interaction: Q9JHJ0; IntAct: EBI-11063313; Score: 0.35
DE  Interaction: P58771; IntAct: EBI-11063826; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: Q8CCJ3; IntAct: EBI-11104920; Score: 0.35
DE  Interaction: Q9Z1Z0; IntAct: EBI-11110688; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: P60033; IntAct: EBI-20568535; Score: 0.60
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q05322; IntAct: EBI-15481401; Score: 0.35
DE  Interaction: P48960; IntAct: EBI-21506471; Score: 0.35
DE  Interaction: P18075; IntAct: EBI-21530438; Score: 0.35
DE  Interaction: P28335; IntAct: EBI-21534882; Score: 0.35
DE  Interaction: Q01415; IntAct: EBI-21540352; Score: 0.35
DE  Interaction: P26842; IntAct: EBI-21555258; Score: 0.35
DE  Interaction: O14530; IntAct: EBI-21558244; Score: 0.35
DE  Interaction: Q2Y0W8; IntAct: EBI-21566582; Score: 0.35
DE  Interaction: Q9NRX5; IntAct: EBI-21567084; Score: 0.35
DE  Interaction: Q16288; IntAct: EBI-21583226; Score: 0.35
DE  Interaction: Q9H813; IntAct: EBI-21593240; Score: 0.35
DE  Interaction: Q9Y262; IntAct: EBI-21610950; Score: 0.35
DE  Interaction: Q9Y345; IntAct: EBI-21615000; Score: 0.35
DE  Interaction: Q2MV58; IntAct: EBI-21625612; Score: 0.35
DE  Interaction: Q5VTA0; IntAct: EBI-21649184; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-21684279; Score: 0.35
DE  Interaction: Q9NRE1; IntAct: EBI-21684885; Score: 0.35
DE  Interaction: Q9GZM7; IntAct: EBI-21699118; Score: 0.35
DE  Interaction: O15496; IntAct: EBI-21699277; Score: 0.35
DE  Interaction: P14091; IntAct: EBI-21699601; Score: 0.35
DE  Interaction: Q6UWB1; IntAct: EBI-21703330; Score: 0.35
DE  Interaction: Q9NVU0; IntAct: EBI-21705041; Score: 0.35
DE  Interaction: P08754; IntAct: EBI-21709056; Score: 0.35
DE  Interaction: Q9UKJ8; IntAct: EBI-21717781; Score: 0.35
DE  Interaction: Q13371; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: Q9NQP4; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: Q99471; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: Q92526; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: Q13148; IntAct: EBI-21726063; Score: 0.67
DE  Interaction: P78371; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: P63218; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: P63092; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: P61758; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: P17987; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: P04083; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: O60925; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: O15212; IntAct: EBI-21726063; Score: 0.35
DE  Interaction: Q9NWX5; IntAct: EBI-21736726; Score: 0.35
DE  Interaction: P48544; IntAct: EBI-21754197; Score: 0.35
DE  Interaction: O95154; IntAct: EBI-21755189; Score: 0.35
DE  Interaction: P08833; IntAct: EBI-21768638; Score: 0.35
DE  Interaction: Q86WS5; IntAct: EBI-21771386; Score: 0.35
DE  Interaction: P30519; IntAct: EBI-21779750; Score: 0.35
DE  Interaction: Q9NTU7; IntAct: EBI-21783449; Score: 0.35
DE  Interaction: Q8WVH0; IntAct: EBI-21802744; Score: 0.35
DE  Interaction: Q6ZMY9; IntAct: EBI-21818150; Score: 0.35
DE  Interaction: Q8N1E6; IntAct: EBI-21820146; Score: 0.35
DE  Interaction: Q8WTQ1; IntAct: EBI-21825173; Score: 0.35
DE  Interaction: Q96GD3; IntAct: EBI-21834539; Score: 0.35
DE  Interaction: Q9UNU6; IntAct: EBI-21839336; Score: 0.35
DE  Interaction: Q99808; IntAct: EBI-21849345; Score: 0.35
DE  Interaction: O43827; IntAct: EBI-21853419; Score: 0.35
DE  Interaction: Q9BZP6; IntAct: EBI-21862020; Score: 0.35
DE  Interaction: P32455; IntAct: EBI-21864916; Score: 0.35
DE  Interaction: O60383; IntAct: EBI-21866276; Score: 0.35
DE  Interaction: Q8N8M0; IntAct: EBI-21867232; Score: 0.35
DE  Interaction: P28799; IntAct: EBI-21877218; Score: 0.35
DE  Interaction: P04278; IntAct: EBI-21877199; Score: 0.35
DE  Interaction: Q96CM8; IntAct: EBI-21877340; Score: 0.40
DE  Interaction: Q3SY56; IntAct: EBI-21877291; Score: 0.35
DE  Interaction: Q99518; IntAct: EBI-21877353; Score: 0.40
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: P23258; IntAct: EBI-16800113; Score: 0.27
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9H0J9; IntAct: EBI-21263845; Score: 0.35
DE  Interaction: O43924; IntAct: EBI-21019227; Score: 0.35
DE  Interaction: Q8N6Q3; IntAct: EBI-21402192; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.53
DE  Interaction: Q13115; IntAct: EBI-25372724; Score: 0.35
DE  Interaction: Q15139; IntAct: EBI-25395029; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: O76071; IntAct: EBI-25477658; Score: 0.35
DE  Interaction: Q9BY14; IntAct: EBI-25504841; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
DE  Interaction: Q5VVX9; IntAct: EBI-25859638; Score: 0.56
DE  Interaction: Q969M7; IntAct: EBI-25859630; Score: 0.56
DE  Interaction: Q8N2K1; IntAct: EBI-25859622; Score: 0.56
DE  Interaction: Q8WVN8; IntAct: EBI-25859614; Score: 0.56
DE  Interaction: Q9H0Y0; IntAct: EBI-25859606; Score: 0.56
DE  Interaction: Q9NT62; IntAct: EBI-25859598; Score: 0.56
DE  Interaction: Q9C0C9; IntAct: EBI-25859588; Score: 0.56
DE  Interaction: Q7Z7E8; IntAct: EBI-25859570; Score: 0.56
DE  Interaction: Q9Y2X8; IntAct: EBI-25859562; Score: 0.56
DE  Interaction: Q9NPD8; IntAct: EBI-25859554; Score: 0.56
DE  Interaction: Q16763; IntAct: EBI-25859546; Score: 0.56
DE  Interaction: Q6NXQ4; IntAct: EBI-25859538; Score: 0.56
DE  Interaction: O00762; IntAct: EBI-25859524; Score: 0.56
DE  Interaction: O14933; IntAct: EBI-25859516; Score: 0.56
DE  Interaction: P61081; IntAct: EBI-25859508; Score: 0.56
DE  Interaction: P61077; IntAct: EBI-25859476; Score: 0.56
DE  Interaction: P62837; IntAct: EBI-25859468; Score: 0.56
DE  Interaction: P51668; IntAct: EBI-25859460; Score: 0.56
DE  Interaction: P61086; IntAct: EBI-25859442; Score: 0.56
DE  Interaction: Q7KZS0; IntAct: EBI-25859500; Score: 0.56
DE  Interaction: P62256; IntAct: EBI-25859492; Score: 0.56
DE  Interaction: P62253; IntAct: EBI-25859484; Score: 0.56
DE  Interaction: O60260; IntAct: EBI-25879531; Score: 0.56
DE  Interaction: P40337; IntAct: EBI-25895413; Score: 0.56
DE  Interaction: Q9Y3C5; IntAct: EBI-25918235; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25930439; Score: 0.56
DE  Interaction: P00441; IntAct: EBI-25934837; Score: 0.56
DE  Interaction: P37840; IntAct: EBI-25940648; Score: 0.56
DE  Interaction: Q13363; IntAct: EBI-27047305; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q05513; IntAct: EBI-28938998; Score: 0.35
DE  Interaction: Q12792; IntAct: EBI-28939213; Score: 0.35
DE  Interaction: Q13188; IntAct: EBI-28939324; Score: 0.35
DE  Interaction: Q86V86; IntAct: EBI-28942203; Score: 0.35
DE  Interaction: Q8IVW4; IntAct: EBI-28942376; Score: 0.35
DE  Interaction: Q8TEA7; IntAct: EBI-28943849; Score: 0.35
DE  Interaction: Q8TF76; IntAct: EBI-28943924; Score: 0.35
DE  Interaction: Q92772; IntAct: EBI-28944167; Score: 0.35
DE  Interaction: Q9HCP0; IntAct: EBI-28946348; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005615;
GO  GO:0005925;
GO  GO:0005834;
GO  GO:0005765;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031982;
GO  GO:0003924;
GO  GO:0051020;
GO  GO:0044877;
GO  GO:0030159;
GO  GO:0007186;
GO  GO:1901379;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLI
SQ  IWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITS
SQ  SGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYA
SQ  FTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGV
SQ  TDDGMAVATGSWDSFLKIWN
//
ID  P62880;
PN  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2;
GN  Gnb2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62879}. Cell membrane {ECO:0000250|UniProtKB:P62879}.
DR  UNIPROT: P62880;
DR  UNIPROT: P11016;
DR  UNIPROT: P54312;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
DE  Reference Proteome: Yes;
DE  Interaction: P37840; IntAct: EBI-2933536; Score: 0.35
DE  Interaction: Q92556; IntAct: EBI-8764414; Score: 0.40
DE  Interaction: P42858; IntAct: EBI-9072041; Score: 0.35
DE  Interaction: Q3U1F9; IntAct: EBI-12603102; Score: 0.35
DE  Interaction: P22682; IntAct: EBI-12600757; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16736255; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-26960892; Score: 0.35
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0005834;
GO  GO:0043209;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0005246;
GO  GO:0003924;
GO  GO:0051020;
GO  GO:0044877;
GO  GO:0030159;
GO  GO:0007186;
GO  GO:1901379;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLI
SQ  IWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITS
SQ  SGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYA
SQ  FTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGV
SQ  TDDGMAVATGSWDSFLKIWN
//
ID  P54313;
PN  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2;
GN  Gnb2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62879}. Cell membrane {ECO:0000250|UniProtKB:P62879}.
DR  UNIPROT: P54313;
DR  UNIPROT: Q71SU9;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
DE  Reference Proteome: Yes;
DE  Interaction: P80386; IntAct: EBI-16400563; Score: 0.35
DE  Interaction: Q2Q0I9; IntAct: EBI-15563359; Score: 0.40
DE  Interaction: O75886; IntAct: EBI-22259612; Score: 0.35
DE  Interaction: P98077; IntAct: EBI-22260014; Score: 0.35
DE  Interaction: Q92835; IntAct: EBI-22260917; Score: 0.35
DE  Interaction: Q7M4L6; IntAct: EBI-22260664; Score: 0.35
DE  Interaction: Q13239; IntAct: EBI-22261339; Score: 0.35
DE  Interaction: O15357; IntAct: EBI-22261281; Score: 0.35
DE  Interaction: Q9UGK3; IntAct: EBI-22262317; Score: 0.35
DE  Interaction: P43403; IntAct: EBI-22266118; Score: 0.35
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0005834;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0005246;
GO  GO:0051020;
GO  GO:0044877;
GO  GO:0030159;
GO  GO:0007186;
GO  GO:1901379;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLI
SQ  IWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITS
SQ  SGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYA
SQ  FTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGV
SQ  TDDGMAVATGSWDSFLKIWN
//
ID  P79147;
PN  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3;
GN  GNB3;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: P79147;
DR  UNIPROT: Q0PY31;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGEMEQLRQEAEQLKKQIADARKACADTTLAELVSGLEVVGRVQMRTRRTLRGHLAKIYAMHWATDSKLLVSASQDGKLI
SQ  VWDTYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNMCSIYSLKSREGNVKVSRELSAHTGYLSCCRFLDDNNIVTS
SQ  SGDTTCALWDIETGQQKTVFVGHTGDCMSLAVSPDFKLFISGACDASAKLWDVREGTCRQTFTGHESDINAICFFPNGEA
SQ  ICTGSDDASCRLFDLRADQELTAYSDESIICGITSVAFSLSGRLLFAGYDDFNCNIWDSMKGERVGILSGHDNRVSCLGV
SQ  TADGMAVATGSWDSFLKVWN
//
ID  Q4R7Y4;
PN  Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed;
GN  GNB2L1;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm {ECO:0000250|UniProtKB:P63244}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000250|UniProtKB:P63244}. Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite {ECO:0000250|UniProtKB:P68040}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery (By similarity). In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity). {ECO:0000250|UniProtKB:P63244, ECO:0000250|UniProtKB:P68040}.
DR  UNIPROT: Q4R7Y4;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression. Binds to and stabilizes activated protein kinase C (PKC), increasing PKC- mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome- mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration (By similarity). Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63244}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0030496;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0001891;
GO  GO:0015935;
GO  GO:0005080;
GO  GO:0030292;
GO  GO:0030971;
GO  GO:0043022;
GO  GO:0042169;
GO  GO:0006915;
GO  GO:0007049;
GO  GO:0071363;
GO  GO:0007369;
GO  GO:0030308;
GO  GO:0050765;
GO  GO:0030178;
GO  GO:0043065;
GO  GO:0030335;
GO  GO:2000543;
GO  GO:0042998;
GO  GO:0043547;
GO  GO:0032436;
GO  GO:0001934;
GO  GO:0031334;
GO  GO:0051726;
GO  GO:0051302;
GO  GO:2000114;
GO  GO:0032880;
GO  GO:0006417;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P63244};
SQ  MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALS
SQ  GSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNS
SQ  SNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALC
SQ  FSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
//
ID  P32456;
PN  Guanylate-binding protein 2;
GN  GBP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:21151871}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21151871}. Golgi apparatus membrane {ECO:0000269|PubMed:21151871}. Membrane; Lipid- anchor {ECO:0000269|PubMed:21151871}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9Z0E6}. Note=GBP2-GBP5 dimers localize to the Golgi apparatus. {ECO:0000269|PubMed:21151871}.
DR  UNIPROT: P32456;
DR  UNIPROT: Q6GPH0;
DR  UNIPROT: Q6IAU2;
DR  UNIPROT: Q86TB0;
DR  PDB: 6VKJ;
DR  PDB: 7E58;
DR  Pfam: PF02263;
DR  Pfam: PF02841;
DR  PROSITE: PS51715;
DR  OMIM: 600412;
DR  DisGeNET: 2634;
DE  Function: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, but the major reaction product is GDP (PubMed:8706832). Exhibits antiviral activity against influenza virus. Promotes oxidative killing and delivers antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity). Confers protection to the protozoan pathogen Toxoplasma gondii (By similarity). {ECO:0000250|UniProtKB:P32455, ECO:0000250|UniProtKB:Q9Z0E6, ECO:0000269|PubMed:8706832}.
DE  Reference Proteome: Yes;
DE  Interaction: O60238; IntAct: EBI-7104878; Score: 0.37
DE  Interaction: Q9Y2M5; IntAct: EBI-731149; Score: 0.00
DE  Interaction: Q9BX70; IntAct: EBI-731425; Score: 0.00
DE  Interaction: P51114; IntAct: EBI-731995; Score: 0.00
DE  Interaction: P61604; IntAct: EBI-732205; Score: 0.00
DE  Interaction: Q15102; IntAct: EBI-732725; Score: 0.00
DE  Interaction: Q12972; IntAct: EBI-732929; Score: 0.00
DE  Interaction: P21673; IntAct: EBI-733247; Score: 0.00
DE  Interaction: P50453; IntAct: EBI-733295; Score: 0.00
DE  Interaction: Q92734; IntAct: EBI-733535; Score: 0.00
DE  Interaction: Q9Y333; IntAct: EBI-735007; Score: 0.00
DE  Interaction: P49903; IntAct: EBI-735757; Score: 0.00
DE  Interaction: A0A348ACF3; IntAct: EBI-2833431; Score: 0.00
DE  Interaction: Q8ZE38; IntAct: EBI-2869144; Score: 0.00
DE  Interaction: A0A3N4B6Z3; IntAct: EBI-2869151; Score: 0.00
DE  Interaction: P20073; IntAct: EBI-7098307; Score: 0.37
DE  Interaction: P55957; IntAct: EBI-7104587; Score: 0.37
DE  Interaction: P67870; IntAct: EBI-7133432; Score: 0.37
DE  Interaction: P24522; IntAct: EBI-7153188; Score: 0.37
DE  Interaction: P49841; IntAct: EBI-7165379; Score: 0.37
DE  Interaction: Q13387; IntAct: EBI-7238167; Score: 0.37
DE  Interaction: Q15418; IntAct: EBI-7369975; Score: 0.37
DE  Interaction: Q13188; IntAct: EBI-7393045; Score: 0.37
DE  Interaction: Q9WMX2; IntAct: EBI-9081889; Score: 0.51
DE  Interaction: Q58FG0; IntAct: EBI-21835834; Score: 0.35
DE  Interaction: Q9UEY8; IntAct: EBI-21835834; Score: 0.35
DE  Interaction: Q9H0R5; IntAct: EBI-21835834; Score: 0.63
DE  Interaction: Q8N8V2; IntAct: EBI-21835834; Score: 0.35
DE  Interaction: Q58FF7; IntAct: EBI-21835834; Score: 0.35
DE  Interaction: P69905; IntAct: EBI-21835834; Score: 0.35
DE  Interaction: P57721; IntAct: EBI-21835834; Score: 0.35
DE  Interaction: P35611; IntAct: EBI-21835834; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-21835834; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-21835834; Score: 0.35
DE  Interaction: P32455; IntAct: EBI-21864916; Score: 0.63
DE  Interaction: P32456; IntAct: EBI-26453963; Score: 0.57
DE  Interaction: Q96PP8; IntAct: EBI-26454129; Score: 0.51
DE  Interaction: Q96PP9; IntAct: EBI-26472562; Score: 0.51
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0071346;
GO  GO:0071347;
GO  GO:0071356;
GO  GO:0050830;
GO  GO:0042832;
GO  GO:0006955;
GO  GO:0034504;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:21151871};
SQ  MAPEINLPGPMSLIDNTKGQLVVNPEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKKNGFSLGSTVKSHTKGIWM
SQ  WCVPHPKKPEHTLVLLDTEGLGDIEKGDNENDSWIFALAILLSSTFVYNSMGTINQQAMDQLHYVTELTDRIKANSSPGN
SQ  NSVDDSADFVSFFPAFVWTLRDFTLELEVDGEPITADDYLELSLKLRKGTDKKSKSFNDPRLCIRKFFPKRKCFVFDWPA
SQ  PKKYLAHLEQLKEEELNPDFIEQVAEFCSYILSHSNVKTLSGGIPVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQI
SQ  ENSAAVEKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFMKNSFKDVDQMFQRKLGAQLEARRDDFCKQNSKA
SQ  SSDCCMALLQDIFGPLEEDVKQGTFSKPGGYRLFTQKLQELKNKYYQVPRKGIQAKEVLKKYLESKEDVADALLQTDQSL
SQ  SEKEKAIEVERIKAESAEAAKKMLEEIQKKNEEMMEQKEKSYQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQERLLK
SQ  EGFENESKRLQKDIWDIQMRSKSLEPICNIL
//
ID  Q9Z0E6;
PN  Guanylate-binding protein 2;
GN  Gbp2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P32456}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P32456}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P32456}. Membrane {ECO:0000250|UniProtKB:P32456}; Lipid-anchor {ECO:0000250|UniProtKB:P32456}. Cytoplasmic vesicle {ECO:0000269|PubMed:18025219, ECO:0000269|PubMed:31964735}. Note=GBP2- GBP5 dimers localize to the Golgi apparatus. {ECO:0000250|UniProtKB:P32456}.
DR  UNIPROT: Q9Z0E6;
DR  UNIPROT: Q4FK03;
DR  UNIPROT: Q8CIC6;
DR  UNIPROT: Q921N2;
DR  UNIPROT: Q9R1I0;
DR  Pfam: PF02263;
DR  Pfam: PF02841;
DR  PROSITE: PS51715;
DE  Function: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, but the major reaction product is GDP (By similarity). Exhibits antiviral activity against influenza virus. Promotes oxidative killing and delivers antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity). Confers protection to the protozoan pathogen Toxoplasma gondii (PubMed:18025219). {ECO:0000250|UniProtKB:P32455, ECO:0000250|UniProtKB:P32456, ECO:0000269|PubMed:18025219}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6P542; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: Q3U1F9; IntAct: EBI-12603102; Score: 0.35
GO  GO:0015629;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0020005;
GO  GO:0012506;
GO  GO:0003779;
GO  GO:0019955;
GO  GO:0019899;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0051879;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0030507;
GO  GO:0044406;
GO  GO:0035458;
GO  GO:0071346;
GO  GO:0071222;
GO  GO:0050830;
GO  GO:0042832;
GO  GO:0009617;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:9858320};
SQ  MASEIHMSEPMCLIENTEAQLVINQEALRILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKRTGFSLGSTVQSHTKGIWM
SQ  WCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAVLLSSTFIYNSIGTINQQAMDQLHYVTELTDLIKSKSSPDQ
SQ  SGVDDSANFVGFFPTFVWTLRDFSLELEVNGKPVTSDEYLEHSLTLKKGADKKTKSFNEPRLCIRKFFPKRKCFIFDRPA
SQ  QRKQLSKLETLREEELCGEFVEQVAEFTSYILSYSSVKTLCGGIIVNGPRLKSLVQTYVGAISNGSLPCMESAVLTLAQI
SQ  ENSAAVQKAITHYEEQMNQKIQMPTETLQELLDLHRPIESEAIEVFLKNSFKDVDQKFQTELGNLLVAKRDAFIKKNMDV
SQ  SSARCSDLLEDIFGPLEEEVKLGTFSKPGGYYLFLQMRQELEKKYNQAPGKGLQAEAMLKNYFDSKADVVETLLQTDQSL
SQ  TEAAKEVEEERTKAEAAEAANRELEKKQKEFELMMQQKEKSYQEHVKKLTEKMKDEQKQLLAEQENIIAAKLREQEKFLK
SQ  EGFENESKKLIREIDTLKQNKSSGKCTIL
//
ID  Q63663;
PN  Guanylate-binding protein 1;
GN  Gbp2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P32456}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P32456}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P32456}. Membrane {ECO:0000250|UniProtKB:P32456}; Lipid-anchor {ECO:0000250|UniProtKB:P32456}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9Z0E6}. Note=GBP2-GBP5 dimers localize to the Golgi apparatus. {ECO:0000250|UniProtKB:P32456}.
DR  UNIPROT: Q63663;
DR  Pfam: PF02263;
DR  Pfam: PF02841;
DR  PROSITE: PS51715;
DE  Function: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, but the major reaction product is GDP (By similarity). Exhibits antiviral activity against influenza virus. Promotes oxidative killing and delivers antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity). Confers protection to the protozoan pathogen Toxoplasma gondii (By similarity). {ECO:0000250|UniProtKB:P32455, ECO:0000250|UniProtKB:P32456, ECO:0000250|UniProtKB:Q9Z0E6}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0044406;
GO  GO:0035458;
GO  GO:0071346;
GO  GO:0071347;
GO  GO:0071222;
GO  GO:0071356;
GO  GO:0050830;
GO  GO:0042832;
GO  GO:0034504;
GO  GO:0009617;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8148370};
SQ  MASEIHMLQPMCLIENTEAHLVINQEALRILSAINQPVVVVAIVGLYRTGKSYLMNKLAGKRTGFSLGSTVQSHTKGIWM
SQ  WCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAVLLSSTFVYNSMGTINQQAMDQLHYVTELTDLIKSKSSPDQ
SQ  SGIDDSANFVGFFPTFVWALRDFSLELEVNGKLVTPDEYLEHSLTLKKGADKKTKSFNEPRLCIRKFFPKRKCFIFDRPA
SQ  LRKQLCKLETLGEEELCSEFVEQVAEFTSYIFSYSAVKTLSGGIIVNGPRLKSLVQTYVGAISSGSLPCMESAVLTLAQI
SQ  ENSAAVQKAITHYEEQMNQKIQMPTETLQELLDLHRLIEREAIEIFLKNSFKDVDQKFQTELGNLLISKRDAFIKKNSDV
SQ  SSAHCSDLIEDIFGPLEEEVKQGTFSKPGGYFLFLQMRQELEKKYNQAPGKGLEAEAVLKKYFESKEDIVETLLKTDQSL
SQ  TEAAKEIEVERIKAETAEAANRELAEKQEKFELMMQQKEESYQEHVRQLTEKMKEEQKKLIEEQDNIIALKLREQEKFLR
SQ  EGYENESKKLLREIENMKRRQSPGKCTIL
//
ID  Q9H0R5;
PN  Guanylate-binding protein 3;
GN  GBP3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17266443}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21151871}. Golgi apparatus membrane {ECO:0000269|PubMed:21151871}. Note=Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a vesicle-like compartment, with GBP2, around the nucleus and with GBP-5, at the Golgi apparatus. {ECO:0000269|PubMed:21151871}.
DR  UNIPROT: Q9H0R5;
DR  UNIPROT: A2A317;
DR  UNIPROT: A6NF86;
DR  UNIPROT: B2RTW0;
DR  UNIPROT: F8UW81;
DR  UNIPROT: Q05D54;
DR  UNIPROT: Q5T8L8;
DR  UNIPROT: Q5T8L9;
DR  UNIPROT: Q6P3V3;
DR  UNIPROT: Q9NV33;
DR  Pfam: PF02263;
DR  Pfam: PF02841;
DR  PROSITE: PS51715;
DR  OMIM: 600413;
DR  DisGeNET: 2635;
DE  Function: Exhibits antiviral activity against influenza virus. {ECO:0000269|PubMed:22106366}.
DE  Reference Proteome: Yes;
DE  Interaction: P32456; IntAct: EBI-21835834; Score: 0.63
DE  Interaction: O95819; IntAct: EBI-8547663; Score: 0.59
DE  Interaction: Q5NF74; IntAct: EBI-2798928; Score: 0.00
DE  Interaction: P32455; IntAct: EBI-21864916; Score: 0.63
DE  Interaction: P60903; IntAct: EBI-20909232; Score: 0.40
DE  Interaction: P16403; IntAct: EBI-20912036; Score: 0.40
DE  Interaction: Q9H0R5; IntAct: EBI-26472578; Score: 0.51
DE  Interaction: Q96PP8; IntAct: EBI-26472594; Score: 0.51
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0000139;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0071346;
GO  GO:0071347;
GO  GO:0071356;
GO  GO:0051607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPEIHMTGPMCLIENTNGELVANPEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKNKGFSLGSTVKSHTKGIWM
SQ  WCVPHPKKPEHTLVLLDTEGLGDVKKGDNQNDSWIFTLAVLLSSTLVYNSMGTINQQAMDQLYYVTELTHRIRSKSSPDE
SQ  NENEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLEYSLKLTQGTSQKDKNFNLPRLCIRKFFPKKKCFVFDLPI
SQ  HRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIKVNGPRLESLVLTYINAISRGDLPCMENAVLALAQI
SQ  ENSAAVQKAIAHYDQQMGQKVQLPAETLQELLDLHRVSEREATEVYMKNSFKDVDHLFQKKLAAQLDKKRDDFCKQNQEA
SQ  SSDRCSALLQVIFSPLEEEVKAGIYSKPGGYCLFIQKLQDLEKKYYEEPRKGIQAEEILQTYLKSKESVTDAILQTDQIL
SQ  TEKEKEIEVECVKAESAQASAKMVEEMQIKYQQMMEEKEKSYQEHVKQLTEKMERERAQLLEEQEKTLTSKLQEQARVLK
SQ  ERCQGESTQLQNEIQKLQKTLKKKTKRYMSHKLKI
//
ID  Q96PP9;
PN  Guanylate-binding protein 4;
GN  GBP4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17266443}. Nucleus {ECO:0000269|PubMed:17266443}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21151871}. Golgi apparatus membrane {ECO:0000269|PubMed:21151871}. Note=Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a vesicle-like compartment, with GBP2, around the nucleus and with GBP-5, at the Golgi apparatus. {ECO:0000269|PubMed:21151871}.
DR  UNIPROT: Q96PP9;
DR  UNIPROT: B2R630;
DR  UNIPROT: Q05D63;
DR  UNIPROT: Q6NSL0;
DR  UNIPROT: Q86T99;
DR  Pfam: PF02263;
DR  Pfam: PF02841;
DR  PROSITE: PS51715;
DR  OMIM: 612466;
DR  DisGeNET: 115361;
DE  Function: Binds GTP, GDP and GMP. Hydrolyzes GTP very efficiently; GDP rather than GMP is the major reaction product. Plays a role in erythroid differentiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P32456; IntAct: EBI-26472562; Score: 0.51
DE  Interaction: Q8TCS8; IntAct: EBI-20907752; Score: 0.40
DE  Interaction: P32455; IntAct: EBI-26472554; Score: 0.51
DE  Interaction: Q96PP9; IntAct: EBI-26472586; Score: 0.51
DE  Interaction: Q96PP8; IntAct: EBI-26472602; Score: 0.51
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0071346;
GO  GO:0050830;
GO  GO:0042832;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGERTLHAAVPTPGYPESESIMMAPICLVENQEEQLTVNSKALEILDKISQPVVVVAIVGLYRTGKSYLMNRLAGKRNGF
SQ  PLGSTVQSETKGIWMWCVPHLSKPNHTLVLLDTEGLGDVEKSNPKNDSWIFALAVLLSSSFVYNSVSTINHQALEQLHYV
SQ  TELAELIRAKSCPRPDEAEDSSEFASFFPDFIWTVRDFTLELKLDGNPITEDEYLENALKLIPGKNPKIQNSNMPRECIR
SQ  HFFRKRKCFVFDRPTNDKQYLNHMDEVPEENLERHFLMQSDNFCSYIFTHAKTKTLREGIIVTGKRLGTLVVTYVDAINS
SQ  GAVPCLENAVTALAQLENPAAVQRAADHYSQQMAQQLRLPTDTLQELLDVHAACEREAIAVFMEHSFKDENHEFQKKLVD
SQ  TIEKKKGDFVLQNEEASAKYCQAELKRLSEHLTESILRGIFSVPGGHNLYLEEKKQVEWDYKLVPRKGVKANEVLQNFLQ
SQ  SQVVVEESILQSDKALTAGEKAIAAERAMKEAAEKEQELLREKQKEQQQMMEAQERSFQEYMAQMEKKLEEERENLLREH
SQ  ERLLKHKLKVQEEMLKEEFQKKSEQLNKEINQLKEKIESTKNEQLRLLKILDMASNIMIVTLPGASKLLGVGTKYLGSRI
//
ID  Q61107;
PN  Guanylate-binding protein 4;
GN  Gbp4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q96PP9}. Nucleus {ECO:0000250|UniProtKB:Q96PP9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PP9}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96PP9}. Note=Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a vesicle-like compartment, with GBP2, around the nucleus and with GBP-5, at the Golgi apparatus. {ECO:0000250|UniProtKB:Q96PP9}.
DR  UNIPROT: Q61107;
DR  UNIPROT: Q8VEC5;
DR  Pfam: PF02263;
DR  Pfam: PF02841;
DR  PROSITE: PS51715;
DE  Function: Binds GTP, GDP and GMP. Hydrolyzes GTP very efficiently; GDP rather than GMP is the major reaction product. Plays a role in erythroid differentiation. {ECO:0000269|PubMed:9659399}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0020005;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0044406;
GO  GO:0035458;
GO  GO:0071346;
GO  GO:0071356;
GO  GO:0050830;
GO  GO:0042832;
GO  GO:0051607;
GO  GO:0001818;
GO  GO:0046426;
GO  GO:0032480;
GO  GO:0034345;
GO  GO:0045070;
GO  GO:0043122;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEAPICLVENWKNQLTVNLEAIRILEQIAQPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHP
SQ  TKPTHTLVLLDTEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINQQALEQLHFVTELTQLIRAKSSPREDKVKDS
SQ  SEFVGFFPDFIWAVRDFALELKLNGRPITEDEYLENALKLIQGDNLKVQQSNMTRECIRYFFPVRKCFVFDRPTSDKRLL
SQ  LQIENVPENQLERNFQVESEKFCSYIFTNGKTKTLRGGVIVTGNRLGTLVQTYVNAINSGTVPCLENAVTTLAQRENSIA
SQ  VQKAADHYSEQMAQRMRLPTDTLQELLTVHAACEKEAIAVFMEHSFKDDEQEFQKKLVVTIEERKEEFIRQNEAASIRHC
SQ  QAELERLSESLRKSISCGAFSVPGGHSLYLEARKKIELGYQQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGER
SQ  AIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERSFRENIAKLQEKMESEKEMLLREQEKMLEHKLKVQEELLIEGFRE
SQ  KSDMLKNEISHLREEMERTRRKPSLFGQILDTIGNAFIMILPGAGKLFGVGLKFLGSLSS
//
ID  P35197;
PN  ADP-ribosylation factor GTPase-activating protein GCS1;
GN  GCS1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11839779}. Mitochondrion {ECO:0000269|PubMed:11839779}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11839779}. Golgi apparatus {ECO:0000305|PubMed:11839779}. Note=Found also in the mitochondria and in the perinuclear region.
DR  UNIPROT: P35197;
DR  UNIPROT: D6VRC9;
DR  PDB: 5FJX;
DR  Pfam: PF01412;
DR  PROSITE: PS50115;
DE  Function: GTPase-activating protein (GAP) for ARF1 and ARF2. Involved in intracellular vesicular transport. Required for transport from the trans-Golgi network. Implicated in the regulation of retrograde transport from the Golgi to the ER and in actin cytoskeletal organization. May be involved in the maintenance of mitochondrial morphology, possibly through organizing the actin cytoskeleton in Saccharomyces. {ECO:0000269|PubMed:11756474, ECO:0000269|PubMed:11839779, ECO:0000269|PubMed:9927415}.
DE  Reference Proteome: Yes;
DE  Interaction: P84077; IntAct: EBI-620364; Score: 0.37
DE  Interaction: P16140; IntAct: EBI-785523; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-785523; Score: 0.53
DE  Interaction: P53919; IntAct: EBI-858904; Score: 0.00
DE  Interaction: P10591; IntAct: EBI-3670433; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3688456; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3725254; Score: 0.35
DE  Interaction: Q12136; IntAct: EBI-16255956; Score: 0.00
DE  Interaction: P38169; IntAct: EBI-16257096; Score: 0.00
DE  Interaction: P39981; IntAct: EBI-16257116; Score: 0.00
DE  Interaction: P40073; IntAct: EBI-16257136; Score: 0.00
DE  Interaction: P53108; IntAct: EBI-16257156; Score: 0.00
DE  Interaction: P53093; IntAct: EBI-16257176; Score: 0.00
DE  Interaction: P53039; IntAct: EBI-16257196; Score: 0.00
DE  Interaction: P14359; IntAct: EBI-16257216; Score: 0.00
DE  Interaction: P12688; IntAct: EBI-16257236; Score: 0.00
DE  Interaction: P36164; IntAct: EBI-16257256; Score: 0.00
DE  Interaction: Q12016; IntAct: EBI-16257276; Score: 0.00
DE  Interaction: P33328; IntAct: EBI-16257296; Score: 0.00
DE  Interaction: P06197; IntAct: EBI-16257316; Score: 0.00
DE  Interaction: P14020; IntAct: EBI-16257336; Score: 0.00
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0005802;
GO  GO:0003779;
GO  GO:0005096;
GO  GO:0046872;
GO  GO:0030037;
GO  GO:0006888;
GO  GO:0043001;
GO  GO:0006890;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDWKVDPDTRRRLLQLQKIGANKKCMDCGAPNPQWATPKFGAFICLECAGIHRGLGVHISFVRSITMDQFKPEELLRME
SQ  KGGNEPLTEWFKSHNIDLSLPQKVKYDNPVAEDYKEKLTCLCEDRVFEEREHLDFDASKLSATSQTAASATPGVAQSREG
SQ  TPLENRRSATPANSSNGANFQKEKNEAYFAELGKKNQSRPDHLPPSQGGKYQGFGSTPAKPPQERSAGSSNTLSLENFQA
SQ  DPLGTLSRGWGLFSSAVTKSFEDVNETVIKPHVQQWQSGELSEETKRAAAQFGQKFQETSSYGFQAFSNFTKNFNGNAED
SQ  SSTAGNTTHTEYQKIDNNDKKNEQDEDKWDDF
//
ID  Q8N9F7;
PN  Lysophospholipase D GDPD1;
GN  GDPD1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:18991142}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18991142}. Endoplasmic reticulum {ECO:0000269|PubMed:27637550}. Note=Concentrated at the perinuclear region and the cell periphery (PubMed:18991142). {ECO:0000269|PubMed:18991142}.
DR  UNIPROT: Q8N9F7;
DR  UNIPROT: A8W735;
DR  UNIPROT: Q56VR1;
DR  UNIPROT: Q8N4E3;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DR  OMIM: 616317;
DE  Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines (PubMed:27637550, PubMed:25596343). Shows a preference for 1-O-alkyl- sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine (lyso-PC) (PubMed:27637550, PubMed:25596343). May be involved in bioactive N-acylethanolamine biosynthesis from both N-acyl-lysoplasmenylethanolamin (N-acyl- lysoPlsEt) and N-acyl-lysophosphatidylethanolamin (N-acyl-lysoPE) (PubMed:27637550, PubMed:25596343). In addition, hydrolyzes glycerophospho-N-acylethanolamine to N-acylethanolamine (PubMed:27637550). Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine (By similarity). {ECO:0000250|UniProtKB:Q9CRY7, ECO:0000269|PubMed:25596343, ECO:0000269|PubMed:27637550}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P62079; IntAct: EBI-21619035; Score: 0.35
DE  Interaction: P69905; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P68871; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P19823; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P19652; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P0C0L4; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P06727; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P04217; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P02790; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P02787; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P02768; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P02765; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P02763; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P02652; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P02647; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P02042; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P01876; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P01859; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P01857; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P01042; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P01024; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P01023; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P01011; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P01009; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P00751; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P00738; IntAct: EBI-21822769; Score: 0.35
DE  Interaction: P00450; IntAct: EBI-21822769; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0004622;
GO  GO:0046872;
GO  GO:0008081;
GO  GO:0046475;
GO  GO:0070291;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSTAAFYLLSTLGGYLVTSFLLLKYPTLLHQRKKQRFLSKHISHRGGAGENLENTMAAFQHAVKIGTDMLELDCHITKD
SQ  EQVVVSHDENLKRATGVNVNISDLKYCELPPYLGKLDVSFQRACQCEGKDNRIPLLKEVFEAFPNTPINIDIKVNNNVLI
SQ  KKVSELVKRYNREHLTVWGNANYEIVEKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKE
SQ  PHTMSRSQKFLIWLSDLLLMRKALFDHLTARGIQVYIWVLNEEQEYKRAFDLGATGVMTDYPTKLRDFLHNFSA
//
ID  Q9CRY7;
PN  Lysophospholipase D GDPD1;
GN  Gdpd1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F7}. Membrane {ECO:0000269|PubMed:25596343}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25596343}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8N9F7}. Note=Concentrated at the perinuclear region and the cell periphery. {ECO:0000250|UniProtKB:Q8N9F7}.
DR  UNIPROT: Q9CRY7;
DR  UNIPROT: Q9CT14;
DR  UNIPROT: Q9D4X7;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DE  Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines (PubMed:25528375, PubMed:25596343, PubMed:27637550). Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine (lyso-PC) (PubMed:25528375, PubMed:25596343, PubMed:27637550). May be involved in bioactive N-acylethanolamine biosynthesis from both N-acyl- lysoplasmenylethanolamin (N-acyl-lysoPlsEt) and N-acyl- lysophosphatidylethanolamin (N-acyl-lysoPE) (PubMed:25596343, PubMed:27637550). In addition, hydrolyzes glycerophospho-N- acylethanolamine to N-acylethanolamine (PubMed:25596343, PubMed:27637550). Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine (PubMed:25528375). {ECO:0000269|PubMed:25528375, ECO:0000269|PubMed:25596343, ECO:0000269|PubMed:27637550}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0004622;
GO  GO:0046872;
GO  GO:0008081;
GO  GO:0046475;
GO  GO:0070291;
GO  GO:0006644;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSTAAFCLLSTLGGYLVTSFLLLKYPALLHQRKKQRFLSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKD
SQ  EQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKCEGKDTRIPLLKEVFEAFPETPINIDIKVNNNVLI
SQ  KKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKE
SQ  PHTISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPTKLKDFLNNFSA
//
ID  Q0VGK4;
PN  Lysophospholipase D GDPD1;
GN  Gdpd1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F7}. Membrane {ECO:0000250|UniProtKB:Q8N9F7}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8N9F7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8N9F7}. Note=Concentrated at the perinuclear region and the cell periphery. {ECO:0000250|UniProtKB:Q8N9F7}.
DR  UNIPROT: Q0VGK4;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DE  Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines. Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine (lyso-PC). May be involved in bioactive N-acylethanolamine biosynthesis from both N-acyl-lysoplasmenylethanolamin (N-acyl-lysoPlsEt) and N- acyl-lysophosphatidylethanolamin (N-acyl-lysoPE). In addition, hydrolyzes glycerophospho-N-acylethanolamine to N-acylethanolamine. Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine. {ECO:0000250|UniProtKB:Q9CRY7}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0004622;
GO  GO:0046872;
GO  GO:0008081;
GO  GO:0046475;
GO  GO:0070291;
GO  GO:0006644;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSTAAFCLLSTLGGYLVTSFLLLKYPALLHQRKKQRFLSRHISHRGGAGENLENTMAAFQHAVTIGTDMLELDCHITKD
SQ  EQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKCEGTDTRIPLLKEVFEAFPETPINIDIKVNNNVLI
SQ  QKVSELVKQYKREHLTVWGNASSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKE
SQ  PHIISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYIWVLNEEHEYKRAFDLGATGVMTDYPTKLKEFLNNMSA
//
ID  Q7L5L3;
PN  Lysophospholipase D GDPD3;
GN  GDPD3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q99LY2}; Multi- pass membrane protein {ECO:0000250|UniProtKB:Q99LY2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99LY2}. Endoplasmic reticulum {ECO:0000269|PubMed:27637550}. Note=Partially co-localized with CANX. {ECO:0000250|UniProtKB:Q99LY2}.
DR  UNIPROT: Q7L5L3;
DR  UNIPROT: Q9H652;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DR  OMIM: 616318;
DR  DisGeNET: 79153;
DE  Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines (PubMed:27637550). Shows a preference for 1-O-alkyl-sn-glycero-3- phosphocholine (lyso-PAF), lysophosphatidylcholine (lyso-PC) and N- acylethanolamine lysophospholipids (PubMed:27637550). Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine. {ECO:0000250|UniProtKB:Q99LY2, ECO:0000269|PubMed:27637550}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: P01160; IntAct: EBI-21572983; Score: 0.35
DE  Interaction: Q5VU43; IntAct: EBI-21573806; Score: 0.35
DE  Interaction: Q15915; IntAct: EBI-21696712; Score: 0.35
DE  Interaction: Q8IW40; IntAct: EBI-21747275; Score: 0.35
DE  Interaction: O43918; IntAct: EBI-21790262; Score: 0.35
DE  Interaction: O43781; IntAct: EBI-28931148; Score: 0.35
DE  Interaction: O95382; IntAct: EBI-28931448; Score: 0.35
DE  Interaction: P54619; IntAct: EBI-28938518; Score: 0.35
DE  Interaction: Q14296; IntAct: EBI-28941126; Score: 0.35
DE  Interaction: Q8IVW4; IntAct: EBI-28942376; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0004622;
GO  GO:0046872;
GO  GO:0008081;
GO  GO:0046475;
GO  GO:0070291;
GO  GO:0034638;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLLLYYALPALGSYAMLSIFFLRRPHLLHTPRAPTFRIRLGAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDR
SQ  VVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVYFSPGHFAHGSDRRMVRLEDLFQRFPRTPMSVEIKGKNEELIR
SQ  EIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYLGLLPFIPIPEKFFFCFLPNIINRTYFP
SQ  FSCSCLNQLLAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGVITDYPTALRHYLDNHGPAARTS
//
ID  Q99LY2;
PN  Lysophospholipase D GDPD3;
GN  Gdpd3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25528375}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25528375}; Multi-pass membrane protein {ECO:0000305}. Note=Partially colocalized with CANX (PubMed:25528375). {ECO:0000269|PubMed:25528375}.
DR  UNIPROT: Q99LY2;
DR  UNIPROT: Q9D1C0;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DE  Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines (PubMed:25528375, PubMed:27637550). Shows a preference for 1-O-alkyl- sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylcholine (lyso- PC) and N-acylethanolamine lysophospholipids (PubMed:25528375). Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine (PubMed:25528375). {ECO:0000269|PubMed:25528375, ECO:0000269|PubMed:27637550}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0004622;
GO  GO:0046872;
GO  GO:0008081;
GO  GO:0046475;
GO  GO:0070291;
GO  GO:0034638;
GO  GO:0006644;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIPLLYFVLPTLGSYVMLSIFFLRRPHLLHTPRAPVFPIRLAAHRGGSGERLENTMEAVENSMAQRADLLEFDCQLTRDG
SQ  VVVVSHDKNLSRQSGLNKDVNTLDFEELPLYKEELEIYFSPGHFAHGSDRHMISLEDVFQKFPRTPMCLEVKERNEELIH
SQ  KVANLTRRFDRNEITIWAAEKSSVMKRCRAANPEMPMAFTIWRSFWILLLYYLGLLPFVSIPEKFFFCFLPTIINRTYFP
SQ  FRCGWMNQLSATITKWIIMRKSLIRHLQDRGVQVLFWCLNEESDFEVAFSLGANGVMTDYPTALRHYLDKQEEETQPPQP
SQ  EALSCLSLKK
//
ID  Q3KTM2;
PN  Glycerophosphodiester phosphodiesterase domain-containing protein 5;
GN  GDPD5;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250|UniProtKB:Q640M6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q640M6}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q640M6}.
DR  UNIPROT: Q3KTM2;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DE  Function: Glycerophosphodiester phosphodiesterase that promotes cell cycle exit and drives spinal motor neuron differentiation (PubMed:16195461, PubMed:19766572, PubMed:23329048). Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane (PubMed:23329048). May contribute to the osmotic regulation of cellular glycerophosphocholine (By similarity). {ECO:0000250|UniProtKB:Q640M6, ECO:0000269|PubMed:16195461, ECO:0000269|PubMed:19766572, ECO:0000269|PubMed:23329048}.
DE  Reference Proteome: Yes;
DE  Interaction: P0CB50; IntAct: EBI-2464235; Score: 0.59
DE  Interaction: Q06830; IntAct: EBI-2464259; Score: 0.40
DE  Interaction: P35700; IntAct: EBI-2464725; Score: 0.40
GO  GO:0012505;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0047389;
GO  GO:0008889;
GO  GO:0004435;
GO  GO:0006629;
GO  GO:0007399;
GO  GO:0045666;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVKHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTKWERLWFLILTSSFFLTLVWFYFWWEVHNDYNEINWFLYNRM
SQ  GYWSDWSIPILVTTAAGFTYITVLLILALCHIAVGQQMNLHWLHKIGLMTTLITTVVTMSSIAQLWDDEWEMVFISLQAT
SQ  APFLHIGALAAVTALSWLIAGQFARMEKATSQMLMVTAYLAVVVALYLVPLTISSPCIMEKKALGPKPAIIGHRGAPMLA
SQ  PENTLMSFQKAVEQKIYGVQADVILSYDGVPFLMHDKTLRRTTNVEEVFPGRAYEHSSMFNWTDLEMLNAGEWFLRNDPF
SQ  WTAGSLSRSDYLEAANQSVCKLADMLEVIKDNTSLILNFQDLPPDHPYYTSYINITLKTILASGIQQQAVMWLPDTERQL
SQ  VRQIAPAFQQTSGLKLDAERLREKGIVKLNLRYTKVTNEDVRDYMAANLSVNLYTVNEPWLYSILWCTGVPSVTSDSSHV
SQ  LRKVPFPIWLMPPDEYRLIWITSDLISFIIIVGVFIFQNYHNDQWRLGSIRTYNPEQIMLSAAVRRSSRDVKIMKEKLIF
SQ  SEINNGVETTDELSLCSENGYANEMVTPTDHRDTRLRMN
//
ID  Q8WTR4;
PN  Glycerophosphodiester phosphodiesterase domain-containing protein 5;
GN  GDPD5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250|UniProtKB:Q640M6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q640M6}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q640M6}. Note=In a punctate perinuclear pattern. {ECO:0000250|UniProtKB:Q640M6}.
DR  UNIPROT: Q8WTR4;
DR  UNIPROT: Q49AQ5;
DR  UNIPROT: Q6UX76;
DR  UNIPROT: Q7Z4S0;
DR  UNIPROT: Q8N781;
DR  UNIPROT: Q8NCB7;
DR  UNIPROT: Q8TB77;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DR  OMIM: 609632;
DR  DisGeNET: 81544;
DE  Function: Glycerophosphodiester phosphodiesterase that promotes neurite formation and drives spinal motor neuron differentiation (By similarity). Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane (By similarity). May contribute to the osmotic regulation of cellular glycerophosphocholine (By similarity). {ECO:0000250|UniProtKB:Q3KTM2, ECO:0000250|UniProtKB:Q640M6}.
DE  Reference Proteome: Yes;
DE  Interaction: O75844; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q14677; IntAct: EBI-16430940; Score: 0.56
DE  Interaction: Q8NC56; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q81WF2; IntAct: EBI-2833213; Score: 0.00
DE  Interaction: P50542; IntAct: EBI-10276098; Score: 0.56
DE  Interaction: Q8IUQ4; IntAct: EBI-10276108; Score: 0.56
DE  Interaction: Q70JA7; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9Y6N7; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9Y6I9; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9Y397; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9UNK0; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9UI09; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9UEU0; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9NV66; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9NUE0; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9NQ84; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9BX95; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9BWL3; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9BTX1; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9BRX8; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q9BRB3; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q969P0; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q969E2; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q92838; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q8WUY1; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q8N4L2; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q6UW68; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q6NUM9; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q5VT66; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q14654; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: P62341; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: P43304; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: O75380; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: O43306; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: O43181; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: O15400; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: O00461; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: P0CG08; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q6PEX3; IntAct: EBI-22134456; Score: 0.37
GO  GO:0012505;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0047389;
GO  GO:0008889;
GO  GO:0004435;
GO  GO:0006629;
GO  GO:0007399;
GO  GO:0045666;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVRHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTPWERLWFLLLTFTFGLTLTWLYFWWEVHNDYDEFNWYLYNRM
SQ  GYWSDWPVPILVTTAAAFAYIAGLLVLALCHIAVGQQMNLHWLHKIGLVVILASTVVAMSAVAQLWEDEWEVLLISLQGT
SQ  APFLHVGAVAAVTMLSWIVAGQFARAERTSSQVTILCTFFTVVFALYLAPLTISSPCIMEKKDLGPKPALIGHRGAPMLA
SQ  PEHTLMSFRKALEQKLYGLQADITISLDGVPFLMHDTTLRRTTNVEEEFPELARRPASMLNWTTLQRLNAGQWFLKTDPF
SQ  WTASSLSPSDHREAQNQSICSLAELLELAKGNATLLLNLRDPPREHPYRSSFINVTLEAVLHSGFPQHQVMWLPSRQRPL
SQ  VRKVAPGFQQTSGSKEAVASLRRGHIQRLNLRYTQVSRQELRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHA
SQ  LSQVPSPLWIMPPDEYCLMWVTADLVSFTLIVGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRDVSIMKEKLIFSEISD
SQ  GVEVSDVLSVCSDNSYDTYANSTATPVGPRGGGSHTKTLIERSGR
//
ID  Q640M6;
PN  Glycerophosphodiester phosphodiesterase domain-containing protein 5;
GN  Gdpd5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000269|PubMed:17275818, ECO:0000269|PubMed:18667693, ECO:0000305|PubMed:15276213}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15276213, ECO:0000269|PubMed:17275818, ECO:0000269|PubMed:18667693}. Cell projection, growth cone {ECO:0000269|PubMed:17275818}.
DR  UNIPROT: Q640M6;
DR  UNIPROT: Q8R0T5;
DR  UNIPROT: Q8R3N5;
DR  Pfam: PF03009;
DR  PROSITE: PS51704;
DE  Function: Glycerophosphodiester phosphodiesterase that promotes neurite formation and drives spinal motor neuron differentiation (PubMed:17275818, PubMed:18667693). Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane (By similarity). May contribute to the osmotic regulation of cellular glycerophosphocholine (PubMed:18667693). {ECO:0000250|UniProtKB:Q3KTM2, ECO:0000269|PubMed:17275818, ECO:0000269|PubMed:18667693}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005789;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0043025;
GO  GO:0097038;
GO  GO:0005886;
GO  GO:0047389;
GO  GO:0008889;
GO  GO:0004435;
GO  GO:0021895;
GO  GO:0006629;
GO  GO:0045746;
GO  GO:0030182;
GO  GO:0031175;
GO  GO:0007219;
GO  GO:0045787;
GO  GO:0045666;
GO  GO:0048505;
GO  GO:0021522;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVRHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTPWERLWFLLLVCTFSLTLTWLYFWWGVHNDYDEFNWYLYNRM
SQ  GYWSDWSVPILVTSAAAFTYIAGLLVLALCHIAVGQQLNLHWIHKMGLVVILASTVVAMSAVAQLWEDEWEVLLISLQGT
SQ  APFLHIGALVAITALSWIVAGQFARAERSSSQLTILCTFFAVVFTFYLIPLTISSPCIMEKKDLGPKPALIGHRGAPMLA
SQ  PEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARRPAAMLNWTVLQRLNAGQWFLKTDPF
SQ  WTASSLSPSDHREVQNQSICSLAELLELAKGNASLLLNLRDPPRDHPYRGSFLNVTLEAVLRSGFPQHQVMWLFNRQRPL
SQ  VRKMAPGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHT
SQ  LSRVPSPLWIMPPDEYCLMWVTADLISFSLIIGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRDVSIMKEKLIFSEISD
SQ  GVEVSDELSVCSDSSYDTYANANSTATPVGPRNAGSRAKTVTEQSGH
//
ID  Q04839;
PN  mRNA transport factor GFD1;
GN  GFD1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10523319}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10523319}. Nucleus membrane {ECO:0000269|PubMed:10523319}; Peripheral membrane protein {ECO:0000269|PubMed:10523319}; Cytoplasmic side {ECO:0000269|PubMed:10523319}.
DR  UNIPROT: Q04839;
DR  UNIPROT: D6W081;
DR  PDB: 3LCN;
DR  Pfam: PF17331;
DE  Function: High-copy suppressor of mutant alleles of ATP-dependent RNA helicase DBP5, which is involved in mRNA export from the nucleus. It may also play an important role in a late stage of NAB2-mRNA export. {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:15208322}.
DE  Reference Proteome: Yes;
DE  Interaction: P20449; IntAct: EBI-7998113; Score: 0.66
DE  Interaction: P30822; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38147; IntAct: EBI-390120; Score: 0.37
DE  Interaction: P32505; IntAct: EBI-390345; Score: 0.80
DE  Interaction: P53040; IntAct: EBI-391560; Score: 0.37
DE  Interaction: P32793; IntAct: EBI-392742; Score: 0.37
DE  Interaction: P15442; IntAct: EBI-8014718; Score: 0.40
DE  Interaction: P39936; IntAct: EBI-6331305; Score: 0.00
DE  Interaction: P50111; IntAct: EBI-2132826; Score: 0.51
DE  Interaction: Q04839; IntAct: EBI-2132792; Score: 0.37
DE  Interaction: P10591; IntAct: EBI-3670521; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3688520; Score: 0.35
DE  Interaction: Q12315; IntAct: EBI-6473225; Score: 0.44
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044877;
GO  GO:0006406;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10523319};
SQ  MPLESIWADAPDEEPIKKQKPSHKRSNNNKKNNNSRWSNESSSNNKKKDSVNKVKNNKGNHESKTKNKIKETLPREKKPP
SQ  HSQGKISPVSESLAINPFSQKATEISPPPVSPSKMKTTKTQSKQDTASKMKLLKKKIEEQREILQKTHHKNQQQQVLMDF
SQ  LNDEGSSNWVDDDEEELILQRLKTSLKI
//
ID  Q32L41;
PN  GTP cyclohydrolase 1 feedback regulatory protein;
GN  GCHFR;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
DR  UNIPROT: Q32L41;
DR  Pfam: PF06399;
DE  Function: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0042470;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0044549;
GO  GO:0009890;
GO  GO:0043105;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPYLLISTQIRMEVGPTVVGDEHSDPELMQHLGASKRSVLGNNFSEYYVNDPPRIVLDKLERRGFRVLSMTGVGQTLVWC
SQ  LHKE
//
ID  Q6PBT6;
PN  GTP cyclohydrolase 1 feedback regulatory protein;
GN  gchfr;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
DR  UNIPROT: Q6PBT6;
DR  Pfam: PF06399;
DE  Function: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0044549;
GO  GO:0009890;
GO  GO:0043105;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPYILISTQIRLETGPTMVGDEYSDPSIMNYLGARKITVLGNNFSEYHVDEPPRLVLDKLDKIGYRVVSMTGVGQTLVWC
SQ  LHKESSNTL
//
ID  P30047;
PN  GTP cyclohydrolase 1 feedback regulatory protein;
GN  GCHFR;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:16778797}. Nucleus membrane {ECO:0000269|PubMed:16778797}. Cytoplasm, cytosol {ECO:0000269|PubMed:16778797}.
DR  UNIPROT: P30047;
DR  UNIPROT: B2R4L6;
DR  UNIPROT: B7ZLM8;
DR  UNIPROT: Q2M1Q2;
DR  UNIPROT: Q99749;
DR  PDB: 6Z80;
DR  PDB: 6Z85;
DR  PDB: 7ACC;
DR  PDB: 7AL9;
DR  PDB: 7ALA;
DR  PDB: 7ALB;
DR  PDB: 7ALC;
DR  PDB: 7ALQ;
DR  Pfam: PF06399;
DR  OMIM: 602437;
DR  DisGeNET: 2644;
DE  Function: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine. {ECO:0000269|PubMed:16778797}.
DE  Reference Proteome: Yes;
DE  Interaction: O75147; IntAct: EBI-21786208; Score: 0.35
DE  Interaction: P30793; IntAct: EBI-958378; Score: 0.37
DE  Interaction: P20155; IntAct: EBI-21762493; Score: 0.35
DE  Interaction: Q8N0Z8; IntAct: EBI-21786208; Score: 0.35
DE  Interaction: Q9Y450; IntAct: EBI-21786208; Score: 0.35
DE  Interaction: Q96RR4; IntAct: EBI-21786208; Score: 0.35
DE  Interaction: Q7Z5L9; IntAct: EBI-21786208; Score: 0.35
DE  Interaction: Q5JSL3; IntAct: EBI-21786208; Score: 0.35
DE  Interaction: Q13951; IntAct: EBI-21786208; Score: 0.35
DE  Interaction: Q04637; IntAct: EBI-21786208; Score: 0.35
DE  Interaction: O76041; IntAct: EBI-21786208; Score: 0.35
DE  Interaction: O00168; IntAct: EBI-21862664; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0042470;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0016597;
GO  GO:0004857;
GO  GO:0044549;
GO  GO:0030742;
GO  GO:0044877;
GO  GO:0009890;
GO  GO:0043105;
GO  GO:0042133;
GO  GO:0006809;
GO  GO:0065003;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPYLLISTQIRMEVGPTMVGDEQSDPELMQHLGASKRRALGNNFYEYYVDDPPRIVLDKLERRGFRVLSMTGVGQTLVWC
SQ  LHKE
//
ID  P99025;
PN  GTP cyclohydrolase 1 feedback regulatory protein;
GN  Gchfr;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
DR  UNIPROT: P99025;
DR  UNIPROT: Q8BH29;
DR  Pfam: PF06399;
DE  Function: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0042470;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0016597;
GO  GO:0019899;
GO  GO:0004857;
GO  GO:0044549;
GO  GO:0030742;
GO  GO:0044877;
GO  GO:0009890;
GO  GO:0043105;
GO  GO:0065003;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPYLLISTQIRMEVGPTMVGDEHSDPELMQHLGASKRSVLGNNFYEYYVNDPPRIVLDKLECKGFRVLSMTGVGQTLVWC
SQ  LHKE
//
ID  P70552;
PN  GTP cyclohydrolase 1 feedback regulatory protein;
GN  Gchfr;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
DR  UNIPROT: P70552;
DR  PDB: 1IS7;
DR  PDB: 1IS8;
DR  PDB: 1JG5;
DR  PDB: 1WPL;
DR  Pfam: PF06399;
DE  Function: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine.
DE  Reference Proteome: Yes;
DE  Interaction: P22288; IntAct: EBI-1032731; Score: 0.62
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0042470;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0016597;
GO  GO:0019899;
GO  GO:0004857;
GO  GO:0044549;
GO  GO:0030742;
GO  GO:0044877;
GO  GO:0009890;
GO  GO:0043105;
GO  GO:0065003;
GO  GO:0045428;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPYLLISTQIRMEVGPTMVGDEHSDPELMQQLGASKRRVLGNNFYEYYVNDPPRIVLDKLECRGFRVLSMTGVGQTLVWC
SQ  LHKE
//
ID  Q6GM84;
PN  GTP cyclohydrolase 1 feedback regulatory protein;
GN  gchfr;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
DR  UNIPROT: Q6GM84;
DR  Pfam: PF06399;
DE  Function: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0009890;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPYVLISTQIRMETGPTIVGDEFSDLVLMAQLEADKRTVLGNNFSEYYVNEPPRVTLNKLERLGYRVVSMTGVGQTLVWC
SQ  LHKE
//
ID  Q6NVA8;
PN  GTP cyclohydrolase 1 feedback regulatory protein;
GN  gchfr;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
DR  UNIPROT: Q6NVA8;
DR  UNIPROT: Q28DT4;
DR  Pfam: PF06399;
DE  Function: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0044549;
GO  GO:0009890;
GO  GO:0043105;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPYVLISTQIRMETGPTIVGDEFSDTQLMAQLEADKRTVLGNNFSEYCVNEPPRVTLNKLEKLGYRVVSMTGVGQTLVWC
SQ  LHKE
//
ID  Q80WJ1;
PN  Gametogenetin;
GN  Ggn;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Cytoplasm, perinuclear region. Note=Localizes along the nuclear membrane. [Isoform 2]: Cytoplasmic vesicle. [Isoform 3]: Nucleus, nucleolus.
DR  UNIPROT: Q80WJ1;
DR  UNIPROT: Q5EBP4;
DR  UNIPROT: Q80WI9;
DR  UNIPROT: Q80WJ0;
DR  Pfam: PF15685;
DE  Function: May be involved in spermatogenesis. {ECO:0000269|PubMed:12574169}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5SV77; IntAct: EBI-4370065; Score: 0.54
DE  Interaction: Q9R109; IntAct: EBI-4370118; Score: 0.54
DE  Interaction: Q6K1E7; IntAct: EBI-3890501; Score: 0.44
GO  GO:0031410;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0031625;
GO  GO:0030154;
GO  GO:0006302;
GO  GO:0007566;
GO  GO:0007276;
GO  GO:0008104;
GO  GO:0065003;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGNVQSEPSAGGGSRKEQASDRASDSRRTPLVEPEVTPSSPAMRLARGLGVWFPGSSGPPGLLIPPEPQASSSPLPLTLE
SQ  LPSPVTPPPEEAAAVSTPPPPPVGTLLPAPSKWRKPTGTSVPRIRGLLEASHRGQGDPPSLRPLPPLPRQLTEKDPVLRA
SQ  PAPPPTPLEPRKQLPPAPSTCDPQPLSRRITLASSATSPTESQVRHSSEGQAAGGAHGGVPPQAGEGEMARSATSESGLS
SQ  LLCKVTFKSGPHLSPTSASGPLAAKASPGAGGGGLFASSGAISYAEVLKQGPQPPGATRPLGEVPPGATRPLGEVPRAAQ
SQ  ETEGGDGDGEGCSGPPSVPAPLARALPPPPYTTFPGSKPKFDWVSPPDGTERHFRFNGAVGGIGAPRRRTTTLSGPWGSP
SQ  PPRSGQTHPSSGPRRPTPALLAPPMFIFPAPNNGEPVRPVPPSPQQIPPLPPPPPTPPATPPPAPPPTPQPPALPRTPIL
SQ  VARPPTPGPGHLESALAPTPPSTLSPTAAADQVPAATPATVTSQVPATATAELSPPMPQPKTRTRRNKGPRAARGVIREE
SQ  GTSGDGPREPNTAPVTDSSSGGGGGGSNGTSTAGASNKGTARHWPPFEVLNSCPCKCYCRHQRRHRRLPRNVSAWLSTPT
SQ  NHLSEPPWVATVKLAGSLVAGLEHYDLQATHST
//
ID  P56966;
PN  Geranylgeranyl pyrophosphate synthase;
GN  GGPS1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95749}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O95749}.
DR  UNIPROT: P56966;
DR  UNIPROT: Q0VC78;
DR  Pfam: PF00348;
DR  PROSITE: PS00723;
DR  PROSITE: PS00444;
DE  Function: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins. {ECO:0000250|UniProtKB:O95749}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0004161;
GO  GO:0004311;
GO  GO:0004337;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0004659;
GO  GO:0045337;
GO  GO:0033384;
GO  GO:0033386;
GO  GO:0008299;
GO  GO:0006720;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPVAH
SQ  SIYGIPSVINSANYVYFLGLEKVLTLNHPDAVKLFTRQLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAV
SQ  GLMQLFSDYKEDLKPLLDTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN
SQ  IDIKKYCVHYLENVGSFEYTRNTLKELESKAYKQIDARGGNPELVALIKHLSKMFKEENE
//
ID  O95749;
PN  Geranylgeranyl pyrophosphate synthase;
GN  GGPS1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:32403198}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32403198}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:32403198}.
DR  UNIPROT: O95749;
DR  UNIPROT: A8MVQ8;
DR  UNIPROT: Q5T2C8;
DR  UNIPROT: Q6NW19;
DR  PDB: 2Q80;
DR  PDB: 6C56;
DR  PDB: 6C57;
DR  PDB: 6G31;
DR  PDB: 6G32;
DR  PDB: 6R4V;
DR  Pfam: PF00348;
DR  PROSITE: PS00723;
DR  PROSITE: PS00444;
DR  OMIM: 606982;
DR  OMIM: 619518;
DR  DisGeNET: 9453;
DE  Function: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins. {ECO:0000269|PubMed:32403198}.
DE  Disease: Muscular dystrophy, congenital hearing loss, and ovarian insufficiency syndrome (MDHLO) [MIM:619518]: An autosomal recessive disorder characterized by early-onset progressive muscle weakness, sensorineural hearing loss, and primary amenorrhea due to ovarian insufficiency. Some patients become wheelchair-bound by the second decade, whereas others have a milder phenotype and maintain independent ambulation into adulthood. Most patients have respiratory insufficiency. {ECO:0000269|PubMed:32403198}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O00244; IntAct: EBI-10179290; Score: 0.56
DE  Interaction: O95749; IntAct: EBI-10483772; Score: 0.74
DE  Interaction: O00560; IntAct: EBI-24510551; Score: 0.56
DE  Interaction: Q7Z5A8; IntAct: EBI-21529283; Score: 0.35
DE  Interaction: Q17RF5; IntAct: EBI-21556823; Score: 0.35
DE  Interaction: Q9NZB2; IntAct: EBI-21564038; Score: 0.35
DE  Interaction: Q9NWH9; IntAct: EBI-21564038; Score: 0.35
DE  Interaction: Q9H7X3; IntAct: EBI-21564038; Score: 0.35
DE  Interaction: Q2TAM9; IntAct: EBI-21564038; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-21564038; Score: 0.35
DE  Interaction: A6NKD9; IntAct: EBI-21564038; Score: 0.35
DE  Interaction: Q12950; IntAct: EBI-21599483; Score: 0.35
DE  Interaction: Q9H9P5; IntAct: EBI-21622067; Score: 0.35
DE  Interaction: Q8WV44; IntAct: EBI-21636495; Score: 0.35
DE  Interaction: Q9Y228; IntAct: EBI-21696444; Score: 0.35
DE  Interaction: O75386; IntAct: EBI-21712804; Score: 0.35
DE  Interaction: Q3SYB3; IntAct: EBI-21720692; Score: 0.35
DE  Interaction: P18509; IntAct: EBI-21725612; Score: 0.35
DE  Interaction: B2RXF5; IntAct: EBI-21730871; Score: 0.35
DE  Interaction: P62701; IntAct: EBI-21738776; Score: 0.35
DE  Interaction: Q96BR6; IntAct: EBI-21784034; Score: 0.35
DE  Interaction: Q9H5V7; IntAct: EBI-21792317; Score: 0.35
DE  Interaction: Q9H8E5; IntAct: EBI-21793591; Score: 0.35
DE  Interaction: Q86TJ2; IntAct: EBI-21794778; Score: 0.35
DE  Interaction: Q6ZMY9; IntAct: EBI-21818150; Score: 0.35
DE  Interaction: P12724; IntAct: EBI-21818048; Score: 0.35
DE  Interaction: Q86W54; IntAct: EBI-21818307; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0004161;
GO  GO:0004311;
GO  GO:0004337;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0004659;
GO  GO:0045337;
GO  GO:0033384;
GO  GO:0033386;
GO  GO:0008299;
GO  GO:0006720;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPVAH
SQ  SIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAV
SQ  GLMQLFSDYKEDLKPLLNTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN
SQ  IDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE
//
ID  Q9WTN0;
PN  Geranylgeranyl pyrophosphate synthase;
GN  Ggps1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95749}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O95749}.
DR  UNIPROT: Q9WTN0;
DR  Pfam: PF00348;
DR  PROSITE: PS00723;
DR  PROSITE: PS00444;
DE  Function: Catalyzes the trans-addition of the three molecules of isopentenyl diphosphate (IPP) onto dimethylallyl pyrophosphate (DMAPP) to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins. {ECO:0000250|UniProtKB:O95749}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0004161;
GO  GO:0004311;
GO  GO:0004337;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0004659;
GO  GO:0045337;
GO  GO:0033384;
GO  GO:0033386;
GO  GO:0008299;
GO  GO:0006720;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKTKEKAERILLEPYRYLLQLPGKQVRSKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDSSKLRRGFPVAH
SQ  SIYGVPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDTYTCPTEEEYKAMVLQKTGGLFGLAV
SQ  GLMQLFSDYKEDLKPLLDTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN
SQ  IDIKKYCVQYLEDVGSFAYTRHTLRELEAKAYKQIEACGGNPSLVALVKHLSKMFTEENK
//
ID  Q6F596;
PN  Geranylgeranyl pyrophosphate synthase;
GN  Ggps1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95749}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O95749}.
DR  UNIPROT: Q6F596;
DR  Pfam: PF00348;
DR  PROSITE: PS00723;
DR  PROSITE: PS00444;
DE  Function: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins. {ECO:0000250|UniProtKB:O95749}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0004161;
GO  GO:0004311;
GO  GO:0004337;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0004659;
GO  GO:0045337;
GO  GO:0033384;
GO  GO:0033386;
GO  GO:0008299;
GO  GO:0006720;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKTKEKAERILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDSSKLRRGFPVAH
SQ  SIYGVPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDTYTCPTEEEYKAMVLQKTGGLFGLAV
SQ  GLMQLFSDYKEDLKPLLDTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN
SQ  IDIKKYCVQYLEDVGSFEYTRYTLRELEAKAYKQIEACGGNPSLVALVKHLSKMFTEENE
//
ID  P36268;
PN  Inactive glutathione hydrolase 2;
GN  GGT2P;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:23682772}. Endoplasmic reticulum {ECO:0000269|PubMed:23682772}. Note=Co-localizes with calnexin in the endoplasmic reticulum.
DR  UNIPROT: P36268;
DR  PROSITE: PS00462;
DR  OMIM: 137181;
DE  Function: [Isoform 1]: Lacks catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer. {ECO:0000269|PubMed:23682772}. [Isoform 2]: Lacks catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer. {ECO:0000269|PubMed:23682772}. [Isoform 3]: Lacks catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer. {ECO:0000269|PubMed:23682772}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0070062;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0006751;
GO  GO:1901750;
GO  GO:0031179;
GO  GO:0002682;
GO  GO:0050727;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAMAADAKQCLEIGRDTLRDGGSAVDAAIAALLCVGLMNA
SQ  HSMGIGVGLFLTIYNSTTGKAEVINAREVAPRLAFASMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPS
SQ  IQLARQGFPVGKGLAAVLENKRTVIEQQPVLWYVFCRDRKVLREGERLTLPRLADTYEMLAIEGAQAFYNGSLMAQIVKD
SQ  IQAAGGIVTAEDLNNYRAELIEHPLNISLGDAVLYMPSARLSGPVLALILNILKGYNFSRESVETPEQKGLTYHRIVEAF
SQ  RFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRSQISDHTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTI
SQ  NLYFGSKVCSPVSGILFNNEWTTSALPAFTNEFGAPPSPANFIQPGKQPLLSMCLTIMVGQDGQVRMVVGAAGGTQITTD
SQ  TALAIIYNLWFGYDVKRAVEEPRLHNKLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAALDS
SQ  RKGGEPAGY
//
ID  Q8N2G8;
PN  GH3 domain-containing protein;
GN  GHDC;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q99J23}. Nucleus envelope {ECO:0000250|UniProtKB:Q99J23}.
DR  UNIPROT: Q8N2G8;
DR  UNIPROT: B4DQS4;
DR  UNIPROT: E9PDB5;
DR  UNIPROT: Q9BXM6;
DR  Pfam: PF03321;
DR  OMIM: 608587;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9R1X4; IntAct: EBI-11011611; Score: 0.35
DE  Interaction: Q14114; IntAct: EBI-11117560; Score: 0.35
DE  Interaction: P22460; IntAct: EBI-21505491; Score: 0.35
DE  Interaction: P32297; IntAct: EBI-21506200; Score: 0.35
DE  Interaction: Q9Y5I4; IntAct: EBI-21510892; Score: 0.35
DE  Interaction: Q9UGM1; IntAct: EBI-21517134; Score: 0.35
DE  Interaction: Q2Y0W8; IntAct: EBI-21566582; Score: 0.35
DE  Interaction: Q9UN71; IntAct: EBI-21584146; Score: 0.35
DE  Interaction: Q96FV3; IntAct: EBI-21591007; Score: 0.35
DE  Interaction: Q9H813; IntAct: EBI-21593240; Score: 0.35
DE  Interaction: Q01814; IntAct: EBI-21599092; Score: 0.35
DE  Interaction: P62079; IntAct: EBI-21619035; Score: 0.35
DE  Interaction: Q15884; IntAct: EBI-21620222; Score: 0.35
DE  Interaction: Q9Y312; IntAct: EBI-21626257; Score: 0.35
DE  Interaction: Q9Y5M8; IntAct: EBI-21633655; Score: 0.35
DE  Interaction: Q7Z3C6; IntAct: EBI-21657035; Score: 0.35
DE  Interaction: Q16281; IntAct: EBI-21687526; Score: 0.35
DE  Interaction: Q9Y5H8; IntAct: EBI-21695064; Score: 0.35
DE  Interaction: Q96T55; IntAct: EBI-21753509; Score: 0.35
DE  Interaction: Q9BY50; IntAct: EBI-21815157; Score: 0.35
DE  Interaction: P48201; IntAct: EBI-21833166; Score: 0.35
DE  Interaction: P07766; IntAct: EBI-21842586; Score: 0.35
DE  Interaction: P49682; IntAct: EBI-21274037; Score: 0.35
DE  Interaction: P32302; IntAct: EBI-21274058; Score: 0.40
DE  Interaction: Q7TLC7; IntAct: EBI-26377368; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005576;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0034774;
GO  GO:0035580;
GO  GO:0016881;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLLWPLLLLLLLLPTLALLRQQRSQDARLSWLAGLQHRVAWGALVWAATWQRRRLEQSTLHVHQSQQQALRWCLQGAQRP
SQ  HCSLRRSTDISTFRNHLPLTKASQTQQEDSGEQPLPPTSNQDLGEASLQATLLGLAALNKAYPEVLAQGRTARVTLTSPW
SQ  PRPLPWPGNTLGQVGTPGTKDPRALLLDALRSPGLRALEAGTAVELLDVFLGLETDGEELAGAIAAGNPGAPLRERAAEL
SQ  REALEQGPRGLALRLWPKLQVVVTLDAGGQAEAVAALGALWCQGLAFFSPAYAASGGVLGLNLQPEQPHGLYLLPPGAPF
SQ  IELLPVKEGTQEEAASTLLLAEAQQGKEYELVLTDRASLTRCRLGDVVRVVGAYNQCPVVRFICRLDQTLSVRGEDIGED
SQ  LFSEALGRAVGQWAGAKLLDHGCVESSILDSSAGSAPHYEVFVALRGLRNLSEENRDKLDHCLQEASPRYKSLRFWGSVG
SQ  PARVHLVGQGAFRALRAALAACPSSPFPPAMPRVLRHRHLAQCLQERVVS
//
ID  Q99J23;
PN  GH3 domain-containing protein;
GN  Ghdc;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum {ECO:0000269|PubMed:11735219}. Nucleus envelope {ECO:0000269|PubMed:11735219}.
DR  UNIPROT: Q99J23;
DR  UNIPROT: A2A5D7;
DR  UNIPROT: Q99J92;
DR  Pfam: PF03321;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0016881;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLLLWLLLLLLLLVPLLAILWQQRSRGARPCWLISLQHRVAWGMLGWAAAWQQWRLDRSTLNVGQSQQQALMWCLKKAQG
SQ  SCCLPREDTDMRTFRNHLPLTQTSHTQEQESEETLPSPASPQYHGDASLQATLLGLITLNKAYPEALAPGSTACVTPTSP
SQ  WPCSVPWLGHALGRVSPDGAKDPRTLLLEALISPGLRVLEARTAVELLDVFVGLEADGEELAEAIAAGILGTLLPKRAAE
SQ  LKEALEQGPRGLARRLWPKLQVVVTLDSGGQAEAVAALRVLWCQGLAFFSPAYAASGGVVALNLWPERPQGSYLLPPGVP
SQ  FIELLPIKEGTQEEAASTLLLTDAQREKEYELVLTNHTSLTRCRLGDVVQVVGTYNQCPVVRFTCRLGQTLNVRGEVTDE
SQ  TVFSVALAQAVGQWPGAKLLDHVCVESRVLDSCEGSAPHYEVFVELRGLRNLSEENRDKLDNCLQEASAQYKSLRFRGSV
SQ  GPAKVHLVRPGSFRVLREALAAFSSSSCRPPEMPRVIRLRHLAQLLQKRVIS
//
ID  Q22663;
PN  Globin-like protein 26;
GN  glb;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}. Nucleus lamina {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}. Cell membrane {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}. Note=Transported to the nucleus by myristoylation of the N-terminal glycine. {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:23251335}.
DR  UNIPROT: Q22663;
DR  Pfam: PF00042;
DE  Function: Plays a role in electron transport. Utilizes the bis-histidyl hexacoordinated complex with iron to transfer electrons to cytochrome c and molecular oxygen. Plays a regulatory role in the periodicity of the defecation cycle under oxidative stress conditions. Not involved in imparting protection against general conditions of oxidative stress. May participate in redox reactions under anaerobic conditions. {ECO:0000269|PubMed:20361867, ECO:0000269|PubMed:21674044, ECO:0000269|PubMed:23251335}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005652;
GO  GO:0005886;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0019825;
GO  GO:0005344;
GO  GO:0015671;
GO  GO:0001666;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:23251335};
SQ  MGSSTSTPAPPPKKNKPEGRKADNQILNSYQKSIVRNAWRHMSQKGPSNCGSTITRRMMARKSTIGDILDRSTLDYHNLQ
SQ  IVEFLQKVMQSLDEPDKISKLCQEIGQKHAKYRRSKGMKIDYWDKLGEAITETIREYQGWKIHRESLRAATVLVSYVVDQ
SQ  LRFGYSRGLHVQGSRETKEDDEE
//
ID  Q95ZK7;
PN  Defective in germ line development protein 3;
GN  gld;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}. Cytoplasmic granule {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}. Note=Localizes to P granules. Found also in particles near but not coincident with P granules. {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:19461891}.
DR  UNIPROT: Q95ZK7;
DR  UNIPROT: Q95ZK6;
DR  PDB: 3N89;
DR  PDB: 4ZRL;
DR  Pfam: PF17905;
DE  Function: Required maternally for germline survival and embryogenesis. Forms a complex with gls-1 which promotes the oogenic cell fate by freeing the translational repressor fbf to repress sperm promoting factors. Promotes maturation of primary spermatocytes to mature sperm. Required during hermaphrodite development to promote sperm fate, which is critical for determining the normal number of sperm. Promotion of sperm fate is at the expense of oogenesis, possibly through the negative regulation of fbf. Required during male development for the continued production of sperm and inhibition of oogenesis. Together with gld-2, promotes the transition from mitosis to meiosis. {ECO:0000269|PubMed:12431376, ECO:0000269|PubMed:15454534, ECO:0000269|PubMed:19461891}.
DE  Reference Proteome: Yes;
DE  Interaction: O17670; IntAct: EBI-334985; Score: 0.00
DE  Interaction: G5EDS1; IntAct: EBI-336095; Score: 0.00
DE  Interaction: G5EFL5; IntAct: EBI-341465; Score: 0.00
DE  Interaction: Q95QA6; IntAct: EBI-341819; Score: 0.00
DE  Interaction: O17087; IntAct: EBI-3891184; Score: 0.51
DE  Interaction: O76572; IntAct: EBI-6535647; Score: 0.37
DE  Interaction: Q10666; IntAct: EBI-11467458; Score: 0.37
DE  Interaction: Q10953; IntAct: EBI-11467642; Score: 0.37
DE  Interaction: Q8I4M5; IntAct: EBI-14989511; Score: 0.63
DE  Interaction: Q09312; IntAct: EBI-14989599; Score: 0.37
DE  Interaction: Q9N5M6; IntAct: EBI-14989696; Score: 0.54
GO  GO:0005737;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0030880;
GO  GO:0031379;
GO  GO:1990749;
GO  GO:0019904;
GO  GO:0003723;
GO  GO:0009792;
GO  GO:0018992;
GO  GO:0042078;
GO  GO:0042006;
GO  GO:0051321;
GO  GO:0000281;
GO  GO:0006378;
GO  GO:0006397;
GO  GO:0051100;
GO  GO:0002119;
GO  GO:0000280;
GO  GO:0010628;
GO  GO:0060903;
GO  GO:0045836;
GO  GO:0045840;
GO  GO:0040018;
GO  GO:0006417;
GO  GO:0043631;
GO  GO:0007283;
GO  GO:0040025;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGEQSHEKDHDEAHSYNPFVRSAVEYDADTRLQMAENAASARKLFVSSALKDIIVNPENFYHDFQQSAQMAEDANQRRQV
SQ  SYNTKREAHIHQLKAQGLPLPSNIPMIEINPTRVTLNMEFESQYYSLMTSDNGDHENVASIMAETNTLIQLPDRSVGGTT
SQ  PDPFAQQVTITGYFGDVDRARMLMRRNCHFTVFMALSKMKMPLHELQAHVRQNPIQNVEMSFVDAPEKNGIVTTYLRITA
SQ  REKNQHELIEAAKRLNEILFRESPAPENNFTLHFTLSTYYVDQVLGSSSTAQLMPVIERETTTIISYPCYNNRNETRGNI
SQ  YEIKVVGNIDNVLKARRYIMDLLPISMCFNIKNTDMAEPSRVSDRNIHMIIDESGIILKMTPSVYEPADLLSGEVPLNCA
SQ  SLRSKEFNIKKLYTAYQKVLSKKFDFIAPQPNDYDNSIWHHSLPANFLKNFNMPCRGELSDGSNGRRHRSSSIASSRSKH
SQ  SYMSKGKQFSESSGGPSRSHTRVSSFSENSSTVPIMQFPTPHFAPPMLTPHHHMLKYVYLQQHQQAQTFLKGAAGLHPGT
SQ  HIMFPPPIIVDGSFVSALPFADPVVFDGFPYVHGLFPVNEAEQHRNHRESSPSLRSTQEIRKPSRNMGNRPSSSTGSYYP
SQ  STTPRQRVYEQVREDDLRSHIGSRRTSVNGDDQNVESMHDQGYERQYPRQHQRLQKDDQQRWKTGSRGDIHSSRTINVHR
SQ  DVRNSNEYDFHVGNSGPAKRSPSLEQVQLQMTHHLKLKSNDVDLDHEKLYMHESPHNDSDTTVSASGFGNDLMDGDFVQR
SQ  FLSNANINESGRRPRTVSCFTEKDGQSARYIDSDGAYSVVDHASTHQSRSYDSFRKVGDNGVTKTILEPRARVEKDYGKI
SQ  SLEHKTKYSNEYGDEEKSAENDTSSLGSRQYRIDPMKLIASVRESSEQLPRIHERQFSDVLNEKEKEIADKSIESTVTQD
SQ  LSLDETSTY
//
ID  G5EFL0;
PN  Poly(A) RNA polymerase gld-4;
GN  gld;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:19339688}. Cytoplasmic granule {ECO:0000269|PubMed:19339688}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19339688}. Note=Localizes to P granules. This association is less apparent during pachytene, becomes obvious in maturing oocytes and is most prominently visible in developing embryos. {ECO:0000269|PubMed:19339688}.
DR  UNIPROT: G5EFL0;
DR  Pfam: PF01909;
DR  Pfam: PF03828;
DE  Function: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. The enzymatic activity is enhanced by its interaction with gls-1. Required, together with gld-2, for early meiotic progression in male and female germ cells and for gld-1 protein accumulation in the hermaphrodite germline. In the germline, forms a complex with gls-1 which directly binds to gld-1 mRNA and prevents its degradation. {ECO:0000269|PubMed:19339688}.
DE  Reference Proteome: Yes;
DE  Interaction: O02101; IntAct: EBI-25616084; Score: 0.35
GO  GO:0005737;
GO  GO:0005730;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0031499;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0004652;
GO  GO:0051321;
GO  GO:0006378;
GO  GO:0031123;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNEDSRLSSSQQPSTSTPRSSIPSTMNSDEPNTCRRLSQSQEQPSTSRTCKSETPEFGYSDSLPFAPWRRKRYGLNIQGL
SQ  HEEIVDMYHWIKPNEIESRLRTKVFEKVRDSVLRRWKQKTIKISMFGSLRTNLFLPTSDIDVLVECDDWVGTPGDWLAET
SQ  ARGLEADNIAESVMVYGGAFVPIVKMVDRDTRLSIDISFNTVQGVRAASYIAKVKEEFPLIEPLVLLLKQFLHYRNLNQT
SQ  FTGGLSSYGLVLLLVNFFQLYALNMRSRTIYDRGVNLGHLLLRFLELYSLEFNFEEMGISPGQCCYIPKSASGARYGHKQ
SQ  AQPGNLALEDPLLTANDVGRSTYNFSSIANAFGQAFQILLVAVTLRERKGKNHVAMRAYKGSLLHLIMPFTSKELTYRNW
SQ  LMSGVLSMPGQEAPASYDLNQLHNTLVSPMVDLSRYAWLRKAPAKAEKRDSRPLTIVNPADDRQTLAQQLKKQILEQTEA
SQ  KKSLEKMPACDDNKKEEELVATRETDVELEAEDTESEGHHNGENDLILTGPPLPTSTQSVNTSATVSTAASISEREDTDS
SQ  PGLSSSMGNQSSEEDEDNGINNRNNSAVPVQFKKPFNEVVAQPARESKRTQTTSEDKMQDQFHFNGYSYPPPSRYAAGTA
SQ  APSHKHRNAHPQRQRPSIRNLSQGSDGSDEYNVESWNNNIRQGRRASSNSPSPSRQQTNTRNCGPTNNIPYDSFRSQNKN
SQ  STLDGSNNSSEEPITMYADVVKKKSSITTSTNTSTADVNVTNGNPIPANGIIPQSMAVVNVGRGSYRNALTTSPMTPPSA
SQ  HTSMQKQHHLRKDNECGFDNNSATSSTDLSHHQPQLVPPVNRLQR
//
ID  Q0WPZ7;
PN  mRNA export factor GLE1;
GN  GLE1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q0WPZ7;
DR  UNIPROT: Q9SAE5;
DR  Pfam: PF07817;
DE  Function: Required for seed viability. {ECO:0000269|PubMed:22898497}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0044614;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006446;
GO  GO:0006449;
GO  GO:0048316;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGIVLEPPCPKSVDGISIDPEPNWNFESLVAEIASVEKKLNGFSMYPQPITNTTLRMGRRGGGFVMHVSEDEMESDEGEE
SQ  SDDEEEEEDHSQICTAGKRFACDELYLSDESDEEFDHEPEYMMNKLGLAESALYEVINDHQTEIKDDIRNQVSVVETEIM
SQ  NEIETSLSAIARVEKYSETRKEVERKLDLQYQRKVAEALDTHLTAVQREHKIKSQIEERKIRSEEAQEEARRKERAHQEE
SQ  KIRQEKARAEAQMLAKIRAEEEKKEVERKAAREVAEKEVADRKAAEQKLAEQKAVIESVTGSSATSNAQAGGNSIRAAES
SQ  ALILENHRLKKLEELETTNQSLKSRSNENFSSFEKHIGRVIRQISGTKDSVSGKINDIVKIFKDPRCPVSISIAAFAKKM
SQ  VTTKEKPNPFACSYVIVYINSQFPQVMDILLAEFHKACIYTVPKHIVNSQSAWDSDAYERLDSIMRLYGALVQTDIRVGN
SQ  ATNVHGIEHGWAWLARFLNKIPANRATATALNSFLQTAGFGLHQRYKSQFLKVVNVVREHFLQKLRAKKDTSDLLVIIAE
SQ  ITAYLDDRMYLKEPEGRAMKTTSTLSSELTAELNQPNYNQNYQRNDYRNYY
//
ID  Q3ZBK7;
PN  mRNA export factor GLE1;
GN  GLE1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q53GS7}. Note=Shuttles between the nucleus and the cytoplasm. Shuttling is essential for its mRNA export function. {ECO:0000250|UniProtKB:Q53GS7}.
DR  UNIPROT: Q3ZBK7;
DR  Pfam: PF07817;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005730;
GO  GO:0042802;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSEGRCWETLQALRSCDKGRLCYDRDWLLRGEDVLQECMSLPKLSSYSGWVVDHVLPHIQKNAPPSETSASSVSTSALD
SQ  QPSSVPRSPLRNPAYSPVSSATSNGTKDKYESPHTEPVVLQSPRGMKVEGCIRMYELVHRMKGAEGLRQWQEEQEKKVRA
SQ  LSEMASEQLKRFDERKELKHHKEFQDLREVMEKSSREALGQQEKLKAEHRHRAKILNLKLREAEQQRLKQEEQERLRKEE
SQ  GQARLRGLYALQEEVLHLSQQLDASDQHRDLLQVDLSAFRTRGNQLCSLVSGIIRATSENGFPTVEDQAAAEGALQEMRD
SQ  LLSNLHQEIRRACEEKRRRDEEEARIKQQESQMQQRPEAHKELPVPNQGPGAKPNEDLQMKVQDSTMQWYQQLQEASSRC
SQ  VLAFEGLSNSKDSQAKKIKMDLQKAATIPVSQISTIAGSKLKEIFDKIHSLLSGKPVQSGGRSVSVTLNPQGLDFVQYKL
SQ  AEKFVKQGEEEVASHHEAAFPIAVVASGIWELHPRVGALILAHLHKKCPYSVPFYPAFKEGMALEDYQRMLGYQVKDSKV
SQ  EQQDNFLKRMSGMIRLYAAIIQLRWPYGNRQETHPHGLNHGWRWLAQILNMEPLSDVTATLLFDFLEVCGNALMKQYQVQ
SQ  FWKMILLIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQHREVPVPKGFLTASFWRS
//
ID  G0S7F3;
PN  mRNA export factor GLE1;
GN  GLE1;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q12315}. Nucleus membrane {ECO:0000250|UniProtKB:Q12315}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12315}; Cytoplasmic side {ECO:0000250|UniProtKB:Q12315}. Nucleus membrane {ECO:0000250|UniProtKB:Q12315}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12315}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q12315}. Note=Biased towards cytoplasmic side. {ECO:0000250|UniProtKB:Q12315}.
DR  UNIPROT: G0S7F3;
DR  UNIPROT: G0ZGT9;
DR  PDB: 6B4G;
DR  PDB: 6B4H;
DR  Pfam: PF07817;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000250|UniProtKB:Q12315}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0016973;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q12315};
SQ  MAGSSPLNHHLWSSPSRTVEEILAEDRNSEARHRYLLELARKEHERVREEAARIYREQLAREERERLLAERRKEEERIRL
SQ  EQQIAAENARLNALKATRIEIPPLLPDPVPAPSTVNGKPTLPAAVATEAKRCPSEPSLVNGIASNGVVEAPAAASIKTLE
SQ  PAKPAASAFKAAGSATTAAPVAPIASVQPSTNGVVSAVASTPKTAPPAPTETPPDRYVEIHRNLKGLRKYMAEQAKTNLK
SQ  LKQRMGDMRREIRKSVGQLTTGGMAANKDKQQKIKSILTEALSNQVESALVDPNNFVVEPRKPVEGATNNDPLLPSIFVY
SQ  LINIFAKAAISQFINEAGARPETADPVGICVAAILSEPDFLWRGASLIDILIAKFRIVCPVLFGYRGSEKTEQGRQRLGW
SQ  WKESGQWISEQQHMDRMTGLGAGFAAISLRKFALSKKQNPYPPRFYWMAMAKIVNTPPAEISNTQCVVLKAMVQNYEAKF
SQ  IEFYGSAAIAALRTALIDFPARAPHKSAAVNSLEVLAQMLKRDTGLDLG
//
ID  Q6DRB1;
PN  mRNA export factor GLE1;
GN  gle1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q53GS7}.
DR  UNIPROT: Q6DRB1;
DR  UNIPROT: Q502U5;
DR  Pfam: PF07817;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005576;
GO  GO:0044614;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0060287;
GO  GO:0006406;
GO  GO:0048666;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0060296;
GO  GO:0006446;
GO  GO:0006449;
GO  GO:0014044;
GO  GO:0014037;
GO  GO:0014010;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSENLRWETLEALKNSPKGKLKYSPDWVEKGEDVLAGCVEVPSLSPLSGQILKRMSPRMLLKNCSRSSSVRDTSPGLSE
SQ  EAAVCRSAPISPRLKRSSCSLPAVSIQTEEEEEKEEEEKAEVVVEAPAVSPEASVSTPPAVSVLSPRATQISGCIRMCEQ
SQ  KHKAKAKMELSLRQEQQERLVATVANHESEQLKRFEEFMELKQRQEHQSIRDTNEKEAQESLGRQEKLREEHRHRMKILN
SQ  LRLREMEQQRLREVELERQRQVEGRERHRAINAIQEEVLQLNRLLQPQQSTHAEVEHAPYITRGNQLCSQLSEVVPAAAD
SQ  DQFPSVEDLSVAERALQEMRSLVRSLQEAVSQAAERKKKKEQEEEEEKRRQEQLKAQQEEQKKSAALSAKEKAKKEGLQT
SQ  GADDSTLKWYNSLQDLANQCAQAFDDLNKAKDTQTKKLKMELQKAATTPVSQIANSSGAPLKEAFEKIDKLLSRRPVTSA
SQ  GKTVSTSQHPQGLEFASYRLAEKFVKQGEEEVASNHSAAFPIGAVASGIWELHPKIGDLILAHLHKKCPYAVPHYPPMES
SQ  GTSVEDYQKILGYRVDEGKVEGQDSFLKRMSGMIRLYAAIIQMRWPYSSKQGLHLHGMNHGWRWMAQILNMEPLADITAT
SQ  ILFDFLEVCGNALMKQYRVQFWKLILIINEEYFPRYLCFASILHFTCIHWLQNIE
//
ID  Q55FW7;
PN  mRNA export factor GLE1;
GN  gle1;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q55FW7;
DR  Pfam: PF07817;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031012;
GO  GO:0044614;
GO  GO:0000922;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNKTSSNNISNTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNRILSPFKRNNSKENGNGSVTITLEPLVSPFKLIK
SQ  SNFKDDVHTNNINNNNNKIKRFLDEDNEFEITIPIRRSGNSINFNIGIVPSSNKKQQQQQQQQQKQKQKKKKTLSPLKKA
SQ  PGIYSLKDLTIDSDSDSDSYSDNDDNEEYNIKLKSPIKNKIVNNNNNQQQQQKQKEKEEKEEKEKVEKDKKEKDKKKLIL
SQ  NSFQSELIINRVEREREIKINRIVEEKNKEIDDKWVEIKEYNQNQMIKERKEFHSQQIRLNNLIKKQHKKDIKEFSIKLK
SQ  QAKQKHQSELSESLSLLNQLNKLEQQEIDRHNEELLKYELAIKEEKRKQQQLIERYEQKKREEKQRQLQQEQKEKQEKLE
SQ  KEEKEKEQQEQQKQLLIKLAKEKEEKEKFEKEQQQQKEKELQKEKELLQQKEKEKEKEKLQQQQQQQQQQQQQQQQQLQQ
SQ  QQQQQNQQNNNLGYIKKDGIIFSLNENSKNFNDFKERSKEFDMIIKFINEKKSMLSREMVEFERQNSKLINIAINQISAS
SQ  QEQVNEKTNKLIKSIQDSQQSDYLKKSTILSIVKKSLSQVESQITFHNASSFPLALVLVRVGEKYPELIDCLLASLNEKC
SQ  CYTVPYYVSPKENESQSSISKRMGYAFSNDIVGDNDKPIETEDEFHKRICGYLSLYCALILKSEQPHKSSSSSSSSSSST
SQ  MMFGFGTQIGNNNNNKLINKNLNIESSLRWLKDLVSLRPRRITSYLFVTFFTHLGNLLSKNQKSSLEFKIIVGKIVEENF
SQ  FNQMNKPGTEGSFSRLKNLIEEYYKTGTFQQHEGVDF
//
ID  Q9V4W1;
PN  mRNA export factor Gle1;
GN  Gle1;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q9V4W1;
DR  Pfam: PF07817;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VT04; IntAct: EBI-9943330; Score: 0.35
DE  Interaction: P18824; IntAct: EBI-9949245; Score: 0.35
DE  Interaction: P49415; IntAct: EBI-9965823; Score: 0.35
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDMMRAMDCLNMAATLRNAALASATCTGRTLGEDREPIWVEGSRKTPEPPLPEESPAPEPNNEIPLLPKIDFEPNISCF
SQ  PDLQAINASIVRRELEEEGKRCVRQQLKAIRDKQDAMRLSRETQQRKEERQRDQLQQKALRERNESLLIQKADQMTAAQL
SQ  EAQQREQLALRQQIDQKLHKLALEGVSRCQRRFNQKYEGIAKILLSLNPETVKVCAAQNTQLKELGQKFEQLVSSVKMGN
SQ  CEMQSQFLCSIIKAEEFCKSLDALELDIIKQLAEFSEQIQQQLKMEAAKKLEDERQRQQQQEEERQKLEEQQKLEEQEKL
SQ  RKEKEESAAKEKQQEAETAKADAANVPAPLEPKSQDVPPAATATSTSVHPDRLKFYNDILALYQSKVDAVKPLQTEESLK
SQ  QYRTGCQRAINLPLNAISAVSPQHLAQNFDKLYSFFAGQPTKVMNGTITINDHPLARDYCMLLMAKKFVSQTETAICSNP
SQ  QAAFPFASVIITFWKLLPDFGKVFLAYMYKESPFLVPYVIPQQQGQTPEQYLKTIGYRLTDKNELEKPDIYLKRQTGLAR
SQ  LYAAVIISQGRKAAGPDECFELNEGWLWLAHMVHVKPLPDISATLIMEILQTLGFELWRTYGKQFVKLLVYIQNIYMPQL
SQ  AAYDEGGPKTRLEMLLAKFLRERQIAQAVGVLPPGFW
//
ID  Q53GS7;
PN  mRNA export factor GLE1;
GN  GLE1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:12668658}. Cytoplasm {ECO:0000269|PubMed:12668658}. Note=Shuttles between the nucleus and the cytoplasm (PubMed:12668658). Shuttling is essential for its mRNA export function (PubMed:12668658). {ECO:0000269|PubMed:12668658}. [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:12668658}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12668658}. Note=Shuttles between the nucleus and the cytoplasm (PubMed:12668658). In the nucleus, isoform 1 localizes to the nuclear pore complex and nuclear envelope (PubMed:12668658). Shuttling is essential for its mRNA export function (PubMed:12668658). {ECO:0000269|PubMed:12668658}.
DR  UNIPROT: Q53GS7;
DR  UNIPROT: O75458;
DR  UNIPROT: Q53GT9;
DR  UNIPROT: Q5VVU1;
DR  UNIPROT: Q8NCP6;
DR  UNIPROT: Q9UFL6;
DR  PDB: 6B4F;
DR  PDB: 6B4I;
DR  PDB: 6B4J;
DR  Pfam: PF07817;
DR  OMIM: 253310;
DR  OMIM: 603371;
DR  OMIM: 611890;
DR  DisGeNET: 2733;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC). {ECO:0000269|PubMed:12668658, ECO:0000269|PubMed:16000379, ECO:0000269|PubMed:9618489}.
DE  Disease: Lethal congenital contracture syndrome 1 (LCCS1) [MIM:253310]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy, and congenital non- progressive joint contractures (arthrogryposis). The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS1 patients manifest early fetal hydrops and akinesia, micrognathia, pulmonary hypoplasia, pterygia, and multiple joint contractures. It leads to prenatal death. {ECO:0000269|PubMed:18204449}. Note=The disease is caused by variants affecting the gene represented in this entry. Congenital arthrogryposis with anterior horn cell disease (CAAHD) [MIM:611890]: An autosomal recessive disorder characterized by fetal akinesia, arthrogryposis and motor neuron loss. The fetus often survives delivery, but dies early as a result of respiratory failure. Neuropathological findings resemble those of lethal congenital contracture syndrome type 1, but are less severe. {ECO:0000269|PubMed:18204449}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O75694; IntAct: EBI-8873568; Score: 0.37
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P06103; IntAct: EBI-1955784; Score: 0.40
DE  Interaction: O00303; IntAct: EBI-1955532; Score: 0.57
DE  Interaction: Q53GS7; IntAct: EBI-8873329; Score: 0.58
DE  Interaction: Q86UP2; IntAct: EBI-8873563; Score: 0.37
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P03427; IntAct: EBI-14404759; Score: 0.35
DE  Interaction: Q9GZY0; IntAct: EBI-21528397; Score: 0.35
DE  Interaction: P10412; IntAct: EBI-21665473; Score: 0.35
DE  Interaction: Q9BTL4; IntAct: EBI-21675209; Score: 0.35
DE  Interaction: Q15050; IntAct: EBI-21678544; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-21728803; Score: 0.35
DE  Interaction: Q8N4J0; IntAct: EBI-21736494; Score: 0.35
DE  Interaction: Q02539; IntAct: EBI-21742951; Score: 0.35
DE  Interaction: P58499; IntAct: EBI-25859236; Score: 0.56
DE  Interaction: Q9UBF1; IntAct: EBI-25859228; Score: 0.56
DE  Interaction: Q9Y575; IntAct: EBI-25859218; Score: 0.56
DE  Interaction: Q9Y2M5; IntAct: EBI-25859210; Score: 0.56
DE  Interaction: Q00994; IntAct: EBI-25859202; Score: 0.56
DE  Interaction: Q9UGC6; IntAct: EBI-25859194; Score: 0.56
DE  Interaction: O75409; IntAct: EBI-25859186; Score: 0.56
DE  Interaction: Q9Y2L8; IntAct: EBI-25859178; Score: 0.56
DE  Interaction: Q29RF7; IntAct: EBI-25859170; Score: 0.56
DE  Interaction: Q9Y483; IntAct: EBI-25859162; Score: 0.56
DE  Interaction: Q9NS23; IntAct: EBI-25859154; Score: 0.56
DE  Interaction: Q16520; IntAct: EBI-25859146; Score: 0.56
DE  Interaction: O76041; IntAct: EBI-25859138; Score: 0.56
DE  Interaction: Q9Y239; IntAct: EBI-25859130; Score: 0.56
DE  Interaction: Q9UNE7; IntAct: EBI-25859122; Score: 0.56
DE  Interaction: O60641; IntAct: EBI-25859114; Score: 0.56
DE  Interaction: Q86V28; IntAct: EBI-25859106; Score: 0.56
DE  Interaction: O75558; IntAct: EBI-25859098; Score: 0.56
DE  Interaction: O75379; IntAct: EBI-25859090; Score: 0.56
DE  Interaction: O75925; IntAct: EBI-25859082; Score: 0.56
DE  Interaction: Q9UNS2; IntAct: EBI-25859074; Score: 0.56
DE  Interaction: Q99598; IntAct: EBI-25859066; Score: 0.56
DE  Interaction: P54274; IntAct: EBI-25859058; Score: 0.56
DE  Interaction: Q12824; IntAct: EBI-25859050; Score: 0.56
DE  Interaction: Q9BR81; IntAct: EBI-25859042; Score: 0.56
DE  Interaction: Q16621; IntAct: EBI-25859034; Score: 0.56
DE  Interaction: P27338; IntAct: EBI-25859026; Score: 0.56
DE  Interaction: P26439; IntAct: EBI-25859018; Score: 0.56
DE  Interaction: P06241; IntAct: EBI-25859010; Score: 0.56
DE  Interaction: O15287; IntAct: EBI-25859002; Score: 0.56
DE  Interaction: O60220; IntAct: EBI-25858994; Score: 0.56
DE  Interaction: Q9UER7; IntAct: EBI-25858986; Score: 0.56
DE  Interaction: P51798; IntAct: EBI-25858978; Score: 0.56
DE  Interaction: P24863; IntAct: EBI-25858970; Score: 0.56
DE  Interaction: Q96D59; IntAct: EBI-25859358; Score: 0.56
DE  Interaction: Q68EA5; IntAct: EBI-25859350; Score: 0.56
DE  Interaction: A5D8V7; IntAct: EBI-25859340; Score: 0.56
DE  Interaction: Q9UII2; IntAct: EBI-25859332; Score: 0.56
DE  Interaction: Q8IY31; IntAct: EBI-25859324; Score: 0.56
DE  Interaction: Q8WYH8; IntAct: EBI-25859316; Score: 0.56
DE  Interaction: Q5T0J7; IntAct: EBI-25859308; Score: 0.56
DE  Interaction: Q9GZS3; IntAct: EBI-25859300; Score: 0.56
DE  Interaction: Q8NHQ1; IntAct: EBI-25859292; Score: 0.56
DE  Interaction: Q969K3; IntAct: EBI-25859284; Score: 0.56
DE  Interaction: Q9NS71; IntAct: EBI-25859268; Score: 0.56
DE  Interaction: Q96FW1; IntAct: EBI-25859260; Score: 0.56
DE  Interaction: Q96EN9; IntAct: EBI-25859252; Score: 0.56
DE  Interaction: Q8TAG9; IntAct: EBI-25859244; Score: 0.56
DE  Interaction: Q8N895; IntAct: EBI-25859382; Score: 0.56
DE  Interaction: Q8IYD9; IntAct: EBI-25859374; Score: 0.56
DE  Interaction: Q86WT6; IntAct: EBI-25859366; Score: 0.56
DE  Interaction: Q68G74; IntAct: EBI-25859424; Score: 0.56
DE  Interaction: Q96M61; IntAct: EBI-25859416; Score: 0.56
DE  Interaction: Q7Z698; IntAct: EBI-25859398; Score: 0.56
DE  Interaction: Q8IZU1; IntAct: EBI-25859390; Score: 0.56
DE  Interaction: Q04912; IntAct: EBI-32725158; Score: 0.27
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0005730;
GO  GO:0042802;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSEGRCWETLKALRSSDKGRLCYYRDWLLRREDVLEECMSLPKLSSYSGWVVEHVLPHMQENQPLSETSPSSTSASALD
SQ  QPSFVPKSPDASSAFSPASPATPNGTKGKDESQHTESMVLQSSRGIKVEGCVRMYELVHRMKGTEGLRLWQEEQERKVQA
SQ  LSEMASEQLKRFDEWKELKQHKEFQDLREVMEKSSREALGHQEKLKAEHRHRAKILNLKLREAEQQRVKQAEQERLRKEE
SQ  GQIRLRALYALQEEMLQLSQQLDASEQHKALLKVDLAAFQTRGNQLCSLISGIIRASSESSYPTAESQAEAERALREMRD
SQ  LLMNLGQEITRACEDKRRQDEEEAQVKLQEAQMQQGPEAHKEPPAPSQGPGGKQNEDLQVKVQDITMQWYQQLQDASMQC
SQ  VLTFEGLTNSKDSQAKKIKMDLQKAATIPVSQISTIAGSKLKEIFDKIHSLLSGKPVQSGGRSVSVTLNPQGLDFVQYKL
SQ  AEKFVKQGEEEVASHHEAAFPIAVVASGIWELHPRVGDLILAHLHKKCPYSVPFYPTFKEGMALEDYQRMLGYQVKDSKV
SQ  EQQDNFLKRMSGMIRLYAAIIQLRWPYGNRQEIHPHGLNHGWRWLAQILNMEPLSDVTATLLFDFLEVCGNALMKQYQVQ
SQ  FWKMLILIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQHKDIPVPKGFLTSSFWRS
//
ID  Q8R322;
PN  mRNA export factor GLE1;
GN  Gle1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q53GS7}. Note=Shuttles between the nucleus and the cytoplasm. Shuttling is essential for its mRNA export function. {ECO:0000250|UniProtKB:Q53GS7}.
DR  UNIPROT: Q8R322;
DR  UNIPROT: A3KGV8;
DR  UNIPROT: Q3TT10;
DR  UNIPROT: Q3TU23;
DR  UNIPROT: Q3UD65;
DR  UNIPROT: Q8BT16;
DR  UNIPROT: Q9D4A6;
DR  Pfam: PF07817;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q4KLN8; IntAct: EBI-26596375; Score: 0.35
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0005730;
GO  GO:0042802;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSDGRCWETLRALRNTSKGRLRYDREWLLRYEDVLEECMSLPKLSSYSGWVVDHILPNTSGHTQESAPSSDNSPSSGSA
SQ  SGLYQSSLLKSPVRSSPQSPSPSSPNGTQSTHESPFTEPIAPQSSRAIKVEGCIRMYELAHRMRGTEGLRQWQEEQERKV
SQ  RALSEMASEQLKRFDELKELKLHKEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKILNLKLREAEQQRVKQAEQEQLRK
SQ  EEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLCGLISSIIRTTLESGYPTAENQAEAERALQEM
SQ  RDLLSDLEQEITRASQVKKKHEEEAKVKRQESQVQQGPAPPTQTSAPSPSPVGAQNEDLQVKVQDSTMQWYQQLQDASAK
SQ  CVLAFEDLTSSKDSQTKKIKMDLQKAATIPVSQISTIAGSKLKEIFDKIHSLLSGKPVQSGGRSVSVTLNPQGLDFVQYK
SQ  LAEKFVKQGEEEVASHHEAAFPIAVVASGIWMLHPKVGDLILAHLHKKCPYSVPFYPAFKEGMALEDYQRMLGYQVTDSK
SQ  VEQQDNFLKRMSGMIRLYAAIIQLQWPYGNRQEAHPHGLNHGWRWLAQVLNMEPLSDVTATLLFDFLEVCGNALMKQYQV
SQ  QFWKMILLIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQRREIPVPRGFLTTSFWRS
//
ID  Q5RAS2;
PN  mRNA export factor GLE1;
GN  GLE1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q53GS7}. Note=Shuttles between the nucleus and the cytoplasm. Shuttling is essential for its mRNA export function. {ECO:0000250|UniProtKB:Q53GS7}.
DR  UNIPROT: Q5RAS2;
DR  Pfam: PF07817;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0016973;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSEGRCWETLQALRSSDKGRLCYYRDWLLRGEDVLEECMCLPKLSSYSGWVVEHVLPHMQENQPLSETSPSSTSASALD
SQ  QPSFVPKSPDTSSAFSPASPATPNGTKGKDESQHTESMVLQSSRGIKVEGCIRMYELVHRMKGTEGLRQWQEEQERKVRA
SQ  LSEMASEQLKRFDEWKELKQHKEFQDLREVMEKSSREALGHQEKLKAEHRHRAKILNLKLREAEQQRVKQAEQERLRKEE
SQ  GQVRLRALYALREEMLQLSQQLDASEQHKGLLKVDLAAFQTRGNQLCSLISGIIRASSESGYPTTESQAEAERALQEMRD
SQ  LLMNLGQEITRACEDKRRQDEEEAQVKLQEAQMQQRPEAHKEPPAPSQGPGGKQNEDLQVKVQDITMQWYQQLQDASMQC
SQ  VLTFEGLTNSKDSQAKKIKMDLQKAATIPVSQISTIAGSKLKEIFDKIHSLLSGKPVQSGGRSVSVTLNPQGLDFVQYKL
SQ  AEKFVKQGEEEVASHHEAAFPIAVVASGIWELHPRVGDLILAHLHKKCPYSVPFYPTFKEGMALEDYQRMLGYQVKDSKV
SQ  EQQDNFLKRMSGMIRLYAAIIQLRWPYGNRQEIHPHGLNHGWRWLAQILNMEPLSDVTATLLFDFLEVCGNALMKQYQVQ
SQ  FWKMLILIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQHKDIPVPKGFLTSSFWRS
//
ID  Q4KLN4;
PN  mRNA export factor GLE1;
GN  Gle1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q53GS7}. Note=Shuttles between the nucleus and the cytoplasm. Shuttling is essential for its mRNA export function. {ECO:0000250|UniProtKB:Q53GS7}.
DR  UNIPROT: Q4KLN4;
DR  Pfam: PF07817;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0044614;
GO  GO:0042802;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSDGRCWETLRALRNSSKGRLRYDREWLLRYEDVLEECMSLPKLSSYSGWVVDHILPNTSHHTQENAPSSDNSPSSGSA
SQ  SGLYQSTLKSPVRSSPQSPSPSTPSGTQSAHESPFTEPIALQSSRAIKVEGCIRMYELAHRMRGTEGLRQWQEEQERKVQ
SQ  ALSEMASEQLKRFDELKELKLHKEFRDLQEVMEKSTREALGHQEKLKAEHRHRAKILNLKLREAEQQRVKQAEQEQLRKE
SQ  EGQIRLRSLYTLQEEVLQLNQQLDASSQHKDLLNVDLAAFQTRGNQLCGLISGIIRTTLESGYPTAENQAEAERVLQEMR
SQ  DLLSNLEQEITRASEMKKKDEEEARVKLQESQVQQGPGAPTKTSAPSPSLVGTQSEDLQVKVQDSTMQWYQQLQDASAKC
SQ  VLAFEDLTSSKDSQIKKIKMDLQKAATIPVSQISTIAGSKLKEVFDKIHSLLSGKPVQSGGRSVCVTLNPQGLDFVQYKL
SQ  AEKFVKQGEEEVASHHEAAFPIAVVASGIWMLHPKVGDLILAHLHKKCPYSVPFYPAFKEGMPLEDYQRMLGYQVTDSKV
SQ  EQQDNFLKRMSGMIRLYAAIIQLQWPYGSRQEAHPHGLNHGWRWLAQILNMEPLSDVTATLLFDFLEVCGNALMKQYQVQ
SQ  FWKMILLIKEDYFPRIEAITSSGQMGSFIRLKQFLEKCLQRREIPVPKGFLTPSFWRS
//
ID  O94652;
PN  mRNA export factor gle1;
GN  gle1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Cytoplasmic side {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Nucleoplasmic side {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94652;
DR  Pfam: PF07817;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved in a terminal step of poly(A)+ mRNA transport through the NPC (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q09847; IntAct: EBI-21243865; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006446;
GO  GO:0006449;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16823372};
SQ  MDTKTTPLIHAKLDEKIISSYNDANGLDIDDLWDIYNEKTRRMIHIISQRYKPKKQSPFPVIADENVRIFPPLHKTIDWA
SQ  KKRNVEEQNLIEQSITESQRIFSEKQRLEQERFNRELLEKKRIEAERQRLKDEEERRKKELMEKEKKEKERIRLIEEQKH
SQ  KENEQRRLKQEQIDAKRKEEEAREKRMKETFKDDPEEDSNMAWSIIHKIKTEVVAPISEKKELKNYCFTQKRKITPRLGQ
SQ  ITKSNSQIMKITQLLQQTFQEARNTDPLVYKWVLNFFCKSVVKQAEAEVAVNPISAYPLAKVCLLLQTQNADLKDLLFAR
SQ  LQKNCPWVIPFWYDHGTENGKKKMGFKKLSDGHWEQNTTYNERQCGIFAVYAAILSLDDSLAPESWRTFSRLLNLPSPSQ
SQ  LMKSDLELGQTLCSIVSTYLDIAGQSLLRIYGRQAKKLIVCSFSEAYLGANGGGSQYGRLRIVGEDWMKGQGGLKFSFEP
//
ID  Q12315;
PN  mRNA export factor GLE1;
GN  GLE1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10523319}. Nucleus membrane {ECO:0000269|PubMed:10523319}; Peripheral membrane protein {ECO:0000269|PubMed:10523319}; Cytoplasmic side {ECO:0000269|PubMed:10523319}. Nucleus membrane {ECO:0000269|PubMed:10523319}; Peripheral membrane protein {ECO:0000269|PubMed:10523319}; Nucleoplasmic side {ECO:0000269|PubMed:10523319}. Note=Biased towards cytoplasmic side.
DR  UNIPROT: Q12315;
DR  UNIPROT: D6VRE7;
DR  PDB: 3PEU;
DR  PDB: 3PEV;
DR  PDB: 3RRM;
DR  PDB: 3RRN;
DR  PDB: 6B4E;
DR  Pfam: PF07817;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved in a terminal step of poly(A)+ mRNA transport through the NPC probably by binding the ATP-dependent RNA helicase DBP5 and GFD1 at the cytoplasmic side of the NPC. These interactions are thought to be important for the dissociation of transport proteins such as the heterogeneous nuclear ribonucleoprotein (hnRNP) NAB2 from exported mRNA. {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11336711, ECO:0000269|PubMed:15208322}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P20449; IntAct: EBI-15806702; Score: 0.76
DE  Interaction: P20676; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P32500; IntAct: EBI-11888204; Score: 0.37
DE  Interaction: P34077; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P35729; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P36161; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P38181; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P39705; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P40064; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P40066; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P40368; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P40477; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P46673; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P47054; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P48837; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P49686; IntAct: EBI-849734; Score: 0.74
DE  Interaction: P49687; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P52593; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P52891; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P53011; IntAct: EBI-849734; Score: 0.32
DE  Interaction: Q02199; IntAct: EBI-849734; Score: 0.32
DE  Interaction: Q02629; IntAct: EBI-849734; Score: 0.53
DE  Interaction: Q02630; IntAct: EBI-849734; Score: 0.32
DE  Interaction: Q03790; IntAct: EBI-849734; Score: 0.32
DE  Interaction: Q04839; IntAct: EBI-6473225; Score: 0.44
DE  Interaction: Q05166; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12445; IntAct: EBI-849734; Score: 0.32
DE  Interaction: Q02159; IntAct: EBI-860728; Score: 0.00
DE  Interaction: P32505; IntAct: EBI-1566458; Score: 0.35
DE  Interaction: Q12315; IntAct: EBI-8873470; Score: 0.53
DE  Interaction: P12385; IntAct: EBI-1928244; Score: 0.40
DE  Interaction: P05453; IntAct: EBI-1954427; Score: 0.52
DE  Interaction: P06103; IntAct: EBI-1955816; Score: 0.40
DE  Interaction: Q04067; IntAct: EBI-1955824; Score: 0.40
DE  Interaction: P38074; IntAct: EBI-8764779; Score: 0.37
DE  Interaction: P33302; IntAct: EBI-20815093; Score: 0.37
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0008047;
GO  GO:0000822;
GO  GO:0005543;
GO  GO:0031369;
GO  GO:0006406;
GO  GO:0006397;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006446;
GO  GO:0006449;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10523319};
SQ  MRFVFDEVFNSDTDSPEFEETCSTTSSTSSQCPTPEPSPAIKLPSFTKVGTKKLVNESVVILDPALENALRDLNLQSKLI
SQ  PINEPIVAASSIIVPHSTNMPLPRASHSSLLDNAKNSNATAPLLEAIEESFQRKMQNLVLANQKEIQSIRENKRRVEEQR
SQ  KRKEEEERKRKEAEEKAKREQELLRQKKDEEERKRKEAEAKLAQQKQEEERKKIEEQNEKERQLKKEHEAKLLQQKDKLG
SQ  KAVTNFDKISKMFWHYKDKIAQIKQDIVLPIKKADVNVRNLLSRHKRKINPKFGQLTNSNQQLFKIQNELTQLINDTKGD
SQ  SLAYHWILNFIAKAVVHQAETEVRVKPESALPLGKLTLYLLVQFPELQELFMARLVKKCPFVIGFTCEIDTEKGRQNMGW
SQ  KRNNENKWEDNTSYDERMGGILSLFAIITRLQLPQEFITTTSHPFPIALSWHILARICNTPLNLITNTHFVILGSWWDAA
SQ  AVQFLQAYGNQASKLLILIGEELTSRMAEKKYVGAARLRILLEAWQNNNMESFPEMSP
//
ID  G0SEA3;
PN  mRNA export factor GLE2;
GN  GLE2;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P40066}. Nucleus membrane {ECO:0000250|UniProtKB:P40066}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40066}; Cytoplasmic side {ECO:0000250|UniProtKB:P40066}. Nucleus membrane {ECO:0000250|UniProtKB:P40066}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40066}; Nucleoplasmic side {ECO:0000250|UniProtKB:P40066}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P40066}.
DR  UNIPROT: G0SEA3;
DR  UNIPROT: G0ZGV3;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically important for nuclear mRNA export. {ECO:0000250|UniProtKB:P40066}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0016973;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P40066};
SQ  MAGLFGTTTSTTTSTLGDLKNDVELGSPPEDSITDLSFNPNPNDPKDFLAVSSWDKKVRVYEIAANGQNQGKVQMEHEGP
SQ  VFAVDFFKDGTKVISAGADKQAKVLDLASGQAMQVAAHDAPIRCVKYFEAGGTPMAVTGSWDKTIKYWDFRSATPAGTVQ
SQ  CQERVYTMDVKENLLVIGTADRYIDVINLKEPVKFYKTLQSPLKWQTRVVSCFTDSQGFAIGSIEGRCAIQYVEDKDQSM
SQ  NFSFKCHRDTPQNNVTNVHAVNAISFHPQHGTFSTAGSDGTFHFWDKDAKHRLKGYPNVGGSITATKFNRNGTIFAYAIS
SQ  YDWSKGYQGNTANYPTKVMLHPVLGDECKPRPSVKKR
//
ID  P40066;
PN  mRNA export factor GLE2;
GN  GLE2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P40066;
DR  UNIPROT: D3DM14;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically important for nuclear mRNA export. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10801828, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:8970155, ECO:0000269|PubMed:9463388}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-797307; Score: 0.44
DE  Interaction: P34077; IntAct: EBI-813993; Score: 0.27
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: Q02630; IntAct: EBI-795280; Score: 0.61
DE  Interaction: P11484; IntAct: EBI-797307; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-797307; Score: 0.35
DE  Interaction: P40368; IntAct: EBI-797307; Score: 0.44
DE  Interaction: P40477; IntAct: EBI-797307; Score: 0.44
DE  Interaction: P10592; IntAct: EBI-813993; Score: 0.27
DE  Interaction: P47054; IntAct: EBI-813993; Score: 0.27
DE  Interaction: P48837; IntAct: EBI-813993; Score: 0.27
DE  Interaction: Q04599; IntAct: EBI-813993; Score: 0.27
DE  Interaction: P36516; IntAct: EBI-813993; Score: 0.27
DE  Interaction: P22353; IntAct: EBI-813993; Score: 0.27
DE  Interaction: P36523; IntAct: EBI-813993; Score: 0.27
DE  Interaction: P36525; IntAct: EBI-813993; Score: 0.27
DE  Interaction: Q06678; IntAct: EBI-813993; Score: 0.27
DE  Interaction: P32337; IntAct: EBI-7490608; Score: 0.40
DE  Interaction: P47019; IntAct: EBI-8229717; Score: 0.22
DE  Interaction: P24870; IntAct: EBI-2611503; Score: 0.35
DE  Interaction: P24869; IntAct: EBI-2617071; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: P38915; IntAct: EBI-4375569; Score: 0.35
DE  Interaction: P38129; IntAct: EBI-4380674; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-4383599; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-4385804; Score: 0.35
DE  Interaction: P53040; IntAct: EBI-4390624; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0003723;
GO  GO:0043130;
GO  GO:0051664;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0015031;
GO  GO:2000728;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSFFNRSNTTSALGTSTAMANEKDLANDIVINSPAEDSISDIAFSPQQDFMFSASSWDGKVRIWDVQNGVPQGRAQHESS
SQ  SPVLCTRWSNDGTKVASGGCDNALKLYDIASGQTQQIGMHSAPIKVLRFVQCGPSNTECIVTGSWDKTIKYWDMRQPQPV
SQ  STVMMPERVYSMDNKQSLLVVATAERHIAIINLANPTTIFKATTSPLKWQTRCVACYNEADGYAIGSVEGRCSIRYIDDG
SQ  MQKKSGFSFKCHRQTNPNRAPGSNGQSLVYPVNSIAFHPLYGTFVTAGGDGTFNFWDKNQRHRLKGYPTLQASIPVCSFN
SQ  RNGSVFAYALSYDWHQGHMGNRPDYPNVIRLHATTDEEVKEKKKR
//
ID  P34689;
PN  ATP-dependent RNA helicase glh-1;
GN  glh;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17699606, ECO:0000269|PubMed:21402787}. Cytoplasmic granule {ECO:0000269|PubMed:17699606}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17699606}. Note=Perinuclear localization in germ cells but disperses into particles in cellularized oocytes. Component of P granules. {ECO:0000269|PubMed:17699606}.
DR  UNIPROT: P34689;
DR  UNIPROT: Q22873;
DR  UNIPROT: Q7KQH5;
DR  UNIPROT: Q9TXH4;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  Pfam: PF00098;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DR  PROSITE: PS50158;
DE  Function: Probable ATP-binding RNA helicase (PubMed:8415696). May act redundantly with the P-granule component glh-4 to regulate the formation of the granular structure of P-granules in embryos (PubMed:21402787, PubMed:24746798). Plays a role in positively regulating the localization of pgl-1 to P-granules (PubMed:18234720). May play a role in transgenerational epigenetic inheritance (PubMed:28533440). May protect somatic cells from excessive apoptosis during normal development (PubMed:27650246). {ECO:0000269|PubMed:18234720, ECO:0000269|PubMed:21402787, ECO:0000269|PubMed:24746798, ECO:0000269|PubMed:27650246, ECO:0000305|PubMed:28533440, ECO:0000305|PubMed:8415696}.
DE  Reference Proteome: Yes;
DE  Interaction: P91001; IntAct: EBI-1571788; Score: 0.51
DE  Interaction: O44408; IntAct: EBI-1571866; Score: 0.40
DE  Interaction: Q9U3F4; IntAct: EBI-1571938; Score: 0.40
DE  Interaction: P34689; IntAct: EBI-1571975; Score: 0.40
DE  Interaction: O01836; IntAct: EBI-1571991; Score: 0.40
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0043186;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0017151;
GO  GO:0008432;
GO  GO:0043621;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0008270;
GO  GO:0030154;
GO  GO:0007276;
GO  GO:0007281;
GO  GO:0009791;
GO  GO:0016070;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDGWSDSESAAKAKTGFGSGGGFGGGNNGGSGFGGGKNGGTGFGGGNTGGSGFGGGNTGGSGFGGGKTGGSGFGGGNTC
SQ  GSGFGGGSTGGSPYGGASSGFGGSTATSGFGSGEKSSAFGGSGGFGGSATGFGSGGGSFGGGNSGFGEGGHGGGERNNNC
SQ  FNCQQPGHRSSDCPEPRKEREPRVCYNCQQPGHTSRECTEERKPREGRTGGFGGGAGFGNNGGNDGFGGDGGFGGGEERG
SQ  PMKCFNCKGEGHRSAECPEPPRGCFNCGEQGHRSNECPNPAKPREGVEGEGPKATYVPVEDNMEDVFNMQKISEGLMFNK
SQ  FFDAEVKLTSSEKTVGIKPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIM
SQ  TRLIDDNNLNTAGEGGCYPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIK
SQ  HFCEEGTIKLDKCRFFVLDEADRMIDAMGFGTDIETIVNYDSMPRKENRQTLMFSATFPDSVQEAARAFLRENYVMIAID
SQ  KIGAANKCVLQEFERCERSEKKDKLLELLGIDIDSYTTEKSAEVYTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAR
SQ  EQRERSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISEDCSLLSEL
SQ  VGVLADAQQIVPDWMQGAAGGNYGASGFGSSVPTQVPQDEEGW
//
ID  Q27994;
PN  Solute carrier family 2, facilitated glucose transporter member 4;
GN  SLC2A4;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P14142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Endomembrane system {ECO:0000250|UniProtKB:P14142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P14142}. Note=Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized (By similarity). The dileucine internalization motif is critical for intracellular sequestration (By similarity). Insulin stimulation induces translocation to the cell membrane (By similarity). {ECO:0000250|UniProtKB:P14142, ECO:0000250|UniProtKB:P14672}.
DR  UNIPROT: Q27994;
DR  UNIPROT: P79104;
DR  UNIPROT: Q29RP5;
DR  UNIPROT: Q6SI69;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DR  PROSITE: PS00217;
DE  Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell. {ECO:0000250|UniProtKB:P19357}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0005768;
GO  GO:0009897;
GO  GO:0070062;
GO  GO:0032593;
GO  GO:0005887;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0042383;
GO  GO:0005802;
GO  GO:0030140;
GO  GO:0005355;
GO  GO:0015304;
GO  GO:0015149;
GO  GO:0010021;
GO  GO:0050873;
GO  GO:0032869;
GO  GO:0071470;
GO  GO:0071356;
GO  GO:0042593;
GO  GO:0044381;
GO  GO:1904659;
GO  GO:0015749;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSGFQQIGSEDGEPPRQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPEGPGSIPPGTLTTL
SQ  WALSVAIFSVGGMISSFLIGIISQWLGRKRAMLFNNALAVLGGTLMGLAKAAASYEMLILGRFFIGAYSGLTSGLVPMYV
SQ  GEIAPTHLRGALGTLNQLAIVTGILIAQVLGLESMLGTATLWPLLLGITVLPALLQMVLLPLCPESPRYLYIIRNLEGPA
SQ  RKSLKRLTGWADVSEVLAELKEEKRKLERERPLSLLQLLGSHTHRQPLVIAIVLQLSQQLSGINAVFYYSTSIFESAGVE
SQ  KPAYATIGAGVVNTVFTLVSVFLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPG
SQ  PIPWFIVAELFSQGPRPAAMAVAGFSNWTCNFIIGMGFQYVADAMGPYVFLLFAVLLLGFFIFTFLKVPETRGRTFDQIS
SQ  AVFHRTPSLLEQEVKPSTELEYLGPDEHD
//
ID  Q9XST2;
PN  Solute carrier family 2, facilitated glucose transporter member 4;
GN  SLC2A4;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P14142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Endomembrane system {ECO:0000250|UniProtKB:P14142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P14142}. Note=Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized (By similarity). The dileucine internalization motif is critical for intracellular sequestration (By similarity). Insulin stimulation induces translocation to the cell membrane (By similarity). {ECO:0000250|UniProtKB:P14142, ECO:0000250|UniProtKB:P14672}.
DR  UNIPROT: Q9XST2;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell. {ECO:0000250|UniProtKB:P19357}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0012505;
GO  GO:0032593;
GO  GO:0005887;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005355;
GO  GO:0015304;
GO  GO:0015149;
GO  GO:0032869;
GO  GO:0044381;
GO  GO:1904659;
GO  GO:0015749;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  TSIFETAGVGQPAYATIGAGVVNTVFTLVSVFLVERAGRRTLHLLGLAGMCGCAILMTIALLLLERLPAMSYVSIVAIFG
SQ  FVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFCNWTSNFIIGMGFQYIAXAMGPYVFLLFAVLLLAFFIFTFLKVPE
SQ  TR
//
ID  P14672;
PN  Solute carrier family 2, facilitated glucose transporter member 4;
GN  SLC2A4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P14142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Endomembrane system {ECO:0000269|PubMed:8300557}; Multi-pass membrane protein {ECO:0000269|PubMed:8300557}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P14142}. Note=Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized (PubMed:8300557). The dileucine internalization motif is critical for intracellular sequestration (PubMed:8300557). Insulin stimulation induces translocation to the cell membrane (By similarity). {ECO:0000250|UniProtKB:P14142, ECO:0000269|PubMed:8300557}.
DR  UNIPROT: P14672;
DR  UNIPROT: Q05BQ3;
DR  UNIPROT: Q14CX2;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DR  PROSITE: PS00217;
DR  OMIM: 125853;
DR  OMIM: 138190;
DR  DisGeNET: 6517;
DE  Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell. {ECO:0000250|UniProtKB:P19357}.
DE  Disease: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:1521731, ECO:0000269|PubMed:1756912, ECO:0000269|PubMed:1918382}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UER7; IntAct: EBI-367160; Score: 0.63
DE  Interaction: P03410; IntAct: EBI-9676334; Score: 0.49
DE  Interaction: O43889; IntAct: EBI-12701388; Score: 0.56
DE  Interaction: Q9UKB3; IntAct: EBI-21896803; Score: 0.35
DE  Interaction: Q8WU79; IntAct: EBI-21896803; Score: 0.35
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0009897;
GO  GO:0070062;
GO  GO:0032593;
GO  GO:0005887;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0005771;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0042383;
GO  GO:0016529;
GO  GO:0030315;
GO  GO:0005802;
GO  GO:0030140;
GO  GO:0012506;
GO  GO:0055056;
GO  GO:0005355;
GO  GO:0015304;
GO  GO:0015149;
GO  GO:0010021;
GO  GO:0050873;
GO  GO:0005975;
GO  GO:0071456;
GO  GO:0032869;
GO  GO:0071470;
GO  GO:0071356;
GO  GO:0042593;
GO  GO:0046323;
GO  GO:0044381;
GO  GO:1904659;
GO  GO:0007611;
GO  GO:0007616;
GO  GO:0015749;
GO  GO:0031550;
GO  GO:0098694;
GO  GO:0045471;
GO  GO:0007614;
GO  GO:0150104;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSGFQQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPEGPSSIPPGTLTTL
SQ  WALSVAIFSVGGMISSFLIGIISQWLGRKRAMLVNNVLAVLGGSLMGLANAAASYEMLILGRFLIGAYSGLTSGLVPMYV
SQ  GEIAPTHLRGALGTLNQLAIVIGILIAQVLGLESLLGTASLWPLLLGLTVLPALLQLVLLPFCPESPRYLYIIQNLEGPA
SQ  RKSLKRLTGWADVSGVLAELKDEKRKLERERPLSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFETAGVG
SQ  QPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPG
SQ  PIPWFIVAELFSQGPRPAAMAVAGFSNWTSNFIIGMGFQYVAEAMGPYVFLLFAVLLLGFFIFTFLRVPETRGRTFDQIS
SQ  AAFHRTPSLLEQEVKPSTELEYLGPDEND
//
ID  P14142;
PN  Solute carrier family 2, facilitated glucose transporter member 4;
GN  Slc2a4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:21907143, ECO:0000269|PubMed:25586176, ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27739494}; Multi-pass membrane protein {ECO:0000269|PubMed:21907143}. Endomembrane system {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27354378}. Note=Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized (PubMed:26629404, PubMed:26240143, PubMed:27354378). The dileucine internalization motif is critical for intracellular sequestration (PubMed:26240143, PubMed:26629404). Insulin stimulation induces translocation to the cell membrane (PubMed:27739494). {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:27354378, ECO:0000269|PubMed:27739494}.
DR  UNIPROT: P14142;
DR  UNIPROT: Q3TPK6;
DR  UNIPROT: Q9JJN9;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DR  PROSITE: PS00217;
DE  Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation (PubMed:26240143, PubMed:26629404). Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells (PubMed:26240143, PubMed:26629404). Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell (PubMed:26240143, PubMed:26629404). {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}.
DE  Disease: Note=Defects in Slc2a4 may be the cause of certain post- receptor defects in non-insulin-dependent diabetes mellitus (NIDDM).
DE  Reference Proteome: Yes;
DE  Interaction: Q6P5E6; IntAct: EBI-7540254; Score: 0.46
DE  Interaction: Q3U7R1; IntAct: EBI-15762008; Score: 0.50
GO  GO:0009986;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0005768;
GO  GO:0009897;
GO  GO:0070062;
GO  GO:0032593;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0005771;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0042383;
GO  GO:0016529;
GO  GO:0030315;
GO  GO:0005802;
GO  GO:0030140;
GO  GO:0031982;
GO  GO:0012506;
GO  GO:0055056;
GO  GO:0005355;
GO  GO:0015304;
GO  GO:0015149;
GO  GO:0005360;
GO  GO:0010021;
GO  GO:0050873;
GO  GO:0071456;
GO  GO:0032869;
GO  GO:0071470;
GO  GO:0071356;
GO  GO:0042593;
GO  GO:0046323;
GO  GO:0044381;
GO  GO:1904659;
GO  GO:0007611;
GO  GO:0007616;
GO  GO:0015749;
GO  GO:0031550;
GO  GO:0098694;
GO  GO:0045471;
GO  GO:0007614;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSGFQQIGSDDGEPPRQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNATWLGRQGPGGPDSIPQGTLTTL
SQ  WALSVAIFSVGGMISSFLIGIISQWLGRKRAMLANNVLAVLGGALMGLANAAASYEILILGRFLIGAYSGLTSGLVPMYV
SQ  GEIAPTHLRGALGTLNQLAIVIGILVAQVLGLESMLGTATLWPLLLALTVLPALLQLILLPFCPESPRYLYIIRNLEGPA
SQ  RKSLKRLTGWADVSDALAELKDEKRKLERERPMSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFESAGVG
SQ  QPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPG
SQ  PIPWFIVAELFSQGPRPAAMAVAGFSNWTCNFIVGMGFQYVADAMGPYVFLLFAVLLLGFFIFTFLKVPETRGRTFDQIS
SQ  AAFRRTPSLLEQEVKPSTELEYLGPDEND
//
ID  Q9XT10;
PN  Solute carrier family 2, facilitated glucose transporter member 4;
GN  SLC2A4;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P14142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Endomembrane system {ECO:0000250|UniProtKB:P14142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P14142}. Note=Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized (By similarity). The dileucine internalization motif is critical for intracellular sequestration (By similarity). Insulin stimulation induces translocation to the cell membrane (By similarity). {ECO:0000250|UniProtKB:P14142, ECO:0000250|UniProtKB:P14672}.
DR  UNIPROT: Q9XT10;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00217;
DE  Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell. {ECO:0000250|UniProtKB:P19357}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0012505;
GO  GO:0032593;
GO  GO:0005887;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005355;
GO  GO:0015304;
GO  GO:0015149;
GO  GO:0032869;
GO  GO:0044381;
GO  GO:1904659;
GO  GO:0015749;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  QQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPNGPGSIPPGTLTTLWALSV
SQ  AIFSVGGMFSSFLLGIISQWLGRKKAMLFNNTLAVLAGALMGLAKAAASYEMLILGRFLIGAYSGLASGLVPMYVGEIAP
SQ  THLRGALGTLNQLA
//
ID  P19357;
PN  Solute carrier family 2, facilitated glucose transporter member 4;
GN  Slc2a4;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:2211693}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Endomembrane system {ECO:0000269|PubMed:26240143}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P14142}. Note=Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized (By similarity). The dileucine internalization motif is critical for intracellular sequestration (By similarity). Insulin stimulation induces translocation to the cell membrane (PubMed:2211693). {ECO:0000250|UniProtKB:P14142, ECO:0000250|UniProtKB:P14672, ECO:0000269|PubMed:2211693}.
DR  UNIPROT: P19357;
DR  UNIPROT: P97900;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DR  PROSITE: PS00217;
DE  Function: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation (PubMed:2649253, PubMed:2645527, PubMed:2211693). Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells (PubMed:2649253, PubMed:2645527, PubMed:2211693). Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell (PubMed:2649253, PubMed:2645527, PubMed:2211693). {ECO:0000269|PubMed:2211693, ECO:0000269|PubMed:2645527, ECO:0000269|PubMed:2649253}.
DE  Disease: Note=It is a candidate for certain post-receptor defects in non-insulin-dependent diabetes mellitus.
DE  Reference Proteome: Yes;
DE  Interaction: O54861; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P10536; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q3L7M0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P34067; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q794F9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O70351; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62246; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z1A6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O55012; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5I0E7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q64428; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63524; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q2PS20; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O70257; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIA1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P97700; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6NX65; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8R490; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P13264; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8R3Z7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JJM9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4QRB4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8K3W5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P12368; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4QQW8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P21263; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8CGU6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8VI04; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q812C4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5U367; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TSP3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TPK5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TPJ0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TPB1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TP77; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TP72; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TP59; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TP54; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TP34; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TP13; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TP11; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TP08; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P26453; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7M0E3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q794E4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q792I0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q75NI5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P05982; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P05765; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P05712; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P69897; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P68182; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P68101; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P05197; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P05065; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04906; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04897; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63095; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04797; IntAct: EBI-921030; Score: 0.50
DE  Interaction: P04785; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04764; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04762; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q3KRE8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62890; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04644; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04642; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04636; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04466; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04462; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04218; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P04182; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62738; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P02600; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63259; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P68136; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P02466; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P01346; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P00507; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O88960; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O88941; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O88767; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O88761; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O88656; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O88638; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O88989; IntAct: EBI-921030; Score: 0.35
DE  Interaction: M0RC99; IntAct: EBI-921030; Score: 0.35
DE  Interaction: G3V7P1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5U1Z2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q52KJ9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5BK63; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q499V7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5EBA9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O70282; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P29266; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P28480; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P28075; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P28042; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P27952; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P27881; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62961; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P27791; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63086; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P27653; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P27615; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P27605; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P26772; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P84083; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P26051; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63245; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P25235; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62919; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62859; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62853; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P24368; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P24268; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P67779; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P24050; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P23965; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P23928; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P23514; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P23358; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62832; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P21708; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P21670; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P21533; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P21213; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P20417; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63074; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P84092; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P20069; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P19945; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P19804; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P97536; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P42667; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P97519; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P83888; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P83732; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P81155; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P80385; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P70645; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIH7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P70550; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P70500; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P70490; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P70470; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62718; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62716; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62703; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62630; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62628; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62425; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62332; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62282; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62278; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62271; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62268; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62260; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62250; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62243; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62198; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62193; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62142; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62138; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62083; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61983; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61980; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61805; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61751; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61621; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61589; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O54980; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O54715; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O35854; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6IFV1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O35796; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O35763; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O35511; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O35509; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5EGY4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P16884; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O35264; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O35244; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O35142; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O35094; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O08839; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O08772; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O08651; IntAct: EBI-921030; Score: 0.35
DE  Interaction: O08618; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P19234; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P06685; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63039; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P18484; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P18421; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P18420; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P18418; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P18163; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P17764; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P17220; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P17209; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P17164; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62828; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P17077; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P17074; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61354; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62909; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P17046; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P16975; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P16638; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62850; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P16036; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P15999; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P15791; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P15651; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P15178; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P14604; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P14562; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P14408; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P84100; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P13803; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P13596; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P13471; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P13437; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P13383; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P13086; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62902; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P12749; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P12001; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11980; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11960; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11884; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11883; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11762; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11730; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9QZK5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9QUR2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JMJ4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JMB5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JLZ1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JLH7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JLA3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JK11; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JIJ7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JI85; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JHY2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JHW5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JHW0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JHU5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JHB5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9HB97; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9ES40; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9ERR2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9ERM8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9ERF9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9ER30; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9EQX9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9EQV6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P7S1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9EPV3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9EPJ3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9EPH8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9EPC6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9EPB1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q99PW3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q99PD4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q99NA6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q99NA5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q71TY3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q71SY3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q71DI1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5M9G3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6W3E9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6TUG0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6RUV5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6RJR6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q2TA68; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6QI88; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6QI86; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6QI16; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6Q7Y5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6Q0N3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6PEC5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6PEC4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6PDV8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6PDV7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6PDV1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6PCU2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6PCT9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q68FQ0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P9V9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P9U9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P9U3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P9U0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P9T8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P7A9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P799; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P792; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P791; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9QXQ0; IntAct: EBI-921030; Score: 0.54
DE  Interaction: Q6P777; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P762; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P6W6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P6V8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9ES53; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9ER34; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P6V0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P6R2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P68370; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P685; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P503; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P502; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P4Z9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P2A5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6P0K8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6NYB7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q68FV6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8R4A1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6AY48; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P56571; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIH3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q3MHT4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z336; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z2X5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z2Q1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z2L0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6IRK9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z1X1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z1W6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z1P2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z1E1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z0V6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z0V5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9Z0U8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9WVK7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9WVK3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9WVC0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9WVB1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q2PQA9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9WU82; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9WVR3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9R1J8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9R063; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9QZV8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9QZR6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q99N27; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q99J82; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q99068; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q924W3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q924S5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q924M6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q923V8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q920L2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q920J4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q920A6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q91ZW6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q91Y81; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P82995; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q91XL4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8VHV7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8VHJ0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8VHI8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8VHF5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIP0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIP9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5M7W1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIU9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIT9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P56574; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q3T1L0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5FVH2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4V8B7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q68FS9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: D3ZJR1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5EBA4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q68FW4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XI73; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6AY55; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5U1Y1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q3KR97; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4V8B5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q66H98; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5BJX1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5FVH0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8R491; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q3KR80; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q32KK2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q66H12; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11598; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61212; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61206; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61107; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P61023; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P60901; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P60892; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P60711; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P60192; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P60123; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P58405; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P55161; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P54921; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P54311; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P54001; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62907; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P52944; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P52555; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P52296; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P51868; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P51583; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P50878; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62815; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P50503; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P50430; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P50408; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P50137; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P49432; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P49242; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P49134; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P48721; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P48679; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P48675; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P48500; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P48037; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P48004; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P47942; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P47853; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P46462; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P45592; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P45479; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63004; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P42930; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6MGB8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P97629; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6MGB5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6MG76; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P55063; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6MG60; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6MG30; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6LED0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6J4T4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62636; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6IRE4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q66X93; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6IN22; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6IMX8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P28073; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6IE67; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6GQP4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9JLJ3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q64591; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q64560; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q64537; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q64536; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q64375; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q64232; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63965; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63750; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63716; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63699; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63635; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63615; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63598; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63584; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63570; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63569; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62870; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q9QZM5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: G3V6H1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5FWT1; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XI43; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5U2V8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4KM74; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5BJK8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5U302; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4QQV0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5EB77; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XII0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XID6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q3B7V5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5BJT7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5FVQ4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4G061; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5M843; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIQ4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: D4A414; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5PQM3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q32PX6; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5U2X8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q68FT7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4G067; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4V8H5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIM0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5PQL2; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TP47; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q68FY0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TP24; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q7TMC7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P05426; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q641X3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q68FR9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5U3Z7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q32KJ5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6AYH5; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5M918; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIM9; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIU4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q3KRE0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q498E0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4FZT0; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIG8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q4AEF8; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P81799; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q66H94; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XI04; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q6AYS3; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q3MIE7; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q68FT4; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P68511; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11507; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11442; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11240; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P11232; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62845; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62963; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P10888; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P10860; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P10760; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P10719; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62755; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63326; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P09895; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P09527; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P09456; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63324; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P09330; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P08503; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P08461; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P08413; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63018; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P08081; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P08010; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P07895; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P07872; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P07871; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P07824; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P07633; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P07154; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P07153; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P07150; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P06761; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P06760; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63100; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P41123; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P40307; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P40112; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P39052; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62914; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P38983; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P38659; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P38650; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P37397; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P37285; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63088; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P36972; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P36202; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P35704; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P35565; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P35435; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P35434; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P35427; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P35286; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P35284; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P35281; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P68255; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63102; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P35213; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P35053; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P34926; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P34064; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P34058; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P32551; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P32089; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P31977; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P31399; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P31232; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P31000; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P30904; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P30839; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P30427; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P29457; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P29419; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P29315; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P29314; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63507; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63448; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62982; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63377; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63347; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63321; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63312; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63258; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63151; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63083; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63081; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P02454; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63016; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q63002; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62952; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62920; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62908; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62902; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62871; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62991; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62786; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62764; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62698; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62667; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q62638; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q60587; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P62997; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P63170; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q10758; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q10728; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q09073; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q08850; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q08163; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q07984; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q07936; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q07266; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q06647; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q05962; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q04462; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q02253; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q01205; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q00972; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P97852; IntAct: EBI-921030; Score: 0.35
GO  GO:0009986;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0005768;
GO  GO:0009897;
GO  GO:0070062;
GO  GO:0032593;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0005771;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0042383;
GO  GO:0016529;
GO  GO:0030315;
GO  GO:0005802;
GO  GO:0030140;
GO  GO:0012506;
GO  GO:0055056;
GO  GO:0005355;
GO  GO:0015304;
GO  GO:0015149;
GO  GO:0010021;
GO  GO:0050873;
GO  GO:0071456;
GO  GO:0032869;
GO  GO:0071470;
GO  GO:0071356;
GO  GO:0042593;
GO  GO:0046323;
GO  GO:0044381;
GO  GO:1904659;
GO  GO:0007611;
GO  GO:0007616;
GO  GO:0015749;
GO  GO:0031550;
GO  GO:0098694;
GO  GO:0045471;
GO  GO:0007614;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSGFQQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNATWLGRQGPGGPDSIPQGTLTTL
SQ  WALSVAIFSVGGMISSFLIGIISQWLGRKRAMLANNVLAVLGGALMGLANAAASYEILILGRFLIGAYSGLTSGLVPMYV
SQ  GEIAPTHLRGALGTLNQLAIVIGILVAQVLGLESMLGTATLWPLLLAITVLPALLQLLLLPFCPESPRYLYIIRNLEGPA
SQ  RKSLKRLTGWADVSDALAELKDEKRKLERERPLSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFELAGVE
SQ  QPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPSMSYVSIVAIFGFVAFFEIGPG
SQ  PIPWFIVAELFSQGPRPAAMAVAGFSNWTCNFIVGMGFQYVADAMGPYVFLLFAVLLLGFFIFTFLRVPETRGRTFDQIS
SQ  ATFRRTPSLLEQEVKPSTELEYLGPDEND
//
ID  Q9VJL6;
PN  Glia maturation factor;
GN  GMF;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell projection, lamellipodium {ECO:0000269|PubMed:25308079}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25308079}. Nucleus {ECO:0000269|PubMed:25308079}. Cytoplasm, cell cortex {ECO:0000269|PubMed:25308079}. Note=Colocalizes with F-actin and Arp2/3-nucleated actin arrays. {ECO:0000269|PubMed:25308079}.
DR  UNIPROT: Q9VJL6;
DR  UNIPROT: Q8MSR7;
DR  UNIPROT: Q9NK59;
DR  Pfam: PF00241;
DR  PROSITE: PS51263;
DE  Function: Inhibits Arp2/3-mediated actin nucleation (PubMed:25308079). Together with flr, promotes Arp2/3-nucleated actin filament array disassembly (PubMed:25308079). Promotes debranching (PubMed:25308079). Regulates lamellipodial protrusion dynamics possibly by facilitating lamellipodial retraction (PubMed:25308079). In egg chambers, enhances the retraction dynamics of cellular extensions in border cells and thus together with flr plays an important role in directional migration of border cell clusters (PubMed:25308079). {ECO:0000269|PubMed:25308079}.
DE  Reference Proteome: Yes;
DE  Interaction: Q95RB1; IntAct: EBI-238317; Score: 0.00
DE  Interaction: Q9VJA1; IntAct: EBI-242035; Score: 0.00
GO  GO:0071944;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0071933;
GO  GO:0071846;
GO  GO:0007298;
GO  GO:0034316;
GO  GO:0030833;
GO  GO:0031344;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDNQICDISNEVLEELKKFRFSKSKNNAALILKVDREKQTVVLDEFIDDISVDELQDTLPGHQPRYVIYTYKMVHDDQR
SQ  ISYPMCFIFYTPRDSQIELQMMYACTKSALQREVDLTRVYEIRELDELTEEWLKAKLK
//
ID  O36388;
PN  Envelope glycoprotein M;
GN  gM;
OS  654901;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: O36388;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MKSSKKDIFILHIWLKLMGCYVFMFITSVVLPIAAMFPNLGFPCYYNTLVDYSKLNLREKNQAQHLTPTLFLEAPEMFFY
SQ  VTYSFIVDCCSLVYYALAAVAVVKAKKHAPGLMALSQWIMAVGSPTLLYMAVLKLWTIQLYIHTLSYKHIYLAAFVYCLH
SQ  WLLSMVYTECYITNVSSQWTSSELKKTIPENILLYRVVHVLKPIMMNVHLSVVALETLIFCLSFMMAIGNSFYVMVSDIV
SQ  FGAINLYLILPIIWYFVTEFWLSKYLPRQFGFYFGVLVASIILILPVVRYDKIFVAAQIHRAVSINIAMIPLCALVALLV
SQ  RACRVYTDRKKIAYTALPSKPQTIKYTKPIEPSTKQAPDSSIFLEEESDTDFEQ
//
ID  P52370;
PN  Envelope glycoprotein M;
GN  gM;
OS  10323;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P52370;
DR  UNIPROT: O39493;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: No;
GO  GO:0044175;
GO  GO:0044177;
GO  GO:0044178;
GO  GO:0033644;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0044423;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MAGSAQPAAVHWRLWLAQVGVFAGLALLLLITLIGAASPGAGLPCFYAAIVNYNARNLSADGGAWAQRELGARHPALFLE
SQ  TPTTAAFSAYTAVVLLAVAAFDVAAAIIIRRENSGGFAAAYHMNALATLATPPGALLLGALAAWTLQAAVLLLSHKIMVL
SQ  AAATYLAHLAPPAAFVGLFCTAGLPGAEYAQAVHALRERSPRAHRLLGPGRAVMINLAGGLLALIIGTAPLMLGQLLGAG
SQ  LGLSLAQTVVAGVTVFCLAAVLFLVLTELVLSRYTQVLPGPAFGTLVAASCIAVASHDYFHQLRGVVRTQAPRAAARVKL
SQ  ALAGVALLAVAMLVLRLVRACLHHRRKGSAFYGHVSAARQQAARYIARARSSRGMAPLEGDAAALLDRGVASDDEEAVYE
SQ  AHAPPRPPTIPLRRPEVPHSRASHPRPPPRSPPPAHVK
//
ID  Q1HVE9;
PN  Envelope glycoprotein M;
GN  gM;
OS  82830;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q1HVE9;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MKSSKNDTFVYRTWFKTLVVYFVMFVMSAVVPITAMFPNLGYPCYFNALVDYGALNLTNYNLAHHLTPTLYLEPPEMFVY
SQ  ITLVFIADCVAFIYYACGEVALIKARKKVSGLTDLSAWVSAVGSPTVLFLAILKLWSIQVFIQVLSYKHVFLSAFVYFLH
SQ  FLASVLHACACVTRFSPVWVVKAQDNSIPQDTFLWWVVFYLKPIVTNLYLGCLALETLVFSLSVFLALGNSFYFMVGDMV
SQ  LGAVNLFLVLPIFWYILTEVWLASFLRHNFGFYCGMFIASIILILPLVRYEAVFVSAKLHTTVAINVAIIPILCSVAMLI
SQ  RICRIFKSMRQGTDYVPVSETVELELESEPRPRPSRTPSPGRNRRRSSTSSSSSRSTRRQRPVSTQALISSVLPMTTDSE
SQ  EEIFP
//
ID  P03215;
PN  Envelope glycoprotein M;
GN  gM;
OS  10377;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P03215;
DR  UNIPROT: Q777D4;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:11070013}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MKSSKNDTFVYRTWVKTLVVYFVMFVMSAVVPITAMFPNLGYPCYFNALVDYGALNLTNYNLAHHLTPTLYLEPPEMFVY
SQ  ITLVFIADCVAFIYYACGEVALIKARKKVSGLTDLSAWVSAVGSPTVLFLAILKLWSIQVFIQVLSYKHVFLSAFVYFLH
SQ  FLASVLHACACVTRFSPVWVVKAQDNSIPQDTFLWWVVFYLKPVVTNLYLGCLALETLVFSLSVFLALGNSFYFMVGDMV
SQ  LGAVNLFLILPIFWYILTEVWLASFLRHNFGFYCGMFIASIILILPLVRYEAVFVSAKLHTTVAINVAIIPILCSVAMLI
SQ  RICRIFKSMRQGTDYVPVSETVELELESEPRPRPSRTPSPGRNRRRSSTSSSSSRSTRRQRPVSTQALVSSVLPMTTDSE
SQ  EEIFP
//
ID  Q3KSR7;
PN  Envelope glycoprotein M;
GN  gM;
OS  10376;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q3KSR7;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: No;
DE  Interaction: Q9NSC5; IntAct: EBI-2622194; Score: 0.37
DE  Interaction: Q02818; IntAct: EBI-2622177; Score: 0.37
DE  Interaction: P0C763; IntAct: EBI-9644923; Score: 0.37
DE  Interaction: Q3KSQ7; IntAct: EBI-9645160; Score: 0.37
DE  Interaction: A6SZC0; IntAct: EBI-9645170; Score: 0.37
DE  Interaction: P0C738; IntAct: EBI-9645175; Score: 0.37
DE  Interaction: P03219; IntAct: EBI-9645248; Score: 0.37
DE  Interaction: K9UT36; IntAct: EBI-9645587; Score: 0.37
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MKSSKNDTFVYRTWVKTLVVYFVMFVMSAVVPITAMFPNLGYPCYFNALVDYGALNLTNYNLAHHLTPTLYLEPPEMFVY
SQ  ITLVFIADCVAFIYYACGEVALIKARKKVSGLTDLSAWVSAVGSPTVLFLAILKLWSIQVFIQVLSYKHVFLSAFVYFLH
SQ  FLASVLHACACVTRFSPVWVVKAQDNSIPQDTFLWWVVFYLKPVVTNLYLGCLALETLVFSLSVFLALGNSFYFMVGDMV
SQ  LGAVNLFLILPIFWYILTEVWLASFMRHNFGFYCGMFIASIILILPLVRYEAVFVSAKLHTTVAINVAIIPILCSVAMLI
SQ  RICRIFKSMRQGTDYVPVSETVELELESEPRPRPSRTPSPGRNRRRSSTSSSSSRSTRRQRPVSTQALVSSVLPMTTDSE
SQ  EEIFP
//
ID  P28948;
PN  Envelope glycoprotein M;
GN  gM;
OS  31520;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P28948;
DR  UNIPROT: Q6DLF9;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:8648751}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MARRGAAVAEEPLLPSSGIVGIGPIEGINWRTWLVQVFCFALTTSVLFITLVTASLPQTGYPCFYGSLVDYTQKNHSVVD
SQ  GVWMRQIAGGVAPTLFLETTSLVAFLYYTTLVLVAISFYLIISAVLVRRYARGKECTAVAGCTRPTTTLIASHVTLVLGT
SQ  LATWLLQVVILLLSHKQAVLGAAVYVVHFVSLVFFCMSFSGLGTASAQYSSNLRILKTNLPALHKMAGPGRAVMTNLGMG
SQ  MLGISLPILSLMLGIILANSFHITLWQTVTVAVGVFVALGLMFLIIVELIVSHYVHVLVGPALAVLVASSTLAVATHSYF
SQ  VHFHAMVSVQAPNLATASKAIVGIMAVISIIMLVVRLVRAIMFHKKRNTEFYGRVKTVSSKARRYANKVRGPRRNPQPLN
SQ  VAESRGMLLAEDSETDAEEPIYDVVSEEFETEYYDDPQRVPERSHRREYR
//
ID  P52371;
PN  Envelope glycoprotein M;
GN  gM;
OS  82831;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P52371;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MKSSKSDLFIYKTWFKLLVLYFVMFVLSATVPIAASFPGLGFPCYYNALVNYSAINLTERNVAKHLTPTLYLEEPEMFAY
SQ  MTFTFLVDCFAAVYYFLGALAIMLAKRHFVVSLTTLSQWIAMVGTPTLILIGMWRMWTIQLFIQTLSYKHIYLSAFVYLI
SQ  HFLLSFLHTQCYISRNSQLWSLKVLEQGIPPNTLLDTVVFTIKPLLANCQLFCLGLEMLVFSLSFMMAIGNSFYVLVSDI
SQ  VFGAINLYLALVLFWVLLTELYLVKYMTFVMGFYLGGLIGCIFLLVPLWRYEQIFVAANLRSPILINILVIFFLCTLSAL
SQ  VRLLRMTWFSPTKPSYEPIQLKNIKHRRVKLQSPSGPSILEEGSSDEGSEDSEEEEEL
//
ID  Q9E6Q6;
PN  Envelope glycoprotein M;
GN  gM;
OS  10389;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q9E6Q6;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MASRARMERNYRGLSHIDYVHKKMWVVQAVCFGIAVLVFFGTLVAASINLTEGFPCFFAAVVDYRTVNTTLVHTGLTYPR
SQ  LGGVVPVLFFQTKAVVFFFYATSIVFVFLVCYITVGAIISSKKHVGAAYMGSGAFVFSLMASPLTILLGTVSIWLLQAVV
SQ  IVLAHKLIVLAAAVYLVHFSTITFFYGYFCGRGVDSKVYAEDISSAKDIDGSLHKLIGNVRAMMVNLLSIVYSIILIMSS
SQ  LMFGMLLANSFTLKFWHVIVTVLITTSVLTLIYLLVIEFLIARYVHIILGAYIGLLIGYGMLWTTTCDYVNRFYYAMGAN
SQ  ASNLRIACHSVLAVFTVLILLAMVVRLIRASLYHRRRSTRAYAKAMKLQQNVKHRLRQLRRSYKQRGSQSEDERALTQSR
SQ  SAEASDEDTIYDRVYSGSESEWDD
//
ID  P16733;
PN  Envelope glycoprotein M;
GN  gM;
OS  10360;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000305|PubMed:11090188}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000305|PubMed:11090188}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP- Rule:MF_04035, ECO:0000305|PubMed:11090188}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000305|PubMed:11090188}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000305|PubMed:11090188}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P16733;
DR  UNIPROT: Q7M6T7;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:11090188, ECO:0000269|PubMed:15681419, ECO:0000269|PubMed:19761540}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MAPSHVDKVNTRTWSASIVFMVLTFVNVSVHLVLSNFPHLGYPCVYYHVVDFERLNMSAYNVMHLHTPMLFLDSVQLVCY
SQ  AVFMQLVFLAVTIYYLVCWIKISMRKDKGMSLNQSTRDISYMGDSLTAFLFILSMDTFQLFTLTMSFRLPSMIAFMAAVH
SQ  FFCLTIFNVSMVTQYRSYKRSLFFFSRLHPKLKGTVQFRTLIVNLVEVALGFNTTVVAMALCYGFGNNFFVRTGHMVLAV
SQ  FVVYAIISIIYFLLIEAVFFQYVKVQFGYHLGAFFGLCGLIYPIVQYDTFLSNEYRTGISWSFGMLFFIWAMFTTCRAVR
SQ  YFRGRGSGSVKYQALATASGEEVAVLSHHDSLESRRLREEEDDDDDEDFEDA
//
ID  Q6SW43;
PN  Envelope glycoprotein M;
GN  gM;
OS  295027;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q6SW43;
DR  UNIPROT: D2K3Q7;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0005886;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MAPSHVDKVNTRTWSASIVFMVLTFVNVSVHLVLSNFPHLGYPCVYYHVVDFERLNMSAYNVMHLHTPMLFLDSVQLVCY
SQ  AVFMQLVFLAVTIYYLVCWIKISMRKDKGMSLNQSTRDISYMGDSLTAFLFILSMDTFQLFTLTMSFRLPSMIAFMAAVH
SQ  FFCLTIFNVSMVTQYRSYKRSLFFFSRLHPKLKGTVQFRTLIVNLVEVALGFNTTVVAMALCYGFGNNFFVRTGHMVLAV
SQ  FVVYAIISIIYFLLIEAVFFQYVKVQFGYHLGAFFGLCGLIYPIVQYDTFLSNEYRTGISWSFGMLFFIWAMFTTCRAVR
SQ  YFRGRGSGSVKYQALATASGEEVAALSHHDSLESRRLREEEDDDDEDFEDA
//
ID  P04288;
PN  Envelope glycoprotein M;
GN  gM;
OS  10299;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:26999189}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:17079321}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:17079321}.
DR  UNIPROT: P04288;
DR  UNIPROT: B9VQD7;
DR  UNIPROT: Q09IC3;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:26999189}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MGRPAPRGSPDSAPPTKGMTGARTAWWVWCVQVATFVVSAVCVTGLLVLASVFRARFPCFYATASSYAGVNSTAEVRGGV
SQ  AVPLRLDTQSLVGTYVITAVLLLAVAVYAVVGAVTSRYDRALDAGRRLAAARMAMPHATLIAGNVCSWLLQITVLLLAHR
SQ  ISQLAHLVYVLHFACLVYFAAHFCTRGVLSGTYLRQVHGLMELAPTHHRVVGPARAVLTNALLLGVFLCTADAAVSLNTI
SQ  AAFNFNFSAPGMLICLTVLFAILVVSLLLVVEGVLCHYVRVLVGPHLGAVAATGIVGLACEHYYTNGYYVVETQWPGAQT
SQ  GVRVALALVAAFALGMAVLRCTRAYLYHRRHHTKFFMRMRDTRHRAHSALKRVRSSMRGSRDGRHRPAPGSPPGIPEYAE
SQ  DPYAISYGGQLDRYGDSDGEPIYDEVADDQTDVLYAKIQHPRHLPDDDPIYDTVGGYDPEPAEDPVYSTVRRW
//
ID  P89433;
PN  Envelope glycoprotein M;
GN  gM;
OS  10315;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P89433;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MGRRAPRGSPEAAPGADVAPGARAAWWVWCVQVATFIVSAICVVGLLVLASVFRDRFPCLYAPATSYAKANATVEVRGGV
SQ  AVPLRLDTQSLLATYAITSTLLLAAAVYAAVGAVTSRYERALDAARRLAAARMAMPHATLIAGNVCAWLLQITVLLLAHR
SQ  ISQLAHLIYVLHFACLVYLAAHFCTRGVLSGTYLRQVHGLIDPAPTHHRIVGPVRAVMTNALLLGTLLCTAAAAVSLNTI
SQ  AALNFNFSAPSMLICLTTLFALLVVSLLLVVEGVLCHYVRVLVGPHLGAIAATGIVGLACEHYHTGGYYVVEQQWPGAQT
SQ  GVRVALALVAAFALAMAVLRCTRAYLYHRRHHTKFFVRMRDTRHRAHSALRRVRSSMRGSRRGGPPGDPGYAETPYASVS
SQ  HHAEIDRYGDSDGDPIYDEVAPDHEAELYARVQRPGPVPDAEPIYDTVEGYAPRSAGEPVYSTVRRW
//
ID  Q04630;
PN  Envelope glycoprotein M;
GN  gM;
OS  10370;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q04630;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MASSRVDTINLRIWLVSIICAALSFINVTVYLIAINFPNLGFPCAYFEINDLKAVNLSANNQIYQMTHQLYINPVQIICY
SQ  VLIMAMLFLLIIIYYIVCCAKVFSSNKTSNVNQTTRDITWMGDTSSCFQFILIMDTFQLFVTALSFRLVALGAFAYCIFF
SQ  VCFTTFNVTLITQFQSADKSFFAFQKIHPNLKGTVQFKTVVINLTELMLGYSTMFLGITTCLGVGNSIYIRSITVAYSSI
SQ  NTFLVMACIYSIVIEAVLVRYVKPLFGYYVGMFCGAVGLSFPILQYETFFESEWSTGLIINLAVIAIISIGFIICRLVRY
SQ  LVKKKRRYKQLVNTESSSLMDENE
//
ID  P52449;
PN  Envelope glycoprotein M;
GN  gM;
OS  36351;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P52449;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MASSRVDTINLRIWLVSIICAALSFINVTVHLIAINFPNLGFPCAYFEINDLKAVNLSANNEIYQMTHQLYINPVQIICY
SQ  VLIMAILFLLIIIYYIVCCAKVFSSNKTSNVNQTTRDITWMGDTSSCFQFILIMDTFQLFVTALSFRLVALGAFAYSIFF
SQ  VCFTTFNVTLITQFQSADKSFFAFQKIHPNLKGTVQFKTVVINLSELMLGYSTMFLGITTCLGVGNSIYIRSITVAFSSI
SQ  NTFLVMACIYSIVIEAVLVRYVKPLFGYYVGMFCGAVGLSFPILQYETFFESEWSTGLIINLSVVAIISIGFIICRLVRY
SQ  LVKKKRRYKQLLNAESSSLMDENE
//
ID  P52372;
PN  Envelope glycoprotein M;
GN  gM;
OS  57278;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P52372;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MALSRVDVINMRIWVLSIICACLTYVNVTVHLVAVHFPNLGFPCAYYEINDMKAINLSIRNDIRSLTPQLYLNPIQLICY
SQ  VVFMDICFFFILVYYIVCCVKVFSSEKTPNINQSTRDITWMGDSLSCFQFVLTMDTYQFFVTCLSFRLVTLAAFTYCLFF
SQ  ICFTAFTLTMITQYQSSERSFFVLKRIHPKLKGTIKYKTIIINMIELMLGFSSMVFAITICLGLGNNFYIKSSTVAFASI
SQ  NTFFVMSFVYSLVIELILHQYVKVQFGLHFGILFGILGLTYPILKYDSLFKTEWTVKFIVNLAVITIVCLSFIICRLIRF
SQ  FMRKHHNYKKLPTTVEDLDVLEEANE
//
ID  F5HDD0;
PN  Envelope glycoprotein M;
GN  gM;
OS  868565;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP- Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035, ECO:0000269|PubMed:12771417}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: F5HDD0;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MRASKSDRFLMSSWVKLLFVAVIMYICSAVVPMAATYEGLGFPCYFNNLVNYSALNLTVRNSAKHLTPTLFLEKPEMLVY
SQ  IFWTFIVDGIAIVYYCLAAVAVYRAKHVHATTMMSMQSWIALLGSHSVLYVAILRMWSMQLFIHVLSYKHVLMAAFVYCI
SQ  HFCISFAHIQSLITCNSAQWEIPLLEQHVPDNTMMESLLTRWKPVCVNLYLSTTALEMLLFSLSTMMAVGNSFYVLVSDA
SQ  IFGAVNMFLALTVVWYINTEFFLVKFMRRQVGFYVGVFVGYLILLLPVIRYENAFVQANLHYIVAINISCIPILCILAIV
SQ  IRVIRSDWGLCTPSAAYMPLATSAPTVDRTPTVHQKPPPLPAKTRARAKVKDISTPAPRTQYQSDHESDSEIDETQMIFI
//
ID  P52373;
PN  Envelope glycoprotein M;
GN  gM;
OS  69156;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P52373;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: No;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MAKAGVMTLSHVDRMNLRTWTMAIACCLLSFVNIVVFSVAAHFPGIGFPCYYPRIIDFDNMNLTMYNAIHHLTPQLFLDP
SQ  VQLIVYVIFTELIFFCVLSYYIVCWVQIYFRSEHGTQVNQSTRDINFMGDSATCFTFVLTMDTFQIFLLSLSFRLPSMVA
SQ  FSKCMYFMCLTAFVVTLVTHYESRERSAFALSKIHPKLQGTIRYRTAVVNLTQLILGFATMVLAMSLALGFGNSFFVKTA
SQ  HVVFGAMVAFAIVACVYFSIIESVLSRYMKVQFGYHIGTILGVCGAMYPIIRYEALNASSYARDINIGITVLLLLCVAFS
SQ  VIRTVRFLLRRNKRYRALALDNEEIRALRSDAE
//
ID  Q6UDH4;
PN  Envelope glycoprotein M;
GN  gM;
OS  670426;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q6UDH4;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MGNYYYGGQESRLERISWRMWMVEAACYIVLVLLTLVSSFASLSSTTGFPCFVGTVGESSFGGDLMGHGMTPARRDGVKI
SQ  FFMSSPSTLFVVFSAVFVWLVVAVYLLLGGVRVKMCNFDSSYGASELSSAVATMTSLVTLSITAWAWQVFVLMLSYRQLT
SQ  LAAVAFVGIFIAGLVFMLSFASGGKSPENYATFNSQLKTVCKDVHAVITAFKAVVLNLFCVVFGVWHLMLVMLGAVIMVL
SQ  NFGVSIPKATTGALVVFIVLGLVYLMMIELVVSRYVHVLLGPHLGMIIALGIAGTSALSYAETLDEIMYASWKPVAAGIL
SQ  GAFSVIVLALAVLRAVRSYKFHKAAQSKFLQQVASVAQTVKNRARRERNGPRVHKRYYDAVPVDAYEDDPYRQSPRRSRH
SQ  GEAEDVIYENMKY
//
ID  Q01017;
PN  Envelope glycoprotein M;
GN  gM;
OS  10383;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q01017;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MMKASRSDTFMLRTWIQLLVLFVIMFIMSAILPIAASVEGLGFPCYFPNLVDYSLLNLTLRNAAKHLTPTLFLEAPELFV
SQ  YITWSVLVDLASAIYYVVGALAILQARKTHLTSMITLQTWINLVGSHTMLFIGIARMWTLQLFIHVLSYKHVMLAAFIYF
SQ  LHFCLSYMHTLSLVSRNSPKWSVLLMEQHIPKQSLLSTILDYGKPLCVNMYLSLLALEMLVFSLGFMMAIGNSFYILVSD
SQ  TVLASINLYFVLTTFWYMMTEMFLQDYLKLQFGFYLGVFSGSLILLLPVLRYEAVFVSANLHKTVAVNIAMIPAMCVIAM
SQ  MFRLFRYSQQVRKPENSYTPLPKRFKKRRQKQDQQLIMVETSDEEL
//
ID  Q85041;
PN  Envelope glycoprotein M;
GN  gM;
OS  33703;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q85041;
DR  UNIPROT: Q5PP86;
DR  UNIPROT: Q85042;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: No;
DE  Interaction: A0A142I9X8; IntAct: EBI-11701393; Score: 0.35
DE  Interaction: Q8QXN7; IntAct: EBI-11689133; Score: 0.37
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0019068;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MCGPRNAEAVSWRSWLIEVCGFALAALTLVLTLIFASLPEMGFPCFYATVADYDTLNDTSGGVWTRQPLVAPALFLETPT
SQ  VTSFFGFTATVLLAHALYAVAGAVVLRREAGRLAFQPSVVLYAASTVAAPGTLMLGALCAWTLQAVVLLMAHKQAGLAAA
SQ  AYITHFVFLALFGACHACKGTGDVRAALAASPPLRRVAVHARAVVTNVVLGAVGLGAAVVGLMLGVLLANSFHISLWKTA
SQ  EAALAVFTLLALALMVFVEVVVSGYVQVLPTPAFCVLVASAAFGVSAHRYFAKFSEALGETHGVVIGTRAVLAVLSLIAL
SQ  AMIVVRLVRACIAHRARGSRFYANVDKARTTARRYLQKRLHGRGNDEYLLAPGSGDDEFDDGDEVVYENLGFE
//
ID  P09298;
PN  Envelope glycoprotein M;
GN  gM;
OS  10338;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: P09298;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MGTQKKGPRSEKVSPYDTTTPEVEALDHQMDTLNWRIWIIQVMMFTLGAVMLLATLIAASSEYTGIPCFYAAVVDYELFN
SQ  ATLDGGVWSGNRGGYSAPVLFLEPHSVVAFTYYTALTAMAMAVYTLITAAIIHRETKNQRVRQSSGVAWLVVDPTTLFWG
SQ  LLSLWLLNAVVLLLAYKQIGVAATLYLGHFATSVIFTTYFCGRGKLDETNIKAVANLRQQSVFLYRLAGPTRAVFVNLMA
SQ  ALMAICILFVSLMLELVVANHLHTGLWSSVSVAMSTFSTLSVVYLIVSELILAHYIHVLIGPSLGTLVACATLGTAAHSY
SQ  MDRLYDPISVQSPRLIPTTRGTLACLAVFSVVMLLLRLMRAYVYHRQKRSRFYGAVRRVPERVRGYIRKVKPAHRNSRRT
SQ  NYPSQGYGYVYENDSTYETDREDELLYERSNSGWE
//
ID  Q77NP2;
PN  Envelope glycoprotein M;
GN  gM;
OS  341980;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Virion membrane {ECO:0000255|HAMAP- Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
DR  UNIPROT: Q77NP2;
DR  Pfam: PF01528;
DE  Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:17977964}.
DE  Reference Proteome: No;
DE  Interaction: Q6QCN0; IntAct: EBI-7927240; Score: 0.37
DE  Interaction: Q6QCM8; IntAct: EBI-7927258; Score: 0.37
DE  Interaction: Q77NP2; IntAct: EBI-7927293; Score: 0.55
DE  Interaction: Q71S71; IntAct: EBI-7927311; Score: 0.37
DE  Interaction: Q8AZM1; IntAct: EBI-7927329; Score: 0.55
DE  Interaction: Q4JQV0; IntAct: EBI-2533294; Score: 0.00
DE  Interaction: Q4JQU8; IntAct: EBI-2533670; Score: 0.00
DE  Interaction: Q0Q8R5; IntAct: EBI-2533782; Score: 0.00
DE  Interaction: Q4JQT6; IntAct: EBI-2534359; Score: 0.00
DE  Interaction: Q77NN8; IntAct: EBI-2534791; Score: 0.00
DE  Interaction: Q77NN5; IntAct: EBI-2534975; Score: 0.00
DE  Interaction: P0C764; IntAct: EBI-2535168; Score: 0.00
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0055036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04035};
SQ  MGTQKKGPRSEKVSPYDTTTPEVEALDHQMDTLNWRIWIIQVMMFTLGAVMLLATLIAASSEYTGIPCFYAAVVDYELFN
SQ  ATLDGGVWSGNRGGYSAPVLFLEPHSVVAFTYYTALTAMAMAVYTLITAAIIHRETKNQRVRQSSGVAWLVVDPTTLFWG
SQ  LLSLWLLNAVVLLLAYKQIGVAATLYLGHFATSVIFTTYFCGRGKLDETNIKAVANLRQQSVFLYRLAGPTRAVFVNLMA
SQ  ALMAICILFVSLMLELVVANHLHTGLWSSVSVAMSTFSTLSVVYLIVSELILAHYIHVLIGPSLGTLVACATLGTAAHSY
SQ  MDRLYDPISVQSPRLIPTTRGTLACLAVFSVVMLLLRLMRAYVYHRQKRSRFYGAVRRVPERVRGYIRKVKPAHRNSRRT
SQ  NYPSQGYGYVYENDSTYETDREDELLYERSNSGWE
//
ID  Q28294;
PN  Guanine nucleotide-binding protein G(q) subunit alpha;
GN  GNAQ;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P50148}; Lipid-anchor {ECO:0000250|UniProtKB:P50148}. Golgi apparatus {ECO:0000250|UniProtKB:P50148}. Nucleus {ECO:0000250|UniProtKB:P21279}. Nucleus membrane {ECO:0000250|UniProtKB:P21279}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:P21279}.
DR  UNIPROT: Q28294;
DR  Pfam: PF00503;
DR  PROSITE: PS51882;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Required for platelet activation. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long- chain fatty acids (LCFAs) (By similarity). Together with GNA11, required for heart development (By similarity). {ECO:0000250|UniProtKB:P21279, ECO:0000250|UniProtKB:P50148}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0005834;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0001750;
GO  GO:0045202;
GO  GO:0001664;
GO  GO:0031683;
GO  GO:0005525;
GO  GO:0005096;
GO  GO:0003924;
GO  GO:0046872;
GO  GO:0001508;
GO  GO:0007189;
GO  GO:0007188;
GO  GO:0009649;
GO  GO:0007213;
GO  GO:0007215;
GO  GO:0007603;
GO  GO:0010543;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P21279};
SQ  MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVY
SQ  QNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYY
SQ  LNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
SQ  ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS
SQ  DKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
//
ID  P50148;
PN  Guanine nucleotide-binding protein G(q) subunit alpha;
GN  GNAQ;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:19001095}; Lipid-anchor {ECO:0000269|PubMed:19001095}. Golgi apparatus {ECO:0000269|PubMed:19001095}. Nucleus {ECO:0000250|UniProtKB:P21279}. Nucleus membrane {ECO:0000250|UniProtKB:P21279}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:P21279}.
DR  UNIPROT: P50148;
DR  UNIPROT: O15108;
DR  UNIPROT: Q13462;
DR  UNIPROT: Q6NT27;
DR  UNIPROT: Q92471;
DR  UNIPROT: Q9BZB9;
DR  PDB: 6VU5;
DR  PDB: 7EZM;
DR  PDB: 7F6H;
DR  PDB: 7F6I;
DR  PDB: 7F8W;
DR  Pfam: PF00503;
DR  PROSITE: PS51882;
DR  OMIM: 163000;
DR  OMIM: 185300;
DR  OMIM: 600998;
DR  DisGeNET: 2776;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Required for platelet activation. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long- chain fatty acids (LCFAs) (PubMed:27852822). Together with GNA11, required for heart development (By similarity). {ECO:0000250|UniProtKB:P21279, ECO:0000269|PubMed:27852822}.
DE  Disease: Capillary malformations, congenital (CMC) [MIM:163000]: A form of vascular malformations that are present from birth, tend to grow with the individual, do not regress spontaneously, and show normal rates of endothelial cell turnover. Capillary malformations are distinct from capillary hemangiomas, which are highly proliferative lesions that appear shortly after birth and show rapid growth, slow involution, and endothelial hypercellularity. {ECO:0000269|PubMed:23656586}. Note=The disease is caused by variants affecting the gene represented in this entry. Sturge-Weber syndrome (SWS) [MIM:185300]: A syndrome characterized by an intracranial vascular anomaly, leptomeningeal angiomatosis, most often involving the occipital and posterior parietal lobes. The most common features are facial cutaneous vascular malformations (port-wine stains), seizures, and glaucoma. Stasis results in ischemia underlying the leptomeningeal angiomatosis, leading to calcification and laminar cortical necrosis. The clinical course is highly variable and some children experience intractable seizures, intellectual disability, and recurrent stroke-like episodes. {ECO:0000269|PubMed:23656586}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P32302; IntAct: EBI-7276612; Score: 0.40
DE  Interaction: P30556; IntAct: EBI-7409738; Score: 0.40
DE  Interaction: P51884; IntAct: EBI-3909602; Score: 0.37
DE  Interaction: P50897; IntAct: EBI-3909621; Score: 0.37
DE  Interaction: Q9H0P0; IntAct: EBI-3918371; Score: 0.37
DE  Interaction: Q8IWW8; IntAct: EBI-3923179; Score: 0.37
DE  Interaction: Q9UGN5; IntAct: EBI-7055495; Score: 0.44
DE  Interaction: P10276; IntAct: EBI-6249283; Score: 0.56
DE  Interaction: Q14254; IntAct: EBI-6249310; Score: 0.35
DE  Interaction: P49407; IntAct: EBI-8309016; Score: 0.52
DE  Interaction: P16284; IntAct: EBI-9984652; Score: 0.40
DE  Interaction: Q61879; IntAct: EBI-11041929; Score: 0.35
DE  Interaction: Q6DN90; IntAct: EBI-11896524; Score: 0.40
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q96QD9; IntAct: EBI-21501187; Score: 0.35
DE  Interaction: Q13503; IntAct: EBI-21501670; Score: 0.35
DE  Interaction: Q53EQ6; IntAct: EBI-21523123; Score: 0.35
DE  Interaction: P21453; IntAct: EBI-21539478; Score: 0.35
DE  Interaction: Q9NRW4; IntAct: EBI-21542541; Score: 0.35
DE  Interaction: P09067; IntAct: EBI-21543288; Score: 0.35
DE  Interaction: Q9NT62; IntAct: EBI-21549217; Score: 0.35
DE  Interaction: Q9UHK0; IntAct: EBI-21549449; Score: 0.35
DE  Interaction: O95136; IntAct: EBI-21551126; Score: 0.35
DE  Interaction: Q6PEY0; IntAct: EBI-21551307; Score: 0.35
DE  Interaction: Q8N5S1; IntAct: EBI-21587332; Score: 0.35
DE  Interaction: Q16854; IntAct: EBI-21603108; Score: 0.35
DE  Interaction: Q9NVR5; IntAct: EBI-21603625; Score: 0.35
DE  Interaction: P02675; IntAct: EBI-21646531; Score: 0.35
DE  Interaction: Q8TAG9; IntAct: EBI-21673041; Score: 0.35
DE  Interaction: Q92845; IntAct: EBI-21702814; Score: 0.35
DE  Interaction: Q96S94; IntAct: EBI-21750627; Score: 0.35
DE  Interaction: Q8NFB2; IntAct: EBI-21757603; Score: 0.35
DE  Interaction: Q6ZNA4; IntAct: EBI-21806464; Score: 0.35
DE  Interaction: Q86VZ1; IntAct: EBI-21809853; Score: 0.35
DE  Interaction: Q86Z23; IntAct: EBI-21814288; Score: 0.35
DE  Interaction: Q9UN70; IntAct: EBI-21824946; Score: 0.35
DE  Interaction: P63215; IntAct: EBI-21830507; Score: 0.35
DE  Interaction: P50150; IntAct: EBI-21830434; Score: 0.35
DE  Interaction: Q96AZ6; IntAct: EBI-21849278; Score: 0.35
DE  Interaction: Q9NYW3; IntAct: EBI-21852327; Score: 0.35
DE  Interaction: Q7Z698; IntAct: EBI-21860016; Score: 0.35
DE  Interaction: Q8TCI5; IntAct: EBI-21862131; Score: 0.35
DE  Interaction: Q8N446; IntAct: EBI-21872004; Score: 0.35
DE  Interaction: Q7RTX9; IntAct: EBI-21871985; Score: 0.35
DE  Interaction: Q8R455; IntAct: EBI-15993574; Score: 0.59
DE  Interaction: Q969F8; IntAct: EBI-21282286; Score: 0.40
DE  Interaction: P60033; IntAct: EBI-25645944; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25686340; Score: 0.35
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0005834;
GO  GO:0005765;
GO  GO:0031965;
GO  GO:0001750;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0001664;
GO  GO:0031683;
GO  GO:0005525;
GO  GO:0005096;
GO  GO:0003924;
GO  GO:0046872;
GO  GO:0001508;
GO  GO:0007202;
GO  GO:0007189;
GO  GO:0007188;
GO  GO:0007596;
GO  GO:0009649;
GO  GO:0007213;
GO  GO:0007215;
GO  GO:0006469;
GO  GO:0007603;
GO  GO:0050821;
GO  GO:0060828;
GO  GO:0010543;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P21279};
SQ  MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVY
SQ  QNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYY
SQ  LNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
SQ  ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS
SQ  DKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
//
ID  P21279;
PN  Guanine nucleotide-binding protein G(q) subunit alpha;
GN  Gnaq;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:19001095}; Lipid-anchor {ECO:0000269|PubMed:19001095}. Golgi apparatus {ECO:0000250|UniProtKB:P50148}. Nucleus {ECO:0000269|PubMed:18802028}. Nucleus membrane {ECO:0000269|PubMed:18802028}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000269|PubMed:18802028}.
DR  UNIPROT: P21279;
DR  UNIPROT: Q6PFF5;
DR  PDB: 2BCJ;
DR  PDB: 2RGN;
DR  PDB: 3AH8;
DR  PDB: 4EKC;
DR  PDB: 4EKD;
DR  PDB: 4GNK;
DR  PDB: 4QJ3;
DR  PDB: 4QJ4;
DR  PDB: 4QJ5;
DR  PDB: 5DO9;
DR  PDB: 7SQ2;
DR  Pfam: PF00503;
DR  PROSITE: PS51882;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (PubMed:9687499). Required for platelet activation (PubMed:9296496). Regulates B-cell selection and survival and is required to prevent B- cell-dependent autoimmunity (PubMed:20624888). Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (PubMed:17938235). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (By similarity). Together with GNA11, required for heart development (PubMed:9687499). {ECO:0000250|UniProtKB:P50148, ECO:0000269|PubMed:17938235, ECO:0000269|PubMed:20624888, ECO:0000269|PubMed:9296496, ECO:0000269|PubMed:9687499}.
DE  Reference Proteome: Yes;
DE  Interaction: O08915; IntAct: EBI-6979702; Score: 0.52
DE  Interaction: P11416; IntAct: EBI-6259164; Score: 0.27
DE  Interaction: P08587; IntAct: EBI-8071193; Score: 0.44
DE  Interaction: O54912; IntAct: EBI-15571558; Score: 0.40
DE  Interaction: Q9ES08; IntAct: EBI-15571606; Score: 0.40
DE  Interaction: Q01970; IntAct: EBI-15939025; Score: 0.75
DE  Interaction: Q8R4D5; IntAct: EBI-15993510; Score: 0.40
DE  Interaction: P41220; IntAct: EBI-16037484; Score: 0.62
DE  Interaction: Q3UHD9; IntAct: EBI-16736255; Score: 0.35
DE  Interaction: P62871; IntAct: EBI-21282654; Score: 0.27
DE  Interaction: P63278; IntAct: EBI-22091990; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-26960892; Score: 0.35
DE  Interaction: P16056; IntAct: EBI-27112678; Score: 0.35
GO  GO:0005901;
GO  GO:0044297;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005794;
GO  GO:0005834;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0047391;
GO  GO:0001664;
GO  GO:0031683;
GO  GO:0005525;
GO  GO:0005096;
GO  GO:0003924;
GO  GO:0046872;
GO  GO:0044877;
GO  GO:0001508;
GO  GO:0007202;
GO  GO:0007189;
GO  GO:0007188;
GO  GO:1904888;
GO  GO:0048066;
GO  GO:0042733;
GO  GO:0086100;
GO  GO:0021884;
GO  GO:0007186;
GO  GO:0007215;
GO  GO:0007507;
GO  GO:0042711;
GO  GO:0010259;
GO  GO:0043066;
GO  GO:0043267;
GO  GO:0006469;
GO  GO:0016322;
GO  GO:0060158;
GO  GO:0007200;
GO  GO:0048661;
GO  GO:0009791;
GO  GO:0050821;
GO  GO:0008217;
GO  GO:0060828;
GO  GO:0045634;
GO  GO:0010543;
GO  GO:0001501;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8227063};
SQ  MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVY
SQ  QNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYY
SQ  LNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
SQ  ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS
SQ  DKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
//
ID  Q2PKF4;
PN  Guanine nucleotide-binding protein G(q) subunit alpha;
GN  GNAQ;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P50148}; Lipid-anchor {ECO:0000250|UniProtKB:P50148}. Golgi apparatus {ECO:0000250|UniProtKB:P50148}. Nucleus {ECO:0000250|UniProtKB:P21279}. Nucleus membrane {ECO:0000250|UniProtKB:P21279}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:P21279}.
DR  UNIPROT: Q2PKF4;
DR  Pfam: PF00503;
DR  PROSITE: PS51882;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Required for platelet activation. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long- chain fatty acids (LCFAs) (By similarity). Together with GNA11, required for heart development (By similarity). {ECO:0000250|UniProtKB:P21279, ECO:0000250|UniProtKB:P50148}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0005834;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0001750;
GO  GO:0045202;
GO  GO:0001664;
GO  GO:0031683;
GO  GO:0005525;
GO  GO:0005096;
GO  GO:0003924;
GO  GO:0046872;
GO  GO:0001508;
GO  GO:0007189;
GO  GO:0007188;
GO  GO:0009649;
GO  GO:0007213;
GO  GO:0007215;
GO  GO:0006469;
GO  GO:0007603;
GO  GO:0050821;
GO  GO:0060828;
GO  GO:0010543;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P21279};
SQ  MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVY
SQ  QNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYY
SQ  LNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
SQ  ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS
SQ  DKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
//
ID  P82471;
PN  Guanine nucleotide-binding protein G(q) subunit alpha;
GN  Gnaq;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P50148}; Lipid-anchor {ECO:0000250|UniProtKB:P50148}. Golgi apparatus {ECO:0000250|UniProtKB:P50148}. Nucleus {ECO:0000250|UniProtKB:P21279}. Nucleus membrane {ECO:0000250|UniProtKB:P21279}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:P21279}.
DR  UNIPROT: P82471;
DR  Pfam: PF00503;
DR  PROSITE: PS51882;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Required for platelet activation. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long- chain fatty acids (LCFAs) (By similarity). Together with GNA11, required for heart development (By similarity). {ECO:0000250|UniProtKB:P21279, ECO:0000250|UniProtKB:P50148}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5XIE8; IntAct: EBI-26438079; Score: 0.35
GO  GO:0005901;
GO  GO:0044297;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005794;
GO  GO:0005834;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0047391;
GO  GO:0001664;
GO  GO:0031683;
GO  GO:0005525;
GO  GO:0005096;
GO  GO:0003924;
GO  GO:0046872;
GO  GO:0044877;
GO  GO:0001508;
GO  GO:0007202;
GO  GO:0007189;
GO  GO:0007188;
GO  GO:1904888;
GO  GO:0048066;
GO  GO:0042733;
GO  GO:0086100;
GO  GO:0021884;
GO  GO:0007186;
GO  GO:0007215;
GO  GO:0007507;
GO  GO:0042711;
GO  GO:0010259;
GO  GO:0043066;
GO  GO:0043267;
GO  GO:0006469;
GO  GO:0016322;
GO  GO:0060158;
GO  GO:0007200;
GO  GO:0048661;
GO  GO:0009791;
GO  GO:0050821;
GO  GO:0008217;
GO  GO:0060828;
GO  GO:0045634;
GO  GO:0010543;
GO  GO:0001501;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P21279};
SQ  MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVY
SQ  QNIFTAMQAMVRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYY
SQ  LNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
SQ  ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS
SQ  DKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
//
ID  P38410;
PN  Guanine nucleotide-binding protein G(q) subunit alpha;
GN  gnaq;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P50148}; Lipid-anchor {ECO:0000250|UniProtKB:P50148}. Golgi apparatus {ECO:0000250|UniProtKB:P50148}. Nucleus {ECO:0000250|UniProtKB:P21279}. Nucleus membrane {ECO:0000250|UniProtKB:P21279}.
DR  UNIPROT: P38410;
DR  Pfam: PF00503;
DR  PROSITE: PS51882;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. {ECO:0000250|UniProtKB:P50148}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0001750;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0001664;
GO  GO:0031683;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0046872;
GO  GO:0009649;
GO  GO:0007213;
GO  GO:0007603;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P21279};
SQ  MTLESIMACCLSEEAEEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVY
SQ  QNIFSAMQAMIRAMETLKIPYKYEHNKGHALLVREVDVEKVASFENPYVDAIKYLWNDPGIQECYDRRREYQLSDSTKYY
SQ  LNDLDRIATHGYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
SQ  ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDS
SQ  DKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
//
ID  F4KHD8;
PN  Nuclear pore complex protein GP210;
GN  GB210;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4KHD8;
DR  UNIPROT: Q9FI62;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVPVSFCFFFLLLLLSAGESSSQLVSGPHITDVNILLPPKMKNPVEYRLQGSDGCFKWSWDHHDILSVTPEFNSSSHCST
SQ  SARLRSISPYSGRKETAVYATDIQTGMVIRCKVFIDNFSRIQIFHNSIKLDLDGLSMLRVRAFDNEDNEFSSLVGLQFIW
SQ  KLMPESGGSTHHLAHVPLKESPLTDCGGLCGYLDIQKKLEDSGVFADLFVVKGTKIGHEKVSVHLLEAPLTHIADEIVLT
SQ  VAEAMSLEPRSPVYVLMGASFGYTLKVMRGNVPQAVDLPSPHHRWSVLNSSVAQVDSLIGLTKALSLGVTTVVVEDTRVA
SQ  GHIQGSSINVVTPDTLILYISPWSMSGDLITESKPFPSSMHWYVVSGRQYLIQMKIFSGRPDAHEIYITETDDIKLYGKD
SQ  SDYWKIVSLPDELSSEYGQRNSRILNAISPGLGELTSTLTYFSGHQESKEVLKVVQEIRVCEKVQFTLNSEDDTPKVLLP
SQ  WTPAVYQEMELIVTGGCAKASSDYKWFTSDISILSVSAYGIIQAKRPGIATVKVVSTFDSQNFDEVIVEVSIPSSMVMLQ
SQ  NFPVETVVGSHLKAAVTMKALNGATFSRCDAFNSLIKWKTGSESFVIVNATSEMMMLDELRSMDSSPPCSRASIYTASTG
SQ  RTVLQATLAKEFHYFDKSLSESIDLKATLTIGAYLPLSVRQDSDGNHHGGYWFDKAQEETDFGVSKLYLVPGTYVDVMLL
SQ  GGPERWDDNVEFTETVKTLYEDEEDLTSRVNVHHEVDRRANMYRISCQKLGSYKLVFLRGNLLGIDHPVPAVAEALLSVH
SQ  CSLPSSVVLIVDEPVNKLDVIRAASQADRAPGRLRVTPVTVANGQIIRVAAVGISEFGEAFSNSSTLSLRWELTSCNNLA
SQ  YWDDDYNSKMTKSGWERFLALRNESGLCTVRATVSGIDYSFKSQYSTLLPQGSESTLTDAVRLQLVSTLRVTPEFNLVFF
SQ  NPNAKVNLSMTGGSCLWEAVVNNSRVAEVIRPPSGLQCSQMMLSPKGLGTTIVTVYDIGVSPPLSALALIKVADVDWIKI
SQ  ASGDEISIMEGSTHSIDLLTGIDDGMTFDSSQYSLMDIMVHIEDDLVEHVTVDEDSLSVGEHVATSSFKIAARRLGITTL
SQ  YVSARQQSGGKVLSQTIKVEVYSPPRLHPQGIFLVPGASYVLTIEGGPTMNVSVDYTTVDNEVAKIEKSGRLYATSPGNT
SQ  TIYATIYGSEGAVICQAIGNAEVGLPATAMLVAQSDTVAVGHEMPVSPSFPEGDLLSFYELCSAYKWTIEDEKVLIFIAS
SQ  SINVEENAGFVNVVQGRSAGKTRVTIAFSCDFVSPGLYSESRTYEASMILSVVPDLPLSLGAPMTWVLPPFYTSSGLLPS
SQ  SSEPQKHRDGQSHRGNIVYSILKDCSSRADFERDTISINGGSVKTTDSNNVACIQAKDRTSGRIEIAACVRVAEVAQIRM
SQ  KSEGIPFHVIDLAVGGELELPINYYDTLGIPFLEAHGVTTYNVETNHRDVVFIKTVNDQPSAYIKGIKHGKALIRVSIGD
SQ  NLRKSDYVLVSVGAHIFPQNPVIHTGNLLNFSITGADNEVTGQWFTSNRSVISVNVASGQAKAISQGSTHVTFKGHGLKL
SQ  QTKVTVLFGNTIYVDSPGETLTNVHVPAEGYKFPVKFRENKFAVTEHGNKATFNCQVDPPFIGYTKPWMDLDTGNTYCLF
SQ  FPYSPEHLVHSMSITKDMKPHVSFSVDASLKEARRVSGSASALLIGGFSVTGPDKLNINPDSNTTIISLVGNTDVQIHCR
SQ  NKGRLSISLIKRDDFGIAGHAQYKVNVLRSEQFTDRIIITLPATGQIVEIDVCYDTGESLVASSKDGYSVLLKILWGVLV
SQ  LVVSVIILMKVIDRQVPTGATGTATYSGNAAQGTPERRSGTVIYHEESPRTPSPFMEYVKRTVDETPYYRREGRRRFNPQ
SQ  NTM
//
ID  Q86D96;
PN  Guanine nucleotide-binding protein subunit alpha-1;
GN  GA1;
OS  5722;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Endomembrane system; Lipid-anchor. Note=Predominantly perinuclear.
DR  UNIPROT: Q86D96;
DR  Pfam: PF00503;
DR  PROSITE: PS51882;
DE  Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0012505;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0031683;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0007186;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGCSASKPSEPSNAKLPSAPVPKKVEQVPEPKPEPQPQPEPQPQPEPPKPAEPAPAPAPAPEPQKPAEPAPKVVAVEDDT
SQ  NEAYGLLLCGAGESGKTTFTRQLKLRYLNGFNEKDCRDFLRTIRGNLVETMQLLLVWLEHNNIEIEDSELSSMAQDIIDV
SQ  DPQDCEFNEELVEKLKALWENEQIKKAFEHKDETAVPDHMPYFFAKIDELAGEDYIPSNEDVLRARIRSIGIEAITFDLQ
SQ  GARIRIFDVGGQKSERSKWANVMNQVEGVIFCVSFAEFDKPMFEDQNVLRINDSLEIFGNITHQEKFSNSPIFLVCNKFD
SQ  VFTEKIKNTDAFVKIFPEFSGDSHNPEACADYLIQRFLDKAAPLSEDRPIIQYKIVALNGDQVVETADAICKFISDKYYQ
SQ  DA
//
ID  B3G515;
PN  G-protein coupled estrogen receptor 1;
GN  gper1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:19228597}; Multi-pass membrane protein {ECO:0000269|PubMed:19228597}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalized with cadherin at the plasma membrane. {ECO:0000250}.
DR  UNIPROT: B3G515;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: Membrane G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Plays a role in the embryonic development of sensory and motor neurons. Specifically induces apoptosis and reduces proliferation of brain cells. Involved in maintenance of meiotic arrest in oocytes. {ECO:0000269|PubMed:18420744, ECO:0000269|PubMed:19228597, ECO:0000269|PubMed:23583372}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0016323;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0032591;
GO  GO:0005769;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0055037;
GO  GO:0004930;
GO  GO:0030284;
GO  GO:0005496;
GO  GO:1990239;
GO  GO:0006915;
GO  GO:0007420;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0071392;
GO  GO:0060047;
GO  GO:0051447;
GO  GO:0043524;
GO  GO:1900194;
GO  GO:0040019;
GO  GO:2000179;
GO  GO:0001934;
GO  GO:0045944;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEEQTTNVIQIYVNGTEQFNASFDFNITDVKESTDTYEFYIIGLFLSCLYTIFLFPIGFIGNILILVVNLNHRERMTIPD
SQ  LYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYVALTSSMSSSPLRTMQHAK
SQ  LSCSLIWMASILATLLPFTIVQTQHTGEVHFCFANVFEIQWLEVTIGFLIPFSIIGLCYSLIVRTLMRAQKHKGLWPRRQ
SQ  KALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSKRTDTTLWHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKL
SQ  RLFIKRKASWSVVYRFCNHTLDLQIPVRSESEV
//
ID  Q99527;
PN  G-protein coupled estrogen receptor 1;
GN  GPER1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Early endosome. Recycling endosome. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18566127}; Multi-pass membrane protein. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalized with BSN to the active zone of presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal synaptosomes (By similarity). Endocytosed in a agonist- and arrestin-independent manner. Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane. Colocalized with transferrin receptor at the plasma membrane and perinuclear region. Accumulated and colocalized with RAB11 proteins in recycling endosomes and trans-Golgi network (TGN), but does neither recycle back to the cell surface nor traffics to late endosome or lysosome. Colocalized with calnexin in the endoplasmic reticulum. Traffics to intracellular sites via cytokeratin intermediate filaments like KRT7 and KRT8 after constitutive endocytosis in epithelial cells. Colocalized with EGFR in the nucleus of agonist-induced cancer-associated fibroblasts (CAF). {ECO:0000250}.
DR  UNIPROT: Q99527;
DR  UNIPROT: A8K6C5;
DR  UNIPROT: B5BUJ1;
DR  UNIPROT: O00143;
DR  UNIPROT: O43494;
DR  UNIPROT: Q13631;
DR  UNIPROT: Q6FHL1;
DR  UNIPROT: Q96F42;
DR  UNIPROT: Q99981;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  OMIM: 601805;
DR  DisGeNET: 2852;
DE  Function: G-protein coupled estrogen receptor that binds to 17-beta- estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells. {ECO:0000269|PubMed:11043579, ECO:0000269|PubMed:15539556, ECO:0000269|PubMed:15705806, ECO:0000269|PubMed:19179659, ECO:0000269|PubMed:19342448, ECO:0000269|PubMed:20203690, ECO:0000269|PubMed:20551055, ECO:0000269|PubMed:21149639, ECO:0000269|PubMed:21242460, ECO:0000269|PubMed:21427217, ECO:0000269|PubMed:23135268, ECO:0000269|PubMed:23283935, ECO:0000269|PubMed:23285008, ECO:0000269|PubMed:23674134}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A6L7HHX2; IntAct: EBI-2833018; Score: 0.00
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043198;
GO  GO:0044327;
GO  GO:0032591;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0098686;
GO  GO:0005887;
GO  GO:0043231;
GO  GO:0045095;
GO  GO:0031966;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0048786;
GO  GO:0042734;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0003682;
GO  GO:0038054;
GO  GO:0004930;
GO  GO:0030284;
GO  GO:0005496;
GO  GO:1990239;
GO  GO:0007189;
GO  GO:0030263;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0071392;
GO  GO:0071333;
GO  GO:0071389;
GO  GO:0071375;
GO  GO:0071356;
GO  GO:0007186;
GO  GO:0006954;
GO  GO:0045087;
GO  GO:0030518;
GO  GO:0010948;
GO  GO:0008285;
GO  GO:0070373;
GO  GO:0045599;
GO  GO:0010629;
GO  GO:0050728;
GO  GO:0002695;
GO  GO:0051055;
GO  GO:0051898;
GO  GO:1904706;
GO  GO:0007399;
GO  GO:0019228;
GO  GO:0030264;
GO  GO:0043065;
GO  GO:2000724;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0043280;
GO  GO:0007204;
GO  GO:2000353;
GO  GO:0045742;
GO  GO:0070374;
GO  GO:2001238;
GO  GO:0045745;
GO  GO:0010628;
GO  GO:0032962;
GO  GO:0032024;
GO  GO:0043410;
GO  GO:0050769;
GO  GO:0001956;
GO  GO:0014068;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0090200;
GO  GO:0051281;
GO  GO:0045944;
GO  GO:0070474;
GO  GO:0051726;
GO  GO:0051480;
GO  GO:0043401;
GO  GO:0042311;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVTSQARGVGLEMYPGTAQPAAPNTTSPELNLSHPLLGTALANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILI
SQ  LVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHERYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALA
SQ  RAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRV
SQ  LVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLN
SQ  PLIYSFLGETFRDKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV
//
ID  F7EQ49;
PN  G-protein coupled estrogen receptor 1;
GN  GPER1;
OS  9544;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Endocytosed in a agonist- and arrestin-independent manner. Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane. Colocalized with transferrin receptor at the plasma membrane and perinuclear region. Accumulated and colocalized with RAB11 proteins in recycling endosomes and trans-Golgi network (TGN), but does neither recycle back to the cell surface nor traffics to late endosome or lysosome. Colocalized with calnexin in the endoplasmic reticulum. Traffics to intracellular sites via cytokeratin intermediate filaments like KRT7 and KRT8 after constitutive endocytosis in epithelial cells. Colocalized with EGFR in the nucleus of agonist-induced cancer- associated fibroblasts (CAF) (By similarity). Colocalized with BSN to the active zone of presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal synaptosomes (By similarity). {ECO:0000250}.
DR  UNIPROT: F7EQ49;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: G-protein coupled estrogen receptor that binds to 17-beta- estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells (By similarity). Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. {ECO:0000250, ECO:0000269|PubMed:19131510}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0016323;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043198;
GO  GO:0044327;
GO  GO:0032591;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0098686;
GO  GO:0099055;
GO  GO:0099056;
GO  GO:0045095;
GO  GO:0031966;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0048786;
GO  GO:0042734;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0003682;
GO  GO:0038054;
GO  GO:0030284;
GO  GO:0005496;
GO  GO:1990239;
GO  GO:0007189;
GO  GO:0030263;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0071392;
GO  GO:0071333;
GO  GO:0071389;
GO  GO:0071375;
GO  GO:0071356;
GO  GO:0006954;
GO  GO:0045087;
GO  GO:0030518;
GO  GO:0010948;
GO  GO:0008285;
GO  GO:0070373;
GO  GO:0045599;
GO  GO:0010629;
GO  GO:0050728;
GO  GO:0002695;
GO  GO:0051055;
GO  GO:0051898;
GO  GO:1904706;
GO  GO:0007399;
GO  GO:0019228;
GO  GO:0030264;
GO  GO:0043065;
GO  GO:2000724;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0043280;
GO  GO:0007204;
GO  GO:2000353;
GO  GO:0045742;
GO  GO:0070374;
GO  GO:2001238;
GO  GO:0045745;
GO  GO:0010628;
GO  GO:0032962;
GO  GO:0032024;
GO  GO:0043410;
GO  GO:0050769;
GO  GO:0001956;
GO  GO:0014068;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0090200;
GO  GO:0051281;
GO  GO:0045944;
GO  GO:0070474;
GO  GO:0051726;
GO  GO:0051480;
GO  GO:0043401;
GO  GO:0042311;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVTSQARGMGLEMYPGTMQPAAPNTTSPELNLSHPLLGASLANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILI
SQ  LVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHEQYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALA
SQ  RAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRV
SQ  LVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLN
SQ  PLIYSFLGETFREKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV
//
ID  B0F9W3;
PN  G-protein coupled estrogen receptor 1;
GN  gper1;
OS  29154;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18420744}; Multi-pass membrane protein {ECO:0000269|PubMed:18420744}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalized with cadherin at the plasma membrane.
DR  UNIPROT: B0F9W3;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: Membrane G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Plays a role in the embryonic development of sensory and motor neurons. May induce apoptosis and reduce proliferation of brain cells. Involved in maintenance of meiotic arrest in oocytes. {ECO:0000269|PubMed:18420744, ECO:0000269|PubMed:19931550}.
DE  Reference Proteome: No;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0016323;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0032591;
GO  GO:0005769;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0055037;
GO  GO:0004930;
GO  GO:0005496;
GO  GO:1990239;
GO  GO:0007189;
GO  GO:0006915;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0071392;
GO  GO:0071371;
GO  GO:0051447;
GO  GO:1900194;
GO  GO:0007399;
GO  GO:0043401;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEEQTTSLVWIYVNSTEQLNTSYEYNTTYLIEDSDKYQSYVIGLFLSCLYTILLFPIGFIGNILILVVNLNHRGKMAIPD
SQ  LYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYIALANSMSSSPLRTMQHAK
SQ  LSCGLIWMASILATLLPFTIVQTQHRGEVHFCFANVFEIQWLEVTIGFLVPFSIIGLCYSLIGRILMRSQKHRGLWPRRQ
SQ  KALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSQRTATTLRHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKL
SQ  RLFIKQKASWSVVNRFCHHGLDLHLPVRSEVSEV
//
ID  Q8BMP4;
PN  G-protein coupled estrogen receptor 1;
GN  Gper1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalized with BSN to the active zone of presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal synaptosomes. Endocytosed in an agonist- and arrestin-independent manner. Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane. Colocalized with transferrin receptor at the plasma membrane and perinuclear region. Accumulated and colocalized with RAB11 proteins in recycling endosomes and trans-Golgi network (TGN), but does neither recycle back to the cell surface nor traffics to late endosome or lysosome. Colocalized with calnexin in the endoplasmic reticulum. Traffics to intracellular sites via cytokeratin intermediate filaments like KRT7 and KRT8 after constitutive endocytosis in epithelial cells. Colocalized with EGFR in the nucleus of agonist-induced cancer- associated fibroblasts (CAF) (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8BMP4;
DR  UNIPROT: B2RRW0;
DR  UNIPROT: Q9D392;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: G-protein coupled estrogen receptor that binds to 17-beta- estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells. {ECO:0000269|PubMed:18063692, ECO:0000269|PubMed:18845638, ECO:0000269|PubMed:19179659, ECO:0000269|PubMed:19430488, ECO:0000269|PubMed:20734455, ECO:0000269|PubMed:21273787, ECO:0000269|PubMed:21673097, ECO:0000269|PubMed:22492045, ECO:0000269|PubMed:23545157, ECO:0000269|PubMed:23674134, ECO:0000269|PubMed:23871778}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043198;
GO  GO:0044327;
GO  GO:0032591;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0098686;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0045095;
GO  GO:0031966;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0048786;
GO  GO:0042734;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0003682;
GO  GO:1903924;
GO  GO:0038054;
GO  GO:0030284;
GO  GO:0005496;
GO  GO:1990239;
GO  GO:0007189;
GO  GO:0030263;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0071392;
GO  GO:0071333;
GO  GO:0071389;
GO  GO:0071375;
GO  GO:0071356;
GO  GO:0007186;
GO  GO:0006954;
GO  GO:0045087;
GO  GO:0030520;
GO  GO:0030518;
GO  GO:0050804;
GO  GO:0010948;
GO  GO:0008285;
GO  GO:0070373;
GO  GO:0045599;
GO  GO:0010629;
GO  GO:0050728;
GO  GO:0002695;
GO  GO:0051055;
GO  GO:0051898;
GO  GO:1900121;
GO  GO:1904706;
GO  GO:0007399;
GO  GO:0019228;
GO  GO:0030264;
GO  GO:0043065;
GO  GO:2000724;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0043280;
GO  GO:0007204;
GO  GO:2000353;
GO  GO:0045742;
GO  GO:0070374;
GO  GO:2001238;
GO  GO:0045745;
GO  GO:0010628;
GO  GO:0032962;
GO  GO:0032024;
GO  GO:0043410;
GO  GO:0050769;
GO  GO:0001956;
GO  GO:0014068;
GO  GO:0042307;
GO  GO:0051897;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0090200;
GO  GO:0051281;
GO  GO:0045944;
GO  GO:0070474;
GO  GO:1905152;
GO  GO:0051726;
GO  GO:0051480;
GO  GO:0007210;
GO  GO:0043401;
GO  GO:0042311;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDATTPAQTVGVEIYLGPVWPAPSNSTPLALNLSLALREDAPGNLTGDLSEHQQYVIALFLSCLYTIFLFPIGFVGNILI
SQ  LVVNISFREKMTIPDLYFINLAAADLILVADSLIEVFNLDEQYYDIAVLCTFMSLFLQINMYSSVFFLTWMSFDRYLALA
SQ  KAMRCGLFRTKHHARLSCGLIWMASVSATLVPFTAVHLRHTEEACFCFADVREVQWLEVTLGFIMPFAIIGLCYSLIVRA
SQ  LIRAHRHRGLRPRRQKALRMIFAVVLVFFICWLPENVFISVHLLQWTQPGDTPCKQSFRHAYPLTGHIVNLAAFSNSCLN
SQ  PLIYSFLGETFRDKLRLYVEQKTSLPALNRFCHATLKAVIPDSTEQSEVRFSSAV
//
ID  O08878;
PN  G-protein coupled estrogen receptor 1;
GN  Gper1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:22919059}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22919059}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21242460}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:21242460, ECO:0000269|PubMed:22919059}; Multi-pass membrane protein. Cell projection, dendrite. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:22919059, ECO:0000269|PubMed:23300088}; Multi-pass membrane protein. Cell projection, axon {ECO:0000269|PubMed:22919059}. Postsynaptic density {ECO:0000269|PubMed:22919059, ECO:0000269|PubMed:23300088}. Mitochondrion membrane {ECO:0000269|PubMed:22919059}; Multi-pass membrane protein. Note=Endocytosed in an agonist- and arrestin-independent manner. Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane. Colocalized with transferrin receptor at the plasma membrane and perinuclear region. Accumulated and colocalized with RAB11 proteins in recycling endosomes and trans-Golgi network (TGN), but does neither recycle back to the cell surface nor traffics to late endosome or lysosome. Colocalized with calnexin in the endoplasmic reticulum. Traffics to intracellular sites via cytokeratin intermediate filaments like KRT7 and KRT8 after constitutive endocytosis in epithelial cells. Colocalized with EGFR in the nucleus of agonist-induced cancer- associated fibroblasts (CAF) (By similarity). Colocalized with BSN to the active zone of presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal synaptosomes. {ECO:0000250}.
DR  UNIPROT: O08878;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DE  Function: G-protein coupled estrogen receptor that binds to 17-beta- estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells. {ECO:0000269|PubMed:19179659, ECO:0000269|PubMed:20132863}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0030425;
GO  GO:0043198;
GO  GO:0044327;
GO  GO:0032591;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0098686;
GO  GO:0016021;
GO  GO:0045095;
GO  GO:0031966;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0048786;
GO  GO:0042734;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0003682;
GO  GO:1903924;
GO  GO:0038054;
GO  GO:0030284;
GO  GO:0005496;
GO  GO:1990239;
GO  GO:0007189;
GO  GO:0030263;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0071392;
GO  GO:0071333;
GO  GO:0071389;
GO  GO:0071375;
GO  GO:0071356;
GO  GO:0007186;
GO  GO:0006954;
GO  GO:0045087;
GO  GO:0030520;
GO  GO:0030518;
GO  GO:0050804;
GO  GO:0010948;
GO  GO:0008285;
GO  GO:0070373;
GO  GO:0045599;
GO  GO:0010629;
GO  GO:0050728;
GO  GO:0002695;
GO  GO:0051055;
GO  GO:0051898;
GO  GO:1900121;
GO  GO:1904706;
GO  GO:0007399;
GO  GO:0019228;
GO  GO:0030264;
GO  GO:0043065;
GO  GO:2000724;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0043280;
GO  GO:0007204;
GO  GO:2000353;
GO  GO:0045742;
GO  GO:0070374;
GO  GO:2001238;
GO  GO:0045745;
GO  GO:0010628;
GO  GO:0032962;
GO  GO:0032024;
GO  GO:0043410;
GO  GO:0050769;
GO  GO:0001956;
GO  GO:0014068;
GO  GO:0042307;
GO  GO:0051897;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0090200;
GO  GO:0051281;
GO  GO:0045944;
GO  GO:0070474;
GO  GO:1905152;
GO  GO:0051726;
GO  GO:0051480;
GO  GO:0007210;
GO  GO:0043401;
GO  GO:0042311;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAATTPAQDVGVEIYLGPVWPAPSNSTPLALNLSLALREDAPGNLTGDLSEHQQYVIALFLSCLYTIFLFPIGFVGNILI
SQ  LVVNISFREKMTIPDLYFINLAAADLILVADSLIEVFNLDEQYYDIAVLCTFMSLFLQINMYSSVFFLTWMSFDRYLALA
SQ  KAMRCGLFRTKHHARLSCGLIWMASVSATLVPFTAVHLRHTEEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRA
SQ  LIRAHRHRGLRPRRQKALRMIFAVVLVFFICWLPENVFISVHLLQWAQPGDTPCKQSFRHAYPLTGHIVNLAAFSNSCLS
SQ  PLIYSFLGETFRDKLRLYVAQKTSLPALNRFCHATLKAVIPDSTEQSDVKFSSAV
//
ID  Q7Z6J2;
PN  Protein TAMALIN;
GN  TAMALIN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8R4T5}. Cell membrane {ECO:0000250|UniProtKB:Q8R4T5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8R4T5}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8R4T5}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q8R4T5}.
DR  UNIPROT: Q7Z6J2;
DR  UNIPROT: Q6PIF8;
DR  UNIPROT: Q7Z741;
DR  PDB: 2PNT;
DR  Pfam: PF00595;
DR  PROSITE: PS50106;
DR  OMIM: 612027;
DR  DisGeNET: 160622;
DE  Function: Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5NHN0; IntAct: EBI-2806502; Score: 0.00
DE  Interaction: Q9BYF1; IntAct: EBI-28949723; Score: 0.40
GO  GO:0070161;
GO  GO:0098978;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098685;
GO  GO:0042802;
GO  GO:0030165;
GO  GO:0031267;
GO  GO:0008104;
GO  GO:0099152;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8R4T5};
SQ  MTLRRLRKLQQKEEAAATPDPAARTPDSEVAPAAPVPTPGPPAAAATPGPPADELYAALEDYHPAELYRALAVSGGTLPR
SQ  RKGSGFRWKNLSQSPEQQRKVLTLEKEDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNG
SQ  LNVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTL
SQ  ESVRSCLYGAGLLPGSLPFGPLLAVPGRPRGGARRARGDADDAVYHTCFFGDSEPPALPPPPPPARAFGPGPAETPAVGP
SQ  GPGPRAALSRSASVRCAGPGGGGGGGAPGALWTEAREQALCGPGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL
//
ID  Q9JJA9;
PN  General receptor for phosphoinositides 1-associated scaffold protein;
GN  Tamalin;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8R4T5}. Cell membrane {ECO:0000250|UniProtKB:Q8R4T5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8R4T5}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8R4T5}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q8R4T5}.
DR  UNIPROT: Q9JJA9;
DR  UNIPROT: Q9JKL0;
DR  Pfam: PF00595;
DR  PROSITE: PS50106;
DE  Function: Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0098978;
GO  GO:0005641;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098685;
GO  GO:0042802;
GO  GO:0030165;
GO  GO:0031267;
GO  GO:0006886;
GO  GO:0008104;
GO  GO:0099152;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8R4T5};
SQ  MTLRRLRKLQQKEEATAAPDPAGRAPDSEAARAAPLPSGPPAAAAPPGAPGEELYAALEDYHPAELYRALAVSGGTLPRR
SQ  KGSGFRWKNFTQSPEQQRKVLTLEKGDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNGL
SQ  NVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTLE
SQ  SVRSCLYGAGLLPGSLPFGPLLAAPGSARGGARRAKGDTDDAVYHTCFFGGAEPQALPPPPPPARALGPSSAETPASVLF
SQ  PAPRSTLSRSASVRCAGPGGGGGAPGALWTEAREQALCGAGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL
//
ID  Q8R4T5;
PN  General receptor for phosphoinositides 1-associated scaffold protein;
GN  Tamalin;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11850456}. Cell membrane {ECO:0000269|PubMed:11850456}; Peripheral membrane protein {ECO:0000269|PubMed:11850456}; Cytoplasmic side {ECO:0000269|PubMed:11850456}. Postsynaptic cell membrane {ECO:0000269|PubMed:11850456}.
DR  UNIPROT: Q8R4T5;
DR  PDB: 2EGK;
DR  PDB: 2EGN;
DR  PDB: 2EGO;
DR  Pfam: PF00595;
DR  PROSITE: PS50106;
DE  Function: Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses. {ECO:0000269|PubMed:11850456}.
DE  Reference Proteome: Yes;
DE  Interaction: P63035; IntAct: EBI-8600171; Score: 0.37
DE  Interaction: Q91Y79; IntAct: EBI-8600241; Score: 0.37
DE  Interaction: P14314; IntAct: EBI-8600313; Score: 0.37
DE  Interaction: O94868; IntAct: EBI-8600330; Score: 0.37
DE  Interaction: O15062; IntAct: EBI-8600386; Score: 0.37
DE  Interaction: Q8R515; IntAct: EBI-8600369; Score: 0.37
DE  Interaction: P97838; IntAct: EBI-8600437; Score: 0.51
DE  Interaction: Q9Y592; IntAct: EBI-8600403; Score: 0.37
DE  Interaction: P11274; IntAct: EBI-8600478; Score: 0.37
DE  Interaction: O88573; IntAct: EBI-8600550; Score: 0.37
DE  Interaction: O35431; IntAct: EBI-8600652; Score: 0.52
DE  Interaction: O88382; IntAct: EBI-8600638; Score: 0.70
DE  Interaction: P31016; IntAct: EBI-8600666; Score: 0.52
DE  Interaction: P97836; IntAct: EBI-8600894; Score: 0.40
DE  Interaction: Q62915; IntAct: EBI-8600971; Score: 0.40
DE  Interaction: Q8R4T5; IntAct: EBI-8600781; Score: 0.67
DE  Interaction: P31424; IntAct: EBI-7361910; Score: 0.63
GO  GO:0070161;
GO  GO:0098978;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0098685;
GO  GO:0042802;
GO  GO:0030165;
GO  GO:0031267;
GO  GO:0008104;
GO  GO:0099152;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11850456};
SQ  MTLRRLRKLQQKEEATAAPDLAGRAPDSEAARAAPTPSGPPAAAAPPGAPGDELYAALEDYHPAELYRALAVSGGTLPRR
SQ  KGSGFRWKNFTQSPEQQRKVLTLEKGDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNGL
SQ  NVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTLE
SQ  SVRSCLYGAGLLPGSLPFGPLLAAPGGARGGSRRAKGDTDDAVYHTCFFGGAEPQALPPPPPPARAPGPGSAETPASVLC
SQ  PAPRATLSRSASVRCAGPGGGGGGGAPGALWTEAREQALCGAGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL
//
ID  Q55AP1;
PN  Metabotropic glutamate receptor-like protein A;
GN  grlA;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cell cortex {ECO:0000269|PubMed:17950724}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17950724}.
DR  UNIPROT: Q55AP1;
DR  Pfam: PF00003;
DR  Pfam: PF02608;
DR  PROSITE: PS50259;
DE  Function: May play an important role in the terminal differentiation. {ECO:0000269|PubMed:17950724}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0004930;
GO  GO:0030587;
GO  GO:0030435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNKLKFLIILFITFLFNLKYINSLKQCKISVLLSGDWSDMGYNYQMNNARIKAESALNLEMSLCYKNLEVSIDLAKQAIE
SQ  DSIKKGANFIVISSSVHTSIGYEYARLHRDKDIYWLIRGRGRPVPDDLPKVAVINFNTHLLHYTLGLVSGYLTTSGTVGF
SQ  ISPGPQILALANSNSFYLGALASRKNVTFLNAYTGSWYNPEVAYKASQMLISNGADFIGMSQDDMSVQKALMDSGKMALG
SQ  ITGFSNRLIWGSDIALSYITDWSDVFIKYAGHILNDTWPEYTDYYTTLAEGGSLLFDTFSYRVPSEVQKLVSLEIEKLKN
SQ  SSYQPFRCNPMYSQINLNFDSNGCANDMEFKNTKLLLKGTDISKTINLGLYTIPIEFVDYSNSMKLGLTIVSGFCILFCI
SQ  ISMVLVIMFRHAKIIKSASPIFCLLILFGCIIIFSGCIIFSLSPTDGICGARVWLLSIGYTIFLGSLLVKNWRIWLLFDN
SQ  PKLKKRSITNWKLYPFVAGILAADVLILALWQGLGDIRSESRIGIDSLTKYQYANVCSSNDQGSVALYILLVFHGIKLLA
SQ  ACFISFKIKAVDIEEFNESKPIASSIYIITFCLFIVIPLMVSPQSVASQVITIVVCAIVTTLISISLLFGSKFYMMATQG
SQ  LALNQTFATNTKSSSFSLSLEKQKSKSNGLEFEDSDESEEKLPQIKNYSNSEIPNLQHNHSRLAHFSSDSCTSAEQDSKL
SQ  DLENQNDENEIENNQNNQNNIVEDCQKVEKLEKDENLEKDENLEKDENLEKDNENQSIIQKKRLSKNFNQSEIDPDDV
//
ID  Q75JT4;
PN  Metabotropic glutamate receptor-like protein J;
GN  grlJ;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Comments: Cell membrane {ECO:0000269|PubMed:17501984}. Membrane {ECO:0000269|PubMed:17501984}; Multi-pass membrane protein {ECO:0000269|PubMed:17501984}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17501984}. Golgi apparatus membrane {ECO:0000269|PubMed:17501984}. Nucleus envelope {ECO:0000269|PubMed:17501984}. Note=May also localize to internal membranes.
DR  UNIPROT: Q75JT4;
DR  UNIPROT: Q559S6;
DR  Pfam: PF00003;
DR  Pfam: PF02608;
DR  PROSITE: PS50259;
DE  Function: May act during the development and be a negative regulator. {ECO:0000269|PubMed:17501984}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031090;
GO  GO:0005886;
GO  GO:0004930;
GO  GO:1902610;
GO  GO:0031153;
GO  GO:0030587;
GO  GO:0030435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKILLYIAIILSFFSLITISSECKIAVLLSGSPNDLGYNYLMNEARVKAESELKLDFSIYYENLEESMEEAEKAFQDALH
SQ  KGANLIVVGSFVHVGLGLKYAALTKDQDIYWIIRGNKRPNPDLPHVVILNFNSFELHYLLGYFSGLMTKTGIVGFVAPGP
SQ  DVNTISTDNSFYLGAKYARPNITFLNVYVQSWYNPNVSYSAAKMLIKNGADLIGMSQDDMSCQKAMMDSGLIGIGATGYP
SQ  THLLFGGNVGVSYITNWTNLYVKYAQHVLNDDWPDYSSYFTNLSREDSIFIDDYSYKVPIDIQNLVNDEIQRLKNTSYIP
SQ  YRSDPYLAQLGIPFDSKGLLVEDQFRANKKLLKGDSISKVIDFGQYSIPIEFIDYPNSLKYGVTIVSGVCIFICLVCMTL
SQ  VVVFKKARVIKSSSPAFLLLILLGCCIIFAACILFAQSPTNQTCSARIWLLSLGYTLFLGNLLVKNWRIWLLFDNPKLKK
SQ  RAITNWKLYPWVFAILAIDVMILAIWQGLGNINAESRIGYDSLTQYQYKNVCSSDDQGSIALYLLLVFHGLVLLVACFIS
SQ  FKIKVVDIEEFNESKPITTSVYIITFCLFIVIPLMVSPQSLTSQTTIICVCAIVTTLISMLLLFGSKFYKMATQGLAINE
SQ  TFATSTKSSSKSSKSSYGKDNPNPNAINFGEDDTSDETSEEKHKSPKQKSVNFSNKSNSHLAVFTSDEETSKTSKLSIDF
SQ  ENSSKDISIDQLQQQKQQPINTNGDLENKSNDKIDDDNDNSSVLSKRISNQQNGETEIDSNNV
//
ID  Q32M21;
PN  Gasdermin-A2, C-terminal;
GN  Gsdma2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: [Gasdermin-A2]: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QA5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5Y4Y6}. [Gasdermin-A2, N-terminal]: Cell membrane {ECO:0000250|UniProtKB:Q5Y4Y6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5Y4Y6}.
DR  UNIPROT: Q32M21;
DR  UNIPROT: Q8CF01;
DR  UNIPROT: Q9D810;
DR  Pfam: PF04598;
DR  Pfam: PF17708;
DE  Function: [Gasdermin-A2]: This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-A2, N-terminal) binds to membranes and forms pores, triggering cell death. {ECO:0000250|UniProtKB:Q96QA5}. [Gasdermin-A2, N-terminal]: Pore-forming protein that causes membrane permeabilization and pyroptosis. Released upon cleavage of Gasdermin-A2, and binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis. Binds to membrane inner leaflet lipids, such as phosphatidylinositol (4,5)- bisphosphate. The functional mechanisms and physiological proteases that cleave and activate this pore-forming protein are unknown. {ECO:0000250|UniProtKB:Q96QA5}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005546;
GO  GO:0070273;
GO  GO:0001786;
GO  GO:0006915;
GO  GO:0042742;
GO  GO:0070269;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5Y4Y6};
SQ  MSMFEDVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVRTDYTLLDVLEPGSSPSDPTLLGNFS
SQ  FKNMLDVRVEGDVEVPTMMKVKGTVGLSQSSTLEVQMLSVAPTALENLHMERKLSADHPFLKEMREYKQNLYVVMEVVKA
SQ  KQEVTLKRASNAISKFSLNLPSLGLQGSVNHKEAVTIPKGCVLAYRVRQLIIYGKDEWGIPYICTDNMPTFNPLCVLQRQ
SQ  GSTVQMISGEMHEDFKTLKKEVQQETQEVEKLSPVGRSSLLTSLSHLLGKKKELQDLEQMLEGALDKGHEVTLEALPKDV
SQ  LLLKDAMDAILYFLGALTELSEEQLKILVKSLENKVLPVQLKLVESILEQNFLQDKEDVFPLRPDLLSSLGEEDQILTEA
SQ  LVGLSGLEVQRSGPQYTWNPDTCHNLCALYAGLSLLHLLSRDS
//
ID  Q96QA5;
PN  Gasdermin-A, C-terminal;
GN  GSDMA;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Gasdermin-A]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17471240}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5Y4Y6}. [Gasdermin-A, N-terminal]: Cell membrane {ECO:0000250|UniProtKB:Q5Y4Y6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5Y4Y6}.
DR  UNIPROT: Q96QA5;
DR  UNIPROT: Q32MC5;
DR  UNIPROT: Q86VE7;
DR  UNIPROT: Q8N1M6;
DR  Pfam: PF04598;
DR  Pfam: PF17708;
DR  OMIM: 611218;
DR  DisGeNET: 284110;
DE  Function: [Gasdermin-A]: This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-A, N-terminal) binds to membranes and forms pores, triggering cell death. {ECO:0000269|PubMed:27281216}. [Gasdermin-A, N-terminal]: Pore-forming protein that causes membrane permeabilization and pyroptosis (PubMed:17471240, PubMed:27281216). Released upon cleavage in vitro of genetically engineered GSDMA, and binds to membrane inner leaflet lipids (PubMed:27281216). Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis (PubMed:27281216). Binds to membrane inner leaflet lipids, such as phosphatidylinositol (4,5)-bisphosphate (PubMed:27281216). The functional mechanisms and physiological proteases that cleave and activate this pore-forming protein are unknown (PubMed:27281216). {ECO:0000269|PubMed:17471240, ECO:0000269|PubMed:27281216}.
DE  Reference Proteome: Yes;
DE  Interaction: O75593; IntAct: EBI-11320921; Score: 0.35
DE  Interaction: P02654; IntAct: EBI-23875424; Score: 0.56
DE  Interaction: P55056; IntAct: EBI-25158560; Score: 0.56
DE  Interaction: O43309; IntAct: EBI-21572679; Score: 0.35
DE  Interaction: Q9NU19; IntAct: EBI-21575852; Score: 0.35
DE  Interaction: Q9UMR2; IntAct: EBI-21616596; Score: 0.35
DE  Interaction: Q15915; IntAct: EBI-21696712; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9P2S5; IntAct: EBI-25486895; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568044; Score: 0.35
DE  Interaction: O43781; IntAct: EBI-28931148; Score: 0.35
DE  Interaction: Q14296; IntAct: EBI-28941126; Score: 0.35
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005546;
GO  GO:0070273;
GO  GO:0001786;
GO  GO:0006915;
GO  GO:0042742;
GO  GO:0070269;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5Y4Y6};
SQ  MTMFENVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVRTDYTLLDVLEPGSSPSDPTDTGNFG
SQ  FKNMLDTRVEGDVDVPKTVKVKGTAGLSQNSTLEVQTLSVAPKALETVQERKLAADHPFLKEMQDQGENLYVVMEVVETV
SQ  QEVTLERAGKAEACFSLPFFAPLGLQGSINHKEAVTIPKGCVLAFRVRQLMVKGKDEWDIPHICNDNMQTFPPGEKSGEE
SQ  KVILIQASDVGDVHEGFRTLKEEVQRETQQVEKLSRVGQSSLLSSLSKLLGKKKELQDLELALEGALDKGHEVTLEALPK
SQ  DVLLSKEAVGAILYFVGALTELSEAQQKLLVKSMEKKILPVQLKLVESTMEQNFLLDKEGVFPLQPELLSSLGDEELTLT
SQ  EALVGLSGLEVQRSGPQYMWDPDTLPRLCALYAGLSLLQQLTKAS
//
ID  Q9EST1;
PN  Gasdermin-A, C-terminal;
GN  Gsdma;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: [Gasdermin-A]: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QA5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5Y4Y6}. [Gasdermin-A, N-terminal]: Cell membrane {ECO:0000250|UniProtKB:Q5Y4Y6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5Y4Y6}.
DR  UNIPROT: Q9EST1;
DR  UNIPROT: A3KFN3;
DR  Pfam: PF04598;
DR  Pfam: PF17708;
DE  Function: [Gasdermin-A]: This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-A, N-terminal) binds to membranes and forms pores, triggering cell death. {ECO:0000250|UniProtKB:Q96QA5}. [Gasdermin-A, N-terminal]: Pore-forming protein that causes membrane permeabilization and pyroptosis. Released upon cleavage of Gasdermin-A, and binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis. Binds to membrane inner leaflet lipids, such as phosphatidylinositol (4,5)- bisphosphate. The functional mechanisms and physiological proteases that cleave and activate this pore-forming protein are unknown. {ECO:0000250|UniProtKB:Q96QA5}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6AXH7; IntAct: EBI-6876709; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005546;
GO  GO:0070273;
GO  GO:0001786;
GO  GO:0006915;
GO  GO:0042742;
GO  GO:0070269;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5Y4Y6};
SQ  MTMFENVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVHTDYTLLDVLEPGSSPSDPTDSGNFS
SQ  FKNMLDARVEGDVDVPKTVKVKGTAGLSRSSTLEVQTLSVAPTALENLHKERKLSADHPFLKEMRERGENLYVVMEVVET
SQ  LQEVTLERAGKAEGCFSLPFFAPLGLQGSVNHKEAVTIPKGCVLAYRVRQLMVNGKDEWGIPHICNDSMQTFPPGEKPGE
SQ  GKFILIQASDVGEMHEDFKTLKEEVQRETQEVEKLSPVGRSSLLTSLSHLLGKKKELQDLEQTLEGALDKGHEVTLEALP
SQ  KDVLLSKDAMDAILYFLGALTVLSEAQQKLLVKSLEKKILPVQLKLVESTMEKNFLQDKEGVFPLQPDLLSSLGEEELIL
SQ  TEALVGLSGLEVQRSGPQYTWDPDTLPHLCALYAGLSLLQLLSKNS
//
ID  F1R0H0;
PN  Solute carrier family 2, facilitated glucose transporter member 10;
GN  slc2a10;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}.
DR  UNIPROT: F1R0H0;
DR  UNIPROT: A8KB28;
DR  UNIPROT: I1SV80;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000269|PubMed:22116938}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005355;
GO  GO:0015293;
GO  GO:0072359;
GO  GO:1904659;
GO  GO:0030903;
GO  GO:0055085;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGCSVLLLTITVSTLGGLVFGYELGIISGALPQLQTHFSLGCVQQEAVVSALLIGSLFASIIGGWLIDRHGRRTSILLSN
SQ  LLILAGSVILTTGTSFFALVIGRAVIGFAMTVSSMSCCIFVSEMVTPERRGLMVTLYEVGITVGILIAYAVNYIFNNVPL
SQ  TGWRYMFGFAIIPSLIQLASIVLLPKQAEVFVIHDDDSRQADRLTEETETSNQHQQSEKYGVSDLFKSKDNMRRRTVIGV
SQ  GLVLSQQFTGQPNVLFYASTILFSVGFQSNASAILASVGFGIVKVIATLLAMLCSDRAGRRSLLIGGCSMLAVGLILTGF
SQ  LCRQSVIDTTKRCTSVGPHSNLTLSAEHDEGVGFSSQTLDVHEHLRSFSQSEDIYKWIIFTCLMAVVSAFSVSFGPMTWV
SQ  VLSEIFPKDIRGRAFSFINCFNVGANLIVSFSFLSIIDVIGLSGVFLMYGVVGIAGVVFIYLVLPETKGKSLQDIDRELS
SQ  QTRMIHRQELCSIFQRRRFSPGYQRVQLTSTAT
//
ID  O95528;
PN  Solute carrier family 2, facilitated glucose transporter member 10;
GN  SLC2A10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000269|PubMed:16550171}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16550171}.
DR  UNIPROT: O95528;
DR  UNIPROT: A8K4J6;
DR  UNIPROT: Q3MIX5;
DR  UNIPROT: Q9H4I6;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DR  OMIM: 208050;
DR  OMIM: 606145;
DR  DisGeNET: 81031;
DE  Function: Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000269|PubMed:11592815, ECO:0000269|PubMed:16550171}.
DE  Disease: Arterial tortuosity syndrome (ATORS) [MIM:208050]: An autosomal recessive disorder characterized by tortuosity and elongation of major arteries, often resulting in death at young age. Other typical features include aneurysms of large arteries and stenosis of the pulmonary artery, in association with facial features and several connective tissue manifestations such as soft skin and joint laxity. Histopathological findings include fragmentation of elastic fibers in the tunica media of large arteries. {ECO:0000269|PubMed:16550171, ECO:0000269|PubMed:17935213}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005351;
GO  GO:0055056;
GO  GO:0033300;
GO  GO:0005355;
GO  GO:0015293;
GO  GO:0060840;
GO  GO:0045454;
GO  GO:0072359;
GO  GO:0070837;
GO  GO:0072498;
GO  GO:0015757;
GO  GO:0098708;
GO  GO:1904659;
GO  GO:0008645;
GO  GO:0032683;
GO  GO:0010629;
GO  GO:2001045;
GO  GO:1902729;
GO  GO:0060392;
GO  GO:0030512;
GO  GO:0010628;
GO  GO:1902730;
GO  GO:0030511;
GO  GO:1903053;
GO  GO:0043588;
GO  GO:0055085;
GO  GO:0150104;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGHSPPVLPLCASVSLLGGLTFGYELAVISGALLPLQLDFGLSCLEQEFLVGSLLLGALLASLVGGFLIDCYGRKQAILG
SQ  SNLVLLAGSLTLGLAGSLAWLVLGRAVVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEAGITVGILLSYALNYALAGT
SQ  PWGWRHMFGWATAPAVLQSLSLLFLPAGTDETATHKDLIPLQGGEAPKLGPGRPRYSFLDLFRARDNMRGRTTVGLGLVL
SQ  FQQLTGQPNVLCYASTIFSSVGFHGGSSAVLASVGLGAVKVAATLTAMGLVDRAGRRALLLAGCALMALSVSGIGLVSFA
SQ  VPMDSGPSCLAVPNATGQTGLPGDSGLLQDSSLPPIPRTNEDQREPILSTAKKTKPHPRSGDPSAPPRLALSSALPGPPL
SQ  PARGHALLRWTALLCLMVFVSAFSFGFGPVTWLVLSEIYPVEIRGRAFAFCNSFNWAANLFISLSFLDLIGTIGLSWTFL
SQ  LYGLTAVLGLGFIYLFVPETKGQSLAEIDQQFQKRRFTLSFGHRQNSTGIPYSRIEISAAS
//
ID  Q8VHD6;
PN  Solute carrier family 2, facilitated glucose transporter member 10;
GN  Slc2a10;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}.
DR  UNIPROT: Q8VHD6;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000250|UniProtKB:O95528}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0005887;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055056;
GO  GO:0033300;
GO  GO:0005355;
GO  GO:0015293;
GO  GO:0060840;
GO  GO:0045454;
GO  GO:0072359;
GO  GO:0070837;
GO  GO:0072498;
GO  GO:0098708;
GO  GO:1904659;
GO  GO:0032683;
GO  GO:0010629;
GO  GO:2001045;
GO  GO:1902729;
GO  GO:0060392;
GO  GO:0030512;
GO  GO:0010628;
GO  GO:1902730;
GO  GO:0030511;
GO  GO:1903053;
GO  GO:0043588;
GO  GO:0055085;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLRPAVLLLCASVSLLGGLTFGYELAVISGALLPLQLNFGLSCLEQELLVGSLLLGALLASLVGGFLIDCYGRRRAILG
SQ  SNAVLLAGSLILGLASSLPWLLLGRLSVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEVGITVGILFSYGLNYVLAGS
SQ  PWGWRHMFGWAAAPALLQSLSLFLLPAGAEGTAAPKDLIPLQGRETSKPGLVKPQYSFLDLFRAQDGMWSRTVVGLGLVL
SQ  FQQLTGQPNVLYYASTIFRSVGFHGGSSAVLASVGLGTVKVAATLVATGLVDRAGRRVLLLFGCALMALSVSGIGLVSFA
SQ  VSLDSGPSCLATSNASQQVDLPGSSGLLVRSSLPPVLHTNGDQGQLVLSVTERPIHPVITASLGPVLNTASPVPTSPILE
SQ  HTLLCWSALVCMMVYVSAFSVGFGPVTWLVLSEIYPAEIRGRAFAFCSSFNWAANLFISLSFLDLIGAIGLAWTFLLYGL
SQ  TAVLGLAFIYLLVPETKGQSLAEIEQQFQTSRFPLNFGHRQRIGIQYHRLDVSSAS
//
ID  Q6GN01;
PN  Solute carrier family 2, facilitated glucose transporter member 10;
GN  slc2a10;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}.
DR  UNIPROT: Q6GN01;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000250|UniProtKB:O95528}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0022857;
GO  GO:0008643;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLRSTTLVLAATSSLLGGLIFGYELGIISGALLMLKTVFQLTCFEQEALVSAVLFGALLASLIGGFIIDRSGRRTSIMG
SQ  SNLVVLAGSIILIATSSFWWLVVGRVTVGFAISISSMACCIYVSEIVRPHQRGTLVSLYETGITVGILISYAMNYFLSAV
SQ  NDGWKYMFGLAIIPAAFQFIVILFLPSKPHTLNFWEQDSDNGFIELEEAGESGEFKPDTYDKQYTFLDLFRSKDNMRTRT
SQ  LLGLGLVLFQQFTGQPNVLYYASTIFRSVGFQSNSSAVLASVGLGVVKVASTLIAICFADKAGRRILLLAGCIVMTIAIS
SQ  GIGIVSFMVELDSHRDCGSIRSKNTSYGDSNASQLLGIIHAGTPTINTKDNLAHQLAMVIQSPSLSNSAGSKHTASMFPN
SQ  STVPPAGPDSNYAILNWITLLSMMAFVSAFSIGFGPMTWLVLSEIYPADIRGRAFAFCNSFNWAANLLITLTFLEVIGSI
SQ  GLGWTFLLYGGVGLLAIAFIYFFIPETKGQSLEEIDQQLSSKRISKRRETSKGVRKRPSTGPPYQRVGKSNWT
//
ID  Q0P4G6;
PN  Solute carrier family 2, facilitated glucose transporter member 10;
GN  slc2a10;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}.
DR  UNIPROT: Q0P4G6;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000250|UniProtKB:O95528}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005355;
GO  GO:0015293;
GO  GO:0072359;
GO  GO:1904659;
GO  GO:0055085;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLSSPTLILAATVSLLGGIVFGYELGIISGALLVLKTVYQLTCFEQEALVSAVLFGALLASLIGGIIIDRWGRRTAILA
SQ  SNLVVLAGSIILIATSTFWWLIVGRVTIGFAISISSMACCIYVSEIVRPHQRGMLVSLYETGITVGILISYAMNYFLSGV
SQ  NESWKYMFGLAIVPAAFQFISILFLPSKPHKLNFWEQDTDDGFIELEETGEAGEFKPDTYDRQYTFLDLFRSKDNMRTRT
SQ  LLGLGLVLFQQFTGQPNVLYYASTIFQSVGFQSNSSAVLASVGLGVVKVASTLIAICFADKAGRRILLLAGCIVMTIAIT
SQ  GIGIVSFTVKMDSHRDCGSVTGRNMSSGESNVSQLLGIVHAETSTINTLDNSVHQLAMAIRSPSLANSASSNHKDLISQN
SQ  STVLPASPELPSNYTILNWITLLSMMAFVSAFSIGFGPMTWIVLSEIYPADIRGRAFAFCNSFNWAANLLITLTFLDVIA
SQ  SIGLSWTFLLYGVVGLLAIAFIYFFIPETKGQSLEEIDKQFSTKRILQKRETSKGVGKRPSSGPPYQRIGKASPS
//
ID  Q5J316;
PN  Solute carrier family 2, facilitated glucose transporter member 12;
GN  SLC2A12;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000269|PubMed:16284803}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TD20}. Note=Localizes primarily perinuclear region in the absence of insulin. {ECO:0000250|UniProtKB:Q8TD20}.
DR  UNIPROT: Q5J316;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Insulin-independent facilitative glucose transporter. {ECO:0000250|UniProtKB:Q8BFW9}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0022857;
GO  GO:0008643;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVPVENAEGPSLLKPKGRAAETDGSDRASGGPHPPWARGCGMYTLLSSVTAAVSGFLVGYELGIISGALLQIRTLLVLTC
SQ  HEQEMVVSSLLIGALLASLIGGVLIDRYGRRAAIILSSCLLGLGSLVLIISLSYTTLIGGRIAIGVFISLSSTATCVYIA
SQ  EIAPQHRRGLLVSLNELMIVIGILFAYISNYAFANISHGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGHEEAASKV
SQ  LGKLRAVLDTTEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAA
SQ  SLASTGVGVVKVISTIPATLLVDQVGSKTFLCIGSSVMAASLVTMGIVNLNIHMNFTSICRNHSPINQSLDESVFYGPGN
SQ  LSASNDTLRESFKGMTFHSRSSLRPTRNDINGRGETTLASLPNAGLSQTEYQIVTDSADVPTFLKWLSLASLLVYVAAFS
SQ  IGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTDLIGLPWVCFIYTVMSLASLVFVIVFIPETKGCS
SQ  LEQISVELAKENYVKNNICFMSHHREELVPKQLQKRKPQEQFLESKKLRGKGQPRQLSSEV
//
ID  Q6NWF1;
PN  Solute carrier family 2, facilitated glucose transporter member 12;
GN  slc2a12;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TD20}. Note=Localizes primarily perinuclear region in the absence of insulin. {ECO:0000250|UniProtKB:Q8TD20}.
DR  UNIPROT: Q6NWF1;
DR  UNIPROT: Q6PHV4;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Insulin-regulated facilitative glucose transporter. {ECO:0000269|PubMed:25326603}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005355;
GO  GO:0015293;
GO  GO:0072359;
GO  GO:0044381;
GO  GO:1904659;
GO  GO:0060047;
GO  GO:0007507;
GO  GO:0003179;
GO  GO:0055085;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDAPEESIRMTSDPQSKIYVQNPDTHIHLEQGPSAKSGNGRALVLCSVSVACLSGLLMGYEMSLISGALLQLRDVLTLSC
SQ  PEQEQVVGSLLLGAFLLSLGGGTILDHYGRRFTIILTALLCVLGTLLSVCVVSFWALVVGRMLVGMSVALSGTASCLYAA
SQ  EVAPAAWRGRCVCVYELMVVLGMLLGFGLSWAFAGVPDGWRFTFGGALLPALLQAGVMPLLPDSPRFLLAQQREKEAHAT
SQ  LLRLRAGIKEVEPVEDELRAIRLAMGAERLHGFLDLFQSRDNMLQRLLVGAALVFLQQATGQPNILAYASTVLSSVGFHG
SQ  NEAATLASTGFGVVKVGGTIPAIFLVDKVGPKALLCVGVVVMMLSTATLGAITMQSRTHVSSLCRGPGNTANFTLFETGD
SQ  ETDIQTNTPLGLYQPQNKLKTNTFLTSINDTREHWILNHTYNHRTALMETAELSKKDSAKIALQSLHEVSPSLKWISLVS
SQ  LLVYVAGFSISLGPMVHVVLSAIFPTGIRGKAVSVISAFNWATNLLISMTFLTLTERIGLPTVIFSYSAMSFLLVVFVIV
SQ  FVPETKGRSLEQISKELAMKNHLRGTLLCHRRKHKATAQPSQEEKALATV
//
ID  Q8TD20;
PN  Solute carrier family 2, facilitated glucose transporter member 12;
GN  SLC2A12;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11832379}. Note=Localizes primarily perinuclear region in the absence of insulin. {ECO:0000269|PubMed:11832379}.
DR  UNIPROT: Q8TD20;
DR  UNIPROT: B3KV17;
DR  UNIPROT: Q7Z6U3;
DR  UNIPROT: Q96MR8;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DR  OMIM: 610372;
DR  DisGeNET: 154091;
DE  Function: Insulin-independent facilitative glucose transporter. {ECO:0000250|UniProtKB:Q8BFW9}.
DE  Reference Proteome: Yes;
DE  Interaction: Q15125; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q8IZQ1; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9UPQ8; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9H1U9; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q6DD88; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P35453; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9Y5Y5; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9Y276; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9UQ90; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9UQ16; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9NWH2; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9NUT2; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9NRX5; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9NPF2; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9H649; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9H3K2; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9BVK2; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9BV35; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q9BRN9; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q96J84; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q96DA6; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q96D53; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q96A46; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q8WUK0; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q8WU79; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q8TD22; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q8TCT6; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q8NHH9; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q8N6M3; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q8N138; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q7Z7B1; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q6Y1H2; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q6P996; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q6P444; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q6NUK1; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q6JQN1; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q5VST6; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q53FV1; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q14156; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q13505; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q13395; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q0P651; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P62341; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P36915; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P33981; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P32189; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P30536; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P24468; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P17152; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P13498; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: O95671; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: O60779; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: O15258; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: Q96BW9; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: A6NJ78; IntAct: EBI-21562097; Score: 0.35
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055056;
GO  GO:0005355;
GO  GO:0015293;
GO  GO:0072359;
GO  GO:1904659;
GO  GO:0008645;
GO  GO:0055085;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVPVENTEGPSLLNQKGTAVETEGSGSRHPPWARGCGMFTFLSSVTAAVSGLLVGYELGIISGALLQIKTLLALSCHEQE
SQ  MVVSSLVIGALLASLTGGVLIDRYGRRTAIILSSCLLGLGSLVLILSLSYTVLIVGRIAIGVSISLSSIATCVYIAEIAP
SQ  QHRRGLLVSLNELMIVIGILSAYISNYAFANVFHGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEGAASKVLGRL
SQ  RALSDTTEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAASLAS
SQ  TGVGVVKVISTIPATLLVDHVGSKTFLCIGSSVMAASLVTMGIVNLNIHMNFTHICRSHNSINQSLDESVIYGPGNLSTN
SQ  NNTLRDHFKGISSHSRSSLMPLRNDVDKRGETTSASLLNAGLSHTEYQIVTDPGDVPAFLKWLSLASLLVYVAAFSIGLG
SQ  PMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTDLIGLPWVCFIYTIMSLASLLFVVMFIPETKGCSLEQI
SQ  SMELAKVNYVKNNICFMSHHQEELVPKQPQKRKPQEQLLECNKLCGRGQSRQLSPET
//
ID  Q9BE72;
PN  Solute carrier family 2, facilitated glucose transporter member 12;
GN  SLC2A12;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TD20}. Note=Localizes primarily perinuclear region in the absence of insulin. {ECO:0000250|UniProtKB:Q8TD20}.
DR  UNIPROT: Q9BE72;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Insulin-independent facilitative glucose transporter. {ECO:0000250|UniProtKB:Q8BFW9}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0022857;
GO  GO:0008643;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVPVENTEGPNLLNQKGTAVETEGSYRASGSRHPPWARGCGMFTFLSSVTAAVSGLLVGYELGIISGALLQIKTLLTLSC
SQ  HEQEMVVSSLLIGALLASLTGGVLIDRYGRRTAIILSSCLLGLGSLVLILSLSYTVLIVGRIAIGVSISLSSIATCVYIA
SQ  EIAPQHRRGLLVSLNELMIVIGILSAYISNYAFANVFHGWKYMFGLVIPLGILQAIAMYFLPPSPRFLVMKGQEGAASKV
SQ  LGRLRALSDATEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAA
SQ  SLASTGVGVVKVISTIPATLLVDHVGSKTFLCIGSSVMAASLVTMGIVNLNIHMNFTNICRSHNSINQSLDESVIYGPGN
SQ  LSASNNTLRDHFKGIASHSRSSLMPLRNDVDKRGETTSASLLNAVLSHTEYQIVTDPGDVPAFLKWLSLASLLVYVAAFS
SQ  IGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTDLIGLPWVCFIYTIMSLASLLFVVMFIPETKGCS
SQ  LEQISMELAKVNYVKNNICFMSHHQEELVPRQPQKRKPQEQLLECNKLCGRGQSRQLSPEN
//
ID  Q8BFW9;
PN  Solute carrier family 2, facilitated glucose transporter member 12;
GN  Slc2a12;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:23041416}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TD20}. Note=Localizes primarily perinuclear region in the absence of insulin. {ECO:0000250|UniProtKB:Q8TD20}.
DR  UNIPROT: Q8BFW9;
DR  UNIPROT: Q14B60;
DR  UNIPROT: Q3UPR6;
DR  UNIPROT: Q8BZB7;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Insulin-independent facilitative glucose transporter. {ECO:0000269|PubMed:23041416}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005355;
GO  GO:0015293;
GO  GO:0072359;
GO  GO:1904659;
GO  GO:0055085;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVPVENTEGPNLLNQKGREAETEGSCGASGGGHPACAGGPSMFTFLTSVTAAISGLLVGYELGLISGALLQIRTLLALTC
SQ  HEQEMVVSSLLIGAFLASLTGGVLIDRYGRRLAIILSSCLLGLGSLVLIMSLSYTLLIMGRVAIGVSISLSSIATCVYIA
SQ  EIAPQHRRGLLVSLNELMIVTGILFAYISNYAFANISNGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEESAGKV
SQ  LRKLRVISDTTEELTLIKSSLKDEYQYSFWDLFRSKDNMRTRILIGLTLVFFVQTTGQPNILFYASTVLKSVGFQSNEAA
SQ  SLASTGVGVVKVVSTIPATLLVDHIGSKTFLCIGSSVMSASLLTMGIVNLNINMNFTNICRSHSLLNQSLEEFVFYATGN
SQ  LSISNSSLREHFKRITPYSKGSFMPMGNGMEPKGEMTFTSSLPNAGLSRTEHQGVTDTAVVPAAYKWLSLASLLVYVAAF
SQ  SIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGVNLLISLTFLTVTDLIGLSWVCFIYTIMSLASLAFVVLFIPETKGC
SQ  SLEQISVELAKANYVKNNICFMSHHQEELVPTQLQKRKPQEQLPECNHLCGRGQSQRPSPDT
//
ID  Q32NG5;
PN  Solute carrier family 2, facilitated glucose transporter member 12;
GN  slc2a12;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TD20}. Note=Localizes primarily perinuclear region in the absence of insulin. {ECO:0000250|UniProtKB:Q8TD20}.
DR  UNIPROT: Q32NG5;
DR  Pfam: PF00083;
DR  PROSITE: PS50850;
DR  PROSITE: PS00216;
DE  Function: Insulin-regulated facilitative glucose transporter. {ECO:0000250|UniProtKB:Q6NWF1}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0022857;
GO  GO:0008643;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLAHSTAQDLILQQRSSDDHPQTNPRQTGCGAFIILSSVIAAISGLLVGYELGIISGALLQLQSLLELTCQQQEIVVSAL
SQ  LIGALVASLVGGCLIDLYGRRTTIIFTSILLVFANLLPVVVVSYGSLIAGRIFIGVSISLSAIATCVYIAELSPQDKRGM
SQ  LVSLNELMIVAGILLAYICNYLFASVNNGWKYMFGLITPLAALQAVAMFFLPRSPRFLIMKGYDDAAGKVLQKLRATTDI
SQ  NEELTAIKSSIKAEYQYKFLDLFCSRDNMRARLLIGLTLSFFVQITGQPNILFYASTVLKSVGFQSTEAASLASTGIGVV
SQ  KVVSTIPAIFLVDKIGSKTFLCIGSAVMAVSLVSVGLVSLQLDVNYNNICKVHTVQNHSLQDSFVYGPVALAKHNESLFE
SQ  ETGTWLESTKASYHSTSQNGTKLLHVSAPEDSSFGFTVKEPKVKSQSDEIPEYMKWLCLSSLLAFVAAFSIGLGPMAWLV
SQ  QSEIFPAGIKGRAFAITSSMNWGMNLLISLTFLTLTEMIGLPWMLFGYALMSIASLVFVIMFVPNTKGRPLEEISKELAN
SQ  RSYMCNAVCHRRRSKKKLTPVALIQSPA
//
ID  P39996;
PN  Glutathione transferase 3;
GN  GTT3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: P39996;
DR  UNIPROT: D3DLN3;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P15565; IntAct: EBI-16294709; Score: 0.00
DE  Interaction: P00359; IntAct: EBI-807469; Score: 0.35
DE  Interaction: P32324; IntAct: EBI-807469; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-807469; Score: 0.35
DE  Interaction: P47088; IntAct: EBI-856729; Score: 0.00
DE  Interaction: Q02159; IntAct: EBI-860107; Score: 0.00
DE  Interaction: P48566; IntAct: EBI-8443637; Score: 0.44
DE  Interaction: P39996; IntAct: EBI-6331316; Score: 0.00
DE  Interaction: P40150; IntAct: EBI-3798470; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3811791; Score: 0.35
DE  Interaction: P48363; IntAct: EBI-3817222; Score: 0.35
DE  Interaction: Q8N6L0; IntAct: EBI-11530258; Score: 0.56
DE  Interaction: Q8N6G5; IntAct: EBI-11530249; Score: 0.56
DE  Interaction: P52290; IntAct: EBI-16254416; Score: 0.00
DE  Interaction: P40582; IntAct: EBI-16298792; Score: 0.00
DE  Interaction: P32621; IntAct: EBI-16298972; Score: 0.00
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0034399;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPTKSTFSRWKKADLIDLANKLEIDGFPNYAKKSDMIDYLESHLNHLEKPVDFKDDYPELRSFYESMTVDQSKDERNEYG
SQ  SGSGNGSGSGSCDTATNDSDLEKAYIKEDDDEKPQSGDETSATKPLSSRNANSNAKTNFNLLDFSTDNDSSTSAFTKFKF
SQ  NFQEYLSDIRYQTQKLNENVQDYLSTISAVDTIFSLLEFSFLVRNILAAGQPTSSSSLASSLEAAVAAHNKYQYTLDFCL
SQ  PILTWLLFFRGIPTLVSYYINFIRYDLNIELDPMTFNLTKFLISLAIFKTCNNKNIDFHSFRCVNQLWTQLCTVNRSLGM
SQ  VPLVFSMVSCLLTLYVL
//
ID  Q7Z2G1;
PN  Histone H2B type W-T;
GN  H2BW1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15475252}. Chromosome {ECO:0000269|PubMed:15475252}.
DR  UNIPROT: Q7Z2G1;
DR  UNIPROT: B1AK72;
DR  UNIPROT: Q147W3;
DR  Pfam: PF00125;
DR  OMIM: 300507;
DR  DisGeNET: 158983;
DE  Function: Atypical histone H2B. Nucleosomes containing it are structurally and dynamically indistinguishable from those containing conventional H2B. However, unlike conventional H2B, does not recruit chromosome condensation factors and does not participate in the assembly of mitotic chromosomes. May be important for telomere function. {ECO:0000269|PubMed:16449661}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6NXS1; IntAct: EBI-24677095; Score: 0.56
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0000786;
GO  GO:0003677;
GO  GO:0046982;
GO  GO:0030527;
GO  GO:0006334;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLRTEVPRLPRSTTAIVWSCHLMATASAMAGPSSETTSEEQLITQEPKEANSTTSQKQSKQRKRGRHGPRRCHSNCRGDS
SQ  FATYFRRVLKQVHQGLSLSREAVSVMDSLVHDILDRIATEAGRLARSTKRQTITAWETRMAVRLLLPGQMGKLAESEGTK
SQ  AVLRTSLYAIQQQRK
//
ID  Q90474;
PN  Heat shock protein HSP 90-alpha 1;
GN  hsp90a;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Melanosome {ECO:0000250|UniProtKB:P07900}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:18347070}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:18347070}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18347070}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Shuttles between the Z line and A band in response to stress conditions and fibril damage.
DR  UNIPROT: Q90474;
DR  UNIPROT: Q5RG13;
DR  UNIPROT: Q6DI33;
DR  Pfam: PF02518;
DR  Pfam: PF00183;
DR  PROSITE: PS00298;
DE  Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (By similarity). Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly (PubMed:10364427, PubMed:17586488, PubMed:18182494, PubMed:18256191). {ECO:0000250|UniProtKB:P07900, ECO:0000269|PubMed:10364427, ECO:0000269|PubMed:17586488, ECO:0000269|PubMed:18182494, ECO:0000269|PubMed:18256191}.
DE  Reference Proteome: Yes;
GO  GO:0031672;
GO  GO:0005829;
GO  GO:0042470;
GO  GO:0043209;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0030018;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0140662;
GO  GO:0097718;
GO  GO:0030235;
GO  GO:0051082;
GO  GO:0034605;
GO  GO:0050900;
GO  GO:0007517;
GO  GO:0030239;
GO  GO:0045429;
GO  GO:0006457;
GO  GO:0050821;
GO  GO:0010038;
GO  GO:0048769;
GO  GO:0030241;
GO  GO:0030240;
GO  GO:0014866;
GO  GO:0071688;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPEKSAQPVMEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSCKDLKIELIPD
SQ  QKERTLTIIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYIWE
SQ  SAAGGSFTVKPDFGESIGRGTKVILHLKEDQSEYVEEKRIKEVVKKHSQFIGYPITLYIEKQREKEVDLEEGEKQEEEEV
SQ  AAGEDKDKPKIEDLGADEDEDSKDGKNKRKKKVKEKYIDAQELNKTKPIWTRNPDDITNEEYGEFYKSLSNDWEDHLAVK
SQ  HFSVEGQLEFRALLFVPRRAAFDLFENKKKRNNIKLYVRRVFIMDNCEELIPEYLNFIKGVVDSEDLPLNISREMLQQSK
SQ  ILKVIRKNLVKKCLDLFTELAEDKDNYKKYYEQFSKNIKLGIHEDSQNRKKLSDLLRYYTSASGDEMVSLKDYVSRMKDT
SQ  QKHIYYITGETKDQVANSAFVERLRKAGLEVIYMIEPIDEYCVQQLKEYDGKNLVSVTKEGLELPEDEEEKKKQDELKAK
SQ  YENLCKIMKDILDKKIEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKSQALRDNSTMGYMTAKKHLEINPAHPIVETLR
SQ  EKAEADKNDKAVKDLVILLFETALLSSGFTLDDPQTHANRIYRMIKLGLGIDDDDSVVEEISQPAEEDMPVLEGDDDTSR
SQ  MEEVD
//
ID  M9PBE2;
PN  E3 ubiquitin-protein ligase Hakai;
GN  Hakai;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000305}. Cell membrane {ECO:0000305|PubMed:19682089}. Cytoplasmic vesicle {ECO:0000305|PubMed:19682089}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:19682089}.
DR  UNIPROT: M9PBE2;
DR  UNIPROT: Q86NQ9;
DR  UNIPROT: Q8INV9;
DR  UNIPROT: Q8INW0;
DR  UNIPROT: Q95RE3;
DR  UNIPROT: Q9VIT1;
DR  Pfam: PF18408;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase required during early development (PubMed:19682089). E3 ubiquitin-protein ligases mediate ubiquitination of target proteins (PubMed:19682089). Required for epithelial integrity and midgut morphogenesis (PubMed:19682089). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189). Its function in the WMM complex is unknown (PubMed:29535189). {ECO:0000250|UniProtKB:Q75N03, ECO:0000250|UniProtKB:Q9JIY2, ECO:0000269|PubMed:19682089, ECO:0000305|PubMed:29535189}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VU72; IntAct: EBI-198772; Score: 0.00
DE  Interaction: A1Z9X0; IntAct: EBI-200042; Score: 0.00
DE  Interaction: Q9VI24; IntAct: EBI-200115; Score: 0.00
DE  Interaction: Q9VI16; IntAct: EBI-200123; Score: 0.00
DE  Interaction: Q24558; IntAct: EBI-200119; Score: 0.00
DE  Interaction: P25171; IntAct: EBI-200127; Score: 0.00
DE  Interaction: Q7KTX7; IntAct: EBI-200132; Score: 0.00
DE  Interaction: Q9W2M4; IntAct: EBI-200136; Score: 0.00
DE  Interaction: Q9VU89; IntAct: EBI-200140; Score: 0.00
DE  Interaction: Q9VU18; IntAct: EBI-200144; Score: 0.00
DE  Interaction: Q9VI55; IntAct: EBI-200148; Score: 0.00
DE  Interaction: Q8T0I9; IntAct: EBI-200152; Score: 0.00
DE  Interaction: Q9V472; IntAct: EBI-200156; Score: 0.00
DE  Interaction: Q4Z8K6; IntAct: EBI-200160; Score: 0.00
DE  Interaction: Q9VGB9; IntAct: EBI-200164; Score: 0.00
DE  Interaction: Q9V9R6; IntAct: EBI-200172; Score: 0.00
DE  Interaction: Q9VN36; IntAct: EBI-200176; Score: 0.00
DE  Interaction: Q9VRC3; IntAct: EBI-200180; Score: 0.00
DE  Interaction: Q9XZU1; IntAct: EBI-200184; Score: 0.00
DE  Interaction: Q9VSQ3; IntAct: EBI-200188; Score: 0.00
DE  Interaction: Q9VC48; IntAct: EBI-200192; Score: 0.00
DE  Interaction: Q9VMS5; IntAct: EBI-200196; Score: 0.00
DE  Interaction: Q8MYW5; IntAct: EBI-200200; Score: 0.00
DE  Interaction: Q9VGU7; IntAct: EBI-200204; Score: 0.00
DE  Interaction: Q9W550; IntAct: EBI-200208; Score: 0.00
DE  Interaction: Q9VZT6; IntAct: EBI-200212; Score: 0.00
DE  Interaction: P54356; IntAct: EBI-200216; Score: 0.00
DE  Interaction: Q9VJE3; IntAct: EBI-200220; Score: 0.00
DE  Interaction: Q9VJ53; IntAct: EBI-200224; Score: 0.00
DE  Interaction: Q9VXD4; IntAct: EBI-200228; Score: 0.00
DE  Interaction: Q9VMD4; IntAct: EBI-200232; Score: 0.00
DE  Interaction: Q9VFU6; IntAct: EBI-200236; Score: 0.00
DE  Interaction: Q9VCM3; IntAct: EBI-200240; Score: 0.00
DE  Interaction: Q8T3Y1; IntAct: EBI-200244; Score: 0.00
DE  Interaction: B7YZT2; IntAct: EBI-200248; Score: 0.00
DE  Interaction: Q9V9V8; IntAct: EBI-200252; Score: 0.00
DE  Interaction: Q9VVV6; IntAct: EBI-200256; Score: 0.00
DE  Interaction: Q9VF73; IntAct: EBI-200260; Score: 0.00
DE  Interaction: P42282; IntAct: EBI-200264; Score: 0.00
DE  Interaction: Q9W3J9; IntAct: EBI-200268; Score: 0.00
DE  Interaction: Q9V9V0; IntAct: EBI-200272; Score: 0.00
DE  Interaction: O46070; IntAct: EBI-200276; Score: 0.00
DE  Interaction: Q9W5B6; IntAct: EBI-200280; Score: 0.00
DE  Interaction: Q9VEA5; IntAct: EBI-200284; Score: 0.00
DE  Interaction: M9MRI4; IntAct: EBI-200288; Score: 0.00
DE  Interaction: Q9VKQ0; IntAct: EBI-200292; Score: 0.00
DE  Interaction: Q9V4B8; IntAct: EBI-200296; Score: 0.00
DE  Interaction: Q9VZM9; IntAct: EBI-200300; Score: 0.00
DE  Interaction: Q9VSB2; IntAct: EBI-200304; Score: 0.00
DE  Interaction: Q9VPE1; IntAct: EBI-200308; Score: 0.00
DE  Interaction: Q9VQF9; IntAct: EBI-200313; Score: 0.00
DE  Interaction: A1ZAC8; IntAct: EBI-200317; Score: 0.00
DE  Interaction: Q9VDC1; IntAct: EBI-200321; Score: 0.00
DE  Interaction: Q9W1R5; IntAct: EBI-200325; Score: 0.00
DE  Interaction: Q9VSY2; IntAct: EBI-200329; Score: 0.00
DE  Interaction: P11455; IntAct: EBI-200333; Score: 0.00
DE  Interaction: Q9Y156; IntAct: EBI-200337; Score: 0.00
DE  Interaction: Q9VAZ1; IntAct: EBI-200345; Score: 0.00
DE  Interaction: Q8IQB8; IntAct: EBI-200341; Score: 0.00
DE  Interaction: Q9VD25; IntAct: EBI-200349; Score: 0.00
DE  Interaction: Q7K4Z4; IntAct: EBI-200353; Score: 0.00
DE  Interaction: Q94981; IntAct: EBI-200357; Score: 0.00
DE  Interaction: O76924; IntAct: EBI-200361; Score: 0.00
DE  Interaction: O97365; IntAct: EBI-200365; Score: 0.00
DE  Interaction: Q7JXC4; IntAct: EBI-200369; Score: 0.00
DE  Interaction: P23696; IntAct: EBI-200373; Score: 0.00
DE  Interaction: Q9V460; IntAct: EBI-200377; Score: 0.00
DE  Interaction: A1Z8L7; IntAct: EBI-200382; Score: 0.00
DE  Interaction: Q9VLP3; IntAct: EBI-200386; Score: 0.00
DE  Interaction: Q9VHR4; IntAct: EBI-200390; Score: 0.00
DE  Interaction: Q7K127; IntAct: EBI-200394; Score: 0.00
DE  Interaction: Q9VHG0; IntAct: EBI-200398; Score: 0.00
DE  Interaction: Q8T3X9; IntAct: EBI-200402; Score: 0.00
DE  Interaction: Q9VHA9; IntAct: EBI-200406; Score: 0.00
DE  Interaction: Q9V428; IntAct: EBI-200410; Score: 0.00
DE  Interaction: Q9W379; IntAct: EBI-200414; Score: 0.00
DE  Interaction: Q9W5X1; IntAct: EBI-200418; Score: 0.00
DE  Interaction: Q9VXE7; IntAct: EBI-200422; Score: 0.00
DE  Interaction: P22810; IntAct: EBI-26730114; Score: 0.49
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0036396;
GO  GO:0045296;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0008270;
GO  GO:0007015;
GO  GO:0040003;
GO  GO:0007391;
GO  GO:0007427;
GO  GO:0060429;
GO  GO:0030237;
GO  GO:0008258;
GO  GO:0007494;
GO  GO:0080009;
GO  GO:0016567;
GO  GO:0000381;
GO  GO:0030155;
GO  GO:0035282;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDTEEVKRGRGRGRGTRARGRGRGRGRGRGKKIDDSSIADAAALAASSCAALEDSPGRLDASEDSVMQELDKDGELETPG
SQ  ALEEPLPHGALGAVAASGNMTPATQQPQVLQQVPPPVMSQTTISLSLARAVDMEADISQLEAPTFTTLSRGPPEPMLRLK
SQ  WNHKVSLIGEKVLNPMIHCCDQCDKPILVYGRMIPCKHVFCLKCARAEPIKSCPRCTDKVLRVEQSGLGTVFMCTHGGSR
SQ  YGSSGCRRTYLSQRDLQAHINHRHVAPQPPPLQPQPQLSAMAEQPKMTDLGGVGLGLELHKQRKLSESSVPISVSASIAS
SQ  RPVLSRLPLTGGVGNIGSIGSIPPPGSAAAAQNAIHGGHSTLTLANLTRINNANAQECHQGKASLHHTLKKGTPHQSESV
SQ  ADASYYSSVLASFGSAAGNPGSGPPGGGATAAAQPANPSGSHSAVGPGALIGGSTDAPTGGSSGNWQQSQYYR
//
ID  O80528;
PN  Serine/threonine-protein kinase haspin homolog;
GN  HASPIN;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:21527018}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21527018}. Nucleus {ECO:0000269|PubMed:21527018}. Chromosome {ECO:0000269|PubMed:21527018}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:21527018}. Note=During interphase, localized in the cytoplasm and at the nuclear periphery. During prometaphase and metaphase, localized on chromosomes, and around the cell plate during cytokinesis. {ECO:0000269|PubMed:21527018}.
DR  UNIPROT: O80528;
DR  UNIPROT: Q84WE0;
DR  PROSITE: PS50011;
DE  Function: Threonine-protein kinase that phosphorylates histone H3 in vitro at 'Thr-3' (H3T3ph) and 'Thr-11' (H3T11ph), but not at 'Ser-10' (H3S10ph) or 'Ser-28' (H3S28ph). Plays a role in mitotic cell division during plant growth (PubMed:21527018). Threonine-protein kinase that phosphorylates histone H3 in vitro at 'Thr-3' (H3T3ph), but not at 'Thr-11' (H3T11ph), 'Ser-10' (H3S10ph) or 'Ser-28' (H3S28ph). Involved in histone H3 phosphorylation in mitotic cells. Contributes to organ and plant development, as well as embryonic patterning (PubMed:21749502). {ECO:0000269|PubMed:21527018, ECO:0000269|PubMed:21749502}.
DE  Reference Proteome: Yes;
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0009524;
GO  GO:0005524;
GO  GO:0035402;
GO  GO:0072354;
GO  GO:0106310;
GO  GO:0035556;
GO  GO:0000278;
GO  GO:0006468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGQRVDLWSEVIKSEEEDGDIPKIEAVFQRRKKPDKSSEAVNFGWLVKGARTSSVNGPKRDSWARSLSTRGRESIAVRAY
SQ  VNNQPQKKAAGRKKPPIPKGKVVKAPDFQKEKEYFRDIDAFELLEESPSPNKSSTWTMGEQVVPEMPHLSTRLEKWLISK
SQ  KLNHTCGPSSTLSKILENSAIHQESVCDNDAFDSLSLKTPDKSSAGNTSVFRLIPSCDENLAAEDVPVRKIKMESIDLED
SQ  ELKRLSLTSDLIPTHQDFDQPILDLLSACGQMRPSNFIEAFSKFCEPESIVKIGEGTYGEAFRAGSSVCKIVPIDGDFRV
SQ  NGEVQKRADELLEEVILSWTLNQLRECETTAQNLCPTYIKTQDIKLCQGPYDPILIKAWEEWDAKHGSENDHPDFPEKQC
SQ  YVMFVLEHGGKDLESFVLLNFDEARSLLVQATAGLAVAEAAFEFEHRDLHWGNILLSRNNSDTLPFILEGKQVCIKTFGV
SQ  QISIIDFTLSRINTGEKILFLDLTSDPYLFKGPKGDKQSETYRKMKAVTEDYWEGSFARTNVLWLIYLVDILLTKKSFER
SQ  SSKHERELRSLKKRMEKYESAKEAVSDPFFSDMLMDQIS
//
ID  P83103;
PN  Serine/threonine-protein kinase haspin homolog;
GN  Haspin;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus lamina {ECO:0000269|PubMed:32750047}. Chromosome {ECO:0000269|PubMed:32750047}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8TF76}.
DR  UNIPROT: P83103;
DR  UNIPROT: Q7PLN2;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DE  Function: Serine/threonine-protein kinase that phosphorylates histone H3 at 'Thr-4' (H3T3ph) during mitosis and interphase (PubMed:32750047). Function is essential for chromosome organization during mitosis and genome organization in interphase cells, thus playing a functional role in gene regulation (PubMed:32750047). During mitosis, may act through H3T3ph to both position and modulate activation of AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment and normal progression through the cell cycle (By similarity). During interphase, associates with the cohesion complex and mediates pds5 binding to chromatin to ensure correct sister chromatid cohesion, chromatin organization, and also functions with Pds5-cohesin to modify Polycomb- dependent homeotic transformations (PubMed:32750047). Function during interphase is required for insulator activity, nuclear compaction, heterochromatin-induced position-effect variegation and PcG-mediated pairing-sensitive silencing (PubMed:32750047). {ECO:0000250|UniProtKB:Q8TF76, ECO:0000269|PubMed:32750047}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005652;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0005524;
GO  GO:0072354;
GO  GO:0106310;
GO  GO:0035556;
GO  GO:0000278;
GO  GO:2000720;
GO  GO:0034093;
GO  GO:0120187;
GO  GO:0043687;
GO  GO:0006468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLSISKTKMDFLEEGRWKDPFDELLDSRTKLSKMNIVKQNVRVTYNIDSSVENSSYIEIKEPNHKNEPLTLEDCSIKVYC
SQ  PSDSISTPCDKRLGGTTGLFETDLSPITRLKLEGVEDSRDKCADTNEADLYVNVEILFQNINSSPKKCSNFGKKRLSNLN
SQ  KMVTAVHPSISLNPGKWRKSLNNFIRSKITETNFTKKVERRSSICQDRKSLVLKGEHKFENKYEEDVLKYCHQCTPLPFN
SQ  TAYEQHKLLNTKKIGEGAYGEVFRCSRNQEVLKDHISDIVLKIIPLEGSTVINGEKQKTFSQILPEIIITKKMCSLRTSK
SQ  TNSTNGFVSIQKVSLVKGRYPPHFIKLWEKYDNEKGSENDHPELFGDNQLFAVLELKFAGSDMANFKFLNSEQSYYALQQ
SQ  IILALAVGEEEYQFEHRDLHLGNILIEYTNKKHIVCTFKSSNLTLLSKGVNVTIIDYTLSRVTINDCCYFNDLSRDEELF
SQ  QATGDYQYDVYRMMRNELKNNWSSFSPKTNIIWLSYVIVKVLDSVKYKSINTKVHRMYIDKIKELKNIIMTFESASHCAN
SQ  YLFNLN
//
ID  Q2KIE2;
PN  HCLS1-associated protein X-1;
GN  HAX1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion {ECO:0000250|UniProtKB:O00165}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O00165}. Nucleus membrane {ECO:0000250|UniProtKB:O00165}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O35387}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O00165}. Cell membrane {ECO:0000250|UniProtKB:O00165}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00165}; Cytoplasmic side {ECO:0000250|UniProtKB:O00165}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q7TSE9}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O00165}. Cytoplasm {ECO:0000250|UniProtKB:O00165}. Nucleus {ECO:0000250|UniProtKB:O00165}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited (in vitro). {ECO:0000250|UniProtKB:O00165}.
DR  UNIPROT: Q2KIE2;
DE  Function: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools. {ECO:0000250|UniProtKB:O00165}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0031410;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0000932;
GO  GO:0005886;
GO  GO:0016529;
GO  GO:0043066;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O00165};
SQ  MSLFDLFRGFFGFSGPRSHRDPFFGGMTRDEDEDDEEEEEEGVTWGRGNSRFEGPQSPEEFSFGFSFSPGGGMRFHDNFG
SQ  FDDLVRDFNNIFSEMGAWTLPSRPPELPGPESETPGERRQEGQTLRDSMLKYPDSHQPKIFGGGLESDARSESSKPAPDW
SQ  GPQRPFHRFDDTWPVTPHSRAREDNDLDTQVSQEGLGPVLQPQPKSYFKSVSVTKITKPDGTVEERRTVVDSEGRKETTV
SQ  THQEAGSSPRDGPESPTPPSLDDSSSILDLFLGRWFRSR
//
ID  O00165;
PN  HCLS1-associated protein X-1;
GN  HAX1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion {ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:9058808}. Endoplasmic reticulum {ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:9058808}. Nucleus membrane {ECO:0000269|PubMed:9058808}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O35387}. Cytoplasm, cell cortex {ECO:0000269|PubMed:26997484}. Cell membrane {ECO:0000269|PubMed:26997484}; Peripheral membrane protein {ECO:0000269|PubMed:26997484}; Cytoplasmic side {ECO:0000269|PubMed:26997484}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q7TSE9}. Cytoplasm, P-body {ECO:0000269|PubMed:23164465}. [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:23164465, ECO:0000269|PubMed:25298122}. Nucleus {ECO:0000269|PubMed:23164465}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited, and in response to cellular stress caused by arsenite (in vitro). {ECO:0000269|PubMed:23164465}. [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:23164465}. Nucleus {ECO:0000269|PubMed:23164465}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited (in vitro). {ECO:0000269|PubMed:23164465}. [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:23164465}. Nucleus {ECO:0000269|PubMed:23164465}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000269|PubMed:23164465}. [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:23164465}. Note=Predominantly cytoplasmic. {ECO:0000269|PubMed:23164465}.
DR  UNIPROT: O00165;
DR  UNIPROT: A8W4W9;
DR  UNIPROT: A8W4X0;
DR  UNIPROT: B4DUJ7;
DR  UNIPROT: Q5VYD5;
DR  UNIPROT: Q5VYD7;
DR  UNIPROT: Q96AU4;
DR  UNIPROT: Q9BS80;
DR  OMIM: 605998;
DR  OMIM: 610738;
DR  DisGeNET: 10456;
DE  Function: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex (PubMed:26997484). Slows down the rate of inactivation of KCNC3 channels (PubMed:26997484). Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools. {ECO:0000269|PubMed:15339924, ECO:0000269|PubMed:16857965, ECO:0000269|PubMed:17545607, ECO:0000269|PubMed:18319618, ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:26997484, ECO:0000269|PubMed:9058808}.
DE  Disease: Neutropenia, severe congenital 3, autosomal recessive (SCN3) [MIM:610738]: A disorder of hematopoiesis characterized by maturation arrest of granulopoiesis at the level of promyelocytes with peripheral blood absolute neutrophil counts below 0.5 x 10(9)/l and early onset of severe bacterial infections. Some patients affected by severe congenital neutropenia type 3 have neurological manifestations such as psychomotor retardation and seizures. {ECO:0000269|PubMed:17187068, ECO:0000269|PubMed:18337561, ECO:0000269|PubMed:19796188, ECO:0000269|PubMed:20220065}. Note=The disease is caused by variants affecting the gene represented in this entry. The clinical phenotype due to HAX1 deficiency appears to depend on the localization of the mutations and their influence on the transcript variants. Mutations affecting exclusively isoform 1 are associated with isolated congenital neutropenia, whereas mutations affecting both isoform 1 and isoform 5 are associated with additional neurologic symptoms (PubMed:18337561). {ECO:0000269|PubMed:18337561}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q99759; IntAct: EBI-362136; Score: 0.00
DE  Interaction: Q04206; IntAct: EBI-363244; Score: 0.00
DE  Interaction: P19438; IntAct: EBI-364357; Score: 0.00
DE  Interaction: P20333; IntAct: EBI-364585; Score: 0.00
DE  Interaction: Q16760; IntAct: EBI-734287; Score: 0.00
DE  Interaction: O12160; IntAct: EBI-7845312; Score: 0.64
DE  Interaction: O00303; IntAct: EBI-758371; Score: 0.37
DE  Interaction: O70127; IntAct: EBI-930216; Score: 0.40
DE  Interaction: Q6PSM0; IntAct: EBI-930234; Score: 0.40
DE  Interaction: Q15714; IntAct: EBI-1085974; Score: 0.00
DE  Interaction: P13569; IntAct: EBI-1171360; Score: 0.35
DE  Interaction: Q8AZK7; IntAct: EBI-9632715; Score: 0.53
DE  Interaction: O46385; IntAct: EBI-7874199; Score: 0.27
DE  Interaction: Q5NE99; IntAct: EBI-2806387; Score: 0.00
DE  Interaction: Q5NFJ2; IntAct: EBI-2806394; Score: 0.00
DE  Interaction: A0A0F7R9R7; IntAct: EBI-2811156; Score: 0.00
DE  Interaction: Q81VT8; IntAct: EBI-2811888; Score: 0.00
DE  Interaction: A0A6L7HRI8; IntAct: EBI-2813096; Score: 0.00
DE  Interaction: Q81M67; IntAct: EBI-2816763; Score: 0.00
DE  Interaction: A0A2P0H993; IntAct: EBI-2816781; Score: 0.00
DE  Interaction: A0A6H3ACS9; IntAct: EBI-2832676; Score: 0.00
DE  Interaction: Q81SR4; IntAct: EBI-2832662; Score: 0.00
DE  Interaction: A0A4Y1WB04; IntAct: EBI-2832641; Score: 0.00
DE  Interaction: A0A6L8PU14; IntAct: EBI-2832669; Score: 0.00
DE  Interaction: Q81KV7; IntAct: EBI-2832655; Score: 0.00
DE  Interaction: Q81WU4; IntAct: EBI-2832648; Score: 0.00
DE  Interaction: A0A6L7HHZ0; IntAct: EBI-2832709; Score: 0.00
DE  Interaction: A0A6L7H2Q9; IntAct: EBI-2832690; Score: 0.00
DE  Interaction: A0A6L7H5N1; IntAct: EBI-2832683; Score: 0.00
DE  Interaction: A0A6L7HH25; IntAct: EBI-2832697; Score: 0.00
DE  Interaction: A0A0J1KLZ7; IntAct: EBI-2832716; Score: 0.00
DE  Interaction: A0A6H3AND8; IntAct: EBI-2832723; Score: 0.00
DE  Interaction: A0A380PD11; IntAct: EBI-2840043; Score: 0.00
DE  Interaction: A0A3N4AYP8; IntAct: EBI-2843166; Score: 0.00
DE  Interaction: A0A3G5LD16; IntAct: EBI-2843155; Score: 0.00
DE  Interaction: A0A380PL54; IntAct: EBI-2847491; Score: 0.00
DE  Interaction: A0A380PNP6; IntAct: EBI-2847479; Score: 0.00
DE  Interaction: Q8CLE0; IntAct: EBI-2868346; Score: 0.00
DE  Interaction: Q8CZR2; IntAct: EBI-2868335; Score: 0.00
DE  Interaction: Q8D014; IntAct: EBI-2868325; Score: 0.00
DE  Interaction: A0A5P8YFI0; IntAct: EBI-2868386; Score: 0.00
DE  Interaction: A0A380PFG3; IntAct: EBI-2868379; Score: 0.00
DE  Interaction: Q8CKN6; IntAct: EBI-2868353; Score: 0.00
DE  Interaction: A0A5P8YJT1; IntAct: EBI-2868365; Score: 0.00
DE  Interaction: A0A5P8YBY1; IntAct: EBI-2868372; Score: 0.00
DE  Interaction: Q7CG77; IntAct: EBI-2868393; Score: 0.00
DE  Interaction: Q8ZBU3; IntAct: EBI-2868430; Score: 0.00
DE  Interaction: Q7ARD3; IntAct: EBI-2868400; Score: 0.00
DE  Interaction: Q8ZHF4; IntAct: EBI-2868407; Score: 0.00
DE  Interaction: Q8ZCH3; IntAct: EBI-2868418; Score: 0.00
DE  Interaction: P69961; IntAct: EBI-2868442; Score: 0.00
DE  Interaction: Q8ZIY3; IntAct: EBI-2868449; Score: 0.00
DE  Interaction: Q8ZDX4; IntAct: EBI-2868456; Score: 0.00
DE  Interaction: P03372; IntAct: EBI-3895734; Score: 0.53
DE  Interaction: P48454; IntAct: EBI-3935613; Score: 0.37
DE  Interaction: P51692; IntAct: EBI-3935643; Score: 0.37
DE  Interaction: P53779; IntAct: EBI-3935623; Score: 0.55
DE  Interaction: P27694; IntAct: EBI-3935633; Score: 0.37
DE  Interaction: P62877; IntAct: EBI-3935653; Score: 0.37
DE  Interaction: Q9P1U0; IntAct: EBI-3941813; Score: 0.37
DE  Interaction: P0DPB6; IntAct: EBI-3941823; Score: 0.37
DE  Interaction: Q8TAQ5; IntAct: EBI-3943650; Score: 0.37
DE  Interaction: Q14451; IntAct: EBI-4288461; Score: 0.51
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: Q8JPQ9; IntAct: EBI-6159460; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6268389; Score: 0.35
DE  Interaction: Q86Z02; IntAct: EBI-6381086; Score: 0.35
DE  Interaction: O14980; IntAct: EBI-8162190; Score: 0.40
DE  Interaction: Q9NPI6; IntAct: EBI-8162243; Score: 0.27
DE  Interaction: Q13619; IntAct: EBI-21324822; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q8NHX9; IntAct: EBI-8817387; Score: 0.59
DE  Interaction: Q9ULQ1; IntAct: EBI-8817427; Score: 0.53
DE  Interaction: Q8TE30; IntAct: EBI-8874742; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-9054212; Score: 0.67
DE  Interaction: P58340; IntAct: EBI-9358437; Score: 0.40
DE  Interaction: Q8K2C9; IntAct: EBI-9358459; Score: 0.40
DE  Interaction: Q13200; IntAct: EBI-9358502; Score: 0.40
DE  Interaction: Q15773; IntAct: EBI-9358480; Score: 0.40
DE  Interaction: Q16659; IntAct: EBI-12502733; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: Q13563; IntAct: EBI-9837080; Score: 0.37
DE  Interaction: P30411; IntAct: EBI-9843662; Score: 0.37
DE  Interaction: P01583; IntAct: EBI-10488769; Score: 0.62
DE  Interaction: Q13418; IntAct: EBI-10103376; Score: 0.53
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: Q9NVH1; IntAct: EBI-11107761; Score: 0.35
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135399; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-11139064; Score: 0.35
DE  Interaction: O94905; IntAct: EBI-11425731; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9BW83; IntAct: EBI-12453281; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-11897791; Score: 0.53
DE  Interaction: Q68871; IntAct: EBI-12518818; Score: 0.51
DE  Interaction: P03452; IntAct: EBI-12577240; Score: 0.35
DE  Interaction: P06821; IntAct: EBI-12577493; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-12579142; Score: 0.35
DE  Interaction: P03428; IntAct: EBI-12579909; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581764; Score: 0.35
DE  Interaction: Q5EP37; IntAct: EBI-12582596; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12588098; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12588729; Score: 0.35
DE  Interaction: Q7RTP6; IntAct: EBI-13945615; Score: 0.35
DE  Interaction: O14829; IntAct: EBI-14024386; Score: 0.35
DE  Interaction: Q9BY84; IntAct: EBI-14027455; Score: 0.35
DE  Interaction: P13591; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q9UQM7; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q9UPY8; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q9ULP0; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q9P121; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q9NRW1; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q9H4G0; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q9H115; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q9BPU6; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q99880; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q92777; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q8NCB2; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q8IZL9; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q16623; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q16555; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q14847; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q14194; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q13554; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q12860; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q05193; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q01484; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P84074; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P62760; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P61764; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P61601; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P61266; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P59768; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P43304; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P42658; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P42262; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P37235; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P32004; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P31323; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P22676; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P21579; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P20648; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P20336; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P17600; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P16401; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P11137; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P09471; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P05090; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: O60641; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: O43854; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: O43602; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: O15075; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: O00429; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: B7Z613; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: Q14195; IntAct: EBI-21602719; Score: 0.35
DE  Interaction: P51674; IntAct: EBI-21648883; Score: 0.35
DE  Interaction: O15126; IntAct: EBI-21648858; Score: 0.35
DE  Interaction: Q9H4B6; IntAct: EBI-16427846; Score: 0.74
DE  Interaction: Q96RS6; IntAct: EBI-20723859; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: O95831; IntAct: EBI-16786283; Score: 0.42
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: P13073; IntAct: EBI-16791533; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797429; Score: 0.27
DE  Interaction: O75880; IntAct: EBI-16799233; Score: 0.27
DE  Interaction: Q9H9B4; IntAct: EBI-16799442; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16795231; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: Q9BRX2; IntAct: EBI-20567704; Score: 0.66
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: X6RFA8; IntAct: EBI-21265624; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P03427; IntAct: EBI-21268420; Score: 0.35
DE  Interaction: Q6ZRI8; IntAct: EBI-25410669; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: O95072; IntAct: EBI-25483697; Score: 0.35
DE  Interaction: P59046; IntAct: EBI-25499386; Score: 0.37
DE  Interaction: P0DTC5; IntAct: EBI-25685699; Score: 0.35
DE  Interaction: Q8N4Q1; IntAct: EBI-25744959; Score: 0.35
DE  Interaction: O43572; IntAct: EBI-26451580; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-25902182; Score: 0.56
DE  Interaction: Q15047; IntAct: EBI-25909133; Score: 0.56
DE  Interaction: Q92993; IntAct: EBI-25912324; Score: 0.56
DE  Interaction: Q8TAP4; IntAct: EBI-25926058; Score: 0.56
DE  Interaction: O43464; IntAct: EBI-27049380; Score: 0.42
DE  Interaction: Q96LU5; IntAct: EBI-27049466; Score: 0.27
DE  Interaction: P83111; IntAct: EBI-27049642; Score: 0.27
DE  Interaction: Q96E52; IntAct: EBI-27049801; Score: 0.27
DE  Interaction: Q9H300; IntAct: EBI-27049982; Score: 0.27
DE  Interaction: Q96TA2; IntAct: EBI-27050177; Score: 0.27
DE  Interaction: O14733; IntAct: EBI-28930089; Score: 0.35
DE  Interaction: O14757; IntAct: EBI-28930743; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-28931531; Score: 0.35
DE  Interaction: P22612; IntAct: EBI-28934688; Score: 0.35
DE  Interaction: P43250; IntAct: EBI-28935197; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-28935882; Score: 0.35
DE  Interaction: P53671; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q6P5Z2; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q7Z695; IntAct: EBI-28941998; Score: 0.35
DE  Interaction: Q92918; IntAct: EBI-28944233; Score: 0.35
DE  Interaction: Q9BXA6; IntAct: EBI-28945972; Score: 0.35
DE  Interaction: Q9H3Y6; IntAct: EBI-28946258; Score: 0.35
DE  Interaction: Q9NR20; IntAct: EBI-28946409; Score: 0.35
DE  Interaction: Q9NRM7; IntAct: EBI-28946455; Score: 0.35
DE  Interaction: Q9NSY0; IntAct: EBI-28946547; Score: 0.35
DE  Interaction: O95476; IntAct: EBI-27113178; Score: 0.35
DE  Interaction: O14595; IntAct: EBI-27113200; Score: 0.35
DE  Interaction: O14830; IntAct: EBI-27113806; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: P35916; IntAct: EBI-32718614; Score: 0.42
DE  Interaction: P08069; IntAct: EBI-32718669; Score: 0.35
DE  Interaction: P06213; IntAct: EBI-32718777; Score: 0.35
DE  Interaction: P04629; IntAct: EBI-32719115; Score: 0.35
DE  Interaction: Q16288; IntAct: EBI-32719212; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-32719716; Score: 0.35
GO  GO:0015629;
GO  GO:0016324;
GO  GO:0005938;
GO  GO:0030136;
GO  GO:0005783;
GO  GO:0030027;
GO  GO:0005758;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0000932;
GO  GO:0016529;
GO  GO:0005667;
GO  GO:0019966;
GO  GO:0047485;
GO  GO:0071345;
GO  GO:0043066;
GO  GO:2000251;
GO  GO:0030854;
GO  GO:0033138;
GO  GO:0050731;
GO  GO:0014068;
GO  GO:0051897;
GO  GO:0045944;
GO  GO:0030833;
GO  GO:0042981;
GO  GO:1903146;
GO  GO:1903214;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:26997484};
SQ  MSLFDLFRGFFGFPGPRSHRDPFFGGMTRDEDDDEEEEEEGGSWGRGNPRFHSPQHPPEEFGFGFSFSPGGGIRFHDNFG
SQ  FDDLVRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDW
SQ  GSQRPFHRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSYFKSISVTKITKPDGIVEERRTVVDSEGRTETTV
SQ  TRHEADSSPRGDPESPRPPALDDAFSILDLFLGRWFRSR
//
ID  O35387;
PN  HCLS1-associated protein X-1;
GN  Hax1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion {ECO:0000269|PubMed:16814492}. Endoplasmic reticulum {ECO:0000269|PubMed:10760273}. Nucleus membrane {ECO:0000305|PubMed:16814492}. Cytoplasmic vesicle {ECO:0000269|PubMed:10760273, ECO:0000269|PubMed:16814492}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O00165}. Cell membrane {ECO:0000250|UniProtKB:O00165}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00165}; Cytoplasmic side {ECO:0000250|UniProtKB:O00165}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q7TSE9}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O00165}. Cytoplasm {ECO:0000250|UniProtKB:O00165}. Nucleus {ECO:0000250|UniProtKB:O00165}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited (in vitro). {ECO:0000250|UniProtKB:O00165}.
DR  UNIPROT: O35387;
DR  UNIPROT: Q542F8;
DE  Function: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools. {ECO:0000250|UniProtKB:O00165}.
DE  Reference Proteome: Yes;
DE  Interaction: P42227; IntAct: EBI-657283; Score: 0.37
DE  Interaction: Q8BWG8; IntAct: EBI-649719; Score: 0.37
DE  Interaction: Q8CIH5; IntAct: EBI-649769; Score: 0.37
DE  Interaction: Q13563; IntAct: EBI-9635489; Score: 0.51
DE  Interaction: O14925; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: Q9H477; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: H3BS42; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: P56199; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: Q92604; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: P12236; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: Q9H061; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: Q7KZ85; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: O15066; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: Q9H078; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: O75165; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: G3XAN4; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: B4E1G1; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: Q5XJY4; IntAct: EBI-15687233; Score: 0.52
DE  Interaction: Q9JIY5; IntAct: EBI-15687275; Score: 0.52
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0015629;
GO  GO:0016324;
GO  GO:0005938;
GO  GO:0030136;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0043231;
GO  GO:0030027;
GO  GO:0005758;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0000932;
GO  GO:0016529;
GO  GO:0005667;
GO  GO:0019966;
GO  GO:0019904;
GO  GO:0047485;
GO  GO:0007166;
GO  GO:0071345;
GO  GO:0043066;
GO  GO:2000251;
GO  GO:0030854;
GO  GO:0033138;
GO  GO:0050731;
GO  GO:0014068;
GO  GO:0051897;
GO  GO:0045944;
GO  GO:0030833;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O00165};
SQ  MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDDDDDDEAEEDRGAWGRESYAFDGSQPPEEFGFSFSPRGGMRFHGNF
SQ  GFDDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESPKPAPD
SQ  WGSQGPFHRLDDTWPVSPHSRAKEDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEERRTVVDSEGRRETT
SQ  VTHQEAHDSSRSDPDSQRSSALDDPFSILDLLLGRWFRSR
//
ID  Q7TSE9;
PN  HCLS1-associated protein X-1;
GN  Hax1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion {ECO:0000269|PubMed:19913549}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O00165}. Nucleus membrane {ECO:0000250|UniProtKB:O00165}. Cytoplasmic vesicle {ECO:0000269|PubMed:15159385}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O00165}. Cell membrane {ECO:0000250|UniProtKB:O00165}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00165}; Cytoplasmic side {ECO:0000250|UniProtKB:O00165}. Sarcoplasmic reticulum {ECO:0000269|PubMed:19913549}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O00165}. Cytoplasm {ECO:0000269|PubMed:23164465}. Nucleus {ECO:0000250|UniProtKB:O00165}. [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:23164465}. Nucleus {ECO:0000250|UniProtKB:O00165}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited, and in response to cellular stress caused by arsenite (in vitro). {ECO:0000250|UniProtKB:O00165}.
DR  UNIPROT: Q7TSE9;
DR  UNIPROT: Q5D1N3;
DR  UNIPROT: Q5D1N4;
DR  UNIPROT: Q7TSE7;
DR  UNIPROT: Q7TSE8;
DE  Function: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools. {ECO:0000250|UniProtKB:O00165, ECO:0000269|PubMed:15159385, ECO:0000269|PubMed:19913549}.
DE  Reference Proteome: Yes;
DE  Interaction: Q08201; IntAct: EBI-930001; Score: 0.51
DE  Interaction: O70127; IntAct: EBI-930049; Score: 0.60
DE  Interaction: Q6PSM0; IntAct: EBI-930069; Score: 0.51
DE  Interaction: O70420; IntAct: EBI-930391; Score: 0.40
GO  GO:0015629;
GO  GO:0016324;
GO  GO:0005938;
GO  GO:0030136;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0043231;
GO  GO:0030027;
GO  GO:0005758;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0000932;
GO  GO:0016529;
GO  GO:0005667;
GO  GO:0019966;
GO  GO:0019904;
GO  GO:0047485;
GO  GO:0071345;
GO  GO:0043066;
GO  GO:2000251;
GO  GO:0030854;
GO  GO:0033138;
GO  GO:0050731;
GO  GO:0014068;
GO  GO:0051897;
GO  GO:0045944;
GO  GO:0030833;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O00165};
SQ  MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDEDDEEEEDSGAWGRESYAFDGFHPTEEFGFSFSPRGGMRFHGNFGF
SQ  DDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGVRLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESSKPAPDWG
SQ  SQGPFHRLDDTWPVSPHSRAREDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEEHRTVVDSEGRRETTVT
SQ  HQEAHDSSRSDPDPPRSSALDDPFSILDLLLGRWFRSR
//
ID  Q5T447;
PN  E3 ubiquitin-protein ligase HECTD3;
GN  HECTD3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q5T447;
DR  UNIPROT: B3KPV7;
DR  UNIPROT: B3KRH4;
DR  UNIPROT: Q5T448;
DR  UNIPROT: Q9H783;
DR  Pfam: PF03256;
DR  Pfam: PF00632;
DR  PROSITE: PS51284;
DR  PROSITE: PS50237;
DR  OMIM: 618638;
DR  DisGeNET: 79654;
DE  Function: E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus facilitating cell cycle progression by regulating the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By similarity). {ECO:0000250|UniProtKB:Q3U487, ECO:0000269|PubMed:18194665}.
DE  Reference Proteome: Yes;
DE  Interaction: P0DTD1; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: Q15796; IntAct: EBI-2691165; Score: 0.00
DE  Interaction: Q7Z434; IntAct: EBI-6115727; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-6425955; Score: 0.40
DE  Interaction: Q8IUH5; IntAct: EBI-9088791; Score: 0.37
DE  Interaction: O60437; IntAct: EBI-24537202; Score: 0.56
DE  Interaction: D2XQB9; IntAct: EBI-14063588; Score: 0.35
DE  Interaction: Q8N5F7; IntAct: EBI-21520423; Score: 0.35
DE  Interaction: P82930; IntAct: EBI-21521832; Score: 0.35
DE  Interaction: P13994; IntAct: EBI-21552344; Score: 0.35
DE  Interaction: Q8N0V3; IntAct: EBI-21561897; Score: 0.35
DE  Interaction: Q8IUX8; IntAct: EBI-21565522; Score: 0.35
DE  Interaction: Q6UWQ5; IntAct: EBI-21641185; Score: 0.35
DE  Interaction: Q7Z4W2; IntAct: EBI-21670934; Score: 0.35
DE  Interaction: O75596; IntAct: EBI-21674079; Score: 0.35
DE  Interaction: Q6IN84; IntAct: EBI-21721548; Score: 0.35
DE  Interaction: Q96NG3; IntAct: EBI-21726764; Score: 0.35
DE  Interaction: P05154; IntAct: EBI-21730352; Score: 0.35
DE  Interaction: Q8N4T0; IntAct: EBI-21731449; Score: 0.35
DE  Interaction: A8MT70; IntAct: EBI-21738250; Score: 0.35
DE  Interaction: O15123; IntAct: EBI-21738454; Score: 0.35
DE  Interaction: P01350; IntAct: EBI-21738479; Score: 0.35
DE  Interaction: P15408; IntAct: EBI-21738528; Score: 0.35
DE  Interaction: E7EPC3; IntAct: EBI-21738429; Score: 0.35
DE  Interaction: Q2MKA7; IntAct: EBI-21738795; Score: 0.35
DE  Interaction: Q9BU40; IntAct: EBI-21739567; Score: 0.35
DE  Interaction: Q6NZI2; IntAct: EBI-21738912; Score: 0.35
DE  Interaction: Q7L0Y3; IntAct: EBI-21739027; Score: 0.35
DE  Interaction: Q8NBL1; IntAct: EBI-21739323; Score: 0.35
DE  Interaction: Q8NBX0; IntAct: EBI-21739378; Score: 0.35
DE  Interaction: Q96EL2; IntAct: EBI-21739451; Score: 0.35
DE  Interaction: Q9BYG5; IntAct: EBI-21739610; Score: 0.35
DE  Interaction: Q9H9Q2; IntAct: EBI-21739689; Score: 0.35
DE  Interaction: Q9H1F0; IntAct: EBI-21739868; Score: 0.35
DE  Interaction: Q99501; IntAct: EBI-21832664; Score: 0.35
DE  Interaction: P62701; IntAct: EBI-21876649; Score: 0.40
DE  Interaction: Q96PQ6; IntAct: EBI-21890582; Score: 0.35
DE  Interaction: P11166; IntAct: EBI-20903936; Score: 0.40
DE  Interaction: O84388; IntAct: EBI-22302856; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P22607; IntAct: EBI-25854798; Score: 0.56
DE  Interaction: Q14957; IntAct: EBI-25862911; Score: 0.56
DE  Interaction: P06396; IntAct: EBI-25864492; Score: 0.56
DE  Interaction: Q9Y649; IntAct: EBI-25901376; Score: 0.56
DE  Interaction: Q9UMX0; IntAct: EBI-25921251; Score: 0.56
DE  Interaction: Q6ZNK6; IntAct: EBI-26453464; Score: 0.35
DE  Interaction: P34972; IntAct: EBI-26880846; Score: 0.35
GO  GO:0048471;
GO  GO:0019905;
GO  GO:0004842;
GO  GO:0043161;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGPGPGAVLESPRQLLGRVRFLAEAARSLRAGRPLPAALAFVPREVLYKLYKDPAGPSRVLLPVWEAEGLGLRVGAAGP
SQ  APGTGSGPLRAARDSIELRRGACVRTTGEELCNGHGLWVKLTKEQLAEHLGDCGLQEGWLLVCRPAEGGARLVPIDTPNH
SQ  LQRQQQLFGVDYRPVLRWEQVVDLTYSHRLGSRPQPAEAYAEAVQRLLYVPPTWTYECDEDLIHFLYDHLGKEDENLGSV
SQ  KQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEGDNL
SQ  KKLSDVSIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPTSLVRYPRLEGTD
SQ  PEVLYRRAVLLQRFIKILDSVLHHLVPAWDHTLGTFSEIKQVKQFLLLSRQRPGLVAQCLRDSESSKPSFMPRLYINRRL
SQ  AMEHRACPSRDPACKNAVFTQVYEGLKPSDKYEKPLDYRWPMRYDQWWECKFIAEGIIDQGGGFRDSLADMSEELCPSSA
SQ  DTPVPLPFFVRTANQGNGTGEARDMYVPNPSCRDFAKYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSKDFPA
SQ  VDSVLVKLLEVMEGMDKETFEFKFGKELTFTTVLSDQQVVELIPGGAGIVVGYGDRSRFIQLVQKARLEESKEQVAAMQA
SQ  GLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLTRFEDFEPSDSRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA
SQ  RIYIYPDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYAAYNCVAIDTDMSPWEE
//
ID  Q3U487;
PN  E3 ubiquitin-protein ligase HECTD3;
GN  Hectd3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:18821010}.
DR  UNIPROT: Q3U487;
DR  UNIPROT: B1AUL1;
DR  UNIPROT: Q3TN76;
DR  UNIPROT: Q641P3;
DR  UNIPROT: Q8BQ74;
DR  UNIPROT: Q8R1L6;
DR  Pfam: PF03256;
DR  Pfam: PF00632;
DR  PROSITE: PS51284;
DR  PROSITE: PS50237;
DE  Function: E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus facilitating cell cycle progression by regulating the turn-over of TRIOBP (By similarity). Mediates also ubiquitination of STX8. {ECO:0000250|UniProtKB:Q5T447, ECO:0000269|PubMed:18821010}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0019905;
GO  GO:0004842;
GO  GO:0043161;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGPGPGAALESPRQLLGRVRFLAEAARSLRAGLPLPAALAFVPREVLYKLYKDPAGPSRVLLPVWEAEGLGLRVGAVGA
SQ  APGTGSGPLRAARDSIELRRGACVRTTGEELCNGHGLWVKLTKEQLAEHLSDCSLDEGWLLVCRPAEGGARLVPIDTPDH
SQ  LQRQQQLFGVDYRPVLRWEQVVDLTYSHRLGSRPQPAEAYTEAIQRLLYVPPTWTYECDEDLIHFLYDHLGKEDENLGSV
SQ  KQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEGDNL
SQ  KKLSDVNIDETLIGDVCVLEDMTVHLPIIEIRIVECRDDGIDVRLRGVKIKSSRQRELGLNADLFQPASLVRYPRLEGTD
SQ  PEVLYRRAVLLQRFIKILDSVLHHLVPAWDHTLGTFSEIKQVKQFLLLSRQRPSLVAQCLRDSESSKPSFMPRLYINRRL
SQ  AMEHRACPSRDPACKNAVFTQVYEGLKPSDKYEKPLDYRWPMRYDQWWECKFIAEGIIDQGGGFRDSLADMSEELCPSSA
SQ  DTPVPLPFFVRTANQGNGTGEARDMYVPNPSCRDFAKYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSKDFPA
SQ  VDSVLVKLLEVMEGVDKETFEFKFGKELTFTTVLSDQQVVELIPGGTGIVVEYEDRSRFIQLVRKARLEESKEQVAAMQA
SQ  GLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDALRKLTRFEDFEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA
SQ  RIYIYPDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYAAYNCVAIDTDMSPWEE
//
ID  Q03281;
PN  Inner nuclear membrane protein HEH2;
GN  HEH2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16929305}; Single-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16929305}. Note=Targeting to the inner nuclear membrane requires the SRP1 and KAP95 karyopherins and the Ran cycle.
DR  UNIPROT: Q03281;
DR  UNIPROT: D6VT82;
DR  PDB: 4PVZ;
DR  Pfam: PF12949;
DR  Pfam: PF09402;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P38181; IntAct: EBI-10052697; Score: 0.44
DE  Interaction: P39929; IntAct: EBI-10052667; Score: 0.58
DE  Interaction: Q02821; IntAct: EBI-15598611; Score: 0.76
DE  Interaction: P32462; IntAct: EBI-789522; Score: 0.35
DE  Interaction: P47088; IntAct: EBI-856789; Score: 0.00
DE  Interaction: P11484; IntAct: EBI-3689025; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3805388; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3811847; Score: 0.35
DE  Interaction: P52917; IntAct: EBI-10053328; Score: 0.40
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0034399;
GO  GO:0003682;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDHRNLDPKTLKVSQLRRVLVENDVAFPANARKPVLVKLFEEKVRQRLQSSPEASKVRTSIQKVVKSGAKNADRKKTLKS
SQ  KKLESSSSESKTVKDENVETNKRKREQISTDNEAKMQIQEEKSPKKKRKKRSSKANKPPESPPQSKSDGKATSADLTSEL
SQ  ETVEELHKKDSSDDKPRVKELPKPELPNLKVSNEFLAQLNKELASAATENYDHSIKSTDLSSIRIETEEPVGPSTGAETR
SQ  NESEVMENINLEVQPEVKEAKEELTKISETFDNQDEEDTSRLSSKKNIRSPKGRTRHFIANKTKRGIDIMKPFIAHLFIW
SQ  LWNGAIFLSIICPILFGLWYREQRIQVGYCGHEKPLKSLAISAFPQTERVDSVLQAYRPNCLECPEHGICSSFMNVECEP
SQ  GYEPKSSILETYGIIPFPKYCAKDESKEKEVDELVWKVNEYLKKKNAQHECGEGENLFESGETETKLYDIFSHSRPSWES
SQ  QREFNDHWKNVLEILKKKDDIIWLPLDFETNGKREKSKSNNTNYIYRSTSKKWVTLQCHLEGDIQEYITKYGGSLFITLG
SQ  VLFLIKKIQSTLDNYVQGEQIIEKLVKEAIDKLKDVKKNKGEEPFLTTVQLRATLLSDIPNIKEQNNLWAQTKEKIMKEQ
SQ  SENIELYLLEENGEIMTCWEWKE
//
ID  Q9UII4;
PN  E3 ISG15--protein ligase HERC5;
GN  HERC5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20542004}. Note=Associated with the polyribosomes, probably via the 60S subunit.
DR  UNIPROT: Q9UII4;
DR  UNIPROT: B2RTQ1;
DR  UNIPROT: Q69G20;
DR  Pfam: PF00632;
DR  Pfam: PF00415;
DR  PROSITE: PS50237;
DR  PROSITE: PS00626;
DR  PROSITE: PS50012;
DR  OMIM: 608242;
DR  DisGeNET: 51191;
DE  Function: Major E3 ligase for ISG15 conjugation. Acts as a positive regulator of innate antiviral response in cells induced by interferon. Functions as part of the ISGylation machinery that recognizes target proteins in a broad and relatively non-specific manner. Catalyzes ISGylation of IRF3 which results in sustained activation, it attenuates IRF3-PIN1 interaction, which antagonizes IRF3 ubiquitination and degradation, and boosts the antiviral response. Catalyzes ISGylation of influenza A viral NS1 which attenuates virulence; ISGylated NS1 fails to form homodimers and thus to interact with its RNA targets. Catalyzes ISGylation of papillomavirus type 16 L1 protein which results in dominant-negative effect on virus infectivity. Physically associated with polyribosomes, broadly modifies newly synthesized proteins in a cotranslational manner. In an interferon-stimulated cell, newly translated viral proteins are primary targets of ISG15. {ECO:0000269|PubMed:16407192, ECO:0000269|PubMed:16815975, ECO:0000269|PubMed:16884686, ECO:0000269|PubMed:20133869, ECO:0000269|PubMed:20308324, ECO:0000269|PubMed:20385878, ECO:0000269|PubMed:20542004}.
DE  Reference Proteome: Yes;
DE  Interaction: P59595; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8K4B0; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9UKV8; IntAct: EBI-7642941; Score: 0.35
DE  Interaction: P51965; IntAct: EBI-2339545; Score: 0.37
DE  Interaction: Q96LR5; IntAct: EBI-2339579; Score: 0.37
DE  Interaction: Q969T4; IntAct: EBI-2339769; Score: 0.37
DE  Interaction: Q8WVJ2; IntAct: EBI-9484933; Score: 0.40
DE  Interaction: Q12952; IntAct: EBI-11321256; Score: 0.35
DE  Interaction: Q08050; IntAct: EBI-11321374; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q9JJR9; IntAct: EBI-11017700; Score: 0.35
DE  Interaction: P33981; IntAct: EBI-11027245; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: F8VQC1; IntAct: EBI-11054725; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-11088773; Score: 0.35
DE  Interaction: P37840; IntAct: EBI-11113842; Score: 0.35
DE  Interaction: Q8TF76; IntAct: EBI-11146909; Score: 0.35
DE  Interaction: Q76RH4; IntAct: EBI-14063348; Score: 0.35
DE  Interaction: Q9GZY0; IntAct: EBI-21528397; Score: 0.35
DE  Interaction: O43159; IntAct: EBI-21627620; Score: 0.35
DE  Interaction: Q9P031; IntAct: EBI-21664473; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-21677299; Score: 0.35
DE  Interaction: Q9BSG1; IntAct: EBI-21680046; Score: 0.35
DE  Interaction: Q8WYQ5; IntAct: EBI-21679517; Score: 0.35
DE  Interaction: Q5T3I0; IntAct: EBI-21681508; Score: 0.35
DE  Interaction: Q07020; IntAct: EBI-21680991; Score: 0.35
DE  Interaction: A2RU67; IntAct: EBI-21694732; Score: 0.35
DE  Interaction: P50914; IntAct: EBI-21741266; Score: 0.35
DE  Interaction: Q9Y3C1; IntAct: EBI-21875103; Score: 0.35
DE  Interaction: P03495; IntAct: EBI-15833966; Score: 0.54
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q99558; IntAct: EBI-21261374; Score: 0.35
DE  Interaction: Q4FZB7; IntAct: EBI-25485626; Score: 0.40
DE  Interaction: A0A0F6B063; IntAct: EBI-27033283; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-27102259; Score: 0.53
DE  Interaction: P15130; IntAct: EBI-27131516; Score: 0.35
DE  Interaction: Q0ZME3; IntAct: EBI-27131755; Score: 0.35
DE  Interaction: Q6Q1R8; IntAct: EBI-27132003; Score: 0.35
DE  Interaction: K9N4V7; IntAct: EBI-27132270; Score: 0.35
DE  Interaction: P33469; IntAct: EBI-27132272; Score: 0.35
DE  Interaction: P46108; IntAct: EBI-30821447; Score: 0.44
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0030332;
GO  GO:0042296;
GO  GO:0003723;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0032020;
GO  GO:0016567;
GO  GO:0000079;
GO  GO:0050688;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERRSRRKSRRNGRSTAGKAAATQPAKSPGAQLWLFPSAAGLHRALLRRVEVTRQLCCSPGRLAVLERGGAGVQVHQLLA
SQ  GSGGARTPKCIKLGKNMKIHSVDQGAEHMLILSSDGKPFEYDNYSMKHLRFESILQEKKIIQITCGDYHSLALSKGGELF
SQ  AWGQNLHGQLGVGRKFPSTTTPQIVEHLAGVPLAQISAGEAHSMALSMSGNIYSWGKNECGQLGLGHTESKDDPSLIEGL
SQ  DNQKVEFVACGGSHSALLTQDGLLFTFGAGKHGQLGHNSTQNELRPCLVAELVGYRVTQIACGRWHTLAYVSDLGKVFSF
SQ  GSGKDGQLGNGGTRDQLMPLPVKVSSSEELKLESHTSEKELIMIAGGNQSILLWIKKENSYVNLKRTIPTLNEGTVKRWI
SQ  ADVETKRWQSTKREIQEIFSSPACLTGSFLRKRRTTEMMPVYLDLNKARNIFKELTQKDWITNMITTCLKDNLLKRLPFH
SQ  SPPQEALEIFFLLPECPMMHISNNWESLVVPFAKVVCKMSDQSSLVLEEYWATLQESTFSKLVQMFKTAVICQLDYWDES
SQ  AEENGNVQALLEMLKKLHRVNQVKCQLPESIFQVDELLHRLNFFVEVCRRYLWKMTVDASENVQCCVIFSHFPFIFNNLS
SQ  KIKLLHTDTLLKIESKKHKAYLRSAAIEEERESEFALRPTFDLTVRRNHLIEDVLNQLSQFENEDLRKELWVSFSGEIGY
SQ  DLGGVKKEFFYCLFAEMIQPEYGMFMYPEGASCMWFPVKPKFEKKRYFFFGVLCGLSLFNCNVANLPFPLALFKKLLDQM
SQ  PSLEDLKELSPDLGKNLQTLLDDEGDNFEEVFYIHFNVHWDRNDTNLIPNGSSITVNQTNKRDYVSKYINYIFNDSVKAV
SQ  YEEFRRGFYKMCDEDIIKLFHPEELKDVIVGNTDYDWKTFEKNARYEPGYNSSHPTIVMFWKAFHKLTLEEKKKFLVFLT
SQ  GTDRLQMKDLNNMKITFCCPESWNERDPIRALTCFSVLFLPKYSTMETVEEALQEAINNNRGFG
//
ID  P59723;
PN  Hypoxia-inducible factor 1-alpha inhibitor;
GN  hif1an;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9NWT6}.
DR  UNIPROT: P59723;
DR  UNIPROT: B8A5K4;
DR  Pfam: PF13621;
DR  PROSITE: PS51184;
DE  Function: Hydroxylates a specific Asn residue in the C-terminal transactivation domain (CAD) of HIF-1 alpha. The hydroxylation prevents interaction of HIF-1 with transcriptional coactivators. Also hydroxylates specific Asn, Asp and His residues within ankyrin repeat domain-containing proteins. {ECO:0000250|UniProtKB:Q9NWT6}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016706;
GO  GO:0071532;
GO  GO:0031406;
GO  GO:0008198;
GO  GO:0102113;
GO  GO:0036140;
GO  GO:0036139;
GO  GO:0042803;
GO  GO:0008270;
GO  GO:0045746;
GO  GO:0061428;
GO  GO:1901343;
GO  GO:0042265;
GO  GO:0042264;
GO  GO:0036138;
GO  GO:0030947;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETDGAAAFTELRDPDWDESQLRQYTFPTRQIPRLSHTDPRAEVLINNEEPVVLTDTSLVYPALKWDIPYLQENIGNGD
SQ  FSVYIAENHKFLYYDEKKMVNFQDFVPKSRRIEMKFSEFVDKMHQTEEQGGKGRVYLQQTLNDTVGRKIVVDFLGFNWNW
SQ  INKQQAKRNWGPLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGHKRCILFPPDQFDCLYPYPVHHPCDRQSQVDFENPDY
SQ  DKFPNFKNAVGYEAVVGPGDVLYIPMYWWHHIESLLNGGETITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEA
SQ  LGDPHEVGPLLNMMIKGRYDHGLS
//
ID  Q9NWT6;
PN  Hypoxia-inducible factor 1-alpha inhibitor;
GN  HIF1AN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Mainly cytoplasmic localization, but interaction with NOTCH1 results in nuclear localization and interaction with ABPA3 results in perinuclear localization in macrophages.
DR  UNIPROT: Q9NWT6;
DR  UNIPROT: D3DR69;
DR  UNIPROT: Q5W147;
DR  UNIPROT: Q969Q7;
DR  UNIPROT: Q9NPV5;
DR  PDB: 1H2K;
DR  PDB: 1H2L;
DR  PDB: 1H2M;
DR  PDB: 1H2N;
DR  PDB: 1IZ3;
DR  PDB: 1MZE;
DR  PDB: 1MZF;
DR  PDB: 1YCI;
DR  PDB: 2CGN;
DR  PDB: 2CGO;
DR  PDB: 2ILM;
DR  PDB: 2W0X;
DR  PDB: 2WA3;
DR  PDB: 2WA4;
DR  PDB: 2XUM;
DR  PDB: 2Y0I;
DR  PDB: 2YC0;
DR  PDB: 2YDE;
DR  PDB: 3D8C;
DR  PDB: 3KCX;
DR  PDB: 3KCY;
DR  PDB: 3OD4;
DR  PDB: 3P3N;
DR  PDB: 3P3P;
DR  PDB: 4AI8;
DR  PDB: 4B7E;
DR  PDB: 4B7K;
DR  PDB: 4BIO;
DR  PDB: 4JAA;
DR  PDB: 4NR1;
DR  PDB: 4Z1V;
DR  PDB: 4Z2W;
DR  PDB: 5JWK;
DR  PDB: 5JWL;
DR  PDB: 5JWP;
DR  PDB: 5OP6;
DR  PDB: 5OP8;
DR  PDB: 5OPC;
DR  PDB: 6H9J;
DR  PDB: 6HA6;
DR  PDB: 6HC8;
DR  PDB: 6HKP;
DR  PDB: 6HL5;
DR  PDB: 6HL6;
DR  PDB: 6RUJ;
DR  PDB: 7A1J;
DR  PDB: 7A1K;
DR  PDB: 7A1L;
DR  PDB: 7A1M;
DR  PDB: 7A1N;
DR  PDB: 7A1O;
DR  PDB: 7A1P;
DR  PDB: 7A1Q;
DR  PDB: 7A1S;
DR  Pfam: PF13621;
DR  PROSITE: PS51184;
DR  OMIM: 606615;
DR  DisGeNET: 55662;
DE  Function: Hydroxylates HIF-1 alpha at 'Asn-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation. {ECO:0000269|PubMed:12042299, ECO:0000269|PubMed:12080085, ECO:0000269|PubMed:17003112, ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18299578, ECO:0000269|PubMed:19245366, ECO:0000269|PubMed:21177872, ECO:0000269|PubMed:21251231}.
DE  Reference Proteome: Yes;
DE  Interaction: O75190; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O95271; IntAct: EBI-8565753; Score: 0.78
DE  Interaction: O96018; IntAct: EBI-15099018; Score: 0.75
DE  Interaction: P58546; IntAct: EBI-15602804; Score: 0.44
DE  Interaction: Q06787; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q86UE4; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q8WXH0; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9H4L5; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q9NUQ3; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q96DX5; IntAct: EBI-754615; Score: 0.78
DE  Interaction: Q8WXK3; IntAct: EBI-755812; Score: 0.55
DE  Interaction: Q9Y283; IntAct: EBI-759370; Score: 0.64
DE  Interaction: Q16665; IntAct: EBI-1035055; Score: 0.92
DE  Interaction: Q6GQQ9; IntAct: EBI-2510717; Score: 0.56
DE  Interaction: Q9H2K2; IntAct: EBI-8565642; Score: 0.74
DE  Interaction: Q8TAK5; IntAct: EBI-8565789; Score: 0.44
DE  Interaction: Q9HBA0; IntAct: EBI-8565771; Score: 0.44
DE  Interaction: Q8IY67; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P54132; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8NB46; IntAct: EBI-12502476; Score: 0.64
DE  Interaction: Q05823; IntAct: EBI-12502476; Score: 0.79
DE  Interaction: Q9NVH0; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9NWX5; IntAct: EBI-12502476; Score: 0.53
DE  Interaction: Q68DC2; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9NU02; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O95218; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q969S3; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8N5A5; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9NUD5; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8WYQ9; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q86T24; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9BQA1; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q96MT7; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q14157; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9UPQ9; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9UM00; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9Y4G6; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q99081; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q15370; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q15369; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9UNL2; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9Y2K2; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P60468; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O43159; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P62847; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P62841; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q5VT52; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P61927; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P61353; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-12502476; Score: 0.50
DE  Interaction: Q7L0Y3; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q04206; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9HCJ3; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q2TAL8; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O00487; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9UNM6; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O75832; IntAct: EBI-12502476; Score: 0.59
DE  Interaction: P62195; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P35998; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q5H9R7; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9UPN7; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O15355; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P62875; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P30876; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q4KWH8; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O60733; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8IZ21; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P08237; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8N3A8; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9BXW6; IntAct: EBI-12502476; Score: 0.53
DE  Interaction: Q9H857; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9UM47; IntAct: EBI-12502476; Score: 0.53
DE  Interaction: Q04721; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9Y3T9; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O00221; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P25963; IntAct: EBI-12502476; Score: 0.73
DE  Interaction: Q00653; IntAct: EBI-12502476; Score: 0.53
DE  Interaction: Q9P032; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9Y6Q9; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9HCH0; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P41227; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9NZJ7; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8TE76; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q5TCX8; IntAct: EBI-12502476; Score: 0.64
DE  Interaction: Q15773; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q96AX9; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O43318; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q7L5Y9; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9BRK4; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P83369; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9ULH0; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8N163; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q7LBC6; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q96SI1; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-12502476; Score: 0.59
DE  Interaction: Q12894; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9ULT8; IntAct: EBI-12502476; Score: 0.64
DE  Interaction: Q00341; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O15379; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9Y450; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9H6D7; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8IYU2; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9UKJ3; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O60547; IntAct: EBI-12502476; Score: 0.53
DE  Interaction: Q9NRA8; IntAct: EBI-12502476; Score: 0.53
DE  Interaction: P06730; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9H9B1; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q96F86; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9Y678; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: A5YKK6; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q99439; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q96ST8; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q5VT06; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q12834; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8WXE0; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9UKZ1; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9BY42; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q6ZUT1; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P20290; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8NBU5; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9H765; IntAct: EBI-12502476; Score: 0.64
DE  Interaction: P27540; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q92625; IntAct: EBI-12502476; Score: 0.64
DE  Interaction: Q9ULJ7; IntAct: EBI-24286767; Score: 0.56
DE  Interaction: Q8N8A2; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: O15084; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q96NW4; IntAct: EBI-12502476; Score: 0.53
DE  Interaction: O75179; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q8IWZ3; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q9P2R3; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770028; Score: 0.70
DE  Interaction: P46531; IntAct: EBI-11473706; Score: 0.44
DE  Interaction: P19838; IntAct: EBI-11322417; Score: 0.74
DE  Interaction: P47086; IntAct: EBI-11532399; Score: 0.56
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q6PG48; IntAct: EBI-24615512; Score: 0.56
DE  Interaction: Q7Z713; IntAct: EBI-24425210; Score: 0.56
DE  Interaction: Q9H672; IntAct: EBI-24534882; Score: 0.56
DE  Interaction: Q8NFD2; IntAct: EBI-25272595; Score: 0.67
DE  Interaction: Q96P71; IntAct: EBI-15098946; Score: 0.40
DE  Interaction: Q9Y575; IntAct: EBI-21571836; Score: 0.35
DE  Interaction: Q9UPU5; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q9H6R7; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q9BQS8; IntAct: EBI-21638930; Score: 0.53
DE  Interaction: Q8WXD9; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q8TES7; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q8TBX8; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q15653; IntAct: EBI-21638930; Score: 0.53
DE  Interaction: Q05086; IntAct: EBI-21638930; Score: 0.53
DE  Interaction: Q04864; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q01484; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: P78356; IntAct: EBI-21638930; Score: 0.53
DE  Interaction: P55196; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: P47974; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: P40222; IntAct: EBI-21638930; Score: 0.53
DE  Interaction: Q12955; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q8WXI3; IntAct: EBI-21754620; Score: 0.35
DE  Interaction: Q9BW85; IntAct: EBI-21758292; Score: 0.35
DE  Interaction: Q9Y574; IntAct: EBI-21801297; Score: 0.35
DE  Interaction: Q8WVL7; IntAct: EBI-21811862; Score: 0.69
DE  Interaction: Q3KP44; IntAct: EBI-21876401; Score: 0.35
DE  Interaction: Q96NS5; IntAct: EBI-21897846; Score: 0.35
DE  Interaction: Q495B1; IntAct: EBI-21900536; Score: 0.40
DE  Interaction: Q9UK73; IntAct: EBI-15602843; Score: 0.59
DE  Interaction: Q9BZF9; IntAct: EBI-15602883; Score: 0.51
DE  Interaction: Q06547; IntAct: EBI-15603005; Score: 0.44
DE  Interaction: P55273; IntAct: EBI-15603110; Score: 0.44
DE  Interaction: O14974; IntAct: EBI-15603359; Score: 0.44
DE  Interaction: Q9UL18; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: P09012; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: O14497; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q4U2R6; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q9Y2X3; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q9Y2T7; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q9UQ35; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q9H4B7; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q9BWF3; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q9BVA1; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q9BU76; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q9BPZ3; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q99700; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q96MR6; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q96EK7; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q92925; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q92784; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q92734; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q8WUZ0; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q8NFD5; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q8N5F7; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q6PKG0; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q4VC05; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q15020; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q13838; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q13243; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q12926; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q07955; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: P82664; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: P51531; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: P51532; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-16814752; Score: 0.53
DE  Interaction: Q7L014; IntAct: EBI-16814752; Score: 0.35
DE  Interaction: Q13772; IntAct: EBI-16814752; Score: 0.35
DE  Interaction: P48668; IntAct: EBI-16814752; Score: 0.35
DE  Interaction: Q969F8; IntAct: EBI-21282024; Score: 0.40
DE  Interaction: Q71UM5; IntAct: EBI-25479285; Score: 0.35
DE  Interaction: P50502; IntAct: EBI-25479285; Score: 0.35
DE  Interaction: Q9Y6H1; IntAct: EBI-25479285; Score: 0.35
DE  Interaction: P40763; IntAct: EBI-25485488; Score: 0.40
DE  Interaction: Q59H18; IntAct: EBI-28941654; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0016706;
GO  GO:0071532;
GO  GO:0031406;
GO  GO:0008198;
GO  GO:0102113;
GO  GO:0051059;
GO  GO:0005112;
GO  GO:0019826;
GO  GO:0036140;
GO  GO:0036139;
GO  GO:0042803;
GO  GO:0008270;
GO  GO:0045746;
GO  GO:0061428;
GO  GO:0042265;
GO  GO:0042264;
GO  GO:0036138;
GO  GO:0045663;
GO  GO:2001214;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEY
SQ  LQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVM
SQ  DFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQS
SQ  QVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMR
SQ  NIEKMLGEALGNPQEVGPLLNTMIKGRYN
//
ID  Q8BLR9;
PN  Hypoxia-inducible factor 1-alpha inhibitor;
GN  Hif1an;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm {ECO:0000250|UniProtKB:Q9NWT6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9NWT6}.
DR  UNIPROT: Q8BLR9;
DR  UNIPROT: A1L3B7;
DR  UNIPROT: Q3U3G4;
DR  Pfam: PF13621;
DR  PROSITE: PS51184;
DE  Function: Hydroxylates HIF-1 alpha at 'Asn-799' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation (By similarity). Positively regulates ASB4 activity, promoting vascular differentiation. {ECO:0000250|UniProtKB:Q9NWT6, ECO:0000269|PubMed:17636018}.
DE  Reference Proteome: Yes;
DE  Interaction: Q07279; IntAct: EBI-26677785; Score: 0.37
DE  Interaction: Q8VIM5; IntAct: EBI-26677793; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016706;
GO  GO:0071532;
GO  GO:0031406;
GO  GO:0008198;
GO  GO:0102113;
GO  GO:0051059;
GO  GO:0005112;
GO  GO:0036140;
GO  GO:0036139;
GO  GO:0042803;
GO  GO:0008270;
GO  GO:0045746;
GO  GO:0061428;
GO  GO:0042265;
GO  GO:0042264;
GO  GO:0036138;
GO  GO:0045663;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAATAAEVAASGSGEAREEAEAPGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEY
SQ  LQENIGNGDFSVYSASTHKFLYYDEKKMGNFQNFKPRSNREEIKFHEFVEKLQAIQQRGGEERLYLQQTLNDTVGRKIVM
SQ  DFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGHKRCILFPPDQFECLYPYPVHHPCDRQS
SQ  QVDFDNPDYERFPNFRNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMR
SQ  NIEKMLGEALGNPQEVGPLLNTMIKGRYN
//
ID  O75146;
PN  Huntingtin-interacting protein 1-related protein;
GN  HIP1R;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Note=Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region.
DR  UNIPROT: O75146;
DR  UNIPROT: A6NHQ6;
DR  UNIPROT: Q6NXG8;
DR  UNIPROT: Q9UED9;
DR  PDB: 1R0D;
DR  Pfam: PF07651;
DR  Pfam: PF16515;
DR  Pfam: PF01608;
DR  PROSITE: PS50942;
DR  PROSITE: PS50945;
DR  OMIM: 605613;
DR  DisGeNET: 9026;
DE  Function: Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3- phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. {ECO:0000269|PubMed:11889126, ECO:0000269|PubMed:14732715}.
DE  Reference Proteome: Yes;
DE  Interaction: O14976; IntAct: EBI-11150908; Score: 0.53
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q62925; IntAct: EBI-9971384; Score: 0.00
DE  Interaction: Q13404; IntAct: EBI-9971384; Score: 0.00
DE  Interaction: P22314; IntAct: EBI-9971384; Score: 0.00
DE  Interaction: P61088; IntAct: EBI-9971384; Score: 0.00
DE  Interaction: P60033; IntAct: EBI-10766934; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q9ERG0; IntAct: EBI-11054044; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079358; Score: 0.35
DE  Interaction: P09497; IntAct: EBI-11081190; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: Q13492; IntAct: EBI-11082344; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: Q9WTI7; IntAct: EBI-11093786; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11098811; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: Q9UBB9; IntAct: EBI-24361039; Score: 0.56
DE  Interaction: O14777; IntAct: EBI-24400766; Score: 0.56
DE  Interaction: P14373; IntAct: EBI-25262907; Score: 0.56
DE  Interaction: C5E519; IntAct: EBI-12583021; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-21512742; Score: 0.35
DE  Interaction: Q6PJG9; IntAct: EBI-21552126; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-21559824; Score: 0.35
DE  Interaction: P46059; IntAct: EBI-21560916; Score: 0.35
DE  Interaction: Q14627; IntAct: EBI-21561326; Score: 0.35
DE  Interaction: P21709; IntAct: EBI-21595997; Score: 0.35
DE  Interaction: Q86VU5; IntAct: EBI-21596714; Score: 0.35
DE  Interaction: Q8N6K0; IntAct: EBI-21599984; Score: 0.35
DE  Interaction: O95274; IntAct: EBI-21607810; Score: 0.35
DE  Interaction: P35813; IntAct: EBI-21660332; Score: 0.35
DE  Interaction: Q96D71; IntAct: EBI-21660332; Score: 0.35
DE  Interaction: Q15311; IntAct: EBI-21660332; Score: 0.35
DE  Interaction: Q10567; IntAct: EBI-21660332; Score: 0.35
DE  Interaction: P23246; IntAct: EBI-21660332; Score: 0.35
DE  Interaction: O75688; IntAct: EBI-21660332; Score: 0.35
DE  Interaction: O00291; IntAct: EBI-21660332; Score: 0.35
DE  Interaction: Q96FJ0; IntAct: EBI-21668214; Score: 0.35
DE  Interaction: O60939; IntAct: EBI-21671922; Score: 0.35
DE  Interaction: A2RU67; IntAct: EBI-21694732; Score: 0.35
DE  Interaction: Q9NZQ7; IntAct: EBI-21740460; Score: 0.35
DE  Interaction: Q9NUM3; IntAct: EBI-21748242; Score: 0.35
DE  Interaction: Q8N468; IntAct: EBI-21785908; Score: 0.35
DE  Interaction: O75146; IntAct: EBI-15564862; Score: 0.56
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.53
DE  Interaction: Q9BYP7; IntAct: EBI-28946054; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-27127141; Score: 0.35
GO  GO:0016324;
GO  GO:0005938;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0030665;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0032839;
GO  GO:0043197;
GO  GO:0043231;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0032587;
GO  GO:0097060;
GO  GO:0051015;
GO  GO:0035615;
GO  GO:0030276;
GO  GO:0032051;
GO  GO:0042802;
GO  GO:0035091;
GO  GO:0005547;
GO  GO:0043325;
GO  GO:0080025;
GO  GO:0005546;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0017124;
GO  GO:0007015;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:0048268;
GO  GO:0055123;
GO  GO:0006897;
GO  GO:0030837;
GO  GO:0043066;
GO  GO:0034316;
GO  GO:0043065;
GO  GO:1905445;
GO  GO:0045742;
GO  GO:1901030;
GO  GO:2000588;
GO  GO:0032092;
GO  GO:0050821;
GO  GO:0006898;
GO  GO:0032956;
GO  GO:2000369;
GO  GO:0030100;
GO  GO:0060453;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNSIKNVPARVLSRRPGHSLEAEREQFDKTQAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSS
SQ  ILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIREIGDLWGHLHDRYGQLVNVYTKLLLTKISFHLKHPQFPAGLEVTDEV
SQ  LEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLLFKLHSC
SQ  LPADTLQGHRDRFHEQFHSLRNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEDEEPENLIE
SQ  ISTGPPAGEPVVVADLFDQTFGPPNGSVKDDRDLQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRK
SQ  QKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQ
SQ  SQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALS
SQ  GAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAERESQEQGLRQRLLDEQFAVLRGAAAEAAGILQDAVS
SQ  KLDDPLHLRCTSSPDYLVSRAQEALDAVSTLEEGHAQYLTSLADASALVAALTRFSHLAADTIINGGATSHLAPTDPADR
SQ  LIDTCRECGARALELMGQLQDQQALRHMQASLVRTPLQGILQLGQELKPKSLDVRQEELGAVVDKEMAATSAAIEDAVRR
SQ  IEDMMNQARHASSGVKLEVNERILNSCTDLMKAIRLLVTTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVG
SQ  WGATQLVEAADKVVLHTGKYEELIVCSHEIAASTAQLVAASKVKANKHSPHLSRLQECSRTVNERAANVVASTKSGQEQI
SQ  EDRDTMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERMRLGELRKQHYVLAGASGSPGEEVAIRPSTAPRSVTTKKPPL
SQ  AQKPSVAPRQDHQLDKKDGIYPAQLVNY
//
ID  Q9JKY5;
PN  Huntingtin-interacting protein 1-related protein;
GN  Hip1r;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Note=Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region.
DR  UNIPROT: Q9JKY5;
DR  UNIPROT: Q3UJ14;
DR  Pfam: PF07651;
DR  Pfam: PF16515;
DR  Pfam: PF01608;
DR  PROSITE: PS50942;
DR  PROSITE: PS50945;
DE  Function: Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3- phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis.
DE  Reference Proteome: Yes;
DE  Interaction: Q01279; IntAct: EBI-27088765; Score: 0.40
DE  Interaction: P04973; IntAct: EBI-7374625; Score: 0.37
DE  Interaction: P04975; IntAct: EBI-7374604; Score: 0.57
DE  Interaction: Q61210; IntAct: EBI-649779; Score: 0.37
DE  Interaction: Q60598; IntAct: EBI-7285203; Score: 0.49
DE  Interaction: Q96B97; IntAct: EBI-7167363; Score: 0.40
DE  Interaction: G3V6K6; IntAct: EBI-27088754; Score: 0.52
GO  GO:0016324;
GO  GO:0005938;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0030665;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0032839;
GO  GO:0043197;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0032587;
GO  GO:0097060;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0035615;
GO  GO:0030276;
GO  GO:0032051;
GO  GO:0042802;
GO  GO:0035091;
GO  GO:0005547;
GO  GO:0043325;
GO  GO:0080025;
GO  GO:0005546;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0017124;
GO  GO:0007015;
GO  GO:0006919;
GO  GO:0006915;
GO  GO:0048268;
GO  GO:0055123;
GO  GO:0006897;
GO  GO:0061024;
GO  GO:0030837;
GO  GO:0043066;
GO  GO:0034316;
GO  GO:0043065;
GO  GO:1905445;
GO  GO:2000370;
GO  GO:0045742;
GO  GO:1901030;
GO  GO:2000588;
GO  GO:0032092;
GO  GO:0050821;
GO  GO:0006898;
GO  GO:0032956;
GO  GO:2000369;
GO  GO:0030100;
GO  GO:0060453;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNSIKNVPARVLSRRPGHSLEAEREQFDKTQAISISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLSSSS
SQ  ILSWKFCHVLHKVLRDGHPNVLHDYQRYRSNIREIGDLWGHLRDQYGHLVNIYTKLLLTKISFHLKHPQFPAGLEVTDEV
SQ  LEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLMFKLHSC
SQ  LPADTLQGHRDRFHEQFHSLKNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEEEEPENLIE
SQ  ISSAPPAGEPVVVADLFDQTFGPPNGSMKDDRDLQIENLKREVETLRAELEKIKMEAQRYISQLKGQVNGLEAELEEQRK
SQ  QKQKALVDNEQLRHELAQLKALQLEGARNQGLREEAERKASATEARYSKLKEKHSELINTHAELLRKNADTAKQLTVTQQ
SQ  SQEEVARVKEQLAFQMEQAKRESEMKMEEQSDQLEKLKRELAARAGELARAQEALSRTEQSGSELSSRLDTLNAEKEALS
SQ  GVVRQREAELLAAQSLVREKEEALSQEQQRSSQEKGELRGQLAEKESQEQGLRQKLLDEQLAVLRSAAAEAEAILQDAVS
SQ  KLDDPLHLRCTSSPDYLVSRAQAALDSVSGLEQGHTQYLASSEDASALVAALTRFSHLAADTIVNGAATSHLAPTDPADR
SQ  LMDTCRECGARALELVGQLQDQTVLPRAQPSLMRAPLQGILQLGQDLKPKSLDVRQEELGAMVDKEMAATSAAIEDAVRR
SQ  IEDMMSQARHESSGVKLEVNERILNSCTDLMKAIRLLVMTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVG
SQ  WGATQLVESADKVVLHMGKYEELIVCSHEIAASTAQLVAASKVKANKNSPHLSRLQECSRTVNERAANVVASTKSGQEQI
SQ  EDRDTMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERVRLGELRKQHYVLAGGMGTPSEEEPSRPSPAPRSGATKKPPL
SQ  AQKPSIAPRTDNQLDKKDGVYPAQLVNY
//
ID  Q9SZN7;
PN  Heavy metal-associated isoprenylated plant protein 26;
GN  HIPP26;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:18974936}. Cell membrane {ECO:0000269|PubMed:18823312}. Note=PubMed:18974936 shows that isopernylation may be important for a speckle-like nuclear localization in a heterologous system, while PubMed:18823312 shows a plasma membrane localization. {ECO:0000269|PubMed:18823312, ECO:0000269|PubMed:18974936}.
DR  UNIPROT: Q9SZN7;
DR  UNIPROT: Q8LGG1;
DR  UNIPROT: Q9ZRE4;
DR  Pfam: PF00403;
DR  PROSITE: PS50846;
DE  Function: Heavy-metal-binding protein. Binds lead, cadmium and copper. May be involved in heavy-metal transport (PubMed:18823312). May be involved in cadmium transport and play a role in cadmium detoxification (PubMed:21072340). {ECO:0000269|PubMed:18823312, ECO:0000269|PubMed:21072340}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9STP8; IntAct: EBI-2008217; Score: 0.58
DE  Interaction: Q9SEZ1; IntAct: EBI-2027471; Score: 0.51
DE  Interaction: Q9LK09; IntAct: EBI-9161847; Score: 0.35
DE  Interaction: Q9SZU7; IntAct: EBI-25529995; Score: 0.56
DE  Interaction: Q9SQR3; IntAct: EBI-25530237; Score: 0.56
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0009506;
GO  GO:0046870;
GO  GO:0005507;
GO  GO:0032791;
GO  GO:0010286;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:18974936};
SQ  MGVLDHVSEMFDCSHGHKIKKRKQLQTVEIKVKMDCEGCERKVRRSVEGMKGVSSVTLEPKAHKVTVVGYVDPNKVVARM
SQ  SHRTGKKVELWPYVPYDVVAHPYAAGVYDKKAPSGYVRRVDDPGVSQLARASSTEVRYTTAFSDENPAACVVM
//
ID  P12683;
PN  3-hydroxy-3-methylglutaryl-coenzyme A reductase 1;
GN  HMG1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8744950}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: P12683;
DR  UNIPROT: D6W0K8;
DR  Pfam: PF00368;
DR  Pfam: PF13323;
DR  Pfam: PF12349;
DR  PROSITE: PS00066;
DR  PROSITE: PS00318;
DR  PROSITE: PS01192;
DR  PROSITE: PS50065;
DR  PROSITE: PS50156;
DE  Function: HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway constitutes by the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:3065625, PubMed:3526336). HMG1 and HMG2 catalyze the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate that is the rate- limiting step within the first mosule (PubMed:3526336). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl- CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3- methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are derived from a single ancestral HMGR gene by gene duplication (PubMed:32679672). {ECO:0000269|PubMed:3065625, ECO:0000269|PubMed:3526336, ECO:0000303|PubMed:32679672}.
DE  Reference Proteome: Yes;
DE  Interaction: P33767; IntAct: EBI-7745273; Score: 0.37
DE  Interaction: P07286; IntAct: EBI-7745296; Score: 0.37
DE  Interaction: Q08421; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P38708; IntAct: EBI-786893; Score: 0.35
DE  Interaction: Q12447; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P38219; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P10659; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P33299; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P38764; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P23641; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P40069; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P39993; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P43535; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P47912; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P53030; IntAct: EBI-803408; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-803408; Score: 0.35
DE  Interaction: P38706; IntAct: EBI-803408; Score: 0.44
DE  Interaction: P0C2I0; IntAct: EBI-803408; Score: 0.35
DE  Interaction: P16370; IntAct: EBI-803408; Score: 0.35
DE  Interaction: P25454; IntAct: EBI-803408; Score: 0.44
DE  Interaction: P46985; IntAct: EBI-803408; Score: 0.35
DE  Interaction: P12684; IntAct: EBI-803408; Score: 0.67
DE  Interaction: P39925; IntAct: EBI-812746; Score: 0.27
DE  Interaction: P32790; IntAct: EBI-7494165; Score: 0.37
DE  Interaction: Q12329; IntAct: EBI-3828992; Score: 0.35
DE  Interaction: P12683; IntAct: EBI-21322239; Score: 0.37
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005778;
GO  GO:0004420;
GO  GO:0015936;
GO  GO:0006696;
GO  GO:0019287;
GO  GO:0008299;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPPLFKGLKQMAKPIAYVSRFSAKRPIHIILFSLIISAFAYLSVIQYYFNGWQLDSNSVFETAPNKDSNTLFQECSHYYR
SQ  DSSLDGWVSITAHEASELPAPHHYYLLNLNFNSPNETDSIPELANTVFEKDNTKYILQEDLSVSKEISSTDGTKWRLRSD
SQ  RKSLFDVKTLAYSLYDVFSENVTQADPFDVLIMVTAYLMMFYTIFGLFNDMRKTGSNFWLSASTVVNSASSLFLALYVTQ
SQ  CILGKEVSALTLFEGLPFIVVVVGFKHKIKIAQYALEKFERVGLSKRITTDEIVFESVSEEGGRLIQDHLLCIFAFIGCS
SQ  MYAHQLKTLTNFCILSAFILIFELILTPTFYSAILALRLEMNVIHRSTIIKQTLEEDGVVPSTARIISKAEKKSVSSFLN
SQ  LSVVVIIMKLSVILLFVFINFYNFGANWVNDAFNSLYFDKERVSLPDFITSNASENFKEQAIVSVTPLLYYKPIKSYQRI
SQ  EDMVLLLLRNVSVAIRDRFVSKLVLSALVCSAVINVYLLNAARIHTSYTADQLVKTEVTKKSFTAPVQKASTPVLTNKTV
SQ  ISGSKVKSLSSAQSSSSGPSSSSEEDDSRDIESLDKKIRPLEELEALLSSGNTKQLKNKEVAALVIHGKLPLYALEKKLG
SQ  DTTRAVAVRRKALSILAEAPVLASDRLPYKNYDYDRVFGACCENVIGYMPLPVGVIGPLVIDGTSYHIPMATTEGCLVAS
SQ  AMRGCKAINAGGGATTVLTKDGMTRGPVVRFPTLKRSGACKIWLDSEEGQNAIKKAFNSTSRFARLQHIQTCLAGDLLFM
SQ  RFRTTTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVRKVLKS
SQ  DVSALVELNIAKNLVGSAMAGSVGGFNAHAANLVTAVFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIG
SQ  GGTVLEPQGAMLDLLGVRGPHATAPGTNARQLARIVACAVLAGELSLCAALAAGHLVQSHMTHNRKPAEPTKPNNLDATD
SQ  INRLKDGSVTCIKS
//
ID  P12684;
PN  3-hydroxy-3-methylglutaryl-coenzyme A reductase 2;
GN  HMG2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8744950}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: P12684;
DR  UNIPROT: D6VZ84;
DR  UNIPROT: E9P8X3;
DR  Pfam: PF00368;
DR  Pfam: PF13323;
DR  Pfam: PF12349;
DR  PROSITE: PS00066;
DR  PROSITE: PS00318;
DR  PROSITE: PS01192;
DR  PROSITE: PS50065;
DR  PROSITE: PS50156;
DE  Function: HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway constitutes by the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:3065625, PubMed:3526336). HMG1 and HMG2 catalyze the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate that is the rate- limiting step within the first mosule (PubMed:3526336). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl- CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3- methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are derived from a single ancestral HMGR gene by gene duplication (PubMed:32679672). {ECO:0000269|PubMed:3065625, ECO:0000269|PubMed:3526336, ECO:0000303|PubMed:32679672}.
DE  Reference Proteome: Yes;
DE  Interaction: P12683; IntAct: EBI-803408; Score: 0.67
DE  Interaction: Q06449; IntAct: EBI-601343; Score: 0.37
DE  Interaction: P38219; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P36008; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P33299; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P40069; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P40341; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P16521; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P26783; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P32905; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P26321; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P38706; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P41805; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P12709; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P39925; IntAct: EBI-806785; Score: 0.35
DE  Interaction: Q02159; IntAct: EBI-860875; Score: 0.00
DE  Interaction: P25694; IntAct: EBI-1008636; Score: 0.35
DE  Interaction: P53044; IntAct: EBI-1008636; Score: 0.35
DE  Interaction: Q04228; IntAct: EBI-1008636; Score: 0.35
DE  Interaction: Q03010; IntAct: EBI-6316649; Score: 0.00
DE  Interaction: P38837; IntAct: EBI-6316638; Score: 0.00
DE  Interaction: P12684; IntAct: EBI-21320996; Score: 0.55
DE  Interaction: Q12469; IntAct: EBI-16282981; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005778;
GO  GO:0000502;
GO  GO:0004420;
GO  GO:0015936;
GO  GO:0006696;
GO  GO:0008299;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLPLKTIVHLVKPFACTARFSARYPIHVIVVAVLLSAAAYLSVTQSYLNEWKLDSNQYSTYLSIKPDELFEKCTHYYRS
SQ  PVSDTWKLLSSKEAADIYTPFHYYLSTISFQSKDNSTTLPSLDDVIYSVDHTRYLLSEEPKIPTELVSENGTKWRLRNNS
SQ  NFILDLHNIYRNMVKQFSNKTSEFDQFDLFIILAAYLTLFYTLCCLFNDMRKIGSKFWLSFSALSNSACALYLSLYTTHS
SQ  LLKKPASLLSLVIGLPFIVVIIGFKHKVRLAAFSLQKFHRISIDKKITVSNIIYEAMFQEGAYLIRDYLFYISSFIGCAI
SQ  YARHLPGLVNFCILSTFMLVFDLLLSATFYSAILSMKLEINIIHRSTVIRQTLEEDGVVPTTADIIYKDETASEPHFLRS
SQ  NVAIILGKASVIGLLLLINLYVFTDKLNATILNTVYFDSTIYSLPNFINYKDIGNLSNQVIISVLPKQYYTPLKKYHQIE
SQ  DSVLLIIDSVSNAIRDQFISKLLFFAFAVSISINVYLLNAAKIHTGYMNFQPQSNKIDDLVVQQKSATIEFSETRSMPAS
SQ  SGLETPVTAKDIIISEEIQNNECVYALSSQDEPIRPLSNLVELMEKEQLKNMNNTEVSNLVVNGKLPLYSLEKKLEDTTR
SQ  AVLVRRKALSTLAESPILVSEKLPFRNYDYDRVFGACCENVIGYMPIPVGVIGPLIIDGTSYHIPMATTEGCLVASAMRG
SQ  CKAINAGGGATTVLTKDGMTRGPVVRFPTLIRSGACKIWLDSEEGQNSIKKAFNSTSRFARLQHIQTCLAGDLLFMRFRT
SQ  TTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVKSVLKSDVSA
SQ  LVELNISKNLVGSAMAGSVGGFNAHAANLVTALFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIGGGTV
SQ  LEPQGAMLDLLGVRGPHPTEPGANARQLARIIACAVLAGELSLCSALAAGHLVQSHMTHNRKTNKANELPQPSNKGPPCK
SQ  TSALL
//
ID  Q10283;
PN  3-hydroxy-3-methylglutaryl-coenzyme A reductase;
GN  hmg1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19486165}; Multi-pass membrane protein {ECO:0000269|PubMed:19486165}. Nucleus envelope {ECO:0000269|PubMed:19486165}.
DR  UNIPROT: Q10283;
DR  UNIPROT: O74425;
DR  Pfam: PF00368;
DR  Pfam: PF12349;
DR  PROSITE: PS00066;
DR  PROSITE: PS00318;
DR  PROSITE: PS50065;
DR  PROSITE: PS50156;
DE  Function: Part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:8896278, PubMed:19486165). Hmg1 catalyzes the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate (PubMed:8896278, PubMed:19486165). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase eg10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl- CoA synthases erg13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hcs1 (Probable). {ECO:0000269|PubMed:19486165, ECO:0000269|PubMed:8896278, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0005778;
GO  GO:0004420;
GO  GO:0015936;
GO  GO:0006696;
GO  GO:0010142;
GO  GO:0019287;
GO  GO:0008299;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIYKLAARYPIQVIAIVGILVSMAYFSFLEALTQEDFPVLIRALKRFGILDGFPNTRLPNEMILKLSSVQGEDASVWEQI
SQ  PAAELGGEGFVDFDITQWYYPANAKVDVAQLVEPYRNDCIFHDASGACHFFFKEVGNWTVSSIALPSNLANPPIDYFLDS
SQ  SSTVIQRILPAIREHGISWSWLLQLIARTWMNTLKIASQASKTELLIVGTAYACMLISIVSLYLKMRRLGSKFWLFFSVL
SQ  LSTLFSVQFAMTLVRASGVRISLVSLIESLPFLINVVALDKAAELTRQVITRCSVSDSHSPMHEDIAKACRNAAPPILRH
SQ  FSFGIVVLAIFSYCNFGIKQFFLFAAVMIYDLLLLFSFFVAILTLKLEMRRYNAKDDVRKVLIEEGLSESTARHVADGND
SQ  SSATTSAGSRYFKVRYGTKIILFIFIAFNLFELCSIPFKHYAATSAAAARLIPLVRSQYPDFKSQRLLDDGVFDDVLSAI
SQ  SSMSNIESPSVRLLPAVFYGAELSSTSFLSTIHSFINNWSHYISASFLSKWIVCALSLSIAVNVFLLNAARLNSIKEEPE
SQ  KKVVEKVVEVVKYIPSSNSSSIDDIQKDEIAQESVVRSLEECITLYNNGQISTLNDEEVVQLTLAKKIPLYALERVLKDV
SQ  TRAVVIRRTVVSRSSRTKTLESSNCPVYHYDYSRVLNACCENVIGYMPLPLGVAGPLIIDGKPFYIPMATTEGALVASTM
SQ  RGCKAINAGGGAVTVLTRDQMSRGPCVAFPNLTRAGRAKIWLDSPEGQEVMKKAFNSTSRFARLQHIKTALAGTRLFIRF
SQ  CTSTGDAMGMNMISKGVEHALVVMSNDAGFDDMQVISVSGNYCTDKKPAAINWIDGRGKSVIAEAIIPGDAVKSVLKTTV
SQ  EDLVKLNVDKNLIGSAMAGSVGGFNAHAANIVTAVYLATGQDPAQNVESSNCITLMDNVDGNLQLSVSMPSIEVGTIGGG
SQ  TVLEPQGAMLDLLGVRGAHMTSPGDNSRQLARVVAAAVMAGELSLCSALASGHLVKSHIGLNRSALNTPAMDSSAKKPAT
SQ  DALKSVNSRVPGR
//
ID  A8WUP2;
PN  Zygote defective protein 12;
GN  zyg;
OS  6238;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localizes to the minus end of microtubules, proximal to the centrosome. Centrosomal localization requires sun-1 and microtubules. {ECO:0000250}.
DR  UNIPROT: A8WUP2;
DR  Pfam: PF19047;
DR  PROSITE: PS50021;
DE  Function: Cytoskeletal linker protein, which is essential for attachment of the centrosome to the nucleus. Required for dynein localization to the nuclear envelope (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0031965;
GO  GO:0051959;
GO  GO:0008017;
GO  GO:0031122;
GO  GO:0030705;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLDLTNQESDSSENGNSKYADSTDGRGIGTSRRLDDEDLDERRKDLADLVFWMSGLKATTLPLDDHTSLCNGRAFAEILH
SQ  EIDRSFFDERWLETMPEMRTSSNLVVKRSNLRKLWRKMSDYIQVLNRKVVSTRWTEIGDRLDGLDETDIPVAADLAMAVV
SQ  SLAFIGKTQEKYIQYSQELPAGEHQHMMANVARLVQIVMEELPEVPTFHEISELDGSQNELNSSHVESSVITNGNGSAER
SQ  RSTLSANDQVLVEAQLEIDELRSERDNLIKDVERLTKALESSQLDTSTCSEPNELSILEKQNEELRVKRRQAEERVLELE
SQ  ASMEHFQAIVVKLTDENDTLQSGQKELNMLKTHLDTAQSDVEEWRTIANKYQSDAEMLKKREKEVKELQGQVKSLTSRLE
SQ  HHVKTATIDEDNKAGIVQLRSQIGTLTANNVELNVGLESKKRIVEQLELQLIQYKEKVKELEDRKEDLIAERNELENKLL
SQ  FKESVTPRSLHESMFEAGHLSFDDKTKLPLEIENKRLTERIQELESLEPLKGEIIKMKSQNGVLEEEKLVITKQMEELER
SQ  QVADLQEKLTKNQQHASGDVVELKVQLEKANVEVERMRETEMRTEAKLAGVEELLRKRNVEKEANETALQKAKAVIDELE
SQ  SRNRPVGEDNKTSVQDFKELKTENELLRQKNEALETALNTTTQSLEQENRLITSAAHQQILDRSSDSMMIMRAQAGSDHP
SQ  QTLLDTQKMTRALPWRFGISSMLIIFMVWFFINTFCEVNAPPKA
//
ID  Q23529;
PN  Zygote defective protein 12;
GN  zyg;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:14697201}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14697201}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14697201}. Note=Localizes to the minus end of microtubules, proximal to the centrosome. Centrosomal localization requires sun-1 and microtubules.
DR  UNIPROT: Q23529;
DR  UNIPROT: Q2V4T6;
DR  UNIPROT: Q7JPD4;
DR  Pfam: PF19047;
DR  PROSITE: PS50021;
DE  Function: Cytoskeletal linker protein, which is essential for attachment of the centrosome to the nucleus (PubMed:14697201). Required for dynein localization to the nuclear envelope (PubMed:14697201). Forms a LINC (LInker of Nucleoskeleton and Cytoskeleton) complex together with unc-84, that may be involved in DNA damage repair (PubMed:27956467). {ECO:0000269|PubMed:14697201, ECO:0000269|PubMed:27956467}.
DE  Reference Proteome: Yes;
DE  Interaction: Q23529; IntAct: EBI-1570329; Score: 0.40
DE  Interaction: G5ECK7; IntAct: EBI-1570311; Score: 0.37
DE  Interaction: Q9U2Z1; IntAct: EBI-6457211; Score: 0.37
DE  Interaction: P91409; IntAct: EBI-6457201; Score: 0.37
DE  Interaction: G5ED30; IntAct: EBI-11465222; Score: 0.51
DE  Interaction: H2KYA1; IntAct: EBI-11469957; Score: 0.37
DE  Interaction: Q93198; IntAct: EBI-11471204; Score: 0.37
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0051959;
GO  GO:0008017;
GO  GO:0043621;
GO  GO:0051642;
GO  GO:0007059;
GO  GO:0031122;
GO  GO:0030705;
GO  GO:0009792;
GO  GO:0051647;
GO  GO:0035046;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLDLTNKESESSDNGNSKYEDSIDGREVGTSKPFKEERSLEDLQADLADMAVWMEGLDATKLPLNDPQLLCNGRAFSEVL
SQ  HNVDKNFFTDGWLETMPENRTTNIMVFRSCTRKLWRKMFDYVNHINRTVVSSRWTDIHERIDGIYESDLPAMVNLGMAVV
SQ  TLAHIGKNAKRFVDYSKALTSTHKSMMSNVAKMVTTVIDEMPENPCFHEISELHGSQSELNSLSESSGKLNGNGSSERRS
SQ  NADQILVDAELEIERLRTETENQRKEIERLTKSFETAQHDMSSNSESGDISILEKQNEELRQKRRELEEKNLELDAAVDQ
SQ  FKGIVFELTNENDVLRRSDKERQRLQTVLDAAQSDLDEWKTVANQYQKEAELSKQQDKEIKELLSQNKALKSRLDHHVKS
SQ  ATLEDANKNGIAQLRTQVGGLTALNTELKASLDSKKRCVEQLEIQLIQHKEKVKELEDRKDELIEERNRLENQLIFKEAV
SQ  TPRSLHESMFEAGNLSFEPFSEKNTLPLEIENKRLTERIQELESLEPLKGELITLKSKNGVLEEEKLFATKQIEELQQQI
SQ  EDLQENLLKNQEHASGDVVGLKIQLEKAEVEAQQMREAKMRAETNQAQVDEILKKRTAELEVNATALQKAKAVIDELEYN
SQ  SRPVSEDSMTSVQAFKEMKEENEKLRQKVEKLEIELNTVTQGFEQENRLLTSASHQQVLNRSIDEVMSMRAHAGSEEPQT
SQ  LLDTQKMSGALPWRSLASETRRELPTAMASILVLGFLVFIAWMFININSALNAPPNA
//
ID  Q23647;
PN  Hypersensitive to pore-forming toxin protein 40;
GN  hpo;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:32338603}. Note=Localizes to perinuclear foci in germ cells (PubMed:32338603). Its localization at perinuclear foci is either adjacent to or co-localized with mutator complex protein mut-16 (PubMed:32338603). {ECO:0000269|PubMed:32338603}.
DR  UNIPROT: Q23647;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:1990633;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNSQQEWEHAYSLAERMYNKQAPTKREELNPTERVICSRFETIFDYDPFKDEYTFRDQALLFSTPVQPKCRTVAEADLHE
SQ  LKENTAKLNIPMPSYINICPIYALLPFTVLVFNNSQHAHKSLSDDMERAAATFRNPHESEIVPGAMYIFKQKHGKAYRCI
SQ  ILSEDGDMNIPDAERKYLVAFIDNVQIVSVKQKTLFVSDQFSIKDYPCALHCARIVGISAIRKSYVSGMNQFILNFYDAK
SQ  EKRKAGMFAFIYKLDKEEKKLVIDYPSLLGTPKTTSTEIRTAVGHQIVASKDPVSLTFEQLNKKEVPEFKYLNSTDDDSD
SQ  VELDLIEHDTKSVNPVASSHPTSSSMDDCPYGRASIARAKDYQLRLPPHSQKGLSSSSLLGSSYPVSNSIKNDITKQSES
SQ  NRADATNISFSSFESTKSDISPQNNQNVEETSTPTVPPNSTIQENEEDEIMSPASIIRAPSRLAGSLNKVSIERPNTPLP
SQ  TSSKNSEHNMSEISTYEASSISSHHLVPQSPSVPKTNYTVPVVQRPLTAPEKFRDPFGGPGSSDILNTKMLCSEKNIVPS
SQ  NKFGRQISPGKDDKNENYQYSRMETKPQTLFAPVLDENQRQSSSSNMMCQIPDISSVAQGSNAPKTAPNDSVNSVAPDDI
SQ  HETDKRGNHCKSVTEDPKDNKDPTAVTTLEDPDINDENFSVQSICSETFVETDQKLMEVETGADAFTESITDQFAQMSEG
SQ  LKKLAINLADSVRTAAIEKNHDAFIANIHAMEIISKKVPDDIDKRFWKMKIVEARKLEAAFD
//
ID  Q960X8;
PN  Hepatocyte growth factor-regulated tyrosine kinase substrate;
GN  Hrs;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cell cortex {ECO:0000269|PubMed:11832215}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11832215}. Note=Locates to vesicles present in the perinuclear regions of muscle cells and in the periphery of Garland cells of third-instar larvae.
DR  UNIPROT: Q960X8;
DR  UNIPROT: A4V018;
DR  UNIPROT: Q8IGU6;
DR  UNIPROT: Q9VQF2;
DR  UNIPROT: Q9VQF3;
DR  PDB: 1DVP;
DR  Pfam: PF01363;
DR  Pfam: PF12210;
DR  Pfam: PF00790;
DR  PROSITE: PS50330;
DR  PROSITE: PS50179;
DR  PROSITE: PS50178;
DE  Function: Essential role in endosome membrane invagination and formation of multivesicular bodies, MVBs. Required during gastrulation and appears to regulate early embryonic signaling pathways. Inhibits tyrosine kinase receptor signaling by promoting degradation of the tyrosine-phosphorylated, active receptor, potentially by sorting activated receptors into MVBs. The MVBs are then trafficked to the lysosome where their contents are degraded. {ECO:0000269|PubMed:11832215}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8IQV9; IntAct: EBI-509966; Score: 0.37
DE  Interaction: P23573; IntAct: EBI-203520; Score: 0.00
DE  Interaction: Q9VNS1; IntAct: EBI-236619; Score: 0.00
DE  Interaction: O46339; IntAct: EBI-248743; Score: 0.00
DE  Interaction: Q9VLJ5; IntAct: EBI-253365; Score: 0.00
DE  Interaction: Q9W4P5; IntAct: EBI-259675; Score: 0.00
DE  Interaction: Q9VAD6; IntAct: EBI-259680; Score: 0.00
DE  Interaction: Q9V397; IntAct: EBI-259684; Score: 0.00
DE  Interaction: Q9XTL2; IntAct: EBI-259688; Score: 0.00
DE  Interaction: O46036; IntAct: EBI-259692; Score: 0.00
DE  Interaction: P68198; IntAct: EBI-300719; Score: 0.40
DE  Interaction: Q9VVT5; IntAct: EBI-509756; Score: 0.37
DE  Interaction: Q9Y103; IntAct: EBI-509763; Score: 0.00
DE  Interaction: P18091; IntAct: EBI-509770; Score: 0.00
DE  Interaction: Q8SXD4; IntAct: EBI-509777; Score: 0.00
DE  Interaction: Q7KLE5; IntAct: EBI-509784; Score: 0.00
DE  Interaction: Q9V595; IntAct: EBI-509791; Score: 0.37
DE  Interaction: Q03017; IntAct: EBI-509798; Score: 0.37
DE  Interaction: Q9VH60; IntAct: EBI-509805; Score: 0.37
DE  Interaction: Q95RP4; IntAct: EBI-509812; Score: 0.37
DE  Interaction: Q9VCB8; IntAct: EBI-509819; Score: 0.37
DE  Interaction: Q23983; IntAct: EBI-509826; Score: 0.37
DE  Interaction: Q9VEN1; IntAct: EBI-509833; Score: 0.00
DE  Interaction: Q00963; IntAct: EBI-509840; Score: 0.37
DE  Interaction: A1Z9J3; IntAct: EBI-509847; Score: 0.37
DE  Interaction: Q9VN68; IntAct: EBI-509854; Score: 0.00
DE  Interaction: Q9VXG4; IntAct: EBI-509861; Score: 0.37
DE  Interaction: Q7YU91; IntAct: EBI-509868; Score: 0.37
DE  Interaction: Q8SXA8; IntAct: EBI-509875; Score: 0.00
DE  Interaction: Q9VW47; IntAct: EBI-509882; Score: 0.37
DE  Interaction: P29742; IntAct: EBI-509896; Score: 0.37
DE  Interaction: Q9VC36; IntAct: EBI-509903; Score: 0.37
DE  Interaction: O44381; IntAct: EBI-509917; Score: 0.37
DE  Interaction: Q9VPL5; IntAct: EBI-509924; Score: 0.37
DE  Interaction: P54360; IntAct: EBI-509931; Score: 0.37
DE  Interaction: P48608; IntAct: EBI-509938; Score: 0.00
DE  Interaction: P07666; IntAct: EBI-509945; Score: 0.37
DE  Interaction: Q8T987; IntAct: EBI-509952; Score: 0.37
DE  Interaction: Q7KN74; IntAct: EBI-509959; Score: 0.37
DE  Interaction: O02373; IntAct: EBI-509973; Score: 0.37
DE  Interaction: Q9VM75; IntAct: EBI-509980; Score: 0.37
DE  Interaction: P08953; IntAct: EBI-15848965; Score: 0.35
DE  Interaction: Q9VUH6; IntAct: EBI-15848965; Score: 0.35
GO  GO:0005938;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005768;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0035091;
GO  GO:0043130;
GO  GO:0045022;
GO  GO:0032456;
GO  GO:0006897;
GO  GO:0016197;
GO  GO:0032509;
GO  GO:1990182;
GO  GO:0045879;
GO  GO:0120177;
GO  GO:0016322;
GO  GO:1903688;
GO  GO:0045752;
GO  GO:0061357;
GO  GO:0031623;
GO  GO:0051726;
GO  GO:2000274;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRSSFDKNLENATSHLRLEPDWPSILLICDEINQKDVTPKNAFAAIKKKMNSPNPHSSCYSLLVLESIVKNCGAPVHEE
SQ  VFTKENCEMFSSFLESTPHENVRQKMLELVQTWAYAFRSSDKYQAIKDTMTILKAKGHTFPELREADAMFTADTAPNWAD
SQ  GRVCHRCRVEFTFTNRKHHCRNCGQVFCGQCTAKQCPLPKYGIEKEVRVCDGCFAALQRPTSGSGGAKSGPRPADSELPA
SQ  EYLNSTLAQQVQTPARKTEQELKEEEELQLALALSQSEAEQQKPKLQSLPPAAYRMQQRSPSPEAPPEPKEYHQQPEEAT
SQ  NPELAKYLNRSYWEQRKISESSSMASPSAPSPMPPTPQPQQIMPLQVKSADEVQIDEFAANMRTQVEIFVNRMKSNSSRG
SQ  RSISNDSSVQTLFMTLTSLHSQQLSYIKEMDDKRMWYEQLQDKLTQIKDSRAALDQLRQEHVEKLRRIAEEQERQRQMQM
SQ  AQKLDIMRKKKQEYLQYQRQLALQRIQEQEREMQLRQEQQKAQYLMGQSAPPFPYMPPSAVPQHGSPSHQLNNVYNPYAA
SQ  GVPGYLPQGPAPAPNGHGQFQAIPPGMYNPAIQQPMPPNLQPGGLMQQPAPPGNPQMMPPMPENQFANNPAAILQLPQQH
SQ  SIAQPPQIPFQPQPQQIPGQQPQQIPGQQPQQIPGQQPQQIPGQQPQQIPVQQPQPQPQMGHVMLQQHQAPPAAQAPPVT
SQ  EIANNQVQAVAAAPAPPQNEPGPAPVKAEEPATAELISFD
//
ID  Q08DJ8;
PN  Heat shock factor protein 1;
GN  HSF1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q00613}. Cytoplasm {ECO:0000250|UniProtKB:Q00613}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q00613}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00613}. Note=The monomeric form is cytoplasmic in unstressed cells. Predominantly nuclear protein in both unstressed and heat shocked cells. Translocates in the nucleus upon heat shock. Nucleocytoplasmic shuttling protein. Colocalizes with IER5 in the nucleus. Colocalizes with BAG3 to the nucleus upon heat stress. Localizes in subnuclear granules called nuclear stress bodies (nSBs) upon heat shock. Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock. Colocalizes with PRKACA/PKA in the nucleus and nSBs upon heat shock. Relocalizes from the nucleus to the cytoplasm during the attenuation and recovery phase period of the heat shock response. Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent manner. Together with histone H2AX, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR). Colocalizes with calcium-responsive transactivator SS18L1 at kinetochore region on the mitotic chromosomes. Colocalizes with gamma tubulin at centrosome. Localizes at spindle pole in metaphase. Colocalizes with PLK1 at spindle poles during prometaphase. {ECO:0000250|UniProtKB:Q00613}.
DR  UNIPROT: Q08DJ8;
DR  Pfam: PF00447;
DR  Pfam: PF06546;
DR  PROSITE: PS00434;
DE  Function: Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage. In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA- binding inactivated monomeric form. Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes. Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival. Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form. Binds to inverted 5'-NGAAN-3' pentamer DNA sequences. Binds to chromatin at heat shock gene promoters. Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH- dependent reductase DHRS2. Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells. Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner. Plays a role in nuclear export of stress-induced HSP70 mRNA. Plays a role in the regulation of mitotic progression. Also plays a role as a negative regulator of non- homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner. Involved in stress-induced cancer cell proliferation in a IER5- dependent manner. {ECO:0000250|UniProtKB:Q00613}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0101031;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0097431;
GO  GO:0097165;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:1990904;
GO  GO:0031490;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0003700;
GO  GO:0031072;
GO  GO:0051879;
GO  GO:0042802;
GO  GO:0046982;
GO  GO:0043621;
GO  GO:0000978;
GO  GO:0043565;
GO  GO:0061770;
GO  GO:0071276;
GO  GO:0071280;
GO  GO:0072738;
GO  GO:0071480;
GO  GO:0034605;
GO  GO:1903936;
GO  GO:0034620;
GO  GO:0006281;
GO  GO:0000165;
GO  GO:0006397;
GO  GO:0051028;
GO  GO:2001033;
GO  GO:0031333;
GO  GO:0000122;
GO  GO:0045931;
GO  GO:1900365;
GO  GO:0045944;
GO  GO:0065003;
GO  GO:1900034;
GO  GO:0006357;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVLDQGQFAKEVLPKYFKHSNMASFVRQLNMYGFRK
SQ  VVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLRSEDIKIRQDSVTKLLTDVQLMKGKQESMDSKLLA
SQ  MKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDGGPAHPMPKYGRQYSLEHIHGPGPY
SQ  PAPSPAYSGSSLYSPDAVTSSGPIISDITELAPGSPVASSGGSVDERPLSSSPLVRVKEEPPSPPQSPRAEGASPGRPSS
SQ  MVETPLSPTTLIDSILRESEPTPVASTTPLVDTGGRPPSPLPASAPEKCLSVACLDKTELSDHLDAMDSNLDNLQTMLTS
SQ  HGFSVDTSTLLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPRPLEAEKSSPDSGKQLVHYTAQPLLLLDPGSVDVG
SQ  SSDLPVLFELGEGSYFSEGDDYSDDPTISLLTGSEPPKAKDPTVS
//
ID  P38529;
PN  Heat shock factor protein 1;
GN  HSF1;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q00613}. Cytoplasm {ECO:0000250|UniProtKB:Q00613}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q00613}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00613}.
DR  UNIPROT: P38529;
DR  UNIPROT: I7GGU6;
DR  Pfam: PF00447;
DR  Pfam: PF06546;
DR  PROSITE: PS00434;
DE  Function: Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones heat shock proteins (HSPs) that protect cells from cellular insults' damage (PubMed:8455593). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form. Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes. Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (By similarity). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form. Binds to inverted 5'-NGAAN-3' pentamer DNA sequences. Binds to chromatin at heat shock gene promoters. Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells. Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells. Plays a role in nuclear export of stress-induced mRNA. Plays a role in the regulation of mitotic progression. Also plays a role as a negative regulator of non- homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner. Involved in stress-induced cancer cell proliferation. {ECO:0000250|UniProtKB:Q00613, ECO:0000269|PubMed:8455593}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0101031;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0097431;
GO  GO:0097165;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0031490;
GO  GO:0001046;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0003700;
GO  GO:0031072;
GO  GO:0042803;
GO  GO:0043621;
GO  GO:0000978;
GO  GO:0043565;
GO  GO:0071276;
GO  GO:0071480;
GO  GO:0034605;
GO  GO:0006281;
GO  GO:0000165;
GO  GO:0006397;
GO  GO:0051028;
GO  GO:2001033;
GO  GO:0031333;
GO  GO:0000122;
GO  GO:1902808;
GO  GO:1902751;
GO  GO:0008284;
GO  GO:0010628;
GO  GO:0045931;
GO  GO:1900365;
GO  GO:0045944;
GO  GO:0070207;
GO  GO:0006357;
GO  GO:0009408;
GO  GO:0009416;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGPGAAAAAVGAGPGGSNVSAFLTKLWTLVEDPETDPLICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNM
SQ  YGFRKVVHIEQGGLVKPEKDDTEFQHPYFIRGQEHLLENIKRKVTSVSSIKNEDIKVRQDNVTKLLTDIQVMKGKQESMD
SQ  SKLIAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSSSAHSMPKYSRQYSLEHVH
SQ  GSSPYAASSPAYSGSNIYSPDSSTNSGPIISDVTELAQSSPSASPSGSLDERSSPVVRIKEEPPSPSRSPKENEPSTTTA
SQ  AAGNSTEQPQPQEKCLSVACLDKNELNDHLDTIDSNLDNLQTMLSTHGFSVDTTALLDLFSPSMTVTDMNLPDLDSSLAS
SQ  IQDLLSSQEQQKPSEADAAAADTGKQLVHYTAQPLFLVDSSAVDVGSGDLPIFFELGEGSYFTDGDEYNEDPTISLLSGT
SQ  EQPKPKDPTVS
//
ID  Q00613;
PN  Heat shock factor protein 1;
GN  HSF1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10413683, ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11514557, ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:19229036, ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27189267, ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:8455624}. Cytoplasm {ECO:0000269|PubMed:10413683, ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:8455624}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10359787}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21085490}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18794143}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18794143}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:18794143}. Note=The monomeric form is cytoplasmic in unstressed cells (PubMed:8455624, PubMed:26159920). Predominantly nuclear protein in both unstressed and heat shocked cells (PubMed:10413683, PubMed:10359787). Translocates in the nucleus upon heat shock (PubMed:8455624). Nucleocytoplasmic shuttling protein (PubMed:26159920). Colocalizes with IER5 in the nucleus (PubMed:27354066). Colocalizes with BAG3 to the nucleus upon heat stress (PubMed:8455624, PubMed:26159920). Localizes in subnuclear granules called nuclear stress bodies (nSBs) upon heat shock (PubMed:11447121, PubMed:11514557, PubMed:10359787, PubMed:25963659, PubMed:10747973, PubMed:24581496, PubMed:19229036). Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock (PubMed:11447121, PubMed:12665592, PubMed:11514557, PubMed:14707147, PubMed:10359787). Colocalizes with PRKACA/PKA in the nucleus and nSBs upon heat shock (PubMed:21085490). Relocalizes from the nucleus to the cytoplasm during the attenuation and recovery phase period of the heat shock response (PubMed:26159920). Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent manner (PubMed:12917326). Together with histone H2AX, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) (PubMed:26359349). Colocalizes with calcium- responsive transactivator SS18L1 at kinetochore region on the mitotic chromosomes (PubMed:18794143). Colocalizes with gamma tubulin at centrosome (PubMed:18794143). Localizes at spindle pole in metaphase (PubMed:18794143). Colocalizes with PLK1 at spindle poles during prometaphase (PubMed:18794143). {ECO:0000269|PubMed:10359787, ECO:0000269|PubMed:10413683, ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11514557, ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:24581496, ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:27354066, ECO:0000269|PubMed:8455624}.
DR  UNIPROT: Q00613;
DR  UNIPROT: A8K4L0;
DR  UNIPROT: A8MW26;
DR  UNIPROT: Q53XT4;
DR  PDB: 2LDU;
DR  PDB: 5D5U;
DR  PDB: 5D5V;
DR  PDB: 5HDG;
DR  PDB: 5HDN;
DR  PDB: 7DCJ;
DR  PDB: 7DCS;
DR  PDB: 7DCT;
DR  Pfam: PF00447;
DR  Pfam: PF06546;
DR  PROSITE: PS00434;
DR  OMIM: 140580;
DR  DisGeNET: 3297;
DE  Function: Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:1871105, PubMed:11447121, PubMed:1986252, PubMed:7760831, PubMed:7623826, PubMed:8946918, PubMed:8940068, PubMed:9341107, PubMed:9121459, PubMed:9727490, PubMed:9499401, PubMed:9535852, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:25963659, PubMed:26754925, PubMed:18451878). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:9727490, PubMed:11583998, PubMed:16278218). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:1871105, PubMed:1986252, PubMed:8455624, PubMed:7935471, PubMed:7623826, PubMed:8940068, PubMed:9727490, PubMed:9499401, PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:25963659, PubMed:26754925). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress- induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925). {ECO:0000269|PubMed:10359787, ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11583998, ECO:0000269|PubMed:12659875, ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:14707147, ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:18451878, ECO:0000269|PubMed:1871105, ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:1986252, ECO:0000269|PubMed:25963659, ECO:0000269|PubMed:26359349, ECO:0000269|PubMed:26727489, ECO:0000269|PubMed:26754925, ECO:0000269|PubMed:34723967, ECO:0000269|PubMed:7623826, ECO:0000269|PubMed:7760831, ECO:0000269|PubMed:7935471, ECO:0000269|PubMed:8455624, ECO:0000269|PubMed:8940068, ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459, ECO:0000269|PubMed:9341107, ECO:0000269|PubMed:9499401, ECO:0000269|PubMed:9535852, ECO:0000269|PubMed:9727490}. (Microbial infection) Plays a role in latent human immunodeficiency virus (HIV-1) transcriptional reactivation. Binds to the HIV-1 long terminal repeat promoter (LTR) to reactivate viral transcription by recruiting cellular transcriptional elongation factors, such as CDK9, CCNT1 and EP300. {ECO:0000269|PubMed:27189267}.
DE  Reference Proteome: Yes;
DE  Interaction: O60271; IntAct: EBI-11911387; Score: 0.00
DE  Interaction: P02545; IntAct: EBI-10682932; Score: 0.35
DE  Interaction: P22392; IntAct: EBI-9394221; Score: 0.35
DE  Interaction: P63165; IntAct: EBI-15799774; Score: 0.44
DE  Interaction: P09104; IntAct: EBI-734427; Score: 0.00
DE  Interaction: Q9UNE7; IntAct: EBI-7902188; Score: 0.40
DE  Interaction: P49137; IntAct: EBI-993295; Score: 0.60
DE  Interaction: Q8N0Z6; IntAct: EBI-7909995; Score: 0.40
DE  Interaction: Q9CQU5; IntAct: EBI-2556745; Score: 0.40
DE  Interaction: Q81JT7; IntAct: EBI-2832104; Score: 0.00
DE  Interaction: Q81VE1; IntAct: EBI-2832111; Score: 0.00
DE  Interaction: P62258; IntAct: EBI-6994351; Score: 0.53
DE  Interaction: O43529; IntAct: EBI-3910513; Score: 0.37
DE  Interaction: P26641; IntAct: EBI-6954536; Score: 0.40
DE  Interaction: Q00534; IntAct: EBI-5293131; Score: 0.44
DE  Interaction: Q04759; IntAct: EBI-6512722; Score: 0.54
DE  Interaction: O00505; IntAct: EBI-9394221; Score: 0.64
DE  Interaction: O95817; IntAct: EBI-9394221; Score: 0.64
DE  Interaction: O95757; IntAct: EBI-9394221; Score: 0.35
DE  Interaction: Q9NZL4; IntAct: EBI-9394221; Score: 0.64
DE  Interaction: Q03933; IntAct: EBI-9394221; Score: 0.73
DE  Interaction: P04792; IntAct: EBI-9394221; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-9394221; Score: 0.64
DE  Interaction: Q9ULV5; IntAct: EBI-9394268; Score: 0.35
DE  Interaction: P14618; IntAct: EBI-9355222; Score: 0.44
DE  Interaction: P54645; IntAct: EBI-10682831; Score: 0.40
DE  Interaction: Q8N4C8; IntAct: EBI-10816412; Score: 0.54
DE  Interaction: Q5VY09; IntAct: EBI-10816421; Score: 0.59
DE  Interaction: Q9UKX3; IntAct: EBI-11141047; Score: 0.35
DE  Interaction: Q53FA3; IntAct: EBI-12450308; Score: 0.35
DE  Interaction: Q8NET4; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: Q5VZK9; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: P34931; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: O43683; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: Q96SB8; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: Q15029; IntAct: EBI-12450281; Score: 0.51
DE  Interaction: Q8NEH6; IntAct: EBI-12451193; Score: 0.51
DE  Interaction: P53350; IntAct: EBI-12451475; Score: 0.51
DE  Interaction: Q9UKN8; IntAct: EBI-11911558; Score: 0.00
DE  Interaction: Q9UBC2; IntAct: EBI-11911549; Score: 0.00
DE  Interaction: Q15555; IntAct: EBI-11911495; Score: 0.00
DE  Interaction: Q14C86; IntAct: EBI-11911477; Score: 0.00
DE  Interaction: Q14683; IntAct: EBI-11911468; Score: 0.00
DE  Interaction: Q14566; IntAct: EBI-11911459; Score: 0.00
DE  Interaction: P61962; IntAct: EBI-11911450; Score: 0.00
DE  Interaction: P51157; IntAct: EBI-11911432; Score: 0.00
DE  Interaction: P49736; IntAct: EBI-11911423; Score: 0.00
DE  Interaction: P33991; IntAct: EBI-11911405; Score: 0.00
DE  Interaction: Q9Y4E8; IntAct: EBI-11911567; Score: 0.00
DE  Interaction: Q9Y6Y0; IntAct: EBI-11911585; Score: 0.00
DE  Interaction: Q9Y6A4; IntAct: EBI-11911576; Score: 0.00
DE  Interaction: Q8IV03; IntAct: EBI-21503643; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-21714606; Score: 0.35
DE  Interaction: O95429; IntAct: EBI-21788135; Score: 0.35
DE  Interaction: Q00613; IntAct: EBI-16190425; Score: 0.57
DE  Interaction: P45983; IntAct: EBI-16203579; Score: 0.35
DE  Interaction: Q96MT8; IntAct: EBI-21379247; Score: 0.00
DE  Interaction: Q6ZMY6; IntAct: EBI-25869741; Score: 0.56
DE  Interaction: Q96CM3; IntAct: EBI-25869733; Score: 0.56
DE  Interaction: Q8NFB2; IntAct: EBI-25869723; Score: 0.56
DE  Interaction: Q9UIH9; IntAct: EBI-25869715; Score: 0.56
DE  Interaction: Q13352; IntAct: EBI-25869705; Score: 0.56
DE  Interaction: Q14693; IntAct: EBI-25869697; Score: 0.56
DE  Interaction: O14744; IntAct: EBI-25869689; Score: 0.56
DE  Interaction: Q9UNY5; IntAct: EBI-25869681; Score: 0.56
DE  Interaction: P11684; IntAct: EBI-25869673; Score: 0.56
GO  GO:0005813;
GO  GO:0101031;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0000791;
GO  GO:0000792;
GO  GO:0000776;
GO  GO:0097431;
GO  GO:0097165;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:1990904;
GO  GO:0031490;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0003700;
GO  GO:0000981;
GO  GO:0001227;
GO  GO:0140296;
GO  GO:0031072;
GO  GO:0051879;
GO  GO:0042802;
GO  GO:1990841;
GO  GO:0046982;
GO  GO:0019901;
GO  GO:0043621;
GO  GO:0000978;
GO  GO:0001162;
GO  GO:0043565;
GO  GO:1990837;
GO  GO:0098847;
GO  GO:0097677;
GO  GO:0000976;
GO  GO:0061770;
GO  GO:1904385;
GO  GO:0071276;
GO  GO:0071280;
GO  GO:0072738;
GO  GO:0071392;
GO  GO:0071480;
GO  GO:0034605;
GO  GO:0070301;
GO  GO:1904845;
GO  GO:0071222;
GO  GO:1904843;
GO  GO:0035865;
GO  GO:1903936;
GO  GO:0034620;
GO  GO:0071466;
GO  GO:0006952;
GO  GO:0006281;
GO  GO:0000165;
GO  GO:0006397;
GO  GO:0009299;
GO  GO:0051028;
GO  GO:0010667;
GO  GO:2001033;
GO  GO:0010629;
GO  GO:0090084;
GO  GO:1901215;
GO  GO:0031333;
GO  GO:0000122;
GO  GO:1902512;
GO  GO:0120162;
GO  GO:0043280;
GO  GO:0051091;
GO  GO:0010628;
GO  GO:0090261;
GO  GO:0045651;
GO  GO:1904528;
GO  GO:0045931;
GO  GO:1900365;
GO  GO:0045944;
GO  GO:0042531;
GO  GO:0065003;
GO  GO:1900034;
GO  GO:0006357;
GO  GO:0014823;
GO  GO:1990910;
GO  GO:0007584;
GO  GO:1990911;
GO  GO:0033574;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRK
SQ  VVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLA
SQ  MKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPY
SQ  SAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEEPPSPPQSPRVEEASPGRPSS
SQ  VDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQT
SQ  MLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPRPPEAENSSPDSGKQLVHYTAQPLFLLDPGS
SQ  VDTGSNDLPVLFELGEGSYFSEGDGFAEDPTISLLTGSEPPKAKDPTVS
//
ID  P38532;
PN  Heat shock factor protein 1;
GN  Hsf1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:26159920}. Cytoplasm {ECO:0000269|PubMed:26159920}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q00613}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00613}. Note=The monomeric form is cytoplasmic in unstressed cells (PubMed:26159920). Predominantly nuclear protein in both unstressed and heat shocked cells. Translocates in the nucleus upon heat shock. Nucleocytoplasmic shuttling protein. Colocalizes with IER5 in the nucleus. Colocalizes with BAG3 to the nucleus upon heat stress. Localizes in subnuclear granules called nuclear stress bodies (nSBs) upon heat shock. Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock. Colocalizes with PRKACA/PKA in the nucleus and nSBs upon heat shock. Relocalizes from the nucleus to the cytoplasm during the attenuation and recovery phase period of the heat shock response. Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent manner. Together with histone H2AX, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR). Colocalizes with calcium-responsive transactivator SS18L1 at kinetochore region on the mitotic chromosomes. Colocalizes with gamma tubulin at centrosome. Localizes at spindle pole in metaphase. Colocalizes with PLK1 at spindle poles during prometaphase. {ECO:0000250|UniProtKB:Q00613, ECO:0000269|PubMed:26159920}.
DR  UNIPROT: P38532;
DR  UNIPROT: O70462;
DR  Pfam: PF00447;
DR  Pfam: PF06546;
DR  PROSITE: PS00434;
DE  Function: Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage. In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA- binding inactivated monomeric form. Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes. Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival. Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form. Binds to inverted 5'-NGAAN-3' pentamer DNA sequences. Binds to chromatin at heat shock gene promoters. Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH- dependent reductase DHRS2. Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells. Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner. Plays a role in nuclear export of stress-induced HSP70 mRNA. Plays a role in the regulation of mitotic progression. Also plays a role as a negative regulator of non- homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner. Involved in stress-induced cancer cell proliferation in a IER5- dependent manner. {ECO:0000250|UniProtKB:Q00613}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UNE7; IntAct: EBI-7902106; Score: 0.44
DE  Interaction: P11142; IntAct: EBI-7902157; Score: 0.44
DE  Interaction: Q969M3; IntAct: EBI-11091232; Score: 0.35
DE  Interaction: O75665; IntAct: EBI-11091232; Score: 0.35
DE  Interaction: Q9UP38; IntAct: EBI-11091232; Score: 0.35
DE  Interaction: Q9HDC5; IntAct: EBI-11091232; Score: 0.35
DE  Interaction: Q8TDY2; IntAct: EBI-11091232; Score: 0.35
DE  Interaction: Q8WYQ5; IntAct: EBI-11091232; Score: 0.35
DE  Interaction: O75771; IntAct: EBI-11091232; Score: 0.35
DE  Interaction: Q4VC44; IntAct: EBI-11091232; Score: 0.35
DE  Interaction: Q13573; IntAct: EBI-11091232; Score: 0.35
DE  Interaction: P19404; IntAct: EBI-11091232; Score: 0.35
DE  Interaction: Q9UHR4; IntAct: EBI-11091232; Score: 0.35
GO  GO:0005813;
GO  GO:0101031;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0000791;
GO  GO:0000792;
GO  GO:0000776;
GO  GO:0097431;
GO  GO:0097165;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0045120;
GO  GO:0032991;
GO  GO:1990904;
GO  GO:0003682;
GO  GO:0031490;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0003700;
GO  GO:0000981;
GO  GO:0001227;
GO  GO:0140296;
GO  GO:0031072;
GO  GO:0051879;
GO  GO:0042802;
GO  GO:1990841;
GO  GO:0046982;
GO  GO:0019901;
GO  GO:0043621;
GO  GO:0000978;
GO  GO:0001162;
GO  GO:0043565;
GO  GO:1990837;
GO  GO:0098847;
GO  GO:0097677;
GO  GO:0000976;
GO  GO:0061770;
GO  GO:0008283;
GO  GO:0071230;
GO  GO:1904385;
GO  GO:0071276;
GO  GO:0071280;
GO  GO:0072738;
GO  GO:0071392;
GO  GO:0071480;
GO  GO:0034605;
GO  GO:0070301;
GO  GO:0071407;
GO  GO:0071478;
GO  GO:1903936;
GO  GO:0034620;
GO  GO:0006952;
GO  GO:0006281;
GO  GO:0001892;
GO  GO:0060136;
GO  GO:0050673;
GO  GO:0007143;
GO  GO:0001701;
GO  GO:0000165;
GO  GO:0006397;
GO  GO:0009299;
GO  GO:0051028;
GO  GO:0010667;
GO  GO:2001033;
GO  GO:0050680;
GO  GO:0010629;
GO  GO:0090084;
GO  GO:1901215;
GO  GO:0031333;
GO  GO:0000122;
GO  GO:0032720;
GO  GO:1902512;
GO  GO:0008284;
GO  GO:0120162;
GO  GO:0043280;
GO  GO:0051091;
GO  GO:0010628;
GO  GO:0090261;
GO  GO:0045651;
GO  GO:1904528;
GO  GO:0045931;
GO  GO:1900365;
GO  GO:0040018;
GO  GO:0045944;
GO  GO:0061408;
GO  GO:0042531;
GO  GO:0006468;
GO  GO:0065003;
GO  GO:1900034;
GO  GO:0006357;
GO  GO:0032355;
GO  GO:0009408;
GO  GO:0032496;
GO  GO:0033574;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLAVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRK
SQ  VVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTRLLTDVQLMKGKQECMDSKLLA
SQ  MKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLSDSNSAHSVPKYGRQYSLEHVHGPGPY
SQ  SAPSPAYSSSSLYSSDAVTSSGPIISDITELAPTSPLASPGRSIDERPLSSSTLVRVKQEPPSPPHSPRVLEASPGRPSS
SQ  MDTPLSPTAFIDSILRESEPTPAASNTAPMDTTGAQAPALPTPSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLTS
SQ  HGFSVDTSALLDLFSPSVTMPDMSLPDLDSSLASIQELLSPQEPPRPIEAENSNPDSGKQLVHYTAQPLFLLDPDAVDTG
SQ  SSELPVLFELGESSYFSEGDDYTDDPTISLLTGTEPHKAKDPTVS
//
ID  P11147;
PN  Heat shock 70 kDa protein cognate 4;
GN  Hsc70;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus. Note=Localized to a meshwork of cytoplasmic fibers around the nucleus. Translocates to the nucleus after thermal stress.
DR  UNIPROT: P11147;
DR  UNIPROT: Q3KN45;
DR  UNIPROT: Q8SXQ4;
DR  UNIPROT: Q9VFB0;
DR  Pfam: PF00012;
DR  PROSITE: PS00297;
DR  PROSITE: PS00329;
DR  PROSITE: PS01036;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: O96757; IntAct: EBI-75193; Score: 0.37
DE  Interaction: Q9VI55; IntAct: EBI-208882; Score: 0.00
DE  Interaction: Q9VMA3; IntAct: EBI-211214; Score: 0.00
DE  Interaction: Q9VNV2; IntAct: EBI-215710; Score: 0.00
DE  Interaction: Q9VLI5; IntAct: EBI-222379; Score: 0.00
DE  Interaction: Q9VVC2; IntAct: EBI-226363; Score: 0.00
DE  Interaction: Q9VRQ6; IntAct: EBI-228980; Score: 0.00
DE  Interaction: Q9VC50; IntAct: EBI-231555; Score: 0.00
DE  Interaction: Q9VJB0; IntAct: EBI-241955; Score: 0.00
DE  Interaction: Q9VIY9; IntAct: EBI-250829; Score: 0.00
DE  Interaction: Q8IR79; IntAct: EBI-254487; Score: 0.00
DE  Interaction: Q9W3N7; IntAct: EBI-255184; Score: 0.00
DE  Interaction: Q9VNE0; IntAct: EBI-259860; Score: 0.00
DE  Interaction: Q9I7H9; IntAct: EBI-262585; Score: 0.00
DE  Interaction: Q9VU81; IntAct: EBI-265621; Score: 0.00
DE  Interaction: Q8IRH9; IntAct: EBI-266258; Score: 0.00
DE  Interaction: Q9VLG9; IntAct: EBI-268283; Score: 0.00
DE  Interaction: Q24216; IntAct: EBI-268762; Score: 0.00
DE  Interaction: Q9W5G1; IntAct: EBI-271186; Score: 0.00
DE  Interaction: Q9V3F2; IntAct: EBI-272607; Score: 0.00
DE  Interaction: Q9XYW6; IntAct: EBI-273001; Score: 0.00
DE  Interaction: P40301; IntAct: EBI-273005; Score: 0.00
DE  Interaction: Q7JXC4; IntAct: EBI-273009; Score: 0.00
DE  Interaction: Q9VUQ1; IntAct: EBI-273014; Score: 0.00
DE  Interaction: Q5BI03; IntAct: EBI-273022; Score: 0.00
DE  Interaction: Q9W0B2; IntAct: EBI-273018; Score: 0.00
DE  Interaction: Q9VRV9; IntAct: EBI-273026; Score: 0.00
DE  Interaction: Q9VIJ0; IntAct: EBI-273030; Score: 0.00
DE  Interaction: P29413; IntAct: EBI-273034; Score: 0.00
DE  Interaction: Q9XZC2; IntAct: EBI-507718; Score: 0.37
DE  Interaction: Q24570; IntAct: EBI-508174; Score: 0.37
DE  Interaction: Q9VZF4; IntAct: EBI-508300; Score: 0.37
DE  Interaction: Q9VWE4; IntAct: EBI-508930; Score: 0.37
DE  Interaction: Q9VML8; IntAct: EBI-512430; Score: 0.37
DE  Interaction: Q9VRQ2; IntAct: EBI-468896; Score: 0.00
DE  Interaction: Q03751; IntAct: EBI-872154; Score: 0.27
DE  Interaction: P83949; IntAct: EBI-878253; Score: 0.48
DE  Interaction: P25439; IntAct: EBI-1368536; Score: 0.40
DE  Interaction: Q24459; IntAct: EBI-7591079; Score: 0.35
DE  Interaction: P42124; IntAct: EBI-7591102; Score: 0.35
DE  Interaction: Q24133; IntAct: EBI-2110992; Score: 0.37
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: O97143; IntAct: EBI-15878339; Score: 0.35
DE  Interaction: Q24592; IntAct: EBI-16151646; Score: 0.35
GO  GO:0071013;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0005726;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0071011;
GO  GO:0098793;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0140662;
GO  GO:0051087;
GO  GO:0031072;
GO  GO:0051787;
GO  GO:0044183;
GO  GO:0051082;
GO  GO:0007411;
GO  GO:0007413;
GO  GO:0035967;
GO  GO:0034620;
GO  GO:0051085;
GO  GO:0061077;
GO  GO:0061738;
GO  GO:0097753;
GO  GO:0000398;
GO  GO:0007399;
GO  GO:0007269;
GO  GO:0030707;
GO  GO:0035194;
GO  GO:0042026;
GO  GO:0070922;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKAPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTQTIFDAKRLIGRKFDD
SQ  AAVQSDMKHWPFEVVSADGKPKIEVTYKDEKKTFFPEEISSMVLTKMKETAEAYLGKTVTNAVITVPAYFNDSQRQATKD
SQ  AGTIAGLNVLRIINEPTAAAIAYGLDKKAVGERNVLIFDLGGGTFDVSILSIDDGIFEVKSTAGDTHLGGEDFDNRLVTH
SQ  FVQEFKRKHKKDLTTNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGTDFYTSITRARFEELNADLFRSTMDPVEKA
SQ  LRDAKLDKSVIHDIVLVGGSTRIPKVQRLLQDLFNGKELNKSINPDEAVAYGAAVQAAILHGDKSQEVQDLLLLDVTPLS
SQ  LGIETAGGVMSVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELSGIPPAPRGVPQIEVTFDI
SQ  DANGILNVTALERSTNKENKITITNDKGRLSKEDIERMVNEAEKYRNEDEKQKETIAAKNGLESYCFNMKATLDEDNLKT
SQ  KISDSDRTTILDKCNETIKWLDANQLADKEEYEHRQKELEGVCNPIITKLYQGAGFPPGGMPGGPGGMPGAAGAAGAAGA
SQ  GGAGPTIEEVD
//
ID  Q61W58;
PN  Heat shock protein 90;
GN  daf;
OS  6238;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Note=Perinuclear region of somatic cells. {ECO:0000250}.
DR  UNIPROT: Q61W58;
DR  UNIPROT: A8WXX6;
DR  Pfam: PF02518;
DR  Pfam: PF00183;
DE  Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. By stabilizing the receptor-type guanylate cyclase daf-11 or another signal transduction component that regulates cGMP levels, plays a role in dauer formation and chemotaxis to non-volatile and volatile attractants detected by AWC sensory neurons. Participates in the control of cell cycle progression at the prophase/metaphase transition in oocyte development by ensuring the activity of wee-1.3 kinase, which negatively regulates cdk-1 through its phosphorylation. Regulates yap-1 nuclear export after heat shock treatment. {ECO:0000250|UniProtKB:Q18688}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:1990565;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0140662;
GO  GO:0097718;
GO  GO:0042802;
GO  GO:0035259;
GO  GO:1990634;
GO  GO:0051082;
GO  GO:0007049;
GO  GO:0034605;
GO  GO:0061077;
GO  GO:0006935;
GO  GO:0040024;
GO  GO:0050829;
GO  GO:0008340;
GO  GO:0032516;
GO  GO:0006470;
GO  GO:0006611;
GO  GO:0006457;
GO  GO:0050821;
GO  GO:0050920;
GO  GO:0045859;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSENAETFAFQAEIAQLMSLIINTFYSNKEIYLRELISNASDALDKIRYQALTEPSELDTGKELFIKITPNKEEKTLTIM
SQ  DTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAFLVADKVVVTSKNNDDDSYQWESSAGGSFVV
SQ  RPYNDPELTRGTKITMYIKEDQVDFLEERKIKEIVKKHSQFIGYPIKLVVEKEREKEVEDEEAVESKDEEKKEGDVENVG
SQ  EDADAEKDKKKTKKIKEKYFEDEELNKTKPIWTRNPDDISNEEYAEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFAPQ
SQ  RAPFDLFENKKSKNSIKLYVRRVFIMENCEELMPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCMELFD
SQ  EIAEDKDNFKKFYEQFGKNLKLGIHEDSTNRKKLSEFLRYATSAGEEPTSLKEYVSRMKENQTQIYYITGESKEVVAASA
SQ  FVERVKSRGFEVLYMCDPIDEYCVQQLKEYDGKKLVSVTKEGLELPETEEEKKKFEEDKVAYENLCKVIKDILEKKIEKV
SQ  AVSNRLVSSPCCIVTSEYGWSANMERIMKAQALRDSSTMGYMAAKKHLEINPDHAIMKTLRERVEADKNDKTVKDLVVLL
SQ  FETALLSSGFSLEEPQSHASRIYRMIKLGLDIGDEDIEESAVPSSCTAEAKIEGADEDASRMEEVD
//
ID  Q18688;
PN  Heat shock protein 90;
GN  daf;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12950278}. Note=Perinuclear region of somatic cells.
DR  UNIPROT: Q18688;
DR  PDB: 4GQT;
DR  PDB: 4I2Z;
DR  Pfam: PF02518;
DR  Pfam: PF00183;
DE  Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. In response to cellular stress, up-regulated in distal tissues in a pqm-1-dependent manner, preventing protein misfolding and maintaining proteostasis (PubMed:29949773). By stabilizing the receptor-type guanylate cyclase daf-11 or another signal transduction component that regulates cGMP levels, plays a role in dauer formation and chemotaxis to non-volatile and volatile attractants detected by AWC sensory neurons (PubMed:10790386, PubMed:7828815). Participates in the control of cell cycle progression at the prophase/metaphase transition in oocyte development by ensuring the activity of wee-1.3 kinase, which negatively regulates cdk-1 through its phosphorylation (PubMed:16466390). Regulates yap-1 nuclear export after heat shock treatment (PubMed:23396260). {ECO:0000269|PubMed:10790386, ECO:0000269|PubMed:16466390, ECO:0000269|PubMed:23396260, ECO:0000269|PubMed:29949773, ECO:0000269|PubMed:7828815}.
DE  Reference Proteome: Yes;
DE  Interaction: G5EG62; IntAct: EBI-8086780; Score: 0.74
DE  Interaction: P02566; IntAct: EBI-8086901; Score: 0.61
DE  Interaction: G5EGG2; IntAct: EBI-336695; Score: 0.37
DE  Interaction: Q21829; IntAct: EBI-339860; Score: 0.37
DE  Interaction: Q03563; IntAct: EBI-332975; Score: 0.00
DE  Interaction: Q9XVV3; IntAct: EBI-333605; Score: 0.00
DE  Interaction: O76840; IntAct: EBI-334535; Score: 0.00
DE  Interaction: Q20308; IntAct: EBI-337241; Score: 0.00
DE  Interaction: O17218; IntAct: EBI-338108; Score: 0.00
DE  Interaction: O17927; IntAct: EBI-338816; Score: 0.00
DE  Interaction: P45897; IntAct: EBI-340136; Score: 0.00
DE  Interaction: G5EFL5; IntAct: EBI-341354; Score: 0.00
DE  Interaction: O02108; IntAct: EBI-6460076; Score: 0.55
DE  Interaction: Q9XWG3; IntAct: EBI-344915; Score: 0.00
DE  Interaction: P90978; IntAct: EBI-345344; Score: 0.00
DE  Interaction: Q27535; IntAct: EBI-345398; Score: 0.00
DE  Interaction: P20792; IntAct: EBI-360290; Score: 0.51
DE  Interaction: Q18688; IntAct: EBI-360299; Score: 0.63
DE  Interaction: P50488; IntAct: EBI-360536; Score: 0.37
DE  Interaction: Q20234; IntAct: EBI-2916414; Score: 0.00
DE  Interaction: Q11184; IntAct: EBI-3864453; Score: 0.51
DE  Interaction: O16259; IntAct: EBI-6514170; Score: 0.66
DE  Interaction: P09446; IntAct: EBI-6918699; Score: 0.40
DE  Interaction: P34447; IntAct: EBI-21396671; Score: 0.40
GO  GO:0101031;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:1990565;
GO  GO:0045121;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0008287;
GO  GO:0032991;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0140662;
GO  GO:0097718;
GO  GO:0042802;
GO  GO:0035259;
GO  GO:1990634;
GO  GO:0051082;
GO  GO:0007049;
GO  GO:0034605;
GO  GO:0061077;
GO  GO:0006935;
GO  GO:0040024;
GO  GO:0050829;
GO  GO:0008340;
GO  GO:0002119;
GO  GO:0032516;
GO  GO:0006470;
GO  GO:0006611;
GO  GO:0006457;
GO  GO:0022417;
GO  GO:0050821;
GO  GO:0050920;
GO  GO:0045859;
GO  GO:0009408;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSENAETFAFQAEIAQLMSLIINTFYSNKEIYLRELISNASDALDKIRYQALTEPSELDTGKELFIKITPNKEEKTLTIM
SQ  DTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAFLVADKVVVTSKNNDDDSYQWESSAGGSFVV
SQ  RPFNDPEVTRGTKIVMHIKEDQIDFLEERKIKEIVKKHSQFIGYPIKLVVEKEREKEVEDEEAVEAKDEEKKEGEVENVA
SQ  DDADKKKTKKIKEKYFEDEELNKTKPIWTRNPDDISNEEYAEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPQRAPF
SQ  DLFENKKSKNSIKLYVRRVFIMENCEELMPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCMELIDEVAE
SQ  DKDNFKKFYEQFGKNLKLGIHEDSTNRKKLSDFLRYSTSAGDEPTSLKEYVSRMKENQTQIYYITGESKDVVAASAFVER
SQ  VKSRGFEVLYMCDPIDEYCVQQLKEYDGKKLVSVTKEGLELPETEEEKKKFEEDKVAYENLCKVIKDILEKKVEKVGVSN
SQ  RLVSSPCCIVTSEYGWSANMERIMKAQALRDSSTMGYMAAKKHLEINPDHAIMKTLRDRVEVDKNDKTVKDLVVLLFETA
SQ  LLASGFSLEEPQSHASRIYRMIKLGLDIGDDEIEDSAVPSSCTAEAKIEGAEEDASRMEEVD
//
ID  A1YER2;
PN  Oxidoreductase HTATIP2;
GN  HTATIP2;
OS  9595;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: A1YER2;
DR  Pfam: PF13460;
DE  Function: Oxidoreductase required for tumor suppression. NADPH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0016491;
GO  GO:0004674;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0030154;
GO  GO:0051170;
GO  GO:0043068;
GO  GO:0045944;
GO  GO:0046777;
GO  GO:0045765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYAS
SQ  AFQGHDVGFCCLGTTRGKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSKFLYLQVKGEVEAKVEELKFD
SQ  RYSVFRPGVLLCDRQESRPGEWLVRKFFGSLPESWASGHSVPVVTVVRAMLNNVVRPRDKQMELLENKAIHDLGKAHGSL
SQ  KP
//
ID  Q9BUP3;
PN  Oxidoreductase HTATIP2;
GN  HTATIP2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15282309}. Nucleus envelope {ECO:0000269|PubMed:15282309}.
DR  UNIPROT: Q9BUP3;
DR  UNIPROT: A8K7S7;
DR  UNIPROT: D3DQY8;
DR  UNIPROT: O15383;
DR  UNIPROT: O60520;
DR  UNIPROT: O95345;
DR  UNIPROT: Q53GC1;
DR  UNIPROT: Q53GG2;
DR  UNIPROT: Q6IBI3;
DR  PDB: 2BKA;
DR  Pfam: PF13460;
DR  OMIM: 605628;
DR  DisGeNET: 10553;
DE  Function: Oxidoreductase required for tumor suppression. NADPH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. Isoform 1 is a metastasis suppressor with proapoptotic as well as antiangiogenic properties. Isoform 2 has an antiapoptotic effect. {ECO:0000269|PubMed:10611237, ECO:0000269|PubMed:11313954, ECO:0000269|PubMed:15282309, ECO:0000269|PubMed:9174052}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5JX71; IntAct: EBI-24643959; Score: 0.56
DE  Interaction: Q9NQG6; IntAct: EBI-24671087; Score: 0.56
DE  Interaction: Q08426; IntAct: EBI-24683997; Score: 0.56
DE  Interaction: Q8N6M3; IntAct: EBI-24694273; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-24700038; Score: 0.56
DE  Interaction: Q8NBQ5; IntAct: EBI-24722966; Score: 0.56
DE  Interaction: Q99541; IntAct: EBI-24727205; Score: 0.56
DE  Interaction: Q12893; IntAct: EBI-24741240; Score: 0.56
DE  Interaction: Q9H6H4; IntAct: EBI-24754940; Score: 0.56
DE  Interaction: Q3KNW5; IntAct: EBI-23834757; Score: 0.56
DE  Interaction: O00258; IntAct: EBI-24780762; Score: 0.56
DE  Interaction: Q9HDC5; IntAct: EBI-24570639; Score: 0.56
DE  Interaction: Q9UKF7; IntAct: EBI-24650569; Score: 0.56
DE  Interaction: Q8TB40; IntAct: EBI-24758449; Score: 0.56
DE  Interaction: Q9Y371; IntAct: EBI-24759832; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-25185978; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-25202074; Score: 0.56
DE  Interaction: Q9H2K0; IntAct: EBI-24799964; Score: 0.56
DE  Interaction: Q8N5M9; IntAct: EBI-25270050; Score: 0.56
DE  Interaction: P03427; IntAct: EBI-14405248; Score: 0.35
DE  Interaction: Q53F39; IntAct: EBI-21694305; Score: 0.35
DE  Interaction: Q9Y2J4; IntAct: EBI-21884579; Score: 0.35
DE  Interaction: Q9HCD5; IntAct: EBI-21884579; Score: 0.35
DE  Interaction: Q13510; IntAct: EBI-21884579; Score: 0.35
DE  Interaction: O75208; IntAct: EBI-21930142; Score: 0.35
DE  Interaction: P54852; IntAct: EBI-21194685; Score: 0.54
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0016491;
GO  GO:0004674;
GO  GO:0003713;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0030154;
GO  GO:0051170;
GO  GO:0043066;
GO  GO:0043068;
GO  GO:0045944;
GO  GO:0046777;
GO  GO:0045765;
GO  GO:0006357;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYAS
SQ  AFQGHDVGFCCLGTTRGKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSNFLYLQVKGEVEAKVEELKFD
SQ  RYSVFRPGVLLCDRQESRPGEWLVRKFFGSLPDSWASGHSVPVVTVVRAMLNNVVRPRDKQMELLENKAIHDLGKAHGSL
SQ  KP
//
ID  Q9Z2G9;
PN  Oxidoreductase HTATIP2;
GN  Htatip2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q9Z2G9;
DR  UNIPROT: Q810Y5;
DR  UNIPROT: Q99KN6;
DR  UNIPROT: Q9D5F8;
DR  UNIPROT: Q9D804;
DR  PDB: 2FMU;
DR  Pfam: PF13460;
DE  Function: Oxidoreductase required for tumor suppression. NADPH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. {ECO:0000269|PubMed:14695192}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0051287;
GO  GO:0016620;
GO  GO:0004674;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0030154;
GO  GO:0051170;
GO  GO:0043068;
GO  GO:0045944;
GO  GO:0046777;
GO  GO:0045765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADKEALPKLREDFKMQNKSVFILGASGETGKVLLKEILGQNLFSKVTLIGRRKLTFEEEAYKNVNQEVVDFEKLDVYAS
SQ  AFQGHDVGFCCLGTTRSKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSRGADKSSSFLYLQVKGEVEAKVEELKFD
SQ  RLSVFRPGVLLCDRQESRPGEWLARKFFGSLPDSWASGYAVPVVTVVRAMLNNLVSPSSGQMELLENKAILHLGKDRDVP
SQ  KL
//
ID  A1YFX9;
PN  Oxidoreductase HTATIP2;
GN  HTATIP2;
OS  9597;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: A1YFX9;
DR  Pfam: PF13460;
DE  Function: Oxidoreductase required for tumor suppression. NADPH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0051287;
GO  GO:0016620;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0030154;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYAS
SQ  AFQGHDVGFCCLGTTRGKAGAEGFARVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSNFLYLQVKGEVEAKVEELKFD
SQ  RYSVFRPGVXLCDRQESRPGEWLVRKFFGSLPDSWASGHSVPVVTVVRAMLNNVVRPRDKQMELLENKAIHDLGKAHGSL
SQ  KP
//
ID  A2T7G9;
PN  Oxidoreductase HTATIP2;
GN  HTATIP2;
OS  9600;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: A2T7G9;
DR  Pfam: PF13460;
DE  Function: Oxidoreductase required for tumor suppression. NADPH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0051287;
GO  GO:0016620;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0030154;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYAS
SQ  AFQGHDVGFCCLGTTRVKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSNFLYLQVKGEVEAKVEELKFD
SQ  RYSVFRPGVLLCDRQESRPGEWLVRKFFGSLPESWASGYSVPVVTVVRAMLNNMVRPRDKQMELLENKAIHDLGKVHGSL
SQ  KP
//
ID  Q9P2D3;
PN  HEAT repeat-containing protein 5B;
GN  HEATR5B;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15758025}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15758025}. Note=Localization at clathrin- coated vesicles depends on AFTPH/aftiphilin. {ECO:0000269|PubMed:15758025}.
DR  UNIPROT: Q9P2D3;
DR  UNIPROT: B5MDU8;
DR  UNIPROT: Q7Z3B2;
DR  UNIPROT: Q9NVL7;
DR  OMIM: 619627;
DR  DisGeNET: 54497;
DE  Function: Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269|PubMed:15758025}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9P0L0; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: A0A6H3A739; IntAct: EBI-2832030; Score: 0.00
DE  Interaction: P56377; IntAct: EBI-11037753; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: P26045; IntAct: EBI-14024867; Score: 0.42
DE  Interaction: O95292; IntAct: EBI-21550215; Score: 0.35
DE  Interaction: O14965; IntAct: EBI-21639587; Score: 0.35
DE  Interaction: Q9Y6Q5; IntAct: EBI-21760726; Score: 0.35
DE  Interaction: Q14160; IntAct: EBI-20731245; Score: 0.44
DE  Interaction: Q12959; IntAct: EBI-20731998; Score: 0.44
DE  Interaction: O00213; IntAct: EBI-21017901; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
GO  GO:0030136;
GO  GO:0005829;
GO  GO:0030139;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0016607;
GO  GO:0048471;
GO  GO:0006897;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:0042147;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELAHSLLLNEEALAQITEAKRPVFIFEWLRFLDKVLVAANKTDVKEKQKKLVEQLTGLISSSPGPPTRKLLAKNLAALY
SQ  SIGDTFTVFQTLDKCNDIIRNKDDTAAYLPTKLAAVACVGAFYEKMGRMLGSAFPETVNNLLKSLKSAESQGRSEILMSL
SQ  QKVLSGLGGAAASSHRDIYKNARSLLTDRSMAVRCAVAKCLLELQNEAVFMWTAELENIATLCFKALENSNYGVRVAVSK
SQ  LLGTVMATALMPKQATVMRQNVKRATFDEVLELMATGFLRGGSGFLKSGGEMLKVGGSVNREVRVGVTQAYVVFVTTLGG
SQ  QWLERSFATFLSHVLDLVSHPRATQTHVEAVYSRRCVSFILRATVGSLLGEKAQIAAAKEICQAIGKQMKAVEAVVNDTS
SQ  GENKSGAADIAASQHVMVCALQELGSLVQSLNATASPLIQEASIGLLEIVTSVLLHPSMAARLAAAWCLRCVAVALPFQL
SQ  TPFLDRCAERLNNLKTSPEAVSGYSFAMAALLGGVHQCPLGIPHAKGKMVVSIAEDLLRTAAQNSRLSLQRTQAGWLLLG
SQ  ALMTLGPSVVRYHLPKMLLLWRNVFPRSLKELEAEKARGDSFTWQVTLEGRAGALCAMRSFVAHCPELLTEDVIRKLMTP
SQ  IECAMTMMSHIPSVMKAHGAHLKASAAMVRLRLYDILALLPPKTYEGSFNALLRELVAEFTLTDNSANTTTSLLRSLCHY
SQ  DDSVLLGSWLQETDHKSIEDQLQPNSASGSGALEHDPSSIYLRIPAGEAVPGPLPLGVSVIDASVALFGVVFPHVSYKHR
SQ  LQMLDHFAECVKQAKGVRQQAVQLNIFTAVLSALKGLAENKSTLGPEEVRKSALTLVMGPLDNPNPILRCAAGEALGRMA
SQ  QVVGEATFIARMAQYSFDKLKSARDVVSRTGHSLALGCLHRYVGGIGSGQHLKTSVSILLALAQDGTSPEVQTWSLHSLA
SQ  LIVDSSGPMYRGYVEPTLSLVLTLLLTVPPSHTEVHQCLGRCLGAIITTVGPELQGNGATTSTIRSSCLVGCAITQDHSD
SQ  SLVQAAAISCLQQLHMFAPRHVNLSSLVPSLCVHLCSSHLLLRRAAVACLRQLAQREAAEVCEYAMSLAKNTGDKESSSA
SQ  NVSPFAPGVSSRTDIHCRHQGVNITETGLEGLLFGMLDRETDRKLCSDIHDTLGHMLSSLAVEKLSHWLMLCKDVLAASS
SQ  DMSTATLLSSGKDEEAEKKDEMDDDTMFTTLGEEDKSKPFVAPRWATRVFAADCLCRIINLCENADQAHFDLALARSAKL
SQ  RNPTNDLLVLHLSDLIRMAFMAATDHSNQLRMAGLQALEDIIKKFASVPEPEFPGHVILEQYQANVGAALRPAFSQDTPS
SQ  DIIAKACQVCSTWIGSGVVSDLNDLRRVHNLLVSSLDKVQAGKGSSSQLYRESATTMEKLAVLKAWAEVYVVAMNIKKEA
SQ  ESKPKRAIKNTDDDDDDCGTIDELPPDSLITLVQPELPTLSRLWLAALKDYALLTLPAEFSSQLPPDGGAFYTPETIDTA
SQ  RLHYRNSWAPILHAVALWLNSTGFTCSESTEAAAISGLQKRSTSVNLNQASGAVGSAKSLPEINKDRMHLILGVSIQFLC
SQ  SPRPEEPIEHVTACLQALHTLLDSPYARVHIAEDQLIGVELLSVLHRLLLTWNPSSVQLLVTGVVQQIVRAAQDYLQEKR
SQ  NTLNEDDMEKEACTVLGEGGDSGGLIPGKSLVFATMELLMFILVRHMPHLSTKVSDSPSHIATKTRLSEESARLVAATVT
SQ  ILSDLPSLCSPAGCMTILPTILFLIARILKDTAIKSADNQVPPPVSAALQGIKSIVTLSMAKTEAGVQKQWTALIRSTLA
SQ  CILEYSQPEDSVPTPDEVSMLTAIALFLWSASNEIIGVQSLQNGCMNRFKNALNSCDPWVQAKCYQLLLSVFQHSNRALS
SQ  TPYIHSLAPIVVEKLKAVERNRPASNIELLAVQEGIKVLETLVALGEEQNRVQLLALLVPTLISYLLDENSFASASSASK
SQ  DLHEFALQNLMHIGPLYPHAFKTVMGAAPELKVRLETAVRASQASKAKAAARQPAPAIHSAPTIKLKTSFF
//
ID  Q8C547;
PN  HEAT repeat-containing protein 5B;
GN  Heatr5b;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9P2D3}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9P2D3}. Note=Localization at clathrin- coated vesicles depends on AFTPH/aftiphilin. {ECO:0000250|UniProtKB:Q9P2D3}.
DR  UNIPROT: Q8C547;
DR  UNIPROT: Q3TPS4;
DR  UNIPROT: Q5DTY0;
DR  UNIPROT: Q5PRF1;
DR  UNIPROT: Q8C6W1;
DR  UNIPROT: Q8C773;
DE  Function: Component of clathrin-coated vesicles (By similarity). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (By similarity). {ECO:0000250|UniProtKB:Q9P2D3}.
DE  Reference Proteome: Yes;
DE  Interaction: P61027; IntAct: EBI-11567802; Score: 0.35
DE  Interaction: P62158; IntAct: EBI-911456; Score: 0.35
GO  GO:0030136;
GO  GO:0005829;
GO  GO:0030139;
GO  GO:0043231;
GO  GO:0016607;
GO  GO:0048471;
GO  GO:0006897;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:0042147;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELAHSLLLNEEALAQITEAKRPVFIFEWLRFLDKVLVAANKTDVKEKQKKLVEQLTGLISSSPGPPTRKLLAKNLAALY
SQ  SIGDTYTVFQTLDKCNDIIRSKDDTAAYLPTKLAAVACVGAFYEKMGRMLGSAFPETVNNLLKSLKSAESQGRSEILMSL
SQ  QKVLTGLGGAAASSHRDIYKNARSLLTDRSMAVRCAVAKCLLELQNEAVFMWTAELENVATLCFKALENSNYGVRVAVSK
SQ  LLGTVMATALMPKQATVMRQNVKRATFDEVLELMATGFLRGGSGFLKSGGEMLKVGGSVNREVRVGVTQAYVVFVTTLGG
SQ  QWLERSFATFLSHVLDLVSHPRATQTHVDAVYSRRCVSFMLRATVGSLLGEKAQIAAAKEICQAIGKQMKAVEAVVNDTS
SQ  SENKSGTADIAASQHVMVCALQELGSLVQSLNATASPLIQEASIGLLEIVTSVLLHPSMAARLAAAWCLRCVAVALPFQL
SQ  TPFLDRCAERLNNLKTSPEAVSGYSFAMAALLGGVHQCPLGIPHAKGKMVVSIAEDLLRTAAQNSRLSLQRTQAGWLLLG
SQ  ALMTLGPSVVRYHLPKMLLLWRNVFPRSLKELEAEKARGDSFTWQVTLEGRAGALCAMRSFVAHCPELLTEDAIRKLMTP
SQ  IECAMTMMSHIPSVIKAHGAHLKASAAMVRLRLYDILALLPPKTYEGSFNALLRELVAEFTLTDNSANTTTSLLRSLCHY
SQ  DDSVLLGSWLQETDHKSIEDQLQPNSASGSGALEHDPSSIYLRIPAGEAVPGPLPLGVSVIDASVALFGVVFPHVSYKHR
SQ  LQMLDHFAECVKQAKGVRQQAVQLNIFTAVLSALKGLAENKSTLGPEEVRKSALTLVMGALDNPNPILRCAAGEALGRMA
SQ  QVVGEASFIARMAQYSFDKLKSARDVVSRTGHSLALGCLHRYVGGIGSGQHLKTSVSILLALAQDGTSPEVQTWSLHSLA
SQ  LIVDSSGPMYRGYVEPTLSLVLTLLLTVPPSHTEVHQCLGRCLGAIITTVGPELQGNAATISTIRSSCLVGCAITQDHSD
SQ  SLVQAAAISCLQQLHMFAPRHVNLSSLVPSLCVHLCSSHLLLRRAAVACLRQLAQREAAEVCEYAMSLAKNAGDKEISGG
SQ  NVNPFTPGVSSRSDVHCRHQGVNITDTGLEGLLFGMLDRETDRKLCSDIHDTLGHMLSSLAVEKLSHWLMLCKDVLAASS
SQ  DMSAATLLSSGKDEESEKKDEMDDDAMFTTLGEEDKSKPFVAPRWATRVFAADCLCRIINLCENSDQAHFDLALARSAKL
SQ  RNPKNDLLVLHLSDLIRMAFMAATDHSNQLRMAGLQALEDIIKKFASVPEPEFPGHVILEQYQANVGAALRPAFSQDTPS
SQ  DIIAKACQVCSTWIGSGVVSDLNDLRRVHNLLVSSLDTVQAGKGSSSQLYRESATTMEKLAVLKAWAEVYVVAMNIKKEA
SQ  ESKPKRAMNNPDDDDDDYGTIDELPPDSLITLVQPELPTLSRLWLAALKDYALLTLPAEFSSQLPPDGGAFYTPETIDTA
SQ  RLHYRNSWAPILHAVALWLNSTGFISQESTEATTVSGVQKRSPAVSLNQVPGAMASAKPLPEVNKDRMHLILGVSIQFLC
SQ  SPRPEEPIEHVTACLQALHTLLGSPYARIHIAEDQLIGVELLSVLHRLLLTWNPPSIQLLVTGVVQQIVRAAQDYLQEKR
SQ  NALNEEDMEKESCPTLGEGGDTGGLIPGKSLVFATMELLMFILVRHMPHLSTKMLDSPSHTAMKTQLSEESARLVAATVA
SQ  ILSDLPSLCSPAGCMTILPTILFLIARILKDTAIKSADNQVPPPVSAALQGIKSIVTLSMAKTEDTQKQWTTLIRSTLAC
SQ  ILEYSQPDDCMPAPDEVSTLTAIALFLWSASSEIIGVQSLQNGCMNRFKSALNSCDPWVQAKCYQLLLSVFQHSNRALST
SQ  PYIHSLAPLVVGKLKAVERHRPASSTELLAVQEGIKVLETLVALGEEQNRVQLLALLVPTLISYLLDENSFASASSISKD
SQ  LHEFALQNLMHIGPLYPHAFKTVMGAAPELKARLETAVRASQASKAKAAARQPAPTTHSTPTIKLKTSFF
//
ID  Q13261;
PN  Soluble interleukin-15 receptor subunit alpha;
GN  IL15RA;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000269|PubMed:10480910}; Single- pass type I membrane protein {ECO:0000269|PubMed:10480910}. Nucleus membrane {ECO:0000269|PubMed:10480910}; Single-pass type I membrane protein {ECO:0000269|PubMed:10480910}. Cell surface {ECO:0000269|PubMed:15123770}. Note=Mainly found associated with the nuclear membrane. [Isoform 5]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single- pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. [Isoform 6]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single- pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. [Isoform 7]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single- pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. [Isoform 8]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single- pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. [Soluble interleukin-15 receptor subunit alpha]: Secreted, extracellular space {ECO:0000269|PubMed:15265897}.
DR  UNIPROT: Q13261;
DR  UNIPROT: B4E2C2;
DR  UNIPROT: Q3B769;
DR  UNIPROT: Q5JVA1;
DR  UNIPROT: Q5JVA2;
DR  UNIPROT: Q5JVA4;
DR  UNIPROT: Q6B0J2;
DR  UNIPROT: Q7LDR4;
DR  UNIPROT: Q7Z609;
DR  PDB: 2ERS;
DR  PDB: 2Z3Q;
DR  PDB: 2Z3R;
DR  PDB: 4GS7;
DR  PROSITE: PS50923;
DR  OMIM: 601070;
DR  DisGeNET: 3601;
DE  Function: High-affinity receptor for interleukin-15 (PubMed:8530383). Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells (By similarity). In neutrophils, binds and activates kinase SYK in response to IL15 stimulation (PubMed:15123770). In neutrophils, required for IL15- induced phagocytosis in a SYK-dependent manner (PubMed:15123770). Expression of different isoforms may alter or interfere with signal transduction (PubMed:10480910). {ECO:0000250|UniProtKB:Q60819, ECO:0000269|PubMed:10480910, ECO:0000269|PubMed:15123770, ECO:0000269|PubMed:8530383}. [Isoform 5]: Does not bind IL15. {ECO:0000269|PubMed:10480910}. [Isoform 6]: Does not bind IL15. {ECO:0000269|PubMed:10480910}. [Isoform 7]: Does not bind IL15. {ECO:0000269|PubMed:10480910}. [Isoform 8]: Does not bind IL15. {ECO:0000269|PubMed:10480910}.
DE  Reference Proteome: Yes;
DE  Interaction: O95999; IntAct: EBI-3910825; Score: 0.37
DE  Interaction: P11802; IntAct: EBI-3906693; Score: 0.37
DE  Interaction: P40933; IntAct: EBI-980314; Score: 0.66
DE  Interaction: P24941; IntAct: EBI-3906648; Score: 0.37
DE  Interaction: P35243; IntAct: EBI-3910805; Score: 0.37
DE  Interaction: O14936; IntAct: EBI-3910815; Score: 0.37
DE  Interaction: Q8N2W9; IntAct: EBI-3918941; Score: 0.37
DE  Interaction: P14784; IntAct: EBI-6858800; Score: 0.59
DE  Interaction: P31785; IntAct: EBI-6858800; Score: 0.52
GO  GO:0009986;
GO  GO:0030659;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0005615;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0004896;
GO  GO:0042010;
GO  GO:0019901;
GO  GO:0035723;
GO  GO:0001779;
GO  GO:0032825;
GO  GO:0050766;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPRRARGCRTLGLPALLLLLLLRPPATRGITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKA
SQ  TNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPAASSPSSNNTAATTAAIVPGSQLMPSKSPST
SQ  GTTEISSHESSHGTPSQTTAKNWELTASASHQPPGVYPQGHSDTTVAISTSTVLLCGLSAVSLLACYLKSRQTPPLASVE
SQ  MEAMEALPVTWGTSSRDEDLENCSHHL
//
ID  Q60819;
PN  Soluble interleukin-15 receptor subunit alpha;
GN  Il15ra;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q13261}; Single- pass type I membrane protein {ECO:0000250|UniProtKB:Q13261}. Nucleus membrane {ECO:0000250|UniProtKB:Q13261}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13261}. Cell surface {ECO:0000250|UniProtKB:Q13261}. [Soluble interleukin-15 receptor subunit alpha]: Secreted, extracellular space {ECO:0000250}.
DR  UNIPROT: Q60819;
DR  UNIPROT: A2AP35;
DR  UNIPROT: A2AP36;
DR  UNIPROT: A2AP37;
DR  UNIPROT: Q80Z90;
DR  UNIPROT: Q80Z91;
DR  UNIPROT: Q80Z92;
DR  UNIPROT: Q8R5E4;
DR  PDB: 2PSM;
DR  Pfam: PF00084;
DR  PROSITE: PS50923;
DE  Function: High-affinity receptor for interleukin-15 (PubMed:17947230). Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells (PubMed:17947230). In neutrophils, binds and activates kinase SYK in response to IL15 stimulation (By similarity). In neutrophils, required for IL15-induced phagocytosis in a SYK-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q13261, ECO:0000269|PubMed:17947230}.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0031410;
GO  GO:0005615;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0042010;
GO  GO:0019901;
GO  GO:0035723;
GO  GO:0001779;
GO  GO:0010977;
GO  GO:0032825;
GO  GO:0050766;
GO  GO:0007259;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASPQLRGYGVQAIPVLLLLLLLLLLPLRVTPGTTCPPPVSIEHADIRVKNYSVNSRERYVCNSGFKRKAGTSTLIECVI
SQ  NKNTNVAHWTTPSLKCIRDPSLAHYSPVPTVVTPKVTSQPESPSPSAKEPEAFSPKSDTAMTTETAIMPGSRLTPSQTTS
SQ  AGTTGTGSHKSSRAPSLAATMTLEPTASTSLRITEISPHSSKMTKVAISTSVLLVGAGVVMAFLAWYIKSRQPSQPCRVE
SQ  VETMETVPMTVRASSKEDEDTGA
//
ID  Q8R412;
PN  Interferon alpha-inducible protein 27-like protein 2A;
GN  Ifi27l2a;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000305|PubMed:22427340}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q8R412;
DR  Pfam: PF06140;
DE  Function: May be involved in the interferon-induced negative regulation of the transcriptional activity of NR4A1, NR4A2 and NR4A3 through the enhancement of XPO1-mediated nuclear export of these nuclear receptors (PubMed:22427340). Through the regulation of NR4A1 transcriptional activity, may play a role in the vascular response to injury (PubMed:22427340). {ECO:0000269|PubMed:22427340}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0042802;
GO  GO:0007568;
GO  GO:0097190;
GO  GO:0009615;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLGTLFGSAIGGALAVAGAPVALAAMGFTGTGIAAASIAAKMMSAAAIANGGGVAAGSLVATLQSAGVLGLSTSTNAILG
SQ  AAGAAVGALL
//
ID  O42254;
PN  Insulin-like growth factor 2 mRNA-binding protein 1;
GN  IGF2BP1;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9NZI8}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9NZI8}. Cell projection, growth cone. Cell projection, filopodium. Cell projection, lamellipodium. Note=In the nucleus, located in discrete foci, coinciding with the sites of ACTB transcription. Export from the nucleus is mediated by XPO1. In the cytoplasm, colocalizes with ACTB mRNA at the leading edge, in growth cone filopodia and along neurites. In these locations, also colocalizes with microtubules. Colocalization with ACTB mRNA is partially lost at the cell periphery, suggesting release of the transcript. In neuronal processes, exhibits fast retrograde and anterograde movements, when associated with ACTB mRNA; this motility is lost when the association is inhibited. In migrating fibroblasts, localizes not only to leading edges, but also to retracting tails. In response to cellular stress, such as oxidative stress or heat shock, recruited to stress granules.
DR  UNIPROT: O42254;
DR  PDB: 2N8L;
DR  PDB: 2N8M;
DR  Pfam: PF00013;
DR  Pfam: PF00076;
DR  PROSITE: PS50084;
DR  PROSITE: PS50102;
DE  Function: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6- methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation in polarized cells, a crucial process for cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves by a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The ribonucleoparticle (RNP) thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, IGF2BP1 prevents beta-actin mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated by SRC. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. The monomeric ACTB protein then assembles into the subcortical actin cytoskeleton, which pushes the leading edge onwards. Binds MYC mRNA. Binding to MYC mRNA is enhanced by m6A-modification of the CRD (By similarity). Promotes the directed movement of cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up- regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. {ECO:0000250|UniProtKB:Q9NZI8, ECO:0000269|PubMed:11502257, ECO:0000269|PubMed:12507992, ECO:0000269|PubMed:12573215, ECO:0000269|PubMed:16306994, ECO:0000269|PubMed:22279049, ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:9121465}.
DE  Reference Proteome: Yes;
GO  GO:0070937;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0030175;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0003730;
GO  GO:0003729;
GO  GO:1990247;
GO  GO:0070934;
GO  GO:0051028;
GO  GO:0017148;
GO  GO:0007399;
GO  GO:0010976;
GO  GO:0010468;
GO  GO:0051252;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNKLYIGNLNESVTPADLEKVFNDHKISFSGQFLVKSGYAFVDCPDEQWAMKAIETFSGKVELHGKQLEIEHSVPKKQRS
SQ  RKIQIRNIPPQLRWEVLDGLLAQYGTVENCEQVNTDSETAVVNVTYTNREQTRQAIMKLNGHQLENHVLKVSYIPDEQSV
SQ  QGPENGRRGGFGARGAPRQGSPVTAGAPVKQQPVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAA
SQ  EKAISIHSTPEGCSAACKMILEIMQKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTL
SQ  YNPERTITVKGSIENCCKAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSNAVPPPPSSVSGAAPYSSFM
SQ  PPEQETVHVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVVITGPPEAQFKAQGRIYGKLKEENFFG
SQ  PKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENEQVIVKIIGHFYASQMAQRKIRDILAQVK
SQ  QQHQKGQSGQLQARRK
//
ID  Q08CK7;
PN  Insulin-like growth factor 2 mRNA-binding protein 1;
GN  igf2bp1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9NZI8}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9NZI8}. Cell projection, growth cone {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}.
DR  UNIPROT: Q08CK7;
DR  Pfam: PF00013;
DR  Pfam: PF00076;
DR  PROSITE: PS50084;
DR  PROSITE: PS50102;
DE  Function: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6- methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation in polarized cells, a crucial process for cell migration and neurite outgrowth. Promotes the directed movement of cells by fine- tuning intracellular signaling networks and enhances the velocity of cell migration (By similarity). {ECO:0000250|UniProtKB:Q9NZI8}.
DE  Reference Proteome: Yes;
GO  GO:0070937;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0030175;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0003730;
GO  GO:0003729;
GO  GO:1990247;
GO  GO:0070934;
GO  GO:0051028;
GO  GO:0007399;
GO  GO:0003407;
GO  GO:0010468;
GO  GO:0051252;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNKLYIGNLNEKVTAEDLVKTFEDYKIPYSGQFLMKTGYASVDCPDDQWAMKAIETFSGKVELHGKRIEVEHSVPKKQRT
SQ  RKLQIRNIPPHLQWEVLDGLLAQYGTVENCEQVNTDSETAVVNVTYGTREQARQAIQKLNGYQFDNNALRVSYIPDENSE
SQ  VDSQRGPDNGRRPGYGPRGTSRQMSPGSGIPSKHQHADIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENA
SQ  GAAEKPISIHSTPEGCSAACRMILEIMNQEAKDTKTADEVPLKVLAHNNFVGRLIGKEGRNLKKVEQDTDTKITISPLQD
SQ  LTLYNPERTITVKGSIEACCLAEQEIMKKVREAYDNDIAAMNQQTHLIPGLNLGAIGLFPPSSAMPPPALGNSVPGPPYG
SQ  PMGASEQETVHVYIPAQAVGALIGKKGQHIKQLSRFAGASIKIAPAEAPDSKMRMVIVTGPPEAQFKAQGRIYGKLKEEN
SQ  FFGPKEEVKLETHIKVAAAAAGRVIGKGGKTVNELQNLTAAEVVVPREQTPDEHDQVIVKIIGHFYASQLAQRKIRDILT
SQ  QVKQQQKGGGMGTPQGPHPQGMTELGSPQGLAQEPRRK
//
ID  Q9NZI8;
PN  Insulin-like growth factor 2 mRNA-binding protein 1;
GN  IGF2BP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body {ECO:0000269|PubMed:29476152}. Cytoplasm, Stress granule {ECO:0000269|PubMed:29476152}. Cell projection, lamellipodium. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell projection, growth cone. Cell projection, filopodium {ECO:0000250}. Cell projection, axon {ECO:0000250}. Note=In the nucleus, located in discrete foci, coinciding with the sites of ACTB transcription (By similarity). In the cytoplasm, localizes in cytoplasmic mRNP granules. Colocalizes with microtubules in growth cone filopodia and along neurites in neuronal cells (By similarity). Cytoplasmic colocalization with ACTB mRNA is partially lost at the cell periphery, suggesting release of the transcript. In neuronal processes, exhibits fast retrograde and anterograde movements, when associated with ACTB mRNA; this motility is lost when the association is inhibited (By similarity). In hippocampal neurons, predominantly located within dendrites, particularly at dendritic branching points in young cells, compared to axons (By similarity). In axons, predominantly found in axonal branches and their growth cones (By similarity). In motile cells, such as migrating fibroblasts, localizes to leading edges where it colocalizes with microtubules and microfilaments and to retracting tails (By similarity). Dendritic levels are regulated by neuronal activity and glutaminergic signals: they are increased by KCl-induced depolarization, which induces rapid efflux from the cell body into dendrites, and decreased by the NMDA receptor agonist (By similarity). In motile cells, transported towards the leading edge into the cortical region of the lamellipodia where it is connected to microfilaments (By similarity). In response to cellular stress, such as oxidative stress or heat shock, recruited to stress granules, but not to processing bodies. {ECO:0000250}.
DR  UNIPROT: Q9NZI8;
DR  UNIPROT: C9JT33;
DR  PDB: 3KRM;
DR  PDB: 6QEY;
DR  Pfam: PF00013;
DR  Pfam: PF00076;
DR  PROSITE: PS50084;
DR  PROSITE: PS50102;
DR  OMIM: 608288;
DR  DisGeNET: 10642;
DE  Function: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6- methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152, PubMed:32245947). Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence preventing MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD (PubMed:29476152). Binding to MYC mRNA is enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA- dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts. {ECO:0000250, ECO:0000269|PubMed:10875929, ECO:0000269|PubMed:16356927, ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:16778892, ECO:0000269|PubMed:17101699, ECO:0000269|PubMed:17255263, ECO:0000269|PubMed:17893325, ECO:0000269|PubMed:18385235, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19541769, ECO:0000269|PubMed:19647520, ECO:0000269|PubMed:20080952, ECO:0000269|PubMed:22279049, ECO:0000269|PubMed:29476152, ECO:0000269|PubMed:32245947, ECO:0000269|PubMed:8132663, ECO:0000269|PubMed:9891060}.
DE  Reference Proteome: Yes;
DE  Interaction: O75569; IntAct: EBI-1081716; Score: 0.00
DE  Interaction: P42704; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q06787; IntAct: EBI-26367348; Score: 0.35
DE  Interaction: Q8NC51; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NX58; IntAct: EBI-1059651; Score: 0.00
DE  Interaction: P62633; IntAct: EBI-1060912; Score: 0.00
DE  Interaction: Q9UHX1; IntAct: EBI-1061218; Score: 0.00
DE  Interaction: Q9NRG4; IntAct: EBI-1063796; Score: 0.00
DE  Interaction: P49841; IntAct: EBI-1064100; Score: 0.00
DE  Interaction: P78330; IntAct: EBI-1064352; Score: 0.00
DE  Interaction: Q9UET6; IntAct: EBI-1067710; Score: 0.00
DE  Interaction: Q13418; IntAct: EBI-1076453; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1076582; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1082794; Score: 0.00
DE  Interaction: P52565; IntAct: EBI-1084000; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.35
DE  Interaction: Q9UL18; IntAct: EBI-7641579; Score: 0.35
DE  Interaction: Q9UKV8; IntAct: EBI-7642941; Score: 0.35
DE  Interaction: P32121; IntAct: EBI-1642567; Score: 0.35
DE  Interaction: Q9HCK5; IntAct: EBI-2269711; Score: 0.35
DE  Interaction: P62960; IntAct: EBI-2560211; Score: 0.40
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-3045543; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-3050465; Score: 0.35
DE  Interaction: O95503; IntAct: EBI-3951754; Score: 0.35
DE  Interaction: Q9HC52; IntAct: EBI-3951861; Score: 0.35
DE  Interaction: P62993; IntAct: EBI-3964621; Score: 0.35
DE  Interaction: Q6QDQ4; IntAct: EBI-5276631; Score: 0.35
DE  Interaction: P67809; IntAct: EBI-5325180; Score: 0.58
DE  Interaction: P03496; IntAct: EBI-6154589; Score: 0.35
DE  Interaction: Q99AU3; IntAct: EBI-6157083; Score: 0.35
DE  Interaction: O56264; IntAct: EBI-6157161; Score: 0.35
DE  Interaction: P04487; IntAct: EBI-6157560; Score: 0.35
DE  Interaction: D1LN35; IntAct: EBI-6159328; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q5U5Q3; IntAct: EBI-8011718; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q13619; IntAct: EBI-21324822; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-21327757; Score: 0.35
DE  Interaction: Q15843; IntAct: EBI-21328206; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q93034; IntAct: EBI-21331078; Score: 0.35
DE  Interaction: Q4VGL6; IntAct: EBI-8759371; Score: 0.35
DE  Interaction: P0C090; IntAct: EBI-8759987; Score: 0.35
DE  Interaction: P41218; IntAct: EBI-9996028; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-11322719; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: P03211; IntAct: EBI-11722110; Score: 0.35
DE  Interaction: Q6VGS8; IntAct: EBI-11733617; Score: 0.35
DE  Interaction: F8VQC1; IntAct: EBI-11054725; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-11088773; Score: 0.58
DE  Interaction: P60229; IntAct: EBI-11148789; Score: 0.35
DE  Interaction: P19712; IntAct: EBI-10901375; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9UBX2; IntAct: EBI-11601780; Score: 0.35
DE  Interaction: O00571; IntAct: EBI-13949286; Score: 0.35
DE  Interaction: O95793; IntAct: EBI-13949286; Score: 0.54
DE  Interaction: Q15366; IntAct: EBI-13949405; Score: 0.43
DE  Interaction: Q9NUL3; IntAct: EBI-13949405; Score: 0.35
DE  Interaction: Q15717; IntAct: EBI-13949405; Score: 0.43
DE  Interaction: Q12906; IntAct: EBI-13949405; Score: 0.35
DE  Interaction: P11940; IntAct: EBI-13949405; Score: 0.35
DE  Interaction: Q9UKA9; IntAct: EBI-13949405; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-13949405; Score: 0.43
DE  Interaction: Q08211; IntAct: EBI-13949405; Score: 0.43
DE  Interaction: P0DJD3; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: P51991; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: P61978; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q99729; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q01826; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q9Y2W6; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: P16989; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q2VIK8; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q96PU8; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: P26599; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: O00425; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q9Y6M1; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: P82930; IntAct: EBI-21521832; Score: 0.35
DE  Interaction: Q12926; IntAct: EBI-21666158; Score: 0.35
DE  Interaction: Q8IYD1; IntAct: EBI-21666681; Score: 0.35
DE  Interaction: Q15050; IntAct: EBI-21678544; Score: 0.35
DE  Interaction: P54645; IntAct: EBI-16361875; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16362252; Score: 0.35
DE  Interaction: Q8VDS3; IntAct: EBI-16248011; Score: 0.50
DE  Interaction: Q9HCE1; IntAct: EBI-16248043; Score: 0.40
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q15646; IntAct: EBI-21262435; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9H9Z2; IntAct: EBI-25480521; Score: 0.35
DE  Interaction: O43572; IntAct: EBI-26451580; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-26396827; Score: 0.35
DE  Interaction: P14240; IntAct: EBI-26968430; Score: 0.35
DE  Interaction: Q99608; IntAct: EBI-26955247; Score: 0.27
DE  Interaction: P0DTC9; IntAct: EBI-26994159; Score: 0.35
DE  Interaction: Q9BZB8; IntAct: EBI-29019560; Score: 0.42
DE  Interaction: Q9UIH9; IntAct: EBI-29019642; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O43474; IntAct: EBI-29020028; Score: 0.35
DE  Interaction: O60248; IntAct: EBI-29371942; Score: 0.42
DE  Interaction: P48431; IntAct: EBI-29373058; Score: 0.35
DE  Interaction: P35711; IntAct: EBI-29375677; Score: 0.35
DE  Interaction: P35712; IntAct: EBI-29384845; Score: 0.35
DE  Interaction: P31314; IntAct: EBI-29607649; Score: 0.35
DE  Interaction: O43763; IntAct: EBI-29612789; Score: 0.35
DE  Interaction: Q8TDD2; IntAct: EBI-29740517; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
GO  GO:0070161;
GO  GO:0070937;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0030175;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:1990247;
GO  GO:0003723;
GO  GO:0045182;
GO  GO:0070934;
GO  GO:0140059;
GO  GO:0051028;
GO  GO:1900152;
GO  GO:0017148;
GO  GO:0007399;
GO  GO:0097150;
GO  GO:0022013;
GO  GO:2000767;
GO  GO:0001817;
GO  GO:0010468;
GO  GO:0010610;
GO  GO:0051252;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRS
SQ  RKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIA
SQ  QGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQQVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAA
SQ  EKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTL
SQ  YNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFM
SQ  QAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVIITGPPEAQFKAQGRIYGKLKEENFF
SQ  GPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQV
SQ  KQQHQKGQSNQAQARRK
//
ID  O88477;
PN  Insulin-like growth factor 2 mRNA-binding protein 1;
GN  Igf2bp1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9NZI8}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9NZI8}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, axon {ECO:0000250}. Note=In the nucleus, located in discrete foci, coinciding with the sites of ACTB transcription (By similarity). In the cytoplasm, localizes in cytoplasmic mRNP granules. Colocalizes with microtubules in growth cone filopodia and along neurites in neuronal cells (By similarity). Cytoplasmic colocalization with ACTB mRNA is partially lost at the cell periphery, suggesting release of the transcript (By similarity). In hippocampal neurons, predominantly located within dendrites, particularly at dendritic branching points in young cells, compared to axons (By similarity). In axons, predominantly found in axonal branches and their growth cones (By similarity). In neuronal processes, exhibits fast retrograde and anterograde movements, when associated with ACTB mRNA; this motility is lost when the association is inhibited (By similarity). Dendritic levels are regulated by neuronal activity and glutaminergic signals: they are increased by KCl-induced depolarization, which induces rapid efflux from the cell body into dendrites, and decreased by NMDA receptor agonists (By similarity). In motile cells, such as migrating fibroblasts, localizes to leading edges where it colocalizes with microtubules and microfilaments and to retracting tails (By similarity). In motile cells, transported towards the leading edge into the cortical region of the lamellipodia where it is connected to microfilaments (By similarity). In response to cellular stress, such as oxidative stress or heat shock, recruited to stress granules, but not to processing bodies (By similarity). {ECO:0000250}.
DR  UNIPROT: O88477;
DR  UNIPROT: Q80US9;
DR  UNIPROT: Q8BRH1;
DR  Pfam: PF00013;
DR  Pfam: PF00076;
DR  PROSITE: PS50084;
DR  PROSITE: PS50102;
DE  Function: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6- methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells (By similarity). Binds to the oncofetal H19 transcript and regulates its localization (By similarity). Binds to and stabilizes BTRC/FBW1A mRNA (By similarity). Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2 (By similarity). During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts (By similarity). Interacts with GAP43 transcript and transports it to axons. Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. Binding to MYC mRNA is enhanced by m6A- modification of the CRD (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA. Binds to the neuron-specific TAU mRNA and regulates its localization. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons. During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing. {ECO:0000250, ECO:0000250|UniProtKB:Q9NZI8, ECO:0000269|PubMed:15355996, ECO:0000269|PubMed:17264115, ECO:0000269|PubMed:21964071, ECO:0000269|PubMed:22465430}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8CJG0; IntAct: EBI-9030750; Score: 0.35
DE  Interaction: A2AG06; IntAct: EBI-11664104; Score: 0.35
DE  Interaction: Q9P2S5; IntAct: EBI-11694751; Score: 0.35
DE  Interaction: Q8K3Y3; IntAct: EBI-15801841; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0070937;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0030175;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:1990247;
GO  GO:0045182;
GO  GO:0070934;
GO  GO:0140059;
GO  GO:0051028;
GO  GO:1900152;
GO  GO:0017148;
GO  GO:0007399;
GO  GO:0097150;
GO  GO:0022013;
GO  GO:2000767;
GO  GO:0010468;
GO  GO:0010610;
GO  GO:0051252;
GO  GO:0006403;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRS
SQ  RKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIT
SQ  QGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQPVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAA
SQ  EKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTL
SQ  YNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFM
SQ  QAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVVITGPPEAQFKAQGRIYGKLKEENFF
SQ  GPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQV
SQ  KQQHQKGQSNLAQARRK
//
ID  Q8CGX0;
PN  Insulin-like growth factor 2 mRNA-binding protein 1;
GN  Igf2bp1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9NZI8}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9NZI8}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, dendrite. Cell projection, dendritic spine. Cell projection, growth cone {ECO:0000250}. Cell projection, filopodium. Cell projection, axon. Note=In the nucleus, located in discrete foci, coinciding with the sites of ACTB transcription (By similarity). In the cytoplasm, localizes in cytoplasmic mRNP granules. Colocalizes with microtubules in growth cone filopodia and along neurites in neuronal cells (By similarity). Cytoplasmic colocalization with ACTB mRNA is partially lost at the cell periphery, suggesting release of the transcript (By similarity). In cultured hippocampal neurons, predominantly located within dendrites, particularly at dendritic branching points in young cells, compared to axons. In axons, predominantly found in axonal branches and their growth cones. In dendrites, can exhibit different types of movements, from fast retrograde and anterograde movements to stable localization. Dendritic levels are regulated by neuronal activity and glutaminergic signals: they are increased by KCl-induced depolarization, which induces rapid efflux from the cell body into dendrites, and decreased by the NMDA receptor agonist AP-5. In motile cells, such as migrating fibroblasts, localizes to leading edges where it colocalizes with microtubules and microfilaments and to retracting tails (By similarity). In motile cells, transported towards the leading edge into the cortical region of the lamellipodia where it is connected to microfilaments (By similarity). In response to cellular stress, such as oxidative stress or heat shock, recruited to stress granules, but not to processing bodies (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8CGX0;
DR  UNIPROT: B1WBP3;
DR  Pfam: PF00013;
DR  Pfam: PF00076;
DR  PROSITE: PS50084;
DR  PROSITE: PS50102;
DE  Function: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6- methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of beta-actin/ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells (By similarity). Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localization (By similarity). Binds to and stabilizes BTRC/FBW1A mRNA (By similarity). Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2 (By similarity). During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD (By similarity). Binding to MYC mRNA is enhanced by m6A-modification of the CRD (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Interacts with GAP43 transcript and transports it to axons. Regulates localized ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co- transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'- UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons. {ECO:0000250|UniProtKB:Q9NZI8, ECO:0000269|PubMed:12716932, ECO:0000269|PubMed:14614102, ECO:0000269|PubMed:21471362, ECO:0000269|PubMed:21964071}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0070937;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0030175;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0003730;
GO  GO:0048027;
GO  GO:0003729;
GO  GO:1990247;
GO  GO:0045182;
GO  GO:0070934;
GO  GO:0140059;
GO  GO:0051028;
GO  GO:1900152;
GO  GO:0017148;
GO  GO:0007399;
GO  GO:0097150;
GO  GO:0022013;
GO  GO:2000767;
GO  GO:0010468;
GO  GO:0010610;
GO  GO:0051252;
GO  GO:0006403;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRS
SQ  RKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIA
SQ  QGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQQVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAA
SQ  EKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTL
SQ  YNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYGSFM
SQ  QAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVVITGPPEAQFKAQGRIYGKLKEENFF
SQ  GPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQV
SQ  KQQHQKGQSNQAQARRK
//
ID  O61955;
PN  Eukaryotic translation initiation factor 4E-3;
GN  ife;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic granule {ECO:0000269|PubMed:31147388}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Note=Localizes to cytoplasmic granules in early embryos (PubMed:31147388). Localizes to puncta in the perinuclear region in the germline syncytium (PubMed:31216475, PubMed:31147388). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
DR  UNIPROT: O61955;
DR  UNIPROT: Q8MNX5;
DR  UNIPROT: Q95X31;
DR  PDB: 5ABX;
DR  PDB: 5ABY;
DR  Pfam: PF01652;
DR  PROSITE: PS00813;
DE  Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps. Ife-3 is essential for viability. Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI- interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Within the pid-1 variant of the PETISCO complex binds to capped 21U-RNA precursor molecules, possibly playing a role in the processing of the 5' end of the molecules to promote binding of other complex components such as pid-3 (PubMed:31147388). However, it is not essential for the biogenesis of 21U-RNAs by itself (PubMed:31147388). Within the tost-1 variant of the PETISCO complex binds to splice leader SL1 RNA fragments to possibly play a role in their processing (PubMed:31147388). {ECO:0000269|PubMed:10744754, ECO:0000269|PubMed:12422237, ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:9553113, ECO:0000305|PubMed:31216475}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9XW13; IntAct: EBI-2411755; Score: 0.62
DE  Interaction: Q20898; IntAct: EBI-2411740; Score: 0.62
DE  Interaction: Q22497; IntAct: EBI-2411744; Score: 0.62
DE  Interaction: Q09293; IntAct: EBI-21449250; Score: 0.52
DE  Interaction: Q1ZXS5; IntAct: EBI-6457351; Score: 0.37
DE  Interaction: G5EDU4; IntAct: EBI-6458345; Score: 0.37
DE  Interaction: Q19541; IntAct: EBI-21448974; Score: 0.46
DE  Interaction: O76616; IntAct: EBI-21449031; Score: 0.35
DE  Interaction: Q20057; IntAct: EBI-21449069; Score: 0.35
DE  Interaction: Q9N405; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: G5EC16; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: O01871; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: G5ED26; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: O45551; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: Q18603; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: Q94279; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: Q18244; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: Q21323; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: P48166; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: Q18490; IntAct: EBI-21449322; Score: 0.35
DE  Interaction: Q22624; IntAct: EBI-21449322; Score: 0.35
GO  GO:0016281;
GO  GO:0048471;
GO  GO:0034518;
GO  GO:0070992;
GO  GO:0000340;
GO  GO:0003743;
GO  GO:0034585;
GO  GO:0009792;
GO  GO:0031047;
GO  GO:0006413;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTSVAENKALSASGDVNASDASVPPELLTRHPLQNRWALWYLKADRNKEWEDCLKMVSLFDTVEDFWSLYNHIQSAGGL
SQ  NWGSDYYLFKEGIKPMWEDVNNVQGGRWLVVVDKQKLQRRTQLLDHYWLELLMAIVGEQFDEYGDYICGAVVNVRQKGDK
SQ  VSLWTRDATRDDVNLRIGQVLKQKLSIPDTEILRYEVHKDSSARTSSTVKPRICLPAKDPAPVKEKGPAATTSPSNPGTE
SQ  ATGTSPATPTP
//
ID  Q10475;
PN  Eukaryotic translation initiation factor 4 gamma;
GN  tif471;
OS  284812;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12581158}. Note=Localized to the perinuclear region, the growing tips and septum.
DR  UNIPROT: Q10475;
DR  UNIPROT: P78832;
DR  Pfam: PF12152;
DR  Pfam: PF02854;
DE  Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. {ECO:0000269|PubMed:12581158}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UUB7; IntAct: EBI-2477389; Score: 0.35
DE  Interaction: Q9USV1; IntAct: EBI-2478191; Score: 0.35
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0016281;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0005198;
GO  GO:0003743;
GO  GO:0002183;
GO  GO:0042273;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSKPPSNTPKFSYARALASSQSNKSNSTKASENNTATAEKQAVKPSGVEPTNTSRANAQKKTESTGKITSEADTEKYNS
SQ  SKSPVNKEGSVEKKSSEKSSTNNKPWRGDNTSKPSANSSAERTSSQHQKPETSSQIGKDNAAPVENVNEKSTSQETAPPV
SQ  STVPIQFGSITRNAAIPSKPKVSGNMQNKSGVSSYSSKSQSVNSSVTSNPPHTEEPVAAKPEASSTATKGPRPTTSASNT
SQ  NTSPANGAPTNKPSTDINTTDPATQTTQVSASNSPALSGSSTPSNTSSRSNRQNHGNFSEKRHYDRYGNSHPSYNKYSHY
SQ  QHGFNYNNSGNNRNESGHPRFRNSRRNYNNQGAYPTYMSNGRSANQSPRNNPQNVNNGSTPIQIPVSLQTPYGQVYGQPQ
SQ  YIVDPNMVQYGPILQPGYVPQYYPVYHQTPYTQNFPNMSRSGSQVSDQVVESPNSSTLSPRNGFAPIVKQQKKSSALKIV
SQ  NPVTHTEVVVPQKNASSPNPSETNSRAETPTAAPPQISEEEASQRKDAIKLAIQQRIQEKAEAEAKRKAEEKARLEAEEN
SQ  AKREAEEQAKREAEEKAKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEK
SQ  AKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEENAKREAEEKVKRETEENAKRKAEEEGKREADKNPEIKSSAP
SQ  LASSEANVDTSKQTNATEPEVVDKTKVEKLKASEGKSTSSLSSPSHSTSSKRDLLSGLESLSLKTNPKSEQCLESLLNSQ
SQ  FITDFSALVYPSTIKPPSTEEALKAGKYEYDVPFLLQFQSVYTDKPMKGWDERMKETVASAFSDKSSRGMYSSSRQSSRS
SQ  GSNTHSHAGPGFGGPSERKGISRLGIDRGFSSSGAGFGSGSNYKSAPSRGVSHHGHGGMSGSHRGSQRGSRRGGGERDKP
SQ  DPSSLTIPVDQVAPLQLSANRWQPKKLTEKPAETKGEDEEALLPPEVVQRKVKGSLNKMTLEKFDKISDQILEIAMQSRK
SQ  ENDGRTLKQVIQLTFEKATDEPNFSNMYARFARKMMDSIDDSIRDEGVLDKNNQPVRGGLLFRKYLLSRCQEDFERGWKA
SQ  NLPSGKAGEAEIMSDEYYVAAAIKRRGLGLVRFIGELFKLSMLSEKIMHECIKRLLGNVTDPEEEEIESLCRLLMTVGVN
SQ  IDATEKGHAAMDVYVLRMETITKIPNLPSRIKFMLMDVMDSRKNGWAVKNEVEKGPKTIAEIHEEAERKKALAESQRPSS
SQ  GRMHGRDMNRGDSRMGGRGSNPPFSSSDWSNNKDGYARLGQGIRGLKSGTQGSHGPTSLSSMLKGGSVSRTPSRQNSALR
SQ  REQSVRAPPSNVAVTSANSFELLEEHDHDNDGGQKDSNSKTSS
//
ID  Q1JPH6;
PN  Eukaryotic translation initiation factor 4H;
GN  EIF4H;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q1JPH6;
DR  UNIPROT: A5D959;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0043024;
GO  GO:0033592;
GO  GO:0034057;
GO  GO:0003743;
GO  GO:0097010;
GO  GO:0001731;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDK
SQ  FKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGFRDDFLGGRGGSRPGDRRTGPPM
SQ  GSRFRDGPPLRGPNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVHKEQE
//
ID  Q15056;
PN  Eukaryotic translation initiation factor 4H;
GN  EIF4H;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q15056;
DR  UNIPROT: A8K3R1;
DR  UNIPROT: D3DXF6;
DR  UNIPROT: D3DXF8;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DR  OMIM: 603431;
DR  DisGeNET: 7458;
DE  Function: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA. {ECO:0000269|PubMed:10585411, ECO:0000269|PubMed:11418588}.
DE  Disease: Note=EIF4H is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of EIF4H may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. {ECO:0000269|PubMed:8812460}.
DE  Reference Proteome: Yes;
DE  Interaction: P0DTD1; IntAct: EBI-25491191; Score: 0.64
DE  Interaction: Q9H3H3; IntAct: EBI-756607; Score: 0.74
DE  Interaction: P23508; IntAct: EBI-1065071; Score: 0.00
DE  Interaction: O60739; IntAct: EBI-1065818; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1075879; Score: 0.00
DE  Interaction: Q6MZP7; IntAct: EBI-1389994; Score: 0.35
DE  Interaction: P60842; IntAct: EBI-2267802; Score: 0.54
DE  Interaction: A0A6L7H7R4; IntAct: EBI-2831788; Score: 0.00
DE  Interaction: A0A5P8YEZ8; IntAct: EBI-2867095; Score: 0.00
DE  Interaction: P10225; IntAct: EBI-6155523; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q8TBB1; IntAct: EBI-10235782; Score: 0.67
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: Q91W50; IntAct: EBI-11079890; Score: 0.35
DE  Interaction: Q9NRD5; IntAct: EBI-24336001; Score: 0.56
DE  Interaction: Q9NZD8; IntAct: EBI-24518067; Score: 0.56
DE  Interaction: Q96D03; IntAct: EBI-25265649; Score: 0.56
DE  Interaction: Q92796; IntAct: EBI-24436218; Score: 0.56
DE  Interaction: Q96EF6; IntAct: EBI-24559599; Score: 0.56
DE  Interaction: P62807; IntAct: EBI-25471348; Score: 0.27
DE  Interaction: P04156; IntAct: EBI-21014477; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-21237916; Score: 0.37
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q8TB24; IntAct: EBI-26518569; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: P36507; IntAct: EBI-28935019; Score: 0.35
DE  Interaction: Q5W0V3; IntAct: EBI-34574999; Score: 0.27
GO  GO:0005829;
GO  GO:0016281;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0045296;
GO  GO:0043024;
GO  GO:0003723;
GO  GO:0033592;
GO  GO:0034057;
GO  GO:0008135;
GO  GO:0003743;
GO  GO:0048589;
GO  GO:0097010;
GO  GO:0001731;
GO  GO:0006446;
GO  GO:0019953;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDK
SQ  FKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGSSRESRGGWDSRDDFNSGFRD
SQ  DFLGGRGGSRPGDRRTGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPRE
SQ  EVVQKEQE
//
ID  Q9WUK2;
PN  Eukaryotic translation initiation factor 4H;
GN  Eif4h;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region.
DR  UNIPROT: Q9WUK2;
DR  UNIPROT: Q9WUK3;
DR  PDB: 2DNG;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0043024;
GO  GO:0033592;
GO  GO:0034057;
GO  GO:0003743;
GO  GO:0048589;
GO  GO:0097010;
GO  GO:0001731;
GO  GO:0019953;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDK
SQ  FKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGGSRESRGGWDSRDDFNSGYRD
SQ  DFLGGRGGSRPGDRRAGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPRE
SQ  EVVQKEQE
//
ID  Q5RBR8;
PN  Eukaryotic translation initiation factor 4H;
GN  EIF4H;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q5RBR8;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0003743;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADFDTYDDRAYNSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDK
SQ  FKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGFRDDFLGGRGGSRPGDRRTGPAM
SQ  GSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE
//
ID  Q5XI72;
PN  Eukaryotic translation initiation factor 4H;
GN  Eif4h;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q5XI72;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UI08; IntAct: EBI-22238608; Score: 0.35
DE  Interaction: P27361; IntAct: EBI-22238588; Score: 0.35
DE  Interaction: P15498; IntAct: EBI-22241288; Score: 0.35
DE  Interaction: P07332; IntAct: EBI-22243434; Score: 0.35
DE  Interaction: P08069; IntAct: EBI-22245613; Score: 0.35
DE  Interaction: P18031; IntAct: EBI-22255654; Score: 0.35
DE  Interaction: Q96RT1; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: O75096; IntAct: EBI-22258804; Score: 0.35
GO  GO:0048471;
GO  GO:0043024;
GO  GO:0033592;
GO  GO:0034057;
GO  GO:0003743;
GO  GO:0048589;
GO  GO:0097010;
GO  GO:0001731;
GO  GO:0019953;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDK
SQ  FKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGGSREPRGGWDSRDDFSSGYRD
SQ  DFLGGRGGSRPGDRRAGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPRE
SQ  EVVQKEQE
//
ID  Q09121;
PN  Eukaryotic translation initiation factor 5A-1;
GN  EIF5A1;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q09121;
DR  UNIPROT: Q5ZLI6;
DR  Pfam: PF01287;
DR  PROSITE: PS00302;
DE  Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63241}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0003746;
GO  GO:0051028;
GO  GO:0045901;
GO  GO:0045905;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMD
SQ  VPNIKRCDFQLIGIQDGFLSLLQDSGEVREDLRLPEGELGREIEQKYDCGEEIITIHGARFTTS
//
ID  Q07460;
PN  Eukaryotic translation initiation factor 5A-2;
GN  EIF5A2;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions. {ECO:0000250}.
DR  UNIPROT: Q07460;
DR  Pfam: PF01287;
DR  PROSITE: PS00302;
DE  Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63241}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0003746;
GO  GO:0051028;
GO  GO:0045901;
GO  GO:0045905;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADELDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFNGKKYEDICPSTHNMD
SQ  VPNIKRNDYQLIGIQDGYLSLLTESGEVREDLKLPEGDLGKEIEGKFNANEDVQISVISAMNEECAVAIKPCK
//
ID  Q9GZV4;
PN  Eukaryotic translation initiation factor 5A-2;
GN  EIF5A2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions. {ECO:0000250}.
DR  UNIPROT: Q9GZV4;
DR  UNIPROT: B2R4V5;
DR  Pfam: PF01287;
DR  PROSITE: PS00302;
DR  OMIM: 605782;
DR  DisGeNET: 56648;
DE  Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63241, ECO:0000269|PubMed:14622290}.
DE  Reference Proteome: Yes;
DE  Interaction: Q96CV9; IntAct: EBI-6115969; Score: 0.35
DE  Interaction: P49366; IntAct: EBI-756238; Score: 0.78
DE  Interaction: P43146; IntAct: EBI-2678596; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: Q15771; IntAct: EBI-3924283; Score: 0.37
DE  Interaction: Q9UKA9; IntAct: EBI-3924886; Score: 0.37
DE  Interaction: P03496; IntAct: EBI-6158649; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-21327757; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: O00560; IntAct: EBI-10304015; Score: 0.72
DE  Interaction: Q04864; IntAct: EBI-10304037; Score: 0.56
DE  Interaction: Q9GZT8; IntAct: EBI-10304047; Score: 0.56
DE  Interaction: Q9UJX2; IntAct: EBI-10304057; Score: 0.56
DE  Interaction: Q9BU89; IntAct: EBI-21850571; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: Q9UQC2; IntAct: EBI-25384304; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0043231;
GO  GO:0005643;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0003746;
GO  GO:0051028;
GO  GO:0010509;
GO  GO:0045901;
GO  GO:0045905;
GO  GO:0015031;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMD
SQ  VPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK
//
ID  Q8BGY2;
PN  Eukaryotic translation initiation factor 5A-2;
GN  Eif5a2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions. {ECO:0000250}.
DR  UNIPROT: Q8BGY2;
DR  Pfam: PF01287;
DR  PROSITE: PS00302;
DE  Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63241}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0043231;
GO  GO:0005643;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0003746;
GO  GO:0051028;
GO  GO:0045901;
GO  GO:0045905;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMD
SQ  VPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK
//
ID  Q5R898;
PN  Eukaryotic translation initiation factor 5A-2;
GN  EIF5A2;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions. {ECO:0000250}.
DR  UNIPROT: Q5R898;
DR  Pfam: PF01287;
DR  PROSITE: PS00302;
DE  Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63241}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0003746;
GO  GO:0051028;
GO  GO:0045901;
GO  GO:0045905;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMD
SQ  VPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK
//
ID  Q6IS14;
PN  Eukaryotic translation initiation factor 5A-1-like;
GN  EIF5AL1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions. {ECO:0000250}.
DR  UNIPROT: Q6IS14;
DR  Pfam: PF01287;
DR  PROSITE: PS00302;
DR  DisGeNET: 143244;
DE  Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63241}.
DE  Reference Proteome: Yes;
DE  Interaction: P03496; IntAct: EBI-6158649; Score: 0.35
DE  Interaction: Q99963; IntAct: EBI-25376320; Score: 0.35
DE  Interaction: Q9UQC2; IntAct: EBI-25384304; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055452; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0003746;
GO  GO:0051028;
GO  GO:0045901;
GO  GO:0045905;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGWPCKIVEMSASKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMD
SQ  VPNIKRNDFQLIGIQDGYLSLLQDSGEVPEDLRLPEGDLGKEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK
//
ID  Q0D2I5;
PN  Non-homologous end joining factor IFFO1;
GN  IFFO1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:31548606}. Nucleus, nucleoplasm {ECO:0000269|PubMed:31548606}. Nucleus inner membrane {ECO:0000269|PubMed:31548606}. Nucleus matrix {ECO:0000269|PubMed:31548606}. Note=Mainly soluble, the remaining is localized in the nuclear matrix (PubMed:31548606). Localized at double- strand break (DSB) sites near the lamina and nuclear matrix structures (PubMed:31548606). {ECO:0000269|PubMed:31548606}.
DR  UNIPROT: Q0D2I5;
DR  UNIPROT: Q24JT6;
DR  UNIPROT: Q7L5J9;
DR  UNIPROT: Q7Z5X4;
DR  UNIPROT: Q9BQ46;
DR  PDB: 6ABO;
DR  PROSITE: PS51842;
DR  OMIM: 610495;
DR  DisGeNET: 25900;
DE  Function: Nuclear matrix protein involved in the immobilization of broken DNA ends and the suppression of chromosome translocation during DNA double-strand breaks (DSBs) (PubMed:31548606). Interacts with the nuclear lamina component LMNA, resulting in the formation of a nucleoskeleton that relocalizes to the DSB sites in a XRCC4-dependent manner and promotes the immobilization of the broken ends, thereby preventing chromosome translocation (PubMed:31548606). Acts as a scaffold that allows the DNA repair protein XRCC4 and LMNA to assemble into a complex at the DSB sites (PubMed:31548606). {ECO:0000269|PubMed:31548606}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-26498092; Score: 0.58
DE  Interaction: P0C6X4; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q13426; IntAct: EBI-753355; Score: 0.71
DE  Interaction: Q96D59; IntAct: EBI-756262; Score: 0.37
DE  Interaction: Q15027; IntAct: EBI-759763; Score: 0.37
DE  Interaction: Q9H6Z9; IntAct: EBI-12503146; Score: 0.35
DE  Interaction: Q99608; IntAct: EBI-21251050; Score: 0.37
DE  Interaction: A0JNW5; IntAct: EBI-11898643; Score: 0.00
DE  Interaction: Q86UE8; IntAct: EBI-11911984; Score: 0.00
DE  Interaction: Q53SF7; IntAct: EBI-11916115; Score: 0.00
DE  Interaction: Q6NT76; IntAct: EBI-11917716; Score: 0.00
DE  Interaction: Q8IY63; IntAct: EBI-11921623; Score: 0.00
DE  Interaction: Q8NEL9; IntAct: EBI-11922796; Score: 0.00
DE  Interaction: Q9BWV3; IntAct: EBI-11930488; Score: 0.00
DE  Interaction: Q9UN30; IntAct: EBI-11939244; Score: 0.00
DE  Interaction: Q96KS9; IntAct: EBI-21503766; Score: 0.35
DE  Interaction: O15460; IntAct: EBI-21563604; Score: 0.35
DE  Interaction: Q9NQX6; IntAct: EBI-21675860; Score: 0.35
DE  Interaction: P46779; IntAct: EBI-21676629; Score: 0.35
DE  Interaction: Q9UBP4; IntAct: EBI-21684976; Score: 0.35
DE  Interaction: Q6ZN55; IntAct: EBI-21720777; Score: 0.35
DE  Interaction: A8MT70; IntAct: EBI-21738250; Score: 0.35
DE  Interaction: Q9H1K0; IntAct: EBI-21777075; Score: 0.35
DE  Interaction: Q86XE0; IntAct: EBI-21777996; Score: 0.35
DE  Interaction: Q6XPS3; IntAct: EBI-21801323; Score: 0.35
DE  Interaction: Q9UP83; IntAct: EBI-21866024; Score: 0.35
DE  Interaction: Q9NPF7; IntAct: EBI-21882357; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9H9Q4; IntAct: EBI-26498051; Score: 0.35
DE  Interaction: P49917; IntAct: EBI-26564737; Score: 0.40
DE  Interaction: P78527; IntAct: EBI-26564743; Score: 0.40
DE  Interaction: P13010; IntAct: EBI-26564743; Score: 0.40
DE  Interaction: Q93009; IntAct: EBI-30842093; Score: 0.44
GO  GO:0005882;
GO  GO:0005637;
GO  GO:0016363;
GO  GO:0005654;
GO  GO:0035861;
GO  GO:1990683;
GO  GO:0006303;
GO  GO:1990166;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNPLFGPNLFLLQQEQQGLAGPLGDSLGGDHFAGGGDLPPAPLSPAGPAAYSPPGPGPAPPAAMALRNDLGSNINVLKTL
SQ  NLRFRCFLAKVHELERRNRLLEKQLQQALEEGKQGRRGLGRRDQAVQTGFVSPIRPLGLQLGARPAAVCSPSARVLGSPA
SQ  RSPAGPLAPSAASLSSSSTSTSTTYSSSARFMPGTIWSFSHARRLGPGLEPTLVQGPGLSWVHPDGVGVQIDTITPEIRA
SQ  LYNVLAKVKRERDEYKRRWEEEYTVRIQLQDRVNELQEEAQEADACQEELALKVEQLKAELVVFKGLMSNNLSELDTKIQ
SQ  EKAMKVDMDICRRIDITAKLCDVAQQRNCEDMIQMFQVPSMGGRKRERKAAVEEDTSLSESEGPRQPDGDEEESTALSIN
SQ  EEMQRMLNQLREYDFEDDCDSLTWEETEETLLLWEDFSGYAMAAAEAQGEQEDSLEKVIKDTESLFKTREKEYQETIDQI
SQ  ELELATAKNDMNRHLHEYMEMCSMKRGLDVQMETCRRLITQSGDRKSPAFTAVPLSDPPPPPSEAEDSDRDVSSDSSMR
//
ID  Q8BXL9;
PN  Non-homologous end joining factor IFFO1;
GN  Iffo1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q0D2I5}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q0D2I5}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q0D2I5}. Nucleus matrix {ECO:0000250|UniProtKB:Q0D2I5}. Note=Mainly soluble, the remaining is localized in the nuclear matrix. Localized at double-strand break (DSB) sites near the lamina and nuclear matrix structures. {ECO:0000250|UniProtKB:Q0D2I5}.
DR  UNIPROT: Q8BXL9;
DR  UNIPROT: Q3TQI1;
DR  UNIPROT: Q6PFE6;
DR  UNIPROT: Q8BXS3;
DR  UNIPROT: Q8C1D6;
DR  PROSITE: PS51842;
DE  Function: Nuclear matrix protein involved in the immobilization of broken DNA ends and the suppression of chromosome translocation during DNA double-strand breaks (DSBs) (PubMed:31548606). Interacts with the nuclear lamina component LMNA, resulting in the formation of a nucleoskeleton that will relocalize to the DSB sites in a XRCC4- dependent manner and promote the immobilization of the broken ends, thereby preventing chromosome translocation (PubMed:31548606). Acts as a scaffold that allows the DNA repair protein XRCC4 and LMNA to assemble into a complex at the DSB sites (PubMed:31548606). {ECO:0000269|PubMed:31548606}.
DE  Reference Proteome: Yes;
GO  GO:0005882;
GO  GO:0005637;
GO  GO:0016363;
GO  GO:0005654;
GO  GO:0035861;
GO  GO:1990683;
GO  GO:0006303;
GO  GO:1990166;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNPLFGPNLFLLQQEQQGLAGPLGDPLGGDHFAGGGDLASAPLASAGPSAYSPPGPGPAPPAAMALRNDLGSNINVLKTL
SQ  NLRFRCFLAKVHELERRNRLLEKQLQQALEEGKQGRRGLARRDQAVQTGFISPIRPLGLPLSSRPAAVCPPSARVLGSPS
SQ  RSPAGPLASSAACHTSSSTSTSTAFSSSTRFMPGTIWSFSHARRLGPGLEPTLVQGPGLSWVHPDGVGVQIDTITPEIRA
SQ  LYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLMSNNLTELDTKIQ
SQ  EKAMKVDMDICRRIDITAKLCDLAQQRNCEDMIQMFQKKLVPSMGGRKRERKAAVEEDTSLSESDGPRQPEGAEEESTAL
SQ  SINEEMQRMLSQLREYDFEDDCDSLTWEETEETLLLWEDFSGYAMAAAEAQGEQEDSLEKVIKDTESLFKTREKEYQETI
SQ  DQIELELATAKNDMNRHLHEYMEMCSMKRGLDVQMETCRRLITQSGDRKSPAFTAVPLSDPPPPPSETEDSDRDVSSDSS
SQ  MR
//
ID  P40305;
PN  Interferon alpha-inducible protein 27, mitochondrial;
GN  IFI27;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion membrane {ECO:0000269|PubMed:18330707, ECO:0000269|PubMed:27673746}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:11722583, ECO:0000269|PubMed:22427340}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22427340}; Multi-pass membrane protein {ECO:0000255}. Note=Exclusive localizations in either the nucleus or the mitochondrion have been reported. {ECO:0000269|PubMed:22427340, ECO:0000269|PubMed:27673746}.
DR  UNIPROT: P40305;
DR  UNIPROT: A0A087WZF8;
DR  UNIPROT: A8K0H0;
DR  UNIPROT: Q53YA6;
DR  UNIPROT: Q6IEC1;
DR  UNIPROT: Q7Z5R0;
DR  UNIPROT: Q7Z5R1;
DR  UNIPROT: Q7Z5R2;
DR  UNIPROT: Q96BK3;
DR  UNIPROT: Q9H4B1;
DR  Pfam: PF06140;
DR  OMIM: 600009;
DR  DisGeNET: 3429;
DE  Function: Probable adapter protein involved in different biological processes (PubMed:22427340, PubMed:27194766). Part of the signaling pathways that lead to apoptosis (PubMed:18330707, PubMed:27673746, PubMed:24970806). Involved in type-I interferon-induced apoptosis characterized by a rapid and robust release of cytochrome C from the mitochondria and activation of BAX and caspases 2, 3, 6, 8 and 9 (PubMed:18330707, PubMed:27673746). Also functions in TNFSF10-induced apoptosis (PubMed:24970806). May also have a function in the nucleus, where it may be involved in the interferon-induced negative regulation of the transcriptional activity of NR4A1, NR4A2 and NR4A3 through the enhancement of XPO1-mediated nuclear export of these nuclear receptors (PubMed:22427340). May thereby play a role in the vascular response to injury (By similarity). In the innate immune response, has an antiviral activity towards hepatitis C virus/HCV (PubMed:27194766, PubMed:27777077). May prevent the replication of the virus by recruiting both the hepatitis C virus non-structural protein 5A/NS5A and the ubiquitination machinery via SKP2, promoting the ubiquitin- mediated proteasomal degradation of NS5A (PubMed:27194766, PubMed:27777077). {ECO:0000250|UniProtKB:Q8R412, ECO:0000269|PubMed:18330707, ECO:0000269|PubMed:22427340, ECO:0000269|PubMed:24970806, ECO:0000269|PubMed:27194766, ECO:0000269|PubMed:27673746, ECO:0000269|PubMed:27777077}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-27124576; Score: 0.40
DE  Interaction: Q5NGF6; IntAct: EBI-2805959; Score: 0.00
DE  Interaction: Q81KT8; IntAct: EBI-2831742; Score: 0.00
DE  Interaction: A0A6H3ABE4; IntAct: EBI-2831749; Score: 0.00
DE  Interaction: A0A6L7HHX2; IntAct: EBI-2831761; Score: 0.00
DE  Interaction: A0A6L7HB40; IntAct: EBI-2831768; Score: 0.00
DE  Interaction: Q8ZCW0; IntAct: EBI-2847220; Score: 0.00
DE  Interaction: A0A5P8YAW1; IntAct: EBI-2867067; Score: 0.00
DE  Interaction: A0A380PNP6; IntAct: EBI-2867060; Score: 0.00
DE  Interaction: P17778; IntAct: EBI-2867046; Score: 0.00
DE  Interaction: A0A3N4BEU0; IntAct: EBI-2867053; Score: 0.00
DE  Interaction: Q8ZG09; IntAct: EBI-2867074; Score: 0.00
DE  Interaction: Q8ZHF1; IntAct: EBI-2867081; Score: 0.00
DE  Interaction: P05549; IntAct: EBI-9679979; Score: 0.37
DE  Interaction: Q92754; IntAct: EBI-9680053; Score: 0.37
DE  Interaction: P55056; IntAct: EBI-24754759; Score: 0.56
DE  Interaction: P22736; IntAct: EBI-27124261; Score: 0.61
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0061629;
GO  GO:0006915;
GO  GO:0097190;
GO  GO:0051607;
GO  GO:0097191;
GO  GO:0045087;
GO  GO:0044827;
GO  GO:0000122;
GO  GO:0043161;
GO  GO:0070936;
GO  GO:0046825;
GO  GO:0060337;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEASALTSSAVTSVAKVVRVASGSAVVLPLARIATVVIGGVVAMAAVPMVLSAMGFTAAGIASSSIAAKMMSAAAIANGG
SQ  GVASGSLVATLQSLGATGLSGLTKFILGSIGSAIAAVIARFY
//
ID  Q01628;
PN  Interferon-induced transmembrane protein 3;
GN  IFITM3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:22511783, ECO:0000269|PubMed:26354436}; Single-pass type II membrane protein {ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:22511783}. Late endosome membrane {ECO:0000269|PubMed:22046135}; Single-pass type II membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000269|PubMed:26354436, ECO:0000269|PubMed:33270927}; Single-pass type II membrane protein. Lysosome membrane {ECO:0000269|PubMed:22046135, ECO:0000269|PubMed:26354436, ECO:0000269|PubMed:33270927}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:30983867}. Note=Co-localizes with BRI3 isoform 1 at the perinuclear region. {ECO:0000269|PubMed:30983867}.
DR  UNIPROT: Q01628;
DR  UNIPROT: Q53Y76;
DR  UNIPROT: Q96HK8;
DR  UNIPROT: Q96J15;
DR  Pfam: PF04505;
DR  OMIM: 605579;
DR  OMIM: 614680;
DR  DisGeNET: 10410;
DE  Function: IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) (PubMed:26354436, PubMed:33270927, PubMed:33239446). Can inhibit: influenza virus hemagglutinin protein- mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS- CoV and SARS-CoV-2 S protein-mediated viral entry and VSV G protein- mediated viral entry (PubMed:33270927). Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation (PubMed:26354436). IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome (PubMed:26354436). Exerts opposing activities on SARS-CoV-2, including amphipathicity-dependent restriction of virus at endosomes and amphipathicity-independent enhancement of infection at the plasma membrane (PubMed:33270927). {ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20534863, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22046135, ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:23601107, ECO:0000269|PubMed:26354436, ECO:0000269|PubMed:33239446, ECO:0000269|PubMed:33270927}.
DE  Reference Proteome: Yes;
DE  Interaction: O95415; IntAct: EBI-25503997; Score: 0.54
DE  Interaction: P43490; IntAct: EBI-7932891; Score: 0.51
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06927; IntAct: EBI-11724813; Score: 0.35
DE  Interaction: P35372; IntAct: EBI-24521211; Score: 0.56
DE  Interaction: P43628; IntAct: EBI-24670376; Score: 0.56
DE  Interaction: O60669; IntAct: EBI-23704678; Score: 0.56
DE  Interaction: O95870; IntAct: EBI-24691282; Score: 0.56
DE  Interaction: O95470; IntAct: EBI-24700847; Score: 0.56
DE  Interaction: Q9NXB9; IntAct: EBI-24702045; Score: 0.56
DE  Interaction: Q9Y680; IntAct: EBI-24738925; Score: 0.56
DE  Interaction: Q9NZD1; IntAct: EBI-24748139; Score: 0.56
DE  Interaction: Q9Y282; IntAct: EBI-24756591; Score: 0.56
DE  Interaction: Q6UWN5; IntAct: EBI-24779968; Score: 0.56
DE  Interaction: P60201; IntAct: EBI-24783936; Score: 0.56
DE  Interaction: O15552; IntAct: EBI-24797538; Score: 0.56
DE  Interaction: Q96KR6; IntAct: EBI-25276379; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-25280796; Score: 0.56
DE  Interaction: Q8N661; IntAct: EBI-25282350; Score: 0.56
DE  Interaction: Q14973; IntAct: EBI-24642589; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-24792170; Score: 0.56
DE  Interaction: Q96HJ5; IntAct: EBI-24801917; Score: 0.56
DE  Interaction: P19397; IntAct: EBI-24808633; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24811070; Score: 0.56
DE  Interaction: Q12908; IntAct: EBI-25269791; Score: 0.56
DE  Interaction: Q9H6H4; IntAct: EBI-25272718; Score: 0.56
DE  Interaction: O15354; IntAct: EBI-20808121; Score: 0.37
DE  Interaction: P25105; IntAct: EBI-20811134; Score: 0.37
DE  Interaction: O43490; IntAct: EBI-21451704; Score: 0.37
GO  GO:0031901;
GO  GO:0016021;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0051607;
GO  GO:0006955;
GO  GO:0046597;
GO  GO:0045071;
GO  GO:0032897;
GO  GO:0035455;
GO  GO:0035456;
GO  GO:0034341;
GO  GO:0009615;
GO  GO:0060337;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNHTVQTFFSPVNSGQPPNYEMLKEEHEVAVLGAPHNPAPPTSTVIHIRSETSVPDHVVWSLFNTLFMNPCCLGFIAFAY
SQ  SVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTILLIVIPVLIFQAYG
//
ID  Q9CQW9;
PN  Interferon-induced transmembrane protein 3;
GN  Ifitm3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q01628}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01628}. Late endosome membrane {ECO:0000269|PubMed:33270927}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01628}. Early endosome membrane {ECO:0000269|PubMed:33270927}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01628}. Lysosome membrane {ECO:0000269|PubMed:33270927}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01628}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q01628}. Note=Co-localizes with BRI3 isoform 1 at the perinuclear region. {ECO:0000250|UniProtKB:Q01628}.
DR  UNIPROT: Q9CQW9;
DR  UNIPROT: Q9D8L6;
DR  Pfam: PF04505;
DE  Function: IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) (PubMed:33270927). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-2 S protein- mediated viral entry and VSV G protein-mediated viral entry (PubMed:33270927). Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v- ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation. IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome. Exerts opposing activities on SARS- CoV-2, including amphipathicity-dependent restriction of virus at endosomes and amphipathicity-independent enhancement of infection at the plasma membrane. {ECO:0000269|PubMed:12124616, ECO:0000269|PubMed:18505827, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22467717, ECO:0000269|PubMed:33270927}.
DE  Reference Proteome: Yes;
GO  GO:0045177;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0031901;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0051607;
GO  GO:0008285;
GO  GO:0046597;
GO  GO:0045071;
GO  GO:0006898;
GO  GO:0035455;
GO  GO:0035456;
GO  GO:0034341;
GO  GO:0009615;
GO  GO:0060337;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNHTSQAFITAASGGQPPNYERIKEEYEVAEMGAPHGSASVRTTVINMPREVSVPDHVVWSLFNTLFMNFCCLGFIAYAY
SQ  SVKSRDRKMVGDVTGAQAYASTAKCLNISTLVLSILMVVITIVSVIIIVLNAQNLHT
//
ID  P26376;
PN  Interferon-induced transmembrane protein 3;
GN  ifitm3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q01628}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01628}. Late endosome membrane {ECO:0000250|UniProtKB:Q01628}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01628}. Early endosome membrane {ECO:0000250|UniProtKB:Q01628}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01628}. Lysosome membrane {ECO:0000250|UniProtKB:Q01628}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q01628}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q01628}. Note=Co-localizes with BRI3 isoform 1 at the perinuclear region. {ECO:0000250|UniProtKB:Q01628}.
DR  UNIPROT: P26376;
DR  UNIPROT: B5DER6;
DR  Pfam: PF04505;
DE  Function: IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses. Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. {ECO:0000250|UniProtKB:Q01628, ECO:0000250|UniProtKB:Q9CQW9}.
DE  Reference Proteome: Yes;
DE  Interaction: P15127; IntAct: EBI-21297848; Score: 0.35
GO  GO:0031901;
GO  GO:0016021;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0051607;
GO  GO:0046597;
GO  GO:0045071;
GO  GO:0035455;
GO  GO:0035456;
GO  GO:0034341;
GO  GO:0060337;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNHTSQAFVNAATGGQPPNYERIKEEYEVSELGAPHGSASVRTTVINMPREVSVPDHVVWSLFNTLFMNFCCLGFIAYAY
SQ  SVKSRDRKMVGDMTGAQAYASTAKCLNISSLVLSILMVIITIVTVVIIALNAPRLQT
//
ID  Q9QZ85;
PN  Interferon-inducible GTPase 1;
GN  Iigp1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Parasitophorous vacuole membrane. Note=Localizes to the bacterial inclusions formed following C.trachomatis infection. Accumulates in a GTP-bound form on the parasitophorous vacuole membranes formed following T.gondii infection but exists in a GDP-bound form in uninfected cells.
DR  UNIPROT: Q9QZ85;
DR  UNIPROT: Q9Z1M3;
DR  PDB: 1TPZ;
DR  PDB: 1TQ2;
DR  PDB: 1TQ4;
DR  PDB: 1TQ6;
DR  PDB: 1TQD;
DR  PDB: 4LV5;
DR  PDB: 4LV8;
DR  PDB: 5FPH;
DR  Pfam: PF05049;
DR  PROSITE: PS51716;
DE  Function: GTPase with low activity. Has higher affinity for GDP than for GTP. Plays a role in resistance to intracellular pathogens. Required for disruption of the parasitophorous vacuole formed following T.gondii infection and subsequent killing of the parasite. Mediates resistance to C.trachomatis infection by targeting bacterial inclusions to autophagosomes for subsequent lysosomal destruction. {ECO:0000269|PubMed:11907101, ECO:0000269|PubMed:12732635, ECO:0000269|PubMed:16304607, ECO:0000269|PubMed:19242543}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6P542; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: A1E140; IntAct: EBI-15902276; Score: 0.54
DE  Interaction: Q9QZ85; IntAct: EBI-15902301; Score: 0.54
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0032580;
GO  GO:0031965;
GO  GO:0020005;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
GO  GO:0035458;
GO  GO:0019221;
GO  GO:0006952;
GO  GO:0050829;
GO  GO:0042832;
GO  GO:0045087;
GO  GO:0010506;
GO  GO:0009617;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MGQLFSSPKSDENNDLPSSFTGYFKKFNTGRKIISQEILNLIELRMRKGNIQLTNSAISDALKEIDSSVLNVAVTGETGS
SQ  GKSSFINTLRGIGNEEEGAAKTGVVEVTMERHPYKHPNIPNVVFWDLPGIGSTNFPPNTYLEKMKFYEYDFFIIISATRF
SQ  KKNDIDIAKAISMMKKEFYFVRTKVDSDITNEADGKPQTFDKEKVLQDIRLNCVNTFRENGIAEPPIFLLSNKNVCHYDF
SQ  PVLMDKLISDLPIYKRHNFMVSLPNITDSVIEKKRQFLKQRIWLEGFAADLVNIIPSLTFLLDSDLETLKKSMKFYRTVF
SQ  GVDETSLQRLARDWEIEVDQVEAMIKSPAVFKPTDEETIQERLSRYIQEFCLANGYLLPKNSFLKEIFYLKYYFLDMVTE
SQ  DAKTLLKEICLRN
//
ID  O13681;
PN  Integral inner nuclear membrane protein ima1;
GN  IMA1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:18692466}; Multi-pass membrane protein {ECO:0000269|PubMed:18692466}.
DR  UNIPROT: O13681;
DR  Pfam: PF09779;
DE  Function: Inner nuclear membrane protein that specifically binds to heterochromatic regions and promotes the tethering of centromeric DNA to the SUN-KASH complex. Couples centromeres to the nuclear envelope, thus contributing to their association with the microtubule organizing center attachment site and to the positioning of the nucleus at the cell center by microtubules. {ECO:0000269|PubMed:18692466}.
DE  Reference Proteome: Yes;
GO  GO:0034506;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0034992;
GO  GO:0044732;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0071765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESSRLFTLGLGNSDDGLKSTFGDKTVTCFYCNKKKEKIRDGTSTWTCSICEATNHIDEKGDILDYRPPTPTQDKGVGPF
SQ  YAIRDFPSSSSFQSPFCEKCQMNQLIVNRMLADYLPDSSHPDYQAYEKALPEYKKSIEEKFPIVCSECYDSVQDQLDAND
SQ  YEAKNQVLGYWLQKSKEQLNAKVPHHYPKASFVLWLLRGFGFSFFYLQSIVWHLYHSMIISLLPDGIRNLFLKAISYFLL
SQ  DGSSSKIFYFNWLGFFVVFWNPYWYKMMDNPSWELFGRDQYIQCQALYLIIRLTCLYLLSCYESEILNLSSDTNLESDFL
SQ  LRQIHAAFFFVTICFTWISISCLKPSPPPEVHLTGEILKPRKKRQESTSSVHRIGKESSDRKDGISGQNKLQQFATISIL
SQ  NNTNATSHLGNQSVRERAPEESPMTFLQKKMAALPTSSPVRPMLKPTLQLQNSPLSKLVPQEVGNKVNDSIHTTSNQPSK
SQ  FSLNPSISLKGDNVIEKNLPFSVSTLKSTAKKDTGKAGDGQNREIQNEPVSLESHFSKSLALQNDPTEVIQVKNVLHRNR
SQ  RNAKLLIAFTILFLVGLICGWRLNRFTMFIYYLCILVLATYYVMKHNFYPLRKVA
//
ID  Q557F4;
PN  Probable importin subunit alpha-A;
GN  DDB_G0273595;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q557F4;
DR  UNIPROT: Q869V5;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Functions in nuclear protein import via a substrate-importin alpha-beta transport complex that passes though the nuclear pore complexes (NPC). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSRDKQDSRKKEFKKSLDSETARRKREENSIGIRKNAREELMLKRRGIVQPNPSTSYQIIVPPEVQEQFQKYENETMEN
SQ  KIKNLPGLVTALNSNDQAYVYSSLVQFRKLLSIHAYPPIDQVIECGIIPKLNQLLQCNNPKVQFESAWALTNIASGNNRQ
SQ  TQTVMESGSVPIFIQLLCAETTDEVKEQCAWALGNIAGDTVDSRNYLLKYGAMNALIPLLHYGEDNGATTTSANSERKIG
SQ  LIQNVVWTISNLCRGKPQPDFSVVSQCLPAINELIRIENLPSEIYGDLCWALSYLCDGPNTKIQAVIDSGVVPRLVKLLE
SQ  YPDSIVFTPALRAVGNIVTGESSQTQIVIDNNGVELITRLLAVQKKSIRKESCWALSNITAGEPSQIDVVVSNPKTVTTL
SQ  ISLLSHSEHDIKREACWALSNSTNNSSTKSIQTLVRHNILKHFIDLLNSQDLVILKIVLEGLINIIKEGEKTKTKTGVNP
SQ  YVNLISEMQGESIIYDLQEHQSKDVYKKAFELIEFFESSDYSDSENSEPNINQNGQYEFSSNYNSNSINI
//
ID  Q71VM4;
PN  Importin subunit alpha-1a;
GN  Os01g0253300;
OS  39947;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9727027}.
DR  UNIPROT: Q71VM4;
DR  UNIPROT: O82783;
DR  PDB: 2YNS;
DR  PDB: 4B8J;
DR  PDB: 4B8O;
DR  PDB: 4B8P;
DR  PDB: 4BPL;
DR  PDB: 4BQK;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Functions in nuclear protein import. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. {ECO:0000269|PubMed:11124253, ECO:0000269|PubMed:9727027}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8S7W1; IntAct: EBI-628940; Score: 0.37
DE  Interaction: Q3HM11; IntAct: EBI-8014436; Score: 0.44
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLRPSERVEVRRNRYKVAVDAEEGRRRREDNMVEIRKSRREESLLKKRREGLQAQAPVPASAATGVDKKLESLPAMIGG
SQ  VYSDDNNLQLEATTQFRKLLSIERSPPIEEVIQSGVVPRFVQFLTREDFPQLQFEAAWALTNIASGTSENTKVVIDHGAV
SQ  PIFVKLLGSSSDDVREQAVWALGNVAGDSPKCRDLVLANGALLPLLAQLNEHTKLSMLRNATWTLSNFCRGKPQPSFEQT
SQ  RPALPALARLIHSNDEEVLTDACWALSYLSDGTNDKIQAVIEAGVCPRLVELLLHPSPSVLIPALRTVGNIVTGDDAQTQ
SQ  CIIDHQALPCLLSLLTQNLKKSIKKEACWTISNITAGNKDQIQAVINAGIIGPLVNLLQTAEFDIKKEAAWAISNATSGG
SQ  SHDQIKYLVSEGCIKPLCDLLICPDIRIVTVCLEGLENILKVGETDKTLAAGDVNVFSQMIDEAEGLEKIENLQSHDNNE
SQ  IYEKAVKILEAYWMDEEDDTMGATTVAAPQGATFDFGQGGGAAQFK
//
ID  Q9SLX0;
PN  Importin subunit alpha-1b;
GN  Os05g0155601;
OS  39947;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11124253}.
DR  UNIPROT: Q9SLX0;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Functions in nuclear protein import. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. In conjunction with importin beta-1, mediates the nuclear envelope docking, and the subsequent translocation into the nucleus of the constitutive morphogenetic 1 (COP1) protein containing bipartite NLS motif. {ECO:0000269|PubMed:11124253}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLRPSERAEVRRSRYKVAVDADEGRRRREDNMVEIRKSRREESLLKKRRDGLPAAAAAAAAASPLLAHSSALQQKLEGL
SQ  PAMVQAVQSDDSAVQLEATTQFRKLLSIERSPPIEEVINTGVVPRFIAFLQREDYPQLQFEAAWALTNIASGTSDNTKVV
SQ  VESGAVPIFVKLLSSPSEDVREQAVWALGNVAGDSPKCRDLVLASGGLYPLLQQLNEHAKLSMLRNATWTLSNFCRGKPQ
SQ  PNFEQVKPALSALQRLIHSQDEEVLTDACWALSYLSDGTNDKIQAVIESGVFPRLVELLMHPSASVLIPALRTVGNIVTG
SQ  DDMQTQCVIDHQALPCLLNLLTNNHKKSIKKEACWTISNITAGNREQIQAVINANIIAPLVHLLQTAEFDIKKEAAWAIS
SQ  NATSGGTHDQIKYLVAQGCIKPLCDLLVCPDPRIVTVCLEGLENILKVGEAEKNLGAGDVNSYAQMIDDAEGLEKIENLQ
SQ  SHDNTEIYEKAVKMLESYWLEEEDDAMPSGDNAQNGFNFGNQQPNVPSGGFNFG
//
ID  Q02821;
PN  Importin subunit alpha;
GN  SRP1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Note=Mainly localized at the periphery of the nucleus.
DR  UNIPROT: Q02821;
DR  UNIPROT: D6W0Z8;
DR  PDB: 1BK5;
DR  PDB: 1BK6;
DR  PDB: 1EE4;
DR  PDB: 1EE5;
DR  PDB: 1UN0;
DR  PDB: 1WA5;
DR  PDB: 2C1T;
DR  PDB: 4PVZ;
DR  PDB: 4XZR;
DR  PDB: 5H2W;
DR  PDB: 5H2X;
DR  PDB: 5T94;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Functions in nuclear protein import as an adapter protein for importin beta nuclear receptors (PubMed:10913188). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (PubMed:10745017). Promotes docking of import substrates to the nuclear envelope (PubMed:8521485). Together with importin beta KAP95, mediates nuclear import of transcription factor GCN4 (PubMed:14648200). Together with tethering factor STS1, targets the proteasome to the nucleus (PubMed:10913188, PubMed:21075847). {ECO:0000269|PubMed:10745017, ECO:0000269|PubMed:10913188, ECO:0000269|PubMed:14648200, ECO:0000269|PubMed:21075847, ECO:0000269|PubMed:8521485}.
DE  Reference Proteome: Yes;
DE  Interaction: P20591; IntAct: EBI-11534426; Score: 0.56
DE  Interaction: P20676; IntAct: EBI-789997; Score: 0.69
DE  Interaction: P32499; IntAct: EBI-801825; Score: 0.78
DE  Interaction: P34160; IntAct: EBI-806268; Score: 0.69
DE  Interaction: P39705; IntAct: EBI-802293; Score: 0.69
DE  Interaction: P40069; IntAct: EBI-804491; Score: 0.53
DE  Interaction: P22768; IntAct: EBI-391461; Score: 0.37
DE  Interaction: P00812; IntAct: EBI-391464; Score: 0.37
DE  Interaction: P33317; IntAct: EBI-391467; Score: 0.37
DE  Interaction: Q12178; IntAct: EBI-391470; Score: 0.37
DE  Interaction: P28240; IntAct: EBI-391473; Score: 0.37
DE  Interaction: P06106; IntAct: EBI-391476; Score: 0.37
DE  Interaction: P53081; IntAct: EBI-391479; Score: 0.37
DE  Interaction: P19881; IntAct: EBI-391482; Score: 0.37
DE  Interaction: P36068; IntAct: EBI-391485; Score: 0.37
DE  Interaction: P35497; IntAct: EBI-391488; Score: 0.37
DE  Interaction: P41835; IntAct: EBI-391491; Score: 0.37
DE  Interaction: P34760; IntAct: EBI-391494; Score: 0.37
DE  Interaction: P47165; IntAct: EBI-391497; Score: 0.37
DE  Interaction: P38749; IntAct: EBI-391500; Score: 0.37
DE  Interaction: P43543; IntAct: EBI-391503; Score: 0.37
DE  Interaction: P53215; IntAct: EBI-391506; Score: 0.37
DE  Interaction: Q05016; IntAct: EBI-391509; Score: 0.37
DE  Interaction: P15108; IntAct: EBI-708957; Score: 0.56
DE  Interaction: Q06142; IntAct: EBI-784458; Score: 0.94
DE  Interaction: P46948; IntAct: EBI-789541; Score: 0.35
DE  Interaction: P38792; IntAct: EBI-791854; Score: 0.53
DE  Interaction: P32799; IntAct: EBI-792386; Score: 0.35
DE  Interaction: P53859; IntAct: EBI-792516; Score: 0.35
DE  Interaction: P27466; IntAct: EBI-793512; Score: 0.35
DE  Interaction: P36124; IntAct: EBI-794754; Score: 0.53
DE  Interaction: Q12149; IntAct: EBI-796196; Score: 0.67
DE  Interaction: Q02724; IntAct: EBI-797293; Score: 0.59
DE  Interaction: Q12124; IntAct: EBI-797390; Score: 0.35
DE  Interaction: Q08278; IntAct: EBI-799246; Score: 0.35
DE  Interaction: P53833; IntAct: EBI-799459; Score: 0.35
DE  Interaction: P13259; IntAct: EBI-799593; Score: 0.69
DE  Interaction: P53256; IntAct: EBI-800712; Score: 0.35
DE  Interaction: P53881; IntAct: EBI-800899; Score: 0.35
DE  Interaction: P50111; IntAct: EBI-803477; Score: 0.35
DE  Interaction: P22215; IntAct: EBI-804242; Score: 0.35
DE  Interaction: P53866; IntAct: EBI-804491; Score: 0.35
DE  Interaction: P32337; IntAct: EBI-804491; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-804491; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-804491; Score: 0.35
DE  Interaction: Q12449; IntAct: EBI-807743; Score: 0.35
DE  Interaction: Q08285; IntAct: EBI-808713; Score: 0.35
DE  Interaction: Q05636; IntAct: EBI-809094; Score: 0.35
DE  Interaction: Q08920; IntAct: EBI-810994; Score: 0.77
DE  Interaction: Q12464; IntAct: EBI-811656; Score: 0.53
DE  Interaction: P28003; IntAct: EBI-815383; Score: 0.27
DE  Interaction: Q06218; IntAct: EBI-817288; Score: 0.27
DE  Interaction: Q12277; IntAct: EBI-6963562; Score: 0.40
DE  Interaction: P25359; IntAct: EBI-6964469; Score: 0.56
DE  Interaction: Q05543; IntAct: EBI-6995482; Score: 0.56
DE  Interaction: Q12460; IntAct: EBI-7021190; Score: 0.40
DE  Interaction: P22579; IntAct: EBI-7021237; Score: 0.67
DE  Interaction: Q06697; IntAct: EBI-7044996; Score: 0.40
DE  Interaction: P53072; IntAct: EBI-7153795; Score: 0.40
DE  Interaction: Q05900; IntAct: EBI-7156793; Score: 0.40
DE  Interaction: P47108; IntAct: EBI-7162569; Score: 0.44
DE  Interaction: P38806; IntAct: EBI-7181311; Score: 0.40
DE  Interaction: P53911; IntAct: EBI-7184902; Score: 0.40
DE  Interaction: Q08162; IntAct: EBI-7271310; Score: 0.56
DE  Interaction: P32324; IntAct: EBI-7286906; Score: 0.56
DE  Interaction: P19659; IntAct: EBI-7307988; Score: 0.40
DE  Interaction: Q12499; IntAct: EBI-7435045; Score: 0.40
DE  Interaction: P53261; IntAct: EBI-7436958; Score: 0.56
DE  Interaction: P53397; IntAct: EBI-7440707; Score: 0.44
DE  Interaction: P22216; IntAct: EBI-7509953; Score: 0.69
DE  Interaction: Q04779; IntAct: EBI-7512888; Score: 0.40
DE  Interaction: P53552; IntAct: EBI-7519241; Score: 0.56
DE  Interaction: P49723; IntAct: EBI-7582150; Score: 0.40
DE  Interaction: P06843; IntAct: EBI-7751879; Score: 0.56
DE  Interaction: Q01476; IntAct: EBI-7792448; Score: 0.40
DE  Interaction: Q04500; IntAct: EBI-7810284; Score: 0.40
DE  Interaction: P22936; IntAct: EBI-7900920; Score: 0.40
DE  Interaction: P36036; IntAct: EBI-8226241; Score: 0.22
DE  Interaction: P33307; IntAct: EBI-1041382; Score: 0.57
DE  Interaction: P32562; IntAct: EBI-2112894; Score: 0.53
DE  Interaction: P06700; IntAct: EBI-2212712; Score: 0.40
DE  Interaction: Q04087; IntAct: EBI-2212766; Score: 0.40
DE  Interaction: Q08904; IntAct: EBI-2344792; Score: 0.37
DE  Interaction: P53184; IntAct: EBI-2345292; Score: 0.37
DE  Interaction: P51601; IntAct: EBI-2345314; Score: 0.37
DE  Interaction: P25367; IntAct: EBI-2345326; Score: 0.37
DE  Interaction: P08536; IntAct: EBI-2345887; Score: 0.37
DE  Interaction: Q03063; IntAct: EBI-2345890; Score: 0.37
DE  Interaction: P17423; IntAct: EBI-2345893; Score: 0.37
DE  Interaction: P60010; IntAct: EBI-2346004; Score: 0.37
DE  Interaction: P38821; IntAct: EBI-2346115; Score: 0.37
DE  Interaction: Q02895; IntAct: EBI-2346118; Score: 0.37
DE  Interaction: Q12306; IntAct: EBI-2346577; Score: 0.37
DE  Interaction: Q06549; IntAct: EBI-2346610; Score: 0.37
DE  Interaction: P32318; IntAct: EBI-2346619; Score: 0.37
DE  Interaction: P43619; IntAct: EBI-2346747; Score: 0.37
DE  Interaction: Q03373; IntAct: EBI-2346812; Score: 0.55
DE  Interaction: P09201; IntAct: EBI-2346852; Score: 0.37
DE  Interaction: Q12189; IntAct: EBI-2347997; Score: 0.37
DE  Interaction: P15202; IntAct: EBI-2348000; Score: 0.37
DE  Interaction: P18759; IntAct: EBI-2348009; Score: 0.37
DE  Interaction: P38716; IntAct: EBI-2348021; Score: 0.37
DE  Interaction: Q12206; IntAct: EBI-2348042; Score: 0.37
DE  Interaction: P37366; IntAct: EBI-2611238; Score: 0.35
DE  Interaction: P13365; IntAct: EBI-2611665; Score: 0.35
DE  Interaction: P32350; IntAct: EBI-2612391; Score: 0.35
DE  Interaction: P40187; IntAct: EBI-2612903; Score: 0.35
DE  Interaction: P38089; IntAct: EBI-2613131; Score: 0.35
DE  Interaction: Q12224; IntAct: EBI-2613375; Score: 0.35
DE  Interaction: P38255; IntAct: EBI-2613514; Score: 0.35
DE  Interaction: P32447; IntAct: EBI-2881693; Score: 0.00
DE  Interaction: Q12495; IntAct: EBI-16280136; Score: 0.53
DE  Interaction: Q02796; IntAct: EBI-2885546; Score: 0.00
DE  Interaction: Q04116; IntAct: EBI-2889029; Score: 0.00
DE  Interaction: P25303; IntAct: EBI-3659819; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3677844; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3784104; Score: 0.35
DE  Interaction: P50875; IntAct: EBI-4376349; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-4380099; Score: 0.35
DE  Interaction: P38129; IntAct: EBI-4380674; Score: 0.35
DE  Interaction: Q05027; IntAct: EBI-4382094; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-4383599; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-4385804; Score: 0.35
DE  Interaction: P53131; IntAct: EBI-10903607; Score: 0.35
DE  Interaction: O00635; IntAct: EBI-11534408; Score: 0.56
DE  Interaction: Q7Z6G3; IntAct: EBI-11534397; Score: 0.56
DE  Interaction: A0A0C4DGF1; IntAct: EBI-11534388; Score: 0.56
DE  Interaction: Q96A10; IntAct: EBI-11534379; Score: 0.56
DE  Interaction: P60709; IntAct: EBI-11534454; Score: 0.56
DE  Interaction: P35520; IntAct: EBI-11534444; Score: 0.56
DE  Interaction: P22234; IntAct: EBI-11534435; Score: 0.56
DE  Interaction: P13196; IntAct: EBI-11534417; Score: 0.56
DE  Interaction: Q13557; IntAct: EBI-11534487; Score: 0.56
DE  Interaction: Q13137; IntAct: EBI-11534474; Score: 0.56
DE  Interaction: P63261; IntAct: EBI-11534464; Score: 0.56
DE  Interaction: Q9NS73; IntAct: EBI-11534541; Score: 0.56
DE  Interaction: Q9HAN9; IntAct: EBI-11534532; Score: 0.56
DE  Interaction: Q8WVF5; IntAct: EBI-11534523; Score: 0.56
DE  Interaction: Q15041; IntAct: EBI-11534514; Score: 0.56
DE  Interaction: Q15038; IntAct: EBI-11534505; Score: 0.56
DE  Interaction: Q13867; IntAct: EBI-11534496; Score: 0.56
DE  Interaction: Q9NVV9; IntAct: EBI-11534559; Score: 0.56
DE  Interaction: Q14974; IntAct: EBI-13942487; Score: 0.44
DE  Interaction: Q03281; IntAct: EBI-15598611; Score: 0.76
DE  Interaction: Q03707; IntAct: EBI-16159762; Score: 0.68
DE  Interaction: P05221; IntAct: EBI-16159838; Score: 0.56
DE  Interaction: P33322; IntAct: EBI-16265066; Score: 0.35
DE  Interaction: P47027; IntAct: EBI-16268315; Score: 0.35
DE  Interaction: P34252; IntAct: EBI-16268369; Score: 0.35
DE  Interaction: P21268; IntAct: EBI-16269078; Score: 0.35
DE  Interaction: P40316; IntAct: EBI-16275395; Score: 0.35
DE  Interaction: P40348; IntAct: EBI-16279429; Score: 0.35
DE  Interaction: Q12749; IntAct: EBI-16279839; Score: 0.35
DE  Interaction: P22470; IntAct: EBI-16281382; Score: 0.35
DE  Interaction: P11978; IntAct: EBI-16282672; Score: 0.35
DE  Interaction: Q00916; IntAct: EBI-16283579; Score: 0.35
DE  Interaction: Q03010; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P38811; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P15019; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P0CS90; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: Q03782; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P38262; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P39954; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: Q02555; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P21538; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P12709; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P29468; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: Q00539; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P33441; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P05694; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P00958; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P17629; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: Q03532; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: Q07623; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P45976; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P14540; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: Q12432; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P54115; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: P19414; IntAct: EBI-16284085; Score: 0.35
DE  Interaction: Q12476; IntAct: EBI-16287516; Score: 0.35
DE  Interaction: Q07930; IntAct: EBI-16290646; Score: 0.35
DE  Interaction: Q00416; IntAct: EBI-16421063; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0042564;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0097718;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0044877;
GO  GO:0051170;
GO  GO:0006607;
GO  GO:0031144;
GO  GO:0006606;
GO  GO:0006612;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDNGTDSSTSKFVPEYRRTNFKNKGRFSADELRRRRDTQQVELRKAKRDEALAKRRNFIPPTDGADSDEEDESSVSADQQ
SQ  FYSQLQQELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEMLQLEAAWALTNIAS
SQ  GTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDYRDYVLQCNAMEPILGLFNSNKPSLIRTATWTLS
SQ  NLCRGKKPQPDWSVVSQALPTLAKLIYSMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPAL
SQ  RAVGNIVTGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPPLVKLLEVAEYKTK
SQ  KEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEVTLDALENILKMGEADKEARGLNINENADFIEKA
SQ  GGMEKIFNCQQNENDKIYEKAYKIIETYFGEEEDAVDETMAPQNAGNTFGFGSNVNQQFNFN
//
ID  P91276;
PN  Importin subunit alpha-2;
GN  ima;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11311162, ECO:0000269|PubMed:12221121}. Nucleus {ECO:0000269|PubMed:11311162, ECO:0000269|PubMed:12221121, ECO:0000269|PubMed:30563860}. Nucleus envelope {ECO:0000269|PubMed:12221121}. Note=In interphase germ cells and embryonic cells, localizes to the cytoplasm and nuclear envelope, whereas in developing oocytes, it localizes in the cytoplasm and nucleus. {ECO:0000269|PubMed:12221121}.
DR  UNIPROT: P91276;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Nuclear transport receptor that mediates nuclear import of proteins, and which is involved in sister chromatid cohesion (PubMed:11311162, PubMed:12221121, PubMed:30563860). Binds specifically and directly to substrates containing either a simple or bipartite nuclear localization signals (NLS) motif (By similarity). Promotes docking of import substrates to the nuclear envelope (By similarity). Together with akir-1 adapter, required for the import and load of cohesin complex proteins in meiotic nuclei (PubMed:30563860). {ECO:0000250|UniProtKB:Q19969, ECO:0000269|PubMed:11311162, ECO:0000269|PubMed:12221121, ECO:0000269|PubMed:30563860}.
DE  Reference Proteome: Yes;
DE  Interaction: V6CLJ5; IntAct: EBI-338966; Score: 0.00
DE  Interaction: G5ECL3; IntAct: EBI-343463; Score: 0.00
DE  Interaction: Q9N2K7; IntAct: EBI-344852; Score: 0.00
DE  Interaction: O44761; IntAct: EBI-6458140; Score: 0.37
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0009792;
GO  GO:0051177;
GO  GO:0007084;
GO  GO:0006607;
GO  GO:0006606;
GO  GO:0051983;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTLTETSLSHNAEEGKDEGGRLQQYKNLTKHEELRRRRTECSVEIRKQKGADMMMKRRNIVDVDEGGNSESELEEPEKIS
SQ  HQQSSTRLSNDEIRAILSNNPSEDDMVRCFESLRKSLSKTKNPPIDEVIHCGLLQALVQALSVENERVQYEAAWALTNIV
SQ  SGSTEQTIAAVEAGVTIPLIHLSVHQSAQISEQALWAVANIAGDSSQLRDYVIKCHGVEALMHLMEKVDQLGDSHVRTIA
SQ  WAFSNMCRHKNPHAPLEVLRVLSKGLVKLVQHTDRQVRQDACWAVSYLTDGPDEQIELARESGVLPHVVAFFKEAENLVA
SQ  PALRTLGNVATGNDSLTQAVIDLGSLDEILPLMEKTRSSSIVKECCWLVSNIIAGTQKQIQAVLDANLLPVLINVLKSGD
SQ  HKCQFEASWALSNLAQGGTNRQVVAMLEDNVVPALCQALLQTNTDMLNNTLETLYTLMLTVQNGYPHKVDILHDQVEENG
SQ  GLDSLERLQESQSEQIYTQAYRIITQFFTDDDAGEKESHENADPQDNKWSF
//
ID  O59809;
PN  Probable importin c550.11;
GN  SPCC550;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O59809;
DR  Pfam: PF08506;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Active in protein import into the nucleus. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0005049;
GO  GO:0061608;
GO  GO:0031267;
GO  GO:0006406;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLVEHFDATLSADPNTRTKAELSLKQLEKEPSFVLAVLQLLSSQEISLPTQQAAVIYLKNRVSRSWSSIDDAPSPLDIP
SQ  EEQKALFRQNILPVLLQSPMSTRSHLMAILNIILSTDFPEYWPGFSEYTSNLVHSTERCEVYAGLICFHELAKVYRWRLD
SQ  DRQRDIGPLVAALFPTILQLGQGLINLEDNDSAEMLRLILKTFKSVIALELPPELLANDMILSWIQLLLAVVQKPLPESL
SQ  MSLEPEVRQSHVWHKCKKWAYYSLNRIFTRYGEPSSLVGDSANKYRAFAKNFITNVVPNILETYIQQTILWTQGQLWLSP
SQ  RVLYFLGCFYEECVKPKSTWALLKPHLQLLIGSFVFPQLCMSEEDEELWELDPVEFIHKYIDIYDDFNSADVAASRFLVK
SQ  LASKRKKYTFMGILSFASDILNQYAASPPNEKNPRQKEGALRMVAAVSNSILSKNSPVAGMMQDFLVAHVMPEFTSPVGY
SQ  LRSRACEMINRFSEIDWSDKSQLLNAYQAVLNCLQDNDLPVRIQAALALQPLMRHLEVHDVMTAHVPIIMQNLLFLANEV
SQ  DIDALSSCMEEFVSSFSHELTPFASQLAKQLRNTFVKLMQETMDESTTVDDFDSLVDDKSIAAIGILNTLSTMILSLENT
SQ  VDVLREIEAILLPMINFVLDNNIFDVYAELFEIIDGCTFASKEISPIMWGVYEKLQKVLKESGIEFVEEATPALSNFITY
SQ  GGKEFASRPDYIAVMVDIIMQVFNSEHLAVNDRVSACKLTELLMLNYRGLLDQYVPAFIEVAGNLLLVTEKPTSQTYRVF
SQ  LLEVIINALYYNPSMSLGVLEMHQWTLPFFALWFENIPSFTRVHDKKLSLVAILSVISLGAQQVAVAIQDSWGNIMKVMI
SQ  TLLNTLPEALAARAELEKEYDGETFNLSGSGWNDGIDWEADDDEGVDDFAVEYGGPDLGGEISADVVDDFDEFEHFQGNY
SQ  LLDEDPLFHTLLDQVDPFSLFQEFMVHLKDNSPVTLQDLVKNLEASEQQSLQRLVTEKPSTLAVASDKT
//
ID  Q76P29;
PN  Importin subunit alpha-B;
GN  DDB_G0272318;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q76P29;
DR  UNIPROT: Q55A47;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Functions in nuclear protein import via a substrate-importin alpha-beta transport complex that passes though the nuclear pore complexes (NPC). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQRSKQETRKSQYKKSIDSDESRRKREEASLSIRKNKREESLLKKRTQAVPGSTPVKVDSLINQRLEQLPSLVAEINSEN
SQ  PDLILKSTTAFRKLLSIEKSPPIEEVIKTGIVPRLVKFLYMQDFPQLQFEAAWALTNIASGTPEQTRVVIENGAIQVFVL
SQ  LLSSPHDDVREQAVWALGNIAGDSHYCRDLVLSHNALPPLLSLLQNPAAIKVSMVRNATWTLSNFCRGKPQPPFEIVRAS
SQ  LPVLAKLIYYQDEEVLIDACWALSYLSDGSNERIQEVIDAKVCRKMVELLGHPTIAVQTPALRTIGNIVTGDDNQTQIVL
SQ  SVQALSHLLNLLQSPKRAIRKEACWTISNITAGDKNQIQQVIDANIIPSLVYLLANAEFEIQKEAAWAISNATSCGTPQQ
SQ  IHFLVSQGCVKPLCDLLKVSDPRIINVALEGIENILVAGKKEAQVTGVNPYKKIIEDADGLGKIYDLQHHMNKDTFEKVS
SQ  RIISTYLEDEQEDEGDLMPEGSSFSFSNQTNSNFNL
//
ID  Q9FYP9;
PN  Importin subunit alpha-2;
GN  P0011G08;
OS  39947;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region.
DR  UNIPROT: Q9FYP9;
DR  UNIPROT: O80332;
DR  UNIPROT: Q0JQJ0;
DR  Pfam: PF00514;
DE  Function: Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. {ECO:0000269|PubMed:11124253}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADDSASPSPSSASPLQHHREALKSSVRNTAASRRREQAIAIGKERREALIRAKRVCRAPISGSDEAEMEEGDMVVDEEK
SQ  ACLEAKTAHAVEELKSALSIQGKGVQKKKIEALRDLRRLLSQPEVPLVDTAIKAGAVPLLVQYLSFGSSDEQLLEAAWCL
SQ  TNIAAGEPEETKSLLPALPLLIAHLGEKSSTLVAEQCAWAIGNVAGEGAELRSTLLAQGALRPLTRLMFSSKGSTARTAA
SQ  WAMSNLIKGPDPKAANELITIDGVLNAIIASLEKEDEELATEVAWVVVYLSALSDRGISLIVRSSVPQLLIGRLFSSENL
SQ  QLLIPVLRGLGNLIAADDYMVDSVLTVGHNIIDQALSGLIKCLKSDNRVLRKESSWALSNIAAGSFEHKKLIFASEATPV
SQ  LIRLVTSMQFDIRREAAYTLGNLCVVPTGNCELPKIIVEHLVAIVDGGALPGFIHLVRSADVDTAGLGLQFLELVMRGYP
SQ  NKQGPKLVEMEDGIEAMERFQFHENEQMRNMANGLVDEYFGEDYGLDE
//
ID  Q14974;
PN  Importin subunit beta-1;
GN  KPNB1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11891849}. Nucleus envelope {ECO:0000269|PubMed:11891849}.
DR  UNIPROT: Q14974;
DR  UNIPROT: B7ZAV6;
DR  UNIPROT: D3DTT3;
DR  UNIPROT: Q14637;
DR  UNIPROT: Q53XN2;
DR  UNIPROT: Q96J27;
DR  PDB: 1F59;
DR  PDB: 1IBR;
DR  PDB: 1M5N;
DR  PDB: 1O6O;
DR  PDB: 1O6P;
DR  PDB: 1QGK;
DR  PDB: 1QGR;
DR  PDB: 2P8Q;
DR  PDB: 2Q5D;
DR  PDB: 2QNA;
DR  PDB: 3LWW;
DR  PDB: 3W5K;
DR  PDB: 6N88;
DR  PDB: 6N89;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DR  OMIM: 602738;
DR  DisGeNET: 3837;
DE  Function: Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:11682607). In association with IPO7, mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports SNAI1 and PRKCI into the nucleus. {ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:24699649, ECO:0000269|PubMed:9687515}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: A6NF01; IntAct: EBI-30827108; Score: 0.44
DE  Interaction: A8CG34; IntAct: EBI-11115566; Score: 0.59
DE  Interaction: O14524; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: O15504; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: O95295; IntAct: EBI-5664409; Score: 0.00
DE  Interaction: P00533; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P04626; IntAct: EBI-4373084; Score: 0.57
DE  Interaction: P14907; IntAct: EBI-1034546; Score: 0.62
DE  Interaction: P35658; IntAct: EBI-30827243; Score: 0.44
DE  Interaction: P46060; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.77
DE  Interaction: P49792; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-11115566; Score: 0.53
DE  Interaction: P63165; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: P70168; IntAct: EBI-2555147; Score: 0.40
DE  Interaction: P78406; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q02821; IntAct: EBI-13942487; Score: 0.44
DE  Interaction: Q12769; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P52292; IntAct: EBI-286795; Score: 0.93
DE  Interaction: Q9GK30; IntAct: EBI-8580826; Score: 0.44
DE  Interaction: Q9NRA8; IntAct: EBI-301394; Score: 0.35
DE  Interaction: Q01201; IntAct: EBI-363445; Score: 0.00
DE  Interaction: P20333; IntAct: EBI-364543; Score: 0.00
DE  Interaction: Q15628; IntAct: EBI-364816; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-365110; Score: 0.00
DE  Interaction: P60709; IntAct: EBI-353790; Score: 0.40
DE  Interaction: Q16637; IntAct: EBI-464895; Score: 0.52
DE  Interaction: O75940; IntAct: EBI-464916; Score: 0.40
DE  Interaction: Q12873; IntAct: EBI-474956; Score: 0.37
DE  Interaction: Q8N2W9; IntAct: EBI-475005; Score: 0.37
DE  Interaction: P21246; IntAct: EBI-475012; Score: 0.37
DE  Interaction: Q15796; IntAct: EBI-7224889; Score: 0.37
DE  Interaction: P51178; IntAct: EBI-7795361; Score: 0.60
DE  Interaction: O92837; IntAct: EBI-8512780; Score: 0.40
DE  Interaction: P03087; IntAct: EBI-8512862; Score: 0.44
DE  Interaction: P03126; IntAct: EBI-8592423; Score: 0.44
DE  Interaction: P03107; IntAct: EBI-7362635; Score: 0.44
DE  Interaction: P03101; IntAct: EBI-7362692; Score: 0.62
DE  Interaction: P63104; IntAct: EBI-7194971; Score: 0.40
DE  Interaction: P13569; IntAct: EBI-1171566; Score: 0.64
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.35
DE  Interaction: P32121; IntAct: EBI-1642843; Score: 0.35
DE  Interaction: Q00005; IntAct: EBI-2211497; Score: 0.35
DE  Interaction: Q9Z0E3; IntAct: EBI-2549710; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: Q9QWT9; IntAct: EBI-2558911; Score: 0.40
DE  Interaction: E9PVX6; IntAct: EBI-2561030; Score: 0.40
DE  Interaction: Q9D4G9; IntAct: EBI-2561931; Score: 0.40
DE  Interaction: Q9D0T1; IntAct: EBI-2563541; Score: 0.40
DE  Interaction: Q8N0X7; IntAct: EBI-2643801; Score: 0.35
DE  Interaction: Q5NEH1; IntAct: EBI-2805872; Score: 0.00
DE  Interaction: Q14974; IntAct: EBI-7166773; Score: 0.44
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q5EWX9; IntAct: EBI-8070469; Score: 0.35
DE  Interaction: Q16658; IntAct: EBI-2893273; Score: 0.35
DE  Interaction: Q9UH99; IntAct: EBI-8021405; Score: 0.40
DE  Interaction: O00629; IntAct: EBI-8291902; Score: 0.74
DE  Interaction: Q8K4J6; IntAct: EBI-8292094; Score: 0.52
DE  Interaction: Q00610; IntAct: EBI-4373239; Score: 0.35
DE  Interaction: Q15075; IntAct: EBI-4373273; Score: 0.35
DE  Interaction: P42566; IntAct: EBI-4373380; Score: 0.40
DE  Interaction: P50570; IntAct: EBI-4373384; Score: 0.35
DE  Interaction: Q14696; IntAct: EBI-7246101; Score: 0.37
DE  Interaction: Q5TAQ9; IntAct: EBI-7817974; Score: 0.40
DE  Interaction: P0C1C7; IntAct: EBI-6157992; Score: 0.35
DE  Interaction: P0C1C6; IntAct: EBI-6158469; Score: 0.35
DE  Interaction: Q05322; IntAct: EBI-6159823; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6191068; Score: 0.53
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: P49761; IntAct: EBI-6380381; Score: 0.35
DE  Interaction: Q9UBE8; IntAct: EBI-6381385; Score: 0.35
DE  Interaction: Q9UQ88; IntAct: EBI-6381526; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.53
DE  Interaction: Q13043; IntAct: EBI-10049645; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-10103376; Score: 0.35
DE  Interaction: O60674; IntAct: EBI-10103554; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: P04620; IntAct: EBI-10687139; Score: 0.58
DE  Interaction: P03225; IntAct: EBI-11722220; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-11016929; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: P34022; IntAct: EBI-11080066; Score: 0.35
DE  Interaction: Q15398; IntAct: EBI-11083028; Score: 0.53
DE  Interaction: Q6PFD6; IntAct: EBI-11093571; Score: 0.35
DE  Interaction: Q9R1K9; IntAct: EBI-11111151; Score: 0.35
DE  Interaction: P18754; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9HCK8; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q96JN0; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q69YN4; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P52294; IntAct: EBI-11115566; Score: 0.69
DE  Interaction: Q96JA3; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q15544; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P62495; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: O60684; IntAct: EBI-11115566; Score: 0.59
DE  Interaction: Q96G23; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: I3L0N3; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q8TEP8; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: O14715; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: O15541; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q96P63; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q8NI27; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q92750; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P51648; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: J3QR07; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6NUQ4; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9BXS6; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q69YH5; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9UDW1; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9UKX7; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q86VU5; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9BW19; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9NXE4; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q8NFH4; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: E9PF10; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: O75448; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q96SK2; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9P0U3; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P43487; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q8TEM1; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9BTX1; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q53EZ4; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q8N2Y8; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P55084; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: O95373; IntAct: EBI-11115566; Score: 0.59
DE  Interaction: Q99567; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: O00505; IntAct: EBI-11115566; Score: 0.71
DE  Interaction: Q9UBU9; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PJT7; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9BW27; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: O14975; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9HB58; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q53GS7; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: O75909; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q86VQ0; IntAct: EBI-11363336; Score: 0.35
DE  Interaction: P48039; IntAct: EBI-11577056; Score: 0.00
DE  Interaction: Q9WMX2; IntAct: EBI-11513409; Score: 0.50
DE  Interaction: O96017; IntAct: EBI-11579031; Score: 0.35
DE  Interaction: P27105; IntAct: EBI-12452286; Score: 0.51
DE  Interaction: Q71U36; IntAct: EBI-11897791; Score: 0.35
DE  Interaction: P03427; IntAct: EBI-14404759; Score: 0.35
DE  Interaction: P46531; IntAct: EBI-13915571; Score: 0.35
DE  Interaction: A9QM74; IntAct: EBI-13950021; Score: 0.44
DE  Interaction: O15355; IntAct: EBI-14023765; Score: 0.35
DE  Interaction: O15297; IntAct: EBI-14024588; Score: 0.53
DE  Interaction: P36873; IntAct: EBI-14025388; Score: 0.42
DE  Interaction: P56180; IntAct: EBI-14025693; Score: 0.42
DE  Interaction: P62140; IntAct: EBI-14026087; Score: 0.42
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.59
DE  Interaction: P10275; IntAct: EBI-15187911; Score: 0.40
DE  Interaction: O43524; IntAct: EBI-15187932; Score: 0.35
DE  Interaction: Q9NPC8; IntAct: EBI-21617697; Score: 0.35
DE  Interaction: P61769; IntAct: EBI-21675069; Score: 0.35
DE  Interaction: Q5SSJ5; IntAct: EBI-21734720; Score: 0.35
DE  Interaction: Q2NL82; IntAct: EBI-21815364; Score: 0.35
DE  Interaction: P54645; IntAct: EBI-16361875; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16362252; Score: 0.35
DE  Interaction: O95149; IntAct: EBI-15577065; Score: 0.44
DE  Interaction: P52298; IntAct: EBI-15798493; Score: 0.52
DE  Interaction: Q09161; IntAct: EBI-15798552; Score: 0.40
DE  Interaction: Q9BUR4; IntAct: EBI-15892338; Score: 0.35
DE  Interaction: P03950; IntAct: EBI-16363282; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-16799122; Score: 0.35
DE  Interaction: O94776; IntAct: EBI-16803315; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: O00429; IntAct: EBI-20305770; Score: 0.35
DE  Interaction: Q99714; IntAct: EBI-20306067; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-20306992; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-20307233; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-20307902; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-20621330; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20722397; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20799058; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21024514; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P56817; IntAct: EBI-20992725; Score: 0.35
DE  Interaction: P04156; IntAct: EBI-21014477; Score: 0.35
DE  Interaction: P04233; IntAct: EBI-21258980; Score: 0.50
DE  Interaction: Q99558; IntAct: EBI-21261374; Score: 0.50
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.50
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.50
DE  Interaction: Q9Y275; IntAct: EBI-21266480; Score: 0.50
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.50
DE  Interaction: P42858; IntAct: EBI-21132926; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-21236861; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-30827879; Score: 0.59
DE  Interaction: P09613; IntAct: EBI-21497303; Score: 0.35
DE  Interaction: Q16526; IntAct: EBI-21981854; Score: 0.35
DE  Interaction: Q13164; IntAct: EBI-25374538; Score: 0.35
DE  Interaction: P11234; IntAct: EBI-25376255; Score: 0.35
DE  Interaction: Q92934; IntAct: EBI-25378368; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9BY14; IntAct: EBI-25505396; Score: 0.35
DE  Interaction: A0A3G5BIZ0; IntAct: EBI-25565269; Score: 0.43
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: B3CRR2; IntAct: EBI-26357604; Score: 0.50
DE  Interaction: B3CTB0; IntAct: EBI-26357616; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-26396827; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27111302; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q05D32; IntAct: EBI-27113232; Score: 0.35
DE  Interaction: P0DTC4; IntAct: EBI-28955127; Score: 0.35
DE  Interaction: Q5HYC2; IntAct: EBI-30827309; Score: 0.44
DE  Interaction: O96028; IntAct: EBI-30827207; Score: 0.44
DE  Interaction: Q6ZQQ2; IntAct: EBI-30827357; Score: 0.44
DE  Interaction: Q6ZUB0; IntAct: EBI-30827368; Score: 0.44
DE  Interaction: Q702N8; IntAct: EBI-30827379; Score: 0.44
DE  Interaction: Q7RTY1; IntAct: EBI-30827390; Score: 0.44
DE  Interaction: Q7Z6M1; IntAct: EBI-30827401; Score: 0.44
DE  Interaction: Q8N398; IntAct: EBI-30827412; Score: 0.44
DE  Interaction: O15397; IntAct: EBI-30827163; Score: 0.44
DE  Interaction: O43307; IntAct: EBI-30827174; Score: 0.44
DE  Interaction: O43520; IntAct: EBI-30827185; Score: 0.44
DE  Interaction: O15321; IntAct: EBI-30827152; Score: 0.44
DE  Interaction: O00750; IntAct: EBI-30827141; Score: 0.44
DE  Interaction: Q15642; IntAct: EBI-30827298; Score: 0.44
DE  Interaction: P0C874; IntAct: EBI-30827232; Score: 0.44
DE  Interaction: Q5XG87; IntAct: EBI-30827320; Score: 0.44
DE  Interaction: Q9H207; IntAct: EBI-30827679; Score: 0.44
DE  Interaction: Q9C0D9; IntAct: EBI-30827646; Score: 0.44
DE  Interaction: Q9BZ95; IntAct: EBI-30827635; Score: 0.44
DE  Interaction: Q96R08; IntAct: EBI-30827624; Score: 0.44
DE  Interaction: Q96HA1; IntAct: EBI-30827588; Score: 0.44
DE  Interaction: Q92615; IntAct: EBI-30827577; Score: 0.44
DE  Interaction: Q8NGY0; IntAct: EBI-30827566; Score: 0.44
DE  Interaction: Q8NGI9; IntAct: EBI-30827537; Score: 0.44
DE  Interaction: Q8NGA6; IntAct: EBI-30827526; Score: 0.44
DE  Interaction: Q8N7C0; IntAct: EBI-30827423; Score: 0.44
DE  Interaction: Q8NCP5; IntAct: EBI-30827434; Score: 0.44
DE  Interaction: Q9H208; IntAct: EBI-30827709; Score: 0.44
DE  Interaction: Q8NGA2; IntAct: EBI-30827490; Score: 0.44
DE  Interaction: Q8NG92; IntAct: EBI-30827464; Score: 0.44
DE  Interaction: Q9H6Z4; IntAct: EBI-30827857; Score: 0.44
DE  Interaction: Q9NRD1; IntAct: EBI-30827868; Score: 0.44
DE  Interaction: Q9Y399; IntAct: EBI-30827920; Score: 0.44
DE  Interaction: Q9NZP0; IntAct: EBI-30827909; Score: 0.44
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0071782;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:1904813;
GO  GO:0016020;
GO  GO:0042564;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0035580;
GO  GO:0019899;
GO  GO:0051879;
GO  GO:0061676;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0019904;
GO  GO:0003723;
GO  GO:0031267;
GO  GO:0008270;
GO  GO:0030953;
GO  GO:0040001;
GO  GO:0045184;
GO  GO:0007079;
GO  GO:0007080;
GO  GO:0090307;
GO  GO:0006607;
GO  GO:0006606;
GO  GO:0031291;
GO  GO:0006610;
GO  GO:0006404;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIKNSLTSKDPDIKAQYQQRW
SQ  LAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQD
SQ  IDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN
SQ  LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQ
SQ  YLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPS
SQ  QLKPLVIQAMPTLIELMKDPSVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA
SQ  AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQ
SQ  VLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLG
SQ  GEFLKYMEAFKPFLGIGLKNYAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI
SQ  ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSF
SQ  IDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
//
ID  P70168;
PN  Importin subunit beta-1;
GN  Kpnb1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: P70168;
DR  UNIPROT: Q62117;
DR  UNIPROT: Q6GTI5;
DR  PDB: 1GCJ;
DR  PDB: 1UKL;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. In association with IPO7, mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Imports SNAI1 and PRKCI into the nucleus (By similarity). {ECO:0000250|UniProtKB:Q14974, ECO:0000269|PubMed:11493596}.
DE  Reference Proteome: Yes;
DE  Interaction: P17955; IntAct: EBI-15732706; Score: 0.36
DE  Interaction: P35922; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-16128776; Score: 0.44
DE  Interaction: P49790; IntAct: EBI-15732587; Score: 0.52
DE  Interaction: P49792; IntAct: EBI-15732742; Score: 0.36
DE  Interaction: P62826; IntAct: EBI-15732723; Score: 0.44
DE  Interaction: P46527; IntAct: EBI-540594; Score: 0.50
DE  Interaction: A3KGF7; IntAct: EBI-688094; Score: 0.37
DE  Interaction: P11798; IntAct: EBI-652692; Score: 0.37
DE  Interaction: Q12772; IntAct: EBI-1037525; Score: 0.44
DE  Interaction: P01580; IntAct: EBI-7892295; Score: 0.40
DE  Interaction: P03070; IntAct: EBI-7892542; Score: 0.40
DE  Interaction: Q9Z0E3; IntAct: EBI-2549816; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-2555147; Score: 0.40
DE  Interaction: P49452; IntAct: EBI-8573213; Score: 0.35
DE  Interaction: Q8BP00; IntAct: EBI-4283417; Score: 0.35
DE  Interaction: Q8CG73; IntAct: EBI-4284701; Score: 0.35
DE  Interaction: Q6AXH7; IntAct: EBI-6876709; Score: 0.35
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q9P2S5; IntAct: EBI-11694751; Score: 0.35
DE  Interaction: O54957; IntAct: EBI-12602113; Score: 0.35
DE  Interaction: P32835; IntAct: EBI-15558546; Score: 0.44
DE  Interaction: Q61712; IntAct: EBI-15558601; Score: 0.44
DE  Interaction: P83953; IntAct: EBI-16128832; Score: 0.44
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0071782;
GO  GO:0042564;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0019899;
GO  GO:0051879;
GO  GO:0061676;
GO  GO:0019894;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0019904;
GO  GO:0044877;
GO  GO:0031267;
GO  GO:0030953;
GO  GO:0040001;
GO  GO:0045184;
GO  GO:0007079;
GO  GO:0007080;
GO  GO:0090307;
GO  GO:0006606;
GO  GO:0031291;
GO  GO:0006610;
GO  GO:0006404;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIKNSLTSKDPDIKAQYQQRW
SQ  LAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVSQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQD
SQ  IDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN
SQ  LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQ
SQ  YLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLSTCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGSILEGPEPN
SQ  QLKPLVIQAMPTLIELMKDPSVVVRDTTAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA
SQ  AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQ
SQ  VLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLG
SQ  GEFLKYMEAFKPFLGIGLKNYAEYQVCLAAVGLVGDLCRALQSNILPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI
SQ  ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDFDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSF
SQ  IDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
//
ID  P52296;
PN  Importin subunit beta-1;
GN  Kpnb1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:7604027}. Nucleus envelope {ECO:0000269|PubMed:7604027}.
DR  UNIPROT: P52296;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. In association with IPO7, mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Imports SNAI1 and PRKCI into the nucleus (By similarity). {ECO:0000250|UniProtKB:Q14974}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P21708; IntAct: EBI-7621986; Score: 0.35
DE  Interaction: A0A142I9X8; IntAct: EBI-11701393; Score: 0.35
DE  Interaction: P16310; IntAct: EBI-15651327; Score: 0.40
DE  Interaction: P09619; IntAct: EBI-22247316; Score: 0.35
DE  Interaction: P19332; IntAct: EBI-26374040; Score: 0.35
GO  GO:0010494;
GO  GO:0071782;
GO  GO:0042564;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0019899;
GO  GO:0051879;
GO  GO:0061676;
GO  GO:0019894;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0019904;
GO  GO:0044877;
GO  GO:0031267;
GO  GO:0030953;
GO  GO:0040001;
GO  GO:0045184;
GO  GO:0007079;
GO  GO:0007080;
GO  GO:0090307;
GO  GO:0006606;
GO  GO:0031291;
GO  GO:0006610;
GO  GO:0006404;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIRLLTSKDPDIKAQYQQRWL
SQ  AIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVSQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDI
SQ  DPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNL
SQ  VKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQY
SQ  LVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLSTCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGSILEGPEPNQ
SQ  LKPLVIQAMPTLIELMKDPSVVVRDTTAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAA
SQ  YEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQV
SQ  LQMESHIQSTSDRIQFNDLQSLLCATLQNVLWKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGG
SQ  EFLKYMEAFKPFLGIGLKNYAECQVCLAAVGLVGDLCRALQSNILPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDIT
SQ  LAIGGEFKKYLEVVLNTLQQASQAQVDKSDFDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFI
SQ  DHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
//
ID  O13864;
PN  Importin subunit beta-1;
GN  kap95;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q06142}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q06142}.
DR  UNIPROT: O13864;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Importin beta subunit that functions in nuclear protein import through association with the importin alpha subunit, which binds to the clasical nuclear localization signal (cNLS) in cargo substrates. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by importin beta through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binds to importin beta and the three components separate, leading to release of the cargo. Importin alpha and beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin beta. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q06142}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:1990023;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0031267;
GO  GO:0051028;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNAGEFLAQTLSPDANVRLNAEKQLENAARTDFAQYMVLLAQELANDNSMPYIRMAAGLALKNAITAREEARKLEYQQLW
SQ  QSLPVEIKQQVKSLALQTLGSSEHQAGQSAAQLVAAIAAYELATNQWPDLMVTLVANVGEGQPSALKQHSLQTIGYICES
SQ  VSPEVLSAQSNAILTAVVAGARKEEPDAAVRLAALGALYDSLEFVRENFNNEYERNYIMQVVCEATQSPEASIQTAAFGC
SQ  LVKIMHLYYDTMPFYMEKALFALTTQGMYNTNEQVALQAVEFWSTVCEEEIEVNLEIQEAQDLNEVPARQNHGFARAAAA
SQ  DILPVLLKLLCNQDEDADEDDWNISMAAATCLQLFAQVVGDLIVNPVLAFVEQNIQNPDWHQREAAVMAFGSVLEGPNVA
SQ  MLTPLVNQALPVLINMMVDPVIFVKDTTAWALGQISSFVADAINPEIHLSPMVSALLQGLTDNPRIVANCCWAFMNLVCH
SQ  FAPVDNHQTSVMTPFYEAIIGSLLHVTDQKGNENNSRTSGYETLGTLITFSSDSVLPMIANVLSIILTRLETSIQMQSQI
SQ  LDVEDRANHDELQSNLCNVLTSIIRRFGPDIRTSSDQIMNLLLQTMQTAPKQSVVHEDVLLAIGAMMNSLEEQFEVYVPS
SQ  FVPFLSSALSNEQEYQLCSVAVGLVGDLARALNAKILPYCDDFMTRLVQDLQSSVLDRNVKPAILSCFSDIALAIGAAFQ
SQ  TYLEAVMVLLQQASSVQAPPGANFSMIDYVDALRLGIVEAYVGITQAVRTDNRLDLIQPYVHSMFTLLNMITADPECSES
SQ  LTRAALGLLGDLAESFPKGELKSYFAADWVAALLNSGKTKISSQQTKDLARWATEQVKRQARA
//
ID  Q06142;
PN  Importin subunit beta-1;
GN  KAP95;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:9321403}. Nucleus {ECO:0000269|PubMed:9321403}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}.
DR  UNIPROT: Q06142;
DR  UNIPROT: D6VYY6;
DR  PDB: 2BKU;
DR  PDB: 3EA5;
DR  PDB: 3ND2;
DR  PDB: 5OWU;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Importin beta subunit that functions in nuclear protein import through association with the importin alpha subunit, which binds to the classical nuclear localization signal (cNLS) in cargo substrates (PubMed:7622450). Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by importin beta through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:8521485). At the nucleoplasmic side of the NPC, GTP- Ran binds to importin beta and the three components separate, leading to release of the cargo (PubMed:15864302). Importin alpha and beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin beta. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015). Mediates the nuclear import of histones H2A and H2B (PubMed:11309407). Mediates the nuclear import of transcription factor GCN4 (PubMed:14648200). {ECO:0000269|PubMed:11309407, ECO:0000269|PubMed:14648200, ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:7622450, ECO:0000269|PubMed:8521485, ECO:0000305|PubMed:11423015}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-1173482; Score: 0.72
DE  Interaction: P20676; IntAct: EBI-789997; Score: 0.77
DE  Interaction: P32499; IntAct: EBI-784458; Score: 0.78
DE  Interaction: P34160; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P39705; IntAct: EBI-802293; Score: 0.77
DE  Interaction: P40069; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P40477; IntAct: EBI-1173489; Score: 0.61
DE  Interaction: P48837; IntAct: EBI-1269406; Score: 0.00
DE  Interaction: P49686; IntAct: EBI-1266067; Score: 0.00
DE  Interaction: P49687; IntAct: EBI-1269395; Score: 0.00
DE  Interaction: Q02199; IntAct: EBI-1269417; Score: 0.00
DE  Interaction: Q02629; IntAct: EBI-1566666; Score: 0.82
DE  Interaction: Q02630; IntAct: EBI-1566676; Score: 0.67
DE  Interaction: Q02821; IntAct: EBI-784458; Score: 0.94
DE  Interaction: Q03790; IntAct: EBI-1269428; Score: 0.00
DE  Interaction: Q05166; IntAct: EBI-1269439; Score: 0.00
DE  Interaction: P53911; IntAct: EBI-531265; Score: 0.56
DE  Interaction: P53261; IntAct: EBI-7108298; Score: 0.59
DE  Interaction: P53552; IntAct: EBI-7108332; Score: 0.59
DE  Interaction: P10863; IntAct: EBI-7108362; Score: 0.40
DE  Interaction: Q06142; IntAct: EBI-7108412; Score: 0.40
DE  Interaction: Q12149; IntAct: EBI-7108426; Score: 0.69
DE  Interaction: P43609; IntAct: EBI-7108460; Score: 0.59
DE  Interaction: P06103; IntAct: EBI-7108489; Score: 0.40
DE  Interaction: Q12499; IntAct: EBI-7108547; Score: 0.40
DE  Interaction: P38219; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-784458; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-784458; Score: 0.53
DE  Interaction: P18888; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P19358; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P10659; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P46654; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P26755; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P32337; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P33892; IntAct: EBI-784458; Score: 0.35
DE  Interaction: Q04673; IntAct: EBI-786726; Score: 0.35
DE  Interaction: Q00578; IntAct: EBI-787928; Score: 0.35
DE  Interaction: P38262; IntAct: EBI-788896; Score: 0.35
DE  Interaction: P28496; IntAct: EBI-793629; Score: 0.35
DE  Interaction: P36124; IntAct: EBI-794754; Score: 0.53
DE  Interaction: Q12504; IntAct: EBI-795637; Score: 0.35
DE  Interaction: Q12476; IntAct: EBI-796671; Score: 0.35
DE  Interaction: Q02724; IntAct: EBI-797293; Score: 0.56
DE  Interaction: P38703; IntAct: EBI-799064; Score: 0.35
DE  Interaction: P53833; IntAct: EBI-799459; Score: 0.35
DE  Interaction: P13259; IntAct: EBI-799593; Score: 0.35
DE  Interaction: Q04779; IntAct: EBI-801204; Score: 0.35
DE  Interaction: Q04182; IntAct: EBI-802063; Score: 0.35
DE  Interaction: P50111; IntAct: EBI-803477; Score: 0.35
DE  Interaction: P22336; IntAct: EBI-804782; Score: 0.35
DE  Interaction: P39004; IntAct: EBI-806863; Score: 0.35
DE  Interaction: Q08920; IntAct: EBI-810994; Score: 0.67
DE  Interaction: P38111; IntAct: EBI-813321; Score: 0.27
DE  Interaction: P28003; IntAct: EBI-815383; Score: 0.27
DE  Interaction: P14832; IntAct: EBI-816973; Score: 0.27
DE  Interaction: Q06218; IntAct: EBI-817288; Score: 0.27
DE  Interaction: P19414; IntAct: EBI-819202; Score: 0.27
DE  Interaction: P47077; IntAct: EBI-854045; Score: 0.35
DE  Interaction: P47026; IntAct: EBI-854100; Score: 0.35
DE  Interaction: Q05543; IntAct: EBI-6995831; Score: 0.40
DE  Interaction: Q12460; IntAct: EBI-7021174; Score: 0.40
DE  Interaction: P53072; IntAct: EBI-7153942; Score: 0.40
DE  Interaction: Q05900; IntAct: EBI-7156472; Score: 0.40
DE  Interaction: P47108; IntAct: EBI-7162619; Score: 0.40
DE  Interaction: P38806; IntAct: EBI-7181361; Score: 0.40
DE  Interaction: P19659; IntAct: EBI-7308345; Score: 0.40
DE  Interaction: P53397; IntAct: EBI-7440746; Score: 0.40
DE  Interaction: P22216; IntAct: EBI-7510088; Score: 0.67
DE  Interaction: P49723; IntAct: EBI-7582061; Score: 0.40
DE  Interaction: P0CG63; IntAct: EBI-7613913; Score: 0.40
DE  Interaction: P0CX31; IntAct: EBI-7651644; Score: 0.40
DE  Interaction: Q08446; IntAct: EBI-7691677; Score: 0.40
DE  Interaction: Q03782; IntAct: EBI-7728183; Score: 0.40
DE  Interaction: Q01476; IntAct: EBI-7791695; Score: 0.40
DE  Interaction: P32357; IntAct: EBI-7893646; Score: 0.40
DE  Interaction: P38991; IntAct: EBI-8082572; Score: 0.40
DE  Interaction: P05694; IntAct: EBI-8435372; Score: 0.40
DE  Interaction: P15019; IntAct: EBI-6317331; Score: 0.00
DE  Interaction: P32562; IntAct: EBI-2112894; Score: 0.53
DE  Interaction: P06700; IntAct: EBI-2212712; Score: 0.40
DE  Interaction: P37366; IntAct: EBI-2611238; Score: 0.35
DE  Interaction: P40187; IntAct: EBI-2612903; Score: 0.35
DE  Interaction: Q12224; IntAct: EBI-2613375; Score: 0.35
DE  Interaction: P32447; IntAct: EBI-2881693; Score: 0.00
DE  Interaction: Q12495; IntAct: EBI-16280136; Score: 0.53
DE  Interaction: P53687; IntAct: EBI-2884664; Score: 0.00
DE  Interaction: Q12529; IntAct: EBI-2887496; Score: 0.00
DE  Interaction: P39723; IntAct: EBI-2887969; Score: 0.00
DE  Interaction: P27692; IntAct: EBI-2888169; Score: 0.00
DE  Interaction: Q04116; IntAct: EBI-2889003; Score: 0.00
DE  Interaction: P39101; IntAct: EBI-3653413; Score: 0.35
DE  Interaction: P32527; IntAct: EBI-3656017; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3671852; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3721078; Score: 0.35
DE  Interaction: P39079; IntAct: EBI-3740059; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3745091; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3757079; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-3809579; Score: 0.35
DE  Interaction: P32835; IntAct: EBI-16270361; Score: 0.35
DE  Interaction: Q08773; IntAct: EBI-16271699; Score: 0.35
DE  Interaction: P42838; IntAct: EBI-16272625; Score: 0.35
DE  Interaction: Q07623; IntAct: EBI-16287594; Score: 0.35
DE  Interaction: Q00416; IntAct: EBI-16421063; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0042564;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0097718;
GO  GO:0005085;
GO  GO:0061676;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0044877;
GO  GO:0031267;
GO  GO:0051170;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0051292;
GO  GO:0006656;
GO  GO:0006606;
GO  GO:0006612;
GO  GO:0046822;
GO  GO:0060188;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTAEFAQLLENSILSPDQNIRLTSETQLKKLSNDNFLQFAGLSSQVLIDENTKLEGRILAALTLKNELVSKDSVKTQQF
SQ  AQRWITQVSPEAKNQIKTNALTALVSIEPRIANAAAQLIAAIADIELPHGAWPELMKIMVDNTGAEQPENVKRASLLALG
SQ  YMCESADPQSQALVSSSNNILIAIVQGAQSTETSKAVRLAALNALADSLIFIKNNMEREGERNYLMQVVCEATQAEDIEV
SQ  QAAAFGCLCKIMSLYYTFMKPYMEQALYALTIATMKSPNDKVASMTVEFWSTICEEEIDIAYELAQFPQSPLQSYNFALS
SQ  SIKDVVPNLLNLLTRQNEDPEDDDWNVSMSAGACLQLFAQNCGNHILEPVLEFVEQNITADNWRNREAAVMAFGSIMDGP
SQ  DKVQRTYYVHQALPSILNLMNDQSLQVKETTAWCIGRIADSVAESIDPQQHLPGVVQACLIGLQDHPKVATNCSWTIINL
SQ  VEQLAEATPSPIYNFYPALVDGLIGAANRIDNEFNARASAFSALTTMVEYATDTVAETSASISTFVMDKLGQTMSVDENQ
SQ  LTLEDAQSLQELQSNILTVLAAVIRKSPSSVEPVADMLMGLFFRLLEKKDSAFIEDDVFYAISALAASLGKGFEKYLETF
SQ  SPYLLKALNQVDSPVSITAVGFIADISNSLEEDFRRYSDAMMNVLAQMISNPNARRELKPAVLSVFGDIASNIGADFIPY
SQ  LNDIMALCVAAQNTKPENGTLEALDYQIKVLEAVLDAYVGIVAGLHDKPEALFPYVGTIFQFIAQVAEDPQLYSEDATSR
SQ  AAVGLIGDIAAMFPDGSIKQFYGQDWVIDYIKRTRSGQLFSQATKDTARWAREQQKRQLSL
//
ID  O14089;
PN  Importin subunit beta-2;
GN  kap104;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O14089;
DE  Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for arginine/glycine-rich nuclear localization signals (rg-NLS) and PY-NLS in cargo substrates. Its predominant cargo substrate seems to be mRNA-binding proteins. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000250|UniProtKB:P38217}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:1990023;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0005525;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0051028;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDNPWVLQEQVLVELSEVIKNSLSENSQTRNAALNLLEKAKDIPDLNNYLTCILINATELSVSIRSAAGLLLKNNVRVS
SQ  SLESGSGLQSLDYTKSTVIRGLCDPEQLIRGISGNVITTIISRWGISTWPEVLPQLMEMLSSPASTTQEGAFSALTKICE
SQ  DSAQELDRDFNGTRPLDFMIPRFIELARHENPKIRTDALFCLNQFVLIQSQSLYAHIDTFLETCYALATDVSPNVRKNVC
SQ  QALVYLLDVRPDKIAPSLGSIVEYMLYSTQDSDQNVALEACEFWLAIAEQPDLCSALGPYLDKIVPMLLQGMVYSDMDLL
SQ  LLGNDADDYDVEDREEDIRPQHAKGKSRITLNTQGPITQQGSSNADADELEDEDEDDDEFDEDDDAFMDWNLRKCSAAAL
SQ  DVLSSFWKQRLLEIILPHLKQSLTSEDWKVQEAGVLAVGAIAEGCMDGMVQYLPELYPYFLSLLDSKKPLVRTITCWTLG
SQ  RYSKWASCLESEEDRQKYFVPLLQGLLRMVVDNNKKVQEAGCSAFAILEEQAGPSLVPYLEPILTNLAFAFQKYQRKNVL
SQ  ILYDAVQTLADYVGSALNDKRYIELLITPLLQKWSMIPDDDPNLFPLFECLSSVAVALRDGFAPFAAETYARTFRILRNT
SQ  LYLITTAQNDPTVDVPDRDFLVTTLDLVSGIIQALGSQVSPLLAQADPPLGQIIGICAKDEVPEVRQSAYALLGDMCMYC
SQ  FDQIRPYCDALLVDMLPQMQLPLLHVSASNNAIWSAGEMALQLGKDMQQWVKPLLERLICILKSKKSNTTVLENVAITIG
SQ  RLGVYNPELVAPHLELFYQPWFEIIKTVGENEEKDSAFRGFCNILACNPQALSYLLPMFVLCVAEYENPSAELRDMFQKI
SQ  LQGSVELFNGKASWQASPEVLAQIQAQYGV
//
ID  P38217;
PN  Importin subunit beta-2;
GN  KAP104;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:8849456}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:8849456}. Nucleus {ECO:0000269|PubMed:8849456}. Note=Predominantly cytoplasmic. {ECO:0000269|PubMed:8849456}.
DR  UNIPROT: P38217;
DR  UNIPROT: D6VQ19;
DR  Pfam: PF02985;
DE  Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for arginine/glycine-rich nuclear localization signals (rg-NLS) and PY-NLS in cargo substrates. Its predominant cargo substrate seems to be mRNA-binding proteins. Required for nuclear transport of NAB2, HRP1/NAB4 and TFG2. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins (PubMed:8849456, PubMed:9488461, PubMed:10506153, PubMed:19366694). The complex is subsequently translocated through the pore by an energy requiring, Ran- dependent mechanism (PubMed:11423015). At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. Efficient GTP-Ran- mediated substrate release requires RNA (PubMed:10506153). The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015). {ECO:0000269|PubMed:10506153, ECO:0000269|PubMed:19366694, ECO:0000269|PubMed:8849456, ECO:0000269|PubMed:9488461, ECO:0000305|PubMed:11423015}.
DE  Reference Proteome: Yes;
DE  Interaction: P22147; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P25491; IntAct: EBI-3663671; Score: 0.35
DE  Interaction: P53755; IntAct: EBI-390534; Score: 0.37
DE  Interaction: P28004; IntAct: EBI-393432; Score: 0.37
DE  Interaction: P32505; IntAct: EBI-7096661; Score: 0.85
DE  Interaction: P23641; IntAct: EBI-787315; Score: 0.53
DE  Interaction: Q99190; IntAct: EBI-787497; Score: 0.35
DE  Interaction: P18414; IntAct: EBI-787591; Score: 0.35
DE  Interaction: P50085; IntAct: EBI-789689; Score: 0.35
DE  Interaction: P53045; IntAct: EBI-790631; Score: 0.35
DE  Interaction: P04840; IntAct: EBI-793754; Score: 0.35
DE  Interaction: P53217; IntAct: EBI-795519; Score: 0.35
DE  Interaction: Q04182; IntAct: EBI-802063; Score: 0.35
DE  Interaction: P40035; IntAct: EBI-805054; Score: 0.35
DE  Interaction: P40970; IntAct: EBI-805812; Score: 0.35
DE  Interaction: P32340; IntAct: EBI-807081; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-810745; Score: 0.53
DE  Interaction: P07259; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-810745; Score: 0.53
DE  Interaction: P09733; IntAct: EBI-810745; Score: 0.53
DE  Interaction: P02994; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P05753; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P05756; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P46654; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P05317; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P26321; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P17079; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P40069; IntAct: EBI-810745; Score: 0.35
DE  Interaction: Q99383; IntAct: EBI-810745; Score: 0.74
DE  Interaction: P33892; IntAct: EBI-810745; Score: 0.44
DE  Interaction: P38737; IntAct: EBI-810745; Score: 0.44
DE  Interaction: Q03690; IntAct: EBI-810745; Score: 0.44
DE  Interaction: P19414; IntAct: EBI-819157; Score: 0.27
DE  Interaction: P37898; IntAct: EBI-819689; Score: 0.27
DE  Interaction: Q06417; IntAct: EBI-7172788; Score: 0.40
DE  Interaction: P46367; IntAct: EBI-7211426; Score: 0.59
DE  Interaction: P05755; IntAct: EBI-7381628; Score: 0.40
DE  Interaction: P25303; IntAct: EBI-3659291; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3726134; Score: 0.35
DE  Interaction: P46988; IntAct: EBI-3737859; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3745075; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3752383; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3780543; Score: 0.53
DE  Interaction: P40150; IntAct: EBI-3798846; Score: 0.35
DE  Interaction: Q00916; IntAct: EBI-15707559; Score: 0.44
DE  Interaction: P04821; IntAct: EBI-15707580; Score: 0.44
DE  Interaction: Q03497; IntAct: EBI-15707601; Score: 0.44
DE  Interaction: P53919; IntAct: EBI-15707664; Score: 0.44
DE  Interaction: P10080; IntAct: EBI-15707685; Score: 0.44
DE  Interaction: P52272; IntAct: EBI-15707706; Score: 0.44
DE  Interaction: P41896; IntAct: EBI-15707727; Score: 0.59
DE  Interaction: P09232; IntAct: EBI-15707748; Score: 0.44
DE  Interaction: Q03063; IntAct: EBI-15707769; Score: 0.44
DE  Interaction: P32611; IntAct: EBI-15707811; Score: 0.44
DE  Interaction: P35637; IntAct: EBI-15707790; Score: 0.44
DE  Interaction: P38333; IntAct: EBI-15707890; Score: 0.59
DE  Interaction: Q12386; IntAct: EBI-15707911; Score: 0.44
DE  Interaction: P04173; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P41920; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P53962; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P40215; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P36139; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P38708; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: Q04013; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: Q12447; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: Q12443; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: Q07395; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P32610; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P07806; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P28274; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P09734; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P00358; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P00360; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P0CS90; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P09435; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P32368; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: Q03940; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P53549; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P33298; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P39006; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P05030; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P37012; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P12709; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P18239; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P32332; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P33201; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P39692; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P38130; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P06168; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P07342; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P28834; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P04806; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P04912; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P19882; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P15992; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P16622; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P32836; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P32835; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P14742; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P07262; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P28007; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P04397; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P14540; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P30624; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P00924; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P04802; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P41819; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P07253; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P29311; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P15703; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P40471; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P07251; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P08566; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P46672; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P07248; IntAct: EBI-16271726; Score: 0.35
DE  Interaction: P10127; IntAct: EBI-16271726; Score: 0.35
GO  GO:0005935;
GO  GO:0005934;
GO  GO:0005829;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0010458;
GO  GO:0051028;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASTWKPAEDYVLQLATLLQNCMSPNPEIRNNAMEAMENFQLQPEFLNYLCYILIEGESDDVLKQHYSLQDLQNNRATAG
SQ  MLLKNSMLGGNNLIKSNSHDLGYVKSNIIHGLYNSNNNLVSNVTGIVITTLFSTYYRQHRDDPTGLQMLYQLLELTSNGN
SQ  EPSIKALSKIMEDSAQFFQLEWSGNTKPMEALLDSFFRFISNPNFSPVIRSESVKCINTVIPLQTQSFIVRLDKFLEIIF
SQ  QLAQNDENDLVRAQICISFSFLLEFRPDKLVSHLDGIVQFMLHLITTVNEEKVAIEACEFLHAFATSPNIPEHILQPYVK
SQ  DIVPILLSKMVYNEESIVLLEASNDDDAFLEDKDEDIKPIAPRIVKKKEAGNGEDADDNEDDDDDDDDEDGDVDTQWNLR
SQ  KCSAATLDVMTNILPHQVMDIAFPFLREHLGSDRWFIREATILALGAMAEGGMKYFNDGLPALIPFLVEQLNDKWAPVRK
SQ  MTCWTLSRFSPWILQDHTEFLIPVLEPIINTLMDKKKDVQEAAISSVAVFIENADSELVETLFYSQLLTSFDKCLKYYKK
SQ  KNLIILYDAIGRFAEKCALDETAMQIILPPLIEKWALLSDSDKELWPLLECLSCVASSLGERFMPMAPEVYNRAFRILCH
SQ  CVELEAKSHQDPTIVVPEKDFIITSLDLIDGLVQGLGAHSQDLLFPQGTKDLTILKIMLECLQDPVHEVRQSCFALLGDI
SQ  VYFFNSELVIGNLEDFLKLIGTEIMHNDDSDGTPAVINAIWALGLISERIDLNTYIIDMSRIILDLFTTNTQIVDSSVME
SQ  NLSVTIGKMGLTHPEVFSSGAFANDSNWNKWCLSVNALDDVEEKSSAYMGFLKIINLTSTEVTMSNDTIHKIVTGLSSNV
SQ  EANVFAQEIYTFLMNHSAQISAINFTPDEISFLQQFTS
//
ID  O74476;
PN  Importin subunit beta-3;
GN  sal3;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O74476;
DR  UNIPROT: Q9US74;
DR  Pfam: PF18808;
DR  Pfam: PF18816;
DR  Pfam: PF18829;
DE  Function: Involved in the nuclear import of cdc25 and mcs1. {ECO:0000269|PubMed:12399381}. Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Involved in the nuclear import of cdc25 and mcs1 (PubMed:12399381). Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250|UniProtKB:P32337, ECO:0000269|PubMed:12399381}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSGFPPEVLSPLLNLVQGLSSPDNTVRNDAEKSLSSDWISQRADLLLNGLAILAYQSEDPAVRSFCLVLCRRISFRTLP
SQ  GDSELEVFSSISNESKQSLQSQLLACFVKESVPTVRNKLCDTIAEIARSIYDCQGEWPELINVIFNAVNSPDESFRESVF
SQ  RTITSLPRLLSGQDSAVTPLFTTGLADPSIRVRISAARAYSAVILESKQSTRDQVIPLLPSLMNILPPLQQDRDSDNLAD
SQ  CLMAITEIAEVFPKLFKPIFESVIAFGLGIIKDKELDNSARQAALELLVCFSEGAPAMCRKSSDYTDQLVLQCLLLMTDV
SQ  AGDPEDEAEELQEWLNTDDLDQDESDANHVVAEQAMDRLSRKLGGKTILPPSFTWLPRLIPSQKWSERHAALMAISSIAE
SQ  GAEKLMKKELSRVLDMVLPLLADPHPRVRWAACNAVGQMSTDFAPDMQVKYPSRILEALVPVLESPESRVQAHAAAAMVN
SQ  FSEEADNKVLEPYLDDILQRLLTLLQSPKRYVQEQAVTTIATVADAAAKKFEKYFDAIMPLLFNVLQQADGKEFRTLRGK
SQ  TMECATLIALAVGKQRFLPVSQELIQILGNIQMGITDSDDPQASYLISAWGRICRVLGSDFVPFLSSVMPPLLVAATSKP
SQ  DFTIIDDEVDESKYSEQDGWEFIPVHGQQVGIRTSTLEDKCTATEMLVCYAAELKADFDPYVNEVLTSVVLPGLKFFFHD
SQ  GVRSACCKCIPQLLNARILASNRDPAKVNELWEPILRKLLDHIQNEPSVEMLADYFECFYQSLEISGLNLSPSSMEALVA
SQ  AVDLQLKGFISRVQQREEEAKNGDIDIEEDEDMILAVENDQNLLNEINKTFSVVLKIHKTAFCPFWERLLPYMDGFLSGN
SQ  DTVAKQWALCMMDDLIEFTGPDSWNYKDHFLPYLAEGIQSSEPEIRQAASYGIGVAAQHGGELYAEICSSALPALFKMLE
SQ  LPDARDEEQIYATENICVAICKICRFCSQRVQDLDKVVTYWINTLPVTHDEDDAPYAYTFLAELMEQNHVAVASQMPTII
SQ  TILAETFASGVLRGRTLTRLMEASKVYLARFPADQVNSVIATLSVDNQRALSAHF
//
ID  O60100;
PN  Probable importin subunit beta-4;
GN  kap123;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus. Nucleus envelope.
DR  UNIPROT: O60100;
DR  UNIPROT: Q9US72;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Required for nuclear protein import, its predominant substrate seems to be ribosomal proteins. Binds to nucleoporins and the GTP-bound form of gsp1 (Ran) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: O59793; IntAct: EBI-1560588; Score: 0.37
DE  Interaction: Q9USJ7; IntAct: EBI-15921699; Score: 0.35
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0031267;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDAQFTLELTQLLFQSIAPDTTQITEATRALETKYLKEPGSLLSLFHIMGTCENPQVRQLAAIEARKLCHKYWSSVDADV
SQ  QNQIRSNLLDITLKEPESIVRHAFGRVIAALAKLDLPEGKWNELSAFLVQATMDQNDSIREMAVYVLYSIAETVDLDNKL
SQ  LLDFVNLFSQTITDSSRTVRVTSVQGLGAIAEVLESDDKKLLHAYRATLPGMLLVLQDVVQVGDVDASKQVFDVFNTFLI
SQ  ASGAIISKALGNIIEIITGIANSKQVDDEIRCMALSFIISCIRFKSRKLQALKLGKPLVLTLMEVATEETTDDIDEDCPA
SQ  RLALRSIDLLSTHLSPSQVFYPMFEAACAFSQSPQASYRKAALLSIGVAVEGSSESVAGNLPNIFPIIINGLCDNDMDVR
SQ  QAALLALSQIAVEIPTEVSKHHAQLLPLVFELMSTQGVKVGKSACNCIDALLEGLDKSEISGYLPMLMERLVGLLEFSDT
SQ  PDIKSCVAAAIGSAAFAAQDDFIPYFERTMASLSQCLHTTDDDEGYELRGTVMDTLGAIANAVGKQAFLPYTEQLIQLAY
SQ  EGIQIDHSRLRECSFCFYAVLARVYKEEFAPFLEHIVPALFKSIDQDESDILSERIGAPTAEEISQLLDSVETNEEENDE
SQ  ELEKAMGVNSAIAMEKEIAADALGEICMYVGAPFTPYLEPTVEKLVACTTHFYEGVRKSALSSLWRCATTYYKVCNVPQW
SQ  QPGLPLKVPVPDTVKNIFEAVRKCTFDTLEEEYEKTVATDILRNFAESIKTCGPVVLGDDYEKLCEVVMEVLQKQHIVQA
SQ  GDVFDDDFEEEDIVSNEEVDDTEQDALLIDSACDVVIALAVALGGSFADSFKVFYPQIVKYYMSKNGNERAMAVACVGEV
SQ  AGGIESAITPFTRDVFSLFMAALEDSEGEVRSNAAYSMGLLCQFSTEDLSSEYLNILQKLQPFFTQEVFRTALDNAIGCI
SQ  SRLILHNQNAIPVDQVLPIVFSKLPLKEDYLENAPLYHMILALYRQQNPCLVQHLGELIPVFASVLTGSPEQLNDELRSE
SQ  LLSMVKEIAPQYESVVSNYPQLVALLQ
//
ID  P40069;
PN  Importin subunit beta-4;
GN  KAP123;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:9238021, ECO:0000269|PubMed:9321403}. Nucleus {ECO:0000269|PubMed:9238021, ECO:0000269|PubMed:9321403}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:9321403}.
DR  UNIPROT: P40069;
DR  UNIPROT: D3DM16;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Its predominant cargo substrate seems to be ribosomal proteins (PubMed:9321403). Required for import of the ribosomal assembly factor NMD3 (PubMed:12612077). May be involved in nuclear transport of YAP1 (PubMed:11274141). Mediates the nuclear import of histones H3 and H4 (PubMed:11694505). Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11423015). At the nucleoplasmic side of the NPC, GTP- Ran binding leads to release of the cargo (PubMed:9321403). The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015). {ECO:0000269|PubMed:11274141, ECO:0000269|PubMed:12612077, ECO:0000269|PubMed:9321403, ECO:0000305|PubMed:11423015}.
DE  Reference Proteome: Yes;
DE  Interaction: P12683; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P12684; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P32499; IntAct: EBI-801825; Score: 0.35
DE  Interaction: P34077; IntAct: EBI-789044; Score: 0.35
DE  Interaction: P38217; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P38242; IntAct: EBI-804270; Score: 0.35
DE  Interaction: P39705; IntAct: EBI-810484; Score: 0.67
DE  Interaction: P39935; IntAct: EBI-7102517; Score: 0.40
DE  Interaction: P38720; IntAct: EBI-738927; Score: 0.35
DE  Interaction: Q06142; IntAct: EBI-784458; Score: 0.35
DE  Interaction: P33892; IntAct: EBI-784561; Score: 0.35
DE  Interaction: P40499; IntAct: EBI-784605; Score: 0.35
DE  Interaction: P16522; IntAct: EBI-784904; Score: 0.35
DE  Interaction: P53012; IntAct: EBI-784913; Score: 0.35
DE  Interaction: Q02785; IntAct: EBI-785248; Score: 0.35
DE  Interaction: P38310; IntAct: EBI-785385; Score: 0.35
DE  Interaction: P36013; IntAct: EBI-785404; Score: 0.35
DE  Interaction: P38085; IntAct: EBI-785720; Score: 0.35
DE  Interaction: P20107; IntAct: EBI-786095; Score: 0.35
DE  Interaction: P53742; IntAct: EBI-786111; Score: 0.35
DE  Interaction: P07262; IntAct: EBI-786325; Score: 0.35
DE  Interaction: P32454; IntAct: EBI-786482; Score: 0.35
DE  Interaction: P35723; IntAct: EBI-786542; Score: 0.35
DE  Interaction: P32905; IntAct: EBI-786584; Score: 0.53
DE  Interaction: P33441; IntAct: EBI-786653; Score: 0.35
DE  Interaction: P21147; IntAct: EBI-786767; Score: 0.35
DE  Interaction: P52910; IntAct: EBI-787020; Score: 0.35
DE  Interaction: P42842; IntAct: EBI-787059; Score: 0.53
DE  Interaction: P11075; IntAct: EBI-787105; Score: 0.35
DE  Interaction: P38152; IntAct: EBI-787191; Score: 0.35
DE  Interaction: Q99190; IntAct: EBI-787497; Score: 0.35
DE  Interaction: P32798; IntAct: EBI-787527; Score: 0.35
DE  Interaction: P18414; IntAct: EBI-787591; Score: 0.35
DE  Interaction: P40060; IntAct: EBI-787692; Score: 0.35
DE  Interaction: Q12029; IntAct: EBI-787943; Score: 0.35
DE  Interaction: Q04013; IntAct: EBI-787999; Score: 0.53
DE  Interaction: Q12345; IntAct: EBI-788466; Score: 0.35
DE  Interaction: P04840; IntAct: EBI-789381; Score: 0.53
DE  Interaction: P22211; IntAct: EBI-789829; Score: 0.35
DE  Interaction: P00546; IntAct: EBI-790005; Score: 0.35
DE  Interaction: P53045; IntAct: EBI-790631; Score: 0.35
DE  Interaction: P38719; IntAct: EBI-791466; Score: 0.53
DE  Interaction: P35191; IntAct: EBI-791750; Score: 0.35
DE  Interaction: P39743; IntAct: EBI-791998; Score: 0.53
DE  Interaction: P40541; IntAct: EBI-792117; Score: 0.35
DE  Interaction: P33333; IntAct: EBI-792539; Score: 0.35
DE  Interaction: P32476; IntAct: EBI-792746; Score: 0.35
DE  Interaction: P32467; IntAct: EBI-792844; Score: 0.35
DE  Interaction: P32803; IntAct: EBI-792992; Score: 0.35
DE  Interaction: P38853; IntAct: EBI-793202; Score: 0.35
DE  Interaction: P28496; IntAct: EBI-793629; Score: 0.35
DE  Interaction: P07279; IntAct: EBI-793825; Score: 0.35
DE  Interaction: P53965; IntAct: EBI-794192; Score: 0.35
DE  Interaction: Q06616; IntAct: EBI-794693; Score: 0.53
DE  Interaction: P36008; IntAct: EBI-794719; Score: 0.35
DE  Interaction: P53217; IntAct: EBI-795519; Score: 0.35
DE  Interaction: P39522; IntAct: EBI-796511; Score: 0.35
DE  Interaction: P48563; IntAct: EBI-796544; Score: 0.35
DE  Interaction: P40416; IntAct: EBI-796874; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-797068; Score: 0.35
DE  Interaction: P32629; IntAct: EBI-797496; Score: 0.35
DE  Interaction: P28003; IntAct: EBI-797693; Score: 0.63
DE  Interaction: Q07084; IntAct: EBI-797765; Score: 0.35
DE  Interaction: Q07804; IntAct: EBI-797939; Score: 0.35
DE  Interaction: P38707; IntAct: EBI-798527; Score: 0.35
DE  Interaction: P36148; IntAct: EBI-798681; Score: 0.35
DE  Interaction: P12385; IntAct: EBI-798708; Score: 0.35
DE  Interaction: P54837; IntAct: EBI-798956; Score: 0.35
DE  Interaction: P38703; IntAct: EBI-799064; Score: 0.35
DE  Interaction: P29496; IntAct: EBI-799159; Score: 0.35
DE  Interaction: Q07560; IntAct: EBI-799843; Score: 0.35
DE  Interaction: P16550; IntAct: EBI-799867; Score: 0.35
DE  Interaction: P38687; IntAct: EBI-800067; Score: 0.35
DE  Interaction: P23500; IntAct: EBI-800292; Score: 0.35
DE  Interaction: P05626; IntAct: EBI-800337; Score: 0.40
DE  Interaction: P53881; IntAct: EBI-800899; Score: 0.35
DE  Interaction: P02309; IntAct: EBI-801642; Score: 0.53
DE  Interaction: Q04182; IntAct: EBI-802063; Score: 0.35
DE  Interaction: Q02336; IntAct: EBI-802105; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-802128; Score: 0.35
DE  Interaction: P50108; IntAct: EBI-802587; Score: 0.53
DE  Interaction: P33748; IntAct: EBI-802616; Score: 0.35
DE  Interaction: P46985; IntAct: EBI-802682; Score: 0.35
DE  Interaction: P22202; IntAct: EBI-802717; Score: 0.35
DE  Interaction: P32903; IntAct: EBI-802959; Score: 0.35
DE  Interaction: P39704; IntAct: EBI-803225; Score: 0.35
DE  Interaction: P32843; IntAct: EBI-803607; Score: 0.35
DE  Interaction: P0CI39; IntAct: EBI-803823; Score: 0.35
DE  Interaction: Q12680; IntAct: EBI-804008; Score: 0.35
DE  Interaction: P22215; IntAct: EBI-804242; Score: 0.35
DE  Interaction: Q03771; IntAct: EBI-804362; Score: 0.35
DE  Interaction: Q02821; IntAct: EBI-804491; Score: 0.53
DE  Interaction: Q04305; IntAct: EBI-804878; Score: 0.35
DE  Interaction: P39969; IntAct: EBI-805048; Score: 0.35
DE  Interaction: P40035; IntAct: EBI-805054; Score: 0.35
DE  Interaction: Q12296; IntAct: EBI-805165; Score: 0.35
DE  Interaction: P40970; IntAct: EBI-805812; Score: 0.35
DE  Interaction: P38264; IntAct: EBI-806188; Score: 0.35
DE  Interaction: P39676; IntAct: EBI-806418; Score: 0.35
DE  Interaction: P25360; IntAct: EBI-806544; Score: 0.35
DE  Interaction: P35200; IntAct: EBI-806623; Score: 0.35
DE  Interaction: P39004; IntAct: EBI-806863; Score: 0.35
DE  Interaction: P40319; IntAct: EBI-807008; Score: 0.35
DE  Interaction: P32340; IntAct: EBI-807081; Score: 0.35
DE  Interaction: P39715; IntAct: EBI-807214; Score: 0.35
DE  Interaction: P07246; IntAct: EBI-807320; Score: 0.35
DE  Interaction: Q05881; IntAct: EBI-807421; Score: 0.35
DE  Interaction: P32502; IntAct: EBI-807537; Score: 0.35
DE  Interaction: Q12449; IntAct: EBI-807743; Score: 0.44
DE  Interaction: P25454; IntAct: EBI-807992; Score: 0.35
DE  Interaction: P21304; IntAct: EBI-808083; Score: 0.35
DE  Interaction: P46956; IntAct: EBI-808284; Score: 0.53
DE  Interaction: P13663; IntAct: EBI-808333; Score: 0.35
DE  Interaction: Q04062; IntAct: EBI-808625; Score: 0.35
DE  Interaction: P27929; IntAct: EBI-808974; Score: 0.35
DE  Interaction: P38689; IntAct: EBI-809021; Score: 0.35
DE  Interaction: P40081; IntAct: EBI-809045; Score: 0.35
DE  Interaction: P51998; IntAct: EBI-809221; Score: 0.35
DE  Interaction: P04451; IntAct: EBI-809374; Score: 0.35
DE  Interaction: P47054; IntAct: EBI-809765; Score: 0.35
DE  Interaction: P52593; IntAct: EBI-809801; Score: 0.35
DE  Interaction: Q03529; IntAct: EBI-810338; Score: 0.35
DE  Interaction: P32492; IntAct: EBI-810383; Score: 0.35
DE  Interaction: P38706; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P41805; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P40010; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P25605; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P28241; IntAct: EBI-810484; Score: 0.35
DE  Interaction: Q12159; IntAct: EBI-810484; Score: 0.53
DE  Interaction: P07259; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P10081; IntAct: EBI-810484; Score: 0.56
DE  Interaction: P02994; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-810484; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-810484; Score: 0.35
DE  Interaction: Q12464; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P26783; IntAct: EBI-810484; Score: 0.53
DE  Interaction: P05753; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P23248; IntAct: EBI-810484; Score: 0.53
DE  Interaction: P33442; IntAct: EBI-810484; Score: 0.53
DE  Interaction: P35271; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P26781; IntAct: EBI-810484; Score: 0.35
DE  Interaction: P32566; IntAct: EBI-811327; Score: 0.35
DE  Interaction: P39011; IntAct: EBI-811463; Score: 0.35
DE  Interaction: P19262; IntAct: EBI-812031; Score: 0.35
DE  Interaction: Q06338; IntAct: EBI-812996; Score: 0.27
DE  Interaction: P18239; IntAct: EBI-816585; Score: 0.51
DE  Interaction: P54115; IntAct: EBI-819644; Score: 0.27
DE  Interaction: P36046; IntAct: EBI-853469; Score: 0.35
DE  Interaction: Q02776; IntAct: EBI-853768; Score: 0.35
DE  Interaction: P47077; IntAct: EBI-854045; Score: 0.35
DE  Interaction: P47026; IntAct: EBI-854100; Score: 0.35
DE  Interaction: P0CG63; IntAct: EBI-7480729; Score: 0.44
DE  Interaction: A0A023PZH5; IntAct: EBI-7178717; Score: 0.40
DE  Interaction: P53921; IntAct: EBI-7182619; Score: 0.40
DE  Interaction: Q08204; IntAct: EBI-7707649; Score: 0.40
DE  Interaction: P38789; IntAct: EBI-7763954; Score: 0.40
DE  Interaction: P36100; IntAct: EBI-7778406; Score: 0.40
DE  Interaction: Q05050; IntAct: EBI-8090720; Score: 0.40
DE  Interaction: P38692; IntAct: EBI-2610613; Score: 0.35
DE  Interaction: P32790; IntAct: EBI-7513567; Score: 0.37
DE  Interaction: P61830; IntAct: EBI-2884222; Score: 0.00
DE  Interaction: P04912; IntAct: EBI-2884694; Score: 0.00
DE  Interaction: Q12692; IntAct: EBI-2885248; Score: 0.00
DE  Interaction: Q12529; IntAct: EBI-2887496; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P46675; IntAct: EBI-2888241; Score: 0.00
DE  Interaction: P40340; IntAct: EBI-2889086; Score: 0.00
DE  Interaction: P52919; IntAct: EBI-7042905; Score: 0.63
DE  Interaction: B5VKC0; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P0CX39; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P23641; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P32332; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P40075; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P39926; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P38555; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P21560; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P17076; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P18238; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P47124; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P38130; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: Q04947; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: Q12690; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P25087; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P32835; IntAct: EBI-6472517; Score: 0.44
DE  Interaction: P10591; IntAct: EBI-6556984; Score: 0.35
DE  Interaction: P38316; IntAct: EBI-16263556; Score: 0.35
DE  Interaction: Q00776; IntAct: EBI-16263794; Score: 0.35
DE  Interaction: P38153; IntAct: EBI-16263895; Score: 0.35
DE  Interaction: Q00684; IntAct: EBI-16265633; Score: 0.35
DE  Interaction: P27636; IntAct: EBI-16265722; Score: 0.35
DE  Interaction: P32562; IntAct: EBI-16266124; Score: 0.35
DE  Interaction: P32601; IntAct: EBI-16268457; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-16268890; Score: 0.35
DE  Interaction: P06774; IntAct: EBI-16270452; Score: 0.35
DE  Interaction: Q08273; IntAct: EBI-16271112; Score: 0.35
DE  Interaction: P42838; IntAct: EBI-16272625; Score: 0.35
DE  Interaction: P23748; IntAct: EBI-16273845; Score: 0.35
DE  Interaction: Q04149; IntAct: EBI-16274423; Score: 0.35
DE  Interaction: P27801; IntAct: EBI-16275426; Score: 0.35
DE  Interaction: Q12223; IntAct: EBI-16278796; Score: 0.35
DE  Interaction: P40348; IntAct: EBI-16279429; Score: 0.35
DE  Interaction: P25343; IntAct: EBI-16281060; Score: 0.35
DE  Interaction: P08458; IntAct: EBI-16283853; Score: 0.35
DE  Interaction: P06245; IntAct: EBI-16285493; Score: 0.35
DE  Interaction: P33296; IntAct: EBI-16286005; Score: 0.35
DE  Interaction: Q12063; IntAct: EBI-16287555; Score: 0.35
DE  Interaction: Q06668; IntAct: EBI-16288187; Score: 0.35
DE  Interaction: P53243; IntAct: EBI-16289027; Score: 0.35
DE  Interaction: P38885; IntAct: EBI-16289603; Score: 0.35
DE  Interaction: Q04437; IntAct: EBI-16290301; Score: 0.35
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0031267;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006606;
GO  GO:2000220;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDQQFLSQLEQTLHAITSGVGLKEATKTLQTQFYTQPTTLPALIHILQNGSDDSLKQLAGVEARKLVSKHWNAIDESTRA
SQ  SIKTSLLQTAFSEPKENVRHSNARVIASIGTEELDGNKWPDLVPNLIQTASGEDVQTRQTAIFILFSLLEDFTSSLSGHI
SQ  DDFLALFSQTINDPSSLEIRSLSAQALNHVSALIEEQETINPVQAQKFAASIPSVVNVLDAVIKADDTMNAKLIFNCLND
SQ  FLLLDSQLTGNFIVDLIKLSLQIAVNSEIDEDVRVFALQFIISSLSYRKSKVSQSKLGPEITVAALKVACEEIDVDDELN
SQ  NEDETGENEENTPSSSAIRLLAFASSELPPSQVASVIVEHIPAMLQSANVFERRAILLAISVAVTGSPDYILSQFDKIIP
SQ  ATINGLKDTEPIVKLAALKCIHQLTTDLQDEVAKFHEEYLPLIIDIIDSAKNIVIYNYATVALDGLLEFIAYDAIAKYLD
SQ  PLMNKLFYMLESNESSKLRCAVVSAIGSAAFAAGSAFIPYFKTSVHYLEKFIQNCSQIEGMSEDDIELRANTFENISTMA
SQ  RAVRSDAFAEFAEPLVNSAYEAIKTDSARLRESGYAFIANLAKVYGENFAPFLKTILPEIFKTLELDEYQFNFDGDAEDL
SQ  AAFADSANEEELQNKFTVNTGISYEKEVASAALSELALGTKEHFLPYVEQSLKVLNEQVDESYGLRETALNTIWNVVKSV
SQ  LLASKVEPESYPKGIPASSYVNADVLAVIQAARETSMGNLSDEFETSMVITVMEDFANMIKQFGAIIIMDNGDSSMLEAL
SQ  CMQVLSVLKGTHTCQTIDIEEDVPRDEELDASETEATLQDVALEVLVSLSQALAGDFAKVFDNFRPVVFGLFQSKSKNKR
SQ  SSAVGAASELALGMKEQNPFVHEMLEALVIRLTSDKSLEVRGNAAYGVGLLCEYASMDISAVYEPVLKALYELLSAADQK
SQ  ALAAEDDEATREIIDRAYANASGCVARMALKNSALVPLEQTVPALLAHLPLNTGFEEYNPIFELIMKLYQENSPVITNET
SQ  PRIIEIFSAVFTKENDRIKLEKESTLGREENMERLKQFQTEEMKHKVIELLKYLNTTYNGIVAQNPVLAAVIA
//
ID  P53067;
PN  Importin subunit beta-5;
GN  KAP114;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: P53067;
DR  UNIPROT: D6VV94;
DR  PDB: 6AHO;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of TATA- binding protein (TBP) and of histones H2A and H2B. {ECO:0000269|PubMed:10535958, ECO:0000269|PubMed:11309407}.
DE  Reference Proteome: Yes;
DE  Interaction: P02294; IntAct: EBI-784971; Score: 0.56
DE  Interaction: P02293; IntAct: EBI-785273; Score: 0.56
DE  Interaction: P25293; IntAct: EBI-786460; Score: 0.56
DE  Interaction: P16140; IntAct: EBI-788245; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-788245; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-788245; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-788245; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-788245; Score: 0.53
DE  Interaction: P41940; IntAct: EBI-788245; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-788245; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-788245; Score: 0.35
DE  Interaction: P25635; IntAct: EBI-789783; Score: 0.35
DE  Interaction: P13393; IntAct: EBI-794073; Score: 0.53
DE  Interaction: P04912; IntAct: EBI-798033; Score: 0.67
DE  Interaction: P12709; IntAct: EBI-814094; Score: 0.27
DE  Interaction: Q02486; IntAct: EBI-814861; Score: 0.27
DE  Interaction: P49956; IntAct: EBI-820231; Score: 0.27
DE  Interaction: Q02159; IntAct: EBI-860968; Score: 0.00
DE  Interaction: P04911; IntAct: EBI-7349861; Score: 0.67
DE  Interaction: Q12692; IntAct: EBI-7359795; Score: 0.67
DE  Interaction: Q12263; IntAct: EBI-8225543; Score: 0.22
DE  Interaction: P32589; IntAct: EBI-3726142; Score: 0.35
DE  Interaction: P46988; IntAct: EBI-3737867; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3745083; Score: 0.35
DE  Interaction: P38910; IntAct: EBI-3751879; Score: 0.35
DE  Interaction: P38632; IntAct: EBI-7841763; Score: 0.53
DE  Interaction: P29055; IntAct: EBI-7841797; Score: 0.35
DE  Interaction: P32835; IntAct: EBI-7841853; Score: 0.58
DE  Interaction: P52488; IntAct: EBI-7841966; Score: 0.37
DE  Interaction: Q06624; IntAct: EBI-7841897; Score: 0.37
DE  Interaction: Q04195; IntAct: EBI-7841984; Score: 0.37
DE  Interaction: Q03048; IntAct: EBI-16267314; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0031267;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDINELIIGAQSADKHTREVAETQLLQWCDSDASQVFKALANVALQHEASLESRQFALLSLRKLITMYWSPGFESYRSTS
SQ  NVEIDVKDFIREVLLKLCLNDNENTKIKNGASYCIVQISAVDFPDQWPQLLTVIYDAISHQHSLNAMSLLNEIYDDVVSE
SQ  EMFFEGGIGLATMEIVFKVLNTETSTLIAKIAALKLLKACLLQMSSHNEYDEASRKSFVSQCLATSLQILGQLLTLNFGN
SQ  VDVISQLKFKSIIYENLVFIKNDFSRKHFSSELQKQFKIMAIQDLENVTHINANVETTESEPLLETVHDCSIYIVEFLTS
SQ  VCTLQFSVEEMNKIITSLTILCQLSSETREIWTSDFNTFVSKETGLAASYNVRDQANEFFTSLPNPQLSLIFKVVSNDIE
SQ  HSTCNYSTLESLLYLLQCILLNDDEITGENIDQSLQILIKTLENILVSQEIPELILARAILTIPRVLDKFIDALPDIKPL
SQ  TSAFLAKSLNLALKSDKELIKSATLIAFTYYCYFAELDSVLGPEVCSETQEKVIRIINQVSSDAEEDTNGALMEVLSQVI
SQ  SYNPKEPHSRKEILQAEFHLVFTISSEDPANVQVVVQSQECLEKLLDNINMDNYKNYIELCLPSFINVLDSNNANNYRYS
SQ  PLLSLVLEFITVFLKKKPNDGFLPDEINQYLFEPLAKVLAFSTEDETLQLATEAFSYLIFNTDTRAMEPRLMDIMKVLER
SQ  LLSLEVSDSAAMNVGPLVVAIFTRFSKEIQPLIGRILEAVVVRLIKTQNISTEQNLLSVLCFLTCNDPKQTVDFLSSFQI
SQ  DNTDALTLVMRKWIEAFEVIRGEKRIKENIVALSNLFFLNDKRLQKVVVNGNLIPYEGDLIITRSMAKKMPDRYVQVPLY
SQ  TKIIKLFVSELSFQSKQPNPEQLITSDIKQEVVNANKDDDNDDWEDVDDVLDYDKLKEYIDDDVDEEADDDSDDITGLMD
SQ  VKESVVQLLVRFFKEVASKDVSGFHCIYETLSDSERKVLSEALL
//
ID  P52297;
PN  Importin subunit beta;
GN  kpnb1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q14974}. Nucleus envelope {ECO:0000250|UniProtKB:Q14974}.
DR  UNIPROT: P52297;
DR  UNIPROT: B0LM40;
DR  Pfam: PF03810;
DR  PROSITE: PS50077;
DR  PROSITE: PS50166;
DE  Function: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. {ECO:0000269|PubMed:7878057}.
DE  Reference Proteome: Yes;
DE  Interaction: P20676; IntAct: EBI-6285121; Score: 0.44
DE  Interaction: P70012; IntAct: EBI-7780729; Score: 0.44
DE  Interaction: P62826; IntAct: EBI-286729; Score: 0.35
DE  Interaction: Q7ZZY7; IntAct: EBI-618939; Score: 0.63
DE  Interaction: Q5EWX9; IntAct: EBI-8070373; Score: 0.50
DE  Interaction: A5XAW2; IntAct: EBI-3511241; Score: 0.35
DE  Interaction: A0A1L8G4G8; IntAct: EBI-3645151; Score: 0.35
DE  Interaction: Q6PAY1; IntAct: EBI-6285093; Score: 0.35
DE  Interaction: Q91349; IntAct: EBI-6285081; Score: 0.35
DE  Interaction: Q6DCP4; IntAct: EBI-6285109; Score: 0.44
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031267;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELVTILEKTVSPDRNELEAAQKFLEQAAVENLPTFVVELSKVLANPANSQVARVAAGLQIKNPLTSRDPDVKAQYQQRW
SQ  LAIDASARGEIKTYVLRTLGTESYRPSSASQCVAGIACAEITVNQWPQLIPQLVANVTDPNSTERMKESTLEAIGYICQD
SQ  IDPEQLQHKSNEILTAIIQGMRKEEPSNNVRLAATNALLNSLEFTKANFDKESERHYIMQVVCEATQCPDTRVRVAALQN
SQ  LVKIMSLYYQYMETYMGPALFAITVEAMKNEIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQ
SQ  YLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPESC
SQ  QLKPLVIQAMPTLIELMKDPSVVVRDTTAWTVGRICELLPEAAINDVYLAPLLQCLIEGLGAEPRVASNVCWAFSSLAEA
SQ  AYEAADVADDQEEPSSYCLSSSFEVIVQKLLETTDRPDGHQNNLRSAAYEALMEIVKNSAKDCYPAVQKTTLVIMERLQQ
SQ  VLQVESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLG
SQ  AEFLKYMEAFKPFLTIGLKNYAEYQVCLAAVGLVGDLCRALQSNILPFCDEMMQFLLENLGNENVHRSVKPQILSVFGDV
SQ  ALAIGGEFKKYLDVVLNTLQQASQAQVDKSDYDMVDYLNELREGCIEAYTGIIQGLKGDQENVHPDVMLVQPRVEFILSF
SQ  IDHIAGDEDHTDSVVACGAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKTKTLATWATKELRKLKNQA
//
ID  Q96321;
PN  Importin subunit alpha-1;
GN  IMPA1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:8776900}.
DR  UNIPROT: Q96321;
DR  UNIPROT: O49599;
DR  UNIPROT: O81520;
DR  UNIPROT: Q940R6;
DR  UNIPROT: Q9C841;
DR  UNIPROT: Q9ZRI5;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Binds to conventional NLS motifs with high affinity in the absence of an importin beta subunit. Mediates nuclear protein import across the nuclear envelope in vitro in the absence of exogenously added importin beta subunit (PubMed:10428841). Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation (PubMed:18836040). {ECO:0000269|PubMed:10428841, ECO:0000269|PubMed:18836040}.
DE  Reference Proteome: Yes;
DE  Interaction: Q94CL9; IntAct: EBI-2131462; Score: 0.00
DE  Interaction: Q9FNY0; IntAct: EBI-2651578; Score: 0.00
DE  Interaction: Q9SCR2; IntAct: EBI-2651636; Score: 0.00
DE  Interaction: F4KAB8; IntAct: EBI-2651692; Score: 0.00
DE  Interaction: Q9SGE2; IntAct: EBI-2651779; Score: 0.00
DE  Interaction: Q29Q81; IntAct: EBI-2651808; Score: 0.00
DE  Interaction: Q9SAD3; IntAct: EBI-2651816; Score: 0.00
DE  Interaction: Q8GX29; IntAct: EBI-4496832; Score: 0.37
DE  Interaction: A2RVU4; IntAct: EBI-4510528; Score: 0.37
DE  Interaction: O22286; IntAct: EBI-4510536; Score: 0.37
DE  Interaction: O22768; IntAct: EBI-4510544; Score: 0.37
DE  Interaction: O22798; IntAct: EBI-4510552; Score: 0.37
DE  Interaction: O64645; IntAct: EBI-4510560; Score: 0.37
DE  Interaction: O65282; IntAct: EBI-4510568; Score: 0.37
DE  Interaction: O65555; IntAct: EBI-4510576; Score: 0.37
DE  Interaction: O80837; IntAct: EBI-4510584; Score: 0.37
DE  Interaction: O81439; IntAct: EBI-4510592; Score: 0.37
DE  Interaction: P49678; IntAct: EBI-4510600; Score: 0.37
DE  Interaction: Q00218; IntAct: EBI-4510608; Score: 0.37
DE  Interaction: Q05466; IntAct: EBI-4510616; Score: 0.37
DE  Interaction: Q058P7; IntAct: EBI-4510624; Score: 0.37
DE  Interaction: Q2VWA2; IntAct: EBI-4510632; Score: 0.37
DE  Interaction: Q6NQ78; IntAct: EBI-4510640; Score: 0.37
DE  Interaction: Q8H1S2; IntAct: EBI-4510648; Score: 0.37
DE  Interaction: Q0WLB5; IntAct: EBI-4510656; Score: 0.37
DE  Interaction: Q8L866; IntAct: EBI-4510664; Score: 0.37
DE  Interaction: Q8LPR2; IntAct: EBI-4510672; Score: 0.37
DE  Interaction: Q8RWF8; IntAct: EBI-4510680; Score: 0.37
DE  Interaction: Q8RWK8; IntAct: EBI-4510688; Score: 0.37
DE  Interaction: Q8VY49; IntAct: EBI-4510696; Score: 0.37
DE  Interaction: Q8VZE5; IntAct: EBI-4510704; Score: 0.37
DE  Interaction: Q8VZL7; IntAct: EBI-4510712; Score: 0.37
DE  Interaction: Q93ZB7; IntAct: EBI-4510720; Score: 0.37
DE  Interaction: Q940I0; IntAct: EBI-4510728; Score: 0.37
DE  Interaction: Q94AF2; IntAct: EBI-4510736; Score: 0.37
DE  Interaction: Q94BU9; IntAct: EBI-4510744; Score: 0.37
DE  Interaction: Q94JQ3; IntAct: EBI-4510752; Score: 0.37
DE  Interaction: Q96292; IntAct: EBI-4510760; Score: 0.37
DE  Interaction: Q9ASW4; IntAct: EBI-4510768; Score: 0.37
DE  Interaction: Q9FKD7; IntAct: EBI-4510776; Score: 0.37
DE  Interaction: Q9FNN2; IntAct: EBI-4510784; Score: 0.37
DE  Interaction: Q9LU63; IntAct: EBI-4510792; Score: 0.37
DE  Interaction: Q9LUK6; IntAct: EBI-4510800; Score: 0.37
DE  Interaction: Q9STS3; IntAct: EBI-4510808; Score: 0.37
DE  Interaction: Q9SZZ4; IntAct: EBI-4510816; Score: 0.37
DE  Interaction: Q9LUA3; IntAct: EBI-4521560; Score: 0.37
DE  Interaction: Q9SIC8; IntAct: EBI-4527472; Score: 0.37
DE  Interaction: F8RP38; IntAct: EBI-6368593; Score: 0.58
DE  Interaction: O22467; IntAct: EBI-6673033; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0009505;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLRPNAKTEVRRNRYKVAVDAEEGRRRREDNMVEIRKSKREESLMKKRREGMQALQGFPSASAASVDKKLDSLKDMVAG
SQ  VWSDDPALQLESTTQFRKLLSIERSPPIEEVISAGVVPRFVEFLKKEDYPAIQFEAAWALTNIASGTSDHTKVVIDHNAV
SQ  PIFVQLLASPSDDVREQAVWALGNVAGDSPRCRDLVLGCGALLPLLNQLNEHAKLSMLRNATWTLSNFCRGKPQPHFDQV
SQ  KPALPALERLIHSDDEEVLTDACWALSYLSDGTNDKIQTVIQAGVVPKLVELLLHHSPSVLIPALRTVGNIVTGDDIQTQ
SQ  CVINSGALPCLANLLTQNHKKSIKKEACWTISNITAGNKDQIQTVVEANLISPLVSLLQNAEFDIKKEAAWAISNATSGG
SQ  SHDQIKYLVEQGCIKPLCDLLVCPDPRIITVCLEGLENILKVGEAEKNLGHTGDMNYYAQLIDDAEGLEKIENLQSHDNN
SQ  EIYEKAVKILETYWLEEEDDETQQPPGVDGSQAGFQFGGNQAPVPSGGFNFS
//
ID  F4JL11;
PN  Importin subunit alpha-2;
GN  IMPA2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
DR  UNIPROT: F4JL11;
DR  UNIPROT: O49600;
DR  UNIPROT: Q9ASV4;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation (PubMed:18836040). {ECO:0000250|UniProtKB:Q96321, ECO:0000269|PubMed:18836040}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9C9M7; IntAct: EBI-1253348; Score: 0.00
DE  Interaction: P24100; IntAct: EBI-2130952; Score: 0.00
DE  Interaction: O23249; IntAct: EBI-2131089; Score: 0.00
DE  Interaction: Q38819; IntAct: EBI-2131146; Score: 0.00
DE  Interaction: Q2V3B2; IntAct: EBI-2131275; Score: 0.00
DE  Interaction: Q9FNY0; IntAct: EBI-2131334; Score: 0.00
DE  Interaction: Q9SCR2; IntAct: EBI-2131413; Score: 0.00
DE  Interaction: Q8GYJ3; IntAct: EBI-2131443; Score: 0.00
DE  Interaction: Q94CL9; IntAct: EBI-2131462; Score: 0.00
DE  Interaction: Q9SGE2; IntAct: EBI-2131649; Score: 0.00
DE  Interaction: Q29Q81; IntAct: EBI-2131683; Score: 0.00
DE  Interaction: Q9SAD3; IntAct: EBI-2131691; Score: 0.00
DE  Interaction: Q9LDM4; IntAct: EBI-2651385; Score: 0.00
DE  Interaction: Q9FGQ7; IntAct: EBI-2651465; Score: 0.00
DE  Interaction: Q9FKB5; IntAct: EBI-2651644; Score: 0.00
DE  Interaction: F4KAB8; IntAct: EBI-2651692; Score: 0.00
DE  Interaction: Q8W4M7; IntAct: EBI-2651824; Score: 0.00
DE  Interaction: Q8GX29; IntAct: EBI-4496840; Score: 0.37
DE  Interaction: O22179; IntAct: EBI-4511048; Score: 0.37
DE  Interaction: O22703; IntAct: EBI-4511056; Score: 0.37
DE  Interaction: O49617; IntAct: EBI-4511064; Score: 0.37
DE  Interaction: O65154; IntAct: EBI-4511072; Score: 0.37
DE  Interaction: P46604; IntAct: EBI-4511080; Score: 0.37
DE  Interaction: P53492; IntAct: EBI-4511088; Score: 0.37
DE  Interaction: Q05466; IntAct: EBI-4511096; Score: 0.37
DE  Interaction: Q058P7; IntAct: EBI-4511104; Score: 0.37
DE  Interaction: Q2VWA2; IntAct: EBI-4511112; Score: 0.37
DE  Interaction: Q56XR0; IntAct: EBI-4511120; Score: 0.37
DE  Interaction: Q56YJ8; IntAct: EBI-4511128; Score: 0.37
DE  Interaction: Q6NQ78; IntAct: EBI-4511136; Score: 0.37
DE  Interaction: Q700E4; IntAct: EBI-4511144; Score: 0.37
DE  Interaction: Q84MB2; IntAct: EBI-4511152; Score: 0.37
DE  Interaction: Q8GYX3; IntAct: EBI-4511168; Score: 0.37
DE  Interaction: Q8H1S2; IntAct: EBI-4511176; Score: 0.37
DE  Interaction: Q8L622; IntAct: EBI-4511184; Score: 0.37
DE  Interaction: Q8L7G9; IntAct: EBI-4511192; Score: 0.37
DE  Interaction: Q8L7I1; IntAct: EBI-4511200; Score: 0.37
DE  Interaction: Q8L8N3; IntAct: EBI-4511208; Score: 0.37
DE  Interaction: Q8RWF8; IntAct: EBI-4511216; Score: 0.37
DE  Interaction: Q93WC7; IntAct: EBI-4511224; Score: 0.37
DE  Interaction: Q93ZB7; IntAct: EBI-4511232; Score: 0.37
DE  Interaction: Q940I0; IntAct: EBI-4511240; Score: 0.37
DE  Interaction: Q96331; IntAct: EBI-4511248; Score: 0.37
DE  Interaction: Q9C826; IntAct: EBI-4511256; Score: 0.37
DE  Interaction: Q9FMM4; IntAct: EBI-4511264; Score: 0.37
DE  Interaction: Q9FNN2; IntAct: EBI-4511272; Score: 0.37
DE  Interaction: Q9LT89; IntAct: EBI-4511280; Score: 0.37
DE  Interaction: Q9LU74; IntAct: EBI-4511288; Score: 0.37
DE  Interaction: Q9LUK6; IntAct: EBI-4511296; Score: 0.37
DE  Interaction: Q9M3B6; IntAct: EBI-4511304; Score: 0.37
DE  Interaction: Q9SIC8; IntAct: EBI-4511312; Score: 0.37
DE  Interaction: Q9SSQ8; IntAct: EBI-4511320; Score: 0.37
DE  Interaction: Q9SZZ4; IntAct: EBI-4511328; Score: 0.37
DE  Interaction: Q9ZUC2; IntAct: EBI-4511336; Score: 0.37
DE  Interaction: Q9C829; IntAct: EBI-4512448; Score: 0.37
DE  Interaction: Q9LUA3; IntAct: EBI-4521568; Score: 0.37
DE  Interaction: O22467; IntAct: EBI-6673033; Score: 0.35
DE  Interaction: Q8L9K1; IntAct: EBI-25516380; Score: 0.56
DE  Interaction: O23160; IntAct: EBI-25516282; Score: 0.56
DE  Interaction: P93830; IntAct: EBI-25516270; Score: 0.56
DE  Interaction: Q39101; IntAct: EBI-25517493; Score: 0.56
DE  Interaction: Q9LRH6; IntAct: EBI-25517475; Score: 0.56
DE  Interaction: Q8GY55; IntAct: EBI-25522338; Score: 0.56
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0009506;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLRPNAKTEVRRNRYKVAVDAEEGRRRREDNMVEIRKSKREESLQKKRREGLQANQLPQFAPSPVPASSTVEKKLESLP
SQ  AMVGGVWSDDRSLQLEATTQFRKLLSIERSPPIEEVIDAGVVPRFVEFLTREDYPQLQFEAAWALTNIASGTSENTKVVI
SQ  EHGAVPIFVQLLASQSDDVREQAVWALGNVAGDSPRCRDLVLGQGALIPLLSQLNEHAKLSMLRNATWTLSNFCRGKPQP
SQ  PFDQVRPALPALERLIHSTDEEVLTDACWALSYLSDGTNDKIQSVIEAGVVPRLVELLQHQSPSVLIPALRSIGNIVTGD
SQ  DLQTQCVISHGALLSLLSLLTHNHKKSIKKEACWTISNITAGNRDQIQAVCEAGLICPLVNLLQNAEFDIKKEAAWAISN
SQ  ATSGGSPDQIKYMVEQGVVKPLCDLLVCPDPRIITVCLEGLENILKVGEAEKVTGNTGDVNFYAQLIDDAEGLEKIENLQ
SQ  SHDNSEIYEKAVKILETYWLEEEDETLPPGDPSAQGFQFGGGNDAAVPPGGFNFQ
//
ID  O80480;
PN  Importin subunit alpha-4;
GN  IMPA4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
DR  UNIPROT: O80480;
DR  UNIPROT: F4HZG6;
DR  UNIPROT: O49602;
DR  UNIPROT: Q94KD4;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope. Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium and is essential for Agrobacterium-mediated root transformation. {ECO:0000269|PubMed:18836040}.
DE  Reference Proteome: Yes;
DE  Interaction: Q94CL9; IntAct: EBI-2131462; Score: 0.00
DE  Interaction: Q058P7; IntAct: EBI-4480696; Score: 0.53
DE  Interaction: Q8GUP4; IntAct: EBI-4496128; Score: 0.37
DE  Interaction: Q8GX29; IntAct: EBI-4496816; Score: 0.37
DE  Interaction: Q9LUA3; IntAct: EBI-4521544; Score: 0.37
DE  Interaction: Q9SIC8; IntAct: EBI-4527464; Score: 0.37
DE  Interaction: F8RP38; IntAct: EBI-6368758; Score: 0.37
DE  Interaction: A8VZX9; IntAct: EBI-6505219; Score: 0.37
DE  Interaction: Q9SZU7; IntAct: EBI-25530008; Score: 0.56
GO  GO:0005737;
GO  GO:0043657;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0080034;
GO  GO:0006607;
GO  GO:0030581;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLRPSTRAELRKKIYKTGVDADEARRRREDNLVEIRKNKREDSLLKKRREGMMLQQQLPLGAGLDGPQTAAAVEKRLEG
SQ  IPMMVQGVYSDDPQAQLEATTQFRKLLSIERSPPIDEVIKAGVIPRFVEFLGRHDHPQLQFEAAWALTNVASGTSDHTRV
SQ  VIEQGAVPIFVKLLTSASDDVREQAVWALGNVAGDSPNCRNLVLNYGALEPLLAQLNENSKLSMLRNATWTLSNFCRGKP
SQ  PTPFEQVKPALPILRQLIYLNDEEVLTDACWALSYLSDGPNDKIQAVIEAGVCPRLVELLGHQSPTVLIPALRTVGNIVT
SQ  GDDSQTQFIIESGVLPHLYNLLTQNHKKSIKKEACWTISNITAGNKLQIEAVVGAGIILPLVHLLQNAEFDIKKEAAWAI
SQ  SNATSGGSHEQIQYLVTQGCIKPLCDLLICPDPRIVTVCLEGLENILKVGEADKEMGLNSGVNLYAQIIEESDGLDKVEN
SQ  LQSHDNNEIYEKAVKILERYWAEEEEEQILQDGGNDNSQQAFNFGNNPAAPVGGFKFA
//
ID  Q9FJ09;
PN  Importin subunit alpha-5;
GN  IMPA5;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
DR  UNIPROT: Q9FJ09;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope. {ECO:0000250|UniProtKB:Q96321}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLRPSTKTEIRRIRYKVSVDAEEGRRRREDFLVEIRKSKRNENLMKKRRVKVLPPDYKLISNDPFESLLEIANMITGVF
SQ  SDDPSLQLEYTTRFRVVLSFDRSPPTDNVIKSGVVPRFVEFLKKDDNPKLQFEAAWALTNIASGASEHTKVVIDHGVVPL
SQ  FVQLLASPDDDVREQAIWGLGNVAGDSIQCRDFVLNSGAFIPLLHQLNNHATLSILRNATWTLSNFFRGKPSPPFDLVKH
SQ  VLPVLKRLVYSDDEQVLIDACWALSNLSDASNENIQSVIEAGVVPRLVELLQHASPVVLVPALRCIGNIVSGNSQQTHCV
SQ  INCGVLPVLADLLTQNHMRGIRREACWTISNITAGLEEQIQSVIDANLIPSLVNLAQHAEFDIKKEAIWAISNASVGGSP
SQ  NQIKYLVEQNCIKALCDILVCPDLRIILVSLGGLEMILIAGEVDKNLRDVNCYSQMIEDAEGLEKIENLQHHGNNEIYEK
SQ  AVKILQTYGLVEEDGRLVEEEDEGGDGCSHPEFQFDFSR
//
ID  Q9FWY7;
PN  Importin subunit alpha-6;
GN  IMPA6;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
DR  UNIPROT: Q9FWY7;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation (PubMed:18836040). {ECO:0000250|UniProtKB:Q96321, ECO:0000269|PubMed:18836040}.
DE  Reference Proteome: Yes;
DE  Interaction: Q058P7; IntAct: EBI-4489888; Score: 0.37
DE  Interaction: O22179; IntAct: EBI-4517240; Score: 0.37
DE  Interaction: O49629; IntAct: EBI-4517248; Score: 0.37
DE  Interaction: O65154; IntAct: EBI-4517256; Score: 0.37
DE  Interaction: O65282; IntAct: EBI-4517264; Score: 0.37
DE  Interaction: O80837; IntAct: EBI-4517272; Score: 0.37
DE  Interaction: O81439; IntAct: EBI-4517280; Score: 0.37
DE  Interaction: Q2VWA2; IntAct: EBI-4517296; Score: 0.37
DE  Interaction: Q56XR0; IntAct: EBI-4517304; Score: 0.37
DE  Interaction: Q6NQ78; IntAct: EBI-4517312; Score: 0.37
DE  Interaction: Q84K72; IntAct: EBI-4517320; Score: 0.37
DE  Interaction: Q8GTS1; IntAct: EBI-4517328; Score: 0.37
DE  Interaction: Q8GYX3; IntAct: EBI-4517336; Score: 0.37
DE  Interaction: Q8H1G0; IntAct: EBI-4517344; Score: 0.37
DE  Interaction: Q8L622; IntAct: EBI-4517352; Score: 0.37
DE  Interaction: F4JCU0; IntAct: EBI-4517360; Score: 0.37
DE  Interaction: Q93Z68; IntAct: EBI-4517368; Score: 0.37
DE  Interaction: Q941A1; IntAct: EBI-4517376; Score: 0.37
DE  Interaction: Q94AU9; IntAct: EBI-4517384; Score: 0.37
DE  Interaction: Q94BU9; IntAct: EBI-4517392; Score: 0.37
DE  Interaction: Q96331; IntAct: EBI-4517400; Score: 0.37
DE  Interaction: Q9C8P0; IntAct: EBI-4517408; Score: 0.37
DE  Interaction: Q9C9V2; IntAct: EBI-4517416; Score: 0.37
DE  Interaction: Q9FH13; IntAct: EBI-4517424; Score: 0.37
DE  Interaction: Q9FKD7; IntAct: EBI-4517432; Score: 0.37
DE  Interaction: Q9FNJ8; IntAct: EBI-4517440; Score: 0.37
DE  Interaction: Q9LIC7; IntAct: EBI-4517448; Score: 0.37
DE  Interaction: Q9LJG8; IntAct: EBI-4517456; Score: 0.37
DE  Interaction: Q9LU63; IntAct: EBI-4517464; Score: 0.37
DE  Interaction: Q9LUK6; IntAct: EBI-4517472; Score: 0.37
DE  Interaction: Q9M336; IntAct: EBI-4517480; Score: 0.37
DE  Interaction: Q9SIC8; IntAct: EBI-4517488; Score: 0.37
DE  Interaction: Q9SK33; IntAct: EBI-4517496; Score: 0.37
DE  Interaction: Q9SMP3; IntAct: EBI-4517504; Score: 0.37
DE  Interaction: Q9SUM2; IntAct: EBI-4517512; Score: 0.37
DE  Interaction: Q9SZE4; IntAct: EBI-4517520; Score: 0.37
DE  Interaction: Q9SZZ4; IntAct: EBI-4517528; Score: 0.37
DE  Interaction: F4IK01; IntAct: EBI-4517536; Score: 0.37
DE  Interaction: Q9ZW18; IntAct: EBI-4517544; Score: 0.37
DE  Interaction: Q9LMT0; IntAct: EBI-4520096; Score: 0.37
DE  Interaction: P93830; IntAct: EBI-25516088; Score: 0.56
DE  Interaction: Q39101; IntAct: EBI-25517401; Score: 0.56
DE  Interaction: O81313; IntAct: EBI-25520641; Score: 0.56
DE  Interaction: Q38830; IntAct: EBI-25521933; Score: 0.56
DE  Interaction: O82132; IntAct: EBI-25522255; Score: 0.56
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSYKPSAKTEVRRNRYKVSVDADEGRRRREDNMVEIRKNKREENLQKKRREGFNPSMASQPGQDFSSSLPTETRLENIQQ
SQ  MIAGVMSEDRDLQLEATASFRRLLSIERNPPINEVVQSGVVPHIVQFLSRDDFTQLQFEAAWALTNIASGTSENTRVIID
SQ  SGAVPLFVKLLSSASEEVREQAVWALGNVAGDSPKCRDHVLSCEAMMSLLAQFHEHSKLSMLRNATWTLSNFCRGKPQPA
SQ  FEQTKAALPALERLLHSTDEEVLTDASWALSYLSDGTNEKIQTVIDAGVIPRLVQLLAHPSPSVLIPALRTIGNIVTGDD
SQ  IQTQAVISSQALPGLLNLLKNTYKKSIKKEACWTISNITAGNTSQIQEVFQAGIIRPLINLLEIGEFEIKKEAVWAISNA
SQ  TSGGNHDQIKFLVSQGCIRPLCDLLPCPDPRVVTVTLEGLENILKVGEAEKNLGNTGNDNLYAQMIEDADGLDKIENLQS
SQ  HDNNEIYEKAVKILESYWAADDEEEDIGGVDAPENVQSSGFQFGNQSGNAPTGGFNFG
//
ID  Q9M9X7;
PN  Importin subunit alpha-7;
GN  IMPA7;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
DR  UNIPROT: Q9M9X7;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  Pfam: PF01749;
DR  PROSITE: PS50176;
DR  PROSITE: PS51214;
DE  Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation (PubMed:18836040). {ECO:0000250|UniProtKB:Q96321, ECO:0000269|PubMed:18836040}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKGGETMSVRRSGYKAVVDGVGGRRRREDDMVEIRKAKREESLLKKRREALPHSPSADSLDQKLISCIWSDERDLLIEAT
SQ  TQIRTLLCGEMFNVRVEEVIQAGLVPRFVEFLTWDDSPQLQFEAAWALTNIASGTSENTEVVIDHGAVAILVRLLNSPYD
SQ  VVREQVVWALGNISGDSPRCRDIVLGHAALPSLLLQLNHGAKLSMLVNAAWTLSNLCRGKPQPPFDQVSAALPALAQLIR
SQ  LDDKELLAYTCWALVYLSDGSNEKIQAVIEANVCARLIGLSIHRSPSVITPALRTIGNIVTGNDSQTQHIIDLQALPCLV
SQ  NLLRGSYNKTIRKEACWTVSNITAGCQSQIQAVFDADICPALVNLLQNSEGDVKKEAAWAICNAIAGGSYKQIMFLVKQE
SQ  CIKPLCDLLTCSDTQLVMVCLEALKKILKVGEVFSSRHAEGIYQCPQTNVNPHAQLIEEAEGLEKIEGLQSHENNDIYET
SQ  AVKILETYWMEEEEEEDQEQQDMIYFPVDNFANMPTSSGTLSEMHCGP
//
ID  Q9FJ92;
PN  Importin subunit alpha-8;
GN  IMPA8;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
DR  UNIPROT: Q9FJ92;
DR  Pfam: PF00514;
DR  Pfam: PF16186;
DR  PROSITE: PS50176;
DR  PROSITE: PS50077;
DE  Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope. {ECO:0000250|UniProtKB:Q96321}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
GO  GO:0048235;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAWKTEVNEVSDDIIDGLWSDDPPLQLESVTKIRRITSQRDISCVIRSGVVPRLVQLLKNQVFPKLQYEVAWALTNIAVD
SQ  NPGVVVNNNAVPVLIQLIASPKDYVREQAIWTLSNVAGHSIHYRDFVLNSGVLMPLLRLLYKDTTLRIATWALRNLCRGK
SQ  PHPAFDQVKPALPALEILLHSHDEDVLKNACMALCHLSEGSEDGIQSVIEAGFVPKLVQILQLPSPVVLVPALLTIGAMT
SQ  AGNHQQTQCVINSGALPIISNMLTRNHENKIKKCACWVISNITAGTKEQIQSVIDANLIPILVNLAQDTDFYMKKEAVWA
SQ  ISNMALNGSHDQIKYMAEQSCIKQLCDILVYSDERTTILKCLDGLENMLKAGEAEKNSEDVNPYCLLIEDAEGLEKISKL
SQ  QMNKNDDIYEKAYKILVTNWFEEDDENNNNNVRCDDVDFQV
//
ID  F4KF65;
PN  Importin subunit alpha-9;
GN  IMPA9;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
DR  UNIPROT: F4KF65;
DR  UNIPROT: Q9LYX8;
DR  Pfam: PF00514;
DE  Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope (By similarity). Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium, but is not essential for Agrobacterium-mediated root transformation (PubMed:18836040). {ECO:0000250|UniProtKB:Q96321, ECO:0000269|PubMed:18836040}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9M7Q7; IntAct: EBI-2131589; Score: 0.00
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0006607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADDGSASNRRDPIKSSVGNVAGQRRRKQAVTVAKERRELLVRAKRLCRVGTNGDVEDALVENEMMVDEEQPILEAQASK
SQ  SVEELKSAVQYQGKGAMQKRVTALRELRRLLSKSEFPPVEAALRAGAIPLLVQCLSFGSPDEQLLESAWCLTNIAAGKPE
SQ  ETKALLPALPLLIAHLGEKSSAPVAEQCAWAIGNVAGEGEDLRNVLLSQGALPPLARMIFPDKGSTVRTAAWALSNLIKG
SQ  PESKAAAQLVKIDGILDAILRHLKKTDEETATEIAWIIVYLSALSDIATSMLLKGGILQLLIDRLATSSSLQLLIPVLRS
SQ  LGNFVAVDPKAVLTILIREQNTEESIIGVLAKCLRSEHRVLKKEAAWVLSNIAAGSIEHKRMIHSTEVMPLLLRILSTSP
SQ  FDIRKEVAYVLGNLCVESAEGDRKPRIIQEHLVSIVSGGCLRGFIELVRSPDIEAARLGLQFIELVLRGMPNGEGPKLVE
SQ  GEDGIDAMERFQFHENEELRVMANSLVDKYFGEDYGIDE
//
ID  E2QYC9;
PN  InaD-like protein;
GN  PATJ;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, tight junction {ECO:0000269|PubMed:12527193, ECO:0000269|PubMed:12771187, ECO:0000269|PubMed:15738264}. Apical cell membrane {ECO:0000269|PubMed:15738264}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NI35}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63ZW7}. Note=Localizes to the apical region at the start of epithelial cell polarization then locates to tight junctions as polarization is completed (PubMed:15738264). Localized in the paranodal region of myelinating Schwann cells (By similarity). Localized to the leading edge of the actin cortex of migrating epithelia cells (PubMed:17235357). {ECO:0000250|UniProtKB:Q63ZW7, ECO:0000269|PubMed:15738264, ECO:0000269|PubMed:17235357}.
DR  UNIPROT: E2QYC9;
DR  Pfam: PF09045;
DR  Pfam: PF00595;
DR  PROSITE: PS51022;
DR  PROSITE: PS50106;
DE  Function: Scaffolding protein that facilitates the localization of proteins to the cell membrane (PubMed:17235357). Required for the correct formation of tight junctions and epithelial apico-basal polarity (PubMed:15738264). Positively regulates epithelial cell microtubule elongation and cell migration, possibly via facilitating localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells (PubMed:17235357). Plays a role in the correct reorientation of the microtubule-organizing center during epithelial migration (PubMed:17235357). May regulate the surface expression and/or function of ASIC3 in sensory neurons (By similarity). May recruit ARHGEF18 to apical cell-cell boundaries (By similarity). {ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35, ECO:0000269|PubMed:15738264, ECO:0000269|PubMed:17235357}.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0048471;
GO  GO:0070160;
GO  GO:0035089;
GO  GO:0031023;
GO  GO:0010634;
GO  GO:0070507;
GO  GO:0032880;
GO  GO:0120192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8NI35};
SQ  MPENPAPDKLQVLQVLDRLKMKLQEKGDTSQNEKLSLFYETLQSPLFNQILTLQQSIKQLKGQLSHIPSDCSTNFDFSRK
SQ  GLLVFTDSAITNGNAQRPSNNLTVSGLFPWTPKSGNEDFNSVIQQMAQGRQIEYIDIERPSTGGLGFSVVALRSQNLGEV
SQ  DIFVKEVQPGSIADRDQRLRENDQILAINHTPLDQNISHQQAIALLQQTTGSLHLVVAREPVHTKSRTSINLTDTTMPET
SQ  VHWGHIEDVELINDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGDTDVQGMTSEQVAQVLRNCGNSV
SQ  RMLVARDPVGETSVTPPTPAALPVALPAVANRSPSTDSSLYETYGVELIKKDGQSLGIRIVGYIGTAHTGEASGIYVKSI
SQ  IPGSAAYHNGQIQVNDKIVAVDGVNIQGFTNQDVVEVLRNAGQVVHLTLVRRKMCSSTSPLERSSDRGTVVEPSGTPARY
SQ  VTGAVETETNLDGGDEETEERMDNLKNDNIQALEKLERVPDSPENELKSRWENLLGPDYEVMVATLDTQIADDAELQKYS
SQ  KLLPIHTLRLGMEVDSFDGHHYISSIAPGGPVDALNLLQPEDELLEVNGVQLYGKSRREAVSFLKEVPPPFTLVCCRRLF
SQ  DDEASVDEPRTTETLLPEMEADHNVDINTEEEEEEELALWSPEVKIVELVKDHKGLGFSILDYQDPLDPTRSVIVIRSLV
SQ  ANGVAEKGGELLPGDRLVSVNEYCLENTTLAEAVEVLKAVPPGIVHLGVCKPLVDNDKEEESHYILHSNNNEDETELSET
SQ  IHDINSSLILEAPKGFRDEPYYKEELVDEPFLDLGKAFQSQQKEIDNSKEAWEMQEFLPPRLQEMGEEREMLVDEECDLY
SQ  QDHFQSMDLYPSSHLQEAAPVSSVKELHFGTQWLHDSEPPELQEARSMMNMYSQETQQYGYSTENMIKENFGIDSLPSIS
SQ  SSEGNSQQGRFDDLENLNSLTKSSLDLGMMIPNDVQGPGMLVELPAVAQRREQEDLPLYQLPRTRVVSKASAYTGASSSR
SQ  YTAGACELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSPAGKTNA
SQ  LKTGDKILEVSGVDLQNASHREAVEAIKNAGNPVVFVVQSLSSTPRVIPSVHNKANKIANNQDQNTEEKKEKRQGTPPPP
SQ  MKLPPPYKAPSDDSDENEEEYAFTNKKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPEGPAATD
SQ  GRMRIGDELLEINNQILYGRSHQNASAVIKTAPSKVKLVFIRNEDAVNQMAVAPFPVPSSSPSSLEDQSGTEPVSSEEDG
SQ  SLEVGIKQLPENESSKLEDISQVAGQGMVAGQQKALDCPTDNAVSQMKPQKYSTKVSFSSQEIPLAPAPSYHSTDVDFTS
SQ  YGGFQAPLSVDPATCPIVPGQEMIIEISKGRSGLGLSIVGGRDTPLDAIVIHEVYEEGAAARDGRLWAGDQILEVNGIDL
SQ  RSASHEEAITALRQTPQKVRLVVYRDEAHYRDEENLEIFPVDLQKKAGRGLGLSIVGKRNGSGVFISDIVKGGAADLDRR
SQ  LIQGDQILSVNGEDMRNASQETVATVLKCAQGLVQLEIGRLRAGSWTSSRKTSQNSQGSQHSTHSSFHPSLAPVITSLQN
SQ  LVGTKRATDPSLKSSGMDMGPRTVEIIRELSDALGISIAGGKGSPLGDIPIFIAMIQASGVAARTQKLKVGDRIVSINGQ
SQ  PLDGLSHADVVNLLKNAYGRIILQVVADTNISAIATQLENMSTGYHLGSPTAEHHPEDTEEPLQMTAG
//
ID  Q8NI35;
PN  InaD-like protein;
GN  PATJ;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, tight junction {ECO:0000269|PubMed:11927608, ECO:0000269|PubMed:11964389, ECO:0000269|PubMed:12021270, ECO:0000269|PubMed:19755384, ECO:0000269|PubMed:22006950}. Apical cell membrane {ECO:0000269|PubMed:11964389}; Peripheral membrane protein {ECO:0000269|PubMed:11964389}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18596123}. Note=Localizes to the apical region at the start of epithelial cell polarization then locates to tight junctions as polarization is completed (PubMed:11964389). Localized in the paranodal region of myelinating Schwann cells (By similarity). Localized to the leading edge of the actin cortex of migrating epithelia cells (By similarity). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7}.
DR  UNIPROT: Q8NI35;
DR  UNIPROT: O15249;
DR  UNIPROT: O43742;
DR  UNIPROT: O60833;
DR  UNIPROT: Q5VUA5;
DR  UNIPROT: Q5VUA6;
DR  UNIPROT: Q5VUA7;
DR  UNIPROT: Q5VUA8;
DR  UNIPROT: Q5VUA9;
DR  UNIPROT: Q5VUB0;
DR  UNIPROT: Q8WU78;
DR  UNIPROT: Q9H3N9;
DR  PDB: 1VF6;
DR  PDB: 2D92;
DR  PDB: 2DAZ;
DR  PDB: 2DB5;
DR  PDB: 2DLU;
DR  PDB: 2DM8;
DR  PDB: 2DMZ;
DR  PDB: 2EHR;
DR  PDB: 4Q2N;
DR  PDB: 6IRD;
DR  Pfam: PF09045;
DR  Pfam: PF00595;
DR  PROSITE: PS51022;
DR  PROSITE: PS50106;
DR  OMIM: 603199;
DE  Function: Scaffolding protein that facilitates the localization of proteins to the cell membrane (PubMed:11927608, PubMed:16678097, PubMed:22006950). Required for the correct formation of tight junctions and epithelial apico-basal polarity (PubMed:11927608, PubMed:16678097). Positively regulates epithelial cell microtubule elongation and cell migration, possibly via facilitating localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells (By similarity). Plays a role in the correct reorientation of the microtubule-organizing center during epithelial migration (By similarity). May regulate the surface expression and/or function of ASIC3 in sensory neurons (By similarity). May recruit ARHGEF18 to apical cell-cell boundaries (PubMed:22006950). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7, ECO:0000269|PubMed:11927608, ECO:0000269|PubMed:16678097, ECO:0000269|PubMed:22006950}.
DE  Reference Proteome: Yes;
DE  Interaction: O94827; IntAct: EBI-21910914; Score: 0.35
DE  Interaction: P35240; IntAct: EBI-3957523; Score: 0.50
DE  Interaction: Q66T02; IntAct: EBI-25409900; Score: 0.35
DE  Interaction: O95049; IntAct: EBI-8417397; Score: 0.56
DE  Interaction: O95832; IntAct: EBI-8417417; Score: 0.40
DE  Interaction: Q9NVP1; IntAct: EBI-736550; Score: 0.00
DE  Interaction: Q8N3R9; IntAct: EBI-8222553; Score: 0.72
DE  Interaction: Q8JZS0; IntAct: EBI-8230712; Score: 0.40
DE  Interaction: P82279; IntAct: EBI-8230772; Score: 0.50
DE  Interaction: Q9NPB6; IntAct: EBI-7053672; Score: 0.40
DE  Interaction: O00254; IntAct: EBI-7206220; Score: 0.46
DE  Interaction: P17252; IntAct: EBI-7206246; Score: 0.27
DE  Interaction: Q92905; IntAct: EBI-2659663; Score: 0.35
DE  Interaction: Q5NI89; IntAct: EBI-2805865; Score: 0.00
DE  Interaction: P31016; IntAct: EBI-7966903; Score: 0.44
DE  Interaction: Q4VCS5; IntAct: EBI-8795849; Score: 0.42
DE  Interaction: Q96S44; IntAct: EBI-6256589; Score: 0.35
DE  Interaction: O14910; IntAct: EBI-6911712; Score: 0.35
DE  Interaction: P46937; IntAct: EBI-6912563; Score: 0.71
DE  Interaction: Q9Y2J4; IntAct: EBI-8795811; Score: 0.35
DE  Interaction: Q7TSJ6; IntAct: EBI-8797641; Score: 0.42
DE  Interaction: O95835; IntAct: EBI-8798552; Score: 0.27
DE  Interaction: Q9H4B6; IntAct: EBI-8799416; Score: 0.27
DE  Interaction: P33215; IntAct: EBI-10993316; Score: 0.35
DE  Interaction: Q96L14; IntAct: EBI-11022408; Score: 0.35
DE  Interaction: P29033; IntAct: EBI-11024719; Score: 0.35
DE  Interaction: E9Q4K7; IntAct: EBI-11042417; Score: 0.35
DE  Interaction: O88952; IntAct: EBI-11079007; Score: 0.35
DE  Interaction: P60006; IntAct: EBI-11091984; Score: 0.35
DE  Interaction: Q8CCJ3; IntAct: EBI-11104920; Score: 0.35
DE  Interaction: Q03933; IntAct: EBI-11107990; Score: 0.35
DE  Interaction: A2APB8; IntAct: EBI-11110977; Score: 0.35
DE  Interaction: Q9R0Q3; IntAct: EBI-11111571; Score: 0.35
DE  Interaction: P37840; IntAct: EBI-11113842; Score: 0.35
DE  Interaction: P04062; IntAct: EBI-11114072; Score: 0.35
DE  Interaction: O75792; IntAct: EBI-11115131; Score: 0.35
DE  Interaction: Q13637; IntAct: EBI-11116348; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135399; Score: 0.35
DE  Interaction: P46938; IntAct: EBI-11138299; Score: 0.35
DE  Interaction: Q9Y5I4; IntAct: EBI-21510892; Score: 0.35
DE  Interaction: Q9NUP9; IntAct: EBI-21627409; Score: 0.35
DE  Interaction: Q96A37; IntAct: EBI-21627270; Score: 0.35
DE  Interaction: Q9NSC5; IntAct: EBI-21639932; Score: 0.35
DE  Interaction: Q96NE9; IntAct: EBI-21910666; Score: 0.35
DE  Interaction: Q8NI35; IntAct: EBI-21910914; Score: 0.35
DE  Interaction: Q05639; IntAct: EBI-21910914; Score: 0.35
DE  Interaction: P62873; IntAct: EBI-21910914; Score: 0.35
DE  Interaction: Q9H4B7; IntAct: EBI-21910914; Score: 0.35
DE  Interaction: Q92619; IntAct: EBI-21910914; Score: 0.35
DE  Interaction: Q86YM7; IntAct: EBI-21910914; Score: 0.35
DE  Interaction: P48668; IntAct: EBI-21910914; Score: 0.35
DE  Interaction: P25311; IntAct: EBI-21910914; Score: 0.35
DE  Interaction: Q96QZ7; IntAct: EBI-21911330; Score: 0.35
DE  Interaction: P16104; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: Q9UNX3; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: Q9NSB8; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: Q9HAV0; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: Q99417; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: Q96EY4; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: Q92600; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: Q8IY63; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: P51572; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: P0C0S5; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: Q9HAP6; IntAct: EBI-21911017; Score: 0.35
DE  Interaction: Q9C0D5; IntAct: EBI-20732770; Score: 0.44
DE  Interaction: Q99569; IntAct: EBI-20732783; Score: 0.44
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: K9N5R3; IntAct: EBI-26973747; Score: 0.40
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q96ED9; IntAct: EBI-34575530; Score: 0.27
GO  GO:0043296;
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0030054;
GO  GO:0034451;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0035089;
GO  GO:0045197;
GO  GO:0035556;
GO  GO:0120192;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11964389};
SQ  MPENPATDKLQVLQVLDRLKMKLQEKGDTSQNEKLSMFYETLKSPLFNQILTLQQSIKQLKGQLNHIPSDCSANFDFSRK
SQ  GLLVFTDGSITNGNVHRPSNNSTVSGLFPWTPKLGNEDFNSVIQQMAQGRQIEYIDIERPSTGGLGFSVVALRSQNLGKV
SQ  DIFVKDVQPGSVADRDQRLKENDQILAINHTPLDQNISHQQAIALLQQTTGSLRLIVAREPVHTKSSTSSSLNDTTLPET
SQ  VCWGHVEEVELINDGSGLGFGIVGGKTSGVVVRTIVPGGLADRDGRLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSV
SQ  RMLVARDPAGDISVTPPAPAALPVALPTVASKGPGSDSSLFETYNVELVRKDGQSLGIRIVGYVGTSHTGEASGIYVKSI
SQ  IPGSAAYHNGHIQVNDKIVAVDGVNIQGFANHDVVEVLRNAGQVVHLTLVRRKTSSSTSPLEPPSDRGTVVEPLKPPALF
SQ  LTGAVETETNVDGEDEEIKERIDTLKNDNIQALEKLEKVPDSPENELKSRWENLLGPDYEVMVATLDTQIADDAELQKYS
SQ  KLLPIHTLRLGVEVDSFDGHHYISSIVSGGPVDTLGLLQPEDELLEVNGMQLYGKSRREAVSFLKEVPPPFTLVCCRRLF
SQ  DDEASVDEPRRTETSLPETEVDHNMDVNTEEDDDGELALWSPEVKIVELVKDCKGLGFSILDYQDPLDPTRSVIVIRSLV
SQ  ADGVAERSGGLLPGDRLVSVNEYCLDNTSLAEAVEILKAVPPGLVHLGICKPLVEDNEEESCYILHSSSNEDKTEFSGTI
SQ  HDINSSLILEAPKGFRDEPYFKEELVDEPFLDLGKSFHSQQKEIEQSKEAWEMHEFLTPRLQEMDEEREILVDEEYELYQ
SQ  DPSPSMELYPLSHIQEATPVPSVNELHFGTQWLHDNEPSESQEARTGRTVYSQEAQPYGYCPENVMKENFVMESLPSVPS
SQ  TEGNSQQGRFDDLENLNSLAKTSLDLGMIPNDVQGPSLLIDLPVVAQRREQEDLPLYQHQATRVISKASAYTGMLSSRYA
SQ  TDTCELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSPAGKTNALK
SQ  TGDKILEVSGVDLQNASHSEAVEAIKNAGNPVVFIVQSLSSTPRVIPNVHNKANKITGNQNQDTQEKKEKRQGTAPPPMK
SQ  LPPPYKALTDDSDENEEEDAFTDQKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPEGPAAADGR
SQ  MRIGDELLEINNQILYGRSHQNASAIIKTAPSKVKLVFIRNEDAVNQMAVTPFPVPSSSPSSIEDQSGTEPISSEEDGSV
SQ  EVGIKQLPESESFKLAVSQMKQQKYPTKVSFSSQEIPLAPASSYHSTDADFTGYGGFQAPLSVDPATCPIVPGQEMIIEI
SQ  SKGRSGLGLSIVGGKDTPLNAIVIHEVYEEGAAARDGRLWAGDQILEVNGVDLRNSSHEEAITALRQTPQKVRLVVYRDE
SQ  AHYRDEENLEIFPVDLQKKAGRGLGLSIVGKRNGSGVFISDIVKGGAADLDGRLIQGDQILSVNGEDMRNASQETVATIL
SQ  KCAQGLVQLEIGRLRAGSWTSARTTSQNSQGSQQSAHSSCHPSFAPVITGLQNLVGTKRVSDPSQKNSGTDMEPRTVEIN
SQ  RELSDALGISIAGGRGSPLGDIPVFIAMIQASGVAARTQKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGRIILQVVA
SQ  DTNISAIAAQLENMSTGYHLGSPTAEHHPEDTEEQLQMTAD
//
ID  Q63ZW7;
PN  InaD-like protein;
GN  Patj;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, tight junction {ECO:0000250|UniProtKB:Q8NI35}. Apical cell membrane {ECO:0000250|UniProtKB:Q8NI35}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NI35}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14988405}. Note=Localizes to the apical region at the start of epithelial cell polarization then locates to tight junctions as polarization is completed (By similarity). Localized in the paranodal region of myelinating Schwann cells (PubMed:12403818). Localized to the leading edge of the actin cortex of migrating epithelia cells (By similarity). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q8NI35, ECO:0000269|PubMed:12403818}. [Isoform 3]: Cytoplasm. Cytoplasm, perinuclear region. Note=Concentrates around the nucleus upon HTR2A coexpression.
DR  UNIPROT: Q63ZW7;
DR  UNIPROT: A2ADS7;
DR  UNIPROT: O70471;
DR  UNIPROT: Q5PRG3;
DR  UNIPROT: Q6P6J1;
DR  UNIPROT: Q80YR8;
DR  UNIPROT: Q8BPB9;
DR  Pfam: PF09045;
DR  Pfam: PF00595;
DR  PROSITE: PS51022;
DR  PROSITE: PS50106;
DE  Function: Scaffolding protein that facilitates the localization of proteins to the cell membrane (PubMed:11872753). Required for the correct formation of tight junctions and epithelial apico-basal polarity (By similarity). Positively regulates epithelial cell microtubule elongation and cell migration, possibly via facilitating localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells (By similarity). Plays a role in the correct reorientation of the microtubule-organizing center during epithelial migration (By similarity). May regulate the surface expression and/or function of ASIC3 in sensory neurons (PubMed:11872753). May recruit ARHGEF18 to apical cell-cell boundaries (By similarity). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q8NI35, ECO:0000269|PubMed:11872753}.
DE  Reference Proteome: Yes;
DE  Interaction: O35240; IntAct: EBI-8158519; Score: 0.51
DE  Interaction: P49655; IntAct: EBI-8689438; Score: 0.37
DE  Interaction: P35436; IntAct: EBI-8689421; Score: 0.51
DE  Interaction: Q62645; IntAct: EBI-8689537; Score: 0.51
DE  Interaction: Q00960; IntAct: EBI-8689473; Score: 0.51
DE  Interaction: Q62644; IntAct: EBI-8689517; Score: 0.37
DE  Interaction: Q99712; IntAct: EBI-8689848; Score: 0.51
DE  Interaction: Q00961; IntAct: EBI-8690026; Score: 0.51
DE  Interaction: Q62888; IntAct: EBI-8690119; Score: 0.37
DE  Interaction: Q63376; IntAct: EBI-8690093; Score: 0.37
DE  Interaction: Q9JM63; IntAct: EBI-8689922; Score: 0.40
DE  Interaction: O88932; IntAct: EBI-8689908; Score: 0.40
DE  Interaction: Q60857; IntAct: EBI-15633398; Score: 0.35
DE  Interaction: Q61327; IntAct: EBI-15633420; Score: 0.35
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0030054;
GO  GO:0034451;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0035003;
GO  GO:0070160;
GO  GO:0035089;
GO  GO:0120192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8NI35};
SQ  MPENPAAEKMQVLQVLDRLRGKLQEKGDTTQNEKLSAFYETLKSPLFNQILTLQQSIKQLKGQLSHIPSDCSANFDFSRK
SQ  GLLVFTDGSITNGNAQRPCSNVTASELLPWTQKSASEDFNSVIQQMAQGRHVEYIDIERPSTGGLGFSVVALRSQSLGLI
SQ  DIFVKEVHPGSVADRDHRLKENDQILAINDTPLDQNISHQQAIALLQQATGSLRLVVAREVGHTQGRASTSSADTTLPET
SQ  VCWGHTEEVELINDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSV
SQ  RMLVARDPVGEIAVTPPTPVSLPVALPAVATRTLDSDRSPFETYSVELVKKDGQSLGIRIVGYVGTAHPGEASGIYVKSI
SQ  IPGSAAYHNGQIQVNDKIVAVDGVNIQGFANQDVVEVLRNAGQVVHLTLVRRKTSLSASPFEHSSSRETVAEPPKVPERA
SQ  GSPKPEANLSVEAEEIGERLDNLKNNTVQALEKPDVYPEKVPGSPENELKSRWENLLGPDYEVMVATLDAQIADDEELQK
SQ  YSKLLPIHTLRLGMEVDSFDGHHYISSVAPGGPVDTLNLLQPEDELLEVNGMQLYGKSRREAVSFLKEVPPPFTLVCCRR
SQ  LFDDEASVDEPRTMEPALLEAEVDHSVDVNIEDDDDGELALWSPEVKTVELVKDCKGLGFSILDYQDPLDPTRSVIVIRS
SQ  LVADGVAERSGELLPGDRLVSVNEFSLDNATLAEAVEVLKAVPPGVVHLGICKPLVEDEKEERFSLHSNNNGDSSEPADA
SQ  VHEIHSSLILEAPQGFRDEPYLEELVDEPFLDLGKSLQFQQKDVDSSSEAWEMHEFLSPPLDGRGEEREMLVDEEYELYQ
SQ  DHLRAMESNPPPPHIREAAPASPVLELQAGTQWLHANLSGGERLECHDAESMMSAYPQEMQQYSYSTADMMEETFGLDSR
SQ  APIPSSEGNGQHGRFDDMGHLHSLTSSSLDLGMMIPSDLQGPGVLVDLPAVAQRREQEDLPLYRLPSARVVTKPSSHMGL
SQ  VSSRHANAACELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSPAG
SQ  KTNALKTGDKILEVSGVDLQNASHAEAVEAIKSAGNPVVFVVQSLSSTPRVIPTVNNKGKTPAPNQDQNTQERKAKRHGT
SQ  APPPMKLPPPYRAPSADMEGSEEDCALTDKKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPEGP
SQ  AAADGRMRIGDELLEINNQILYGRSHQNASAIIKTAPTRVKLVFIRNEDAVSQMAVAPFPELSHSPSPVEDLGGTELVSS
SQ  EEESSVDAKHLPEPESSKPEDLSQVVDDNMVAEQQKESESPDSAACQIKQQTYSTQVSSSSQDSPSSPAPLCQSAHADVT
SQ  GSGNFQAPLPVDPAPLSVDPATCPIVPGQEMIIEISKGRSGLGLSIVGGKDTPLDAIVIHEVYEEGAAARDGRLWAGDQI
SQ  LEVNGVDLRSSSHEEAITALRQTPQKVRLVVYRDEAQYRDEENLEVFLVDLQKKTGRGLGLSIVGKRSGSGVFISDIVKG
SQ  GAADLDGRLIRGDQILSVNGEDMRHASQETVATILKCVQGLVQLEIGRLRAGSWAASRKTSQNSQGDQHSAHSSCRPSFA
SQ  PVITSLQNLVGTKRSSDPPQKCTEEEPRTVEIIRELSDALGISIAGGKGSPLGDIPIFIAMIQANGVAARTQKLKVGDRI
SQ  VSINGQPLDGLSHTDAVNLLKNAFGRIILQVVADTNISAIATQLEIMSAGSQLGSPTADRHPEDTEEQMQRTAD
//
ID  F1MAD2;
PN  InaD-like protein;
GN  Patj;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, tight junction {ECO:0000250|UniProtKB:Q8NI35}. Apical cell membrane {ECO:0000250|UniProtKB:Q8NI35}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NI35}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63ZW7}. Note=Localizes to the apical region at the start of epithelial cell polarization then locates to tight junctions as polarization is completed (By similarity). Localized in the paranodal region of myelinating Schwann cells (By similarity). Localized to the leading edge of the actin cortex of migrating epithelia cells (By similarity). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35}.
DR  UNIPROT: F1MAD2;
DR  PDB: 3UIT;
DR  Pfam: PF09045;
DR  Pfam: PF00595;
DR  PROSITE: PS51022;
DR  PROSITE: PS50106;
DE  Function: Scaffolding protein that facilitates the localization of proteins to the cell membrane (By similarity). Required for the correct formation of tight junctions and epithelial apico-basal polarity (By similarity). Positively regulates epithelial cell microtubule elongation and cell migration, possibly via facilitating localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells (By similarity). Plays a role in the correct reorientation of the microtubule-organizing center during epithelial migration (By similarity). May regulate the surface expression and/or function of ASIC3 in sensory neurons (By similarity). May recruit ARHGEF18 to apical cell-cell boundaries (By similarity). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35}.
DE  Reference Proteome: Yes;
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0035003;
GO  GO:0070160;
GO  GO:0035089;
GO  GO:0120192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8NI35};
SQ  MPENPAAEKMQVLQVLDRLRGKLQEKGDTTQNEKLSAFYETLKSPLFNQILTLQQSIKQLKGQLSHIPSDCSANFDFSRK
SQ  GLLVFTDGSITNGNAHRPCSSITASESLPWTQRSGNEDFTSVIQQMAQGRHIEYIDIERPSTGGLGFSVVALRSQSLGLI
SQ  DIFVKEVHPGSVADRDQRLKENDQILAINDTPLDQNISHQQAIALLQQATGSLRLVVAREVGHTQSRTSTSSADTTLPET
SQ  VRWGHTEDVELINDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGSTNVQGMTSEQVAQVLRNCGNSV
SQ  RMLVARDPVGEIAVTPPTPASLPVALPVVATRTLGSDSSPFETYNVELVKKDGQSLGIRIVGYVGTAHPGEASGIYVKSI
SQ  IPGSAAYHNGQIQVNDKIVAVDGVNIQGFANQDVVEVLRNAGQVVHLTLVRRKTSLSASPFEQPSSREAVAEPPEVPELT
SQ  GSLKPETNSRMEAEEIGERLDNLRKDTVQALEKPDVYPEDIPGCPENELKSRWENLLGPDYEVMVATLDTQIADDEELQK
SQ  YSKLLPIHTLRLGMEVDSFDGHHYISSIAPGGPVDTLNLLQPEDELLEVNGVQLYGKSRREAVSFLKEVPPPFTLVCCRR
SQ  LFDDEASVDEPRTVEPSLLEAEVDRSVDVSTEDDDGELALWSPEVKTVELVKDCKGLGFSILDYQDPLDPMRSVIVIRSL
SQ  VADGVAERSGELLPGDRLVSVNEFSLDNATLAEAVEVLKAVPPGVVHLGICKPLVEEEKEEKEEHFIFHSNNNGDNSESP
SQ  ETVHEIHSSLILEAPQGFRDEPYLEELVDEPFLDLGKSLQFQQKDMDSSSEAWEMHEFLSPRLERRGEEREMLVDEEYEI
SQ  YQDRLRDMEAHPPPPHIREPTSASPRLDLQAGPQWLHADLSGGEILECHDTESMMTAYPQEMQDYSFSTTDMMKETFGLD
SQ  SRPPMPSSEGNGQHGRFDDLEHLHSLVSHGLDLGMMTPSDLQGPGVLVDLPAVTQRREQEELPLYRLPSARVVTKPSSHV
SQ  GMVSSRHANAACELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSP
SQ  AGKTKALKTGDKILEVSGVDLQNASHAEAVEAIKSAGNPVVFVVQSLSSTPRVIPSVNNKGKTPPQNQDQNTQEKKAKRH
SQ  GTAPPPMKLPPPYRAPSADTEESEEDSALTDKKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPD
SQ  GPAAADGRMRVGDELLEINNQILYGRSHQNASAIIKTAPTRVKLVFIRNEDAVNQMAVAPFPVPSHSPSPVEDLGGTEPV
SQ  SSEEDSSVDAKPLPERESSKPEDLTQAVDDSMVAEQEKASESPDSAARQMKQPGYSAQVSSSSQEIPSAPAPLCQSTHAD
SQ  VTGSGNFQAPLSVDPAPLSVDPATCPIVPGQEMIIEISKGRSGLGLSIVGGKDTPLDAIVIHEVYEEGAAARDGRLWAGD
SQ  QILEVNGVDLRSSSHEEAITALRQTPQKVRLVIYRDEAQYRDEENLEVFLVDLQKKTGRGLGLSIVGKRSGSGVFISDIV
SQ  KGGAADLDGRLIRGDQILSVNGEDVRQASQETVATILKCVQGLVQLEIGRLRAGSWASSRKTSQNSQGDQHSAHSSCRPS
SQ  FAPVITSLQNLVGTKRSSDPPQKCTEEEPRTVEIIRELSDALGVSIAGGKGSPLGDIPIFIAMIQANGVAARTQKLKVGD
SQ  RIVSINGQPLDGLSHTDAVNLLKNAFGRIILQVVADTNISAIATQLEMMSAGSQLGSPTADRHPQDPEELLQRTAD
//
ID  Q27J81;
PN  Inverted formin-2;
GN  INF2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20023659}.
DR  UNIPROT: Q27J81;
DR  UNIPROT: Q27J83;
DR  UNIPROT: Q69YL8;
DR  UNIPROT: Q6P1X7;
DR  UNIPROT: Q6PK22;
DR  UNIPROT: Q86TR7;
DR  UNIPROT: Q9BRM1;
DR  UNIPROT: Q9H6N1;
DR  Pfam: PF06367;
DR  Pfam: PF06371;
DR  Pfam: PF02181;
DR  Pfam: PF02205;
DR  PROSITE: PS51444;
DR  PROSITE: PS51232;
DR  PROSITE: PS51082;
DR  OMIM: 610982;
DR  OMIM: 613237;
DR  OMIM: 614455;
DR  DisGeNET: 64423;
DE  Function: Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000250}.
DE  Disease: Focal segmental glomerulosclerosis 5 (FSGS5) [MIM:613237]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:20023659, ECO:0000269|PubMed:21258034, ECO:0000269|PubMed:21866090, ECO:0000269|PubMed:22971997, ECO:0000269|PubMed:23014460, ECO:0000269|PubMed:25165188}. Note=The disease is caused by variants affecting the gene represented in this entry. Charcot-Marie-Tooth disease, dominant, intermediate type, E (CMTDIE) [MIM:614455]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type E is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. Patients additionally manifest focal segmental glomerulonephritis, proteinuria, progression to end-stage renal disease, and a characteristic histologic pattern on renal biopsy. {ECO:0000269|PubMed:22187985, ECO:0000269|PubMed:24174593, ECO:0000269|PubMed:24750328, ECO:0000269|PubMed:25165188, ECO:0000269|PubMed:25676889}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O14976; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P84089; IntAct: EBI-2557894; Score: 0.40
DE  Interaction: A0A0F7RE19; IntAct: EBI-2831512; Score: 0.00
DE  Interaction: A0A380PMD7; IntAct: EBI-2847144; Score: 0.00
DE  Interaction: Q712K3; IntAct: EBI-7412118; Score: 0.37
DE  Interaction: P68400; IntAct: EBI-5309997; Score: 0.44
DE  Interaction: Q9WMX2; IntAct: EBI-9081849; Score: 0.37
DE  Interaction: P03220; IntAct: EBI-11722152; Score: 0.35
DE  Interaction: P03225; IntAct: EBI-11722220; Score: 0.35
DE  Interaction: P06428; IntAct: EBI-11722493; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: P0CK58; IntAct: EBI-11732874; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11004631; Score: 0.35
DE  Interaction: Q9NQW6; IntAct: EBI-11009421; Score: 0.35
DE  Interaction: O08917; IntAct: EBI-11025136; Score: 0.35
DE  Interaction: Q60634; IntAct: EBI-11025478; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-11030093; Score: 0.35
DE  Interaction: O00159; IntAct: EBI-11030803; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: P21333; IntAct: EBI-11038784; Score: 0.35
DE  Interaction: Q61879; IntAct: EBI-11041929; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q80X90; IntAct: EBI-11053320; Score: 0.35
DE  Interaction: Q9ERG0; IntAct: EBI-11054044; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062262; Score: 0.35
DE  Interaction: Q9JHJ0; IntAct: EBI-11063313; Score: 0.35
DE  Interaction: P58771; IntAct: EBI-11063826; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-11092730; Score: 0.35
DE  Interaction: Q9WTI7; IntAct: EBI-11093786; Score: 0.35
DE  Interaction: P35749; IntAct: EBI-11098041; Score: 0.35
DE  Interaction: Q9NQX4; IntAct: EBI-11100755; Score: 0.35
DE  Interaction: Q91YI4; IntAct: EBI-11102575; Score: 0.35
DE  Interaction: Q9Z1Z0; IntAct: EBI-11112182; Score: 0.35
DE  Interaction: Q61166; IntAct: EBI-11113235; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: P35611; IntAct: EBI-11118761; Score: 0.35
DE  Interaction: P46108; IntAct: EBI-11119999; Score: 0.35
DE  Interaction: Q80UG5; IntAct: EBI-11121465; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-11128681; Score: 0.35
DE  Interaction: Q9P2B7; IntAct: EBI-11131339; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-11132927; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-11142496; Score: 0.35
DE  Interaction: P61160; IntAct: EBI-11156891; Score: 0.35
DE  Interaction: Q9NYL9; IntAct: EBI-21701240; Score: 0.35
DE  Interaction: P35080; IntAct: EBI-21776651; Score: 0.35
DE  Interaction: Q96DX4; IntAct: EBI-21834193; Score: 0.35
DE  Interaction: P62136; IntAct: EBI-16370519; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: P30411; IntAct: EBI-20803487; Score: 0.37
DE  Interaction: Q14108; IntAct: EBI-21264396; Score: 0.35
DE  Interaction: O84793; IntAct: EBI-22302936; Score: 0.35
DE  Interaction: Q92685; IntAct: EBI-25468462; Score: 0.37
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: P11274; IntAct: EBI-28931791; Score: 0.35
DE  Interaction: Q8TAS1; IntAct: EBI-28943630; Score: 0.35
DE  Interaction: Q8TDX7; IntAct: EBI-28943744; Score: 0.35
DE  Interaction: Q96GD4; IntAct: EBI-28944360; Score: 0.35
DE  Interaction: Q99816; IntAct: EBI-30839695; Score: 0.44
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P09619; IntAct: EBI-32724964; Score: 0.27
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0031267;
GO  GO:0030036;
GO  GO:0090140;
GO  GO:0051056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSVKEGAQRKWAALKEKLGPQDSDPTEANLESADPELCIRLLQMPSVVNYSGLRKRLEGSDGGWMVQFLEQSGLDLLLEA
SQ  LARLSGRGVARISDALLQLTCVSCVRAVMNSRQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCIYSPEGHVL
SQ  TLDALDHYKTVCSQQYRFSIVMNELSGSDNVPYVVTLLSVINAVILGPEDLRARTQLRNEFIGLQLLDVLARLRDLEDAD
SQ  LLIQLEAFEEAKAEDEEELLRVSGGVDMSSHQEVFASLFHKVSCSPVSAQLLSVLQGLLHLEPTLRSSQLLWEALESLVN
SQ  RAVLLASDAQECTLEEVVERLLSVKGRPRPSPLVKAHKSVQANLDQSQRGSSPQNTTTPKPSVEGQQPAAAAACEPVDHA
SQ  QSESILKVSQPRALEQQASTPPPPPPPPLLPGSSAEPPPPPPPPPLPSVGAKALPTAPPPPPLPGLGAMAPPAPPLPPPL
SQ  PGSCEFLPPPPPPLPGLGCPPPPPPLLPGMGWGPPPPPPPLLPCTCSPPVAGGMEEVIVAQVDHGLGSAWVPSHRRVNPP
SQ  TLRMKKLNWQKLPSNVAREHNSMWASLSSPDAEAVEPDFSSIERLFSFPAAKPKEPTMVAPRARKEPKEITFLDAKKSLN
SQ  LNIFLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLASADHFYLLLLAIPCYQLRIEC
SQ  MLLCEGAAAVLDMVRPKAQLVLAACESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLTETKSQQNRVTL
SQ  LHHVLEEAEKSHPDLLQLPRDLEQPSQAAGINLEIIRSEASSNLKKLLETERKVSASVAEVQEQYTERLQASISAFRALD
SQ  ELFEAIEQKQRELADYLCEDAQQLSLEDTFSTMKAFRDLFLRALKENKDRKEQAAKAERRKQQLAEEEARRPRGEDGKPV
SQ  RKGPGKQEEVCVIDALLADIRKGFQLRKTARGRGDTDGGSKAASMDPPRATEPVATSNPAGDPVGSTRCPASEPGLDATT
SQ  ASESRGWDLVDAVTPGPQPTLEQLEEGGPRPLERRSSWYVDASDVLTTEDPQCPQPLEGAWPVTLGDAQALKPLKFSSNQ
SQ  PPAAGSSRQDAKDPTSLLGVLQAEADSTSEGLEDAVHSRGARPPAAGPGGDEDEDEEDTAPESALDTSLDKSFSEDAVTD
SQ  SSGSGTLPRARGRASKGTGKRRKKRPSRSQEEVPPDSDDNKTKKLCVIQ
//
ID  Q0GNC1;
PN  Inverted formin-2;
GN  Inf2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q0GNC1;
DR  UNIPROT: Q14C56;
DR  UNIPROT: Q499F7;
DR  UNIPROT: Q6P9T3;
DR  Pfam: PF06367;
DR  Pfam: PF06371;
DR  Pfam: PF02181;
DR  Pfam: PF02205;
DR  PROSITE: PS51444;
DR  PROSITE: PS51232;
DR  PROSITE: PS51082;
DE  Function: Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000269|PubMed:16818491}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q9P2S5; IntAct: EBI-11694751; Score: 0.35
DE  Interaction: Q93KQ6; IntAct: EBI-16142761; Score: 0.35
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0031267;
GO  GO:0030036;
GO  GO:0032535;
GO  GO:0090140;
GO  GO:0051056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSVKEGAQRKWAALKEKLGPQDSDPTEANLESAEPELCIRLLQMPSVVNYSGLRKRLESSDGGWMVQFLEQSGLDLLLEA
SQ  LARLSGRGVARISDALLQLTCISCVRAVMNSQQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCIYSPEGHAL
SQ  TLDALDHYKMVCSQQYRFSVIMSELSDSDNVPYVVTLLSVINAIILGPEDLRSRAQLRSEFIGLQLLDILTRLRDLEDAD
SQ  LLIQLEAFEEAKAEDEEELQRISDGINMNSHQEVFASLFHKVSCSPASAQLLSVLQGLMHLEPAGRSGQLLWEALENLVN
SQ  RAVLLASDAQACTLEEVVERLLSIKGRPRPSPLDKAHKSVQTNSVQNQGSSSQNTTTPTTKVEGQQPVVASPCQHVGSIQ
SQ  SSSVDIAPQPVALEQCITALPLPTPPLSSSTPVLPPTPPPLPGPGATSPLPPPPPPLPPPLPGSGTTSPPPPPPPPPPLP
SQ  PPLPGSGTISPPPPPPPPPLPGTGAVSPPPPPPLPSLPDSHKTQPPPPPPPPLPGMCPVPPPPPLPRAGQIPPPPPLPGF
SQ  SVPSMMGGVEEIIVAQVDHSLGSAWVPSHRRVNPPTLRMKKLNWQKLPSNVARERNSMWATLGSPCTAAVEPDFSSIEQL
SQ  FSFPTAKPKEPSAAPARKEPKEVTFLDSKKSLNLNIFLKQFKCSNEEVTSMIQAGDTSKFDVEVLKQLLKLLPEKHEIEN
SQ  LRAFTEERAKLSNADQFYVLLLDIPCYPLRVECMMLCEGTAIVLDMVRPKAQLVLTACESLLTSQRLPVFCQLILKIGNF
SQ  LNYGSHTGDADGFKISTLLKLTETKSQQSRVTLLHHVLEEVEKSHPDLLQLSRDLEPPSQAAGINVEIIHSEASANLKKL
SQ  LEAERKVSASIPEVQKQYAERLQASIEASQELDKVFDAIEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLFTRALKEN
SQ  KDRKEQMAKAERRKQQLAEEEARRPRDEDGKPIRKGPGKQEEVCVIDALLADIRKGFQLRKTARGRGDTEASGRVAPTDP
SQ  PKATEPATASNPTQGTNHPASEPLDTTAADEPQGWDLVDAVTPSPQPSKEEDGPPALERRSSWYVDAIDFLDPEDTPDAQ
SQ  PSEGVWPVTLGDGQALNPLEFSSNKPPGVKSSHQDATDPEALWGVHQTEADSTSEGPEDEAQRGQSTHLPRTGPGEDEDG
SQ  EDTAPESALDTSLDRSFSEDAVTDSSGSGTLPRVQGRVSKGTSKRRKKRPSRNQEEFVPDSDDIKAKRLCVIQ
//
ID  B3LVQ1;
PN  Protein asunder;
GN  asun;
OS  7217;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B3LVQ1;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0051301;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFEQNQKTIFVLDHTRYFSIASEDYISMDFLKGKPSVDTGTGAGVGGASGLGTQFSKSLWTCACESSIEYCRVVWDLFPG
SQ  KKHVRFIVSDTAAHIVNTWSTSTQNMSHVMNAMVMVGVPSRSMPQSSDYSVIHGLRAAIEALAEPTDEQLATIASGEPVH
SQ  IPNEGRVICITSARDNTSMKSLEDIFNTVLIQQNALAGPPAKKGLAIDHCHLVILNIVPLGVESLVTNRGLLNISPLLDV
SQ  EIHTVSAPDISHKLTHLILDHYNLASTTVTNIPMKEEQNANSSANYDVEILHSRSAHSIACGPDFSLPTSIKPGATYETV
SQ  TLKWCTPRGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKAGSKATSHMLSARGGEIFIHSLCITR
SQ  SCMDEAPAIGDGPGGRVTDYRTTELGQLMKMSRMVPLKAKDPTAPGLPRRMPRYFPLTNGSSILFHLQRHISWMPHFLHL
SQ  LVKEDMDKQEEVRCQQHIHELYKSASRGDMLPFTHTNGARLKLSKAKDQYRLLYRELEQLIHLNATTVHHKNLLESLQSL
SQ  RAAYGEAKSEPNSSLLRSYTESPHSPERLEPIPSGGSSGSNSNSLLKASKRRMSSCGQRSLLDIISSAERSQANKRLDFS
SQ  GRLCTPLGQVAKLYPDFGNKEKDSLLAGTTAAPNVKEESIRS
//
ID  B3P100;
PN  Protein asunder;
GN  asun;
OS  7220;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B3P100;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSADGGATGAAGNATGGGGSQFSKSLWTCACESSIEYCRVVWDLFP
SQ  GKKHVRFIVSDTAAHIVNTWSHSTQNMSHVMNAMVMVGVPSRNVATSSDYSVIHGLRAAIEALAEPTDEQLAAMADLGTD
SQ  ELPRIPNKGRVICITSARDNTSMKSLEDIFNTVLVQQNALAAPPAKKGLVIDHCHLVILNIVPLGVESLVTNRSLLKISP
SQ  LLDVEIHTVSAPDISYKLTHLILNHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGAT
SQ  YETVTLKWCTPRGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFVHSL
SQ  CITRSCMDEAPSITDGPGGRVSDYRTAELGQLIKMSRMVPLKVKDPSAPPLARRLPRYFPLTTSSSILFHLQRHINWLPH
SQ  FLHILVKEDMDKQDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKLSKAKDQYRLLYRELEQLIQLNATTMHHKNLLES
SQ  LQSLRAAYGDAPLKSEPGASLLRSYTESPLSPERLEPITSGSASGSSNSNSLLKASKRRMSSCGQRSLLDIISSAERSQS
SQ  NKRLDFSGRLCTPLGQVAKLYPDFGNKDKDSVVTAASITPNVKEESVRS
//
ID  B4JHB4;
PN  Protein asunder;
GN  asun;
OS  7222;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B4JHB4;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNEKTIFVLDHTRYFSISSEQYISMDYLKGKPMPAETPAAGSSVGTQLSKSLWTCAVESSIEYCRIVWDLFPGRKHV
SQ  RFIVSDTAAHIVNTWSPSTQNMSHVSNAMMMVSVPSRSIPQSSDYSVIHGLRAAIEALAEPTDEQLQAAQVGCKKISNEG
SQ  RVICITSARDNTSMKSLEDIFNTVLLQQNALVGPPGKKGLSIDHCHLVILNIVPLGVESLVTNRSLLEISPLLDVEIHTV
SQ  HAPNISDKLLHLIMGHYDLASTTVTNIPMKEEQNANSSANYDVEILHARAAHTKVCGPDFTLTTSIKPGTSYETVTLKWC
SQ  TPRGCGSSDLQPCVGQYNVTPVDVTSRPSSCLINFLLNGRSVLLEVPRKTGTKTTSHMLSARGGEIFVHSLSIARSAMDE
SQ  APSITDGPGGRVADYRIPELGQLLKMSRMVPLKAKPKGKMSQGEHLWRRLPRYFPRTMNVTILFNLQRQLSWLPHFLHLL
SQ  VKEDMDKQDEVRCQQQIHELYKSASRGDMLPFTNTNNTRPKMSKTKDQYRLFYRELEQLIQLNVQTVHHKNLLESLQSLR
SQ  AAYGDVTNKSEPGAAHLRSYTESPLSPERLEPNSTSSSSNSLLKASKRRMSSSGQRSLLDMISSAERSQSSKRLDFTGRL
SQ  CTPIGQTAKLYPDFGNKDKDILTPGVIPSNLKDDSIRS
//
ID  Q9VEX5;
PN  Protein asunder;
GN  Asun;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:19357193, ECO:0000269|PubMed:23097424}. Cytoplasm {ECO:0000269|PubMed:19357193, ECO:0000269|PubMed:23097424, ECO:0000269|PubMed:9799434}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19357193}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes (PubMed:19357193). Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M (PubMed:23904267). {ECO:0000269|PubMed:19357193, ECO:0000269|PubMed:23904267}.
DR  UNIPROT: Q9VEX5;
DR  UNIPROT: Q27924;
DR  UNIPROT: Q7JP08;
DR  Pfam: PF10221;
DE  Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box- dependent processing (PubMed:23097424). Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1 and U5 (PubMed:23097424). Plays a role as a regulator of spermatogenesis (PubMed:19357193). Crucial regulator of the mitotic cell cycle and development (PubMed:15737938, PubMed:19357193). Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes (PubMed:19357193,PubMed:23904267). Plays a role in sperm motility and fertility (PubMed:19357193). May have a role in the PNG/PLU/GNU pathway (PubMed:15737938). {ECO:0000269|PubMed:15737938, ECO:0000269|PubMed:19357193, ECO:0000269|PubMed:23097424, ECO:0000269|PubMed:23904267}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VYQ0; IntAct: EBI-224684; Score: 0.00
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSADGGATGAAGNATGSGGSQFSKSLWTCACESSIEYCRVVWDLFP
SQ  GKKHVRFIVSDTAAHIVNTWRPSTQNMAHVMNAMLIVGVPSRNVPTSSDYSVIHGLRAAIEALAEPTDEQLAAMADFGTD
SQ  ELPRIPNKGRVICITSARDNTSMKSLEDIFNTVLVQQNTLAAPPSKKGLVIDHCHLVILNIVPLGVESLVTNRSLLKISP
SQ  LLDVEIHTVSAPDISYKLTHLILNHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGAT
SQ  YETVTLKWCTPRGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFVHSL
SQ  CITRSCMDEAPSITDGPGGRVSDYRTAELGQLIKMSRVVPLKVKDPSAPPLTRRLPRYFPLTTSSSILFHLQRHISWLPH
SQ  FLHLLVKEDMDKQDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKLSKAKDQYRLLYRELEQLIQLNATTMHHKNLLES
SQ  LQSLRAAYGDAPLKSEPGASLLRTYTESPLSPERLEPISSVGASGSSSSNSLLKASKRRMSSCGQRSLLDIISSAERSQS
SQ  NKRLDFSGRLCTPLGQVAKLYPDFGTKDKDTVTTGASITPNVKEESVRS
//
ID  B4K5S8;
PN  Protein asunder;
GN  asun;
OS  7230;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B4K5S8;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSISSEQYISMDYLKGKPVAESPGSGSSIVGTQLSKSLWTCAVESSIEYCRIVWDLFPGKKHV
SQ  RFIVSDTAAHIVNTWSPSTQNMSHVSNAMMMVSVPSRSIPQSSDYSVIHGLRAAIEALAEPTDEQLQAAHAGCKRIGNKG
SQ  RVICITSARDNTSMKSLEDIFNTVLIQQNALVAPPSKKGLQIDHCHLVILNIVPLGVESLVTNRSLLEISPFLNAEIHTV
SQ  NAPEISDKLLHLIMGHYDLASTTVTNIPMKEEQNANSSANYDVEILHERAAHTKVCGPDFTFTTSIKPGTAYETVTLKWC
SQ  TPRGCGSADLQPCVGQYNVTPVDVTSRPSSCLINFLLNGRSVLLEVPRKSGTKTTSHMLSARGGEIFVHSLSIARSAMDE
SQ  APSITDGPGGRVPDYRIPEMGQLLKMSRLVPLKTRPKGKCSQGEHLWRRMPRYFPRTANATILFNLQRQLSWLPHFLHLL
SQ  VKEDMDKQDEVRCQQQIHELYKSASRGDLLPFSNSNNARLKVNKTKDQYRLFYRELEQLIQLNAHTPHHKNLLESLQSLR
SQ  AAYGDASNKSDPSAAHLRSYTESPLSPERLEPTNSVNSSSSSILKASKRRMSGCGQRSLLDIISSAERSQSSKRLDFSGR
SQ  LCTPLGQTAKLYPEFGNKDKEILTPGVIPSSLKDESIRS
//
ID  B4GFN8;
PN  Protein asunder;
GN  asun;
OS  7234;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B4GFN8;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSAHSSAGGSSQFSKSLWTCACESSIEYCRVVWDLFPGKKHVRFIV
SQ  SDTAAHIVNTWSASTQNMSHVMNAMVMVGVPSRSMPQSSDYSVIHGLRAAIEALAEPTDEQSQAMASGIPDDLILNEGRV
SQ  ICITSARDNTSMKSLEDIFNTVLIQQNVLSATPPKKGLGINHCHLVILNIVPLGIDSMVTNRNLLEISPLLDVEIHTVGA
SQ  PDISYKLTHLILDHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGATYETVTLKWCTP
SQ  RGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFIHSLCITRSCMDEAP
SQ  SIADGPGGRVNDYRTSELGQLMKMSRMVPLKSRDPAAPNLPRRLPRYFPLTTTSTVLFHLQRHLSWLPHFLHLLVKEMDK
SQ  QDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKPHKAKDQYRLLYRELEQLIQLNASTVHHKNLLESLQTLRAAYGDAP
SQ  SKSEAGTVNLRSFTESPLSPERLEAMSNVSISSSTNSNSLLKASKRRMSNCGTRSLLDIISSAERSQSNKRLDFSGRICT
SQ  PIGQIAKLYPDFGNKEKDAAAAAAASGVGVAPKE
//
ID  Q295U5;
PN  Protein asunder;
GN  asun;
OS  46245;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: Q295U5;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSAHSSAGGSSQFSKSLWTCACESSIEYCRVVWDLFPGKKHVRFIV
SQ  SDTAAHIVNTWSASTQNMSHVMNAMVMVGVPSRSMPQSSDYSVIHGLRAAIEALAEPTDEQSQAMASGVPDDLILNEGRV
SQ  ICITSARDNTSMKSLEDIFNTVLIQQNVLSATPPKKGLGINHCHLVILNIVPLGIDSMVTNRNLLEISPLLDVEIHTVGA
SQ  PDISYKLTHLILDHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGATYETVTLKWCTP
SQ  RGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFIHSLCITRSCMDEAP
SQ  SIADGPGGRVNDYRTSELGQLMKMSRMVPLKSRDPAAPNLPRRLPRYFPLTTTSTVLFHLQRHLSWLPHFLHLLVKEMDK
SQ  QDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKPHKAKDQYRLLYRELEQLIQLNASTVHHKNLLESLQTLRAAYGDAP
SQ  SKSEAGTANLRSFTESPLSPERLEAMSNVSISSSTNSNSLLKASKRRMSNCGTRSLLDIISSAERSQSNKRLDFSGRICT
SQ  PIGQIAKLYPDFGNKEKDAAAAAAASGVGVAPKE
//
ID  B4IBY5;
PN  Protein asunder;
GN  asun;
OS  7238;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B4IBY5;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSGDGGATGAAGNATGSGGSQFSKSLWTCACESSIEYCRVVWDLFP
SQ  GKKHVRFIVSDTAAHIVNTWSPSTQNMSHVMNAMVMVGVPSRNLPTSSDYSVIHGLRAAIEALAEPTDEQLAAMADLGTD
SQ  ELSRIPNKGRVICITSARDNTSMKSLEDIFNTVLVQQNTLAAPPAKKGLIIDHCHLVILNIVPLGVESLVTNRSLLKISP
SQ  LLDVEIHTVSAPDISYKLTHLILNHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGAT
SQ  YETVTLKWCTPRGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFVHSL
SQ  CITRSCMDEAPSITDGPGGRVSDYRTAELGQLIKMSRMVPLKVKDPSAPPLTRRLPRYFPLTTSSSILFHLQRHISWLSH
SQ  FLHLLVKEDMDKQDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKLSKAKDQYRLLYRELEQLIQLNATTMHHKNLLES
SQ  LQSLRAAYGDAPLKSEPGASLLRSFTESPLSPERLEPISSVGASGSSNSNSLLKASKRRMSSCGQRSLLDIISSAERSQS
SQ  NKRLDFSGRLCTPLGQVAKLYPDFGTKDKDAVTTGASITPNVKEESVRS
//
ID  B4QX59;
PN  Protein asunder;
GN  asun;
OS  7240;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B4QX59;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSGDGGATGAAGNATGSGGSQFSKSLWTCACESSIEYCRVVWDLFP
SQ  GKKHVRFIVSDTAAHIVNTWSPSTQNMSHVMNAMVMVGVPSRNVPTSSDYSVIHGLRAAIEALAEPTDEQLAAMADLGTD
SQ  ELPRIPNKGRVICITSARDNTSMKSLEDIFNTVLVQQNTLAAPPAKKGLVIDHCHLVILNIVPLGVESLVTNRSLLKISP
SQ  LLDVEIHTVSAPDISYKLTHLILNHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGAT
SQ  YETVTLKWCTPRGCGSAHLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFVHSL
SQ  CITRSCMDEAPSITDGPGGRVSDYRTAELGQLIKMSRMVPLKVKDPSAPPLTRRLPRYFPLTTSSSILFHLQRHISWLPH
SQ  FLHLLVKEDMDKQDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKLSKAKDQYRLLYRELEQLIQLNATTMHHKNLLES
SQ  LQSLRAAYGDAPLKSEPGASLLRSFTESPLSPERLEPISSVGASGSSNSNSLLKASKRRMSSCGQRSLLDIISSAERSQS
SQ  NKRLDFSGRLCTPLGQVAKLYPEFGTKDKDAVTTGASITPNVKEESVRS
//
ID  B4LWT5;
PN  Protein asunder;
GN  asun;
OS  7244;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B4LWT5;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSISSEQYISMDYLKGKPVQETPASGSSSMVVGTQLSKSLWTCAVESSIEYCRIVWDLFPGKK
SQ  HVRFIVSDTAAHIVNTWSPSTQNMSHVSNAMMMVSVPSRSIPQSSDYSVIHGLRAAIEALAEPTDEQLLATQVGCKQIPN
SQ  KGRVICITSARDNTSMKSLEDIFNTVLLQQNALVAPPSKKGLQIDHCHLVILNIVPLGVESLVTNRNLLEISPLLDVEIH
SQ  TVNAPDISDKLLHLIMGHYDLASTTVTNIPMKEEQNANSSANYDVEILHERAAHTRVCGPDFTLTTSIKPGTTYETVTLK
SQ  WCTPRGCGSSDLQPCVGQYNVTPVDVTSRPSSCLINFLLNGRSVLLEVPRKTGTKTTSHMLSARGGEIFVHSLSIARSAM
SQ  DEAPSISDGPGGRVSDYRIPELGQLFKMSRMVPLKTKPKGKCSQGEHLWRRLPRYFPRTTNVTILFNLQRQLNWLPHFLH
SQ  LIVKEDMDKQDEVRCQQQIHELYKSASRGDMLPFNTTNNARPKVGKTKDQYRLFYRELEQLIQLNAQTPHHKNLLESLQS
SQ  LRAAYGDVSSKLDPGASHLRSYTESPLSPERLEPTSSASNSSSSILKASKRRMSSSGQRSLLDMISIAERSQSNKRLDFS
SQ  GRLCTPLGQTAKLYPDFGNKEKDILTPGVVTSNLKDESIRS
//
ID  B4NIM7;
PN  Protein asunder;
GN  asun;
OS  7260;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B4NIM7;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSIASEEYISMEYLKGKQTGLEAGANGGTQFSKSLWTCACESSIEYCRVVWDLFPGTKHVRFI
SQ  VSDTAAHIVNTWSPSTQNMSHVMNAMVMVGVPSMPQSSDSSVIHGLRAAIEALAEPTDEQMQAMGGKQTLHIPNEGRVIC
SQ  ITSARDNTSMKSLEDIFHTVLVQQNSLMTSPPSKKGLPIDHCHLVILNIVPLGVESLVTNRSLLEISPLLNVEIHTVPAP
SQ  DISYKLTHLILDHYELASTTVTNIPMKEEQNANSSANYDVEILHSRQAHTIAGGPDFNLPTSIKTGSTYETVTLKWCTPR
SQ  GCSSADLQPCLGQFRVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGTKATSHMLSARGGEIFVHALSILRSCMDEAPA
SQ  IQDGPGGRVTDYRFGELGQLIKLSRMIPLKAKDPSHPTHSTLRRRLPRYFPWTTSSSILFNLQRQINWLPHFLHLLVKED
SQ  MDKQDEVRCQQHIHELYKSASRGDMLPFTNSNGGRLKLSKAKDQYRLLYRELEQLIQLNSFTPHHKNLLESLQSLRSAYG
SQ  DAPTKSESANALLRSYTESPLSPERLEPTSSSSSNSLLKARKRRMSTCGQRSLFDIISSAERSQSNKRLDFSGRLCTLPG
SQ  QVAKLYPDFGNKDKDSLVIAGGVASTTASAKEESIRG
//
ID  B4PR20;
PN  Protein asunder;
GN  asun;
OS  7245;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin on the nuclear surface at the meiotic G2/prophase transition in primary spermatocytes. Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
DR  UNIPROT: B4PR20;
DR  Pfam: PF10221;
DE  Function: Plays a role as a regulator of spermatogenesis. Crucial regulator of the mitotic cell cycle and development. Required for the correct dynein-dynactin perinuclear localization important for nucleus- centrosome coupling that occur upon meiotic progression of primary spermatocytes. Crucial regulator of the mitotic cell cycle and development. Plays a role in sperm motility and fertility. May have a role in the PNG/PLU/GNU pathway (By similarity). {ECO:0000250|UniProtKB:Q9VEX5}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0032039;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051301;
GO  GO:0051642;
GO  GO:0046843;
GO  GO:0030317;
GO  GO:0051321;
GO  GO:0051663;
GO  GO:0060814;
GO  GO:0080154;
GO  GO:0007346;
GO  GO:0034472;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFERNQKTIFVLDHTRYFSIASEEYISMDFLKGKPSADGGATGAAGNASGGGGSQFSKSLWTCACESSIEYCRVVWDLFP
SQ  GKKHVRFIVSDTAAHIVNTWSPSTQNMSHVMNAMVMVGVPSRNVPTSSDYSVIHGLRAAIEALAEPTDEQLAAMADLGTD
SQ  ELPRIPNKGRVICITSARDNTSMKSLEDIFNTVLVQQNALAAPPAKKGLVIDHCHLVILNIVPLGVESLVTNRSLLKISP
SQ  LLDVEIHTVSAPDISYKLTHLILNHYDLASTTVTNIPMKEEQNANSSANYDVEILHSRRAHSITCGPDFSLPTSIKQGAT
SQ  YETVTLKWCTPRGCGSADLQPCLGQFLVTPVDVTSRPSSCLINFLLNGRSVLLEMPRKTGSKATSHMLSARGGEIFVHSL
SQ  CITRSCMDEAPSITDGPGGRVSDYRTAELGQLIKMSRMLPLKVKDPSAPPLTRRLPRYFPLTTSSSILFHLQRHISWLPH
SQ  FLHLLVKEDMDKQDEVRCQQHIHELYKSASRGDVLPFTHTNGARLKLSKAKDQYRLLYRELEQLIQLNATTMHHKNLLES
SQ  LQSLRAAYGDAPLKSEPGASLLRSYTESPLSPERLEPNSSGSASGSSNSNSLLKASKRRMSSCGQRSLLDIISSAERSQS
SQ  NKRLDFSGRLCTPLGQVAKLYPDFGNKDKDTVASGASITPNVKEESVRS
//
ID  Q9W1C5;
PN  Integrator complex subunit 1;
GN  IntS1;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:23288851}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9W1C5;
DR  UNIPROT: Q8IGA9;
DR  Pfam: PF12432;
DE  Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box- dependent processing (PubMed:21078872, PubMed:23097424). Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 (PubMed:21078872, PubMed:23097424, PubMed:23288851). Required for the normal expression of the Integrator complex component IntS12 (PubMed:23288851). May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity). {ECO:0000250|UniProtKB:Q8N201, ECO:0000269|PubMed:21078872, ECO:0000269|PubMed:23097424, ECO:0000269|PubMed:23288851}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KMQ0; IntAct: EBI-230031; Score: 0.00
DE  Interaction: Q9V4A1; IntAct: EBI-250364; Score: 0.00
DE  Interaction: Q9VP27; IntAct: EBI-264252; Score: 0.00
DE  Interaction: Q01083; IntAct: EBI-511436; Score: 0.37
DE  Interaction: Q24322; IntAct: EBI-2889720; Score: 0.00
DE  Interaction: P34082; IntAct: EBI-9928090; Score: 0.35
DE  Interaction: Q0E8S4; IntAct: EBI-9930145; Score: 0.46
DE  Interaction: Q9VJW9; IntAct: EBI-9930427; Score: 0.35
DE  Interaction: O97159; IntAct: EBI-9943837; Score: 0.35
DE  Interaction: P18431; IntAct: EBI-9950635; Score: 0.35
DE  Interaction: Q9VPR7; IntAct: EBI-9953078; Score: 0.35
DE  Interaction: M9NFI9; IntAct: EBI-9959939; Score: 0.35
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0045666;
GO  GO:0034472;
GO  GO:0016180;
GO  GO:0034474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDRGKGSGSNRSQKKVPLGGELFALGKSVRDDSKSKILPIKGMSSSDRKREASTALASSSKRFRGNLKDAGAPDMSSGSS
SQ  QCETWEQFAVDCDLDTVVETIYAALEQNDSETVGRLVCGVIKQTTTSSSRSKVDNIALLALIYVAKVQPSIFCTDIVACA
SQ  LLSFLRREANVKMRYNTNLHILFANLLTRGFMEISQWPEVLLRIYIDDAVNERYWADNELCAPLVKNICAAFKTRTPHIS
SQ  LLRWDVSSSLPSGQAHRDSMTVDDDSGDNSTQSLDASPLNTESEPIPDAMCTTKSRFSDAVVQKHVSDAIRDQLNKRQQQ
SQ  DNYTRNFLKFLCTTSGIAEVRCLSISRLELWIHNGKLVKFAQQLLSYICFNIKGRNTQDNEVLLVLVKMRLKTKPLINHY
SQ  MSCLKEMIFLQPEILSTVMKLVVQNELSNTRNPNNMGMLATMFQTSADQSAATLAEIYQEFLLQRDDCLRTLRVFLRELV
SQ  RMLRFDVNLVKFCKTFLSEREDLTPQIEMFEFKERIFNSMVDIVCLCMFLSATPQAREASLSLKTNRDTKNNHALLKLYN
SQ  QMSQIQLDTVSWMYETVPTLFKIPAAEYHQALHKLLLLDSPEQYSRCDQWPSEPERGAILRIISETPIHEETLLRIILIG
SQ  ITKDIPFSIANTFDVLLLVIKRVSGMKATNIPAVQANKFDIIDFLFSMSEYHHPENIRLPAEYEPPKLAIIAFYWKAWLI
SQ  LLMISAHNPSSFGAFCWDHYPTMKMMMEICITNQFNNSSATKDELQIITMERDHILQFETYLAAQTSPHAVITEETAILI
SQ  TQLMLMDPMGTPRKVPSMVLDQLKFLNQTYKLGHLFCRCRKPDLLLDIIQRQGTTQSMPWLSDLVQNSEGDFSHLPVQCL
SQ  CEFLLFNAHIINEENSRDAELVNFLRNLIFDGNLSHQIVCELLDYIFRRLSSTVKQSRVAALSGLKIIFRHSGDFENEWL
SQ  LKSLQQIPHFYEVKPFIIPQLRAACQVENCPELIMAYIQFITAHTLNDPVNEMLDHVIDMAQLIVERSTMFQHIIISQED
SQ  YDYVPDENRIQTLKCLFVMFNNYIIKLREYHEPYEWTEYPDLLMVQFDDGVQLPLHINIIHAFIILLTYSNSNMPESIPI
SQ  LDYWFPPGRPAPVAFLPSMPQEQVQLLPDWLKLKMIRSSVDRLIEAALNDLTPDQIVLFVQNFGTPVNSMSKLLAMLDTA
SQ  VLEQFDLVKNAILNKAYLAQLIEIQQARGAKNGHYTVQALDLHSHSQTVPDLPKISVVIQEAVEIDDYDSSDSDDRPTNF
SQ  LATKEVAQTILTQPDQLTESRSDCRSLIQKLLDMLASPNSNRADVVNAITEVLAVGCSVTMSRHACTFLRTFFSCMLHSD
SQ  KYHILENALQKNLSMFKHTFADSSLLQKSELYHESLVFMLRNSREIYAQQFKANTALVARKRIVRAIVQSFDQTKDSKTV
SQ  AKSKSDQLFHNGLFIDWLSEMDPEIVSTQLMKERFLFSKSCSEFRFYLLSLINHQTNWDTIERIAEYLFKNFHEDYDYAT
SQ  VLNYFEALTTNPKLWKGRDKYMSKNVRPDAFFMLRTSELEPFSHFILHEGLSEVKLDSKNYDFKLCSRMNLLFKLTEKRR
SQ  DLMVKVMEHVEKSSVSDYLKLQVLQQMYIMYPRIKFLKPGKTGEQAYKLQNLKGCQADKVSNNLITCLGSLVGKKDFETL
SQ  STDTELLLRKLAASHPLLFLRQLGVLSSIMQGRAQLSMKALREEHHFHRFVQILRTLELLQPTIFEEAYKNEIQNTLSCY
SQ  FNFFKHHSNVKEACQMLNKFVQMLQAYINYNPSSALLFIEQYVGILKELAAKYTSLGKLQVLVQAVALLQHKSHSATELD
SQ  DEEVKYEYDLDEHFDVKPSASKPVVTEDPIEVNPQTPIDPSSSRGPLSVLTLGSYSRSNYTDISPHFLDLVKIIKQSNTE
SQ  DVVLGPMQELECLTSKRFVFINELFERLLNLIFSPSAQIRSIAFIILIRHLKHNPGNSDINLCTLNAYIQCLRDENSSVA
SQ  ATAIDNLPEMSVLLQEHAIDILTVAFSLGLKSCLNTGHQIRKVLQTLVIQHGY
//
ID  Q8N201;
PN  Integrator complex subunit 1;
GN  INTS1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q8N201;
DR  UNIPROT: A6NJ44;
DR  UNIPROT: Q6NT70;
DR  UNIPROT: Q6UX74;
DR  UNIPROT: Q8WV40;
DR  UNIPROT: Q96D36;
DR  UNIPROT: Q9NTD1;
DR  UNIPROT: Q9P2A8;
DR  UNIPROT: Q9Y3W8;
DR  PDB: 7CUN;
DR  PDB: 7PKS;
DR  Pfam: PF12432;
DR  OMIM: 611345;
DR  OMIM: 618571;
DR  DisGeNET: 26173;
DE  Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (PubMed:23904267). {ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
DE  Disease: Neurodevelopmental disorder with cataracts, poor growth, and dysmorphic facies (NDCAGF) [MIM:618571]: An autosomal recessive neurodevelopmental disorder characterized by severe global developmental delay with motor impairment, cognitive delays, absent or severely limited speech, dysmorphic features, hypotonia and cataracts. {ECO:0000269|PubMed:28542170, ECO:0000269|PubMed:30622326, ECO:0000269|PubMed:31428919}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P0DTC7; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q86WV6; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: O75398; IntAct: EBI-736610; Score: 0.00
DE  Interaction: P03372; IntAct: EBI-2878124; Score: 0.53
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: P83916; IntAct: EBI-4407371; Score: 0.35
DE  Interaction: Q76MZ3; IntAct: EBI-10991736; Score: 0.35
DE  Interaction: Q96BD8; IntAct: EBI-11000226; Score: 0.35
DE  Interaction: P30153; IntAct: EBI-11055988; Score: 0.57
DE  Interaction: P49286; IntAct: EBI-11578409; Score: 0.00
DE  Interaction: C5E526; IntAct: EBI-12585110; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12589250; Score: 0.35
DE  Interaction: P67775; IntAct: EBI-14026281; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-21537775; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-21559824; Score: 0.35
DE  Interaction: P49146; IntAct: EBI-21569349; Score: 0.35
DE  Interaction: O75251; IntAct: EBI-21611249; Score: 0.35
DE  Interaction: P35372; IntAct: EBI-21672468; Score: 0.35
DE  Interaction: P51648; IntAct: EBI-21787778; Score: 0.35
DE  Interaction: A1L0T0; IntAct: EBI-21879063; Score: 0.35
DE  Interaction: Q96CB8; IntAct: EBI-21895368; Score: 0.40
DE  Interaction: P19387; IntAct: EBI-15710289; Score: 0.35
DE  Interaction: P68431; IntAct: EBI-16793336; Score: 0.27
DE  Interaction: P59635; IntAct: EBI-25688593; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574478; Score: 0.35
DE  Interaction: Q9NVR2; IntAct: EBI-26618296; Score: 0.40
DE  Interaction: Q9NVM9; IntAct: EBI-26618901; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0001833;
GO  GO:0043154;
GO  GO:0034243;
GO  GO:0016180;
GO  GO:0034474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNRAKPTTVRRPSAAAKPSGHPPPGDFIALGSKGQANESKTASTLLKPAPSGLPSERKRDAAAALSSASALTGLTKRPKL
SQ  SSTPPLSALGRLAEAAVAEKRAISPSIKEPSVVPIEVLPTVLLDEIEAAELEGNDDRIEGVLCGAVKQLKVTRAKPDSTL
SQ  YLSLMYLAKIKPNIFATEGVIEALCSLLRRDASINFKAKGNSLVSVLACNLLMAAYEEDENWPEIFVKVYIEDSLGERIW
SQ  VDSPHCKTFVDNIQTAFNTRMPPRSVLLQGEAGRVAGDLGAGSSPHPSLTEEEDSQTELLIAEEKLSPEQEGQLMPRYEE
SQ  LAESVEEYVLDMLRDQLNRRQPIDNVSRNLLRLLTSTCGYKEVRLLAVQKLEMWLQNPKLTRPAQDLLMSVCMNCNTHGS
SQ  EDMDVISHLIKIRLKPKVLLNHFMLCIRELLSAHKDNLGTTIKLVIFNELSSARNPNNMQVLYTALQHSSELAPKFLAMV
SQ  FQDLLTNKDDYLRASRALLREIIKQTKHEINFQAFCLGLMQERKEPQYLEMEFKERFVVHITDVLAVSMMLGITAQVKEA
SQ  GIAWDKGEKRNLEVLRSFQNQIAAIQRDAVWWLHTVVPSISKLAPKDYVHCLHKVLFTEQPETYYKWDNWPPESDRNFFL
SQ  RLCSEVPILEDTLMRILVIGLSRELPLGPADAMELADHLVKRAAAVQADDVEVLKVGRTQLIDAVLNLCTYHHPENIQLP
SQ  PGYQPPNLAISTLYWKAWPLLLVVAAFNPENIGLAAWEEYPTLKMLMEMVMTNNYSYPPCTLTDEETRTEMLNRELQTAQ
SQ  REKQEILAFEGHLAAASTKQTITESSSLLLSQLTSLDPQGPPRRPPPHILDQVKSLNQSLRLGHLLCRSRNPDFLLHIIQ
SQ  RQASSQSMPWLADLVQSSEGSLDVLPVQCLCEFLLHDAVDDAASGEEDDEGESKEQKAKKRQRQQKQRQLLGRLQDLLLG
SQ  PKADEQTTCEVLDYFLRRLGSSQVASRVLAMKGLSLVLSEGSLRDGEEKEPPMEEDVGDTDVLQGYQWLLRDLPRLPLFD
SQ  SVRSTTALALQQAIHMETDPQTISAYLIYLSQHTPVEEQAQHSDLALDVARLVVERSTIMSHLFSKLSPSAASDAVLSAL
SQ  LSIFSRYVRRMRQSKEGEEVYSWSESQDQVFLRWSSGETATMHILVVHAMVILLTLGPPRADDSEFQALLDIWFPEEKPL
SQ  PTAFLVDTSEEALLLPDWLKLRMIRSEVLRLVDAALQDLEPQQLLLFVQSFGIPVSSMSKLLQFLDQAVAHDPQTLEQNI
SQ  MDKNYMAHLVEVQHERGASGGQTFHSLLTASLPPRRDSTEAPKPKSSPEQPIGQGRIRVGTQLRVLGPEDDLAGMFLQIF
SQ  PLSPDPRWQSSSPRPVALALQQALGQELARVVQGSPEVPGITVRVLQALATLLSSPHGGALVMSMHRSHFLACPLLRQLC
SQ  QYQRCVPQDTGFSSLFLKVLLQMLQWLDSPGVEGGPLRAQLRMLASQASAGRRLSDVRGGLLRLAEALAFRQDLEVVSST
SQ  VRAVIATLRSGEQCSVEPDLISKVLQGLIEVRSPHLEELLTAFFSATADAASPFPACKPVVVVSSLLLQEEEPLAGGKPG
SQ  ADGGSLEAVRLGPSSGLLVDWLEMLDPEVVSSCPDLQLRLLFSRRKGKGQAQVPSFRPYLLTLFTHQSSWPTLHQCIRVL
SQ  LGKSREQRFDPSASLDFLWACIHVPRIWQGRDQRTPQKRREELVLRVQGPELISLVELILAEAETRSQDGDTAACSLIQA
SQ  RLPLLLSCCCGDDESVRKVTEHLSGCIQQWGDSVLGRRCRDLLLQLYLQRPELRVPVPEVLLHSEGAASSSVCKLDGLIH
SQ  RFITLLADTSDSRALENRGADASMACRKLAVAHPLLLLRHLPMIAALLHGRTHLNFQEFRQQNHLSCFLHVLGLLELLQP
SQ  HVFRSEHQGALWDCLLSFIRLLLNYRKSSRHLAAFINKFVQFIHKYITYNAPAAISFLQKHADPLHDLSFDNSDLVMLKS
SQ  LLAGLSLPSRDDRTDRGLDEEGEEESSAGSLPLVSVSLFTPLTAAEMAPYMKRLSRGQTVEDLLEVLSDIDEMSRRRPEI
SQ  LSFFSTNLQRLMSSAEECCRNLAFSLALRSMQNSPSIAAAFLPTFMYCLGSQDFEVVQTALRNLPEYALLCQEHAAVLLH
SQ  RAFLVGMYGQMDPSAQISEALRILHMEAVM
//
ID  Q6P4S8;
PN  Integrator complex subunit 1;
GN  Ints1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q6P4S8;
DR  UNIPROT: Q0KK58;
DR  UNIPROT: Q80UQ7;
DR  UNIPROT: Q91Z01;
DR  UNIPROT: Q9CTF7;
DR  Pfam: PF12432;
DE  Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q8N201}.
DE  Reference Proteome: Yes;
DE  Interaction: Q80Z64; IntAct: EBI-8820601; Score: 0.35
DE  Interaction: Q9WTV7; IntAct: EBI-15985088; Score: 0.35
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0001832;
GO  GO:0001833;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:0016180;
GO  GO:0034474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNRAKPTTVRRPSAAAKPSGHPPPGDFIALGSKGQASESKTTSTLLKPAPSGLPSERKRDASASLSGTSALTGLTKRPKL
SQ  SSTPPLSALGRLAEAAVAEKRAISPSIKEPSVVPIEVLPTVLLDEIEAAELEGNDDRIEGVLCGAVKQLKVTRAKPDSTL
SQ  YLSLMYLAKIKPNIFATEGVIEALCSLLRRDASVNFKAKGNSLVSVLACNLLMAAYEEDENWPEIFVKVYIEDSLGERIW
SQ  VDSPHCRTFVDNIQTAFNTKMPPKSVLLQGEGARSGGELGAGSSPHPSLTEEEDSQTELLIAEEKLSPEQEGQLMPRPRY
SQ  DELTESVEEYVLDMLRDQLNRRQPIDNVSRNLLRLLTATCGYKEVRLLAVQRLEMWLQNPKLTRPAQDLLMSVCMNCNSH
SQ  GSEDMDVISHLIKIRLKPKVLLNHYMLCIRELLNAHKDNLGTTIKFVIFNELSNARNPNNMQILYTVLQHSSELAPKFLA
SQ  MVFQDLLTNKDDYLRASRALLREIIKQTKHEINFQAFCLGLMQERKEPQYLEMEFKERFVVHITDVLAVSMMLGITAQVK
SQ  EAGVAWDKGEKRNLEVLRTFQNQIAAIQRDAVWWLHTVVPSVSKLAPKDYVHCLHKVLFTEQPETYYKWDNWPPESDRNF
SQ  FLRLCSEVPILEDTLMRVLVIGLSRELPLGPADAMELADHLVKRAAAVQADDVEVLKVERIQLIDAVLNLCTYHHPENIQ
SQ  LPPGYQPPNLAISTLYWKAWPLLLVVAAFNPENIGLAAWEEYPTLKMLMEMVMTNNYSYPPCTLTDEETRTEMINRELQI
SQ  SQREKQEILAFEGHLAAASTKQTITESSSLLLSQLTSLDPQGPPRRPPPHILDQVKALNQSLRLGHLLCRSRNPDFLLHI
SQ  IQRQASSQSMPWLADLVQSSEGSLDVLPVQCLCEFLLHDAADSTASGEEDDEGESREQKAKKRQRQQKQRQLLGRLQDLL
SQ  LGPKADEQTTCEVLDYFLRRLGSSQVASRVLAMKGLSLVLSEGGLRDKEEKEPPMEEDIGETDALQGYQWLLRDLPRLPL
SQ  FDSVRTTTALALQQAIHMETDPQTISAYLIYLSQHTPVEEQGPHSDLALDVARLVVERSTIMAHLFSKPSCSTASDAVLS
SQ  ALLSVFSRYVRRMRKSKEGEEVYSWSESQDQVFLRWSSGETATMHILVVHAMVILLTLGPPRSGDSEFSELLDIWFPEKK
SQ  PLPTAFLVDTSEEALLLPDWLKLRMIRSEVPRLVDAALQDLEPQQLLLFVQSFGIPVSSMSKLLQYLDQAVAQDPQTLEQ
SQ  NIMDKNYMAHLVEVQHERGASGGQTFHSLLTASLPPRRDSTEAPKPESSPEPPPGQGRTRAGTQVPVLGPEDDLAGIFLQ
SQ  IFPLSPDPRWQSSSPRPLALALQQALGQELARVRQGNPEVPGITVRLLQAMTTLLSSPHGGTLALAMHHSHFLSCPLMRQ
SQ  LYQYQRAVPQDTGFSSLFLKVLMQILQWLDSPAVEDGPLQAQLKLFATRYSARHRISDVRSGLLHLADALSFHGDLEVAN
SQ  STARAVIATLRSGEKCPVEPELISKVLRGLIEVRSPHLEELLTALFSATTETSCPSPASGPIVVVSSLLLQEKEELLGPS
SQ  KQEVEGASTEAMRLGPASGLLVDWLETLDPEVVCSCPDLQWKLLFSRRKGKGHISAQVLSFRPYLLALLTHQASWSTLHC
SQ  CIRVLLGKSREQRLDPSASLDFLWACIHVPRIWQGRDQRTPQKRREELVLHVQGPELLSLVELILSEAETRSQDGDSAAR
SQ  TLIQTRLPLLLSCCRSNDESIGKVTEHLTSCIQQWGDSVLGQRCRDLLLQLYLQRPEVRVPVPEVLLQSEGATSSSICKL
SQ  DGLVHRFITLLADTSDSRSSESRVADANMACRKLAVAHPVLLLRHLPMIAALLHGRTHLNFQEFRQQNHLAFFLHVLGIL
SQ  ELLQPRVFQSEHQGALWDCLRSFIRLLLNYRKSSRHLAPFISKFVQFIHKYVGCSAPAAVAFLQKHAEPLHDLSFDNSDL
SQ  VMLKSLLAGLSLPSRDGRTDQGLDEEGEDERSAGSLPLVSVSLSTPLTVADVAPHMKRLSRGRAVEDVLETLSDIDEMSR
SQ  RRPEVLGFFSTNLQRLMSSAEESCRNLAFSLALRSIQNNPSIAADFLPTFMYCLGSRDFEVVQTALRNLPEYTLLCQEHA
SQ  AVLLHRAFLVGVYGQIDTSAQISEALKILHMEAVM
//
ID  Q5ZKU4;
PN  Integrator complex subunit 2;
GN  INTS2;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9H0H0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9H0H0}.
DR  UNIPROT: Q5ZKU4;
DR  Pfam: PF14750;
DE  Function: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'- box-dependent processing. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0034472;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAECSGLQFVSPYAFEAMQKVDVVRLAALSDPELRLLLPCLVRMALCAPADQSQSWAQDKKLILRLLSGVEAVNSIVALL
SQ  SVDFHALEQDASKEQQLRHKLGGGSGESILVSQLQHGLTLEFEHSDSPRRLRLVLSELLAIMNKVSESNGEFFLKSSELF
SQ  ESPVYLEEAADVLCILQAELPSLLPIVDVAEALLHVKNGAWFLCLLVANVPDSFNEVCRGLIKNGERQDEESVGGRRRTE
SQ  ALRHLCKMNPSQALRVRGMVVEECHLPGLGVALTLDHTKNESSDDGVSDLVCFVSGLLLGTNAKVRTWFGTFIRNGQQRK
SQ  RDNISSVLWQMRRQLLLELMGILPTVRSTHIVEEADVDTEPNVSVYSGLKEEHVVKASALLRLYCALMGIAGLKPTDEEA
SQ  EQLLQLMTSRPPATPAGVRFVSLSFCMLLAFSTLVSTPEQEQLMVMWLSWMIKEEAYFESISGVSASFGEMLLLVAMYFH
SQ  SNQLSAIIDLVCSTLGMKIVIKPSSLSRMKTIFTQEIFTEQVVTAHAVRVPVTGSLSANITGFLPIHCIYQLLRSRSFTK
SQ  HKVSIKDWIYRQLCETTTPLHPQLLPLIDVYINSILTPASKSNPEATNQPVTEQEILNVFQGLTGGENTRPAQRYSITTQ
SQ  LLVLYYVLSYEEALLANTKILAAMQRKPKSYSSALMDQIPIKYLIRQAQGLQQELGGLHSALLRLLATNYPHLCIVEDWI
SQ  CEEQITGTDALLRRMLLTTIAKNHSPKQLQEAFSMLPGNHTQLMQILEHLTLLSAGELIPYAEVLTSNMNCLLNAGVPRR
SQ  ILQTVNKLWMVLNTVMPRRLWVMTVNALQPSVKIVRQQKYTQNDLMIDPLIVLRCDQRVHRSPPLMDITLHMLNGYLLAS
SQ  KAYLNAHLKETAEQDIRPSQNNAMGPETPEVTREELKNALLAAQDSAAVQILLEICLPTEEEKAQSSSTYSLLKSVQSTT
SQ  SPKSSDVEEEEDSLLCNLREVQCLICCLLHQMYIADPNIVKLVHFQGYPCELLALTVAGIPSMHICLDFIPELIAQPELE
SQ  KQIFAIQLLSFLCIQYALPKSLSVARLAINVMGTLLTVLTQSKRYAFFMPTLPCLVSFCQAFPPLYEDIMSLLIQIGQVC
SQ  ASDVATQTRDFDPIITRLQQLKERPNEVSGLCKDSPYKSCSRDITSVDPDVQLCQCVESTIIEIINMSVSGV
//
ID  Q9VX31;
PN  Integrator complex subunit 2;
GN  IntS2;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9H0H0}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9VX31;
DR  Pfam: PF14750;
DE  Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box- dependent processing (PubMed:21078872, PubMed:23097424). Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 (PubMed:21078872, PubMed:23097424). May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity). {ECO:0000250|UniProtKB:Q9H0H0, ECO:0000269|PubMed:21078872, ECO:0000269|PubMed:23097424}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0010628;
GO  GO:0045666;
GO  GO:0034472;
GO  GO:0016180;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPVRMYDVSPRVFCAMQNLDITLLASYPEAEIRPVLPSLVRMSLLSPLDNTESSMESRKEILAVLIGIEVVNSIVSYLQV
SQ  NYHELENELKKELQARQKSAFFEGQQHEYGLQSGIALGFERADVARKVRVVLSEIFNLQQQVSEQKPAAHSEMLDDGIYL
SQ  EEVVDILCIALAELPSLLNILELTDALVHVPNGHRIICALVANFPDCYRDVVSHVIANCDEDGSDGKHRLMLLMGLSEMN
SQ  PSQALANRSMCVDMLKVPSFMLKLTLKHPEDLIAFLTGLLLGNDQNLRSWFAAYIRSSQKRKGDALNLVRVELLQKVIQT
SQ  TTNAAELRDFNLQGAVLLRLYCALRGIGGLKFNDDEINALSQLVTSCPQATPSGVRFVTLALCMLIACPSLVSTIPLENK
SQ  AVEWLQWLIREDAFFCKRPGTSTSLGEMLLLLAIHFHSNQISAISEMVCSTLAMKIPIRPNSTNRIKQLFTQDLFTEQVV
SQ  ALHAVRVPVTPNLNGTILCYLPVHCIQQLLKSRTFLKHKVPIKSWIFKQICSSVRPVHPVMPALVEVFVNTLIIPNPTGK
SQ  VNIDHMHRPFTEAEILHVFRTSKLTFFAEELPPMAESQELNQIEVTCPLTAQLLMIYYLMLYEDTRLMNLSALGGRKQKE
SQ  YSNNFLGGLPLKYLLQKAHHYHNDYLSLFHPLLRLIISNYPHLSMVDDWLEEHNLAQGNSTVVVSKHELKPETLDRALAA
SQ  IQTKPHLAIRVFKQLLQMPPETQAQYGQQLVKHLPMVFAKSVPRYVKDLYNDIWLRLNAVLPTTLWIMSLRAITNGSDTM
SQ  DRRTFANESLLEPMEVLSCPRFVFCSPYLLMILLRILKGSLAASKTYLNVHMQMQQKQVLDKNGMMQTDAIWEDLRTTLI
SQ  ASQESAAVHILLEVLDYIASKATDRVSHLELREIQGIIGTYVHQAFISEPSLAKLVHFQTYPKSVIPMMVASVPSMHICI
SQ  DFVHEFLNVTEMEKQIFTIDLTSHLVLNYSIPKSLGVSKFCLNVIQTTLSMLTASTKCRFLRNVMPAMVRFVETFPILAD
SQ  DCVNILMTTGRILHSQSSLGMTTMEMPLTDSDKLCTYRDAQLHIIMIEDAFKALVTAVMKKSDLY
//
ID  Q9H0H0;
PN  Integrator complex subunit 2;
GN  INTS2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:16239144}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:23904267}.
DR  UNIPROT: Q9H0H0;
DR  UNIPROT: Q9ULD3;
DR  PDB: 7CUN;
DR  PDB: 7PKS;
DR  Pfam: PF14750;
DR  OMIM: 611346;
DR  DisGeNET: 57508;
DE  Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (PubMed:23904267). {ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
DE  Reference Proteome: Yes;
DE  Interaction: O43463; IntAct: EBI-8471498; Score: 0.37
DE  Interaction: P0DTC7; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q86WV6; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: O60341; IntAct: EBI-8471617; Score: 0.37
DE  Interaction: Q2TAC2; IntAct: EBI-24529057; Score: 0.56
DE  Interaction: Q9H4E7; IntAct: EBI-24620161; Score: 0.56
DE  Interaction: O43639; IntAct: EBI-24639852; Score: 0.56
DE  Interaction: P30153; IntAct: EBI-14025056; Score: 0.35
DE  Interaction: P67775; IntAct: EBI-14026281; Score: 0.35
DE  Interaction: Q8TBP5; IntAct: EBI-21502646; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-21512742; Score: 0.35
DE  Interaction: P16444; IntAct: EBI-21514808; Score: 0.35
DE  Interaction: Q9UK85; IntAct: EBI-21531225; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-21559824; Score: 0.35
DE  Interaction: P46059; IntAct: EBI-21560916; Score: 0.35
DE  Interaction: O60939; IntAct: EBI-21671922; Score: 0.35
DE  Interaction: Q86XK7; IntAct: EBI-21739948; Score: 0.35
DE  Interaction: Q9NZQ7; IntAct: EBI-21740460; Score: 0.35
DE  Interaction: P25445; IntAct: EBI-21766342; Score: 0.35
DE  Interaction: P19387; IntAct: EBI-15710289; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P59635; IntAct: EBI-25688593; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574619; Score: 0.35
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0034243;
GO  GO:0034472;
GO  GO:0016180;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKDQQTVIMTECTSLQFVSPFAFEAMQKVDVVCLASLSDPELRLLLPCLVRMALCAPADQSQSWAQDKKLILRLLSGVEA
SQ  VNSIVALLSVDFHALEQDASKEQQLRHKLGGGSGESILVSQLQHGLTLEFEHSDSPRRLRLVLSELLAIMNKVSESNGEF
SQ  FFKSSELFESPVYLEEAADVLCILQAELPSLLPIVDVAEALLHVRNGAWFLCLLVANVPDSFNEVCRGLIKNGERQDEES
SQ  LGGRRRTDALRFLCKMNPSQALKVRGMVVEECHLPGLGVALTLDHTKNEACEDGVSDLVCFVSGLLLGTNAKVRTWFGTF
SQ  IRNGQQRKRETSSSVLWQMRRQLLLELMGILPTVRSTRIVEEADVDMEPNVSVYSGLKEEHVVKASALLRLYCALMGIAG
SQ  LKPTEEEAEQLLQLMTSRPPATPAGVRFVSLSFCMLLAFSTLVSTPEQEQLMVVWLSWMIKEEAYFESTSGVSASFGEML
SQ  LLVAMYFHSNQLSAIIDLVCSTLGMKIVIKPSSLSRMKTIFTQEIFTEQVVTAHAVRVPVTSNLSANITGFLPIHCIYQL
SQ  LRSRSFTKHKVSIKDWIYRQLCETSTPLHPQLLPLIDVYINSILTPASKSNPEATNQPVTEQEILNIFQGVIGGDNIRLN
SQ  QRFSITAQLLVLYYILSYEEALLANTKTLAAMQRKPKSYSSSLMDQIPIKFLIRQAQGLQQELGGLHSALLRLLATNYPH
SQ  LCIVDDWICEEEITGTDALLRRMLLTNNAKNHSPKQLQEAFSAVPVNNTQVMQIIEHLTLLSASELIPYAEVLTSNMSQL
SQ  LNSGVPRRILQTVNKLWMVLNTVMPRRLWVMTVNALQPSIKFVRQQKYTQNDLMIDPLIVLRCDQRVHRCPPLMDITLHM
SQ  LNGYLLASKAYLSAHLKETEQDRPSQNNTIGLVGQTDAPEVTREELKNALLAAQDSAAVQILLEICLPTEEEKANGVNPD
SQ  SLLRNVQSVITTSAPNKGMEEGEDNLLCNLREVQCLICCLLHQMYIADPNIAKLVHFQGYPCELLPLTVAGIPSMHICLD
SQ  FIPELIAQPELEKQIFAIQLLSHLCIQYALPKSLSVARLAVNVMGTLLTVLTQAKRYAFFMPTLPSLVSFCRAFPPLYED
SQ  IMSLLIQIGQVCASDVATQTRDIDPIITRLQQIKEKPSGWSQICKDSSYKNGSRDTGSMDPDVQLCHCIERTVIEIINMS
SQ  VSGI
//
ID  Q80UK8;
PN  Integrator complex subunit 2;
GN  Ints2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9H0H0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9H0H0}.
DR  UNIPROT: Q80UK8;
DR  UNIPROT: Q5SXZ5;
DR  UNIPROT: Q5SXZ6;
DR  UNIPROT: Q6PCY7;
DR  UNIPROT: Q6ZPU6;
DR  UNIPROT: Q8CB15;
DR  UNIPROT: Q9CSE0;
DR  Pfam: PF14750;
DE  Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q9H0H0}.
DE  Reference Proteome: Yes;
DE  Interaction: D0ZIB5; IntAct: EBI-27035694; Score: 0.35
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0034472;
GO  GO:0016180;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTPEGTGLQFVSPFAFEAMQKVDVVRLASLSDPELRLLLPCLVRMALCAPADQSQSWAQDKKLILRLLSGVEAVNSIVAL
SQ  LSVDFHALEQDASKEQQLRHKLGGGSGESILVSQLQHGLTLEFEHSDSPRRLRLVLSELLAIMNKVSECNGEFFFKSSEL
SQ  FESAVYLEEAADVLCILQAELPSLLPIVDVAEALLRVRNGAWFLCLLVANVPDSFNEVCRGLIKNGERQDEESLGGRRRT
SQ  DALRFLCRMNPSQALKVRGMVVEECHLPGLGVALTLDHTKTEACEDGVSDLVCFVSGLLLGTNAKVRTWFGTFIRNGQQR
SQ  KRETSGSVLWQMRRQLLLELMGILPTVRSTRIVEEADVEMEPTVSVYSGLKEEHVVKASALLRLYCALMGIAGLKPTEEE
SQ  AEQLLQLMTSRPPATPAGVRFVSLSFCMLLAFSTLVSTPEQEQLMVLWLSWMIKEEAYFESTSGVSASFGEMLLLVAMYF
SQ  HSNQLSAIIDLVCSTLGMKIVIKPSSLSRMKTIFTQEIFTEQVVTAHAVRVPVTSNLSANITGFLPIHCIYQLLRSRSFT
SQ  KHKVSIKDWIYRQLCETSTPLHPQLLPLIDVYINSILTPASKSNPEATNQPVTEQEILNLFQEVIGGDSVRLTQRFSITA
SQ  QLLVLYYILSYEEALLANTKTLASMQRKPKSYSSSLMDQIPIKFLIRQAQGLQQELGGLHSALLRLLATNYPHLCIVDDW
SQ  ICEEEITGTDALLRRMLLTSNAKTHSPKQLQEAFSAVPVSHTQVMQIMEHLTLLSASELIPYAEVLTSNMNQLLNSGVPR
SQ  RILQTVNKLWMVLNTVMPRRLWVMTVNALQPSIKFIRQQKYTQNDLMIDPLIVLRCDRRVHRCPPLMDVTLHMLNGYLLA
SQ  SKAYLSAHLKETAEQDRPSPNNTVGLVGQTDAPEVTREELKNALLAAQDSAAVQILLEICLPTEEEKAKGANSDISLRNT
SQ  QGVTTISTPSKETEEGEDNLLCNLREVQCLICCLLHQMYIADPNIAKLVHFQGYPCELLPLTVAGIPSMHICLDFIPELI
SQ  AQPELEKQIFAIQLLSHLCIQYALPKSLSVARLAVNVMGTLLTVLTQAKRYSFFMPTLPSLVSFCRAFPPLYEDIMSLLI
SQ  QIGQVCASDVATQTRDIDPIITRLQQIKEKPSGWSQICKDPSYKNGSRDTGSMDPDVQLCHCIESTIIEIINMSVSGI
//
ID  Q9VFS6;
PN  Integrator complex subunit 5;
GN  omd;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q6P9B9}. Cytoplasm {ECO:0000250|UniProtKB:Q6P9B9}.
DR  UNIPROT: Q9VFS6;
DR  UNIPROT: Q95R54;
DR  Pfam: PF14838;
DR  Pfam: PF14837;
DE  Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box- dependent processing (PubMed:21078872, PubMed:23097424). Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 (PubMed:21078872). May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity). {ECO:0000250|UniProtKB:Q6P9B9, ECO:0000269|PubMed:21078872, ECO:0000269|PubMed:23097424}.
DE  Reference Proteome: Yes;
DE  Interaction: O96607; IntAct: EBI-213285; Score: 0.00
DE  Interaction: Q9VA83; IntAct: EBI-9968819; Score: 0.35
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0010628;
GO  GO:0045666;
GO  GO:0034472;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLRQNLLDQLKHFIETVSNGHSCPQLLTSPNLIKLALGFLEELPATRDIVFEYFALLAEISVQLYVSPEMADPKTGMPVS
SQ  QVKLAGNRQQQQRAPEYEAFNLVKTALQSLVWKGPPAWSPLIANWSLELVAKLSDKYTQRRMTITASCNYWLECSAMHGL
SQ  MTLINSCFRKLTQPEEEACVEIMLNAFHRFPMTFDWIVARLGGCFPYKIIMQILQCGIKRFVDDYRCHLDSEAGILDYMT
SQ  SCHEQHLRAAFREMLREGFAPKKPLDVAVVPFLLITTNYSDTILQSLVNVLVEIYTEDMCEVIVQKAPLWLSNKMFAGMQ
SQ  PTLNNAVLRLNERGATLLLTAAKMAEKYVWCQDFLDNSMQELEQWVLNQRNFPLLADLAYEETKYMLWKSCLSTNLFEQQ
SQ  TAVRLLLVVSSQHPNIYYQTISQLLKKSYAQNPNGIGALIRLLGGQSGMVNFPGFTPGFKMVLEDITLDVQVNNRLPVPP
SQ  GTPTEAFNTFSNLNILARMHKSKNVAPYIKAQHLNQALNECLPKILQIFDCTVNKLVLRIDRDAAERIADKFRAQQSKNS
SQ  NNNNELCNGKDYGKRTKLEPGEDKVDDEDATRMRLAHLIVDLLNNIEAGSRTTVLRTPLVLKLATLSVKYFFVGLTEKTV
SQ  IRRAAASHRSYTLLQRQCSARKIARTVCLRELVERALFYHGHLLGQLEVYQLDELEIPEHEHLILQNLHTSSGANSNRSV
SQ  LHSGIIGRGLRPVLPPSERNCDAEKQALYLKALNACCADLEKPNNVEGYSLVSLLLVELVSTDVMYNGLPFPDEEFTRVT
SQ  MERDMLIRRAFINSPVLWAVLGLIAGHRPALCYSSVLLRALCATCLHHWRGKNVNRFQPTAANDELMLCTKKMLQLLAMS
SQ  QLIPPPLTNLHLIIEHFESAEIALLLRECIWNYLKDHVPSPALFHVDNNGLHWRNTNTQLAKVPPQYVDPLRHLMQRKLS
SQ  TLGPHYHQMFIMGELMEGDSEPDPTARLQIVEID
//
ID  Q6P9B9;
PN  Integrator complex subunit 5;
GN  INTS5;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:23904267}. Cytoplasm {ECO:0000269|PubMed:23904267}.
DR  UNIPROT: Q6P9B9;
DR  UNIPROT: Q8N6W5;
DR  UNIPROT: Q9C0G5;
DR  PDB: 7CUN;
DR  PDB: 7PKS;
DR  Pfam: PF14838;
DR  Pfam: PF14837;
DR  OMIM: 611349;
DR  DisGeNET: 80789;
DE  Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (PubMed:23904267). {ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
DE  Reference Proteome: Yes;
DE  Interaction: P0DTC7; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P10909; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: Q76MZ3; IntAct: EBI-10991736; Score: 0.35
DE  Interaction: A5YKK6; IntAct: EBI-11005861; Score: 0.35
DE  Interaction: P80315; IntAct: EBI-11016531; Score: 0.35
DE  Interaction: Q8IX90; IntAct: EBI-11028949; Score: 0.35
DE  Interaction: P67775; IntAct: EBI-11058007; Score: 0.53
DE  Interaction: Q8BH65; IntAct: EBI-11109889; Score: 0.35
DE  Interaction: Q9D1D4; IntAct: EBI-11111397; Score: 0.35
DE  Interaction: Q9CY25; IntAct: EBI-11113050; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-11113387; Score: 0.35
DE  Interaction: E9Q512; IntAct: EBI-11157436; Score: 0.35
DE  Interaction: Q96SY0; IntAct: EBI-11160850; Score: 0.35
DE  Interaction: P60410; IntAct: EBI-24441770; Score: 0.56
DE  Interaction: P30153; IntAct: EBI-14025056; Score: 0.42
DE  Interaction: P32970; IntAct: EBI-21512742; Score: 0.35
DE  Interaction: Q9UN75; IntAct: EBI-21537575; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-21537775; Score: 0.35
DE  Interaction: P35613; IntAct: EBI-21560440; Score: 0.35
DE  Interaction: Q9UQV4; IntAct: EBI-21563011; Score: 0.35
DE  Interaction: P49146; IntAct: EBI-21569349; Score: 0.35
DE  Interaction: Q8WWB7; IntAct: EBI-21569743; Score: 0.35
DE  Interaction: P01889; IntAct: EBI-21611619; Score: 0.35
DE  Interaction: P40259; IntAct: EBI-21668943; Score: 0.35
DE  Interaction: P01375; IntAct: EBI-21702931; Score: 0.35
DE  Interaction: P08173; IntAct: EBI-21707586; Score: 0.35
DE  Interaction: Q8WVE6; IntAct: EBI-21754350; Score: 0.35
DE  Interaction: Q9NS69; IntAct: EBI-21755768; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q75QN2; IntAct: EBI-26617208; Score: 0.61
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0034243;
GO  GO:0034472;
GO  GO:0016180;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSALCDPPGAPGPPGPAPATHGPAPLSAQELSQEIKAFLTGVDPILGHQLSAREHARCGLLLLRSLPPARAAVLDHLRGV
SQ  FDESVRAHLAALDETPVAGPPHLRPPPPSHVPAGGPGLEDVVQEVQQVLSEFIRANPKAWAPVISAWSIDLMGQLSSTYS
SQ  GQHQRVPHATGALNELLQLWMGCRATRTLMDIYVQCLSALIGSCPDACVDALLDTSVQHSPHFDWVVAHIGSSFPGTIIS
SQ  RVLSCGLKDFCVHGGAGGGAGSSGGSSSQTPSTDPFPGSPAIPAEKRVPKIASVVGILGHLASRHGDSIRRELLRMFHDS
SQ  LAGGSGGRSGDPSLQATVPFLLQLAVMSPALLGTVSGELVDCLKPPAVLSQLQQHLQGFPREELDNMLNLAVHLVSQASG
SQ  AGAYRLLQFLVDTAMPASVITTQGLAVPDTVREACDRLIQLLLLHLQKLVHHRGGSPGEGVLGPPPPPRLVPFLDALKNH
SQ  VGELCGETLRLERKRFLWQHQLLGLLSVYTRPSCGPEALGHLLSRARSPEELSLATQLYAGLVVSLSGLLPLAFRSCLAR
SQ  VHAGTLQPPFTARFLRNLALLVGWEQQGGEGPAALGAHFGESASAHLSDLAPLLLHPEEEVAEAAASLLAICPFPSEALS
SQ  PSQLLGLVRAGVHRFFASLRLHGPPGVASACQLLTRLSQTSPAGLKAVLQLLVEGALHRGNTELFGGQVDGDNETLSVVS
SQ  ASLASASLLDTNRRHTAAVPGPGGIWSVFHAGVIGRGLKPPKFVQSRNQQEVIYNTQSLLSLLVHCCSAPGGTECGECWG
SQ  APILSPEAAKAVAVTLVESVCPDAAGAELAWPPEEHARATVERDLRIGRRFREQPLLFELLKLVAAAPPALCYCSVLLRG
SQ  LLAALLGHWEASRHPDTTHSPWHLEASCTLVAVMAEGSLLPPALGNMHEVFSQLAPFEVRLLLLSVWGFLREHGPLPQKF
SQ  IFQSERGRFIRDFSREGGGEGGPHLAVLHSVLHRNIDRLGLFSGRFQAPSPSTLLRQGT
//
ID  Q8CHT3;
PN  Integrator complex subunit 5;
GN  Ints5;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q6P9B9}. Cytoplasm {ECO:0000250|UniProtKB:Q6P9B9}.
DR  UNIPROT: Q8CHT3;
DR  UNIPROT: Q3TM44;
DR  Pfam: PF14838;
DR  Pfam: PF14837;
DE  Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex. {ECO:0000250|UniProtKB:Q6P9B9}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0032039;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0034472;
GO  GO:0016180;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSALCDPPGAPGPPGPAPATHGPAPLSAQELSQEIKAFLTGVDPILGHQLSAREHARCGLLLLRSLPPARAAVLDHLRGV
SQ  FDESVRAHLAALEESPVAGPPHLRPPPPSHVPTGGPGLEDVVHEVQQVLCEFIRANPKAWAPVISAWSIDLMGQLSSTYS
SQ  GQHQRVPHATGSLNELLQLWMGCRATRTLMDIYVQCLSALIGSCPDACVDALLDTSVQHSPHFDWVVAHIGSSFPGTIIS
SQ  RVLSCGLKDFCVHSGAGGGASACGNSSQPPSTDPFPGSPAIPGEKRVPKIASVVGILGHLASRHGDSIRRELLRMFHDSL
SQ  AGGSGGRNGEPSLQATVPFLLQLAVMSPALLGTVSGELVDCLKPPAVLSQLQQHLQGFPREELDNMLNLAVHLVSQASGT
SQ  GAYRLLQFLVDTAMPASVITTQGLAVPDTVREACDRLIQLLLLHLQKLVHHRGGSPGEGVLGPPPPPRPVPFLDALRNHV
SQ  GELCGETLRLERKRFLWQHQLLGLLSVYTRPSCGPEALGHLLSRARSPEELSLATQLYAGLVVSLSGLLPLAFRSCLARV
SQ  HAGTLQPPFTARFLRNLALLVGWEQQGGEGPSALGARFGESASAHLADLAPLLLHPEEEVAEAAASLLAICPFPSEALSP
SQ  SQLLGLVRAGVHHFFSSLRLHGPPGVASASQLLTRLSQTSPAGLKAVLQLLVEGALHRGNTELFGGEMDGDNETLSIVST
SQ  PLASASLLDINRRHTAAVPGPGGIWSVFHAGVIGRGLKPPKIVQSRNHQEVIYNTQSLVSLLVHCCSASGNSEREGCWGA
SQ  PTLSPEAAKAVAVTLVESVCPDAAGAELAWPPEDHARATVERDLRIGRRFREQPLLFELLKLVAAAPPALCYCSVLLRGL
SQ  LAALLSHWEASRHPDTTHSPWHLEASCILVAVMAEGSLLPPALGNMHEVFSQLAPFEVRLLLLSVWGFLREHGPLPQKFI
SQ  FQSERGRFIRDFAREGGAEGGPHLSVLHSVLHRNIDRLGLFSGRFQAPPPSTLLRQGT
//
ID  O89019;
PN  Inversin;
GN  Invs;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Nucleus. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, spindle. Note=Associates with several components of the cytoskeleton including ciliary, random and polarized microtubules. During mitosis, it is recruited to mitotic spindle (By similarity). Membrane localization is dependent upon cell-cell contacts and is redistributed when cell adhesion is disrupted after incubation of the cell monolayer with low-calcium/EGTA medium. Also nuclear and perinuclear. {ECO:0000250}.
DR  UNIPROT: O89019;
DR  UNIPROT: O88849;
DR  Pfam: PF00023;
DR  Pfam: PF12796;
DR  Pfam: PF00612;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS50096;
DE  Function: Required for normal renal development and establishment of left-right axis. Probably acts as a molecular switch between different Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting cytoplasmic disheveled (DVL1) for degradation by the ubiquitin- proteasome. This suggests that it is required in renal development to oppose the repression of terminal differentiation of tubular epithelial cells by Wnt signaling (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP1, NPHP4 and RPGRIP1L/NPHP8. Does not seem to be strictly required for ciliogenesis. {ECO:0000250, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:9744276, ECO:0000269|PubMed:9771707}.
DE  Reference Proteome: Yes;
DE  Interaction: P11499; IntAct: EBI-4282363; Score: 0.35
DE  Interaction: Q8BP00; IntAct: EBI-4282363; Score: 0.52
DE  Interaction: P63017; IntAct: EBI-4282363; Score: 0.35
DE  Interaction: Q91ZR4; IntAct: EBI-4282363; Score: 0.64
DE  Interaction: P38647; IntAct: EBI-4282363; Score: 0.35
DE  Interaction: P20029; IntAct: EBI-4282363; Score: 0.35
DE  Interaction: Q9QZZ4; IntAct: EBI-4281305; Score: 0.40
DE  Interaction: Q9QY53; IntAct: EBI-4288095; Score: 0.40
DE  Interaction: Q8K3E5; IntAct: EBI-4288102; Score: 0.40
GO  GO:0097546;
GO  GO:0097543;
GO  GO:0005576;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0005516;
GO  GO:0048513;
GO  GO:0060971;
GO  GO:0060287;
GO  GO:0001822;
GO  GO:0090090;
GO  GO:0031016;
GO  GO:0009791;
GO  GO:1904108;
GO  GO:0006468;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MNISEDVLSTGSSLASQVHAAAVNGDKGALQRLIVGNSALRDKEDRFGRTPLMYCVLADRVDCADALLKAGADVNKTDHS
SQ  RRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGEVDTQDKNKQTALHWSAYYN
SQ  NPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDPSAVHTVRCILDAAPTESLLNWQDYEGRTPLHFAVADGNLTVVDVL
SQ  TSYESCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTIPSDSQGATPLHYAAQSNFAETVKVFLQHPSVKDDSDL
SQ  EGRTSFMWAAGKGNDDVLRTMLSLKSDIDINMSDKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEM
SQ  GHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNA
SQ  DPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAF
SQ  KIQAVYKGYKVRKAFRDRKNLLMKHEQLRKDAAAKKREEENKRKEAEQQKGQLDTDPPRSHCSSSAPVLPCPPSPQNEGS
SQ  KQDATPSKQPPASHTVQSPDPEHSRLPGRCPGRASQGDSSIDLQGTASRKPSETPIEHCRGPSACVHPRSWEGGNSSKNQ
SQ  GTSSVEKRRGETNGKHRRCEEGPSSARQPLCTGSGRPAEKGEDSSPAVASASQQDHPRKPNKRQDRAARPRGASQKRRTH
SQ  QLRDRCSPAGSSRPGSAKGEVACADQSSLHRHTPRSKVTQDKLIGGVSSGLPLSTEASRSGCKQLYEDICASPETGVAHG
SQ  PPPGQCMNIHLLPVEQRLLIIQRERSRKELFRRKNKAAAVIQRAWRSYQLRKHLSRLLHLKQLGAREVLRCTQVCTALLL
SQ  QVWRKELELKFPKSISVSRTSKSPSKGSSATKYARHSVLRQIYGCSQEGKGHHPIKSSKAPAVLHLSSVNSLQSIHLDNS
SQ  GRSKKFSYNLQPSSQSKNKPKL
//
ID  Q54C85;
PN  Importin-13 homolog A;
GN  ipo13A;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q54C85;
DR  Pfam: PF18806;
DR  Pfam: PF08389;
DE  Function: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031267;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYNNNGFHEETNIDESQFTVEKVETVLKSLYFPQNNDYSALPQIQQWLIQFQKSFSSWSIAPLLLMSNIKEIQYFGASTI
SQ  ENKIKNNWLSLSQDMKKEFLDNLLLFLKTQITKCSTVVITRLCLAVSVIACHSTTDLWANPILDVLQLSFQDINNLDCFN
SQ  PNLVNLTLELLTIFPEELTNADYITQEKRNKVGLQFNKHNSKVFEILCKIMSLPQNQQTLIFMKSSLKCFKSWILFDCSP
SQ  REYLIDSDLILKCFEAVSNNPKLVEDFLMVLDEMFTFMGGKIFRSYTSAFSLVLSRILMIFPSFYILALQEENQIFNQIF
SQ  LLFSHIAENHIKTLLKNPELSNNFFKALIQMALKGDFETCELLSPVITEIAALHELHSTSSTTEATTTTIATTTTPTTTS
SQ  DCDISGWYQYLGEMVEVFRLKSMYPLDKDISDLYEEDAEKFFAFRVIAGDSVLEVYNILEGKILQQLLNSLWSDIQSFPT
SQ  TKCWQSIEATIYLLSCLSESITEDTEFVPQLFSILGQLPIQSTPLIKSTMTLAGNYSNLIDKSTIFLEKIVKDFFPAFEN
SQ  PDLKSVASQSFLSISKNSKCASILSNSITQLISLCAPILSNNNKILDDPSNFNILEALLYIISTLPSDSQVLNYSTQLLY
SQ  PFILFIKNYYTNQLQQQQQQQQQQQTELRLLLSSINLLTKFCKIYDDEQVNEYGTTQQENNNNNNNNNNNNNNNNNNNNN
SQ  NNNNNIKPVFEIINNIIPIYGELLSLNTLESSIIEAISIFYKKAIMINNNHQNITNIPEINRQLTLAFLKHKPLSLVLST
SQ  LSISIVNLPKEQHLDFLADSLSSISSKMIQIWSEKSNQNNKKNNKKINNNIDIDNDNENNNNNNQIQFENNELNEFKNLK
SQ  ISIYPDITKEYFTMITQYIRYNAVSIPQGVISHLFSIILVNITKIHDKVTARACFSFMALIITKSKEMKSQIKWEPLLNE
SQ  INGWLSIHGELFIKQILYSAGGGIPRSVVQFISEVIASLVSSYPDVFRISALKCLSVDGFPSSNITKEQKEKFLNSLMLY
SQ  RSKKLPLKIVTDFSLVSLGIATNQ
//
ID  Q54WT9;
PN  Importin-13 homolog B;
GN  ipo13B;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q54WT9;
DR  Pfam: PF03810;
DE  Function: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031267;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNTNAMDQYENCPSYGSFDVKSFSDSPIPFTNNNNNNNNNNNNNSICVMPSNYNNKNNNNNNNEKLEPEATLDVLTHALH
SQ  TLYKSNDSNQRKLAEKWLILFQKQPIAWEFCPRLLLETNIFELQYFGASTLESKLKNEWNECNVEMKSKILNTIVSIIQN
SQ  STKLPICCVTRVSVTLTIAVMYTFPEIWRNAIFDIIHLSIKQDINTLSLHDPSQNHFNTDRLLMVLEFLSILPDELKKQD
SQ  LALCKYSEIQKELKLIIDKIYKFLLSVLFLPINENFEFIKISYKALSAWLKYMLPSNGTMLQSCFEISFTVGQQKVSNNS
SQ  NGNGNGNNNNNNNRNSIGYPLIDSLALVLEGSSLSIEGQSNGSCYIEAFRYAIEQSLTIFPTFYNEATVMNQDDSKAKPI
SQ  FNVFVQFISSNNSQLFTTDLIHRCLNLLISFIEIGSRETISLLFYLIDDFKTHTMLVQQDQNILKFFFLKLLNRFLDVSM
SQ  YPNGKDYCPIENGTNPLSTSQNAQFNGVLCETNIETLLDDDIEQFRSCSSDCLMNIQENDIIPKSTFLKFLIEKLNAFIN
SQ  EKCPHWEQYESILYYIYAFSGGSQDGQLEYVPILLNIIPLIPIKSIPLVRTSIKLIGRYSSFLKTNTDYLAKVVSDLLPA
SQ  LSHAELIGSAASSLLSICVSDKCSTMLWPHFNQILDQIEPILLGPQKSNPSIVLVYKSLLHILHKAPIHELSPLFTRLIS
SQ  PVIPNITDHIPRVKSKDHYNQLLVQLSILYSVNEIIEYDEFATMGANGEFTSPSKHPLYPFFQTTIPIQGQLLKHYKSEF
SQ  EIIDCITTFYRYMMLYFREIANDFVDEILQQATQSFNQYPIASLLQIISSIIIPKLQPLTITNIKNSISLISNTFINTLK
SQ  SVILATNNNNKNNDNTNNNDDNNNKNDNNNNNNNNDNDKSNFILDFTITPDITKDYLILITKILKTSPQCIEPNIISTIC
SQ  IYIIYNLTDLTKDKPTTGNCCLFLTNCLSLNNGKLQISDPNGNKVLEQIKNEMNALFESDPKHSYVLVYNILMNICWTPT
SQ  SIQVTQHFSDVLLSFAIGYPNLLKLHATNILNDPNFIKDKQINPHDKQSFLTNILKSNSTQVDYRSSVRTFSFICNDKE
//
ID  A7MB64;
PN  Inositol 1,4,5-trisphosphate receptor-interacting protein;
GN  ITPRIP;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWB1}; Single-pass type I membrane protein {ECO:0000255}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q3TNL8}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: A7MB64;
DR  Pfam: PF03281;
DE  Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5- triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000250|UniProtKB:Q8IWB1}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:0004860;
GO  GO:0008625;
GO  GO:1902042;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALGLFRVCLVVVTAIINHPLLFPRENTTVPENEEEIIRQMQAHQEKLQLEQLRLEEEMARLAADKEAEKEALERVAEEG
SQ  QQQNESRTAWDLWSTLCMILFLVIEVWRQDHQDAPSPECLGSDEDELPDLEGAPLRGLTLPNRATLDHFYERCIRGATAD
SQ  AARTREFVEGFVDDLLEALRSLCSRDSDMEVEDFIGVDSMYENWQVNKPLLCDLFVPFMPPEPYHFHPELWCSSRSVPLD
SQ  RQGYGQIKVVRADEDTLGCICGKTKLGEDMLCLLHGRNNVVHHGSKAADPLCAPNSPYLDTMRVMKWFQTALTRAWHRIE
SQ  HKYEFDLAFGQLDTPGSLKIRFRSGKFMPFNLIPVIQCDDSDLYFVSHLAREPGGGTRASSTDWLLSFAVYERHFLRVTS
SQ  KALPEGACHLSCLQIASFLLSKQSRLTGPSGLGSYHLKTALLHLLLARRPADWKAEQLDARLHELLCFLEKSLLEKKLQH
SQ  FFIGNRKVPQAMGLPEAVRRAEPLNLFRPFVLQRSLYRKTVDSFYEMLKNAPALISEYSLHIPSDHASLPPKTVIL
//
ID  Q567X9;
PN  Inositol 1,4,5-trisphosphate receptor-interacting protein;
GN  itprip;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWB1}; Single-pass type I membrane protein {ECO:0000255}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q3TNL8}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: Q567X9;
DR  Pfam: PF03281;
DE  Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5- triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000250|UniProtKB:Q8IWB1}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005640;
GO  GO:0005886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQGAIARVCMVVVAAILNHPLLFPNENTTVPEQDEDLLARMKEHQEKLEAEQKRLEQEISQNETSVIGDQDGYGWYFWSA
SQ  LCLVIFFTIEVCRQDLISAEIPDPAEDEDGDCSTGYHSAKSIALDRGTLNNFCKTRFFPYTNESGRVREFIEGFADDLLE
SQ  ALRSICDLKADLEVEDFAGIGSMFESWRVSKPPTCDLIVPFSPPQPLRFQFELWCDPSTEIPLDLQGCGRIQLIKPGGNG
SQ  TDCLCGSIDLGDDMLCLLHNRNECEVLEDDALPELLCARDTTYLSKGQIMRWFQISVSKAWGKISHKYDFELAFRNLDFP
SQ  GALKIKFPSGKTVVLNLTPAVQFENTDAYLISHFPSDTSNSSDTHWQLSLSVYEKNLLKHLAKSLPTNSCHIHCLQIVAF
SQ  LHKKQTTLTGRSAFCNYHIKTALLHLLLSKRPAMWQPQNLDSRLRDLLSFLQQSLEEKKLYHALVGNPRIPVEILVPKII
SQ  RTAEPINLYRPLVLQRHVYAKMEEHFEEMVRNTSVLVQEYTPHFSNGHVRHEFSSAEQI
//
ID  Q8IWB1;
PN  Inositol 1,4,5-trisphosphate receptor-interacting protein;
GN  ITPRIP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cell membrane {ECO:0000269|PubMed:16990268}; Single-pass type I membrane protein. Nucleus outer membrane {ECO:0000250|UniProtKB:Q3TNL8}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: Q8IWB1;
DR  UNIPROT: D3DRA5;
DR  UNIPROT: Q5JU17;
DR  UNIPROT: Q96MS8;
DR  UNIPROT: Q9C0A9;
DR  Pfam: PF03281;
DR  DisGeNET: 85450;
DE  Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5- triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000269|PubMed:16990268}.
DE  Reference Proteome: Yes;
DE  Interaction: O15173; IntAct: EBI-23781080; Score: 0.56
DE  Interaction: Q99MK9; IntAct: EBI-2556403; Score: 0.40
DE  Interaction: Q9NS23; IntAct: EBI-6912010; Score: 0.35
DE  Interaction: Q8K2C9; IntAct: EBI-9379702; Score: 0.40
DE  Interaction: Q9HB71; IntAct: EBI-9379744; Score: 0.40
DE  Interaction: Q9BPW0; IntAct: EBI-9379763; Score: 0.40
DE  Interaction: Q3UJD6; IntAct: EBI-9379723; Score: 0.40
DE  Interaction: Q96EQ0; IntAct: EBI-24531039; Score: 0.56
DE  Interaction: Q86WH2; IntAct: EBI-23878826; Score: 0.56
DE  Interaction: Q8WXA8; IntAct: EBI-21508371; Score: 0.35
DE  Interaction: P04201; IntAct: EBI-21538834; Score: 0.35
DE  Interaction: Q86T26; IntAct: EBI-21582478; Score: 0.35
DE  Interaction: Q8WW62; IntAct: EBI-21589315; Score: 0.35
DE  Interaction: Q96FT7; IntAct: EBI-21589962; Score: 0.35
DE  Interaction: Q92187; IntAct: EBI-21641713; Score: 0.35
DE  Interaction: P62195; IntAct: EBI-21656272; Score: 0.35
DE  Interaction: Q9Y5F2; IntAct: EBI-21658599; Score: 0.35
DE  Interaction: P40259; IntAct: EBI-21668943; Score: 0.35
DE  Interaction: P29016; IntAct: EBI-21693940; Score: 0.35
DE  Interaction: P46098; IntAct: EBI-21749232; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-21777303; Score: 0.35
DE  Interaction: Q6PIU2; IntAct: EBI-21801768; Score: 0.35
DE  Interaction: Q86YC3; IntAct: EBI-21811436; Score: 0.35
DE  Interaction: O60603; IntAct: EBI-21859955; Score: 0.35
DE  Interaction: P55058; IntAct: EBI-21861097; Score: 0.35
DE  Interaction: Q4U2R8; IntAct: EBI-21864696; Score: 0.35
DE  Interaction: Q9NZ94; IntAct: EBI-16423332; Score: 0.54
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:0004860;
GO  GO:0008625;
GO  GO:1902042;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAMGLFRVCLVVVTAIINHPLLFPRENATVPENEEEIIRKMQAHQEKLQLEQLRLEEEVARLAAEKEALEQVAEEGRQQN
SQ  ETRVAWDLWSTLCMILFLMIEVWRQDHQEGPSPECLGGEEDELPGLGGAPLQGLTLPNKATLGHFYERCIRGATADAART
SQ  REFLEGFVDDLLEALRSLCNRDTDMEVEDFIGVDSMYENWQVDRPLLCHLFVPFTPPEPYRFHPELWCSGRSVPLDRQGY
SQ  GQIKVVRADGDTLSCICGKTKLGEDMLCLLHGRNSMAPPCGDMENLLCATDSLYLDTMQVMKWFQTALTRAWKGIAHKYE
SQ  FDLAFGQLDSPGSLKIKFRSGKFMPFNLIPVIQCDDSDLYFVSHLPREPSEGTPASSTDWLLSFAVYERHFLRTTLKALP
SQ  EGACHLSCLQIASFLLSKQSRLTGPSGLSSYHLKTALLHLLLLRQAADWKAGQLDARLHELLCFLEKSLLQKKLHHFFIG
SQ  NRKVPEAMGLPEAVLRAEPLNLFRPFVLQRSLYRKTLDSFYEMLKNAPALISEYSLHVPSDQPTPKS
//
ID  Q3TNL8;
PN  Inositol 1,4,5-trisphosphate receptor-interacting protein;
GN  Itprip;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWB1}; Single-pass type I membrane protein {ECO:0000255}. Nucleus outer membrane {ECO:0000269|PubMed:31142202}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: Q3TNL8;
DR  UNIPROT: Q3TAD9;
DR  UNIPROT: Q3TB01;
DR  UNIPROT: Q571G7;
DR  UNIPROT: Q6P400;
DR  Pfam: PF03281;
DE  Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5- triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000250|UniProtKB:Q8IWB1}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3TBT3; IntAct: EBI-10729637; Score: 0.35
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005640;
GO  GO:0005886;
GO  GO:0004860;
GO  GO:0008625;
GO  GO:1902042;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAMELFRVCLVVVTAIINHPLLFPRENATIPENEEEIIRKMQEHQEKLRLEQLRLEEEVSRLEAEKEALRQVEEEQQQLE
SQ  AHTAWDLWTTLCMVLFLIIEVLRQNHQEGTFPECLGGDEDELSGLGGTLLQGLPLPNRATLDHFYEHCIRSTTGDATRTQ
SQ  EFVEGFVDDLLEALRSTYNGKTDMELEDFIGVGSMYENWQVERPLRCHLFIPFIPPEPYSFHPEFWCSSLSTPLERQGYG
SQ  QIKVTLADGNPLGCVCGKAKLEEDMLCLLYGKNRGAWPSSAGCGEMEGLLCSRESSYLDVMQVMKWFQMALTRAWHRIAH
SQ  KYEFDLAFGELDTPGSLKIKFRSGKSMPFILTPVIQCNDSDLYFILQLPKEPCGGGPASSAHWLLSFAVYEREFLRMTGK
SQ  ALPEGACHLSCLQIASFLLSKQTRLTGPSGLSDYHLKTALLHLLLSRQASDWKASKLDVRLQDLFCFLERSLLEKKLYHF
SQ  FMGNHKVPEALGLPEVVRRAEPLNLFRPFVLQRTLYRNTVDSFYEMLKNAPALISEYSLHVPSVRASPPPKAVVS
//
ID  Q90XY5;
PN  Inositol 1,4,5-trisphosphate receptor-interacting protein;
GN  itprip;
OS  31033;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8IWB1}; Single-pass type I membrane protein {ECO:0000255}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q3TNL8}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: Q90XY5;
DR  Pfam: PF03281;
DE  Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5- triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000250|UniProtKB:Q8IWB1}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005640;
GO  GO:0005886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQGAIARMCVLVAAAILNHPLLSPQENATLHDQDEELMARMREHEEMLEKEQAKLEKEFSQLTPEPENIGSEEEYSGYLW
SQ  SSVVFLVFLVIEMFRMHGAHTEIAPFGDEDIYSEGGSLAPRLKALDKEVLNNFCDKCTYTSSNEIWRVREFVEGFADDLL
SQ  ESLRSVCDRDADMEVGDFVGIGSVFESWKVCKPLMCDLLVPFSPPDPFALQFHLWCSCSSNVPPNMQGCGKIKVSKSGGN
SQ  EGCLCGSANMGEDMLCLLHNGNDVPSVERSPDDLLCTRNTSFLSKDQVMKWFQISVTKAWGRISHKYDFEVTFRNLDAAG
SQ  ALKVRFHSGKVVVLNMIPVVQLQDTDAYFVSHFPSGSESPPDPYWPLSFAVYERNLLKLISKRLPQNSCHLHCLQIVTFL
SQ  HRKQASLTGRTALTNYHIKTVLLHLLLGKRASSWGTEHMESRLCDLLSFLHRSLQEKRLHHVMIGNSKVTELIQVPEIIS
SQ  RAEPVNLLRCLVLQAELHAQTLQHFNEMLKNAPALLQDYTPHWSNGLCLLGDGV
//
ID  Q93WC9;
PN  Adenylate isopentenyltransferase 3, chloroplastic;
GN  IPT3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Plastid, chloroplast {ECO:0000269|PubMed:14726522}. Nucleus membrane {ECO:0000269|PubMed:18184738}; Lipid-anchor {ECO:0000269|PubMed:18184738}. Cytoplasm {ECO:0000269|PubMed:18184738}. Note=Farnesylation directs most of the protein to the nucleus/cytoplasm despite the presence of a chloroplast transit peptide (PubMed:18184738).
DR  UNIPROT: Q93WC9;
DR  UNIPROT: Q9LYB1;
DE  Function: Involved in cytokinin biosynthesis. Catalyzes the transfer of an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP and ADP. {ECO:0000269|PubMed:11313355, ECO:0000269|PubMed:15998742, ECO:0000269|PubMed:17062755}.
DE  Reference Proteome: Yes;
GO  GO:0009507;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0009536;
GO  GO:0052623;
GO  GO:0009824;
GO  GO:0005524;
GO  GO:0052622;
GO  GO:0052381;
GO  GO:0009691;
GO  GO:0006400;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:18184738};
SQ  MIMKISMAMCKQPLPPSPTLDFPPARFGPNMLTLNPYGPKDKVVVIMGATGTGKSRLSVDIATRFRAEIINSDKIQVHQG
SQ  LDIVTNKITSEESCGVPHHLLGVLPPEADLTAANYCHMANLSIESVLNRGKLPIIVGGSNSYVEALVDDKENKFRSRYDC
SQ  CFLWVDVALPVLHGFVSERVDKMVESGMVEEVREFFDFSNSDYSRGIKKAIGFPEFDRFFRNEQFLNVEDREELLSKVLE
SQ  EIKRNTFELACRQREKIERLRKVKKWSIQRVDATPVFTKRRSKMDANVAWERLVAGPSTDTVSRFLLDIASRRPLVEAST
SQ  AVAAAMERELSRCLVA
//
ID  Q9SG11;
PN  Protein IQ-DOMAIN 15;
GN  IQD15;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Cell membrane {ECO:0000269|PubMed:28115582}. Nucleus envelope {ECO:0000269|PubMed:28115582}.
DR  UNIPROT: Q9SG11;
DR  Pfam: PF13178;
DR  Pfam: PF00612;
DR  PROSITE: PS50096;
DE  Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post- transcriptional level (By similarity). {ECO:0000250|UniProtKB:Q9SF32}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0005516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGKTDGSSWFTAVKNVFRSPEKLIPRRINRRQDNDLVEEVEDELHQRPKRRKRRWLFKKVSSDPCAINVGINTTSTAINA
SQ  IAAEETEKTVSPAAKETVFFCRTSVYLKRHVAAILIQTAFRGCLARTAVRALKGVVKLQALVRGHNVRRRTSITLQRVQA
SQ  LVRIQALALDHRKKLTTKLGDEISYSHAFSKQMWRTMEREAHSESELEDKRPSRLNGYGYQETGRRMSTDQAIVEPVKIV
SQ  EIDKYNNTYSHHQQLNDQTPRGNSFVTRQAHSIPNYMSTTASTVARFRRPQSVPKQRSNRTCLDNNEPRLRLVRKRLSFH
SQ  NDNPQSYGYIAGDGYFWYDIDKRTNAHEDFQY
//
ID  Q9ZU28;
PN  Protein IQ-DOMAIN 27;
GN  IQD27;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus envelope {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}.
DR  UNIPROT: Q9ZU28;
DR  Pfam: PF13178;
DR  Pfam: PF00612;
DR  PROSITE: PS50096;
DE  Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post- transcriptional level (By similarity). {ECO:0000250|UniProtKB:Q9SF32}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005635;
GO  GO:0005516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGRAARWFKGMFGTKKSKDRSHVSGGDSVKGGDHSGDFNVPRDSVLLGTILTDTEKDQNKNAIAVATATATAADAAVSAA
SQ  VVRLTSEGRAGDIIITKEERWAAVKIQKVFRGSLARKALRALKGIVKLQALVRGYLVRKRAAAMLQSIQTLIRVQTAMRS
SQ  KRINRSLNKEYNNMFQPRQSFDKFDEATFDDRRTKIVEKDDRYMRRSSSRSRSRQVHNVVSMSDYEGDFVYKGNDLELCF
SQ  SDEKWKFATAQNTPRLLHHHSANNRYYVMQSPAKSVGGKALCDYESSVSTPGYMEKTKSFKAKVRSHSAPRQRSERQRLS
SQ  LDEVMASKSSVSGVSMSHQHPPRHSCSCDPL
//
ID  A0A1P8B0B7;
PN  Protein IQ-DOMAIN 29;
GN  IQD29;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus envelope {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24134884, ECO:0000269|PubMed:28115582}. Cell membrane {ECO:0000269|PubMed:28115582}. Note=Associates to cortical microtubules (MTs). {ECO:0000269|PubMed:24134884}.
DR  UNIPROT: A0A1P8B0B7;
DR  UNIPROT: O64504;
DR  UNIPROT: Q56Y97;
DR  Pfam: PF13178;
DR  Pfam: PF00612;
DR  PROSITE: PS50096;
DE  Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post- transcriptional level (By similarity). {ECO:0000250|UniProtKB:Q9SF32}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0005516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGKTPSPGKWIKSLLGKKSSKSSLEKGGEKLRSAKKEELVVKVKDNNVSKLPTEPPVVSSQEVAATQTVVVPDVVIAEKQ
SQ  LSGDIEGDESSNVNLESGNDSEEVKLEEAATKVQAALRAQQAREESQNLKGITRVQAVIRGHLVRRQAVATYSCIWGIVK
SQ  VQALVRGKKARSSETVAQLQKTNTETETSETLQGSTYSWMENPTKLSMIDKLLVSSPTTLPLKIQYSPEDPNSAKVWLGR
SQ  WTQLQVWAPGPLVVKNLVPKSQTKKRSFQAVEAEKGKLKRGVRKPTGVSTTANSSTSRSTADNEKPKRTVRKASTLGKEL
SQ  SKIENDKSKQSSRKSTSAIKEGSSVEVKDEKPRISHKKASLSNGIGKATRKSAEKKKEIADAVQKELPIEEVSVSLVDAP
SQ  EDEKMNLIPVTISKESDLDKDEKSLVLDKPEQDELRTAERDDKAEEELKTAERDDSAEEKIQEPDAQISSENGNVASENT
SQ  KPSDRRASLPAKIENHHQDDGLTQSGRKIPSYMAPTASAKARIRGQGSPRIAQEKPEKNGTTRRHSLPPAANGKLSTMSP
SQ  RAHRLLIASAKGSMNSDRSFSSSKDIGDKSTKAEWKR
//
ID  Q501D2;
PN  Protein IQ-DOMAIN 30;
GN  IQD30;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}.
DR  UNIPROT: Q501D2;
DR  UNIPROT: B9DH53;
DR  UNIPROT: Q2NND8;
DR  UNIPROT: Q9M9V3;
DR  Pfam: PF13178;
DR  Pfam: PF00612;
DR  PROSITE: PS50096;
DE  Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post- transcriptional level (By similarity). {ECO:0000250|UniProtKB:Q9SF32}.
DE  Reference Proteome: Yes;
GO  GO:0005856;
GO  GO:0005635;
GO  GO:0000325;
GO  GO:0005516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGKPARWLKSVLLGKKPSKSSGSKDKERIVNGKEVVVISKIEESDVVSDLSSIGNAAVYTSGIVETQNLKHEDVSDDEIQ
SQ  VSEVQPTDSQDVASVPDDSLSESEKIQQEIAAVTVQAAYRGYLARRAFKILKGIIRLQALIRGHMVRRQAVSTLCCVMGI
SQ  VRLQALARGREIRHSDIGVEVQRKCHLHHQPLENKANSVVDTHSYLGINKLTGNAFAQKLLASSPNVLPLSLDNDSSNSI
SQ  WLENWSASCFWKPVPQPKKASLRKSQKKFASNPQIVEAEFARPKKSVRKVPSSNLDNSSVAQTSSELEKPKRSFRKVSTS
SQ  QSVEPLPSMDNPQVDLEKVKRGLRKVHNPVVENSIQPQLVPQIAVEKPNGSLEESVNAFDEEKEDEVAETVVQQPEELIQ
SQ  THTPLGTNESLDSTLVNQIEESEENVMAEEKEDVKEERTPKQNHKENSAGKENQKSGKKASSVTATQTAEFQESGNGNQT
SQ  SSPGIPSYMQATKSAKAKLRLQGSSSPRQLGTTEKASRRYSLPSSGNSAKITSHSPKTRVSNSSGKSGNKTEKTLLSSRE
SQ  GNGKATPVEWKR
//
ID  Q8L4D8;
PN  Protein IQ-DOMAIN 31;
GN  IQD31;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus envelope {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24134884, ECO:0000269|PubMed:28115582}. Cell membrane {ECO:0000269|PubMed:28115582}. Note=Associates to cortical microtubules (MTs). {ECO:0000269|PubMed:24134884}.
DR  UNIPROT: Q8L4D8;
DR  UNIPROT: Q9CA49;
DR  UNIPROT: Q9SSF5;
DR  Pfam: PF13178;
DR  Pfam: PF00612;
DR  PROSITE: PS50096;
DE  Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post- transcriptional level (By similarity). {ECO:0000250|UniProtKB:Q9SF32}.
DE  Reference Proteome: Yes;
DE  Interaction: P25854; IntAct: EBI-4499168; Score: 0.37
DE  Interaction: Q94AZ4; IntAct: EBI-4499176; Score: 0.37
GO  GO:0005875;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0005516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGKSTKWLKNVLLGKKTSKSSGSKDKERVVSGKEVLVTSKVEESDVVSDLPSFEVAETNTVDRSGGMLETQNVGPEEISD
SQ  DEIELPEGKSTDSQNVAPVQDHSLSDAERIQREIAATSVQAAFRGYLARRAFWALKGIIRLQALIRGHLVRRQAVATLFS
SQ  VMGIVRLQAFARGREIRKSDIGVQVYRKCRLQLLQGNKLANPTDAYLGIKKLTANAFAQKLLASSPKVLPVHAYDTSNPN
SQ  SNLIWLENWSASCFWKPVPQPKKTISRKPQNRLLVEAESAKPKKSVRKVPASNFESSSVQTSFEFEKPKRSFRKVSSQSI
SQ  EPPAVEDPQIELEKVKRSLRKVHNPVVESSIQPQRSPRKEVEKPKLGVEKTRESSYPLVHETAEEPVNVCDEKKKQEISE
SQ  QPEEEVHALEMEVHTPGPLETNEALDSSLVNQIDSNEKAMVEEKPSMEKDTKEEKTPKPNNKENSAGKENQKSRKKGSAT
SQ  SKTEREESNGHHETSPSIPSYMQATKSAKAKLRLQGSPKSAEQDGTEKATVPRRHSLPSPGNGRITSHSPRTTRLANSGD
SQ  KTGNKKEKPLLSSREGNAKTTPAERKR
//
ID  Q2NND9;
PN  Protein IQ-DOMAIN 7;
GN  IQD7;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus envelope {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}.
DR  UNIPROT: Q2NND9;
DR  UNIPROT: Q9LNQ7;
DR  UNIPROT: Q9LQK1;
DR  Pfam: PF00612;
DR  PROSITE: PS50096;
DE  Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post- transcriptional level (By similarity). {ECO:0000250|UniProtKB:Q9SF32}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0009524;
GO  GO:0009574;
GO  GO:0005516;
GO  GO:0007105;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGGSGNWIRSLISNRKPVNDQQEKLSDKSSKKKWKLWRISSESLASSSFKSRGSYAASSLGSELPSFSADEAFTTAMAAL
SQ  IRAPPRDFLMVKREWASTRIQAAFRAFLARQAFRALKAVVRIQAIFRGRQVRKQAAVTLRCMQALVRVQSRVRAHRRAPS
SQ  DSLELKDPVKQTEKGWCGSPRSIKEVKTKLQMKQEGAIKRERAMVYALTHQSRTCPSPSGRAITHHGLRKSSPGWNWYDD
SQ  VGTFSRKSSESSVLSEYETVTVRKNNLSSTRVLARPPLLLPPVSSGMSYDSLHDETSTSSTSQSPVAFSSSVLDGGGYYR
SQ  KPSYMSLTQSTQAKQRQSGLSCNGDARRSAGSDQCTDLYPPGNVWAKSQRS
//
ID  Q9CAI2;
PN  Protein IQ-DOMAIN 8;
GN  IQD8;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}. Nucleus envelope {ECO:0000269|PubMed:28115582}. Note=Recruits calmodulin (CaM2) to microtubules. {ECO:0000269|PubMed:28115582}.
DR  UNIPROT: Q9CAI2;
DR  Pfam: PF00612;
DR  PROSITE: PS50096;
DE  Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post- transcriptional level (By similarity). {ECO:0000250|UniProtKB:Q9SF32}.
DE  Reference Proteome: Yes;
DE  Interaction: O23160; IntAct: EBI-25517206; Score: 0.56
GO  GO:0005635;
GO  GO:0009524;
GO  GO:0009574;
GO  GO:0005516;
GO  GO:2000073;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGGSGNWIKSLITNKKNITDDQEKNIKKKWKLWRTSSEGLISSSKGFKSRGGSYGTPSLGSDPPSFSADDSFTAAVAAVI
SQ  RAPPKDFFLVKREWAATRIQAAFRAFLARQALRALKAVVRIQAIFRGRQVRKQADVTLRCMQALVRVQARVRAHCNRGPS
SQ  DGQELEKPSDQQKDDPAKQAEKGWCDSPGSINEVRTKLQMRQEGAIKRERAMVYALTHQPRTCPSPAKASKQGSVKKNNG
SQ  SCKSSPGWNWLDRWVADRPWEGRLMEGPTNSSENARKSESSVSEHDTVQVRKNNLTTRVLARPPPMSSSATSSESSSTSQ
SQ  SPVPFSGSFLEEGGYYRKPSYMSLTQSIKAKQRRSGSSSSCSKTPFEKKQSMSYNGDVNVRRSAGSDPLNNQWTDLYPPA
SQ  QVTGRHMWAKSQRG
//
ID  K7NAJ3;
PN  Interferon alpha/beta receptor 1b;
GN  ifnar1b;
OS  8022;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P17181}; Single-pass membrane protein {ECO:0000250|UniProtKB:P17181}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24244163}. Note=Mainly detected in perinuclear regions, when overexpressed in RTG-2 cell line. {ECO:0000269|PubMed:24244163}.
DR  UNIPROT: K7NAJ3;
DR  Pfam: PF09294;
DR  Pfam: PF01108;
DE  Function: Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) (PubMed:24244163). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response (By similarity). Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross- phosphorylate one another (By similarity). The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (By similarity). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes (By similarity). {ECO:0000250|UniProtKB:P17181, ECO:0000269|PubMed:24244163}.
DE  Reference Proteome: No;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004905;
GO  GO:0001934;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLAELPQPQNLTLLTLNTQYVLTWDWDQTTTGNSVSFTVEYMAKYKMKMKKKNWSRVCERTTRTRCDLTGSDLHYLGMYV
SQ  LRVRASADGVDSDWVNKDFCPDIDASLGPPSRAELAPVGNLLDVTISDPLTSTQHSMKEHVLFLYYRILYWSRSDDPQGL
SQ  KPKVLDSSNNLVTPPELEAWAWYCVMIQSRYDYYNKTSSYTEPQCMQTEGDTPYGQIFLYFLVSMMVCFLLVLLSSYAFF
SQ  RFYRGLKNTFYPSIQLPAHIQEYLCDSSPGSDMPRLITADSEAELCCDKLTICPEVVLLEIHVPPPLTAPPSELEQDSGR
SQ  HIRQDSGDSGIYSTEGGSAQQGRSGGEPIRRDQEVDSWQTLEQVKMEEMGRELADERDLDEGVVDVCV
//
ID  Q9N1F0;
PN  Inositol 1,4,5-triphosphate receptor associated 1;
GN  IRAG1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Sarcoplasmic reticulum {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10724174}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q9N1F0;
DR  UNIPROT: Q9N1E9;
DR  Pfam: PF05781;
DE  Function: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO- dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation. {ECO:0000269|PubMed:10724174, ECO:0000269|PubMed:16166082}.
DE  Reference Proteome: Yes;
DE  Interaction: P00516; IntAct: EBI-10094529; Score: 0.44
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0016529;
GO  GO:0019934;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVKAPQSEERLAGGGKGNNSVLACGAQASWSIFGADAAEVPGTRSHSRQEAAMPHIPEDEEPPGEPQAAQSPAGQDPATT
SQ  GISCSPPTIILTGDASSPEGETDKNPVNRAHSPHRRLSHRHLKVSTASLTSVDPAGHVIDLVNDQLPDISISEEDKKKNL
SQ  ALLEEAKLVSERFLTRRGRKSRSSPGESSPAVSPNLSPGASPASSQSNSLTVPTPPGLDVCSGPPSPLPGAPPQKGDEAE
SQ  VPSPHLGESNVLKGLADRKQNDQRTLSQGRLTARSPTVEKSKEITIEQKENFDPLQRPEAIPKGPASGPGSGGKMALNSP
SQ  QPGPVESELGKPLAKTAKEGNPLPRGPTQGSGGVAPQASQGKSTVGEPAGSKVGSKAELWPPTSRPPLLRGVSWDSGPEE
SQ  PGPRLQKVLAKLPLAEEEKRFTGKAGSKLAKAPGLKDFQIQVQPVRMQKLTKLREEHILLRNQNLVGLKLPELSEAAEQE
SQ  KGHPSELSSAIEEEESKGGLDVMPNISDVLLRKLRVHKSLPGSAPPLTEKEVENVFVQLSLAFRNDSYTLESRINQAERE
SQ  RNLTEENTEKELENFKASITSSASLWHHCEHRETYQKLLEDIAVLHRLAARLSSRAEMVGAVRQEKRMSKATEVMMQYVE
SQ  NLKRTYEKDHAELMEFKKLANQNSSRSCGPSEDGVPRTARSMSLSLGKNMPRRRVSVAVVPKFNILNLPGQSPSSSPIPS
SQ  LPALSESSNGKGNPPVSSALPALLENGKTNGDPDCEASASVPTPSCLEGISQEAKARMEEEAYNKGYQEGLKKTKELQGL
SQ  REEEEEQKSESPEEPEEVAETEEEEKEQRSSKLEELVHFLQVMYPKLCQHWQVIWMMAAAMLVLTVVLGLYGSHNSCVEQ
SQ  ADGSLGKSTCSAAQRDSWWSSGLQHEQPTEQ
//
ID  Q9Y6F6;
PN  Inositol 1,4,5-triphosphate receptor associated 1;
GN  IRAG1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Sarcoplasmic reticulum {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q9Y6F6;
DR  UNIPROT: B7Z3T4;
DR  UNIPROT: B7Z6I2;
DR  UNIPROT: B7Z9A3;
DR  UNIPROT: E9PQY6;
DR  UNIPROT: F5H6A1;
DR  UNIPROT: J3KQZ7;
DR  UNIPROT: Q17S00;
DR  UNIPROT: Q9UNY1;
DR  Pfam: PF05781;
DR  OMIM: 604673;
DR  DisGeNET: 10335;
DE  Function: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO- dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation. {ECO:0000269|PubMed:14729908}.
DE  Reference Proteome: Yes;
DE  Interaction: P08473; IntAct: EBI-1389788; Score: 0.35
DE  Interaction: Q5NFP9; IntAct: EBI-22298736; Score: 0.37
DE  Interaction: Q5NHT8; IntAct: EBI-22298726; Score: 0.37
DE  Interaction: Q5NHH2; IntAct: EBI-22298746; Score: 0.37
DE  Interaction: Q5NEC5; IntAct: EBI-22298756; Score: 0.37
DE  Interaction: P07339; IntAct: EBI-25840046; Score: 0.56
DE  Interaction: P28799; IntAct: EBI-25860891; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25898051; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25931556; Score: 0.56
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0031095;
GO  GO:0016529;
GO  GO:0019934;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGMDLTCPFGISPACGAQASWSIFGADAAEVPGTRGHSQQEAAMPHIPEDEEPPGEPQAAQSPAGQGPPAAGVSCSPTPT
SQ  IVLTGDATSPEGETDKNLANRVHSPHKRLSHRHLKVSTASLTSVDPAGHIIDLVNDQLPDISISEEDKKKNLALLEEAKL
SQ  VSERFLTRRGRKSRSSPGDSPSAVSPNLSPSASPTSSRSNSLTVPTPPGLDVCSGPPSPLPGAPPQQKGDEADVSSPHPG
SQ  EPNVPKGLADRKQNDQRKVSQGRLAPRPPPVEKSKEIAIEQKENFDPLQYPETTPKGLAPVTNSSGKMALNSPQPGPVES
SQ  ELGKQLLKTGWEGSPLPRSPTQDAAGVGPPASQGRGPAGEPMGPEAGSKAELPPTVSRPPLLRGLSWDSGPEEPGPRLQK
SQ  VLAKLPLAEEEKRFAGKAGGKLAKAPGLKDFQIQVQPVRMQKLTKLREEHILMRNQNLVGLKLPDLSEAAEQEKGLPSEL
SQ  SPAIEEEESKSGLDVMPNISDVLLRKLRVHRSLPGSAPPLTEKEVENVFVQLSLAFRNDSYTLESRINQAERERNLTEEN
SQ  TEKELENFKASITSSASLWHHCEHRETYQKLLEDIAVLHRLAARLSSRAEVVGAVRQEKRMSKATEVMMQYVENLKRTYE
SQ  KDHAELMEFKKLANQNSSRSCGPSEDGVPRTARSMSLTLGKNMPRRRVSVAVVPKFNALNLPGQTPSSSSIPSLPALSES
SQ  PNGKGSLPVTSALPALLENGKTNGDPDCEASAPALTLSCLEELSQETKARMEEEAYSKGFQEGLKKTKELQDLKEEEEEQ
SQ  KSESPEEPEEVEETEEEEKGPRSSKLEELVHFLQVMYPKLCQHWQVIWMMAAVMLVLTVVLGLYNSYNSCAEQADGPLGR
SQ  STCSAAQRDSWWSSGLQHEQPTEQ
//
ID  Q9WUX5;
PN  Inositol 1,4,5-triphosphate receptor associated 1;
GN  Irag1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15388327}. Sarcoplasmic reticulum {ECO:0000269|PubMed:15388327}.
DR  UNIPROT: Q9WUX5;
DR  UNIPROT: Q3U069;
DR  UNIPROT: Q9R2C5;
DR  Pfam: PF05781;
DE  Function: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO- dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation. {ECO:0000269|PubMed:10321731, ECO:0000269|PubMed:15388327, ECO:0000269|PubMed:15483626, ECO:0000269|PubMed:16990611}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0016529;
GO  GO:0019934;
GO  GO:0045986;
GO  GO:0060087;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGRSLTCPFGISPACGAQASWSIFGVGTAEVPGTHSHSNQAAAMPHIPEDEEPPGEPQAAQTQDSPSAGPFPSPPTIVLT
SQ  GDASSPEGETDKNLVNRAPSPHRRLSHRHLKVSTASLTSVDPSGHVIDLVNDQLPDISISEEDKKKNLALLEEAKLVSER
SQ  FLTRRGRKSRSSLGDSPSAVSPNLSSGASPASSRSCSLTISTSPGLDICSGPQSPLPGAPPQQKGHEDGVSSPCPGEPNV
SQ  SKGLADLKQNDQRKVSQGRLAPRSPTVEKTKELTVEQKENFDPLQHVEATPMAQASGASISGKMALNSPQPGPAEMELGR
SQ  QLLKTAREGNPLPRTTAQGSGGTVSPHSLGQGSAGEPMGPKAGSKAELRSPVSRPPLIRGVSWDSSPEEPGPLLQKVLAK
SQ  LPLAEEEKRFPGKAKPAKPPGLKDFQIQVQPVRMQKLTKLREEHILMRNQNLVGFKLPELSEAAEQDKGVSPELAPAAEE
SQ  EESKSGLDVMPNISDILLRKLRVHKSLTGSAPPLTEKEVENVFVQLSLAFRNDSYTLESRINQAERERNLTEENTEKELE
SQ  NFKASITSSANIWYHCEHRETYQKLLEDIAVLHRLAARLSSRAEVVGAVRQEKRMSKATEVMMQYVENLKRTYEKDHAEL
SQ  MEFKKLANQNSSRSCGPSEDGVPRTARSMSLTMGKNMPRRRVSVAVVPKFNALNLPGQAPSSSPMPSLPALSESSNGKSS
SQ  ISVSPALPALLENGKTNAEANCEVGAPVPLPSCLEETSQETKAKAEEEAYSKGYQEGVKKTEELQDLKEEEEEEQKTESP
SQ  EEPEEVEETQEDEKDQGSSKLEELVHFLQVMYPKLCQHWQVIWMMAAVMLVLSVVLGLYSSYNSCTEEADGPPGRSTCSA
SQ  AQRDSWWSSGLQQELPAEQ
//
ID  Q5RHB5;
PN  Inositol 1,4,5-triphosphate receptor associated 2;
GN  irag2;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22542100}; Single-pass type IV membrane protein {ECO:0000269|PubMed:22542100}. Nucleus envelope {ECO:0000269|PubMed:22542100}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:22542100}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:22542100}. Chromosome {ECO:0000269|PubMed:22542100}. Note=Localized at both male and female pronuclear membranes during pronuclear congression and fusion. Colocalized with tubulin at the centrosome adjacent to the nuclear membrane. At prophase is localized at the centrosome on opposite sides of the zygotic nucleus and at the reforming nuclear membrane. At metaphase is juxtaposed with the centrosomes at the mitotic spindle poles. During chromosome segregation is localized with the chromatin. Undetectable at the centrosome at the onset of anaphase, but becomes again apparent by late mitosis.
DR  UNIPROT: Q5RHB5;
DR  UNIPROT: J9WMP5;
DR  Pfam: PF14658;
DR  Pfam: PF14662;
DR  Pfam: PF05781;
DE  Function: A maternally expressed membrane and cytoskeletal linker protein, which is essential for attachment of the centrosome to the male pronucleus. Promotes male and female pronucleus congression and subsequent fusion after fertilization. Congression is mediated by the sperm aster microtubules. {ECO:0000269|PubMed:12874114, ECO:0000269|PubMed:22542100}.
DE  Disease: Note=Defects in irag2 are a cause of pronuclear congression/fusion and chromosomal segregation abnormalities in the zygote named futile cycle (fue), a lethal recessive maternal-effect mutant. Mutant embryos undergo several cycles of anucleate cleavage and die. {ECO:0000269|PubMed:12874114}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0000785;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0072686;
GO  GO:0097431;
GO  GO:0031965;
GO  GO:0007052;
GO  GO:0051028;
GO  GO:0051984;
GO  GO:0007344;
GO  GO:0035046;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVGVTPRRHNPVDSICRKLQTIQRRDQEINSPFQIPKFQTNSYDSPHSGLRFNLEAILKKHTVRPDDSDSASSAGMLTP
SQ  TASPGPGSSCNTPRAPITPVNATYSITSTLGTLGTIGDRRTSGTYSRPFRRNCSTPSAQTGDNYFNFTPRYSTQSQGPDT
SQ  DVRTSKIPTPGLFSYNLNFSSDISNMDSELAYPALVVKRLSLGEGSLFTSEPKKESMAEVSLICEEDLLDTIFQACDTQC
SQ  RGKVYVSHIVDFLRHTTCRSSEDSGLEELCNMLDPERKDISIDLDTYHAIMKEWIEDCRNQGKDLKNDTQQESSKLRDSL
SQ  SAKRSALLNMTSGSLEAFGGEASRADLETSDLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKM
SQ  GQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNAD
SQ  LQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQMMQPDVTIPGLSLSVAYRLNQTSSG
SQ  SLQTELALAQNPLEGLEHLSTSVCFASSLDETLDREVLLLLQGPTPEQLSLEFKSLISRLKREFKEDGLTFLTAIRSLTE
SQ  NSETQEANTDLKMQGLEVQLEQRRTDWIRSLEQLDQYRDSLERELLKMASNMRRSRTEILHLSVKVQEQENQKQQLREEV
SQ  DRLKTPLDNREASSQTPDHLQQVVEELDGPSLEWDEEYVLSESPPLQELGPDQQMLEELCCDEEVLQALKQEEEEPTETV
SQ  SDKEKITAKSEGEGEATYDSGVENEEPQRDFTLSHMCLPDKKSERESNEAPFVGEGGEQRPCMSLKEEDRLPECTGPEDA
SQ  HEQAAPLPHTHCECAGDQPLTYDNLEVTSVKDHILSTEPSSLMTCELVSPSTGHPEVGNSITGRTEQLVGTNGEPEEERL
SQ  TTGADMSDLQRLGEGQLSKVSAKSDKSLLLPVAEEEEAMPEAVEVTSAGVNSPDKHKTGSKKTVVTSDSNSTGSADSLKD
SQ  PSEKVKDMTFDPAASEDNIPTVPATQSPKKDPLASRNKLKKEMSSMEVIEEQKAQEDGEPTVVTEKEGDTSVSSENASDS
SQ  TKDDKNSLSPSDKEIEAEFHRLSLGFKCDMFTLEKRLRLEERSRDLAEENVRKEVISCKALLQALIPRCEEDNQSMEIIH
SQ  RVQKNLEILVQSMTRVSSRSEMLGAIHQETRVGKTVEVMIQHVENLRRMYTKEHAELLELRENLTPNERSFGSHSERDDF
SQ  RNKKQTTSNIFKTTSRRISIATIPRSIGGQTHFDMPKDMAETEVERLSRRSPWNMAAKRPPLKRFVSSGTWADIDEPTLM
SQ  NSPTPSPTDNAPPSLMEGRPAVSRGARGIWIWVALFVVLAVLLALLASLMLQPAVDAAPVGTGDSWMTIQQLLWPYTGLR
SQ  HNGQPPV
//
ID  Q12912;
PN  Processed inositol 1,4,5-triphosphate receptor associated 2;
GN  IRAG2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: [Processed inositol 1,4,5-triphosphate receptor associated 2]: Cytoplasm {ECO:0000250|UniProtKB:Q60664}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q60664}; Single-pass type IV membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q60664}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5RHB5}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q5RHB5}. Chromosome {ECO:0000250|UniProtKB:Q5RHB5}. Note=Colocalized with ITPR3 on the endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:Q60664}.
DR  UNIPROT: Q12912;
DR  UNIPROT: A0AVM2;
DR  UNIPROT: B4E077;
DR  UNIPROT: Q8N301;
DR  Pfam: PF05781;
DR  OMIM: 602003;
DR  DisGeNET: 4033;
DE  Function: Plays a role in the delivery of peptides to major histocompatibility complex (MHC) class I molecules; this occurs in a transporter associated with antigen processing (TAP)-independent manner. May play a role in taste signal transduction via ITPR3. May play a role during fertilization in pronucleus congression and fusion. Plays a role in maintaining nuclear shape, maybe as a component of the LINC complex and through interaction with microtubules. {ECO:0000250|UniProtKB:Q60664}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A6L7H2W2; IntAct: EBI-2839314; Score: 0.00
DE  Interaction: A0A6L8PL56; IntAct: EBI-2839333; Score: 0.00
DE  Interaction: A0A6L7HNZ8; IntAct: EBI-2839321; Score: 0.00
DE  Interaction: Q81JR3; IntAct: EBI-2839359; Score: 0.00
DE  Interaction: P62258; IntAct: EBI-3452822; Score: 0.00
DE  Interaction: Q9H4A3; IntAct: EBI-3453824; Score: 0.00
DE  Interaction: Q9ULV4; IntAct: EBI-20907264; Score: 0.40
DE  Interaction: P21709; IntAct: EBI-32720516; Score: 0.27
GO  GO:0035577;
GO  GO:0005694;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0016020;
GO  GO:0005815;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0000922;
GO  GO:0008017;
GO  GO:0002376;
GO  GO:0006997;
GO  GO:0007338;
GO  GO:0006906;
GO  GO:0006903;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESTPFSGVANQIHTLCERPTYGEVKDGALDVKRQHKCPGPTSGPSPGTNLSGCIRMNDDPSMEENGVERVCPESLLQSR
SQ  EYSSLPLPRHTSSTDGTITSSDPGLEILNMASCDLDRNSLCKKEEDTRSASPTIEAQGTSPAHDNIAFQDSTSKDKTILN
SQ  LEAKEEPETIEEHKKEHASGDSVVSPLPVTTVKSVNLRQSENTSANEKEVEAEFLRLSLGFKCDWFTLEKRVKLEERSRD
SQ  LAEENLKKEITNCLKLLESLTPLCEDDNQAQEIIKKLEKSIKFLSQCAARVASRAEMLGAINQESRVSKAVEVMIQHVEN
SQ  LKRMYAKEHAELEELKQVLLQNERSFNPLEDDDDCQIKKRSASLNSKPSSLRRVTIASLPRNIGNAGMVAGMENNDRFSR
SQ  RSSSWRILGSKQSEHRPSLPRFISTYSWADAEEEKCELKTKDDSEPSGEETVERTRKPSLSEKKNNPSKWDVSSVYDTIA
SQ  SWATNLKSSIRKANKALWLSIAFIVLFAALMSFLTGQLFQKSVDAAPTQQEDSWTSLEHILWPFTRLRHNGPPPV
//
ID  Q60664;
PN  Processed inositol 1,4,5-triphosphate receptor associated 2;
GN  Irag2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: [Processed inositol 1,4,5-triphosphate receptor associated 2]: Cytoplasm {ECO:0000269|PubMed:8798562}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20071408}; Single-pass type IV membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000305|PubMed:29878215}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5RHB5}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q5RHB5}. Chromosome {ECO:0000250|UniProtKB:Q5RHB5}. Note=Colocalized with ITPR3 on the endoplasmic reticulum membrane. {ECO:0000269|PubMed:20071408}.
DR  UNIPROT: Q60664;
DR  UNIPROT: Q7TMU8;
DR  Pfam: PF05781;
DE  Function: Plays a role in the delivery of peptides to major histocompatibility complex (MHC) class I molecules; this occurs in a transporter associated with antigen processing (TAP)-independent manner. May play a role in taste signal transduction via ITPR3. May play a role during fertilization in pronucleus congression and fusion (PubMed:9314557). Plays a role in maintaining nuclear shape, maybe as a component of the LINC complex and through interaction with microtubules (PubMed:29878215). {ECO:0000269|PubMed:29878215, ECO:0000269|PubMed:9314557}.
DE  Reference Proteome: Yes;
DE  Interaction: A3KGF7; IntAct: EBI-688126; Score: 0.37
DE  Interaction: P70227; IntAct: EBI-9212709; Score: 0.27
DE  Interaction: Q63269; IntAct: EBI-9212784; Score: 0.46
DE  Interaction: E9Q401; IntAct: EBI-20567306; Score: 0.35
GO  GO:0005694;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0005815;
GO  GO:0005635;
GO  GO:0000922;
GO  GO:0008017;
GO  GO:0002376;
GO  GO:0006997;
GO  GO:0007338;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLCVKGPPEQEPEDGALDVTRGCQCPLPTEDSILGQELLDCTRMNEDQSTDENGAGHFYSESPSQLREYLTQPSSEQTSS
SQ  SESTVTSSESGSDILHMASGDLDCKPLCEKEEEARAASAMQGTSLAPAAYGDYTSVGVAKAASQLEAGEELRTTENGGKG
SQ  SAPGETEISMPPKASVKLVNFQQSENTSANEKEVEAEFLRLSLGLKCDWFTLEKRVKLEERSRDLAEENLKKEITNCLKL
SQ  LESLTPLCEEDNQAQEIVKKLEKSIVLLSQCTARVASRAEMLGAINQESRVSRAVEVMIQHVENLKRMYAKEHAELEDLK
SQ  QALLQNDRSFNSLPDEDDCQIKKRSSSLNSKPSSLRRVTIASLPRNLGNVGLVSGMENNDRFSRRSSSWRILGTKQGEHR
SQ  PSLHRFISTYSWADAEDERSDVKARDAPEPQGEEAVERTRKPSLSERRSSTLAWDRGTICSSVASWVTHLQASFRRANRA
SQ  LWLTGLIIILIAALMSFLTGQLFQTAVEAAPTQEGDSWLSLEHILWPFTRLGHDGPPPV
//
ID  Q9Y7X6;
PN  Stress response protein ish1;
GN  ish1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:11751918}.
DR  UNIPROT: Q9Y7X6;
DR  UNIPROT: Q09149;
DR  Pfam: PF10281;
DE  Function: Has a role in maintaining cell viability during stationary phase induced by stress response. Activated by the spc1 MAPK pathway. {ECO:0000269|PubMed:11751918}.
DE  Reference Proteome: Yes;
DE  Interaction: O13712; IntAct: EBI-21242557; Score: 0.37
DE  Interaction: O59793; IntAct: EBI-1559660; Score: 0.54
DE  Interaction: Q9Y7X6; IntAct: EBI-1559712; Score: 0.37
DE  Interaction: P05752; IntAct: EBI-1559775; Score: 0.37
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005886;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRSRSVASLGVLLAIVFYIFTYGFSTYRKNDTSAVKTWLEEHSIPYGSRSSPSDFQQFISESYDSLVPNLDKWSGHNLNS
SQ  WLGKKTESSYLDAISNKIRKTGRKLSGSVEDARDATQEAWESQKASLFESWSDSQLRAFLARHSPQFAAKEKKGILEKLS
SQ  PASLRETAAKEYDALTSKLGNTGDWIYDTWSDNELRTWLHDVGVPISSHESTRSHLLRKLKNYISTKADEAQPSVEAVKG
SQ  KASEKAKQAGEFVSDKAGDAKELVNEKSSEAGQYAGQKMEEGGELLQEISKRRGRFGNWWANSGLKAYFDAHGIPAYQPS
SQ  PIDQFYAHLRRQYYLKTNGYQALKSKAYEEASNVADSASSIASNVASGATEAYQGAASGASRFTEGAKTAAESVTSAFEH
SQ  NKDTATSKAKQMKGKAASLGSTASEKVGEAADYAAETASKVASKAASKVRETIDETIIERWQDSKLKEFLFLRGVPVPQR
SQ  STKDQLLDLVRKHFNKGAVPNWAAYFDTLSSKELSAWIKEYKKHYHGKLHPSKDREHLFQNACNIYRAIAEKADKSVLQS
SQ  IQSKFPKATVPGYDSWSNEDLKSALKEYGDSIGKVFNRKDAIERLKRHDILFYGPVVADKAKSGVSGFLRRVASFMGFGT
SQ  RDVAEIKLGENIQKVKDTASKASSAVSSAGDYVETNVKKAQRVL
//
ID  Q3ZBV1;
PN  IST1 homolog;
GN  IST1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasmic vesicle {ECO:0000250|UniProtKB:P53990}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53990}. Midbody {ECO:0000250|UniProtKB:P53990}. Nucleus envelope {ECO:0000250|UniProtKB:P53990}. Note=Localizes to centrosome and midbody of dividing cells. Colocalized with SPART to the ends of Flemming bodies during cytokinesis. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. {ECO:0000250|UniProtKB:P53990}.
DR  UNIPROT: Q3ZBV1;
DR  Pfam: PF03398;
DE  Function: ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation (By similarity). Is required for efficient abscission during cytokinesis (By similarity). Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells (By similarity). During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing (By similarity). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (By similarity). Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST (By similarity). {ECO:0000250|UniProtKB:P53990}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005815;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLGSGIKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLL
SQ  ARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKI
SQ  LVERYLIEIAKNYNVPYEPDSVVMAEAPPGVETDLIDVGFTDDVKKGGPGRGGGGGFTAPVGGPDGTVPMPMPMPMPSPN
SQ  TPFSYPLPKGPSDFNGLPVGTYQAFPNIHPPQIPATPPSYESVDDINADKNVSSTQIVGPGPKPEPPAKPASRLTETYDN
SQ  FVLPELPSVPDTLPTASPGANTSASEDIDFDDLSRRFEELKKKT
//
ID  P53990;
PN  IST1 homolog;
GN  IST1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasmic vesicle {ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20719964}. Midbody {ECO:0000269|PubMed:20719964}. Nucleus envelope {ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}. Note=Localizes to centrosome and midbody of dividing cells (PubMed:19129480, PubMed:19129479, PubMed:20719964). Colocalized with SPART to the ends of Flemming bodies during cytokinesis (PubMed:20719964). Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. {ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:20719964, ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}.
DR  UNIPROT: P53990;
DR  UNIPROT: A8KAH5;
DR  UNIPROT: J3QLU7;
DR  UNIPROT: Q3SYM4;
DR  UNIPROT: Q9BQ81;
DR  UNIPROT: Q9BWN2;
DR  PDB: 3FRR;
DR  PDB: 3FRS;
DR  PDB: 3JC1;
DR  PDB: 4U7E;
DR  PDB: 4U7I;
DR  PDB: 4U7Y;
DR  PDB: 4WZX;
DR  PDB: 6E8G;
DR  PDB: 6TZ4;
DR  PDB: 6TZ5;
DR  PDB: 6TZA;
DR  Pfam: PF03398;
DR  OMIM: 616434;
DR  DisGeNET: 9798;
DE  Function: ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation (PubMed:19129479, PubMed:26040712, PubMed:28242692). Is required for efficient abscission during cytokinesis (PubMed:19129479). Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells (PubMed:19129480, PubMed:19129479). During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing (PubMed:26040712). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (PubMed:28242692). Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST (PubMed:23897888). {ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:23897888, ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}.
DE  Reference Proteome: Yes;
DE  Interaction: P13798; IntAct: EBI-760177; Score: 0.75
DE  Interaction: P54253; IntAct: EBI-24534663; Score: 0.72
DE  Interaction: Q7ARD3; IntAct: EBI-2866257; Score: 0.00
DE  Interaction: Q9Y6W3; IntAct: EBI-8301445; Score: 0.68
DE  Interaction: P38606; IntAct: EBI-4324466; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q7Z479; IntAct: EBI-10213458; Score: 0.56
DE  Interaction: Q9UMX0; IntAct: EBI-10213468; Score: 0.56
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: Q8BT07; IntAct: EBI-11014656; Score: 0.35
DE  Interaction: Q92734; IntAct: EBI-11029015; Score: 0.35
DE  Interaction: Q8C5L3; IntAct: EBI-11029298; Score: 0.35
DE  Interaction: Q9JLQ0; IntAct: EBI-11033702; Score: 0.35
DE  Interaction: O75787; IntAct: EBI-11037152; Score: 0.35
DE  Interaction: P51148; IntAct: EBI-11046231; Score: 0.35
DE  Interaction: P51149; IntAct: EBI-11050319; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q3THE2; IntAct: EBI-11063194; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: Q9QYY8; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q61187; IntAct: EBI-11090666; Score: 0.35
DE  Interaction: Q6PB44; IntAct: EBI-11097749; Score: 0.35
DE  Interaction: Q9R0Q3; IntAct: EBI-11111571; Score: 0.35
DE  Interaction: P46467; IntAct: EBI-11115954; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q9UHD9; IntAct: EBI-24483554; Score: 0.56
DE  Interaction: Q9HD42; IntAct: EBI-25265048; Score: 0.56
DE  Interaction: O95429; IntAct: EBI-24532094; Score: 0.56
DE  Interaction: Q96K76; IntAct: EBI-21756437; Score: 0.35
DE  Interaction: Q9UBP0; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q9UBP5; IntAct: EBI-21874302; Score: 0.35
DE  Interaction: Q7LBR1; IntAct: EBI-15788871; Score: 0.63
DE  Interaction: P53990; IntAct: EBI-15788908; Score: 0.52
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: Q83D60; IntAct: EBI-21285718; Score: 0.37
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21393011; Score: 0.00
DE  Interaction: Q5NGE3; IntAct: EBI-22298572; Score: 0.37
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
GO  GO:0035578;
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0005793;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0090543;
GO  GO:0043231;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0045296;
GO  GO:0042802;
GO  GO:0090541;
GO  GO:0019904;
GO  GO:0044877;
GO  GO:0009838;
GO  GO:0051301;
GO  GO:0048668;
GO  GO:0061640;
GO  GO:1904903;
GO  GO:0045184;
GO  GO:0036258;
GO  GO:0048672;
GO  GO:0045862;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:0046745;
GO  GO:0019076;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLL
SQ  ARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKI
SQ  LVERYLIEIAKNYNVPYEPDSVVMAEAPPGVETDLIDVGFTDDVKKGGPGRGGSGGFTAPVGGPDGTVPMPMPMPMPSAN
SQ  TPFSYPLPKGPSDFNGLPMGTYQAFPNIHPPQIPATPPSYESVDDINADKNISSAQIVGPGPKPEASAKLPSRPADNYDN
SQ  FVLPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
//
ID  Q9CX00;
PN  IST1 homolog;
GN  Ist1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasmic vesicle {ECO:0000250|UniProtKB:P53990}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53990}. Midbody {ECO:0000250|UniProtKB:P53990}. Nucleus envelope {ECO:0000250|UniProtKB:P53990}. Note=Localizes to centrosome and midbody of dividing cells. Colocalized with SPART to the ends of Flemming bodies during cytokinesis. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. {ECO:0000250|UniProtKB:P53990}.
DR  UNIPROT: Q9CX00;
DR  UNIPROT: Q80U68;
DR  Pfam: PF03398;
DE  Function: ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation (By similarity). Is required for efficient abscission during cytokinesis (By similarity). Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells (By similarity). During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing (By similarity). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (By similarity). Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST (By similarity). {ECO:0000250|UniProtKB:P53990}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0000785;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005793;
GO  GO:0070062;
GO  GO:0090543;
GO  GO:0043231;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0042802;
GO  GO:0090541;
GO  GO:0019904;
GO  GO:0044877;
GO  GO:0009838;
GO  GO:0051301;
GO  GO:0048668;
GO  GO:0061640;
GO  GO:0045184;
GO  GO:0048672;
GO  GO:0045862;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:0046745;
GO  GO:0019076;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLL
SQ  ARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKI
SQ  LVERYLIEIAKNYNVPYEPDSVVMAEAPVGVETDLIDVGFTDDVKKGGPGRGGGGGFTAPVGGPDGIVPMPMPMPMPSPN
SQ  APFAYPLPKGPSDFSGLPVGTYQAFPNIHPPQIPATPPSYESVDDINGDKTVSSAQIVGPKPEAPAKPPSRPVDNYNTFV
SQ  LPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
//
ID  Q5R6G8;
PN  IST1 homolog;
GN  IST1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasmic vesicle {ECO:0000250|UniProtKB:P53990}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53990}. Midbody {ECO:0000250|UniProtKB:P53990}. Nucleus envelope {ECO:0000250|UniProtKB:P53990}. Note=Localizes to centrosome and midbody of dividing cells. Colocalized with SPART to the ends of Flemming bodies during cytokinesis. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. {ECO:0000250|UniProtKB:P53990}.
DR  UNIPROT: Q5R6G8;
DR  Pfam: PF03398;
DE  Function: ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation (By similarity). Is required for efficient abscission during cytokinesis (By similarity). Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells (By similarity). During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing (By similarity). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (By similarity). Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST (By similarity). {ECO:0000250|UniProtKB:P53990}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005815;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLL
SQ  ARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKGYGKLCRTNQIGTVNDRLMHKLSVEAPPKI
SQ  LVERYLIEIAKNYNVPYEPDSVVMAEAPPGVETDLIDVGFTDDVKKGGPGRGGGGGFTAPVGGPEGTVPMPMPMPMPSAN
SQ  TPFSYPLPKGPSDFNGLPMGTYQAFPIIHPPQIPATPPSYESVDDINADKNISSAQIVGPGPKPEASAKLPSRPADNYDN
SQ  FVLPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
//
ID  Q568Z6;
PN  IST1 homolog;
GN  Ist1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasmic vesicle {ECO:0000250|UniProtKB:P53990}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53990}. Midbody {ECO:0000250|UniProtKB:P53990}. Nucleus envelope {ECO:0000250|UniProtKB:P53990}. Note=Localizes to centrosome and midbody of dividing cells. Colocalized with SPART to the ends of Flemming bodies during cytokinesis. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. {ECO:0000250|UniProtKB:P53990}.
DR  UNIPROT: Q568Z6;
DR  Pfam: PF03398;
DE  Function: ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation (By similarity). Is required for efficient abscission during cytokinesis (By similarity). Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells (By similarity). During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing (By similarity). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (By similarity). Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST (By similarity). {ECO:0000250|UniProtKB:P53990}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0000785;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005793;
GO  GO:0090543;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0090541;
GO  GO:0019904;
GO  GO:0044877;
GO  GO:0009838;
GO  GO:0051301;
GO  GO:0048668;
GO  GO:0061640;
GO  GO:0045184;
GO  GO:0048672;
GO  GO:0045862;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:0046745;
GO  GO:0019076;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLL
SQ  ARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKI
SQ  LVERYLIEIAKNYNVPYEPDSVVMAEAPVGVETDLIDVGFTDDVKKGGPGRGGGGGFTAPVGAPDGTMPMPMPMPMPMPS
SQ  PSPNAPFAYPLPKGPSDFSGLPVGTYQAFPNIHPPQIPATPPSYESVDDINADKNVSSAQIVGPKPEAPAKPPSRPVDNY
SQ  NTFVLPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
//
ID  Q9TU34;
PN  Inositol 1,4,5-trisphosphate receptor type 1;
GN  ITPR1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11584008}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:11584008}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14643}. Note=Endoplasmic reticulum and secretory granules (PubMed:11584008). {ECO:0000269|PubMed:11584008}.
DR  UNIPROT: Q9TU34;
DR  UNIPROT: Q7M2U0;
DR  Pfam: PF08709;
DR  Pfam: PF00520;
DR  Pfam: PF02815;
DR  Pfam: PF08454;
DR  Pfam: PF01365;
DR  PROSITE: PS50919;
DE  Function: Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5- trisphosphate. Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways. {ECO:0000250|UniProtKB:P11881, ECO:0000269|PubMed:11584008}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0030176;
GO  GO:0048471;
GO  GO:0098793;
GO  GO:0005791;
GO  GO:0030141;
GO  GO:0030658;
GO  GO:0015278;
GO  GO:0070679;
GO  GO:0005220;
GO  GO:0035091;
GO  GO:0070059;
GO  GO:0051209;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGA
SQ  NSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSW
SQ  FYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVV
SQ  RLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDP
SQ  DFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVH
SQ  STNIPIDKEEEKPVMLKIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDL
SQ  VYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVL
SQ  RHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVS
SQ  MNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWVFWRDSNKEVRSKSVRELAQDAK
SQ  EGQKEDRDVLGYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPSDLRASFCRLMLHMHVDRDPQEQVTP
SQ  VKYARLWSEIPSEIAIDDYDSSGTSKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYN
SQ  FSDLLRLTKILLAILDCVHVTTIFPISKMAKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPTATAPEGNVKQAEP
SQ  EKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSETSSGNSSQEGPSNVPGALDFEHIEEQAEGI
SQ  FGGSEETTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLD
SQ  QLRSIVEKSELWVYKGQGPDEAMDGASGENEHKKTEEGNNKSQQHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQ
SQ  QQRLLRNMGAHAVVLELLQIPYEKAEDTMMQEIMRLAHEFLQNFCAGNHPNQALLHKHINLFLNPGILEAVTMQHIFMNN
SQ  FQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRS
SQ  ERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDPEVEMKEI
SQ  YTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYH
SQ  CNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNLVQKTAMNWRLTARNAARRDSVLPVSRDYRNII
SQ  ERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLRE
SQ  MMTKDRGYGEKGEALRQILVNRYYGNIRPSGRRESLTSFGNGPLSPGGPSKPGGGGGGSGSSPMSRGEMSLAEVQCHLDK
SQ  EGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSD
SQ  LGNKKKDDEVDRDAPSRKKAKEPATQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQSGEGAQAAADKSKDDLEMSA
SQ  VITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLT
SQ  EYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKEL
SQ  VEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQTMLKPGGQVDGDETLDFYAQPTGPNEIVRL
SQ  DRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISF
SQ  NLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFN
SQ  VCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLXLLICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSI
SQ  ILMAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETSLPEASESLASEFLYSDVCRVETGENCSSPAPKEELVPAEETE
SQ  QDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQ
SQ  KKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAM
SQ  SLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGLLSELKDQMTDQRKQKQRMGLLGHPPHINVNPQQPA
//
ID  Q14643;
PN  Inositol 1,4,5-trisphosphate receptor type 1;
GN  ITPR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000305|PubMed:27108798}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27108798}. Note=Endoplasmic reticulum and secretory granules (By similarity). {ECO:0000250|UniProtKB:Q9TU34}.
DR  UNIPROT: Q14643;
DR  UNIPROT: E7EPX7;
DR  UNIPROT: E9PDE9;
DR  UNIPROT: Q14660;
DR  UNIPROT: Q99897;
DR  Pfam: PF08709;
DR  Pfam: PF00520;
DR  Pfam: PF02815;
DR  Pfam: PF08454;
DR  Pfam: PF01365;
DR  PROSITE: PS50919;
DR  OMIM: 117360;
DR  OMIM: 147265;
DR  OMIM: 206700;
DR  OMIM: 606658;
DR  DisGeNET: 3708;
DE  Function: Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5- trisphosphate (PubMed:27108797). Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (By similarity). Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways (By similarity). {ECO:0000250|UniProtKB:P11881, ECO:0000269|PubMed:27108797}.
DE  Disease: Spinocerebellar ataxia 15 (SCA15) [MIM:606658]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA15 is an autosomal dominant cerebellar ataxia (ADCA). It is very slow progressing form with a wide range of onset, ranging from childhood to adult. Most patients remain ambulatory. {ECO:0000269|PubMed:17590087, ECO:0000269|PubMed:18579805}. Note=The disease is caused by variants affecting the gene represented in this entry. Spinocerebellar ataxia 29 (SCA29) [MIM:117360]: An autosomal dominant, congenital spinocerebellar ataxia characterized by early motor delay, hypotonia and mild cognitive delay. Affected individuals develop a very slowly progressive or non-progressive gait and limb ataxia associated with cerebellar atrophy on brain imaging. Additional variable features include nystagmus, dysarthria, and tremor. {ECO:0000269|PubMed:22986007, ECO:0000269|PubMed:26770814}. Note=The disease is caused by variants affecting the gene represented in this entry. Gillespie syndrome (GLSP) [MIM:206700]: A rare disease characterized by bilateral iris hypoplasia, congenital hypotonia, non- progressive ataxia, progressive cerebellar atrophy, and intellectual disability. {ECO:0000269|PubMed:27108797, ECO:0000269|PubMed:27108798}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O14966; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P04626; IntAct: EBI-25368139; Score: 0.37
DE  Interaction: P10415; IntAct: EBI-15801089; Score: 0.40
DE  Interaction: Q9Y3M8; IntAct: EBI-2649793; Score: 0.37
DE  Interaction: Q9BS26; IntAct: EBI-541636; Score: 0.40
DE  Interaction: A0A6L7HLX1; IntAct: EBI-2831356; Score: 0.00
DE  Interaction: P21796; IntAct: EBI-10637640; Score: 0.38
DE  Interaction: P38646; IntAct: EBI-10637630; Score: 0.38
DE  Interaction: P31749; IntAct: EBI-10638019; Score: 0.54
DE  Interaction: P30405; IntAct: EBI-10637710; Score: 0.27
DE  Interaction: Q9Z1B5; IntAct: EBI-10996176; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-11027413; Score: 0.35
DE  Interaction: Q61879; IntAct: EBI-11041929; Score: 0.35
DE  Interaction: Q9ERG0; IntAct: EBI-11054044; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-11092730; Score: 0.35
DE  Interaction: Q9WTI7; IntAct: EBI-11093786; Score: 0.35
DE  Interaction: P56959; IntAct: EBI-11103888; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: Q6ZYL4; IntAct: EBI-11129915; Score: 0.35
DE  Interaction: Q9NYY3; IntAct: EBI-11148674; Score: 0.35
DE  Interaction: P35219; IntAct: EBI-21615486; Score: 0.35
DE  Interaction: Q96LR4; IntAct: EBI-21703554; Score: 0.35
DE  Interaction: Q8N1E6; IntAct: EBI-21820146; Score: 0.35
DE  Interaction: A2RU30; IntAct: EBI-21861544; Score: 0.35
DE  Interaction: Q13976; IntAct: EBI-15726455; Score: 0.35
DE  Interaction: O76074; IntAct: EBI-15726508; Score: 0.35
DE  Interaction: Q53ET0; IntAct: EBI-15980837; Score: 0.40
DE  Interaction: Q13557; IntAct: EBI-16812871; Score: 0.35
DE  Interaction: Q15149; IntAct: EBI-20919796; Score: 0.40
DE  Interaction: Q14108; IntAct: EBI-21264396; Score: 0.35
DE  Interaction: Q96GC9; IntAct: EBI-21267986; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21379742; Score: 0.00
DE  Interaction: O43561; IntAct: EBI-22080929; Score: 0.40
DE  Interaction: Q9HD36; IntAct: EBI-22188044; Score: 0.66
DE  Interaction: O43865; IntAct: EBI-22188149; Score: 0.50
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: O75582; IntAct: EBI-28931316; Score: 0.35
DE  Interaction: Q13555; IntAct: EBI-28939534; Score: 0.35
GO  GO:0005955;
GO  GO:0030659;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0031088;
GO  GO:0031094;
GO  GO:0031095;
GO  GO:0014069;
GO  GO:0016529;
GO  GO:0098685;
GO  GO:0030667;
GO  GO:0030658;
GO  GO:0019855;
GO  GO:0005509;
GO  GO:0015085;
GO  GO:0015278;
GO  GO:0070679;
GO  GO:0098695;
GO  GO:0005220;
GO  GO:0035091;
GO  GO:0019904;
GO  GO:0006816;
GO  GO:0000902;
GO  GO:0032469;
GO  GO:0042045;
GO  GO:0070059;
GO  GO:0050849;
GO  GO:0009791;
GO  GO:0010506;
GO  GO:0051209;
GO  GO:0001666;
GO  GO:0007165;
GO  GO:0050882;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGA
SQ  NSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSW
SQ  FYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVV
SQ  RLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDP
SQ  DFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVH
SQ  STNIPIDKEEEKPVMLKIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDL
SQ  VYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVL
SQ  RHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVS
SQ  MNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDA
SQ  KEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVT
SQ  PVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFY
SQ  NFSDLLRLTKILLAILDCVHVTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAA
SQ  PEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSETSSGNSSQEGPSNVPGALDF
SQ  EHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVD
SQ  NYKQIKQDLDQLRSIVEKSELWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQE
SQ  SASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEA
SQ  VTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRAS
SQ  FQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCY
SQ  VDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQ
SQ  LLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVL
SQ  AASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKL
SQ  CIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENATEELEPSPPLRQLEDHKRGEALRQVLVNRYYGNVRPSG
SQ  RRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALL
SQ  EGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEV
SQ  RDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQN
SQ  NKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILN
SQ  DINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNV
SQ  GHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTE
SQ  RDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGL
SQ  LWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEF
SQ  LYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVD
SQ  RLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPREELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDV
SQ  LRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHI
SQ  KEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNL
SQ  SGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA
//
ID  P11881;
PN  Inositol 1,4,5-trisphosphate receptor type 1;
GN  Itpr1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000305|PubMed:25368151}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14643}. Note=Endoplasmic reticulum and secretory granules. {ECO:0000250|UniProtKB:Q9TU34, ECO:0000269|PubMed:16990611, ECO:0000269|PubMed:24374158}.
DR  UNIPROT: P11881;
DR  UNIPROT: P20943;
DR  UNIPROT: Q99LG5;
DR  PDB: 1N4K;
DR  PDB: 1XZZ;
DR  PDB: 5GUG;
DR  PDB: 5X9Z;
DR  PDB: 5XA0;
DR  PDB: 5XA1;
DR  Pfam: PF08709;
DR  Pfam: PF00520;
DR  Pfam: PF02815;
DR  Pfam: PF08454;
DR  Pfam: PF01365;
DR  PROSITE: PS50919;
DE  Function: Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5- trisphosphate. Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (PubMed:23542070). Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways. {ECO:0000269|PubMed:19752026, ECO:0000269|PubMed:20813840, ECO:0000269|PubMed:23542070, ECO:0000269|PubMed:2554142}.
DE  Reference Proteome: Yes;
DE  Interaction: P10415; IntAct: EBI-15801106; Score: 0.52
DE  Interaction: Q9D1Q6; IntAct: EBI-541595; Score: 0.61
DE  Interaction: Q99KI0; IntAct: EBI-541623; Score: 0.40
DE  Interaction: P62158; IntAct: EBI-911456; Score: 0.35
DE  Interaction: P05131; IntAct: EBI-2931605; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-6271507; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-9072132; Score: 0.35
DE  Interaction: P42859; IntAct: EBI-9674781; Score: 0.40
DE  Interaction: O35668; IntAct: EBI-9674795; Score: 0.35
DE  Interaction: Q60932; IntAct: EBI-10637680; Score: 0.27
DE  Interaction: Q99KR7; IntAct: EBI-10637672; Score: 0.27
DE  Interaction: P38647; IntAct: EBI-10637771; Score: 0.27
DE  Interaction: O35157; IntAct: EBI-15559496; Score: 0.50
DE  Interaction: Q8VDN2; IntAct: EBI-15559478; Score: 0.50
DE  Interaction: Q6PIE5; IntAct: EBI-15559605; Score: 0.50
DE  Interaction: Q8BNY6; IntAct: EBI-15612731; Score: 0.40
DE  Interaction: Q3U182; IntAct: EBI-15980785; Score: 0.40
DE  Interaction: Q6NZM9; IntAct: EBI-26471064; Score: 0.35
DE  Interaction: Q9CQE6; IntAct: EBI-26472808; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-26573447; Score: 0.35
DE  Interaction: P16056; IntAct: EBI-27118288; Score: 0.35
GO  GO:0005955;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0030425;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0098982;
GO  GO:0030176;
GO  GO:0043231;
GO  GO:0045121;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031088;
GO  GO:0031094;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0098793;
GO  GO:0032991;
GO  GO:0016529;
GO  GO:0098685;
GO  GO:0030667;
GO  GO:0030868;
GO  GO:0045202;
GO  GO:0097060;
GO  GO:0030658;
GO  GO:0019855;
GO  GO:0005509;
GO  GO:0015278;
GO  GO:0042802;
GO  GO:0070679;
GO  GO:0098695;
GO  GO:0005220;
GO  GO:0035091;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0019903;
GO  GO:0044877;
GO  GO:0044325;
GO  GO:0006816;
GO  GO:0000902;
GO  GO:0071320;
GO  GO:0032469;
GO  GO:0042045;
GO  GO:0070059;
GO  GO:0097421;
GO  GO:0050849;
GO  GO:1901215;
GO  GO:0043065;
GO  GO:0051928;
GO  GO:0007204;
GO  GO:2000347;
GO  GO:0010976;
GO  GO:0009791;
GO  GO:0051209;
GO  GO:0001666;
GO  GO:0050882;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGA
SQ  NSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSW
SQ  FYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVV
SQ  RLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDP
SQ  DFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVH
SQ  STNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDL
SQ  VYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVL
SQ  RHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVS
SQ  MNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAK
SQ  EGQKEDRDILSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTP
SQ  VKYARLWSEIPSEIAIDDYDSSGTSKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYN
SQ  FSDLLRLTKILLAILDCVHVTTIFPISKMTKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEP
SQ  EKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQSSETSSGNSSQEGPSNVPGALDFEHIEEQAEGI
SQ  FGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLD
SQ  QLRSIVEKSELWVYKGQGPDEPMDGASGENEHKKTEEGTSKPLKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQ
SQ  QQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNN
SQ  FQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRS
SQ  ERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEI
SQ  YTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYH
SQ  CNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNIVQKTALNWRLSARNAARRDSVLAASRDYRNII
SQ  ERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLRE
SQ  MMTKDRGYGEKQISIDESENAELPQAPEAENSTEQELEPSPPLRQLEDHKRGEALRQILVNRYYGNIRPSGRRESLTSFG
SQ  NGPLSPGGPSKPGGGGGGPGSSSTSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQH
SQ  SFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASA
SQ  ATRKAFTTFRREADPDDHYQSGEGTQATTDKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVC
SQ  ETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKR
SQ  MDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAH
SQ  QLARHNKELQTMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKIN
SQ  DFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISL
SQ  AIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLLI
SQ  CAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVP
SQ  ETGESLANDFLYSDVCRVETGENCTSPAPKEELLPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEP
SQ  LFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHY
SQ  LCFIVLVKVKDSTEYTGPESYVAEMIRERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKD
SQ  QMTEQRKQKQRIGLLGHPPHMNVNPQQPA
//
ID  P29994;
PN  Inositol 1,4,5-trisphosphate receptor type 1;
GN  Itpr1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14643}. Note=Endoplasmic reticulum and secretory granules (By similarity). {ECO:0000250|UniProtKB:Q9TU34}.
DR  UNIPROT: P29994;
DR  UNIPROT: Q62869;
DR  PDB: 3JAV;
DR  PDB: 3T8S;
DR  PDB: 3UJ0;
DR  PDB: 3UJ4;
DR  PDB: 6MU1;
DR  PDB: 6MU2;
DR  PDB: 7LHE;
DR  PDB: 7LHF;
DR  Pfam: PF08709;
DR  Pfam: PF00520;
DR  Pfam: PF02815;
DR  Pfam: PF08454;
DR  Pfam: PF01365;
DR  PROSITE: PS50919;
DE  Function: Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5- trisphosphate. Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways. {ECO:0000250|UniProtKB:P11881}.
DE  Reference Proteome: Yes;
DE  Interaction: Q96RG2; IntAct: EBI-8614700; Score: 0.44
DE  Interaction: P54256; IntAct: EBI-9674257; Score: 0.58
DE  Interaction: P51111; IntAct: EBI-9674682; Score: 0.52
DE  Interaction: P42858; IntAct: EBI-9674812; Score: 0.52
DE  Interaction: P31749; IntAct: EBI-15683723; Score: 0.40
DE  Interaction: P29994; IntAct: EBI-15939786; Score: 0.53
DE  Interaction: Q3U182; IntAct: EBI-15980711; Score: 0.40
DE  Interaction: P19332; IntAct: EBI-26374040; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26438079; Score: 0.35
DE  Interaction: F1M0Z1; IntAct: EBI-26961439; Score: 0.35
GO  GO:0005955;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0030425;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0098982;
GO  GO:0030176;
GO  GO:0043231;
GO  GO:0045121;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031088;
GO  GO:0031094;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0098793;
GO  GO:0032991;
GO  GO:0016529;
GO  GO:0098685;
GO  GO:0030667;
GO  GO:0030868;
GO  GO:0045202;
GO  GO:0097060;
GO  GO:0030658;
GO  GO:0019855;
GO  GO:0005509;
GO  GO:0015278;
GO  GO:0042802;
GO  GO:0070679;
GO  GO:0098695;
GO  GO:0005220;
GO  GO:0035091;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0019903;
GO  GO:0044877;
GO  GO:0044325;
GO  GO:0006816;
GO  GO:0000902;
GO  GO:0071320;
GO  GO:0071456;
GO  GO:0016358;
GO  GO:0032469;
GO  GO:0042045;
GO  GO:0070059;
GO  GO:0097421;
GO  GO:0050849;
GO  GO:1901215;
GO  GO:0043065;
GO  GO:0051928;
GO  GO:0007204;
GO  GO:2000347;
GO  GO:0010976;
GO  GO:0009791;
GO  GO:0051209;
GO  GO:0001666;
GO  GO:0050882;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGA
SQ  NSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSW
SQ  FYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVV
SQ  RLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDP
SQ  DFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVH
SQ  STNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDL
SQ  VYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVL
SQ  RHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVS
SQ  MNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAK
SQ  EGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTP
SQ  VKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYN
SQ  FSDLLRLTKILLAILDCVHVTTIFPISKMTKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEP
SQ  EKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQSSETSSGNSSQEGPSNVPGALDFEHIEEQAEGI
SQ  FGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLD
SQ  QLRSIVEKSELWVYKGQGPDEPMDGASGENEHKKTEEGTSKPLKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQ
SQ  QQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNN
SQ  FQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRS
SQ  ERDRMDENSPLFMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKE
SQ  IYTSNHMWKLFENFLVDICRACNNTSDRKHADSVLEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVY
SQ  HCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNIVQKTAMNWRLSARNAARRDSVLAASRDYRNI
SQ  IERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLR
SQ  EMMTKDRGYGEKQISIDELENAELPQPPEAENSTEQELEPSPPLRQLEDHKRGEALRQILVNRYYGNIRPSGRRESLTSF
SQ  GNGPLSPGGPSKPGGGGGGPGSGSTSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQ
SQ  HSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEAS
SQ  AATRKAFTTFRREADPDDHYQSGEGTQATTDKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLV
SQ  CETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKK
SQ  RMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILA
SQ  HQLARHNKELQTMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKI
SQ  NDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLIS
SQ  LAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLL
SQ  ICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRPIILTAALALILVYLFSIVGYLFFKDDFILEVDRLPNETAG
SQ  PETGESLANDFLYSDVCRVETGENCTSPAPKEELLPVEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEE
SQ  PLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWH
SQ  YLCFIVLVKVKDSTEYTGPESYVAEMIRERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELK
SQ  DQMTEQRKQKQRIGLLGHPPHMNVNPQQPA
//
ID  Q15811;
PN  Intersectin-1;
GN  ITSN1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endomembrane system {ECO:0000269|PubMed:11744688}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9WVE9}. Cell projection, lamellipodium {ECO:0000269|PubMed:11744688}. Cell membrane {ECO:0000269|PubMed:11744688, ECO:0000269|PubMed:20946875}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:20946875, ECO:0000269|PubMed:29887380}. Recycling endosome {ECO:0000269|PubMed:29030480}. Endosome {ECO:0000250|UniProtKB:Q9Z0R4}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9Z0R4}. Note=Colocalizes with SGIP1 at the plasma membrane in structures corresponding most probably to clathrin-coated pits (PubMed:20946875). Colocalizes with RAB13 on cytoplasmic vesicles that are most likely recycling endosomes (PubMed:29030480). {ECO:0000269|PubMed:20946875, ECO:0000269|PubMed:29030480}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:29599122}. Endomembrane system {ECO:0000269|PubMed:21712076}. Nucleus envelope {ECO:0000269|PubMed:29599122}. Note=Shuttles between the cytoplasm and nucleus in an XPO1/CRM1-dependent manner. {ECO:0000269|PubMed:29599122}. [Isoform 5]: Endomembrane system {ECO:0000269|PubMed:21712076}.
DR  UNIPROT: Q15811;
DR  UNIPROT: A7Y322;
DR  UNIPROT: A8CTX8;
DR  UNIPROT: A8CTY3;
DR  UNIPROT: A8CTY7;
DR  UNIPROT: A8D7D0;
DR  UNIPROT: A8DCP3;
DR  UNIPROT: B4DTM2;
DR  UNIPROT: E7ERJ1;
DR  UNIPROT: E9PE44;
DR  UNIPROT: E9PG01;
DR  UNIPROT: E9PHV2;
DR  UNIPROT: O95216;
DR  UNIPROT: Q0PW94;
DR  UNIPROT: Q0PW95;
DR  UNIPROT: Q0PW97;
DR  UNIPROT: Q14BD3;
DR  UNIPROT: Q1ED40;
DR  UNIPROT: Q20BK3;
DR  UNIPROT: Q9UET5;
DR  UNIPROT: Q9UK60;
DR  UNIPROT: Q9UNK1;
DR  UNIPROT: Q9UNK2;
DR  UNIPROT: Q9UQ92;
DR  PDB: 1KI1;
DR  PDB: 2KGR;
DR  PDB: 2KHN;
DR  PDB: 3FIA;
DR  PDB: 3QBV;
DR  PDB: 4IIM;
DR  PDB: 5HZI;
DR  PDB: 5HZJ;
DR  PDB: 5HZK;
DR  PDB: 6GBU;
DR  PDB: 6H5T;
DR  Pfam: PF00168;
DR  Pfam: PF12763;
DR  Pfam: PF16617;
DR  Pfam: PF16652;
DR  Pfam: PF00621;
DR  Pfam: PF00018;
DR  Pfam: PF07653;
DR  Pfam: PF14604;
DR  PROSITE: PS50004;
DR  PROSITE: PS00741;
DR  PROSITE: PS50010;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS50031;
DR  PROSITE: PS50003;
DR  PROSITE: PS50002;
DR  OMIM: 602442;
DR  DisGeNET: 6453;
DE  Function: Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery (PubMed:11584276, PubMed:29887380). Acts as guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex (PubMed:11584276). Plays a role in the assembly and maturation of clathrin-coated vesicles (By similarity). Recruits FCHSD2 to clathrin-coated pits (PubMed:29887380). Involved in endocytosis of activated EGFR, and probably also other growth factor receptors (By similarity). Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2 (PubMed:22648170). Promotes ubiquitination and subsequent degradation of EGFR, and thereby contributes to the down-regulation of EGFR-dependent signaling pathways. In chromaffin cells, required for normal exocytosis of catecholamines. Required for rapid replenishment of release-ready synaptic vesicles at presynaptic active zones (By similarity). Inhibits ARHGAP31 activity toward RAC1 (PubMed:11744688). {ECO:0000250|UniProtKB:Q9WVE9, ECO:0000250|UniProtKB:Q9Z0R4, ECO:0000269|PubMed:11584276, ECO:0000269|PubMed:11744688, ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:29887380}. [Isoform 1]: Plays a role in synaptic vesicle endocytosis in brain neurons. {ECO:0000250|UniProtKB:Q9Z0R4}.
DE  Reference Proteome: Yes;
DE  Interaction: O43426; IntAct: EBI-7965393; Score: 0.40
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P09917; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: P35658; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: P60880; IntAct: EBI-8589666; Score: 0.35
DE  Interaction: Q12840; IntAct: EBI-730237; Score: 0.00
DE  Interaction: P42566; IntAct: EBI-6951101; Score: 0.56
DE  Interaction: Q07889; IntAct: EBI-7222790; Score: 0.64
DE  Interaction: O00401; IntAct: EBI-7987685; Score: 0.70
DE  Interaction: P60953; IntAct: EBI-602095; Score: 0.54
DE  Interaction: P61968; IntAct: EBI-7222047; Score: 0.37
DE  Interaction: Q05193; IntAct: EBI-7591434; Score: 0.62
DE  Interaction: P50570; IntAct: EBI-7591943; Score: 0.71
DE  Interaction: P68104; IntAct: EBI-730234; Score: 0.00
DE  Interaction: Q13432; IntAct: EBI-730240; Score: 0.00
DE  Interaction: Q9BYC9; IntAct: EBI-732259; Score: 0.00
DE  Interaction: Q9Y5X3; IntAct: EBI-732262; Score: 0.00
DE  Interaction: Q8TAQ2; IntAct: EBI-734884; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-928807; Score: 0.55
DE  Interaction: P09172; IntAct: EBI-8589642; Score: 0.27
DE  Interaction: Q15811; IntAct: EBI-8589666; Score: 0.35
DE  Interaction: O75940; IntAct: EBI-1068586; Score: 0.00
DE  Interaction: O15357; IntAct: EBI-8052389; Score: 0.60
DE  Interaction: P22681; IntAct: EBI-8611246; Score: 0.73
DE  Interaction: Q925Q9; IntAct: EBI-8555189; Score: 0.52
DE  Interaction: P04370; IntAct: EBI-7728309; Score: 0.40
DE  Interaction: P39053; IntAct: EBI-7965349; Score: 0.40
DE  Interaction: Q2M1Z3; IntAct: EBI-7965368; Score: 0.40
DE  Interaction: P22682; IntAct: EBI-7965471; Score: 0.40
DE  Interaction: Q62245; IntAct: EBI-7965553; Score: 0.40
DE  Interaction: Q3TTA7; IntAct: EBI-7965508; Score: 0.40
DE  Interaction: P63010; IntAct: EBI-30816498; Score: 0.59
DE  Interaction: O43150; IntAct: EBI-2654148; Score: 0.00
DE  Interaction: Q6ZUJ8; IntAct: EBI-2654176; Score: 0.00
DE  Interaction: Q15427; IntAct: EBI-2654196; Score: 0.00
DE  Interaction: P22674; IntAct: EBI-2654206; Score: 0.00
DE  Interaction: Q99471; IntAct: EBI-2654186; Score: 0.00
DE  Interaction: Q9Y2W2; IntAct: EBI-2654216; Score: 0.00
DE  Interaction: A0A6H3A910; IntAct: EBI-2831328; Score: 0.00
DE  Interaction: P67870; IntAct: EBI-7133985; Score: 0.37
DE  Interaction: Q16659; IntAct: EBI-7210088; Score: 0.37
DE  Interaction: Q13387; IntAct: EBI-7238306; Score: 0.37
DE  Interaction: P53350; IntAct: EBI-7313057; Score: 0.37
DE  Interaction: O75582; IntAct: EBI-7373257; Score: 0.37
DE  Interaction: Q99962; IntAct: EBI-7387564; Score: 0.37
DE  Interaction: P04183; IntAct: EBI-7398611; Score: 0.37
DE  Interaction: P61086; IntAct: EBI-7411905; Score: 0.37
DE  Interaction: Q9NYL2; IntAct: EBI-7418184; Score: 0.37
DE  Interaction: Q3UQN2; IntAct: EBI-6097080; Score: 0.56
DE  Interaction: O43175; IntAct: EBI-9395254; Score: 0.35
DE  Interaction: Q92734; IntAct: EBI-11029015; Score: 0.35
DE  Interaction: Q9NS91; IntAct: EBI-11143700; Score: 0.35
DE  Interaction: Q96CW1; IntAct: EBI-21520588; Score: 0.35
DE  Interaction: Q8NB37; IntAct: EBI-21611026; Score: 0.35
DE  Interaction: Q9NZQ3; IntAct: EBI-21676174; Score: 0.35
DE  Interaction: Q9NVZ3; IntAct: EBI-21720899; Score: 0.35
DE  Interaction: Q8N9I9; IntAct: EBI-21791883; Score: 0.35
DE  Interaction: Q59EK9; IntAct: EBI-21795241; Score: 0.35
DE  Interaction: P53680; IntAct: EBI-21808127; Score: 0.35
DE  Interaction: Q86X29; IntAct: EBI-21808254; Score: 0.35
DE  Interaction: Q9HCN6; IntAct: EBI-15816584; Score: 0.40
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: P15311; IntAct: EBI-16792219; Score: 0.27
DE  Interaction: Q13444; IntAct: EBI-21226632; Score: 0.44
DE  Interaction: O43184; IntAct: EBI-21227583; Score: 0.44
DE  Interaction: Q6NSK7; IntAct: EBI-21386219; Score: 0.00
DE  Interaction: Q15599; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: P22307; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: O95757; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: P51659; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: Q9UBC2; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: Q13011; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: P09496; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: Q969X6; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: P04040; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: O94973; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: O95782; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: Q9BYB0; IntAct: EBI-26514359; Score: 0.37
DE  Interaction: Q9BZD6; IntAct: EBI-26604363; Score: 0.44
DE  Interaction: P07355; IntAct: EBI-27094310; Score: 0.52
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: Q6ZMQ8; IntAct: EBI-32723474; Score: 0.27
GO  GO:0070161;
GO  GO:0005905;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030027;
GO  GO:0043005;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0055037;
GO  GO:0005509;
GO  GO:0005085;
GO  GO:0060090;
GO  GO:0070064;
GO  GO:0150007;
GO  GO:0006897;
GO  GO:0016197;
GO  GO:0006887;
GO  GO:0035556;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:0051056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQFPTPFGGSLDIWAITVEERAKHDQQFHSLKPISGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSI
SQ  AMKLIKLKLQGYQLPSALPPVMKQQPVAISSAPAFGMGGIASMPPLTAVAPVPMGSIPVVGMSPTLVSSVPTAAVPPLAN
SQ  GAPPVIQPLPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASVPPVAEWAVPQSSRLKYRQLFNSHDKTMSGHL
SQ  TGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPVLPPEYIPPSFRRVRSGSGISVI
SQ  SSTSVDQRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQE
SQ  QERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEF
SQ  ELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSL
SQ  HRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKII
SQ  ELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRLFHQHQEPAKPAV
SQ  QAPWSTAEKGPLTISAQENVKVVYYRALYPFESRSHDEITIQPGDIVMVKGEWVDESQTGEPGWLGGELKGKTGWFPANY
SQ  AEKIPENEVPAPVKPVTDSTSAPAPKLALRETPAPLAVTSSEPSTTPNNWADFSSTWPTSTNEKPETDNWDAWAAQPSLT
SQ  VPSAGQLRQRSAFTPATATGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKNDVITVLEQQDMWWFGEVQGQKGW
SQ  FPKSYVKLISGPIRKSTSMDSGSSESPASLKRVASPAAKPVVSGEEFIAMYTYESSEQGDLTFQQGDVILVTKKDGDWWT
SQ  GTVGDKAGVFPSNYVRLKDSEGSGTAGKTGSLGKKPEIAQVIASYTATGPEQLTLAPGQLILIRKKNPGGWWEGELQARG
SQ  KKRQIGWFPANYVKLLSPGTSKITPTEPPKSTALAAVCQVIGMYDYTAQNDDELAFNKGQIINVLNKEDPDWWKGEVNGQ
SQ  VGLFPSNYVKLTTDMDPSQQWCSDLHLLDMLTPTERKRQGYIHELIVTEENYVNDLQLVTEIFQKPLMESELLTEKEVAM
SQ  IFVNWKELIMCNIKLLKALRVRKKMSGEKMPVKMIGDILSAQLPHMQPYIRFCSRQLNGAALIQQKTDEAPDFKEFVKRL
SQ  AMDPRCKGMPLSSFILKPMQRVTRYPLIIKNILENTPENHPDHSHLKHALEKAEELCSQVNEGVREKENSDRLEWIQAHV
SQ  QCEGLSEQLVFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYKMYKTPI
SQ  FLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKREKAYLVRSQRATGIGRLMV
SQ  NVVEGIELKPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTEI
SQ  RVADIKKDQGSKGPVTKCLLLHEVPTGEIVVRLDLQLFDEP
//
ID  Q9Z0R4;
PN  Intersectin-1;
GN  Itsn1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endomembrane system {ECO:0000269|PubMed:16914641}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9WVE9}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q15811}. Cell membrane {ECO:0000250|UniProtKB:Q15811}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q15811}. Recycling endosome {ECO:0000250|UniProtKB:Q15811}. Endosome {ECO:0000269|PubMed:16914641}. Cytoplasmic vesicle {ECO:0000269|PubMed:16914641, ECO:0000269|PubMed:23633571}. Note=Colocalizes with SGIP1 at the plasma membrane in structures corresponding most probably to clathrin-coated pits. Colocalizes with RAB13 on cytoplasmic vesicles that are most likely recycling endosomes. {ECO:0000250|UniProtKB:Q15811}. [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q15811}. Nucleus envelope {ECO:0000250|UniProtKB:Q15811}. Note=Shuttles between the cytoplasm and nucleus in an XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:Q15811}.
DR  UNIPROT: Q9Z0R4;
DR  UNIPROT: F8VQE5;
DR  UNIPROT: Q9R143;
DR  PDB: 3HS8;
DR  PDB: 3JV3;
DR  Pfam: PF00168;
DR  Pfam: PF12763;
DR  Pfam: PF16617;
DR  Pfam: PF16652;
DR  Pfam: PF00621;
DR  Pfam: PF00018;
DR  Pfam: PF07653;
DR  Pfam: PF14604;
DR  PROSITE: PS50004;
DR  PROSITE: PS00741;
DR  PROSITE: PS50010;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS50031;
DR  PROSITE: PS50003;
DR  PROSITE: PS50002;
DE  Function: Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery (PubMed:10064583). Acts as guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex (By similarity). Plays a role in the assembly and maturation of clathrin- coated vesicles (By similarity). Recruits FCHSD2 to clathrin-coated pits (By similarity). Involved in endocytosis of activated EGFR, and probably also other growth factor receptors (PubMed:16914641). Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2 (By similarity). Promotes ubiquitination and subsequent degradation of EGFR, and thereby contributes to the down-regulation of EGFR-dependent signaling pathways (PubMed:16914641). In chromaffin cells, required for normal exocytosis of catecholamines (PubMed:18676989). Required for rapid replenishment of release-ready synaptic vesicles at presynaptic active zones (PubMed:23633571). Inhibits ARHGAP31 activity toward RAC1 (By similarity). {ECO:0000250|UniProtKB:Q15811, ECO:0000250|UniProtKB:Q9WVE9, ECO:0000269|PubMed:10064583, ECO:0000269|PubMed:16914641, ECO:0000269|PubMed:18676989, ECO:0000269|PubMed:23633571}. [Isoform 1]: Plays a role in synaptic vesicle endocytosis in brain neurons. {ECO:0000269|PubMed:18676989}.
DE  Reference Proteome: Yes;
DE  Interaction: P42567; IntAct: EBI-6951130; Score: 0.44
DE  Interaction: Q60902; IntAct: EBI-6951169; Score: 0.37
DE  Interaction: P39054; IntAct: EBI-10919841; Score: 0.37
DE  Interaction: P39053; IntAct: EBI-10919863; Score: 0.44
DE  Interaction: O00401; IntAct: EBI-7583677; Score: 0.40
DE  Interaction: Q07889; IntAct: EBI-7583891; Score: 0.40
DE  Interaction: Q9EQ32; IntAct: EBI-654271; Score: 0.37
DE  Interaction: Q80VP1; IntAct: EBI-7340792; Score: 0.37
DE  Interaction: Q6P549; IntAct: EBI-8052797; Score: 0.40
DE  Interaction: P22682; IntAct: EBI-8611151; Score: 0.40
DE  Interaction: Q8K382; IntAct: EBI-7186752; Score: 0.52
DE  Interaction: A6X8Z5; IntAct: EBI-4326020; Score: 0.52
DE  Interaction: Q640N3; IntAct: EBI-4326092; Score: 0.40
DE  Interaction: P50516; IntAct: EBI-6272793; Score: 0.35
DE  Interaction: P98078; IntAct: EBI-6307040; Score: 0.46
DE  Interaction: Q9Y2D8; IntAct: EBI-11694681; Score: 0.35
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: Q8BIZ1; IntAct: EBI-26595802; Score: 0.35
GO  GO:0070161;
GO  GO:0097440;
GO  GO:0044305;
GO  GO:0005905;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0030139;
GO  GO:0098978;
GO  GO:0097708;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0098871;
GO  GO:0098833;
GO  GO:0055037;
GO  GO:0045202;
GO  GO:0005509;
GO  GO:0005085;
GO  GO:0019209;
GO  GO:0060090;
GO  GO:0070064;
GO  GO:0150007;
GO  GO:0006897;
GO  GO:0016197;
GO  GO:0006887;
GO  GO:0043524;
GO  GO:0051402;
GO  GO:2001288;
GO  GO:0060999;
GO  GO:0060124;
GO  GO:0051897;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:1905274;
GO  GO:0007264;
GO  GO:0048488;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQFPTPFGGSLDVWAITVEERAKHDQQFLSLKPIAGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSI
SQ  AMKLIKLKLQGYQLPSTLPPVMKQQPVAISSAPAFGIGGIASMPPLTAVAPVPMGSIPVVGMSPPLVSSVPPAAVPPLAN
SQ  GAPPVIQPLPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASAPPAAEWAVPQSSRLKYRQLFNSHDKTMSGHL
SQ  TGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPVLPPEYIPPSFRRVRSGSGMSVI
SQ  SSSSVDQRLPEEPSSEDEQQPEKKLPVTFEDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQ
SQ  ERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFE
SQ  LEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLH
SQ  RDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQEIDVFNNQLKELREIHSKQQLQKQRSLEAARLKQKEQERKSLE
SQ  LEKQKEDAQRRVQERDKQWLEHVQQEEQPRPRKPHEEDRLKREDSVRKKEAEERAKPEMQDKQSRLFHPHQEPAKLATQA
SQ  PWSTTEKGPLTISAQESVKVVYYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEKIPEN
SQ  EVPTPAKPVTDLTSAPAPKLALRETPAPLPVTSSEPSTTPNNWADFSSTWPSSSNEKPETDNWDTWAAQPSLTVPSAGQL
SQ  RQRSAFTPATATGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKSDVITVLEQQDMWWFGEVQGQKGWFPKSYVK
SQ  LISGPVRKSTSIDTGPTESPASLKRVASPAAKPAIPGEEFIAMYTYESSEQGDLTFQQGDVIVVTKKDGDWWTGTVGDKS
SQ  GVFPSNYVRLKDSEGSGTAGKTGSLGKKPEIAQVIASYAATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGW
SQ  FPANYVKLLSPGTSKITPTELPKTAVQPAVCQVIGMYDYTAQNDDELAFSKGQIINVLNKEDPDWWKGEVSGQVGLFPSN
SQ  YVKLTTDMDPSQQWCSDLHLLDMLTPTERKRQGYIHELIVTEENYVNDLQLVTEIFQKPLTESELLTEKEVAMIFVNWKE
SQ  LIMCNIKLLKALRVRKKMSGEKMPVKMIGDILSAQLPHMQPYIRFCSCQLNGAALIQQKTDEAPDFKEFVKRLAMDPRCK
SQ  GMPLSSFILKPMQRVTRYPLIIKNILENTPENHPDHSHLKHALEKAEELCSQVNEGVREKENSDRLEWIQAHVQCEGLSE
SQ  QLVFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYKMYKTPIFLNEVLV
SQ  KLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKREKAYLVRSQRATGIGRLMVNVVEGIE
SQ  LKPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTEIRVADIKK
SQ  DQGSKGPVTKCLLLHEVPTGEIVVRLDLQLFDEP
//
ID  Q9WVE9;
PN  Intersectin-1;
GN  Itsn1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Endomembrane system {ECO:0000250|UniProtKB:Q15811}. Synapse, synaptosome {ECO:0000269|PubMed:10373452, ECO:0000269|PubMed:26797119}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q15811}. Cell membrane {ECO:0000250|UniProtKB:Q15811}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:11584276, ECO:0000269|PubMed:20448150}. Recycling endosome {ECO:0000250|UniProtKB:Q15811}. Endosome {ECO:0000250|UniProtKB:Q9Z0R4}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9Z0R4}. Note=Colocalizes with SGIP1 at the plasma membrane in structures corresponding most probably to clathrin- coated pits. Colocalizes with RAB13 on cytoplasmic vesicles that are most likely recycling endosomes. {ECO:0000250|UniProtKB:Q15811}. [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q15811}. Nucleus envelope {ECO:0000250|UniProtKB:Q15811}. Note=Shuttles between the cytoplasm and nucleus in an XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:Q15811}.
DR  UNIPROT: Q9WVE9;
DR  UNIPROT: D3ZV52;
DR  UNIPROT: F1M823;
DR  UNIPROT: Q9WVE1;
DR  PDB: 3HS9;
DR  Pfam: PF00168;
DR  Pfam: PF12763;
DR  Pfam: PF16617;
DR  Pfam: PF16652;
DR  Pfam: PF00621;
DR  Pfam: PF00018;
DR  Pfam: PF07653;
DR  Pfam: PF14604;
DR  PROSITE: PS50004;
DR  PROSITE: PS00741;
DR  PROSITE: PS50010;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS50031;
DR  PROSITE: PS50003;
DR  PROSITE: PS50002;
DE  Function: Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery. Acts as guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex (By similarity). Plays a role in the assembly and maturation of clathrin- coated vesicles (PubMed:20448150). Recruits FCHSD2 to clathrin-coated pits (By similarity). Involved in endocytosis of activated EGFR, and probably also other growth factor receptors (By similarity). Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2 (By similarity). Promotes ubiquitination and subsequent degradation of EGFR, and thereby contributes to the down-regulation of EGFR-dependent signaling pathways. In chromaffin cells, required for normal exocytosis of catecholamines (By similarity). Required for rapid replenishment of release-ready synaptic vesicles at presynaptic active zones (PubMed:23633571). Inhibits ARHGAP31 activity toward RAC1 (By similarity). {ECO:0000250|UniProtKB:Q15811, ECO:0000250|UniProtKB:Q9Z0R4, ECO:0000269|PubMed:20448150, ECO:0000269|PubMed:23633571}. [Isoform 1]: Plays a role in synaptic vesicle endocytosis in brain neurons. {ECO:0000250|UniProtKB:Q9Z0R4}.
DE  Reference Proteome: Yes;
DE  Interaction: P60881; IntAct: EBI-7031678; Score: 0.60
DE  Interaction: E9PSY8; IntAct: EBI-10919034; Score: 0.40
DE  Interaction: P21575; IntAct: EBI-7031625; Score: 0.56
DE  Interaction: O70377; IntAct: EBI-7031784; Score: 0.44
DE  Interaction: P14668; IntAct: EBI-8589490; Score: 0.27
DE  Interaction: Q3UQN2; IntAct: EBI-6095200; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26440627; Score: 0.35
GO  GO:0070161;
GO  GO:0097440;
GO  GO:0044305;
GO  GO:0005905;
GO  GO:0005737;
GO  GO:0043197;
GO  GO:0030139;
GO  GO:0098978;
GO  GO:0097708;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0098871;
GO  GO:0098833;
GO  GO:0055037;
GO  GO:0045202;
GO  GO:0043195;
GO  GO:0005509;
GO  GO:0005085;
GO  GO:0019209;
GO  GO:0060090;
GO  GO:0070064;
GO  GO:0007420;
GO  GO:0150007;
GO  GO:0006897;
GO  GO:0016197;
GO  GO:0006887;
GO  GO:0043524;
GO  GO:0051402;
GO  GO:2001288;
GO  GO:0060999;
GO  GO:0060124;
GO  GO:0051897;
GO  GO:0008104;
GO  GO:0015031;
GO  GO:1905274;
GO  GO:0007264;
GO  GO:0048488;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQFPTPFGGSLDIWAITVEERAKHDQQFQSLKPISGFITGDQARNFFFQSGLPQPVLAQIWALADMNKDGRMDQVEFSI
SQ  AMKLIKLKLQGYQLPPALPPVMKQQPAAISSAPAFGIGGMAGMPPLTAVAPVPMGSIPVVGMSPPLVSSVPQAAVPPLAN
SQ  GAPPVIQPLPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASAPAAAEWAVPQSSRLKYRQLFNSHDKTMSGHL
SQ  TGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPVLPPEYIPPSFRRVRSGSGMSVI
SQ  SSSSADQRLPEEPSSEDEQQVEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQ
SQ  ERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLTQRNKDQEGIVVLKARRKTLEFE
SQ  LEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLH
SQ  RDSLLTLKRALEAKELARQQLREQLDEVEKETRSKLQEIDVFNNQLKELREIHSKQQLQKQRSIEAERLKQKEQERKSLE
SQ  LEKQKEEGQRRVQERDKQWQEHVQQEEQQRPRKPHEEDKLKREDSVKKKEAEERAKPEVQDKQSRLFHPHQEPAKPAQAP
SQ  WPTTEKGPLTISAQESAKVVYYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEKIPENE
SQ  IPTPAKPVTDLTSAPAPKLALRETPAPLPVTSSEPSTTPNNWADFSSTWPSSTNEKPETDNWDTWAAQPSLTVPSAGQLR
SQ  QRSAFTPATATGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKSDVITVLEQQDMWWFGEVQGQKGWFPKSYVKL
SQ  ISGPVRKSTSIDTGPTEAPSSLKRVASPAAKPAIPGEEFVAMYTYESSEHGDLTFQQGDVIVVTKKDGDWWTGTVGETSG
SQ  VFPSNYVRLKDSEGSGTAGKTGSLGKKPEIAQVIASYTATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWF
SQ  PANYVKLLSPGTSKITPTELPKTAVQPAVCQVIGMYDYTAQNDDELAFSKGQIINVLSKEDPDWWKGEVSGQVGLFPSNY
SQ  VKLTTDMDPSQQWCSDLHLLDMLTPTERKRQGYIHELIVTEENYVNDLQLVTEIFQKPLTESELLTEKEVAMIFVNWKEL
SQ  IMCNIKLLKALRVRKKMSGEKMPVKMIGDILSAQLPHMQPYIRFCSCQLNGAALIQQKTDEAPDFKEFVKRLAMDPRCKG
SQ  MPLSSFILKPMQRVTRYPLIIKNILENTPENHPDHSHLKHALEKAEELCSQVNEGVREKENSDRLEWIQAHVQCEGLSEQ
SQ  LVFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSSTDKVFSPKSNLQYKMYKTPIFLNEVLVK
SQ  LPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKREKAYLVRSQRATGIGRLMVNVVEGIEL
SQ  KPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTEIRVADIKKD
SQ  QGSKGPVTKCLLLHEVPTGEIVVRLDLQLFDEP
//
ID  O42287;
PN  Intersectin-1;
GN  itsn1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Endomembrane system {ECO:0000250|UniProtKB:Q15811}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9WVE9}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q15811}. Cell membrane {ECO:0000250|UniProtKB:Q15811}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q15811}. Recycling endosome {ECO:0000250|UniProtKB:Q15811}. [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q15811}. Nucleus envelope {ECO:0000250|UniProtKB:Q15811}. Note=Shuttles between the cytoplasm and nucleus in an XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:Q15811}.
DR  UNIPROT: O42287;
DR  UNIPROT: A0A1L8HCG8;
DR  Pfam: PF00168;
DR  Pfam: PF12763;
DR  Pfam: PF16617;
DR  Pfam: PF16652;
DR  Pfam: PF00621;
DR  Pfam: PF00018;
DR  Pfam: PF07653;
DR  Pfam: PF14604;
DR  PROSITE: PS50004;
DR  PROSITE: PS00741;
DR  PROSITE: PS50010;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS50031;
DR  PROSITE: PS50003;
DR  PROSITE: PS50002;
DE  Function: Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery. Acts as guanine nucleotide exchange factor (GEF) for cdc42, and thereby stimulates actin nucleation mediated by wasl and the arp2/3 complex (By similarity). Involved in endocytosis of activated egfr, and probably also other growth factor receptors (By similarity). {ECO:0000250|UniProtKB:Q15811, ECO:0000250|UniProtKB:Q9Z0R4}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005905;
GO  GO:0005737;
GO  GO:0030027;
GO  GO:0043005;
GO  GO:0005635;
GO  GO:0055037;
GO  GO:0045202;
GO  GO:0005509;
GO  GO:0005085;
GO  GO:0006897;
GO  GO:0006887;
GO  GO:0035556;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQFGTPFGGNLDIWAITVEERAKHDQQFHGLKPTAGYITGDQARNFFLQSGLPQPVLAQIWALADMNNDGRMDQLEFSI
SQ  AMKLIKLKLQGYPLPSILPSNMLKQPVAMPAAAVAGFGMSGIVGIPPLAAVAPVPMPSIPVVGMSPPLVSSVPTVPPLSN
SQ  GAPAVIQSHPAFAHSATLPKSSSFGRSVAGSQINTKLQKAQSFDVPAPPLVVEWAVPSSSRLKYRQLFNSQDKTMSGNLT
SQ  GPQARTILMQSSLPQSQLATIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPILPPEYIPPSFRRVRSGSGLSIMS
SQ  SVSVDQRLPEEPEEEEPQNADKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQDQE
SQ  RKRQQDLEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNREQEDIVVLKAKKKTLEFEL
SQ  EALNDKKHQLEGKLQDIRCRLTTQRHEIESTNKSRELRIAEITHLQQQLQESQQLLGKMIPEKQSLNDQLKQVQQNSLHR
SQ  DSLLTLKRALETKEIGRQQLRDQLDEVEKETRAKLQEIDVFNNQLKELRELYNKQQFQKQQDFETEKIKQKELERKTSEL
SQ  DKLKEEDKRRMLEHDKLWQDRVKQEEERYKFQDEEKEKREESIQKCEVEKKPEIQEKPNKPFHQPPEPGKLGGQIPWMNT
SQ  EKAPLTINQGDVKVVYYRALYPFDARSHDEITIEPGDIIMVDESQTGEPGWLGGELKGKTGWFPANYAERMPESEFPSTT
SQ  KPAAETTAKPTVHVAPSPVAPAAFTNTSTNSNNWADFSSTWPTNNTDKVESDNWDTWAAQPSLTVPSAGQHRQRSAFTPA
SQ  TVTGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKNDVITVLEQQDMWWFGEVQGQKGWFPKSYVKLISGPLRKS
SQ  TSIDSTSSESPASLKRVSSPAFKPAIQGEEYISMYTYESNEQGDLTFQQGDLIVVIKKDGDWWTGTVGEKTGVFPSNYVR
SQ  PKDSEAAGSGGKTGSLGKKPEIAQVIASYAATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWFPANYVKLL
SQ  SPGTNKSTPTEPPKPTSLPPTCQVIGMYDYIAQNDDELAFSKGQVINVLNKEDPDWWKGELNGHVGLFPSNYVKLTTDMD
SQ  PSQQWCADLHLLDMLSPTERKRQGYIHELIVTEENYVSDLQLVTETFQKPLLESDLLTEKEVAMIFVNWKELIMCNIKLL
SQ  KALRVRKKMSGEKMPVKMIGDILTAQLPHMQPYIRFCSCQLNGAALIQQKTDEVPEFKEFVKRLAMDPRCKGMPLSSFLL
SQ  KPMQRVTRYPLIIKNIIENTPENHPDHSHLKQALEKAEELCSQVNEGVREKENSDRLEWIQGHVQCEGLSEQLVFNSVTN
SQ  CLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQIIKPLGSSGNDKVFSPKSNLQYKMYKTPIFLNEVLVKLPTDPSGD
SQ  EPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKREKAYLVRSQRATGIGRLMVNIVEGIELKPCRTHGK
SQ  SNPYCEITMGSQCHITKTIQDTLNPKWNSNCQFFIKDLEQDVLCITVFERDQFSPDDFLGRTEIRVADIKKDQGSKGPVT
SQ  KCLLLHEVPTGEIVVRLDLQLFDEP
//
ID  P40358;
PN  DnaJ-like chaperone JEM1;
GN  JEM1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9148890}; Single-pass type IV membrane protein {ECO:0000269|PubMed:9148890}. Nucleus membrane {ECO:0000269|PubMed:15282802}.
DR  UNIPROT: P40358;
DR  UNIPROT: D6VWB0;
DR  Pfam: PF00226;
DR  PROSITE: PS50076;
DE  Function: Acts as a DnaJ-like chaperone required for nuclear membrane fusion during mating. {ECO:0000269|PubMed:9148890}.
DE  Reference Proteome: Yes;
DE  Interaction: P32499; IntAct: EBI-3657516; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-3657508; Score: 0.35
DE  Interaction: P39685; IntAct: EBI-3657572; Score: 0.35
DE  Interaction: P39705; IntAct: EBI-3657524; Score: 0.35
DE  Interaction: P47069; IntAct: EBI-1560984; Score: 0.51
DE  Interaction: P80210; IntAct: EBI-3657180; Score: 0.35
DE  Interaction: P38009; IntAct: EBI-3657188; Score: 0.35
DE  Interaction: P53730; IntAct: EBI-3657196; Score: 0.35
DE  Interaction: P36000; IntAct: EBI-3657204; Score: 0.35
DE  Interaction: P38328; IntAct: EBI-3657212; Score: 0.35
DE  Interaction: Q12386; IntAct: EBI-3657220; Score: 0.35
DE  Interaction: P32447; IntAct: EBI-3657228; Score: 0.35
DE  Interaction: P43583; IntAct: EBI-3657244; Score: 0.35
DE  Interaction: P48361; IntAct: EBI-3657236; Score: 0.35
DE  Interaction: P14682; IntAct: EBI-3657252; Score: 0.35
DE  Interaction: P53622; IntAct: EBI-3657260; Score: 0.35
DE  Interaction: P53859; IntAct: EBI-3657268; Score: 0.35
DE  Interaction: Q03375; IntAct: EBI-3657276; Score: 0.35
DE  Interaction: P40487; IntAct: EBI-3657292; Score: 0.35
DE  Interaction: P32898; IntAct: EBI-3657284; Score: 0.35
DE  Interaction: P32461; IntAct: EBI-3657300; Score: 0.35
DE  Interaction: P40557; IntAct: EBI-3657308; Score: 0.35
DE  Interaction: P53743; IntAct: EBI-3657316; Score: 0.35
DE  Interaction: P53849; IntAct: EBI-3657332; Score: 0.35
DE  Interaction: P25569; IntAct: EBI-3657324; Score: 0.35
DE  Interaction: P20448; IntAct: EBI-3657340; Score: 0.35
DE  Interaction: P61830; IntAct: EBI-3657348; Score: 0.35
DE  Interaction: P00815; IntAct: EBI-3657356; Score: 0.35
DE  Interaction: P17629; IntAct: EBI-3657364; Score: 0.35
DE  Interaction: Q06706; IntAct: EBI-3657372; Score: 0.35
DE  Interaction: P50094; IntAct: EBI-3657380; Score: 0.35
DE  Interaction: P25642; IntAct: EBI-3657388; Score: 0.35
DE  Interaction: P40089; IntAct: EBI-3657404; Score: 0.35
DE  Interaction: P40070; IntAct: EBI-3657396; Score: 0.35
DE  Interaction: P35192; IntAct: EBI-3657412; Score: 0.35
DE  Interaction: Q12387; IntAct: EBI-3657420; Score: 0.35
DE  Interaction: P46151; IntAct: EBI-3657428; Score: 0.35
DE  Interaction: P33441; IntAct: EBI-3657436; Score: 0.35
DE  Interaction: P09440; IntAct: EBI-3657444; Score: 0.35
DE  Interaction: Q00539; IntAct: EBI-3657452; Score: 0.35
DE  Interaction: P12945; IntAct: EBI-3657460; Score: 0.35
DE  Interaction: Q07896; IntAct: EBI-3657468; Score: 0.35
DE  Interaction: P53742; IntAct: EBI-3657476; Score: 0.35
DE  Interaction: Q12499; IntAct: EBI-3657484; Score: 0.35
DE  Interaction: P53261; IntAct: EBI-3657492; Score: 0.35
DE  Interaction: Q01560; IntAct: EBI-3657500; Score: 0.35
DE  Interaction: P50874; IntAct: EBI-3657532; Score: 0.35
DE  Interaction: P32896; IntAct: EBI-3657540; Score: 0.35
DE  Interaction: P16861; IntAct: EBI-3657548; Score: 0.35
DE  Interaction: P16862; IntAct: EBI-3657556; Score: 0.35
DE  Interaction: P00560; IntAct: EBI-3657564; Score: 0.35
DE  Interaction: P32345; IntAct: EBI-3657580; Score: 0.35
DE  Interaction: P32263; IntAct: EBI-3657588; Score: 0.35
DE  Interaction: Q12417; IntAct: EBI-3657596; Score: 0.35
DE  Interaction: P40164; IntAct: EBI-3657604; Score: 0.35
DE  Interaction: P06777; IntAct: EBI-3657612; Score: 0.35
DE  Interaction: Q04231; IntAct: EBI-3657620; Score: 0.35
DE  Interaction: P12753; IntAct: EBI-3657628; Score: 0.35
DE  Interaction: P22336; IntAct: EBI-3657636; Score: 0.35
DE  Interaction: P26754; IntAct: EBI-3657644; Score: 0.35
DE  Interaction: P21524; IntAct: EBI-3657652; Score: 0.35
DE  Interaction: P27999; IntAct: EBI-3657660; Score: 0.35
DE  Interaction: P07703; IntAct: EBI-3657668; Score: 0.35
DE  Interaction: P17079; IntAct: EBI-3657676; Score: 0.35
DE  Interaction: P38764; IntAct: EBI-3657684; Score: 0.35
DE  Interaction: Q05022; IntAct: EBI-3657692; Score: 0.35
DE  Interaction: P40856; IntAct: EBI-3657700; Score: 0.35
DE  Interaction: Q12745; IntAct: EBI-3657708; Score: 0.35
DE  Interaction: Q03067; IntAct: EBI-3657716; Score: 0.35
DE  Interaction: P39000; IntAct: EBI-3657724; Score: 0.35
DE  Interaction: Q12460; IntAct: EBI-3657732; Score: 0.35
DE  Interaction: P17883; IntAct: EBI-3657740; Score: 0.35
DE  Interaction: P32908; IntAct: EBI-3657748; Score: 0.35
DE  Interaction: P43321; IntAct: EBI-3657756; Score: 0.35
DE  Interaction: P32558; IntAct: EBI-3657764; Score: 0.35
DE  Interaction: P32585; IntAct: EBI-3657772; Score: 0.35
DE  Interaction: P36008; IntAct: EBI-3657780; Score: 0.35
DE  Interaction: P43637; IntAct: EBI-3657788; Score: 0.35
DE  Interaction: P22515; IntAct: EBI-3657796; Score: 0.35
DE  Interaction: P39538; IntAct: EBI-3657804; Score: 0.35
DE  Interaction: P50101; IntAct: EBI-3657812; Score: 0.35
DE  Interaction: P54860; IntAct: EBI-3657820; Score: 0.35
DE  Interaction: P32861; IntAct: EBI-3657828; Score: 0.35
DE  Interaction: P39735; IntAct: EBI-3657836; Score: 0.35
DE  Interaction: Q12457; IntAct: EBI-3657844; Score: 0.35
DE  Interaction: P40521; IntAct: EBI-3657852; Score: 0.35
DE  Interaction: P40566; IntAct: EBI-3657864; Score: 0.35
DE  Interaction: P36076; IntAct: EBI-3657872; Score: 0.35
DE  Interaction: P38746; IntAct: EBI-3657880; Score: 0.35
DE  Interaction: Q07825; IntAct: EBI-3657888; Score: 0.35
DE  Interaction: Q08422; IntAct: EBI-3657896; Score: 0.35
DE  Interaction: Q12532; IntAct: EBI-3657904; Score: 0.35
DE  Interaction: P46951; IntAct: EBI-3657912; Score: 0.35
DE  Interaction: P53900; IntAct: EBI-3657920; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0051087;
GO  GO:0051787;
GO  GO:0051082;
GO  GO:0000742;
GO  GO:0034975;
GO  GO:0030433;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MILISGYCLLVYSVILPVLISASKLCDLAELQRLNKNLKVDTESLPKYQWIAGQLEQNCMTADPASENMSDVIQLANQIY
SQ  YKIGLIQLSNDQHLRAINTFEKIVFNETYKGSFGKLAEKRLQELYVDFGMWDKVHQKDDQYAKYLSLNETIRNKISSKDV
SQ  SVEEDISELLRITPYDVNVLSTHIDVLFHKLAEEIDVSLAAAIILDYETILDKHLASLSIDTRLSIHYVISVLQTFVLNS
SQ  DASFNIRKCLSIDMDYDKCKKLSLTISKLNKVNPSKRQILDPATYAFENKKFRSWDRIIEFYLKDKKPFITPMKILNKDT
SQ  NFKNNYFFLEEIIKQLIEDVQLSRPLAKNLFEDPPITDGFVKPKSYYHTDYLVYIDSILCQASSMSPDVKRAKLAAPFCK
SQ  KSLRHSLTLETWKHYQDAKSEQKPLPETVLSDVWNSNPHLLMYMVNSILNKSRSKPHSQFKKQLYDQINKFFQDNGLSES
SQ  TNPYVMKNFRLLQKQLQTYKEHKHRNFNQQYFQQQQQQQQHQRHQAPPAAPNYDPKKDYYKILGVSPSASSKEIRKAYLN
SQ  LTKKYHPDKIKANHNDKQESIHETMSQINEAYETLSDDDKRKEYDLSRSNPRRNTFPQGPRQNNMFKNPGSGFPFGNGFK
SQ  MNFGL
//
ID  Q9UQF2;
PN  C-Jun-amino-terminal kinase-interacting protein 1;
GN  MAPK8IP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane. Mitochondrion membrane. Note=Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreting cells, detected in both the cytoplasm and nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9UQF2;
DR  UNIPROT: D3DQP4;
DR  UNIPROT: O43407;
DR  PDB: 2G01;
DR  PDB: 2GMX;
DR  PDB: 2H96;
DR  PDB: 3OXI;
DR  PDB: 3PTG;
DR  PDB: 3VUD;
DR  PDB: 3VUG;
DR  PDB: 3VUH;
DR  PDB: 3VUI;
DR  PDB: 3VUK;
DR  PDB: 3VUL;
DR  PDB: 3VUM;
DR  PDB: 4E73;
DR  PDB: 4G1W;
DR  PDB: 4H39;
DR  PDB: 4HYS;
DR  PDB: 4HYU;
DR  PDB: 4IZY;
DR  PDB: 5LW1;
DR  PDB: 6FUZ;
DR  PDB: 7NYK;
DR  PDB: 7NYL;
DR  PDB: 7NYM;
DR  PDB: 7NYN;
DR  PDB: 7NYO;
DR  PDB: 7NZB;
DR  Pfam: PF00640;
DR  Pfam: PF14604;
DR  PROSITE: PS01179;
DR  PROSITE: PS50002;
DR  OMIM: 125853;
DR  OMIM: 604641;
DR  DisGeNET: 9479;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response. Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells. {ECO:0000250|UniProtKB:Q9WVI9}.
DE  Disease: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:10700186}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-7876199; Score: 0.44
DE  Interaction: P04626; IntAct: EBI-7873480; Score: 0.59
DE  Interaction: Q86Y07; IntAct: EBI-2122041; Score: 0.46
DE  Interaction: Q9ESN9; IntAct: EBI-7017807; Score: 0.40
DE  Interaction: Q9UPT6; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-78422; Score: 0.72
DE  Interaction: P12023; IntAct: EBI-286558; Score: 0.51
DE  Interaction: P05106; IntAct: EBI-8612295; Score: 0.44
DE  Interaction: O94762; IntAct: EBI-735599; Score: 0.00
DE  Interaction: Q8CD76; IntAct: EBI-7299159; Score: 0.40
DE  Interaction: P27824; IntAct: EBI-1779262; Score: 0.27
DE  Interaction: O43318; IntAct: EBI-2121802; Score: 0.72
DE  Interaction: P45983; IntAct: EBI-2121802; Score: 0.62
DE  Interaction: O14733; IntAct: EBI-2121802; Score: 0.62
DE  Interaction: Q15750; IntAct: EBI-2121802; Score: 0.35
DE  Interaction: Q9UQF2; IntAct: EBI-2122091; Score: 0.40
DE  Interaction: P20505; IntAct: EBI-8568176; Score: 0.40
DE  Interaction: Q9UK73; IntAct: EBI-21639159; Score: 0.35
DE  Interaction: Q7Z333; IntAct: EBI-21639159; Score: 0.35
DE  Interaction: Q14679; IntAct: EBI-21639159; Score: 0.35
DE  Interaction: Q13509; IntAct: EBI-21639159; Score: 0.35
DE  Interaction: Q13387; IntAct: EBI-21639159; Score: 0.35
DE  Interaction: Q01484; IntAct: EBI-21639159; Score: 0.35
DE  Interaction: P45984; IntAct: EBI-21639159; Score: 0.35
DE  Interaction: P31273; IntAct: EBI-21639159; Score: 0.35
DE  Interaction: Q12955; IntAct: EBI-21639159; Score: 0.35
DE  Interaction: Q96HI0; IntAct: EBI-21639159; Score: 0.35
DE  Interaction: P06241; IntAct: EBI-21392427; Score: 0.00
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0044302;
GO  GO:0005789;
GO  GO:0031966;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0019901;
GO  GO:0004860;
GO  GO:0007258;
GO  GO:2001243;
GO  GO:0043508;
GO  GO:0046330;
GO  GO:2000564;
GO  GO:0006355;
GO  GO:0046328;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAERESGGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGG
SQ  GGAGSRLQAEMLQMDLIDATGDTPGAEDDEEDDDEERAARRPGAGPPKAESGQEPASRGQGQSQGQSQGPGSGDTYRPKR
SQ  PTTLNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQSGPAPTTDRGTSTDSPCRRS
SQ  TATQMAPPGGPPAAPPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDAAEPTSAFLPPTESRMSVSSDPDPAAYPS
SQ  TAGRPHPSISEEEEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCF
SQ  GDYSDESDSATVYDNCASVSSPYESAIGEEYEEAPRPQPPACLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLF
SQ  SCIINGEEQEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKN
SQ  SDWVDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDSQEAKGNKCSHFFQ
SQ  LKNISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE
//
ID  Q9WVI9;
PN  C-Jun-amino-terminal kinase-interacting protein 1;
GN  Mapk8ip1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Mitochondrion membrane {ECO:0000250}. Note=Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreting cells, detected in both the cytoplasm and nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9WVI9;
DR  UNIPROT: O35145;
DR  UNIPROT: Q925J8;
DR  UNIPROT: Q9R1H9;
DR  UNIPROT: Q9R1Z1;
DR  UNIPROT: Q9WVI7;
DR  UNIPROT: Q9WVI8;
DR  PDB: 1UKH;
DR  PDB: 1UKI;
DR  PDB: 3O17;
DR  PDB: 3O2M;
DR  PDB: 3V3V;
DR  PDB: 6F5E;
DR  Pfam: PF00640;
DR  Pfam: PF14604;
DR  PROSITE: PS01179;
DR  PROSITE: PS50002;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and thus inhibiting the JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response (By similarity). Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells (PubMed:23963642). {ECO:0000250, ECO:0000269|PubMed:11562351, ECO:0000269|PubMed:23963642}.
DE  Reference Proteome: Yes;
DE  Interaction: Q86Y07; IntAct: EBI-2121669; Score: 0.54
DE  Interaction: Q60700; IntAct: EBI-7248484; Score: 0.40
DE  Interaction: P05067; IntAct: EBI-78735; Score: 0.40
DE  Interaction: P12023; IntAct: EBI-78826; Score: 0.62
DE  Interaction: P45983; IntAct: EBI-286507; Score: 0.50
DE  Interaction: P92208; IntAct: EBI-74543; Score: 0.40
DE  Interaction: P14599; IntAct: EBI-77506; Score: 0.40
DE  Interaction: A2ARV4; IntAct: EBI-300886; Score: 0.51
DE  Interaction: Q91ZX7; IntAct: EBI-300946; Score: 0.51
DE  Interaction: Q924X6; IntAct: EBI-300997; Score: 0.37
DE  Interaction: Q62073; IntAct: EBI-1778409; Score: 0.50
DE  Interaction: Q8CF89; IntAct: EBI-1778466; Score: 0.35
DE  Interaction: Q923A8; IntAct: EBI-1778490; Score: 0.35
DE  Interaction: Q15750; IntAct: EBI-2120694; Score: 0.35
DE  Interaction: Q9JI18; IntAct: EBI-8521435; Score: 0.51
DE  Interaction: Q8VI56; IntAct: EBI-8521772; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-6530145; Score: 0.40
DE  Interaction: O88704; IntAct: EBI-16730213; Score: 0.35
GO  GO:0030424;
GO  GO:0044295;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0044294;
GO  GO:0044302;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0031966;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0042802;
GO  GO:0008432;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0031434;
GO  GO:0031435;
GO  GO:0019901;
GO  GO:0007258;
GO  GO:0043066;
GO  GO:2001243;
GO  GO:0046329;
GO  GO:0043508;
GO  GO:0046330;
GO  GO:2000564;
GO  GO:0006355;
GO  GO:0046328;
GO  GO:0007165;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAERESGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGSS
SQ  GSAGSRLQAEMLQMDLIDAAGDTPGAEDDEEEEDDELAAQRPGVGPPKAESNQDPAPRSQGQGPGTGSGDTYRPKRPTTL
SQ  NLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQGSPVPTQDRGTSTDSPCRRSAATQ
SQ  MAPPSGPPATAPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDPAEPTSTFMPPTESRMSVSSDPDPAAYSVTAGR
SQ  PHPSISEEDEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDYS
SQ  DESDSATVYDNCASASSPYESAIGEEYEEAPQPRPPTCLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLFSCVI
SQ  NGEEHEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKNSDWI
SQ  DQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDALEAKGNKCSHFFQLKNI
SQ  SFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE
//
ID  Q9R237;
PN  C-Jun-amino-terminal kinase-interacting protein 1;
GN  Mapk8ip1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus. Endoplasmic reticulum membrane {ECO:0000250}. Mitochondrion membrane {ECO:0000250}. Note=Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreting cells, detected in both the cytoplasm and nucleus.
DR  UNIPROT: Q9R237;
DR  UNIPROT: B0VXR5;
DR  UNIPROT: O88979;
DR  UNIPROT: Q9R1H8;
DR  UNIPROT: Q9WVI5;
DR  UNIPROT: Q9WVI6;
DR  PDB: 2FPD;
DR  PDB: 2FPE;
DR  PDB: 2FPF;
DR  Pfam: PF00640;
DR  Pfam: PF14604;
DR  PROSITE: PS01179;
DR  PROSITE: PS50002;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and thus inhibiting the JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response. Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells. {ECO:0000250|UniProtKB:Q9WVI9, ECO:0000269|PubMed:21076496}.
DE  Reference Proteome: Yes;
DE  Interaction: P49185; IntAct: EBI-7936738; Score: 0.40
DE  Interaction: P47196; IntAct: EBI-7936797; Score: 0.40
DE  Interaction: Q9R237; IntAct: EBI-8051903; Score: 0.67
DE  Interaction: G3V9M2; IntAct: EBI-8052000; Score: 0.40
DE  Interaction: Q16584; IntAct: EBI-8052429; Score: 0.40
DE  Interaction: P45983; IntAct: EBI-8052446; Score: 0.40
DE  Interaction: O14733; IntAct: EBI-8052475; Score: 0.40
GO  GO:0030424;
GO  GO:0044295;
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0044294;
GO  GO:0044302;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0031966;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0042802;
GO  GO:0008432;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0031434;
GO  GO:0031435;
GO  GO:0019901;
GO  GO:0007258;
GO  GO:0043066;
GO  GO:2001243;
GO  GO:0046329;
GO  GO:0043508;
GO  GO:0046330;
GO  GO:2000564;
GO  GO:0006355;
GO  GO:0046328;
GO  GO:0007165;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAERESGLSGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGSS
SQ  GSAGSRLQAEMLQMDLIDAASDTPGAEDDEEDDDELAAQRPGVGPSKAESGQEPASRSQGQGQGPGTGSGDTYRPKRPTT
SQ  LNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQGSPVPTQDRGTSTDSPCRRTAAT
SQ  QMAPPSGPPATAPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDPAEPTSTFLPPTESRMSVSSDPDPAAYSVTAG
SQ  RPHPSISEEDEGFDCLSSPEQAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDY
SQ  SDESDSATVYDNCASASSPYESAIGEEYEEAPQPRPPTCLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLFSCV
SQ  INGEEHEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKNSDW
SQ  IDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADEAQEAKGNKCSHFFQLKN
SQ  ISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE
//
ID  Q9UPT6;
PN  C-Jun-amino-terminal kinase-interacting protein 3;
GN  MAPK8IP3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9ESN9}. Golgi apparatus {ECO:0000250|UniProtKB:Q9ESN9}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9ESN9}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9ESN9}. Cell projection, axon {ECO:0000250|UniProtKB:E9PSK7}. Cell projection, dendrite {ECO:0000250|UniProtKB:E9PSK7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:E9PSK7}. Note=Localized in the soma and growth cones of differentiated neurites and the Golgi and vesicles of the early secretory compartment of epithelial cells. KIF5A/B/C-mediated transportation to axon tips is essential for its function in enhancing neuronal axon elongation. {ECO:0000250|UniProtKB:E9PSK7, ECO:0000250|UniProtKB:Q9ESN9}.
DR  UNIPROT: Q9UPT6;
DR  UNIPROT: A2A2B3;
DR  UNIPROT: A7E2B3;
DR  UNIPROT: Q96RY4;
DR  UNIPROT: Q9H4I4;
DR  UNIPROT: Q9H7P1;
DR  UNIPROT: Q9NUG0;
DR  PDB: 4PXJ;
DR  Pfam: PF16471;
DR  Pfam: PF09744;
DR  PROSITE: PS51776;
DR  PROSITE: PS51777;
DR  OMIM: 605431;
DR  OMIM: 618443;
DR  DisGeNET: 23162;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module (PubMed:12189133). May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development (By similarity). Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation (PubMed:21775604). {ECO:0000250|UniProtKB:Q9ESN9, ECO:0000269|PubMed:12189133, ECO:0000269|PubMed:21775604}.
DE  Disease: Neurodevelopmental disorder with or without variable brain abnormalities (NEDBA) [MIM:618443]: A disorder characterized by global developmental delay, impaired intellectual development, delayed walking, poor or absent speech, and variable brain anomalies including perisylvian polymicrogyria, cerebral or cerebellar atrophy, and hypoplasia of the corpus callosum. {ECO:0000269|PubMed:30612693, ECO:0000269|PubMed:30945334}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O60271; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: O95271; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: P61026; IntAct: EBI-25437687; Score: 0.40
DE  Interaction: Q06609; IntAct: EBI-9064650; Score: 0.37
DE  Interaction: P49703; IntAct: EBI-733846; Score: 0.00
DE  Interaction: Q9NPQ8; IntAct: EBI-735046; Score: 0.00
DE  Interaction: P41182; IntAct: EBI-765648; Score: 0.35
DE  Interaction: Q5SW96; IntAct: EBI-11773591; Score: 0.72
DE  Interaction: O75771; IntAct: EBI-24283411; Score: 0.56
DE  Interaction: Q9BR01; IntAct: EBI-24292821; Score: 0.56
DE  Interaction: Q86XF7; IntAct: EBI-24446837; Score: 0.56
DE  Interaction: Q07866; IntAct: EBI-24450497; Score: 0.56
DE  Interaction: Q9UQF2; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: Q9UJW0; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: Q9NZ32; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: Q9H977; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: Q9H2K2; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: Q13387; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: O00399; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: A6NED2; IntAct: EBI-21716445; Score: 0.35
DE  Interaction: Q147U7; IntAct: EBI-21768421; Score: 0.35
DE  Interaction: P61006; IntAct: EBI-25436861; Score: 0.40
DE  Interaction: P51114; IntAct: EBI-26510762; Score: 0.37
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0030425;
GO  GO:0000139;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0008432;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0030159;
GO  GO:0099641;
GO  GO:0061564;
GO  GO:0031103;
GO  GO:0043066;
GO  GO:0046330;
GO  GO:0050821;
GO  GO:0046328;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVEL
SQ  ELLREDNEQLLTQYEREKALRRQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKE
SQ  YNALHQRHTEMIQTYVEHIERSKMQQVGGNSQTESSLPGRRKERPTSLNVFPLADGTVRAQIGGKLVPAGDHWHLSDLGQ
SQ  LQSSSSYQCPQDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGVGSKNSKRAREKRDSRNMEVQ
SQ  VTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDMCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEG
SQ  ADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELE
SQ  EELKRVKSEAIIARREPKEEAEDVSSYLCTESDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE
SQ  HPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRPYPSVNIHYKSPTTAGFSQRRNHAMCPISAGSRPLEFFPDDDCTSSARR
SQ  EQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPTMKLWCAAGVNLSGWRP
SQ  NEDDAGNGVKPAPGRDPLTCDREGDGEPKSAHTSPEKKKAKELPEMDATSSRVWILTSTLTTSKVVIIDANQPGTVVDQF
SQ  TVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDPGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGEVAT
SQ  IANGKVNPSQSTEEATEATEVPDPGPSEPETATLRPGPLTEHVFTDPAPTPSSGPQPGSENGPEPDSSSTRPEPEPSGDP
SQ  TGAGSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQWDLSNYHLM
SQ  DLGHPHHSIRCMAVVYDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLRLYHAHTHQ
SQ  HLQDVDIEPYVSKMLGTGKLGFSFVRITALLVAGSRLWVGTGNGVVISIPLTETVVLHRGQLLGLRANKTSPTSGEGARP
SQ  GGIIHVYGDDSSDRAASSFIPYCSMAQAQLCFHGHRDAVKFFVSVPGNVLATLNGSVLDSPAEGPGPAAPASEVEGQKLR
SQ  NVLVLSGGEGYIDFRIGDGEDDETEEGAGDMSQVKPVLSKAERSHIIVWQVSYTPE
//
ID  Q9ESN9;
PN  C-Jun-amino-terminal kinase-interacting protein 3;
GN  Mapk8ip3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10629060}. Golgi apparatus {ECO:0000269|PubMed:11106729}. Cytoplasmic vesicle {ECO:0000269|PubMed:11106729}. Cell projection, growth cone {ECO:0000269|PubMed:10629060}. Cell projection, axon {ECO:0000269|PubMed:25944905}. Cell projection, dendrite {ECO:0000250|UniProtKB:E9PSK7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:E9PSK7}. Note=Localized in the soma and growth cones of differentiated neurites and the Golgi and vesicles of the early secretory compartment of epithelial cells (PubMed:10629060, PubMed:11106729). KIF5A/B/C-mediated transportation to axon tips is essential for its function in enhancing neuronal axon elongation (By similarity). {ECO:0000250|UniProtKB:E9PSK7, ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:11106729}.
DR  UNIPROT: Q9ESN9;
DR  UNIPROT: Q5D062;
DR  UNIPROT: Q99KU7;
DR  UNIPROT: Q9EQD8;
DR  UNIPROT: Q9ESN7;
DR  UNIPROT: Q9ESN8;
DR  UNIPROT: Q9ESP0;
DR  UNIPROT: Q9JLH2;
DR  UNIPROT: Q9JLH3;
DR  UNIPROT: Q9R0U7;
DR  PDB: 6EJN;
DR  Pfam: PF16471;
DR  Pfam: PF09744;
DR  PROSITE: PS51776;
DR  PROSITE: PS51777;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (PubMed:10523642, PubMed:10629060). Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner (PubMed:23576431, PubMed:25944905, PubMed:28259553). Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation (PubMed:23576431, PubMed:25944905, PubMed:28259553). Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration (PubMed:23576431, PubMed:25944905, PubMed:28259553). Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development (PubMed:23576431, PubMed:25944905, PubMed:28259553). Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation (PubMed:23576431, PubMed:25944905, PubMed:28259553). {ECO:0000269|PubMed:10523642, ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:23576431, ECO:0000269|PubMed:25944905, ECO:0000269|PubMed:28259553}.
DE  Reference Proteome: Yes;
DE  Interaction: O88448; IntAct: EBI-297849; Score: 0.68
DE  Interaction: O88447; IntAct: EBI-297849; Score: 0.72
DE  Interaction: P63101; IntAct: EBI-2255635; Score: 0.35
DE  Interaction: P62331; IntAct: EBI-7986308; Score: 0.60
DE  Interaction: P28738; IntAct: EBI-7017356; Score: 0.59
DE  Interaction: Q9ESN9; IntAct: EBI-7017786; Score: 0.40
DE  Interaction: Q9ERE9; IntAct: EBI-7017828; Score: 0.40
DE  Interaction: Q9UQF2; IntAct: EBI-7017807; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-6530187; Score: 0.40
DE  Interaction: Q61831; IntAct: EBI-9549479; Score: 0.54
DE  Interaction: Q9WTU6; IntAct: EBI-9549854; Score: 0.40
DE  Interaction: Q91Y86; IntAct: EBI-9549815; Score: 0.40
DE  Interaction: P47809; IntAct: EBI-9549947; Score: 0.50
DE  Interaction: P31938; IntAct: EBI-9550942; Score: 0.50
DE  Interaction: P53349; IntAct: EBI-9550988; Score: 0.50
DE  Interaction: P04049; IntAct: EBI-9637077; Score: 0.50
DE  Interaction: O88704; IntAct: EBI-16730213; Score: 0.35
DE  Interaction: Q80VP2; IntAct: EBI-21018622; Score: 0.35
DE  Interaction: P16056; IntAct: EBI-27118288; Score: 0.35
GO  GO:0030673;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0030425;
GO  GO:0000139;
GO  GO:0030426;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005790;
GO  GO:0008432;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0031434;
GO  GO:0031435;
GO  GO:0030159;
GO  GO:0099641;
GO  GO:0061564;
GO  GO:0007411;
GO  GO:0031103;
GO  GO:0030900;
GO  GO:0001701;
GO  GO:0007254;
GO  GO:0048286;
GO  GO:0060425;
GO  GO:0043066;
GO  GO:0046330;
GO  GO:0043507;
GO  GO:0045666;
GO  GO:2001224;
GO  GO:0009791;
GO  GO:0008104;
GO  GO:0050821;
GO  GO:0010468;
GO  GO:0046328;
GO  GO:0007585;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVEL
SQ  ELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKE
SQ  YNALHQRHTEMIQTYVEHIERSKMQQVGGSGQTESSLPGRSRKERPTSLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLG
SQ  QLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYVSVTKNNKQAREKRNSRNMEV
SQ  QVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLERTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDE
SQ  GADLLGEFSVRDDFFGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKEL
SQ  EEELKRVKSEAVTARREPREEVEDVSSYLCTELDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASR
SQ  EHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTAAGFSQRRSHALCQISAGSRPLEFFPDDDCTSSAR
SQ  REQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWK
SQ  PHEEDSSNGPKPVPGRDPLTCDREGEGEPKSTHPSPEKKKAKETPEADATSSRVWILTSTLTTSKVVIIDANQPGTIVDQ
SQ  FTVCNAHVLCISSIPAASDSDYPPGEMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVA
SQ  TTANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTPSSSTQPASENGSESNGTIVQPQVEPSGE
SQ  LSTTTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQWDLSNYHL
SQ  MDLGHPHHSIRCMAVVNDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLRLYHAHTH
SQ  QHLQDVDIEPYVSKMLGTGKLGFSFVRITALLIAGNRLWVGTGNGVVISIPLTETVVLHRGQLLGLRANKTSPTSGEGTR
SQ  PGGIIHVYGDDSSDKAASSFIPYCSMAQAQLCFHGHRDAVKFFVSVPGNVLATLNGSVLDSPSEGPGPAAPAADAEGQKL
SQ  KNALVLSGGEGYIDFRIGDGEDDETEECAGDVNQTKPSLSKAERSHIIVWQVSYTPE
//
ID  E9PSK7;
PN  C-Jun-amino-terminal kinase-interacting protein 3;
GN  Mapk8ip3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9ESN9}. Golgi apparatus {ECO:0000250|UniProtKB:Q9ESN9}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9ESN9}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9ESN9}. Cell projection, axon {ECO:0000269|PubMed:21775604, ECO:0000269|PubMed:23576431}. Cell projection, dendrite {ECO:0000269|PubMed:21775604}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21775604}. Note=Localized in the soma and growth cones of differentiated neurites and the Golgi and vesicles of the early secretory compartment of epithelial cells. KIF5A/B/C-mediated transportation to axon tips is essential for its function in enhancing neuronal axon elongation. {ECO:0000250|UniProtKB:Q9ESN9, ECO:0000269|PubMed:23576431}.
DR  UNIPROT: E9PSK7;
DR  UNIPROT: B0VXR4;
DR  Pfam: PF16471;
DR  Pfam: PF09744;
DR  PROSITE: PS51776;
DR  PROSITE: PS51777;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development. Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation. {ECO:0000250|UniProtKB:Q9ESN9, ECO:0000269|PubMed:21076496, ECO:0000269|PubMed:21775604, ECO:0000269|PubMed:23576431, ECO:0000269|PubMed:25944905}.
DE  Reference Proteome: Yes;
GO  GO:0030673;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0030425;
GO  GO:0000139;
GO  GO:0030426;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005790;
GO  GO:0008432;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0031434;
GO  GO:0031435;
GO  GO:0030159;
GO  GO:0099641;
GO  GO:0061564;
GO  GO:0007411;
GO  GO:0031103;
GO  GO:0030900;
GO  GO:0001701;
GO  GO:0007254;
GO  GO:0048286;
GO  GO:0060425;
GO  GO:0043066;
GO  GO:0031175;
GO  GO:0046330;
GO  GO:0043507;
GO  GO:0045666;
GO  GO:2001224;
GO  GO:0009791;
GO  GO:0008104;
GO  GO:0050821;
GO  GO:0010468;
GO  GO:0046328;
GO  GO:0007585;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVEL
SQ  ELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKE
SQ  YNALHQRHTEMIQTYVEHIERSKMQQVGGGGQTESSLPGRSRKERPTSLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLG
SQ  QLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGSVTKNNKRAREKRNSRNMEV
SQ  QVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDE
SQ  GADLLGEFSGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKR
SQ  VKSEAVTARREPREEVEDDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQ
SQ  FFSRLFSSSSSPPPAKRSYPSVNIHYKSPTTAGFSQRRNHALCQISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHV
SQ  RNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWKPNEEDSSNGPKPAPG
SQ  RDPLTCDREGEGEPKSTHPSPEKKKAKEVPEADATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIP
SQ  AASDSDYPPGDMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVAATANGKVNPSQSTEE
SQ  ATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTQSSSTQPASENGSESDGSIVQPQVEPSGESSATTSSAAPTMWLG
SQ  AQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQWDLSNYHLMDLGHPHHSIRCMAV
SQ  VDDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLRLYHAHTHQHLQDVDIEPYVSKM
SQ  LGTGKLGFSFVRITALLIAGNRLWVGTGNGVVISIPLTETVVLHRGQLLGLRANKTSPTSGEGTRPGGIIHVYGDDSSDK
SQ  TASSFIPYCSMAQAQLCFHGHRDAVKFFVSVPGNVLATLNGSVLDSPSEGPGPAAPAADAEGQKLKNALVLSGGEGYIDF
SQ  RIGDGEDDETEEGTGDVNQTKPSLSKAERSHIIVWQVSYTPE
//
ID  O60271;
PN  C-Jun-amino-terminal kinase-interacting protein 4;
GN  SPAG9;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q58A65}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q58A65}. Lysosome membrane {ECO:0000269|PubMed:29146937}. Note=Perinuclear distribution in response to stress signals such as UV radiation. {ECO:0000250|UniProtKB:Q58A65}. [Isoform 5]: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15693750}. Note=Associated with the plasma membrane of the acrosomal compartment and also localizes in the acrosome matrix. {ECO:0000269|PubMed:15693750}.
DR  UNIPROT: O60271;
DR  UNIPROT: A6H8U5;
DR  UNIPROT: A8MSX0;
DR  UNIPROT: B4DHH2;
DR  UNIPROT: O60905;
DR  UNIPROT: Q3KQU8;
DR  UNIPROT: Q3MKM7;
DR  UNIPROT: Q86WC7;
DR  UNIPROT: Q86WC8;
DR  UNIPROT: Q8IZX7;
DR  UNIPROT: Q96II0;
DR  UNIPROT: Q9H811;
DR  PDB: 2W83;
DR  Pfam: PF16471;
DR  Pfam: PF09744;
DR  PROSITE: PS51776;
DR  PROSITE: PS51777;
DR  OMIM: 605430;
DR  DisGeNET: 9043;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module (PubMed:14743216). Regulates lysosomal positioning by acting as an adapter protein which links PIP4P1-positive lysosomes to the dynein- dynactin complex (PubMed:29146937). Assists PIKFYVE selective functionality in microtubule-based endosome-to-TGN trafficking (By similarity). {ECO:0000250|UniProtKB:Q58A65, ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:29146937}.
DE  Reference Proteome: Yes;
DE  Interaction: P19838; IntAct: EBI-353534; Score: 0.69
DE  Interaction: O88447; IntAct: EBI-7681059; Score: 0.27
DE  Interaction: Q14240; IntAct: EBI-1068469; Score: 0.00
DE  Interaction: P53350; IntAct: EBI-2372594; Score: 0.73
DE  Interaction: Q07832; IntAct: EBI-2560950; Score: 0.40
DE  Interaction: Q8ZED8; IntAct: EBI-2866304; Score: 0.00
DE  Interaction: P62330; IntAct: EBI-7140974; Score: 0.62
DE  Interaction: O60271; IntAct: EBI-7141074; Score: 0.44
DE  Interaction: P84077; IntAct: EBI-7141242; Score: 0.44
DE  Interaction: Q9HC52; IntAct: EBI-3951861; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-7190550; Score: 0.37
DE  Interaction: Q9NPJ4; IntAct: EBI-7316035; Score: 0.37
DE  Interaction: P62331; IntAct: EBI-7832567; Score: 0.40
DE  Interaction: Q96A65; IntAct: EBI-9817790; Score: 0.56
DE  Interaction: P23771; IntAct: EBI-10891010; Score: 0.35
DE  Interaction: A3KN83; IntAct: EBI-11898766; Score: 0.00
DE  Interaction: Q9UQ88; IntAct: EBI-11901851; Score: 0.00
DE  Interaction: Q9UKN8; IntAct: EBI-11901842; Score: 0.00
DE  Interaction: Q9UBC2; IntAct: EBI-11901833; Score: 0.00
DE  Interaction: Q8WUA4; IntAct: EBI-11901824; Score: 0.00
DE  Interaction: P11274; IntAct: EBI-11901815; Score: 0.00
DE  Interaction: P30291; IntAct: EBI-11907279; Score: 0.00
DE  Interaction: P33991; IntAct: EBI-11907576; Score: 0.00
DE  Interaction: P33993; IntAct: EBI-11907675; Score: 0.00
DE  Interaction: P49736; IntAct: EBI-11908484; Score: 0.00
DE  Interaction: Q00613; IntAct: EBI-11911387; Score: 0.00
DE  Interaction: Q06945; IntAct: EBI-11911777; Score: 0.00
DE  Interaction: Q12955; IntAct: EBI-11912325; Score: 0.00
DE  Interaction: Q14566; IntAct: EBI-11913337; Score: 0.00
DE  Interaction: Q14C86; IntAct: EBI-11913870; Score: 0.00
DE  Interaction: Q14683; IntAct: EBI-11913616; Score: 0.00
DE  Interaction: Q6IN85; IntAct: EBI-11917442; Score: 0.00
DE  Interaction: Q96BY7; IntAct: EBI-11926258; Score: 0.00
DE  Interaction: Q9NY27; IntAct: EBI-11934518; Score: 0.00
DE  Interaction: Q9P260; IntAct: EBI-11935551; Score: 0.00
DE  Interaction: Q9UQE7; IntAct: EBI-11939891; Score: 0.00
DE  Interaction: Q9Y4E8; IntAct: EBI-11941617; Score: 0.00
DE  Interaction: Q9Y6Y0; IntAct: EBI-11942633; Score: 0.00
DE  Interaction: Q8TBP5; IntAct: EBI-21502646; Score: 0.35
DE  Interaction: Q8N6T3; IntAct: EBI-21541414; Score: 0.35
DE  Interaction: Q9UF02; IntAct: EBI-21554221; Score: 0.35
DE  Interaction: Q86VU5; IntAct: EBI-21596714; Score: 0.35
DE  Interaction: Q6EMK4; IntAct: EBI-21651359; Score: 0.35
DE  Interaction: P08247; IntAct: EBI-21652717; Score: 0.35
DE  Interaction: Q2TBA0; IntAct: EBI-21658220; Score: 0.35
DE  Interaction: Q96MC5; IntAct: EBI-21663233; Score: 0.35
DE  Interaction: Q9UPT6; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: O96006; IntAct: EBI-21692488; Score: 0.35
DE  Interaction: A6NED2; IntAct: EBI-21716445; Score: 0.35
DE  Interaction: P31350; IntAct: EBI-21732275; Score: 0.35
DE  Interaction: Q7LG56; IntAct: EBI-21732528; Score: 0.35
DE  Interaction: Q8WYK0; IntAct: EBI-21732608; Score: 0.35
DE  Interaction: O00592; IntAct: EBI-21750748; Score: 0.35
DE  Interaction: Q96CA5; IntAct: EBI-21754959; Score: 0.35
DE  Interaction: O14863; IntAct: EBI-21768088; Score: 0.35
DE  Interaction: O95159; IntAct: EBI-21768155; Score: 0.35
DE  Interaction: P06753; IntAct: EBI-21768209; Score: 0.35
DE  Interaction: P09493; IntAct: EBI-21768262; Score: 0.35
DE  Interaction: P16150; IntAct: EBI-21768371; Score: 0.35
DE  Interaction: Q14108; IntAct: EBI-21768396; Score: 0.35
DE  Interaction: Q147U7; IntAct: EBI-21768421; Score: 0.35
DE  Interaction: Q2T9K0; IntAct: EBI-21768445; Score: 0.35
DE  Interaction: Q5XKK7; IntAct: EBI-21768464; Score: 0.35
DE  Interaction: Q8N565; IntAct: EBI-21768514; Score: 0.35
DE  Interaction: Q96L93; IntAct: EBI-21768545; Score: 0.35
DE  Interaction: Q9BWT6; IntAct: EBI-21768576; Score: 0.35
DE  Interaction: Q9NWA0; IntAct: EBI-21768607; Score: 0.35
DE  Interaction: Q9NPJ6; IntAct: EBI-25472202; Score: 0.27
DE  Interaction: P61006; IntAct: EBI-21006330; Score: 0.62
DE  Interaction: Q5NFC5; IntAct: EBI-22299450; Score: 0.37
DE  Interaction: Q5NES6; IntAct: EBI-22299440; Score: 0.37
DE  Interaction: P61026; IntAct: EBI-25436875; Score: 0.40
DE  Interaction: H9EJ66; IntAct: EBI-25685143; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25686340; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: P22612; IntAct: EBI-28934688; Score: 0.35
DE  Interaction: P36507; IntAct: EBI-28935019; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-28935882; Score: 0.35
DE  Interaction: Q8TDX7; IntAct: EBI-28943744; Score: 0.35
DE  Interaction: Q92918; IntAct: EBI-28944233; Score: 0.35
DE  Interaction: Q96QS6; IntAct: EBI-28944559; Score: 0.35
DE  Interaction: Q99502; IntAct: EBI-27113432; Score: 0.35
DE  Interaction: O15297; IntAct: EBI-27113880; Score: 0.35
DE  Interaction: O14830; IntAct: EBI-27113806; Score: 0.35
DE  Interaction: Q8N3J5; IntAct: EBI-27114011; Score: 0.35
DE  Interaction: P56180; IntAct: EBI-27115406; Score: 0.35
GO  GO:0001669;
GO  GO:0034451;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005765;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0008432;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0030159;
GO  GO:0032418;
GO  GO:1903860;
GO  GO:0045665;
GO  GO:0001933;
GO  GO:0030335;
GO  GO:0045666;
GO  GO:0042147;
GO  GO:0051146;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRD
SQ  DNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALH
SQ  QRHTEMIHNYMEHLERTKLHQLSGSDQLESTAHSRIRKERPISLGIFPLPAGDGLLTPDAQKGGETPGSEQWKFQELSQP
SQ  RSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIPTDTPLKEENEGFVKVTDAPNKSEISKHIEVQ
SQ  VAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGDVDEG
SQ  ADLLGMGREVENLILENTQLLETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEEKNRELEEELRKARAEA
SQ  EDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLF
SQ  SSSSNTTKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKAFDFLSEETEASLASRREQKREQYRQVKAHVQKED
SQ  GRVQAFGWSLPQKYKQVTNGQGENKMKNLPVPVYLRPLDEKDTSMKLWCAVGVNLSGGKTRDGGSVVGASVFYKDVAGLD
SQ  TEGSKQRSASQSSLDKLDQELKEQQKELKNQEELSSLVWICTSTHSATKVLIIDAVQPGNILDSFTVCNSHVLCIASVPG
SQ  ARETDYPAGEDLSESGQVDKASLCGSMTSNSSAETDSLLGGITVVGCSAEGVTGAATSPSTNGASPVMDKPPEMEAENSE
SQ  VDENVPTAEEATEATEGNAGSAEDTVDISQTGVYTEHVFTDPLGVQIPEDLSPVYQSSNDSDAYKDQISVLPNEQDLVRE
SQ  EAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCLHSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDGQWDLSNYHL
SQ  LDLGRPHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDSTLRLYHAHTY
SQ  QHLQDVDIEPYVSKMLGTGKLGFSFVRITALMVSCNRLWVGTGNGVIISIPLTETNKTSGVPGNRPGSVIRVYGDENSDK
SQ  VTPGTFIPYCSMAHAQLCFHGHRDAVKFFVAVPGQVISPQSSSSGTDLTGDKAGPSAQEPGSQTPLKSMLVISGGEGYID
SQ  FRMGDEGGESELLGEDLPLEPSVTKAERSHLIVWQVMYGNE
//
ID  Q58A65;
PN  C-Jun-amino-terminal kinase-interacting protein 4;
GN  Spag9;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:15767678, ECO:0000269|PubMed:19056739}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:19056739}. Lysosome membrane {ECO:0000250|UniProtKB:O60271}. Note=Perinuclear distribution in response to stress signals such as UV radiation. {ECO:0000269|PubMed:12391307}.
DR  UNIPROT: Q58A65;
DR  UNIPROT: Q3UH77;
DR  UNIPROT: Q3UHF0;
DR  UNIPROT: Q58VQ4;
DR  UNIPROT: Q5NC70;
DR  UNIPROT: Q5NC78;
DR  UNIPROT: Q6A057;
DR  UNIPROT: Q6PAS3;
DR  UNIPROT: Q8CJC2;
DR  Pfam: PF16471;
DR  Pfam: PF09744;
DR  PROSITE: PS51776;
DR  PROSITE: PS51777;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module (PubMed:12391307, PubMed:15767678). Regulates lysosomal positioning by acting as an adapter protein which links PIP4P1-positive lysosomes to the dynein-dynactin complex (By similarity). Assists PIKFYVE selective functionality in microtubule-based endosome-to-TGN trafficking (PubMed:19056739). {ECO:0000250|UniProtKB:O60271, ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:15767678, ECO:0000269|PubMed:19056739}.
DE  Reference Proteome: Yes;
DE  Interaction: O88447; IntAct: EBI-7681081; Score: 0.58
DE  Interaction: P62331; IntAct: EBI-7986227; Score: 0.60
DE  Interaction: Q5S007; IntAct: EBI-6530261; Score: 0.40
GO  GO:0034451;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005765;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0008432;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0030159;
GO  GO:0032418;
GO  GO:1903860;
GO  GO:0045665;
GO  GO:0001933;
GO  GO:0030335;
GO  GO:0043410;
GO  GO:0045666;
GO  GO:0042147;
GO  GO:0051146;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRD
SQ  DNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALH
SQ  QRHTEMIHNYMEHLERTKLHQLSGSDQLEATAHSRIRKERPISLGIFPLPAGDGLLTPDTQKGGETPGSEQWKFQELSQP
SQ  RSHTSLKVSHSPEPPKAVEQEDELSDISQGGSKATTPASTANSDVSAIPPDTPSKEDNEGFVKGTDTSNKSEISKHIEVQ
SQ  VAQETRNVSTESGENEEKSEVQAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGDVDEG
SQ  ADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEA
SQ  EDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLF
SQ  SSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKAFDFLSEETEASLASRREQKREQYRQVKAHVQKED
SQ  GRVQAFGWSLPQKYKQVANGQGETKMKNLPVPVYLRPLDEKDASMKLWCAVGVNLSGGKTRDGGSVVGASVFYKDIAGLD
SQ  TEGSKQRSASQSSLDKLDQELKEQQKEFKNQEELSSQVWICTSTHSTTKVIIIDAVQPGNILDSFTVCNSHVLCIASVPG
SQ  ARETDYPAGEELSESGQVDKASLCGSMTSNSSAEMDSLLGGITVVGCSTEGLTGAATSPSTNGASPVIEKPPEMETENSE
SQ  VDENIPTAEEATEATEGNAGSTEDTVDISQPGVYTEHVFTDPLGVQIPEDLSPVFQSSNDSDVYKDQISVLPNEQDLARE
SQ  EAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCLHSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDGQWDLSNYHL
SQ  LDLGRPHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDSTLRLYHAHTY
SQ  QHLQDVDIEPYVSKMLGTGKLGFSFVRITALMVSCNRLWVGTGNGVIISIPLTETNKTSGTPGNRPGSVIRVYGDENSDK
SQ  VTPGTFIPYCSMAHAQLCFHGHRDAVKFFVAVPGQVISPQSSSGGADLTADKAGSSAQEPSSQTPLKSMLVISGGEGYID
SQ  FRMGDEGGESELLGEDLPLEPSVTKAERSHLIVWQVMCGNE
//
ID  P34609;
PN  JNK-interacting protein;
GN  unc;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10393177, ECO:0000269|PubMed:11738026}. Note=Diffusely localized throughout cell body but intensely localized in regions adjacent to nucleus and at presumptive tips of neural processes.
DR  UNIPROT: P34609;
DR  UNIPROT: A7LPE3;
DR  UNIPROT: A7LPE4;
DR  UNIPROT: C0P271;
DR  UNIPROT: C7FZT6;
DR  UNIPROT: Q95V72;
DR  UNIPROT: S6EZN6;
DR  UNIPROT: S6EZP3;
DR  UNIPROT: S6F548;
DR  UNIPROT: S6F556;
DR  UNIPROT: S6FD02;
DR  UNIPROT: S6FN04;
DR  UNIPROT: S6FN08;
DR  UNIPROT: S6FWP4;
DR  UNIPROT: S6FWP6;
DR  UNIPROT: U4MKU8;
DR  Pfam: PF16471;
DR  Pfam: PF09744;
DR  PROSITE: PS51776;
DR  PROSITE: PS51777;
DE  Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of synaptic vesicle transport, through interactions with the JNK-signaling components and motor proteins. Binds specific components of the JNK signaling pathway namely jnk-1, jkk-1 and sek-1. Associates with components of the motor protein, kinesin-1. Pre-assembled unc-16 scaffolding complexes are then transported as a cargo of kinesin, to the required subcellular location. Regulates the retrograde transport of autophagosomes from the neurites to the cell body of AIY interneurons (PubMed:30880001). {ECO:0000269|PubMed:10393177, ECO:0000269|PubMed:11738026, ECO:0000269|PubMed:30880001}.
DE  Reference Proteome: Yes;
DE  Interaction: P46822; IntAct: EBI-2413629; Score: 0.62
DE  Interaction: Q5WRT0; IntAct: EBI-337898; Score: 0.00
DE  Interaction: H2L0F6; IntAct: EBI-343424; Score: 0.00
DE  Interaction: P34686; IntAct: EBI-345569; Score: 0.00
DE  Interaction: Q93345; IntAct: EBI-345563; Score: 0.00
DE  Interaction: Q18668; IntAct: EBI-345566; Score: 0.00
DE  Interaction: Q8WQG9; IntAct: EBI-1811901; Score: 0.40
DE  Interaction: G5EDT6; IntAct: EBI-1811913; Score: 0.40
GO  GO:0030424;
GO  GO:0043194;
GO  GO:0043679;
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0008432;
GO  GO:0019900;
GO  GO:0019894;
GO  GO:0005078;
GO  GO:0030159;
GO  GO:0030421;
GO  GO:0040011;
GO  GO:0018991;
GO  GO:0046328;
GO  GO:0030431;
GO  GO:0048489;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MACNLSPVNEMADSITSSTPSEIVYGGPGSPDEHRTMSDKVQTMASAIYRELETMIKVHGEDGVKTLMPLVVNVLEALDL
SQ  AYLERDEQTAELEMLKEDNEQLQTQYEREKALRKQTEQKYIEIEDTLIGQNKELDKKIESLESIMRMLELKAKNATDHAS
SQ  RLEEREVEQKLEFDRLHERYNTLLRTHVDHMERTKYLMGSEKFELMQNMPLPNMQLRNKMGMAASVDASSIRGVSDLISA
SQ  HMTQSTTMDVNLANHITNEDWQDEFSSDIEPSPRDIPQSSADALTSPITTKEPTPKREAASPKQSEEEEADETTSVDPKE
SQ  NNDLLGADLTDDESDWNGLGLIPRRHRPNEMLDDDDTSDDGSLGMGREVENLIKENSELLDMKNALNIVKNDLINQVDEL
SQ  NSENMILRDENLSRQMVSEKMQEQITKHEEEIKTLKQKLMEKENEQEEDDVPMAMRKRFTRSEMQRVLMDRNAYKEKLME
SQ  LEESIKWTEMQRAKKMQQQQQNVNQKKSGGIWEFFSSLLGDSVTPPASSRGNRASSSRGKMTRSVEYIDPDMISERRAAE
SQ  RREQYKLVREHVKKEDGRIEAYGWSLPNVEAEVSSVPIPVCCRPLLDNEPSLKIWCATGVVLRGGRDERGQWIVGDPIYF
SQ  APASMKKTKTSNHRPELEDEIKRARNLDARESELDEWQSSSLVWVVSSNQGKSLIAVLDANNPNNIIETFPACDSHLLCI
SQ  QAVSGVMEGEPEMNEEQSKKYLSGGGKIKDLPEGLDGTDLGACEWVELRKMEDSEDGVPTYCSNDMKPSPKRTRDFSISE
SQ  VAPVDSSAPVKEDPLPPPANRPGGRAALPPHIRDAMSKYDGVSGQMSGALPTVWMGGQNQYIYIHSAVTAWKQCLRRIKM
SQ  PDAVLSIVHYKSRIFAALANGTIAIFHRNKHGEWSDEGYHSLRVGSATSSVRSLCLVSTNIWATYKNCVVVLDAESLQIV
SQ  KVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVDIEPYVTKMLGTSKLDFSYMRTTALLVSNRRLW
SQ  IGTGTGVIISVPFSGQLEKKIETKDSKRPAGPGGLVRVYGATSENATNDEKTNDDFIPYCNLAHAQLSFHGHKDSVKFFL
SQ  GVPGASKNGEDESAEVTLRRMLIMSGGDGYIDFRIGEENEPELTGQSIRPRDMSHLIIWEVDAELPILSK
//
ID  P05783;
PN  Keratin, type I cytoskeletal 18;
GN  KRT18;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. Cytoplasm, perinuclear region. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Cytoplasm {ECO:0000250|UniProtKB:Q5BJY9}.
DR  UNIPROT: P05783;
DR  UNIPROT: Q53G38;
DR  UNIPROT: Q5U0N8;
DR  UNIPROT: Q9BW26;
DR  Pfam: PF00038;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  OMIM: 148070;
DR  OMIM: 215600;
DR  DisGeNET: 3875;
DE  Function: Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}.
DE  Disease: Cirrhosis (CIRRH) [MIM:215600]: A liver disease characterized by severe panlobular liver-cell swelling with Mallory body formation, prominent pericellular fibrosis, and marked deposits of copper. Clinical features include abdomen swelling, jaundice and pulmonary hypertension. {ECO:0000269|PubMed:12724528, ECO:0000269|PubMed:9011570}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O15027; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: O75190; IntAct: EBI-1255173; Score: 0.62
DE  Interaction: P01112; IntAct: EBI-3930926; Score: 0.37
DE  Interaction: Q925J2; IntAct: EBI-7985760; Score: 0.53
DE  Interaction: P62993; IntAct: EBI-297464; Score: 0.35
DE  Interaction: P29353; IntAct: EBI-298042; Score: 0.27
DE  Interaction: P05787; IntAct: EBI-445615; Score: 0.94
DE  Interaction: P04049; IntAct: EBI-7291105; Score: 0.49
DE  Interaction: P63104; IntAct: EBI-7293055; Score: 0.67
DE  Interaction: Q9BVR6; IntAct: EBI-753352; Score: 0.37
DE  Interaction: P19012; IntAct: EBI-754231; Score: 0.55
DE  Interaction: O95751; IntAct: EBI-756694; Score: 0.37
DE  Interaction: Q8IYI6; IntAct: EBI-756712; Score: 0.37
DE  Interaction: Q15834; IntAct: EBI-757168; Score: 0.37
DE  Interaction: O14964; IntAct: EBI-758998; Score: 0.78
DE  Interaction: Q9Y5B8; IntAct: EBI-759004; Score: 0.67
DE  Interaction: O75688; IntAct: EBI-1060989; Score: 0.00
DE  Interaction: P23508; IntAct: EBI-1078134; Score: 0.00
DE  Interaction: P05452; IntAct: EBI-1085136; Score: 0.00
DE  Interaction: P02671; IntAct: EBI-1255726; Score: 0.37
DE  Interaction: P27348; IntAct: EBI-1255734; Score: 0.37
DE  Interaction: Q15628; IntAct: EBI-1371586; Score: 0.60
DE  Interaction: Q8NFJ9; IntAct: EBI-1805760; Score: 0.44
DE  Interaction: Q96RK4; IntAct: EBI-1805921; Score: 0.44
DE  Interaction: Q9BXC9; IntAct: EBI-1805991; Score: 0.44
DE  Interaction: Q8IWZ6; IntAct: EBI-1806052; Score: 0.44
DE  Interaction: Q99816; IntAct: EBI-2339235; Score: 0.67
DE  Interaction: Q8NFA0; IntAct: EBI-2513538; Score: 0.40
DE  Interaction: O46385; IntAct: EBI-7872249; Score: 0.37
DE  Interaction: P63103; IntAct: EBI-8673294; Score: 0.35
DE  Interaction: P63101; IntAct: EBI-8686577; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-3453257; Score: 0.00
DE  Interaction: P28799; IntAct: EBI-3909889; Score: 0.37
DE  Interaction: Q9Y6K9; IntAct: EBI-3911087; Score: 0.57
DE  Interaction: Q14094; IntAct: EBI-3915486; Score: 0.37
DE  Interaction: Q9NUX5; IntAct: EBI-3917886; Score: 0.49
DE  Interaction: Q99459; IntAct: EBI-3926990; Score: 0.37
DE  Interaction: Q09472; IntAct: EBI-3929095; Score: 0.37
DE  Interaction: P52292; IntAct: EBI-3931399; Score: 0.37
DE  Interaction: O43913; IntAct: EBI-3931539; Score: 0.37
DE  Interaction: Q96GM5; IntAct: EBI-3931549; Score: 0.37
DE  Interaction: Q5VU43; IntAct: EBI-3931569; Score: 0.44
DE  Interaction: Q14161; IntAct: EBI-3931579; Score: 0.44
DE  Interaction: Q92837; IntAct: EBI-3934896; Score: 0.37
DE  Interaction: Q99757; IntAct: EBI-3938277; Score: 0.37
DE  Interaction: Q6PKC3; IntAct: EBI-3939414; Score: 0.37
DE  Interaction: Q8N2W9; IntAct: EBI-3939424; Score: 0.37
DE  Interaction: Q96MU7; IntAct: EBI-3939434; Score: 0.37
DE  Interaction: P15336; IntAct: EBI-5529812; Score: 0.35
DE  Interaction: Q12815; IntAct: EBI-5652482; Score: 0.31
DE  Interaction: Q13895; IntAct: EBI-5652463; Score: 0.31
DE  Interaction: P19320; IntAct: EBI-6190694; Score: 0.53
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-6871566; Score: 0.37
DE  Interaction: P13569; IntAct: EBI-6898303; Score: 0.53
DE  Interaction: Q99959; IntAct: EBI-9074403; Score: 0.40
DE  Interaction: Q13835; IntAct: EBI-9073560; Score: 0.58
DE  Interaction: P27958; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-10194630; Score: 0.78
DE  Interaction: Q8IYE0; IntAct: EBI-10263041; Score: 0.56
DE  Interaction: Q96CS2; IntAct: EBI-10283572; Score: 0.56
DE  Interaction: P05783; IntAct: EBI-10483950; Score: 0.37
DE  Interaction: Q9D7I8; IntAct: EBI-11048266; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-11051725; Score: 0.35
DE  Interaction: A0A0S2Z505; IntAct: EBI-16437711; Score: 0.56
DE  Interaction: P07196; IntAct: EBI-16437697; Score: 0.56
DE  Interaction: A0A0S2Z4Q4; IntAct: EBI-16437687; Score: 0.56
DE  Interaction: Q5JVL4; IntAct: EBI-24291369; Score: 0.56
DE  Interaction: Q3SY84; IntAct: EBI-24361934; Score: 0.56
DE  Interaction: P02538; IntAct: EBI-24367348; Score: 0.56
DE  Interaction: Q5XKE5; IntAct: EBI-24620654; Score: 0.56
DE  Interaction: Q9NX04; IntAct: EBI-24396239; Score: 0.56
DE  Interaction: P48668; IntAct: EBI-24419624; Score: 0.68
DE  Interaction: Q9P2K3; IntAct: EBI-24420285; Score: 0.56
DE  Interaction: Q9BVG8; IntAct: EBI-24553060; Score: 0.56
DE  Interaction: Q8WW24; IntAct: EBI-24557965; Score: 0.56
DE  Interaction: Q14533; IntAct: EBI-24563479; Score: 0.56
DE  Interaction: Q8TD31; IntAct: EBI-24572327; Score: 0.56
DE  Interaction: Q8N0S2; IntAct: EBI-12703058; Score: 0.56
DE  Interaction: O75022; IntAct: EBI-14032442; Score: 0.43
DE  Interaction: Q14457; IntAct: EBI-16020615; Score: 0.50
DE  Interaction: Q5SQX6; IntAct: EBI-16086797; Score: 0.35
DE  Interaction: Q9BQ69; IntAct: EBI-16880214; Score: 0.65
DE  Interaction: P61417; IntAct: EBI-20817152; Score: 0.37
DE  Interaction: P61416; IntAct: EBI-20817281; Score: 0.37
DE  Interaction: P68640; IntAct: EBI-20817402; Score: 0.37
DE  Interaction: O30878; IntAct: EBI-20817508; Score: 0.37
DE  Interaction: P69974; IntAct: EBI-20817667; Score: 0.37
DE  Interaction: A0A5P8YI02; IntAct: EBI-20818482; Score: 0.37
DE  Interaction: Q0WD22; IntAct: EBI-20818419; Score: 0.37
DE  Interaction: Q86U44; IntAct: EBI-20594935; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: A0A087WXM9; IntAct: EBI-20917996; Score: 0.40
DE  Interaction: P08670; IntAct: EBI-20917772; Score: 0.40
DE  Interaction: Q5HYC2; IntAct: EBI-20918276; Score: 0.40
DE  Interaction: Q15149; IntAct: EBI-20919124; Score: 0.40
DE  Interaction: Q96M95; IntAct: EBI-20921148; Score: 0.40
DE  Interaction: Q12860; IntAct: EBI-20920940; Score: 0.40
DE  Interaction: Q8WWL7; IntAct: EBI-20922150; Score: 0.40
DE  Interaction: Q8WYP5; IntAct: EBI-20924394; Score: 0.40
DE  Interaction: Q8IYB4; IntAct: EBI-20926658; Score: 0.40
DE  Interaction: P01730; IntAct: EBI-20930576; Score: 0.40
DE  Interaction: Q9Y616; IntAct: EBI-20935164; Score: 0.40
DE  Interaction: Q9NY99; IntAct: EBI-20938524; Score: 0.40
DE  Interaction: Q66PJ3; IntAct: EBI-20938316; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q14108; IntAct: EBI-21264396; Score: 0.35
DE  Interaction: B7UM99; IntAct: EBI-22228314; Score: 0.66
DE  Interaction: P61158; IntAct: EBI-22229062; Score: 0.27
DE  Interaction: Q96CS3; IntAct: EBI-25770166; Score: 0.35
DE  Interaction: Q8IWF2; IntAct: EBI-25770736; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-25951430; Score: 0.56
DE  Interaction: P51114; IntAct: EBI-26510698; Score: 0.37
DE  Interaction: P51116; IntAct: EBI-26511933; Score: 0.37
DE  Interaction: Q53F19; IntAct: EBI-26396827; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q9UNH5; IntAct: EBI-27115490; Score: 0.27
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
GO  GO:0005912;
GO  GO:0071944;
GO  GO:0034451;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005882;
GO  GO:0045095;
GO  GO:0005815;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0098641;
GO  GO:0003723;
GO  GO:0097110;
GO  GO:0005198;
GO  GO:0009653;
GO  GO:0007049;
GO  GO:0097191;
GO  GO:0043000;
GO  GO:0097284;
GO  GO:0045104;
GO  GO:0043066;
GO  GO:0033209;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFTTRSTFSTNYRSLGSVQAPSYGARPVSSAASVYAGAGGSGSRISVSRSTSFRGGMGSGGLATGIAGGLAGMGGIQNE
SQ  KETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQVRDWSHYFKIIEDLRAQIFANTVDNARIVLQIDNARLA
SQ  ADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEVDAP
SQ  KSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASL
SQ  ENSLREVEARYALQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFNLGDALDSSN
SQ  SMQTIQKTTTRRIVDGKVVSETNDTKVLRH
//
ID  P05784;
PN  Keratin, type I cytoskeletal 18;
GN  Krt18;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05783}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P05783}. Cytoplasm {ECO:0000250|UniProtKB:Q5BJY9}.
DR  UNIPROT: P05784;
DR  UNIPROT: Q3TIX1;
DR  UNIPROT: Q3TJH6;
DR  UNIPROT: Q3TJW7;
DR  UNIPROT: Q61766;
DR  Pfam: PF00038;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DE  Function: When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:17213200}.
DE  Reference Proteome: Yes;
DE  Interaction: P63101; IntAct: EBI-8180960; Score: 0.35
DE  Interaction: Q64337; IntAct: EBI-10052425; Score: 0.38
GO  GO:0071944;
GO  GO:0034451;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0009897;
GO  GO:0005615;
GO  GO:0005882;
GO  GO:0045095;
GO  GO:0005815;
GO  GO:0016363;
GO  GO:0005730;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0097110;
GO  GO:0005198;
GO  GO:0097191;
GO  GO:0043000;
GO  GO:0097284;
GO  GO:0045104;
GO  GO:0043066;
GO  GO:0033209;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFTTRSTTFSTNYRSLGSVRTPSQRVRPASSAASVYAGAGGSGSRISVSRSVWGGSVGSAGLAGMGGIQTEKETMQDLN
SQ  DRLASYLDKVKSLETENRRLESKIREHLEKKGPQGVRDWGHYFKIIEDLRAQIFANSVDNARIVLQIDNARLAADDFRVK
SQ  YETELAMRQSVESDIHGLRKVVDDTNITRLQLETEIEALKEELLFMKKNHEEEVQGLEAQIASSGLTVEVDAPKSQDLSK
SQ  IMADIRAQYEALAQKNREELDKYWSQQIEESTTVVTTKSAEIRDAETTLTELRRTLQTLEIDLDSMKNQNINLENSLGDV
SQ  EARYKAQMEQLNGVLLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFSLNDALDSSNSMQTVQK
SQ  TTTRKIVDGRVVSETNDTRVLRH
//
ID  Q5BJY9;
PN  Keratin, type I cytoskeletal 18;
GN  Krt18;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus matrix {ECO:0000269|PubMed:16128803, ECO:0000269|PubMed:16998620}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05783}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P05783}. Cytoplasm {ECO:0000269|PubMed:16128803, ECO:0000269|PubMed:16998620}.
DR  UNIPROT: Q5BJY9;
DR  UNIPROT: Q63278;
DR  Pfam: PF00038;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DE  Function: When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection (By similarity). Involved in the uptake of thrombin- antithrombin complexes by hepatic cells. {ECO:0000250|UniProtKB:P05783, ECO:0000269|PubMed:9353322}.
DE  Reference Proteome: Yes;
DE  Interaction: P54645; IntAct: EBI-16399805; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16400563; Score: 0.35
GO  GO:0071944;
GO  GO:0034451;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0009897;
GO  GO:0005615;
GO  GO:0005882;
GO  GO:0045095;
GO  GO:0005815;
GO  GO:0016363;
GO  GO:0005730;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0097110;
GO  GO:0005198;
GO  GO:1902488;
GO  GO:0097191;
GO  GO:0043000;
GO  GO:0097284;
GO  GO:0070365;
GO  GO:0045104;
GO  GO:0072497;
GO  GO:0043066;
GO  GO:0009750;
GO  GO:0031667;
GO  GO:0033209;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFTTRSTTFSTNYRSLGSVRTPSQRVRPASSAASVYAGAGGSGSRISVSRSVWGGSVGSAGLAGMGGVQTEKETMQDLN
SQ  DRLASYLDKVKNLETENRRLESKIREYLEKRGPQGVRDWGHYFKTIEDLRAQIFANSVDNARIVLQIDNARLAADDFRVK
SQ  YETELAMRQSVESDIHGLRKVVDDTNITRLQLETEIEALKEELLFMKKNHEEEVQGLEAQIASSGLTVEVDAPKSQDLSK
SQ  IMADIRAQYEQLAQKNREELDKYWSQQIEESTTVVTTKSAEIRDAETTLLELRRTLQTLEIDLDSMKNQNINLENNLGEV
SQ  EARYRVQMEQLNGVLLHLESELAQTRAEGQRQTQEYEALLNIKVKLEAEIATYRRLLEDGDDFSLNDALDSSNSMQTVQR
SQ  TTTRKVVDGKVVSETNDTRVLRH
//
ID  P32767;
PN  Importin beta-like protein KAP122;
GN  KAP122;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:10525531, ECO:0000269|PubMed:10617640}.
DR  UNIPROT: P32767;
DR  UNIPROT: D6VUC1;
DR  PDB: 6Q82;
DR  PDB: 6Q83;
DR  PDB: 6Q84;
DE  Function: Nuclear transport factor (karyopherin) involved in protein transport between the cytoplasm and nucleoplasm. Required for the nuclear import of the complex composed the large subunit (TOA1) and the small subunit (TOA2) of the general transcription factor IIA (TFIIA). Required for the nuclear import of the RNR2-RNR4 heterodimer, also called beta-beta' subunit, which corresponds to the small subunit of the ribonucleotide reductase (RNR). May play a role in regulation of pleiotropic drug resistance. {ECO:0000269|PubMed:10525531, ECO:0000269|PubMed:16432237, ECO:0000269|PubMed:1882553, ECO:0000269|PubMed:18838542}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-3764975; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-800949; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-800949; Score: 0.35
DE  Interaction: P09734; IntAct: EBI-800949; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-800949; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-800949; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-800949; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-800949; Score: 0.35
DE  Interaction: Q04062; IntAct: EBI-800949; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-800949; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-800949; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-800949; Score: 0.35
DE  Interaction: P00830; IntAct: EBI-800949; Score: 0.44
DE  Interaction: P50085; IntAct: EBI-810540; Score: 0.35
DE  Interaction: P39925; IntAct: EBI-812746; Score: 0.27
DE  Interaction: Q00955; IntAct: EBI-814773; Score: 0.27
DE  Interaction: Q06625; IntAct: EBI-820843; Score: 0.27
DE  Interaction: P06103; IntAct: EBI-7560214; Score: 0.40
DE  Interaction: P40019; IntAct: EBI-8225157; Score: 0.22
DE  Interaction: Q12363; IntAct: EBI-15565947; Score: 0.40
DE  Interaction: P38316; IntAct: EBI-16263556; Score: 0.35
DE  Interaction: P32381; IntAct: EBI-16264169; Score: 0.35
DE  Interaction: P07703; IntAct: EBI-16280355; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0006606;
GO  GO:0008361;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSIHEVVALIEELYSPHPKHDVNQIQQSLQSIQKSEQGFHLANELLSDDKYSANVKYFGALTLTVQLNTRGENDYETLW
SQ  NVFRSNLLYLTKFSTLYVSNPNMYGQSLIIIKKLMSNLSLIFTKINDPQLNNAGNENMIKQWNNPINTFIQLMSVQNQNI
SQ  NADQLLLDSINCSLTYEQLSQFVSLSQKHNELALTFTEVIVEDLTKFQTKRHSMSQIHEVVHEHLYISTMALINLNLTAQ
SQ  AVFNPTVFDCITAWINYISLTRSVSSSGRMDLSEIFQNLIDLMYQSTEGSDGYENAEKILTIFGNVFANDPLLMSYDLRQ
SQ  QIECIFLGVVRPDSGITDISNKNSWMLQYMNYLVTNDFFSELKELAICIVDFLQINTLSVCNKLFTNIQAADNGQVQDEY
SQ  IQEYIKVLLQMTNFPLTPVLQEFFSVRMVDFWLDLSDAYTNLASETLRPNSIELSTQIFQQLINIYLPKISLSVKQRIIE
SQ  EEGESTSVNEFEDFRNAVSDLAQSLWSILGNDNLTNVLIDGMGQMPAASDETLIIKDTDVLFRIETMCFVLNTILVDMTL
SQ  SESPWIKNIVDANKFFNQNVISVFQTGFQTSASTKVSQILKLDFVRTSTTLIGTLAGYFKQEPFQLNPYVEALFQGLHTC
SQ  TNFTSKNEQEKISNDKLEVMVIKTVSTLCETCREELTPYLMHFISFLNTVIMPDSNVSHFTRTKLVRSIGYVVQCQVSNG
SQ  PEEQAKYILQLTNLLSGSIEHCLASSVQLQEQQDYINCLLYCISELATSLIQPTEIIENDALLQRLSEFQSFWSSDPLQI
SQ  RSKIMCTIDKVLDNSIYCKNSAFVEIGCLIVGKGLNLPDGEPYFLKYNMSEVMNFVLRHVPNCELATCLPYFVYLLEKLI
SQ  SEFRKELTPQEFDFMFEKILLVYYDAYIINDPDLLQMTIGFVNNVLDVKPGLAIGSKHWTSFILPQFLKLIPSREKFTIV
SQ  AVAKFWTKLINNKKYNQEELTTVRQQVSSIGGDLVYQIMYGLFHTQRSDLNSYTDLLRALVAKFPIEAREWLVAVLPQIC
SQ  NNPAGHEKFINKLLITRGSRAAGNVILQWWLDCTTLPNYQG
//
ID  Q949W6;
PN  Protein KAKU4;
GN  KAKU4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:24824484}.
DR  UNIPROT: Q949W6;
DR  UNIPROT: F4JS05;
DR  UNIPROT: O49592;
DE  Function: Required for nucleus structure organization (e.g. size and shape). {ECO:0000269|PubMed:24824484}.
DE  Reference Proteome: Yes;
DE  Interaction: O49653; IntAct: EBI-4484696; Score: 0.37
DE  Interaction: Q8LBH4; IntAct: EBI-4501160; Score: 0.37
DE  Interaction: Q9LPU9; IntAct: EBI-4508208; Score: 0.37
DE  Interaction: Q9LZM7; IntAct: EBI-4508216; Score: 0.37
DE  Interaction: Q9FFS8; IntAct: EBI-4513992; Score: 0.37
DE  Interaction: Q9SZB2; IntAct: EBI-4531112; Score: 0.37
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005886;
GO  GO:0005802;
GO  GO:0071763;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDSVSGYAAGAGQPRVGGKIVRPRRTAVVRTPCERPVQRSRDPPQQNPSWISRLVYKPASVIASGAGKFISSVVFSDSSS
SQ  SSEEDEDSSSDIDGDEDVEKNNPDFTEEDLLSAQQPSIQRLSSKRVIEQLLLQETFAREEGDRLIDIIKARVVDHPSVPS
SQ  AIETSHDDYGLTSDVNVGEMSNTAVMEARKWLEEKKSGSSSKYKATEDGAGSPVDVAKSYMRARLPWGSPAANNLDFRSP
SQ  SSARVQGTPLPYSAGNFSSSKLKRKSGSNQSWNIQDEIRKVRAKATEEMLKSPSSVASLEPKYSPYVLATDMLKGNASSL
SQ  NADGAVRNEQSRALPNSAIPTSEHNQTTEANQAVKETGVLHTRSRGVGLEETFISTQGVKPSEDTNTAPQSGTAVDDFND
SQ  QDGDFIQPTSTIGNTTNAVLALGATLDPTGNSCIPKDVFETSKEADEIGASRHTSNGFPSSSPSGYGRSTKTHTTRRNQG
SQ  FSAYS
//
ID  Q759Y0;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q759Y0;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031301;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLEILLFLCVIIQRSHINAEITHVVSHLAETALRQDTNFQLLSQDIIAKKFPILDSSCVRRALSDFLPQCLQYGFETVPS
SQ  DVRTQAAVKLSICELQASGVDNMPPECVGAVHFGACLRAMERTPQWWTTYSGNYQHLPSTCFENALPYEKEQLLSLFLNI
SQ  TDVYSNFQDDLVVDLEKYRANFEATVEASLRLMKASLMEGTHEIVNQLKDDLNYVNSKLADMGETITEHTDNVRTVFNDI
SQ  SDELNDYDMAGQIAHLKEDTMSLWQKINSDMGTYHDVQMSSLYNINAVFDTFYNRATESVQQVRTSVIESQLETLDLIAD
SQ  FNSLVRKSILPVLADELQPQLQEMSVSISRSLVGLSASYNEHLQAWSNRVNETLSEMESHLNNTMSQVEHMNDSIETLEN
SQ  KVFVLVSLGNALTTYVKWIYTFSRALISGYGIVTLIMSMLVVRYSIKLNSSWIKVLGRSTFILVAVVLGARTGSMLSY
//
ID  Q59WU8;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  237561;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q59WU8;
DR  UNIPROT: A0A1D8PPH8;
DR  UNIPROT: A0A1D8PPH9;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031301;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNIVLLIYCLAMVVAHDLQLFGDFKFELSDNWRNDCAKKALEPIINQCAEGIETISPFQQKSIAIQLSICEFENAEISYP
SQ  SECRSQNLDTCILLLEKSPQYWTTFSGYYREIRNICHQVSLPFAKDQILQVYGNITEFYRTLMDEMTNSSKYTENMQNEL
SQ  KAKFDKLIGVIDLILADREKNREDLKSSFNMFKNNFEKSLNNALVVMKHSYEDANSNVKELESHLNYFINDMSQVYILIN
SQ  EKALEVKSQQDRIKEHNADILNQIEEIKKNLDNAYEEASEVQISNNQLVHDIQSSLDYSLFTVSNLNSHLQLSINDFIEK
SQ  NEDIRSRAPIIFEEIFGLFLNHLNESGQLAMDSFEAALDLSLNMLHQKLNQTERSIDNLNSKVSDLAHFADSLKKYASSI
SQ  FNVPNYVRTSMNHKIQQWREFGNIMVVGGVFFFVVLTLLVLSFIRTQVMKVFRFAFIGIPMITGIALAIFILRLLSMPMK
SQ  VVDID
//
ID  Q6FU40;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6FU40;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSMSITQPIKDLLSSQFQSYNISEQVKLYDIFPLLKPSCIKEAITDVVEVCTGYGPESLDPSIRAKAAVKLSLCEFEAVG
SQ  LSIIPQGCYSNSIEEMMDCMLEIEHSSHWWTTYSGNYQRLSDVCSTYREYYQEKAIIETFLNITDFMADFHNQFKSSVVS
SQ  ETQEFQSNMKDKFAGVYNQFTHFESLLSQMIQKHSGIINDSIVAIKNKLSTEFVDELQMLKNDRYILINQILESDTEIKK
SQ  TIDSMLVELTEDMKNQISAKSEFLINHMNITRLNESTALHDIIEENLQERFKDIAIFLDKFMVEIQTETNKVLLEVNEKL
SQ  PTLEQQYLGNFAQALSNIDKQVLSASLQWQYDYDVVFANLYAALDLLNSNLNSSVKKIEQIEHVIDTIIVDTSFLNDQLA
SQ  NLILIPSTILRAFSFIGVKRVIIAIIVLYFKSTLLCLVHYGQSFRIAALLMSATAGIFCSKLLMSYIYN
//
ID  Q6BNJ4;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  284592;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6BNJ4;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDCVNISWFLITLFAAIATSTMHDGENNNVGKMLQEPTYLQSEMIESIMSRHLESFSLTESDFEDIIFMKPRSKCVKDAL
SQ  KDIIPECMRLGVDSIEPGLQKKAAIQLSICEFENSKVTYPSSCYNMINDNDFDSCIFDIERAPQYWTTFSGYYREITKIC
SQ  YEESLPFEKEQIISLYSNITKLYSKMFQDLNDSYKDSTHIQQMMKNEFKELQRMMKVILDQNEKTSEEVKEKYEEFSEQY
SQ  SSMLSTSLEISKKFSLGTENLVEDMANNIKYLDFELSRISIAIEDLDFETKLTDMKNSVLDDVRNLSDESISLLDSILTN
SQ  LESLDILSQDAQNITNGISQSLKKNEVLSNNMNNALIETDTQLHEHNEVIRFEFEETISYLSQFSDQAIDNAIRDTSEEI
SQ  TKHVATFIDSINLRLEETTTKLEEVIYNIDDLSDKVGNASSYLIEGLNLLTSNGIMDALLLTYNNVASGLESGFGMLTTL
SQ  KSDIFKIVRFITACILFAILFIWSMNRLFSQNRTKHTTLSSISPIGILNFRRIFRFLTNLALWLSVMGGTLLAVIVTNFL
SQ  IQLKVYISKLSTND
//
ID  Q6CIJ3;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6CIJ3;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MWFLVFSIWIASGQLLPHISNVIEKELDQLEITELSREYINNKFPITQSSCVKNALGEFLEICMRKGFEFVDADLRVITA
SQ  VRLSVCEFESSGLTNYPSECHEKRLGGIDTISCVNALESSPQWWTTYSGNYQNLPHICMENSLPFEKEQILELFLNITDM
SQ  YSEFQRNIENYWKSFSSDLEINGKENIDMIQNLFNSLVNDLIQNHKMKDEELITEFDKMKAEFDIRFFNFTESFDNLNDE
SQ  VNEDLSLIKSHLIETFRQVDSEYMAQLQKNKNSTDKAFNELESMSTYILDHQKTSMELIDSFFSDLIDLTRDKNLVISDE
SQ  LMQTQEETIHLIFQYNKLVHESVIPLLTDDLLPVVRGVSNSIVENLDNMNVELTSHLENVSQTIEVKFKALEKETDRSLL
SQ  KAKEVESNLRNLNNLVSTSLKGLQTIVRLLTFLLKRQVVLVGILQIFLRKYISMNLYLYAIAVVVTALAGSKVGSWGSLL
SQ  MKSFVTR
//
ID  A5E4Z8;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  379508;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A5E4Z8;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVGASAISGVVIIANVVAAIAAAAGDGDGGIASTTDTILTLDGIKILNNALLQWKDDCNQRALAEVMPQCIHGVENITPS
SQ  QQKHTAMELSICEFENNGLDYPLECHASVRNLNTNTCIQALEKSPQYWTTFSGNYRAVKDICHQISLPYEKDQIIEVYEN
SQ  MTLLYRSVMEDLKSSHHKYTVELEMKIQNKFNKLFSVVDDLMRSRAEENNKVNQTFNKFYENFQVSISNALVVMQNSYDG
SQ  ANTNFELMQRHVSYFATELQRILLLVQEQGEKLQVQQEQLVTGNVKLSIQQERLFDNMQLFGNELDKLHNAEVSRVSSVN
SQ  KQLKLTEFSIRHANSILRENTDELHLQRMLIAEYTPIILGNITTLLMHFLNQSASEIVENFEHSLNLSLEKLSLKIDETA
SQ  NSLAVVNATIARCSIFASSVVETLDSLKNSTIRMMMLFMSMITPSVTFDGLISGAKAIIAFFTLVTRLAAVIAICLLIIL
SQ  IWPIVKSLFFQPLCYLMRRCSYIVVSILVGVAAANFSVWLLQK
//
ID  A5DJU3;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  294746;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A5DJU3;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKKILRLVFILVYTNISTFVSAHELEDAASFTADELDRLLEDPPGCIQLAMRPIFEKCVLNGIHAVDPKDRRSSAIEMSV
SQ  CEFESAGVEYPAECSTTDYDTCIWKLGLVPQYWTTFSGNYRDIGLFCEGVSRNNEKEQLVLLYSNITKVFAGFRHAFYES
SQ  YSKSQEMKDEMEEGFSRWSADFDIAKDQHKEFYEFVAKQQEHIKIELMKNQKVIFDFHDEQEVRFNSYSNHIVDVIDSMA
SQ  VDLDIILAKLADDGIIEDMENQKSKSLDIMKSYSEDAELTLSRIVSELERVGIIQKNDVSIVENLNSGLADTSNKVSKLN
SQ  KDFEDLDSHFQHTKDLIESEVSFLFANLIGEMETKLSQALENVDDRIELHFVSQLEFLDKSLNETWEAILTFKQDWQIFT
SQ  SIFENFENIPKSISHFVTSGLYKTNEILTQTSYFWSTILNIPVSLLSNILRYTMAASWIAILFILISLRYGSTKSFLLVI
SQ  MVLLVVFLNTHRW
//
ID  Q09684;
PN  Nuclear fusion protein tht1;
GN  tht1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9442101}; Multi-pass membrane protein {ECO:0000269|PubMed:9442101}. Nucleus membrane {ECO:0000269|PubMed:9442101}; Multi-pass membrane protein {ECO:0000269|PubMed:9442101}.
DR  UNIPROT: Q09684;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000269|PubMed:9442101}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0031309;
GO  GO:0031301;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKFHPTRPFGLYFEFFIIISFFFTSESTGDVESFMKYSNVAFSEGLAGFDSLAHVYQALLKKSTCYQEVAATLISKCSLL
SQ  NTELTIDNRIHSAIQMTLCDFERSQILAPSECVRGSQSECVSKLESTSTWWLSFTSHFHDVNHLCRLANLEMQKELSIEV
SQ  NMNVTLVQKQFLEMVILHLRNFESVTDKMNQRIDKFDGKFNSVIENSFKDINFRVNQEIMGLVELQNHQQEGMVQQKEIL
SQ  STIKQLKSEIFDINSFFANFIEESAGYSNSLIEKLNEKFTSENAIALSAIGKYTSEFSAFMEKRIKNLITTTEDSLQQSV
SQ  QSNIDFVNSGFQPLYDLTIQLKEELQSLKRLSSEQQNLQHEQILQWKSDFLNVSKDHLKVLQQLRPLIDIVEKFMNVYFK
SQ  GLSNIISSFAFIGFTLFATLSSLFFKVLKIHRRPIIVFGSLSIIFIHIYCFKITSWVNLYGWITCTIARTLSFIKLNIRT
SQ  FYLTAFLCALLNFLRYLKYRNSKKDTELSLFLPAPEECNIYHNEHIQVQEDNYLCPIENSLIDLFGSENNKEKLGKQENV
SQ  RFAFLNSESLEQSPWWD
//
ID  Q6C994;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  284591;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6C994;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031301;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLSYSFNTTIFTENRDLVAALQPQTNCARTALTLIVSDCGKLSSFNEDQQLRVSLAVGLAVCEFKAAQVTYPDACNNIE
SQ  DWMSTSACTQQLVSSPQWWTTYHGCYNSVKQICHMHEASRECDRALKTHSQIVDMQEKLHTKMDQYWELVETMSDHRDAV
SQ  LDYWNDTFDFMSETLAHMKETSVSLNAVYRDNFAQAQEHFQMLSENLQEARVQMENLGWAAQDAVVSLSKSTLAEQSLVS
SQ  ERLKNDASSLHKLLVLAHQDTTESFETQLQQSLTILVESSDNVLLNHVQQVSSRLSALMSDLEESQKKNMDMQHQLQQKV
SQ  RTINDDIEGFTDTVKQGLEASHSLLNLVKSKIQLVNGVVSIFSRPVRSAFQLASFIIMIRAAFIGGIYTSIGLVMGSMLG
SQ  VLVMQQV
//
ID  A6ZMC4;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein.
DR  UNIPROT: A6ZMC4;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy.
DE  Reference Proteome: No;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFAMRYVYLFAICIKFVSSSELGKINNLLQGRLIYTDNSVATNVLESKFPFLKSTCVKDALKLFLPQCIANGLESIDAET
SQ  RVETAIKLSICEFQASGLGEIPENCMVDDLGSMMDCMFELESSSQWWTTYSGNYQRLSSICYENLLPFEKEQILKLFLNI
SQ  TELYDSFGDDVDTKLNHLMFQMEQDSQNFLDDLARMFRNYDNELRNATESNRIILENDLSFFRNKVNDVLYETSEQLEVQ
SQ  IIEKNSQLMNEVDTVHHIMSDLADELAKNDIKSKINDLKDDSLNNLQDLVEMSNDVKEYYSRNNKLVNTELENFSMGLKK
SQ  QLGGMSKDLSESQMEAIELLQGFNSILHDSLLPSMTDEIVPEMTNFKNTLLQEWTAITSTLNGDFALWNEEIFSTFNDIS
SQ  EKLNGTKKKLDDIEIRVSLVHKNVMTMMRVLDFMWKTSKMIIRCGYLAVKNKYYWLLCSVVWIWSKYRTSRVNVKMIPIK
SQ  RYYQWAALLLSIYLGAKTGSLIDF
//
ID  Q04746;
PN  Nuclear fusion protein KAR5;
GN  KAR5;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein.
DR  UNIPROT: Q04746;
DR  UNIPROT: D6VZN9;
DR  Pfam: PF04163;
DE  Function: Required for nuclear membrane fusion during karyogamy. {ECO:0000269|PubMed:10069807, ECO:0000269|PubMed:8051211, ECO:0000269|PubMed:9382856, ECO:0000269|PubMed:9456310}.
DE  Reference Proteome: Yes;
DE  Interaction: P41901; IntAct: EBI-599525; Score: 0.37
DE  Interaction: P38989; IntAct: EBI-599534; Score: 0.37
DE  Interaction: P47037; IntAct: EBI-599543; Score: 0.37
DE  Interaction: Q06179; IntAct: EBI-599561; Score: 0.37
DE  Interaction: P39013; IntAct: EBI-599570; Score: 0.37
DE  Interaction: P40073; IntAct: EBI-7768639; Score: 0.37
DE  Interaction: Q07914; IntAct: EBI-857938; Score: 0.00
DE  Interaction: Q02159; IntAct: EBI-859813; Score: 0.00
DE  Interaction: P38788; IntAct: EBI-3790287; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-3809587; Score: 0.35
GO  GO:0005789;
GO  GO:0031301;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFEMRYVYLFAICIKFVSSSELGKINNLLQGRLIYTDNSVATNVLESKFPFLKSTCVKDALKLFLPQCIANGLESIDAET
SQ  RVETAIKLSICEFQASGLGEIPENCMVDDLGSMMDCMFELESSSQWWTTYSGNYQRLSSICYENLLPFEKEQILKLFLNI
SQ  TELYDSFGDDVDTKLNHLMFQMEQDSQNFLDDLARMFRNYDNELRNATESNRIILENDLSFFRNKVNDVLYETSEQLEVQ
SQ  IIEKNSQLMNEVDTVHHIMSDLADELAKNDIKSKINDLKDDSLNNLQDLVEMSNDVKEYYSRNNKLVNTELENFSMGLKK
SQ  QLGGMSKDLSESQMEAIELLQGFNSILHDSLLPSMTDEIVPEMTNFKNTLLQEWTAITSTLNGDFALWNEEIFSTFNDIS
SQ  EKLNGTKKKLDDIEIRVSLVHKNVMTMMRVLDFMWKTSKMIIRCGYLAVKNKYYWLLCSVVWIWSKYRTSRVNVKMIPIK
SQ  RYYQWAALLLSIYLGAKTGSLIDF
//
ID  Q2T9R2;
PN  Protein KASH5;
GN  KASH5;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q80VJ8, ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q80VJ8}. Chromosome, telomere {ECO:0000250|UniProtKB:Q80VJ8}. Note=Localized exclusively at telomeres from the leptotene to diplotene stages. Colocalizes with SUN2 at sites of telomere attachment in meiocytes. At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. {ECO:0000250|UniProtKB:Q80VJ8}.
DR  UNIPROT: Q2T9R2;
DR  UNIPROT: F1N496;
DR  Pfam: PF14658;
DR  Pfam: PF14662;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Required for telomere attachment to nuclear envelope in the prophase of meiosis and for rapid telomere prophase movements implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly. Required for homolog pairing during meiotic prophase in spermatocytes and probably oocytes. Essential for male and female gametogenesis. Recruits cytoplasmic dynein to telomere attachment sites at the nuclear envelope in spermatocytes. In oocytes is involved in meiotic resumption and spindle formation. {ECO:0000250|UniProtKB:Q80VJ8}.
DE  Reference Proteome: Yes;
GO  GO:0000781;
GO  GO:0016021;
GO  GO:0000800;
GO  GO:0034993;
GO  GO:0090619;
GO  GO:0005640;
GO  GO:0070840;
GO  GO:0007015;
GO  GO:0090220;
GO  GO:0007129;
GO  GO:0090172;
GO  GO:0051225;
GO  GO:0051653;
GO  GO:0034397;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDMPEDQAGGPTAKMYLWDQAEDRSLGTLLSLEEQILNSTFEACDPQRTGTVAVTHLLAYLEAVTGRGPQDARLQTLACS
SQ  LDPSGEGPQATVDLDTFLVVMRDWITACQLDGGLELEEETAFEGALTSQQLPSGCPEVEDPANLESFGGEDPRPELPATA
SQ  DLLSSLEDLELSNRRLAGENAKLQRSVETAEEGSARLGEEISALRKQLRSTQQALQLARGVDEELEDLKTLAKSLEEQNR
SQ  SLLAQARHTEKEQQRLVAEMETLQEENGKLLAERDGVKRRSEELASEKDILKRQLYECEHLICQRDAILSERTRHAESLT
SQ  KTLEEYRATTQELRLEISHLEEQLSQTQEGLDELSEGAQVRRVDCTNLLPPSLGVELQAIQQRNLQEESAHPQEGREEPS
SQ  TRLPRREEEDGAEIQVMVDLPLHPEDSHPGDILGNPPESSPSEPELQQALVPMVKELVPVRRPVWGQLCLWPLHLRRLRV
SQ  TRHLLIPAPLLGLLLLLLLSVLLLGQSPPPTWPHLQLCYLQPPPV
//
ID  Q8N6L0;
PN  Protein KASH5;
GN  KASH5;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q80VJ8, ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q80VJ8}. Chromosome, telomere {ECO:0000250|UniProtKB:Q80VJ8}. Note=Localized exclusively at telomeres from the leptotene to diplotene stages. Colocalizes with SUN2 at sites of telomere attachment in meiocytes. At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. {ECO:0000250|UniProtKB:Q80VJ8}.
DR  UNIPROT: Q8N6L0;
DR  UNIPROT: Q96MC3;
DR  PDB: 6R2I;
DR  PDB: 6WMF;
DR  Pfam: PF14658;
DR  Pfam: PF14662;
DR  OMIM: 618125;
DR  DisGeNET: 147872;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Required for telomere attachment to nuclear envelope in the prophase of meiosis and for rapid telomere prophase movements implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly. Required for homolog pairing during meiotic prophase in spermatocytes and probably oocytes. Essential for male and female gametogenesis. Recruits cytoplasmic dynein to telomere attachment sites at the nuclear envelope in spermatocytes. In oocytes is involved in meiotic resumption and spindle formation. {ECO:0000250|UniProtKB:Q80VJ8}.
DE  Reference Proteome: Yes;
DE  Interaction: P03185; IntAct: EBI-11736405; Score: 0.37
DE  Interaction: P39996; IntAct: EBI-11530258; Score: 0.56
DE  Interaction: P50402; IntAct: EBI-11774371; Score: 0.79
DE  Interaction: Q06616; IntAct: EBI-11535750; Score: 0.56
DE  Interaction: Q12382; IntAct: EBI-11537331; Score: 0.56
DE  Interaction: Q5SQN1; IntAct: EBI-24469364; Score: 0.56
DE  Interaction: Q8IY26; IntAct: EBI-24446133; Score: 0.56
DE  Interaction: Q9NVE4; IntAct: EBI-757171; Score: 0.37
DE  Interaction: Q5NID9; IntAct: EBI-2802245; Score: 0.00
DE  Interaction: O60341; IntAct: EBI-8466533; Score: 0.37
DE  Interaction: Q63HK5; IntAct: EBI-10171916; Score: 0.56
DE  Interaction: A8K660; IntAct: EBI-10174501; Score: 0.56
DE  Interaction: B2R9H7; IntAct: EBI-10175724; Score: 0.56
DE  Interaction: D3DR40; IntAct: EBI-10176580; Score: 0.56
DE  Interaction: O00155; IntAct: EBI-10178982; Score: 0.72
DE  Interaction: O00526; IntAct: EBI-10179689; Score: 0.56
DE  Interaction: O00631; IntAct: EBI-10180799; Score: 0.56
DE  Interaction: O14653; IntAct: EBI-10181300; Score: 0.72
DE  Interaction: O43765; IntAct: EBI-10185924; Score: 0.79
DE  Interaction: O75379; IntAct: EBI-10188020; Score: 0.56
DE  Interaction: O75431; IntAct: EBI-10188246; Score: 0.72
DE  Interaction: O95210; IntAct: EBI-10191271; Score: 0.56
DE  Interaction: O95954; IntAct: EBI-10192646; Score: 0.56
DE  Interaction: P11836; IntAct: EBI-10197695; Score: 0.56
DE  Interaction: P15622; IntAct: EBI-10199056; Score: 0.56
DE  Interaction: P16234; IntAct: EBI-10199272; Score: 0.56
DE  Interaction: P17544; IntAct: EBI-10200009; Score: 0.56
DE  Interaction: P23763; IntAct: EBI-10201363; Score: 0.56
DE  Interaction: P29373; IntAct: EBI-10204814; Score: 0.72
DE  Interaction: P42857; IntAct: EBI-10208892; Score: 0.72
DE  Interaction: P50281; IntAct: EBI-10211798; Score: 0.56
DE  Interaction: P56748; IntAct: EBI-10215655; Score: 0.56
DE  Interaction: P60520; IntAct: EBI-10217795; Score: 0.56
DE  Interaction: Q04941; IntAct: EBI-10223541; Score: 0.56
DE  Interaction: Q07325; IntAct: EBI-10224666; Score: 0.56
DE  Interaction: Q10471; IntAct: EBI-10226993; Score: 0.72
DE  Interaction: Q13021; IntAct: EBI-10227634; Score: 0.56
DE  Interaction: Q13190; IntAct: EBI-10228578; Score: 0.72
DE  Interaction: Q3B820; IntAct: EBI-10240519; Score: 0.56
DE  Interaction: Q53XK0; IntAct: EBI-10242941; Score: 0.56
DE  Interaction: Q5QGT7; IntAct: EBI-10244785; Score: 0.56
DE  Interaction: Q5T3I0; IntAct: EBI-10245269; Score: 0.72
DE  Interaction: Q5TAB7; IntAct: EBI-10246926; Score: 0.79
DE  Interaction: Q6N075; IntAct: EBI-10250847; Score: 0.56
DE  Interaction: Q6NYC8; IntAct: EBI-10251924; Score: 0.72
DE  Interaction: Q6P1J9; IntAct: EBI-10252374; Score: 0.72
DE  Interaction: Q6PKG0; IntAct: EBI-10254142; Score: 0.56
DE  Interaction: Q6UX06; IntAct: EBI-10254551; Score: 0.56
DE  Interaction: Q7L4I2; IntAct: EBI-10256242; Score: 0.56
DE  Interaction: Q86YD7; IntAct: EBI-10260946; Score: 0.56
DE  Interaction: Q8IVW4; IntAct: EBI-10261805; Score: 0.56
DE  Interaction: Q8N511; IntAct: EBI-10265839; Score: 0.56
DE  Interaction: Q8N5M9; IntAct: EBI-10266794; Score: 0.72
DE  Interaction: Q8N6R1; IntAct: EBI-10267201; Score: 0.72
DE  Interaction: Q8TAF8; IntAct: EBI-10271708; Score: 0.81
DE  Interaction: Q92843; IntAct: EBI-10279533; Score: 0.79
DE  Interaction: Q969F0; IntAct: EBI-10280499; Score: 0.72
DE  Interaction: Q96BZ8; IntAct: EBI-10282764; Score: 0.56
DE  Interaction: Q96DI8; IntAct: EBI-10284698; Score: 0.56
DE  Interaction: Q96HV5; IntAct: EBI-10288899; Score: 0.56
DE  Interaction: Q96JW4; IntAct: EBI-10290136; Score: 0.72
DE  Interaction: Q96Q77; IntAct: EBI-10292805; Score: 0.56
DE  Interaction: Q96SE0; IntAct: EBI-10293347; Score: 0.56
DE  Interaction: Q9BQ70; IntAct: EBI-10296328; Score: 0.56
DE  Interaction: Q9BQA9; IntAct: EBI-10296518; Score: 0.72
DE  Interaction: Q9BRI3; IntAct: EBI-10296832; Score: 0.81
DE  Interaction: Q9HC62; IntAct: EBI-10310610; Score: 0.72
DE  Interaction: Q9NQ35; IntAct: EBI-10311733; Score: 0.72
DE  Interaction: Q9NRQ5; IntAct: EBI-10312978; Score: 0.56
DE  Interaction: Q9NRS4; IntAct: EBI-10313004; Score: 0.56
DE  Interaction: Q9NTX7; IntAct: EBI-11774361; Score: 0.70
DE  Interaction: Q9P0N8; IntAct: EBI-10317638; Score: 0.56
DE  Interaction: Q9P0S9; IntAct: EBI-10317744; Score: 0.56
DE  Interaction: Q9UL15; IntAct: EBI-10323400; Score: 0.72
DE  Interaction: Q9Y228; IntAct: EBI-10325376; Score: 0.72
DE  Interaction: Q9Y287; IntAct: EBI-10325842; Score: 0.56
DE  Interaction: Q9Y3D6; IntAct: EBI-10327740; Score: 0.56
DE  Interaction: P0C739; IntAct: EBI-11736458; Score: 0.37
DE  Interaction: P06197; IntAct: EBI-11522953; Score: 0.56
DE  Interaction: P0CD91; IntAct: EBI-11523095; Score: 0.56
DE  Interaction: P11972; IntAct: EBI-11523210; Score: 0.56
DE  Interaction: P12945; IntAct: EBI-11523283; Score: 0.56
DE  Interaction: P23968; IntAct: EBI-11524128; Score: 0.56
DE  Interaction: P28496; IntAct: EBI-11525135; Score: 0.56
DE  Interaction: P32453; IntAct: EBI-11525349; Score: 0.56
DE  Interaction: P32502; IntAct: EBI-11526099; Score: 0.56
DE  Interaction: P35179; IntAct: EBI-11527246; Score: 0.56
DE  Interaction: P38084; IntAct: EBI-11527720; Score: 0.56
DE  Interaction: P38206; IntAct: EBI-11527956; Score: 0.56
DE  Interaction: P38695; IntAct: EBI-11529286; Score: 0.56
DE  Interaction: P38736; IntAct: EBI-11529354; Score: 0.56
DE  Interaction: P38842; IntAct: EBI-11529602; Score: 0.56
DE  Interaction: P38837; IntAct: EBI-11529584; Score: 0.56
DE  Interaction: P40312; IntAct: EBI-11530656; Score: 0.56
DE  Interaction: P40533; IntAct: EBI-11531474; Score: 0.56
DE  Interaction: P40567; IntAct: EBI-11531531; Score: 0.56
DE  Interaction: P46956; IntAct: EBI-11532079; Score: 0.56
DE  Interaction: P46965; IntAct: EBI-11532098; Score: 0.56
DE  Interaction: P47013; IntAct: EBI-11532127; Score: 0.56
DE  Interaction: P53012; IntAct: EBI-11532979; Score: 0.56
DE  Interaction: P53142; IntAct: EBI-11533081; Score: 0.56
DE  Interaction: P53337; IntAct: EBI-11533532; Score: 0.56
DE  Interaction: P53730; IntAct: EBI-11533568; Score: 0.56
DE  Interaction: P53906; IntAct: EBI-11533819; Score: 0.56
DE  Interaction: Q01590; IntAct: EBI-11534163; Score: 0.56
DE  Interaction: Q02724; IntAct: EBI-11534307; Score: 0.56
DE  Interaction: Q03579; IntAct: EBI-11534893; Score: 0.56
DE  Interaction: Q03714; IntAct: EBI-11534941; Score: 0.56
DE  Interaction: Q03860; IntAct: EBI-11535004; Score: 0.56
DE  Interaction: Q04969; IntAct: EBI-11535341; Score: 0.56
DE  Interaction: Q08144; IntAct: EBI-11536212; Score: 0.56
DE  Interaction: Q12118; IntAct: EBI-11536557; Score: 0.56
DE  Interaction: Q12259; IntAct: EBI-11537012; Score: 0.56
DE  Interaction: Q12431; IntAct: EBI-11537378; Score: 0.56
DE  Interaction: Q12746; IntAct: EBI-11537533; Score: 0.56
DE  Interaction: Q6Q595; IntAct: EBI-11537600; Score: 0.56
DE  Interaction: Q8TGQ7; IntAct: EBI-11537661; Score: 0.56
DE  Interaction: P34897; IntAct: EBI-11774291; Score: 0.49
DE  Interaction: Q96HA8; IntAct: EBI-11774311; Score: 0.49
DE  Interaction: P17152; IntAct: EBI-11774321; Score: 0.70
DE  Interaction: O43561; IntAct: EBI-11774341; Score: 0.49
DE  Interaction: Q969S0; IntAct: EBI-24288362; Score: 0.56
DE  Interaction: P52803; IntAct: EBI-24297738; Score: 0.56
DE  Interaction: O00264; IntAct: EBI-24315794; Score: 0.56
DE  Interaction: Q9UHJ9; IntAct: EBI-24336298; Score: 0.56
DE  Interaction: Q96HH6; IntAct: EBI-24338645; Score: 0.56
DE  Interaction: P63027; IntAct: EBI-24343261; Score: 0.56
DE  Interaction: Q53FD0; IntAct: EBI-24350172; Score: 0.56
DE  Interaction: Q96LL9; IntAct: EBI-24351872; Score: 0.56
DE  Interaction: Q96D05; IntAct: EBI-24358633; Score: 0.56
DE  Interaction: O15155; IntAct: EBI-24361171; Score: 0.56
DE  Interaction: Q5W5X9; IntAct: EBI-25246714; Score: 0.56
DE  Interaction: Q8N2M4; IntAct: EBI-25251117; Score: 0.56
DE  Interaction: O75841; IntAct: EBI-24480378; Score: 0.56
DE  Interaction: A5PKU2; IntAct: EBI-24482338; Score: 0.56
DE  Interaction: P01375; IntAct: EBI-24492243; Score: 0.56
DE  Interaction: Q96HB5; IntAct: EBI-24497344; Score: 0.56
DE  Interaction: O95159; IntAct: EBI-24375600; Score: 0.56
DE  Interaction: Q8IVJ1; IntAct: EBI-24380121; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-24388099; Score: 0.56
DE  Interaction: Q9BVK8; IntAct: EBI-24391713; Score: 0.56
DE  Interaction: Q14802; IntAct: EBI-24404702; Score: 0.56
DE  Interaction: Q86Y82; IntAct: EBI-24409778; Score: 0.56
DE  Interaction: Q9BUN8; IntAct: EBI-24409708; Score: 0.56
DE  Interaction: Q8N912; IntAct: EBI-25261754; Score: 0.56
DE  Interaction: Q96DZ9; IntAct: EBI-24419119; Score: 0.56
DE  Interaction: Q86W74; IntAct: EBI-24441079; Score: 0.56
DE  Interaction: Q9H490; IntAct: EBI-24449445; Score: 0.56
DE  Interaction: Q9Y247; IntAct: EBI-24449816; Score: 0.56
DE  Interaction: Q9NY91; IntAct: EBI-24450486; Score: 0.56
DE  Interaction: P11215; IntAct: EBI-24452528; Score: 0.56
DE  Interaction: O75425; IntAct: EBI-24454568; Score: 0.56
DE  Interaction: Q9UEU0; IntAct: EBI-24455064; Score: 0.56
DE  Interaction: Q96F15; IntAct: EBI-24463545; Score: 0.56
DE  Interaction: Q4LDR2; IntAct: EBI-24465439; Score: 0.56
DE  Interaction: Q9UHP6; IntAct: EBI-24468231; Score: 0.56
DE  Interaction: O75427; IntAct: EBI-24473887; Score: 0.56
DE  Interaction: Q15848; IntAct: EBI-12702786; Score: 0.56
GO  GO:0000781;
GO  GO:0016021;
GO  GO:0000800;
GO  GO:0034993;
GO  GO:0090619;
GO  GO:0005640;
GO  GO:0070840;
GO  GO:0042802;
GO  GO:0007015;
GO  GO:0090220;
GO  GO:0000724;
GO  GO:0007129;
GO  GO:0090172;
GO  GO:0048477;
GO  GO:0007283;
GO  GO:0051225;
GO  GO:0051653;
GO  GO:0034397;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLPEGPVGGPTAEMYLRERPEEARLGMPVSLEEQILNSTFEACDPQRTGTVAVAQVLAYLEAVTGQGPQDARLQTLANS
SQ  LDPNGEGPKATVDLDTFLVVMRDWIAACQLHGGLELEEETAFQGALTSRQLPSGCPEAEEPANLESFGGEDPRPELQATA
SQ  DLLSSLEDLELSNRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNR
SQ  SLLAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLA
SQ  QTLEEYRVTTQELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGWTELLPPSLGLEIEAIRQKQEVATADLSNPLCGVWQ
SQ  WEEVIHETSEETEFPSEAPAGGQRNFQGEPAHPEEGRKEPSMWLTRREEEEDAESQVTADLPVPLGAPRPGDIPENPPER
SQ  PARRELQQALVPVMKKLVPVRRRAWGQLCLPPQRLRVTRHPLIPAPVLGLLLLLLLSVLLLGPSPPPTWPHLQLCYLQPP
SQ  PV
//
ID  Q80VJ8;
PN  Protein KASH5;
GN  Kash5;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:26842404}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000269|PubMed:22826121}. Chromosome, telomere {ECO:0000269|PubMed:22826121}. Note=Localized exclusively at telomeres from the leptotene to diplotene stages. Colocalizes with SUN2 at sites of telomere attachment in meiocytes. At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. {ECO:0000269|PubMed:24586178, ECO:0000269|PubMed:26842404}.
DR  UNIPROT: Q80VJ8;
DR  UNIPROT: E9QNS3;
DR  UNIPROT: E9QQ69;
DR  Pfam: PF14658;
DR  Pfam: PF14662;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Required for telomere attachment to nuclear envelope in the prophase of meiosis and for rapid telomere prophase movements implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly. Required for homolog pairing during meiotic prophase in spermatocytes and probably oocytes. Essential for male and female gametogenesis. Recruits cytoplasmic dynein to telomere attachment sites at the nuclear envelope in spermatocytes. In oocytes is involved in meiotic resumption and spindle formation. {ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:25892231, ECO:0000269|PubMed:26842404}.
DE  Reference Proteome: Yes;
DE  Interaction: O08788; IntAct: EBI-11666413; Score: 0.35
DE  Interaction: O94901; IntAct: EBI-11685143; Score: 0.27
DE  Interaction: Q9D666; IntAct: EBI-11666366; Score: 0.59
DE  Interaction: Q8BJS4; IntAct: EBI-11666392; Score: 0.37
DE  Interaction: Q7TSY8; IntAct: EBI-11685119; Score: 0.37
DE  Interaction: Q8C0V1; IntAct: EBI-16089819; Score: 0.35
GO  GO:0000781;
GO  GO:0016021;
GO  GO:0000800;
GO  GO:0034993;
GO  GO:0090619;
GO  GO:0005640;
GO  GO:0070840;
GO  GO:0042802;
GO  GO:0007015;
GO  GO:0090220;
GO  GO:0000724;
GO  GO:0007129;
GO  GO:0090172;
GO  GO:0048477;
GO  GO:0007283;
GO  GO:0051225;
GO  GO:0051653;
GO  GO:0034397;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MHSILRSSLSSREALRMRQLKGLRKERPGRHPLGVRLRAIWTSFLFPNPPHSGGKLRASTAAVEEHQEWSMDLPEGQAGG
SQ  PTAQMYLWEQPEEASSRPLLSLEEQILNSTFEACDPHKTGTVTVAHLLAYLEAVTGQGPQDVRLQTLARSLDPYGEGAGA
SQ  TVELDTFLVVMRDWIAACQLQGGLERAEETAYEGALASPHLPSVCPEAEESANLESFGGEDPRPEGPATAELLSNLEDLE
SQ  LSNRRLAGENAKLQRSVETAEEGSARLGEEITALRKQLRSTQQALQVAKALDEELEDLKTLAKSLEEQNRSLMAQARHTE
SQ  KEQQHLAAEVETLQEENEKLLAERDGVKRRSEELATEKDALKRQLCECERLICQREAVLSERTRHAESLARTLEEYRTTT
SQ  QELRQEISNLEEQLSQSQEGPEELLEGAEAGRVGWIMALPPSLDLEIQAIRQEQDVASAGLSSPLYGVWQWEEVEPEPEP
SQ  EPEPEPEPEPQEVEFPSEDPARQQTDLQREPVRALEGSRAPCLRLSRSQEEEEEEEESWVLADPSSPLGTYHHKLAPGSS
SQ  RESCHIVPEMHQALMPVVRDLVPVERSRTQHCLHPQHSPGIRISQHPLVPTPVLGLLLLLLLSILLFSQSPPPTWPHLQL
SQ  YYLQPPPV
//
ID  Q92993;
PN  Histone acetyltransferase KAT5;
GN  KAT5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:11262386, ECO:0000269|PubMed:11416127, ECO:0000269|PubMed:12551922, ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17704809, ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:25301942, ECO:0000269|PubMed:33938178}. Chromosome {ECO:0000269|PubMed:25560918, ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:29335245, ECO:0000269|PubMed:33076429}. Cytoplasm {ECO:0000269|PubMed:25301942}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:26829474}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:34608293}. Nucleus, nucleolus {ECO:0000269|PubMed:16387653}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11262386}. Note=Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region and UV irradiation induces translocation into punctuate subnuclear structures named nuclear bodies (PubMed:11262386). Transiently localizes to kinetochores in early mitosis (PubMed:26829474). Localizes to spindle poles when chromosomes align during metaphase (PubMed:34608293). Localizes in the cytoplasm and nucleus of round spermatids (By similarity). {ECO:0000250|UniProtKB:Q8CHK4, ECO:0000269|PubMed:11262386, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:34608293}.
DR  UNIPROT: Q92993;
DR  UNIPROT: B4E3C7;
DR  UNIPROT: C9JL99;
DR  UNIPROT: O95624;
DR  UNIPROT: Q13430;
DR  UNIPROT: Q17RW5;
DR  UNIPROT: Q561W3;
DR  UNIPROT: Q6GSE8;
DR  UNIPROT: Q9BWK7;
DR  PDB: 2EKO;
DR  PDB: 2OU2;
DR  PDB: 4QQG;
DR  Pfam: PF01853;
DR  Pfam: PF11717;
DR  Pfam: PF17772;
DR  PROSITE: PS51726;
DR  OMIM: 601409;
DR  OMIM: 619103;
DR  DisGeNET: 10524;
DE  Function: Catalytic subunit of the NuA4 histone acetyltransferase complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H2A and H4 (PubMed:12776177, PubMed:15042092, PubMed:15121871, PubMed:15310756, PubMed:14966270, PubMed:16387653, PubMed:19909775, PubMed:25865756, PubMed:27153538, PubMed:29335245, PubMed:29174981, PubMed:33076429, PubMed:32822602). Histone acetylation alters nucleosome-DNA interactions and promotes interaction of the modified histones with other proteins which positively regulate transcription (PubMed:12776177, PubMed:15042092, PubMed:15121871, PubMed:15310756, PubMed:14966270). The NuA4 histone acetyltransferase complex is required for the activation of transcriptional programs associated with proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (PubMed:17709392, PubMed:19783983, PubMed:32832608). The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) by promoting homologous recombination (HR): the complex inhibits TP53BP1 binding to chromatin via MBTD1, which recognizes and binds histone H4 trimethylated at 'Lys-20' (H4K20me), and KAT5 that catalyzes acetylation of 'Lys-15' of histone H2A (H2AK15ac), thereby blocking the ubiquitination mark required for TP53BP1 localization at DNA breaks (PubMed:27153538, PubMed:32832608). Also involved in DSB repair by mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac), promoting NBN/NBS1 assembly at the sites of DNA damage (PubMed:17709392, PubMed:26438602). The NuA4 complex plays a key role in hematopoietic stem cell maintenance and is required to maintain acetylated H2A.Z/H2AZ1 at MYC target genes (By similarity). The NuA4 complex is also required for spermatid development by promoting acetylation of histones: histone hyperacetylation is required for histone replacement during the transition from round to elongating spermatids (By similarity). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (PubMed:24463511). Also acetylates non-histone proteins, such as ARNTL/BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF, LPIN1, NDC80/HEC1, NR1D2, RAN, SOX4, FOXP3, ULK1 and RUBCNL/Pacer (PubMed:16141325, PubMed:17360565, PubMed:17996965, PubMed:24835996, PubMed:26829474, PubMed:29040603, PubMed:30409912, PubMed:30704899, PubMed:32034146, PubMed:32817552, PubMed:34077757). Directly acetylates and activates ATM (PubMed:16141325). Promotes nucleotide excision repair (NER) by mediating acetylation of ERCC4/XPF, thereby promoting formation of the ERCC4-ERCC1 complex (PubMed:32034146). Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2 (PubMed:17996965). Acts as a regulator of regulatory T-cells (Treg) by catalyzing FOXP3 acetylation, thereby promoting FOXP3 transcriptional repressor activity (PubMed:17360565, PubMed:24835996). Involved in skeletal myoblast differentiation by mediating acetylation of SOX4 (PubMed:26291311). Catalyzes acetylation of APBB1/FE65, increasing its transcription activator activity (PubMed:33938178). Promotes transcription elongation during the activation phase of the circadian cycle by catalyzing acetylation of ARNTL/BMAL1, promoting elongation of circadian transcripts (By similarity). Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Acts as a regulator of the cGAS-STING innate antiviral response by catalyzing acetylation the N-terminus of CGAS, thereby promoting CGAS DNA-binding and activation (PubMed:32817552). Also regulates lipid metabolism by mediating acetylation of CHKA or LPIN1 (PubMed:34077757). Promotes lipolysis of lipid droplets following glucose deprivation by mediating acetylation of isoform 1 of CHKA, thereby promoting monomerization of CHKA and its conversion into a tyrosine-protein kinase (PubMed:34077757). Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of LPIN1, thereby promoting the synthesis of diacylglycerol (PubMed:29765047). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) and 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to mediate protein crotonylation and 2-hydroxyisobutyrylation, respectively (PubMed:29192674, PubMed:34608293). Acts as a key regulator of chromosome segregation and kinetochore-microtubule attachment during mitosis by mediating acetylation or crotonylation of target proteins (PubMed:26829474, PubMed:29040603, PubMed:30409912, PubMed:34608293). Catalyzes acetylation of AURKB at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis (PubMed:26829474). Acetylates RAN during mitosis, promoting microtubule assembly at mitotic chromosomes (PubMed:29040603). Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore- microtubule attachment (PubMed:30409912). Catalyzes crotonylation of MAPRE1/EB1, thereby ensuring accurate spindle positioning in mitosis (PubMed:34608293). {ECO:0000250|UniProtKB:Q8CHK4, ECO:0000269|PubMed:12776177, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:15042092, ECO:0000269|PubMed:15121871, ECO:0000269|PubMed:15310756, ECO:0000269|PubMed:16141325, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17709392, ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:19783983, ECO:0000269|PubMed:19909775, ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:24835996, ECO:0000269|PubMed:25865756, ECO:0000269|PubMed:26291311, ECO:0000269|PubMed:26438602, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:29174981, ECO:0000269|PubMed:29192674, ECO:0000269|PubMed:29335245, ECO:0000269|PubMed:29765047, ECO:0000269|PubMed:30409912, ECO:0000269|PubMed:30704899, ECO:0000269|PubMed:32034146, ECO:0000269|PubMed:32817552, ECO:0000269|PubMed:32822602, ECO:0000269|PubMed:32832608, ECO:0000269|PubMed:33076429, ECO:0000269|PubMed:33938178, ECO:0000269|PubMed:34077757, ECO:0000269|PubMed:34608293}.
DE  Disease: Neurodevelopmental disorder with dysmorphic facies, sleep disturbance, and brain abnormalities (NEDFASB) [MIM:619103]: A neurodevelopmental disorder characterized by severe global developmental delay, intellectual disability, poor or absent language, behavioral abnormalities, severe sleep disturbance, seizures, cerebral malformations, and craniofacial dysmorphism. Progressive cerebellar atrophy is also observed. Additional features may include genitourinary tract anomalies, hearing loss, and mild distal skeletal defects. {ECO:0000269|PubMed:32822602}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O00165; IntAct: EBI-25912324; Score: 0.56
DE  Interaction: O14656; IntAct: EBI-25847296; Score: 0.56
DE  Interaction: O94972; IntAct: EBI-10279849; Score: 0.56
DE  Interaction: O95295; IntAct: EBI-730852; Score: 0.00
DE  Interaction: P02545; IntAct: EBI-730261; Score: 0.00
DE  Interaction: P04406; IntAct: EBI-25857246; Score: 0.56
DE  Interaction: Q3YBM2; IntAct: EBI-25912439; Score: 0.56
DE  Interaction: Q6PIV2; IntAct: EBI-11319459; Score: 0.35
DE  Interaction: P10275; IntAct: EBI-7011232; Score: 0.51
DE  Interaction: P04326; IntAct: EBI-8673000; Score: 0.37
DE  Interaction: Q9NV56; IntAct: EBI-399119; Score: 0.74
DE  Interaction: Q9Y230; IntAct: EBI-449133; Score: 0.53
DE  Interaction: Q9Y265; IntAct: EBI-449133; Score: 0.76
DE  Interaction: P60709; IntAct: EBI-449133; Score: 0.35
DE  Interaction: Q9Y4A5; IntAct: EBI-449133; Score: 0.35
DE  Interaction: O96019; IntAct: EBI-449133; Score: 0.53
DE  Interaction: Q9P2H0; IntAct: EBI-473590; Score: 0.51
DE  Interaction: O95257; IntAct: EBI-473601; Score: 0.51
DE  Interaction: Q99728; IntAct: EBI-474165; Score: 0.37
DE  Interaction: Q5T3J3; IntAct: EBI-475117; Score: 0.37
DE  Interaction: Q96RU7; IntAct: EBI-728799; Score: 0.00
DE  Interaction: P31942; IntAct: EBI-728967; Score: 0.00
DE  Interaction: P21673; IntAct: EBI-729255; Score: 0.00
DE  Interaction: P17028; IntAct: EBI-729444; Score: 0.00
DE  Interaction: O95376; IntAct: EBI-729537; Score: 0.00
DE  Interaction: Q5T8Z1; IntAct: EBI-729633; Score: 0.00
DE  Interaction: Q7L5D6; IntAct: EBI-729684; Score: 0.00
DE  Interaction: Q9HC52; IntAct: EBI-5273178; Score: 0.57
DE  Interaction: Q99832; IntAct: EBI-729729; Score: 0.00
DE  Interaction: Q96SN8; IntAct: EBI-729756; Score: 0.00
DE  Interaction: P33240; IntAct: EBI-729840; Score: 0.00
DE  Interaction: O43261; IntAct: EBI-710053; Score: 0.51
DE  Interaction: P78417; IntAct: EBI-730090; Score: 0.00
DE  Interaction: Q13123; IntAct: EBI-730216; Score: 0.00
DE  Interaction: Q15013; IntAct: EBI-730291; Score: 0.00
DE  Interaction: Q9BQD7; IntAct: EBI-730333; Score: 0.00
DE  Interaction: Q96NT1; IntAct: EBI-730378; Score: 0.00
DE  Interaction: O14737; IntAct: EBI-730489; Score: 0.00
DE  Interaction: P56282; IntAct: EBI-730549; Score: 0.00
DE  Interaction: Q9H1D9; IntAct: EBI-730567; Score: 0.00
DE  Interaction: P29074; IntAct: EBI-710446; Score: 0.51
DE  Interaction: Q13332; IntAct: EBI-730633; Score: 0.00
DE  Interaction: P60953; IntAct: EBI-731524; Score: 0.00
DE  Interaction: Q96HD1; IntAct: EBI-731638; Score: 0.00
DE  Interaction: P20827; IntAct: EBI-731770; Score: 0.00
DE  Interaction: Q6N063; IntAct: EBI-731908; Score: 0.00
DE  Interaction: Q9H840; IntAct: EBI-732022; Score: 0.00
DE  Interaction: Q9BWC9; IntAct: EBI-732211; Score: 0.00
DE  Interaction: Q8IYL3; IntAct: EBI-732342; Score: 0.00
DE  Interaction: Q9NRX3; IntAct: EBI-732365; Score: 0.00
DE  Interaction: P19404; IntAct: EBI-732629; Score: 0.00
DE  Interaction: Q9H4M7; IntAct: EBI-732863; Score: 0.00
DE  Interaction: O15211; IntAct: EBI-733082; Score: 0.00
DE  Interaction: P62316; IntAct: EBI-733355; Score: 0.00
DE  Interaction: P17600; IntAct: EBI-733451; Score: 0.00
DE  Interaction: Q49AJ0; IntAct: EBI-734968; Score: 0.00
DE  Interaction: Q8N5W9; IntAct: EBI-735106; Score: 0.00
DE  Interaction: Q9Y4R8; IntAct: EBI-736985; Score: 0.00
DE  Interaction: Q15906; IntAct: EBI-769790; Score: 0.56
DE  Interaction: P54253; IntAct: EBI-1170127; Score: 0.71
DE  Interaction: P04637; IntAct: EBI-1799764; Score: 0.50
DE  Interaction: P16104; IntAct: EBI-7847385; Score: 0.35
DE  Interaction: Q01130; IntAct: EBI-8542152; Score: 0.54
DE  Interaction: Q9NPJ6; IntAct: EBI-8580402; Score: 0.35
DE  Interaction: Q96BR9; IntAct: EBI-3925101; Score: 0.67
DE  Interaction: P00520; IntAct: EBI-4370190; Score: 0.44
DE  Interaction: P10085; IntAct: EBI-7440605; Score: 0.57
DE  Interaction: Q9BVJ7; IntAct: EBI-7144423; Score: 0.37
DE  Interaction: P13805; IntAct: EBI-7405580; Score: 0.37
DE  Interaction: O14757; IntAct: EBI-6267516; Score: 0.27
DE  Interaction: Q9UPV0; IntAct: EBI-6267482; Score: 0.27
DE  Interaction: P08238; IntAct: EBI-6426082; Score: 0.40
DE  Interaction: Q15773; IntAct: EBI-9382362; Score: 0.40
DE  Interaction: Q9UIM3; IntAct: EBI-9382384; Score: 0.40
DE  Interaction: Q9BTE6; IntAct: EBI-9382403; Score: 0.40
DE  Interaction: P62805; IntAct: EBI-9254817; Score: 0.68
DE  Interaction: Q15672; IntAct: EBI-9254773; Score: 0.44
DE  Interaction: P50222; IntAct: EBI-10279809; Score: 0.56
DE  Interaction: O43829; IntAct: EBI-10279829; Score: 0.56
DE  Interaction: O75558; IntAct: EBI-10279839; Score: 0.72
DE  Interaction: P11926; IntAct: EBI-10279859; Score: 0.72
DE  Interaction: P14373; IntAct: EBI-10279869; Score: 0.56
DE  Interaction: P36406; IntAct: EBI-10279889; Score: 0.56
DE  Interaction: P35711; IntAct: EBI-10279879; Score: 0.56
DE  Interaction: P60411; IntAct: EBI-10279899; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-10279909; Score: 0.56
DE  Interaction: Q17RB8; IntAct: EBI-10279919; Score: 0.56
DE  Interaction: Q53SE7; IntAct: EBI-10279931; Score: 0.56
DE  Interaction: Q5JR59; IntAct: EBI-24410260; Score: 0.67
DE  Interaction: Q6A162; IntAct: EBI-10279951; Score: 0.56
DE  Interaction: Q6NT76; IntAct: EBI-10279961; Score: 0.72
DE  Interaction: Q8IXK0; IntAct: EBI-10279981; Score: 0.56
DE  Interaction: Q8N8E2; IntAct: EBI-10279991; Score: 0.56
DE  Interaction: Q8NEA9; IntAct: EBI-10280012; Score: 0.56
DE  Interaction: Q96JN2; IntAct: EBI-10280034; Score: 0.56
DE  Interaction: Q99750; IntAct: EBI-10280046; Score: 0.56
DE  Interaction: Q9BRK4; IntAct: EBI-10280056; Score: 0.72
DE  Interaction: Q9NNX1; IntAct: EBI-10280066; Score: 0.56
DE  Interaction: Q9NQM4; IntAct: EBI-10280076; Score: 0.72
DE  Interaction: Q9UKT9; IntAct: EBI-10280086; Score: 0.72
DE  Interaction: Q9Y2D8; IntAct: EBI-10280096; Score: 0.56
DE  Interaction: Q9Y2I6; IntAct: EBI-10280108; Score: 0.56
DE  Interaction: A8MYZ6; IntAct: EBI-11319145; Score: 0.35
DE  Interaction: P60122; IntAct: EBI-11023741; Score: 0.35
DE  Interaction: Q9WTM5; IntAct: EBI-11048350; Score: 0.35
DE  Interaction: Q9NXR8; IntAct: EBI-21817019; Score: 0.53
DE  Interaction: O95619; IntAct: EBI-21817019; Score: 0.53
DE  Interaction: Q9HC29; IntAct: EBI-10898987; Score: 0.51
DE  Interaction: Q88489; IntAct: EBI-11423202; Score: 0.37
DE  Interaction: Q96IK5; IntAct: EBI-11771420; Score: 0.70
DE  Interaction: Q96MP8; IntAct: EBI-24279273; Score: 0.56
DE  Interaction: O00505; IntAct: EBI-24294666; Score: 0.56
DE  Interaction: Q86Z20; IntAct: EBI-24322121; Score: 0.56
DE  Interaction: Q9Y2K1; IntAct: EBI-24328474; Score: 0.56
DE  Interaction: A0A0C3SFZ9; IntAct: EBI-24330536; Score: 0.56
DE  Interaction: Q9UBB9; IntAct: EBI-24337536; Score: 0.56
DE  Interaction: O00629; IntAct: EBI-24355694; Score: 0.56
DE  Interaction: Q96I34; IntAct: EBI-24479059; Score: 0.56
DE  Interaction: O75420; IntAct: EBI-24490761; Score: 0.56
DE  Interaction: Q9Y250; IntAct: EBI-24498393; Score: 0.56
DE  Interaction: Q9NRD5; IntAct: EBI-24509305; Score: 0.56
DE  Interaction: Q3B820; IntAct: EBI-24514424; Score: 0.56
DE  Interaction: O60684; IntAct: EBI-24516849; Score: 0.56
DE  Interaction: Q9NZ72; IntAct: EBI-24662444; Score: 0.56
DE  Interaction: Q96BW1; IntAct: EBI-24670487; Score: 0.56
DE  Interaction: Q9UM82; IntAct: EBI-24682942; Score: 0.56
DE  Interaction: Q96FV2; IntAct: EBI-24688534; Score: 0.56
DE  Interaction: Q9BW85; IntAct: EBI-24692554; Score: 0.56
DE  Interaction: Q8NAM6; IntAct: EBI-23728519; Score: 0.56
DE  Interaction: Q02535; IntAct: EBI-24699219; Score: 0.56
DE  Interaction: Q8TAU3; IntAct: EBI-24705679; Score: 0.56
DE  Interaction: Q6ZSJ9; IntAct: EBI-24707908; Score: 0.56
DE  Interaction: P29084; IntAct: EBI-24722218; Score: 0.56
DE  Interaction: Q8NDD1; IntAct: EBI-23790372; Score: 0.56
DE  Interaction: Q8TF42; IntAct: EBI-24738229; Score: 0.56
DE  Interaction: Q8NB15; IntAct: EBI-25284233; Score: 0.56
DE  Interaction: Q86VP1; IntAct: EBI-24380938; Score: 0.56
DE  Interaction: Q16254; IntAct: EBI-24393206; Score: 0.56
DE  Interaction: Q9NQX0; IntAct: EBI-24398367; Score: 0.56
DE  Interaction: Q9BU19; IntAct: EBI-24401478; Score: 0.56
DE  Interaction: Q8N680; IntAct: EBI-24408131; Score: 0.56
DE  Interaction: Q6NZI2; IntAct: EBI-24420443; Score: 0.56
DE  Interaction: Q8TF50; IntAct: EBI-24446962; Score: 0.56
DE  Interaction: Q9BYV9; IntAct: EBI-24447273; Score: 0.56
DE  Interaction: Q5VSY0; IntAct: EBI-24461854; Score: 0.56
DE  Interaction: Q8NHQ1; IntAct: EBI-24463727; Score: 0.56
DE  Interaction: Q14140; IntAct: EBI-24467005; Score: 0.56
DE  Interaction: O75031; IntAct: EBI-24467814; Score: 0.56
DE  Interaction: P23508; IntAct: EBI-24473562; Score: 0.56
DE  Interaction: Q9H2G9; IntAct: EBI-24476277; Score: 0.56
DE  Interaction: Q86WR7; IntAct: EBI-24541652; Score: 0.56
DE  Interaction: Q9H2F5; IntAct: EBI-24542665; Score: 0.56
DE  Interaction: O00213; IntAct: EBI-24556121; Score: 0.56
DE  Interaction: Q15699; IntAct: EBI-24566370; Score: 0.56
DE  Interaction: O15131; IntAct: EBI-24567185; Score: 0.56
DE  Interaction: Q8N0S2; IntAct: EBI-24592068; Score: 0.56
DE  Interaction: Q8IY31; IntAct: EBI-24654576; Score: 0.56
DE  Interaction: Q53FD0; IntAct: EBI-25273396; Score: 0.72
DE  Interaction: Q8IVT5; IntAct: EBI-14035664; Score: 0.35
DE  Interaction: Q96A08; IntAct: EBI-21579454; Score: 0.35
DE  Interaction: Q8NFN8; IntAct: EBI-21600104; Score: 0.35
DE  Interaction: Q6PJQ5; IntAct: EBI-21623731; Score: 0.35
DE  Interaction: P12524; IntAct: EBI-21709838; Score: 0.35
DE  Interaction: Q9HAF1; IntAct: EBI-21750318; Score: 0.35
DE  Interaction: Q9HBJ0; IntAct: EBI-21786331; Score: 0.35
DE  Interaction: Q9UBU8; IntAct: EBI-21788568; Score: 0.35
DE  Interaction: Q15014; IntAct: EBI-21816626; Score: 0.53
DE  Interaction: Q9Y546; IntAct: EBI-21817019; Score: 0.35
DE  Interaction: Q9NWZ5; IntAct: EBI-21817019; Score: 0.35
DE  Interaction: Q9NPF5; IntAct: EBI-21817019; Score: 0.53
DE  Interaction: Q9H0E9; IntAct: EBI-21817019; Score: 0.35
DE  Interaction: Q96L91; IntAct: EBI-21817019; Score: 0.53
DE  Interaction: Q52LR7; IntAct: EBI-21817019; Score: 0.53
DE  Interaction: Q05BQ5; IntAct: EBI-21817019; Score: 0.53
DE  Interaction: P23921; IntAct: EBI-21817019; Score: 0.35
DE  Interaction: Q9BZS1; IntAct: EBI-15626922; Score: 0.40
DE  Interaction: P04198; IntAct: EBI-15670804; Score: 0.35
DE  Interaction: P03966; IntAct: EBI-15670865; Score: 0.40
DE  Interaction: Q92804; IntAct: EBI-15705327; Score: 0.52
DE  Interaction: P35637; IntAct: EBI-15705501; Score: 0.52
DE  Interaction: Q01844; IntAct: EBI-15705629; Score: 0.52
DE  Interaction: P03372; IntAct: EBI-15953345; Score: 0.52
DE  Interaction: Q96GD4; IntAct: EBI-16194767; Score: 0.60
DE  Interaction: Q13422; IntAct: EBI-21269412; Score: 0.37
DE  Interaction: Q9BYV2; IntAct: EBI-21271700; Score: 0.37
DE  Interaction: P0C0S5; IntAct: EBI-20795364; Score: 0.53
DE  Interaction: Q9BTT0; IntAct: EBI-21001557; Score: 0.40
DE  Interaction: Q9NX40; IntAct: EBI-20937860; Score: 0.40
DE  Interaction: Q9ULK4; IntAct: EBI-25472569; Score: 0.27
DE  Interaction: P01023; IntAct: EBI-25830111; Score: 0.56
DE  Interaction: P23560; IntAct: EBI-25833106; Score: 0.56
DE  Interaction: P35520; IntAct: EBI-25836738; Score: 0.56
DE  Interaction: G5E9A7; IntAct: EBI-25842556; Score: 0.56
DE  Interaction: P50570; IntAct: EBI-25844908; Score: 0.56
DE  Interaction: P07900; IntAct: EBI-25871998; Score: 0.56
DE  Interaction: P51608; IntAct: EBI-25875914; Score: 0.56
DE  Interaction: D3DTS7; IntAct: EBI-25883086; Score: 0.56
DE  Interaction: Q14114; IntAct: EBI-25903392; Score: 0.56
DE  Interaction: Q9HBH6; IntAct: EBI-25911872; Score: 0.56
DE  Interaction: Q13072; IntAct: EBI-25911888; Score: 0.56
DE  Interaction: P04183; IntAct: EBI-25912178; Score: 0.56
DE  Interaction: Q92481; IntAct: EBI-25912168; Score: 0.56
DE  Interaction: P15884; IntAct: EBI-25912160; Score: 0.56
DE  Interaction: Q13586; IntAct: EBI-25912144; Score: 0.56
DE  Interaction: P56693; IntAct: EBI-25912136; Score: 0.56
DE  Interaction: Q92673; IntAct: EBI-25912128; Score: 0.56
DE  Interaction: Q01105; IntAct: EBI-25912120; Score: 0.56
DE  Interaction: Q99643; IntAct: EBI-25912112; Score: 0.56
DE  Interaction: P18077; IntAct: EBI-25912104; Score: 0.56
DE  Interaction: P62913; IntAct: EBI-25912096; Score: 0.56
DE  Interaction: P07225; IntAct: EBI-25912088; Score: 0.56
DE  Interaction: Q15759; IntAct: EBI-25912080; Score: 0.56
DE  Interaction: Q16342; IntAct: EBI-25912072; Score: 0.56
DE  Interaction: Q2M1J6; IntAct: EBI-25912064; Score: 0.56
DE  Interaction: P00491; IntAct: EBI-25912056; Score: 0.56
DE  Interaction: P49821; IntAct: EBI-25912048; Score: 0.56
DE  Interaction: Q16718; IntAct: EBI-25912040; Score: 0.56
DE  Interaction: P41218; IntAct: EBI-25912032; Score: 0.56
DE  Interaction: P80192; IntAct: EBI-25912024; Score: 0.56
DE  Interaction: P51884; IntAct: EBI-25912016; Score: 0.56
DE  Interaction: P60228; IntAct: EBI-25912008; Score: 0.56
DE  Interaction: P26951; IntAct: EBI-25912000; Score: 0.56
DE  Interaction: P17936; IntAct: EBI-25911992; Score: 0.56
DE  Interaction: P78318; IntAct: EBI-25911984; Score: 0.56
DE  Interaction: Q02363; IntAct: EBI-25911976; Score: 0.56
DE  Interaction: Q03933; IntAct: EBI-25911968; Score: 0.56
DE  Interaction: P09017; IntAct: EBI-25911960; Score: 0.56
DE  Interaction: P52597; IntAct: EBI-25911952; Score: 0.56
DE  Interaction: P19440; IntAct: EBI-25911944; Score: 0.56
DE  Interaction: Q06547; IntAct: EBI-25911936; Score: 0.56
DE  Interaction: P21728; IntAct: EBI-25911920; Score: 0.56
DE  Interaction: P43234; IntAct: EBI-25911912; Score: 0.56
DE  Interaction: P15169; IntAct: EBI-25911904; Score: 0.56
DE  Interaction: Q14032; IntAct: EBI-25911880; Score: 0.56
DE  Interaction: Q15836; IntAct: EBI-25912274; Score: 0.56
DE  Interaction: Q14202; IntAct: EBI-25912266; Score: 0.56
DE  Interaction: O43761; IntAct: EBI-25912258; Score: 0.56
DE  Interaction: P20042; IntAct: EBI-25912242; Score: 0.56
DE  Interaction: Q99598; IntAct: EBI-25912186; Score: 0.56
DE  Interaction: O43292; IntAct: EBI-25912226; Score: 0.56
DE  Interaction: O15535; IntAct: EBI-25912210; Score: 0.56
DE  Interaction: Q15776; IntAct: EBI-25912202; Score: 0.56
DE  Interaction: P62837; IntAct: EBI-25912194; Score: 0.56
DE  Interaction: O95498; IntAct: EBI-25912234; Score: 0.56
DE  Interaction: Q9UL40; IntAct: EBI-25912407; Score: 0.56
DE  Interaction: O14926; IntAct: EBI-25912415; Score: 0.56
DE  Interaction: Q14141; IntAct: EBI-25912390; Score: 0.56
DE  Interaction: Q13573; IntAct: EBI-25912382; Score: 0.56
DE  Interaction: Q9Y4X4; IntAct: EBI-25912374; Score: 0.56
DE  Interaction: Q9UNA4; IntAct: EBI-25912364; Score: 0.56
DE  Interaction: Q96F32; IntAct: EBI-25912356; Score: 0.56
DE  Interaction: O43598; IntAct: EBI-25912348; Score: 0.56
DE  Interaction: Q99828; IntAct: EBI-25912340; Score: 0.56
DE  Interaction: Q92826; IntAct: EBI-25912332; Score: 0.56
DE  Interaction: Q9Y6X2; IntAct: EBI-25912314; Score: 0.56
DE  Interaction: O94844; IntAct: EBI-25912306; Score: 0.56
DE  Interaction: Q9UJD0; IntAct: EBI-25912298; Score: 0.56
DE  Interaction: O95837; IntAct: EBI-25912282; Score: 0.56
DE  Interaction: Q15027; IntAct: EBI-25912290; Score: 0.56
DE  Interaction: Q8TAP6; IntAct: EBI-25912671; Score: 0.56
DE  Interaction: Q8N5Z5; IntAct: EBI-25912661; Score: 0.56
DE  Interaction: Q9BQ24; IntAct: EBI-25912645; Score: 0.56
DE  Interaction: Q9H2C1; IntAct: EBI-25912637; Score: 0.56
DE  Interaction: Q9GZT6; IntAct: EBI-25912629; Score: 0.56
DE  Interaction: Q9ULK6; IntAct: EBI-25912619; Score: 0.56
DE  Interaction: Q05CR2; IntAct: EBI-25912611; Score: 0.56
DE  Interaction: Q96A33; IntAct: EBI-25912603; Score: 0.56
DE  Interaction: Q9Y508; IntAct: EBI-25912595; Score: 0.56
DE  Interaction: Q9NPJ3; IntAct: EBI-25912587; Score: 0.56
DE  Interaction: Q3YEC7; IntAct: EBI-25912577; Score: 0.56
DE  Interaction: Q9NWQ4; IntAct: EBI-25912569; Score: 0.56
DE  Interaction: Q5JUW0; IntAct: EBI-25912561; Score: 0.56
DE  Interaction: Q8N0Y2; IntAct: EBI-25912553; Score: 0.56
DE  Interaction: Q9NWS8; IntAct: EBI-25912545; Score: 0.56
DE  Interaction: Q9NX63; IntAct: EBI-25912537; Score: 0.56
DE  Interaction: Q8IWZ3; IntAct: EBI-25912529; Score: 0.56
DE  Interaction: Q9BRX2; IntAct: EBI-25912521; Score: 0.56
DE  Interaction: Q9NZC7; IntAct: EBI-25912513; Score: 0.56
DE  Interaction: Q9Y576; IntAct: EBI-25912505; Score: 0.56
DE  Interaction: Q9UJA5; IntAct: EBI-25912497; Score: 0.56
DE  Interaction: Q9Y234; IntAct: EBI-25912489; Score: 0.56
DE  Interaction: Q66PJ3; IntAct: EBI-25912479; Score: 0.56
DE  Interaction: Q13033; IntAct: EBI-25912471; Score: 0.56
DE  Interaction: Q9Y5X0; IntAct: EBI-25912463; Score: 0.56
DE  Interaction: Q9H213; IntAct: EBI-25912455; Score: 0.56
DE  Interaction: O95424; IntAct: EBI-25912431; Score: 0.56
DE  Interaction: Q9H8H3; IntAct: EBI-25912423; Score: 0.56
DE  Interaction: O43307; IntAct: EBI-25912399; Score: 0.56
DE  Interaction: Q96I51; IntAct: EBI-25912679; Score: 0.56
DE  Interaction: Q9BYR8; IntAct: EBI-25912687; Score: 0.56
DE  Interaction: Q6PH81; IntAct: EBI-25912831; Score: 0.56
DE  Interaction: Q8N7T0; IntAct: EBI-25912823; Score: 0.56
DE  Interaction: Q8WV41; IntAct: EBI-25912807; Score: 0.56
DE  Interaction: A0JLT2; IntAct: EBI-25912799; Score: 0.56
DE  Interaction: Q7Z7K6; IntAct: EBI-25912791; Score: 0.56
DE  Interaction: Q6P1J6; IntAct: EBI-25912783; Score: 0.56
DE  Interaction: Q96NE9; IntAct: EBI-25912767; Score: 0.56
DE  Interaction: Q8IVH2; IntAct: EBI-25912759; Score: 0.56
DE  Interaction: Q969K7; IntAct: EBI-25912751; Score: 0.56
DE  Interaction: Q96FT9; IntAct: EBI-25912743; Score: 0.56
DE  Interaction: Q96J88; IntAct: EBI-25912735; Score: 0.56
DE  Interaction: Q96HJ3; IntAct: EBI-25912727; Score: 0.56
DE  Interaction: Q86T03; IntAct: EBI-25912719; Score: 0.56
DE  Interaction: Q96GV9; IntAct: EBI-25912711; Score: 0.56
DE  Interaction: Q8NB14; IntAct: EBI-25912703; Score: 0.56
DE  Interaction: Q8N983; IntAct: EBI-25912695; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25931616; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25939229; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25944742; Score: 0.56
DE  Interaction: Q99986; IntAct: EBI-26434632; Score: 0.65
DE  Interaction: Q99816; IntAct: EBI-30840043; Score: 0.44
DE  Interaction: Q99607; IntAct: EBI-29014893; Score: 0.27
DE  Interaction: P41235; IntAct: EBI-29017068; Score: 0.27
DE  Interaction: Q99612; IntAct: EBI-29018743; Score: 0.27
DE  Interaction: O95600; IntAct: EBI-29018812; Score: 0.27
DE  Interaction: P01106; IntAct: EBI-29661630; Score: 0.27
DE  Interaction: P25490; IntAct: EBI-29795992; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0000776;
GO  GO:0097431;
GO  GO:0035267;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0000786;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032777;
GO  GO:0000812;
GO  GO:0005667;
GO  GO:0016407;
GO  GO:0003682;
GO  GO:0140297;
GO  GO:0043998;
GO  GO:0004402;
GO  GO:0043999;
GO  GO:0046972;
GO  GO:0042393;
GO  GO:0046872;
GO  GO:0106226;
GO  GO:0140065;
GO  GO:0140064;
GO  GO:0061733;
GO  GO:0003713;
GO  GO:0003712;
GO  GO:0006915;
GO  GO:0006974;
GO  GO:0071392;
GO  GO:0042149;
GO  GO:0071333;
GO  GO:0090398;
GO  GO:0006978;
GO  GO:0006302;
GO  GO:0000724;
GO  GO:0000132;
GO  GO:0016573;
GO  GO:0043968;
GO  GO:0043967;
GO  GO:0045087;
GO  GO:1905691;
GO  GO:0045892;
GO  GO:0032703;
GO  GO:0000122;
GO  GO:0021915;
GO  GO:0022008;
GO  GO:0006289;
GO  GO:0018394;
GO  GO:1902425;
GO  GO:0010508;
GO  GO:0042753;
GO  GO:0045893;
GO  GO:1905168;
GO  GO:1900051;
GO  GO:0062033;
GO  GO:0045663;
GO  GO:1901985;
GO  GO:0045591;
GO  GO:0045944;
GO  GO:0010867;
GO  GO:0043161;
GO  GO:0042981;
GO  GO:0051726;
GO  GO:2000779;
GO  GO:1902036;
GO  GO:0010212;
GO  GO:0035092;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTK
SQ  NGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPV
SQ  PSETAPASVFPQNGAARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRH
SQ  RLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLA
SQ  KCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTG
SQ  TPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDI
SQ  VDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW
//
ID  Q8CHK4;
PN  Histone acetyltransferase KAT5;
GN  Kat5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:28694333}. Chromosome {ECO:0000250|UniProtKB:Q92993}. Cytoplasm {ECO:0000269|PubMed:28694333}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q92993}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q92993}. Nucleus, nucleolus {ECO:0000269|PubMed:12036595}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92993}. Note=Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region and UV irradiation induces translocation into punctuate subnuclear structures named nuclear bodies (By similarity). Transiently localizes to kinetochores in early mitosis (By similarity). Localizes to spindle poles when chromosomes align during metaphase (By similarity). Localizes in the cytoplasm and nucleus of round spermatids (PubMed:28694333). {ECO:0000250|UniProtKB:Q92993, ECO:0000269|PubMed:28694333}.
DR  UNIPROT: Q8CHK4;
DR  UNIPROT: A0A494B9U8;
DR  UNIPROT: A1L394;
DR  UNIPROT: Q3YFI9;
DR  UNIPROT: Q8CGZ3;
DR  UNIPROT: Q8CGZ4;
DR  UNIPROT: Q8VIH0;
DR  Pfam: PF01853;
DR  Pfam: PF11717;
DR  Pfam: PF17772;
DR  PROSITE: PS51726;
DE  Function: Catalytic subunit of the NuA4 histone acetyltransferase complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H2A and H4 (PubMed:28694333, PubMed:30297459, PubMed:32542325). Histone acetylation alters nucleosome-DNA interactions and promotes interaction of the modified histones with other proteins which positively regulate transcription (By similarity). The NuA4 histone acetyltransferase complex is required for the activation of transcriptional programs associated with proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (PubMed:17728759). The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) by promoting homologous recombination (HR): the complex inhibits TP53BP1 binding to chromatin via MBTD1, which recognizes and binds histone H4 trimethylated at 'Lys-20' (H4K20me), and KAT5 that catalyzes acetylation of 'Lys-15' of histone H2A (H2AK15ac), thereby blocking the ubiquitination mark required for TP53BP1 localization at DNA breaks (PubMed:30297459). Also involved in DSB repair by mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac), promoting NBN/NBS1 assembly at the sites of DNA damage (By similarity). The NuA4 complex plays a key role in hematopoietic stem cell maintenance and is required to maintain acetylated H2A.Z/H2AZ1 at MYC target genes (PubMed:32542325). The NuA4 complex is also required for spermatid development by promoting acetylation of histones: histone hyperacetylation is required for histone replacement during the transition from round to elongating spermatids (PubMed:28694333). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (By similarity). Also acetylates non-histone proteins, such as ARNTL/BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF, LPIN1, NDC80/HEC1, NR1D2, RAN, SOX4, FOXP3, ULK1 and RUBCNL/Pacer (PubMed:22539723, PubMed:24835996, PubMed:31294688). Directly acetylates and activates ATM (By similarity). Promotes nucleotide excision repair (NER) by mediating acetylation of ERCC4/XPF, thereby promoting formation of the ERCC4-ERCC1 complex (By similarity). Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2 (By similarity). Acts as a regulator of regulatory T-cells (Treg) by catalyzing FOXP3 acetylation, thereby promoting FOXP3 transcriptional repressor activity (PubMed:24835996). Involved in skeletal myoblast differentiation by mediating acetylation of SOX4 (PubMed:26291311). Catalyzes acetylation of APBB1/FE65, increasing its transcription activator activity (By similarity). Promotes transcription elongation during the activation phase of the circadian cycle by catalyzing acetylation of ARNTL/BMAL1, promoting elongation of circadian transcripts (PubMed:31294688). Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:22539723). Acts as a regulator of the cGAS-STING innate antiviral response by catalyzing acetylation the N-terminus of CGAS, thereby promoting CGAS DNA-binding and activation (By similarity). Also regulates lipid metabolism by mediating acetylation of CHKA or LPIN1 (PubMed:29765047). Promotes lipolysis of lipid droplets following glucose deprivation by mediating acetylation of isoform 1 of CHKA, thereby promoting monomerization of CHKA and its conversion into a tyrosine-protein kinase (By similarity). Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of LPIN1, thereby promoting the synthesis of diacylglycerol (PubMed:29765047). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) and 2- hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to mediate protein crotonylation and 2-hydroxyisobutyrylation, respectively (By similarity). Acts as a key regulator of chromosome segregation and kinetochore-microtubule attachment during mitosis by mediating acetylation or crotonylation of target proteins (By similarity). Catalyzes acetylation of AURKB at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis (By similarity). Acetylates RAN during mitosis, promoting microtubule assembly at mitotic chromosomes (By similarity). Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore-microtubule attachment (By similarity). Catalyzes crotonylation of MAPRE1/EB1, thereby ensuring accurate spindle positioning in mitosis (By similarity). {ECO:0000250|UniProtKB:Q92993, ECO:0000269|PubMed:17728759, ECO:0000269|PubMed:22539723, ECO:0000269|PubMed:24835996, ECO:0000269|PubMed:26291311, ECO:0000269|PubMed:28694333, ECO:0000269|PubMed:29765047, ECO:0000269|PubMed:30297459, ECO:0000269|PubMed:31294688, ECO:0000269|PubMed:32542325}.
DE  Reference Proteome: Yes;
DE  Interaction: P54254; IntAct: EBI-1170000; Score: 0.40
DE  Interaction: P54253; IntAct: EBI-1170016; Score: 0.40
DE  Interaction: Q6ZPV5; IntAct: EBI-7225941; Score: 0.40
DE  Interaction: P28574; IntAct: EBI-2942690; Score: 0.46
DE  Interaction: Q9JI44; IntAct: EBI-2942815; Score: 0.46
DE  Interaction: P06151; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: P51859; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: Q80YV3; IntAct: EBI-2942957; Score: 0.46
DE  Interaction: Q8CHI8; IntAct: EBI-2942957; Score: 0.46
DE  Interaction: Q8WTY4; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: Q8R3B7; IntAct: EBI-2942957; Score: 0.46
DE  Interaction: P60762; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: P63268; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: Q9Z2N8; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: P63260; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: Q8VEK6; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: Q15906; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: Q8C9X6; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: Q8C0I4; IntAct: EBI-2942957; Score: 0.35
DE  Interaction: P01108; IntAct: EBI-2943518; Score: 0.35
DE  Interaction: Q3SYK5; IntAct: EBI-4370296; Score: 0.40
DE  Interaction: P0C0S6; IntAct: EBI-6667063; Score: 0.35
DE  Interaction: P35583; IntAct: EBI-6667070; Score: 0.35
DE  Interaction: P49452; IntAct: EBI-20739126; Score: 0.37
DE  Interaction: Q5F2C3; IntAct: EBI-20739344; Score: 0.37
DE  Interaction: O88495; IntAct: EBI-21227879; Score: 0.54
DE  Interaction: P60122; IntAct: EBI-26898362; Score: 0.35
DE  Interaction: Q9Y230; IntAct: EBI-26898451; Score: 0.35
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0000776;
GO  GO:0097431;
GO  GO:0035267;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0000786;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032777;
GO  GO:0032991;
GO  GO:0000812;
GO  GO:0005667;
GO  GO:0003682;
GO  GO:0140297;
GO  GO:0043998;
GO  GO:0004402;
GO  GO:0043999;
GO  GO:0046972;
GO  GO:0042393;
GO  GO:0046872;
GO  GO:0106226;
GO  GO:0140065;
GO  GO:0140064;
GO  GO:0061733;
GO  GO:0043274;
GO  GO:0044877;
GO  GO:0003713;
GO  GO:0003712;
GO  GO:0006915;
GO  GO:0006974;
GO  GO:0071392;
GO  GO:0042149;
GO  GO:0071333;
GO  GO:0006978;
GO  GO:0006302;
GO  GO:0000724;
GO  GO:0000132;
GO  GO:0016573;
GO  GO:0043968;
GO  GO:0043967;
GO  GO:0045087;
GO  GO:1905691;
GO  GO:0045892;
GO  GO:0032703;
GO  GO:0000122;
GO  GO:0021915;
GO  GO:0022008;
GO  GO:0006289;
GO  GO:0018394;
GO  GO:1902425;
GO  GO:0010508;
GO  GO:0042753;
GO  GO:0045893;
GO  GO:1905168;
GO  GO:1900051;
GO  GO:0062033;
GO  GO:0045663;
GO  GO:1901985;
GO  GO:0045591;
GO  GO:0045944;
GO  GO:0010867;
GO  GO:0043161;
GO  GO:0006473;
GO  GO:0042981;
GO  GO:0051726;
GO  GO:1902275;
GO  GO:2000779;
GO  GO:1902036;
GO  GO:0006357;
GO  GO:0010212;
GO  GO:0035092;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTK
SQ  NGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPV
SQ  PSETAPASVFPQNGSARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRH
SQ  RLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLA
SQ  KCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTG
SQ  TPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDI
SQ  VDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW
//
ID  Q5RBG4;
PN  Histone acetyltransferase KAT5;
GN  KAT5;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q92993}. Chromosome {ECO:0000250|UniProtKB:Q92993}. Cytoplasm {ECO:0000250|UniProtKB:Q92993}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q92993}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q92993}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92993}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92993}. Note=Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region and UV irradiation induces translocation into punctuate subnuclear structures named nuclear bodies. Transiently localizes to kinetochores in early mitosis. Localizes to spindle poles when chromosomes align during metaphase (By similarity). Localizes in the cytoplasm and nucleus of round spermatids (By similarity). {ECO:0000250|UniProtKB:Q8CHK4, ECO:0000250|UniProtKB:Q92993}.
DR  UNIPROT: Q5RBG4;
DR  Pfam: PF01853;
DR  Pfam: PF11717;
DR  Pfam: PF17772;
DR  PROSITE: PS51726;
DE  Function: Catalytic subunit of the NuA4 histone acetyltransferase complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H2A and H4. Histone acetylation alters nucleosome-DNA interactions and promotes interaction of the modified histones with other proteins which positively regulate transcription. The NuA4 histone acetyltransferase complex is required for the activation of transcriptional programs associated with proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) by promoting homologous recombination (HR): the complex inhibits TP53BP1 binding to chromatin via MBTD1, which recognizes and binds histone H4 trimethylated at 'Lys- 20' (H4K20me), and KAT5 that catalyzes acetylation of 'Lys-15' of histone H2A (H2AK15ac), thereby blocking the ubiquitination mark required for TP53BP1 localization at DNA breaks. Also involved in DSB repair by mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac), promoting NBN/NBS1 assembly at the sites of DNA damage (By similarity). The NuA4 complex plays a key role in hematopoietic stem cell maintenance and is required to maintain acetylated H2A.Z/H2AZ1 at MYC target genes. The NuA4 complex is also required for spermatid development by promoting acetylation of histones: histone hyperacetylation is required for histone replacement during the transition from round to elongating spermatids (By similarity). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome. Also acetylates non-histone proteins, such as ARNTL/BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF, LPIN1, NDC80/HEC1, NR1D2, RAN, SOX4, FOXP3, ULK1 and RUBCNL/Pacer. Directly acetylates and activates ATM. Promotes nucleotide excision repair (NER) by mediating acetylation of ERCC4/XPF, thereby promoting formation of the ERCC4-ERCC1 complex. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2. Acts as a regulator of regulatory T-cells (Treg) by catalyzing FOXP3 acetylation, thereby promoting FOXP3 transcriptional repressor activity. Involved in skeletal myoblast differentiation by mediating acetylation of SOX4. Catalyzes acetylation of APBB1/FE65, increasing its transcription activator activity (By similarity). Promotes transcription elongation during the activation phase of the circadian cycle by catalyzing acetylation of ARNTL/BMAL1, promoting elongation of circadian transcripts (By similarity). Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer. Acts as a regulator of the cGAS-STING innate antiviral response by catalyzing acetylation the N-terminus of CGAS, thereby promoting CGAS DNA-binding and activation. Also regulates lipid metabolism by mediating acetylation of CHKA or LPIN1. Promotes lipolysis of lipid droplets following glucose deprivation by mediating acetylation of isoform 1 of CHKA, thereby promoting monomerization of CHKA and its conversion into a tyrosine-protein kinase. Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of LPIN1, thereby promoting the synthesis of diacylglycerol. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) and 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to mediate protein crotonylation and 2-hydroxyisobutyrylation, respectively. Acts as a key regulator of chromosome segregation and kinetochore-microtubule attachment during mitosis by mediating acetylation or crotonylation of target proteins. Catalyzes acetylation of AURKB at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis. Acetylates RAN during mitosis, promoting microtubule assembly at mitotic chromosomes. Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore- microtubule attachment. Catalyzes crotonylation of MAPRE1/EB1, thereby ensuring accurate spindle positioning in mitosis (By similarity). {ECO:0000250|UniProtKB:Q8CHK4, ECO:0000250|UniProtKB:Q92993}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0035267;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032777;
GO  GO:0000922;
GO  GO:0000812;
GO  GO:0003682;
GO  GO:0043998;
GO  GO:0004402;
GO  GO:0046872;
GO  GO:0106226;
GO  GO:0140065;
GO  GO:0140064;
GO  GO:0061733;
GO  GO:0003713;
GO  GO:0006974;
GO  GO:0042149;
GO  GO:0006325;
GO  GO:0006978;
GO  GO:0006302;
GO  GO:0000724;
GO  GO:0000132;
GO  GO:0045087;
GO  GO:1905691;
GO  GO:0006289;
GO  GO:0018394;
GO  GO:1902425;
GO  GO:0010508;
GO  GO:0042753;
GO  GO:0045893;
GO  GO:1905168;
GO  GO:1900051;
GO  GO:0062033;
GO  GO:0045663;
GO  GO:0045591;
GO  GO:0045944;
GO  GO:0010867;
GO  GO:1902036;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTK
SQ  NGLPGSRPGSPEREVKRKVEVVSPATPVPSETAPASVFPQNGAARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRM
SQ  TGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNE
SQ  IYRKGTISFFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILT
SQ  LPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKK
SQ  EDVISTLQYLNLINYYKGQYILTLSEDIVDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW
//
ID  Q99MK2;
PN  Histone acetyltransferase KAT5;
GN  Kat5;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q92993}. Chromosome {ECO:0000250|UniProtKB:Q92993}. Cytoplasm {ECO:0000250|UniProtKB:Q92993}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q92993}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q92993}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92993}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92993}. Note=Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region and UV irradiation induces translocation into punctuate subnuclear structures named nuclear bodies. Transiently localizes to kinetochores in early mitosis. Localizes to spindle poles when chromosomes align during metaphase (By similarity). Localizes in the cytoplasm and nucleus of round spermatids (By similarity). {ECO:0000250|UniProtKB:Q8CHK4, ECO:0000250|UniProtKB:Q92993}.
DR  UNIPROT: Q99MK2;
DR  UNIPROT: Q5XI16;
DR  Pfam: PF01853;
DR  Pfam: PF11717;
DR  Pfam: PF17772;
DR  PROSITE: PS51726;
DE  Function: Catalytic subunit of the NuA4 histone acetyltransferase complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H2A and H4. Histone acetylation alters nucleosome-DNA interactions and promotes interaction of the modified histones with other proteins which positively regulate transcription. The NuA4 histone acetyltransferase complex is required for the activation of transcriptional programs associated with proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) by promoting homologous recombination (HR): the complex inhibits TP53BP1 binding to chromatin via MBTD1, which recognizes and binds histone H4 trimethylated at 'Lys- 20' (H4K20me), and KAT5 that catalyzes acetylation of 'Lys-15' of histone H2A (H2AK15ac), thereby blocking the ubiquitination mark required for TP53BP1 localization at DNA breaks. Also involved in DSB repair by mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac), promoting NBN/NBS1 assembly at the sites of DNA damage (By similarity). The NuA4 complex plays a key role in hematopoietic stem cell maintenance and is required to maintain acetylated H2A.Z/H2AZ1 at MYC target genes. The NuA4 complex is also required for spermatid development by promoting acetylation of histones: histone hyperacetylation is required for histone replacement during the transition from round to elongating spermatids (By similarity). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome. Also acetylates non-histone proteins, such as ARNTL/BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF, LPIN1, NDC80/HEC1, NR1D2, RAN, SOX4, FOXP3, ULK1 and RUBCNL/Pacer. Directly acetylates and activates ATM. Promotes nucleotide excision repair (NER) by mediating acetylation of ERCC4/XPF, thereby promoting formation of the ERCC4-ERCC1 complex. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2. Acts as a regulator of regulatory T-cells (Treg) by catalyzing FOXP3 acetylation, thereby promoting FOXP3 transcriptional repressor activity. Involved in skeletal myoblast differentiation by mediating acetylation of SOX4. Catalyzes acetylation of APBB1/FE65, increasing its transcription activator activity (By similarity). Promotes transcription elongation during the activation phase of the circadian cycle by catalyzing acetylation of ARNTL/BMAL1, promoting elongation of circadian transcripts (By similarity). Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer. Acts as a regulator of the cGAS-STING innate antiviral response by catalyzing acetylation the N-terminus of CGAS, thereby promoting CGAS DNA-binding and activation. Also regulates lipid metabolism by mediating acetylation of CHKA or LPIN1. Promotes lipolysis of lipid droplets following glucose deprivation by mediating acetylation of isoform 1 of CHKA, thereby promoting monomerization of CHKA and its conversion into a tyrosine-protein kinase. Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of LPIN1, thereby promoting the synthesis of diacylglycerol. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) and 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to mediate protein crotonylation and 2-hydroxyisobutyrylation, respectively. Acts as a key regulator of chromosome segregation and kinetochore-microtubule attachment during mitosis by mediating acetylation or crotonylation of target proteins. Catalyzes acetylation of AURKB at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis. Acetylates RAN during mitosis, promoting microtubule assembly at mitotic chromosomes. Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore- microtubule attachment. Catalyzes crotonylation of MAPRE1/EB1, thereby ensuring accurate spindle positioning in mitosis (By similarity). {ECO:0000250|UniProtKB:Q8CHK4, ECO:0000250|UniProtKB:Q92993}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0097431;
GO  GO:0035267;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0000786;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032777;
GO  GO:0032991;
GO  GO:0000812;
GO  GO:0005667;
GO  GO:0003682;
GO  GO:0140297;
GO  GO:0043998;
GO  GO:0004402;
GO  GO:0043999;
GO  GO:0046972;
GO  GO:0042393;
GO  GO:0046872;
GO  GO:0106226;
GO  GO:0140065;
GO  GO:0140064;
GO  GO:0061733;
GO  GO:0043274;
GO  GO:0044877;
GO  GO:0003713;
GO  GO:0003712;
GO  GO:0006915;
GO  GO:0006974;
GO  GO:0071392;
GO  GO:0042149;
GO  GO:0071333;
GO  GO:0070301;
GO  GO:0071481;
GO  GO:0006978;
GO  GO:0006302;
GO  GO:0000724;
GO  GO:0000132;
GO  GO:0016573;
GO  GO:0043968;
GO  GO:0043967;
GO  GO:0045087;
GO  GO:1905691;
GO  GO:0045892;
GO  GO:0032703;
GO  GO:0000122;
GO  GO:0021915;
GO  GO:0022008;
GO  GO:0006289;
GO  GO:0018394;
GO  GO:1902425;
GO  GO:0010508;
GO  GO:0042753;
GO  GO:0045893;
GO  GO:1905168;
GO  GO:1900051;
GO  GO:0062033;
GO  GO:0045663;
GO  GO:1901985;
GO  GO:0045591;
GO  GO:0045944;
GO  GO:0010867;
GO  GO:0043161;
GO  GO:0006473;
GO  GO:0051726;
GO  GO:1902036;
GO  GO:0006357;
GO  GO:0009408;
GO  GO:0010212;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTK
SQ  NGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPV
SQ  PSETAPASVFPQNGSARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRH
SQ  RLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLA
SQ  KCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTG
SQ  TPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDI
SQ  VDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW
//
ID  P39962;
PN  Casein kinase I homolog 3;
GN  YCK3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane; Lipid-anchor; Cytoplasmic side. Nucleus membrane; Lipid-anchor; Cytoplasmic side. Vacuole membrane; Lipid-anchor; Cytoplasmic side. Note=Targeting to the vacuolar membrane may depend on AP-3 pathway.
DR  UNIPROT: P39962;
DR  UNIPROT: D3DM29;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
DE  Reference Proteome: Yes;
DE  Interaction: P53953; IntAct: EBI-2614274; Score: 0.35
DE  Interaction: Q12292; IntAct: EBI-2614274; Score: 0.35
DE  Interaction: P09440; IntAct: EBI-2614274; Score: 0.35
DE  Interaction: P08431; IntAct: EBI-2614274; Score: 0.35
DE  Interaction: P50222; IntAct: EBI-11530204; Score: 0.56
DE  Interaction: P23291; IntAct: EBI-16286993; Score: 0.35
DE  Interaction: P39109; IntAct: EBI-20800580; Score: 0.49
GO  GO:0005737;
GO  GO:0000324;
GO  GO:0000329;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0006897;
GO  GO:0018105;
GO  GO:0007165;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:14668479};
SQ  MSQRSSQHIVGIHYAVGPKIGEGSFGVIFEGENILHSCQAQTGSKRDSSIIMANEPVAIKFEPRHSDAPQLRDEFRAYRI
SQ  LNGCVGIPHAYYFGQEGMHNILIIDLLGPSLEDLFEWCGRKFSVKTTCMVAKQMIDRVRAIHDHDLIYRDIKPDNFLISQ
SQ  YQRISPEGKVIKSCASSSNNDPNLIYMVDFGMAKQYRDPRTKQHIPYRERKSLSGTARYMSINTHFGREQSRRDDLESLG
SQ  HVFFYFLRGSLPWQGLKAPNNKLKYEKIGMTKQKLNPDDLLLNNAIPYQFATYLKYARSLKFDEDPDYDYLISLMDDALR
SQ  LNDLKDDGHYDWMDLNGGKGWNIKINRRANLHGYGNPNPRVNGNTARNNVNTNSKTRNTTPVATPKQQAQNSYNKDNSKS
SQ  RISSNPQSFTKQQHVLKKIEPNSKYIPETHSNLQRPIKSQSQTYDSISHTQNSPFVPYSSSKANPKRSNNEHNLPNHYTN
SQ  LANKNINYQSQRNYEQENDAYSDDENDTFCSKIYKYCCCCFCCC
//
ID  P35508;
PN  Casein kinase I isoform delta;
GN  CSNK1D;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity (By similarity). {ECO:0000250}.
DR  UNIPROT: P35508;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down- regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate (By similarity). {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q9DC28}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000139;
GO  GO:0005815;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005876;
GO  GO:0005524;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0050321;
GO  GO:0032922;
GO  GO:1905515;
GO  GO:0018105;
GO  GO:0090263;
GO  GO:0032436;
GO  GO:0006468;
GO  GO:0042752;
GO  GO:0007165;
GO  GO:0051225;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVM
SQ  VMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDAR
SQ  THQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVL
SQ  CKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRN
SQ  PATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQI
SQ  PGRVASSGLQSVVHR
//
ID  P48730;
PN  Casein kinase I isoform delta;
GN  CSNK1D;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, perinuclear region. Cell membrane. Cytoplasm, cytoskeleton, spindle. Golgi apparatus. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity.
DR  UNIPROT: P48730;
DR  UNIPROT: A2I2P2;
DR  UNIPROT: Q96KZ6;
DR  UNIPROT: Q9BTN5;
DR  PDB: 3UYS;
DR  PDB: 3UYT;
DR  PDB: 3UZP;
DR  PDB: 4HGT;
DR  PDB: 4HNF;
DR  PDB: 4KB8;
DR  PDB: 4KBA;
DR  PDB: 4KBC;
DR  PDB: 4KBK;
DR  PDB: 4TN6;
DR  PDB: 4TW9;
DR  PDB: 4TWC;
DR  PDB: 5IH4;
DR  PDB: 5IH5;
DR  PDB: 5IH6;
DR  PDB: 5MQV;
DR  PDB: 5OKT;
DR  PDB: 5W4W;
DR  PDB: 6F1W;
DR  PDB: 6F26;
DR  PDB: 6GZM;
DR  PDB: 6HMP;
DR  PDB: 6HMR;
DR  PDB: 6PXN;
DR  PDB: 6PXO;
DR  PDB: 6PXP;
DR  PDB: 6RCG;
DR  PDB: 6RCH;
DR  PDB: 6RU6;
DR  PDB: 6RU7;
DR  PDB: 6RU8;
DR  PDB: 7P7F;
DR  PDB: 7P7G;
DR  PDB: 7P7H;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 600864;
DR  OMIM: 615224;
DR  DisGeNET: 1453;
DE  Function: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down- regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate. {ECO:0000250|UniProtKB:Q9DC28, ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16027726, ECO:0000269|PubMed:17562708, ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:19043076, ECO:0000269|PubMed:20041275, ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:20407760, ECO:0000269|PubMed:20637175, ECO:0000269|PubMed:20696890, ECO:0000269|PubMed:20699359, ECO:0000269|PubMed:21084295, ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:23636092}.
DE  Disease: Advanced sleep phase syndrome, familial, 2 (FASPS2) [MIM:615224]: A disorder characterized by very early sleep onset and offset. Individuals are 'morning larks' with a 4 hours advance of the sleep, temperature and melatonin rhythms. {ECO:0000269|PubMed:15800623, ECO:0000269|PubMed:23636092}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O15027; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: O15055; IntAct: EBI-24428236; Score: 0.68
DE  Interaction: P35240; IntAct: EBI-25878153; Score: 0.56
DE  Interaction: Q92997; IntAct: EBI-759547; Score: 0.67
DE  Interaction: P23508; IntAct: EBI-28935490; Score: 0.56
DE  Interaction: P78396; IntAct: EBI-1065642; Score: 0.00
DE  Interaction: Q15796; IntAct: EBI-2695978; Score: 0.40
DE  Interaction: P84022; IntAct: EBI-25839846; Score: 0.56
DE  Interaction: A0A2U2GXH6; IntAct: EBI-2847037; Score: 0.00
DE  Interaction: Q00987; IntAct: EBI-2910627; Score: 0.61
DE  Interaction: Q8IYT8; IntAct: EBI-3622897; Score: 0.35
DE  Interaction: Q96RY5; IntAct: EBI-7129036; Score: 0.37
DE  Interaction: O95758; IntAct: EBI-7851121; Score: 0.35
DE  Interaction: Q9JIY2; IntAct: EBI-7646605; Score: 0.35
DE  Interaction: P48729; IntAct: EBI-6255977; Score: 0.53
DE  Interaction: P49674; IntAct: EBI-6256083; Score: 0.35
DE  Interaction: Q60838; IntAct: EBI-7886728; Score: 0.44
DE  Interaction: P04637; IntAct: EBI-6595015; Score: 0.27
DE  Interaction: P56817; IntAct: EBI-6595322; Score: 0.27
DE  Interaction: P37840; IntAct: EBI-25940591; Score: 0.56
DE  Interaction: Q8IUH5; IntAct: EBI-9087880; Score: 0.51
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: Q96LR2; IntAct: EBI-10210505; Score: 0.61
DE  Interaction: Q9C026; IntAct: EBI-10210535; Score: 0.56
DE  Interaction: Q5S007; IntAct: EBI-25987321; Score: 0.56
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q07866; IntAct: EBI-11004416; Score: 0.35
DE  Interaction: P97784; IntAct: EBI-11034076; Score: 0.35
DE  Interaction: D6RFU6; IntAct: EBI-11044384; Score: 0.35
DE  Interaction: O15169; IntAct: EBI-11057858; Score: 0.35
DE  Interaction: Q66JX5; IntAct: EBI-11072722; Score: 0.35
DE  Interaction: Q6ZRV2; IntAct: EBI-11087735; Score: 0.53
DE  Interaction: P51398; IntAct: EBI-11129856; Score: 0.35
DE  Interaction: P31323; IntAct: EBI-11146630; Score: 0.53
DE  Interaction: Q8BSA9; IntAct: EBI-11150193; Score: 0.35
DE  Interaction: Q15154; IntAct: EBI-11362583; Score: 0.57
DE  Interaction: Q6ZU80; IntAct: EBI-11370150; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q5T7W0; IntAct: EBI-24303069; Score: 0.56
DE  Interaction: Q6PGQ1; IntAct: EBI-24499675; Score: 0.56
DE  Interaction: O75382; IntAct: EBI-24386661; Score: 0.56
DE  Interaction: Q49A88; IntAct: EBI-24404075; Score: 0.56
DE  Interaction: Q9H2S9; IntAct: EBI-24421056; Score: 0.56
DE  Interaction: Q96BR9; IntAct: EBI-24421640; Score: 0.56
DE  Interaction: Q9BRK4; IntAct: EBI-24456715; Score: 0.56
DE  Interaction: Q9P286; IntAct: EBI-24458001; Score: 0.56
DE  Interaction: O60447; IntAct: EBI-24459342; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q9Y698; IntAct: EBI-21523302; Score: 0.35
DE  Interaction: Q9GZY0; IntAct: EBI-21528397; Score: 0.35
DE  Interaction: Q9UF02; IntAct: EBI-21554221; Score: 0.35
DE  Interaction: O75695; IntAct: EBI-21661543; Score: 0.35
DE  Interaction: Q9H063; IntAct: EBI-21704986; Score: 0.35
DE  Interaction: Q99996; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q5VU43; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: O75330; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q9Y343; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q9UIM3; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q9NUW8; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q9H4H8; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q8WVL7; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q8TC76; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q7Z7G8; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q6PEV8; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q49AN0; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q16526; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q14C86; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: O15534; IntAct: EBI-21737245; Score: 0.35
DE  Interaction: Q8WWF3; IntAct: EBI-21811588; Score: 0.35
DE  Interaction: P23468; IntAct: EBI-16363467; Score: 0.44
DE  Interaction: Q62000; IntAct: EBI-26896836; Score: 0.44
DE  Interaction: Q13158; IntAct: EBI-20736966; Score: 0.35
DE  Interaction: Q9Y6K9; IntAct: EBI-20737021; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: Q8NFZ5; IntAct: EBI-20738016; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: Q86UY5; IntAct: EBI-21993597; Score: 0.35
DE  Interaction: Q5T0W9; IntAct: EBI-21993614; Score: 0.53
DE  Interaction: Q2M2I3; IntAct: EBI-21993651; Score: 0.35
DE  Interaction: A6ND36; IntAct: EBI-25466555; Score: 0.40
DE  Interaction: P17813; IntAct: EBI-22197897; Score: 0.35
DE  Interaction: O15530; IntAct: EBI-25375702; Score: 0.35
DE  Interaction: Q5FWK3; IntAct: EBI-25409394; Score: 0.35
DE  Interaction: Q9UNA1; IntAct: EBI-25412137; Score: 0.35
DE  Interaction: O60563; IntAct: EBI-25477219; Score: 0.35
DE  Interaction: O76071; IntAct: EBI-25477658; Score: 0.35
DE  Interaction: O94992; IntAct: EBI-25479174; Score: 0.35
DE  Interaction: P23497; IntAct: EBI-25485215; Score: 0.35
DE  Interaction: P25098; IntAct: EBI-25830618; Score: 0.56
DE  Interaction: P50454; IntAct: EBI-25836405; Score: 0.56
DE  Interaction: Q03135; IntAct: EBI-25836381; Score: 0.56
DE  Interaction: P06850; IntAct: EBI-25838892; Score: 0.56
DE  Interaction: Q8IU99; IntAct: EBI-25839938; Score: 0.56
DE  Interaction: Q96GW7; IntAct: EBI-25839930; Score: 0.56
DE  Interaction: Q96L34; IntAct: EBI-25839920; Score: 0.56
DE  Interaction: Q9NRS4; IntAct: EBI-25839912; Score: 0.56
DE  Interaction: Q9UBQ0; IntAct: EBI-25839904; Score: 0.56
DE  Interaction: Q9BS26; IntAct: EBI-25839896; Score: 0.56
DE  Interaction: Q9BVJ6; IntAct: EBI-25839888; Score: 0.56
DE  Interaction: Q92624; IntAct: EBI-25839880; Score: 0.56
DE  Interaction: O14494; IntAct: EBI-25839872; Score: 0.56
DE  Interaction: Q8IUQ4; IntAct: EBI-25839862; Score: 0.56
DE  Interaction: P07602; IntAct: EBI-25839854; Score: 0.56
DE  Interaction: Q16539; IntAct: EBI-25839838; Score: 0.56
DE  Interaction: Q8WTV0; IntAct: EBI-25839830; Score: 0.56
DE  Interaction: Q01658; IntAct: EBI-25845573; Score: 0.56
DE  Interaction: P17302; IntAct: EBI-25858946; Score: 0.56
DE  Interaction: Q00403; IntAct: EBI-25865067; Score: 0.56
DE  Interaction: D3DTS7; IntAct: EBI-25882682; Score: 0.56
DE  Interaction: P17612; IntAct: EBI-25884585; Score: 0.56
DE  Interaction: P54725; IntAct: EBI-25889335; Score: 0.56
DE  Interaction: P04271; IntAct: EBI-25891005; Score: 0.56
DE  Interaction: P37173; IntAct: EBI-25892565; Score: 0.56
DE  Interaction: Q14114; IntAct: EBI-25903352; Score: 0.56
DE  Interaction: Q9Y5Q9; IntAct: EBI-25906914; Score: 0.56
DE  Interaction: Q6NUL7; IntAct: EBI-25912869; Score: 0.56
DE  Interaction: Q6ZW49; IntAct: EBI-25914220; Score: 0.56
DE  Interaction: P45973; IntAct: EBI-25917302; Score: 0.56
DE  Interaction: Q9H8Y8; IntAct: EBI-25917935; Score: 0.56
DE  Interaction: P00441; IntAct: EBI-25934753; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25937655; Score: 0.56
DE  Interaction: P35637; IntAct: EBI-25939987; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25943660; Score: 0.56
DE  Interaction: Q13148; IntAct: EBI-25983774; Score: 0.56
DE  Interaction: Q9BYB0; IntAct: EBI-26513965; Score: 0.37
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: Q9UJF2; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q9P2F5; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q9NUJ1; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q9H9T3; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q9H9R9; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q9H3U1; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q9BQ89; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q96L94; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q96GA3; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q96EY7; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q7Z5H3; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q6IA86; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q5T4S7; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q53GT1; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q1W6H9; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q16610; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q15050; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q13895; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q13426; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P82930; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P61964; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P61081; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P54727; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P49917; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P48047; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P30153; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P23258; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P13861; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: O95163; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: A7E2V4; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: A2VDJ0; IntAct: EBI-28935490; Score: 0.35
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0033116;
GO  GO:0005794;
GO  GO:0043005;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0005876;
GO  GO:0005524;
GO  GO:0045296;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0050321;
GO  GO:1990090;
GO  GO:0032922;
GO  GO:0048208;
GO  GO:0007030;
GO  GO:0007020;
GO  GO:1905515;
GO  GO:0018105;
GO  GO:0090263;
GO  GO:2000052;
GO  GO:0032436;
GO  GO:0001934;
GO  GO:1905426;
GO  GO:0071539;
GO  GO:0061512;
GO  GO:0034067;
GO  GO:0006468;
GO  GO:0042752;
GO  GO:0007165;
GO  GO:0051225;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVM
SQ  VMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDAR
SQ  THQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVL
SQ  CKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRN
SQ  PATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQI
SQ  PGRVASSGLQSVVHR
//
ID  Q9DC28;
PN  Casein kinase I isoform delta;
GN  Csnk1d;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:10848614, ECO:0000269|PubMed:17101137, ECO:0000269|PubMed:19414593}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9DC28;
DR  UNIPROT: Q3TZK2;
DR  UNIPROT: Q99KK4;
DR  PDB: 4JJR;
DR  PDB: 5X17;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (PubMed:29191835). EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate. {ECO:0000269|PubMed:10848614, ECO:0000269|PubMed:16014721, ECO:0000269|PubMed:17101137, ECO:0000269|PubMed:19414593, ECO:0000269|PubMed:19948962, ECO:0000269|PubMed:20145109, ECO:0000269|PubMed:20192920, ECO:0000269|PubMed:20421981, ECO:0000269|PubMed:21930935, ECO:0000269|PubMed:29191835}.
DE  Reference Proteome: Yes;
DE  Interaction: O54943; IntAct: EBI-15900328; Score: 0.40
DE  Interaction: Q5U651; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: Q7TN08; IntAct: EBI-6392514; Score: 0.40
DE  Interaction: Q0PHV7; IntAct: EBI-6392534; Score: 0.40
DE  Interaction: P35813; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: Q8WUZ0; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: Q96K37; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: P49674; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: O15534; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: Q8NG31; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: Q15651; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: P13861; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: O75382; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: O00308; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: Q6ZRV2; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: Q14C86; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: P56199; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: Q6YHK3; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: Q9Y343; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: O35973; IntAct: EBI-15900175; Score: 0.40
DE  Interaction: Q3UL36; IntAct: EBI-26888124; Score: 0.35
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0043005;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0005876;
GO  GO:0005524;
GO  GO:0016301;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0050321;
GO  GO:0032922;
GO  GO:0007030;
GO  GO:0007020;
GO  GO:1905515;
GO  GO:0018105;
GO  GO:0090263;
GO  GO:2000052;
GO  GO:0032436;
GO  GO:0001934;
GO  GO:0030177;
GO  GO:1905426;
GO  GO:0071539;
GO  GO:0061512;
GO  GO:0034067;
GO  GO:0006468;
GO  GO:0042752;
GO  GO:0007165;
GO  GO:0051225;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVM
SQ  VMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDAR
SQ  THQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVL
SQ  CKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRN
SQ  PATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNVSSSDLTGRQDTSRMSTSQI
SQ  PGRVASSGLQSVVHR
//
ID  Q5RC72;
PN  Casein kinase I isoform delta;
GN  CSNK1D;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5RC72;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down- regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate (By similarity). {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q9DC28}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0005815;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0005524;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0050321;
GO  GO:0032922;
GO  GO:0032436;
GO  GO:0006468;
GO  GO:0042752;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKPPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVM
SQ  VMELLGPSLEDLFNFCSRKFSLKTILLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDAR
SQ  THQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVL
SQ  CKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRN
SQ  PATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQI
SQ  PGRVASSGLQSVVHR
//
ID  Q06486;
PN  Casein kinase I isoform delta;
GN  Csnk1d;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity (By similarity). {ECO:0000250}.
DR  UNIPROT: Q06486;
DR  UNIPROT: Q99KK4;
DR  PDB: 1CKI;
DR  PDB: 1CKJ;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down- regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate (By similarity). {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q9DC28, ECO:0000269|PubMed:15961172}.
DE  Reference Proteome: Yes;
DE  Interaction: O54943; IntAct: EBI-6145987; Score: 0.00
DE  Interaction: P60192; IntAct: EBI-7089182; Score: 0.27
DE  Interaction: Q9Z266; IntAct: EBI-7088881; Score: 0.51
DE  Interaction: P04637; IntAct: EBI-7089288; Score: 0.44
DE  Interaction: P10636; IntAct: EBI-7089339; Score: 0.44
DE  Interaction: P27816; IntAct: EBI-7089314; Score: 0.44
DE  Interaction: P78559; IntAct: EBI-7089360; Score: 0.44
DE  Interaction: Q00987; IntAct: EBI-2910302; Score: 0.44
DE  Interaction: Q9Y6Q9; IntAct: EBI-5274781; Score: 0.44
DE  Interaction: Q8QG92; IntAct: EBI-6257547; Score: 0.44
DE  Interaction: P09803; IntAct: EBI-6261836; Score: 0.44
DE  Interaction: P22455; IntAct: EBI-22244803; Score: 0.35
GO  GO:0005813;
GO  GO:0036064;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0005876;
GO  GO:0005524;
GO  GO:0016301;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0050321;
GO  GO:1990090;
GO  GO:0032922;
GO  GO:0007030;
GO  GO:0007020;
GO  GO:1905515;
GO  GO:0018105;
GO  GO:0090263;
GO  GO:2000052;
GO  GO:0032436;
GO  GO:0001934;
GO  GO:0030177;
GO  GO:0071539;
GO  GO:0061512;
GO  GO:0034067;
GO  GO:0006468;
GO  GO:0042752;
GO  GO:0007165;
GO  GO:0051225;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVM
SQ  VMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDAR
SQ  THQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVL
SQ  CKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRN
SQ  PATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNVSSSDLTGRQDTSRMSTSQI
SQ  PGRVASSGLQSVVHR
//
ID  O18965;
PN  Potassium voltage-gated channel subfamily H member 1;
GN  KCNH1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:9524140}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Nucleus inner membrane {ECO:0000250|UniProtKB:O95259}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63472}. Cell projection, axon {ECO:0000250|UniProtKB:Q63472}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q63472}. Perikaryon {ECO:0000250|UniProtKB:Q63472}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q63472}. Early endosome membrane {ECO:0000250|UniProtKB:O95259}. Note=Perinuclear KCNH1 is located to NPC-free islands. {ECO:0000250|UniProtKB:O95259}.
DR  UNIPROT: O18965;
DR  UNIPROT: O18966;
DR  Pfam: PF00027;
DR  Pfam: PF00520;
DR  Pfam: PF13426;
DR  PROSITE: PS50042;
DR  PROSITE: PS50113;
DR  PROSITE: PS50112;
DE  Function: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:9524140). Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow- derived mesenchymal stem cells (MSCs) (By similarity). {ECO:0000250|UniProtKB:O95259, ECO:0000269|PubMed:9524140}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0030425;
GO  GO:0031901;
GO  GO:0005887;
GO  GO:0005637;
GO  GO:0043204;
GO  GO:0098839;
GO  GO:0042734;
GO  GO:0008076;
GO  GO:0005516;
GO  GO:0005251;
GO  GO:1902936;
GO  GO:0005249;
GO  GO:0071277;
GO  GO:0048015;
GO  GO:0071805;
GO  GO:0042127;
GO  GO:0034765;
GO  GO:0042391;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q63472};
SQ  MTMAGGRKGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTI
SQ  EKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTS
SQ  SRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVS
SQ  FKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSA
SQ  FMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSI
SQ  GDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFA
SQ  VAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICP
SQ  KDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGK
SQ  GDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEER
SQ  MKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGSVLTEHSHHGLAKASVVTVRESPATPVAFPA
SQ  AAAPAGLDHARLQAPGAEGLGPKAGGADCAKRKGWARFKDACGQAEDWSKVSKAESMETLPERTKAAGEATLKKTDSCDS
SQ  GITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQAAVLEVKHELKEDIKALSTKMTSIEKQLSEILRILTSRR
SQ  SSQSPQELFEISRPQSPESERDIFGAS
//
ID  O95259;
PN  Potassium voltage-gated channel subfamily H member 1;
GN  KCNH1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:10880439, ECO:0000269|PubMed:11943152, ECO:0000269|PubMed:21559285, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:22841712, ECO:0000269|PubMed:25556795, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660, ECO:0000269|PubMed:9738473}; Multi-pass membrane protein {ECO:0000269|PubMed:21559285}. Nucleus inner membrane {ECO:0000269|PubMed:21559285}; Multi-pass membrane protein {ECO:0000269|PubMed:21559285}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63472}. Cell projection, axon {ECO:0000250|UniProtKB:Q63472}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q63472}. Perikaryon {ECO:0000250|UniProtKB:Q63472}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q63472}. Early endosome membrane {ECO:0000269|PubMed:22841712}. Note=Perinuclear KCNH1 is located to NPC-free islands.
DR  UNIPROT: O95259;
DR  UNIPROT: B1AQ26;
DR  UNIPROT: O76035;
DR  UNIPROT: Q14CL3;
DR  PDB: 5J7E;
DR  Pfam: PF00027;
DR  Pfam: PF00520;
DR  Pfam: PF13426;
DR  PROSITE: PS50042;
DR  PROSITE: PS50113;
DR  PROSITE: PS50112;
DR  OMIM: 135500;
DR  OMIM: 603305;
DR  OMIM: 611816;
DR  DisGeNET: 3756;
DE  Function: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:9738473, PubMed:11943152, PubMed:10880439, PubMed:22732247, PubMed:25556795, PubMed:27325704, PubMed:27005320, PubMed:27618660). Channel properties are modulated by subunit assembly (PubMed:11943152). Mediates IK(NI) current in myoblasts (PubMed:9738473). Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (PubMed:23881642). {ECO:0000269|PubMed:10880439, ECO:0000269|PubMed:11943152, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:23881642, ECO:0000269|PubMed:25556795, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660, ECO:0000269|PubMed:9738473}.
DE  Disease: Temple-Baraitser syndrome (TMBTS) [MIM:611816]: A developmental disorder characterized by intellectual disability, epilepsy, hypoplasia or aplasia of the thumb and great toe nails, and broadening and/or elongation of the thumbs and halluces, which have a tubular aspect. Some patients show facial dysmorphism. {ECO:0000269|PubMed:25420144}. Note=The disease is caused by variants affecting the gene represented in this entry. Zimmermann-Laband syndrome 1 (ZLS1) [MIM:135500]: A form of Zimmermann-Laband syndrome, a rare developmental disorder characterized by facial dysmorphism with bulbous nose and thick floppy ears, gingival enlargement, hypoplasia or aplasia of terminal phalanges and nails, hypertrichosis, joint hyperextensibility, and hepatosplenomegaly. Some patients manifest intellectual disability with or without epilepsy. ZLS1 inheritance is autosomal dominant. {ECO:0000269|PubMed:25915598}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P02638; IntAct: EBI-8161978; Score: 0.54
DE  Interaction: P62158; IntAct: EBI-8162095; Score: 0.72
DE  Interaction: O35550; IntAct: EBI-7991537; Score: 0.37
DE  Interaction: Q63472; IntAct: EBI-7991588; Score: 0.37
DE  Interaction: Q15276; IntAct: EBI-7991852; Score: 0.27
DE  Interaction: P18067; IntAct: EBI-7991934; Score: 0.27
DE  Interaction: P62490; IntAct: EBI-7991888; Score: 0.27
DE  Interaction: O00560; IntAct: EBI-10179865; Score: 0.56
DE  Interaction: Q7L8L6; IntAct: EBI-10256563; Score: 0.56
DE  Interaction: Q96HA8; IntAct: EBI-10287297; Score: 0.56
DE  Interaction: Q86U44; IntAct: EBI-20594935; Score: 0.35
GO  GO:0070161;
GO  GO:0030673;
GO  GO:0009986;
GO  GO:0030425;
GO  GO:0031901;
GO  GO:0005887;
GO  GO:0099056;
GO  GO:0043231;
GO  GO:0005637;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098839;
GO  GO:0008076;
GO  GO:0071889;
GO  GO:0005516;
GO  GO:0005251;
GO  GO:0042802;
GO  GO:1902936;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0044325;
GO  GO:0005249;
GO  GO:0071277;
GO  GO:0007520;
GO  GO:0048015;
GO  GO:0071805;
GO  GO:0006813;
GO  GO:0042127;
GO  GO:0034765;
GO  GO:0042391;
GO  GO:0001964;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q63472};
SQ  MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTI
SQ  EKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTS
SQ  SRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVS
SQ  FKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSA
SQ  FMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSI
SQ  GDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFA
SQ  VAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICP
SQ  KDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGK
SQ  GDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEER
SQ  MKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNVLTEHASANHSLVKASVVTVRESPATPVSF
SQ  QAASTSGVPDHAKLQAPGSECLGPKGGGGDCAKRKSWARFKDACGKSEDWNKVSKAESMETLPERTKASGEATLKKTDSC
SQ  DSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVRHELKEDIKALNAKMTNIEKQLSEILRILTS
SQ  RRSSQSPQELFEISRPQSPESERDIFGAS
//
ID  Q60603;
PN  Potassium voltage-gated channel subfamily H member 1;
GN  Kcnh1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:19671703, ECO:0000269|PubMed:23975098}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Nucleus inner membrane {ECO:0000250|UniProtKB:O95259}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63472}. Cell projection, axon {ECO:0000250|UniProtKB:Q63472}. Presynaptic cell membrane {ECO:0000269|PubMed:25556795}. Perikaryon {ECO:0000250|UniProtKB:Q63472}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q63472}. Early endosome membrane {ECO:0000250|UniProtKB:O95259}. Note=Perinuclear KCNH1 is located to NPC-free islands. {ECO:0000250|UniProtKB:O95259}.
DR  UNIPROT: Q60603;
DR  UNIPROT: Q32MR6;
DR  UNIPROT: Q3USQ9;
DR  PDB: 4F8A;
DR  PDB: 4HOI;
DR  PDB: 4LLO;
DR  PDB: 5HIT;
DR  Pfam: PF00027;
DR  Pfam: PF00520;
DR  Pfam: PF13426;
DR  PROSITE: PS50042;
DR  PROSITE: PS50113;
DR  PROSITE: PS50112;
DE  Function: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:19671703, PubMed:23975098). Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity). {ECO:0000250|UniProtKB:O95259, ECO:0000269|PubMed:19671703, ECO:0000269|PubMed:23975098}.
DE  Reference Proteome: Yes;
DE  Interaction: O35551; IntAct: EBI-7991806; Score: 0.40
GO  GO:0070161;
GO  GO:0030673;
GO  GO:0030424;
GO  GO:0009986;
GO  GO:0030425;
GO  GO:0031901;
GO  GO:0005887;
GO  GO:0099056;
GO  GO:0043231;
GO  GO:0043025;
GO  GO:0005637;
GO  GO:0098688;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098839;
GO  GO:0034705;
GO  GO:0042734;
GO  GO:0045202;
GO  GO:0008076;
GO  GO:0071889;
GO  GO:0005516;
GO  GO:0005251;
GO  GO:0042802;
GO  GO:1902936;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0044325;
GO  GO:0099508;
GO  GO:0005249;
GO  GO:0071277;
GO  GO:0034220;
GO  GO:0048015;
GO  GO:0071805;
GO  GO:0042127;
GO  GO:0034765;
GO  GO:0042391;
GO  GO:0099509;
GO  GO:2000300;
GO  GO:0001964;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q63472};
SQ  MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSACSFMYGELTDKDTV
SQ  EKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTS
SQ  SRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVS
SQ  FKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSA
SQ  FMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSI
SQ  GDYEIFDEDTKTIRNNSWLYQLALDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFA
SQ  VAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICP
SQ  KDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGK
SQ  GDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEER
SQ  MKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNALTDHTSANHSLVKASVVTVRESPATPVSF
SQ  QAATTSTVSDHAKLHAPGSECLGPKAVSCDPAKRKGWARFKDACGKGEDWNKVSKAESMETLPERTKAPGEATLKKTDSC
SQ  DSGITKSDLRLDNVGETRSPQDRSPILAEVKHSFYPIPEQTLQATVLEVKYELKEDIKALNAKMTSIEKQLSEILRILMS
SQ  RGSAQSPQETGEISRPQSPESDRDIFGAS
//
ID  Q63472;
PN  Potassium voltage-gated channel subfamily H member 1;
GN  Kcnh1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:24495567, ECO:0000269|PubMed:27516594, ECO:0000269|PubMed:7925287, ECO:0000269|PubMed:9400421}; Multi-pass membrane protein {ECO:0000269|PubMed:27516594}. Nucleus inner membrane {ECO:0000250|UniProtKB:O95259}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Cell projection, dendrite {ECO:0000269|PubMed:24495567}. Cell projection, axon {ECO:0000269|PubMed:24495567}. Presynaptic cell membrane {ECO:0000269|PubMed:25556795}. Perikaryon {ECO:0000269|PubMed:24495567}. Postsynaptic density membrane {ECO:0000269|PubMed:24495567}. Early endosome membrane {ECO:0000250|UniProtKB:O95259}. Note=Perinuclear KCNH1 is located to NPC-free islands. {ECO:0000250|UniProtKB:O95259}.
DR  UNIPROT: Q63472;
DR  PDB: 5K7L;
DR  PDB: 6PBX;
DR  PDB: 6PBY;
DR  Pfam: PF00027;
DR  Pfam: PF00520;
DR  Pfam: PF13426;
DR  PROSITE: PS50042;
DR  PROSITE: PS50113;
DR  PROSITE: PS50112;
DE  Function: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:7925287, PubMed:9400421, PubMed:24495567, PubMed:27516594). Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity). {ECO:0000250|UniProtKB:O95259, ECO:0000269|PubMed:24495567, ECO:0000269|PubMed:27516594, ECO:0000269|PubMed:7925287, ECO:0000269|PubMed:9400421}.
DE  Reference Proteome: Yes;
DE  Interaction: O95259; IntAct: EBI-7991588; Score: 0.37
DE  Interaction: O35550; IntAct: EBI-7991730; Score: 0.40
GO  GO:0070161;
GO  GO:0030673;
GO  GO:0030424;
GO  GO:0009986;
GO  GO:0030425;
GO  GO:0031901;
GO  GO:0005887;
GO  GO:0099056;
GO  GO:0043025;
GO  GO:0005637;
GO  GO:0098688;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098839;
GO  GO:0034705;
GO  GO:0042734;
GO  GO:0045202;
GO  GO:0008076;
GO  GO:0071889;
GO  GO:0005516;
GO  GO:0005251;
GO  GO:0042802;
GO  GO:1902936;
GO  GO:0019901;
GO  GO:0044877;
GO  GO:0044325;
GO  GO:0099508;
GO  GO:0005249;
GO  GO:0071277;
GO  GO:0034220;
GO  GO:0048015;
GO  GO:0071805;
GO  GO:0042127;
GO  GO:0034765;
GO  GO:0042391;
GO  GO:0099509;
GO  GO:2000300;
GO  GO:0001964;
TP  Membrane Topology: Transmembrane; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:27516594};
SQ  MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSACSFMYGELTDKDTV
SQ  EKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTS
SQ  SRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVS
SQ  FKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEGIS
SQ  SLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSIGDYEIFDEDTKTIRNNSWLYQLALDIG
SQ  TPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQMYA
SQ  NTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASD
SQ  GCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYC
SQ  DLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQ
SQ  KEARLAAERGGRDLDDLDVEKGNALTDHTSANHSLVKASVVTVRESPATPVSFQAASTSTVSDHAKLHAPGSECLGPKAG
SQ  GGDPAKRKGWARFKDACGKGEDWNKVSKAESMETLPERTKASGEATLKKTDSCDSGITKSDLRLDNVGEARSPQDRSPIL
SQ  AEVKHSFYPIPEQTLQATVLEVKHELKEDIKALNAKMTSIEKQLSEILRILMSRGSSQSPQDTCEVSRPQSPESDRDIFG
SQ  AS
//
ID  F0JAI6;
PN  Kinetochore and Eb1-associated basic protein;
GN  Kebab;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:21912673}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21912673}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:21912673}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21912673}. Note=During metaphase expressed in the kinetochores. During anaphase expression in the kinetochores progressively increases, and at late anaphase it is also expressed in the microtubules, specifically in the central spindle and centrosomal region. During telophase expression increases in the microtubules, and it is associated with residual spindle microtubules between chromosomes that have separated. At interphase it is expressed in the cytoplasm particularly around the nucleus. {ECO:0000269|PubMed:21912673}.
DR  UNIPROT: F0JAI6;
DR  UNIPROT: Q961C7;
DR  UNIPROT: Q9VQ69;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q7JN06; IntAct: EBI-198980; Score: 0.00
GO  GO:0000776;
GO  GO:0048471;
GO  GO:0005876;
GO  GO:0043515;
GO  GO:0008017;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSMAKSPDMRTPGCCSPLRTKELLERQRSSRCTPAKGYLTPRNCQSPKHPEMRIPSIFVTDADYGLERPKQLLQRLERS
SQ  LYRSSSASKVPPKHSLLASQNRQRTWEGPKTPEFRSRTNKTIPASEPRPRRAKELLEDLRSKHQGTPATKIPSQRNPKEN
SQ  QELSKSHTCIPSSEPQPIRPKLILERERQESITNRLASTSIDRLKTKPPRSSFTSSRLLVPQMGFSYPKDPKRLHESDKG
SQ  IKLTTSKRKLDFKTELGTDWLRRELEKIGKEWRKKTDYQLRQLISGFVKQLVRLLPFNGITFSHLSRDCYVQQMVEALQQ
SQ  LQYTKKVNKSWLQTPNSTQAIAHVLELLNFLLDVLEHRKGEGMCALPVVSEKQRIEQLASASGTSYDVMSLQQKFENIKI
SQ  EKERLNNYQESLMPESPVSKDMDKVTERDGNQDFVRLLDFQKETLHELQLQRLRLQEFSELVSLAKIKLKRCCKANKQCI
SQ  EAFNDQIQDLADCVVLRNRNIGLLTQLHLNDNPKEEELHERMKQLQRLYEDNYSNLLQLNIKPPQGSP
//
ID  Q8IX03;
PN  Protein KIBRA;
GN  WWC1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Cell projection, ruffle membrane. Note=Colocalizes with PRKCZ in the perinuclear region.
DR  UNIPROT: Q8IX03;
DR  UNIPROT: B4DK05;
DR  UNIPROT: O94946;
DR  UNIPROT: Q6MZX4;
DR  UNIPROT: Q6Y2F8;
DR  UNIPROT: Q7Z4G8;
DR  UNIPROT: Q8WVM4;
DR  UNIPROT: Q9BT29;
DR  PDB: 2Z0U;
DR  PDB: 6FB4;
DR  PDB: 6FD0;
DR  PDB: 6FJC;
DR  PDB: 6FJD;
DR  Pfam: PF00397;
DR  PROSITE: PS50004;
DR  PROSITE: PS01159;
DR  PROSITE: PS50020;
DR  OMIM: 610533;
DR  OMIM: 615602;
DR  DisGeNET: 23286;
DE  Function: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Modulates directional migration of podocytes. Acts as a substrate for PRKCZ. Plays a role in cognition and memory performance. {ECO:0000269|PubMed:15081397, ECO:0000269|PubMed:16684779, ECO:0000269|PubMed:18190796, ECO:0000269|PubMed:18596123, ECO:0000269|PubMed:18672031, ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:23778582}.
DE  Reference Proteome: Yes;
DE  Interaction: O95831; IntAct: EBI-737309; Score: 0.00
DE  Interaction: P29991; IntAct: EBI-8826686; Score: 0.37
DE  Interaction: Q6P1J9; IntAct: EBI-732306; Score: 0.00
DE  Interaction: Q5UIP0; IntAct: EBI-732309; Score: 0.00
DE  Interaction: Q8IW50; IntAct: EBI-736430; Score: 0.00
DE  Interaction: Q2I360; IntAct: EBI-912586; Score: 0.37
DE  Interaction: P63104; IntAct: EBI-7198403; Score: 0.40
DE  Interaction: Q9UKE5; IntAct: EBI-1105950; Score: 0.00
DE  Interaction: Q16659; IntAct: EBI-7231830; Score: 0.37
DE  Interaction: Q04917; IntAct: EBI-6911631; Score: 0.53
DE  Interaction: Q15678; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: P62258; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: Q9Y2J2; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: O43491; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: Q96FJ2; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: Q9Y297; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: Q9UKB1; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: Q4VCS5; IntAct: EBI-6911631; Score: 0.48
DE  Interaction: P31946; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-6911631; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-6911631; Score: 0.53
DE  Interaction: Q99MK9; IntAct: EBI-11005346; Score: 0.35
DE  Interaction: Q9UGJ1; IntAct: EBI-11083142; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q8TCX5; IntAct: EBI-21683074; Score: 0.35
DE  Interaction: Q9BYG5; IntAct: EBI-21739610; Score: 0.35
DE  Interaction: Q8N5I2; IntAct: EBI-21770417; Score: 0.35
DE  Interaction: Q05513; IntAct: EBI-21790005; Score: 0.35
DE  Interaction: Q8TD19; IntAct: EBI-21913050; Score: 0.35
DE  Interaction: Q7Z794; IntAct: EBI-21913050; Score: 0.35
DE  Interaction: P19013; IntAct: EBI-21913050; Score: 0.35
DE  Interaction: P13646; IntAct: EBI-21913050; Score: 0.35
DE  Interaction: P04259; IntAct: EBI-21913050; Score: 0.35
DE  Interaction: Q9UPU5; IntAct: EBI-21913087; Score: 0.35
DE  Interaction: Q9BYG4; IntAct: EBI-21913087; Score: 0.35
DE  Interaction: Q16825; IntAct: EBI-21913087; Score: 0.35
DE  Interaction: Q14315; IntAct: EBI-21913087; Score: 0.35
DE  Interaction: P48668; IntAct: EBI-21913087; Score: 0.35
DE  Interaction: P41743; IntAct: EBI-21913087; Score: 0.35
DE  Interaction: Q9P1Y5; IntAct: EBI-21913148; Score: 0.35
DE  Interaction: Q92738; IntAct: EBI-21913148; Score: 0.35
DE  Interaction: Q14118; IntAct: EBI-21913148; Score: 0.35
DE  Interaction: Q62824; IntAct: EBI-15812480; Score: 0.52
DE  Interaction: Q9NV70; IntAct: EBI-15812551; Score: 0.41
DE  Interaction: O95219; IntAct: EBI-16042750; Score: 0.35
DE  Interaction: Q83A11; IntAct: EBI-21286751; Score: 0.37
DE  Interaction: Q99459; IntAct: EBI-21375503; Score: 0.00
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0032587;
GO  GO:0019900;
GO  GO:0060090;
GO  GO:0003713;
GO  GO:0016477;
GO  GO:0030010;
GO  GO:0035331;
GO  GO:0046621;
GO  GO:0000122;
GO  GO:0043410;
GO  GO:0006355;
GO  GO:0035330;
GO  GO:0032386;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPRPELPLPEGWEEARDFDGKVYYIDHTNRTTSWIDPRDRYTKPLTFADCISDELPLGWEEAYDPQVGDYFIDHNTKTTQ
SQ  IEDPRVQWRREQEHMLKDYLVVAQEALSAQKEIYQVKQQRLELAQQEYQQLHAVWEHKLGSQVSLVSGSSSSSKYDPEIL
SQ  KAEIATAKSRVNKLKREMVHLQHELQFKERGFQTLKKIDKKMSDAQGSYKLDEAQAVLRETKAIKKAITCGEKEKQDLIK
SQ  SLAMLKDGFRTDRGSHSDLWSSSSSLESSSFPLPKQYLDVSSQTDISGSFGINSNNQLAEKVRLRLRYEEAKRRIANLKI
SQ  QLAKLDSEAWPGVLDSERDRLILINEKEELLKEMRFISPRKWTQGEVEQLEMARKRLEKDLQAARDTQSKALTERLKLNS
SQ  KRNQLVRELEEATRQVATLHSQLKSLSSSMQSLSSGSSPGSLTSSRGSLVASSLDSSTSASFTDLYYDPFEQLDSELQSK
SQ  VEFLLLEGATGFRPSGCITTIHEDEVAKTQKAEGGGRLQALRSLSGTPKSMTSLSPRSSLSSPSPPCSPLMADPLLAGDA
SQ  FLNSLEFEDPELSATLCELSLGNSAQERYRLEEPGTEGKQLGQAVNTAQGCGLKVACVSAAVSDESVAGDSGVYEASVQR
SQ  LGASEAAAFDSDESEAVGATRIQIALKYDEKNKQFAILIIQLSNLSALLQQQDQKVNIRVAVLPCSESTTCLFRTRPLDA
SQ  SDTLVFNEVFWVSMSYPALHQKTLRVDVCTTDRSHLEECLGGAQISLAEVCRSGERSTRWYNLLSYKYLKKQSRELKPVG
SQ  VMAPASGPASTDAVSALLEQTAVELEKRQEGRSSTQTLEDSWRYEETSENEAVAEEEEEEVEEEEGEEDVFTEKASPDMD
SQ  GYPALKVDKETNTETPAPSPTVVRPKDRRVGTPSQGPFLRGSTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPPFVR
SQ  NSLERRSVRMKRPSSVKSLRSERLIRTSLDLELDLQATRTWHSQLTQEISVLKELKEQLEQAKSHGEKELPQWLREDERF
SQ  RLLLRMLEKRQMDRAEHKGELQTDKMMRAAAKDVHRLRGQSCKEPPEVQSFREKMAFFTRPRMNIPALSADDV
//
ID  Q5SXA9;
PN  Protein KIBRA;
GN  Wwc1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:18190796}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Note=Colocalizes with PRKCZ in the perinuclear region. {ECO:0000250}.
DR  UNIPROT: Q5SXA9;
DR  UNIPROT: Q571D0;
DR  UNIPROT: Q8K1Y3;
DR  UNIPROT: Q8VD17;
DR  UNIPROT: Q922W3;
DR  PDB: 6J68;
DR  PDB: 6J69;
DR  PDB: 6JJW;
DR  PDB: 6JJX;
DR  PDB: 6JJY;
DR  Pfam: PF00168;
DR  Pfam: PF00397;
DR  PROSITE: PS50004;
DR  PROSITE: PS01159;
DR  PROSITE: PS50020;
DE  Function: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Modulates directional migration of podocytes. Acts as a substrate for PRKCZ and may be associated with memory performance (By similarity). Regulates collagen-stimulated activation of the ERK/MAPK cascade. {ECO:0000250, ECO:0000269|PubMed:18190796}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0032587;
GO  GO:0019900;
GO  GO:0060090;
GO  GO:0030674;
GO  GO:0003713;
GO  GO:0016477;
GO  GO:0035331;
GO  GO:0046621;
GO  GO:0000122;
GO  GO:0043410;
GO  GO:0006355;
GO  GO:0035330;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPRPELPLPEGWEEARDFDGKVYYIDHRNRTTSWIDPRDRYTKPLTFADCISDELPLGWEEAYDPQVGDYFIDHNTKTTQ
SQ  IEDPRVQWRREQEHMLKDYLVVAQEALSAQKEIYQVKQQRLELAQQEYQQLHAVWEHKLGSQVSLVSGSSSSSKYDPEIL
SQ  KAEIATAKSRVNKLKREMVHLQHELQFKERGFQTLKKIDERMSDAQGGYKLDEAQAVLRETKAIKKAITCGEKEKQDLIK
SQ  SLAMLKDGFRTDRGSHSDLWSSSSSLESSSFPMPKQFLDVSSQTDISGSFSTSSNNQLAEKVRLRLRYEEAKRRIANLKI
SQ  QLAKLDSEAWPGVLDSERDRLILINEKEELLKEMRFISPRKWTQGEVEQLEMARRRLEKDLQAARDTQSKALTERLKLNS
SQ  KRNQLVRELEEATRQVATLHSQLKSLSSSMQSLSSGSSPGSLTSSRGSLAASSLDSSTSASFTDLYYDPFEQLDSELQSK
SQ  VELLFLEGATGFRPSGCITTIHEDEVAKTQKAEGGSRLQALRSLSGTPRSMTSLSPRSSLSSPSPPCSPLITDPLLTGDA
SQ  FLAPLEFEDTELSTTLCELNLGGSGTQERYRLEEPGPEGKPLGQAASVAPGCGLKVACVSAAVSDESVAGDSGVYEASAQ
SQ  RPGTSEAAAFDSDESEAVGATRVQIALKYDEKNKQFAILIIQLSHLSALSLQQDQKVNIRVAILPCSESSTCLFRTRPLD
SQ  SANTLVFNEAFWVSISYPALHQKTLRVDVCTTDRSHTEECLGGAQISLAEVCRSGERSTRWYNLLSYKYLKKQCREPQPT
SQ  EAPGPDHVDAVSALLEQTAVELEKRQEGRSSSQTLEGSWTYEEEASENEAVAEEEEEGEEDVFTEKVSPEAEECPALKVD
SQ  RETNTDSVAPSPTVVRPKDRRVGAPSTGPFLRGNTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPPFVRNSLERRSV
SQ  RMKRPSSVKSLRTERLIRTSLDLELDLQATRTWHSQLTQEISVLKELKEHLEQAKNHGEKELPQWLREDERFRLLLRMLE
SQ  KKVDRGEHKSELQADKMMRAAAKDVHRLRGQSCKEPPEVQSFREKMAFFTRPRMNIPALSADDV
//
ID  Q12756;
PN  Kinesin-like protein KIF1A;
GN  KIF1A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21376300}. Cell projection, neuron projection {ECO:0000269|PubMed:25265257, ECO:0000269|PubMed:32652677, ECO:0000269|PubMed:33880452}. Cell projection, axon {ECO:0000250|UniProtKB:P33173}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P33173}. Synapse {ECO:0000250|UniProtKB:P33173}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle membrane {ECO:0000250|UniProtKB:F1M4A4}; Peripheral membrane protein {ECO:0000250|UniProtKB:F1M4A4}; Cytoplasmic side {ECO:0000250|UniProtKB:F1M4A4}. Note=Within neuronal cells concentrated in the axon, with smaller amounts in the perinuclear and synaptic regions (By similarity). Accumulates at the distal tip of growing neurites. {ECO:0000250|UniProtKB:P33173, ECO:0000269|PubMed:25265257, ECO:0000269|PubMed:33880452}.
DR  UNIPROT: Q12756;
DR  UNIPROT: B0I1S5;
DR  UNIPROT: F5H045;
DR  UNIPROT: O95068;
DR  UNIPROT: Q13355;
DR  UNIPROT: Q14752;
DR  UNIPROT: Q2NKJ6;
DR  UNIPROT: Q4LE42;
DR  UNIPROT: Q53T78;
DR  UNIPROT: Q59GH1;
DR  UNIPROT: Q63Z40;
DR  UNIPROT: Q6P1R9;
DR  UNIPROT: Q7KZ57;
DR  PDB: 4EGX;
DR  PDB: 4EJQ;
DR  PDB: 4UXO;
DR  PDB: 4UXP;
DR  PDB: 4UXR;
DR  PDB: 4UXS;
DR  Pfam: PF12473;
DR  Pfam: PF00498;
DR  Pfam: PF12423;
DR  Pfam: PF00225;
DR  Pfam: PF16183;
DR  Pfam: PF00169;
DR  PROSITE: PS50006;
DR  PROSITE: PS00411;
DR  PROSITE: PS50067;
DR  PROSITE: PS50003;
DR  OMIM: 601255;
DR  OMIM: 610357;
DR  OMIM: 614213;
DR  OMIM: 614255;
DR  DisGeNET: 547;
DE  Function: Motor for anterograde axonal transport of synaptic vesicle precursors (PubMed:33880452). Also required for neuronal dense core vesicles (DCVs) transport to the dendritic spines and axons. The interaction calcium-dependent with CALM1 increases vesicle motility and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. {ECO:0000250|UniProtKB:F1M4A4, ECO:0000269|PubMed:33880452}.
DE  Disease: Spastic paraplegia 30 (SPG30) [MIM:610357]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. Some SPG30 patients have a pure form of the disorder, limited to spastic paraplegia, whereas others may have a complicated form that includes additional features such as cognitive dysfunction, learning disabilities, peripheral sensorimotor neuropathy, urinary sphincter problems, and/or cerebellar atrophy. SPG30 is characterized by onset in the first or second decades of unsteady spastic gait and hyperreflexia of the lower limbs. Inheritance can be autosomal dominant or autosomal recessive. {ECO:0000269|PubMed:21487076, ECO:0000269|PubMed:22258533, ECO:0000269|PubMed:25265257, ECO:0000269|PubMed:25585697, ECO:0000269|PubMed:26125038, ECO:0000269|PubMed:26410750, ECO:0000269|PubMed:28832565, ECO:0000269|PubMed:29159194, ECO:0000269|PubMed:29934652, ECO:0000269|PubMed:31488895, ECO:0000269|PubMed:31796088, ECO:0000269|PubMed:32096284, ECO:0000269|PubMed:32652677, ECO:0000269|PubMed:33880452}. Note=The disease is caused by variants affecting the gene represented in this entry. Neuropathy, hereditary sensory, 2C (HSN2C) [MIM:614213]: A neurodegenerative disorder characterized by onset in the first decade of progressive distal sensory loss leading to ulceration and amputation of the fingers and toes. Affected individuals also develop distal muscle weakness, primarily affecting the lower limbs. {ECO:0000269|PubMed:21820098}. Note=The disease is caused by variants affecting the gene represented in this entry. NESCAV syndrome (NESCAVS) [MIM:614255]: An autosomal dominant neurodegenerative disorder with variable manifestations. Main features are delayed psychomotor development, progressive spasticity, intellectual disability, speech delay, and learning disabilities. Some patients never achieve ambulation. Additional variable features are cortical visual impairment, often associated with optic atrophy, axonal peripheral neuropathy, seizures, dysautonomia, ataxia, and dystonia. Brain imaging often shows progressive cerebellar atrophy and thin corpus callosum. Disease onset is in infancy or early childhood. {ECO:0000269|PubMed:21376300, ECO:0000269|PubMed:25253658, ECO:0000269|PubMed:25265257, ECO:0000269|PubMed:26125038, ECO:0000269|PubMed:26354034, ECO:0000269|PubMed:26486474, ECO:0000269|PubMed:27034427, ECO:0000269|PubMed:31805580, ECO:0000269|PubMed:32096284, ECO:0000269|PubMed:32652677, ECO:0000269|PubMed:33880452}. Note=The disease is caused by variants affecting the gene represented in this entry. Note=KIF1A dysfunction is associated with a large spectrum of neurologic disorders, including HSN2C, SPG30 and NESCAVS. It has been proposed to collectively name them KIF1A-Associated Neurological Disorder (KAND). Some variants reported here are based on this broad classification. {ECO:0000269|PubMed:28834584, ECO:0000269|PubMed:32652677, ECO:0000269|PubMed:33880452}.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-21249906; Score: 0.37
DE  Interaction: Q12756; IntAct: EBI-7151012; Score: 0.74
DE  Interaction: P08047; IntAct: EBI-2679824; Score: 0.00
DE  Interaction: P31016; IntAct: EBI-7969315; Score: 0.44
DE  Interaction: Q15654; IntAct: EBI-21249990; Score: 0.37
DE  Interaction: P14373; IntAct: EBI-21249982; Score: 0.37
DE  Interaction: Q13077; IntAct: EBI-21249974; Score: 0.37
DE  Interaction: Q63HR2; IntAct: EBI-21249964; Score: 0.37
DE  Interaction: O43597; IntAct: EBI-21249956; Score: 0.37
DE  Interaction: Q96EP0; IntAct: EBI-21249946; Score: 0.37
DE  Interaction: O76081; IntAct: EBI-21249938; Score: 0.37
DE  Interaction: Q8HWS3; IntAct: EBI-21249930; Score: 0.37
DE  Interaction: Q93062; IntAct: EBI-21249922; Score: 0.37
DE  Interaction: P25788; IntAct: EBI-21249914; Score: 0.37
DE  Interaction: Q7Z3S9; IntAct: EBI-21249898; Score: 0.37
DE  Interaction: Q5JR59; IntAct: EBI-21249890; Score: 0.37
DE  Interaction: Q13064; IntAct: EBI-21249882; Score: 0.37
DE  Interaction: Q9UJV3; IntAct: EBI-21249872; Score: 0.37
DE  Interaction: Q99750; IntAct: EBI-21249864; Score: 0.37
DE  Interaction: P51116; IntAct: EBI-21249856; Score: 0.37
DE  Interaction: Q6UY14; IntAct: EBI-21249846; Score: 0.37
DE  Interaction: O94986; IntAct: EBI-11381405; Score: 0.27
DE  Interaction: P56945; IntAct: EBI-15099463; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q7Z5A8; IntAct: EBI-21529283; Score: 0.35
DE  Interaction: Q12798; IntAct: EBI-21576600; Score: 0.35
DE  Interaction: Q9BTE6; IntAct: EBI-21593012; Score: 0.35
DE  Interaction: Q8TE96; IntAct: EBI-21601615; Score: 0.35
DE  Interaction: P17980; IntAct: EBI-21604348; Score: 0.35
DE  Interaction: Q9UPQ4; IntAct: EBI-21609883; Score: 0.35
DE  Interaction: Q8NB37; IntAct: EBI-21611026; Score: 0.35
DE  Interaction: Q96EK5; IntAct: EBI-21618538; Score: 0.35
DE  Interaction: Q6UWN0; IntAct: EBI-21625737; Score: 0.35
DE  Interaction: Q96A37; IntAct: EBI-21627270; Score: 0.35
DE  Interaction: Q9H7D0; IntAct: EBI-21689344; Score: 0.35
DE  Interaction: O60333; IntAct: EBI-25914332; Score: 0.56
DE  Interaction: Q9H6L5; IntAct: EBI-16159487; Score: 0.37
DE  Interaction: Q96RS6; IntAct: EBI-20723859; Score: 0.35
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21382678; Score: 0.00
DE  Interaction: Q9UKE5; IntAct: EBI-21382663; Score: 0.00
DE  Interaction: P07339; IntAct: EBI-25839962; Score: 0.56
DE  Interaction: P28799; IntAct: EBI-25859987; Score: 0.56
DE  Interaction: P02766; IntAct: EBI-25893971; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25896658; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25930203; Score: 0.56
DE  Interaction: Q15349; IntAct: EBI-28941290; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0030425;
GO  GO:0098674;
GO  GO:0005871;
GO  GO:0005874;
GO  GO:0098992;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003774;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0003777;
GO  GO:0008574;
GO  GO:0008089;
GO  GO:1990048;
GO  GO:0030705;
GO  GO:0099519;
GO  GO:0007018;
GO  GO:0060998;
GO  GO:0061001;
GO  GO:1990049;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:F1M4A4};
SQ  MAGASVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKQPKETPKSFSFDYSYWSHTSPEDINYASQKQVYRDIGEE
SQ  MLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEKDQQGIIPQLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRDLLNP
SQ  KNKGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITTEK
SQ  VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPNKNKKKKKTDFIPYRDSVLTWLLRENLG
SQ  GNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAVINEDPNNKLIRELKDEVTRLRDLLYAQGLGDITDMTNALVG
SQ  MSPSSSLSALSSRAASVSSLHERILFAPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIRMEREALLAEMGVAMREDG
SQ  GTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGREDGERRQDIVLSGHFIKEEHCVFRSDSRGGSEAVVTLEPC
SQ  EGADTYVNGKKVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERERTPCAETPAEPVDWAFAQRELLEKQGIDMKQEMEQ
SQ  RLQELEDQYRREREEATYLLEQQRLDYESKLEALQKQMDSRYYPEVNEEEEEPEDEVQWTERECELALWAFRKWKWYQFT
SQ  SLRDLLWGNAIFLKEANAISVELKKKVQFQFVLLTDTLYSPLPPDLLPPEAAKDRETRPFPRTIVAVEVQDQKNGATHYW
SQ  TLEKLRQRLDLMREMYDRAAEVPSSVIEDCDNVVTGGDPFYDRFPWFRLVGRAFVYLSNLLYPVPLVHRVAIVSEKGEVK
SQ  GFLRVAVQAISADEEAPDYGSGVRQSGTAKISFDDQHFEKFQSESCPVVGMSRSGTSQEELRIVEGQGQGADVGPSADEV
SQ  NNNTCSAVPPEGLLLDSSEKAALDGPLDAALDHLRLGNTFTFRVTVLQASSISAEYADIFCQFNFIHRHDEAFSTEPLKN
SQ  TGRGPPLGFYHVQNIAVEVTKSFIEYIKSQPIVFEVFGHYQQHPFPPLCKDVLSPLRPSRRHFPRVMPLSKPVPATKLST
SQ  LTRPCPGPCHCKYDLLVYFEICELEANGDYIPAVVDHRGGMPCMGTFLLHQGIQRRITVTLLHETGSHIRWKEVRELVVG
SQ  RIRNTPETDESLIDPNILSLNILSSGYIHPAQDDRTFYQFEAAWDSSMHNSLLLNRVTPYREKIYMTLSAYIEMENCTQP
SQ  AVVTKDFCMVFYSRDAKLPASRSIRNLFGSGSLRASESNRVTGVYELSLCHVADAGSPGMQRRRRRVLDTSVAYVRGEEN
SQ  LAGWRPRSDSLILDHQWELEKLSLLQEVEKTRHYLLLREKLETAQRPVPEALSPAFSEDSESHGSSSASSPLSAEGRPSP
SQ  LEAPNERQRELAVKCLRLLTHTFNREYTHSHVCVSASESKLSEMSVTLLRDPSMSPLGVATLTPSSTCPSLVEGRYGATD
SQ  LRTPQPCSRPASPEPELLPEADSKKLPSPARATETDKEPQRLLVPDIQEIRVSPIVSKKGYLHFLEPHTSGWARRFVVVR
SQ  RPYAYMYNSDKDTVERFVLNLATAQVEYSEDQQAMLKTPNTFAVCTEHRGILLQAASDKDMHDWLYAFNPLLAGTIRSKL
SQ  SRRRSAQMRV
//
ID  P33173;
PN  Kinesin-like protein KIF1A;
GN  Kif1a;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q12756}. Cell projection, axon {ECO:0000269|PubMed:7539720}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:7539720}. Synapse. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q12756}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle membrane {ECO:0000250|UniProtKB:F1M4A4}; Peripheral membrane protein {ECO:0000250|UniProtKB:F1M4A4}; Cytoplasmic side {ECO:0000250|UniProtKB:F1M4A4}. Note=Within neuronal cells concentrated in the axon, with smaller amounts in the perinuclear and synaptic regions (PubMed:7539720). Expressed in distal regions of neurites. {ECO:0000250|UniProtKB:Q12756, ECO:0000269|PubMed:7539720}.
DR  UNIPROT: P33173;
DR  UNIPROT: Q61770;
DR  PDB: 1I5S;
DR  PDB: 1I6I;
DR  PDB: 1IA0;
DR  PDB: 1VFV;
DR  PDB: 1VFW;
DR  PDB: 1VFX;
DR  PDB: 1VFZ;
DR  PDB: 2HXF;
DR  PDB: 2HXH;
DR  PDB: 2ZFI;
DR  PDB: 2ZFJ;
DR  PDB: 2ZFK;
DR  PDB: 2ZFL;
DR  PDB: 2ZFM;
DR  PDB: 7EO9;
DR  PDB: 7EOB;
DR  Pfam: PF12473;
DR  Pfam: PF00498;
DR  Pfam: PF12423;
DR  Pfam: PF00225;
DR  Pfam: PF16183;
DR  Pfam: PF00169;
DR  PROSITE: PS50006;
DR  PROSITE: PS00411;
DR  PROSITE: PS50067;
DR  PROSITE: PS50003;
DE  Function: Motor for anterograde axonal transport of synaptic vesicle precursors (Probable). Also required for neuronal dense core vesicles (DCVs) transport to the dendritic spines and axons. The interaction calcium-dependent with CALM1 increases vesicle motility and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites (By similarity). {ECO:0000250|UniProtKB:F1M4A4, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: Q06335; IntAct: EBI-2013377; Score: 0.40
DE  Interaction: P33173; IntAct: EBI-16002374; Score: 0.40
DE  Interaction: Q6NZM9; IntAct: EBI-26472902; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0098674;
GO  GO:0005871;
GO  GO:0005874;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0098992;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0098793;
GO  GO:0032991;
GO  GO:0008021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0003777;
GO  GO:0008574;
GO  GO:0008089;
GO  GO:1990048;
GO  GO:0030705;
GO  GO:0099519;
GO  GO:0022027;
GO  GO:0007018;
GO  GO:0098840;
GO  GO:0060998;
GO  GO:0061001;
GO  GO:1990049;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:F1M4A4};
SQ  MAGASVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKQPKETPKSFSFDYSYWSHTSPEDINYASQKQVYRDIGEE
SQ  MLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEKDQQGIIPQLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRDLLNP
SQ  KNKGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKPRTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITTEK
SQ  VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPNKNKKKKKTDFIPYRDSVLTWLLRENLG
SQ  GNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIINEDPNNKLIRELKDEVTRLRDLLYAQGLGDITDMTNALVG
SQ  MSPSSSLSALSSRAASVSSLHERILFAPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIRMEREALLAEMGVAMREDG
SQ  GTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFRSDSRGGGEAVVTLEPC
SQ  EGADTYVNGKKVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERERTPCAETPAEPVDWAFAQRELLEKQGIDMKQEMEQ
SQ  RLQELEDQYRREREEATYLLEQQRLDYESKLEALQKQMDSRYYPEVNEEEEEPEDEVQWTERECELALWAFRKWKWYQFT
SQ  SLRDLLWGNAIFLKEANAISVELKKKVQFQFVLLTDTLYSPLPPDLLPPEAAKDRETRPFPRTIVAVEVQDQKNGATHYW
SQ  TLEKLRQRLDLMREMYDRAAEVPSSVVEDCDNVVTGGDPFYDRFPWFRLVGRAFVYLSNLLYPVPLVHRVAIVSEKGEVK
SQ  GFLRVAVQAISADEEAPDYGSGVRQSGTAKISFDDQHFEKFQSESCPVVGMSRSGTSQEELRIVEGQGQGADAGPSADEV
SQ  NNNTCSAVPPEGLMDSPEKAALDGPLDTALDHLRLGSTFTFRVTVLQASSISAEYADIFCQFNFIHRHDEAFSTEPLKNT
SQ  GRGPPLGFYHVQNIAVEVTKSFIEYIKSQPIVFEVFGHYQQHPFPPLCKDVLSPLRPSRRHFPRVMPLSKPVPATKLSTM
SQ  TRPSPGPCHCKYDLLVYFEICELEANGDYIPAVVDHRGACMGTFLLHQGIQRRITVTLLHETGSHIRWKEVRELVVGRIR
SQ  NTPETDEALIDPNILSLNILSSGYVHPAQDDRVFFGNDTRTFYQFEAAWDSSMHNSLLLNRVTPYREKIYMTLSAYIEME
SQ  NCTQPAVITKDFCMVFYSRDAKLPASRSIRNLFGSGSLRATEGNRVTGVYELSLCHVADAGSPGMQRRRRRVLDTSVAYV
SQ  RGEENLAGWRPRSDSLILDHQWELEKLSLLQEVEKTRHYLLLREKLETTQRPGPEVLSPASSEDSESRSSSGASSPLSAE
SQ  GQPSPLEAPNERQRELAVKCLRLLMHTFNREYTHSHVCISASESKLSEMSVTLMRDPSMSPLGAATLTPSSTCPSLIEGR
SQ  YGATDVRTPQPCSRPASPEPELLPELDSKKTPSPVRATETEKEPQRLLVPDIQEIRVSPIVSKKGYLHFLEPHTAGWAKR
SQ  FVVVRRPYAYMYNSDKDTVERFVLNLSTAQVEYSEDQQAMLKTPNTFAVCTEHRGILLQANSDKDMHDWLYAFNPLLAGT
SQ  IRSKLSRRRSAQMRV
//
ID  F1M4A4;
PN  Kinesin-like protein KIF1A;
GN  Kif1a;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q12756}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q12756}. Cell projection, axon {ECO:0000250|UniProtKB:P33173}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P33173}. Synapse {ECO:0000250|UniProtKB:P33173}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle membrane {ECO:0000269|PubMed:29166604, ECO:0000269|PubMed:30021165}; Peripheral membrane protein {ECO:0000305|PubMed:30021165}; Cytoplasmic side {ECO:0000305|PubMed:30021165}. Note=Within neuronal cells concentrated in the axon, with smaller amounts in the perinuclear and synaptic regions (By similarity). Expressed in distal regions of neurites. {ECO:0000250|UniProtKB:P33173, ECO:0000250|UniProtKB:Q12756}.
DR  UNIPROT: F1M4A4;
DR  Pfam: PF12473;
DR  Pfam: PF00498;
DR  Pfam: PF12423;
DR  Pfam: PF00225;
DR  Pfam: PF16183;
DR  Pfam: PF00169;
DR  PROSITE: PS50006;
DR  PROSITE: PS00411;
DR  PROSITE: PS50067;
DR  PROSITE: PS50003;
DE  Function: Motor for anterograde axonal transport of synaptic vesicle precursors (Probable). Also required for neuronal dense core vesicles (DCVs) transport to the dendritic spines and axons (PubMed:29166604, PubMed:30021165). The interaction calcium-dependent with CALM1 increases vesicle motility and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites (PubMed:30021165). {ECO:0000269|PubMed:29166604, ECO:0000269|PubMed:30021165, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I9X8; IntAct: EBI-11701393; Score: 0.50
GO  GO:0070161;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0098674;
GO  GO:0005871;
GO  GO:0005874;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0098992;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0098793;
GO  GO:0032991;
GO  GO:0008021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0003777;
GO  GO:0008574;
GO  GO:0008089;
GO  GO:1990048;
GO  GO:0030705;
GO  GO:0099519;
GO  GO:0022027;
GO  GO:0007018;
GO  GO:0098840;
GO  GO:0060998;
GO  GO:0061001;
GO  GO:1990049;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:30021165};
SQ  MAGASVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKQPKETPKSFSFDYSYWSHTSPEDINYASQKQVYRDIGEE
SQ  MLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEKDQQGIIPQLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRDLLNP
SQ  KNKGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITTEK
SQ  VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPNKNKKKKKTDFIPYRDSVLTWLLRENLG
SQ  GNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIINEDPNNKLIRELKDEVTRLRDLLYAQGLGDITDTNTVPGG
SQ  PKLTNALVGMSPSSSLSALSSRAASVSSLHERILFAPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIRMEREALLAE
SQ  MGVAMREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFRSDSRGGG
SQ  EAVVTLEPCEGADTYVNGKKVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERERTPCAETPAEPVDWAFAQRELLEKQG
SQ  IDMKQEMEQRLQELEDQYRREREEATYLLEQQRLDYESKLEALQKQMDSRYYPEVNEEEEEPEDEVQWTERECELALWAF
SQ  RKWKWYQFTSLRDLLWGNAIFLKEANAISVELKKKVQFQFVLLTDTLYSPLPPDLLPPEAAKDRETRPFPRTIVAVEVQD
SQ  QKNGATHYWTLEKLRQRLDLMREMYDRAAEVPSSVVEDCDNVVTGGDPFYDRFPWFRLVGRAFVYLSNLLYPVPLVHRVA
SQ  IVSEKGEVKGFLRVAVQAISADEEAPDYGSGVRQSGTAKISFDDQHFEKFQSESCPVVGMSRSGTSQEELRIVEGQGQGA
SQ  DAGPSADEVNNNTCSAVPPEGLLDSPEKAALDGPLDTALDHLRLGSTFTFRVTVLQASSISAEYADIFCQFNFIHRHDEA
SQ  FSTEPLKNTGRGPPLGFYHVQNIAVEVTKSFIEYIKSQPIVFEVFGHYQQHPFPPLCKDVLSPLRPSRRHFPRVMPLSKP
SQ  VPATKLSTMTRPSPGPCHCKYDLLVYFEICELEANGDYIPAVVDHRGGMPCMGTFLLHQGIQRRITVTLLHETGSHIRWK
SQ  EVRELVVGRIRNTPETDEALIDPNILSLNILSSGYVHPAQDDRQFLDSDIPRTFYQFEAAWDSSMHNSLLLNRVTPYREK
SQ  IYMTLSAYIEMENCTQPAVITKDFCMVFYSRDAKLPASRSIRNLFGSGSLRATEGNRVTGVYELSLCHVADAGSPGMQRR
SQ  RRRVLDTSVAYVRGEENLAGWRPRSDSLILDHQWELEKLSLLQEVEKTRHYLLLREKLETTQRPVPEVLSPASSEDSESR
SQ  SSSGASSPLSAEGQPSPLEVPNERQRELAVKCLRLLMHTFNREYTHSHVCISASESKLSEMSVTLMRDPSMSPLGAATLT
SQ  PSSTCPSLIEGRYGATDVRTPQPCSRPASPEPELLPELDSKKTPSPVRATETEKEPQRLLVPDIQEIRVSPIVSKKGYLH
SQ  FLEPHTAGWAKRFVVVRRPYAYMYNSDKDTVERFVLNLSTAQVEYSEDQQAMLKTPNTFAVCTEHRGILLQANSDKDMHD
SQ  WLYAFNPLLAGTIRSKLSRRRSAQMRV
//
ID  Q12840;
PN  Kinesin heavy chain isoform 5A;
GN  KIF5A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6QLM7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6QLM7}. Perikaryon {ECO:0000250|UniProtKB:Q6QLM7}. Note=Concentrated in the cell body of the neurons, particularly in the perinuclear region. {ECO:0000250|UniProtKB:Q6QLM7}.
DR  UNIPROT: Q12840;
DR  UNIPROT: A6H8M5;
DR  UNIPROT: Q4LE26;
DR  PDB: 4UXT;
DR  PDB: 4UXY;
DR  PDB: 4UY0;
DR  Pfam: PF00225;
DR  PROSITE: PS00411;
DR  PROSITE: PS50067;
DR  OMIM: 602821;
DR  OMIM: 604187;
DR  OMIM: 617235;
DR  OMIM: 617921;
DR  DisGeNET: 3798;
DE  Function: Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. The ZFYVE27-KIF5A complex contributes to the vesicular transport of VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 proteins in neurons. Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation. {ECO:0000250|UniProtKB:P33175, ECO:0000250|UniProtKB:Q6QLM7}.
DE  Disease: Spastic paraplegia 10, autosomal dominant (SPG10) [MIM:604187]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:12355402, ECO:0000269|PubMed:15452312, ECO:0000269|PubMed:16476820, ECO:0000269|PubMed:16489470, ECO:0000269|PubMed:18203753, ECO:0000269|PubMed:18245137, ECO:0000269|PubMed:18853458, ECO:0000269|PubMed:21107874}. Note=The disease is caused by variants affecting the gene represented in this entry. Myoclonus, intractable, neonatal (NEIMY) [MIM:617235]: An autosomal dominant neurologic disorder characterized by severe, infantile-onset myoclonic seizures, hypotonia, optic nerve abnormalities, dysphagia, apnea, and early developmental arrest. Brain imaging shows a progressive leukoencephalopathy. Some patients may die in infancy. {ECO:0000269|PubMed:24215330, ECO:0000269|PubMed:27414745, ECO:0000269|PubMed:27463701}. Note=The disease is caused by variants affecting the gene represented in this entry. Amyotrophic lateral sclerosis 25 (ALS25) [MIM:617921]: A form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5- 10% of the cases. ALS25 is an autosomal dominant form with variable adult onset and incomplete penetrance. {ECO:0000269|PubMed:29342275, ECO:0000269|PubMed:29566793}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. The mutation NM_004984.2:c.33019A>G encoding the predicted missence variant p.Arg1007Gly, may also affect splicing and induce the skipping of exon 27, resulting in a frameshift and a premature stop codon producing a truncated protein p.Asn999Valfs*39. {ECO:0000269|PubMed:29342275}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-20931480; Score: 0.40
DE  Interaction: Q06787; IntAct: EBI-21379882; Score: 0.00
DE  Interaction: Q15811; IntAct: EBI-730237; Score: 0.00
DE  Interaction: Q13625; IntAct: EBI-731035; Score: 0.00
DE  Interaction: Q8TDR0; IntAct: EBI-1105986; Score: 0.00
DE  Interaction: Q00987; IntAct: EBI-2684894; Score: 0.00
DE  Interaction: P28702; IntAct: EBI-2689772; Score: 0.00
DE  Interaction: P61457; IntAct: EBI-2690406; Score: 0.00
DE  Interaction: O95819; IntAct: EBI-3443453; Score: 0.00
DE  Interaction: Q9Y4G8; IntAct: EBI-3450200; Score: 0.00
DE  Interaction: Q9Y6H6; IntAct: EBI-7183878; Score: 0.37
DE  Interaction: Q13526; IntAct: EBI-7302782; Score: 0.37
DE  Interaction: Q16637; IntAct: EBI-7389325; Score: 0.37
DE  Interaction: P04183; IntAct: EBI-7398825; Score: 0.37
DE  Interaction: Q96NW4; IntAct: EBI-6125591; Score: 0.58
DE  Interaction: Q9UPV9; IntAct: EBI-8786097; Score: 0.40
DE  Interaction: Q8R2H7; IntAct: EBI-8785998; Score: 0.40
DE  Interaction: P54256; IntAct: EBI-9638913; Score: 0.37
DE  Interaction: Q92731; IntAct: EBI-9996422; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: P06213; IntAct: EBI-10769013; Score: 0.35
DE  Interaction: Q9WH76; IntAct: EBI-10823922; Score: 0.37
DE  Interaction: Q4G0F5; IntAct: EBI-11141405; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-12579531; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12588098; Score: 0.35
DE  Interaction: Q9UGM1; IntAct: EBI-21517134; Score: 0.35
DE  Interaction: Q15654; IntAct: EBI-21559268; Score: 0.35
DE  Interaction: Q96EV8; IntAct: EBI-21651992; Score: 0.35
DE  Interaction: Q8N205; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q9NV70; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q9Y2V7; IntAct: EBI-21673529; Score: 0.35
DE  Interaction: P12524; IntAct: EBI-21709838; Score: 0.35
DE  Interaction: O60296; IntAct: EBI-21729552; Score: 0.35
DE  Interaction: P13497; IntAct: EBI-21764992; Score: 0.35
DE  Interaction: Q07866; IntAct: EBI-21768919; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-21902679; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-21903886; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21907689; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-21909838; Score: 0.35
DE  Interaction: Q921C5; IntAct: EBI-15847851; Score: 0.41
DE  Interaction: Q9NPJ6; IntAct: EBI-25472202; Score: 0.27
DE  Interaction: Q9BYV6; IntAct: EBI-22022921; Score: 0.00
DE  Interaction: Q92574; IntAct: EBI-26515740; Score: 0.37
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q05DH4; IntAct: EBI-34574576; Score: 0.27
DE  Interaction: Q86V87; IntAct: EBI-34575191; Score: 0.27
GO  GO:1904115;
GO  GO:0035253;
GO  GO:0005829;
GO  GO:0032839;
GO  GO:0005871;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003774;
GO  GO:0019894;
GO  GO:0008017;
GO  GO:0003777;
GO  GO:0008574;
GO  GO:0099641;
GO  GO:0098971;
GO  GO:0007411;
GO  GO:0007268;
GO  GO:0030705;
GO  GO:0007018;
GO  GO:1990049;
GO  GO:0048489;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNG
SQ  TIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDK
SQ  NRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVS
SQ  KTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMF
SQ  GQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEEAALGAELCEETPVN
SQ  DNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAA
SQ  KDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSE
SQ  FSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKI
SQ  RSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDE
SQ  INEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKL
SQ  FVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALK
SQ  EAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNSLFQNYQNLYLQ
SQ  ATPSSTSDMYFANSCTSSGATSSGGPLASYQKANMDNGNATDINDNRSDLPCGYEAEDQAKLFPLHQETAAS
//
ID  P33175;
PN  Kinesin heavy chain isoform 5A;
GN  Kif5a;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6QLM7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6QLM7}. Perikaryon {ECO:0000250|UniProtKB:Q6QLM7}. Note=Concentrated in the cell body of the neurons, particularly in the perinuclear region. {ECO:0000250|UniProtKB:Q6QLM7}.
DR  UNIPROT: P33175;
DR  UNIPROT: Q5DTP1;
DR  UNIPROT: Q6PDY7;
DR  UNIPROT: Q9Z2F9;
DR  Pfam: PF00225;
DR  PROSITE: PS00411;
DR  PROSITE: PS50067;
DE  Function: Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL) (PubMed:12682084). Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. The ZFYVE27-KIF5A complex contributes to the vesicular transport of VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 proteins in neurons (PubMed:21976701). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity). {ECO:0000250|UniProtKB:Q6QLM7, ECO:0000269|PubMed:12682084, ECO:0000269|PubMed:21976701}.
DE  Reference Proteome: Yes;
DE  Interaction: O08788; IntAct: EBI-8013466; Score: 0.40
DE  Interaction: Q61026; IntAct: EBI-8310937; Score: 0.37
DE  Interaction: O70585; IntAct: EBI-349734; Score: 0.70
DE  Interaction: O35668; IntAct: EBI-8013423; Score: 0.40
DE  Interaction: Q96NW4; IntAct: EBI-6125974; Score: 0.52
DE  Interaction: P50516; IntAct: EBI-6272793; Score: 0.35
DE  Interaction: P54256; IntAct: EBI-9652128; Score: 0.40
DE  Interaction: P35922; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-26572965; Score: 0.35
GO  GO:0097440;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0090724;
GO  GO:0035253;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0032839;
GO  GO:0005871;
GO  GO:0005874;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0000932;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0019894;
GO  GO:0008017;
GO  GO:0003777;
GO  GO:0008574;
GO  GO:0044877;
GO  GO:0097110;
GO  GO:0099641;
GO  GO:0098971;
GO  GO:0007411;
GO  GO:0030705;
GO  GO:0007018;
GO  GO:1990049;
GO  GO:0048489;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNG
SQ  TIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDK
SQ  NRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQKLSGKLYLVDLAGSEKVS
SQ  KTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMF
SQ  GQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEDSALGAELCEETPVN
SQ  DNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAA
SQ  KDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMRDLSE
SQ  FSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKI
SQ  RSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARLRDE
SQ  INEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKL
SQ  FVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALK
SQ  EAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNNLFQNYQNLHLQ
SQ  AAPSSTSDMYFASSGATSVAPLASYQKANMDNGNATDINDNRSDLPCGYEAEDQAKLFPLHQETAAS
//
ID  Q5R9K7;
PN  Kinesin heavy chain isoform 5A;
GN  KIF5A;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6QLM7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6QLM7}. Perikaryon {ECO:0000250|UniProtKB:Q6QLM7}. Note=Concentrated in the cell body of the neurons, particularly in the perinuclear region. {ECO:0000250|UniProtKB:Q6QLM7}.
DR  UNIPROT: Q5R9K7;
DR  Pfam: PF00225;
DR  PROSITE: PS00411;
DR  PROSITE: PS50067;
DE  Function: Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. The ZFYVE27-KIF5A complex contributes to the vesicular transport of VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 proteins in neurons. Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation. {ECO:0000250|UniProtKB:P33175, ECO:0000250|UniProtKB:Q6QLM7}.
DE  Reference Proteome: Yes;
GO  GO:1904115;
GO  GO:0005874;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0008017;
GO  GO:0003777;
GO  GO:0099641;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNG
SQ  TIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDK
SQ  NRVPFVKGCTERFVSGPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVS
SQ  KTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMF
SQ  GQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEEAALGAELCEETPVN
SQ  DNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQQELSHLQSENDAA
SQ  KDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSE
SQ  FSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVERHRKMEVTGRELSSCQLLISQHEAKI
SQ  RSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDE
SQ  INEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKL
SQ  FVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALK
SQ  EAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNSLFQNYQNLYLQ
SQ  ATPSSTSDMYFANSCTGSGATSSGGPLASYQKANMDNGNATDIKDNRSDLPCGYEAEDQAKLFPLHQETAAS
//
ID  Q6QLM7;
PN  Kinesin heavy chain isoform 5A;
GN  Kif5a;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:7514426}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7514426}. Perikaryon {ECO:0000269|PubMed:7514426}. Note=Concentrated in the cell body of the neurons, particularly in the perinuclear region.
DR  UNIPROT: Q6QLM7;
DR  PDB: 2KIN;
DR  PDB: 3KIN;
DR  Pfam: PF00225;
DR  PROSITE: PS50067;
DE  Function: Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. The ZFYVE27-KIF5A complex contributes to the vesicular transport of VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 proteins in neurons (By similarity). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (PubMed:23576431). {ECO:0000250|UniProtKB:P33175, ECO:0000269|PubMed:23576431}.
DE  Reference Proteome: Yes;
DE  Interaction: O70585; IntAct: EBI-8053419; Score: 0.35
DE  Interaction: P04688; IntAct: EBI-15728888; Score: 0.49
DE  Interaction: P05219; IntAct: EBI-15728888; Score: 0.49
DE  Interaction: Q10113; IntAct: EBI-15728926; Score: 0.49
DE  Interaction: Q03555; IntAct: EBI-15780606; Score: 0.35
DE  Interaction: P07727; IntAct: EBI-15780624; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26438079; Score: 0.35
GO  GO:0097440;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0090724;
GO  GO:0035253;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0032839;
GO  GO:0005871;
GO  GO:0005874;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0000932;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0019894;
GO  GO:0008017;
GO  GO:0003777;
GO  GO:0008574;
GO  GO:0044877;
GO  GO:0097110;
GO  GO:0099641;
GO  GO:0098971;
GO  GO:0007411;
GO  GO:0071361;
GO  GO:1990090;
GO  GO:0021987;
GO  GO:0030705;
GO  GO:0021766;
GO  GO:0007018;
GO  GO:0007017;
GO  GO:0048666;
GO  GO:1904647;
GO  GO:1990049;
GO  GO:0048489;
GO  GO:0021794;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNG
SQ  TIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDK
SQ  NRVPFVRGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENIETEQKLSGKLYLADLAGSEKVS
SQ  KTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMF
SQ  GQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEDSALAAEICEETPVN
SQ  DNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAA
SQ  KEEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESEPQRLQEVSGHQRKRIAEVLNGLMKDLSE
SQ  FSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKI
SQ  RSLTEYMQTVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARLRDE
SQ  INEKQKTIDELKDLDQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKL
SQ  FVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTEVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALK
SQ  EAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNNLFQNYQNLHLQ
SQ  AAPSSTSDVYFASNGATSVAPLASYQKANTDNGNATDINDNRSDLPCGYEAEDPAKLFPLHQETAAS
//
ID  Q54TL0;
PN  Kinesin-related protein 7;
GN  kif7;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:9693369}; Single-pass membrane protein {ECO:0000269|PubMed:9693369}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:9693369}.
DR  UNIPROT: Q54TL0;
DR  UNIPROT: Q94463;
DR  Pfam: PF00225;
DR  PROSITE: PS00411;
DR  PROSITE: PS50067;
DE  Function: Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end. May be involved in cell motility or cell differentiation during prestalk formation. {ECO:0000269|PubMed:9693369}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005871;
GO  GO:0005874;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0008017;
GO  GO:0003777;
GO  GO:0008574;
GO  GO:0030705;
GO  GO:0007018;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESPVVEGNSGEVATPTLPQPPTPVSSNIRVVCRVRPLTELEKGRNEHSIVHFFDSKSISIRANGPQFTFDRIFGYQETQ
SQ  SQIFEDVAEPIVNDFLDGYHGTIIAYGQTASGKTFTMVGDPDSHGIIPRVIESIFVGISKMREKDTSLSLAFCLKISALE
SQ  LYNEKLYDLYDASKSNLNIREHKQNGIYVEGISEIVITSIEEAYNFLNISNNNRAIASTKMSAASSRSHSVLMIELSQQN
SQ  LSMESSKISKLFLVDLAGSERAHKTGAEGDRMQEAKNINLSLSALGKVINALTCGANYVPYRDSKLTRVLQDSLGGNSKT
SQ  SLIINCSPSNNNEHETITTLQFGTRAKTIKNQPKINKKITYHELELFIIKLAKDLEKSRKECEEITRSKNLEINNLLIQL
SQ  ENNQKMVVESNQKLELLNSQISSNHSFDNTFKEIENTCENSKIIFDDLNDHINNNNNVDENNNTNNNDNNNNDNNNNNQY
SQ  QEESNQYQQENNQKDGDQNNSSFDSIKVEDLRDLDDEPDIEDIILNSTLGNISDDDDDDDDHHSNNNNVDDNNNGEINND
SQ  SDGYLNRSLKDIKIPEISDLNDHNINNNNNNNNNINNDNNSNSGGLRVSTSYITSSPNLSPSKSMDVNNSPPLFSYFKTK
SQ  DFPPSSDENDKFFNDLIAKGENEQQQQQQQHNDDDEDIKSTTSNATTTTITTIDMNASHPSGIDDPIEFTIIKSDKTITS
SQ  TIERETIQPSSLSNSTSLLDIETVESSTLPAPPPVTTTTTLTTVTTTKLTKTTNIPSNTNDINSIDDFGFSKIEEEGSSS
SQ  NRKPNDTAILSFGDDDDEENEDNENEDVIVDSDEDTHSGKNNLLNTFKNDHHRGDFGATPTKSIFNKNGNITIKEFETPQ
SQ  QQQQQQQQQQQQQQQQQQQQQPLILQTTSTNPTIISIKSNKEPSPSSSTTTSIKKKNFNKRRSWIIFTIILTITLVSSSL
SQ  LCLYLPEYKERLVQRRGYLNKLGIYSDYPTNEKISLAQHNQISLAKELYGGNSKQYYDEMSSFNTAYNHLIEMNHLETAV
SQ  SKIFGSAIDLRFSGDDVINSIECKRAIHKLKTNNYVNGDLDQQQQQHNYITKIDQLSEQSKEQNQLIENFKLDLKNKTSE
SQ  IEKLEKEIKQKDNKIKEKEEKIELIESRVLNEEKGGEKVLEDQIISLRNDKNTLSTQILNLEGDKKSLGVLVIKLNSDKT
SQ  EIQNEVKELKRKVQELEDAPIALIPNPFVKWVKSFYVEKKSWFVENIYKIWNWFK
//
ID  Q9Y0E4;
PN  Klarsicht protein;
GN  klar;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10556085, ECO:0000269|PubMed:15579692, ECO:0000269|PubMed:18820457, ECO:0000269|PubMed:22927463}. Nucleus membrane {ECO:0000269|PubMed:14617811, ECO:0000269|PubMed:15579692, ECO:0000269|PubMed:18820457}. Nucleus envelope {ECO:0000269|PubMed:14617811}. Note=Associated with microtubules, both apical to the nucleus and also at the basal-most area of the eye disk (PubMed:15579692, PubMed:18820457, PubMed:14617811). Koi is required for perinuclear localization of Klar (PubMed:18820457). Nuclear envelope localization requires nuclear lam (PubMed:14617811). {ECO:0000269|PubMed:14617811, ECO:0000269|PubMed:15579692, ECO:0000269|PubMed:18820457}.
DR  UNIPROT: Q9Y0E4;
DR  Pfam: PF10541;
DR  PROSITE: PS51049;
DE  Function: Component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (By similarity). Plays a role in the nuclear positioning and links the nucleus to the microtubule organizing center (MTOC) (PubMed:10556085, PubMed:22927463, PubMed:15579692). Collaborates with Klar to promote even spacing of the myonuclei at the periphery of striated muscle fibers by mediating a tight association between a nuclear ring structure of Msp300 and the plus ends of a unique astral microtubule (MT) network (PubMed:22927463). {ECO:0000250|UniProtKB:Q8WXH0, ECO:0000269|PubMed:10556085, ECO:0000269|PubMed:15579692, ECO:0000269|PubMed:22927463}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8MQJ7; IntAct: EBI-467675; Score: 0.00
DE  Interaction: P50445; IntAct: EBI-467678; Score: 0.00
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0048471;
GO  GO:0019894;
GO  GO:0001745;
GO  GO:0042051;
GO  GO:0060361;
GO  GO:0007523;
GO  GO:0031887;
GO  GO:0006869;
GO  GO:0040011;
GO  GO:0035149;
GO  GO:0061024;
GO  GO:0034453;
GO  GO:0045855;
GO  GO:0007097;
GO  GO:0051647;
GO  GO:0006997;
GO  GO:0032386;
GO  GO:0035239;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MEMQQENETGREGVIPNSEKEVALISNQETEKAAMISGGKEGSVRDLESPNETATTQKIEHTTKPLKLDGIFAMPATPPN
SQ  KAGLATKSASSSRSSSLKKQRRGSRGSANLNVAGMGDGAPKRSAPGGGQLNYGTNSVGNDLMKQSQSMTSLKASNEEQQE
SQ  SRDVIQAKLHLERPYNSLKKNSHSNKMHRYSWGSGNSQCSSTSLHSSATLGLGSSGKDDLWAAIQTNYNYIMDTNLLDTC
SQ  KEARCEIEGAATVLEKSSECSFKMLDETQRPEGLCEDPKELRRSWREMENKLESSPTITELTLFGNAELQRHLAVHSVLY
SQ  HEIASHARVVSSCIRAAEKEQQLQQQQQLSSQQPASLTSNCSSESTSESATKSSSLSSGFASDPVTTPIGTAAAAPPSSS
SQ  THPSKKGEGNLERLRDRYHLLYLKAFELQLCLDNLLRKRSSAANGLDDDEDEEEDTEDDSFGYEGEATEDDLNEVNSDLD
SQ  LENSESKSATPAELILQRCQIAATQIVCGLDETQSQSRSQQVPSQAKSPSADQPRDCLAPQKPGDEADEELEEEDEDPDI
SQ  GTDVVDFLIAKRSWRQVNHPNPSGTATLTDFEADSESSDFEQVQQLSRRGLPPTVGSTRRVLNLIEMPQSSNTNISSSNS
SQ  LLQQRNHNIGNKMLPNKAHGKNIAVAVITPNSHGNTSHGHGLGHGLGHELNKSPLGLRKTRHHHNDTSKFNRSNRKSKNC
SQ  AIFYFKHLDTDNEQGNAAGSDLQSEDDPSLIHRRRAGGDILKSADASTDDDDEGCLYTATAAATLEVATAATAAPTAAAA
SQ  TSSVDGLQSTAVSSTTATGGPLPPSDDSDKENKVALVSASTITAARTATATSIATLHSSNYDSSSACSSSNSNSNSNSNS
SQ  NGRLTETSATSRVTQLQMQIHSQSQSQSQMELQINGNAIDGRHIISNNNCYSSMQHQPQNNNEGEAAEDLAKIKMGDDEA
SQ  AADMANGNATKSQQMSNGVYSRADSCNFTVWAAETVASCHLPPRSPAKSAKSTKSQASNATVSGSTLVSPVKGKVSHDSI
SQ  KQLVLKAEHLVRDAQETALKTPTKQKHSIIKISSTVKKREVTMPHPIKQRVEEWLEHQPSTPQLLTRSHTNELLPSCKPD
SQ  DCEASGEASETDSVPQAGAGVNGGAPNGAGSDTSEGFTDSIATCMQTSTNSYGNSTERIGGSAEPIGQPVTPLGFGSSNQ
SQ  SLNVKIVKRSQTRRKSERPWSVSCLSQLTTDAAQLTTARIVENSPSGLASHSISESALDSLSPGPRPRAASSSGTGSNAA
SQ  KKADSKGSLRRRKARKKRISAASAGRKSDSGSELGGDLTQTLMKSCESMSSQQLQEFTNALLSIQKGAVVAPLSPKGEVS
SQ  GVPSLHDGEGGETQLMLPKFRVGSFTTAGLLATDTRLGALAALSNYMNEDEQQAELSTEDHHSSISETAWDNYQEKYNSE
SQ  NYSEGFDSDAARRLLEFGDDYRNFIDSQSDCCSSLSAANNLDSFSPPRMDSLQKHELKSLHINQDTITSSVDHARRQRAL
SQ  ELQYERRRKTLEVRRKSCQDMDESLMASPQSDQQQQQLQVTPSLSASATALMTTPKNQSTSHQISHRAESVGRKLDFGGM
SQ  SHSAQSLLRRTSESDTSTRRRRTVTADERRRSSRNLEKCIKLIPATTSSSSGSDSEDGEQEMRSLLQQSRDRLDDTRALK
SQ  IRCHLLRPEDYNEIINTCRDNIRCLEAVLRGPPGTVLSNHCAGQTKDLLGAWEDLLSWSENASAARKLQQEMSVLKSSLQ
SQ  RLGDKPTPELLDTEPAIQIAVEALKLEQTQLTSYRTNMLRLNASVHSWLTKQERRLQSALEEQEQQQESEQLKQQKLVEE
SQ  EKGADVQKELASTGAVAITVTDSNGNQVEALATGEASTSTPAWDVHSLMSSEQEFHKHLKNEVSDMYSAWDEADARINTQ
SQ  LEMLTNSLIAWRQLESGLSEFQLALGQDRGTLKGLEGALDKGQATPVELAQNVKLVAKLLSEKVHVSQEQLLAVQQHLDP
SQ  NHIYHITKFTASNGSLSDSGISDGGATSDGGLSERERRLGVLRRLAKQLELALAPGSEAMRSIAARMESAEADLKHLQNT
SQ  CRDLIVRTAASHQQKQQIQQNQTQQVSPKANGHIKKQAAKGKAEPQSPGRRGKGARKARQAKKAGEDQQVEEPSLSPEQQ
SQ  KMVLKQLKTLTSGDGGDDPSDDPSLLFNLESSEEDGEGADPAQTSKRGWAWRIARAAVPMQVALFTIFCAACLMQPNCCD
SQ  NLNNLSMSFTPQLRYIRGPPPI
//
ID  P46822;
PN  Kinesin light chain;
GN  klc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:19605495}. Nucleus envelope {ECO:0000269|PubMed:19605495}. Note=Recruited to the nuclear envelope by unc-83 during nuclear migrations. {ECO:0000269|PubMed:19605495}.
DR  UNIPROT: P46822;
DR  UNIPROT: Q18088;
DR  UNIPROT: Q6BEW4;
DR  UNIPROT: Q8I7M2;
DR  UNIPROT: Q8TA80;
DR  UNIPROT: Q95QV1;
DR  PROSITE: PS01160;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport (Probable). The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (Probable). Recruits unc-83 (within the unc-83-unc-84 LINC complex) to the nuclear envelope during nuclear migration to mediate the link between the nuclear envelope and the microtubule cytoskeleton in hypodermal precursor cells (PubMed:19605495, PubMed:27697906). {ECO:0000269|PubMed:19605495, ECO:0000269|PubMed:27697906, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: P34609; IntAct: EBI-2413629; Score: 0.62
DE  Interaction: O01482; IntAct: EBI-333962; Score: 0.00
DE  Interaction: Q17581; IntAct: EBI-333959; Score: 0.00
DE  Interaction: P91001; IntAct: EBI-333956; Score: 0.00
DE  Interaction: P46822; IntAct: EBI-333971; Score: 0.00
DE  Interaction: Q93228; IntAct: EBI-333968; Score: 0.00
DE  Interaction: G5EBU5; IntAct: EBI-333965; Score: 0.00
DE  Interaction: P25807; IntAct: EBI-333977; Score: 0.00
DE  Interaction: P91131; IntAct: EBI-333974; Score: 0.00
DE  Interaction: Q95Y99; IntAct: EBI-333989; Score: 0.00
DE  Interaction: H2L044; IntAct: EBI-333986; Score: 0.00
DE  Interaction: O01802; IntAct: EBI-333983; Score: 0.00
DE  Interaction: Q9XW20; IntAct: EBI-333998; Score: 0.00
DE  Interaction: Q9TZH8; IntAct: EBI-333995; Score: 0.00
DE  Interaction: P34540; IntAct: EBI-333992; Score: 0.00
DE  Interaction: Q95XR0; IntAct: EBI-334004; Score: 0.00
DE  Interaction: Q966C7; IntAct: EBI-334001; Score: 0.00
DE  Interaction: G5EFD7; IntAct: EBI-337850; Score: 0.00
DE  Interaction: Q23130; IntAct: EBI-342512; Score: 0.00
DE  Interaction: Q23064; IntAct: EBI-2904924; Score: 0.00
GO  GO:0005737;
GO  GO:0016938;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0019894;
GO  GO:0048675;
GO  GO:0051295;
GO  GO:0040011;
GO  GO:0007018;
GO  GO:0002119;
GO  GO:0030473;
GO  GO:0040038;
GO  GO:0008104;
GO  GO:0048489;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNMSQDDVTTGLRTVQQGLEALREEHSTISNTLETSVKGVKEDEAPLPKQKLSQINDNLDKLVCGVDETSLMLMVFQLT
SQ  QGMDAQHQKYQAQRRRLCQENAWLRDELSSTQIKLQQSEQMVAQLEEENKHLKYMASIKQFDDGTQSDTKTSVDVGPQPV
SQ  TNETLQELGFGPEDEEDMNASQFNQPTPANQMAASANVGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTS
SQ  GHDHPDVATMLNILALVYRDQNKYKEAANLLNEALSIREKCLGESHPAVAATLNNLAVLFGKRGKFKDAEPLCKRALEIR
SQ  EKVLGDDHPDVAKQLNNLALLCQNQGKYEEVEKYYKRALEIYESKLGPDDPNVAKTKNNLSSAYLKQGKYKEAEELYKQI
SQ  LTRAHEREFGQISGENKPIWQIAEEREENKHKGEGATANEQAGWAKAAKVDSPTVTTTLKNLGALYRRQGKYEAAETLED
SQ  VALRAKKQHEPLRSGAMGGIDEMSQSMMASTIGGSRNSMTTSTSQTGLKNKLMNALGFNS
//
ID  Q08DK3;
PN  Kelch-like protein 20;
GN  KLHL20;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN-gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (By similarity). {ECO:0000250}.
DR  UNIPROT: Q08DK3;
DR  Pfam: PF07707;
DR  Pfam: PF00651;
DR  Pfam: PF01344;
DR  PROSITE: PS50097;
DE  Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis. The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination. Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking. Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (By similarity). {ECO:0000250|UniProtKB:Q9Y2M5}.
DE  Reference Proteome: Yes;
DE  Interaction: P19711; IntAct: EBI-9524158; Score: 0.37
DE  Interaction: P21530; IntAct: EBI-9524126; Score: 0.37
GO  GO:0030424;
GO  GO:0031463;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0005802;
GO  GO:0003779;
GO  GO:0019964;
GO  GO:0004842;
GO  GO:0006895;
GO  GO:0043066;
GO  GO:0043161;
GO  GO:1990390;
GO  GO:0015031;
GO  GO:0016567;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIY
SQ  AHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEF
SQ  LKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVK
SQ  YSIQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVL
SQ  FAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTS
SQ  TCRTSVGVAVLGGFLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERY
SQ  NPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVG
SQ  GFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW
//
ID  Q5ZKD9;
PN  Kelch-like protein 20;
GN  KLHL20;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.
DR  UNIPROT: Q5ZKD9;
DR  Pfam: PF07707;
DR  Pfam: PF00651;
DR  Pfam: PF01344;
DR  PROSITE: PS50097;
DE  Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome. It also specifically mediates 'Lys-33'-linked ubiquitination (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031463;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0005802;
GO  GO:0019964;
GO  GO:0004842;
GO  GO:0006895;
GO  GO:0043066;
GO  GO:0043161;
GO  GO:1990390;
GO  GO:0015031;
GO  GO:0016567;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDGKPMRRCTSTRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIY
SQ  AHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTSLPAACLLQLAEIQEACCEF
SQ  LKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWV
SQ  KYSIQERRPQLPQVLQHVRLPLLSTKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEV
SQ  LFAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPT
SQ  STCRTSVGVAVLGGYLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVER
SQ  YNPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAV
SQ  GGFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW
//
ID  Q9Y2M5;
PN  Kelch-like protein 20;
GN  KLHL20;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus. Golgi apparatus, trans-Golgi network. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN- gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (PubMed:20389280). {ECO:0000269|PubMed:20389280}.
DR  UNIPROT: Q9Y2M5;
DR  UNIPROT: B3KMA0;
DR  UNIPROT: B4DUR0;
DR  UNIPROT: Q5TZF2;
DR  UNIPROT: Q5ZF45;
DR  UNIPROT: Q9H457;
DR  PDB: 5YQ4;
DR  PDB: 6GY5;
DR  Pfam: PF07707;
DR  Pfam: PF00651;
DR  Pfam: PF01344;
DR  PROSITE: PS50097;
DR  OMIM: 617679;
DR  DisGeNET: 27252;
DE  Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis (PubMed:20389280). The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination (PubMed:24768539). Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking (PubMed:24768539). Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (PubMed:21670212). In case of tumor, the BCR(KLHL20) E3 ubiquitin ligase complex is involved in tumor hypoxia: following hypoxia, the BCR(KLHL20)complex mediates ubiquitination and degradation of PML, potentiating HIF-1 signaling and cancer progression (PubMed:21840486). {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17395875, ECO:0000269|PubMed:20389280, ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:24768539}.
DE  Reference Proteome: Yes;
DE  Interaction: O43463; IntAct: EBI-8472700; Score: 0.37
DE  Interaction: P0DTD1; IntAct: EBI-26949933; Score: 0.49
DE  Interaction: P32456; IntAct: EBI-731149; Score: 0.00
DE  Interaction: Q14203; IntAct: EBI-25840739; Score: 0.56
DE  Interaction: Q53GS7; IntAct: EBI-25859210; Score: 0.56
DE  Interaction: Q7L5N1; IntAct: EBI-2510262; Score: 0.40
DE  Interaction: Q9UKR5; IntAct: EBI-731146; Score: 0.00
DE  Interaction: Q9P2H0; IntAct: EBI-731152; Score: 0.00
DE  Interaction: Q9Y383; IntAct: EBI-731155; Score: 0.00
DE  Interaction: Q5UIP0; IntAct: EBI-731158; Score: 0.00
DE  Interaction: Q14194; IntAct: EBI-733755; Score: 0.00
DE  Interaction: Q13526; IntAct: EBI-733758; Score: 0.00
DE  Interaction: P53355; IntAct: EBI-7904028; Score: 0.66
DE  Interaction: Q13618; IntAct: EBI-7904270; Score: 0.56
DE  Interaction: P29590; IntAct: EBI-7904383; Score: 0.74
DE  Interaction: Q5NEV5; IntAct: EBI-2805488; Score: 0.00
DE  Interaction: Q7ARD3; IntAct: EBI-2865898; Score: 0.00
DE  Interaction: Q8CZU2; IntAct: EBI-2865891; Score: 0.00
DE  Interaction: Q96GG9; IntAct: EBI-21333338; Score: 0.35
DE  Interaction: Q96LA8; IntAct: EBI-8472821; Score: 0.51
DE  Interaction: Q9CQ43; IntAct: EBI-11064426; Score: 0.35
DE  Interaction: P48039; IntAct: EBI-11577038; Score: 0.00
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9UPW6; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: O00625; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q9Y573; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q9UPN9; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q9UF56; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q9NXC5; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q9NTZ6; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q9NQG5; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q9BY77; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q96T17; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q92686; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q8IVD9; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q7Z4V5; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q6P474; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q53HC5; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q53GT1; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q2VPK5; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: P57737; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: P55789; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: P49643; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: P49642; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: P42694; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: P32929; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: P30566; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: P23193; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: P22061; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: O75391; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: O43776; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: E9PNY5; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: A5PL33; IntAct: EBI-21546141; Score: 0.35
DE  Interaction: Q15884; IntAct: EBI-21620222; Score: 0.35
DE  Interaction: Q02363; IntAct: EBI-21622099; Score: 0.35
DE  Interaction: Q01201; IntAct: EBI-21654455; Score: 0.35
DE  Interaction: Q9Y5G8; IntAct: EBI-21697051; Score: 0.35
DE  Interaction: O43283; IntAct: EBI-21732152; Score: 0.35
DE  Interaction: O76039; IntAct: EBI-21766676; Score: 0.35
DE  Interaction: P61081; IntAct: EBI-21805700; Score: 0.35
DE  Interaction: Q96EY4; IntAct: EBI-21806027; Score: 0.35
DE  Interaction: O75030; IntAct: EBI-21854855; Score: 0.35
DE  Interaction: Q86VS8; IntAct: EBI-21881416; Score: 0.35
DE  Interaction: Q96M83; IntAct: EBI-20914520; Score: 0.40
DE  Interaction: P02489; IntAct: EBI-25839275; Score: 0.56
DE  Interaction: P09172; IntAct: EBI-25840297; Score: 0.56
DE  Interaction: G5E9A7; IntAct: EBI-25842795; Score: 0.56
DE  Interaction: Q86V38; IntAct: EBI-25846622; Score: 0.56
DE  Interaction: P00488; IntAct: EBI-25852777; Score: 0.56
DE  Interaction: P22607; IntAct: EBI-25854248; Score: 0.56
DE  Interaction: P14136; IntAct: EBI-25858324; Score: 0.56
DE  Interaction: P28799; IntAct: EBI-25861115; Score: 0.56
DE  Interaction: P06396; IntAct: EBI-25864069; Score: 0.56
DE  Interaction: P04792; IntAct: EBI-25870985; Score: 0.56
DE  Interaction: P51608; IntAct: EBI-25875954; Score: 0.56
DE  Interaction: P19404; IntAct: EBI-25876902; Score: 0.56
DE  Interaction: P29474; IntAct: EBI-25878778; Score: 0.56
DE  Interaction: Q13153; IntAct: EBI-25879295; Score: 0.56
DE  Interaction: O60260; IntAct: EBI-25880365; Score: 0.56
DE  Interaction: O14832; IntAct: EBI-25882197; Score: 0.56
DE  Interaction: D3DTS7; IntAct: EBI-25883216; Score: 0.56
DE  Interaction: P60891; IntAct: EBI-25886508; Score: 0.56
DE  Interaction: Q92876; IntAct: EBI-25887704; Score: 0.56
DE  Interaction: Q86WV8; IntAct: EBI-25893605; Score: 0.56
DE  Interaction: P02766; IntAct: EBI-25894149; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25898536; Score: 0.56
DE  Interaction: P46379; IntAct: EBI-25903927; Score: 0.56
DE  Interaction: O14901; IntAct: EBI-25905328; Score: 0.56
DE  Interaction: O14908; IntAct: EBI-25913294; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25915590; Score: 0.56
DE  Interaction: Q9Y3C5; IntAct: EBI-25918945; Score: 0.56
DE  Interaction: O43464; IntAct: EBI-25920225; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25931972; Score: 0.56
DE  Interaction: P37840; IntAct: EBI-25942418; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25945460; Score: 0.56
DE  Interaction: P54252; IntAct: EBI-25974866; Score: 0.56
DE  Interaction: P54253; IntAct: EBI-25978588; Score: 0.56
DE  Interaction: Q13148; IntAct: EBI-25985998; Score: 0.56
DE  Interaction: Q92574; IntAct: EBI-26295987; Score: 0.40
DE  Interaction: Q8N4C8; IntAct: EBI-28943316; Score: 0.35
GO  GO:0015629;
GO  GO:0030424;
GO  GO:0031463;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0005802;
GO  GO:0003779;
GO  GO:0019964;
GO  GO:0004842;
GO  GO:0007010;
GO  GO:0006895;
GO  GO:0043066;
GO  GO:0043161;
GO  GO:1990390;
GO  GO:0015031;
GO  GO:0016567;
GO  GO:0035455;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIY
SQ  AHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEF
SQ  LKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVK
SQ  YSIQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVL
SQ  FAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTS
SQ  TCRTSVGVAVLGGFLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERY
SQ  NPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVG
SQ  GFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW
//
ID  Q8VCK5;
PN  Kelch-like protein 20;
GN  Klhl20;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN-gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8VCK5;
DR  UNIPROT: Q5DTH3;
DR  UNIPROT: Q8BWA2;
DR  Pfam: PF07707;
DR  Pfam: PF00651;
DR  Pfam: PF01344;
DR  PROSITE: PS50097;
DE  Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis. The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination. Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking. Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (By similarity). {ECO:0000250|UniProtKB:Q9Y2M5}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0031463;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0005802;
GO  GO:0003779;
GO  GO:0019964;
GO  GO:0004842;
GO  GO:0006895;
GO  GO:0043066;
GO  GO:0043161;
GO  GO:1990390;
GO  GO:0015031;
GO  GO:0016567;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVI
SQ  LSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQL
SQ  DPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSIQE
SQ  RRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVLFAVGG
SQ  WCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTSTCRTS
SQ  VGVAVLGGFLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERYNPQEN
SQ  RWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVGGFDGT
SQ  TYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW
//
ID  Q5R7B8;
PN  Kelch-like protein 20;
GN  KLHL20;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN-gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5R7B8;
DR  Pfam: PF07707;
DR  Pfam: PF00651;
DR  Pfam: PF01344;
DR  PROSITE: PS50097;
DE  Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis. The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination. Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking. Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (By similarity). {ECO:0000250|UniProtKB:Q9Y2M5}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0031463;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0005802;
GO  GO:0003779;
GO  GO:0019964;
GO  GO:0004842;
GO  GO:0006895;
GO  GO:0043066;
GO  GO:0043161;
GO  GO:1990390;
GO  GO:0015031;
GO  GO:0016567;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIY
SQ  AHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEF
SQ  LKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVK
SQ  YSTQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVL
SQ  FAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTS
SQ  TCRTSVGVAVLGGFLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERY
SQ  NPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVR
SQ  GFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW
//
ID  D3Z8N4;
PN  Kelch-like protein 20;
GN  Klhl20;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell projection, axon {ECO:0000269|PubMed:21670212}. Cell projection, dendrite {ECO:0000269|PubMed:21670212}. Note=Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN-gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (By similarity). {ECO:0000250}.
DR  UNIPROT: D3Z8N4;
DR  Pfam: PF07707;
DR  Pfam: PF00651;
DR  Pfam: PF01344;
DR  PROSITE: PS50097;
DE  Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis. The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination. Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking. Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (By similarity). {ECO:0000250|UniProtKB:Q9Y2M5}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0031463;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0005802;
GO  GO:0003779;
GO  GO:0019964;
GO  GO:0004842;
GO  GO:0006895;
GO  GO:0043066;
GO  GO:0043161;
GO  GO:1990390;
GO  GO:0015031;
GO  GO:0016567;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIY
SQ  AHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEF
SQ  LKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVK
SQ  YSIQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVL
SQ  FAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTS
SQ  TCRTSVGVAVLGGFLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERY
SQ  NPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVG
SQ  GFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW
//
ID  Q6DFF6;
PN  Kelch-like protein 20;
GN  klhl20;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.
DR  UNIPROT: Q6DFF6;
DR  Pfam: PF07707;
DR  Pfam: PF00651;
DR  Pfam: PF01344;
DR  PROSITE: PS50097;
DE  Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome. It also specifically mediates 'Lys-33'-linked ubiquitination (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031463;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0005802;
GO  GO:0019964;
GO  GO:0004842;
GO  GO:0006895;
GO  GO:0043066;
GO  GO:0043161;
GO  GO:1990390;
GO  GO:0015031;
GO  GO:0016567;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRRCLNTRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYVSDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVI
SQ  LSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFSYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQL
SQ  DPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSIQE
SQ  RRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVLFAVGG
SQ  WCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTSTCRTS
SQ  VGVAVLGGYLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERYNPQEN
SQ  RWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVGGFDGT
SQ  TYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW
//
ID  A0A0B4KEE4;
PN  Klaroid protein;
GN  koi;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18820457}. Note=Lam is required for perinuclear localization of Koi. {ECO:0000269|PubMed:18820457}.
DR  UNIPROT: A0A0B4KEE4;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (By similarity). Is required to nuclear migration in eye and to anchor klar in the nuclear membrane (PubMed:18820457). {ECO:0000250|UniProtKB:O94901, ECO:0000269|PubMed:18820457}.
DE  Reference Proteome: Yes;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0048471;
GO  GO:0043495;
GO  GO:0000724;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051647;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSENTYQIETRRRSRSKTPFLRSSCDHENCEHAGEEGHVHHLKRKSAAPNVQTIIEEHIVESSISKKTRAKAFAQLTSDY
SQ  SSDDMTPDAKRKQNSITATVTSILTKRSGGATSTPRNRSQLETTQNTLNSAQEKLNQSNGNLSSGNVSDYLAYIEYRDAG
SQ  EYWNKTPKTDYTYSELSPHRRQLAPGIVAMPNMSRKSLENHNDRVNYMVQQNPAQEEFIRRRYQSKYTQQVNYDSADELD
SQ  ATFGQQKQSWWLIRLIQLVVSSITTVWSRVTNLSATETTAYQNYHAKRQQSQQVGLWWKIVQTIGGGLASLLRYLYVFIG
SQ  SVLSLDTWLLRSSDAENKSKKRFLIFLLILLPLLLLSGWLLLQEDQRSAYVQRAEALLPLPLSIFGSLRSRFSNAGATLK
SQ  SWMEVPTVRSPQREAEAIKVNMASIEQNIQKALTAEEYENILNHVNSYVQQLVELKMQQHSKELAPQQIELFVKLMKENL
SQ  KQIMYKTELSEKDLSDLAIKLKLELQSSGGWQDGAKLSQANLEEITKLIKAEVHLHESHYTIQLDRIDFASLLERILAAP
SQ  ALADFVDARISLRVGELEPKESSGSSDAEVQIERLNREIAFIKLALSDKQAENADLHQSISNLKLGQEDLLERIQQHELS
SQ  QDRRFHGLLAEIENKLSALNDSQFALLNKQIKLSLVEILGFKQSTAGGSAGQLDDFDLQTWVRSMFVAKDYLEQQLLELN
SQ  KRTNNNIRDEIERSSILLMSDISQRLKREILLVVEAKHNESTKALKGHIREEEVRQIVKTVLAIYDADKTGLVDFALESA
SQ  GGQILSTRCTESYQTKSAQISVFGIPLWYPTNTPRVAISPNVQPGECWAFQGFPGFLVLKLNSLVYVTGFTLEHIPKSLS
SQ  PTGRIESAPRNFTVWGLEQEKDQEPVLFGDYQFEDNGASLQYFAVQNLDIKRPYEIVELRIETNHGHPTYTCLYRFRVHG
SQ  KPPAT
//
ID  Q5PU49;
PN  Protein kinase C delta type catalytic subunit;
GN  PRKCD;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q05655}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05655}. Nucleus {ECO:0000250|UniProtKB:Q05655}. Cell membrane {ECO:0000250|UniProtKB:Q05655}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q05655}. Mitochondrion {ECO:0000250|UniProtKB:Q05655}. Endomembrane system {ECO:0000250|UniProtKB:Q05655}. Note=Translocates to the mitochondria upon apoptotic stimulation. Upon activation, translocates to the plasma membrane followed by partial location to the endolysosomes. {ECO:0000250|UniProtKB:Q05655}.
DR  UNIPROT: Q5PU49;
DR  Pfam: PF00130;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti- apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N- formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. Involved in antifungal immunity by mediating phosphorylation and activation of CARD9 downstream of C-type lectin receptors activation, promoting interaction between CARD9 and BCL10, followed by activation of NF- kappa-B and MAP kinase p38 pathways (By similarity). May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin (By similarity). The catalytic subunit phosphorylates 14- 3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion. Phosphorylates ELAVL1 in response to angiotensin-2 treatment (By similarity). Phosphorylates mitochondrial phospholipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis (By similarity). Phosphorylates SMPD1 which induces SMPD1 secretion (By similarity). {ECO:0000250|UniProtKB:P28867, ECO:0000250|UniProtKB:Q05655}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0036019;
GO  GO:0005783;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0046872;
GO  GO:0004715;
GO  GO:0004697;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0006915;
GO  GO:0007049;
GO  GO:1904385;
GO  GO:0034644;
GO  GO:0042742;
GO  GO:0035556;
GO  GO:0030837;
GO  GO:0051490;
GO  GO:0034351;
GO  GO:0090331;
GO  GO:0018105;
GO  GO:0032930;
GO  GO:0006468;
GO  GO:2000303;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q05655};
SQ  MAPFLRIAFTSYELGSLQAADEASQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEP
SQ  MSEVTVGVSVLAERCKKNNXKAEFWLDLQPQAKVLMSVQYFLEDIDCRQSMHGEDEAKLPTMNRRGAIKQAKIHYIKNHE
SQ  FIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVYNYMS
SQ  PTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCQKKVANLCGINQKLLAEALNQVTQRSSRKSETESVGIYQNFERKPGVS
SQ  GDIAPGEDNGTYGKIWEGSTRCNIDNFIFHKVLGKGSFGKVLLVELKGKKEFFAIKALKKDVVLIDDDVECTMVEKRVLA
SQ  LAWENPFLTHLFCTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIVCGLQFLHNKGIIYRDLKLDNVMLD
SQ  QDGHIKIADFGMCKENIFGEKQASTFCGTPDYIAPEILQGLKYSFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRV
SQ  DTPHYPRWITKESKDILEKLLERDTTKRLGVTGNIKIHPFFKTINWTLLEKRAVEPPFKPKVKSPGDYSNFDQEFLNEKA
SQ  RLSYTDKNLIDSMDQTAFAGFSFVNPKFERFLEK
//
ID  Q05655;
PN  Protein kinase C delta type catalytic subunit;
GN  PRKCD;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:17303575, ECO:0000269|PubMed:17603046, ECO:0000269|PubMed:18285462}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12649167, ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:17603046}. Nucleus {ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:17603046, ECO:0000269|PubMed:18285462}. Cell membrane {ECO:0000269|PubMed:17303575, ECO:0000269|PubMed:17603046}; Peripheral membrane protein {ECO:0000305|PubMed:17603046}. Mitochondrion {ECO:0000269|PubMed:12649167}. Endomembrane system {ECO:0000269|PubMed:17303575}. Note=Translocates to the mitochondria upon apoptotic stimulation. Upon activation, translocates to the plasma membrane followed by partial location to the endolysosomes (PubMed:17303575). {ECO:0000269|PubMed:12649167, ECO:0000269|PubMed:17303575}.
DR  UNIPROT: Q05655;
DR  UNIPROT: B0KZ81;
DR  UNIPROT: B2R834;
DR  UNIPROT: Q15144;
DR  UNIPROT: Q86XJ6;
DR  PDB: 1YRK;
DR  PDB: 2YUU;
DR  Pfam: PF00130;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DR  OMIM: 176977;
DR  OMIM: 615559;
DR  DisGeNET: 5580;
DE  Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti- apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses (PubMed:21810427, PubMed:21406692). Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction (By similarity). Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis (PubMed:21810427, PubMed:21406692). In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53 (PubMed:21810427, PubMed:21406692). In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53 (PubMed:21810427, PubMed:21406692). In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation (By similarity). Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1 (PubMed:15774464). Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Involved in antifungal immunity by mediating phosphorylation and activation of CARD9 downstream of C-type lectin receptors activation, promoting interaction between CARD9 and BCL10, followed by activation of NF- kappa-B and MAP kinase p38 pathways (By similarity). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N- formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways (PubMed:19801500). May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA (PubMed:11748588). In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation (PubMed:16940418). Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release (PubMed:19587372). Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin (PubMed:11877440). The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion (By similarity). Phosphorylates ELAVL1 in response to angiotensin-2 treatment (PubMed:18285462). Phosphorylates mitochondrial phospholipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis (PubMed:12649167). Phosphorylates SMPD1 which induces SMPD1 secretion (PubMed:17303575). {ECO:0000250|UniProtKB:P28867, ECO:0000269|PubMed:11748588, ECO:0000269|PubMed:11877440, ECO:0000269|PubMed:12649167, ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:16940418, ECO:0000269|PubMed:17303575, ECO:0000269|PubMed:18285462, ECO:0000269|PubMed:19587372, ECO:0000269|PubMed:19801500, ECO:0000303|PubMed:21406692, ECO:0000303|PubMed:21810427}.
DE  Disease: Autoimmune lymphoproliferative syndrome 3 (ALPS3) [MIM:615559]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. CVID9 patients have B-cell deficiency and severe autoimmunity. {ECO:0000269|PubMed:23319571}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P00519; IntAct: EBI-8488876; Score: 0.40
DE  Interaction: P12931; IntAct: EBI-7607017; Score: 0.40
DE  Interaction: Q9H5V8; IntAct: EBI-7606833; Score: 0.67
DE  Interaction: P06241; IntAct: EBI-706296; Score: 0.74
DE  Interaction: P83312; IntAct: EBI-7063004; Score: 0.44
DE  Interaction: P14598; IntAct: EBI-7062990; Score: 0.44
DE  Interaction: P17677; IntAct: EBI-1267520; Score: 0.60
DE  Interaction: Q05655; IntAct: EBI-7482319; Score: 0.44
DE  Interaction: P29353; IntAct: EBI-2615019; Score: 0.53
DE  Interaction: Q5M824; IntAct: EBI-8428651; Score: 0.35
DE  Interaction: P48168; IntAct: EBI-7069266; Score: 0.44
DE  Interaction: Q9NYF8; IntAct: EBI-5333715; Score: 0.35
DE  Interaction: Q12816; IntAct: EBI-5652336; Score: 0.46
DE  Interaction: Q9NR28; IntAct: EBI-7806057; Score: 0.40
DE  Interaction: Q9JIY2; IntAct: EBI-7646605; Score: 0.35
DE  Interaction: Q14254; IntAct: EBI-6249310; Score: 0.35
DE  Interaction: P05771; IntAct: EBI-6256338; Score: 0.53
DE  Interaction: Q04759; IntAct: EBI-6256338; Score: 0.53
DE  Interaction: Q07021; IntAct: EBI-6376505; Score: 0.40
DE  Interaction: P41594; IntAct: EBI-6595666; Score: 0.27
DE  Interaction: P33993; IntAct: EBI-6875195; Score: 0.35
DE  Interaction: P24001; IntAct: EBI-8800964; Score: 0.73
DE  Interaction: P17947; IntAct: EBI-9547613; Score: 0.40
DE  Interaction: C6GKH1; IntAct: EBI-9547473; Score: 0.46
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.53
DE  Interaction: P11388; IntAct: EBI-9982299; Score: 0.68
DE  Interaction: Q02880; IntAct: EBI-9982310; Score: 0.35
DE  Interaction: P78527; IntAct: EBI-9984602; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-9986022; Score: 0.60
DE  Interaction: Q96A56; IntAct: EBI-9986115; Score: 0.40
DE  Interaction: P19878; IntAct: EBI-10040465; Score: 0.54
DE  Interaction: Q9GZU8; IntAct: EBI-11134877; Score: 0.35
DE  Interaction: P51114; IntAct: EBI-11134877; Score: 0.35
DE  Interaction: A5PLN9; IntAct: EBI-11134877; Score: 0.35
DE  Interaction: Q13523; IntAct: EBI-11134877; Score: 0.35
DE  Interaction: E7EVG6; IntAct: EBI-11134877; Score: 0.35
DE  Interaction: Q562R1; IntAct: EBI-11134877; Score: 0.35
DE  Interaction: P29401; IntAct: EBI-11134877; Score: 0.35
DE  Interaction: Q9BRD0; IntAct: EBI-11135975; Score: 0.35
DE  Interaction: O60231; IntAct: EBI-11135975; Score: 0.35
DE  Interaction: Q9P013; IntAct: EBI-11135975; Score: 0.35
DE  Interaction: Q3L8U1; IntAct: EBI-11135975; Score: 0.35
DE  Interaction: P61513; IntAct: EBI-11135975; Score: 0.35
DE  Interaction: Q8IV50; IntAct: EBI-11135975; Score: 0.35
DE  Interaction: O60814; IntAct: EBI-11135975; Score: 0.35
DE  Interaction: P52739; IntAct: EBI-11135975; Score: 0.35
DE  Interaction: Q9H3D4; IntAct: EBI-11292628; Score: 0.40
DE  Interaction: Q9BXL7; IntAct: EBI-11692838; Score: 0.62
DE  Interaction: Q9UDY8; IntAct: EBI-11692872; Score: 0.40
DE  Interaction: Q9Y4K3; IntAct: EBI-11692880; Score: 0.40
DE  Interaction: Q8N5V2; IntAct: EBI-21868110; Score: 0.35
DE  Interaction: Q9Y2R2; IntAct: EBI-15673502; Score: 0.44
DE  Interaction: Q9UBQ0; IntAct: EBI-25885434; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25938241; Score: 0.56
DE  Interaction: P17252; IntAct: EBI-28939125; Score: 0.35
GO  GO:0035578;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0036019;
GO  GO:0005783;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0005739;
GO  GO:0016363;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004699;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0043560;
GO  GO:0046872;
GO  GO:0004715;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0004697;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0032147;
GO  GO:0006915;
GO  GO:0042100;
GO  GO:0060326;
GO  GO:0007049;
GO  GO:1904385;
GO  GO:0070301;
GO  GO:0071447;
GO  GO:0034644;
GO  GO:0090398;
GO  GO:0042742;
GO  GO:0038096;
GO  GO:0016064;
GO  GO:0035556;
GO  GO:0008631;
GO  GO:0030837;
GO  GO:0051490;
GO  GO:0034351;
GO  GO:0050728;
GO  GO:0046627;
GO  GO:0043407;
GO  GO:0050732;
GO  GO:0090331;
GO  GO:0032091;
GO  GO:0042119;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:2001235;
GO  GO:2000304;
GO  GO:0032079;
GO  GO:2000753;
GO  GO:1900163;
GO  GO:0035307;
GO  GO:0042307;
GO  GO:2001022;
GO  GO:2000755;
GO  GO:0032930;
GO  GO:0043687;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:0032956;
GO  GO:2000303;
GO  GO:0043488;
GO  GO:0010469;
GO  GO:0007165;
GO  GO:0023021;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:17603046};
SQ  MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEP
SQ  VSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHE
SQ  FIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMS
SQ  PTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKT
SQ  GVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRV
SQ  LTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVL
SQ  LDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI
SQ  RVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNE
SQ  KARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED
//
ID  P28867;
PN  Protein kinase C delta type catalytic subunit;
GN  Prkcd;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q05655}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05655}. Nucleus {ECO:0000250|UniProtKB:Q05655}. Cell membrane {ECO:0000250|UniProtKB:Q05655}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q05655}. Mitochondrion {ECO:0000250|UniProtKB:Q05655}. Endomembrane system {ECO:0000250|UniProtKB:Q05655}. Note=Translocates to the mitochondria upon apoptotic stimulation. Upon activation, translocates to the plasma membrane followed by partial location to the endolysosomes. {ECO:0000250|UniProtKB:Q05655}.
DR  UNIPROT: P28867;
DR  UNIPROT: Q91V85;
DR  UNIPROT: Q9Z333;
DR  PDB: 1PTQ;
DR  PDB: 1PTR;
DR  PDB: 3UEJ;
DR  PDB: 3UEY;
DR  PDB: 3UFF;
DR  PDB: 3UGD;
DR  PDB: 3UGI;
DR  PDB: 3UGL;
DR  Pfam: PF00130;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti- apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction (PubMed:11976686, PubMed:11976687). Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage- induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up- regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation (PubMed:19917613). Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA (By similarity). In N-formyl- methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways (PubMed:18025218). Involved in antifungal immunity by mediating phosphorylation and activation of CARD9 downstream of C-type lectin receptors activation, promoting interaction between CARD9 and BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways (PubMed:22265677). May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion (PubMed:9705322). Phosphorylates ELAVL1 in response to angiotensin-2 treatment (By similarity). Phosphorylates mitochondrial phospholipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis (By similarity). Phosphorylates SMPD1 which induces SMPD1 secretion (By similarity). {ECO:0000250|UniProtKB:Q05655, ECO:0000269|PubMed:11976686, ECO:0000269|PubMed:11976687, ECO:0000269|PubMed:18025218, ECO:0000269|PubMed:19917613, ECO:0000269|PubMed:9705322}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9JKS4; IntAct: EBI-7048669; Score: 0.40
DE  Interaction: Q8WV44; IntAct: EBI-1551354; Score: 0.40
DE  Interaction: Q80U72; IntAct: EBI-1766131; Score: 0.27
DE  Interaction: Q07014; IntAct: EBI-8680025; Score: 0.35
DE  Interaction: P23242; IntAct: EBI-10763851; Score: 0.56
DE  Interaction: Q3UP24; IntAct: EBI-16006703; Score: 0.46
DE  Interaction: Q8CIN4; IntAct: EBI-16006728; Score: 0.35
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0036019;
GO  GO:0005783;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0016363;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0099524;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004699;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0043560;
GO  GO:0046872;
GO  GO:0004715;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0004697;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0070976;
GO  GO:0032147;
GO  GO:0006915;
GO  GO:0042100;
GO  GO:0060326;
GO  GO:0007049;
GO  GO:1904385;
GO  GO:0070301;
GO  GO:0071447;
GO  GO:0034599;
GO  GO:0034644;
GO  GO:0090398;
GO  GO:0032963;
GO  GO:0070779;
GO  GO:0042742;
GO  GO:0016064;
GO  GO:0035556;
GO  GO:0030837;
GO  GO:0051490;
GO  GO:0034351;
GO  GO:0046627;
GO  GO:0043407;
GO  GO:0050732;
GO  GO:0090331;
GO  GO:0042119;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0043065;
GO  GO:2001235;
GO  GO:2000304;
GO  GO:0032079;
GO  GO:0046326;
GO  GO:2000753;
GO  GO:0043406;
GO  GO:0043410;
GO  GO:1900163;
GO  GO:0035307;
GO  GO:0042307;
GO  GO:2001022;
GO  GO:2000755;
GO  GO:0032930;
GO  GO:0043687;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0032956;
GO  GO:2000303;
GO  GO:0042325;
GO  GO:0006979;
GO  GO:0023021;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q05655};
SQ  MAPFLRISFNSYELGSLQVEDEASQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKTTFDAHIYEGRVIQIVLMRAAEDP
SQ  VSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMCVQYFLEDGDCKQSMRSEEEAKFPTMNRRGAIKQAKIHYIKNHE
SQ  FIATFFGQPTFCSVCKEFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTATNSRDTIFQKERFNIDMPHRFKVYNYMS
SQ  PTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRSSRKLDTTESVGIYQGFEKKPEV
SQ  SGSDILDNNGTYGKIWEGSTRCTLENFTFQKVLGKGSFGKVLLAELKGKDKYFAIKCLKKDVVLIDDDVECTMVEKRVLA
SQ  LAWESPFLTHLICTFQTKDHLFFVMEFLNGGDLMFHIQDKGRFELYRATFYAAEIICGLQFLHSKGIIYRDLKLDNVMLD
SQ  RDGHIKIADFGMCKENIFGEGRASTFCGTPDYIAPEILQGLKYSFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRV
SQ  DTPHYPRWITKESKDIMEKLFERDPDKRLGVTGNIRIHPFFKTINWSLLEKRKVEPPFKPKVKSPSDYSNFDPEFLNEKP
SQ  QLSFSDKNLIDSMDQEAFHGFSFVNPKFEQFLDI
//
ID  P09215;
PN  Protein kinase C delta type catalytic subunit;
GN  Prkcd;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17562707}. Nucleus {ECO:0000269|PubMed:17562707}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17562707}. Cell membrane {ECO:0000250|UniProtKB:Q05655}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q05655}. Mitochondrion {ECO:0000250|UniProtKB:Q05655}. Endomembrane system {ECO:0000250|UniProtKB:Q05655}. Note=Translocates to the mitochondria upon apoptotic stimulation. Upon activation, translocates to the plasma membrane followed by partial location to the endolysosomes. {ECO:0000250|UniProtKB:Q05655}.
DR  UNIPROT: P09215;
DR  UNIPROT: Q6DG48;
DR  UNIPROT: Q9JK29;
DR  UNIPROT: Q9JL03;
DR  PDB: 1BDY;
DR  Pfam: PF00130;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti- apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N- formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. Involved in antifungal immunity by mediating phosphorylation and activation of CARD9 downstream of C-type lectin receptors activation, promoting interaction between CARD9 and BCL10, followed by activation of NF- kappa-B and MAP kinase p38 pathways (By similarity). May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin (By similarity). The catalytic subunit phosphorylates 14- 3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion. Phosphorylates ELAVL1 in response to angiotensin-2 treatment (By similarity). Phosphorylates mitochondrial phospholipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis (By similarity). Phosphorylates SMPD1 which induces SMPD1 secretion (By similarity). {ECO:0000250|UniProtKB:P28867, ECO:0000250|UniProtKB:Q05655}. Truncated isoform 2 is inactive.
DE  Reference Proteome: Yes;
DE  Interaction: O35658; IntAct: EBI-6376153; Score: 0.40
DE  Interaction: O35796; IntAct: EBI-6376392; Score: 0.27
DE  Interaction: P53667; IntAct: EBI-12598115; Score: 0.40
DE  Interaction: P36871; IntAct: EBI-22239685; Score: 0.35
DE  Interaction: Q6ZUJ8; IntAct: EBI-22239749; Score: 0.35
DE  Interaction: P27986; IntAct: EBI-22239735; Score: 0.35
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0036019;
GO  GO:0005783;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0016363;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0099524;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004699;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0043560;
GO  GO:0019900;
GO  GO:0046872;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0004697;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0004713;
GO  GO:0070976;
GO  GO:0032147;
GO  GO:0007568;
GO  GO:0006915;
GO  GO:0042100;
GO  GO:0060326;
GO  GO:0007049;
GO  GO:1904385;
GO  GO:0042149;
GO  GO:0070301;
GO  GO:0071447;
GO  GO:0032869;
GO  GO:0034599;
GO  GO:0034644;
GO  GO:0090398;
GO  GO:0032963;
GO  GO:0070779;
GO  GO:0042742;
GO  GO:0016064;
GO  GO:0035556;
GO  GO:0030837;
GO  GO:0051490;
GO  GO:0034351;
GO  GO:0046627;
GO  GO:0043407;
GO  GO:0050732;
GO  GO:0090331;
GO  GO:0042119;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0043065;
GO  GO:2001235;
GO  GO:2000304;
GO  GO:0032079;
GO  GO:0046326;
GO  GO:2000753;
GO  GO:0043406;
GO  GO:0043410;
GO  GO:1900163;
GO  GO:0035307;
GO  GO:0042307;
GO  GO:2001022;
GO  GO:2000755;
GO  GO:0032930;
GO  GO:0043687;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0032956;
GO  GO:2000303;
GO  GO:0042325;
GO  GO:0043200;
GO  GO:0045471;
GO  GO:0009749;
GO  GO:0009408;
GO  GO:0042542;
GO  GO:0001666;
GO  GO:0009612;
GO  GO:0014070;
GO  GO:0010243;
GO  GO:0006979;
GO  GO:0009410;
GO  GO:0023021;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q05655};
SQ  MAPFLRISFNSYELGSLQAEDDASQPFCAVKMKEALTTDRGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEDP
SQ  MSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMCVQYFLEDGDCKQSMRSEEEAMFPTMNRRGAIKQAKIHYIKNHE
SQ  FIATFFGQPTFCSVCKEFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTATNSRDTIFQKERFNIDMPHRFKVYNYMS
SQ  PTFCDHCGTLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQKASRKPETPETVGIYQGFEKKTAV
SQ  SGNDIPDNNGTYGKIWEGSNRCRLENFTFQKVLGKGSFGKVLLAELKGKERYFAIKYLKKDVVLIDDDVECTMVEKRVLA
SQ  LAWENPFLTHLICTFQTKDHLFFVMEFLNGGDLMFHIQDKGRFELYRATFYAAEIICGLQFLHGKGIIYRDLKLDNVMLD
SQ  KDGHIKIADFGMCKENIFGENRASTFCGTPDYIAPEILQGLKYSFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRV
SQ  DTPHYPRWITKESKDIMEKLFERDPAKRLGVTGNIRLHPFFKTINWNLLEKRKVEPPFKPKVKSPSDYSNFDPEFLNEKP
SQ  QLSFSDKNLIDSMDQTAFKGFSFVNPKYEQFLE
//
ID  Q02156;
PN  Protein kinase C epsilon type;
GN  PRKCE;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17603037, ECO:0000269|PubMed:19542546}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17603037}. Cell membrane {ECO:0000269|PubMed:17603037}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P16054}. Nucleus {ECO:0000250|UniProtKB:P16054}. Note=Translocated to plasma membrane in epithelial cells stimulated by HGF (PubMed:17603037). Associated with the Golgi at the perinuclear site in pre-passage fibroblasts (By similarity). In passaging cells, translocated to the cell periphery (By similarity). Translocated to the nucleus in PMA-treated cells (By similarity). {ECO:0000250|UniProtKB:P16054, ECO:0000269|PubMed:17603037}.
DR  UNIPROT: Q02156;
DR  UNIPROT: B0LPH7;
DR  UNIPROT: Q32MQ3;
DR  UNIPROT: Q53SL4;
DR  UNIPROT: Q53SM5;
DR  UNIPROT: Q9UE81;
DR  PDB: 2WH0;
DR  PDB: 5LIH;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DR  OMIM: 176975;
DR  DisGeNET: 5581;
DE  Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin- dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell- cell detachment prior to migration. In HeLa cells, contributes to hepatocyte growth factor (HGF)-induced cell migration, and in human corneal epithelial cells, plays a critical role in wound healing after activation by HGF. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). In prostate cancer cells, interacts with and phosphorylates STAT3, which increases DNA-binding and transcriptional activity of STAT3 and seems to be essential for prostate cancer cell invasion. Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. Phosphorylates NLRP5/MATER and may thereby modulate AKT pathway activation in cumulus cells (PubMed:19542546). {ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:1374067, ECO:0000269|PubMed:15355962, ECO:0000269|PubMed:16757566, ECO:0000269|PubMed:17603037, ECO:0000269|PubMed:17875639, ECO:0000269|PubMed:17875724, ECO:0000269|PubMed:19542546}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-9689399; Score: 0.55
DE  Interaction: P31689; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P15056; IntAct: EBI-8559942; Score: 0.59
DE  Interaction: P17252; IntAct: EBI-8559959; Score: 0.56
DE  Interaction: Q15349; IntAct: EBI-8560070; Score: 0.40
DE  Interaction: P16284; IntAct: EBI-1766278; Score: 0.44
DE  Interaction: Q07812; IntAct: EBI-1767339; Score: 0.40
DE  Interaction: P63104; IntAct: EBI-7150817; Score: 0.73
DE  Interaction: O95819; IntAct: EBI-3443522; Score: 0.00
DE  Interaction: P15924; IntAct: EBI-3447870; Score: 0.00
DE  Interaction: P08238; IntAct: EBI-6423388; Score: 0.64
DE  Interaction: P14618; IntAct: EBI-9353379; Score: 0.44
DE  Interaction: Q9HAW7; IntAct: EBI-9543892; Score: 0.44
DE  Interaction: C6GKH1; IntAct: EBI-9548220; Score: 0.40
DE  Interaction: O75807; IntAct: EBI-9979270; Score: 0.40
DE  Interaction: Q86XR7; IntAct: EBI-15585787; Score: 0.44
DE  Interaction: Q02156; IntAct: EBI-15585807; Score: 0.44
DE  Interaction: Q15139; IntAct: EBI-15740808; Score: 0.44
DE  Interaction: Q9UBS0; IntAct: EBI-22086386; Score: 0.35
DE  Interaction: P29597; IntAct: EBI-22091428; Score: 0.35
DE  Interaction: Q9BPZ7; IntAct: EBI-22186575; Score: 0.52
DE  Interaction: O15530; IntAct: EBI-22186610; Score: 0.40
DE  Interaction: O60256; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P11908; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P12236; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P27708; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P31939; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P31947; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P50395; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P50453; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P50452; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: O75830; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P30740; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P62258; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P62979; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P68363; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: P68371; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q00796; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q02790; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q02952; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q14145; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q14257; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q15843; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q16658; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q3ZCM7; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q58FF8; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q9BV86; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q9NYF8; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q9Y2W1; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: Q9Y617; IntAct: EBI-25378052; Score: 0.35
DE  Interaction: O43252; IntAct: EBI-25389608; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-25389608; Score: 0.35
DE  Interaction: P11413; IntAct: EBI-25389608; Score: 0.35
DE  Interaction: P28838; IntAct: EBI-25389608; Score: 0.35
DE  Interaction: P34897; IntAct: EBI-25389608; Score: 0.35
DE  Interaction: Q13011; IntAct: EBI-25389608; Score: 0.35
DE  Interaction: Q16822; IntAct: EBI-25389608; Score: 0.35
DE  Interaction: Q9UHL4; IntAct: EBI-25389608; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-25938167; Score: 0.56
DE  Interaction: P37840; IntAct: EBI-25940781; Score: 0.56
DE  Interaction: O15111; IntAct: EBI-28930872; Score: 0.35
DE  Interaction: Q9NZT2; IntAct: EBI-28938908; Score: 0.35
DE  Interaction: Q9H3G5; IntAct: EBI-28938908; Score: 0.35
DE  Interaction: Q14289; IntAct: EBI-28938908; Score: 0.35
DE  Interaction: P61011; IntAct: EBI-28938908; Score: 0.35
DE  Interaction: Q8IV63; IntAct: EBI-28942353; Score: 0.35
DE  Interaction: Q8WU08; IntAct: EBI-28944017; Score: 0.35
DE  Interaction: Q9BXA7; IntAct: EBI-28946010; Score: 0.35
GO  GO:0071944;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0045111;
GO  GO:0043231;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0071889;
GO  GO:0003785;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004699;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0035276;
GO  GO:0046872;
GO  GO:0004672;
GO  GO:0004697;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0030546;
GO  GO:0006915;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0031589;
GO  GO:0071361;
GO  GO:0071456;
GO  GO:0071380;
GO  GO:0051649;
GO  GO:0038096;
GO  GO:0030073;
GO  GO:0035556;
GO  GO:0031663;
GO  GO:0035641;
GO  GO:0002281;
GO  GO:0000165;
GO  GO:0070254;
GO  GO:0031397;
GO  GO:2000650;
GO  GO:0018105;
GO  GO:0030838;
GO  GO:0010811;
GO  GO:2001031;
GO  GO:0032467;
GO  GO:0010634;
GO  GO:0010763;
GO  GO:0043123;
GO  GO:0032024;
GO  GO:0050996;
GO  GO:0043410;
GO  GO:0070257;
GO  GO:1903078;
GO  GO:0032230;
GO  GO:0090303;
GO  GO:0006468;
GO  GO:0061178;
GO  GO:0050730;
GO  GO:0051279;
GO  GO:0043278;
GO  GO:0007165;
GO  GO:0051932;
GO  GO:0035669;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIE
SQ  LAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAV
SQ  RRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVN
SQ  MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRR
SQ  KKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQA
SQ  KRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKD
SQ  RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILN
SQ  GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKA
SQ  FMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQI
SQ  NQEEFKGFSYFGEDLMP
//
ID  P16054;
PN  Protein kinase C epsilon type;
GN  Prkce;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02156}. Cell membrane {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17611075}. Nucleus {ECO:0000269|PubMed:17611075}. Note=Translocated to plasma membrane in epithelial cells stimulated by HGF (By similarity). Associated with the Golgi at the perinuclear site in pre-passage fibroblasts (PubMed:17611075). In passaging cells, translocated to the cell periphery (PubMed:17611075). Translocated to the nucleus in PMA-treated cells (PubMed:17611075). {ECO:0000250|UniProtKB:Q02156, ECO:0000269|PubMed:17611075}.
DR  UNIPROT: P16054;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin- dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell- cell detachment prior to migration. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin- induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma- aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. Phosphorylates NLRP5/MATER and may thereby modulate AKT pathway activation in cumulus cells (By similarity). {ECO:0000250|UniProtKB:Q02156, ECO:0000269|PubMed:11746497, ECO:0000269|PubMed:12407104, ECO:0000269|PubMed:15949469, ECO:0000269|PubMed:16270034, ECO:0000269|PubMed:16445938, ECO:0000269|PubMed:16757566, ECO:0000269|PubMed:18604201}.
DE  Reference Proteome: Yes;
DE  Interaction: P05480; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P70313; IntAct: EBI-298523; Score: 0.35
DE  Interaction: O35643; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P14901; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q61221; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P31938; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q05769; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q9R0B8; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P29477; IntAct: EBI-298523; Score: 0.35
DE  Interaction: O35558; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q63844; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q61194; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q9WTU6; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q91Y86; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P49138; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P47811; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P31750; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P97504; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P06240; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P23242; IntAct: EBI-298523; Score: 0.56
DE  Interaction: P70304; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P51667; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P51637; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P31001; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q61033; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q62486; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q921M4; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P67778; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P58771; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q6P3Z7; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q61275; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q9QVP9; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P23927; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P14602; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q61696; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P45376; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q9CQR4; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9D6R2; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P61979; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9CR62; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q03265; IntAct: EBI-299155; Score: 0.35
DE  Interaction: O35737; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9D051; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9CRB9; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P98086; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9DCT8; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P70318; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9CZX8; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P62270; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P62908; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q8BFR5; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9Z130; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q91Z83; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q99020; IntAct: EBI-299155; Score: 0.35
DE  Interaction: O88569; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P62806; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P43277; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q60668; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q8BMS1; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q60932; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q62425; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9CQA3; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P48962; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q99JY0; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P16858; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P17182; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9CQ62; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P07310; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P56480; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P51881; IntAct: EBI-299155; Score: 0.35
DE  Interaction: O70433; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9JJW5; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P63038; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9DC41; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9JKS4; IntAct: EBI-299155; Score: 0.56
DE  Interaction: Q9CRA2; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q8CI51; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P50462; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q64727; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P20152; IntAct: EBI-299155; Score: 0.64
DE  Interaction: O55134; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P48787; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P19123; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P49813; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q02566; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P48678; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P47757; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P47754; IntAct: EBI-299155; Score: 0.35
DE  Interaction: Q9JI91; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P35438; IntAct: EBI-396959; Score: 0.46
DE  Interaction: Q9R0U5; IntAct: EBI-7274427; Score: 0.52
DE  Interaction: P07356; IntAct: EBI-7274491; Score: 0.52
DE  Interaction: Q921I1; IntAct: EBI-7274461; Score: 0.52
DE  Interaction: Q9WVM1; IntAct: EBI-7274517; Score: 0.52
DE  Interaction: P60710; IntAct: EBI-7274504; Score: 0.52
DE  Interaction: Q9CQV8; IntAct: EBI-7000302; Score: 0.64
DE  Interaction: Q7TMB8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: F6SEU4; IntAct: EBI-16733301; Score: 0.53
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16726570; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16736255; Score: 0.35
DE  Interaction: P16056; IntAct: EBI-27118288; Score: 0.35
GO  GO:0071944;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0098978;
GO  GO:0000139;
GO  GO:0045111;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0031594;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0099523;
GO  GO:0030315;
GO  GO:0071889;
GO  GO:0003785;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004699;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0035276;
GO  GO:0046872;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0004697;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0017124;
GO  GO:0030546;
GO  GO:0005102;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0031589;
GO  GO:0071361;
GO  GO:0071456;
GO  GO:0036120;
GO  GO:0071380;
GO  GO:0007635;
GO  GO:0051649;
GO  GO:0030073;
GO  GO:0035556;
GO  GO:0031663;
GO  GO:0035641;
GO  GO:0002281;
GO  GO:0000165;
GO  GO:0070254;
GO  GO:0043066;
GO  GO:0051562;
GO  GO:0010917;
GO  GO:0031397;
GO  GO:0051280;
GO  GO:0018105;
GO  GO:0030838;
GO  GO:0010811;
GO  GO:2001031;
GO  GO:0032467;
GO  GO:0010634;
GO  GO:0010763;
GO  GO:0043123;
GO  GO:0032024;
GO  GO:0050996;
GO  GO:0043410;
GO  GO:0070257;
GO  GO:0032230;
GO  GO:0090303;
GO  GO:0006468;
GO  GO:0061178;
GO  GO:0019216;
GO  GO:0050730;
GO  GO:0051279;
GO  GO:2000300;
GO  GO:0043278;
GO  GO:0051932;
GO  GO:0035669;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIE
SQ  LAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAV
SQ  RRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDEVGSQRFSVN
SQ  MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRR
SQ  KKLAAGAESPQPASGNSPSEDDRSKSAPTSPCDQELKELENNIRKALSFDNRGEEHRASSATDGQLASPGENGEVRPGQA
SQ  KRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKD
SQ  RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGIMN
SQ  GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKA
SQ  FMTKNPHKRLGCVAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPILTLVDEAIIKQI
SQ  NQEEFKGFSYFGEDLMP
//
ID  P10830;
PN  Protein kinase C epsilon type;
GN  PRKCE;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02156}. Cell membrane {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P16054}. Nucleus {ECO:0000250|UniProtKB:P16054}. Note=Translocated to plasma membrane in epithelial cells stimulated by HGF (By similarity). Associated with the Golgi at the perinuclear site in pre-passage fibroblasts (By similarity). In passaging cells, translocated to the cell periphery (By similarity). Translocated to the nucleus in PMA-treated cells (By similarity). {ECO:0000250|UniProtKB:P16054, ECO:0000250|UniProtKB:Q02156}.
DR  UNIPROT: P10830;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin- dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell- cell detachment prior to migration. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin- induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma- aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1 (By similarity). Phosphorylates NLRP5/MATER and may thereby modulate AKT pathway activation in cumulus cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q02156}.
DE  Reference Proteome: Yes;
GO  GO:0071944;
GO  GO:0005856;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003785;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004699;
GO  GO:0046872;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0007155;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0002376;
GO  GO:0031663;
GO  GO:0030838;
GO  GO:0032467;
GO  GO:0010634;
GO  GO:0010763;
GO  GO:0090303;
GO  GO:0006468;
GO  GO:0035669;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIE
SQ  LAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAV
SQ  RRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKVAGLKKQETPDEVGSQRFSVN
SQ  MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRR
SQ  KKLIGGAESPQPTSGSSPSEEDRSKSAPTSPCDQELKELENNIRKALSFDNRGEEHRAASSTDGQLGSPENGEVRQGQAK
SQ  RLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDR
SQ  LFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG
SQ  VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAF
SQ  MTKNPHKRLGCVAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQIN
SQ  QEEFKGFSYFGEDLMP
//
ID  P09216;
PN  Protein kinase C epsilon type;
GN  Prkce;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02156}. Cell membrane {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9360998}. Nucleus {ECO:0000250|UniProtKB:P16054}. Note=Translocated to plasma membrane in epithelial cells stimulated by HGF (By similarity). Associated with the Golgi at the perinuclear site in pre-passage fibroblasts (By similarity). In passaging cells, translocated to the cell periphery (By similarity). Translocated to the nucleus in PMA-treated cells (By similarity). {ECO:0000250|UniProtKB:P16054, ECO:0000250|UniProtKB:Q02156}.
DR  UNIPROT: P09216;
DR  PDB: 1GMI;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin- dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell- cell detachment prior to migration. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin- induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma- aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. Phosphorylates NLRP5/MATER and may thereby modulate AKT pathway activation in cumulus cells (By similarity). {ECO:0000250|UniProtKB:Q02156, ECO:0000269|PubMed:11278835, ECO:0000269|PubMed:12665800, ECO:0000269|PubMed:17157309}.
DE  Reference Proteome: Yes;
DE  Interaction: P15336; IntAct: EBI-6049627; Score: 0.44
DE  Interaction: P48442; IntAct: EBI-6140389; Score: 0.40
DE  Interaction: O35658; IntAct: EBI-6376159; Score: 0.40
DE  Interaction: P53667; IntAct: EBI-12598123; Score: 0.40
DE  Interaction: Q62920; IntAct: EBI-12597968; Score: 0.37
GO  GO:0071944;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0098978;
GO  GO:0000139;
GO  GO:0016020;
GO  GO:0005739;
GO  GO:0031594;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0099523;
GO  GO:0030315;
GO  GO:0071889;
GO  GO:0003785;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004699;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0035276;
GO  GO:0046872;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0004697;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0017124;
GO  GO:0030546;
GO  GO:0005102;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0031589;
GO  GO:0071361;
GO  GO:0071456;
GO  GO:0036120;
GO  GO:0071380;
GO  GO:0051649;
GO  GO:0030073;
GO  GO:0035556;
GO  GO:0031663;
GO  GO:0035641;
GO  GO:0002281;
GO  GO:0000165;
GO  GO:0070254;
GO  GO:0043066;
GO  GO:0051562;
GO  GO:0010917;
GO  GO:0031397;
GO  GO:0051280;
GO  GO:0018105;
GO  GO:0030838;
GO  GO:0010811;
GO  GO:2001031;
GO  GO:0032467;
GO  GO:0010634;
GO  GO:0010763;
GO  GO:0043123;
GO  GO:0032024;
GO  GO:0050996;
GO  GO:0043410;
GO  GO:0070257;
GO  GO:0032230;
GO  GO:0090303;
GO  GO:0006468;
GO  GO:0061178;
GO  GO:0019216;
GO  GO:0050730;
GO  GO:0051279;
GO  GO:2000300;
GO  GO:0043278;
GO  GO:0051932;
GO  GO:0035669;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIE
SQ  LAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAV
SQ  RRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDEVGSQRFSVN
SQ  MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRR
SQ  KKLAAGAESPQPASGNSPSEDDRSKSAPTSPCDQELKELENNIRKALSFDNRGEEHRASSSTDGQLASPGENGEVRQGQA
SQ  KRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKD
SQ  RLFFVMEYVNGGDLMFQIQRSRKFDEPRSGFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHSKLADFGMCKEGILN
SQ  GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKA
SQ  FMTKNPHKRLGCVAAQNGEDAIKQHPFFKEIDWVLLEQKKMKPPFKPRIKTKRDVNNFDQDFTREEPILTLVDEAIVKQI
SQ  NQEEFKGFSYFGEDLMP
//
ID  P05128;
PN  Protein kinase C gamma type;
GN  PRKCG;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P63318}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P63318}; Peripheral membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250|UniProtKB:P63318}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Translocates to synaptic membranes on stimulation. {ECO:0000250|UniProtKB:P63318}.
DR  UNIPROT: P05128;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-activated, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5- dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock. {ECO:0000250|UniProtKB:P05129, ECO:0000250|UniProtKB:P63318, ECO:0000250|UniProtKB:P63319}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0008270;
GO  GO:0035556;
GO  GO:0043524;
GO  GO:1901799;
GO  GO:0031397;
GO  GO:0018105;
GO  GO:0042752;
GO  GO:0032095;
GO  GO:0043278;
GO  GO:0048265;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  RPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTD
SQ  DPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTSDEIHV
SQ  TVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDF
SQ  MGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCNLLQKFEACNYPLELYERVRTGPSSSPIPSPSPSPTDSK
SQ  RCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPH
SQ  FLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIK
SQ  ITDFGMCKENVFPGSTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYP
SQ  KSLSREAVAICKGFLTKHPAKRLGSGPDGEPTIRAHGFFRWIDWDRLERLEIAPPFRPRPCGRSGENFDKFFTRAAPALT
SQ  PPDRLVLASIDQAEFQGFTYVNPDFVHPDARSPISPTPVPVM
//
ID  P05129;
PN  Protein kinase C gamma type;
GN  PRKCG;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P63318}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:29053796}; Peripheral membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250|UniProtKB:P63318}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Translocates to synaptic membranes on stimulation. {ECO:0000250|UniProtKB:P63318}.
DR  UNIPROT: P05129;
DR  UNIPROT: B7Z8Q0;
DR  PDB: 2E73;
DR  PDB: 2UZP;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DR  OMIM: 176980;
DR  OMIM: 605361;
DR  DisGeNET: 5582;
DE  Function: Calcium-activated, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5- dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress (By similarity). Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (By similarity). {ECO:0000250|UniProtKB:P63318, ECO:0000250|UniProtKB:P63319, ECO:0000269|PubMed:16377624}.
DE  Disease: Spinocerebellar ataxia 14 (SCA14) [MIM:605361]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA14 is an autosomal dominant cerebellar ataxia (ADCA). {ECO:0000269|PubMed:12644968, ECO:0000269|PubMed:29053796}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95831; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: Q9NRD5; IntAct: EBI-953356; Score: 0.00
DE  Interaction: Q86UR1; IntAct: EBI-953368; Score: 0.00
DE  Interaction: O00471; IntAct: EBI-953374; Score: 0.00
DE  Interaction: Q8TD31; IntAct: EBI-953380; Score: 0.00
DE  Interaction: P18031; IntAct: EBI-7078187; Score: 0.37
DE  Interaction: P48168; IntAct: EBI-7069192; Score: 0.44
DE  Interaction: P08238; IntAct: EBI-6423400; Score: 0.56
DE  Interaction: P17252; IntAct: EBI-21789938; Score: 0.64
DE  Interaction: Q9QZC1; IntAct: EBI-15767920; Score: 0.44
DE  Interaction: O60256; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: O95816; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P11908; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P17066; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P48741; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P31689; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P36776; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P60891; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P68371; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: Q14257; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: Q14558; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: Q16822; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: Q58FF8; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: Q9BQ70; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: Q9Y6Y0; IntAct: EBI-25379555; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-25390652; Score: 0.35
DE  Interaction: P11413; IntAct: EBI-25390652; Score: 0.35
DE  Interaction: Q14766; IntAct: EBI-25390652; Score: 0.35
DE  Interaction: Q8N6K7; IntAct: EBI-25885474; Score: 0.56
DE  Interaction: Q8TDR4; IntAct: EBI-25885466; Score: 0.56
DE  Interaction: Q96KS9; IntAct: EBI-25885458; Score: 0.56
DE  Interaction: O75925; IntAct: EBI-25885450; Score: 0.56
DE  Interaction: P08727; IntAct: EBI-25885442; Score: 0.56
DE  Interaction: Q8IXB1; IntAct: EBI-28931575; Score: 0.35
DE  Interaction: P05771; IntAct: EBI-28931584; Score: 0.35
GO  GO:0044305;
GO  GO:0005911;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0099524;
GO  GO:0014069;
GO  GO:0099523;
GO  GO:0097060;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004672;
GO  GO:0004697;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0004712;
GO  GO:0008270;
GO  GO:0007268;
GO  GO:0007635;
GO  GO:0060384;
GO  GO:0035556;
GO  GO:0007611;
GO  GO:0060291;
GO  GO:0043524;
GO  GO:1901799;
GO  GO:0042177;
GO  GO:0031397;
GO  GO:0018105;
GO  GO:0016310;
GO  GO:0032425;
GO  GO:0099171;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0042752;
GO  GO:0050764;
GO  GO:0032095;
GO  GO:2000300;
GO  GO:0043278;
GO  GO:0048265;
GO  GO:1990911;
GO  GO:0009636;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEF
SQ  VTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGR
SQ  LQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRL
SQ  SVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPS
SQ  SSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEK
SQ  RVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRD
SQ  LKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDE
SQ  EELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSG
SQ  ENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM
//
ID  Q4R4U2;
PN  Protein kinase C gamma type;
GN  PRKCG;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P63318}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P63318}; Peripheral membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250|UniProtKB:P63318}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Translocates to synaptic membranes on stimulation. {ECO:0000250|UniProtKB:P63318}.
DR  UNIPROT: Q4R4U2;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-activated, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5- dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock. {ECO:0000250|UniProtKB:P05129, ECO:0000250|UniProtKB:P63318, ECO:0000250|UniProtKB:P63319}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0106310;
GO  GO:0008270;
GO  GO:0043524;
GO  GO:1901799;
GO  GO:0031397;
GO  GO:0006468;
GO  GO:0042752;
GO  GO:0032095;
GO  GO:0043278;
GO  GO:0048265;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAGLGPGGGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEF
SQ  VTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGR
SQ  LQLEIRAPTADEIHITVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRL
SQ  SVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPS
SQ  SSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEK
SQ  RVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRD
SQ  LKLDNVVLDAEGLIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDE
SQ  EELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSG
SQ  ENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM
//
ID  P63318;
PN  Protein kinase C gamma type;
GN  Prkcg;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17904530}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:17904530, ECO:0000269|PubMed:18473171}; Peripheral membrane protein. Synapse, synaptosome {ECO:0000269|PubMed:18473171}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Translocates to synaptic membranes on stimulation. {ECO:0000269|PubMed:18473171}.
DR  UNIPROT: P63318;
DR  UNIPROT: P05697;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-activated, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5- dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contribute to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (PubMed:23185022). {ECO:0000269|PubMed:11246146, ECO:0000269|PubMed:11278552, ECO:0000269|PubMed:11356858, ECO:0000269|PubMed:11731061, ECO:0000269|PubMed:17904530, ECO:0000269|PubMed:23185022, ECO:0000269|PubMed:8269509, ECO:0000269|PubMed:9323205}.
DE  Reference Proteome: Yes;
DE  Interaction: P35922; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P35438; IntAct: EBI-396959; Score: 0.46
DE  Interaction: Q9JKS4; IntAct: EBI-7048648; Score: 0.40
DE  Interaction: O08785; IntAct: EBI-7314742; Score: 0.44
DE  Interaction: P63101; IntAct: EBI-2255635; Score: 0.35
DE  Interaction: Q8BPN8; IntAct: EBI-6272767; Score: 0.35
DE  Interaction: Q8R4A3; IntAct: EBI-6392577; Score: 0.40
DE  Interaction: Q0PHV7; IntAct: EBI-6392575; Score: 0.40
DE  Interaction: Q7TN08; IntAct: EBI-6392579; Score: 0.40
DE  Interaction: P49286; IntAct: EBI-11576525; Score: 0.35
DE  Interaction: Q80YA9; IntAct: EBI-16727082; Score: 0.35
DE  Interaction: Q7TMB8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q7TMY8; IntAct: EBI-16730939; Score: 0.35
DE  Interaction: F6SEU4; IntAct: EBI-16733301; Score: 0.53
DE  Interaction: Q80YT7; IntAct: EBI-16732484; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
DE  Interaction: Q9EP53; IntAct: EBI-16734894; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16726570; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16736255; Score: 0.35
GO  GO:0044305;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0099524;
GO  GO:0014069;
GO  GO:0099523;
GO  GO:0097060;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004672;
GO  GO:0004697;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0004712;
GO  GO:0008270;
GO  GO:0007268;
GO  GO:0007635;
GO  GO:0060384;
GO  GO:0035556;
GO  GO:0007611;
GO  GO:0060291;
GO  GO:0043524;
GO  GO:1901799;
GO  GO:0042177;
GO  GO:0031397;
GO  GO:0018105;
GO  GO:0016310;
GO  GO:0032425;
GO  GO:0099171;
GO  GO:0046777;
GO  GO:0042752;
GO  GO:0050764;
GO  GO:0032095;
GO  GO:2000300;
GO  GO:0043278;
GO  GO:0048265;
GO  GO:1990911;
GO  GO:0009636;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAGLGPGGGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEF
SQ  VTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGR
SQ  LQLEIRAPTSDEIHITVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTKTVKATLNPVWNETFVFNLKPGDVERRL
SQ  SVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPS
SQ  SSPIPSPSPSPTDSKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEK
SQ  RVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRD
SQ  LKLDNVMLDAEGHIKITDFGMCKENVFPGSTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDE
SQ  EELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIAPPFRPRPCGRSG
SQ  ENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM
//
ID  P10829;
PN  Protein kinase C gamma type;
GN  PRKCG;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P63318}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P63318}; Peripheral membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250|UniProtKB:P63318}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Translocates to synaptic membranes on stimulation. {ECO:0000250|UniProtKB:P63318}.
DR  UNIPROT: P10829;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-activated, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5- dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum (By similarity). Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock. {ECO:0000250|UniProtKB:P05129, ECO:0000250|UniProtKB:P63318, ECO:0000250|UniProtKB:P63319, ECO:0000269|PubMed:15642736}.
DE  Reference Proteome: Yes;
DE  Interaction: P62258; IntAct: EBI-7332081; Score: 0.40
GO  GO:0070161;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0106310;
GO  GO:0008270;
GO  GO:0043524;
GO  GO:1901799;
GO  GO:0031397;
GO  GO:0006468;
GO  GO:0042752;
GO  GO:0032095;
GO  GO:0043278;
GO  GO:0048265;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAGLGPGGGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEF
SQ  VTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRTVPSLCGVDHTERRGR
SQ  LQLEIRAPTSDEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRL
SQ  SVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPS
SQ  SSPIPSPSPSPTDSKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEK
SQ  RVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRD
SQ  LKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDE
SQ  EELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIAPPFRPRPCGRSG
SQ  ENFDKFFTRAAPAVTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPSSPVPVPVM
//
ID  P63319;
PN  Protein kinase C gamma type;
GN  Prkcg;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P63318}. Cytoplasm, perinuclear region. Cell membrane {ECO:0000269|PubMed:12471040, ECO:0000269|PubMed:14688616}; Peripheral membrane protein. Synapse, synaptosome {ECO:0000269|PubMed:14688616}. Cell projection, dendrite {ECO:0000269|PubMed:10336135}. Note=Translocates to synaptic membranes on stimulation. {ECO:0000269|PubMed:14688616}.
DR  UNIPROT: P63319;
DR  UNIPROT: P05697;
DR  UNIPROT: Q5FWS3;
DR  PDB: 1TBN;
DR  PDB: 1TBO;
DR  Pfam: PF00130;
DR  Pfam: PF00168;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS50004;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Calcium-activated, phospholipid- and diacylglycerol (DAG)- dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5- dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (By similarity). {ECO:0000250|UniProtKB:P63318, ECO:0000269|PubMed:10336135, ECO:0000269|PubMed:12471040, ECO:0000269|PubMed:15705736, ECO:0000269|PubMed:15936117, ECO:0000269|PubMed:9271501, ECO:0000269|PubMed:9287082}.
DE  Reference Proteome: Yes;
DE  Interaction: P53667; IntAct: EBI-12598091; Score: 0.52
DE  Interaction: Q5XIE8; IntAct: EBI-26438079; Score: 0.35
GO  GO:0044305;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0099524;
GO  GO:0014069;
GO  GO:0099523;
GO  GO:0097060;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004672;
GO  GO:0004697;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0004712;
GO  GO:0008270;
GO  GO:0007268;
GO  GO:0007635;
GO  GO:0060384;
GO  GO:0035556;
GO  GO:0007611;
GO  GO:0060291;
GO  GO:0043524;
GO  GO:1901799;
GO  GO:0042177;
GO  GO:0031397;
GO  GO:0018105;
GO  GO:0016310;
GO  GO:0032425;
GO  GO:0099171;
GO  GO:0046777;
GO  GO:0042752;
GO  GO:0050764;
GO  GO:0032095;
GO  GO:2000300;
GO  GO:0043278;
GO  GO:0048265;
GO  GO:1990911;
GO  GO:0009636;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAGLGPGGGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEF
SQ  VTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGR
SQ  LQLEIRAPTSDEIHITVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTKTVKATLNPVWNETFVFNLKPGDVERRL
SQ  SVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPS
SQ  SSPIPSPSPSPTDSKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEK
SQ  RVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRD
SQ  LKLDNVMLDAEGHIKITDFGMCKENVFPGSTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDE
SQ  EELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIAPPFRPRPCGRSG
SQ  ENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM
//
ID  Q751U7;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: Q751U7;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSTKDTSGQSGYANDIRKLGEQTAHVSEQVLVQQERQRLGALEELHQSIIQIAEENSFVTPIKKDAANVHIDPRGIAVSV
SQ  QQFKQLAEVLKVTHLEQETLDNFLRYTISDNDQLLDIKSVADSRYARLAEEVCQLEQEELRHLENEIISLNGNITEQTTK
SQ  VIDANEKVKEECLEVSNGIERCWGLLNELETLRSTTDEGNVELGPLEETYQKWKSVDHFLQQKLHLKEQLRVLEDTRKSL
SQ  SEVTKSSGNRAPDLDASEKFVTYRLLDSMWKKQFVDTTKIRDLELYPRTGKIQFQVADTIYVLAISGDQISNIQLFNDKL
SQ  PAADLENNTQDLNKRFLGTSDVRRVVDFITHQQAVPQAQVH
//
ID  Q6FSC7;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: Q6FSC7;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MEAQLHELQEEITRSSDLVLTEQDKRLQGTLREIDQSIRKLIETSDYLKLSGDADSLIDIKQLEVKSRELDSLMDLLRKL
SQ  YWREESLDLFLKYTINSDAEQVPVFSDTDPKYQSLQDEVSHLRDDVMTVKNQEIDQITGEILQVAHEITEKQDQVNMLYL
SQ  ETTNELDKCWELLDEWQRLQDDQRITKNEDNSNRKDTELNAMEECYEEWKTLEELAVLNDNLQKQIDELEKVDNKAINST
SQ  QLAEESIVNTVQLNDLIDMWKRRIIASIHEDISEIVLYPYSRKLQLRVANRYTIIIQLDKHQTHDGKSTIHDIDLFTEQD
SQ  SRIIPMRELRKQVLQECKGHSNILQALKNIINRVINNDN
//
ID  Q6CV05;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: Q6CV05;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTHYHSEYYSEVEKFEYQVTHVTEQILQEQDRLRGSTLHEYNQTILQLVSDYEMFNSNGQCDPSEINLPLEKLESWTNSL
SQ  KQIHLELESIDNFLRYAIPSDQTILNLSKFNESKYETLQAEVSELRDINVVQLQKEIESLQQQITTKSDENLLISEKIKE
SQ  SCLEASQDIDQCWKLLEQLEAYENANPSTEVITTTDPAFSTYNQWKWNQLAESELKHINQQLITLRATKEKLDKVFSKRS
SQ  ELETSPKSIETFTSYQLLSQLWRSKFIRQLLPDIANLEVYPQSGKLKFEVGIMQVIMQIESGIIKSVSLFSYELSYDRIE
SQ  TIKEDILGRIEHQKSLFKVLVVITDYIVNSL
//
ID  C5DK07;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  559295;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: C5DK07;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADDPTINGLELQLNAAEEHATALTEEALQNQDLHYKEVVEQLKRSVEQLVEDNESLFTAVDLPPEVDPTCISGRILDLA
SQ  QLTQQLKSTHLQQETLDNFLRYTISSTDILQLESESDERYASVSRAVSQLQDNDIIQLDSEVDQIKQDIRKAGQTIADQR
SQ  EALNELCLETGNLADECHTLLSELEEATRTREMVEKQAAVEVTNDHPVEEMYASWQSLKEELQQESHLRRHLNQLKQSKA
SQ  SLEAILGTKNGNEHKDTNVMQEYASYDAFIRFWISKFTNKEMENLEVFPRSNKFQFTHRGTDVVISLGPRGISRVELYGK
SQ  GIPLEKIAAARKDVNEEASRGEELYMSINRIIDKIKEHTTVS
//
ID  A7TFD7;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  436907;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: A7TFD7;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  METQAVKTIRDELRELENTVAQASDMVLSEQDHRNASAIREMTQSVIAMSKENSLISVSNEIDYNEEIGNLAIDPSLIDE
SQ  KIKQSNNFVELLKLTHLEQEALDYFLRYTISSTNTLELESTSDPKFVSLENEVTELENKTLTEHRDKIQEAKKDISDKSK
SQ  DLANKQDQINELCLGAANSVDECWKMLNELEDIHSQRDNDVKETLSQDTTTTSDLIEETYKEWSSLQTSLTELNNSKDEL
SQ  DQLIAFKNEKHKDNDSTKIRNANIKNKTITENVKMLKLLINFWESNFIVPGSKKSKLSNLEVYPQTKKFQFKCAEQYTVI
SQ  IQLNQNGGSIKSIEIFENDGKSVQENKNLSSLILNKYKNPLSSYPIFQVINDIVEELK
//
ID  B3LFD9;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  285006;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: B3LFD9;
DR  Pfam: PF17097;
DE  Function: Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKI
SQ  LSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQE
SQ  TGHNFAEKQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQR
SQ  LTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDM
SQ  QYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEANSKFNNKYRNNTKVQIFEVMDDIISELTNE
//
ID  C7GKW3;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  574961;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: C7GKW3;
DR  Pfam: PF17097;
DE  Function: Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKI
SQ  LSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQE
SQ  TGHNFAEKQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQR
SQ  LTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDM
SQ  QYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEANSKFNNKYRNNTKVQIFEVMDDIISELTNE
//
ID  B5VH51;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  545124;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: B5VH51;
DR  Pfam: PF17097;
DE  Function: Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKI
SQ  LSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQE
SQ  TGHNFAEKQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQR
SQ  LTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDM
SQ  QYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEANSKFNNKYRNNTKVQIFEVMDDIISELTNE
//
ID  A6ZZB9;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: A6ZZB9;
DR  Pfam: PF17097;
DE  Function: Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKI
SQ  LSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQE
SQ  TGHNFAEKQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQR
SQ  LTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDM
SQ  QYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEANSKFNNKYRNNTKVQIFEVMDDIISELTNE
//
ID  C8Z692;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  643680;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: C8Z692;
DR  Pfam: PF17097;
DE  Function: Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKI
SQ  LSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQE
SQ  TGHNFAEKQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQR
SQ  LTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDM
SQ  QYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEANSKFNNKYRNNTKVQIFEVMDDIISELTNE
//
ID  Q04431;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Chromosome, centromere, kinetochore. Note=Localizes to the nuclear side of the spindle pole body.
DR  UNIPROT: Q04431;
DR  UNIPROT: D6VTF3;
DR  UNIPROT: Q6Q537;
DR  Pfam: PF17097;
DE  Function: Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint. {ECO:0000269|PubMed:19893618}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-3664804; Score: 0.35
DE  Interaction: P53148; IntAct: EBI-7384815; Score: 0.66
DE  Interaction: P32361; IntAct: EBI-390519; Score: 0.37
DE  Interaction: P53743; IntAct: EBI-861238; Score: 0.00
DE  Interaction: P40568; IntAct: EBI-1543715; Score: 0.35
DE  Interaction: P39731; IntAct: EBI-1543771; Score: 0.35
DE  Interaction: P40460; IntAct: EBI-2343287; Score: 0.37
DE  Interaction: Q07978; IntAct: EBI-2344403; Score: 0.37
DE  Interaction: P28004; IntAct: EBI-2344578; Score: 0.37
DE  Interaction: P43592; IntAct: EBI-2344838; Score: 0.37
DE  Interaction: P11484; IntAct: EBI-3698908; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3717706; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3722662; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3731786; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3753047; Score: 0.35
DE  Interaction: P25300; IntAct: EBI-16253676; Score: 0.00
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0051382;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKI
SQ  LSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQE
SQ  TGHNFAERQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQR
SQ  LTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDM
SQ  QYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEASSKFNNKYRNNTKVQIFEVMDDIISELTNE
//
ID  C5DZ48;
PN  Spindle pole body component KRE28;
GN  KRE28;
OS  559307;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to the nuclear side of the spindle pole body. {ECO:0000250}.
DR  UNIPROT: C5DZ48;
DR  UNIPROT: B2G406;
DR  Pfam: PF17097;
DE  Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MKSDLDGYEVRIKSLENQTAHYSEQALLEQEQRVLASLREITQNVIAMGQENSLVEIKGELESKEESELVIDPSGFQEKI
SQ  DTFVELVELLKVTHLEQETLDNFLRYTISSSNLLQINSVQDAKYVELESQVKELEQGTLESHKREIEATKGQIKNLCQEL
SQ  SMAQDSINETFLDTSNALEECDALLNELTQLRMEKQTSEEADTIEDDPVSQTYEDWESLQKSKLELRLLEEETSRLQSRV
SQ  ESYEDYQKRSRQLSNNDPRMLQNHKALELLVELWMTKFLPQPGISHLELFPQSRKFQFDVEPTFTVVITLADQTTFQNVQ
SQ  VYRKDAKSLVMDHGLNDEIKNSYLGTNNIYNGLNDIIHTLQRRVQAKGSN
//
ID  A0A1I9LN01;
PN  Protein LONG AFTER FAR-RED 3;
GN  LAF3;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14645728}.
DR  UNIPROT: A0A1I9LN01;
DR  UNIPROT: F4IY42;
DR  UNIPROT: Q7Y048;
DR  UNIPROT: Q7Y049;
DR  UNIPROT: Q93ZE1;
DR  UNIPROT: Q9LY60;
DR  Pfam: PF07969;
DE  Function: Required for phyA-controlled responses to continuous far-red light (FRc) conditions, including the inhibition of hypocotyl elongation and the regulation of XTH15/XTR7 expression. {ECO:0000269|PubMed:14645728}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0016810;
GO  GO:0009704;
GO  GO:0010218;
GO  GO:0009845;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTGWYEFPVMIGFVSAAVFLLISVAYLPLLNDLYWSTLKSLTPPAGIVADLLVTNGTIFTSDSSLPFADSMAIRNGRILK
SQ  VGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWN
SQ  NDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPW
SQ  VKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDELSWKDFQDVYLYADSSKKMMIRTCLFFPITTWSRLLDLK
SQ  LQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMIL
SQ  DMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALL
SQ  ALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSW
SQ  DEFSKDVSASVLATYVGGKQLYP
//
ID  P08928;
PN  Lamin Dm0;
GN  Lam;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:7593280, ECO:0000269|PubMed:9199347}. Nucleus inner membrane {ECO:0000269|PubMed:16439308}. Nucleus envelope {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:8999964, ECO:0000269|PubMed:9199347, ECO:0000269|PubMed:9632815}. Nucleus lamina {ECO:0000269|PubMed:18723885}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:27402967}. Cytoplasm {ECO:0000269|PubMed:9199347}. Note=Nuclear periphery (PubMed:7593280). At metaphase and anaphase, weakly expressed in the nuclear envelope and spindle poles (PubMed:16439308). Expression in oocyte cytoplasm increases after stages 6 to 7 of egg development (PubMed:9199347). In spermatocytes detected at the spindle envelope, spindle poles and astral membrane throughout meiosis I, whereas mostly depleted in meiosis II (PubMed:27402967). Colocalizes with nuclear pore complex component Nup107 throughout meiosis I (PubMed:27402967). {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:7593280, ECO:0000269|PubMed:9199347}.
DR  UNIPROT: P08928;
DR  UNIPROT: Q9VMQ0;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin (PubMed:3126192, PubMed:15035436). May have a role in the localization of the LEM domain proteins Ote, bocks and MAN1 to the nuclear membrane (PubMed:15035436, PubMed:16439308). In spermatocytes, plays a role in maintaining type-A lamin LamC nuclear localization; regulates meiotic cytokinesis by maintaining the structure of the spindle envelope, and by contributing to the formation of the contractile ring and central spindle (PubMed:27402967). Required for nuclear migration and to link the microtubule organizing center (MTOC) to the nucleus (PubMed:14617811). In addition, is required for nuclear envelope localization of klar (PubMed:14617811). {ECO:0000269|PubMed:14617811, ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:3126192}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VR64; IntAct: EBI-251111; Score: 0.00
DE  Interaction: P52295; IntAct: EBI-275111; Score: 0.00
DE  Interaction: P20240; IntAct: EBI-873490; Score: 0.50
DE  Interaction: Q9VD23; IntAct: EBI-281902; Score: 0.00
DE  Interaction: Q8T3J9; IntAct: EBI-281906; Score: 0.00
DE  Interaction: Q9VAU6; IntAct: EBI-281910; Score: 0.00
DE  Interaction: Q9XTM1; IntAct: EBI-510092; Score: 0.00
DE  Interaction: P16568; IntAct: EBI-871614; Score: 0.27
DE  Interaction: P25028; IntAct: EBI-872894; Score: 0.27
DE  Interaction: O01382; IntAct: EBI-873330; Score: 0.27
DE  Interaction: P08928; IntAct: EBI-873494; Score: 0.27
DE  Interaction: P34082; IntAct: EBI-9928090; Score: 0.53
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: Q24247; IntAct: EBI-9936906; Score: 0.35
DE  Interaction: Q9V9S0; IntAct: EBI-9937938; Score: 0.35
DE  Interaction: Q9VMV9; IntAct: EBI-9939888; Score: 0.35
DE  Interaction: Q9VPX2; IntAct: EBI-9940633; Score: 0.46
DE  Interaction: Q9VMT1; IntAct: EBI-9940945; Score: 0.35
DE  Interaction: P23226; IntAct: EBI-9942879; Score: 0.35
DE  Interaction: Q8IQX8; IntAct: EBI-9943015; Score: 0.35
DE  Interaction: Q9VT04; IntAct: EBI-9943330; Score: 0.35
DE  Interaction: Q8SXF0; IntAct: EBI-9943546; Score: 0.35
DE  Interaction: A0A0B4KGY6; IntAct: EBI-9952257; Score: 0.35
DE  Interaction: M9NFI9; IntAct: EBI-9959939; Score: 0.35
DE  Interaction: Q8IPM8; IntAct: EBI-9961408; Score: 0.35
GO  GO:0005737;
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005641;
GO  GO:0005637;
GO  GO:0005652;
GO  GO:0005634;
GO  GO:0000922;
GO  GO:0003682;
GO  GO:0005102;
GO  GO:0005200;
GO  GO:0007417;
GO  GO:0040003;
GO  GO:0001745;
GO  GO:0048546;
GO  GO:0035262;
GO  GO:0031507;
GO  GO:0070828;
GO  GO:0007112;
GO  GO:0007110;
GO  GO:0007084;
GO  GO:0008285;
GO  GO:0050777;
GO  GO:0006998;
GO  GO:0071763;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0006997;
GO  GO:0030838;
GO  GO:2000433;
GO  GO:1900182;
GO  GO:1905832;
GO  GO:0090435;
GO  GO:0048137;
GO  GO:0007283;
GO  GO:0007430;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSKSRRAGTATPQPGNTSTPRPPSAGPQPPPPSTHSQTASSPLSPTRHSRVAEKVELQNLNDRLATYIDRVRNLETENS
SQ  RLTIEVQTTRDTVTRETTNIKNIFEAELLETRRLLDDTARDRARAEIDIKRLWEENEELKNKLDKKTKECTTAEGNVRMY
SQ  ESRANELNNKYNQANADRKKLNEDLNEALKELERLRKQFEETRKNLEQETLSRVDLENTIQSLREELSFKDQIHSQEINE
SQ  SRRIKQTEYSEIDGRLSSEYDAKLKQSLQELRAQYEEQMQINRDEIQSLYEDKIQRLQEAAARTSNSTHKSIEELRSTRV
SQ  RIDALNANINELEQANADLNARIRDLERQLDNDRERHGQEIDLLEKELIRLREEMTQQLKEYQDLMDIKVSLDLEIAAYD
SQ  KLLVGEEARLNITPATNTATVQSFSQSLRNSTRATPSRRTPSAAVKRKRAVVDESEDHSVADYYVSASAKGNVEIKEIDP
SQ  EGKFVRLFNKGSEEVAIGGWQLQRLINEKGPSTTYKFHRSVRIEPNGVITVWSADTKASHEPPSSLVMKSQKWVSADNTR
SQ  TILLNSEGEAVANLDRIKRIVSQHTSSSRLSRRRSVTAVDGNEQLYHQQGDPQQSNEKCAIM
//
ID  Q03427;
PN  Lamin-C;
GN  LamC;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus {ECO:0000269|PubMed:7593280}. Nucleus lamina {ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:27402967}. Note=Nuclear periphery (PubMed:7593280). In premeiotic nuclei of primary spermatocytes, localization to the nuclear lamina depends on type-B lamin Lam. In spermatocytes, temporarily depleted between anaphase I and telophase I, and anaphase II and telophase II. {ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:7593280}.
DR  UNIPROT: Q03427;
DR  UNIPROT: Q24374;
DR  UNIPROT: Q9V729;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin (By similarity). In spermatocytes, regulates cytokinesis during meiosis (PubMed:27402967). {ECO:0000250|UniProtKB:P08928, ECO:0000269|PubMed:27402967}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VJ29; IntAct: EBI-198363; Score: 0.00
DE  Interaction: Q8T0N1; IntAct: EBI-504244; Score: 0.00
DE  Interaction: O76417; IntAct: EBI-510610; Score: 0.37
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0034399;
GO  GO:0070732;
GO  GO:0005200;
GO  GO:0006325;
GO  GO:0031507;
GO  GO:0007112;
GO  GO:0060415;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0090435;
GO  GO:0030833;
GO  GO:0035989;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSARRVTLNTRVSRASTSTPVGGASTSSRVGATSPTSPTRTSRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNL
SQ  AQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVN
SQ  GKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQVHTQELTETRSRRQIE
SQ  ISEIDGRLSRQYEAKLQQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAK
SQ  LQNLEDTNAGLNARIRELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQEYQGLMDIKVSLDLEIAAYDKLLCGEER
SQ  RLNIESPGRPTTDSGISSNGSHLTASASSRSGRVTPSGRRSATPGISGSSAVKRRRTVIDESEDRTLSEYSVNAAAKGDL
SQ  EIIEADVEGRFIKLHNKGTEEINLTGWQLTRIAGDEELAFKFSRGSKVLGGASVTIWSVDAGTAHDPPNNLVMKKKWPVA
SQ  NSMRSVLANADKEDVASYDRVRANVSSHTSRHRSSGTPSTGFTLGSGAGSTGVRSLFSLLF
//
ID  P09010;
PN  Lamin-L(I);
GN  LAML1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side.
DR  UNIPROT: P09010;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
DE  Reference Proteome: Yes;
GO  GO:0005882;
GO  GO:0005637;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MATATPSGPRSSGRRSSMSTPLSPTRITRLQEKVDLQELNDRLALYIDTVRSLESENSLLHVQVTEREEVRSREVSGIKE
SQ  LYETELADARRSLDDTAREKARLQLELSKVSVEHQDLQASFSKRESELESTQARFRETEALLNSKNAALATAQSENKSLQ
SQ  GEVEDLKAEIGQLGSALALAKKQLEEEILMKVDLENRCQSLIEELNFRKNIYEEEIKETSRRHETRLVEVDSGRQVDYEY
SQ  KLSQALSEMREQQESQIGLYKEELEQTYQSKLENARLASEMNSSAVNSTREELMESRIRIDSLTSQLSELQKESRAWHDR
SQ  MQELEDMLAKEKDNSRKMLAEREREMADIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSRVTVS
SQ  RASSSRAVRTTKGKRKRIDVEESEASSSVSIDHSAAATGDVSIEEVDVDGKYIRLKNNSEKDHPLGGWELTRTIGEASVN
SQ  FKFTSRYVLKAEQTVTIWAADAGVKASPPSDLIWKNQNSWGTGEDVKATLKNSQGEEVAQRTTIYTTNIPEEEFEEGEEI
SQ  FEETAKEFHYPQQKSGNKNCAIM
//
ID  P21910;
PN  Lamin-L(II);
GN  LAML2;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side.
DR  UNIPROT: P21910;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
DE  Reference Proteome: Yes;
GO  GO:0005882;
GO  GO:0005637;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MATTTPSRSTRSSMQSPARGTSTPLSPTRISRLQEKEELRHLNDRLAVYIDRVRALELENDRLMVKISEKEEVTTREVSG
SQ  IKNLYESELADARKVLDETARERARLQIELGKFRSDLDELNKNYKKKDADLSTAQGRIKDLEALFHRSEAELGTALGEKR
SQ  SLEAEVADLRAQLSKTEDAHRVAKKQLEKETLMRVDFENRMQSLQEEMDFRKNIYEEESRETRKRHERRIVEVDRGHHYD
SQ  YESKLAQALDELRKQHDEQVKMYKEELEQTYQAKLDNIKRSSDHNDKAANTALEELTERRMRIETLGYQLSGLQKQANAA
SQ  EERIRELEELLSSDRDKYRKLLDSKEREMAEMRDQMQQQLNEYQELLDVKLALDLEINAYRKLLEGEEERLKLSPSPESR
SQ  VTVSRATSSSSSATRTSRSKRRRVEEEYEEGGASTGFGAGHSLGSSRITASEGSSRTITSGQSSTTRFHLSQQASATGSI
SQ  SIEEIDLEGKYVHLKNNSDKDQSLGNWRLKRKIGEEEEIVYKFTPKYVLKAGQSVKIYSADAGVAHSPPSILVWKNQSSW
SQ  GTGSNIRTYLVNTEEEEVAVRTVTKSVLRNVEEEEDEDADFGEEDLFHQQGDPRTTSRGCSVM
//
ID  P10999;
PN  Lamin-L(III);
GN  LAML3;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side.
DR  UNIPROT: P10999;
DR  UNIPROT: P23420;
DR  UNIPROT: Q6AZG7;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
DE  Reference Proteome: Yes;
GO  GO:0005882;
GO  GO:0005637;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MATSTPSRAREHASAAQSPGSPTRISRMQEKEDLRHLNDRLAAYIERVRSLEADKSLLKIQLEEREEVSSREVTNLRQLY
SQ  ETELADARKLLDQTANERARLQVELGKVREEYRQLQARNSKKENDLSLAQNQLRDLESKLNTKEAELATALSGKRGLEEQ
SQ  LQEQRAQIAGLESSLRDTTKQLHDEMLWRVDLENKMQTIREQLDFQKNIHTQEVKEIKKRHDTRIVEIDSGRRVEFESKL
SQ  AEALQELRRDHEQQILEYKEHLEKNFSAKLENAQLAAAKNSDYASATREEIMATKLRVDTLSSQLNHYQKQNSALEAKVR
SQ  DLQDMLDRAHDMHRRQMTEKDREVTEIRQTLQGQLEEYEQLLDVKLALDMEINAYRKMLEGEEQRLKLSPSPSQRSTVSR
SQ  ASTSQTSRLLRGKKRKLDETGRSVTKRSYKVVQQASSTGPVSVEDIDPEGNYVRLLNNTEEDFSLHGWVVKRMHMSLPEI
SQ  AFKLPCRFILKSSQRVTIWAAGAGAVHSPPTDLVWKSQKTWGTGDNIKITLLDSTGEECAERTLYRVIGEEGETDEDFVE
SQ  EEELERQFRSQSHQSVDPSCSIM
//
ID  P42167;
PN  Thymopentin;
GN  TMPO;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane; Single-pass type II membrane protein. Note=Tightly associated with the nuclear lamina. [Isoform Zeta]: Cytoplasm {ECO:0000269|PubMed:18403046}.
DR  UNIPROT: P42167;
DR  UNIPROT: A2T926;
DR  UNIPROT: Q14861;
DR  Pfam: PF03020;
DR  Pfam: PF08198;
DR  PROSITE: PS50954;
DR  PROSITE: PS50955;
DR  OMIM: 188380;
DR  DisGeNET: 7112;
DE  Function: May help direct the assembly of the nuclear lamina and thereby help maintain the structural organization of the nuclear envelope. Possible receptor for attachment of lamin filaments to the inner nuclear membrane. May be involved in the control of initiation of DNA replication through its interaction with NAKAP95. Thymopoietin (TP) and Thymopentin (TP5) may play a role in T- cell development and function. TP5 is an immunomodulating pentapeptide.
DE  Reference Proteome: Yes;
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P00519; IntAct: EBI-1958393; Score: 0.40
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-11061883; Score: 0.57
DE  Interaction: P0DTD1; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P20700; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P35222; IntAct: EBI-8577520; Score: 0.40
DE  Interaction: P06241; IntAct: EBI-1961535; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-1964262; Score: 0.40
DE  Interaction: P16333; IntAct: EBI-1967089; Score: 0.40
DE  Interaction: Q00005; IntAct: EBI-2211497; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-5297130; Score: 0.44
DE  Interaction: Q77M19; IntAct: EBI-6268389; Score: 0.35
DE  Interaction: O14862; IntAct: EBI-9995694; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q99JP4; IntAct: EBI-11005491; Score: 0.35
DE  Interaction: O95229; IntAct: EBI-11007376; Score: 0.35
DE  Interaction: O14646; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q6IE81; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q7KZ85; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P35232; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q9BXS6; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P98160; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P62807; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: O95696; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P26640; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P49916; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P61421; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P17480; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q10589; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q14978; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P46100; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P55197; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: B4E2V5; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q9P2E9; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q8WWQ0; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: E7ESK6; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q9BW71; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P42766; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: O95251; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: P23258; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q96B26; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q8NHU3; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q969G5; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q9Y587; IntAct: EBI-11139678; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-11155257; Score: 0.35
DE  Interaction: Q99IB8; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q8NBJ4; IntAct: EBI-24667677; Score: 0.56
DE  Interaction: Q8WZ60; IntAct: EBI-24574881; Score: 0.56
DE  Interaction: P27105; IntAct: EBI-24649281; Score: 0.56
DE  Interaction: P06821; IntAct: EBI-12577493; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-12578858; Score: 0.35
DE  Interaction: C5E519; IntAct: EBI-12583021; Score: 0.35
DE  Interaction: C5E524; IntAct: EBI-12584280; Score: 0.35
DE  Interaction: Q14191; IntAct: EBI-16155310; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.42
DE  Interaction: P68431; IntAct: EBI-16793336; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: Q9NQB0; IntAct: EBI-21265942; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: Q8NHP6; IntAct: EBI-25617558; Score: 0.35
DE  Interaction: Q5U458; IntAct: EBI-26450034; Score: 0.35
DE  Interaction: P06401; IntAct: EBI-26871590; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-28938584; Score: 0.35
DE  Interaction: Q86YV6; IntAct: EBI-28942265; Score: 0.35
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0005521;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLPAGTNSKGPPDFSSDEEREPTPVLGSG
SQ  AAAAGRSRAAVGRKATKKTDKPRQEDKDDLDVTELTNEDLLDQLVKYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSST
SQ  PLPTISSSAENTRQNGSNDSDRYSDNEEDSKIELKLEKREPLKGRAKTPVTLKQRRVEHNQSYSQAGITETEWTSGSSKG
SQ  GPLQALTRESTRGSRRTPRKRVETSEHFRIDGPVISESTPIAETIMASSNESLVVNRVTGNFKHASPILPITEFSDIPRR
SQ  APKKPLTRAEVGEKTEERRVERDILKEMFPYEASTPTGISASCRRPIKGAAGRPLELSDFRMEESFSSKYVPKYVPLADV
SQ  KSEKTKKGRSIPVWIKILLFVVVAVFLFLVYQAMETNQVNPFSNFLHVDPRKSN
//
ID  Q61029;
PN  Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gamma;
GN  Tmpo;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Chromosome {ECO:0000250}. Note=Tightly associated with the nuclear lamina. {ECO:0000250}.
DR  UNIPROT: Q61029;
DR  UNIPROT: Q3UCI5;
DR  UNIPROT: Q61030;
DR  UNIPROT: Q61031;
DR  UNIPROT: Q61032;
DR  Pfam: PF03020;
DR  Pfam: PF08198;
DR  PROSITE: PS50954;
DR  PROSITE: PS50955;
DE  Function: May help direct the assembly of the nuclear lamina and thereby help maintain the structural organization of the nuclear envelope. Possible receptor for attachment of lamin filaments to the inner nuclear membrane. May be involved in the control of initiation of DNA replication through its interaction with NAKAP95 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q64321; IntAct: EBI-6172093; Score: 0.50
DE  Interaction: O88895; IntAct: EBI-6172144; Score: 0.35
DE  Interaction: O88609; IntAct: EBI-13951426; Score: 0.35
DE  Interaction: P70326; IntAct: EBI-16360068; Score: 0.35
GO  GO:0000785;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0006355;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLAAGANSKGPPDFSSDEEREPTPVLGSG
SQ  ASVGRGRGAVGRKATKKTDKPRLEDKDDLDVTELSNEELLDQLVRYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTP
SQ  LPTVSSSAENTRQNGSNDSDRYSDNDEDSKIELKLEKREPLKGRAKTPVTLKQRRTEHNQSYSQAGVTETEWTSGSSTGG
SQ  PLQALTRESTRGSRRTPRKRVETSQHFRIDGAVISESTPIAETIKASSNESLVANRLTGNFKHASSILPITEFSDITRRT
SQ  PKKPLTRAEVGEKTEERRVDRDILKEMFPYEASTPTGISASCRRPIKGAAGRPLELSDFRMEESFSSKYVPKYAPLADVK
SQ  SEKTKKRRSVPMWIKMLLFALVAVFLFLVYQAMETNQGNPFTNFLQDTKISN
//
ID  Q62733;
PN  Lamina-associated polypeptide 2, isoform beta;
GN  Tmpo;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane; Single-pass type II membrane protein. Chromosome {ECO:0000250}. Note=Tightly associated with the nuclear lamina.
DR  UNIPROT: Q62733;
DR  Pfam: PF03020;
DR  Pfam: PF08198;
DR  PROSITE: PS50954;
DR  PROSITE: PS50955;
DE  Function: Binds directly to lamin B1 and chromosomes in a mitotic phosphorylation-regulated manner. May play an important role in nuclear envelope reassembly at the end of mitosis and/or anchoring of the nuclear lamina and interphase chromosomes to the nuclear envelope.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0003677;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0031468;
GO  GO:0006355;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLAAGANSKGPPDFSSDEEREPTPVLGSG
SQ  ASVGRGRGAVGRKATKKTDKPRPEDKDDLDVTELSNEELLEQLVRYGVNPGPIVGTTRKLYEKKLLKLREQGAESRSSTP
SQ  LPTVSSSAENTRQNGSNDSDRYSDNDEDSKIELKLEKREPLKGRAKTPVTLKQRRIEHNQSYSEAGVTETEWTSGSSKGG
SQ  PLQALTRESTRGSRRTPRRRVEPSQHFRVDGAVISESTPIAETIKASSNDSLVANRLTGNFKHASSILPITEFSDITRRT
SQ  PKKPLTRAEVGEKTEERRVERDILKEMFPYEASTPTGISASCRRPIKGAAGRPLELSDFRMEESFSSKYVPKYVPLADVK
SQ  SEKTKKGRSVPMWIKMLLFALVAGFLFLVYQAMETNQGNPFTNFLQDTKISN
//
ID  P23913;
PN  Delta(14)-sterol reductase LBR;
GN  LBR;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:2170422}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q14739}.
DR  UNIPROT: P23913;
DR  PDB: 2L8D;
DR  Pfam: PF01222;
DR  Pfam: PF09465;
DR  PROSITE: PS01017;
DR  PROSITE: PS01018;
DE  Function: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity). {ECO:0000250|UniProtKB:Q14739, ECO:0000250|UniProtKB:Q3U9G9}.
DE  Reference Proteome: Yes;
DE  Interaction: Q96RG2; IntAct: EBI-8613487; Score: 0.44
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0050613;
GO  GO:0003677;
GO  GO:0070402;
GO  GO:0016627;
GO  GO:0006695;
GO  GO:0030223;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPNRKYADGEVVMGRWPGSVLYYEVQVTSYDDASHLYTVKYKDGTELALKESDIRLQSSFKQRKSQSSSSSPSRRSRSRS
SQ  RSRSPGRPAKGRRRSSSHSREHKEDKKKIIQETSLAPPKPSENNTRRYNGEPDSTERNDTSSKLLEQQKLKPDVEMERVL
SQ  DQYSLRSRREEKKKEEIYAEKKIFEAIKTPEKPSSKTKELEFGGRFGTFMLMFFLPATVLYLVLMCKQDDPSLMNFPPLP
SQ  ALESLWETKVFGVFLLWFFFQALFYLLPIGKVVEGLPLSNPRKLQYRINGFYAFLLTAAAIGTLLYFQFELHYLYDHFVQ
SQ  FAVSAAAFSMALSIYLYIRSLKAPEEDLAPGGNSGYLVYDFFTGHELNPRIGSFDLKYFCELRPGLIGWVVINLAMLLAE
SQ  MKIHNQSMPSLSMILVNSFQLLYVVDALWNEEAVLTTMDITHDGFGFMLAFGDLVWVPFVYSLQAFYLVGHPIAISWPVA
SQ  AAITILNCIGYYIFRSANSQKNNFRRNPADPKLSYLKVIPTATGKGLLVTGWWGFVRHPNYLGDIIMALAWSLPCGFNHI
SQ  LPYFYVIYFICLLVHREARDEHHCKKKYGLAWERYCQRVPYTHISLHLLEHSTYLICKLKYTSHLCTWSVCYLGFKH
//
ID  Q8MLV1;
PN  Lamin-B receptor;
GN  LBR;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:15054108}; Multi-pass membrane protein {ECO:0000269|PubMed:15054108}; Nucleoplasmic side {ECO:0000269|PubMed:15054108}.
DR  UNIPROT: Q8MLV1;
DR  UNIPROT: Q0E8Z1;
DR  UNIPROT: Q709R7;
DR  UNIPROT: Q9W2D2;
DR  Pfam: PF01222;
DE  Function: Anchors the lamina and the heterochromatin to the inner nuclear membrane. {ECO:0000269|PubMed:15054108}.
DE  Reference Proteome: Yes;
DE  Interaction: P13607; IntAct: EBI-253095; Score: 0.00
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: P18824; IntAct: EBI-9923731; Score: 0.35
DE  Interaction: M9PFN0; IntAct: EBI-9927063; Score: 0.35
DE  Interaction: Q9W0L7; IntAct: EBI-9930751; Score: 0.35
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0003682;
GO  GO:0003677;
GO  GO:0005521;
GO  GO:0006997;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQHSPSTTTDHIHFAARFFDRNSYTMDRRLRRPRRTEDVSSGPLLAQSKQPSLLPVTRRTGSVTAAGATATATATAGPAT
SQ  RTRASPSRNKVVAPPSPDLGPRTRRSSRPRSSVGPLTGSGSGSSLPIKAAIKARTPIPEVSEVSSPIRLSTSNLPMTLTT
SQ  NTSSGAPNKAFNTSSVNSGNSFSRTTTSSTTTTTERIEIRAEGDGEVDTDSIRKRITERLRRSVSKTISNLAGTPVTNTE
SQ  EGSRYSRSVSRSVYDDEKSSKRSYSTGEEDIDEEDELEEDQFRSFNVTRKSATPAEISCRQLKAPREFGGWLGAFLFLLL
SQ  LPTAVYYLTWSCTARNACQFKHLNLGILLDVNYLTRQVFQPRVVGAFAAYQVVVFLLVALLPGRRVHLTRETYKFNCLAV
SQ  SLTLLIASGVAEYLKYPVVTFVLRHYLRFCIFGLVGAFVAAAWSYWLVDTAKYNVLRQTLTNDYGRTGSFVVDFALGRQL
SQ  NPKWLGRVDWKQFQYRLSLVTTLIYATCYIYQTLVWPQKPQLGEQEGYLYQAKYYWNNVNYDPATLFSASCLLFYVLDAI
SQ  IFEHHLSSSFELQHEGYGCLLLLRYAATPYLLTAVTKYFYEQRVPISCWYAPLAVAALLSLGLLVKRFSCAYKYKYRLNS
SQ  QSPIFANIETIHTYQGSRLLLSGMWGWVRQPNYLGDIVALLALAAPMALRPAWPPVLGLSLIILLLLHRATRANARNQAR
SQ  YHSSWQRYSTQVRSYILPRVY
//
ID  Q14739;
PN  Delta(14)-sterol reductase LBR;
GN  LBR;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:8157662}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21327084}. Cytoplasm {ECO:0000269|PubMed:21327084}. Nucleus {ECO:0000269|PubMed:21327084}. Note=Nucleus; nuclear rim. {ECO:0000269|PubMed:21327084}.
DR  UNIPROT: Q14739;
DR  UNIPROT: B2R5P3;
DR  UNIPROT: Q14740;
DR  UNIPROT: Q53GU7;
DR  UNIPROT: Q59FE6;
DR  PDB: 2DIG;
DR  Pfam: PF01222;
DR  Pfam: PF09465;
DR  PROSITE: PS01017;
DR  PROSITE: PS01018;
DR  OMIM: 169400;
DR  OMIM: 215140;
DR  OMIM: 600024;
DR  OMIM: 613471;
DR  OMIM: 618019;
DR  DisGeNET: 3930;
DE  Function: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:9630650, PubMed:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (PubMed:10828963). {ECO:0000250|UniProtKB:Q3U9G9, ECO:0000269|PubMed:10828963, ECO:0000269|PubMed:12618959, ECO:0000269|PubMed:16784888, ECO:0000269|PubMed:21327084, ECO:0000269|PubMed:27336722, ECO:0000269|PubMed:9630650}.
DE  Disease: Pelger-Huet anomaly (PHA) [MIM:169400]: An autosomal dominant inherited abnormality of granulocytes, characterized by abnormal ovoid shape, reduced nuclear segmentation and an apparently looser chromatin structure. {ECO:0000269|PubMed:14617022}. Note=The disease is caused by variants affecting the gene represented in this entry. Greenberg dysplasia (GRBGD) [MIM:215140]: A rare autosomal recessive chondrodystrophy characterized by early in utero lethality. Affected fetuses typically present with fetal hydrops, short-limbed dwarfism, and a marked disorganization of chondro-osseous calcification, and ectopic ossification centers. {ECO:0000269|PubMed:12618959, ECO:0000269|PubMed:21327084, ECO:0000269|PubMed:27336722}. Note=The disease is caused by variants affecting the gene represented in this entry. Reynolds syndrome (REYNS) [MIM:613471]: A syndrome specifically associating limited cutaneous systemic sclerosis and primary biliary cirrhosis. It is characterized by liver disease, telangiectasia, abrupt onset of digital paleness or cyanosis in response to cold exposure or stress (Raynaud phenomenon), and variable features of scleroderma. The liver disease is characterized by pruritis, jaundice, hepatomegaly, increased serum alkaline phosphatase and positive serum mitochondrial autoantibodies, all consistent with primary biliary cirrhosis. {ECO:0000269|PubMed:20522425}. Note=The disease may be caused by variants affecting the gene represented in this entry. Pelger-Huet anomaly with mild skeletal anomalies (PHASK) [MIM:618019]: A disease characterized by abnormal nuclear shape and chromatin organization in blood granulocytes, short stature, and mild skeletal anomalies. Initial skeletal features may improve with age. {ECO:0000269|PubMed:23824842, ECO:0000269|PubMed:25348816}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.42
DE  Interaction: P61981; IntAct: EBI-7301287; Score: 0.59
DE  Interaction: P31946; IntAct: EBI-7307463; Score: 0.40
DE  Interaction: Q9Y5J5; IntAct: EBI-1061712; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-1068530; Score: 0.00
DE  Interaction: P32121; IntAct: EBI-1642567; Score: 0.35
DE  Interaction: Q13185; IntAct: EBI-1787288; Score: 0.62
DE  Interaction: P45973; IntAct: EBI-1787307; Score: 0.61
DE  Interaction: Q96SB4; IntAct: EBI-7160017; Score: 0.44
DE  Interaction: Q8NCN4; IntAct: EBI-8569133; Score: 0.35
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: P49761; IntAct: EBI-6380381; Score: 0.53
DE  Interaction: Q8NE63; IntAct: EBI-6381132; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q9Z1B5; IntAct: EBI-10996176; Score: 0.35
DE  Interaction: Q8R5L1; IntAct: EBI-11085290; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11372136; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q9WMX2; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: P60033; IntAct: EBI-24613403; Score: 0.56
DE  Interaction: O75596; IntAct: EBI-21674079; Score: 0.35
DE  Interaction: Q9NQ29; IntAct: EBI-21728243; Score: 0.35
DE  Interaction: Q7RTS1; IntAct: EBI-21831672; Score: 0.35
DE  Interaction: Q8NAF0; IntAct: EBI-21886699; Score: 0.35
DE  Interaction: Q9Y3Y2; IntAct: EBI-21886699; Score: 0.35
DE  Interaction: Q15013; IntAct: EBI-21886699; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21907689; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.42
DE  Interaction: P68431; IntAct: EBI-16793336; Score: 0.42
DE  Interaction: P22087; IntAct: EBI-16792571; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-16795231; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-16799122; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-16799786; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800982; Score: 0.42
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P03427; IntAct: EBI-25769715; Score: 0.37
DE  Interaction: Q8IW00; IntAct: EBI-20905192; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-20922762; Score: 0.40
DE  Interaction: C4AMC7; IntAct: EBI-20935852; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: P63000; IntAct: EBI-25375986; Score: 0.35
DE  Interaction: P05771; IntAct: EBI-25379671; Score: 0.35
DE  Interaction: P06241; IntAct: EBI-25385167; Score: 0.35
DE  Interaction: Q07021; IntAct: EBI-25302051; Score: 0.35
DE  Interaction: Q14CB8; IntAct: EBI-25409097; Score: 0.35
DE  Interaction: O08908; IntAct: EBI-25410059; Score: 0.35
DE  Interaction: Q6ZRI8; IntAct: EBI-25410669; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9NVX0; IntAct: EBI-25479027; Score: 0.35
DE  Interaction: O60671; IntAct: EBI-25483382; Score: 0.35
DE  Interaction: P0DTD3; IntAct: EBI-25510342; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.35
DE  Interaction: Q6ZNK6; IntAct: EBI-26453464; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q8WXR4; IntAct: EBI-28944037; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: P50552; IntAct: EBI-30845389; Score: 0.44
DE  Interaction: Q9UIH9; IntAct: EBI-29019642; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
DE  Interaction: O43763; IntAct: EBI-29612789; Score: 0.35
DE  Interaction: P52952; IntAct: EBI-29653951; Score: 0.35
DE  Interaction: Q04912; IntAct: EBI-32725158; Score: 0.27
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005639;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0070087;
GO  GO:0050613;
GO  GO:0003677;
GO  GO:0005521;
GO  GO:0070402;
GO  GO:0016627;
GO  GO:0003723;
GO  GO:0006695;
GO  GO:0030223;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIKPLTSFRQRKGGSTSSSPSRRRGSRS
SQ  RSRSRSPGRPPKSARRSASASHQADIKEARREVEVKLTPLILKPFGNSISRYNGEPEHIERNDAPHKNTQEKFSLSQESS
SQ  YIATQYSLRPRREEVKLKEIDSKEEKYVAKELAVRTFEVTPIRAKDLEFGGVPGVFLIMFGLPVFLFLLLLMCKQKDPSL
SQ  LNFPPPLPALYELWETRVFGVYLLWFLIQVLFYLLPIGKVVEGTPLIDGRRLKYRLNGFYAFILTSAVIGTSLFQGVEFH
SQ  YVYSHFLQFALAATVFCVVLSVYLYMRSLKAPRNDLSPASSGNAVYDFFIGRELNPRIGTFDLKYFCELRPGLIGWVVIN
SQ  LVMLLAEMKIQDRAVPSLAMILVNSFQLLYVVDALWNEEALLTTMDIIHDGFGFMLAFGDLVWVPFIYSFQAFYLVSHPN
SQ  EVSWPMASLIIVLKLCGYVIFRGANSQKNAFRKNPSDPKLAHLKTIHTSTGKNLLVSGWWGFVRHPNYLGDLIMALAWSL
SQ  PCGFNHILPYFYIIYFTMLLVHREARDEYHCKKKYGVAWEKYCQRVPYRIFPYIY
//
ID  Q3U9G9;
PN  Delta(14)-sterol reductase LBR;
GN  Lbr;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:18785926}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q14739}.
DR  UNIPROT: Q3U9G9;
DR  UNIPROT: Q3TSW2;
DR  UNIPROT: Q811V8;
DR  UNIPROT: Q811V9;
DR  UNIPROT: Q8BST3;
DR  UNIPROT: Q8K2Y8;
DR  UNIPROT: Q8VDM0;
DR  UNIPROT: Q91YS5;
DR  UNIPROT: Q91Z27;
DR  Pfam: PF01222;
DR  Pfam: PF09465;
DR  PROSITE: PS01017;
DR  PROSITE: PS01018;
DE  Function: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:18785926). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (PubMed:22140257). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (PubMed:22140257). Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity). {ECO:0000250|UniProtKB:Q14739, ECO:0000269|PubMed:18785926, ECO:0000269|PubMed:22140257}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7TSJ6; IntAct: EBI-7861456; Score: 0.35
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0051087;
GO  GO:0070087;
GO  GO:0050613;
GO  GO:0003677;
GO  GO:0070402;
GO  GO:0008139;
GO  GO:0016627;
GO  GO:0006695;
GO  GO:0030223;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSRKFVEGEVVRGRWPGSSLYYEVEILSHDNKSQLYTVKYKDGTELELKESDIKPLKSFKQRKSGSISSSPSRRRGSRS
SQ  RSRSRSRSRSPGRAPKGSRRSVSASHEGDVKEKKEKEMRREILQVKLTPLVLKPFGNSVSVYNGEPEHMEKNATPYKDKQ
SQ  ERIILSTEDRYIVTQYSLRPRREEVKAKEIESEEQNLVTKGPAPLGTFQVTTPQRKDLEFGGVPGAVLIMLGLPACVLLL
SQ  LLQCRQKDPGLLHFPPPLPALHELWEPRVCGVYLLWFFVQALFHLLPVGKVAEGTPLVDGRRLQYRLNGLYAFILTSAAL
SQ  GAAVFWGVELCYLYTHFLQLALAATGFSVLLSAYLYVRSLRAPREELSPASSGNAVYDFFIGRELNPRLGAFDLKFFCEL
SQ  RPGLIGWVVINLVMLLMEMKIQERAAPSLAMILVNSFQLLYVVDALWNEEALLTSMDIMHDGFGFMLAFGDLVWVPFTYS
SQ  LQAFYLVSHPHDLSWPLASVIIALKLCGYVIFRCANSQKNAFRKNPTDPKLAHLKTIHTSTGKSLLVSGWWGFVRHPNYL
SQ  GDLIMALAWSLPCGFNHLLPYFYIIYFTALLIHREARDEHQCRRKYGLAWEKYCQRVPYRIFPYIY
//
ID  Q5R7H4;
PN  Delta(14)-sterol reductase LBR;
GN  LBR;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q14739}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q14739}.
DR  UNIPROT: Q5R7H4;
DR  Pfam: PF01222;
DR  Pfam: PF09465;
DR  PROSITE: PS01017;
DR  PROSITE: PS01018;
DE  Function: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (By similarity). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity). {ECO:0000250|UniProtKB:Q14739, ECO:0000250|UniProtKB:Q3U9G9}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0050613;
GO  GO:0003677;
GO  GO:0070402;
GO  GO:0006695;
GO  GO:0030223;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSASQLYTVKYKDGTELELKENDIKPLTSFRQRKGGSTSSSPSRRRGSRS
SQ  RSRSRSPGRPPKSARRSASASHQADIKEARREVEVKLTPLILKPFGNSISRYNGEPEHIERNDVPHKNTQEKFNLSQESS
SQ  YIATQCSLRPKREEVKLKEIDSKEEKFVAKELAVRTFEVTPIRAKDLEFGGVPGVFLIMFGLPVFLFLLLLMCKQKDPSL
SQ  LNFPPPLPALYELWETRVFGVYLLWFLIQVVFYLLPIGKVVEGTPLIDGRRLKYRLNGFYAFILTSAVIGTSLFQGVEFH
SQ  YVYSHFLQFALAATVFCVVLSVYLYMRSLKAPRNDLSPASSGNAVYDFFIGRELNPRIGTFDLKYFCELRPGLIGWVVIN
SQ  LVMLLAEMKIQDRAVPSLAMILVNSFQLLYVVDALWNEEALLTTMDIIHDGFGFMLAFGDLVWVPFIYSFQAFYLVSHPN
SQ  EVSWPMASLIIVLKFCGYVIFRGANSQKNAFRKNPSDPKLAHLKTIHTSTGKNLLVSGWWGFARHPNYLGDLIMALAWSL
SQ  ACGFNHILPYFYIIYFTMLLVHREARDEYHCKKKYGVAWEKYCQRVPYRIFPYIY
//
ID  O08984;
PN  Delta(14)-sterol reductase LBR;
GN  Lbr;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q14739}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q14739}.
DR  UNIPROT: O08984;
DR  Pfam: PF01222;
DR  Pfam: PF09465;
DR  PROSITE: PS01017;
DR  PROSITE: PS01018;
DE  Function: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (By similarity). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity). {ECO:0000250|UniProtKB:Q14739, ECO:0000250|UniProtKB:Q3U9G9}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0051087;
GO  GO:0070087;
GO  GO:0050613;
GO  GO:0003677;
GO  GO:0070402;
GO  GO:0008139;
GO  GO:0016627;
GO  GO:0006695;
GO  GO:0000278;
GO  GO:0030223;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPGRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKESDIKPLKSFKQRKSGSTSSSPSRRRSSRS
SQ  RSRSRSRSPGRAPKGSRRSVSASYQADAKEKEMRREILQVKLTPLVLKPFANSVSVYNGEPEHMEKSATPPKNKQERVIL
SQ  STEDSYIATQYSLRPRREEVKPKHRVRGTNLVTRGPVPLGTFQVTTPQRRDLEFGGVPGALLIMLGLPACVFLLLLQCAQ
SQ  KDPGLLQFPPPLPALRELWEARVCGVYLLWFFLQALFSLLPVGKVVEGTPLVDGRRLKYRLNGLYAFILTSAAVGTAVFW
SQ  DIELYYLYTHFLQFALAAIVFSVVLSVYLYARSLKVPRDELSPASSGNAVYDFFIGRELNPRIGAFDLKFFCELRPGLIG
SQ  WVVINLVMLLAEMKVQERSAPSLAMTLVNSFQLLYVVDALWFEEALLTTMDIIHDGFGFMLAFGDLVWVPFTYSLQAFYL
SQ  VNHPQDLSWPLTSVIIALKLCGYVIFRCANSQKNAFRKNPTDPKLAHLKTIPTSTWKSLLVSGWWGFVRHPNYLGDLIMA
SQ  LAWSLPCGFNHILPYFYVIYFTALLIHREARDEHQCRRKYGLAWEKYCQRVPYRIFPYIY
//
ID  O75112;
PN  LIM domain-binding protein 3;
GN  LDB3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10427098}. Cell projection, pseudopodium {ECO:0000269|PubMed:10427098}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10427098}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10427098}. Note=Localized to the cytoplasm around nuclei and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2 at the Z-lines.
DR  UNIPROT: O75112;
DR  UNIPROT: A2TDB7;
DR  UNIPROT: A6NIV4;
DR  UNIPROT: B4E3K3;
DR  UNIPROT: Q5K6N9;
DR  UNIPROT: Q5K6P0;
DR  UNIPROT: Q5K6P1;
DR  UNIPROT: Q96FH2;
DR  UNIPROT: Q9Y4Z3;
DR  UNIPROT: Q9Y4Z4;
DR  UNIPROT: Q9Y4Z5;
DR  PDB: 1RGW;
DR  PDB: 4YDP;
DR  Pfam: PF15936;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DR  OMIM: 601493;
DR  OMIM: 605906;
DR  OMIM: 609452;
DR  DisGeNET: 11155;
DE  Function: May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton. {ECO:0000305}.
DE  Disease: Cardiomyopathy, dilated 1C, with or without left ventricular non-compaction (CMD1C) [MIM:601493]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Cardiomyopathy dilated type 1C is associated with left ventricular non-compaction in some patients. Left ventricular non- compaction is characterized by numerous prominent trabeculations and deep intertrabecular recesses in hypertrophied and hypokinetic segments of the left ventricle. {ECO:0000269|PubMed:14660611, ECO:0000269|PubMed:14662268}. Note=The disease is caused by variants affecting the gene represented in this entry. Left ventricular non-compaction 3 (LVNC3) [MIM:601493]: A form of left ventricular non-compaction, a cardiomyopathy due to myocardial morphogenesis arrest and characterized by a hypertrophic left ventricle, a severely thickened 2-layered myocardium, numerous prominent trabeculations, deep intertrabecular recesses, and poor systolic function. Clinical manifestations are variable. Some affected individuals experience no symptoms at all, others develop heart failure. In some cases, left ventricular non-compaction is associated with other congenital heart anomalies. LVNC3 is an autosomal dominant condition. Note=The disease is caused by variants affecting the gene represented in this entry. Myopathy, myofibrillar, 4 (MFM4) [MIM:609452]: A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM4 is characterized by distal and proximal muscle weakness with signs of cardiomyopathy and neuropathy. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P02768; IntAct: EBI-1222961; Score: 0.35
DE  Interaction: P61916; IntAct: EBI-21645691; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-21645691; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-21257148; Score: 0.37
GO  GO:0005912;
GO  GO:0005856;
GO  GO:0031941;
GO  GO:0048471;
GO  GO:0031143;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0008092;
GO  GO:0046872;
GO  GO:0051371;
GO  GO:0005080;
GO  GO:0030036;
GO  GO:0007507;
GO  GO:0061061;
GO  GO:0045214;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTL
SQ  QKSKRPIPISTTAPPVQTPLPVIPHQKDPALDTNGSLVAPSPSPEARASPGTPGTPELRPTFSPAFSRPSAFSSLAEASD
SQ  PGPPRASLRAKTSPEGARDLLGPKALPGSSQPRQYNNPIGLYSAETLREMAQMYQMSLRGKASGVGLPGGSLPIKDLAVD
SQ  SASPVYQAVIKSQNKPEDEADEWARRSSNLQSRSFRILAQMTGTEFMQDPDEEALRRSSTPIEHAPVCTSQATTPLLPAS
SQ  AQPPAAASPSAASPPLATAAAHTAIASASTTAPASSPADSPRPQASSYSPAVAASSAPATHTSYSEGPAAPAPKPRVVTT
SQ  ASIRPSVYQPVPASTYSPSPGANYSPTPYTPSPAPAYTPSPAPAYTPSPVPTYTPSPAPAYTPSPAPNYNPAPSVAYSGG
SQ  PAEPASRPPWVTDDSFSQKFAPGKSTTSISKQTLPRGGPAYTPAGPQVPPLARGTVQRAERFPASSRTPLCGHCNNVIRG
SQ  PFLVAMGRSWHPEEFTCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPLCAKCNTKIMGEVMHALRQTWHTTCFVCAACK
SQ  KPFGNSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDRPLCKK
SQ  HAHTINL
//
ID  Q9JKS4;
PN  LIM domain-binding protein 3;
GN  Ldb3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10391924}. Cell projection, pseudopodium {ECO:0000269|PubMed:10391924}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10391924}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10391924}. Note=Localized to the cytoplasm around nuclei and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2 at the Z-lines.
DR  UNIPROT: Q9JKS4;
DR  UNIPROT: B2RSB0;
DR  UNIPROT: B7ZNT6;
DR  UNIPROT: Q6A038;
DR  UNIPROT: Q811P2;
DR  UNIPROT: Q811P3;
DR  UNIPROT: Q811P4;
DR  UNIPROT: Q811P5;
DR  UNIPROT: Q9D130;
DR  UNIPROT: Q9JKS3;
DR  UNIPROT: Q9R0Z1;
DR  UNIPROT: Q9WVH1;
DR  UNIPROT: Q9WVH2;
DR  PDB: 1WJL;
DR  Pfam: PF15936;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DE  Function: May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton. {ECO:0000303|PubMed:10391924}.
DE  Reference Proteome: Yes;
DE  Interaction: P16054; IntAct: EBI-299155; Score: 0.56
DE  Interaction: P28867; IntAct: EBI-7048669; Score: 0.40
DE  Interaction: P63318; IntAct: EBI-7048648; Score: 0.40
DE  Interaction: Q9JI91; IntAct: EBI-7048448; Score: 0.57
DE  Interaction: P68404; IntAct: EBI-7048489; Score: 0.49
DE  Interaction: P20444; IntAct: EBI-7048605; Score: 0.40
DE  Interaction: Q02956; IntAct: EBI-7048713; Score: 0.40
DE  Interaction: P51637; IntAct: EBI-20565496; Score: 0.35
DE  Interaction: A2AKD7; IntAct: EBI-20566393; Score: 0.35
GO  GO:0005912;
GO  GO:0005856;
GO  GO:0031941;
GO  GO:0048471;
GO  GO:0031143;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0008092;
GO  GO:0019899;
GO  GO:0046872;
GO  GO:0051371;
GO  GO:0008022;
GO  GO:0005080;
GO  GO:0030036;
GO  GO:0007507;
GO  GO:0061061;
GO  GO:0045214;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTL
SQ  QKSKRPIPISTTAPPIQSPLPVIPHQKDPALDTNGSLATPSPSPEARASPGALEFGDTFSSSFSQTSVCSPLMEASGPVL
SQ  PLGSPVAKASSEGAQGSVSPKVLPGPSQPRQYNNPIGLYSAETLREMAQMYQMSLRGKASGAGLLGGSLPVKDLAVDSAS
SQ  PVYQAVIKTQSKPEDEADEWARRSSNLQSRSFRILAQMTGTEYMQDPDEEALRRSSTPIEHAPVCTSQATSPLLPASAQS
SQ  PAAASPIAASPTLATAAATHAAAASAAGPAASPVENPRPQASAYSPAAAASPAPSAHTSYSEGPAAPAPKPRVVTTASIR
SQ  PSVYQPVPASSYSPSPGANYSPTPYTPSPAPAYTPSPAPTYTPSPAPTYSPSPAPAYTPSPAPNYTPTPSAAYSGGPSES
SQ  ASRPPWVTDDSFSQKFAPGKSTTTVSKQTLPRGAPAYNPTGPQVTPLARGTFQRAERFPASSRTPLCGHCNNVIRGPFLV
SQ  AMGRSWHPEEFNCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPICAKCNTKIMGEVMHALRQTWHTTCFVCAACKKPFG
SQ  NSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDKPLCKKHAHA
SQ  INV
//
ID  P03263;
PN  I-leader protein;
GN  LEAD;
OS  10515;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:3005631}. Note=Might be loosely associated with the nuclear membrane.
DR  UNIPROT: P03263;
DR  Pfam: PF03052;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0044220;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRADREELDLPPPVGGVAVDVVKVEVPATGRTLVLAFVKTCAVLAAVHGLYILHEVDLTTAHKEAEWEFEPLAWRVWLVV
SQ  FYFGCLSLTVWLLEGSYGGSDHHAARAQSPDVRARRSELDDNIAQMGAVHGLELPRRQVLRHRGT
//
ID  Q2KS19;
PN  I-leader protein;
GN  LEAD;
OS  28285;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region. Note=Might be loosely associated with the nuclear membrane. {ECO:0000250}.
DR  UNIPROT: Q2KS19;
DR  Pfam: PF03052;
DE  Function: 
DE  Reference Proteome: No;
GO  GO:0044220;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRADREELDLPPPIGGVAIDVVKVEVPATGRTLVLAFVKTCAVLAAVHGLYILHEVDLTTAHKEAEWEFEPLAWRVWLVV
SQ  FYFGCLSLTVWLLEGSYGGSDHHAARAQSPDVRARRSELDDNIAQMGAVHGLELPRRQVLRRRGT
//
ID  Q9XTB5;
PN  LEM protein 2;
GN  lem;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:12684533}; Multi-pass membrane protein {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:12684533}; Nucleoplasmic side {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:21176223, ECO:0000269|PubMed:25653391, ECO:0000269|PubMed:32271860}. Chromosome {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:25653391, ECO:0000269|PubMed:32271860}. Note=Remains in the nuclear envelope until mid-late anaphase and reassociates with the chromatin periphery at telophase (PubMed:10982402). Recruited to the reforming nuclear envelope initially at the apical surfaces of chromatin, from where it spreads to the lateral surfaces facing the spindle microtubules (PubMed:25653391). Requires mel-28 for chromatin reassociation after mitosis and for nuclear envelope localization (PubMed:16950114). In meiosis at anaphase II, appears on the chromatin surface farthest from the extruding polar body (PubMed:32271860). After anaphase II, forms a plaque on the oocyte-derived pronucleus adjacent to the meiotic spindle (PubMed:32271860). Later disperses into a uniform rim around the oocyte-derived pronucleus (PubMed:32271860). {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:25653391, ECO:0000269|PubMed:32271860}.
DR  UNIPROT: Q9XTB5;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Nuclear lamina-associated inner nuclear membrane protein that is involved in cell division, nuclear structure organization, maintenance of nuclear envelope integrity and nuclear envelope reformation after mitosis (PubMed:12684533, PubMed:21176223, PubMed:22171324, PubMed:25653391, PubMed:32271860). In interphase cells, plays a role in anchoring and spatial arrangement of chromosome arms at the nuclear periphery, forming so-called lem-2 subdomains (PubMed:21176223). Both arms of autosomes but only the left arm of the X chromosome are anchored in lem-2 subdomains; sequences bound by lem-2 are mainly repetitive chromosome sequences and inactive genes (PubMed:21176223). Involved in chromosome segregation and cell division, probably via its interaction with the nuclear intermediate filament protein lmn-1, the main component of nuclear lamina (PubMed:12684533). Required to organize the distribution of lmn-1, nuclear pore complexes (NPCs) and chromatin in mitotically active cells (PubMed:22171324). Involved in the nuclear positioning and efficient anchoring of microtubule-organizing centers (MTOCs) to the nuclear envelope during mitosis as well as on maintaining correct nuclear morphology (PubMed:25653391). Contributes to closure of nuclear envelope (NE) holes and prevents excess nuclear membranes after meiosis and mitosis (PubMed:32271860). Together with emr-1, plays a role in baf-1 enrichment at the nuclear envelope in anaphase (PubMed:12684533). Together with emr-1, involved in muscle cell attachment to hypodermal cells, as well as muscle cell location and sarcomere organization (PubMed:22171324). May play a role in radiation-induced DNA damage repair response (PubMed:22383942). {ECO:0000269|PubMed:12684533, ECO:0000269|PubMed:21176223, ECO:0000269|PubMed:22171324, ECO:0000269|PubMed:22383942, ECO:0000269|PubMed:25653391, ECO:0000269|PubMed:32271860}.
DE  Reference Proteome: Yes;
DE  Interaction: O01971; IntAct: EBI-6260324; Score: 0.27
DE  Interaction: Q21443; IntAct: EBI-2535415; Score: 0.53
DE  Interaction: Q03565; IntAct: EBI-2535622; Score: 0.44
GO  GO:0005694;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0031490;
GO  GO:0005521;
GO  GO:0051276;
GO  GO:0007059;
GO  GO:0031023;
GO  GO:0000281;
GO  GO:0030514;
GO  GO:0006998;
GO  GO:0031468;
GO  GO:1902531;
GO  GO:0010165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVDVEKMSDAELRAELNVRGANVGPVTGTTRSLYEKKLKKLLSGGAKTPARPTVAKPAPKPTPKSAPAPKSPKSPPARRS
SQ  IPRAAATAANSTINSTFNRSEIEEMSDSDDDMRDDDDDDEEILSPKSKQSSFRSANSTASSVGRGRPVSSTPNKRLSPVY
SQ  KPSPVPKNTPRTTSSSSKTTINTTTTRIPSTPRRITSVPGLITDFTPSFSTFGSDRPGATPPRKSIYTSKVSKVLHDLGN
SQ  TTGEEDDDDEFEGQETSRIIYKTEEPSRRGIVKNAWNKVLGYGFDASKNPGDSYDLRAGASRIRVQKNPRTGKVTVKQTN
SQ  IFNEAIYFALYVILILFVVLGIAYALTTTHRPKTADFSGYWGVLKAAGRDSLNFFYNYAILPVVSLGIFVVLGAGIYFGH
SQ  RKYKEAKEQEEAKLYELIERITELIRESSIDGDPYVSQPHVRDVLFPPAKRRSAELARWEQAVKFIDTNESRVATDVLVL
SQ  PSGNECAVWKWIGNQSQKRW
//
ID  Q10109;
PN  Lap-Emerin-Man domain protein 2;
GN  lem2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18692466}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18692466}.
DR  UNIPROT: Q10109;
DR  PDB: 5YCA;
DR  Pfam: PF12949;
DR  Pfam: PF09402;
DE  Function: Nucleus inner membrane protein involved in meiosis (PubMed:20404563). Plays a role in regulating nuclear envelope (NE) morphology and nuclear integrity, particularly during spindle pole body (SPB) extrusion or insertion through the NE, and perhaps during karyokinesis (PubMed:28242692). {ECO:0000269|PubMed:20404563, ECO:0000269|PubMed:28242692}.
DE  Reference Proteome: Yes;
GO  GO:0061638;
GO  GO:0034506;
GO  GO:0099115;
GO  GO:0005639;
GO  GO:0140599;
GO  GO:0044732;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005721;
GO  GO:0097038;
GO  GO:0033553;
GO  GO:0140449;
GO  GO:0019237;
GO  GO:0003682;
GO  GO:0003690;
GO  GO:0062239;
GO  GO:0140698;
GO  GO:0072766;
GO  GO:0070828;
GO  GO:0051321;
GO  GO:0007084;
GO  GO:0071765;
GO  GO:0071763;
GO  GO:0140462;
GO  GO:0097355;
GO  GO:0140464;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDNWEDPNFELRNLRVIDLKKILHESGVSFPVNARKIEYIRMVDRIRKNKLSSGPQHLLSHLQKEENSNTSKASSSEDEI
SQ  APKYLYPSSPSKSTKKPHNETEPLLSPQFIDKPSNIETPVKIESPHVSQNNTFQSYSELSPNVETSLTMKTPPAHASTPK
SQ  FRSHKSHRVAVPMSFMDSSALHTSPAFSERLKLLSSSNNFSPQLRSPKISHRLQTSATSSPLQHKRPFTNVPERVSRDIE
SQ  FAPLDSARPSESSSPYSEVDSAEEDDELFQNYVLQQTRKESKLWSFIKKVFHDIKYANYRLLHNLRAFPGISAISSSYLV
SQ  HIFMILLGVVAAIFLALLREKMFTAGFCDSGASGSSASILGISFPSLCRTCPPNAICPSPNYVECKPGYVLYEPWYSSLG
SQ  FWPSKYCVSDTSREESVNIFREECLSVLRSWNAILHCSNNSSDLLERNMSYNAHPYVADNLNISSDHISFPSKPFALGLL
SQ  HDTLLERKSPTLGLEMFEDLFKASLAVLSETNEVVMDSKLICYDSWAGIPLRCRLKQQLIKFVWRNKVFLFGILALSGVI
SQ  FKLINFFRTRSIVAKYLPSASRFCVESLKRQKANYQMSRSQEPVIPLIEMHDILFHGNGPLEQIHMTKATARTLWEAIVE
SQ  RVEQVGSVRTRESEVDGEWTRVWEWVGTNTLDFQTDRSFINTTSPLRE
//
ID  Q8NC56;
PN  LEM domain-containing protein 2;
GN  LEMD2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17097643, ECO:0000269|PubMed:28242692, ECO:0000269|PubMed:30905398, ECO:0000269|PubMed:32494070}; Multi-pass membrane protein {ECO:0000269|PubMed:16339967}. Nucleus envelope {ECO:0000269|PubMed:28242692}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:32494070}. Note=Lamina-associated protein residing in the inner nuclear membrane (INM) of the nuclear envelope (NE) (PubMed:16339967). The localization to the INM is dependent on LMNA (PubMed:16339967). Evenly distributed around the NE during interphase (PubMed:16339967). During metaphase, found in a reticular network (PubMed:28242692). Recruited to the reforming NE on chromatin disks in early anaphase (PubMed:28242692). In late anaphase, concentrates at the NE core proximal to spindle microtubules, and then broadening to a distributed nuclear rim pattern (PubMed:28242692, PubMed:32494070). {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:28242692, ECO:0000269|PubMed:32494070}.
DR  UNIPROT: Q8NC56;
DR  UNIPROT: B4DVH5;
DR  UNIPROT: E7EVT2;
DR  UNIPROT: Q5T972;
DR  UNIPROT: Q5T974;
DR  Pfam: PF03020;
DR  Pfam: PF09402;
DR  PROSITE: PS50954;
DR  OMIM: 212500;
DR  OMIM: 616312;
DR  OMIM: 619322;
DR  DisGeNET: 221496;
DE  Function: Nuclear lamina-associated inner nuclear membrane protein that is involved in nuclear structure organization, maintenance of nuclear envelope integrity and nuclear envelope reformation after mitosis (PubMed:16339967, PubMed:17097643, PubMed:28242692, PubMed:32494070). Plays a role as transmembrane adapter for the endosomal sorting complexes required for transport (ESCRT), and is thereby involved in ESCRT-mediated nuclear envelope reformation (PubMed:28242692, PubMed:32494070). Promotes ESCRT-mediated nuclear envelope closure by recruiting CHMP7 and downstream ESCRT-III proteins IST1/CHMP8 and CHMP2A to the reforming NE during anaphase (PubMed:28242692). During nuclear reassembly, condenses into a liquid-like coating around microtubule spindles and coassembles with CHMP7 to form a macromolecular O-ring seal at the confluence between membranes, chromatin, and the spindle to facilitate early nuclear sealing (PubMed:32494070). Required for embryonic development and involved in regulation of several signaling pathways such as MAPK and AKT (By similarity). Required for myoblast differentiation involving regulation of ERK signaling (By similarity). {ECO:0000250|UniProtKB:Q6DVA0, ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17097643, ECO:0000269|PubMed:28242692, ECO:0000269|PubMed:32494070}.
DE  Disease: Cataract 46, juvenile-onset, with or without arrhythmic cardiomyopathy (CTRCT46) [MIM:212500]: A form of cataract, an opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT46 can be associated with variable onset of a severe form of arrhythmic cardiomyopathy resulting in sudden cardiac death. {ECO:0000269|PubMed:26788539}. Note=The disease is caused by variants affecting the gene represented in this entry. Marbach-Rustad progeroid syndrome (MARUPS) [MIM:619322]: An autosomal dominant syndrome characterized by progeria-like appearance with little subcutaneous fat and triangular facies, growth retardation, short stature, hypoplastic mandible crowded with unerupted supernumerary teeth, and cerebellar intention tremor. {ECO:0000269|PubMed:30905398}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-10901984; Score: 0.49
DE  Interaction: P90495; IntAct: EBI-6156892; Score: 0.35
DE  Interaction: O14862; IntAct: EBI-9995694; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-11069711; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104527; Score: 0.35
DE  Interaction: Q9R0Q3; IntAct: EBI-11111571; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-11153302; Score: 0.35
DE  Interaction: Q99523; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P56945; IntAct: EBI-15100330; Score: 0.35
DE  Interaction: O00322; IntAct: EBI-21504674; Score: 0.35
DE  Interaction: P08473; IntAct: EBI-21505285; Score: 0.35
DE  Interaction: P22460; IntAct: EBI-21505491; Score: 0.35
DE  Interaction: P30825; IntAct: EBI-21505748; Score: 0.35
DE  Interaction: P32297; IntAct: EBI-21506200; Score: 0.35
DE  Interaction: P48960; IntAct: EBI-21506471; Score: 0.35
DE  Interaction: Q03721; IntAct: EBI-21513277; Score: 0.35
DE  Interaction: Q6P5W5; IntAct: EBI-21515976; Score: 0.35
DE  Interaction: Q9UGM1; IntAct: EBI-21517134; Score: 0.35
DE  Interaction: P80370; IntAct: EBI-21555448; Score: 0.35
DE  Interaction: Q8WTR4; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q504Y0; IntAct: EBI-21572157; Score: 0.35
DE  Interaction: Q01814; IntAct: EBI-21599092; Score: 0.35
DE  Interaction: Q12797; IntAct: EBI-21649522; Score: 0.35
DE  Interaction: Q99871; IntAct: EBI-21670231; Score: 0.35
DE  Interaction: Q16322; IntAct: EBI-21690666; Score: 0.35
DE  Interaction: P04004; IntAct: EBI-21709311; Score: 0.35
DE  Interaction: Q4KMQ2; IntAct: EBI-21730510; Score: 0.35
DE  Interaction: P46098; IntAct: EBI-21749232; Score: 0.35
DE  Interaction: O43505; IntAct: EBI-21751424; Score: 0.35
DE  Interaction: Q9C0K1; IntAct: EBI-21813298; Score: 0.35
DE  Interaction: Q05901; IntAct: EBI-21881670; Score: 0.35
DE  Interaction: Q96HU1; IntAct: EBI-21896050; Score: 0.40
DE  Interaction: P14316; IntAct: EBI-21260627; Score: 0.35
DE  Interaction: Q9BWW4; IntAct: EBI-21265722; Score: 0.35
DE  Interaction: Q9NQB0; IntAct: EBI-21265942; Score: 0.35
DE  Interaction: Q8N5H7; IntAct: EBI-25387159; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27111302; Score: 0.35
DE  Interaction: P23771; IntAct: EBI-34580747; Score: 0.35
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005639;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005819;
GO  GO:0031490;
GO  GO:0060914;
GO  GO:0030514;
GO  GO:0043409;
GO  GO:0051898;
GO  GO:0022008;
GO  GO:0006998;
GO  GO:0071168;
GO  GO:0035914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGEARLRDEERLREEARPRGEERLREEARLREDAPLRARPAA
SQ  ASPRAEPWLSQPASGSAYATPGAYGDIRPSAASWVGSRGLAYPARPAQLRRRASVRGSSEEDEDARTPDRATQGPGLAAR
SQ  RWWAASPAPARLPSSLLGPDPRPGLRATRAGPAGAARARPEVGRRLERWLSRLLLWASLGLLLVFLGILWVKMGKPSAPQ
SQ  EAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPENLKSKCIPVMEAQEYIANVTSSSSAKF
SQ  EAALTWILSSNKDVGIWLKGEDQSELVTTVDKVVCLESAHPRMGVGCRLSRALLTAVTNVLIFFWCLAFLWGLLILLKYR
SQ  WRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNESRIQTESH
SQ  RVAGEDMLVWRWTKPSSFSDSER
//
ID  Q6DVA0;
PN  LEM domain-containing protein 2;
GN  Lemd2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17062158}; Multi-pass membrane protein {ECO:0000269|PubMed:16339967}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NC56}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NC56}. Note=Lamina-associated protein residing in the inner nuclear membrane (INM) of the nuclear envelope (NE) (PubMed:16339967). The localization to the INM is dependent on LMNA (By similarity). Evenly distributed around the NE during interphase (PubMed:16339967). During metaphase, found in a reticular network (By similarity). Recruited to the reforming NE on chromatin disks in early anaphase (By similarity). In late anaphase, concentrates at the NE core proximal to spindle microtubules, and then broadening to a distributed nuclear rim pattern (By similarity). {ECO:0000250|UniProtKB:Q8NC56, ECO:0000269|PubMed:16339967}.
DR  UNIPROT: Q6DVA0;
DR  UNIPROT: Q8C4H8;
DR  UNIPROT: Q8R0N2;
DR  Pfam: PF03020;
DR  Pfam: PF09402;
DR  PROSITE: PS50954;
DE  Function: Nuclear lamina-associated inner nuclear membrane protein that is involved in nuclear structure organization and maintenance of nuclear structure integrity and nuclear envelope reformation after mitosis (PubMed:16339967). Plays a role as transmembrane adapter for the endosomal sorting complexes required for transport (ESCRT), and is thereby involved in ESCRT-mediated nuclear envelope reformation (By similarity). Promotes ESCRT-mediated nuclear envelope closure by recruiting CHMP7 and downstream ESCRT-III proteins IST1/CHMP8 and CHMP2A to the reforming NE during anaphase (By similarity). During nuclear reassembly, condenses into a liquid-like coating around microtubule spindles and coassembles with CHMP7 to form a macromolecular O-ring seal at the confluence between membranes, chromatin, and the spindle to facilitate early nuclear sealing (By similarity). Required for embryonic development and is involved in regulation of several signaling pathways such as MAPK and AKT (PubMed:25790465). Required for myoblast differentiation involving regulation of ERK signaling (PubMed:17062158, PubMed:19720741). {ECO:0000250|UniProtKB:Q8NC56, ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19720741, ECO:0000269|PubMed:25790465}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8VI24; IntAct: EBI-26885060; Score: 0.35
GO  GO:0000785;
GO  GO:0005783;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005819;
GO  GO:0031490;
GO  GO:0060914;
GO  GO:0030514;
GO  GO:0043409;
GO  GO:0051898;
GO  GO:0022008;
GO  GO:0006998;
GO  GO:0071168;
GO  GO:0035914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGLSDLELRRELQALGFQPGPITDTTRNVYRNKLRRLRGEARLRDDERLREDAGPREDAGPRGPERQREEARLREEAPL
SQ  RARPAASVLRSEPWPLSPSPPAPSAASDASGPYGNFGASASPWAASRGLSYPPHAGPGPLRRRASVRGSSEDDEDTRTPD
SQ  RHAPGRGRHWWAPPSASARPHSALLGADARPGLKGSRTGSAGAGRTRPEVGRWLERCLSRLLLWASLGLLLGFLAILWVK
SQ  MGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPEKLKSKCIPVLEAQEYIANV
SQ  TSSPSSRFKAALTWILSSNKDVGIWLKGEDPSELATTVDKVVCLESARPRMGIGCRLSRALLTAVTHVLIFFWCLAFLWG
SQ  LLILLKYRWRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNE
SQ  SRIQTESHRVAGEDMLVWRWTKPSSFSDSER
//
ID  O94559;
PN  Nuclear bridge Ish domain protein les1;
GN  les1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:32848252}. Note=Concentrates at the stalk of each daughter nucleus during anaphase. {ECO:0000269|PubMed:32848252}.
DR  UNIPROT: O94559;
DR  Pfam: PF10281;
DE  Function: Inner nuclear envelope protein involved in nuclear fission, which is achieved via local disassembly of nuclear pores within the narrow bridge that links segregating daughter nuclei (PubMed:32848252). Les1 restricts the process of local nuclear envelope breakdown to the bridge midzone to prevent the leakage of material from daughter nuclei during mitosis (PubMed:32848252). {ECO:0000269|PubMed:32848252}.
DE  Reference Proteome: Yes;
GO  GO:0140511;
GO  GO:0005637;
GO  GO:0051301;
GO  GO:0140515;
GO  GO:1905557;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQPRFLLHGALLALGIQLCLSIGKITGHISSIEATAADIHDAPSTTTKYVQRTVYAGREKGKIGGPADSWPQRKLDDFLQ
SQ  NHGVKSLDVPPIETPSQFWRKPLQYVSKVTDKCKSFYEKEKNHASHNAQKLDVWIFNSWTNSELSRWLIKNKYEVPEPGT
SQ  REQLLETVFQASMGDAISTNDELESWSNNLLLSMLDQKNITVPIGASHDDLIVLARRYYDIEERKSQDKVTNITDSQPAP
SQ  YMKEIIHLWSDGRLIDFLRERNIPISVLSPRETLLKEAYANRFTPRVMIASNVLDGWSSEDLLDWIWKYNKRGSIFSHVA
SQ  YNSRHELIHAAKLFYMDVASEWSSSDMASLNDSLYSHPSVSKQSTWTEEELKEELESFGELVPVPFSSTKAFERLLPHLY
SQ  YYLRGPAFLNRIHYWQTFLGNSLKRAFVLSQ
//
ID  P53671;
PN  LIM domain kinase 2;
GN  LIMK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22328514}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25849865}. [Isoform LIMK2a]: Cytoplasm {ECO:0000269|PubMed:8954941}. Nucleus {ECO:0000269|PubMed:8954941}. [Isoform LIMK2b]: Cytoplasm {ECO:0000269|PubMed:8954941}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8954941}. Nucleus {ECO:0000269|PubMed:8954941}. Note=Mainly present in the cytoplasm and is scarcely translocated to the nucleus. {ECO:0000269|PubMed:8954941}.
DR  UNIPROT: P53671;
DR  UNIPROT: A8K6H5;
DR  UNIPROT: Q7KZ80;
DR  UNIPROT: Q7L3H5;
DR  UNIPROT: Q96E10;
DR  UNIPROT: Q99464;
DR  UNIPROT: Q9UFU0;
DR  PDB: 1X6A;
DR  PDB: 4TPT;
DR  PDB: 5NXD;
DR  PDB: 7QHG;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  Pfam: PF07714;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  OMIM: 601988;
DR  DisGeNET: 3985;
DE  Function: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics (PubMed:10436159, PubMed:11018042). Acts downstream of several Rho family GTPase signal transduction pathways (PubMed:10436159, PubMed:11018042). Involved in astral microtubule organization and mitotic spindle orientation during early stages of mitosis by mediating phosphorylation of TPPP (PubMed:22328514). Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro (PubMed:8537403). Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of directional trafficking of ciliary vesicles to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (PubMed:25849865). {ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:22328514, ECO:0000269|PubMed:25849865, ECO:0000269|PubMed:8537403}.
DE  Reference Proteome: Yes;
DE  Interaction: O00165; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: O15027; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P11802; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P31689; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: Q9H422; IntAct: EBI-7234718; Score: 0.37
DE  Interaction: Q8TEW0; IntAct: EBI-7047934; Score: 0.40
DE  Interaction: Q5NGC7; IntAct: EBI-2805285; Score: 0.00
DE  Interaction: P08238; IntAct: EBI-6423874; Score: 0.64
DE  Interaction: Q16543; IntAct: EBI-9482950; Score: 0.56
DE  Interaction: Q15293; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P68366; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: O43852; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: O60884; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: Q9UJS0; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P53007; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: Q13451; IntAct: EBI-10103591; Score: 0.53
DE  Interaction: Q9H936; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: Q14257; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: O95816; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: Q96IX5; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: Q9Y230; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P13639; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: P46531; IntAct: EBI-13915571; Score: 0.35
DE  Interaction: P56381; IntAct: EBI-20931736; Score: 0.40
DE  Interaction: Q96C90; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: O75594; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q9Y241; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q99614; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q96TA2; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q96T76; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q92616; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q6DN90; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q5VYK3; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q58FG1; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q58FF6; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q14318; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q13501; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q02790; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: P53041; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: P50454; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: P50336; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: P40939; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: P27708; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: P25685; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: P09543; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: O43347; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: O00487; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q86UX6; IntAct: EBI-28942129; Score: 0.35
DE  Interaction: Q9Y6S9; IntAct: EBI-28948011; Score: 0.35
GO  GO:0005813;
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0072686;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0030036;
GO  GO:0030953;
GO  GO:0061303;
GO  GO:0051650;
GO  GO:0060322;
GO  GO:1902018;
GO  GO:0016310;
GO  GO:1900182;
GO  GO:0001934;
GO  GO:0006468;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSALAGEDVWRCPGCGDHIAPSQIWYRTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDYWGKFGEFCHGCSLLMT
SQ  GPFMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQEQLPYSVTLISMPATTE
SQ  GRRGFSVSVESACSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAISQTSQTLQLLIEHDPV
SQ  SQRLDQLRLEARLAPHMQNAGHPHALSTLDTKENLEGTLRRRSLRRSNSISKSPGPSSPKEPLLFSRDISRSESLRCSSS
SQ  YSQQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKK
SQ  LNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEER
SQ  KRAPMEKATTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNV
SQ  KLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALSLYLGELGIPLPAELEELDHTVSMQYGLTRDSPP
//
ID  O54785;
PN  LIM domain kinase 2;
GN  Limk2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P53671}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53671}. [Isoform LIMK2a]: Cytoplasm {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}. [Isoform LIMK2b]: Cytoplasm {ECO:0000250|UniProtKB:P53671}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}.
DR  UNIPROT: O54785;
DR  UNIPROT: O54776;
DR  UNIPROT: O55238;
DR  UNIPROT: Q9QUL4;
DR  PDB: 2YUB;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  Pfam: PF07714;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DE  Function: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Involved in astral microtubule organization and mitotic spindle orientation during early stages of mitosis by mediating phosphorylation of TPPP. Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of directional trafficking of ciliary vesicles to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity). {ECO:0000250|UniProtKB:P53671}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0072686;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0030036;
GO  GO:0030953;
GO  GO:0061303;
GO  GO:0051650;
GO  GO:0060322;
GO  GO:1902018;
GO  GO:1900182;
GO  GO:0001934;
GO  GO:0006468;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALAGDEAWRCRGCGTYVPLSQRLYRTANEAWHGSCFRCSECQESLTNWYYEKDGKLYCHKDYWAKFGEFCHGCSLLMT
SQ  GPAMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQDQLPYSVTLISMPATTE
SQ  CRRGFSVTVESASSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAIKQTSQTLQLLIEHDPV
SQ  PQRLDQLRLDARLPPHMQSTGHTLMLSTLDTKENQEGTLRRRSLRRSNSISKSPGPSSPKEPLLLSRDISRSESLRCSSS
SQ  YSQQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKK
SQ  LNLLTEYIEGGTLKDFLRSVDPFPWQQKVRFAKGISSGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEER
SQ  KRPPVEKATTKKRTLRKSDRKKRYTVVGNPYWMAPEMLNGKSYDETVDVFSFGIVLCEIIGQVYADPDCLPRTLDFGLNV
SQ  KLFWEKFVPTDCPPAFFPLAAICCKLEPESRPAFSKLEDSFEALSLFLGELAIPLPAELEDLDHTVSMEYGLTRDSPP
//
ID  P53670;
PN  LIM domain kinase 2;
GN  Limk2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform LIMK2A]: Cytoplasm {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}. [Isoform LIMK2B]: Cytoplasm {ECO:0000250|UniProtKB:P53671}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P53671}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53671}.
DR  UNIPROT: P53670;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  Pfam: PF07714;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DE  Function: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Involved in astral microtubule organization and mitotic spindle orientation during early stages of mitosis by mediating phosphorylation of TPPP. Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, directional trafficking of ciliary vesicles to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity). {ECO:0000250|UniProtKB:P53671}.
DE  Reference Proteome: Yes;
DE  Interaction: O54874; IntAct: EBI-9029887; Score: 0.44
GO  GO:0005813;
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0030036;
GO  GO:0030953;
GO  GO:0061303;
GO  GO:0051650;
GO  GO:0060322;
GO  GO:1902018;
GO  GO:1900182;
GO  GO:0001934;
GO  GO:0006468;
GO  GO:0007286;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALAGEEAWRCRGCGNYVPLSQRLYRTANEAWHSSCFRCSECQESLTNWYYEKDGKLYCHKDYWAKFGEFCHGCSLLMT
SQ  GPAMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQDQLPYSVTLISMPATTE
SQ  CRRGFSVSVESASSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAINQTSQTLQLLIEHDPV
SQ  PQRLDQLRLDTRLSPHMQSSGHTLMLSTLDAKENQEGTLRRRSLRRSNSISKSPGPSSPKEPLLLSRDISRSESLRCSSS
SQ  YSQQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKK
SQ  LNLLTEYIEGGTLKDFLRNVDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEER
SQ  KRPPVEKAATKKRTLRKSDRKKRYTVVGNPYWMAPEMLNGKSYDETVDVFSFGIVLCEIIGQVYADPDCLPRTLDFGLNV
SQ  KLFWEKFVPTDCPPAFFPLAAICCKLEPESRPAFSKLEDSFEALSLFLGELAIPLPAELEELDHTVSMEYGLTRDSPP
//
ID  P43033;
PN  Platelet-activating factor acetylhydrolase IB subunit beta;
GN  PAFAH1B1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP- Rule:MF_03141, ECO:0000269|PubMed:14584027}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP- Rule:MF_03141, ECO:0000269|PubMed:14584027}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes (By similarity). May localize to the nuclear membrane. {ECO:0000255|HAMAP-Rule:MF_03141}.
DR  UNIPROT: P43033;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in the PAF inactivation (PubMed:10542206). Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (PubMed:10542206). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing (By similarity). Required for pronuclear migration during fertilization. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity). May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P63005, ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:10542206, ECO:0000269|PubMed:14584027}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9ES39; IntAct: EBI-1007885; Score: 0.51
DE  Interaction: O35264; IntAct: EBI-1102249; Score: 0.51
DE  Interaction: O35263; IntAct: EBI-1007943; Score: 0.40
GO  GO:0008247;
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0005815;
GO  GO:0031965;
GO  GO:0005819;
GO  GO:0034452;
GO  GO:0070840;
GO  GO:0008201;
GO  GO:0008017;
GO  GO:0043274;
GO  GO:0046982;
GO  GO:0030154;
GO  GO:0051301;
GO  GO:0000132;
GO  GO:0016042;
GO  GO:0051012;
GO  GO:0007399;
GO  GO:0046469;
GO  GO:0038026;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVLSQRQRDELNRAIADYLRSNGYEAAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFT
SQ  SGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVEDISFDH
SQ  SGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
SQ  RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI
SQ  KMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSV
SQ  DQTVKVWECR
//
ID  Q9NDC9;
PN  Lissencephaly-1 homolog;
GN  lis;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP- Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Chromosome, centromere, kinetochore {ECO:0000305}. Nucleus envelope {ECO:0000305|PubMed:20005871}. Note=Localizes to the plus end of microtubules (By similarity). Concentrates in the vicinity of microtubule asters, kinetochores, the cell cortex and the perinuclear region (PubMed:15331665). Probably recruited to the nuclear envelope by unc-83 (PubMed:20005871). {ECO:0000250|UniProtKB:P63004, ECO:0000269|PubMed:15331665, ECO:0000305|PubMed:20005871}.
DR  UNIPROT: Q9NDC9;
DR  UNIPROT: O45742;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as nuclear migration during cell division (PubMed:11685578, PubMed:15331665). Part of a complex with nud-2, which is recruited to the nuclear envelope by unc-83, where, in turn, it recruits dynein to the nuclear surface and regulates nuclear migration in hypodermal precursor cells (PubMed:20005871). Plays a role in GABAergic synaptic vesicle localization in the ventral nerve cord (PubMed:16996038). Required for neuronal cell differentiation (PubMed:15254012). {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:11685578, ECO:0000269|PubMed:15254012, ECO:0000269|PubMed:15331665, ECO:0000269|PubMed:16996038, ECO:0000269|PubMed:20005871}.
DE  Reference Proteome: Yes;
DE  Interaction: P13508; IntAct: EBI-6456381; Score: 0.37
DE  Interaction: P91001; IntAct: EBI-6460941; Score: 0.37
GO  GO:0005818;
GO  GO:1904115;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0005881;
GO  GO:0000776;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0005815;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0070840;
GO  GO:0051010;
GO  GO:0048854;
GO  GO:0051301;
GO  GO:0051026;
GO  GO:0009792;
GO  GO:0043652;
GO  GO:0000132;
GO  GO:0007281;
GO  GO:0040011;
GO  GO:0051661;
GO  GO:0031023;
GO  GO:0051012;
GO  GO:0007018;
GO  GO:0007100;
GO  GO:0007097;
GO  GO:0031022;
GO  GO:0048477;
GO  GO:0035046;
GO  GO:0008090;
GO  GO:0051225;
GO  GO:0051932;
GO  GO:0048489;
GO  GO:0047496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLSERQKEEINRAIAEYMQNNGYSESFSVFLKESSLSENDIKPLGGILEKKWTTVLRLQRKVNDLESKLQESQREINHG
SQ  APTRDKRQAADWIPRPPETQKLTGHRLPITRVIFHPLWTIMASCSEDATIKVWDYETGQLERTLKGHTDAVNDIAIDAAG
SQ  KQLVSCSSDLSIKLWDFGQTYDCLKSLKGHEHTVSSVTFLPTGDFVLSASRDHTIKQWDISTGYCVYTFRGHNDWVRMIR
SQ  ISNDGTLFASASLDQTVTVWSFATKSAKLVLRDHEHAVECVEWAPDTAYTNVTGQQPEGNSTHILFSGSRDRSIKAWNIN
SQ  TGDVLFTLLAHENWVRGLAFHPKGKYLISVADDKTLRVWELSAQRCMKAIEAHEHFVSTVAFHQTSPFVITGSVDMSCKV
SQ  WECR
//
ID  B0LSW3;
PN  Platelet-activating factor acetylhydrolase IB subunit beta;
GN  PAFAH1B1;
OS  9685;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP- Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes. {ECO:0000255|HAMAP- Rule:MF_03141}.
DR  UNIPROT: B0LSW3;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition- dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule- dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos. May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P63005, ECO:0000255|HAMAP-Rule:MF_03141}.
DE  Reference Proteome: Yes;
GO  GO:0008247;
GO  GO:0000235;
GO  GO:1904115;
GO  GO:0005938;
GO  GO:0031252;
GO  GO:0005813;
GO  GO:0005881;
GO  GO:0000776;
GO  GO:0005875;
GO  GO:0031514;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0032420;
GO  GO:0045202;
GO  GO:0070840;
GO  GO:0042802;
GO  GO:0051010;
GO  GO:0051219;
GO  GO:0046982;
GO  GO:0001675;
GO  GO:0030036;
GO  GO:0008344;
GO  GO:0001667;
GO  GO:0060117;
GO  GO:0048854;
GO  GO:0051301;
GO  GO:0007268;
GO  GO:0090102;
GO  GO:0021540;
GO  GO:0043622;
GO  GO:0000132;
GO  GO:0042249;
GO  GO:0007281;
GO  GO:0021766;
GO  GO:1904936;
GO  GO:0007254;
GO  GO:0021819;
GO  GO:0007611;
GO  GO:0016042;
GO  GO:0051661;
GO  GO:0090176;
GO  GO:0031023;
GO  GO:0051012;
GO  GO:0097529;
GO  GO:0046329;
GO  GO:0007405;
GO  GO:0050885;
GO  GO:0051081;
GO  GO:0007097;
GO  GO:0036035;
GO  GO:0001961;
GO  GO:0061003;
GO  GO:0040019;
GO  GO:0009306;
GO  GO:0140650;
GO  GO:0038026;
GO  GO:0043087;
GO  GO:0070507;
GO  GO:0008090;
GO  GO:0019226;
GO  GO:0047496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFT
SQ  SGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDH
SQ  SGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
SQ  RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI
SQ  KMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSV
SQ  DQTVKVWECR
//
ID  P43034;
PN  Platelet-activating factor acetylhydrolase IB subunit beta;
GN  PAFAH1B1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP- Rule:MF_03141}. Note=Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes (By similarity). Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. {ECO:0000250}.
DR  UNIPROT: P43034;
DR  UNIPROT: B2R7Q7;
DR  UNIPROT: Q8WZ88;
DR  UNIPROT: Q8WZ89;
DR  PDB: 7MT1;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 247200;
DR  OMIM: 601545;
DR  OMIM: 607432;
DR  DisGeNET: 5048;
DE  Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition- dependent manner (By similarity). Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (PubMed:22956769). May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P63005, ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:22956769}.
DE  Disease: Lissencephaly 1 (LIS1) [MIM:607432]: A classical lissencephaly. It is characterized by agyria or pachygyria and disorganization of the clear neuronal lamination of normal six-layered cortex. The cortex is abnormally thick and poorly organized with 4 primitive layers. Associated with enlarged and dysmorphic ventricles and often hypoplasia of the corpus callosum. {ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:11502906, ECO:0000269|PubMed:15007136, ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:9063735}. Note=The disease is caused by variants affecting the gene represented in this entry. Subcortical band heterotopia (SBH) [MIM:607432]: SBH is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal. {ECO:0000269|PubMed:10441340, ECO:0000269|PubMed:14581661}. Note=The disease is caused by variants affecting the gene represented in this entry. Miller-Dieker lissencephaly syndrome (MDLS) [MIM:247200]: A contiguous gene deletion syndrome of chromosome 17p13.3, characterized by classical lissencephaly and distinct facial features. Additional congenital malformations can be part of the condition. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: Q15046; IntAct: EBI-734890; Score: 0.00
DE  Interaction: Q9GZM8; IntAct: EBI-1009436; Score: 0.64
DE  Interaction: Q66J96; IntAct: EBI-1009443; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-26611091; Score: 0.57
DE  Interaction: O35685; IntAct: EBI-2272786; Score: 0.37
DE  Interaction: Q9CZA6; IntAct: EBI-2272814; Score: 0.65
DE  Interaction: P49454; IntAct: EBI-2298103; Score: 0.35
DE  Interaction: P63005; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: Q9ERR1; IntAct: EBI-7611948; Score: 0.53
DE  Interaction: P58680; IntAct: EBI-2865357; Score: 0.00
DE  Interaction: A0A5P8YFD8; IntAct: EBI-2865350; Score: 0.00
DE  Interaction: Q15051; IntAct: EBI-4286917; Score: 0.35
DE  Interaction: Q61206; IntAct: EBI-11068161; Score: 0.35
DE  Interaction: Q3UHI0; IntAct: EBI-11073637; Score: 0.35
DE  Interaction: Q80WE4; IntAct: EBI-11094761; Score: 0.35
DE  Interaction: Q14204; IntAct: EBI-11148090; Score: 0.64
DE  Interaction: Q14203; IntAct: EBI-11382201; Score: 0.48
DE  Interaction: Q66GS9; IntAct: EBI-11386281; Score: 0.27
DE  Interaction: Q6ZU80; IntAct: EBI-11388429; Score: 0.27
DE  Interaction: P63172; IntAct: EBI-12449878; Score: 0.51
DE  Interaction: Q8TF09; IntAct: EBI-12449857; Score: 0.51
DE  Interaction: Q9NWU2; IntAct: EBI-12450239; Score: 0.51
DE  Interaction: Q15691; IntAct: EBI-12451110; Score: 0.51
DE  Interaction: Q13409; IntAct: EBI-12451445; Score: 0.51
DE  Interaction: Q9Y6G9; IntAct: EBI-12451445; Score: 0.51
DE  Interaction: P51808; IntAct: EBI-12451445; Score: 0.51
DE  Interaction: Q9NXR1; IntAct: EBI-12451445; Score: 0.51
DE  Interaction: P68402; IntAct: EBI-12451445; Score: 0.51
DE  Interaction: Q15555; IntAct: EBI-11914619; Score: 0.00
DE  Interaction: Q8N157; IntAct: EBI-11922073; Score: 0.00
DE  Interaction: Q8WW35; IntAct: EBI-11924972; Score: 0.00
DE  Interaction: P11142; IntAct: EBI-12737498; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-12737498; Score: 0.35
DE  Interaction: Q15102; IntAct: EBI-21868674; Score: 0.40
DE  Interaction: Q8IVD9; IntAct: EBI-15585562; Score: 0.52
DE  Interaction: P07900; IntAct: EBI-15832137; Score: 0.61
DE  Interaction: Q8WVJ2; IntAct: EBI-15832137; Score: 0.64
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9UKE5; IntAct: EBI-21381127; Score: 0.00
DE  Interaction: P17813; IntAct: EBI-22197897; Score: 0.35
DE  Interaction: O76071; IntAct: EBI-25477658; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
DE  Interaction: Q6ZMQ8; IntAct: EBI-32723474; Score: 0.27
GO  GO:0008247;
GO  GO:0000235;
GO  GO:1904115;
GO  GO:0005938;
GO  GO:0031252;
GO  GO:0090724;
GO  GO:0005813;
GO  GO:0005881;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005871;
GO  GO:0000776;
GO  GO:0005875;
GO  GO:0031514;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0032420;
GO  GO:0045202;
GO  GO:0034452;
GO  GO:0070840;
GO  GO:0045505;
GO  GO:0008201;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0043274;
GO  GO:0051219;
GO  GO:0046982;
GO  GO:0001675;
GO  GO:0030036;
GO  GO:0008344;
GO  GO:0001667;
GO  GO:0060117;
GO  GO:0048854;
GO  GO:0021987;
GO  GO:0021895;
GO  GO:0007268;
GO  GO:0090102;
GO  GO:0021540;
GO  GO:0043622;
GO  GO:0051660;
GO  GO:0000132;
GO  GO:0042249;
GO  GO:0007281;
GO  GO:0021766;
GO  GO:1904936;
GO  GO:0007254;
GO  GO:0021819;
GO  GO:0007611;
GO  GO:0016042;
GO  GO:0051661;
GO  GO:0000226;
GO  GO:0090176;
GO  GO:0031023;
GO  GO:0051012;
GO  GO:0007017;
GO  GO:0097529;
GO  GO:0046329;
GO  GO:0010977;
GO  GO:0007405;
GO  GO:0050885;
GO  GO:0001764;
GO  GO:0051081;
GO  GO:0007097;
GO  GO:0036035;
GO  GO:0046469;
GO  GO:0045773;
GO  GO:0001961;
GO  GO:0061003;
GO  GO:0040019;
GO  GO:0045931;
GO  GO:0009306;
GO  GO:0140650;
GO  GO:0038026;
GO  GO:0043087;
GO  GO:0070507;
GO  GO:0008090;
GO  GO:0017145;
GO  GO:0019226;
GO  GO:0047496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDVNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFT
SQ  SGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDH
SQ  SGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
SQ  RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI
SQ  KMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSV
SQ  DQTVKVWECR
//
ID  Q8HXX0;
PN  Platelet-activating factor acetylhydrolase IB subunit alpha;
GN  PAFAH1B1;
OS  9541;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP- Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes. {ECO:0000255|HAMAP- Rule:MF_03141}.
DR  UNIPROT: Q8HXX0;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition- dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule- dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos. May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P63005, ECO:0000255|HAMAP-Rule:MF_03141}.
DE  Reference Proteome: Yes;
GO  GO:0008247;
GO  GO:0000235;
GO  GO:0005938;
GO  GO:0005813;
GO  GO:0000776;
GO  GO:0005875;
GO  GO:0031965;
GO  GO:0070840;
GO  GO:0046982;
GO  GO:0008344;
GO  GO:0048854;
GO  GO:0051301;
GO  GO:0021987;
GO  GO:0021540;
GO  GO:0000132;
GO  GO:0016042;
GO  GO:0031023;
GO  GO:0051012;
GO  GO:0050885;
GO  GO:0001764;
GO  GO:0038026;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFT
SQ  SGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDH
SQ  SGKLLTSCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHLVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
SQ  RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI
SQ  KMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSV
SQ  DQTVKVWECR
//
ID  P63005;
PN  Platelet-activating factor acetylhydrolase IB subunit beta;
GN  Pafah1b1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=May localize to the nuclear membrane (By similarity). Localizes to the plus end of microtubules and to the centrosome. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes. {ECO:0000250}.
DR  UNIPROT: P63005;
DR  UNIPROT: O35592;
DR  UNIPROT: P43035;
DR  UNIPROT: P81692;
DR  UNIPROT: Q9R2A6;
DR  PDB: 1UUJ;
DR  PDB: 1VYH;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition- dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule- dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity). May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (PubMed:17330141). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034, ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:11056530, ECO:0000269|PubMed:11344260, ECO:0000269|PubMed:12796778, ECO:0000269|PubMed:12911752, ECO:0000269|PubMed:14507966, ECO:0000269|PubMed:14578885, ECO:0000269|PubMed:14691133, ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:15473966, ECO:0000269|PubMed:16107726, ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:16369480, ECO:0000269|PubMed:16481446, ECO:0000269|PubMed:17330141}.
DE  Reference Proteome: Yes;
DE  Interaction: O14976; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: P43034; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: P49454; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q9ERR1; IntAct: EBI-6934381; Score: 0.80
DE  Interaction: Q61205; IntAct: EBI-1007634; Score: 0.51
DE  Interaction: Q155P7; IntAct: EBI-2272212; Score: 0.32
DE  Interaction: Q9CZA6; IntAct: EBI-2431156; Score: 0.44
DE  Interaction: P68402; IntAct: EBI-2557468; Score: 0.56
DE  Interaction: Q16658; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: Q9NXR1; IntAct: EBI-2557468; Score: 0.56
DE  Interaction: O43854; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: P07951; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: P62136; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: P13797; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: Q15102; IntAct: EBI-2557468; Score: 0.56
DE  Interaction: P47755; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: Q6PJM5; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: Q9GZM8; IntAct: EBI-2557468; Score: 0.78
DE  Interaction: Q9NYL9; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: Q6NYC8; IntAct: EBI-2557468; Score: 0.40
DE  Interaction: Q9H7U1; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: O43237; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q9Y6G9; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q9Y6M0; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q66GS9; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: O75746; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: P28066; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: J3KPF0; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q4LE39; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q9P2X3; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q8TEX9; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q155Q3; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q13409; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q08AN1; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q8IXH7; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: G3V3R7; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q96MM7; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q14204; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q9NP97; IntAct: EBI-11041417; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0008247;
GO  GO:0000235;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005938;
GO  GO:0031252;
GO  GO:0090724;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005881;
GO  GO:0005829;
GO  GO:0030426;
GO  GO:0005871;
GO  GO:0000776;
GO  GO:0005875;
GO  GO:0015630;
GO  GO:0031514;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0032420;
GO  GO:0045202;
GO  GO:0031982;
GO  GO:0070840;
GO  GO:0045505;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0051219;
GO  GO:0046982;
GO  GO:0044877;
GO  GO:0001675;
GO  GO:0030036;
GO  GO:0008344;
GO  GO:0001667;
GO  GO:0060117;
GO  GO:0048854;
GO  GO:0016477;
GO  GO:0021987;
GO  GO:0021895;
GO  GO:0007268;
GO  GO:0090102;
GO  GO:0021540;
GO  GO:0043622;
GO  GO:0051660;
GO  GO:0051649;
GO  GO:0000132;
GO  GO:0042249;
GO  GO:0007281;
GO  GO:0021766;
GO  GO:1904936;
GO  GO:0007254;
GO  GO:0021819;
GO  GO:0007611;
GO  GO:0016042;
GO  GO:0051661;
GO  GO:0000226;
GO  GO:0090176;
GO  GO:0031023;
GO  GO:0051012;
GO  GO:0007017;
GO  GO:0097529;
GO  GO:0046329;
GO  GO:0010977;
GO  GO:0007405;
GO  GO:0050885;
GO  GO:0001764;
GO  GO:0051081;
GO  GO:0007097;
GO  GO:0036035;
GO  GO:0045773;
GO  GO:0051130;
GO  GO:0001961;
GO  GO:0061003;
GO  GO:0040019;
GO  GO:0045931;
GO  GO:0009306;
GO  GO:0140650;
GO  GO:0038026;
GO  GO:0043087;
GO  GO:0070507;
GO  GO:0008090;
GO  GO:0017145;
GO  GO:0019226;
GO  GO:0047496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFT
SQ  SGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDH
SQ  SGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
SQ  RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI
SQ  KMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSV
SQ  DQTVKVWECR
//
ID  Q5IS43;
PN  Platelet-activating factor acetylhydrolase IB subunit alpha;
GN  PAFAH1B1;
OS  9598;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP- Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes. {ECO:0000255|HAMAP- Rule:MF_03141}.
DR  UNIPROT: Q5IS43;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition- dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule- dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos. May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P63005, ECO:0000255|HAMAP-Rule:MF_03141}.
DE  Reference Proteome: Yes;
GO  GO:0008247;
GO  GO:1904115;
GO  GO:0005881;
GO  GO:0000776;
GO  GO:0005875;
GO  GO:0005815;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005819;
GO  GO:0070840;
GO  GO:0051010;
GO  GO:0046982;
GO  GO:0048854;
GO  GO:0051301;
GO  GO:0000132;
GO  GO:0007281;
GO  GO:0016042;
GO  GO:0031023;
GO  GO:0051012;
GO  GO:0007097;
GO  GO:0038026;
GO  GO:0008090;
GO  GO:0047496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFT
SQ  SGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDH
SQ  SGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
SQ  RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI
SQ  KMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGFV
SQ  DQTVKVWECR
//
ID  Q9GL51;
PN  Platelet-activating factor acetylhydrolase IB subunit alpha;
GN  PAFAH1B1;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP- Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes. {ECO:0000255|HAMAP- Rule:MF_03141}.
DR  UNIPROT: Q9GL51;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition- dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule- dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos. May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P63005, ECO:0000255|HAMAP-Rule:MF_03141}.
DE  Reference Proteome: Yes;
GO  GO:0008247;
GO  GO:0005737;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0005815;
GO  GO:0031965;
GO  GO:0005819;
GO  GO:0070840;
GO  GO:0046982;
GO  GO:0030154;
GO  GO:0051301;
GO  GO:0000132;
GO  GO:0016042;
GO  GO:0051012;
GO  GO:0007399;
GO  GO:0038026;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFT
SQ  SGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDH
SQ  SGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSAARDKTIKMWEVQTGYCVKTFTGHREWVRMV
SQ  RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI
SQ  KMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSV
SQ  DQTVKVWECR
//
ID  Q5REG7;
PN  Platelet-activating factor acetylhydrolase IB subunit alpha;
GN  PAFAH1B1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP- Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes. {ECO:0000255|HAMAP- Rule:MF_03141}.
DR  UNIPROT: Q5REG7;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition- dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule- dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos. May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P63005, ECO:0000255|HAMAP-Rule:MF_03141}.
DE  Reference Proteome: Yes;
GO  GO:0008247;
GO  GO:0005737;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0005815;
GO  GO:0031965;
GO  GO:0005819;
GO  GO:0070840;
GO  GO:0046982;
GO  GO:0030154;
GO  GO:0051301;
GO  GO:0000132;
GO  GO:0016042;
GO  GO:0051012;
GO  GO:0007399;
GO  GO:0038026;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFT
SQ  SGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSIQDIPFDH
SQ  SGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
SQ  RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI
SQ  KMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSV
SQ  DQTVKVWECR
//
ID  P63004;
PN  Platelet-activating factor acetylhydrolase IB subunit alpha;
GN  Pafah1b1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP- Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes (By similarity). Redistributes to axons during neuronal development. {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:11001923, ECO:0000269|PubMed:11056530, ECO:0000269|PubMed:16481446}.
DR  UNIPROT: P63004;
DR  UNIPROT: O35592;
DR  UNIPROT: P43035;
DR  UNIPROT: P81692;
DR  UNIPROT: Q9R2A6;
DR  Pfam: PF08513;
DR  Pfam: PF00400;
DR  PROSITE: PS50896;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition- dependent manner (By similarity). Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule- dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity). May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P63005, ECO:0000269|PubMed:11056532, ECO:0000269|PubMed:16144905}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q78PB6; IntAct: EBI-27039409; Score: 0.40
GO  GO:0008247;
GO  GO:0000235;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005938;
GO  GO:0031252;
GO  GO:0090724;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005881;
GO  GO:0005829;
GO  GO:0030426;
GO  GO:0005871;
GO  GO:0000776;
GO  GO:0005875;
GO  GO:0015630;
GO  GO:0031514;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0032420;
GO  GO:0045202;
GO  GO:0031982;
GO  GO:0070840;
GO  GO:0045505;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0051010;
GO  GO:0051219;
GO  GO:0047179;
GO  GO:0046982;
GO  GO:0044877;
GO  GO:0001675;
GO  GO:0030036;
GO  GO:0008344;
GO  GO:0001667;
GO  GO:0060117;
GO  GO:0007420;
GO  GO:0048854;
GO  GO:0016477;
GO  GO:0021987;
GO  GO:0021895;
GO  GO:0007268;
GO  GO:0090102;
GO  GO:0021540;
GO  GO:0043622;
GO  GO:0051660;
GO  GO:0051649;
GO  GO:0000132;
GO  GO:0042249;
GO  GO:0007281;
GO  GO:0021766;
GO  GO:1904936;
GO  GO:0007254;
GO  GO:0021819;
GO  GO:0007611;
GO  GO:0016042;
GO  GO:0051661;
GO  GO:0000226;
GO  GO:0090176;
GO  GO:0031023;
GO  GO:0051012;
GO  GO:0007017;
GO  GO:0097529;
GO  GO:0046329;
GO  GO:0010977;
GO  GO:0007405;
GO  GO:0050885;
GO  GO:0001764;
GO  GO:0051081;
GO  GO:0007097;
GO  GO:0036035;
GO  GO:0045773;
GO  GO:0051130;
GO  GO:0001961;
GO  GO:0061003;
GO  GO:0040019;
GO  GO:0045931;
GO  GO:0009306;
GO  GO:0140650;
GO  GO:0038026;
GO  GO:0043087;
GO  GO:0070507;
GO  GO:0008090;
GO  GO:0017145;
GO  GO:0019226;
GO  GO:0047496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFT
SQ  SGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDH
SQ  SGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
SQ  RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI
SQ  KMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSV
SQ  DQTVKVWECR
//
ID  Q21443;
PN  Lamin-1;
GN  lmn;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16950114}. Nucleus inner membrane {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:12490171, ECO:0000269|PubMed:25057012}; Lipid-anchor {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:12490171}; Nucleoplasmic side {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:12490171}. Note=Remains in the nuclear envelope until late anaphase in early embryos. Depends on mel-28 for nuclear envelope localization after mitosis. {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:16950114}.
DR  UNIPROT: Q21443;
DR  UNIPROT: O62127;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Major component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:11071918, PubMed:25057012). Provides a framework for the nuclear envelope and probably also interacts with chromatin (PubMed:11071918, PubMed:25057012). Essential to maintain the shape and integrity of the nucleus, and for DNA replication (PubMed:11071918). Involved in spatial organization of nuclear pore complexes (PubMed:11071918). It is not a target for ced-3 during apoptosis, suggesting that lamin cleavage is not essential for apoptosis in C.elegans (PubMed:12064941). {ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:12064941, ECO:0000269|PubMed:25057012}.
DE  Reference Proteome: Yes;
DE  Interaction: G5EEH9; IntAct: EBI-6455606; Score: 0.37
DE  Interaction: Q09601; IntAct: EBI-6460126; Score: 0.37
DE  Interaction: Q18508; IntAct: EBI-6459403; Score: 0.37
DE  Interaction: Q20924; IntAct: EBI-15599068; Score: 0.44
DE  Interaction: O44452; IntAct: EBI-333329; Score: 0.00
DE  Interaction: Q19633; IntAct: EBI-336260; Score: 0.00
DE  Interaction: Q19969; IntAct: EBI-336722; Score: 0.00
DE  Interaction: P91505; IntAct: EBI-342362; Score: 0.00
DE  Interaction: Q9XXH8; IntAct: EBI-343838; Score: 0.00
DE  Interaction: Q7JLR4; IntAct: EBI-2415544; Score: 0.49
DE  Interaction: Q9XTB5; IntAct: EBI-2535415; Score: 0.53
DE  Interaction: G5EDM4; IntAct: EBI-2913499; Score: 0.00
DE  Interaction: Q09284; IntAct: EBI-2915636; Score: 0.00
DE  Interaction: G5ECZ8; IntAct: EBI-2915821; Score: 0.00
DE  Interaction: C1P635; IntAct: EBI-2917320; Score: 0.00
DE  Interaction: O44548; IntAct: EBI-6455593; Score: 0.37
DE  Interaction: G5ECR7; IntAct: EBI-6459638; Score: 0.37
DE  Interaction: P34402; IntAct: EBI-6459648; Score: 0.37
DE  Interaction: Q19749; IntAct: EBI-6459668; Score: 0.37
DE  Interaction: Q9U3C1; IntAct: EBI-6459698; Score: 0.37
DE  Interaction: Q21295; IntAct: EBI-6459688; Score: 0.37
DE  Interaction: O01585; IntAct: EBI-6459708; Score: 0.37
DE  Interaction: P30642; IntAct: EBI-6459718; Score: 0.37
DE  Interaction: P91457; IntAct: EBI-6459728; Score: 0.37
DE  Interaction: Q86S68; IntAct: EBI-6459738; Score: 0.37
DE  Interaction: Q95XY1; IntAct: EBI-6459748; Score: 0.37
DE  Interaction: Q65XX1; IntAct: EBI-6459758; Score: 0.37
DE  Interaction: G5ECG0; IntAct: EBI-6459768; Score: 0.37
DE  Interaction: Q95QC4; IntAct: EBI-6459778; Score: 0.37
DE  Interaction: O02217; IntAct: EBI-6460096; Score: 0.37
DE  Interaction: Q8WQC0; IntAct: EBI-6460116; Score: 0.37
DE  Interaction: P39745; IntAct: EBI-6460106; Score: 0.37
DE  Interaction: Q95Y84; IntAct: EBI-6460136; Score: 0.37
DE  Interaction: P12114; IntAct: EBI-6460546; Score: 0.37
DE  Interaction: Q8MPS6; IntAct: EBI-6460556; Score: 0.37
DE  Interaction: Q23593; IntAct: EBI-6460571; Score: 0.37
DE  Interaction: Q09583; IntAct: EBI-6460581; Score: 0.37
DE  Interaction: Q17391; IntAct: EBI-6461424; Score: 0.37
DE  Interaction: Q21443; IntAct: EBI-6461509; Score: 0.64
DE  Interaction: O01527; IntAct: EBI-6748850; Score: 0.00
DE  Interaction: Q9GYG1; IntAct: EBI-6748863; Score: 0.00
DE  Interaction: O62090; IntAct: EBI-11466936; Score: 0.37
DE  Interaction: P34288; IntAct: EBI-11470392; Score: 0.37
DE  Interaction: Q95ZY7; IntAct: EBI-11471304; Score: 0.37
DE  Interaction: Q965F9; IntAct: EBI-11471316; Score: 0.37
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005652;
GO  GO:0034399;
GO  GO:0042393;
GO  GO:0042802;
GO  GO:0005200;
GO  GO:0005198;
GO  GO:0008340;
GO  GO:0009792;
GO  GO:0007281;
GO  GO:0031507;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0030473;
GO  GO:0051664;
GO  GO:0006997;
GO  GO:0008284;
GO  GO:0008104;
GO  GO:0090435;
GO  GO:0051983;
GO  GO:0007346;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSRKGTRSSRIVTLERSANSSLSNNGGGDDSFGSTLLETSRLQEKDHLTSLNSRLATYIDKVRQLEQENNRLQVQIRDI
SQ  EVVEKKEKSNLADRFEAEKARLRRALDSAQDELAKYRIEYDAAKVEVKKLKPQVEKLERELAGAEEQALHAQSIADQSQA
SQ  KQKTLQARNDKLVVENDDLKKQNITLRDTVEGLKKAVEDETLLRTAANNKIKALEEDLAFALQQHKGELEEVRHKRQVDM
SQ  TTYAKQINDEYQSKLQDQIEEMRAQFKNNLHQNKTAFEDAYKNKLNAARERQEEAVSEAIHLRARVRDLETSSSGNASLI
SQ  ERLRSELDTLKRSFQEKLDDKDARIAELNQEIERMMSEFHDLLDVKIQLDAELKTYQALLEGEEERLNLTQEAPQNTSVH
SQ  HVSFSSGGASAQRGVKRRRVVDVNGEDQDIDYLNRRSKLNKETVGPVGIDEVDEEGKWVRVANNSEEEQSIGGYKLVVKA
SQ  GNKEASFQFSSRMKLAPHASATVWSADAGAVHHPPEVYVMKKQQWPIGDNPSARLEDSEGDTVSSITVEFSESSDPSDPA
SQ  DRCSIM
//
ID  A0A125S9M5;
PN  Lamin-2;
GN  LMN2;
OS  2072580;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side {ECO:0000269|PubMed:26840051}. Note=Localization is restricted to the nuclear periphery which is consistent with the presence of a C-terminal isoprenylation motif (PubMed:26840051). {ECO:0000269|PubMed:26840051}.
DR  UNIPROT: A0A125S9M5;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Intermediate filament (IF) protein, component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope (PubMed:26840051). {ECO:0000305|PubMed:26840051}.
DE  Reference Proteome: No;
GO  GO:0005882;
GO  GO:0005637;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:26840051};
SQ  MSAQVSKKRGGSNPPKTGQHAASSTTSRTESSATSQTIYERQEVETRTQRTPGGLLLAASSAEVSSGTAGLAGSPLSRHQ
SQ  EKEEFKLLNNRFANYIDTIRAQQEEISVLRRKVETVSSKEVVENQKIKERYNLEIANLRRALDEVSRDLAAAIIERDSLR
SQ  PERDARLLLDNEKKTLQKRSKDAEAALKDAKNQLAALRDQAKDHDNEIHGLTTENSSLKLQIENLKKDLSQETNLRVDAE
SQ  NRLQSEREKNALLEGIHNEEIVSLRNQRRTEITEVETRMGEEYQSKIVEQLNDLRADLEAVAHEMRLDLERSYQNQLEDS
SQ  QDLANRYRDEARALLADLSAAQDRIKETQTRSEKQLQELRLQLQRLQAELNGKDDEVQRLQKLLADRQAELQNTHHELSR
SQ  QIASYQELLDEKIHLDAELATYNALLRTEEERLNMKSPPFPSTPDSQRRGTKRRIADSYTRTRFRNEASATGDIHISEID
SQ  AEGQFVRLENKSGQDVVIGGWKLLMVSDNGEDNKTDYKIHSNQVIKAHSSTTIWSANTNVVHEPPADIVMEGRWLVGDHT
SQ  SVTLSTSDGVEVARREMTQSSTRDDSYLGPSGLPKRSRLVVADSSDHQKNCVIM
//
ID  P02545;
PN  Lamin-A/C;
GN  LMNA;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus {ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:31548606}. Nucleus envelope {ECO:0000269|PubMed:29599122}. Nucleus lamina. Nucleus, nucleoplasm. Nucleus matrix {ECO:0000269|PubMed:31548606}. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C. [Isoform C]: Nucleus speckle {ECO:0000269|PubMed:16061563}.
DR  UNIPROT: P02545;
DR  UNIPROT: B4DI32;
DR  UNIPROT: D3DVB0;
DR  UNIPROT: D6RAQ3;
DR  UNIPROT: E7EUI9;
DR  UNIPROT: P02546;
DR  UNIPROT: Q5I6Y4;
DR  UNIPROT: Q5I6Y6;
DR  UNIPROT: Q5TCJ2;
DR  UNIPROT: Q5TCJ3;
DR  UNIPROT: Q6UYC3;
DR  UNIPROT: Q969I8;
DR  UNIPROT: Q96JA2;
DR  PDB: 1IFR;
DR  PDB: 1IVT;
DR  PDB: 1X8Y;
DR  PDB: 2XV5;
DR  PDB: 2YPT;
DR  PDB: 3GEF;
DR  PDB: 3V4Q;
DR  PDB: 3V4W;
DR  PDB: 3V5B;
DR  PDB: 6GHD;
DR  PDB: 6JLB;
DR  PDB: 6RPR;
DR  PDB: 6SNZ;
DR  PDB: 6YF5;
DR  PDB: 6YJD;
DR  PDB: 7CRG;
DR  PDB: 7D9N;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DR  OMIM: 115200;
DR  OMIM: 150330;
DR  OMIM: 151660;
DR  OMIM: 176670;
DR  OMIM: 181350;
DR  OMIM: 212112;
DR  OMIM: 248370;
DR  OMIM: 605588;
DR  OMIM: 610140;
DR  OMIM: 613205;
DR  OMIM: 616516;
DR  OMIM: 619793;
DR  DisGeNET: 4000;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:22431096, PubMed:10814726, PubMed:11799477, PubMed:18551513). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:18551513, ECO:0000269|PubMed:18611980, ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:23666920, ECO:0000269|PubMed:31548606}. Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence.
DE  Disease: Emery-Dreifuss muscular dystrophy 2, autosomal dominant (EDMD2) [MIM:181350]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10739764, ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:10908904, ECO:0000269|PubMed:10939567, ECO:0000269|PubMed:11503164, ECO:0000269|PubMed:11525883, ECO:0000269|PubMed:11792809, ECO:0000269|PubMed:12032588, ECO:0000269|PubMed:12467752, ECO:0000269|PubMed:12649505, ECO:0000269|PubMed:12673789, ECO:0000269|PubMed:14684700, ECO:0000269|PubMed:14985400, ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:15744034, ECO:0000269|PubMed:17136397, ECO:0000269|PubMed:19933576, ECO:0000269|PubMed:20848652, ECO:0000269|PubMed:27234031}. Note=The disease is caused by variants affecting the gene represented in this entry. Emery-Dreifuss muscular dystrophy 3, autosomal recessive (EDMD3) [MIM:616516]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:27234031}. Note=The disease is caused by variants affecting the gene represented in this entry. Cardiomyopathy, dilated 1A (CMD1A) [MIM:115200]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:11561226, ECO:0000269|PubMed:11792809, ECO:0000269|PubMed:11897440, ECO:0000269|PubMed:12486434, ECO:0000269|PubMed:12628721, ECO:0000269|PubMed:12920062, ECO:0000269|PubMed:14675861, ECO:0000269|PubMed:14684700, ECO:0000269|PubMed:15140538, ECO:0000269|PubMed:15219508, ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:16061563, ECO:0000269|PubMed:18606848, ECO:0000269|PubMed:19167105, ECO:0000269|PubMed:20160190, ECO:0000269|PubMed:21846512}. Note=The disease is caused by variants affecting the gene represented in this entry. Lipodystrophy, familial partial, 2 (FPLD2) [MIM:151660]: A disorder characterized by the loss of subcutaneous adipose tissue in the lower parts of the body (limbs, buttocks, trunk). It is accompanied by an accumulation of adipose tissue in the face and neck causing a double chin, fat neck, or cushingoid appearance. Adipose tissue may also accumulate in the axillae, back, labia majora, and intraabdominal region. Affected patients are insulin-resistant and may develop glucose intolerance and diabetes mellitus after age 20 years, hypertriglyceridemia, and low levels of high density lipoprotein cholesterol. {ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10655060, ECO:0000269|PubMed:10739751, ECO:0000269|PubMed:11792809, ECO:0000269|PubMed:12015247, ECO:0000269|PubMed:12196663, ECO:0000269|PubMed:12629077, ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:17250669, ECO:0000269|PubMed:19220582, ECO:0000269|PubMed:24485160}. Note=The disease is caused by variants affecting the gene represented in this entry. Charcot-Marie-Tooth disease 2B1 (CMT2B1) [MIM:605588]: A recessive axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. {ECO:0000269|PubMed:11799477}. Note=The disease is caused by variants affecting the gene represented in this entry. Hutchinson-Gilford progeria syndrome (HGPS) [MIM:176670]: Rare genetic disorder characterized by features reminiscent of marked premature aging. {ECO:0000269|PubMed:12714972, ECO:0000269|PubMed:12768443, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15060110, ECO:0000269|PubMed:15286156, ECO:0000269|PubMed:15622532, ECO:0000269|PubMed:19933576, ECO:0000269|PubMed:21791255, ECO:0000269|PubMed:22355414, ECO:0000269|PubMed:23666920}. Note=The disease is caused by variants affecting the gene represented in this entry. HGPS is caused by the toxic accumulation of a truncated form of lamin-A/C. This mutant protein, called progerin (isoform 6), acts to deregulate mitosis and DNA damage signaling, leading to premature cell death and senescence. The mutant form is mainly generated by a silent or missense mutation at codon 608 of prelamin A that causes activation of a cryptic splice donor site, resulting in production of isoform 6 with a deletion of 50 amino acids near the C terminus. Progerin lacks the conserved ZMPSTE24/FACE1 cleavage site and therefore remains permanently farnesylated. Thus, although it can enter the nucleus and associate with the nuclear envelope, it cannot incorporate normally into the nuclear lamina (PubMed:12714972). {ECO:0000269|PubMed:12714972}. Cardiomyopathy, dilated, with hypergonadotropic hypogonadism (CMDHH) [MIM:212112]: A disorder characterized by the association of genital anomalies, hypergonadotropic hypogonadism and dilated cardiomyopathy. Patients can present other variable clinical manifestations including intellectual disability, skeletal anomalies, scleroderma-like skin, graying and thinning of hair, osteoporosis. Dilated cardiomyopathy is characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. {ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:17150192, ECO:0000269|PubMed:19283854}. Note=The disease is caused by variants affecting the gene represented in this entry. Mandibuloacral dysplasia with type A lipodystrophy (MADA) [MIM:248370]: A form of mandibuloacral dysplasia, a rare progeroid disorder with clinical and genetic heterogeneity, characterized by growth retardation, craniofacial dysmorphic features due to distal bone resorption, musculoskeletal and skin abnormalities associated with lipodystrophy. MADA is an autosomal recessive disease characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, progeroid appearance, partial alopecia, soft tissue calcinosis, joint contractures, and partial lipodystrophy with loss of subcutaneous fat from the extremities. Adipose tissue in the face, neck and trunk is normal or increased. {ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:15998779, ECO:0000269|PubMed:16278265}. Note=The disease is caused by variants affecting the gene represented in this entry. Restrictive dermopathy 2 (RSDM2) [MIM:619793]: An autosomal dominant form of restrictive dermopathy, a genodermatosis mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial dysmorphism, sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. {ECO:0000269|PubMed:15317753}. Note=The disease is caused by variants affecting the gene represented in this entry. Heart-hand syndrome Slovenian type (HHS-Slovenian) [MIM:610140]: Heart-hand syndrome (HHS) is a clinically and genetically heterogeneous disorder characterized by the co-occurrence of a congenital cardiac disease and limb malformations. {ECO:0000269|PubMed:18611980}. Note=The disease is caused by variants affecting the gene represented in this entry. Muscular dystrophy congenital LMNA-related (MDCL) [MIM:613205]: A form of congenital muscular dystrophy. Patients present at birth, or within the first few months of life, with hypotonia, muscle weakness and often with joint contractures. {ECO:0000269|PubMed:18551513}. Note=The disease is caused by variants affecting the gene represented in this entry. Note=Defects in LMNA may cause a late-onset cardiocutaneous progeria syndrome characterized by cutaneous manifestations of aging appearing in the third decade of life, cardiac valve calcification and dysfunction, prominent atherosclerosis, and cardiomyopathy, leading to death on average in the fourth decade. {ECO:0000269|PubMed:23666920}.
DE  Reference Proteome: Yes;
DE  Interaction: A8CG34; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O15027; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: O15173; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O60238; IntAct: EBI-849933; Score: 0.37
DE  Interaction: O75531; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: O75694; IntAct: EBI-16795756; Score: 0.67
DE  Interaction: O75844; IntAct: EBI-16043055; Score: 0.56
DE  Interaction: O94901; IntAct: EBI-22057187; Score: 0.40
DE  Interaction: P00533; IntAct: EBI-10043997; Score: 0.35
DE  Interaction: P62993; IntAct: EBI-350217; Score: 0.35
DE  Interaction: A0JLT2; IntAct: EBI-394580; Score: 0.35
DE  Interaction: Q92993; IntAct: EBI-730261; Score: 0.00
DE  Interaction: P12830; IntAct: EBI-727492; Score: 0.40
DE  Interaction: P03247; IntAct: EBI-849870; Score: 0.37
DE  Interaction: P63104; IntAct: EBI-7193814; Score: 0.56
DE  Interaction: P13569; IntAct: EBI-1171566; Score: 0.64
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.53
DE  Interaction: P08473; IntAct: EBI-1389788; Score: 0.35
DE  Interaction: P18054; IntAct: EBI-1633241; Score: 0.51
DE  Interaction: P10215; IntAct: EBI-7183643; Score: 0.40
DE  Interaction: P10218; IntAct: EBI-7183692; Score: 0.40
DE  Interaction: P04296; IntAct: EBI-9631489; Score: 0.35
DE  Interaction: P16104; IntAct: EBI-2564373; Score: 0.60
DE  Interaction: Q99469; IntAct: EBI-2654226; Score: 0.00
DE  Interaction: Q9D666; IntAct: EBI-8034322; Score: 0.53
DE  Interaction: P49790; IntAct: EBI-8034338; Score: 0.45
DE  Interaction: Q71DI3; IntAct: EBI-8042534; Score: 0.44
DE  Interaction: O46385; IntAct: EBI-7872537; Score: 0.37
DE  Interaction: A0A6L8PR63; IntAct: EBI-2830464; Score: 0.00
DE  Interaction: A0A6L8P438; IntAct: EBI-2830452; Score: 0.00
DE  Interaction: A0A6L8P912; IntAct: EBI-2830478; Score: 0.00
DE  Interaction: Q81X15; IntAct: EBI-2830490; Score: 0.00
DE  Interaction: Q81KT8; IntAct: EBI-2830471; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.67
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: Q9BQS8; IntAct: EBI-3242919; Score: 0.35
DE  Interaction: Q13155; IntAct: EBI-8578984; Score: 0.35
DE  Interaction: Q96RG2; IntAct: EBI-8614564; Score: 0.44
DE  Interaction: Q5VWP3; IntAct: EBI-3895433; Score: 0.37
DE  Interaction: Q5FW52; IntAct: EBI-3895559; Score: 0.44
DE  Interaction: Q96Q15; IntAct: EBI-3903995; Score: 0.35
DE  Interaction: P20700; IntAct: EBI-3931729; Score: 0.85
DE  Interaction: P11217; IntAct: EBI-5663157; Score: 0.00
DE  Interaction: Q9NRM7; IntAct: EBI-7452196; Score: 0.35
DE  Interaction: P38398; IntAct: EBI-7615501; Score: 0.35
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6515052; Score: 0.35
DE  Interaction: Q9UH99; IntAct: EBI-6838684; Score: 0.64
DE  Interaction: P33993; IntAct: EBI-6875195; Score: 0.35
DE  Interaction: P25490; IntAct: EBI-6921458; Score: 0.35
DE  Interaction: O41970; IntAct: EBI-9641606; Score: 0.37
DE  Interaction: P27661; IntAct: EBI-9699779; Score: 0.40
DE  Interaction: P30411; IntAct: EBI-9843668; Score: 0.37
DE  Interaction: P60409; IntAct: EBI-10193818; Score: 0.56
DE  Interaction: Q9UII6; IntAct: EBI-10322036; Score: 0.78
DE  Interaction: P02545; IntAct: EBI-12689943; Score: 0.60
DE  Interaction: Q13418; IntAct: EBI-10103376; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-10103481; Score: 0.35
DE  Interaction: P53671; IntAct: EBI-10103591; Score: 0.35
DE  Interaction: O60307; IntAct: EBI-10103761; Score: 0.35
DE  Interaction: P42166; IntAct: EBI-10091520; Score: 0.63
DE  Interaction: Q00613; IntAct: EBI-10682932; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q8NF91; IntAct: EBI-10759435; Score: 0.40
DE  Interaction: E9QKK1; IntAct: EBI-10995761; Score: 0.35
DE  Interaction: P42167; IntAct: EBI-11061883; Score: 0.57
DE  Interaction: Q8NC56; IntAct: EBI-10901984; Score: 0.49
DE  Interaction: Q9P2K1; IntAct: EBI-11378868; Score: 0.27
DE  Interaction: Q9E7P0; IntAct: EBI-11423244; Score: 0.37
DE  Interaction: Q9UBX2; IntAct: EBI-11601780; Score: 0.35
DE  Interaction: Q96FA3; IntAct: EBI-24751139; Score: 0.56
DE  Interaction: Q8TBZ8; IntAct: EBI-25186746; Score: 0.56
DE  Interaction: Q8IV20; IntAct: EBI-12508068; Score: 0.35
DE  Interaction: Q8N0S2; IntAct: EBI-12703072; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: O60684; IntAct: EBI-16795756; Score: 0.42
DE  Interaction: Q8IYT4; IntAct: EBI-16421609; Score: 0.35
DE  Interaction: P78527; IntAct: EBI-15913272; Score: 0.35
DE  Interaction: Q03252; IntAct: EBI-16795756; Score: 0.71
DE  Interaction: P50402; IntAct: EBI-16795756; Score: 0.80
DE  Interaction: Q8N726; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P27694; IntAct: EBI-16795756; Score: 0.42
DE  Interaction: Q6NSI4; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q13356; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9Y6X4; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9Y6H1; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9Y5M8; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9Y2U8; IntAct: EBI-16795756; Score: 0.42
DE  Interaction: Q9P287; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9P0L0; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9NXE4; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9HAV7; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9H089; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9BTT0; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q99856; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q96A33; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q969J2; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8WVM8; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8WUQ7; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8WUM0; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8TDD1; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8NFW8; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8NFH4; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8N766; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8IX18; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q86Y07; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q86UE4; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q7Z4V5; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q5VVJ2; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q5VV52; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q5JTV8; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q16775; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q15006; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q14739; IntAct: EBI-16795756; Score: 0.42
DE  Interaction: Q13586; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q12769; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P57740; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P52948; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P52294; IntAct: EBI-16795756; Score: 0.42
DE  Interaction: P51858; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P49257; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P46013; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P39748; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P22087; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P18031; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P09874; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P08240; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P05556; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O95573; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O75937; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O75475; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O15498; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: A6NHR9; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9Y314; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9UKX7; IntAct: EBI-16795756; Score: 0.42
DE  Interaction: Q9P0U3; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9NW82; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9H5V9; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9BW27; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9BUI4; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9BRR0; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q96S55; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q96HA1; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q96EE3; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q96AT1; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q93009; IntAct: EBI-16795756; Score: 0.63
DE  Interaction: Q92917; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8WYP5; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8WUA2; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8NFH3; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q8N1G2; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q86V97; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q6P6C2; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q14974; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q07021; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P78406; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P52292; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P49585; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O95551; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O75928; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O60869; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O15131; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O00629; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O00505; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: O00267; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q92878; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P35244; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P15927; IntAct: EBI-16795953; Score: 0.42
DE  Interaction: Q9C005; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q9BVP2; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q96HS1; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q96EV2; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q7Z739; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q7L2E3; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q6NT76; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q15008; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P51665; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P22061; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P17029; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P12270; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: O43813; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: A8MTY0; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q9ULX6; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q709F0; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q04837; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q00059; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q9UEE9; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q9NZ63; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q9H814; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q9H444; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q9H2H8; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q9H0H5; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q9GZR1; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q9BZJ0; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q96NC0; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q96NB3; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q92541; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q8NFH5; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q8NAV1; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q8N6N3; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q8IWZ8; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q8IVW6; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q7L2J0; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q6UX04; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q6PD62; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q69YN2; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q5HYI8; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q15723; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q13618; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: Q12857; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: P55081; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: P51648; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: P49916; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: P49642; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: P18887; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: P13984; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: O95292; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: O95218; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: O76031; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: O75940; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: O75787; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: O75391; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: O60231; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: O15541; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: O15347; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: P41212; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: Q9Y3C6; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: Q9Y2X9; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: Q9ULW0; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: Q9NQC7; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: Q9H6R4; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: Q9H5Z1; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: Q96PK6; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: Q92620; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: P78332; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: P53814; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: P28347; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: P08651; IntAct: EBI-16796283; Score: 0.27
DE  Interaction: O95714; IntAct: EBI-16811848; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-20306992; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: Q86U44; IntAct: EBI-20594935; Score: 0.35
DE  Interaction: Q15007; IntAct: EBI-20595349; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: P06400; IntAct: EBI-20735701; Score: 0.40
DE  Interaction: P22681; IntAct: EBI-20912558; Score: 0.40
DE  Interaction: P16401; IntAct: EBI-20912406; Score: 0.40
DE  Interaction: Q07283; IntAct: EBI-20914880; Score: 0.40
DE  Interaction: Q6ZVC0; IntAct: EBI-20915312; Score: 0.40
DE  Interaction: P04908; IntAct: EBI-20917416; Score: 0.40
DE  Interaction: Q86Y22; IntAct: EBI-20918092; Score: 0.40
DE  Interaction: O43818; IntAct: EBI-20918636; Score: 0.40
DE  Interaction: Q9UBT6; IntAct: EBI-20918596; Score: 0.40
DE  Interaction: Q8NCW0; IntAct: EBI-20920124; Score: 0.40
DE  Interaction: Q53EL6; IntAct: EBI-20920396; Score: 0.40
DE  Interaction: Q9HBL0; IntAct: EBI-20920300; Score: 0.40
DE  Interaction: Q9ULE6; IntAct: EBI-20926394; Score: 0.40
DE  Interaction: O75379; IntAct: EBI-20926322; Score: 0.40
DE  Interaction: Q16778; IntAct: EBI-20926298; Score: 0.40
DE  Interaction: Q8WWQ0; IntAct: EBI-20929920; Score: 0.40
DE  Interaction: Q96C24; IntAct: EBI-20929912; Score: 0.40
DE  Interaction: Q76NI1; IntAct: EBI-20930704; Score: 0.40
DE  Interaction: O75185; IntAct: EBI-20930664; Score: 0.40
DE  Interaction: Q12840; IntAct: EBI-20931480; Score: 0.40
DE  Interaction: Q14690; IntAct: EBI-20937108; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P13693; IntAct: EBI-20992046; Score: 0.35
DE  Interaction: Q63HN8; IntAct: EBI-21264166; Score: 0.35
DE  Interaction: Q8WXH0; IntAct: EBI-22056370; Score: 0.46
DE  Interaction: P36956; IntAct: EBI-22057623; Score: 0.63
DE  Interaction: P17813; IntAct: EBI-22197429; Score: 0.44
DE  Interaction: Q15311; IntAct: EBI-25375541; Score: 0.35
DE  Interaction: Q15256; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: B2RWW0; IntAct: EBI-25410472; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: O94992; IntAct: EBI-25479174; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: Q8NHP6; IntAct: EBI-25617558; Score: 0.35
DE  Interaction: O43572; IntAct: EBI-26451580; Score: 0.35
DE  Interaction: Q99612; IntAct: EBI-25874703; Score: 0.56
DE  Interaction: P10074; IntAct: EBI-25874713; Score: 0.56
DE  Interaction: Q13123; IntAct: EBI-25874721; Score: 0.56
DE  Interaction: Q14005; IntAct: EBI-25874729; Score: 0.56
DE  Interaction: Q12986; IntAct: EBI-25874739; Score: 0.56
DE  Interaction: Q03181; IntAct: EBI-25874747; Score: 0.56
DE  Interaction: P62701; IntAct: EBI-25874755; Score: 0.56
DE  Interaction: P17024; IntAct: EBI-25874771; Score: 0.56
DE  Interaction: Q15776; IntAct: EBI-25874779; Score: 0.56
DE  Interaction: P46379; IntAct: EBI-25874787; Score: 0.56
DE  Interaction: Q9UNS2; IntAct: EBI-25874795; Score: 0.56
DE  Interaction: O75925; IntAct: EBI-25874803; Score: 0.56
DE  Interaction: Q96GN5; IntAct: EBI-25874819; Score: 0.56
DE  Interaction: O43309; IntAct: EBI-25874835; Score: 0.56
DE  Interaction: P54274; IntAct: EBI-25874763; Score: 0.56
DE  Interaction: Q13133; IntAct: EBI-25874851; Score: 0.56
DE  Interaction: Q9Y4E8; IntAct: EBI-25874843; Score: 0.56
DE  Interaction: Q9UNE7; IntAct: EBI-25874867; Score: 0.56
DE  Interaction: Q9Y239; IntAct: EBI-25874875; Score: 0.56
DE  Interaction: O76041; IntAct: EBI-25874883; Score: 0.56
DE  Interaction: Q9HC96; IntAct: EBI-25874891; Score: 0.56
DE  Interaction: Q8TBE0; IntAct: EBI-25874899; Score: 0.56
DE  Interaction: Q8WW38; IntAct: EBI-25874915; Score: 0.56
DE  Interaction: Q8N488; IntAct: EBI-25874923; Score: 0.56
DE  Interaction: O75886; IntAct: EBI-25874859; Score: 0.56
DE  Interaction: Q14585; IntAct: EBI-25874939; Score: 0.56
DE  Interaction: Q6X4W1; IntAct: EBI-25874947; Score: 0.56
DE  Interaction: Q9ULD4; IntAct: EBI-25874955; Score: 0.56
DE  Interaction: Q04323; IntAct: EBI-25874963; Score: 0.56
DE  Interaction: Q8WXF7; IntAct: EBI-25874971; Score: 0.56
DE  Interaction: Q8WVD3; IntAct: EBI-25874979; Score: 0.56
DE  Interaction: P58499; IntAct: EBI-25874987; Score: 0.56
DE  Interaction: Q9HBE1; IntAct: EBI-25874931; Score: 0.56
DE  Interaction: Q96EL1; IntAct: EBI-25875231; Score: 0.56
DE  Interaction: P10073; IntAct: EBI-25875215; Score: 0.56
DE  Interaction: Q6ZNE9; IntAct: EBI-25875205; Score: 0.56
DE  Interaction: Q3SX64; IntAct: EBI-25875197; Score: 0.56
DE  Interaction: Q7Z698; IntAct: EBI-25875189; Score: 0.56
DE  Interaction: Q8IZU1; IntAct: EBI-25875181; Score: 0.56
DE  Interaction: Q6ZNH5; IntAct: EBI-25875173; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25875165; Score: 0.56
DE  Interaction: Q70EL1; IntAct: EBI-25875157; Score: 0.56
DE  Interaction: Q8NA54; IntAct: EBI-25875149; Score: 0.56
DE  Interaction: Q96LX8; IntAct: EBI-25875141; Score: 0.56
DE  Interaction: Q86WT6; IntAct: EBI-25875133; Score: 0.56
DE  Interaction: Q96DX5; IntAct: EBI-25875125; Score: 0.56
DE  Interaction: Q7Z3I7; IntAct: EBI-25875117; Score: 0.56
DE  Interaction: Q96MN9; IntAct: EBI-25875109; Score: 0.56
DE  Interaction: Q8TCX5; IntAct: EBI-25875101; Score: 0.56
DE  Interaction: Q6H8Q1; IntAct: EBI-25875093; Score: 0.56
DE  Interaction: Q3B820; IntAct: EBI-25875083; Score: 0.56
DE  Interaction: Q9C0F3; IntAct: EBI-25875075; Score: 0.56
DE  Interaction: Q9GZS3; IntAct: EBI-25875067; Score: 0.56
DE  Interaction: Q6ZN57; IntAct: EBI-25875059; Score: 0.56
DE  Interaction: Q96KP6; IntAct: EBI-25875051; Score: 0.56
DE  Interaction: Q5VYS8; IntAct: EBI-25875043; Score: 0.56
DE  Interaction: Q9BS31; IntAct: EBI-25875035; Score: 0.56
DE  Interaction: Q8NEA9; IntAct: EBI-25875027; Score: 0.56
DE  Interaction: Q8N0Y2; IntAct: EBI-25875019; Score: 0.56
DE  Interaction: Q8IYM2; IntAct: EBI-25875011; Score: 0.56
DE  Interaction: Q9BZ95; IntAct: EBI-25875003; Score: 0.56
DE  Interaction: Q9NWB1; IntAct: EBI-25874995; Score: 0.56
DE  Interaction: A6H8Z2; IntAct: EBI-25875239; Score: 0.56
DE  Interaction: Q09161; IntAct: EBI-26397353; Score: 0.35
DE  Interaction: Q6ZNK6; IntAct: EBI-26453464; Score: 0.35
DE  Interaction: Q0D2I5; IntAct: EBI-26498092; Score: 0.58
DE  Interaction: Q13426; IntAct: EBI-26498177; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.35
DE  Interaction: Q9H9E1; IntAct: EBI-26656693; Score: 0.35
DE  Interaction: O14593; IntAct: EBI-26656719; Score: 0.35
DE  Interaction: P06401; IntAct: EBI-26871710; Score: 0.35
DE  Interaction: A0A0H3NG92; IntAct: EBI-27055968; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q86V86; IntAct: EBI-28942203; Score: 0.35
DE  Interaction: Q8IWB6; IntAct: EBI-28942423; Score: 0.35
DE  Interaction: Q8TEA7; IntAct: EBI-28943849; Score: 0.35
DE  Interaction: Q9BVS4; IntAct: EBI-28944998; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: P40305; IntAct: EBI-27124576; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: Q86V87; IntAct: EBI-34575191; Score: 0.27
DE  Interaction: Q96ED9; IntAct: EBI-34575530; Score: 0.27
GO  GO:0005829;
GO  GO:0005882;
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0035861;
GO  GO:0042802;
GO  GO:0005200;
GO  GO:0005198;
GO  GO:0071456;
GO  GO:0090398;
GO  GO:1990683;
GO  GO:0030951;
GO  GO:0031507;
GO  GO:0007517;
GO  GO:1903243;
GO  GO:0008285;
GO  GO:2001237;
GO  GO:0072201;
GO  GO:0090201;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0010628;
GO  GO:1900114;
GO  GO:0006606;
GO  GO:0008104;
GO  GO:0090435;
GO  GO:0034504;
GO  GO:0030334;
GO  GO:1900180;
GO  GO:0031647;
GO  GO:0032204;
GO  GO:0055015;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8175923,};
SQ  METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAA
SQ  YEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEG
SQ  ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESR
SQ  LADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKL
SQ  RDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRG
SQ  RASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLT
SQ  YRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDD
SQ  LLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDN
SQ  LVTRSYLLGNSSPRTQSPQNCSIM
//
ID  P48678;
PN  Lamin-A/C;
GN  Lmna;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus {ECO:0000269|PubMed:26436652}. Nucleus envelope {ECO:0000250|UniProtKB:P02545}. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus matrix {ECO:0000250|UniProtKB:P02545}. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C (By similarity). {ECO:0000250}.
DR  UNIPROT: P48678;
DR  UNIPROT: B3RH23;
DR  UNIPROT: B3RH24;
DR  UNIPROT: P11516;
DR  UNIPROT: P97859;
DR  UNIPROT: Q3TIH0;
DR  UNIPROT: Q3TTS8;
DR  UNIPROT: Q3U733;
DR  UNIPROT: Q3U7I5;
DR  UNIPROT: Q3UCA0;
DR  UNIPROT: Q3UCJ8;
DR  UNIPROT: Q3UCU3;
DR  UNIPROT: Q91WF2;
DR  UNIPROT: Q9DC21;
DR  PDB: 1UFG;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (By similarity). Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Required for cardiac homeostasis (PubMed:26436652). Isoform C2 may have a role in determining the organization of nuclear and chromosomal structures during spermatogenesis. {ECO:0000250|UniProtKB:P02545, ECO:0000269|PubMed:10579712, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:19124654, ECO:0000269|PubMed:21547077, ECO:0000269|PubMed:21982926, ECO:0000269|PubMed:23535822, ECO:0000269|PubMed:26436652}. Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: A2A8U2; IntAct: EBI-12591514; Score: 0.40
DE  Interaction: P16054; IntAct: EBI-299155; Score: 0.35
DE  Interaction: P20700; IntAct: EBI-11044755; Score: 0.35
DE  Interaction: Q08460; IntAct: EBI-2024267; Score: 0.35
DE  Interaction: P31750; IntAct: EBI-7881525; Score: 0.56
DE  Interaction: Q5FW52; IntAct: EBI-3895570; Score: 0.49
DE  Interaction: A2AM57; IntAct: EBI-4282630; Score: 0.35
DE  Interaction: Q9QY53; IntAct: EBI-4281129; Score: 0.35
DE  Interaction: P27661; IntAct: EBI-9699747; Score: 0.27
DE  Interaction: P15924; IntAct: EBI-11044755; Score: 0.35
DE  Interaction: Q5QNY5; IntAct: EBI-11044755; Score: 0.35
DE  Interaction: P25685; IntAct: EBI-11044755; Score: 0.35
DE  Interaction: P13995; IntAct: EBI-11044755; Score: 0.35
DE  Interaction: O94927; IntAct: EBI-11044755; Score: 0.35
DE  Interaction: Q03252; IntAct: EBI-11044755; Score: 0.35
DE  Interaction: O35963; IntAct: EBI-11566169; Score: 0.35
DE  Interaction: Q9R1S0; IntAct: EBI-11784907; Score: 0.35
DE  Interaction: Q8BJS4; IntAct: EBI-12591503; Score: 0.35
DE  Interaction: Q9D2G2; IntAct: EBI-20313723; Score: 0.35
DE  Interaction: P35486; IntAct: EBI-20313969; Score: 0.35
DE  Interaction: Q8K2B3; IntAct: EBI-20314053; Score: 0.35
DE  Interaction: P08228; IntAct: EBI-20314123; Score: 0.35
DE  Interaction: P51637; IntAct: EBI-20565496; Score: 0.35
DE  Interaction: A2AKD7; IntAct: EBI-20566393; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0035861;
GO  GO:0042802;
GO  GO:0008157;
GO  GO:0005200;
GO  GO:0071456;
GO  GO:0090398;
GO  GO:1990683;
GO  GO:0030010;
GO  GO:0030951;
GO  GO:0031507;
GO  GO:0007517;
GO  GO:1904178;
GO  GO:1903243;
GO  GO:0008285;
GO  GO:2001237;
GO  GO:0072201;
GO  GO:0090201;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0006997;
GO  GO:0010628;
GO  GO:1900114;
GO  GO:0045669;
GO  GO:0006606;
GO  GO:0008104;
GO  GO:0090435;
GO  GO:0034504;
GO  GO:0030334;
GO  GO:1900180;
GO  GO:0031647;
GO  GO:0032204;
GO  GO:0055015;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAA
SQ  YEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEG
SQ  ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESR
SQ  LADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKL
SQ  RDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRG
SQ  RASSHSSQSQGGGSVTKKRKLESSESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIRRQNGDDPLMT
SQ  YRFPPKFTLKAGQVVTIWASGAGATHSPPTDLVWKAQNTWGCGSSLRTALINSTGEEVAMRKLVRSLTMVEDNEDDDEDG
SQ  EELLHHHRGSHCSGSGDPAEYNLRSRTVLCGTCGQPADKAAGGAGAQVGGSISSGSSASSVTVTRSFRSVGGSGGGSFGD
SQ  NLVTRSYLLGNSSPRSQSSQNCSIM
//
ID  Q3ZD69;
PN  Lamin-A/C;
GN  LMNA;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P02545}. Nucleus envelope {ECO:0000250|UniProtKB:P02545}. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus matrix {ECO:0000250|UniProtKB:P02545}. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C (By similarity). {ECO:0000250}.
DR  UNIPROT: Q3ZD69;
DR  UNIPROT: Q3ZD68;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (By similarity). Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Required for cardiac homeostasis. {ECO:0000250|UniProtKB:P02545, ECO:0000250|UniProtKB:P48678}. Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005882;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0035861;
GO  GO:0005200;
GO  GO:0090398;
GO  GO:1990683;
GO  GO:0031507;
GO  GO:1903243;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0090435;
GO  GO:0034504;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKSA
SQ  YEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLMAAQARLKDLEALLNSKEAALSTALSEKRTLEG
SQ  ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESR
SQ  LADALQDLRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKL
SQ  RDLEDSLARERDTSRRLLADKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRG
SQ  RASSHSSQTQSGGSVTKKRKLESSESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLT
SQ  YRFPPKFTLKAGQVVTIWAAGAGATHSPPADLVWKSQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTMIEDDEDEDGDD
SQ  LLHHHHGSHGSSSGDPAEYNLRSRTVLCGTCGQPADKASASSSGAQVGGSISSGSSASSVTVTRSYRSVGGSGGGSFGDN
SQ  LVTRSYLLGNSRPRTQSPQNCSIM
//
ID  P48679;
PN  Lamin-A/C;
GN  Lmna;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P02545}. Nucleus envelope {ECO:0000250|UniProtKB:P02545}. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus matrix {ECO:0000250|UniProtKB:P02545}. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C (By similarity). Phosphorylation status of S-22 determines its localization between double-strand break (DSB) sites and the nuclear matrix (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P02545}.
DR  UNIPROT: P48679;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (By similarity). Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Required for cardiac homeostasis. {ECO:0000250|UniProtKB:P02545, ECO:0000250|UniProtKB:P48678}. Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P16599; IntAct: EBI-1374179; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26438079; Score: 0.35
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0035861;
GO  GO:0008157;
GO  GO:0005200;
GO  GO:0071456;
GO  GO:0090398;
GO  GO:1990683;
GO  GO:0030951;
GO  GO:0031507;
GO  GO:0007517;
GO  GO:1904178;
GO  GO:1903243;
GO  GO:0008285;
GO  GO:2001237;
GO  GO:0072201;
GO  GO:0090201;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0006997;
GO  GO:0010628;
GO  GO:1900114;
GO  GO:0045669;
GO  GO:0006606;
GO  GO:0090435;
GO  GO:0034504;
GO  GO:0030334;
GO  GO:1900180;
GO  GO:0031647;
GO  GO:0032204;
GO  GO:0009612;
GO  GO:0007283;
GO  GO:0055015;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  METPSQRRPTRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAA
SQ  YEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEG
SQ  ELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESR
SQ  LADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKL
SQ  RDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRG
SQ  RASSHSSQSQGGGSVTKKRKLESSESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLMT
SQ  YRFPPKFTLKAGQVVTIWASGAGATHSPPTDLVWKAQNTWGCGTSLRTALINATGEEVAMRKLVRSLTMVEDNDDEEEDG
SQ  DELLHHHRGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKAASGSGAQVGGSISSGSSASSVTVTRSFRSVGGSGGGSFGD
SQ  NLVTRSYLLGNSSPRTQSSQNCSIM
//
ID  P11048;
PN  Lamin-A;
GN  lmna;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus. Nucleus envelope {ECO:0000269|PubMed:25157132}.
DR  UNIPROT: P11048;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
DE  Reference Proteome: Yes;
GO  GO:0005882;
GO  GO:0005635;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  METPGQKRATRSTHTPLSPTRITRLQEKEDLQGLNDRLAVYIDKVRSLELENARLRLRITESEDVISREVTGIKSAYETE
SQ  LADARKTLDSVAKERARLQLELSKIREEHKELKARNAKKESDLLTAQARLKDLEALLNSKDAALTTALGEKRNLENEIRE
SQ  LKAHIAKLEASLADTKKQLQDEMLRRVDTENRNQTLKEELEFQKSIYNEEMRETKRRHETRLVEVDNGRQREFESKLADA
SQ  LHELRAQHEGQIGLYKEELGKTYNAKLENAKQSAERNSSLVGEAQEEIQQSRIRIDSLSAQLSQLQKQLAAREAKLRDLE
SQ  DAYARERDSSRRLLADKDREMAEMRARMQQQLDEYQELLDIKLALDMEINAYRKLLEGEEERLRLSPSPNTQKRSARTIA
SQ  SHSGAHISSSASKRRRLEEGESRSSSFTQHARTTGKVSVEEVDPEGKYVRLRNKSNEDQSLGNWQIKRQIGDETPIVYKF
SQ  PPRLTLKAGQTVTIWASGAGATNSPPSDLVWKAQSSWGTGDSIRTALLTSSNEEVAMRKLVRTVVINDEDDEDNDDMEHH
SQ  HHHHHHHHDGQNSSGDPGEYNLRSRTIVCTSCGRPAEKSVLASQGSGLVTGSSGSSSSSVTLTRTYRSTGGTSGGSGLGE
SQ  SPVTRNFIVGNGQRAQVAPQNCSIM
//
ID  P14731;
PN  Lamin-B1;
GN  LMNB1;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus lamina {ECO:0000250|UniProtKB:P20700}.
DR  UNIPROT: P14731;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. {ECO:0000250|UniProtKB:P20700}.
DE  Reference Proteome: Yes;
GO  GO:0005882;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0005200;
GO  GO:0031507;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0090435;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAAAVAPLSPQPRGAAASAALSPTRISRLQEKEELRQLNDRLAVYIDKVRSLETENSALQRRVSEREQVCGREISGLKEL
SQ  FETELADARKTLDDTARERAKLQIELGKLRAEHEQVLSSYAKKDSDLNAAQVKLREFEAALNAKEAALATALGDKRSQEE
SQ  ELEDLRDQIAQLEVSLAAAKKELADETLQKVDLENRCQSLIEDLEFRKNVYEEEIKETRRKHETRLVEVDSGRQIEYEYK
SQ  LAQALKEIREQHDAQVKLYKEELEQTYSSKLENIRQSSEMHSCTANTVREELHESRMRIETLSSHIADIQKESRAWQDRV
SQ  HELEDTLSKERENYRKILAENEREVAEMRNQMQQQFSDYEQLLDVKLALDMEISAYRKLLESEEERLRLSPGPSSRVTVS
SQ  RASSSRSVRTTRGKRKRIDVEESEASSSVSISHSASATGNISIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSAS
SQ  YRYTSRYVLKAGQTVTIWAANAGVTASPPTDLIWKNQNSWGTGEDVKVVLKNSQGEEVAQRSTVFKTTVNEGEEEEEEGE
SQ  EEILEDVIHQQGSPRKPERSCVVM
//
ID  Q54HI5;
PN  Lamin-like protein;
GN  lmnB;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:19466752}. Nucleus inner membrane {ECO:0000269|PubMed:22090348}.
DR  UNIPROT: Q54HI5;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane. Helps to maintain integrity of nuclear structures in response to mechanical stress. {ECO:0000269|PubMed:22090348}.
DE  Reference Proteome: Yes;
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005652;
GO  GO:0030527;
GO  GO:0007098;
GO  GO:0051642;
GO  GO:0010847;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDMSKKKSKRASPIESSQEEIAISTSKTATTEKPKKTKTTTKKKASQPSQEVVMETESEVEITTTTTSTSTTNNNNITTT
SQ  STSSQQSNGTLSSSSSPTIQSIPTTPISKYIPSLSQIGTPLSPNRAAQRLREKDELSLIHNRLKSALKKLESAETELEKK
SQ  NQEYEELDQKHTATIKQLKQRSDQVEKQLIEEQNQNSDLTSNRNILENELKSKESVWKKEKDEILLKFQESINKLNQENS
SQ  LAQSQLKSEIVSKEYEIDGLKSEINRLKDDLQYRIREGEEKSRKLLENEYNRFKGKEEEYNQLIVSKDEEIKKYKFELKE
SQ  KEKSSNAMNKKENELNNLIQAHERQIEDMRDSINREWELKAAQMMEEHHARTIHLQQAVDSFNEEKERIKSQMETLNGQI
SQ  EDINIKNNEYEDRIKEMNVLLSQKDNSIGELGVEIEESKKKMRKQMADLKSKDGQIALLQIEINTKDNKCNTLQTETNRL
SQ  KSELYSITNQIDPEIPLDPEINSLKELVKGFEKTVDDRKRKRSKLQHEFNAAANQDQNGMTIEEQSSTSTTTTTSATGSS
SQ  SSTSHLDNIDSSKLPTGPEQSELFNPDTVSFSLVDSNQEFIKLSVHGDMDNGLSISKWRLIVVKPDGSKSGFSFPDGIQP
SQ  FKGIKSVTVWTGRPRPQGTPTENEFYWARTELWTSPVEGTIVKLVSPSEETTTVTLPADGIYQKPSSAGKSNCLIM
//
ID  P20700;
PN  Lamin-B1;
GN  LMNB1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus lamina {ECO:0000269|PubMed:28716252, ECO:0000269|PubMed:32910914}.
DR  UNIPROT: P20700;
DR  UNIPROT: B2R6J6;
DR  UNIPROT: Q3SYN7;
DR  UNIPROT: Q96EI6;
DR  PDB: 2KPW;
DR  PDB: 3JT0;
DR  PDB: 3TYY;
DR  PDB: 3UMN;
DR  PDB: 5VVX;
DR  PDB: 7DTG;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DR  OMIM: 150340;
DR  OMIM: 169500;
DR  OMIM: 619179;
DR  DisGeNET: 4001;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. {ECO:0000269|PubMed:28716252, ECO:0000269|PubMed:32910914}.
DE  Disease: Leukodystrophy, demyelinating, autosomal dominant, adult-onset (ADLD) [MIM:169500]: A slowly progressive and fatal demyelinating leukodystrophy, presenting in the fourth or fifth decade of life. Clinically characterized by early autonomic abnormalities, pyramidal and cerebellar dysfunction, and symmetric demyelination of the CNS. It differs from multiple sclerosis and other demyelinating disorders in that neuropathology shows preservation of oligodendroglia in the presence of subtotal demyelination and lack of astrogliosis. {ECO:0000269|PubMed:16951681, ECO:0000269|PubMed:28716252, ECO:0000269|PubMed:32910914}. Note=The disease is caused by variants affecting the gene represented in this entry. Microcephaly 26, primary, autosomal dominant (MCPH26) [MIM:619179]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH26 is an autosomal dominant, progressive form apparent at birth or in early infancy. It is associated with relative short stature, variable severity of intellectual disability, and neurological features as the core symptoms. Brain imaging shows a simplified gyral pattern of the cortex and abnormal corpus callosum in some patients. {ECO:0000269|PubMed:32910914, ECO:0000269|PubMed:33033404}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95295; IntAct: EBI-24720012; Score: 0.56
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-3931729; Score: 0.85
DE  Interaction: O00442; IntAct: EBI-1074462; Score: 0.00
DE  Interaction: O75815; IntAct: EBI-1076745; Score: 0.00
DE  Interaction: O94817; IntAct: EBI-1078202; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1080502; Score: 0.00
DE  Interaction: P63104; IntAct: EBI-7193843; Score: 0.40
DE  Interaction: Q9Z0E3; IntAct: EBI-2549710; Score: 0.35
DE  Interaction: O43918; IntAct: EBI-2571569; Score: 0.40
DE  Interaction: O95229; IntAct: EBI-2554675; Score: 0.40
DE  Interaction: Q62388; IntAct: EBI-2561739; Score: 0.40
DE  Interaction: P03208; IntAct: EBI-2622779; Score: 0.37
DE  Interaction: Q8N0X7; IntAct: EBI-2643801; Score: 0.35
DE  Interaction: Q5NID1; IntAct: EBI-2797339; Score: 0.00
DE  Interaction: Q5NGF6; IntAct: EBI-2805221; Score: 0.00
DE  Interaction: Q5NFX8; IntAct: EBI-2805214; Score: 0.00
DE  Interaction: A0A6L8P0F0; IntAct: EBI-2830445; Score: 0.00
DE  Interaction: A0A0F7RE19; IntAct: EBI-2830438; Score: 0.00
DE  Interaction: Q96RG2; IntAct: EBI-8614760; Score: 0.44
DE  Interaction: O75928; IntAct: EBI-8635777; Score: 0.37
DE  Interaction: P01011; IntAct: EBI-3904297; Score: 0.37
DE  Interaction: P18848; IntAct: EBI-3905626; Score: 0.37
DE  Interaction: Q14161; IntAct: EBI-3911123; Score: 0.37
DE  Interaction: Q9NS73; IntAct: EBI-3919112; Score: 0.37
DE  Interaction: Q9H221; IntAct: EBI-3919122; Score: 0.37
DE  Interaction: P20700; IntAct: EBI-7660681; Score: 0.44
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6515052; Score: 0.62
DE  Interaction: P33993; IntAct: EBI-6875195; Score: 0.35
DE  Interaction: P25490; IntAct: EBI-6921458; Score: 0.35
DE  Interaction: Q14781; IntAct: EBI-8831509; Score: 0.35
DE  Interaction: Q8NDX5; IntAct: EBI-8834623; Score: 0.35
DE  Interaction: Q9WMX2; IntAct: EBI-9081801; Score: 0.37
DE  Interaction: Q13418; IntAct: EBI-10103376; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-11322719; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q8IYM1; IntAct: EBI-10820442; Score: 0.43
DE  Interaction: P48678; IntAct: EBI-11044755; Score: 0.35
DE  Interaction: P57716; IntAct: EBI-11047104; Score: 0.35
DE  Interaction: P42167; IntAct: EBI-11061883; Score: 0.35
DE  Interaction: Q9Z2X1; IntAct: EBI-11066678; Score: 0.35
DE  Interaction: P52294; IntAct: EBI-11101301; Score: 0.67
DE  Interaction: P48681; IntAct: EBI-11119785; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-11155257; Score: 0.35
DE  Interaction: O96017; IntAct: EBI-11579031; Score: 0.35
DE  Interaction: Q05BL1; IntAct: EBI-24309992; Score: 0.56
DE  Interaction: Q03252; IntAct: EBI-24353827; Score: 0.75
DE  Interaction: Q8TC57; IntAct: EBI-24673547; Score: 0.56
DE  Interaction: Q7KZS0; IntAct: EBI-24764330; Score: 0.56
DE  Interaction: Q9NPF5; IntAct: EBI-24769028; Score: 0.56
DE  Interaction: Q96KQ4; IntAct: EBI-24381926; Score: 0.56
DE  Interaction: A6NC98; IntAct: EBI-24395535; Score: 0.56
DE  Interaction: Q9H3R5; IntAct: EBI-24404669; Score: 0.56
DE  Interaction: Q9Y6X4; IntAct: EBI-24534698; Score: 0.56
DE  Interaction: O60684; IntAct: EBI-24538749; Score: 0.56
DE  Interaction: O15131; IntAct: EBI-24569702; Score: 0.56
DE  Interaction: Q8WWB5; IntAct: EBI-24591506; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q05322; IntAct: EBI-15481401; Score: 0.50
DE  Interaction: P04899; IntAct: EBI-21767972; Score: 0.35
DE  Interaction: Q9UID3; IntAct: EBI-16150241; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-16183096; Score: 0.68
DE  Interaction: Q9BXW4; IntAct: EBI-16183136; Score: 0.44
DE  Interaction: Q9H492; IntAct: EBI-16183296; Score: 0.44
DE  Interaction: O95166; IntAct: EBI-16183467; Score: 0.44
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-20306992; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-20307902; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-20623276; Score: 0.35
DE  Interaction: O00160; IntAct: EBI-20915992; Score: 0.40
DE  Interaction: Q5TID7; IntAct: EBI-20918404; Score: 0.40
DE  Interaction: P18433; IntAct: EBI-20918972; Score: 0.40
DE  Interaction: O95863; IntAct: EBI-20920860; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.53
DE  Interaction: Q16526; IntAct: EBI-21981854; Score: 0.35
DE  Interaction: P36956; IntAct: EBI-22057635; Score: 0.49
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC5; IntAct: EBI-26495256; Score: 0.35
DE  Interaction: Q8TB24; IntAct: EBI-26518569; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NG92; IntAct: EBI-27055968; Score: 0.27
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
GO  GO:0005638;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043274;
GO  GO:1990837;
GO  GO:0005200;
GO  GO:0005198;
GO  GO:0031507;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0090435;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:2684976};
SQ  MATATPVPPRMGSRAGGPTTPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKA
SQ  LYETELADARRALDDTARERAKLQIELGKCKAEHDQLLLNYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLE
SQ  GDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEY
SQ  KLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLER
SQ  IQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTV
SQ  SRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSV
SQ  SYKYTSRYVLKAGQTVTIWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEEA
SQ  AGVVVEEELFHQQGTPRASNRSCAIM
//
ID  P14733;
PN  Lamin-B1;
GN  Lmnb1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus lamina {ECO:0000250|UniProtKB:P20700}.
DR  UNIPROT: P14733;
DR  UNIPROT: Q61791;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. {ECO:0000250|UniProtKB:P20700}.
DE  Reference Proteome: Yes;
DE  Interaction: A3KGF7; IntAct: EBI-688106; Score: 0.37
DE  Interaction: P03096; IntAct: EBI-7785954; Score: 0.27
DE  Interaction: P12908; IntAct: EBI-7786038; Score: 0.27
DE  Interaction: Q9Z0E3; IntAct: EBI-2549816; Score: 0.35
DE  Interaction: P49452; IntAct: EBI-8573213; Score: 0.35
DE  Interaction: Q6AXH7; IntAct: EBI-6876709; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
DE  Interaction: Q80YT7; IntAct: EBI-16732484; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
DE  Interaction: Q9D2G2; IntAct: EBI-20313723; Score: 0.35
DE  Interaction: Q8K2B3; IntAct: EBI-20314053; Score: 0.35
DE  Interaction: Q60932; IntAct: EBI-20314167; Score: 0.35
DE  Interaction: P08228; IntAct: EBI-20314123; Score: 0.35
DE  Interaction: Q01815; IntAct: EBI-20565155; Score: 0.35
DE  Interaction: A2AKD7; IntAct: EBI-20566393; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
GO  GO:0005737;
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003690;
GO  GO:0008432;
GO  GO:0043274;
GO  GO:1990837;
GO  GO:0005200;
GO  GO:1904609;
GO  GO:0031507;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0010971;
GO  GO:0046330;
GO  GO:0090435;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MATATPVQQQRAGSRASAPATPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLK
SQ  ALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSL
SQ  EGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYE
SQ  YKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLE
SQ  RIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVT
SQ  VSRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTS
SQ  VSYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVILKNSQGEEVAQRSTVFKTTIPEEEEEEEE
SQ  EPIGVAVEEERFHQQGAPRASNKSCAIM
//
ID  P70615;
PN  Lamin-B1;
GN  Lmnb1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus lamina {ECO:0000250|UniProtKB:P20700}.
DR  UNIPROT: P70615;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. {ECO:0000250|UniProtKB:P20700}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5XIE8; IntAct: EBI-26438079; Score: 0.35
GO  GO:0005737;
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003690;
GO  GO:0043274;
GO  GO:1990837;
GO  GO:0005200;
GO  GO:0006915;
GO  GO:0071386;
GO  GO:1904609;
GO  GO:0071407;
GO  GO:0031507;
GO  GO:0022008;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0090435;
GO  GO:0046677;
GO  GO:0009410;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MATATPVQQRAGSRASAPATPFSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKA
SQ  LYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLE
SQ  GDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEY
SQ  KLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSARGGMMESRMRIESLSSQLSNLQKDSRACLER
SQ  IQELEDMLAKERDNSRRMLSDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTV
SQ  SRASSSRSVRTTRGKRKRVDVEESEASSSVSISHSASATGNVCIEEIDVDGKFIRLKNTSEQDQPMGGWEMIRKIGDTSV
SQ  SYKYTSRYVLKAGQTVTVWAANAGVTASPPTDLIWKNQNSWGTGEDVKVVLKNSQGEEVAQRSTVFKTTIPEEEEEEEEE
SQ  PIGVPLEEERFHQQGTPRASNKSCAIM
//
ID  P14732;
PN  Lamin-B2;
GN  LMNB2;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus lamina {ECO:0000250|UniProtKB:Q03252}.
DR  UNIPROT: P14732;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. {ECO:0000250|UniProtKB:Q03252}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8AYS8; IntAct: EBI-3059009; Score: 0.35
GO  GO:0005882;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0005200;
GO  GO:0031507;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0090435;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSGTPIRGTPGGTPLSPTRISRLQEKEELRQLNDRLAVYIDRVRALELENDRLLVKISEKEEVTTREVSGIKNLYESELA
SQ  DARRVLDETAKERARLQIEIGKLRAELEEFNKSYKKKDADLSVAQGRIKDLEVLFHRSEAELNTVLNEKRSLEAEVADLR
SQ  AQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEDLDFRKNVFEEEIRETRKRHEHRLVEVDTSRQQEYENKMAQALE
SQ  DLRNQHDEQVKLYKMELEQTYQAKLENAILASDQNDKAAGAAREELKEARMRIESLSHQLSGLQKQASATEDRIRELKET
SQ  MAGERDKFRKMLDAKEREMTEMRDQMQLQLTEYQELLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSRVTVSRATSSS
SQ  SSSSTSLVRSSRGKRRRIEAEELSGSGTSGIGTGSISGSSSSSSFQMSQQASATGSISIEEIDLEGKYVQLKNNSEKDQS
SQ  LGNWRLKRQIGDGEEIAYKFTPKYVLRAGQTVTIWGADAGVSHSPPSVLVWKNQGSWGTGGNIRTYLVNSDGEEVAVRTV
SQ  TKSVVVRENEEEEDEADFGEEDLFNQQGDPRTTSRGCLVM
//
ID  Q03252;
PN  Lamin-B2;
GN  LMNB2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus lamina {ECO:0000305|PubMed:33033404}.
DR  UNIPROT: Q03252;
DR  UNIPROT: O75292;
DR  UNIPROT: Q14734;
DR  UNIPROT: Q96DF6;
DR  PDB: 2LLL;
DR  PDB: 5BNW;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DR  OMIM: 150341;
DR  OMIM: 608709;
DR  OMIM: 616540;
DR  OMIM: 619180;
DR  DisGeNET: 84823;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. {ECO:0000269|PubMed:33033404}.
DE  Disease: Partial acquired lipodystrophy (APLD) [MIM:608709]: A rare childhood disease characterized by loss of subcutaneous fat from the face and trunk. Fat deposition on the pelvic girdle and lower limbs is normal or excessive. Most frequently, onset between 5 and 15 years of age. Most affected subjects are females and some show no other abnormality, but many develop glomerulonephritis, diabetes mellitus, hyperlipidemia, and complement deficiency. Intellectual disability in some cases. APLD is a sporadic disorder of unknown etiology. {ECO:0000269|PubMed:16826530, ECO:0000269|PubMed:22768673}. Note=The disease is caused by variants affecting the gene represented in this entry. Epilepsy, progressive myoclonic 9 (EPM9) [MIM:616540]: A form of progressive myoclonic epilepsy, a clinically and genetically heterogeneous group of disorders defined by the combination of action and reflex myoclonus, other types of epileptic seizures, and progressive neurodegeneration and neurocognitive impairment. EPM9 is an autosomal recessive form characterized by myoclonus, tonic-clonic seizures, ataxia, and delayed psychomotor development. {ECO:0000269|PubMed:25954030}. Note=The disease may be caused by variants affecting the gene represented in this entry. Microcephaly 27, primary, autosomal dominant (MCPH27) [MIM:619180]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH27 is an autosomal dominant form apparent in early childhood and associated with global developmental delay, delayed walking, inability to walk, impaired intellectual development, and poor or absent speech. Brain imaging may show enlarged ventricles or gyral abnormalities in some patients. {ECO:0000269|PubMed:33033404}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O75604; IntAct: EBI-24339221; Score: 0.56
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.71
DE  Interaction: P20700; IntAct: EBI-24353827; Score: 0.75
DE  Interaction: P48678; IntAct: EBI-11044755; Score: 0.35
DE  Interaction: O46385; IntAct: EBI-7872590; Score: 0.37
DE  Interaction: Q81VE0; IntAct: EBI-2830424; Score: 0.00
DE  Interaction: Q8ZIY9; IntAct: EBI-2846832; Score: 0.00
DE  Interaction: Q5S007; IntAct: EBI-6515504; Score: 0.56
DE  Interaction: P33993; IntAct: EBI-6875195; Score: 0.35
DE  Interaction: P25490; IntAct: EBI-6921458; Score: 0.35
DE  Interaction: Q8NDX5; IntAct: EBI-8834623; Score: 0.35
DE  Interaction: P55318; IntAct: EBI-11317309; Score: 0.35
DE  Interaction: Q12952; IntAct: EBI-11318689; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q8WVC0; IntAct: EBI-11014006; Score: 0.35
DE  Interaction: Q7LBC6; IntAct: EBI-11060458; Score: 0.35
DE  Interaction: P23258; IntAct: EBI-11085623; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-24277630; Score: 0.56
DE  Interaction: Q96HB5; IntAct: EBI-24285109; Score: 0.56
DE  Interaction: Q9Y3C0; IntAct: EBI-24337647; Score: 0.56
DE  Interaction: A6NC98; IntAct: EBI-24341739; Score: 0.56
DE  Interaction: Q15911; IntAct: EBI-24344091; Score: 0.56
DE  Interaction: Q03252; IntAct: EBI-24344716; Score: 0.56
DE  Interaction: P35219; IntAct: EBI-24344911; Score: 0.56
DE  Interaction: P14373; IntAct: EBI-24345024; Score: 0.56
DE  Interaction: Q16543; IntAct: EBI-24353311; Score: 0.56
DE  Interaction: Q05BL1; IntAct: EBI-24363443; Score: 0.56
DE  Interaction: Q9UBB9; IntAct: EBI-25249646; Score: 0.56
DE  Interaction: Q9Y2J4; IntAct: EBI-24485359; Score: 0.56
DE  Interaction: A2BDD9; IntAct: EBI-24491013; Score: 0.56
DE  Interaction: Q3SY00; IntAct: EBI-24506638; Score: 0.56
DE  Interaction: Q9NVV9; IntAct: EBI-24375624; Score: 0.56
DE  Interaction: Q9Y250; IntAct: EBI-24393406; Score: 0.56
DE  Interaction: Q5JST6; IntAct: EBI-25260431; Score: 0.56
DE  Interaction: P55081; IntAct: EBI-25260706; Score: 0.56
DE  Interaction: Q4G0R1; IntAct: EBI-25263414; Score: 0.56
DE  Interaction: P78424; IntAct: EBI-24423801; Score: 0.56
DE  Interaction: Q9UJV3; IntAct: EBI-24456443; Score: 0.56
DE  Interaction: Q96KQ4; IntAct: EBI-24465907; Score: 0.56
DE  Interaction: P07954; IntAct: EBI-24586829; Score: 0.56
DE  Interaction: Q53FD0; IntAct: EBI-25190275; Score: 0.56
DE  Interaction: O14753; IntAct: EBI-25274406; Score: 0.56
DE  Interaction: P49356; IntAct: EBI-21502393; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-20306992; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-20307902; Score: 0.35
DE  Interaction: A0A380PHX5; IntAct: EBI-20818585; Score: 0.37
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: Q9H5J0; IntAct: EBI-20919428; Score: 0.40
DE  Interaction: Q96P66; IntAct: EBI-20926698; Score: 0.40
DE  Interaction: A8K8P3; IntAct: EBI-20930992; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P04156; IntAct: EBI-21014654; Score: 0.35
DE  Interaction: O43924; IntAct: EBI-21019227; Score: 0.35
DE  Interaction: P17813; IntAct: EBI-22197897; Score: 0.35
DE  Interaction: Q9H1R3; IntAct: EBI-25381841; Score: 0.35
DE  Interaction: Q8NF50; IntAct: EBI-25409278; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9H9E1; IntAct: EBI-26656693; Score: 0.35
DE  Interaction: O14593; IntAct: EBI-26656719; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-27084109; Score: 0.35
GO  GO:0005882;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0042802;
GO  GO:0005200;
GO  GO:0031507;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0090435;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSPPSPGRRREQRRPRAAATMATPLPGRAGGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLKISE
SQ  KEEVTTREVSGIKALYESELADARRVLDETARERARLQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSE
SQ  VELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELDFRKSVFEEEVRETRRRHERR
SQ  LVEVDSSRQQEYDFKMAQALEELRSQHDEQVRLYKLELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQ
SQ  LSGLQKQASAAEDRIRELEEAMAGERDKFRKMLDAKEQEMTEMRDVMQQQLAEYQELLDVKLALDMEINAYRKLLEGEEE
SQ  RLKLSPSPSSRVTVSRATSSSSGSLSATGRLGRSKRKRLEVEEPLGSGPSVLGTGTGGSGGFHLAQQASASGSVSIEEID
SQ  LEGKFVQLKNNSDKDQSLGNWRIKRQVLEGEEIAYKFTPKYILRAGQMVTVWAAGAGVAHSPPSTLVWKGQSSWGTGESF
SQ  RTVLVNADGEEVAMRTVKKSSVMRENENGEEEEEEAEFGEEDLFHQQGDPRTTSRGCYVM
//
ID  P21619;
PN  Lamin-B2;
GN  Lmnb2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus lamina {ECO:0000250|UniProtKB:Q03252}.
DR  UNIPROT: P21619;
DR  UNIPROT: P48680;
DR  UNIPROT: Q8CGB1;
DR  Pfam: PF00038;
DR  Pfam: PF00932;
DR  PROSITE: PS00226;
DR  PROSITE: PS51842;
DR  PROSITE: PS51841;
DE  Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. {ECO:0000250|UniProtKB:Q03252}.
DE  Reference Proteome: Yes;
DE  Interaction: Q80YT7; IntAct: EBI-16732484; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
DE  Interaction: P08228; IntAct: EBI-20314123; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
GO  GO:0005638;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0042802;
GO  GO:0005200;
GO  GO:0031507;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0051664;
GO  GO:0090435;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MASLPPHAGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLYESELAD
SQ  ARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRA
SQ  QLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALED
SQ  LRSQHDEQVRLYRVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHELEEAL
SQ  AGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDMEISAYRKLLEGEEERLKLSPSPSSRITISRATSSSS
SQ  SSSGVGMSVGQGRGKRRRLETEDTSGSPSRASRVSSGSRLAQQTVATGVVNIDEVDPEGRFVRLKNSSDKDQSLGNWRIK
SQ  RQVLEGEDIAYKFTPKYVLRAGQTVTVWAAGAGATHSPPSTLVWKSQTNWGPGESFRTALVSADGEEVAVKAAKHSSVQG
SQ  RENGEEEEEEEAEFGEEDLFHQQGDPRTTSRGCRLM
//
ID  Q1HVJ2;
PN  Latent membrane protein 2;
GN  LMP2;
OS  82830;
SL  Nucleus Position: SL-0382;
SL  Comments: [Isoform LMP2A]: Host cell membrane; Multi-pass membrane protein. Note=Isoform LMP2A is localized in plasma membrane lipid rafts. {ECO:0000250|UniProtKB:P13285}. [Isoform LMP2B]: Host endomembrane system; Multi- pass membrane protein. Host cytoplasm, host perinuclear region. Note=Isoform LMP2B localizes to perinuclear regions. {ECO:0000250|UniProtKB:P13285}.
DR  UNIPROT: Q1HVJ2;
DR  UNIPROT: Q1HVJ1;
DR  Pfam: PF07415;
DE  Function: Isoform LMP2A maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin-negative cells to colonize peripheral lymphoid organs (By similarity). {ECO:0000250}. Isoform LMP2B may be a negative regulator of isoform LMP2A. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033645;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0039648;
GO  GO:0039649;
GO  GO:0019042;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGSLEMVPMGAGPPSPGGDPDGDDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQ
SQ  DQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALS
SQ  LLLLAAVASSYAAAQRKLLTPVTVLTAVVTFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWR
SQ  RLTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAALLTLAAALALLASLILGTLN
SQ  LTTMFLLMLLWTLVVLLICSSCSSCPLSKILLARLFLYALALLLLASALIAGGSILQTNFKSLSSTEFIPNLFCMLLLIV
SQ  AGILFILAILTEWGSGNRTYGPVFMCLGGLLTMVAGAVWLTVMTNTLLSAWILTAGFLIFLIGFALFGVIRCCRYCCYYC
SQ  LTLESEERPPTPYRNTV
//
ID  P13285;
PN  Latent membrane protein 2;
GN  LMP2;
OS  10377;
SL  Nucleus Position: SL-0382;
SL  Comments: [Isoform LMP2A]: Host cell membrane {ECO:0000269|PubMed:11163230, ECO:0000269|PubMed:11961256}; Multi-pass membrane protein {ECO:0000269|PubMed:11163230, ECO:0000269|PubMed:11961256}. Note=Isoform LMP2A is localized in plasma membrane lipid rafts. {ECO:0000269|PubMed:11163230}. [Isoform LMP2B]: Host endomembrane system {ECO:0000269|PubMed:11961256}; Multi-pass membrane protein {ECO:0000269|PubMed:11961256}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:11961256}. Note=Isoform LMP2B localizes to perinuclear regions. {ECO:0000269|PubMed:11961256}.
DR  UNIPROT: P13285;
DR  UNIPROT: Q777H4;
DR  UNIPROT: Q8AZK9;
DR  PDB: 1UXS;
DR  PDB: 1UXW;
DR  PDB: 2JO9;
DR  PDB: 3BVN;
DR  PDB: 3REW;
DR  PDB: 5GRD;
DR  PDB: 5GSD;
DR  Pfam: PF07415;
DE  Function: Isoform LMP2A maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin-negative cells to colonize peripheral lymphoid organs. Isoform LMP2B may be a negative regulator of isoform LMP2A.
DE  Reference Proteome: Yes;
DE  Interaction: P0CK48; IntAct: EBI-9645790; Score: 0.37
DE  Interaction: Q96J02; IntAct: EBI-7181105; Score: 0.59
DE  Interaction: P08107; IntAct: EBI-8661700; Score: 0.35
DE  Interaction: P25939; IntAct: EBI-9645775; Score: 0.37
DE  Interaction: G3E2M5; IntAct: EBI-9645780; Score: 0.37
DE  Interaction: P03219; IntAct: EBI-9645785; Score: 0.37
DE  Interaction: M1FZY5; IntAct: EBI-9645805; Score: 0.37
DE  Interaction: Q1HVD3; IntAct: EBI-9645800; Score: 0.37
DE  Interaction: P03199; IntAct: EBI-9645795; Score: 0.37
DE  Interaction: Q3KSQ7; IntAct: EBI-9645814; Score: 0.37
DE  Interaction: Q9NZM1; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O60494; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O00308; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q9H0M0; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q9BQB6; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q16739; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q8TF42; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q8NBM4; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q5JTV8; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q9H0E2; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P37173; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O15260; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q9UQ35; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O15269; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O60493; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q9P0P0; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O95456; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q14997; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P61289; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q9UL46; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q06323; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P48556; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P51665; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q15008; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P55036; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O43242; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O00487; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q99460; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P62333; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P62195; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P43686; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P17980; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P35998; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P62191; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P28065; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P28062; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q99436; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P28072; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P28074; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P28070; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P49720; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P49721; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P20618; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O14818; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P60900; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P28066; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P25789; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P25788; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P25787; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P25786; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O60831; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: O15031; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q96PU5; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P46934; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q96N66; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q7Z4F1; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q15012; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q8TED1; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q14517; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q9GZU8; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q96CS3; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q9H5V8; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P16070; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q8NC54; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P98194; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q8IZ07; IntAct: EBI-11733017; Score: 0.35
GO  GO:0033645;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0039648;
GO  GO:0039649;
GO  GO:0019042;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGSLEMVPMGAGPPSPGGDPDGYDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQ
SQ  DQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALS
SQ  LLLLAAVASSYAAAQRKLLTPVTVLTAVVTFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWR
SQ  RLTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAALLTLAAALALLASLILGTLN
SQ  LTTMFLLMLLWTLVVLLICSSCSSCPLSKILLARLFLYALALLLLASALIAGGSILQTNFKSLSSTEFIPNLFCMLLLIV
SQ  AGILFILAILTEWGSGNRTYGPVFMCLGGLLTMVAGAVWLTVMSNTLLSAWILTAGFLIFLIGFALFGVIRCCRYCCYYC
SQ  LTLESEERPPTPYRNTV
//
ID  P0C729;
PN  Latent membrane protein 2;
GN  LMP2;
OS  10376;
SL  Nucleus Position: SL-0382;
SL  Comments: [Isoform LMP2A]: Host cell membrane; Multi-pass membrane protein. Note=Isoform LMP2A is localized in plasma membrane lipid rafts. {ECO:0000250|UniProtKB:P13285}. [Isoform LMP2B]: Host endomembrane system; Multi- pass membrane protein. Host cytoplasm, host perinuclear region. Note=Isoform LMP2B localizes to perinuclear regions. {ECO:0000250|UniProtKB:P13285}.
DR  UNIPROT: P0C729;
DR  Pfam: PF07415;
DE  Function: Isoform LMP2A maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin-negative cells to colonize peripheral lymphoid organs (By similarity). {ECO:0000250}. Isoform LMP2B may be a negative regulator of isoform LMP2A. {ECO:0000250}.
DE  Reference Proteome: No;
DE  Interaction: Q3KSS5; IntAct: EBI-2621223; Score: 0.00
DE  Interaction: Q08380; IntAct: EBI-2623752; Score: 0.37
GO  GO:0033645;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0039648;
GO  GO:0039649;
GO  GO:0019042;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGSLEMVPMGAGPPSPGGDPDGDDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQ
SQ  DQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALS
SQ  LLLLAAVASSYAAAQRKLLTPVTVLTAVVFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWRR
SQ  LTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAALLTLAAALALLASLILGTLNL
SQ  TTMFLLMLLWTLVVLLICSSCSSCPLTKILLARLFLYALALLLLASALIAGGSILQTNFKSLSSTEFIPNLFCMLLLIVA
SQ  GILFILAILTEWGSGNRTYGPVFMCLGGLLTMVAGAVWLTVMTNTLLSAWILTAGFLIFLIGFALFGVIRCCRYCCYYCL
SQ  TLESEERPPTPYRNTV
//
ID  Q6ZMQ8;
PN  Serine/threonine-protein kinase LMTK1;
GN  AATK;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:10837911}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10837911}. Note=Predominantly perinuclear.
DR  UNIPROT: Q6ZMQ8;
DR  UNIPROT: O75136;
DR  UNIPROT: Q6ZN31;
DR  UNIPROT: Q86X28;
DR  Pfam: PF07714;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  OMIM: 605276;
DR  DisGeNET: 9625;
DE  Function: May be involved in neuronal differentiation. {ECO:0000269|PubMed:10837911}.
DE  Reference Proteome: Yes;
DE  Interaction: O95248; IntAct: EBI-20980276; Score: 0.37
DE  Interaction: P04626; IntAct: EBI-25367655; Score: 0.37
DE  Interaction: P31689; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: P43034; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P61810; IntAct: EBI-2008524; Score: 0.40
DE  Interaction: Q06787; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q14203; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q15078; IntAct: EBI-2008413; Score: 0.59
DE  Interaction: Q15256; IntAct: EBI-20980062; Score: 0.37
DE  Interaction: Q15811; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q6ULP2; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q03114; IntAct: EBI-2008524; Score: 0.40
DE  Interaction: Q00535; IntAct: EBI-2008624; Score: 0.40
DE  Interaction: P62136; IntAct: EBI-5549776; Score: 0.67
DE  Interaction: P51571; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: Q9UJS0; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-10101253; Score: 0.66
DE  Interaction: Q15293; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-10101253; Score: 0.53
DE  Interaction: P04792; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: P68032; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: O75746; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: Q9H936; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: Q96EY1; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: P13674; IntAct: EBI-10101253; Score: 0.53
DE  Interaction: O60762; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: Q02978; IntAct: EBI-10101253; Score: 0.48
DE  Interaction: P53007; IntAct: EBI-10101253; Score: 0.35
DE  Interaction: Q96N21; IntAct: EBI-23805010; Score: 0.56
DE  Interaction: P30411; IntAct: EBI-20803497; Score: 0.37
DE  Interaction: P35236; IntAct: EBI-20980082; Score: 0.37
DE  Interaction: P16298; IntAct: EBI-20979982; Score: 0.37
DE  Interaction: Q08209; IntAct: EBI-20979972; Score: 0.37
DE  Interaction: P62140; IntAct: EBI-20979952; Score: 0.55
DE  Interaction: P35813; IntAct: EBI-20979992; Score: 0.37
DE  Interaction: P29350; IntAct: EBI-20980072; Score: 0.37
DE  Interaction: Q15750; IntAct: EBI-20980052; Score: 0.52
DE  Interaction: Q9H0C8; IntAct: EBI-20980042; Score: 0.37
DE  Interaction: Q96MI6; IntAct: EBI-20980032; Score: 0.37
DE  Interaction: Q8N3J5; IntAct: EBI-20980022; Score: 0.37
DE  Interaction: O75688; IntAct: EBI-20980002; Score: 0.37
DE  Interaction: P49593; IntAct: EBI-20980012; Score: 0.37
DE  Interaction: Q68J44; IntAct: EBI-20980172; Score: 0.37
DE  Interaction: Q06124; IntAct: EBI-20980092; Score: 0.37
DE  Interaction: Q16690; IntAct: EBI-20980132; Score: 0.37
DE  Interaction: Q05209; IntAct: EBI-20980102; Score: 0.37
DE  Interaction: Q99952; IntAct: EBI-20980112; Score: 0.37
DE  Interaction: Q99956; IntAct: EBI-20980152; Score: 0.37
DE  Interaction: Q16828; IntAct: EBI-20980142; Score: 0.37
DE  Interaction: P28562; IntAct: EBI-20980122; Score: 0.37
DE  Interaction: O95147; IntAct: EBI-20980162; Score: 0.37
DE  Interaction: Q6XPS3; IntAct: EBI-20980222; Score: 0.37
DE  Interaction: P60484; IntAct: EBI-20980212; Score: 0.37
DE  Interaction: A2A3K4; IntAct: EBI-20980202; Score: 0.37
DE  Interaction: Q9UNH5; IntAct: EBI-20980192; Score: 0.37
DE  Interaction: Q8WUJ0; IntAct: EBI-20980182; Score: 0.37
DE  Interaction: Q9NXD2; IntAct: EBI-20980316; Score: 0.37
DE  Interaction: Q96QG7; IntAct: EBI-20980306; Score: 0.37
DE  Interaction: Q9Y217; IntAct: EBI-20980286; Score: 0.37
DE  Interaction: Q96EF0; IntAct: EBI-20980296; Score: 0.37
DE  Interaction: O95677; IntAct: EBI-20980346; Score: 0.37
DE  Interaction: O00167; IntAct: EBI-20980336; Score: 0.37
DE  Interaction: P30305; IntAct: EBI-20980326; Score: 0.37
DE  Interaction: Q15326; IntAct: EBI-30825123; Score: 0.44
DE  Interaction: O95747; IntAct: EBI-30834562; Score: 0.57
DE  Interaction: P07900; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: Q9UKB1; IntAct: EBI-32718899; Score: 0.42
DE  Interaction: Q92598; IntAct: EBI-32718899; Score: 0.42
DE  Interaction: Q16543; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: Q9Y297; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: P35241; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: O95757; IntAct: EBI-32718899; Score: 0.42
DE  Interaction: Q00325; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: Q01813; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: Q709F0; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: Q86XK2; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: Q9UBX3; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: P04114; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: O00483; IntAct: EBI-32718899; Score: 0.42
DE  Interaction: Q9BSD7; IntAct: EBI-32718899; Score: 0.35
DE  Interaction: O15197; IntAct: EBI-32721423; Score: 0.27
DE  Interaction: O43615; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q8IXI1; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9UMZ2; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q6P1N0; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P50851; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P78527; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q14204; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P42566; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9BXF6; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q6WKZ4; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q7Z3T8; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9H0B6; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q8N8S7; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P63010; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q96B97; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P47897; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q15435; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O95782; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9UJW0; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q658Y4; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q641Q2; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q12972; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: A5YKK6; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q15643; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P38606; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q13643; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O76021; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q8N3F8; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q15046; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q3YEC7; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P05198; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O60264; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P62495; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9NZM3; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q8NDI1; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P42025; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9P260; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P41236; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q12768; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q96Q05; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q96SB3; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q2M389; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O60282; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q15276; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9UEW8; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9P2R3; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q10567; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q15311; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P50454; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9NZ32; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9BQ67; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P06493; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q8NFP9; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9NZ52; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q8NHV4; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P48553; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P18085; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P49023; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P26038; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P04637; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9UJC3; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O60927; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q92600; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9GZT9; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P16333; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q96CW1; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q8N1F7; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9Y4L1; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9H6R7; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P09543; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q15025; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q96PK6; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q08379; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q8IVF2; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9UIG0; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O43318; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q6ZS11; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P51116; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9UKD2; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9P2D6; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O75935; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9H2J4; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q96GQ7; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q96A65; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9NQC7; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q8IWJ2; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P61088; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9ULJ8; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P00491; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9H9A5; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q14689; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P82675; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9Y3P9; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P13667; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9Y3A5; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q8IUR0; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O00399; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P62158; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O60826; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q96A49; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q6GYQ0; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9H939; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9NVI1; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O00203; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9Y4W6; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q15058; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9Y296; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O75131; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: O94979; IntAct: EBI-32723474; Score: 0.27
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0004713;
GO  GO:0007420;
GO  GO:0038083;
GO  GO:0006468;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSSFFNPSFAFSSHFDPDGAPLSELSWPSSLAVVAVSFSGLFAVIVLMLACLCCKKGGIGFKEFENAEGDEYAADLAQG
SQ  SPATAAQNGPDVYVLPLTEVSLPMAKQPGRSVQLLKSTDVGRHSLLYLKEIGRGWFGKVFLGEVNSGISSAQVVVKELQA
SQ  SASVQEQMQFLEEVQPYRALKHSNLLQCLAQCAEVTPYLLVMEFCPLGDLKGYLRSCRVAESMAPDPRTLQRMACEVACG
SQ  VLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLAHCKYREDYFVTADQLWVPLRWIAPELVDEVHSNLLVVDQTKSGNV
SQ  WSLGVTIWELFELGTQPYPQHSDQQVLAYTVREQQLKLPKPQLQLTLSDRWYEVMQFCWLQPEQRPTAEEVHLLLSYLCA
SQ  KGATEAEEEFERRWRSLRPGGGGVGPGPGAAGPMLGGVVELAAASSFPLLEQFAGDGFHADGDDVLTVTETSRGLNFEYK
SQ  WEAGRGAEAFPATLSPGRTARLQELCAPDGAPPGVVPVLSAHSPSLGSEYFIRLEEAAPAAGHDPDCAGCAPSPPATADQ
SQ  DDDSDGSTAASLAMEPLLGHGPPVDVPWGRGDHYPRRSLARDPLCPSRSPSPSAGPLSLAEGGAEDADWGVAAFCPAFFE
SQ  DPLGTSPLGSSGAPPLPLTGEDELEEVGARRAAQRGHWRSNVSANNNSGSRCPESWDPVSAGGHAEGCPSPKQTPRASPE
SQ  PGYPGEPLLGLQAASAQEPGCCPGLPHLCSAQGLAPAPCLVTPSWTETASSGGDHPQAEPKLATEAEGTTGPRLPLPSVP
SQ  SPSQEGAPLPSEEASAPDAPDALPDSPTPATGGEVSAIKLASALNGSSSSPEVEAPSSEDEDTAEATSGIFTDTSSDGLQ
SQ  ARRPDVVPAFRSLQKQVGTPDSLDSLDIPSSASDGGYEVFSPSATGPSGGQPRALDSGYDTENYESPEFVLKEAQEGCEP
SQ  QAFAELASEGEGPGPETRLSTSLSGLNEKNPYRDSAYFSDLEAEAEATSGPEKKCGGDRAPGPELGLPSTGQPSEQVCLR
SQ  PGVSGEAQGSGPGEVLPPLLQLEGSSPEPSTCPSGLVPEPPEPQGPAKVRPGPSPSCSQFFLLTPVPLRSEGNSSEFQGP
SQ  PGLLSGPAPQKRMGGPGTPRAPLRLALPGLPAALEGRPEEEEEDSEDSDESDEELRCYSVQEPSEDSEEEAPAVPVVVAE
SQ  SQSARNLRSLLKMPSLLSETFCEDLERKKKAVSFFDDVTVYLFDQESPTRELGEPFPGAKESPPTFLRGSPGSPSAPNRP
SQ  QQADGSPNGSTAEEGGGFAWDDDFPLMTAKAAFAMALDPAAPAPAAPTPTPAPFSRFTVSPAPTSRFSITHVSDSDAESK
SQ  RGPEAGAGGESKEA
//
ID  Q80YE4;
PN  Serine/threonine-protein kinase LMTK1;
GN  Aatk;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000269|PubMed:17651901}; Single- pass type I membrane protein {ECO:0000269|PubMed:17651901}. Cytoplasm {ECO:0000269|PubMed:17651901}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, dendrite {ECO:0000269|PubMed:17651901}. Cell projection, axon {ECO:0000269|PubMed:17651901}. Cell projection, growth cone {ECO:0000269|PubMed:17651901}. Note=Predominantly perinuclear. {ECO:0000250}. [Isoform 2]: Membrane. Note=Peripheral membrane protein. [Isoform 3]: Membrane; Single-pass type I membrane protein.
DR  UNIPROT: Q80YE4;
DR  UNIPROT: A6BLY8;
DR  UNIPROT: O35211;
DR  UNIPROT: Q3U2U5;
DR  UNIPROT: Q3UHR8;
DR  UNIPROT: Q66JN3;
DR  UNIPROT: Q80YE3;
DR  UNIPROT: Q8CB63;
DR  UNIPROT: Q8CHE2;
DR  Pfam: PF07714;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: May be involved in neuronal differentiation. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Z1W9; IntAct: EBI-1768690; Score: 0.37
GO  GO:0030425;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0004713;
GO  GO:0006915;
GO  GO:0007420;
GO  GO:0051402;
GO  GO:0038083;
GO  GO:0006468;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSSFFNPSFAFSSHFDPDGAPLSELSWSSSLAVVAVSFSGIFTVVILMLACLCCKKGGIGFKEFENAEGDEYVADFSEQ
SQ  GSPAAAAQTGPDVYVLPLTEVSLPMAKQPGRSVQLLKSTDLGRHSLLYLKEIGHGWFGKVFLGEVHSGVSGTQVVVKELK
SQ  VSASVQEQMQFLEEAQPYRALQHSNLLQCLAQCAEVTPYLLVMEFCPLGDLKGYLRSCRVTESMAPDPLTLQRMACEVAC
SQ  GVLHLHRHNYVHSDLALRNCLLTADLTVKVGDYGLSHCKYREDYLVTADQLWVPLRWIAPELVDEVHGNLLVVDQTKSSN
SQ  VWSLGVTIWELFELGAQPYPQHSDRQVLAYAVREQQLKLPKPQLQLALSDRWYEVMQFCWLQPEQRPTAEEVHLLLSYLC
SQ  AKGTTELEEEFERRWRSLRPGGSTGLGSGSAAPAAATAASAELTAASSFPLLERFTSDGFHVDSDDVLTVTETSHGLNFE
SQ  YKWEAGCGAEEYPPSGAASSPGSAARLQELCAPDSSPPGVVPVLSAHSPSVGSEYFIRLEGAVPAAGHDPDCAGCAPSPQ
SQ  AVTDQDNNSEESTVASLAMEPLLGHAPPTEGLWGPCDHHSHRRQGSPCPSRSPSPGTPMLPAEDIDWGVATFCPPFFDDP
SQ  LGASPSGSPGAQPSPSDEEPEEGKVGLAAQCGHWSSNMSANNNSASRDPESWDPGYVSSFTDSYRDDCSSLEQTPRASPE
SQ  VGHLLSQEDPRDFLPGLVAVSPGQEPSRPFNLLPLCPAKGLAPAACLITSPWTEGAVGGAENPIVEPKLAQEAEGSAEPQ
SQ  LPLPSVPSPSCEGASLPSEEASAPDILPASPTPAAGSWVTVPEPAPTLESSGSSLGQEAPSSEDEDTTEATSGVFTDLSS
SQ  DGPHTEKSGIVPALRSLQKQVGTPDSLDSLDIPSSASDGGCEVLSPSAAGPPGGQPRAVDSGYDTENYESPEFVLKEAHE
SQ  SSEPEAFGEPASEGESPGPDPLLSVSLGGLSKKSPYRDSAYFSDLDAESEPTFGPEKHSGIQDSQKEQDLRSPPSPGHQS
SQ  VQAFPRSAVSSEVLSPPQQSEEPLPEVPRPEPLGAQGPVGVQPVPGPSHSKCFPLTSVPLISEGSGTEPQGPSGQLSGRA
SQ  QQGQMGNPSTPRSPLCLALPGHPGALEGRPEEDEDTEDSEESDEELRCYSVQEPSEDSEEEPPAVPVVVAESQSARNLRS
SQ  LLKMPSLLSEAFCDDLERKKKAVSFFDDVTVYLFDQESPTRETGEPFPSTKESLPTFLEGGPSSPSATGLPLRAGHSPDS
SQ  SAPEPGSRFEWDGDFPLVPGKAALVTELDPADPVLAAPPTPAAPFSRFTVSPTPASRFSITHISDSDAQSVGGPAAGAGG
SQ  RYTEA
//
ID  P09917;
PN  Polyunsaturated fatty acid 5-lipoxygenase;
GN  ALOX5;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0184;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P48999, ECO:0000269|PubMed:18978352}. Nucleus matrix {ECO:0000269|PubMed:19233132}. Nucleus membrane {ECO:0000269|PubMed:16275640}; Peripheral membrane protein {ECO:0000269|PubMed:16275640}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19022417}. Cytoplasm, cytosol {ECO:0000269|PubMed:19233132}. Nucleus envelope {ECO:0000269|PubMed:16275640, ECO:0000269|PubMed:19233132, ECO:0000269|PubMed:8245774}. Nucleus intermembrane space {ECO:0000269|PubMed:8245774}. Note=Shuttles between cytoplasm and nucleus (PubMed:19233132). Found exclusively in the nucleus, when phosphorylated on Ser-272 (PubMed:18978352). Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association (PubMed:19233132, PubMed:3118366, PubMed:8245774, PubMed:16275640). {ECO:0000269|PubMed:16275640, ECO:0000269|PubMed:18978352, ECO:0000269|PubMed:19233132, ECO:0000269|PubMed:3118366, ECO:0000269|PubMed:8245774}.
DR  UNIPROT: P09917;
DR  UNIPROT: B7ZLS0;
DR  UNIPROT: E5FPY5;
DR  UNIPROT: E5FPY7;
DR  UNIPROT: E5FPY8;
DR  UNIPROT: Q5JQ14;
DR  PDB: 3O8Y;
DR  PDB: 3V92;
DR  PDB: 3V98;
DR  PDB: 3V99;
DR  PDB: 6N2W;
DR  PDB: 6NCF;
DR  Pfam: PF00305;
DR  Pfam: PF01477;
DR  PROSITE: PS00711;
DR  PROSITE: PS00081;
DR  PROSITE: PS51393;
DR  PROSITE: PS50095;
DR  OMIM: 152390;
DR  DisGeNET: 240;
DE  Function: Catalyzes the oxygenation of arachidonate ((5Z,8Z,11Z,14Z)- eicosatetraenoate) to 5-hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which are potent mediators of inflammation (PubMed:8631361, PubMed:21233389, PubMed:22516296, PubMed:24282679, PubMed:19022417, PubMed:23246375, PubMed:8615788, PubMed:24893149, PubMed:31664810). Also catalyzes the oxygenation of arachidonate into 8- hydroperoxyicosatetraenoate (8-HPETE) and 12- hydroperoxyicosatetraenoate (12-HPETE) (PubMed:23246375). Displays lipoxin synthase activity being able to convert (15S)-HETE into a conjugate tetraene (PubMed:31664810). Although arachidonate is the preferred substrate, this enzyme can also metabolize oxidized fatty acids derived from arachidonate such as (15S)-HETE, eicosapentaenoate (EPA) such as (18R)- and (18S)-HEPE or docosahexaenoate (DHA) which lead to the formation of specialized pro-resolving mediators (SPM) lipoxin and resolvins E and D respectively, therefore it participates in anti-inflammatory responses (PubMed:21206090, PubMed:31664810, PubMed:8615788, PubMed:17114001, PubMed:32404334). Oxidation of DHA directly inhibits endothelial cell proliferation and sprouting angiogenesis via peroxisome proliferator-activated receptor gamma (PPARgamma) (By similarity). It does not catalyze the oxygenation of linoleic acid and does not convert (5S)-HETE to lipoxin isomers (PubMed:31664810). In addition to inflammatory processes, it participates in dendritic cell migration, wound healing through an antioxidant mechanism based on heme oxygenase-1 (HO-1) regulation expression, monocyte adhesion to the endothelium via ITGAM expression on monocytes (By similarity). Moreover, it helps establish an adaptive humoral immunity by regulating primary resting B cells and follicular helper T cells and participates in the CD40-induced production of reactive oxygen species (ROS) after CD40 ligation in B cells through interaction with PIK3R1 that bridges ALOX5 with CD40 (PubMed:21200133). May also play a role in glucose homeostasis, regulation of insulin secretion and palmitic acid-induced insulin resistance via AMPK (By similarity). Can regulate bone mineralization and fat cell differentiation increases in induced pluripotent stem cells (By similarity). {ECO:0000250|UniProtKB:P48999, ECO:0000269|PubMed:17114001, ECO:0000269|PubMed:19022417, ECO:0000269|PubMed:21200133, ECO:0000269|PubMed:21206090, ECO:0000269|PubMed:21233389, ECO:0000269|PubMed:22516296, ECO:0000269|PubMed:23246375, ECO:0000269|PubMed:24282679, ECO:0000269|PubMed:24893149, ECO:0000269|PubMed:31664810, ECO:0000269|PubMed:32404334, ECO:0000269|PubMed:8615788, ECO:0000269|PubMed:8631361}.
DE  Reference Proteome: Yes;
DE  Interaction: Q14019; IntAct: EBI-79944; Score: 0.70
DE  Interaction: Q8CLD8; IntAct: EBI-2865332; Score: 0.00
DE  Interaction: Q8D078; IntAct: EBI-2865325; Score: 0.00
DE  Interaction: P49137; IntAct: EBI-9207055; Score: 0.44
DE  Interaction: P07947; IntAct: EBI-9207225; Score: 0.44
DE  Interaction: P17612; IntAct: EBI-9207166; Score: 0.44
DE  Interaction: P08631; IntAct: EBI-9207213; Score: 0.44
DE  Interaction: P09769; IntAct: EBI-9207193; Score: 0.44
DE  Interaction: Q13555; IntAct: EBI-9207248; Score: 0.44
DE  Interaction: P50221; IntAct: EBI-10196635; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-10196645; Score: 0.56
DE  Interaction: Q6UWX4; IntAct: EBI-10196663; Score: 0.72
DE  Interaction: Q86Y26; IntAct: EBI-10196677; Score: 0.67
DE  Interaction: Q8IYX8; IntAct: EBI-10196689; Score: 0.56
DE  Interaction: Q8N0S2; IntAct: EBI-10196701; Score: 0.72
DE  Interaction: Q96MT8; IntAct: EBI-24376612; Score: 0.72
DE  Interaction: Q9Y6D9; IntAct: EBI-10196727; Score: 0.81
DE  Interaction: P31025; IntAct: EBI-25265094; Score: 0.56
DE  Interaction: Q9P0N9; IntAct: EBI-25265715; Score: 0.56
DE  Interaction: P14061; IntAct: EBI-24629482; Score: 0.56
DE  Interaction: A6NGQ2; IntAct: EBI-24683876; Score: 0.56
DE  Interaction: Q6PII3; IntAct: EBI-24692426; Score: 0.56
DE  Interaction: Q8IYJ2; IntAct: EBI-24699339; Score: 0.56
DE  Interaction: O43716; IntAct: EBI-24435599; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24476244; Score: 0.56
DE  Interaction: Q6P2R3; IntAct: EBI-12696314; Score: 0.56
DE  Interaction: Q15811; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: O94830; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q9UQ49; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q9UPU7; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q9NYA4; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q9BXB4; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q9BWT6; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q96RR4; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q96L93; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q96C34; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q96AD5; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q92530; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q8WXG6; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q8ND83; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q8N3R9; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q8IY63; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q86SX3; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q7Z2K6; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q7LBC6; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q6PJ69; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q6P474; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q6P1M9; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q6P1K2; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q4VCS5; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q2NKX8; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q15349; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q15042; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q14746; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q14008; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q13615; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q13042; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q09019; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q00653; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: P48449; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: P30566; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: P29144; IntAct: EBI-21805075; Score: 0.35
DE  Interaction: Q92542; IntAct: EBI-21836991; Score: 0.35
DE  Interaction: Q9Y252; IntAct: EBI-21839887; Score: 0.35
DE  Interaction: Q7Z699; IntAct: EBI-25930186; Score: 0.56
GO  GO:0005829;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:1904813;
GO  GO:0005635;
GO  GO:0005641;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0034774;
GO  GO:0004052;
GO  GO:0004051;
GO  GO:0036403;
GO  GO:0016787;
GO  GO:0005506;
GO  GO:0016702;
GO  GO:0019369;
GO  GO:0036336;
GO  GO:0042593;
GO  GO:0051122;
GO  GO:0006959;
GO  GO:0002232;
GO  GO:0002523;
GO  GO:1901753;
GO  GO:0019370;
GO  GO:0006691;
GO  GO:0002540;
GO  GO:0043651;
GO  GO:0034440;
GO  GO:2001301;
GO  GO:0019372;
GO  GO:0042759;
GO  GO:0016525;
GO  GO:0001937;
GO  GO:0050728;
GO  GO:1903573;
GO  GO:1903671;
GO  GO:0061044;
GO  GO:0061045;
GO  GO:0030501;
GO  GO:1904999;
GO  GO:1900407;
GO  GO:1900015;
GO  GO:0045598;
GO  GO:0050727;
GO  GO:0106014;
GO  GO:0050796;
GO  GO:1903426;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16275640};
SQ  MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDD
SQ  WYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKC
SQ  HKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNG
SQ  CNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANK
SQ  IVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAH
SQ  VRFTIAINTKAREQLICECGLFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWE
SQ  AIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLTVVIFTASAQHAAVNFGQYD
SQ  WCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRK
SQ  NLEAIVSVIAERNKKKQLPYYYLSPDRIPNSVAI
//
ID  P51399;
PN  Polyunsaturated fatty acid 5-lipoxygenase;
GN  ALOX5;
OS  10036;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0184;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P09917, ECO:0000250|UniProtKB:P48999}. Nucleus matrix {ECO:0000250|UniProtKB:P09917}. Nucleus membrane {ECO:0000250|UniProtKB:P09917}; Peripheral membrane protein {ECO:0000250|UniProtKB:P09917}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P09917}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P09917}. Nucleus envelope {ECO:0000250|UniProtKB:P09917}. Nucleus intermembrane space {ECO:0000250|UniProtKB:P09917}. Note=Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser- 272. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association. {ECO:0000250|UniProtKB:P09917}.
DR  UNIPROT: P51399;
DR  Pfam: PF00305;
DR  Pfam: PF01477;
DR  PROSITE: PS00711;
DR  PROSITE: PS00081;
DR  PROSITE: PS51393;
DR  PROSITE: PS50095;
DE  Function: Catalyzes the oxygenation of arachidonate to 5- hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which are potent mediators of inflammation. Also catalyzes the oxygenation of arachidonate into 8- hydroperoxyicosatetraenoate (8-HPETE) and 12- hydroperoxyicosatetraenoate (12-HPETE). Displays lipoxin synthase activity being able to convert (15S)-HETE into a conjugate tetraene. Although arachidonate is the preferred substrate, this enzyme can also metabolize oxidized fatty acids derived from arachidonate such as (15S)-HETE, eicosapentaenoate (EPA) such as (18R)- and (18S)-HEPE or docosahexaenoate (DHA) which lead to the formation of specialized pro- resolving mediators (SPM) lipoxin and resolvins E and D respectively, therefore it participates in anti-inflammatory responses (By similarity). Oxidation of DHA directly inhibits endothelial cell proliferation and sprouting angiogenesis via peroxisome proliferator- activated receptor gamma (PPARgamma). It does not catalyze the oxygenation of linoleic acid and does not convert (5S)-HETE to lipoxin isomers. In addition to inflammatory processes, it participates in dendritic cell migration, wound healing through an antioxidant mechanism based on heme oxygenase-1 (HO-1) regulation expression, monocyte adhesion to the endothelium via ITGAM expression on monocytes. Moreover, it helps establish an adaptive humoral immunity by regulating primary resting B cells and follicular helper T cells and participates in the CD40-induced production of reactive oxygen species (ROS) after CD40 ligation in B cells through interaction with PIK3R1 that bridges ALOX5 with CD40. May also play a role in glucose homeostasis, regulation of insulin secretion and palmitic acid-induced insulin resistance via AMPK. Can regulate bone mineralization and fat cell differentiation increases in induced pluripotent stem cells (By similarity). {ECO:0000250|UniProtKB:P09917, ECO:0000250|UniProtKB:P48999}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005641;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0004052;
GO  GO:0004051;
GO  GO:0036403;
GO  GO:0016787;
GO  GO:0005506;
GO  GO:0036336;
GO  GO:0042593;
GO  GO:0006959;
GO  GO:0002232;
GO  GO:0002523;
GO  GO:1901753;
GO  GO:0019370;
GO  GO:2001301;
GO  GO:0016525;
GO  GO:0001937;
GO  GO:0050728;
GO  GO:1903573;
GO  GO:1903671;
GO  GO:0061044;
GO  GO:0061045;
GO  GO:0030501;
GO  GO:1904999;
GO  GO:1900407;
GO  GO:1900015;
GO  GO:0045598;
GO  GO:0050727;
GO  GO:0106014;
GO  GO:0050796;
GO  GO:1903426;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P09917};
SQ  MPSYTVTVATGSQWFAGTDDYIYLSLIGSAGCSEKHLLDKAFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLHDD
SQ  WYLKYITLKTPTDYIEFPCYRWITGEGEIVLRDGRAKLARDDQIHILKQHRRKELEARQKQYRWMEWNPGFPLSIDAKCH
SQ  KDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVKNHWQEDLMFGYQFLNGC
SQ  NPVLIKRCRELPQKLPVTTEMVECSLERHLSLEQEVQEGNIFIVDYELLDGIDANKTDPCTHQFLAAPICLLYKNLANKI
SQ  VPIAIQLNQAPGEKNPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLCTHLVSEVFGIAMYRQLPAVHPIFKLLVAHV
SQ  RFTIAINTKAREQLICEYGLFDKANATGGGGHVQMVQRAVQDLTYSSLCFPEAIKARGMDSTEDIPYYFYRDDGLLVWEA
SQ  IQSFTSEVVSIYYEDDQVVMEDQELQDFVKDVYVYGMRGRKASGFPKSIKSREKLSEYLTVVIFTASAQHAAVNFGQYDW
SQ  CSWIPNAPPTMRAPPATAKGVVTIEQIVATLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMTRFRKN
SQ  LEAIVNVIAERNKNKKLPYYYLSPDRIPNSVAI
//
ID  P48999;
PN  Polyunsaturated fatty acid 5-lipoxygenase;
GN  Alox5;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0184;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P09917, ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:7629107}. Nucleus matrix {ECO:0000269|PubMed:7629107}. Nucleus membrane {ECO:0000250|UniProtKB:P09917}; Peripheral membrane protein {ECO:0000250|UniProtKB:P09917}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P09917}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P09917}. Nucleus envelope {ECO:0000250|UniProtKB:P09917}. Nucleus intermembrane space {ECO:0000250|UniProtKB:P09917}. Note=Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser- 272. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association. {ECO:0000250|UniProtKB:P09917}.
DR  UNIPROT: P48999;
DR  UNIPROT: Q3TB75;
DR  Pfam: PF00305;
DR  Pfam: PF01477;
DR  PROSITE: PS00711;
DR  PROSITE: PS00081;
DR  PROSITE: PS51393;
DR  PROSITE: PS50095;
DE  Function: Catalyzes the oxygenation of arachidonate to 5- hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which are potent mediators of inflammation (PubMed:7629107, PubMed:7809134, PubMed:7969451, PubMed:23246375, PubMed:31642348). Also catalyzes the oxygenation of arachidonic acid into 8-hydroperoxyicosatetraenoic acid (8-HPETE) and 12-hydroperoxyicosatetraenoic acid (12-HPETE) (PubMed:23246375). Displays lipoxin synthase activity being able to convert (15S)-HETE into a conjugate tetraene (By similarity). Although arachidonate is the preferred substrate, this enzyme can also metabolize oxidized fatty acids derived from arachidonate such as (15S)-HETE, eicosapentaenoate (EPA) such as (18R)- and (18S)-HEPE or docosahexaenoate (DHA) which lead to the formation of specialized pro-resolving mediators (SPM) lipoxin and resolvins E and D respectively, therefore it participates in anti-inflammatory responses (PubMed:31642348). Oxidation of DHA directly inhibits endothelial cell proliferation and sprouting angiogenesis via peroxisome proliferator-activated receptor gamma (PPARgamma)(PubMed:21307302). It does not catalyze the oxygenation of linoleic acid and does not convert (5S)-HETE to lipoxin isomers (PubMed:31642348). In addition to inflammatory processes, participates in dendritic cell migration, wound healing through an antioxidant mechanism based on heme oxygenase-1 (HO-1) regulation expression, monocyte adhesion to the endothelium via ITGAM expression on monocytes (PubMed:24226420, PubMed:23720274, PubMed:17392829, PubMed:28965882). Moreover, it helps establish an adaptive humoral immunity by regulating primary resting B cells and follicular helper T cells and participates in the CD40-induced production of reactive oxygen species (ROS) after CD40 ligation in B cells through interaction with PIK3R1 that bridges ALOX5 with CD40 (PubMed:21224059). May also play a role in glucose homeostasis, regulation of insulin secretion and palmitic acid-induced insulin resistance via AMPK (PubMed:28694473, PubMed:18421434). Can regulate bone mineralization and fat cell differentiation increases in induced pluripotent stem cells (PubMed:24906289). {ECO:0000250|UniProtKB:P09917, ECO:0000269|PubMed:17392829, ECO:0000269|PubMed:18421434, ECO:0000269|PubMed:21224059, ECO:0000269|PubMed:21307302, ECO:0000269|PubMed:23246375, ECO:0000269|PubMed:23720274, ECO:0000269|PubMed:24226420, ECO:0000269|PubMed:24906289, ECO:0000269|PubMed:28694473, ECO:0000269|PubMed:28965882, ECO:0000269|PubMed:31642348, ECO:0000269|PubMed:7629107, ECO:0000269|PubMed:7809134, ECO:0000269|PubMed:7969451}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0005641;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042383;
GO  GO:0004052;
GO  GO:0004051;
GO  GO:0036403;
GO  GO:0016787;
GO  GO:0005506;
GO  GO:0016702;
GO  GO:0002526;
GO  GO:0019369;
GO  GO:0036336;
GO  GO:0042593;
GO  GO:0051122;
GO  GO:0006959;
GO  GO:0006954;
GO  GO:0002232;
GO  GO:0002523;
GO  GO:1901753;
GO  GO:0019370;
GO  GO:0006691;
GO  GO:0002540;
GO  GO:0043651;
GO  GO:0034440;
GO  GO:2001301;
GO  GO:0019372;
GO  GO:0016525;
GO  GO:0001937;
GO  GO:0050728;
GO  GO:1903573;
GO  GO:1903671;
GO  GO:0061044;
GO  GO:0061045;
GO  GO:0030501;
GO  GO:1904960;
GO  GO:1904999;
GO  GO:0045907;
GO  GO:1900407;
GO  GO:1900015;
GO  GO:0045598;
GO  GO:0050727;
GO  GO:0106014;
GO  GO:0050796;
GO  GO:1903426;
GO  GO:0019233;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P09917};
SQ  MPSYTVTVATGSQWFAGTDDYIYLSLIGSAGCSEKHLLDKAFYNDFERGAVDSYDVTVDEELGEIYLVKIEKRKYWLHDD
SQ  WYLKYITLKTPHGDYIEFPCYRWITGEGEIVLRDGRAKLARDDQIHILKQHRRKELEARQKQYRWMEWNPGFPLSIDAKC
SQ  HKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWHDFADFEKIFVKISNTISERVKNHWQEDLMFGYQFLNG
SQ  CNPVLIKRCTALPPKLPVTTEMVECSLERQLSLEQEVQEGNIFIVDYELLDGIDANKTDPCTHQFLAAPICLLYKNLANK
SQ  IVPIAIQLNQTPGESNPIFLPTDSKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPLFKLLVAH
SQ  VRFTIAINTKAREQLICEYGLFDKANATGGGGHVQMVQRAVQDLTYSSLCFPEAIKARGMDSTEDIPFYFYRDDGLLVWE
SQ  AIQSFTMEVVSIYYENDQVVEEDQELQDFVKDVYVYGMRGKKASGFPKSIKSREKLSEYLTVVIFTASAQHAAVNFGQYD
SQ  WCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMIRFRK
SQ  NLEAIVSVIAERNKNKKLPYYYLSPDRIPNSVAI
//
ID  P12527;
PN  Polyunsaturated fatty acid 5-lipoxygenase;
GN  Alox5;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0184;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P09917, ECO:0000250|UniProtKB:P48999}. Nucleus matrix {ECO:0000250|UniProtKB:P09917}. Nucleus membrane {ECO:0000250|UniProtKB:P09917}; Peripheral membrane protein {ECO:0000250|UniProtKB:P09917}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P09917}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P09917}. Nucleus envelope {ECO:0000250|UniProtKB:P09917}. Nucleus intermembrane space {ECO:0000250|UniProtKB:P09917}. Note=Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser- 272. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association. {ECO:0000250|UniProtKB:P09917}.
DR  UNIPROT: P12527;
DR  Pfam: PF00305;
DR  Pfam: PF01477;
DR  PROSITE: PS00711;
DR  PROSITE: PS00081;
DR  PROSITE: PS51393;
DR  PROSITE: PS50095;
DE  Function: Catalyzes the oxygenation of arachidonate to 5- hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which are potent mediators of inflammation. Also catalyzes the oxygenation of arachidonate into 8- hydroperoxyicosatetraenoate (8-HPETE) and 12- hydroperoxyicosatetraenoate (12-HPETE). Displays lipoxin synthase activity being able to convert (15S)-HETE into a conjugate tetraene. Although arachidonate is the preferred substrate, this enzyme can also metabolize oxidized fatty acids derived from arachidonate such as (15S)-HETE, eicosapentaenoate (EPA) such as (18R)- and (18S)-HEPE or docosahexaenoate (DHA) which lead to the formation of specialized pro- resolving mediators (SPM) lipoxin and resolvins E and D respectively, therefore it participates in anti-inflammatory responses (By similarity). Oxidation of DHA directly inhibits endothelial cell proliferation and sprouting angiogenesis via peroxisome proliferator- activated receptor gamma (PPARgamma). It does not catalyze the oxygenation of linoleic acid and does not convert (5S)-HETE to lipoxin isomers. In addition to inflammatory processes, it participates in dendritic cell migration, wound healing through an antioxidant mechanism based on heme oxygenase-1 (HO-1) regulation expression, monocyte adhesion to the endothelium via ITGAM expression on monocytes. Moreover, it helps establish an adaptive humoral immunity by regulating primary resting B cells and follicular helper T cells and participates in the CD40-induced production of reactive oxygen species (ROS) after CD40 ligation in B cells through interaction with PIK3R1 that bridges ALOX5 with CD40. May also play a role in glucose homeostasis, regulation of insulin secretion and palmitic acid-induced insulin resistance via AMPK. Can regulate bone mineralization and fat cell differentiation increases in induced pluripotent stem cells (By similarity). {ECO:0000250|UniProtKB:P09917, ECO:0000250|UniProtKB:P48999}.
DE  Reference Proteome: Yes;
DE  Interaction: P20291; IntAct: EBI-15746644; Score: 0.49
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0005641;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042383;
GO  GO:0004052;
GO  GO:0004051;
GO  GO:0036403;
GO  GO:0016787;
GO  GO:0005506;
GO  GO:0016702;
GO  GO:0002526;
GO  GO:0019369;
GO  GO:0036336;
GO  GO:0042593;
GO  GO:0051122;
GO  GO:0006959;
GO  GO:0006954;
GO  GO:0002232;
GO  GO:0002523;
GO  GO:1901753;
GO  GO:0019370;
GO  GO:0006691;
GO  GO:0002540;
GO  GO:0043651;
GO  GO:0034440;
GO  GO:2001301;
GO  GO:0019372;
GO  GO:0016525;
GO  GO:0001937;
GO  GO:0050728;
GO  GO:1903573;
GO  GO:1903671;
GO  GO:0061044;
GO  GO:0061045;
GO  GO:0030501;
GO  GO:1904960;
GO  GO:1904999;
GO  GO:0045907;
GO  GO:1900407;
GO  GO:1900015;
GO  GO:0045598;
GO  GO:0050727;
GO  GO:0106014;
GO  GO:0050796;
GO  GO:1903426;
GO  GO:0055093;
GO  GO:0007584;
GO  GO:0019233;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P09917};
SQ  MPSYTVTVATGSQWFAGTDDYIYLSLIGSAGCSEKHLLDKAFYNDFERGGRDSYDVTVDEELGEIYLVKIEKRKYRLHDD
SQ  WYLKYITLKTPHDYIEFPCYRWITGEGEIVLRDGCAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCH
SQ  KDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWHDFADFEKIFVKISNTISERVKNHWQEDLMFGYQFLNGC
SQ  NPVLIKRCTELPKKLPVTTEMVECSLERQLSLEQEVQEGNIFIVDYELLDGIDANKTDPCTHQFLAAPICLLYKNLANKI
SQ  VPIAIQLNQTPGEKNPIFLPTDSKYDWLLAKIWVRSSDFHIHQTITHLLRTHLVSEVFGIAMYRQLPAVHPLFKLLVAHV
SQ  RFTIAINTKAREQLNCEYGLFDKANATGGGGHVQMVQRAVQDLTYSSLCFPEAIKARGMDNTEDIPYYFYRDDGLLVWEA
SQ  IQSFTTEVVSIYYEDDQVVEEDQELQDFVKDVYVYGMRGRKASGFPKSIKSREKLSEYLTVVIFTASAQHAAVNFGQYDW
SQ  CSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMIRFRKN
SQ  LEAIVSVIAERNKNKKLPYYYLSPDRIPNSVAI
//
ID  Q14693;
PN  Phosphatidate phosphatase LPIN1;
GN  LPIN1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:29765047}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:29765047}. Nucleus membrane {ECO:0000250|UniProtKB:Q91ZP3}. Note=Translocates from the cytosol to the endoplasmic reticulum following acetylation by KAT5. {ECO:0000269|PubMed:29765047}.
DR  UNIPROT: Q14693;
DR  UNIPROT: A8MU38;
DR  UNIPROT: B4DET9;
DR  UNIPROT: B4DGS4;
DR  UNIPROT: B4DGZ6;
DR  UNIPROT: B5MC18;
DR  UNIPROT: B7Z858;
DR  UNIPROT: D6W506;
DR  UNIPROT: E7ESE7;
DR  UNIPROT: F5GY24;
DR  UNIPROT: Q53T25;
DR  Pfam: PF16876;
DR  Pfam: PF04571;
DR  Pfam: PF08235;
DR  OMIM: 268200;
DR  OMIM: 605518;
DR  DisGeNET: 23175;
DE  Function: Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis and therefore controls the metabolism of fatty acids at different levels (PubMed:20231281, PubMed:29765047). Is involved in adipocyte differentiation (By similarity). Acts also as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression (By similarity). Recruited at the mitochondrion outer membrane and is involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol (By similarity). {ECO:0000250|UniProtKB:Q91ZP3, ECO:0000269|PubMed:20231281, ECO:0000269|PubMed:29765047}.
DE  Disease: Myoglobinuria, acute recurrent, autosomal recessive (ARARM) [MIM:268200]: Recurrent myoglobinuria is characterized by recurrent attacks of rhabdomyolysis (necrosis or disintegration of skeletal muscle) associated with muscle pain and weakness and followed by excretion of myoglobin in the urine. Renal failure may occasionally occur. {ECO:0000269|PubMed:18817903}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P12931; IntAct: EBI-25892196; Score: 0.56
DE  Interaction: Q00613; IntAct: EBI-25869697; Score: 0.56
DE  Interaction: Q00534; IntAct: EBI-5293262; Score: 0.44
DE  Interaction: Q8TEQ6; IntAct: EBI-11086338; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9BQK8; IntAct: EBI-21854905; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: P62136; IntAct: EBI-16370519; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-20905656; Score: 0.40
DE  Interaction: P62258; IntAct: EBI-25384933; Score: 0.35
DE  Interaction: P09172; IntAct: EBI-25840287; Score: 0.56
DE  Interaction: Q01658; IntAct: EBI-25845745; Score: 0.56
DE  Interaction: P21333; IntAct: EBI-25856444; Score: 0.56
DE  Interaction: P01100; IntAct: EBI-25856887; Score: 0.56
DE  Interaction: P50440; IntAct: EBI-25857412; Score: 0.56
DE  Interaction: P14136; IntAct: EBI-25858196; Score: 0.56
DE  Interaction: P62993; IntAct: EBI-25859867; Score: 0.56
DE  Interaction: P28799; IntAct: EBI-25861035; Score: 0.56
DE  Interaction: Q00403; IntAct: EBI-25865181; Score: 0.56
DE  Interaction: P04792; IntAct: EBI-25870897; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25898341; Score: 0.56
DE  Interaction: Q9Y5Q9; IntAct: EBI-25907060; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25915429; Score: 0.56
DE  Interaction: Q9UBB4; IntAct: EBI-25917615; Score: 0.56
DE  Interaction: Q9Y3C5; IntAct: EBI-25918856; Score: 0.56
DE  Interaction: Q8N2W9; IntAct: EBI-25922910; Score: 0.56
DE  Interaction: Q8WXH2; IntAct: EBI-25927801; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25944050; Score: 0.56
DE  Interaction: Q15326; IntAct: EBI-30825002; Score: 0.44
DE  Interaction: Q93009; IntAct: EBI-30842269; Score: 0.44
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005741;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0008195;
GO  GO:0003713;
GO  GO:0031100;
GO  GO:0044255;
GO  GO:0032869;
GO  GO:0009062;
GO  GO:0007077;
GO  GO:0031642;
GO  GO:1903741;
GO  GO:0006654;
GO  GO:0046473;
GO  GO:0120162;
GO  GO:0045740;
GO  GO:0045944;
GO  GO:0019432;
GO  GO:0006642;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVIRQPNGNLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKL
SQ  GDNGEAFFVQETDNDQEVIPMHLATSPILSEGASRMECQLKRGSVDRMRGLDPSTPAQVIAPSETPSSSSVVKKRRKRRR
SQ  KSQLDSLKRDDNMNTSEDEDMFPIEMSSDEAMELLESSRTLPNDIPPFQDDIPEENLSLAVIYPQSASYPNSDREWSPTP
SQ  SPSGSRPSTPKSDSELVSKSTERTGQKNPEMLWLWGELPQAAKSSSPHKMKESSPLSSRKICDKSHFQAIHSESSDTFSD
SQ  QSPTLVGGALLDQNKPQTEMQFVNEEDLETLGAAAPLLPMIEELKPPSASVVQTANKTDSPSRKRDKRSRHLGADGVYLD
SQ  DLTDMDPEVAALYFPKNGDPSGLAKHASDNGARSANQSPQSVGSSGVDSGVESTSDGLRDLPSIAISLCGGLSDHREITK
SQ  DAFLEQAVSYQQFVDNPAIIDDPNLVVKIGSKYYNWTTAAPLLLAMQAFQKPLPKATVESIMRDKMPKKGGRWWFSWRGR
SQ  NTTIKEESKPEQCLAGKAHSTGEQPPQLSLATRVKHESSSSDEERAAAKPSNAGHLPLLPNVSYKKTLRLTSEQLKSLKL
SQ  KNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFL
SQ  YCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGN
SQ  RPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFPLLKRSHSSDFPCSDTFSNFTFWREPLPPF
SQ  ENQDIHSASA
//
ID  Q91ZP3;
PN  Phosphatidate phosphatase LPIN1;
GN  Lpin1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Mitochondrion outer membrane {ECO:0000269|PubMed:21397848}. Cytoplasm {ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:21397848}. Nucleus membrane {ECO:0000269|PubMed:21397848}. Note=Recruited at the mitochondrion outer membrane following phosphatidic acid formation mediated by PLD6. In neuronals cells, isoform 1 is exclusively cytoplasmic (PubMed:21397848). In 3T3-L1 pre-adipocytes, it primarily located in the cytoplasm (PubMed:16049017). {ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:21397848}. [Isoform 2]: Nucleus {ECO:0000269|PubMed:11138012, ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:17105729, ECO:0000269|PubMed:19753306, ECO:0000269|PubMed:22134922}. Cytoplasm {ECO:0000269|PubMed:19753306}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14693}. Note=Nuclear localization requires both CNEP1R1 and CTDNEP1 (PubMed:22134922). In neuronals cells, localized in both the cytoplasm and the nucleus (PubMed:19753306). In 3T3-L1 pre-adipocytes, it is predominantly nuclear (PubMed:16049017). Translocates from the cytosol to the endoplasmic reticulum following acetylation by KAT5 (By similarity). {ECO:0000250|UniProtKB:Q14693, ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:19753306, ECO:0000269|PubMed:22134922}.
DR  UNIPROT: Q91ZP3;
DR  UNIPROT: Q9CQI2;
DR  UNIPROT: Q9JLG6;
DR  PDB: 7KIH;
DR  PDB: 7KIL;
DR  Pfam: PF16876;
DR  Pfam: PF04571;
DR  Pfam: PF08235;
DE  Function: Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis and therefore controls the metabolism of fatty acids at different levels (PubMed:17158099). Acts also as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression (PubMed:16950137). Is involved in adipocyte differentiation (PubMed:16049017). {ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:16950137, ECO:0000269|PubMed:17158099}. [Isoform 1]: Recruited at the mitochondrion outer membrane and is involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol. {ECO:0000269|PubMed:21397848}.
DE  Disease: Note=Defects in Lpin1 are the cause of the fatty liver dystrophy phenotype (fld). Fld mutant mice are characterized by neonatal fatty liver and hypertriglyceridemia that resolve at weaning, and neuropathy affecting peripheral nerve in adulthood. Adipose tissue deficiency, glucose intolerance and increased susceptibility to atherosclerosis are associated with this mutation too. Two independent mutant alleles are characterized in this phenotype, fld and fld2j. {ECO:0000269|PubMed:11138012}.
DE  Reference Proteome: Yes;
DE  Interaction: O95476; IntAct: EBI-5323701; Score: 0.27
DE  Interaction: P31946; IntAct: EBI-7640098; Score: 0.35
DE  Interaction: P62137; IntAct: EBI-16369626; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005741;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005667;
GO  GO:0042826;
GO  GO:0042975;
GO  GO:0008195;
GO  GO:0061629;
GO  GO:0003713;
GO  GO:0031532;
GO  GO:0044255;
GO  GO:0032869;
GO  GO:0045444;
GO  GO:0009062;
GO  GO:0006955;
GO  GO:0006629;
GO  GO:0000266;
GO  GO:0031642;
GO  GO:1903741;
GO  GO:0000122;
GO  GO:0046473;
GO  GO:0120162;
GO  GO:0045740;
GO  GO:0031065;
GO  GO:0045944;
GO  GO:0045598;
GO  GO:0031529;
GO  GO:0019432;
GO  GO:0006642;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVIRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKL
SQ  GDNGEAFFVQETDNDQEIIPMYLATSPILSEGAARMESQLKRNSVDRIRCLDPTTAAQGLPPSDTPSTGSLGKKRRKRRR
SQ  KAQLDNLKRDDNVNSSEDEDMFPIEMSSDEDTAPMDGSRTLPNDVPPFQDDIPKENFPSISTHPQSASYPSSDREWSPSP
SQ  SSLVDCQRTPPHLAEGVLSSSCPLQSCHFHASESPSGSRPSTPKSDSELVSKSADRLTPKNNLEMLWLWGELPQAAKSSS
SQ  PHKMKESSPLGSRKTPDKMNFQAIHSESSDTFSDQSPTMARGLLIHQSKAQTEMQFVNEEDLESLGAAAPPSPVAEELKA
SQ  PYPNTAQSSSKTDSPSRKKDKRSRHLGADGVYLDDLTDMDPEVAALYFPKNGDPGGLPKQASDNGARSANQSPQSVGGSG
SQ  IDSGVESTSDSLRDLPSIAISLCGGLSDHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKVGNKYYNWTTAAPLLLAM
SQ  QAFQKPLPKATVESIMRDKMPKKGGRWWFSWRGRNATIKEESKPEQCLTGKGHNTGEQPAQLGLATRIKHESSSSDEEHA
SQ  AAKPSGSSHLSLLSNVSYKKTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRS
SQ  DTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHRE
SQ  VIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVV
SQ  DHVFPLLKRSHSCDFPCSDTFSNFTFWREPLPPFENQDMHSASA
//
ID  P42704;
PN  Leucine-rich PPR motif-containing protein, mitochondrial;
GN  LRPPRC;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Mitochondrion. Nucleus, nucleoplasm. Nucleus inner membrane. Nucleus outer membrane. Note=Seems to be predominantly mitochondrial.
DR  UNIPROT: P42704;
DR  UNIPROT: A0PJE3;
DR  UNIPROT: A8K1V1;
DR  UNIPROT: Q53PC0;
DR  UNIPROT: Q53QN7;
DR  UNIPROT: Q6ZUD8;
DR  UNIPROT: Q7Z7A6;
DR  UNIPROT: Q96D84;
DR  Pfam: PF01535;
DR  Pfam: PF13812;
DR  Pfam: PF17177;
DR  PROSITE: PS51375;
DR  OMIM: 220111;
DR  OMIM: 607544;
DR  DisGeNET: 10128;
DE  Function: May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters. Binds single-stranded DNA (By similarity). {ECO:0000250, ECO:0000269|PubMed:11585913, ECO:0000269|PubMed:12832482, ECO:0000269|PubMed:15081402, ECO:0000269|PubMed:15139850, ECO:0000269|PubMed:15272088, ECO:0000269|PubMed:17050673}.
DE  Disease: Mitochondrial complex IV deficiency, nuclear type 5 (MC4DN5) [MIM:220111]: An autosomal recessive, severe mitochondrial disease with multisystemic manifestations and early onset. Clinical features include delayed psychomotor development, impaired intellectual development with speech delay, mild dysmorphic facial features, hypotonia, ataxia, and seizures. Brain imaging shows bilaterally symmetrical necrotic lesions in subcortical brain regions. Mortality is high, due to episodes of severe metabolic acidosis and coma. {ECO:0000269|PubMed:12529507, ECO:0000269|PubMed:26510951}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-8770853; Score: 0.53
DE  Interaction: Q9Y6K9; IntAct: EBI-361392; Score: 0.00
DE  Interaction: Q15653; IntAct: EBI-365313; Score: 0.00
DE  Interaction: P60709; IntAct: EBI-353790; Score: 0.40
DE  Interaction: O75365; IntAct: EBI-1060175; Score: 0.00
DE  Interaction: Q9Y5J5; IntAct: EBI-1060455; Score: 0.00
DE  Interaction: Q9P2S5; IntAct: EBI-1060482; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.67
DE  Interaction: Q9Y4K3; IntAct: EBI-1065456; Score: 0.00
DE  Interaction: Q9HC98; IntAct: EBI-1066112; Score: 0.00
DE  Interaction: P60520; IntAct: EBI-1066983; Score: 0.00
DE  Interaction: P23508; IntAct: EBI-1068590; Score: 0.00
DE  Interaction: P78396; IntAct: EBI-1070328; Score: 0.00
DE  Interaction: P19532; IntAct: EBI-1071516; Score: 0.00
DE  Interaction: P43360; IntAct: EBI-1073949; Score: 0.00
DE  Interaction: Q9UBN6; IntAct: EBI-1074138; Score: 0.00
DE  Interaction: P62330; IntAct: EBI-1074333; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1075130; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1076912; Score: 0.00
DE  Interaction: P11171; IntAct: EBI-1079980; Score: 0.00
DE  Interaction: Q9Y2Q3; IntAct: EBI-1083828; Score: 0.00
DE  Interaction: Q9Y5V3; IntAct: EBI-1084294; Score: 0.00
DE  Interaction: P63104; IntAct: EBI-7192962; Score: 0.40
DE  Interaction: O70343; IntAct: EBI-1371067; Score: 0.40
DE  Interaction: Q9UBK2; IntAct: EBI-1371136; Score: 0.52
DE  Interaction: Q8AZK7; IntAct: EBI-9632715; Score: 0.35
DE  Interaction: P06730; IntAct: EBI-8582156; Score: 0.58
DE  Interaction: O94966; IntAct: EBI-2511876; Score: 0.40
DE  Interaction: Q70CQ1; IntAct: EBI-2512828; Score: 0.40
DE  Interaction: Q9NXR7; IntAct: EBI-2514089; Score: 0.40
DE  Interaction: Q81ME0; IntAct: EBI-2830399; Score: 0.00
DE  Interaction: Q9Z381; IntAct: EBI-2865280; Score: 0.00
DE  Interaction: Q9BSB4; IntAct: EBI-3255690; Score: 0.35
DE  Interaction: Q14197; IntAct: EBI-7825470; Score: 0.35
DE  Interaction: Q6QDQ4; IntAct: EBI-5276631; Score: 0.35
DE  Interaction: Q15327; IntAct: EBI-5653419; Score: 0.00
DE  Interaction: Q9GZT3; IntAct: EBI-7503132; Score: 0.56
DE  Interaction: O75381; IntAct: EBI-5911953; Score: 0.35
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P05919; IntAct: EBI-6175288; Score: 0.46
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: Q5U5Q3; IntAct: EBI-8011718; Score: 0.35
DE  Interaction: O35658; IntAct: EBI-6393534; Score: 0.35
DE  Interaction: P21860; IntAct: EBI-8771060; Score: 0.35
DE  Interaction: P20963; IntAct: EBI-9512492; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-11322719; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q9Y6E7; IntAct: EBI-10715009; Score: 0.35
DE  Interaction: P03177; IntAct: EBI-11721652; Score: 0.35
DE  Interaction: P06428; IntAct: EBI-11722493; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: Q9DUG7; IntAct: EBI-11734217; Score: 0.35
DE  Interaction: A2APR8; IntAct: EBI-11001201; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-11009211; Score: 0.35
DE  Interaction: P09803; IntAct: EBI-11019737; Score: 0.35
DE  Interaction: P51149; IntAct: EBI-11050319; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: Q9HBM1; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: Q14573; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: P28715; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: Q9NPL8; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: Q9BZQ6; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: J3KS15; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: A8K7Q2; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: Q9P2K8; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: J3QL56; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: Q6UB35; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: P38117; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: Q6PJT7; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: Q02224; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: B4DR80; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: P39748; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: P36776; IntAct: EBI-11137058; Score: 0.35
DE  Interaction: P42768; IntAct: EBI-11139448; Score: 0.35
DE  Interaction: Q96EB6; IntAct: EBI-11139448; Score: 0.35
DE  Interaction: Q14CZ7; IntAct: EBI-11426979; Score: 0.35
DE  Interaction: P63000; IntAct: EBI-12451898; Score: 0.51
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q9NZI8; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: O14829; IntAct: EBI-14024386; Score: 0.35
DE  Interaction: Q96KR7; IntAct: EBI-14027299; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: P62136; IntAct: EBI-16370519; Score: 0.35
DE  Interaction: Q96EV8; IntAct: EBI-16749117; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-16786806; Score: 0.27
DE  Interaction: P10809; IntAct: EBI-16790769; Score: 0.27
DE  Interaction: O14880; IntAct: EBI-16796475; Score: 0.27
DE  Interaction: Q15118; IntAct: EBI-16796954; Score: 0.27
DE  Interaction: Q9BVS5; IntAct: EBI-16802257; Score: 0.27
DE  Interaction: O95714; IntAct: EBI-16811848; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: Q9H6K4; IntAct: EBI-21937258; Score: 0.35
DE  Interaction: Q15007; IntAct: EBI-20595349; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: O96013; IntAct: EBI-26962273; Score: 0.35
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: O95183; IntAct: EBI-21267749; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21132574; Score: 0.58
DE  Interaction: Q5T9A4; IntAct: EBI-21981699; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-21981790; Score: 0.35
DE  Interaction: Q9NTX7; IntAct: EBI-22117924; Score: 0.35
DE  Interaction: P28562; IntAct: EBI-25377052; Score: 0.35
DE  Interaction: Q16828; IntAct: EBI-25377680; Score: 0.35
DE  Interaction: P27361; IntAct: EBI-25386687; Score: 0.35
DE  Interaction: O15530; IntAct: EBI-25387801; Score: 0.35
DE  Interaction: O94776; IntAct: EBI-25389141; Score: 0.35
DE  Interaction: P08631; IntAct: EBI-25390400; Score: 0.35
DE  Interaction: Q13480; IntAct: EBI-25393000; Score: 0.35
DE  Interaction: Q15256; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: O84648; IntAct: EBI-22303579; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9BY14; IntAct: EBI-25504841; Score: 0.35
DE  Interaction: Q8NHP6; IntAct: EBI-25617558; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-26396507; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-26396827; Score: 0.35
DE  Interaction: Q6ZNK6; IntAct: EBI-26453464; Score: 0.35
DE  Interaction: O14561; IntAct: EBI-26494947; Score: 0.40
DE  Interaction: Q96T52; IntAct: EBI-27049069; Score: 0.27
DE  Interaction: Q96LU5; IntAct: EBI-27049466; Score: 0.27
DE  Interaction: Q9H300; IntAct: EBI-27049982; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: P36507; IntAct: EBI-28935019; Score: 0.35
DE  Interaction: Q05513; IntAct: EBI-28938998; Score: 0.35
DE  Interaction: Q8NI60; IntAct: EBI-28943519; Score: 0.35
DE  Interaction: Q9H5K3; IntAct: EBI-28948637; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q86VG3; IntAct: EBI-28997277; Score: 0.35
DE  Interaction: Q8N612; IntAct: EBI-34574737; Score: 0.27
DE  Interaction: Q5W0V3; IntAct: EBI-34574999; Score: 0.27
DE  Interaction: Q86V87; IntAct: EBI-34575191; Score: 0.27
DE  Interaction: P12830; IntAct: EBI-34581511; Score: 0.35
GO  GO:0000794;
GO  GO:0005856;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0042645;
GO  GO:0005739;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0048487;
GO  GO:0008017;
GO  GO:0003730;
GO  GO:0003723;
GO  GO:0003697;
GO  GO:0031625;
GO  GO:0000957;
GO  GO:0047497;
GO  GO:0051028;
GO  GO:0000961;
GO  GO:0070129;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALLRSARWLLRAGAAPRLPLSLRLLPGGPGRLHAASYLPAARAGPVAGGLLSPARLYAIAAKEKDIQEESTFSSRKIS
SQ  NQFDWALMRLDLSVRRTGRIPKKLLQKVFNDTCRSGGLGGSHALLLLRSCGSLLPELKLEERTEFAHRIWDTLQKLGAVY
SQ  DVSHYNALLKVYLQNEYKFSPTDFLAKMEEANIQPNRVTYQRLIASYCNVGDIEGASKILGFMKTKDLPVTEAVFSALVT
SQ  GHARAGDMENAENILTVMRDAGIEPGPDTYLALLNAYAEKGDIDHVKQTLEKVEKSELHLMDRDLLQIIFSFSKAGYPQY
SQ  VSEILEKVTCERRYIPDAMNLILLLVTEKLEDVALQILLACPVSKEDGPSVFGSFFLQHCVTMNTPVEKLTDYCKKLKEV
SQ  QMHSFPLQFTLHCALLANKTDLAKALMKAVKEEGFPIRPHYFWPLLVGRRKEKNVQGIIEILKGMQELGVHPDQETYTDY
SQ  VIPCFDSVNSARAILQENGCLSDSDMFSQAGLRSEAANGNLDFVLSFLKSNTLPISLQSIRSSLLLGFRRSMNINLWSEI
SQ  TELLYKDGRYCQEPRGPTEAVGYFLYNLIDSMSDSEVQAKEEHLRQYFHQLEKMNVKIPENIYRGIRNLLESYHVPELIK
SQ  DAHLLVESKNLDFQKTVQLTSSELESTLETLKAENQPIRDVLKQLILVLCSEENMQKALELKAKYESDMVTGGYAALINL
SQ  CCRHDKVEDALNLKEEFDRLDSSAVLDTGKYVGLVRVLAKHGKLQDAINILKEMKEKDVLIKDTTALSFFHMLNGAALRG
SQ  EIETVKQLHEAIVTLGLAEPSTNISFPLVTVHLEKGDLSTALEVAIDCYEKYKVLPRIHDVLCKLVEKGETDLIQKAMDF
SQ  VSQEQGEMVMLYDLFFAFLQTGNYKEAKKIIETPGIRARSARLQWFCDRCVANNQVETLEKLVELTQKLFECDRDQMYYN
SQ  LLKLYKINGDWQRADAVWNKIQEENVIPREKTLRLLAEILREGNQEVPFDVPELWYEDEKHSLNSSSASTTEPDFQKDIL
SQ  IACRLNQKKGAYDIFLNAKEQNIVFNAETYSNLIKLLMSEDYFTQAMEVKAFAETHIKGFTLNDAANSRLIITQVRRDYL
SQ  KEAVTTLKTVLDQQQTPSRLAVTRVIQALAMKGDVENIEVVQKMLNGLEDSIGLSKMVFINNIALAQIKNNNIDAAIENI
SQ  ENMLTSENKVIEPQYFGLAYLFRKVIEEQLEPAVEKISIMAERLANQFAIYKPVTDFFLQLVDAGKVDDARALLQRCGAI
SQ  AEQTPILLLFLLRNSRKQGKASTVKSVLELIPELNEKEEAYNSLMKSYVSEKDVTSAKALYEHLTAKNTKLDDLFLKRYA
SQ  SLLKYAGEPVPFIEPPESFEFYAQQLRKLRENSS
//
ID  Q6PB66;
PN  Leucine-rich PPR motif-containing protein, mitochondrial;
GN  Lrpprc;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Mitochondrion {ECO:0000250}. Nucleus {ECO:0000269|PubMed:12071956}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus inner membrane {ECO:0000250}. Nucleus outer membrane {ECO:0000250}.
DR  UNIPROT: Q6PB66;
DR  UNIPROT: Q8K4V0;
DR  UNIPROT: Q9CRX4;
DR  Pfam: PF01535;
DR  Pfam: PF17177;
DR  PROSITE: PS51375;
DE  Function: May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters (By similarity). Binds single-stranded DNA. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: O70343; IntAct: EBI-1371242; Score: 0.44
DE  Interaction: Q8VHJ7; IntAct: EBI-1371302; Score: 0.40
DE  Interaction: Q9R1E0; IntAct: EBI-1371337; Score: 0.52
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: O54957; IntAct: EBI-12602258; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: P51637; IntAct: EBI-20565496; Score: 0.35
DE  Interaction: A2AKD7; IntAct: EBI-20566393; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0000794;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005874;
GO  GO:0042645;
GO  GO:0005739;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0048487;
GO  GO:0003730;
GO  GO:0003723;
GO  GO:0003697;
GO  GO:0031625;
GO  GO:0000957;
GO  GO:0051028;
GO  GO:0000961;
GO  GO:0070129;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALLRPARWLLGAAAAPRLPLSLRLPAGVPGRLSSVVRVAAVGSRPAAGERLSQARLYAIVAEKRDLQEEPAPVRKNSS
SQ  QFDWALMRLDNSVRRTGRITKGLLQRVFESTCSSGSPGSNQALLLLRSCGSLLPELSLAERTEFAHKIWDKLQQLGVVYD
SQ  VSHYNALLKVYLQNEYKFSPTDFLAKMEGANIQPNRVTYQRLIAAYCNVGDIEGASKILGFMKTKDLPITEAVFSALVTG
SQ  HARAGDMENAENILTVMKQAGIEPGPDTYLALLNAHAERGDIGQVRQILEKVEKSDHYFMDRDFLQVIFSFSKAGYPQYV
SQ  SEILEKITYERRSIPDAMNLILFLATEKLEDTAFQVLLALPLSKDESSDNFGSFFLRHCVTLDLPPEKLIDYCRRLRDAK
SQ  LHSSSLQFTLHCALQANRTALAKAVMEALREEGFPIRPHYFWPLLAGHQKTKNVQGIIDILKIMNKVGVDPDQETYINYV
SQ  FPCFDSAQSVRAALQENECLLASSTFAQAEVKNEAINGNLQNILSFLESNTLPFSFSSLRNSLILGFRRSMNIDLWSKIT
SQ  ELLYKDERYCSKPPGPAEAVGYFLYNLIDSMSDSEVQAKEERLRQYFHQLQEMNVKVPENIYKGICNLLNTYHVPELIKD
SQ  IKVLVDREKVDSQKTSQVTSSDLESTLEKLKAEGQPVGSALKQLLLLLCSEENMQKALEVKAKYESDMVIGGYAALINLC
SQ  CRHDNAEDAWNLKQEVDRLDASAILDTAKYVALVKVLGKHSRLQDAINILKEMKEKDVVIKDATVLSFFHILNGAALRGE
SQ  IETVKQLHEAIVTLGLAKPSSNISFPLVTVHLEKGDLPAALEASIACHKKYKVLPRIHDVLCKLVEKGETDLIQKAMDFV
SQ  SQEQGEMTMLYDLFFAFLQTGNYKEAKKIIETPGIRARPTRLQWFCDRCIASNQVEALEKLVELTEKLFECDRDQMYYNL
SQ  LKLYKISSDWQRADAAWTKMQEENIIPRERTLRLLAEILKTSNQEVPFDVPELWFGDDRPSLSPSSRSAGEDVTEKTLLS
SQ  NCKLKKSKDAYNIFLKAEKQNVVFSSETYSTLIGLLLSKDDFTQAMHVKDFAETHIKGFTLNDAANSLLIIRQVRRDYLK
SQ  GALATLRAALDLKQVPSQIAVTRLIQALALKGDVESIEAIQRMVAGLDTIGLSKMVFINNIALAQMKNNKLDAAIENIEH
SQ  LLASENQAIEPQYFGLSYLFRKVIEEQMEPALEKLSIMSERMANQFALYKPVTDLFLQLVDSGKVDEARALLERCGAIAE
SQ  QSSLLSVFCLRTSQKPKKAPVLKTLLELIPELRDNDKVYSCSMKSYALDKDVASAKALYEYLTAKNLKLDDLFLKRYAAL
SQ  LKDVGEPVPFPEPPESFAFYIKQLKEARESPS
//
ID  Q5SGE0;
PN  Leucine-rich PPR motif-containing protein, mitochondrial;
GN  Lrpprc;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Mitochondrion {ECO:0000269|PubMed:15525270}. Nucleus {ECO:0000269|PubMed:15525270}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus inner membrane {ECO:0000250}. Nucleus outer membrane {ECO:0000250}.
DR  UNIPROT: Q5SGE0;
DR  Pfam: PF01535;
DR  Pfam: PF13812;
DR  Pfam: PF17177;
DR  PROSITE: PS51375;
DE  Function: May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters. Binds single-stranded DNA (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000794;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005874;
GO  GO:0042645;
GO  GO:0005739;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0048487;
GO  GO:0003730;
GO  GO:0003723;
GO  GO:0003697;
GO  GO:0031625;
GO  GO:0000957;
GO  GO:0051028;
GO  GO:0000961;
GO  GO:0070129;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSALLRPARWLLGAAAVPRLPLSLRLPAGGPGRLPSVVRVAAAGGRPAAGELLSQARLYAIVAEKKDLPEEPAPVRRSGS
SQ  QFDWALMRLDNSVRRTGRITKGLLQKVFESTCRSGSPGSNQALLLLRSCGSLLPELSLAERTEFAHKIWDKLQQLGTVYD
SQ  VSHYNALLKVYLQNEYRFSPTDFLAKMEGANIQPNRVTYQRLIAAYCSVGDIEGASKILGFMKTRDLPITEAVFSALVTG
SQ  HARAGDMESAENILTVMKQAGIEPGPDTYLALLNAHAEKGDIDHVKQILEKVEKSDHYFMDRDFLQIIVSFSKAGYPQYV
SQ  SEILEKITYERRSIPDAMNLILLLVTEKLEDTAFQVLLALPLARDETSSSFGSFFLRHCVTMDTPAEKLIDYCKRLRDAK
SQ  VHSSSLQFTLHCALQANKTALAKAVMEALRDEGFPIRTHYFWPLLVGHQKTKNVQGIIDILKIMKEMGVDPDQETYINYV
SQ  FPCFGSVQSARAALQENKCLPKSTTFAQAEVRNEAINGNLQNILSFLESNALPFSFNSLRGSLILGFRRSMNIDLWSKIT
SQ  ELLYKDDRYCQKPPGPTEAVGYFLYNLIDSMSDSEVQAKEERLRQYFHQLREMNVKVSENIYKGICNLLDNYHVPELIKD
SQ  VKVLVDREKIDSRKTSQFTSSDLESTLEKLKAEGHPVGDPLKQLILLLCSEENMQKALEVKAKYESDMVIGGYAALINLC
SQ  CRHDNAEDALNLKQEFDRLDPSAVLDTAKYVALVKVLGKHGRVQDAINILKEMKEKDVVIKDAAVLSFFHILNGAALRGE
SQ  IETVKQLHEAIVTLGLAKPSSNISFPLVTVHLEKDDLPAALEASIACHEKYKVLPRIHDVLCKLIEKGETDLIQKAMDFV
SQ  SQEQGEMSMLYDLFFAFLQTGNYKEAKKIIETPGIRARPTRLQWFCDRCIANNQVETLEKLVELTEKLFECDRDQMYYNL
SQ  LKLYKISGDWQRADAVWNKMQEENLIPRERTLRLLAGILKTSNQEVPFDVPELWFGDDRSSLSSSSPSAGDTVTEKMLLS
SQ  DCRLKKSKDAYNIFLKAEKQDVVFSSEAYSTLVGLLLSKDDFTRAMHVKDFAETHIKGFTLNGAASSLLIIAQVRRDYLK
SQ  VALETLKAALDLEQVPSELAVTRLIQALALQGDVKSIETIQKMVKGLDAIELSRMVFINNIALAQMKNNEIDAAIENIEH
SQ  MLASENQTVEHQYFGLSYLFRKVIEEQMEPALEKLSIMSERLANQFALYKPVTDLFLQLVDSGKVDEARALLERCGAIAE
SQ  QTSILSVFCLRTSQKPKKAPVLKTLLELIPELRENDRVYSCSMKSYVADKDVASAKALYEHLTAKNMKLDDLFLKRYASL
SQ  LKDVGEPVPFTEPPESFGFYIKQLKEARENPS
//
ID  O60711;
PN  Leupaxin;
GN  LPXN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cell junction, focal adhesion. Nucleus. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, podosome. Cell membrane. Note=Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin.
DR  UNIPROT: O60711;
DR  UNIPROT: B2R8B4;
DR  UNIPROT: B4DV71;
DR  UNIPROT: Q53FW6;
DR  UNIPROT: Q6FI07;
DR  PDB: 1X3H;
DR  PDB: 4XEF;
DR  PDB: 4XEK;
DR  PDB: 4XEV;
DR  Pfam: PF00412;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  OMIM: 605390;
DR  DisGeNET: 9404;
DE  Function: Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin- induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling. {ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:18451096, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:20543562}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9BUY5; IntAct: EBI-753886; Score: 0.37
DE  Interaction: Q96BD5; IntAct: EBI-754372; Score: 0.37
DE  Interaction: Q9NV31; IntAct: EBI-755833; Score: 0.37
DE  Interaction: P48059; IntAct: EBI-755887; Score: 0.37
DE  Interaction: P49639; IntAct: EBI-758764; Score: 0.37
DE  Interaction: Q96HA1; IntAct: EBI-24358856; Score: 0.56
DE  Interaction: Q5NGW8; IntAct: EBI-2805204; Score: 0.00
DE  Interaction: A0A6H3AGX8; IntAct: EBI-2830392; Score: 0.00
DE  Interaction: Q8D0I3; IntAct: EBI-2865247; Score: 0.00
DE  Interaction: Q8ZBT8; IntAct: EBI-2865240; Score: 0.00
DE  Interaction: Q8CLR7; IntAct: EBI-2865261; Score: 0.00
DE  Interaction: Q8CZX0; IntAct: EBI-2865254; Score: 0.00
DE  Interaction: A0A5P8YKZ2; IntAct: EBI-2865268; Score: 0.00
DE  Interaction: Q06455; IntAct: EBI-10224246; Score: 0.56
DE  Interaction: Q9NRQ2; IntAct: EBI-8646488; Score: 0.37
DE  Interaction: P18206; IntAct: EBI-24389026; Score: 0.56
DE  Interaction: O14733; IntAct: EBI-3912623; Score: 0.37
DE  Interaction: Q9Y473; IntAct: EBI-3913887; Score: 0.37
DE  Interaction: P09022; IntAct: EBI-3957720; Score: 0.57
DE  Interaction: Q9UBN7; IntAct: EBI-7173812; Score: 0.37
DE  Interaction: Q16659; IntAct: EBI-7210390; Score: 0.37
DE  Interaction: Q05397; IntAct: EBI-7326264; Score: 0.55
DE  Interaction: Q9Y6K9; IntAct: EBI-5773611; Score: 0.00
DE  Interaction: P13612; IntAct: EBI-6082976; Score: 0.40
DE  Interaction: Q9WMX2; IntAct: EBI-9078253; Score: 0.37
DE  Interaction: P25800; IntAct: EBI-10203411; Score: 0.74
DE  Interaction: P31274; IntAct: EBI-10205826; Score: 0.78
DE  Interaction: Q494U1; IntAct: EBI-10241520; Score: 0.56
DE  Interaction: Q8N3L3; IntAct: EBI-10243799; Score: 0.56
DE  Interaction: Q8IVE3; IntAct: EBI-10261607; Score: 0.67
DE  Interaction: Q99608; IntAct: EBI-21251068; Score: 0.37
DE  Interaction: Q63HR2; IntAct: EBI-24282289; Score: 0.56
DE  Interaction: Q8TAP4; IntAct: EBI-24292538; Score: 0.56
DE  Interaction: P01137; IntAct: EBI-24372152; Score: 0.56
DE  Interaction: P21549; IntAct: EBI-24402036; Score: 0.56
DE  Interaction: P29972; IntAct: EBI-24467413; Score: 0.56
DE  Interaction: Q7Z3B4; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: Q9Y2X9; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q9Y2X7; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q9ULM0; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q9UGP4; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q9NXC5; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q9NVD7; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q9NR12; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q9H939; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q99700; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q96SN8; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q96F86; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q93052; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q8IZD4; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q86YT6; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q76N32; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q69YQ0; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q2TAL8; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q16204; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q15654; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q15154; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q15052; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q14161; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q14155; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q13177; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q13153; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: Q05209; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: P29558; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: O95613; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: P68640; IntAct: EBI-20817414; Score: 0.37
DE  Interaction: A0A5P8YF53; IntAct: EBI-20818304; Score: 0.37
DE  Interaction: Q14289; IntAct: EBI-21392269; Score: 0.00
DE  Interaction: Q96CV9; IntAct: EBI-25910777; Score: 0.56
GO  GO:0042995;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0016020;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0002102;
GO  GO:0046872;
GO  GO:0003712;
GO  GO:0007155;
GO  GO:0043542;
GO  GO:0050859;
GO  GO:0007162;
GO  GO:0065003;
GO  GO:0033628;
GO  GO:0007165;
GO  GO:0034446;
GO  GO:0007179;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELDALLEELERSTLQDSDEYSNPAPLPLDQHSRKETNLDETSEILSIQDNTSPLPAQLVYTTNIQELNVYSEAQEPKE
SQ  SPPPSKTSAAAQLDELMAHLTEMQAKVAVRADAGKKHLPDKQDHKASLDSMLGGLEQELQDLGIATVPKGHCASCQKPIA
SQ  GKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHC
SQ  GEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELH
SQ  YHHRRGTLCHGCGQPITGRCISAMGYKFHPEHFVCAFCLTQLSKGIFREQNDKTYCQPCFNKLFPL
//
ID  Q99N69;
PN  Leupaxin;
GN  Lpxn;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cell junction, focal adhesion. Nucleus. Cytoplasm, perinuclear region. Cell projection, podosome. Cell membrane. Note=Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin (By similarity). {ECO:0000250}.
DR  UNIPROT: Q99N69;
DR  Pfam: PF00412;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DE  Function: Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin- induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling. {ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:19917054}.
DE  Reference Proteome: Yes;
DE  Interaction: Q62406; IntAct: EBI-658892; Score: 0.37
DE  Interaction: A0A0F6AW51; IntAct: EBI-13950465; Score: 0.40
GO  GO:0042995;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0002102;
GO  GO:0046872;
GO  GO:0003712;
GO  GO:0043542;
GO  GO:0050859;
GO  GO:0007162;
GO  GO:0033628;
GO  GO:0034446;
GO  GO:0007179;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELDALLEELERCTFQDSEEYSNPVSCHLDQQSTEESKIPQTPKTLSSQGNTSPLKVQLVYATNIQEPNVYSEVQEPKE
SQ  SVLPPKTSAAAQLDELMAHLSEMQAKVSVKADTSRKPLPDQQDHKASLDSMLGDLEQELQDLGIATVPKGYCASCQKPIA
SQ  GKVIHALGQSWHPEHFVCTHCKEELGSSPFFERSGLAYCSKDYHRLFSPRCAYCAAPITDKVLTAMNKTWHPEHFFCSHC
SQ  GEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMNTVWHPECFVCGDCFSSFSSGSFFELDGRPFCELH
SQ  YHHRRGTLCHDCGQPITGRCISAMGHKFHPEHFVCAFCLTQLPKGIFKEQNNKTYCEKCFTKLFSQ
//
ID  Q9N261;
PN  Leupaxin;
GN  LPXN;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, podosome {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9N261;
DR  UNIPROT: G1TMN6;
DR  Pfam: PF00412;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DE  Function: Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin- induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0042995;
GO  GO:0005925;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0002102;
GO  GO:0046872;
GO  GO:0007155;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELDALLEELERSTLQDSDEYSNSAPLPLDQSSRKESNLDETSKMLSVQDSTNPFPVQLVYTTNIQDRNVYSEVQEPKK
SQ  SPPPAKTSAAAQLDELMAHLSEMQAKVSVKADAGKKPVSENLDHKASLDSMLGGLEQELQNLGIPTVPKGHCASCQKPIV
SQ  GKVIHALGQSWHPEHFICTHCKEEIGSSPFFERSGLAYCPKDYHHLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHC
SQ  GEVFGTEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMNTVWHPECFVCGDCFSSFSTGSFFELEGRPFCELH
SQ  YHQRRGTLCHGCGQPITGRCISAMGHKFHPEHFVCAFCLTQLSKGVFREQNDKTYCQPCFNKLFSL
//
ID  Q9BGL2;
PN  Lecithin retinol acyltransferase;
GN  LRAT;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Rough endoplasmic reticulum {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9BGL2;
DR  Pfam: PF04970;
DR  PROSITE: PS51934;
DE  Function: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters (PubMed:9920938, PubMed:2722792). Retinyl esters are storage forms of vitamin A (Probable). LRAT plays a critical role in vision (Probable). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis- retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (Probable). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (By similarity). {ECO:0000250|UniProtKB:Q9JI60, ECO:0000269|PubMed:2722792, ECO:0000269|PubMed:9920938, ECO:0000305|PubMed:9920938}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005771;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0102279;
GO  GO:0047173;
GO  GO:0050896;
GO  GO:0042572;
GO  GO:0007601;
GO  GO:0006776;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKNPMLEAVSLVLEKLLFISYFKFFSSGAPGQDKAGNTLYEISSFLRGDVLEVPRTHLTHYGIYLGDNRVAHMMPDILLA
SQ  LTDDKGRTQKVVSNKRLILGVIGRVASIRVDTVEDFAYGAEILVNHLDRSLKKKALLNEEVAQRAEKLLGITPYSLLWNN
SQ  CEHFVTYCRYGTPISPQADKFCENVKIIIRDQRSVLASAVLGLASIFCLGLTSYTTLPAIFIPFLLWMAG
//
ID  O95237;
PN  Lecithin retinol acyltransferase;
GN  LRAT;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Rough endoplasmic reticulum {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells (By similarity). {ECO:0000250}.
DR  UNIPROT: O95237;
DR  UNIPROT: A8K983;
DR  UNIPROT: Q8N716;
DR  Pfam: PF04970;
DR  PROSITE: PS51934;
DR  OMIM: 604863;
DR  OMIM: 613341;
DR  DisGeNET: 9227;
DE  Function: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters (PubMed:9920938). Retinyl esters are storage forms of vitamin A (Probable). LRAT plays a critical role in vision (Probable). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis- retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (Probable). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (By similarity). {ECO:0000250|UniProtKB:Q9JI60, ECO:0000269|PubMed:9920938, ECO:0000305|PubMed:9920938}.
DE  Disease: Leber congenital amaurosis 14 (LCA14) [MIM:613341]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:11381255, ECO:0000269|PubMed:17011878, ECO:0000269|PubMed:18055821}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y320; IntAct: EBI-23786490; Score: 0.56
DE  Interaction: P62952; IntAct: EBI-24746858; Score: 0.56
DE  Interaction: Q7Z5P4; IntAct: EBI-25181851; Score: 0.56
DE  Interaction: O60361; IntAct: EBI-21771578; Score: 0.40
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005771;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0016746;
GO  GO:0102279;
GO  GO:0016416;
GO  GO:0047173;
GO  GO:0001972;
GO  GO:0019841;
GO  GO:1990830;
GO  GO:0032370;
GO  GO:0009617;
GO  GO:0032526;
GO  GO:0033189;
GO  GO:0001523;
GO  GO:0042572;
GO  GO:0007601;
GO  GO:0006776;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTHYGIYLGDNRVAHMMPDILLA
SQ  LTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGANILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNN
SQ  CEHFVTYCRYGTPISPQSDKFCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
//
ID  Q9JI60;
PN  Lecithin retinol acyltransferase;
GN  Lrat;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17114808, ECO:0000269|PubMed:28758396}; Single-pass membrane protein {ECO:0000269|PubMed:17114808}. Rough endoplasmic reticulum {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9JI60;
DR  PDB: 4Q95;
DR  Pfam: PF04970;
DR  PROSITE: PS51934;
DE  Function: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A (PubMed:28758396). LRAT plays a critical role in vision (By similarity). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis- retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (By similarity). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (PubMed:25416279). {ECO:0000250|UniProtKB:O95237, ECO:0000269|PubMed:25416279, ECO:0000269|PubMed:28758396}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005771;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0102279;
GO  GO:0008374;
GO  GO:0047173;
GO  GO:0001972;
GO  GO:0019841;
GO  GO:0006653;
GO  GO:1990830;
GO  GO:0032370;
GO  GO:0009617;
GO  GO:0032526;
GO  GO:0033189;
GO  GO:0042572;
GO  GO:0007601;
GO  GO:0006776;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKNPMLEAASLLLEKLLLISNFKLFSVSVPGGGTGKNRPYEISSFVRGDVLEVSRTHFIHYGIYLGENRVAHLMPDILLA
SQ  LTNDKERTQKVVSNKRLLLGVICKVASIRVDTVEDFAYGADILVNHLDGTLKKKSLLNEEVARRAEQQLGLTPYSLLWNN
SQ  CEHFVTYCRYGSRISPQAEKFYDTVKIIIRDQRSSLASAVLGLASIVYTGLASYMTLPAICIPFCLWMMSG
//
ID  Q9JI61;
PN  Lecithin retinol acyltransferase;
GN  Lrat;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Rough endoplasmic reticulum {ECO:0000269|PubMed:18544127}. Endosome, multivesicular body {ECO:0000269|PubMed:18544127}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18544127}. Note=Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells.
DR  UNIPROT: Q9JI61;
DR  Pfam: PF04970;
DR  PROSITE: PS51934;
DE  Function: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters (PubMed:3410848). Retinyl esters are storage forms of vitamin A (By similarity). LRAT plays a critical role in vision (By similarity). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis- retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (By similarity). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (By similarity). {ECO:0000250|UniProtKB:O95237, ECO:0000250|UniProtKB:Q9JI60, ECO:0000269|PubMed:17158102, ECO:0000269|PubMed:3410848}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005771;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0102279;
GO  GO:0008374;
GO  GO:0047173;
GO  GO:0001972;
GO  GO:0019841;
GO  GO:1990830;
GO  GO:0032370;
GO  GO:0009617;
GO  GO:0032526;
GO  GO:0033189;
GO  GO:0042572;
GO  GO:0007601;
GO  GO:0006776;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKNSMLEAASLLLEKLLLISNFKIFSVCAPGGGTGKKHPYEINSFLRGDVLEVSRTHFTHYGIYLGDNRVAHLMPDILLA
SQ  LTSDKERTQKVVSNKRLLPGVICKVASIRVDTVEDFAYGADILVNHLDETLKKKSLLNEEVARRAEQQLGLTPYSLLWNN
SQ  CEHFVTYCRYGSPISPQAEKFHETVKILIRDQRSCLASAVLGLVSIIYTGLASYMTLPAVCIPFCLWMMSG
//
ID  Q5E9X4;
PN  Leucine-rich repeat-containing protein 59, N-terminally processed;
GN  LRRC59;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear envelope depends upon the nuclear import machinery, including KPNB1. {ECO:0000250}.
DR  UNIPROT: Q5E9X4;
DR  UNIPROT: Q17QQ7;
DR  Pfam: PF13855;
DR  PROSITE: PS51450;
DE  Function: Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P19711; IntAct: EBI-16593373; Score: 0.35
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0042645;
GO  GO:0005635;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKAGSKGGNLRDKLDGNELDLSLSDLNEVPVKELAALPKATVLDLSCNKLTTLPSDFCGLTHLVKLDLSKNKLRQLPAD
SQ  FGRLVNLQHLDLLNNRLVTLPVSFAQLKSLKWLDLKDNPLDPVLAKVAGDCLDEKQCKQCANKVLQHMKAVQADQERERQ
SQ  RRLEIDREAEKKWEAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKETNQAPKSKSSSRPRKPPPRK
SQ  HTRSWAVLKLLLLLLLCVAGGLVACRVTELQQQPLCTSVNTIYDNAVRGLRSHDILQWVLQTDSQQ
//
ID  Q5F334;
PN  Leucine-rich repeat-containing protein 59;
GN  LRRC59;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Comments: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear envelope depends upon the nuclear import machinery. {ECO:0000250}.
DR  UNIPROT: Q5F334;
DR  Pfam: PF13855;
DE  Function: Required for nuclear import of FGF1. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARGGGKSGSLKDKLDGNELDLSLCGLSEVPVRELAALPKATVLDLSCNSLVSLPSDFCSLTHLVKLDLSKNRLQQLPVD
SQ  FGRLVSLQHLDLLNNRLVTLPVSFAQLKLSLHHSPVEILSRLLGTPSSLLVFHSFHSWENQNLKWLDLKDNPLDPVLAKV
SQ  AGDCLDEKQCKQAAVRVLQHMKVIQSEQDRERQRKLQAEREMEKKREAEQRAREAQERELRKREKAEEKERRRREYDAQR
SQ  AAKQEMEKKTKKETVQTRKLASSSRPPQPARHKHSWSRSVLRALLLVLLCILCTLAVCKLTELQHQPLCVSVNTLYEDVV
SQ  AAVQNHKTLQNMLQQNSQQ
//
ID  Q6NWG1;
PN  Leucine-rich repeat-containing protein 59;
GN  lrrc59;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear envelope depends upon the nuclear import machinery. {ECO:0000250}.
DR  UNIPROT: Q6NWG1;
DR  Pfam: PF13855;
DR  PROSITE: PS51450;
DE  Function: Required for nuclear import of FGF1. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0046579;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNKGKIENIKDKIDGNELDLSLSNLTEVPVKELAAFPKATFLDLSCNNLITLTPEFCSLTHLIKIDLNKNQLVCLPEEIG
SQ  QLVNLQHLDLYNNKLKMLPIGFSQLKSLKWLDLKDNPLEPTLAKAAGDCLDEKQCRQCASRVLQHMKVLQEEAEKELERR
SQ  LLKEREQEKKKEAKQREKEAREKEAQKKKKAEEKERKRKEYQAQVAAVAAQEQQKKKKEEKKKKAAQNQGKKAAPESVPK
SQ  AKRSICSLFFSLLLKLVLLLVIGVSSVVAVCQLTELRKEAFCIPLNVHFEETVRWAQGLDVVQQVIQKMSDLRT
//
ID  Q96AG4;
PN  Leucine-rich repeat-containing protein 59, N-terminally processed;
GN  LRRC59;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane; Single-pass type II membrane protein. Nucleus envelope. Note=Localization in the nuclear envelope depends upon the nuclear import machinery, including KPNB1.
DR  UNIPROT: Q96AG4;
DR  UNIPROT: B2RE83;
DR  UNIPROT: D3DTX8;
DR  UNIPROT: Q9P189;
DR  Pfam: PF13855;
DR  PROSITE: PS51450;
DR  OMIM: 614854;
DR  DisGeNET: 55379;
DE  Function: Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores. {ECO:0000269|PubMed:22321063}.
DE  Reference Proteome: Yes;
DE  Interaction: P00519; IntAct: EBI-10101379; Score: 0.35
DE  Interaction: P00533; IntAct: EBI-702075; Score: 0.35
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P12931; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q15125; IntAct: EBI-24548327; Score: 0.56
DE  Interaction: Q5BJF2; IntAct: EBI-24560640; Score: 0.56
DE  Interaction: P19438; IntAct: EBI-364474; Score: 0.00
DE  Interaction: P40337; IntAct: EBI-1061500; Score: 0.00
DE  Interaction: P78396; IntAct: EBI-1065388; Score: 0.00
DE  Interaction: P23508; IntAct: EBI-1066087; Score: 0.00
DE  Interaction: Q9UET6; IntAct: EBI-1069061; Score: 0.00
DE  Interaction: Q9H1Y0; IntAct: EBI-1070756; Score: 0.00
DE  Interaction: P56537; IntAct: EBI-1071348; Score: 0.00
DE  Interaction: Q9UKE5; IntAct: EBI-1073298; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1075053; Score: 0.00
DE  Interaction: P11171; IntAct: EBI-1076336; Score: 0.00
DE  Interaction: O75815; IntAct: EBI-1077503; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-1078796; Score: 0.00
DE  Interaction: Q9Y478; IntAct: EBI-1079493; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1083352; Score: 0.00
DE  Interaction: P29372; IntAct: EBI-1084066; Score: 0.00
DE  Interaction: P48039; IntAct: EBI-1188258; Score: 0.53
DE  Interaction: Q9UL18; IntAct: EBI-7641579; Score: 0.35
DE  Interaction: Q9Y2K6; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: P01100; IntAct: EBI-2687467; Score: 0.00
DE  Interaction: Q92731; IntAct: EBI-2880211; Score: 0.46
DE  Interaction: Q9Y371; IntAct: EBI-3622855; Score: 0.35
DE  Interaction: P51858; IntAct: EBI-4409719; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-5321978; Score: 0.44
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: P67809; IntAct: EBI-8853354; Score: 0.56
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: P10398; IntAct: EBI-10101513; Score: 0.35
DE  Interaction: O60307; IntAct: EBI-10103761; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: P06461; IntAct: EBI-11723785; Score: 0.35
DE  Interaction: Q9JLQ0; IntAct: EBI-11033702; Score: 0.35
DE  Interaction: P35749; IntAct: EBI-11098041; Score: 0.35
DE  Interaction: Q9NPD3; IntAct: EBI-11126463; Score: 0.35
DE  Interaction: Q15006; IntAct: EBI-11130215; Score: 0.35
DE  Interaction: Q9NVD3; IntAct: EBI-11154093; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q96Q45; IntAct: EBI-11396533; Score: 0.27
DE  Interaction: Q99IB8; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q9H2L4; IntAct: EBI-24519719; Score: 0.56
DE  Interaction: Q9H0R3; IntAct: EBI-24521426; Score: 0.56
DE  Interaction: Q96MX0; IntAct: EBI-24523693; Score: 0.56
DE  Interaction: Q6UX34; IntAct: EBI-24629651; Score: 0.56
DE  Interaction: P55061; IntAct: EBI-24424978; Score: 0.56
DE  Interaction: Q5VZY2; IntAct: EBI-24537950; Score: 0.56
DE  Interaction: P56851; IntAct: EBI-24543931; Score: 0.56
DE  Interaction: Q5TGU0; IntAct: EBI-24553760; Score: 0.56
DE  Interaction: O95406; IntAct: EBI-24558366; Score: 0.56
DE  Interaction: Q6RW13; IntAct: EBI-24562799; Score: 0.56
DE  Interaction: Q96DZ9; IntAct: EBI-24576076; Score: 0.56
DE  Interaction: Q9ULP0; IntAct: EBI-24580735; Score: 0.56
DE  Interaction: Q8N609; IntAct: EBI-24593407; Score: 0.56
DE  Interaction: P29972; IntAct: EBI-24603065; Score: 0.56
DE  Interaction: P56945; IntAct: EBI-15099384; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q12797; IntAct: EBI-21649522; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16685608; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.42
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-20821761; Score: 0.35
DE  Interaction: O95819; IntAct: EBI-20900495; Score: 0.40
DE  Interaction: Q00765; IntAct: EBI-20901832; Score: 0.40
DE  Interaction: Q9Y5A6; IntAct: EBI-20903696; Score: 0.40
DE  Interaction: O76021; IntAct: EBI-20906176; Score: 0.40
DE  Interaction: P62917; IntAct: EBI-20907960; Score: 0.40
DE  Interaction: Q9UL63; IntAct: EBI-20908464; Score: 0.40
DE  Interaction: B3KS81; IntAct: EBI-20908696; Score: 0.40
DE  Interaction: Q9Y3D0; IntAct: EBI-20909184; Score: 0.40
DE  Interaction: Q15648; IntAct: EBI-20910000; Score: 0.40
DE  Interaction: Q8ND76; IntAct: EBI-20923706; Score: 0.40
DE  Interaction: Q9UPN4; IntAct: EBI-20923938; Score: 0.40
DE  Interaction: Q5VUA4; IntAct: EBI-20932048; Score: 0.40
DE  Interaction: Q9ULD8; IntAct: EBI-20933132; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-21236980; Score: 0.37
DE  Interaction: Q00059; IntAct: EBI-21980665; Score: 0.35
DE  Interaction: Q04837; IntAct: EBI-21980936; Score: 0.35
DE  Interaction: O15530; IntAct: EBI-25375702; Score: 0.35
DE  Interaction: O84008; IntAct: EBI-22302433; Score: 0.35
DE  Interaction: P0DJI4; IntAct: EBI-22303808; Score: 0.35
DE  Interaction: Q8NF50; IntAct: EBI-25409278; Score: 0.35
DE  Interaction: Q6ZRI8; IntAct: EBI-25410669; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q8NHP6; IntAct: EBI-25617558; Score: 0.35
DE  Interaction: P60033; IntAct: EBI-25645944; Score: 0.35
DE  Interaction: Q8NBM4; IntAct: EBI-25771384; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-26396827; Score: 0.35
DE  Interaction: Q8TB24; IntAct: EBI-26518569; Score: 0.35
DE  Interaction: Q8NDZ4; IntAct: EBI-26597064; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NG92; IntAct: EBI-27055968; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NJM6; IntAct: EBI-27055978; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-27087549; Score: 0.35
DE  Interaction: O60285; IntAct: EBI-28931176; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-28931531; Score: 0.35
DE  Interaction: P20794; IntAct: EBI-28934658; Score: 0.35
DE  Interaction: P32298; IntAct: EBI-28934990; Score: 0.35
DE  Interaction: P36507; IntAct: EBI-28935019; Score: 0.35
DE  Interaction: Q86V86; IntAct: EBI-28942203; Score: 0.35
DE  Interaction: Q8NI60; IntAct: EBI-28943519; Score: 0.35
DE  Interaction: Q9UPE1; IntAct: EBI-28946981; Score: 0.35
DE  Interaction: Q9UIH9; IntAct: EBI-29019642; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-29661630; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32718189; Score: 0.35
DE  Interaction: P08069; IntAct: EBI-32718669; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-32719716; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0042645;
GO  GO:0005635;
GO  GO:0045296;
GO  GO:0003723;
GO  GO:0046579;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKAGSKGGNLRDKLDGNELDLSLSDLNEVPVKELAALPKATILDLSCNKLTTLPSDFCGLTHLVKLDLSKNKLQQLPAD
SQ  FGRLVNLQHLDLLNNKLVTLPVSFAQLKNLKWLDLKDNPLDPVLAKVAGDCLDEKQCKQCANKVLQHMKAVQADQERERQ
SQ  RRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQAPKSKSGSRPRKPPPRK
SQ  HTRSWAVLKLLLLLLLFGVAGGLVACRVTELQQQPLCTSVNTIYDNAVQGLRRHEILQWVLQTDSQQ
//
ID  Q922Q8;
PN  Leucine-rich repeat-containing protein 59, N-terminally processed;
GN  Lrrc59;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear envelope depends upon the nuclear import machinery, including KPNB1. {ECO:0000250}.
DR  UNIPROT: Q922Q8;
DR  UNIPROT: Q3TJ35;
DR  UNIPROT: Q3TLC7;
DR  UNIPROT: Q3TWT9;
DR  UNIPROT: Q3TX86;
DR  Pfam: PF13855;
DR  PROSITE: PS51450;
DE  Function: Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P22366; IntAct: EBI-658942; Score: 0.37
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: A0A0F6AZI6; IntAct: EBI-13950226; Score: 0.35
DE  Interaction: P14094; IntAct: EBI-20566937; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0042645;
GO  GO:0005635;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKAGSKGGNLRDKLDGNELDLSLSDLNEVPVKELAALPKATVLDLSCNKLSTLPSDFCGLTHLVKLDLSKNKLQQLPAD
SQ  FGRLVNLQHLDLLNNRLVTLPVSFAQLKNLKWLDLKDNPLDPVLAKVAGDCLDEKQCKQCANKVLQHMKAVQADQERERQ
SQ  RRLEVEREAEKKREAKQQAKEAKERELRKREKAEEKERRRKEYDAQKASKREQEKKPKKEANQAPKSKSGSRPRKPPPRK
SQ  HTRSWAVLKVLLLLLLLCVAGGLVVCRVTGLHQQPLCTSVNTIYDNAVQGLRHHEILQWVLQTDSQQ
//
ID  Q5RJR8;
PN  Leucine-rich repeat-containing protein 59, N-terminally processed;
GN  Lrrc59;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear envelope depends upon the nuclear import machinery, including KPNB1. {ECO:0000250}.
DR  UNIPROT: Q5RJR8;
DR  UNIPROT: Q63742;
DR  Pfam: PF13855;
DR  PROSITE: PS51450;
DE  Function: Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P11362; IntAct: EBI-22243924; Score: 0.35
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0042645;
GO  GO:0005635;
GO  GO:0046579;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKTGSKGGNLRDKLDGNELDLSLSDLNEVPVKELAALPKATVLDLSCNKLSTLPSDFCGLTHLVKLDLSKNKLQQLPAD
SQ  FGRLVNLQHLDLLNNRLVTLPVSFAQLKNLKWLDLKDNPLDPVLAKVAGDCLDEKQCKQCANKVLQHMKAVQADQERERQ
SQ  RRLEVEREAEKKREAKQQAKEAKERELRKREKAEEKERRRKEYDAQKASKREQEKKPKKETNQAPKSKSGSRPRKPPPRK
SQ  HNRSWAVLKGLLLLLLLCVAGGLVVCRVTGLQQQPLCTSVNAIYDNAVQGLRHHEILQWVLQTDSQQ
//
ID  Q8AVS8;
PN  Leucine-rich repeat-containing protein 59;
GN  lrrc59;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear envelope depends upon the nuclear import machinery. {ECO:0000250}.
DR  UNIPROT: Q8AVS8;
DR  Pfam: PF13855;
DR  PROSITE: PS51450;
DE  Function: Required for nuclear import of FGF1. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARANGRSQNLRDKLDGNELDLSLSDLSEVPVRDLVAIPKATALDLSCNKLTTLPDDFCNLSHIVRLDLSKNQIVQLPSE
SQ  FGRLMNLQHLDLLQNHLMSLPVSFAQLKSLKWLDLKDNPLKPDLAKVAGDCLDEKQCKECAQRVLQYMKSVQSDHEIELQ
SQ  RKLQLDKERKKKLEAKQRVKEEQEREMRKRKKQQQKERKRRDYNAMQEAERALNSNKKAEEEPTENHKRMATPKEKKLAQ
SQ  RQSRLRKIACILLFGLLVVLLVVVACRFTDLKAINMCTSVNAIYKETLSALHSNPVLERFLQDPSSQ
//
ID  Q6NX28;
PN  Leucine-rich repeat-containing protein 59;
GN  lrrc59;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Comments: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear envelope depends upon the nuclear import machinery. {ECO:0000250}.
DR  UNIPROT: Q6NX28;
DR  Pfam: PF13855;
DE  Function: Required for nuclear import of FGF1. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARANGRSQNLRDKLDGNELDLSLSDLSEVPVRDLVAIPKATALDLSCNKLTSLPDDFCNLSYIVRLDLSKNQIAQLPSE
SQ  FGRLVNLQHLDLLQNRIVALPVSFAQLKSLKWLDLKDNPLKPALAKVAGDCLDEKQCKECAQGVLQYMKSVQSDHERELQ
SQ  RKLQLDKDRKQRLEAQQRVKEEQDRELRKRMKQQQKERKRRDYNAMQEAQKALNNNKKKAEEEPSENHKPVPTPKEKKLA
SQ  RRQSRLRKIACILLFGLMVALLGVVACRFTDLKTFEVCRSVNAVYKETLSALHSNPVLERFLQDPSSQ
//
ID  Q2NKS0;
PN  Leukotriene C4 synthase;
GN  LTC4S;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Nucleus membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}.
DR  UNIPROT: Q2NKS0;
DR  Pfam: PF01124;
DE  Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity. Can also catalyzes the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions. {ECO:0000250|UniProtKB:Q16873}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0008047;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0042802;
GO  GO:0004464;
GO  GO:0008289;
GO  GO:0019370;
GO  GO:0006691;
GO  GO:0042759;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q16873};
SQ  MKDEVALLASVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERIYRAQVNCSEYFPLFLAMLWVAGIFFHEGAAA
SQ  LCGLVYLFARLRYFQGYARSAQQRLAPLYASARALWLLVALAALGLLAHFLPAELRAALLGQLRKLLLRS
//
ID  A6XA80;
PN  Leukotriene C4 synthase;
GN  LTC4S;
OS  10141;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Nucleus membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}.
DR  UNIPROT: A6XA80;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity. Can also catalyzes the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions. {ECO:0000250|UniProtKB:Q16873}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0008047;
GO  GO:0004464;
GO  GO:0016740;
GO  GO:0019370;
GO  GO:0006691;
GO  GO:0042759;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q16873};
SQ  MKDEVALLATVTLLGVLLQAYFSLQVIRARRAHRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGVYFHEGAAA
SQ  LCGLVYLFTRLRYFWGYARSAQLRLAPLYASARALWLLLALATLGLLAHFLPAAARAALLRLLRALLRTA
//
ID  Q16873;
PN  Leukotriene C4 synthase;
GN  LTC4S;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:12023288}; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12023288, ECO:0000269|PubMed:19233132}; Multi-pass membrane protein. Nucleus membrane {ECO:0000269|PubMed:19233132}; Multi-pass membrane protein.
DR  UNIPROT: Q16873;
DR  UNIPROT: Q8N6P0;
DR  UNIPROT: Q9UC73;
DR  UNIPROT: Q9UD18;
DR  PDB: 2PNO;
DR  PDB: 2UUH;
DR  PDB: 2UUI;
DR  PDB: 3B29;
DR  PDB: 3HKK;
DR  PDB: 3LEO;
DR  PDB: 3PCV;
DR  PDB: 4BPM;
DR  PDB: 4J7T;
DR  PDB: 4J7Y;
DR  PDB: 4JC7;
DR  PDB: 4JCZ;
DR  PDB: 4JRZ;
DR  PDB: 4WAB;
DR  PDB: 5HV9;
DR  PDB: 6R7D;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DR  OMIM: 246530;
DR  DisGeNET: 4056;
DE  Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity (PubMed:7937884, PubMed:27791009, PubMed:27365393, PubMed:9153254, PubMed:23409838). Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions (PubMed:27791009). {ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:27365393, ECO:0000269|PubMed:27791009, ECO:0000269|PubMed:7937884, ECO:0000269|PubMed:9153254}.
DE  Disease: Note=LTC4 synthase deficiency is associated with a neurometabolic developmental disorder characterized by muscular hypotonia, psychomotor retardation, failure to thrive, and microcephaly. {ECO:0000269|PubMed:10896305, ECO:0000269|PubMed:9820300}.
DE  Reference Proteome: Yes;
DE  Interaction: Q15125; IntAct: EBI-23732251; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-24691036; Score: 0.56
DE  Interaction: Q4KMG9; IntAct: EBI-24796155; Score: 0.56
DE  Interaction: O15529; IntAct: EBI-23926961; Score: 0.56
DE  Interaction: Q96BA8; IntAct: EBI-24431627; Score: 0.56
DE  Interaction: P11912; IntAct: EBI-24648231; Score: 0.56
DE  Interaction: Q8TBB6; IntAct: EBI-25159097; Score: 0.56
DE  Interaction: Q14802; IntAct: EBI-25185672; Score: 0.56
DE  Interaction: O14843; IntAct: EBI-24791564; Score: 0.56
DE  Interaction: Q16873; IntAct: EBI-15532004; Score: 0.75
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0008047;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0042802;
GO  GO:0004464;
GO  GO:0008289;
GO  GO:0019370;
GO  GO:0006691;
GO  GO:0042759;
TP  Membrane Topology: Transmembrane; Source: UniProt - Curator Inference {ECO:0000305|PubMed:12023288,};
SQ  MKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGIFFHEGAAA
SQ  LCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVALAALGLLAHFLPAALRAALLGRLRTLLPWA
//
ID  Q60860;
PN  Leukotriene C4 synthase;
GN  Ltc4s;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Nucleus membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}.
DR  UNIPROT: Q60860;
DR  UNIPROT: Q5SVR7;
DR  UNIPROT: Q9QVS1;
DR  PDB: 4NTA;
DR  PDB: 4NTB;
DR  PDB: 4NTF;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity (PubMed:8706658, PubMed:11319240). Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy- docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti- inflammatory and proresolving actions (By similarity). {ECO:0000250|UniProtKB:Q16873, ECO:0000269|PubMed:11319240, ECO:0000269|PubMed:8706658}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0008047;
GO  GO:0043295;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0042802;
GO  GO:0004464;
GO  GO:0008289;
GO  GO:0044877;
GO  GO:0019370;
GO  GO:0006691;
GO  GO:0042759;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q16873};
SQ  MKDEVALLATVTLVGVLLQAYFSLQVISARRAFHVSPPLTSGPPEFERVFRAQVNCSEYFPLFLATLWVAGIFFHEGAAA
SQ  LCGLFYLFARLRYFQGYARSAQLRLTPLYASARALWLLVAMAALGLLVHFLPGTLRTALFRWLQMLLPMA
//
ID  Q925U2;
PN  Leukotriene C4 synthase;
GN  Ltc4s;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Nucleus membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}.
DR  UNIPROT: Q925U2;
DR  UNIPROT: G3V6E6;
DR  Pfam: PF01124;
DR  PROSITE: PS01297;
DE  Function: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity (PubMed:12445492). Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions (By similarity). {ECO:0000250|UniProtKB:Q16873, ECO:0000269|PubMed:12445492}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0008047;
GO  GO:0043295;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0042802;
GO  GO:0004464;
GO  GO:0008289;
GO  GO:0044877;
GO  GO:0071222;
GO  GO:0071299;
GO  GO:0019370;
GO  GO:0006691;
GO  GO:0042759;
GO  GO:0048678;
GO  GO:0010035;
GO  GO:0032496;
GO  GO:0009410;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q16873};
SQ  MKEETALLATVTLLGVLLQAYFSLQVISARRTFHVSPPLTSGPPEFERVFRAQVNCSEYFPLFLATLWVAGIFFHEGAAA
SQ  LCGLFYLFARLRYFQGYARSAQHRLDPLYASARALWLLVAMAALGLLVHFLPGTLRAALFRWLQVLLPMA
//
ID  O75342;
PN  Arachidonate 12-lipoxygenase, 12R-type;
GN  ALOX12B;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9837935}.
DR  UNIPROT: O75342;
DR  Pfam: PF00305;
DR  Pfam: PF01477;
DR  PROSITE: PS00711;
DR  PROSITE: PS00081;
DR  PROSITE: PS51393;
DR  PROSITE: PS50095;
DR  OMIM: 242100;
DR  OMIM: 603741;
DR  DisGeNET: 242;
DE  Function: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:9837935, PubMed:9618483, PubMed:21558561). In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins (PubMed:21558561). Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss (PubMed:21558561). May also play a role in the regulation of the expression of airway mucins (PubMed:22441738). {ECO:0000269|PubMed:21558561, ECO:0000269|PubMed:22441738, ECO:0000269|PubMed:9618483, ECO:0000269|PubMed:9837935}.
DE  Disease: Ichthyosis, congenital, autosomal recessive 2 (ARCI2) [MIM:242100]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non- bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. {ECO:0000269|PubMed:11773004, ECO:0000269|PubMed:15629692, ECO:0000269|PubMed:16116617, ECO:0000269|PubMed:19131948, ECO:0000269|PubMed:19890349}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9BYJ1; IntAct: EBI-6925923; Score: 0.47
DE  Interaction: P22735; IntAct: EBI-6926188; Score: 0.27
DE  Interaction: P19838; IntAct: EBI-11322719; Score: 0.35
DE  Interaction: O43309; IntAct: EBI-21572679; Score: 0.35
DE  Interaction: O94842; IntAct: EBI-21572856; Score: 0.35
DE  Interaction: P01160; IntAct: EBI-21572983; Score: 0.35
DE  Interaction: P02794; IntAct: EBI-21573202; Score: 0.35
DE  Interaction: Q96IK5; IntAct: EBI-21574693; Score: 0.35
DE  Interaction: Q9NU19; IntAct: EBI-21575852; Score: 0.35
DE  Interaction: Q15915; IntAct: EBI-21696712; Score: 0.35
DE  Interaction: Q8IW40; IntAct: EBI-21747275; Score: 0.35
DE  Interaction: Q96ER9; IntAct: EBI-21756041; Score: 0.35
DE  Interaction: Q14943; IntAct: EBI-21772679; Score: 0.35
DE  Interaction: Q2M243; IntAct: EBI-21790384; Score: 0.35
DE  Interaction: Q9H3H5; IntAct: EBI-21790524; Score: 0.35
DE  Interaction: Q7L190; IntAct: EBI-21790421; Score: 0.35
DE  Interaction: O95872; IntAct: EBI-21790341; Score: 0.35
DE  Interaction: O43918; IntAct: EBI-21790262; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0106237;
GO  GO:0004052;
GO  GO:0047677;
GO  GO:0005506;
GO  GO:0016853;
GO  GO:1990136;
GO  GO:0016829;
GO  GO:0016702;
GO  GO:0019369;
GO  GO:0046513;
GO  GO:0061436;
GO  GO:0051122;
GO  GO:0043651;
GO  GO:0034440;
GO  GO:0019372;
GO  GO:0010628;
GO  GO:0043410;
GO  GO:0070257;
GO  GO:0006497;
GO  GO:0006665;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATYKVRVATGTDLLSGTRDSISLTIVGTQGESHKQLLNHFGRDFATGAVGQYTVQCPQDLGELIIIRLHKERYAFFPKD
SQ  PWYCNYVQICAPNGRIYHFPAYQWMDGYETLALREATGKTTADDSLPVLLEHRKEEIRAKQDFYHWRVFLPGLPSYVHIP
SQ  SYRPPVRRHRNPNRPEWNGYIPGFPILINFKATKFLNLNLRYSFLKTASFFVRLGPMALAFKVRGLLDCKHSWKRLKDIR
SQ  KIFPGKKSVVSEYVAEHWAEDTFFGYQYLNGVNPGLIRRCTRIPDKFPVTDDMVAPFLGEGTCLQAELEKGNIYLADYRI
SQ  MEGIPTVELSGRKQHHCAPLCLLHFGPEGKMMPIAIQLSQTPGPDCPIFLPSDSEWDWLLAKTWVRYAEFYSHEAIAHLL
SQ  ETHLIAEAFCLALLRNLPMCHPLYKLLIPHTRYTVQINSIGRAVLLNEGGLSAKGMSLGVEGFAGVMVRALSELTYDSLY
SQ  LPNDFVERGVQDLPGYYYRDDSLAVWNALEKYVTEIITYYYPSDAAVEGDPELQSWVQEIFKECLLGRESSGFPRCLRTV
SQ  PELIRYVTIVIYTCSAKHAAVNTGQMEFTAWMPNFPASMRNPPIQTKGLTTLETFMDTLPDVKTTCITLLVLWTLSREPD
SQ  DRRPLGHFPDIHFVEEAPRRSIEAFRQRLNQISHDIRQRNKCLPIPYYYLDPVLIENSISI
//
ID  O70582;
PN  Arachidonate 12-lipoxygenase, 12R-type;
GN  Alox12b;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9837935}.
DR  UNIPROT: O70582;
DR  Pfam: PF00305;
DR  Pfam: PF01477;
DR  PROSITE: PS00711;
DR  PROSITE: PS00081;
DR  PROSITE: PS51393;
DR  PROSITE: PS50095;
DE  Function: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:16129665). Does not convert arachidonic acid to (12R)-hydroperoxyeicosatetraenoic acid/(12R)-HPETE (PubMed:10100631, PubMed:11256953). In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega- hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss (PubMed:17403930, PubMed:17429434, PubMed:21558561). May also play a role in the regulation of the expression of airway mucins (By similarity). {ECO:0000250|UniProtKB:O75342, ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953, ECO:0000269|PubMed:16129665, ECO:0000269|PubMed:17403930, ECO:0000269|PubMed:17429434, ECO:0000269|PubMed:21558561}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0106237;
GO  GO:0004052;
GO  GO:0047677;
GO  GO:0003824;
GO  GO:0005506;
GO  GO:1990136;
GO  GO:0016702;
GO  GO:0019369;
GO  GO:0046513;
GO  GO:0061436;
GO  GO:0051122;
GO  GO:0043651;
GO  GO:0034440;
GO  GO:0019372;
GO  GO:0010628;
GO  GO:0043410;
GO  GO:0070257;
GO  GO:0006497;
GO  GO:0006665;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATYKVKVATGTDFFSGTLDSISLTIVGTQGESHKQRLNHFGRDFATGAVDDYTVQCQQDLGELIIIRLHKEPHSFLAKD
SQ  PWYCNYVQICAPDCRVYHFPAYQWMDGYETLALREATGKITADDTLPILLEHRQEEIRAKKDFYHWRVFVPGLPNYVDIP
SQ  SYHPPPRRCRNPNRPEWDGYIPGFPILINIKATRFLNSNLRFSFVKTASFFYRLGPMALAFKLRGLVDRKRSWKRLKDIK
SQ  NIFPATKSVVSEYVAEHWTEDSFFGYQYLNGINPGLIRRCTQIPDKFPVTDEMVAPFLGEGTCLQAELERGNIYLADYRI
SQ  LDGIPTVELNGQQQHHCAPMCLLHFGPDGNMMPIAIQLSQTPGPDCPIFLPNDSEWDWLLAKTWVRYAEFYSHEAVAHLL
SQ  ESHLIGEAFCLALLRNLPMCHPLYKLLIPHTRYNVQINSIGRALLLNKGGLSARAMSLGLEGFAQVMVRGLSELTYKSLC
SQ  IPNDFVERGVQDLPGYYFRDDSLAVWYAMERYVTEIITYYYPNDAAVEGDPELQCWVQEIFKECLLGRESSGFPTCLRTI
SQ  PELIEYVTMVMYTCSARHAAVNSGQLEYTSWMPNFPSSMRNPPMQTKGLTTLQTYMDTLPDVKTTCIVLLVLWTLCREPD
SQ  DRRPLGHFPDIHFVEEGPRRSIEAFRQNLNQISHNIRQRNKCLTLPYYYLDPVLIENSISI
//
ID  Q2KMM4;
PN  Arachidonate 12-lipoxygenase, 12R-type;
GN  Alox12b;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75342}.
DR  UNIPROT: Q2KMM4;
DR  UNIPROT: Q2KMM5;
DR  Pfam: PF00305;
DR  Pfam: PF01477;
DR  PROSITE: PS00711;
DR  PROSITE: PS00081;
DR  PROSITE: PS51393;
DR  PROSITE: PS50095;
DE  Function: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:23382512). In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega- hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. May also play a role in the regulation of the expression of airway mucins (By similarity). {ECO:0000250|UniProtKB:O75342, ECO:0000269|PubMed:23382512}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0106237;
GO  GO:0004052;
GO  GO:0047677;
GO  GO:0005506;
GO  GO:1990136;
GO  GO:0016702;
GO  GO:0019369;
GO  GO:0046513;
GO  GO:0061436;
GO  GO:0051122;
GO  GO:0043651;
GO  GO:0034440;
GO  GO:0019372;
GO  GO:0010628;
GO  GO:0043410;
GO  GO:0070257;
GO  GO:0006497;
GO  GO:0006665;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATYKVKVATGTDFFSGTLDSISLTIVGTQGESHKQRLNHFGRDFATGAVDDYTVQCQQDLGELIIIRLHKEPHSFLPKD
SQ  PWYCNYVQICAPNCRVYHFPAYQWMDGYETLSLREATGKTTADDTLPILLEHRQEEIRAKKDFYHWRVFVPGLPNYVDIP
SQ  SYHPPPRRCRNPNRPEWNGYIPGFPILINIKATRFLNLNLRFSFVKTASFFYRLGPMALAFKLRGLVDRKRSWKRLKDIK
SQ  NIFPATKTVVSEYVAEHWTEDSFFGYQYLNGINPGHIRRCMQIPDKFPVTDEMVAPFLGEGTCLQAELEKGNIYLADYRI
SQ  LDGIPTVELNGQKQHHCAPICLLHFGPDGNMMPIAIQLSQTPGPDCPIFLPNDSEWDWLLAKTWVRYAEFYSHEAVAHLL
SQ  ESHLIGEAFCLALLRNLPMCHPLYKLLIPHTRYNVQINSIGRALLLNKGGLSARAMSLGLEGFAQVMVRGLSELTYKSLC
SQ  IPNDFVERGVQDLPGYYFRDDSLAVWYAMERYVTEIITYYYPNDAAVEGDPELQCWVQEIFKECLLERESSGFPTCLRTV
SQ  PELIEYVTMVMYTCSARHAAVNTGQLEYTSWMPNFPSSMRNPPMQSKGLTTLQTFMDTLPDVKTTCIVLLVLWTLCREPD
SQ  DRRPLGHFPDIHFVEEAPRRSMEAFRQNLNQISHNIRQRNKCLNLPYYYLDPVLIENSISI
//
ID  P07948;
PN  Tyrosine-protein kinase Lyn;
GN  LYN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane. Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus. Membrane {ECO:0000305}; Lipid- anchor {ECO:0000305}. Note=Accumulates in the nucleus by inhibition of CRM1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the plasma membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport. Detected on plasma membrane lipid rafts.
DR  UNIPROT: P07948;
DR  UNIPROT: A0AVQ5;
DR  PDB: 1W1F;
DR  PDB: 1WA7;
DR  PDB: 3A4O;
DR  PDB: 5XY1;
DR  PDB: 6NMW;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DR  OMIM: 165120;
DR  DisGeNET: 4067;
DE  Function: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Mediates phosphorylation of the BCR-ABL fusion protein. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3- kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-107'; this enhances binding of SCIMP to TLR4, promoting the phosphorylation of TLR4, and a selective cytokine response to lipopolysaccharide in macrophages (By similarity). Phosphorylates CLNK (By similarity). Phosphorylates BCAR1/CAS and NEDD9/HEF1 (PubMed:9020138). {ECO:0000250|UniProtKB:P25911, ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:10748115, ECO:0000269|PubMed:10891478, ECO:0000269|PubMed:11435302, ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:11825908, ECO:0000269|PubMed:14726379, ECO:0000269|PubMed:15795233, ECO:0000269|PubMed:16467205, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:17977829, ECO:0000269|PubMed:18056483, ECO:0000269|PubMed:18070987, ECO:0000269|PubMed:18235045, ECO:0000269|PubMed:18577747, ECO:0000269|PubMed:18802065, ECO:0000269|PubMed:19290919, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:7687428, ECO:0000269|PubMed:9020138}.
DE  Disease: Note=Constitutively phosphorylated and activated in cells from a number of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) patients. Mediates phosphorylation of the BCR-ABL fusion protein. Abnormally elevated expression levels or activation of LYN signaling may play a role in survival and proliferation of some types of cancer cells.
DE  Reference Proteome: Yes;
DE  Interaction: O92972; IntAct: EBI-710647; Score: 0.59
DE  Interaction: P00533; IntAct: EBI-1188138; Score: 0.82
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q05397; IntAct: EBI-7859736; Score: 0.57
DE  Interaction: P29353; IntAct: EBI-8561534; Score: 0.44
DE  Interaction: P61980; IntAct: EBI-8561634; Score: 0.47
DE  Interaction: Q07666; IntAct: EBI-8561649; Score: 0.61
DE  Interaction: P22681; IntAct: EBI-8676674; Score: 0.56
DE  Interaction: P20273; IntAct: EBI-79477; Score: 0.50
DE  Interaction: P67870; IntAct: EBI-348799; Score: 0.00
DE  Interaction: Q99759; IntAct: EBI-362379; Score: 0.00
DE  Interaction: Q15642; IntAct: EBI-8565817; Score: 0.51
DE  Interaction: Q9HCN6; IntAct: EBI-515295; Score: 0.64
DE  Interaction: Q8R5G7; IntAct: EBI-621597; Score: 0.56
DE  Interaction: P14317; IntAct: EBI-7563395; Score: 0.50
DE  Interaction: P03407; IntAct: EBI-7355086; Score: 0.40
DE  Interaction: Q9QPN3; IntAct: EBI-7355202; Score: 0.40
DE  Interaction: P04604; IntAct: EBI-7355408; Score: 0.40
DE  Interaction: P26660; IntAct: EBI-710635; Score: 0.40
DE  Interaction: P27958; IntAct: EBI-710656; Score: 0.70
DE  Interaction: Q913V3; IntAct: EBI-710808; Score: 0.40
DE  Interaction: Q9WMX2; IntAct: EBI-710977; Score: 0.67
DE  Interaction: P07948; IntAct: EBI-762547; Score: 0.44
DE  Interaction: Q9QWY8; IntAct: EBI-848100; Score: 0.40
DE  Interaction: Q90VU7; IntAct: EBI-7975448; Score: 0.40
DE  Interaction: Q13177; IntAct: EBI-7975774; Score: 0.40
DE  Interaction: Q13444; IntAct: EBI-7976419; Score: 0.61
DE  Interaction: Q9NRA0; IntAct: EBI-985362; Score: 0.44
DE  Interaction: Q8CI15; IntAct: EBI-985396; Score: 0.40
DE  Interaction: Q9JIA7; IntAct: EBI-985456; Score: 0.40
DE  Interaction: P11802; IntAct: EBI-1063758; Score: 0.00
DE  Interaction: P46527; IntAct: EBI-1201624; Score: 0.54
DE  Interaction: Q06649; IntAct: EBI-8637397; Score: 0.35
DE  Interaction: P22575; IntAct: EBI-7815650; Score: 0.56
DE  Interaction: Q8K4S7; IntAct: EBI-8667105; Score: 0.40
DE  Interaction: P48023; IntAct: EBI-2481502; Score: 0.40
DE  Interaction: Q80X56; IntAct: EBI-2561540; Score: 0.40
DE  Interaction: P05556; IntAct: EBI-2609328; Score: 0.43
DE  Interaction: P13612; IntAct: EBI-2609459; Score: 0.43
DE  Interaction: A0A3G5L2D0; IntAct: EBI-2865064; Score: 0.00
DE  Interaction: Q7CJG3; IntAct: EBI-2865076; Score: 0.00
DE  Interaction: Q8IZP0; IntAct: EBI-8050357; Score: 0.44
DE  Interaction: P31994; IntAct: EBI-7044322; Score: 0.35
DE  Interaction: Q9NWQ8; IntAct: EBI-7731789; Score: 0.64
DE  Interaction: P40763; IntAct: EBI-11358894; Score: 0.35
DE  Interaction: P06239; IntAct: EBI-11359535; Score: 0.53
DE  Interaction: P12931; IntAct: EBI-11359552; Score: 0.67
DE  Interaction: Q9WNA9; IntAct: EBI-7555573; Score: 0.44
DE  Interaction: Q7Z7K6; IntAct: EBI-7613090; Score: 0.40
DE  Interaction: Q96PU4; IntAct: EBI-6051501; Score: 0.40
DE  Interaction: P05106; IntAct: EBI-6123588; Score: 0.40
DE  Interaction: P05107; IntAct: EBI-6123608; Score: 0.40
DE  Interaction: P11049; IntAct: EBI-6139088; Score: 0.50
DE  Interaction: P29350; IntAct: EBI-6139770; Score: 0.40
DE  Interaction: P21145; IntAct: EBI-6264198; Score: 0.35
DE  Interaction: P25063; IntAct: EBI-6267068; Score: 0.50
DE  Interaction: P27361; IntAct: EBI-6267068; Score: 0.35
DE  Interaction: P28482; IntAct: EBI-6267068; Score: 0.35
DE  Interaction: Q8NF50; IntAct: EBI-6390188; Score: 0.40
DE  Interaction: P08238; IntAct: EBI-6424409; Score: 0.56
DE  Interaction: P33993; IntAct: EBI-6868885; Score: 0.59
DE  Interaction: P63244; IntAct: EBI-9072792; Score: 0.40
DE  Interaction: P05771; IntAct: EBI-9072836; Score: 0.40
DE  Interaction: P10275; IntAct: EBI-9451242; Score: 0.44
DE  Interaction: Q13480; IntAct: EBI-9457390; Score: 0.44
DE  Interaction: P10721; IntAct: EBI-9466280; Score: 0.44
DE  Interaction: P08581; IntAct: EBI-9473641; Score: 0.44
DE  Interaction: O95684; IntAct: EBI-11001986; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11004631; Score: 0.35
DE  Interaction: Q9NQW6; IntAct: EBI-11009421; Score: 0.35
DE  Interaction: Q61879; IntAct: EBI-11041929; Score: 0.35
DE  Interaction: Q9D620; IntAct: EBI-11042984; Score: 0.35
DE  Interaction: Q99598; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q80X90; IntAct: EBI-11053320; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062262; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: Q8BWU5; IntAct: EBI-11101768; Score: 0.35
DE  Interaction: Q68FF7; IntAct: EBI-11102719; Score: 0.35
DE  Interaction: Q9H0B6; IntAct: EBI-11140662; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q71U36; IntAct: EBI-11897464; Score: 0.35
DE  Interaction: Q08857; IntAct: EBI-13940921; Score: 0.50
DE  Interaction: P16671; IntAct: EBI-13940953; Score: 0.50
DE  Interaction: P09067; IntAct: EBI-21543288; Score: 0.35
DE  Interaction: Q08345; IntAct: EBI-22034655; Score: 0.35
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: Q13443; IntAct: EBI-21225857; Score: 0.44
DE  Interaction: O43184; IntAct: EBI-21225965; Score: 0.56
DE  Interaction: Q9H013; IntAct: EBI-21226800; Score: 0.44
DE  Interaction: Q6UWF3; IntAct: EBI-21230084; Score: 0.50
DE  Interaction: Q8N6Q3; IntAct: EBI-21402192; Score: 0.35
DE  Interaction: Q969Q1; IntAct: EBI-22019674; Score: 0.00
DE  Interaction: Q9BYV6; IntAct: EBI-22023360; Score: 0.00
DE  Interaction: Q5U3Y8; IntAct: EBI-22239142; Score: 0.40
DE  Interaction: Q13115; IntAct: EBI-25372724; Score: 0.35
DE  Interaction: O43172; IntAct: EBI-25379971; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-25379971; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-25379971; Score: 0.35
DE  Interaction: P08631; IntAct: EBI-25379971; Score: 0.53
DE  Interaction: P09769; IntAct: EBI-25379971; Score: 0.53
DE  Interaction: P15924; IntAct: EBI-25379971; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-25379971; Score: 0.35
DE  Interaction: Q8IX12; IntAct: EBI-25379971; Score: 0.35
DE  Interaction: Q9NWB6; IntAct: EBI-25379971; Score: 0.35
DE  Interaction: Q9UQ35; IntAct: EBI-25379971; Score: 0.35
DE  Interaction: Q6P2Q9; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q9BUQ8; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q58FF7; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: P29144; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q8NEV1; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: P84090; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q02413; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q12874; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q15029; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q15428; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q15459; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q8IWX8; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q99873; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q9Y2W1; IntAct: EBI-25390944; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
DE  Interaction: P01023; IntAct: EBI-25829928; Score: 0.56
DE  Interaction: P50570; IntAct: EBI-25844552; Score: 0.56
DE  Interaction: Q96GW7; IntAct: EBI-25875537; Score: 0.56
DE  Interaction: Q96L34; IntAct: EBI-25875527; Score: 0.56
DE  Interaction: Q9BS26; IntAct: EBI-25875519; Score: 0.56
DE  Interaction: P07602; IntAct: EBI-25875511; Score: 0.56
DE  Interaction: P27986; IntAct: EBI-25875503; Score: 0.56
DE  Interaction: P51608; IntAct: EBI-25875818; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25930624; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25936566; Score: 0.56
DE  Interaction: P37840; IntAct: EBI-25940462; Score: 0.56
DE  Interaction: Q8NDB2; IntAct: EBI-26450927; Score: 0.59
DE  Interaction: Q9BZD6; IntAct: EBI-26604023; Score: 0.44
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: P63252; IntAct: EBI-28956270; Score: 0.27
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: O43187; IntAct: EBI-28930939; Score: 0.35
DE  Interaction: P51451; IntAct: EBI-28931687; Score: 0.35
DE  Interaction: Q8N1W1; IntAct: EBI-28931687; Score: 0.35
DE  Interaction: Q6NXT1; IntAct: EBI-28931687; Score: 0.35
DE  Interaction: Q12774; IntAct: EBI-28931687; Score: 0.35
DE  Interaction: O75674; IntAct: EBI-28931687; Score: 0.35
DE  Interaction: Q7Z695; IntAct: EBI-28941998; Score: 0.35
DE  Interaction: Q86V86; IntAct: EBI-28942203; Score: 0.35
DE  Interaction: Q8TEA7; IntAct: EBI-28943849; Score: 0.35
DE  Interaction: Q8TF76; IntAct: EBI-28943924; Score: 0.35
DE  Interaction: Q9NSY0; IntAct: EBI-28946547; Score: 0.35
DE  Interaction: Q9BYF1; IntAct: EBI-28953063; Score: 0.44
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
GO  GO:0005912;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030666;
GO  GO:0070062;
GO  GO:0031234;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0034666;
GO  GO:0043231;
GO  GO:0005765;
GO  GO:0045121;
GO  GO:0030061;
GO  GO:0005758;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0099091;
GO  GO:0005524;
GO  GO:0019899;
GO  GO:0046875;
GO  GO:0043015;
GO  GO:0043208;
GO  GO:0005178;
GO  GO:0016301;
GO  GO:0004715;
GO  GO:0051219;
GO  GO:0140031;
GO  GO:0005161;
GO  GO:0004713;
GO  GO:0097110;
GO  GO:0017124;
GO  GO:0005102;
GO  GO:0044325;
GO  GO:0031625;
GO  GO:0002250;
GO  GO:0001782;
GO  GO:0050853;
GO  GO:0038159;
GO  GO:0030154;
GO  GO:0006974;
GO  GO:0031668;
GO  GO:0034605;
GO  GO:0071300;
GO  GO:0097028;
GO  GO:0048013;
GO  GO:0030218;
GO  GO:0002774;
GO  GO:0002431;
GO  GO:0038095;
GO  GO:0038096;
GO  GO:0060397;
GO  GO:0002244;
GO  GO:0002553;
GO  GO:0002768;
GO  GO:0045087;
GO  GO:0035556;
GO  GO:0050900;
GO  GO:0031663;
GO  GO:0030889;
GO  GO:0008285;
GO  GO:0070373;
GO  GO:0050777;
GO  GO:0002862;
GO  GO:1902532;
GO  GO:0043407;
GO  GO:0070667;
GO  GO:0002762;
GO  GO:0001933;
GO  GO:0034136;
GO  GO:0034144;
GO  GO:0031175;
GO  GO:0014003;
GO  GO:0018108;
GO  GO:0002576;
GO  GO:1902961;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:2000670;
GO  GO:0060369;
GO  GO:0060252;
GO  GO:0070668;
GO  GO:0010976;
GO  GO:0070447;
GO  GO:0043552;
GO  GO:0001934;
GO  GO:0070304;
GO  GO:0042531;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0002902;
GO  GO:0050855;
GO  GO:0033628;
GO  GO:0001817;
GO  GO:0070372;
GO  GO:0045646;
GO  GO:0033003;
GO  GO:0043304;
GO  GO:0090025;
GO  GO:0090330;
GO  GO:0001932;
GO  GO:0051279;
GO  GO:0043200;
GO  GO:0048678;
GO  GO:0009743;
GO  GO:0009725;
GO  GO:0032868;
GO  GO:0014070;
GO  GO:0006991;
GO  GO:0009636;
GO  GO:0009410;
GO  GO:0007165;
GO  GO:0002223;
GO  GO:0031295;
GO  GO:0002513;
GO  GO:0034142;
GO  GO:0007169;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:18817770};
SQ  MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPD
SQ  DLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESET
SQ  LKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAW
SQ  EIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITE
SQ  YMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAR
SQ  EGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCW
SQ  KEKAEERPTFDYLQSVLDDFYTATEGQYQQQP
//
ID  P25911;
PN  Tyrosine-protein kinase Lyn;
GN  Lyn;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P07948}; Lipid-anchor {ECO:0000250|UniProtKB:P07948}. Note=Accumulates in the nucleus by inhibition of Crm1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the cell membrane occurs in a kinase domain- dependent but kinase activity independent manner and is mediated by exocytic vesicular transport (By similarity). {ECO:0000250}.
DR  UNIPROT: P25911;
DR  UNIPROT: Q62127;
DR  PDB: 2ZV7;
DR  PDB: 2ZV8;
DR  PDB: 2ZV9;
DR  PDB: 2ZVA;
DR  PDB: 4TZI;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DE  Function: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-96'; this enhances binding of SCIMP to TLR4, promoting the phosphorylation of TLR4, and a selective cytokine response to lipopolysaccharide in macrophages (PubMed:28098138). Phosphorylates CLNK (PubMed:12681493). Phosphorylates BCAR1/CAS and NEDD9/HEF1 (By similarity). {ECO:0000250|UniProtKB:P07948, ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10594694, ECO:0000269|PubMed:10640270, ECO:0000269|PubMed:10672044, ECO:0000269|PubMed:11007759, ECO:0000269|PubMed:11435302, ECO:0000269|PubMed:11672542, ECO:0000269|PubMed:12077122, ECO:0000269|PubMed:12681493, ECO:0000269|PubMed:12874221, ECO:0000269|PubMed:14525964, ECO:0000269|PubMed:14726379, ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:16034130, ECO:0000269|PubMed:16116174, ECO:0000269|PubMed:16249387, ECO:0000269|PubMed:16272347, ECO:0000269|PubMed:16731527, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:19492092, ECO:0000269|PubMed:20189992, ECO:0000269|PubMed:20385881, ECO:0000269|PubMed:28098138, ECO:0000269|PubMed:7513017, ECO:0000269|PubMed:7584145, ECO:0000269|PubMed:7585947, ECO:0000269|PubMed:8128248, ECO:0000269|PubMed:8621063, ECO:0000269|PubMed:8629002, ECO:0000269|PubMed:9036984, ECO:0000269|PubMed:9064343, ECO:0000269|PubMed:9252121, ECO:0000269|PubMed:9469421, ECO:0000269|PubMed:9480991, ECO:0000269|PubMed:9547345, ECO:0000269|PubMed:9573010, ECO:0000269|PubMed:9590210, ECO:0000269|PubMed:9601638}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9QZE2; IntAct: EBI-8631097; Score: 0.40
DE  Interaction: Q3UND0; IntAct: EBI-8631358; Score: 0.40
DE  Interaction: O35601; IntAct: EBI-8631376; Score: 0.40
DE  Interaction: P49710; IntAct: EBI-7064072; Score: 0.70
DE  Interaction: Q60598; IntAct: EBI-7064061; Score: 0.31
DE  Interaction: P81122; IntAct: EBI-7064122; Score: 0.31
DE  Interaction: Q64355; IntAct: EBI-7064111; Score: 0.52
DE  Interaction: Q61140; IntAct: EBI-7064099; Score: 0.31
DE  Interaction: O70469; IntAct: EBI-7064144; Score: 0.31
DE  Interaction: Q62418; IntAct: EBI-7064133; Score: 0.31
DE  Interaction: Q8R4X3; IntAct: EBI-651232; Score: 0.37
DE  Interaction: P61979; IntAct: EBI-658993; Score: 0.37
DE  Interaction: Q91WK7; IntAct: EBI-659013; Score: 0.37
DE  Interaction: Q9Z0Z7; IntAct: EBI-659023; Score: 0.37
DE  Interaction: B9EKI5; IntAct: EBI-688631; Score: 0.37
DE  Interaction: P46109; IntAct: EBI-8552062; Score: 0.40
DE  Interaction: Q8CIH5; IntAct: EBI-8659012; Score: 0.52
DE  Interaction: Q91YX7; IntAct: EBI-8659034; Score: 0.40
DE  Interaction: P26450; IntAct: EBI-8659072; Score: 0.40
DE  Interaction: P14753; IntAct: EBI-8688220; Score: 0.35
DE  Interaction: Q9XC73; IntAct: EBI-16463675; Score: 0.35
DE  Interaction: P11911; IntAct: EBI-15582283; Score: 0.27
DE  Interaction: P29351; IntAct: EBI-15753859; Score: 0.40
DE  Interaction: Q9Z1S8; IntAct: EBI-15753841; Score: 0.50
DE  Interaction: O35305; IntAct: EBI-15753841; Score: 0.35
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0005912;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0034666;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0030061;
GO  GO:0005758;
GO  GO:0031966;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0099091;
GO  GO:0032991;
GO  GO:0005524;
GO  GO:0019899;
GO  GO:0046875;
GO  GO:0005128;
GO  GO:0043015;
GO  GO:0043208;
GO  GO:0005178;
GO  GO:0004715;
GO  GO:0051219;
GO  GO:0140031;
GO  GO:0005161;
GO  GO:0004672;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0097110;
GO  GO:0017124;
GO  GO:0005102;
GO  GO:0044325;
GO  GO:0031625;
GO  GO:0002250;
GO  GO:0001782;
GO  GO:0050853;
GO  GO:0038159;
GO  GO:0030154;
GO  GO:0006974;
GO  GO:0031668;
GO  GO:0034605;
GO  GO:0071300;
GO  GO:0097028;
GO  GO:0030218;
GO  GO:0002774;
GO  GO:0002431;
GO  GO:0002244;
GO  GO:0042541;
GO  GO:0030097;
GO  GO:0002553;
GO  GO:0002768;
GO  GO:0045087;
GO  GO:0035556;
GO  GO:0031663;
GO  GO:0030889;
GO  GO:0008285;
GO  GO:0070373;
GO  GO:1902532;
GO  GO:0043407;
GO  GO:0070667;
GO  GO:0002762;
GO  GO:0001933;
GO  GO:0034136;
GO  GO:0034144;
GO  GO:0031175;
GO  GO:0014003;
GO  GO:0018108;
GO  GO:0002576;
GO  GO:1902961;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:2000670;
GO  GO:0060369;
GO  GO:0060252;
GO  GO:0070668;
GO  GO:0010976;
GO  GO:0070447;
GO  GO:0043552;
GO  GO:0042327;
GO  GO:0001934;
GO  GO:0070304;
GO  GO:0042531;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0002902;
GO  GO:0050855;
GO  GO:0033628;
GO  GO:0001817;
GO  GO:0070372;
GO  GO:0045646;
GO  GO:0050727;
GO  GO:0033003;
GO  GO:0043304;
GO  GO:0090025;
GO  GO:0090330;
GO  GO:0051279;
GO  GO:0043200;
GO  GO:0048678;
GO  GO:0009743;
GO  GO:0009725;
GO  GO:0032868;
GO  GO:0014070;
GO  GO:0006991;
GO  GO:0009636;
GO  GO:0009410;
GO  GO:0007165;
GO  GO:0002513;
GO  GO:0034142;
GO  GO:0007169;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGCIKSKRKDNLNDDEVDSKTQPVRNTDRTIYVRDPTSNKQQRPVPEFHLLPGQRFQTKDPEEQGDIVVALYPYDGIHPD
SQ  DLSFKKGEKMKVLEEHGEWWKAKSLSSKREGFIPSNYVAKVNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESET
SQ  LKGSFSLSVRDYDPMHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQSDGLCRRLEKACISPKPQKPWDKDAW
SQ  EIPRESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITE
SQ  FMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAR
SQ  EGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMSALSQGYRMPRMENCPDELYDIMKMCW
SQ  KEKAEERPTFDYLQSVLDDFYTATEGQYQQQP
//
ID  Q07014;
PN  Tyrosine-protein kinase Lyn;
GN  Lyn;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P07948}; Lipid-anchor {ECO:0000250|UniProtKB:P07948}. Note=Accumulates in the nucleus by inhibition of Crm1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the cell membrane occurs in a kinase domain- dependent but kinase activity independent manner and is mediated by exocytic vesicular transport (By similarity). {ECO:0000250}.
DR  UNIPROT: Q07014;
DR  UNIPROT: Q63320;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DE  Function: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B (By similarity). Phosphorylates LPXN on 'Tyr-72' (By similarity). Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-96'; this enhances binding of SCIMP to TLR4, promoting the phosphorylation of TLR4, and a selective cytokine response to lipopolysaccharide in macrophages (By similarity). Phosphorylates CLNK (By similarity). Phosphorylates BCAR1/CAS and NEDD9/HEF1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P07948, ECO:0000250|UniProtKB:P25911}.
DE  Reference Proteome: Yes;
DE  Interaction: P28867; IntAct: EBI-8680025; Score: 0.35
DE  Interaction: Q06649; IntAct: EBI-8637352; Score: 0.27
DE  Interaction: Q1PS21; IntAct: EBI-6869828; Score: 0.40
DE  Interaction: Q13523; IntAct: EBI-22240189; Score: 0.35
DE  Interaction: P07333; IntAct: EBI-22241657; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-22247578; Score: 0.35
DE  Interaction: Q6ZW31; IntAct: EBI-22259810; Score: 0.35
DE  Interaction: O15357; IntAct: EBI-22261203; Score: 0.35
GO  GO:0005912;
GO  GO:0005737;
GO  GO:0031234;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0034666;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0030061;
GO  GO:0005758;
GO  GO:0031966;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0099091;
GO  GO:0032991;
GO  GO:0005524;
GO  GO:0019899;
GO  GO:0046875;
GO  GO:0043015;
GO  GO:0043208;
GO  GO:0005178;
GO  GO:0016301;
GO  GO:0004715;
GO  GO:0051219;
GO  GO:0140031;
GO  GO:0005161;
GO  GO:0004672;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0097110;
GO  GO:0017124;
GO  GO:0005102;
GO  GO:0044325;
GO  GO:0031625;
GO  GO:0002250;
GO  GO:0001782;
GO  GO:0050853;
GO  GO:0038159;
GO  GO:0030154;
GO  GO:0006974;
GO  GO:0031668;
GO  GO:0034605;
GO  GO:0071300;
GO  GO:0097028;
GO  GO:0030218;
GO  GO:0002774;
GO  GO:0002431;
GO  GO:0002244;
GO  GO:0030097;
GO  GO:0002553;
GO  GO:0002768;
GO  GO:0045087;
GO  GO:0035556;
GO  GO:0031663;
GO  GO:0030889;
GO  GO:0008285;
GO  GO:0070373;
GO  GO:1902532;
GO  GO:0043407;
GO  GO:0070667;
GO  GO:0002762;
GO  GO:0001933;
GO  GO:0034136;
GO  GO:0034144;
GO  GO:0031175;
GO  GO:0014003;
GO  GO:0018108;
GO  GO:0002576;
GO  GO:1902961;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:2000670;
GO  GO:0060369;
GO  GO:0060252;
GO  GO:0070668;
GO  GO:0010976;
GO  GO:0070447;
GO  GO:0043552;
GO  GO:0042327;
GO  GO:0001934;
GO  GO:0070304;
GO  GO:0042531;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:0002902;
GO  GO:0050855;
GO  GO:0033628;
GO  GO:0001817;
GO  GO:0070372;
GO  GO:0045646;
GO  GO:0050727;
GO  GO:0033003;
GO  GO:0043304;
GO  GO:0090025;
GO  GO:0090330;
GO  GO:0051279;
GO  GO:0043200;
GO  GO:0048678;
GO  GO:0009743;
GO  GO:0009725;
GO  GO:0032868;
GO  GO:0014070;
GO  GO:0043434;
GO  GO:0006991;
GO  GO:0009636;
GO  GO:0009410;
GO  GO:0002513;
GO  GO:0034142;
GO  GO:0007169;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGCIKSKRKDNLNDDGVDMKTQPVRNTDRTIYVRDPTSNKQQRPVPESQLLPGQRFQAKDPEEQGDIVVALYPYDGIHPD
SQ  DLSFKKGEKMKVLEEHGEWWKAKSLSSKREGFIPSNYVAKVNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESET
SQ  LKGSFSLSVRDYDPMHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQSDGLCRRLEKACISPKPQKPWDKDAW
SQ  EIPRESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSAQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITE
SQ  FMAKGSLLDFLKSDEGSKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAR
SQ  EGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRMENCPDELYDIMKMCW
SQ  KESAEERPTFDYLQSVLDDFYTATEGQYQQQP
//
ID  Q3MHR0;
PN  Acyl-protein thioesterase 1;
GN  LYPLA1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O75608}. Cell membrane {ECO:0000250|UniProtKB:O75608}. Nucleus membrane {ECO:0000250|UniProtKB:O75608}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O75608}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000250|UniProtKB:O75608}.
DR  UNIPROT: Q3MHR0;
DR  Pfam: PF02230;
DE  Function: Acts as a acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (By similarity). Has depalmitoylating activity toward KCNMA1 (By similarity). Could also depalmitoylate ADRB2 (By similarity). Acts as a lysophospholipase hydrolyzing various lysophospholipids including lysophosphatidylcholine (lyso-PC), lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso- PI) and lysophosphatidylserine (lyso-PS) (By similarity). Has much higher thioesterase activity than lysophospholipase activity (By similarity). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (By similarity). {ECO:0000250|UniProtKB:O75608, ECO:0000250|UniProtKB:P70470}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0052689;
GO  GO:0004622;
GO  GO:0008474;
GO  GO:0004620;
GO  GO:0006631;
GO  GO:0002084;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCGNNMSAPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSAHIKYICPHAPVMPVTLNMNMAMPSWFDIIGLSP
SQ  DSLEDETGIKQAAENVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGV
SQ  NRDISILQCHGDLDPLVPLMFGSLTAEKLKTLVNPANVTFRTYAGMMHSSCQQEMMDIKQFIDKLLPPVD
//
ID  O75608;
PN  Acyl-protein thioesterase 1;
GN  LYPLA1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:19439193}. Cell membrane {ECO:0000269|PubMed:19439193}. Nucleus membrane {ECO:0000269|PubMed:19439193}. Endoplasmic reticulum {ECO:0000269|PubMed:19439193}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000269|PubMed:19439193}.
DR  UNIPROT: O75608;
DR  UNIPROT: O43202;
DR  UNIPROT: Q9UQF9;
DR  PDB: 1FJ2;
DR  PDB: 5SYM;
DR  PDB: 6QGN;
DR  PDB: 6QGO;
DR  PDB: 6QGQ;
DR  PDB: 6QGS;
DR  Pfam: PF02230;
DR  OMIM: 605599;
DR  DisGeNET: 10434;
DE  Function: Acts as a acyl-protein thioesterase (PubMed:19439193, PubMed:20418879). Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (PubMed:20418879). Has depalmitoylating activity toward KCNMA1 (PubMed:22399288). Could also depalmitoylate ADRB2 (PubMed:27481942). Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC) (PubMed:19439193). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso- PI) and lysophosphatidylserine (lyso-PS) (By similarity). Has much higher thioesterase activity than lysophospholipase activity (PubMed:19439193). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (PubMed:21393252). {ECO:0000250|UniProtKB:P70470, ECO:0000269|PubMed:19439193, ECO:0000269|PubMed:20418879, ECO:0000269|PubMed:21393252, ECO:0000269|PubMed:22399288, ECO:0000269|PubMed:27481942}.
DE  Reference Proteome: Yes;
DE  Interaction: P40337; IntAct: EBI-1072614; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1085474; Score: 0.00
DE  Interaction: P03496; IntAct: EBI-2548141; Score: 0.37
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-24390480; Score: 0.56
DE  Interaction: Q5VUG0; IntAct: EBI-24453381; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: P29084; IntAct: EBI-21499432; Score: 0.35
DE  Interaction: Q9Y324; IntAct: EBI-21632422; Score: 0.35
DE  Interaction: Q96F44; IntAct: EBI-21673880; Score: 0.35
DE  Interaction: Q96K76; IntAct: EBI-21756437; Score: 0.35
DE  Interaction: Q15561; IntAct: EBI-21797712; Score: 0.35
DE  Interaction: P43234; IntAct: EBI-21797693; Score: 0.35
DE  Interaction: Q8N3Z0; IntAct: EBI-21937501; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0070062;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0052689;
GO  GO:0016298;
GO  GO:0004622;
GO  GO:0008474;
GO  GO:0004620;
GO  GO:0006631;
GO  GO:0042997;
GO  GO:0002084;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSP
SQ  DSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGA
SQ  NRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
//
ID  P97823;
PN  Acyl-protein thioesterase 1;
GN  Lypla1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O75608}. Cell membrane {ECO:0000250|UniProtKB:O75608}. Nucleus membrane {ECO:0000250|UniProtKB:O75608}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O75608}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000250|UniProtKB:O75608}.
DR  UNIPROT: P97823;
DR  UNIPROT: Q3TJZ0;
DR  UNIPROT: Q7TPX1;
DR  UNIPROT: Q8BWM6;
DR  Pfam: PF02230;
DE  Function: Acts as a acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (By similarity). Has depalmitoylating activity toward KCNMA1 (By similarity). Could also depalmitoylate ADRB2 (By similarity). Acts as a lysophospholipase hydrolyzing various lysophospholipids including lysophosphatidylcholine (lyso-PC), lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso- PI) and lysophosphatidylserine (lyso-PS)(PubMed:9139730). Has much higher thioesterase activity than lysophospholipase activity (By similarity). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (By similarity). {ECO:0000250|UniProtKB:O75608, ECO:0000250|UniProtKB:P70470, ECO:0000269|PubMed:9139730}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0052689;
GO  GO:0016298;
GO  GO:0004622;
GO  GO:0008474;
GO  GO:0004620;
GO  GO:0006631;
GO  GO:0042997;
GO  GO:0002084;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCGNNMSAPMPAVVPAARKATAAVIFLHGLGDTGHGWAEAFAGIKSPHIKYICPHAPVMPVTLNMNMAMPSWFDIVGLSP
SQ  DSQEDESGIKQAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFSQGPINSA
SQ  NRDISVLQCHGDCDPLVPLMFGSLTVERLKALINPANVTFKIYEGMMHSSCQQEMMDVKHFIDKLLPPID
//
ID  Q5RBR7;
PN  Acyl-protein thioesterase 1;
GN  LYPLA1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O75608}. Cell membrane {ECO:0000250|UniProtKB:O75608}. Nucleus membrane {ECO:0000250|UniProtKB:O75608}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O75608}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000250|UniProtKB:O75608}.
DR  UNIPROT: Q5RBR7;
DR  Pfam: PF02230;
DE  Function: Acts as a acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (By similarity). Has depalmitoylating activity toward KCNMA1 (By similarity). Could also depalmitoylate ADRB2 (By similarity). Acts as a lysophospholipase hydrolyzing various lysophospholipids including lysophosphatidylcholine (lyso-PC), lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso- PI) and lysophosphatidylserine (lyso-PS) (By similarity). Has much higher thioesterase activity than lysophospholipase activity (By similarity). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (By similarity). {ECO:0000250|UniProtKB:O75608, ECO:0000250|UniProtKB:P70470}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0004622;
GO  GO:0008474;
GO  GO:0004620;
GO  GO:0006631;
GO  GO:0002084;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVTLNMNMAMPSWFDIIGLSP
SQ  DSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGA
SQ  NRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
//
ID  O77821;
PN  Acyl-protein thioesterase 1;
GN  LYPLA1;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O75608}. Cell membrane {ECO:0000250|UniProtKB:O75608}. Nucleus membrane {ECO:0000250|UniProtKB:O75608}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O75608}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000250|UniProtKB:O75608}.
DR  UNIPROT: O77821;
DR  Pfam: PF02230;
DE  Function: Acts as a acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (By similarity). Has depalmitoylating activity toward KCNMA1 (By similarity). Could also depalmitoylate ADRB2 (By similarity). Acts as a lysophospholipase hydrolyzing various lysophospholipids including lysophosphatidylcholine (lyso-PC), lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso- PI) and lysophosphatidylserine (lyso-PS) (By similarity). Has much higher thioesterase activity than lysophospholipase activity (By similarity). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (By similarity). {ECO:0000250|UniProtKB:O75608, ECO:0000250|UniProtKB:P70470}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0004622;
GO  GO:0008474;
GO  GO:0004620;
GO  GO:0006631;
GO  GO:0002084;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCGNNMSAPMPAVVPAARKATAAVIFLHGLGDTGHGWAEAFAGIKSPHIKYICPHAPVMPVTLNMNMAMPSWFDIVGLSP
SQ  DSQEDESGIKQAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFSQGPINSA
SQ  NRDISVLQCHGDCDPLVPLMFGSLTVERLKALINPANVTFKIYEGMMHSSCQQEMMDVKHFIDKLLPPID
//
ID  P70470;
PN  Acyl-protein thioesterase 1;
GN  Lypla1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:9624183}. Cell membrane {ECO:0000250|UniProtKB:O75608}. Nucleus membrane {ECO:0000250|UniProtKB:O75608}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O75608}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000250|UniProtKB:O75608}.
DR  UNIPROT: P70470;
DR  Pfam: PF02230;
DE  Function: Acts as a acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (PubMed:9624183). Has depalmitoylating activity toward KCNMA1 (By similarity). Could also depalmitoylate ADRB2 (By similarity). Acts as a lysophospholipase hydrolyzing various lysophospholipids including lysophosphatidylcholine (lyso-PC), lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso- PI) and lysophosphatidylserine (lyso-PS) (PubMed:8631810, PubMed:9644627). Has much higher thioesterase activity than lysophospholipase activity (By similarity). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (By similarity). {ECO:0000250|UniProtKB:O75608, ECO:0000269|PubMed:8631810, ECO:0000269|PubMed:9624183, ECO:0000269|PubMed:9644627}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0052689;
GO  GO:0016298;
GO  GO:0004622;
GO  GO:0008474;
GO  GO:0004620;
GO  GO:0006631;
GO  GO:0042997;
GO  GO:0002084;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCGNNMSAPMPAVVPAARKATAAVIFLHGLGDTGHGWAEAFAGIKSSHIKYICPHAPVMPVTLNMSMMMPSWFDIIGLSP
SQ  DSQEDESGIKQAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFSQGPINSA
SQ  NRDISVLQCHGDCDPLVPLMFGSLTVERLKGLVNPANVTFKVYEGMMHSSCQQEMMDVKYFIDKLLPPID
//
ID  Q86UE4;
PN  Protein LYRIC;
GN  MTDH;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region. Note=In epithelial cells, recruited to tight junctions (TJ) during the maturation of the TJ complexes. A nucleolar staining may be due to nuclear targeting of an isoform lacking the transmembrane domain (By similarity). TNF-alpha causes translocation from the cytoplasm to the nucleus. {ECO:0000250}.
DR  UNIPROT: Q86UE4;
DR  UNIPROT: Q05DH2;
DR  UNIPROT: Q52QU9;
DR  UNIPROT: Q6PK07;
DR  UNIPROT: Q8TCX3;
DR  PDB: 4QMG;
DR  Pfam: PF15686;
DR  OMIM: 610323;
DR  DisGeNET: 92140;
DE  Function: Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269|PubMed:15927426, ECO:0000269|PubMed:16452207, ECO:0000269|PubMed:18316612, ECO:0000269|PubMed:19111877}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P0DTD1; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q06787; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q9NX58; IntAct: EBI-1071224; Score: 0.00
DE  Interaction: O60739; IntAct: EBI-1082494; Score: 0.00
DE  Interaction: P08473; IntAct: EBI-1389788; Score: 0.35
DE  Interaction: Q04206; IntAct: EBI-1645908; Score: 0.40
DE  Interaction: Q92793; IntAct: EBI-1645935; Score: 0.40
DE  Interaction: Q8N6M0; IntAct: EBI-2510899; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-2878124; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-3623491; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-5321912; Score: 0.44
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q9UKV8; IntAct: EBI-9682647; Score: 0.50
DE  Interaction: Q7KZF4; IntAct: EBI-9682601; Score: 0.79
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: Q9NPD3; IntAct: EBI-11126463; Score: 0.35
DE  Interaction: Q96Q45; IntAct: EBI-11377173; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q8IXJ6; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: Q5JR59; IntAct: EBI-21751261; Score: 0.35
DE  Interaction: Q9Y466; IntAct: EBI-21889982; Score: 0.35
DE  Interaction: Q9C0D3; IntAct: EBI-21893037; Score: 0.35
DE  Interaction: O75324; IntAct: EBI-21894151; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: Q9NWT6; IntAct: EBI-16813719; Score: 0.35
DE  Interaction: Q83A11; IntAct: EBI-21286679; Score: 0.37
DE  Interaction: Q8NEH6; IntAct: EBI-20933740; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P14316; IntAct: EBI-21260627; Score: 0.35
DE  Interaction: Q99558; IntAct: EBI-21261374; Score: 0.35
DE  Interaction: P28562; IntAct: EBI-25377052; Score: 0.35
DE  Interaction: Q9ULX6; IntAct: EBI-26451653; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.35
DE  Interaction: Q8NDZ4; IntAct: EBI-26597064; Score: 0.35
DE  Interaction: A0A0H3NG92; IntAct: EBI-27055968; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P43405; IntAct: EBI-28935283; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-27102375; Score: 0.35
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: P14616; IntAct: EBI-32723232; Score: 0.27
DE  Interaction: Q04912; IntAct: EBI-32725158; Score: 0.27
DE  Interaction: Q07020; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q96CW1; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: P36578; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: P46777; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: P61313; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: P05388; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q96GQ7; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: P39023; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: P62906; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q13428; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: O95782; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: O60832; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q02878; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q9UKN8; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q9NR30; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q8WXX5; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q5SSJ5; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q9Y5B9; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q9Y3B7; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q8TDN6; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q14690; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q15397; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q03426; IntAct: EBI-34580762; Score: 0.35
DE  Interaction: Q8IYB3; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q08211; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q9NW13; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q8TDD1; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: O76021; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: P18124; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q9P2E9; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q13247; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q9Y4P3; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q9UN81; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q9UKV3; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: P51114; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q9BRJ6; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q99848; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: P46087; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: O95793; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q9Y4W2; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q08945; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: Q7L2E3; IntAct: EBI-34580994; Score: 0.35
DE  Interaction: P42696; IntAct: EBI-34581001; Score: 0.35
DE  Interaction: P16989; IntAct: EBI-34581001; Score: 0.35
DE  Interaction: P11388; IntAct: EBI-34581001; Score: 0.35
DE  Interaction: Q8IY81; IntAct: EBI-34581001; Score: 0.35
DE  Interaction: P51116; IntAct: EBI-34581001; Score: 0.35
DE  Interaction: P09132; IntAct: EBI-34581001; Score: 0.35
DE  Interaction: Q9UHB9; IntAct: EBI-34581001; Score: 0.35
DE  Interaction: O94973; IntAct: EBI-34581001; Score: 0.35
DE  Interaction: P62424; IntAct: EBI-34581001; Score: 0.35
DE  Interaction: Q12906; IntAct: EBI-34581001; Score: 0.35
DE  Interaction: Q9H4G0; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q15050; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q13310; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q8WTT2; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q7Z2W4; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q15024; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q9GZR7; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q13868; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q9BQ39; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q9UKD2; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: O95104; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q13243; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q00577; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: P42285; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q13523; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: O43169; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q9H6W3; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q02543; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: P50914; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: P52272; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q9BQG0; IntAct: EBI-34581556; Score: 0.35
DE  Interaction: Q96SB4; IntAct: EBI-34581556; Score: 0.35
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0001650;
GO  GO:0016021;
GO  GO:0046581;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003725;
GO  GO:0051059;
GO  GO:0003723;
GO  GO:0061629;
GO  GO:0003713;
GO  GO:0003712;
GO  GO:0031663;
GO  GO:0043066;
GO  GO:0000122;
GO  GO:0045766;
GO  GO:0010508;
GO  GO:0043123;
GO  GO:0051092;
GO  GO:0051897;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARK
SQ  KRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNE
SQ  KSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASF
SQ  PVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPS
SQ  AWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEE
SQ  WGNWVDEERASLLKSQEPIPDDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKT
SQ  RPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPILQETDKSKSNTKQNSVPPSQT
SQ  KSETSWESPKQIKKKKKARRET
//
ID  Q80WJ7;
PN  Protein LYRIC;
GN  Mtdh;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=In epithelial cells, recruited to tight junctions (TJ) during the maturation of the TJ complexes. A nucleolar staining may be due to nuclear targeting of an isoform lacking the transmembrane domain. TNF- alpha causes translocation from the cytoplasm to the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q80WJ7;
DR  UNIPROT: B2RSG8;
DR  UNIPROT: Q05CM0;
DR  UNIPROT: Q3U9F8;
DR  UNIPROT: Q3UAQ8;
DR  UNIPROT: Q8BN67;
DR  UNIPROT: Q8CBT9;
DR  UNIPROT: Q8CDL0;
DR  UNIPROT: Q8CGI7;
DR  UNIPROT: Q9D052;
DR  Pfam: PF15686;
DE  Function: Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q78PY7; IntAct: EBI-9682947; Score: 0.52
DE  Interaction: P70326; IntAct: EBI-16360068; Score: 0.35
DE  Interaction: P11531; IntAct: EBI-20567174; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26472902; Score: 0.35
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0001650;
GO  GO:0016021;
GO  GO:0046581;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003725;
GO  GO:0051059;
GO  GO:0061629;
GO  GO:0003713;
GO  GO:0003712;
GO  GO:0031663;
GO  GO:0043066;
GO  GO:0000122;
GO  GO:0045766;
GO  GO:0010508;
GO  GO:0043123;
GO  GO:0051092;
GO  GO:0051897;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAARSWQDELAQQAEEGSARLRELLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARK
SQ  KRRSPPRKREEAAPPTPAPDDLAQLKNLRSEEQKKKNRKKLPEKPKPNGRTVEVPEDEVVRNPRSITAKQAPETDKKNEK
SQ  SKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENIITVTTEQLTTASFP
SQ  VGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSRLNENLTVNGGGWSEKSVKLSSQLSEEKWNSVPPASAGKRKTEPSAWT
SQ  QDTGDTNANGKDWGRNWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPSSDWNAPAEEWGN
SQ  WVDEDRASLLKSQEPISNDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSHTQDTEDLEKDTREELPVNTSKARPK
SQ  QEKACSLKTMSTSDPAEVLIKNSQPVKTLPPAISAEPSITLSKGDSDNSSSQVPPMLQDTDKPKSNAKQNSVPPSQTKSE
SQ  TNWESPKQIKKKKKARRET
//
ID  Q9Z1W6;
PN  Protein LYRIC;
GN  Mtdh;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=In epithelial cells, recruited to tight junctions (TJ) during the maturation of the TJ complexes. A nucleolar staining may be due to nuclear targeting of an isoform lacking the transmembrane domain. TNF- alpha causes translocation from the cytoplasm to the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9Z1W6;
DR  Pfam: PF15686;
DE  Function: Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q96RT1; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: P35968; IntAct: EBI-22252438; Score: 0.35
DE  Interaction: O75096; IntAct: EBI-22258804; Score: 0.35
DE  Interaction: O75886; IntAct: EBI-22259612; Score: 0.35
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0046581;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003725;
GO  GO:0051059;
GO  GO:0061629;
GO  GO:0003713;
GO  GO:0003712;
GO  GO:0070830;
GO  GO:0031663;
GO  GO:0043066;
GO  GO:0000122;
GO  GO:0045766;
GO  GO:0010508;
GO  GO:0043123;
GO  GO:0051092;
GO  GO:0051897;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAARSWQDELAQQAEEGSARLRELLSVGLGFLRTELGLDLGLEPKRYPSWVILVGTGALGLLLLFLLGYGWAAACAGARK
SQ  KRRSPPRKREEVTPPTPAPEDPAQLKNLRSEEQKKKNRKKLPEKPKPNGRTVEIPEDEVVRTPRSITAKQPPETDKKNEK
SQ  SKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFP
SQ  VGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENITVNGGGWSEKSVKLSSQLSAGEEKWNSVPPASAGKRKTEQSA
SQ  WTQDPGDTNANGKDWGRNWSDRSIFSGIGSTAEPVSQSTTSDYQWDGSRNQPHIDDEWSGLNGLSSADPSSDWNAPAEEW
SQ  GNWVDEDRASLLKSQEPISNDQKDSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSITQDTEDLEKDTREELPVNTSKAR
SQ  PKQEKACSLKTMSTSDPVEVLIKNSQPIKTLPPAISAEPSVTLSKGDSDKSSSQVPPMLQDTDKPKSNAKQNSVPPSQTK
SQ  SETNWESPKQIKKKKKARRET
//
ID  Q9E005;
PN  cap-snatching endonuclease;
GN  L;
OS  1980456;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q9YQR5}.
DR  UNIPROT: Q9E005;
DR  PDB: 6Q99;
DR  Pfam: PF04196;
DR  Pfam: PF12426;
DR  PROSITE: PS50525;
DE  Function: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs (Probable). These short capped RNAs are then used as primers for viral transcription. Cleaves ssRNA substrates but not DNA (PubMed:27300328). Seems to downregulate the expression of its own and heterologous mRNAs through its endonuclease activity (PubMed:23576516). {ECO:0000269|PubMed:23576516, ECO:0000269|PubMed:27300328, ECO:0000305|PubMed:27300328}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0004519;
GO  GO:0046872;
GO  GO:0000166;
GO  GO:0003968;
GO  GO:0075526;
GO  GO:0006351;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKYREIHQRVRDLAPGTVSALECIDLLDRLYAVRHDLVDQMIKHDWSDNKDVERPIGQVLLMAGIPNDIIQGMEKKIIP
SQ  NSPSGQVLKSFFRMTPDNYKITGNLIEFIEVTVTADVSRGIREKKIKYEGGLQFVEHLLETESRKGNIPQPYKITFSVVA
SQ  VKTDGSNISTQWPSRRNDGVVQHMRLVQADINYVREHLIKLDERASLEAMFNLKFHVSGPKLRYFNIPDYRPQQLCEPRI
SQ  DNLIQYCKNWLTKEHKFVFKEVSGANVIQAFESHEQLHLQKYNESRKPRNFLLLQLTVQGAYLPSTISSDQCNTRIGCLE
SQ  ISKNQPETPVQMLALDISYKYLSLTRDELINYYSPRVHFQSSPNVKEPGTLKLGLSQLNPLSKSILDNVGKHKKDKGLFG
SQ  EIIDSINVASQIQINACAKIIEQILSNLEINIGEINASMPSPNKTTGVDDLLNKFYDNELGKYMLSILRKTAAWHIGHLV
SQ  RDITESLIAHAGLRRSKYWSVHAYDHGNVILFILPSKSLEVVGSYIRYFTVFKDGIGLIDADNIDSKAEIDGVTWCYSKV
SQ  MSIDLNRLLALNIAFEKSLLATATWFQYYTEDQGHFPLQHALRSIFSFHFLLCVSQKMKLCAIFDNLRYLIPSVTSLYSG
SQ  YELLIEKFFERPFKSSLDVYLYSIIKSLLISLAQNNKVRFYSRVRLLGLTVDHSTVGASGVYPSLMSRVVYKHYRSLISE
SQ  ATTCFFLFEKGLHGNLPEEAKIHLETIEWARKFQEKEKQYGDILLKEGYTIESVINGEVDVEQQLFCQEVSELSAQELNK
SQ  YLQAKSQVLCANIMNKHWDKPYFSQTRNISLKGMSGALQEDGHLAASVTLIEAIRFLNRSQTNPNVIDMYEQTKQSKAQA
SQ  RIVRKYQRTEADRGFFITTLPTRVRLEIIEDYFDAIAKVVPEEYISYGGDKKVLNIQNALEKALRWASGVSEITTSTGKS
SQ  IKFKRKLMYVSADATKWSPGDNSAKFRRFTQAIYDGLSDNKLKCCVVDALRNIYETEFFMSRKLHRYIDSMENHSDAVED
SQ  FLAFFSNGVSANVKGNWLQGNLNKCSSLFGAAVSLLFREVWKQLFPELECFFEFAHHSDDALFIYGYLEPEDDGTDWFLY
SQ  VSQQIQAGNFHWHAINQEMWKSMFNLHEHLLLMGSIKVSPKKTTVSPTNAEFLSTFFEGCAVSIPFVKILLGSLSDLPGL
SQ  GFFDDLAAAQSRCVKSLDLGACPQLAQLAIVLCTSKVERLYGTADGMVNSPTAFLKVNKAHVPVPLGGDGSMSIMELATA
SQ  GFGMADKNILKNAFISYKHTRRDGDRYVLGLFKFLMSLSEDVFQHDRLGEFSFVGKVQWKVFTPKAEFEFHDQFSHNYLL
SQ  EWTRQHPVYDYIIPRNRDNLLVYLVRKLNDPSIITAMTMQSPLQLRFRMQAKQHMKVCRYEGEWVTFREVLAAADSFATS
SQ  YQPTERDMDLFNTLVSCTFSKEYAWKDFLNEVRCEVLTTRHVHRPKIARTFTVREKDQAIQNPINSVIGYKYALTVDEVS
SQ  DVLDSAFFPESLSADLQVMKDGVYRELGLDISSPEVLKRIAPLLYKAGRSRVVIVEGNVEGTAESICSYWLKTMSLIKTI
SQ  RVRPKKEVLKAMSLYSVKENIGLQDDIAATRLCIEIWRWCKANEQDVKEWLTSLYFEKQTLMDWVERFRRKGVVPIDPEI
SQ  QCIGLLLYDVLGYKSVLQMQANRRAYSGKQYDAYCVQTYNEETKLYEGDLRVTFNFGLDCARLEVFWDKKEYILETSITQ
SQ  RHVLRLLMEEVSQELIRCGMRFKTEQVNQTRSLVLFKTEAGFEWGKPNVPCIVYKHCVLRTGLRTKQPINKEFMINVQSD
SQ  GFRAIAQMDIESPRFLLAHAYHTLRDIRYQAVQAVGNVWFKTEQHKLFINPIISSGLLENFMKGLPAAIPPAAYSLIMNK
SQ  AKISVDLFMFNELLALINRNNILNLDGIEETSEGYSTVTSMSSKQWSEEMSLMSDDDIDDMEDFTIALDDIDFEQINLEE
SQ  DIQHFLQDESAYVGDLLIQTEDIEVKKIRGVTRVLEPVKLLKSWVSKGLAIDKVYNPIGIILMARYMSKTYNFSSTPLAL
SQ  LNPYDLTELESVVKGWGETVNDRFKDLDIEAQTVVKEKGVQPEDVLPDSLFSFRHVDVLLRRLFPRDPVSTFY
//
ID  V5IVB1;
PN  cap-snatching endonuclease;
GN  RdRp;
OS  1980460;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q9YQR5}.
DR  UNIPROT: V5IVB1;
DR  Pfam: PF04196;
DR  Pfam: PF12426;
DR  PROSITE: PS50525;
DE  Function: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap- snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. Cleaves ssRNA substrates but not DNA (By similarity). Seems to downregulate the expression of its own and heterologous mRNAs through its endonuclease activity (By similarity). {ECO:0000250|UniProtKB:Q9E005}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0004519;
GO  GO:0046872;
GO  GO:0000166;
GO  GO:0003968;
GO  GO:0075526;
GO  GO:0006351;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKYREIHQRVREIAPGTGSALDCMDLLDRLYAVRHDLVDQMIKHDWSDNKDVETPIGQVLLMAGVPNDIIQGMEKKIIP
SQ  NSPTGQILKSFFKMTPDNFKITGNQIEFIEVTVTADVARGIREKRLKYESGLRFTEELLELEVKKGNLQQVYRISFNVVA
SQ  VKTDGSNISTQWPSRRNEGVVQQMRLVQADINYVREHLIMQDERASLEAMFNLKFHVTGPRLRYFSIPDYRPQPLCNPTI
SQ  DGLLQYCKQWLTEEHKFIFKEVSGTNVMGSFEVNEKKHKERYLESRKPRNFLLLQTTIQGSYLPSTISSDQCNTRIGCLE
SQ  ICKNIPETPVQALASDIAFKYISLDKDEVINYYNPRIHFKPGQNVKEPGTLKIGLSQMNPLSKAILDNIGKHKSDKGLFG
SQ  QAIESINIASQIQLNECSKVIEQILSNLEINISDVSENIPLPKKTTCVDELLGKFYENEITKYMLGILRKTVAWHIGHLI
SQ  RDITESLIAHSGLRRSKYWSVHAYDHGNVILFILPSKSLEVAGSYIRFFTVFKDGIGLVDNDNTDSKTEIDGITWIYSKV
SQ  MSIDLNRLLALNIAFEKALLATATWFQYYTEDQGHFPLQHALRSVFSFHLLLCVSQKMKICAIFDNLRYLIPSVTSLYSG
SQ  YELLIEKFFERPFKSALDVYLYSIIKSLLVSLAQNNKVRFYSKVRLLGLTVDQSTVGASGVYPSLMSRVVYKHYRSLISE
SQ  ATTCFFLFEKGLHGNLTEEAKIHLETVEWARKFNEKENRYGDILMKEGYTIELVENQNVTVEQQLFCQEVVELSAMELNK
SQ  YLHAKSQVLCANIMNKHWDKPYFSQVRNISLKGMSGSLQEDGHLASSVTLIEAIRFLNSSQINPNVIDMYERTKHCKAQA
SQ  RIVRKYQRTEADRGFFITTLPTRVRLEIIEDYYDAIAKVVPEEYISYGGERKILNIQSALEKALRWASGISEIITSTGKK
SQ  IRFKRKLMYVSADATKWSPGDNSAKFRRFTQAIYDGLNDDKLKCCVVDSLKNIYETEFFMSRKLHRYIDSMESKSEAVED
SQ  FLSFFSGGVSATVKGNWLQGNLNKCSSLFGVAVSLLFKRVWVELFPELECFFEFAHHSDDALFIYGYLEPEDDGTDWFMY
SQ  VSQQIQAGHYHWHAVNQEMWKSMFNLHEQLLLMGSIRVSPKKTTVSPTNAEFLSTFFEGCAVSIPFIKILLGSLSDLPGL
SQ  GFFDDLAASQSRCVKALDLGACPQLAQLAIVLCTSKVERLYGTADGMINSPISFLKVNKAHIPIALGGDGSMSIMELATA
SQ  GIGMADKNILKKAFYSYKHTKRDGDRYILGLFKFLMSLSDDVFQHDRLGEFSFVGKVQWKVFTPKSEFEFYDQYSMTYLQ
SQ  AWSKQHPVYDYIIPRGRDNLLVYLVRKLNDPSIITAMTMQSPLQLRFRMQAKQHMKVCKLEGEWVTFREILAAADSFAST
SQ  YQPNEKDLDLFNTLVSCTFSKEYAWKDFLNEVRCEVTTARHVHRPKVARTFTVREKDQVIQNPITSVIGYKYASTVDEIS
SQ  DVLDSAFFPDSLSADLQVMKEGVYRELGLDIGLPEVLKRIAPLLYKAGKSRIVIVEGNIEGTAESICSYWLKNMSLIKTI
SQ  KVKPRKEVLKAVSLYGTKDNLSLQDDLAATRICIEVWRWCKANNQNVQEWFTALYFENQTLYDWIERFRRKGVVPVDPEI
SQ  QCMALLLYDVLGFKNVLQMQANRRAYSGKQYDAYCVQTYNEETKLYEGDLRVTFNFGLDCARLEVFWDKKEYVLETSITQ
SQ  KHVLRLMMEEVSKELVRCGMRFKTEQVSHTRSLVLFKTESGFEWGKPNIPCIVYKHCALRTGLRTKHPINKEFMINIQSD
SQ  GFRAIAQMDIESPRFLLAHAYHTLRDVRYQAVQAVGNVWFRTEQHKLFINPIISSGLLENFMKGLPAAIPPAAYSLIMNK
SQ  AKISVDLFMFNELLALINKNNILDLSGIEETSEGYSTVTSMSSKQWSEEMSLMSDDDIDDDEEFTIALDDIDFEQVDLEE
SQ  DIQHFLQDESAYVGDLLIQTEEVEVKRIRGVTRILEPVKLIKSWVSKGLAIDKVYNPVGILLMARYMSKNYDFHSVPLAL
SQ  MNPYDLTEFESVVKGWGETINDRFQEIDLEAQRLVREQNIQPEDILPDSLFSFRHVDVLLKRLFPRDPISSFY
//
ID  Q806Y6;
PN  cap-snatching endonuclease;
GN  L;
OS  1980467;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q9YQR5}.
DR  UNIPROT: Q806Y6;
DR  Pfam: PF04196;
DR  Pfam: PF12426;
DR  PROSITE: PS50525;
DE  Function: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap- snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. Cleaves ssRNA substrates but not DNA (By similarity). Seems to downregulate the expression of its own and heterologous mRNAs through its endonuclease activity (By similarity). {ECO:0000250|UniProtKB:Q9E005}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0004519;
GO  GO:0046872;
GO  GO:0000166;
GO  GO:0003968;
GO  GO:0075526;
GO  GO:0006351;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKYREIHRDLQSFPVGSLTAVECIDYLDRLYAIRHDIVDQMIKHDWSDNKDSEESIGKVLLFAGVPNNVITAMEKKIIP
SQ  DHPSGKTLRSFFKMTPDNYKITGSTIEFVEVTVTVDVDKGIREKRLKYEAGLKYIEQELHNHFLRGDIPQPYKITFQVVS
SQ  VRTDGSNISTQWPSRRNDGVVQYMRLVQAEISYVREHLIRQEERAALEAMFNLKFNISNIKNQPYYIPDYRGIPLIHPNI
SQ  NDLVVYMRDWLSKSHKFSFHEGKVPAVFDCFNENELEHAVKYPISRHPRNFLLIQCSLLSSYNPATILSDQVDSRRACNS
SQ  VLNLIPETPTSFLIHDMAYRYINLTREDMVSFYAPKTQFIPTQNVKEPGTFKLTANSMRPESKAMLDMLGSHEPGEKKGA
SQ  LIESLNLSSHIVQSECVSLITKILSDLELNISEPTSHGSFTTKHTYVDNVLEKFFQNEIQRYLLDVLKKTTAWHIGHLIR
SQ  DITESLIAHSGLKRSKYWSVHAYNNGNVILFILPSKSLEVAGSYIRFVTVFRMGPGLVDKDNLDTILTDQDVTWGVSKVM
SQ  SIDLNRLLALNIAFEKALIATATWFQYYTEDQGQFPLQHAIRSVFAYHLLLAVCQKMKLCAIFDNLRYLIPAVTSLYSGF
SQ  PSLINKLFERPFKSALEVYVYYNIKSLLVALAQNNKARFYSKVKLLGLTVDQSTVGASGIYPSFMSRVIYKHYRSLISEV
SQ  TTCFFLFEKGLHGNMNEEAKIHLETVEWALKFRQKEDQYGESMVENGYTIGELNDNQDLVEQQLYCQDAVELAAVELNKI
SQ  LSTKSQVVANSILNKYWEVPYFSQTRNISLKGMSGQVQEDGHLAASVTIIEAIRYLSSSQNNPSVLQLYEETRKVKAQAR
SQ  IVRKYQRTEADRGFFITTLPTRCRLEIIEDYYDAISKNVAEEYISYGGERKILCIQSALEKALRWASGESFIELSNGKFI
SQ  RMKRKLMYVSADATKWSPGDNSAKFRRFTAALHNGLPDDRLKNCVIDALRNVYKTDFYMSRKLRAYIDNMNGHEPAVKNF
SQ  LEFFPDGHCGEVRGNWLQGNLNKCSSLFGVGMSLLFKQLWNELFPELDCFFEFAHHSDDALFIYGYLEPIDDGTDWFLYV
SQ  SQQIQAGHLHWFSVNTEMWKSMFNLHEHVLLLGSIKISPKKTTLSPTNAEFLSTFFESCAVSIPFIKILLGSLSDLPGLG
SQ  YFDDLAAAQSRCVKAMDLGASPQVAQLAVALCTNKVERLYGTAVGMIKHPSTYLQVKHGDTPIPLGGSGAMSIMELATAG
SQ  IGMSDKNLLKRALLGYIHKRQKNMAYILGLFKFLMNLSKDTFQHERLGEFSFIGKVQWKIFIPKSEFEFFDMYTPKFLKL
SQ  WSEQHVTYDYIIPKGRDNLLIYLVRKINDPSIVTAMTMQSPLQLRFRMQAKQHMKVCKLDDDWVTFREILAAANSFAQLY
SQ  EVTQEDLDLFQTLTSCTFSKEYAWKDFLNGVQCDVIPTKQIQRAKVARTFTVREKDQIIQNSIPAVIGYKFAVTVDEMSD
SQ  VLDSAKFPDSLAVDLKTMKDGVYRELGLDISQAEVMKKVAPMLYKSSKSRVVIVQGNVEGTAEAICGYWLRTMSLVKTIR
SQ  VKPHKEVLKAVSIFNRKEDIGQQKDLAALRLCIEVWRWCKANNAPYQEWFHALWFEDKTFSEWLDRFIRVGVPPVDPEIQ
SQ  CAALMIADIRGDLSVLQVQANRRAYSGKQYDAYCVQTYNEETKLYEGDLRVTFNFGLDCARLEIFWDKQTYILETSITQK
SQ  HVLKIMMDEVTKELLRCGMRFKTEQVSNVKHLVLFKTEAGFEWGKPNIPCIVYKNCALRTGLRANQTVNHKFMISIKDNG
SQ  LRAIAQYDDESPRFLLAHAFHTIRDIRYQAVDAVSNVWFIHKGIKLFLNPIISSGLLENFMKNLPAAIPPAAYSLIMNRA
SQ  KISVDLFMFNDLLRLINPSNTLDLSGLQPTEDGFSTVSSMSSRLWSEEVSFVDEDEEIDDEFTIDLQDVDFENIDVEADI
SQ  EHFLQDESSYTGDLLIMSEETEVKKMRGIIKLLEPVRLIKSWVSKGLCIEKVYSPTNIILMTRYLSKNFNFSGRQVSLLD
SQ  PYDLTEFESIVKGWGECVVDQFSTFDQETQLLVSQKGICPEDVVPDSLFSFRHTIVLLRRLFPQDSVSTFY
//
ID  P23456;
PN  cap-snatching endonuclease;
GN  L;
OS  11602;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q9YQR5}.
DR  UNIPROT: P23456;
DR  PDB: 5IZE;
DR  Pfam: PF04196;
DR  Pfam: PF12426;
DR  PROSITE: PS50525;
DE  Function: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap- snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs (PubMed:27304209). These short capped RNAs are then used as primers for viral transcription. Cleaves ssRNA substrates but not DNA (By similarity). Seems to downregulate the expression of its own and heterologous mRNAs through its endonuclease activity (By similarity). {ECO:0000250|UniProtKB:Q9E005, ECO:0000269|PubMed:27304209}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0004519;
GO  GO:0046872;
GO  GO:0000166;
GO  GO:0003968;
GO  GO:0075526;
GO  GO:0006351;
GO  GO:0039689;
GO  GO:0039696;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDKYREIHNKLKEFSPGTLTAVECIDYLDRLYAVRHDIVDQMIKHDWSDNKDSEEAIGKVLLFAGVPSNIITALEKKIIP
SQ  NHPTGKSLKAFFKMTPDNYKISGTTIEFVEVTVTADVDKGIREKKLKYEAGLTYIEQELHKFFLKGEIPQPYKITFNVVA
SQ  VRTDGSNITTQWPSRRNDGVVQYMRLVQAEISYVREHLIKTEERAALEAMFNLKFNISTHKSQPYYIPDYKGMEPIGANI
SQ  EDLVDYSKDWLSRARNFSFFEVKGTAVFECFNSNEANHCQRYPMSRKPRNFLLIQCSLITSYKPATTLSDQIDSRRACSY
SQ  ILNLIPDTPASYLIHDMAYRYINLTREDMINYYAPRIQFKQTQNVREPGTFKLTSSMLRAESKAMLDLLNNHKSGEKHGA
SQ  QIESLNIASHIVQSESVSLITKILSDLELNITEPSTQEYSTTKHTYVDTVLDKFFQNETQKYLIDVLKKTTAWHIGHLIR
SQ  DITESLIAHSGLKRSKYWSLHSYNNGNVILFILPSKSLEVAGSFIRFITVFRIGPGLVDKDNLDTILIDGDSQWGVSKVM
SQ  SIDLNRLLALNIAFEKALIATATWFQYYTEDQGQFPLQYAIRSVFANHFLLAICQKMKLCAIFDNLRYLIPAVTSLYSGF
SQ  PSLIEKLFERPFKSSLEVYIYYNIKSLLVALAQNNKARFYSKVKLLGLTVDQSTVGASGVYPSFMSRIVYKHYRSLISEV
SQ  TTCFFLFEKGLHGNMNEEAKIHLETVEWALKFREKEEKYGESLVENGYMMWELRANAELAEQQLYCQDAIELAAIELNKV
SQ  LATKSSVVANSILSKNWEEPYFSQTRNISLKGMSGQVQEDGHLSSSVTIIEAIRYLSNSRHNPSLLKLYEETREQKAMAR
SQ  IVRKYQRTEADRGFFITTLPTRCRLEIIEDYYDAIAKNISEEYISYGGEKKILAIQGALEKALRWASGESFIELSNHKFI
SQ  RMKRKLMYVSADATKWSPGDNSAKFRRFTSMLHNGLPNNKLKNCVIDALKQVYKTDFFMSRKLRNYIDSMESLDPHIKQF
SQ  LDFFPDGHHGEVKGNWLQGNLNKCSSLFGVAMSLLFKQVWTNLFPELDCFFEFAHHSDDALFIYGYLEPVDDGTDWFLFV
SQ  SQQIQAGHLHWFSVNTEMWKSMFNLHEHILLLGSIKISPKKTTVSPTNAEFLSTFFEGCAVSIPFVKILLGSLSDLPGLG
SQ  YFDDLAAAQSRCVKALDLGASPQVAQLAVALCTSKVERLYGTAPGMVNHPAAYLQVKHTDTPIPLGGNGAMSIMELATAG
SQ  IGMSDKNLLKRALLGYSHKRQKSMLYILGLFKFLMKLSDETFQHERLGQFSFIGKVQWKIFTPKSEFEFADMYTSKFLEL
SQ  WSSQHVTYDYIIPKGRDNLLIYLVRKLNDPSIVTAMTMQSPLQLRFRMQAKQHMKVCRLDGEWVTFREVLAAANSFAENY
SQ  SATSQDMDLFQTLTSCTFSKEYAWKDFLNGIHCDVIPTKQVQRAKVARTFTVREKDQIIQNSIPAVIGYKFAVTVEEMSD
SQ  VLDTAKFPDSLSVDLKTMKDGVYRELGLDISLPDVMKRIAPMLYKSSKSRVVIVQGNVEGTAEAICRYWLKSMSLVKTIR
SQ  VKPHKEVLQAVSIFNRKEDIGQQKDLAALKLCIEVWRWCKANSAPYRDWFQALWFEDKTFSEWLDRFCRVGVPPIDPEIQ
SQ  CAALMIADIKGDYSVLQLQANRRAYSGKQYDAYCVQTYNEVTKLYEGDLRVTFNFGLDCARLEIFWDKKAYILETSITQK
SQ  HVLKIMMDEVSKELIKCGMRFNTEQVQGVRHMVLFKTESGFEWGKPNIPCIVYKNCVLRTSLRTTQAINHKFMITIKDDG
SQ  LRAIAQHDEDSPRFLLAHAFHTIRDIRYQAVDAVSNVWFIHKGVKLYLNPIISSGLLENFMKNLPAAIPPAAYSLIMNRA
SQ  KISVDLFMFNDLLKLINPRNTLDLSGLETTGDEFSTVSSMSSRLWSEEMSLVDDDEELDDEFTIDLQDVDFENIDIEADI
SQ  EHFLQDESSYTGDLLISTEETESKKMRGIVKILEPVRLIKSWVSRGLSIEKVYSPVNIILMSRYISKTFNLSTKQVSLLD
SQ  PYDLTELESIVRGWGECVIDQFESLDREAQNMVVNKGICPEDVIPDSLFSFRHTMVLLRRLFPQDSISSFY
//
ID  P27176;
PN  cap-snatching endonuclease;
GN  L;
OS  1337063;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q9YQR5}.
DR  UNIPROT: P27176;
DR  Pfam: PF04196;
DR  Pfam: PF12426;
DR  PROSITE: PS50525;
DE  Function: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap- snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. Cleaves ssRNA substrates but not DNA (By similarity). Seems to downregulate the expression of its own and heterologous mRNAs through its endonuclease activity (By similarity). {ECO:0000250|UniProtKB:Q9E005}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0004519;
GO  GO:0046872;
GO  GO:0000166;
GO  GO:0003968;
GO  GO:0075526;
GO  GO:0006351;
GO  GO:0039689;
GO  GO:0039696;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKYREIHERVKEAVPGETSAVECLDLLDRLYAVRHDVVDQMIKHDWSDNKDKEQPIGLVLLMAGVPNDVIQSMEKRIIP
SQ  GSPSGQILRSFFKMTPDNYKITGNLIEFIEVTVTADVARGVREKILKYQGGLEFIEQLLQIEAQKGNCQSGFRIKFDVVA
SQ  IRTDGSNISTQWPSRRNEGVVQAMRLIQADINFVREHLIKNDERGALEAMFNLKFHVTGPKVRTFDIPNYRPQQLCQPVL
SQ  ENLVEYCKNWLGTDHAFAFKEVTGQRVFNVFRDEEELHASKYGHSRKPRNFLLCQISLQVPYLPSTIASDQYDTRLACSE
SQ  ILKNYPETPLQLLARDMAYKYITLDNEDIINYYNPRVYFKPTQNIKEPGTFKLNLSNMDPKSKALIDVISKDSKKGVFGE
SQ  LIDSIDVASQVQQNECAKTIEKILSDLEVNLGDSTAGLDQPKRTTGVDDILRKFYDNELVKYLISVIRKTTARHLGHLLR
SQ  DITESLIAHAGLKRSKYWSAHGYAYGSVLLCILPSKSLEVAGSFIRFFTVFKEGLGLIDADNLDSKVEIDGVTWCFSKII
SQ  SLDLNRLLALNIAFEKSLLATATWFQYYTEDQGHFPLQHALRSVFAFHFLLATSQKMKLCAIFDNLRYLIPAVTSTYSGF
SQ  EPLIRKFFERPFKSALEVYLYNIIKTLLVSLAQNNKIRFYSRVRLLGLTVDQSSIGASGVYPSLMSRVVYKHYRSLISEA
SQ  TTCFFLFEKGLHGNLTEEAKIHLETVEWARKFREKERKLGSYIMEEGYHIQDVLNNQVVVEQQLFCQEVVELAAQELNTY
SQ  LHAKSQVMASNIMNKHWDKPYFSQTRNISLKGMSGALQEDGHLAASVTLIEAIRFLNHSQNNPTVLELYEQTKKQKAQAR
SQ  IVRKYQRTEADRGFFITTLPTRVRLEIIEDYYDAIARVVPEEYISYGGETKILNIQQALEKALRWASGESEIQSSIGHSI
SQ  KLKRKLMYVSADATKWSPGDNSAKFRRFTQSLYDGLRDDKLKNCVVDALRNIYETDFFISRKLHRYIDNMGELSDEVLDF
SQ  LSFFPNKVSASIKGNWLQGNLNKCSSLFGAAVSLLFKRVWAKLYPELECFFEFAHHSDDALFIYGYLEPVDDGTEWFQYV
SQ  TQQIQAGNFHWHAVNQEMWKSMFNLHEHILLMGSIKISPKKTTVSPTNAEFLSTFFEGCAVSIPFIKILLGSLSDLPGLG
SQ  YFDDLAAAQSRCVKALDMGACPQLAQLGIVLCTSKVERLYGTAPGMVNNPTAYLKVDRSLIPIPLGGDGSMSIMELATAG
SQ  IGMADKNILKNAFITYKHAKKDNDRYVLGLFKFLMSLSDDIFQHDRLGEFSFVGKVQWKVFTPKSEFEFYDQYSRKYLEL
SQ  WSEQHPVYDYIIPRGRDNLLVYLVRKLNDPSIVTAMTMQSPLQLRFRMQAKQHMKVCKLDGEWVTFREVLAAADAFASEY
SQ  RPTLQDMELFQTLVNCTFSKEYAWRDFLNEVQCDVLTTRQIHRPKVARTFTVKEKDQTIQNPITAVIGYKYASKVDEISD
SQ  VLDSAIHPDSLSTDLQLMREGVYRELGLDISQPNVLKKVAPLLYKSGKSRIVIVQGNVEGTAESICSYWLKTMSLVKTIK
SQ  VKPKKEVLKAVSLYGKKEKAGDLTHLAAMRLCIEVWRWCKANEQDSVSWLKYLMFENKTLEQWIDSFCSRGVLPVDPEIQ
SQ  CLGLLVYDLKGQKGLLQIQANRRAYSGKQYDAYCVQTYNEETKLYEGDLRVTFNFGIDCARLEIFWDKREYILETSITQR
SQ  NVLKILMEEVTKELLRCGMRFKTEQVNSSRSVVLFKTESGFEWGKPNVPCIVYRNCTLRTGLRVRQPTNKAFSITIQANG
SQ  FRAMAQLDEENPRFLLAHAYHNLKDVRYQALQAVGNVWFKMTQHKLFINPIISAGLLENFMKGLPAAIPPAAYSLIMNKA
SQ  KISVDLFMFNELLALINPQNVLNLDGIEETSEGYTTVSTISSTQWSEEVSLTMDDSDDDGDASQLDYTIDLDDIDFETID
SQ  LKEDIEHFLQDESAYTGDLLIQTEETEIRKLRGMIKILEPVKLIKSWVSKGLSIDKIYNPVNIILMTRYMSKHYNFHAKQ
SQ  LSLMDPYDLTEFESIVKGWGECVKDRFIELDQEAQRKVTEERVLPEDVLPDSLFSFRHADILLKRLFPRDSASSFY
//
ID  P0C760;
PN  cap-snatching endonuclease;
GN  L;
OS  39002;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q9YQR5}.
DR  UNIPROT: P0C760;
DR  UNIPROT: I4EPA5;
DR  Pfam: PF04196;
DR  Pfam: PF12426;
DR  PROSITE: PS50525;
DE  Function: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap- snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. Cleaves ssRNA substrates but not DNA (By similarity). Seems to downregulate the expression of its own and heterologous mRNAs through its endonuclease activity (By similarity). {ECO:0000250|UniProtKB:Q9E005}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0004519;
GO  GO:0046872;
GO  GO:0000166;
GO  GO:0003968;
GO  GO:0075526;
GO  GO:0006351;
GO  GO:0039689;
GO  GO:0039696;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKYRDIHERVKEAVPGETSAVECLDLLDRLYAVRHDVVDQMIKHDWSDNKDREQPIGLVLLMAGVPNDVIQSMEKRVIP
SQ  GSPSGQILRSFFKMTPDNYKITGNLIEFIEVTVTADVARGVREKILKYQGGLEFIEQLLQIEAQKGNCQSGFKIKFNVVA
SQ  VRTDGSNISTQWPSRRNEGVVQAMRLIQADINFVREHLIKNDERGALEAMFNLKFHVTGPKVRTFDIPNYRPQPLCQPIL
SQ  ENLVDYCKNWLGTDHAFAFKEVTGQRVFNVFREEEEIHASKYGHSRKPRNFLLCQISLQSPYLPSTIASDQYDTRLACSE
SQ  ILKNYPETPLQLLARDMAYKYITLDHDDIINYYNPRVYFKPTQNIKEPGTFKLNLSNMDPKSKALIDVISKDSKKGVFGE
SQ  LIDSVDVASQVQHNECSKTIEKILSDLEVNLGDVANGLDQPKKTTGVDDILRKFYDNELVKYLISVIRKTTAWHLGHLLR
SQ  DITESLIAHAGLKRSKYWSAHGYACGSVLLCILPSKSLEVAGSFIRFFTVFKEGLGLIDTDNLDSKAEIDGVSWCFSKII
SQ  SLDLNRLLALNIAFEKSLLATATWFQYYTEDQGHFPLQHALRSVFAFHFLLSVSQKMKLCAIFDNLRYLIPAVTSTYSGF
SQ  EPLIRKFFERPFKSALEVYLYGIIKVLLVSLAQNNKIRFYSRVRLLGLTVDQSTIGASGVYPSLMSRVVYKHYRSLISEA
SQ  TTCFFLFEKGLHGNLTEEAKIHLETVEWARKFREKERELGSYIMEEGYHIQDVLNNQVAVEQQLFCQEVVELAAQELNTY
SQ  LHAKSQVMASNIMNKHWDKPYFSQTRNISLKGMSGALQEDGHLAASVTLIEAIRFLNHSQNNPTVLELYEQTKKQRAQAR
SQ  IVRKYQRTEADRGFFITTLPTRVRLEIIEDYYDAIAKVVPEEYISYGGERKILNIQQALEKALRWASGESEIQSSLGHSI
SQ  KLKRKLMYVSADATKWSPGDNSAKFRRFTQSLYDGLRDDKLKNCVVDALRNIYETDFFISRKLHRYIDNMGELSDEVLDF
SQ  LSFFPNKVSASIKGNWLQGNLNKCSSLFGAAISLLFKRVWAKLYPELECFFEFAHHSDDALFIYGYLEPIDDGTEWFQYV
SQ  TQQIQAGNFHWHAVNQEMWKSMFNLHEHILLMGSIKISPKKTTVSPTNAEFLSTFFEGCAVSIPFIKILLGSLSDLPGLG
SQ  YFDDLAAAQSRCVKALDMGACPQLAQLGIVLCTSKVERLYGTAPGMVNNPTAYLKVDRNLIPIPLGGDGSMSIMELATAG
SQ  IGMADKNILKNAFITYKHAKKDNDRYVLGLFKFLMSLSDDIFQHDRLGEFSFVGKVQWKVFTPKSEFEFYDQYSRKYLEL
SQ  WSEQHPVYDYIIPRGRDNLLVYLVRKLNDPSIVTAMTMQSPLQLRFRMQAKQHMKVCKLGGEWVTFREVLAAADAFASEY
SQ  RPTLQDMELFQTLVNCTFSKEYAWRDFLNEVQCDVLTTRQIHRPKVARTFTVKERDQTIQNPITAVIGYKYASKVDEISD
SQ  VLDSALHPDSLSTDLQLMREGVYRELGLDISQPNVLKKVAPLLYKSGKSRIVIVQGNVEGTAESICSYWLKTMSLVKTIK
SQ  VKPKKEVLKAVSLYGKKEKVGDLTHLAAMRLCIEVWRWCKANEQDSVTWLKYLVFENKTLEQWVDLFCSRGVLPIDPEIQ
SQ  CLGLLVYDLKGQKGLLQIQANRRAYSGKQYDAYCVQTYNEETKLYEGDLRVTFNFGIDCARLEIFWDKKEYILETSITQR
SQ  NVLKILMEEVTKELLRCGMRFKTEQVNSSRSVVLFKTESGFEWGKPNVPCIVYRNCTLRTGLRVRHPTNKAFSITIQANG
SQ  FRAMAQLDEENPRFLLAHAYHNLKDVRYQALQAVGNVWFKMTQHKLFINPIISAGLLENFMKGLPAAIPPAAYSLIMNKA
SQ  KISVDLFMFNELLALINPQNVLNLDGIEETSEGFTTVSTISSTQWSEEVSLTLDDSDDDDDASNLDYTIDLDDIDFETID
SQ  LKEDIEHFLQDESAYTGDLLIQTEETEVRKLRGMIKILEPVKLIKSWVSKGLSIDKIYNPVNIILMTRYMSKHYNFQAKQ
SQ  LSLMDPYDLTEFESVVKGWGECVKDRFIELDQEAQRKVTEERVLPEDVLPDSFFSFRHADILLKRLFPRDSASSFY
//
ID  P27314;
PN  cap-snatching endonuclease;
GN  L;
OS  12557;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q9YQR5}.
DR  UNIPROT: P27314;
DR  Pfam: PF04196;
DR  Pfam: PF12426;
DR  PROSITE: PS50525;
DE  Function: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap- snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. Cleaves ssRNA substrates but not DNA (By similarity). Seems to downregulate the expression of its own and heterologous mRNAs through its endonuclease activity (By similarity). {ECO:0000250|UniProtKB:Q9E005}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0004519;
GO  GO:0046872;
GO  GO:0000166;
GO  GO:0003968;
GO  GO:0075526;
GO  GO:0006351;
GO  GO:0039689;
GO  GO:0039696;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKYREIHRDLKEFTINSLTAVECMDYLDRLYAVRHDIVDQMIKHEWSDNKDSEEPISKVLLFAGIPNNVITALEKKVIP
SQ  DHPSGKTLRSFFKMTPDNYRITGSLIEFVEVTVTADVDKGIREKKMKYELGLKYLEQELMTFFHRGELQNPYKITFKVVA
SQ  VRTDGSNISTQWPSARNDGVVQYMRLVQAEISYVREHLVKTEERAALEAMFNLKFNISSLKTQPYFIPEYKGIDLIRPDI
SQ  DGLVNYAQSWMSKTQEFSFFEVKGSAVFDCFNENEQGHIVKYPMSRHPRNFLLIQCTVLTAYKPATILSDQLDSRRACIQ
SQ  FLNLIPETPASILAHDMAHRYINLTRDDLLAYYAPRIQFNPTQNIKEPGTFKLTSNMMRPESKIMLDMLSQHEPRENLGK
SQ  SIESLNISSHIVQSDCVSLITKILSDLELNISEPSSHEQITAKHTHVDTVLDKFFQNETQKYLIDILKKTTAWHIGHLVR
SQ  DITESLIAHSGLRRSKYWSIHAYNNGSVILFILPSKSLEVAGSFVRFMTAFKLGPGLVDKDNLDSILADGDILWGVSKIM
SQ  SLDLNRLLALNIAFEKALLATATWFQYYTEDQSQFPLQHSIRSVFAYHFLLAICQKMKLCAIFDNLRYLIPAVTSLYSGF
SQ  PSLVEKLFERPFKSALEVYVYYNIKSLLVALAQNNKARFYSKVKLLGLTVDQSTVGASGIYPSFMSRVVYKHYKSLISEV
SQ  TTCFFLFEKGLHGNVNEEAKIHLETVEWATKFKEKEDKYGEMLVEHGYTIGELVESSELAVQQLYCQDAVELAANELNRV
SQ  LIAKSQVVANSILNKYWEEPYFSQTRNISLKGMSGQVQEDGHLSSSTTIIEAIRYLSNSRNNPNVLQLYEETRHQKAQAR
SQ  IVRKFQRTEADRGFFITTLPTRCRLEIIEDYYDAISKNVAEEYISYGGERKILCIQAALEKALRWASGESFIELSNGKFI
SQ  RMKRKLMYVSADATKWSPGDNSAKFRRFTAALHNGLPDDRLKNCVIDALRHVYKTDFYMSRKLRHYIDSMDTYEPHVRDF
SQ  LNFFPDGHHGEVRGNWLQGNLNKCSSLFGVAMSLLFKEIWTRLFPELDCFFEFAHHSDDALFIYGYLEPADDGTDWFLFV
SQ  SQQIQAGKLHWFNVNTEMWKSMFNLHEHILLLGSIKISPKKTTLSPTNAEFLSTFFEGCAVSIPFIKILLGSLSDLPGLG
SQ  YFDDLAAAQTRCVKAMDLGASPQISQLAVSLSTSKVERLYGTSIGMVNYPGTYLRTKHSETPIPLGGSGAMSIMELSTAG
SQ  IGMSDKNLLKQALIGYMHKHQKQMSYILGLFKFLMDLSGETFQHERLGQFSFIGKVQWKIFTPKSEFEFSDMYSQKFLKV
SQ  WSEQHPTYDYIIPKGRDNLLIYLVRKLNDPSIITAMTMQSPLQLRFRMQAKQHMKVCRLDGDWVTFREVLAAANSFAESY
SQ  EPSQNDIDLFQTLTSCTFSKEYAWKDFLNNVHCDVIPTKQVQRAKVARTFTVREKDRIIQNSIPAVIGYKFAVTVDEMSD
SQ  VLDTAKFPDSLAVDLKTMKDGVYRELGLDISSPDVMKKVAPMLYKSAKSRVVIVQGNVEGTAEAICAYWLRNMSLIKTIK
SQ  VKPHKEVLQAVSIFNRKEDIGQQKDLSALKLCIEVWRWAKANNAPYRDWFHALWFEDKTFSEWLDRFIRVGVPPIDPEIQ
SQ  CAALMIADVKGDRSVLQLQANRRAYSGKQYDAYCVQTYNEETKLYEGDLRVTFNFGLDCARLEIFWDKKTYILETSITQK
SQ  HVLKIMMEEVSKELVRCGMRFNTEQVNGVKHLVLFKTDSGFEWGKPNIPCIVYKNCALRTGLRTNQAINHKFMITIKDDG
SQ  LRAIAQYDEDSPRFLLAHAFHTIRDVRYQAVDAVSNVWFTHKGIKLYLNPIISSGLLEYFMKNIPAAIPPAAYSLIMNRA
SQ  KISVDLFMFNDLLRLINPGNTLDLSGLEITGEGYSTVNSLSSRLWSEEMSLVDDEEEMDDEFTIDLQDVDFENIDIEADV
SQ  EHFLQDESAYTGDLLIMSEETEVKKMRGIIKLLEPVKLIKSWVSRGLSIEKVYNPVNIILMTRYISKNFNFSGKQVSLLD
SQ  PYDLTELESIVKGWGESVVDQFDSLDLEAQNLVQKQGIVPEDVIPDSLFSFRHTMVLLRRLFGQDSVSTFY
//
ID  Q89709;
PN  cap-snatching endonuclease;
GN  L;
OS  1980491;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q9YQR5}.
DR  UNIPROT: Q89709;
DR  UNIPROT: A0A059WB91;
DR  Pfam: PF04196;
DR  Pfam: PF12426;
DR  PROSITE: PS50525;
DE  Function: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap- snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. Cleaves ssRNA substrates but not DNA (By similarity). Seems to downregulate the expression of its own and heterologous mRNAs through its endonuclease activity (By similarity). {ECO:0000250|UniProtKB:Q9E005}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0004519;
GO  GO:0046872;
GO  GO:0000166;
GO  GO:0003968;
GO  GO:0075526;
GO  GO:0006351;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKYREIHQRVKEIPPGGASALECLDLLDRLYAVRHDVVDQMIKHDWSDNKDMERPIGQVLLMAGVPNDVIQGMEKKVIP
SQ  TSPSGQILKSFFRMTPDNYKITGALIEFIEVTVTADVAKGIREKKLKYESGLQFVESLLSQEHKKGNINQAYKITFDVVA
SQ  VKTDGSNISTQWPSRRNDGVVQHMRLVQADINYVREHLIKPDERASLEAMFNLKFHVGGPKLRYFNIPDYKPQSLCQPEI
SQ  TNLIQYCKHWLTEDHDFVFKEVTGNNVMNSFENNESVYMSRYRESRKPRNFLLIQGSIQGPYLPSTISSDQCDTRIGCLE
SQ  VLKVHPETPVQAIAVDMAYKYMELNRDEIINYYNPRVHFQATQSVKEPGTFKLGLSQLNPMSKSILDQVGKHKSEKGLFG
SQ  EPLESINISSQIQQNECSRIIESILSNLEINVGEVTMSLANPRKTTGVDELLGKFYENELSKYLISILRKTAAWHIGHLI
SQ  RDITESLIAHAGLKRSKYWSIHAYDHGGVILFILPSKSLEVVGSYIRYFTVFKDGIGLIDEENLDSKVDIDGVQWCFSKV
SQ  MSIDLNRLLALNIAFEKALLATATWFQYYTEDQGHFPLQHALRSVFSFHFLLCVSQKMKICAIFDNLRYLIPAVTSLYSG
SQ  YELLIEKFFERPFKSALEVYLYNIIKALLISLAQNNKVRFYSKVRLLGLTVDHSTVGASGVYPSLMSRVVYKHYRSLISE
SQ  ATTCFFLFEKGLHGNLNEEAKIHLETVEWARKFEAKERKYGDILMREGYTIDAIRVGDVQVEQQLFCQEVVELSAEELNK
SQ  YLQAKSQVLSSNIMNKHWDKPYFSQTRNISLKGMSGALQEDGHLAASVTLIEAIRFLNRSQTNPNVIDMYEQTKQHKAQA
SQ  RIVRKYQRTEADRGFFITTLPTRVRLEIIEDYYDAIARVVPEEYISYGGDKKILNIQTALEKALRWASGSSEVITSTGNV
SQ  IKFKRRLMYVSADATKWSPGDNSAKFKRFTQALYDGLSDEKLKCCVVDALRHVYETEFFMSRKLHRYIDSMDEHSEAVQD
SQ  FLDFFKGGVSATVKGNWLQGNLNKCSSLFGAAVSLLFRRIWAELFPELECFFEFAHHSDDALFIYGYLEPEDDGTDWFLY
SQ  VSQQIQAGNYHWHAVNQEMWKSMFNLHEHLLLMGSIKVSPKKTTVSPTNAEFLSTFFEGCAVSIPFIKILLGSLSDLPGL
SQ  GFFDDLAAAQSRCVKAMDLGASPQLAQLAVVICTSKVERLYGTADGMVNSPVAFLKVTKAHVPIPLGGDGSMSIMELATA
SQ  GIGMADKNILKQAFYSYKHTRRDGDRYVLGLFKFLMSLSEDVFQHDRLGEFSFVGKVQWKVFTPKNEFEFFDQFSQSYLK
SQ  SWTNQHPVYDYIIPRGRDNLLVYLVRKLNDPSIVTAMTMQSPLQLRFRMQAKQHMKVCKLEGEWVTFREVLAAADSFATK
SQ  YNPTEKDLDLFNTLVSCTFSKEYAWKDFLNEVRCEVVPTKHVHRSKIARTFTVREKDQAIQNPITAVIGYKYASTVDEIS
SQ  DVLDSSFFPDSLSADLQVMKEGVYRELGLDIGLPEVLKRIAPLLYKAGRSRVVIVEGNVEGTAESICSYWLRSMSLVKTI
SQ  KVRPKKEVLRAVSLYSTKENIGLQDDVAATRLCIEVWRWCKANDQNVNDWLNALYFEKQTLMDWVERFRRKGVVPIDPEI
SQ  QCIALLLYDVLGYKSVLQMQANRRAYSGKQYDAYCVQTYNEETRLYEGDLRVTFNFGLDCARLEIFWDKKEYILETSITQ
SQ  RHVLKLMMEEVTQELLRCGMRFKTEQVSHTRSLVLFKTESGFEWGKPNVPCIVFKHCALRTGLRTKQAINKEFMINVQAD
SQ  GFRAIAQMDMESPRFLLAHAYHTLRDVRYQAVQAVGNVWFQTAQHKLFINPIISSGLLENFMKGLPAAIPPAAYSLIMNK
SQ  AKISVDLFMFNELLALVNPRNVLNLDGIEETSEGYSTVTSISSRQWSEEVSLMADDDIDDEEEFTIALDDIDFEQINLDE
SQ  DIQHFLQDESAYTGDLTIQTEEVEVKRIRGVTRVLEPVKLIKSWVSKGLAIDKVYNPIGIVLMARYMSKNYDFSKIPLAL
SQ  LNPYDLTEFESVVKGWGETVNDRFLEVDNDAQRLVREKNILPEDILPDSLFSFRHVDVLLKRLFPHDPVSSFY
//
ID  Q9YQR5;
PN  cap-snatching endonuclease;
GN  L;
OS  1980494;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:15105534}.
DR  UNIPROT: Q9YQR5;
DR  Pfam: PF04196;
DR  Pfam: PF12426;
DR  PROSITE: PS50525;
DE  Function: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap- snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. Cleaves ssRNA substrates but not DNA (By similarity). Seems to downregulate the expression of its own and heterologous mRNAs through its endonuclease activity (By similarity). {ECO:0000250|UniProtKB:Q9E005}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0004519;
GO  GO:0046872;
GO  GO:0000166;
GO  GO:0003968;
GO  GO:0075526;
GO  GO:0006351;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKYTEIHNRMRECVPGEVSAVECLDLLDRFYAVRHDVVDQMIKHDWSDNKDKEQPIGHVLLMAGVPNEVIQGMEKKIIP
SQ  GSPSGQILRSFFKMTPDNYKITGSLIEFIEVTVTADVARGTREKILKYQAGLEYIEQLLHQESERGNLPGGYRIKFDVVA
SQ  VRTDGSNISTQWPSQRNEGVVQTMRLIQADINYVREHLIKNDERSALEAMFNLKFHVSGPKARTFDIPDYRPQQLCNPNI
SQ  DNLLNYCKNWLTREHEFAFDEVKGQRVFNIFEAEEIKHKERYNPSRKPRNFLLIQGTVQGPYLPSTIASDQYDTKVGCLE
SQ  ILKNHPETPIQILARDMALKYIMLDKDDLINYYNPRAYFKQTANIKEPGTFKLNLSSMDPKAKALLDVISKNSKKGVFGE
SQ  VIDSIEISSLIQQNECSKVIEKILSDLEINVGETSQGLDNPKRTTGVDDILKKFYDNELVKYMLHIVRKTTAWHMGHLLR
SQ  DITECLIAHAGLKRSKYWSIHGFSHGGILLMILPSKSLEVAGSYIRFFTVFKDGLGLIDYENLDSTVVIDGVSWCFSKVM
SQ  SLDLNRLLALNISFEKTLLATATWFQYYTEDQGHFPLQHALRSVFAFHFLLTVTQKMKLCAIFDNLRYLIPAVTSLYSGY
SQ  KPLIVKFFERPFKSALDVYLYTIIKTLLVSLAQNNKIRFYSKVRLLGLTVDQSTIGASGVYPSLMSRVVYKHYKSLISEA
SQ  TTCFFLFEKGLHGNLTEEAKIHLETVEWARKFSDKEKAYGAYIMEEGYTIKDVVDGNIPVEQQLFCQEVVELSAMELNTY
SQ  LEAKSQVMAANIMNKHWDRPYFSQTRNISLKGMSGALQEDGHLSASVTLIEAIRFLNQSQQNPSVLEMYEQTKRQKAMAR
SQ  IVRKYQRTEADRGFFITTLPTRVRLEIIEDYFDAIAKVVPEEYISYGGERKILNIQQALEKALRWASGESEIQISMGQVI
SQ  KLKRKLMYVSADATKWSPGDNSAKFRRFTQALHDGLRDDKLKRCVVDALRNIYETDFFMSRKLHRYIDGMDDLSEFVEDF
SQ  LSFFPNKVSAAIKGNWLQGNLNKCSSLFGAAVSLLFRKIWSLLYPELDCFFEFAHHSDDALFIYGYLEPTDDGTEWFRFV
SQ  TQQIQAGNLHWYAVNQEMWKSMFNLHEHILLMGSIKISPKKTTVSPTNAEFLSTFFEGCAVSIPFIKILLGSLSDLPGLG
SQ  YFDDLAAAQSRCVKALDMGACPQLAQLGIVLCTSKVERLYGTATGMVNNPTSFLKVERSSIPIPLGGDGSMSIMELATAG
SQ  IGMADKNVLKNAYISFKHTKRDSDRYILGLFKFLMSLSDDVFQHDRLGEFSFVGKVQWKVFTPKSEFEFFDQYSSKYLQL
SQ  WTEQHPVYDYIIPRGRDNLLVYLVRKLNDPSIVTAMTMQSPLQLRFRMQAKQHMKVCRLNGEWVTFREVLAAADSFAQSF
SQ  KPSQSDMELFQTLVNCTFSKEYAWRDFLNEVKCEVLTTRQVHRPKVARTFTVKERDQAIQNSITAVIGYKYANKADEISD
SQ  VLDSAVHPDSLSTDLQVMREGVYRELGLDINYPNVLKRVAPLLYKSGKSRVVIVQGNIEGTAESICSYWLKTMSLVKTIK
SQ  VRPKKEVLKAVSLFSKKEKIGDLTHLAATRLCIDVWRWCKANEQDPKAWLSALYFEGRTLMQWVDVFLDKGVVPVDPEIQ
SQ  CMGLMIYDLTGQKNLLQMQANRRAYSGKQYDAYCVQTYNEETKLYEGDLRVTFNFGIDCARLEIFWDKQDYLLETSITQR
SQ  HVLKILMEEVTKELLRCGMRFKTEQVNSSRSVVLFKTDAGFEWGKPNIPCIVFRNCALRTGLRVRHPINKSFTITIQAGG
SQ  FRAMAQLDEENPRFLLAHAYHNLKDIRYQALQAIGNIWFKTQQHKLFINPIISAGLLENFMKGLPAAIPPAAYSLIMNKA
SQ  KISVDLFMFNELLALINPKNVLNLDGIEETSEGYSTVSTISSTQWSEEVSLVMDDSDDEDQPDYTIDLDDIDFETIDLKE
SQ  DIEHFLQDESAYTGDLLIQTDDTEIKKLRGMTRILEPIKLIKSWVSKGLSIEKVYSPVGIILMARYMSKHYDFNKAPLSL
SQ  LNPYDLTEFESIVKGWGECVNDRFIEYDHEAERKVKEEKIQPEDVLPDSLFSFRHADILLRRLFPKDSAASFY
//
ID  Q9Y6R4;
PN  Mitogen-activated protein kinase kinase kinase 4;
GN  MAP3K4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized in perinuclear vesicular-like structures, probably Golgi-associated vesicles. {ECO:0000250}.
DR  UNIPROT: Q9Y6R4;
DR  UNIPROT: A6H8W0;
DR  UNIPROT: B7ZLD3;
DR  UNIPROT: B9EG75;
DR  UNIPROT: Q5VTT8;
DR  UNIPROT: Q5VTT9;
DR  UNIPROT: Q92612;
DR  UNIPROT: Q9H408;
DR  Pfam: PF19431;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 602425;
DR  DisGeNET: 4216;
DE  Function: Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. {ECO:0000269|PubMed:12052864, ECO:0000269|PubMed:9305639}.
DE  Reference Proteome: Yes;
DE  Interaction: P12270; IntAct: EBI-3443161; Score: 0.00
DE  Interaction: Q14289; IntAct: EBI-7426200; Score: 0.46
DE  Interaction: Q9NRD5; IntAct: EBI-21380388; Score: 0.00
DE  Interaction: P52564; IntAct: EBI-448103; Score: 0.52
DE  Interaction: Q9Y6R4; IntAct: EBI-448214; Score: 0.37
DE  Interaction: P24522; IntAct: EBI-448179; Score: 0.37
DE  Interaction: O75293; IntAct: EBI-448183; Score: 0.57
DE  Interaction: O95257; IntAct: EBI-448198; Score: 0.37
DE  Interaction: P29350; IntAct: EBI-7426234; Score: 0.40
DE  Interaction: P07355; IntAct: EBI-7426270; Score: 0.40
DE  Interaction: Q96B97; IntAct: EBI-7862134; Score: 0.59
DE  Interaction: P0CG48; IntAct: EBI-7862277; Score: 0.52
DE  Interaction: O75369; IntAct: EBI-8585510; Score: 0.50
DE  Interaction: Q7Z7A1; IntAct: EBI-3443147; Score: 0.00
DE  Interaction: P63104; IntAct: EBI-3443168; Score: 0.00
DE  Interaction: P60953; IntAct: EBI-6590248; Score: 0.27
DE  Interaction: P46734; IntAct: EBI-6590776; Score: 0.27
DE  Interaction: O15264; IntAct: EBI-6590847; Score: 0.27
DE  Interaction: Q562R1; IntAct: EBI-21540493; Score: 0.35
DE  Interaction: Q8N7X8; IntAct: EBI-21585341; Score: 0.35
DE  Interaction: Q5VX52; IntAct: EBI-21635815; Score: 0.35
DE  Interaction: Q06187; IntAct: EBI-21836035; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-20200875; Score: 0.35
DE  Interaction: Q9Y4C4; IntAct: EBI-20590738; Score: 0.44
DE  Interaction: P62851; IntAct: EBI-20903808; Score: 0.40
DE  Interaction: Q14137; IntAct: EBI-20912982; Score: 0.40
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004709;
GO  GO:0046872;
GO  GO:0106310;
GO  GO:0060718;
GO  GO:0035556;
GO  GO:0019100;
GO  GO:0000165;
GO  GO:0001890;
GO  GO:0043507;
GO  GO:1900745;
GO  GO:0051973;
GO  GO:1904355;
GO  GO:0032212;
GO  GO:0006468;
GO  GO:0010468;
GO  GO:0010225;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MREAAAALVPPPAFAVTPAAAMEEPPPPPPPPPPPPEPETESEPECCLAARQEGTLGDSACKSPESDLEDFSDETNTENL
SQ  YGTSPPSTPRQMKRMSTKHQRNNVGRPASRSNLKEKMNAPNQPPHKDTGKTVENVEEYSYKQEKKIRAALRTTERDRKKN
SQ  VQCSFMLDSVGGSLPKKSIPDVDLNKPYLSLGCSNAKLPVSVPMPIARPARQTSRTDCPADRLKFFETLRLLLKLTSVSK
SQ  KKDREQRGQENTSGFWLNRSNELIWLELQAWHAGRTINDQDFFLYTARQAIPDIINEILTFKVDYGSFAFVRDRAGFNGT
SQ  SVEGQCKATPGTKIVGYSTHHEHLQRQRVSFEQVKRIMELLEYIEALYPSLQALQKDYEKYAAKDFQDRVQALCLWLNIT
SQ  KDLNQKLRIMGTVLGIKNLSDIGWPVFEIPSPRPSKGNEPEYEGDDTEGELKELESSTDESEEEQISDPRVPEIRQPIDN
SQ  SFDIQSRDCISKKLERLESEDDSLGWGAPDWSTEAGFSRHCLTSIYRPFVDKALKQMGLRKLILRLHKLMDGSLQRARIA
SQ  LVKNDRPVEFSEFPDPMWGSDYVQLSRTPPSSEEKCSAVSWEELKAMDLPSFEPAFLVLCRVLLNVIHECLKLRLEQRPA
SQ  GEPSLLSIKQLVRECKEVLKGGLLMKQYYQFMLQEVLEDLEKPDCNIDAFEEDLHKMLMVYFDYMRSWIQMLQQLPQASH
SQ  SLKNLLEEEWNFTKEITHYIRGGEAQAGKLFCDIAGMLLKSTGSFLEFGLQESCAEFWTSADDSSASDEIRRSVIEISRA
SQ  LKELFHEARERASKALGFAKMLRKDLEIAAEFRLSAPVRDLLDVLKSKQYVKVQIPGLENLQMFVPDTLAEEKSIILQLL
SQ  NAAAGKDCSKDSDDVLIDAYLLLTKHGDRARDSEDSWGTWEAQPVKVVPQVETVDTLRSMQVDNLLLVVMQSAHLTIQRK
SQ  AFQQSIEGLMTLCQEQTSSQPVIAKALQQLKNDALELCNRISNAIDRVDHMFTSEFDAEVDESESVTLQQYYREAMIQGY
SQ  NFGFEYHKEVVRLMSGEFRQKIGDKYISFARKWMNYVLTKCESGRGTRPRWATQGFDFLQAIEPAFISALPEDDFLSLQA
SQ  LMNECIGHVIGKPHSPVTGLYLAIHRNSPRPMKVPRCHSDPPNPHLIIPTPEGFSTRSMPSDARSHGSPAAAAAAAAAAV
SQ  AASRPSPSGGDSVLPKSISSAHDTRGSSVPENDRLASIAAELQFRSLSRHSSPTEERDEPAYPRGDSSGSTRRSWELRTL
SQ  ISQSKDTASKLGPIEAIQKSVRLFEEKRYREMRRKNIIGQVCDTPKSYDNVMHVGLRKVTFKWQRGNKIGEGQYGKVYTC
SQ  ISVDTGELMAMKEIRFQPNDHKTIKETADELKIFEGIKHPNLVRYFGVELHREEMYIFMEYCDEGTLEEVSRLGLQEHVI
SQ  RLYSKQITIAINVLHEHGIVHRDIKGANIFLTSSGLIKLGDFGCSVKLKNNAQTMPGEVNSTLGTAAYMAPEVITRAKGE
SQ  GHGRAADIWSLGCVVIEMVTGKRPWHEYEHNFQIMYKVGMGHKPPIPERLSPEGKDFLSHCLESDPKMRWTASQLLDHSF
SQ  VKVCTDEE
//
ID  O08648;
PN  Mitogen-activated protein kinase kinase kinase 4;
GN  Map3k4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16157600}. Note=Localized in perinuclear vesicular- like structures, probably Golgi-associated vesicles.
DR  UNIPROT: O08648;
DR  UNIPROT: O08649;
DR  UNIPROT: O70124;
DR  UNIPROT: Q6PDG6;
DR  Pfam: PF19431;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. {ECO:0000269|PubMed:16157600, ECO:0000269|PubMed:9079650}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004709;
GO  GO:0046872;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0060718;
GO  GO:0048263;
GO  GO:0035556;
GO  GO:0019100;
GO  GO:0000165;
GO  GO:0001890;
GO  GO:0043507;
GO  GO:1900745;
GO  GO:0051973;
GO  GO:1904355;
GO  GO:0032212;
GO  GO:0006468;
GO  GO:0010468;
GO  GO:0010225;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRDAIAEPVPPPALADTPAAAMEELRPAPPPQPEPDPECCPAARQECMLGESARKSMESDPEDFSDETNTETLYGTSPPS
SQ  TPRQMKRLSAKHQRNSAGRPASRSNLKEKMNTPSQSPHKDLGKGVETVEEYSYKQEKKIRATLRTTERDHKKNAQCSFML
SQ  DSVAGSLPKKSIPDVDLNKPYLSLGCSNAKLPVSMPMPIARTARQTSRTDCPADRLKFFETLRLLLKLTSVSKKKDREQR
SQ  GQENTAAFWFNRSNELIWLELQAWHAGRTINDQDLFLYTARQAIPDIINEILTFKVNYGSIAFSSNGAGFNGPLVEGQCR
SQ  TPQETNRVGCSSYHEHLQRQRVSFEQVKRIMELLEYMEALYPSLQALQKDYERYAAKDFEDRVQALCLWLNITKDLNQKL
SQ  RIMGTVLGIKNLSDIGWPVFEIPSPRPSKGYEPEDEVEDTEVELRELESGTEESDEEPTPSPRVPELRLSTDAILDSRSQ
SQ  GCVSRKLERLESEEDSIGWGTADCGPEASRHCLTSIYRPFVDKALKQMGLRKLILRLHKLMNGSLQRARVALVKDDRPVE
SQ  FSDFPGPMWGSDYVQLSGTPPSSEQKCSAVSWEELRAMDLPSFEPAFLVLCRVLLNVIHECLKLRLEQRPAGEPSLLSIK
SQ  QLVRECKEVLKGGLLMKQYYQFMLQEVLGGLEKTDCNMDAFEEDLQKMLMVYFDYMRSWIQMLQQLPQASHSLKNLLEEE
SQ  WNFTKEITHYIRGGEAQAGKLFCDIAGMLLKSTGSFLESGLQESCAELWTSADDNGAADELRRSVIEISRALKELFHEAR
SQ  ERASKALGFAKMLRKDLEIAAEFVLSASARELLDALKAKQYVKVQIPGLENLHVFVPDSLAEEKKIILQLLNAATGKDCS
SQ  KDPDDVFMDAFLLLTKHGDRARDSEDGWGTWEARAVKIVPQVETVDTLRSMQVDNLLLVVMESAHLVLQRKAFQQSIEGL
SQ  MTVRHEQTSSQPIIAKGLQQLKNDALELCNRISDAIDRVDHMFTLEFDAEVEESESATLQQYYREAMIQGYNFGFEYHKE
SQ  VVRLMSGEFRQKIGDKYISFAQKWMNYVLTKCESGRGTRPRWATQGFDFLQAIEPAFISALPEDDFLSLQALMNECIGHV
SQ  IGKPHSPVTAIHRNSPRPVKVPRCHSDPPNPHLIIPTPEGFSTRSVPSDARTHGNSVAAAAAVAAAATTAAGRPGPGGGD
SQ  SVPAKPVNTAPDTRGSSVPENDRLASIAAELQFRSLSRHSSPTEERDEPAYPRSDSSGSTRRSWELRTLISQTKDSASKQ
SQ  GPIEAIQKSVRLFEERRYREMRRKNIIGQVCDTPKSYDNVMHVGLRKVTFKWQRGNKIGEGQYGKVYTCISVDTGELMAM
SQ  KEIRFQPNDHKTIKETADELKIFEGIKHPNLVRYFGVELHREEMYIFMEYCDEGTLEEVSRLGLQEHVIRLYTKQITVAI
SQ  NVLHEHGIVHRDIKGANIFLTSSGLIKLGDFGCSVKLKNNAQTMPGEVNSTLGTAAYMAPEVITRAKGEGHGRAADIWSL
SQ  GCVVIEMVTGKRPWHEYEHNFQIMYKVGMGHKPPIPERLSPEGKAFLSHCLESDPKIRWTASQLLDHAFVKVCTDEE
//
ID  P91193;
PN  Macoilin;
GN  maco;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Rough endoplasmic reticulum membrane {ECO:0000269|PubMed:21437263, ECO:0000269|PubMed:21589894}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:21437263}; Multi-pass membrane protein {ECO:0000255}. Note=Restricted to neuronal cell bodies, absent from dendrites and axons (PubMed:21437263). {ECO:0000269|PubMed:21437263}.
DR  UNIPROT: P91193;
DR  Pfam: PF09726;
DE  Function: Plays a role in the regulation of neuronal activity. In AWA and AWC neurons, plays a role in regulating olfactory adaptation by controlling the forgetting sensory responses to odorants such as diacetyl and isoamyl alcohol (PubMed:28924007). May play a role in regulating daf-7 expression in ASI neurons in response to bacterial small RNAs (PubMed:32908307). In ASI neurons, promotes dauer formation in response to pheromones such as the ascarosides ascr#2 and ascr#3 (PubMed:26976437). {ECO:0000269|PubMed:21437263, ECO:0000269|PubMed:21589894, ECO:0000269|PubMed:26976437, ECO:0000269|PubMed:28924007, ECO:0000269|PubMed:32908307}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0043025;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005791;
GO  GO:0030867;
GO  GO:0008017;
GO  GO:0006935;
GO  GO:0040011;
GO  GO:0023041;
GO  GO:0043052;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMQQQKPGKPKKINRIDKIKRLQINRSRRPDINQTVPSPLFYVRIVVTWLGMVSLDAMTGFRFELLWPTWLMIRAAAESI
SQ  QMRNQHCVTTIANPTAARFSVLFICVTATSDLICYLFIPIRMLIFLATTYVWISLYYHTQGGFLRSLATVYGGERLQSWP
SQ  IVFITCFIVIFELFLRIRSHPILISFFPNVAEYAGVSPVWPRSLNAFFGAHSIGYPVILITVSMHYYFNEWKLRRKQCDV
SQ  SNRNEQLFRILVEGLPAEYEGPKDYTSQQCLEDDLYYLDPPVQTLQPMQAIQAASATPPTSSKKNGIHKRNGDVTSSTTT
SQ  SSRKKKHNGNSGFNSTPPNDKKKGKSIRDVDMDDGDDSDDDYSYRDTSSSTIEDQRRGGGISIIRFIFSSAAWLFSFVFE
SQ  SSTPSENSLSNQQIDDDEDYEDGDGDKKNGRTDSMTSTTKGRANTMPSTTRSQNNNNSQKQQKQSNGKSHHQHSSHQNNH
SQ  QKSNGNSNGHARGFAAVRDSSHDTNASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLK
SQ  VEQMEIKCSSIERHRESDKHQLEQAERKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRI
SQ  ELKSKDESNMRMESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQEF
SQ  QIKNGSSIGGGSSETLMNGRSSTEANNENDTTASDQSSPHQHSAMGSPVPFAKMPLSVNVSNRHGSPFNGKVSPIASIGS
SQ  VLAAAGGPAPPDYMMAVGANVTATTGPVPQKQPRAGFHGISRYNEFTNIASGGEHRLFDTPASAISASAINGSNPEDDFL
SQ  MNKGKFGAPSQPAARLA
//
ID  Q2TLY2;
PN  Macoilin-1;
GN  Maco1a;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q7TQE6}; Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q2TLY2;
DR  UNIPROT: Q1L869;
DR  UNIPROT: Q2TLY0;
DR  Pfam: PF09726;
DE  Function: May play a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030867;
GO  GO:0008017;
GO  GO:0006935;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIHSSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSDIICLLFIPKQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQRQERETEEATSKGMSEADSVLVAQNGTAINK
SQ  KLPISLPELEYKEKGKDSAKDKKQQQHSIGINNNILQTVDAKLQDIEYMENHLNAKRLNNELGGSAENLFLKEEVGAGGG
SQ  SAPSKHYKNSSPRSHNSTNGSVPSSSSNRSDKKQKCTGKNLAPHRDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQAS
SQ  RQVEQDLRSQISSLSSAERSMRSELGQLRQENELLQNKLHNAVQAKQKDKQTIVQLEKRLKAEQEARAAVEKQLAEEKKR
SQ  KKMEEATAARAVALAAASRGECTDSLKSRIRELESECKKLTHDMKLKEEQIRELELKAQELHKYKENEKDTEVLMSALSA
SQ  MQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKEQEIKELKQKIAEVMAVMPSITYSAETNNMTPVTPHY
SQ  SSKFMDTSPSSLDPNASVYQPLKK
//
ID  Q2TLY1;
PN  Macoilin-2;
GN  maco1b;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q7TQE6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7TQE6}. Cell projection, axon {ECO:0000250|UniProtKB:Q7TQE6}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q2TLY1;
DR  UNIPROT: B7ZUY4;
DR  Pfam: PF09726;
DE  Function: May play a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030867;
GO  GO:0008017;
GO  GO:0006935;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQLIQRQEREAEEAAAAAAAAASKSIHDVDSPAVAQ
SQ  NGSAGGKKPSSNTLPELEYREKERGKNESKKQHNHNQNHHSSTSSSILPSVDNKAQEMEYMENHVNSKRLSSSDLLGSTE
SQ  NLLKDEHSSSSSSSTSSNSNKNYKNASGGGGGGGSSSPRGHGTANGSVPSSSGPSSSASSSSKGDRKQKYGGGKNSASHR
SQ  DPVENCIPNNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQA
SQ  KQKDKQTLGQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAECKKLTLDIK
SQ  VKEDQIRELELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQ
SQ  EIKDLKQKIAEVMAVMPSVVYSADTGSMTPVTPHYSSKFMDTSPSGLDPNASVYQPLKK
//
ID  Q2TLZ3;
PN  Macoilin;
GN  MACO1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P91193}; Multi- pass membrane protein {ECO:0000255}. Note=Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells. {ECO:0000250|UniProtKB:Q7TQE6}.
DR  UNIPROT: Q2TLZ3;
DR  Pfam: PF09726;
DE  Function: Plays a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0044306;
GO  GO:0031965;
GO  GO:0030867;
GO  GO:0045202;
GO  GO:0007420;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPAN
SQ  KKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSK
SQ  NYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKSPSAHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQAS
SQ  RQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKR
SQ  KKLEEATAARAVAFAAASRGECTETLRNRIRELEAEGKKLTMDMKVKEDQIRELELKVQELRKYKENEKDTEVLMSALSA
SQ  MQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAAASPLSPVSPHY
SQ  SSKFVETSPSGLDPNASVYQPLKK
//
ID  Q2TLZ1;
PN  Macoilin;
GN  MACO1;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P91193}; Multi- pass membrane protein {ECO:0000255}. Note=Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells. {ECO:0000250|UniProtKB:Q7TQE6}.
DR  UNIPROT: Q2TLZ1;
DR  Pfam: PF09726;
DE  Function: Plays a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0044306;
GO  GO:0031965;
GO  GO:0030867;
GO  GO:0045202;
GO  GO:0007420;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPAN
SQ  KKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSK
SQ  NYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKSPSTHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQAS
SQ  RQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKR
SQ  KKLEEATAARAVAFAAASRGECTETLRNRIRELEAEGKKLTMDMKVKEDQIRELELKVQELRKYKENEKDTEVLMSALSA
SQ  MQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAATSPLSPVSPHY
SQ  SSKFVETSPSGLDPNASVYQPLKK
//
ID  Q8N5G2;
PN  Macoilin;
GN  MACO1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q7TQE6}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:Q7TQE6}. Rough endoplasmic reticulum membrane {ECO:0000269|PubMed:21589894}; Multi-pass membrane protein {ECO:0000255}. Note=Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells. {ECO:0000250|UniProtKB:Q7TQE6}.
DR  UNIPROT: Q8N5G2;
DR  UNIPROT: B1AK00;
DR  UNIPROT: Q2TLX5;
DR  UNIPROT: Q2TLX6;
DR  UNIPROT: Q9NVG6;
DR  Pfam: PF09726;
DR  OMIM: 610301;
DR  DisGeNET: 55219;
DE  Function: Plays a role in the regulation of neuronal activity. {ECO:0000269|PubMed:21589894}.
DE  Reference Proteome: Yes;
DE  Interaction: O15198; IntAct: EBI-7259624; Score: 0.37
DE  Interaction: P28702; IntAct: EBI-2683504; Score: 0.00
DE  Interaction: A0A6L7HPH6; IntAct: EBI-2830137; Score: 0.00
DE  Interaction: A0A6L7H2Q9; IntAct: EBI-2830118; Score: 0.00
DE  Interaction: P42858; IntAct: EBI-9051540; Score: 0.37
DE  Interaction: E9QKK1; IntAct: EBI-10995761; Score: 0.35
DE  Interaction: P35278; IntAct: EBI-11012136; Score: 0.35
DE  Interaction: Q80SY4; IntAct: EBI-11073706; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104527; Score: 0.35
DE  Interaction: Q969M3; IntAct: EBI-11127233; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135399; Score: 0.35
DE  Interaction: Q86UK5; IntAct: EBI-11372136; Score: 0.27
DE  Interaction: Q96Q45; IntAct: EBI-11396533; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11398030; Score: 0.27
DE  Interaction: Q91B85; IntAct: EBI-11423711; Score: 0.37
DE  Interaction: Q6L8G8; IntAct: EBI-24291548; Score: 0.56
DE  Interaction: Q9UGL9; IntAct: EBI-24305412; Score: 0.56
DE  Interaction: Q5T752; IntAct: EBI-24309004; Score: 0.56
DE  Interaction: Q701N4; IntAct: EBI-24310314; Score: 0.56
DE  Interaction: P0DPK4; IntAct: EBI-24351641; Score: 0.56
DE  Interaction: Q92570; IntAct: EBI-25248670; Score: 0.56
DE  Interaction: P48745; IntAct: EBI-22746356; Score: 0.56
DE  Interaction: Q5T754; IntAct: EBI-24520187; Score: 0.56
DE  Interaction: Q5TA76; IntAct: EBI-24531368; Score: 0.56
DE  Interaction: P49901; IntAct: EBI-24625366; Score: 0.56
DE  Interaction: A0JP26; IntAct: EBI-23808076; Score: 0.56
DE  Interaction: Q8N720; IntAct: EBI-24763284; Score: 0.56
DE  Interaction: A8MW99; IntAct: EBI-23928235; Score: 0.56
DE  Interaction: Q5T753; IntAct: EBI-24373601; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24410810; Score: 0.56
DE  Interaction: Q5TA81; IntAct: EBI-24265291; Score: 0.56
DE  Interaction: Q8WZ59; IntAct: EBI-24553302; Score: 0.56
DE  Interaction: Q5T5B0; IntAct: EBI-24565659; Score: 0.56
DE  Interaction: P49639; IntAct: EBI-24568937; Score: 0.56
DE  Interaction: Q96FE5; IntAct: EBI-24583447; Score: 0.56
DE  Interaction: Q5T751; IntAct: EBI-24638348; Score: 0.56
DE  Interaction: Q9Y5I4; IntAct: EBI-21510892; Score: 0.35
DE  Interaction: Q16581; IntAct: EBI-21515265; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-21650356; Score: 0.35
DE  Interaction: Q9Y5F2; IntAct: EBI-21658599; Score: 0.35
DE  Interaction: O43505; IntAct: EBI-21751424; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q16659; IntAct: EBI-16814198; Score: 0.35
DE  Interaction: Q9UKM9; IntAct: EBI-20899752; Score: 0.40
DE  Interaction: P62937; IntAct: EBI-20909224; Score: 0.40
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: Q5JRV8; IntAct: EBI-21266273; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: A6NI28; IntAct: EBI-25410626; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC5; IntAct: EBI-25685699; Score: 0.35
DE  Interaction: P59596; IntAct: EBI-26376514; Score: 0.35
DE  Interaction: Q92729; IntAct: EBI-27116760; Score: 0.27
DE  Interaction: Q16832; IntAct: EBI-32717626; Score: 0.35
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0044306;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0030867;
GO  GO:0045202;
GO  GO:0008017;
GO  GO:0007420;
GO  GO:0006935;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPAN
SQ  KKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSK
SQ  NYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKSPSTHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQAS
SQ  RQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKR
SQ  KKLEEATAARAVAFAAASRGECTETLRNRIRELEAEGKKLTMDMKVKEDQIRELELKVQELRKYKENEKDTEVLMSALSA
SQ  MQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAATSPLSPVSPHY
SQ  SSKFVETSPSGLDPNASVYQPLKK
//
ID  Q2TLZ4;
PN  Macoilin;
GN  MACO1;
OS  9544;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P91193}; Multi- pass membrane protein {ECO:0000255}. Note=Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells. {ECO:0000250|UniProtKB:Q7TQE6}.
DR  UNIPROT: Q2TLZ4;
DR  UNIPROT: Q2TLX3;
DR  Pfam: PF09726;
DE  Function: Plays a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030867;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPAN
SQ  KKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSK
SQ  NYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKSPSTHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQAS
SQ  RQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKHNISQLEKKLKAEQEARSFVEKQLMEEKKR
SQ  KKLEEATAARAVAFAAASRGECTETLRNRIRELEAEGKKLTMDMKVKEDQIRELELKVQELRKYKENEKDTEVLMSALSA
SQ  MQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKELKQKIAEVMAVMPSITYSAATSPLSPVSPHY
SQ  SSKFVETSPSGLDPNASVYQPLKK
//
ID  Q7TQE6;
PN  Macoilin;
GN  Maco1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P91193}; Multi- pass membrane protein {ECO:0000255}. Note=Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells (PubMed:15255972). {ECO:0000269|PubMed:15255972}.
DR  UNIPROT: Q7TQE6;
DR  Pfam: PF09726;
DE  Function: Plays a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5F2C3; IntAct: EBI-20739590; Score: 0.37
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0043005;
GO  GO:0044306;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0030867;
GO  GO:0045202;
GO  GO:0008017;
GO  GO:0007420;
GO  GO:0006935;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPAN
SQ  KKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSK
SQ  NYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKGPSAHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQAS
SQ  RQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKR
SQ  KKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRKYKENEKDTEVLMSALSA
SQ  MQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAATSPLSPVSPHY
SQ  SSKFVETSPSGLDPNASVYQPLKK
//
ID  Q2TLZ5;
PN  Macoilin;
GN  MACO1;
OS  9598;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P91193}; Multi- pass membrane protein {ECO:0000255}. Note=Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells. {ECO:0000250|UniProtKB:Q7TQE6}.
DR  UNIPROT: Q2TLZ5;
DR  UNIPROT: Q2TLX4;
DR  Pfam: PF09726;
DE  Function: Plays a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0030867;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVVEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPAN
SQ  KKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSK
SQ  NYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKSPSTHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQAS
SQ  RQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKR
SQ  KKLEEATAARAVAFAAASRGECTETLRNRIRELEAEGKKLTMDMKVKEDQIRELELKVQELRKYKENEKDTEVLMSALSA
SQ  MQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAATSPLSPVSPHY
SQ  SSKFVETSPSGLDPNASVYQPLKK
//
ID  Q2TLZ2;
PN  Macoilin;
GN  MACO1;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P91193}; Multi- pass membrane protein {ECO:0000255}. Note=Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells. {ECO:0000250|UniProtKB:Q7TQE6}.
DR  UNIPROT: Q2TLZ2;
DR  Pfam: PF09726;
DE  Function: Plays a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0044306;
GO  GO:0031965;
GO  GO:0030867;
GO  GO:0045202;
GO  GO:0008017;
GO  GO:0007420;
GO  GO:0006935;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPAN
SQ  KKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSK
SQ  NYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKSPSAHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQAS
SQ  RQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKR
SQ  KKLEEATAARAVAFAAASRGECTETLRNRIRELEAEGKKLTMDMKVKEDQIRELELKVQELRKYKENEKDTEVLMSALSA
SQ  MQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAATSPLSPVSPHY
SQ  SSKFVETSPSGLDPNASVYQPLKK
//
ID  Q4V7D3;
PN  Macoilin;
GN  Maco1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P91193}; Multi- pass membrane protein {ECO:0000255}. Note=Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells. {ECO:0000250|UniProtKB:Q7TQE6}.
DR  UNIPROT: Q4V7D3;
DR  UNIPROT: Q2TLZ0;
DR  Pfam: PF09726;
DE  Function: Plays a role in the regulation of neuronal activity. {ECO:0000250|UniProtKB:Q8N5G2}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0016021;
GO  GO:0043005;
GO  GO:0044306;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0030867;
GO  GO:0045202;
GO  GO:0008017;
GO  GO:0007420;
GO  GO:0006935;
GO  GO:0023041;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFF
SQ  VCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIG
SQ  YPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPAN
SQ  KKLSTALPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSK
SQ  NYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQRCTSKGPSAHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQAS
SQ  RQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKRLKAEQEARGFVEKQLMEEKKR
SQ  KKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDLKVKEEQIRELELKVQELRKYKENEKDTEVLMSALSA
SQ  MQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAATSPLSPVSPHY
SQ  SSKFVETSPSGLDPNASVYQPLKK
//
ID  Q9LTY1;
PN  Mitotic spindle checkpoint protein MAD1;
GN  MAD1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:22457071}. Note=The nucleus envelope association requires the presence of NUA. {ECO:0000269|PubMed:22457071}.
DR  UNIPROT: Q9LTY1;
DR  Pfam: PF05557;
DE  Function: Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and delays the onset of anaphase when this process is not complete. It inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. Required for anchoring MAD2 to the nuclear envelope. {ECO:0000269|PubMed:22457071}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0007094;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MILRTPQPKRLRSDAGESPFPTGATGSGNQLIIYEDSPLPAPAPLQTSHDHSADQHLCTYQCRQMVKADVLDALSTAEKQ
SQ  VEESKTKLQTLNANFTEADAERKHFRDKFLYSEQELAAAKAREKMLQEQLLMEINNSQERYTKELQSCHELEVKLQNEMN
SQ  LRKKAESSAATAEEKAKLLEDKLTQLSGSVDREKKRLNNDIAQLGKEAKLSVARIGADLERMQCRAQNAETESNLLRSQL
SQ  EHLKLIFDECLQEKTEVDKKLSSFTSEAASSSDNSVLVKHLQEELKRYEAEVREARKLKSRHLDAELLNVNLLEEQSRRE
SQ  RAESELSKFHDLQLSMEKLENELSSWKSLLNDIPGVSCPDDIVMRFSVLQNEVVQSTMKIGEASTRIKQLEETLEAIQLG
SQ  RQNAVSEAALAKEKSEALKTDVKRIEVMLTLVTEEKEQLKAVVNELRKSNSEGSVSGAADGALIQGFESSLAKKENYIKD
SQ  LEQDLNQLKDVNNRQRTEIELLNEKLVDEARRNKSLERDSDRLRSEISLLESKLGHGDYSAANTRVLRMVNTLGVENEAK
SQ  QTIEALQAELQKTKERLQAVEELKSQSGDAGKLVDSHITGKIAQLKEQNATLEKREERYKTVFADRISVFRRACCELFGY
SQ  KIVMDEHQRPNGIPVTRFTLQSIYAQSDDEKLEFEYESGNTSILNNEYASQGDIAKQIEIFIRKFNSIPAFTANLTMESF
SQ  NRRTLY
//
ID  Q9LU93;
PN  Mitotic spindle checkpoint protein MAD2;
GN  MAD2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:19710914, ECO:0000269|PubMed:22457071}. Nucleus envelope {ECO:0000269|PubMed:22457071}. Chromosome {ECO:0000269|PubMed:19710914}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19710914}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19710914}. Cytoplasm {ECO:0000269|PubMed:19710914, ECO:0000269|PubMed:22457071}. Note=Cytoplasmic in interphase cells. Accumulates onto both kinetochores and the spindle microtubules in cell arrested in metaphase. Present in chromocenters. Associates with unattached kinetochores upon spindle assembly checkpoint (SAC) activation. The nucleus envelope association requires the presence of NUA. {ECO:0000269|PubMed:22457071}.
DR  UNIPROT: Q9LU93;
DR  UNIPROT: Q67YV5;
DR  Pfam: PF02301;
DR  PROSITE: PS50815;
DE  Function: Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and delays the onset of anaphase when this process is not complete. It inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. {ECO:0000269|PubMed:19710914}.
DE  Reference Proteome: Yes;
DE  Interaction: P92960; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: O82782; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q940Y8; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q9FIQ0; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q9SIH1; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q9ZVX3; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q9FLL1; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q8GXK3; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q9M0I4; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q9ZVJ4; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q9SZP8; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q9LW88; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q9SN19; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q6NLH0; IntAct: EBI-2131492; Score: 0.00
DE  Interaction: Q8LPJ4; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: O48802; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: Q9M0Z6; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: Q8GYU3; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: Q9FT72; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: Q9SF16; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: O64768; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: Q9C5C8; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: Q9SB63; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: Q93VP3; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: Q93ZX4; IntAct: EBI-2651676; Score: 0.00
DE  Interaction: Q9C774; IntAct: EBI-2651676; Score: 0.00
GO  GO:0010369;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005876;
GO  GO:0051301;
GO  GO:0007094;
GO  GO:0007346;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASKTAAAKDIITLHGSAAIVSEFFCYAANSILYNRAVYPEESFVKVKKYGLPMLLIEDESVKSFMSNLTSQISEWLEAG
SQ  KLQRVVLVIMSKATGEVLERWNFRIETDNEVVDKGVSREKSDKEIMREIQAIMRQVASSVTYLPCLDETCVFDVLAYTDT
SQ  DVAVPFTWIESDPKLIANPQMVKLHGFDTKIHKVDTLVSYKNDEWDEEE
//
ID  Q9M7N6;
PN  MFP1 attachment factor 1;
GN  MAF1;
OS  4081;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope. Cytoplasm. Golgi apparatus. Nucleus. Nucleus matrix. Note=Associated with the immature cell plate during cytokinesis. Accumulate in speckles of the cytoplasm belonging to the Golgi apparatus.
DR  UNIPROT: Q9M7N6;
DR  Pfam: PF13943;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P93203; IntAct: EBI-1112530; Score: 0.53
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0016363;
GO  GO:0048527;
GO  GO:0000278;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEIDSAQSQETVTQETQNKPMTTSFSIWPPTQRTRDAVINRLIESLSTPSILSKRYGTLPQDEASETARLIEEEAFAAA
SQ  GSTASDADDGIEILQVYSKEISKRMIDTVKSRSAPAAASEGESKPSELPADASEPSSASGLTGEVSSVETEP
//
ID  Q9HCI5;
PN  Melanoma-associated antigen E1;
GN  MAGEE1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=In the skeletal muscle, found at the postsynaptic membrane and is associated with a subset of myonuclei. May reside within nuclei and/or in perinuclear compartments. In peripheral nerves, colocalizes with DTNA in the Schwann cell membrane (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9HCI5;
DR  UNIPROT: Q5JXC7;
DR  UNIPROT: Q86TG0;
DR  UNIPROT: Q8TD92;
DR  UNIPROT: Q9H216;
DR  Pfam: PF01454;
DR  PROSITE: PS50838;
DR  OMIM: 300759;
DR  DisGeNET: 57692;
DE  Function: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. {ECO:0000269|PubMed:20864041}.
DE  Reference Proteome: Yes;
DE  Interaction: Q93009; IntAct: EBI-30844403; Score: 0.59
DE  Interaction: Q8ZAW9; IntAct: EBI-2865026; Score: 0.00
DE  Interaction: Q13263; IntAct: EBI-5651510; Score: 0.52
DE  Interaction: Q96D98; IntAct: EBI-24354283; Score: 0.68
DE  Interaction: P23508; IntAct: EBI-24430902; Score: 0.56
DE  Interaction: Q96RY5; IntAct: EBI-21858269; Score: 0.35
DE  Interaction: Q9ULH0; IntAct: EBI-21858269; Score: 0.35
DE  Interaction: Q9H6U6; IntAct: EBI-21858269; Score: 0.35
DE  Interaction: Q9BSU1; IntAct: EBI-21858269; Score: 0.35
DE  Interaction: Q8WXI9; IntAct: EBI-21858269; Score: 0.35
DE  Interaction: Q8N6I1; IntAct: EBI-21858269; Score: 0.35
DE  Interaction: Q2TBE0; IntAct: EBI-21858269; Score: 0.35
DE  Interaction: P49750; IntAct: EBI-21858269; Score: 0.35
DE  Interaction: P20936; IntAct: EBI-25373525; Score: 0.35
DE  Interaction: P30086; IntAct: EBI-25381702; Score: 0.35
GO  GO:0030425;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045211;
GO  GO:0000122;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLVSQNSRRRRRRVAKATAHNSSWGEMQAPNAPGLPADVPGSDVPQGPSDSQILQGLCASEGPSTSVLPTSAEGPSTFV
SQ  PPTISEASSASGQPTISEGPGTSVLPTPSEGLSTSGPPTISKGLCTSVTLAASEGRNTSRPPTSSEEPSTSVPPTASEVP
SQ  STSLPPTPGEGTSTSVPPTAYEGPSTSVVPTPDEGPSTSVLPTPGEGPGTSVPLAATEGLSTSVQATPDEGPSTSVPPTA
SQ  TEGLSTPVPPTRDEGPSTSVPATPGEGPSTSVLPAASDGQSISLVPTRGKGSSTSVPPTATEGLSTSVQPTAGEGSSTSV
SQ  PPTPGGGLSTSVPPTATEELSTSVPPTPGEGPSTSVLPIPGEGLSTSVPPTASDGSDTSVPPTPGEGASTLVQPTAPDGP
SQ  GSSVLPNPGEGPSTLFSSSASVDRNPSKCSLVLPSPRVTKASVDSDSEGPKGAEGPIEFEVLRDCESPNSISIMGLNTSR
SQ  VAITLKPQDPMEQNVAELLQFLLVKDQSKYPIRESEMREYIVKEYRNQFPEILRRAAAHLECIFRFELRELDPEAHTYIL
SQ  LNKLGPVPFEGLEESPNGPKMGLLMMILGQIFLNGNQAKEAEIWEMLWRMGVQRERRLSIFGNPKRLLSVEFVWQRYLDY
SQ  RPVTDCKPVEYEFFWGPRSHLETTKMKILKFMAKIYNKDPMDWPEKYNEALEEDAARAFAEGWQALPHFRRPFFEEAAAE
SQ  VPSPDSEVSSYSSKYAPHSWPESRLESKARKLVQLFLLMDSTKLPIPKKGILYYIGRECSKVFPDLLNRAARTLNHVYGT
SQ  ELVVLDPRNHSYTLYNRREMEETEEIVDSPNRPGNNFLMQVLSFIFIMGNHARESAVWAFLRGLGVQAGRKHVITCRYLS
SQ  QRYIDSLRVPDSDPVQYEFVWGPRARLETSKMKALRYVARIHRKEPQDWPQQYREAMEDEANRADVGHRQIFVHNFR
//
ID  Q9BE18;
PN  Melanoma-associated antigen E1;
GN  MAGEE1;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=In the skeletal muscle, found at the postsynaptic membrane and is associated with a subset of myonuclei. May reside within nuclei and/or in perinuclear compartments. In peripheral nerves, colocalizes with DTNA in the Schwann cell membrane (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9BE18;
DR  Pfam: PF01454;
DR  PROSITE: PS50838;
DE  Function: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030425;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045211;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLVSQNSRRRRRRVAKATAHNSSWDEMQAPNAPGFPADMPGSDVPQGPSDSQILQGLCASEGPSTSVLPTSAEGPSTFV
SQ  PPTISEASSASGQPTVSEGPGTSLLATPSEGLSTSGPPTISKGLCTSVTLAASEGRNTSRPPTSSEEPSTSVPATPGEGT
SQ  STSVPPTASEGPSTSVVPTPDEGPSTSVQSTAGEGPSTPVPLTATEGLSTSVPDTPDEGLSTSVPPTATEGLSTPVPPTP
SQ  DEGPSTSMPATPGEGRSTTMLPAASDGQSISLVPTPGKGSSTSGPPTATEGLSTSVQPTAGEGPSTSVPPTPCGGLSTSV
SQ  PPTPGEGLSTSVPPTATEGLSTSVPPTPGEGPSTSVLPTPGEGRSTSVPPTASDGSDTSVPPTPGEGPSTLVQPTASDRP
SQ  GSSVLPNPGEGPSTLFSSSASVDRNPSKCSIVLPSPRVTKASVDSDSEGPKGAEGPIEFEVLRDCESPNSITIMGLSTPR
SQ  VAITLKPQDPMEQNVAELLQFLLVKDQSKYPIRESEMREYIVKEYRNQFPEILRRAAAHLECIFRFELRELDPEARTYIL
SQ  LNKLGPVPFEGLEESPNGPKMGLLMMILGQIFLNGNQAKEAEICEMLWRMGVQRERRLSIFGNPKRLLSVEFVWQRYLDY
SQ  RPVTDCKPVEYEFFWGPRSHLETTKMKILKFMAKIYNKDPMDWPEQYNEALEEDAARAFAEGWQALPHFRRPFFEEAAAE
SQ  VASPDSEVSSYSSKYAPHSWPESRLESKARKLVQLFLLMDSTKLPIPKEGILYYIGRECSKVFPDLLNRAARTLNHVYGT
SQ  ELVVLDPRNHSYTLYNRREMEETEEIVDSPNRPGNNFLMQVLSFIFIMGNHARESAVWAFLRGLGVQSGRKHVITCRYLS
SQ  QRYIDSLRVPDSDPVQYEFVWGPRARLETSKMKALRYVARIHRKEPQDWPQQYREAMEDEANRADVGHRQFFVHNFR
//
ID  Q6PCZ4;
PN  Melanoma-associated antigen E1;
GN  Magee1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:14623885}. Nucleus {ECO:0000269|PubMed:14623885}. Cell membrane {ECO:0000269|PubMed:14623885}. Note=In the skeletal muscle, found at the postsynaptic membrane and is associated with a subset of myonuclei. May reside within nuclei and/or in perinuclear compartments. In peripheral nerves, colocalizes with DTNA in the Schwann cell membrane.
DR  UNIPROT: Q6PCZ4;
DR  UNIPROT: Q8BG82;
DR  UNIPROT: Q8BQ37;
DR  UNIPROT: Q99PB2;
DR  Pfam: PF01454;
DR  PROSITE: PS50838;
DE  Function: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8BP00; IntAct: EBI-4283417; Score: 0.35
GO  GO:0030425;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045211;
GO  GO:0000122;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLVSQNSRRRRGGRANARRNNGKGHPAAVPGPDVPRDRNDPKILQGLRASEGPGTSMLPTPREGPSASVPPTASEGSSA
SQ  PRQFIISQGPNTSEMPTSRKGRGASRPPAVSAGLNTAMSITASEGPNSPVPPTAPKGSKAYEHLPVSEGLAISEQRHSDG
SQ  GPNMEPTLGEGPGISVPPTFSEESGISDEGLSIFMSPNISEGPGINEPYSVSEDPSTSVPPTDSNGLGINLPPTFGEGLS
SQ  ISMLFSALEEPDIFAPPPSAEGLFASMSPPSGEIQSSWVSPIIMEGCNVNVPPTSKKGLRTSVPSAACESPSTSAEGLSS
SQ  SLSSISAEGFCSSLAPCAAEGSCELLPCGEGRSTSELHCLGEGSSTSQMSLAAEGPSASGMPTEANNPEEALSCCASERR
SQ  NKSTSRALQKAKDPSVRPKREDRFLDFQVLRDSKNSNSITIMGLGTSRVALTLKPQDPMEQNVAELLQFLLLKDQTKYPI
SQ  KESDMREFIDKDYRHQFPEILRRAAVHLECIFRFELKELDTEEHIYILLNKLGPVPFEGLEDVPNGPKMGLLMMILGHIL
SQ  LNGNQAREADIWEMLWRFGVQRERRLSVFGNVKRLLSVEFVWQRYLDYRPLTDCVPVEYEFYWGPRSRAETTKMKILKFM
SQ  AKIYNKDPMDWPALYNEALEEDADRVVVNNFRVARPFRRPLFAEVAPELDASGSKYSPHSWPESRLESKARKLVQLFLLM
SQ  DSTKLPIPKKGILYYIGRECTKVFPDLLNRAARTLNHVYGTELVVLDPRNHSYTLYNRREMEDTEEIMDSPNRPGNNFLM
SQ  QVLSFIFIMGNHARESAVWAFLRGLGVQNGRKHVITCRYLSQRYLDSLRVPDSDPVQYDFVWGPRARLETSKMKALRYVA
SQ  RIHRKEPEDWPEQYREAMEDEANRAEAGRRPLIVRNLR
//
ID  A1A5P9;
PN  Melanoma-associated antigen E1;
GN  Magee1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=In the skeletal muscle, found at the postsynaptic membrane and is associated with a subset of myonuclei. May reside within nuclei and/or in perinuclear compartments. In peripheral nerves, colocalizes with DTNA in the Schwann cell membrane (By similarity). {ECO:0000250}.
DR  UNIPROT: A1A5P9;
DR  Pfam: PF01454;
DR  PROSITE: PS50838;
DE  Function: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030425;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045211;
GO  GO:0000122;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLVSQNSRRRRGGRANGRKNSGKGRPAAVPGPAVPRDRSDPQILQGLGATEGPGTSVLPTPRGGSSTSVPPTASEGSSA
SQ  PGQLITSEGRNTSQLPTSRKGRGTRRPPAVSAGLNAAASITASEGASTPVLPTAPKGSKASEHLTISEGASISEQPQSHE
SQ  GPNVQPTLGEGSGTSVPPTFSEESGISEPLPSGEGLSISVSPTISEGAGINEPSPASKAPSTSVPPTASNGLGINLPPTS
SQ  SEGLSISVLFSASEESDISVPPPSAEGLSTSMPPPSGEVQSTWVPPIILEGCSVKVRSTSRKGRRTPVRSAACESPSPSA
SQ  ECLSTSLSSISAEGFCSSLAPCAEGSDTCELLPCGEGPSTSGLHDLEEESSISQMPLAAEGPSASGSSIEDENPEEALSC
SQ  GASVGMNLCKCTSLALQKADDPSVRPKRAEGFLDFQVLRDSENSNSITIMGLGTAHVALTLKPQDPMEQNVAELLQFLLL
SQ  KDQTKYPIKESEMREFIVQEYRNQFPEILRRAAAHLECIFRFELKELDPEEHTYILLNKLGPVPFEGLEDIPNGPKMGLL
SQ  MMILGQIFLNGNQAREADIWEMLWRFGVQRERRLSVFGNPKRLLSVEFVWQRYLDYRPITDCVPVEYEFYWGPRSHVETT
SQ  KMKILKFMARIYNKDPMDWPAQYNEALEEEAERDVPNNWRAVPHFRRPLFQEVSPELLASDSDAPGCPSKYSPHSWPESR
SQ  LESKSRKLVQLFLLMDSTKLPIPKKGILYYIGRECSKVFPDLLNRAARTLNHVYGTELVVLDPRNHSYTLYNRREMEDME
SQ  EIMDSPNRPGNNFLMQVLSFIFIMGNHARESAVWAFLRGLGVQNGRKHVITCRYLSQRYIDSLRVPDSDPVQYDFVWGPR
SQ  ARLETSKMKALRYVARIHRKEPQDWPDQYREALEDEANRAEAGRRPLVVRNLR
//
ID  Q3KP22;
PN  Membrane-anchored junction protein;
GN  MAJIN;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D992}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D992}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9D992}. Note=In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D992}.
DR  UNIPROT: Q3KP22;
DR  UNIPROT: B3KS99;
DR  UNIPROT: E9PPE5;
DR  PDB: 6GNX;
DR  PDB: 6GNY;
DR  PDB: 6J08;
DR  Pfam: PF15077;
DR  OMIM: 617130;
DR  DisGeNET: 283129;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the complex, MAJIN acts as the anchoring subunit to the nucleus inner membrane. MAJIN shows DNA-binding activity, possibly for the stabilization of telomere attachment on the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D992}.
DE  Reference Proteome: Yes;
DE  Interaction: P27658; IntAct: EBI-24669930; Score: 0.56
DE  Interaction: Q9BSW7; IntAct: EBI-24682491; Score: 0.56
DE  Interaction: Q8NHR7; IntAct: EBI-23751777; Score: 0.56
DE  Interaction: Q9Y5W9; IntAct: EBI-24744300; Score: 0.56
DE  Interaction: Q86WT6; IntAct: EBI-24767358; Score: 0.56
DE  Interaction: O43741; IntAct: EBI-24773475; Score: 0.56
DE  Interaction: P53350; IntAct: EBI-21859936; Score: 0.35
DE  Interaction: P26998; IntAct: EBI-21859936; Score: 0.35
GO  GO:0000781;
GO  GO:0005639;
GO  GO:0003677;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0045141;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLKPFTYPFPETRFLHAGPNVYKFKIRYGKSIRGEEIENKEVITQELEVPVEKKAVGAVMRKRKHMDEPSSPSRPGLDR
SQ  AKIGTSSQGPSKKKPPVETRRNRERKTQQGLQETLASDITDVQKQDSEWGHSLPGRIVPPLQHNSPPPKERAATGFFGFL
SQ  SSLFPFRYFFRKSSHS
//
ID  Q9D992;
PN  Membrane-anchored junction protein;
GN  Majin;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:26548954}; Single-pass membrane protein {ECO:0000305|PubMed:26548954}. Chromosome, telomere {ECO:0000269|PubMed:26548954}. Note=Localizes to telomeres throughout meiotic prophase I and disappears in metaphase I. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000269|PubMed:26548954}.
DR  UNIPROT: Q9D992;
DR  UNIPROT: E9Q4N4;
DR  Pfam: PF15077;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the complex, MAJIN acts as the anchoring subunit to the nucleus inner membrane. MAJIN shows DNA-binding activity, possibly for the stabilization of telomere attachment on the nucleus inner membrane. {ECO:0000269|PubMed:26548954}.
DE  Reference Proteome: Yes;
GO  GO:0000781;
GO  GO:0005639;
GO  GO:0003677;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0045141;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLKPFTYPFPETRFLHAGPNVYKFKIRYGNSIRGEEIEDKEVIVQELEDSIRAVLANMDSLQPFVTEHFIVFPYKSKWE
SQ  RVSHLKFKHGESILTPYPFVFTLYIEMKWFAEDLPSGKPADDIPLELVLAETEAEEATMRKWKRKLMEEPSSPSRQGPHR
SQ  AKMETSSEASSNKKPLKESKRSTDEEAQQEYQDTPASNAIAVKEQDAALGHGLQGLVVPPLQHSSPPPPKEPGARGFLGF
SQ  LSALFPFRYFFKKSGQ
//
ID  Q6AYM7;
PN  Membrane-anchored junction protein;
GN  Majin;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D992}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D992}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9D992}. Note=In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D992}.
DR  UNIPROT: Q6AYM7;
DR  Pfam: PF15077;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the complex, MAJIN acts as the anchoring subunit to the nucleus inner membrane. MAJIN shows DNA-binding activity, possibly for the stabilization of telomere attachment on the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D992}.
DE  Reference Proteome: Yes;
GO  GO:0000781;
GO  GO:0005639;
GO  GO:0003677;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0045141;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLKPFTYPFPETRFLHAGTNVYKFKIRYGNSIRGEEIEDKGVIIQELEDSIRAVLANMDSLQPFVTEHFIVFPYKSKWE
SQ  RVSHLKFKHGEIILTPYPFVFTLYIEMKCFAESLPSGKPTDDIPLELVLTAKEAEEATMRKRKLMEEPSTPSRPGPHRAK
SQ  METWSEASSTKKALKEHKRSWGEDSQQDTPASDSTAVTEQDPMLGHSLPGLVVPPLEHSNPPPLKEPAARGFLGFLSALF
SQ  PFRYFFRKSTQ
//
ID  P20484;
PN  Protein MAK11;
GN  MAK11;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleolus {ECO:0000269|PubMed:2826479}. Nucleus membrane {ECO:0000269|PubMed:2826479}; Peripheral membrane protein {ECO:0000269|PubMed:2826479}. Note=Membrane associated.
DR  UNIPROT: P20484;
DR  UNIPROT: D6VXR4;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Essential for cell growth. Plays a role in assembly of 60S pre-ribosomal particles in the nucleolus. Also required for replication of the M1 double-stranded RNA of the L-A virus. This latter function may reflect an enhanced requirement for free 60S ribosomal particles for the translation of viral mRNAs which lack poly-A tails. {ECO:0000269|PubMed:12808088, ECO:0000269|PubMed:2826479, ECO:0000269|PubMed:7739558}.
DE  Reference Proteome: Yes;
DE  Interaction: P53136; IntAct: EBI-801364; Score: 0.35
DE  Interaction: Q12024; IntAct: EBI-801364; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-801364; Score: 0.53
DE  Interaction: Q05022; IntAct: EBI-801364; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-801364; Score: 0.35
DE  Interaction: Q03532; IntAct: EBI-801364; Score: 0.35
DE  Interaction: P39014; IntAct: EBI-859327; Score: 0.00
DE  Interaction: Q12329; IntAct: EBI-3829080; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-6556984; Score: 0.35
DE  Interaction: Q06511; IntAct: EBI-10706275; Score: 0.57
DE  Interaction: P0CX43; IntAct: EBI-10916915; Score: 0.35
DE  Interaction: Q07915; IntAct: EBI-10916915; Score: 0.35
DE  Interaction: P36160; IntAct: EBI-10918966; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53261; IntAct: EBI-16273123; Score: 0.35
DE  Interaction: Q12522; IntAct: EBI-16273123; Score: 0.35
DE  Interaction: P40991; IntAct: EBI-16273123; Score: 0.35
DE  Interaction: P22147; IntAct: EBI-16273123; Score: 0.35
DE  Interaction: P53119; IntAct: EBI-16273123; Score: 0.35
DE  Interaction: Q04660; IntAct: EBI-16273123; Score: 0.35
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0000466;
GO  GO:0000463;
GO  GO:0000027;
GO  GO:0042273;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:2826479};
SQ  MSAIGDKNQFRIIVGSYEHNILCLSLDIPNQKENDAAKTPHFMPIFHFQAHSLSIKCLAVSRRYLVSGSNDEHIRIYDLQ
SQ  KRKELGTLLSHQGSITALQFSHPASSSEDAAVSKGSKNSKWLLSASEDHKIMVWRVKDWETVGTLKGHTARVNDVDIHPT
SQ  NRIAISVSDDHSIRLWNLMTLRNAAVLKLRKYNTNGTCVRWLGAKGDYFAVGLRDRVLIYETGSAKVFKEIVFQRKTLMH
SQ  IETHILPFDNKEYLSVGISDGNVHFYPCEELFEKVEENEKQEDDDDKEDISPAFSLLGHTNRIKDFKFYTNEFGTYLVTI
SQ  GSDGKIVVWDMSTKEQVAVYDCGERLNCLTLCDESIEKYNTMKKRDAETADIGDQSEVESDTEELKKIMFGEKKKLNKKK
SQ  RKQLKKSKVSVELE
//
ID  Q969L2;
PN  Protein MAL2;
GN  MAL2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Endomembrane system. Cytoplasm, perinuclear region. Note=Associated with lipid rafts. In polarized epithelial cells, restricted to the apical surface. In hepatocytes, as well as in polarized hepatoma Hep-G2 cells, found in the canalicular membrane, equivalent to the apical surface, beneath the canalicular actin cytoskeleton. In non-polarized Hep-G2 cells, distributed to the perinuclear region.
DR  UNIPROT: Q969L2;
DR  UNIPROT: B2R520;
DR  UNIPROT: Q6ZMD9;
DR  Pfam: PF01284;
DR  PROSITE: PS51225;
DR  OMIM: 609684;
DR  DisGeNET: 114569;
DE  Function: Member of the machinery of polarized transport. Required for the indirect transcytotic route at the step of the egress of the transcytosing cargo from perinuclear endosomes in order for it to travel to the apical surface via a raft-dependent pathway. {ECO:0000269|PubMed:12370246}.
DE  Reference Proteome: Yes;
DE  Interaction: P55327; IntAct: EBI-944304; Score: 0.37
DE  Interaction: Q9H221; IntAct: EBI-3943706; Score: 0.37
DE  Interaction: P62136; IntAct: EBI-5564558; Score: 0.37
DE  Interaction: P43378; IntAct: EBI-10209175; Score: 0.67
DE  Interaction: P53365; IntAct: EBI-10213310; Score: 0.72
DE  Interaction: Q05329; IntAct: EBI-10223597; Score: 0.72
DE  Interaction: Q5JS98; IntAct: EBI-10244469; Score: 0.56
DE  Interaction: Q5ST30; IntAct: EBI-10244973; Score: 0.56
DE  Interaction: Q5SU16; IntAct: EBI-10245042; Score: 0.56
DE  Interaction: Q6FGM0; IntAct: EBI-10249609; Score: 0.56
DE  Interaction: Q6IQ43; IntAct: EBI-10250437; Score: 0.56
DE  Interaction: Q969Z0; IntAct: EBI-10281551; Score: 0.56
DE  Interaction: Q96AX2; IntAct: EBI-10282129; Score: 0.56
DE  Interaction: Q9BU27; IntAct: EBI-10298617; Score: 0.56
DE  Interaction: P00431; IntAct: EBI-11522771; Score: 0.56
DE  Interaction: P04819; IntAct: EBI-11522898; Score: 0.56
DE  Interaction: P32453; IntAct: EBI-11525358; Score: 0.56
DE  Interaction: P34897; IntAct: EBI-16437285; Score: 0.56
DE  Interaction: A8MRB1; IntAct: EBI-16437275; Score: 0.56
DE  Interaction: Q9ULP0; IntAct: EBI-16437265; Score: 0.72
DE  Interaction: A0A0S2Z4D9; IntAct: EBI-16437255; Score: 0.56
DE  Interaction: Q99259; IntAct: EBI-16437245; Score: 0.72
DE  Interaction: Q9BSJ6; IntAct: EBI-16437235; Score: 0.56
DE  Interaction: Q5VYK3; IntAct: EBI-24295491; Score: 0.56
DE  Interaction: Q9UKF7; IntAct: EBI-24304896; Score: 0.56
DE  Interaction: Q9UBD0; IntAct: EBI-24305130; Score: 0.56
DE  Interaction: Q8WY91; IntAct: EBI-24306725; Score: 0.56
DE  Interaction: Q96AL5; IntAct: EBI-24333526; Score: 0.56
DE  Interaction: P49638; IntAct: EBI-24344012; Score: 0.56
DE  Interaction: Q9Y371; IntAct: EBI-24351738; Score: 0.72
DE  Interaction: Q99961; IntAct: EBI-25252609; Score: 0.56
DE  Interaction: Q96E29; IntAct: EBI-24498551; Score: 0.56
DE  Interaction: Q9NQG6; IntAct: EBI-22732927; Score: 0.56
DE  Interaction: Q9HB07; IntAct: EBI-22734634; Score: 0.56
DE  Interaction: Q9BW92; IntAct: EBI-22733879; Score: 0.56
DE  Interaction: Q8NI60; IntAct: EBI-24373384; Score: 0.56
DE  Interaction: Q9UGP5; IntAct: EBI-25265360; Score: 0.56
DE  Interaction: Q9H6H4; IntAct: EBI-24686147; Score: 0.56
DE  Interaction: O15342; IntAct: EBI-24696156; Score: 0.56
DE  Interaction: Q9NQQ7; IntAct: EBI-24702032; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-24712148; Score: 0.56
DE  Interaction: P08034; IntAct: EBI-24724178; Score: 0.56
DE  Interaction: Q8NET5; IntAct: EBI-23826916; Score: 0.56
DE  Interaction: P34810; IntAct: EBI-24768375; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-25275978; Score: 0.56
DE  Interaction: Q9NY72; IntAct: EBI-25279023; Score: 0.56
DE  Interaction: O95971; IntAct: EBI-24374871; Score: 0.56
DE  Interaction: Q9P2R7; IntAct: EBI-24398006; Score: 0.56
DE  Interaction: O00141; IntAct: EBI-24398525; Score: 0.56
DE  Interaction: Q6IN84; IntAct: EBI-24537360; Score: 0.56
DE  Interaction: Q96BA8; IntAct: EBI-24555371; Score: 0.56
DE  Interaction: Q3SXY8; IntAct: EBI-25171682; Score: 0.56
DE  Interaction: P15941; IntAct: EBI-24747016; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-24799535; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-25222259; Score: 0.56
DE  Interaction: P55212; IntAct: EBI-25835921; Score: 0.56
DE  Interaction: P13473; IntAct: EBI-25874292; Score: 0.56
DE  Interaction: P13569; IntAct: EBI-27087549; Score: 0.35
GO  GO:0016324;
GO  GO:0070062;
GO  GO:0098978;
GO  GO:0098686;
GO  GO:0016021;
GO  GO:0030285;
GO  GO:0045121;
GO  GO:0048471;
GO  GO:0019911;
GO  GO:0042552;
GO  GO:0045056;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAGGASVPPPPNPAVSFPPPRVTLPAGPDILRTYSGAFVCLEILFGGLVWILVASSNVPLPLLQGWVMFVSVTAFFFSL
SQ  LFLGMFLSGMVAQIDANWNFLDFAYHFTVFVFYFGAFLLEAAATSLHDLHCNTTITGQPLLSDNQYNINVAASIFAFMTT
SQ  ACYGCSLGLALRRWRP
//
ID  Q9UDY8;
PN  Mucosa-associated lymphoid tissue lymphoma translocation protein 1;
GN  MALT1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16123224}. Nucleus {ECO:0000269|PubMed:16123224}. Note=Shuttles between the nucleus and cytoplasm. Found in perinuclear structures together with BCL10. {ECO:0000269|PubMed:16123224}.
DR  UNIPROT: Q9UDY8;
DR  UNIPROT: Q9NTB7;
DR  UNIPROT: Q9ULX4;
DR  PDB: 2G7R;
DR  PDB: 3BFO;
DR  PDB: 3K0W;
DR  PDB: 3UO8;
DR  PDB: 3UOA;
DR  PDB: 3V4O;
DR  PDB: 3V55;
DR  PDB: 4I1P;
DR  PDB: 4I1R;
DR  PDB: 6F7I;
DR  PDB: 6GK2;
DR  PDB: 6H4A;
DR  PDB: 6YN8;
DR  PDB: 6YN9;
DR  PDB: 7A41;
DR  PDB: 7AK0;
DR  PDB: 7AK1;
DR  PDB: 7PAV;
DR  PDB: 7PAW;
DR  Pfam: PF13895;
DR  Pfam: PF18703;
DR  PROSITE: PS50208;
DR  PROSITE: PS50835;
DR  OMIM: 604860;
DR  OMIM: 615468;
DR  DisGeNET: 10892;
DE  Function: Protease that enhances BCL10-induced activation: acts via formation of CBM complexes that channel adaptive and innate immune signaling downstream of CARD domain-containing proteins (CARD9, CARD11 and CARD14) to activate NF-kappa-B and MAP kinase p38 pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:11262391, PubMed:18264101, PubMed:24074955). Mediates BCL10 cleavage: MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion (PubMed:11262391, PubMed:18264101). Involved in the induction of T helper 17 cells (Th17) differentiation (PubMed:11262391, PubMed:18264101). Cleaves RC3H1 and ZC3H12A in response to T-cell receptor (TCR) stimulation which releases their cooperatively repressed targets to promote Th17 cell differentiation (By similarity). Also mediates cleavage of N4BP1 in T-cells following TCR-mediated activation, leading to N4BP1 inactivation (PubMed:31133753). May also have ubiquitin ligase activity: binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity (PubMed:14695475). {ECO:0000250|UniProtKB:Q2TBA3, ECO:0000269|PubMed:11262391, ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:18264101, ECO:0000269|PubMed:24074955, ECO:0000269|PubMed:31133753}.
DE  Disease: Immunodeficiency 12 (IMD12) [MIM:615468]: A primary immunodeficiency characterized by onset in infancy of recurrent bacterial and candidal infections resulting in bronchiectasis and growth delay. Manifestations include mastoiditis, aphthous ulcers, cheilitis, gingivitis, esophagitis, gastritis, duodenitis, and meningitis. Levels of absolute lymphocytes and serum immunoglobulins are normal, but specific antibody titers are low despite immunization, and T-cells show impaired proliferative responses to mitogens. {ECO:0000269|PubMed:23727036}. Note=The disease is caused by variants affecting the gene represented in this entry. Note=A chromosomal aberration involving MALT1 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with BIRC2. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma. {ECO:0000269|PubMed:10339464, ECO:0000269|PubMed:10523859, ECO:0000269|PubMed:10702396, ECO:0000269|PubMed:11090634}.
DE  Reference Proteome: Yes;
DE  Interaction: O43463; IntAct: EBI-8474830; Score: 0.37
DE  Interaction: O95999; IntAct: EBI-7661911; Score: 0.92
DE  Interaction: Q05655; IntAct: EBI-11692872; Score: 0.40
DE  Interaction: Q92905; IntAct: EBI-7006117; Score: 0.35
DE  Interaction: Q13501; IntAct: EBI-8585097; Score: 0.52
DE  Interaction: P40337; IntAct: EBI-1066026; Score: 0.00
DE  Interaction: P60604; IntAct: EBI-1075706; Score: 0.00
DE  Interaction: Q04759; IntAct: EBI-7334632; Score: 0.40
DE  Interaction: P0CG48; IntAct: EBI-7661943; Score: 0.52
DE  Interaction: Q9NYJ8; IntAct: EBI-7662076; Score: 0.40
DE  Interaction: Q9Y6K9; IntAct: EBI-7661964; Score: 0.66
DE  Interaction: Q9Y4K3; IntAct: EBI-7662154; Score: 0.69
DE  Interaction: O43318; IntAct: EBI-7662088; Score: 0.40
DE  Interaction: Q9BXL7; IntAct: EBI-7662385; Score: 0.59
DE  Interaction: Q13098; IntAct: EBI-7006294; Score: 0.35
DE  Interaction: P98078; IntAct: EBI-6100356; Score: 0.35
DE  Interaction: Q14790; IntAct: EBI-6262854; Score: 0.50
DE  Interaction: Q9H257; IntAct: EBI-6253076; Score: 0.35
DE  Interaction: Q9ULZ3; IntAct: EBI-6253076; Score: 0.35
DE  Interaction: O60341; IntAct: EBI-8474867; Score: 0.37
DE  Interaction: Q86X55; IntAct: EBI-8474887; Score: 0.37
DE  Interaction: Q96LA8; IntAct: EBI-8474924; Score: 0.37
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9H0F6; IntAct: EBI-11692007; Score: 0.40
DE  Interaction: Q13489; IntAct: EBI-11691703; Score: 0.35
DE  Interaction: Q96JP0; IntAct: EBI-24331393; Score: 0.56
DE  Interaction: Q9BSK4; IntAct: EBI-24485236; Score: 0.56
DE  Interaction: Q96RU8; IntAct: EBI-21873209; Score: 0.35
DE  Interaction: P48729; IntAct: EBI-15748744; Score: 0.50
DE  Interaction: O14920; IntAct: EBI-15748744; Score: 0.35
DE  Interaction: Q9UDY8; IntAct: EBI-15958502; Score: 0.56
DE  Interaction: Q13114; IntAct: EBI-16718612; Score: 0.40
DE  Interaction: P0DOF2; IntAct: EBI-25607852; Score: 0.35
DE  Interaction: G5E9A7; IntAct: EBI-25842596; Score: 0.56
DE  Interaction: P50570; IntAct: EBI-25844932; Score: 0.56
DE  Interaction: P28799; IntAct: EBI-25860949; Score: 0.56
DE  Interaction: P04792; IntAct: EBI-25870865; Score: 0.56
DE  Interaction: O14832; IntAct: EBI-25882171; Score: 0.56
DE  Interaction: P60891; IntAct: EBI-25886436; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25898191; Score: 0.56
DE  Interaction: P46379; IntAct: EBI-25903821; Score: 0.56
DE  Interaction: O14901; IntAct: EBI-25905104; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25915339; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25931695; Score: 0.56
DE  Interaction: P54252; IntAct: EBI-25974833; Score: 0.56
DE  Interaction: Q96PU8; IntAct: EBI-26969019; Score: 0.40
GO  GO:0032449;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0001650;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0002096;
GO  GO:0032991;
GO  GO:0004197;
GO  GO:0004175;
GO  GO:0042802;
GO  GO:0008233;
GO  GO:0002020;
GO  GO:0043621;
GO  GO:0036094;
GO  GO:0004842;
GO  GO:0007250;
GO  GO:0042113;
GO  GO:0001923;
GO  GO:0006952;
GO  GO:0045087;
GO  GO:0031663;
GO  GO:0043066;
GO  GO:0051168;
GO  GO:0043280;
GO  GO:0043123;
GO  GO:0032731;
GO  GO:0032743;
GO  GO:0051092;
GO  GO:0031398;
GO  GO:0002726;
GO  GO:2000321;
GO  GO:0006508;
GO  GO:0051603;
GO  GO:0042981;
GO  GO:0050856;
GO  GO:0009620;
GO  GO:0042098;
GO  GO:0050852;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLLGDPLQALPPSAAPTGPLLAPPAGATLNRLREPLLRRLSELLDQAPEGRGWRRLAELAGSRGRLRLSCLDLEQCSLK
SQ  VLEPEGSPSLCLLKLMGEKGCTVTELSDFLQAMEHTEVLQLLSPPGIKITVNPESKAVLAGQFVKLCCRATGHPFVQYQW
SQ  FKMNKEIPNGNTSELIFNAVHVKDAGFYVCRVNNNFTFEFSQWSQLDVCDIPESFQRSVDGVSESKLQICVEPTSQKLMP
SQ  GSTLVLQCVAVGSPIPHYQWFKNELPLTHETKKLYMVPYVDLEHQGTYWCHVYNDRDSQDSKKVEIIIGRTDEAVECTED
SQ  ELNNLGHPDNKEQTTDQPLAKDKVALLIGNMNYREHPKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMRNAVDEFLL
SQ  LLDKGVYGLLYYAGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCRKRNDYDDTIPILDAL
SQ  KVTANIVFGYATCQGAEAFEIQHSGLANGIFMKFLKDRLLEDKKITVLLDEVAEDMGKCHLTKGKQALEIRSSLSEKRAL
SQ  TDPIQGTEYSAESLVRNLQWAKAHELPESMCLKFDCGVQIQLGFAAEFSNVMIIYTSIVYKPPEIIMCDAYVTDFPLDLD
SQ  IDPKDANKGTPEETGSYLVSKDLPKHCLYTRLSSLQKLKEHLVFTVCLSYQYSGLEDTVEDKQEVNVGKPLIAKLDMHRG
SQ  LGRKTCFQTCLMSNGPYQSSAATSGGAGHYHSLQDPFHGVYHSHPGNPSNVTPADSCHCSRTPDAFISSFAHHASCHFSR
SQ  SNVPVETTDEIPFSFSDRLRISEK
//
ID  Q2TBA3;
PN  Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog;
GN  Malt1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UDY8}. Nucleus {ECO:0000250|UniProtKB:Q9UDY8}. Note=Shuttles between the nucleus and cytoplasm. Found in perinuclear structures together with BCL10 (By similarity). {ECO:0000250|UniProtKB:Q9UDY8}.
DR  UNIPROT: Q2TBA3;
DR  UNIPROT: Q2TBA2;
DR  UNIPROT: Q811E3;
DR  UNIPROT: Q8BFT0;
DR  UNIPROT: Q8C7N9;
DR  PDB: 3V4L;
DR  Pfam: PF13895;
DR  Pfam: PF18703;
DR  PROSITE: PS50208;
DR  PROSITE: PS50835;
DE  Function: Protease that enhances BCL10-induced activation: acts via formation of CBM complexes that channel adaptive and innate immune signaling downstream of CARD domain-containing proteins (CARD9, CARD11 and CARD14) to activate NF-kappa-B and MAP kinase p38 pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (By similarity). Mediates BCL10 cleavage: MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor- induced integrin adhesion (By similarity). Involved in the induction of T helper 17 cells (Th17) differentiation (By similarity). Cleaves RC3H1 and ZC3H12A in response to T-cell receptor (TCR) stimulation which releases their cooperatively repressed targets to promote Th17 cell differentiation (PubMed:25282160). Also mediates cleavage of N4BP1 in T-cells following TCR-mediated activation, leading to N4BP1 inactivation. May also have ubiquitin ligase activity: binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity (By similarity). {ECO:0000250|UniProtKB:Q9UDY8, ECO:0000269|PubMed:25282160}.
DE  Reference Proteome: Yes;
DE  Interaction: P47741; IntAct: EBI-15909866; Score: 0.35
DE  Interaction: Q60855; IntAct: EBI-15909932; Score: 0.35
DE  Interaction: Q60803; IntAct: EBI-16718608; Score: 0.40
GO  GO:0032449;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0001650;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0002096;
GO  GO:0032991;
GO  GO:0004197;
GO  GO:0004175;
GO  GO:0042802;
GO  GO:0019209;
GO  GO:0008233;
GO  GO:0002020;
GO  GO:0043621;
GO  GO:0004842;
GO  GO:0007250;
GO  GO:0042113;
GO  GO:0001923;
GO  GO:0071222;
GO  GO:0045087;
GO  GO:0031663;
GO  GO:0051168;
GO  GO:0043280;
GO  GO:0032731;
GO  GO:0032743;
GO  GO:0051092;
GO  GO:0050870;
GO  GO:0002726;
GO  GO:2000321;
GO  GO:0006508;
GO  GO:0051603;
GO  GO:0042981;
GO  GO:0050856;
GO  GO:0009620;
GO  GO:0042098;
GO  GO:0050852;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLWGQPLQASPPLAVRQPPTASSGPSTSPPAGATLNRLPEPLLRRLSESLDRAPEGRGWRQLAELAGSRGRLRLSGLDL
SQ  EQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDFLQALEHTEVLPLLNPPGLKITVNPESKAVLAGQFVKLCCRATGHP
SQ  FVQYQWFKMNKEIPYGNSSELVFNTVHVKDAGFYVCRVNNSSTFEFSQWSQLDVCDVAEVTDSFQGSMDGISESRLQICV
SQ  EPRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKHYTVPYVDIEHEGTYWCHVYNDRDSQDSKKAEVTIGRT
SQ  DEAVECTEDELNNLGHPDNKEQTGQPLAKDKVALLIGNMSYWEHPKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMC
SQ  NAVDEFLLLLDKGVYGLLYYAGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCRKRNDYDD
SQ  TIPILDALKVTANIVFGYATCQGAEAFEIQHSGLANGIFMKFLKDRLLEDKKITVLLDEVAEDMGKCHLTKGRQALEIRS
SQ  SLSEKRALTDPVQGAPCSAEALVRNLQWAKAHELPESMCLKFQCGVHIQLGFAAEFSNVMIIYTSIVHKPPEIIMCDAYV
SQ  TDFPLDLDIDPKHANKGTPEETGSYLVSKDLPKHCLYTRLSSLQKLKEHLIFTVCLSYQYSGLEDTVEEKQEVNVGKPLI
SQ  AKLDMHRGLGRKTCFQACRMPDEPYHSSTSTSAGAGHFHSSQDSFHDVYHSHLGNADSGMPPDRCHCSRTPHTFISNYPP
SQ  HHYCQFGRSNVPVETTDEMPFSFSDRLMISEN
//
ID  Q7JRE4;
PN  Inner nuclear membrane protein Man1;
GN  MAN1;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16439308}; Multi-pass membrane protein {ECO:0000269|PubMed:16439308}. Cytoplasm {ECO:0000269|PubMed:16439308}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16439308}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16439308}. Note=During anaphase and metaphase, detected in the nuclear envelope and spindle poles. {ECO:0000269|PubMed:16439308}.
DR  UNIPROT: Q7JRE4;
DR  UNIPROT: Q961B2;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Inner nuclear membrane protein (PubMed:16439308). Acts as a negative regulator of the BMP (Dpp) signaling cascade during crossvein development in pupal wings and possibly during synaptic transmission at the neuromuscular junction (NMJ) (PubMed:18723885, PubMed:20036230). Appears to be required for pupal development and consequently transition to the adult stage (PubMed:18723885, PubMed:20036230). During pupal development, plays essential and redundant functions with the other LEM domain proteins; bocks and Ote (PubMed:24700158). {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:20036230, ECO:0000269|PubMed:24700158}.
DE  Reference Proteome: Yes;
DE  Interaction: P18431; IntAct: EBI-9925534; Score: 0.35
GO  GO:0005737;
GO  GO:0012505;
GO  GO:0005639;
GO  GO:0005654;
GO  GO:0000922;
GO  GO:0031490;
GO  GO:0030514;
GO  GO:0006998;
GO  GO:1902531;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSTESLNSLSDKELHRKLIQSGFPSTPVTETTRAVLIEKLRKHTRADKLKKRSNKYVLYSKEQQESPPFPQYHQYHAPQP
SQ  PQNYANGLDNNNDLDQTGGSSAYNRSLDESDSSPLQLSASKMYAPPPVVASNYDGDCSPHSLGLNGKYLQPCSMPYAIDT
SQ  SNNYGKPSGKAKLSDGGVVNRLLSFRDTTIQRKFNYPTGQASRIPLRKERLTRFALSDLKSFIRNPDIRPYVIPRVLISL
SQ  FLIFLTIITVLYVGKRFEQSPIDKAALKYTLCNPNDMQMISEKVNCIEKDSLRGALDMSEELFRHLNERARLHHCKDANL
SQ  SPALEIGEFVREMVSNPKTHRGNLHSNLMAAKYLITENPQWSIQVVDSTKHLGQTSHFELSEPNLPLKCIVLKKVTRFFT
SQ  VIGALLLIVAGFLIVYVAVVIYRVKQKEALLAVDQFQKDIINELIYLSSQSESPEVVINQLQEKFLPAKKRSKLLSSWNK
SQ  ALKQLEKNDSRVLFGMVNRDGKAMRTIAWNRNVDKKDVGLVKKWQSPAFDNSNKIANPPTPCLKIRHMFDSSEVDQANLK
SQ  QSIVESIIEKVGTRCKICDVQLDVQSCCVYIRCASEEDAGTIHKEINGWWFDKRLISIKFLRLERYLSRFPKPSAEPLYF
SQ  HTNEAANTHS
//
ID  Q9Y2U8;
PN  Inner nuclear membrane protein Man1;
GN  LEMD3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:15647271}; Multi-pass membrane protein {ECO:0000269|PubMed:15647271}.
DR  UNIPROT: Q9Y2U8;
DR  UNIPROT: Q9NT47;
DR  UNIPROT: Q9NYA5;
DR  PDB: 2CH0;
DR  PDB: 5ZOJ;
DR  PDB: 5ZOK;
DR  Pfam: PF03020;
DR  Pfam: PF09402;
DR  PROSITE: PS50954;
DR  OMIM: 166700;
DR  OMIM: 607844;
DR  DisGeNET: 23592;
DE  Function: Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest. {ECO:0000269|PubMed:15601644, ECO:0000269|PubMed:15647271}.
DE  Disease: Buschke-Ollendorff syndrome (BOS) [MIM:166700]: A disease characterized by osteopoikilosis and disseminated connective-tissue nevi. Osteopoikilosis is a skeletal dysplasia characterized by a symmetric but unequal distribution of multiple hyperostotic areas in different parts of the skeleton. Elastic-type nevi (juvenile elastoma) and collagen-type nevi (dermatofibrosis lenticularis disseminata) have been described in BOS. Skin or bony lesions can be absent in some family members, whereas other relatives may have both. {ECO:0000269|PubMed:15489854, ECO:0000269|PubMed:19438932}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.42
DE  Interaction: Q8N205; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q15797; IntAct: EBI-7252846; Score: 0.67
DE  Interaction: O15198; IntAct: EBI-24403985; Score: 0.67
DE  Interaction: Q8BUN5; IntAct: EBI-2561434; Score: 0.56
DE  Interaction: Q15796; IntAct: EBI-2695978; Score: 0.40
DE  Interaction: P84022; IntAct: EBI-2696171; Score: 0.56
DE  Interaction: Q9RMZ3; IntAct: EBI-2830066; Score: 0.00
DE  Interaction: Q81LK0; IntAct: EBI-2830059; Score: 0.00
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: Q9ULZ3; IntAct: EBI-10687267; Score: 0.35
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q9H6H4; IntAct: EBI-24679596; Score: 0.56
DE  Interaction: Q9UI14; IntAct: EBI-24413053; Score: 0.56
DE  Interaction: P08473; IntAct: EBI-21505285; Score: 0.35
DE  Interaction: Q8WXA8; IntAct: EBI-21508371; Score: 0.35
DE  Interaction: Q92633; IntAct: EBI-21508694; Score: 0.35
DE  Interaction: Q9H8X2; IntAct: EBI-21509881; Score: 0.35
DE  Interaction: P16070; IntAct: EBI-21554944; Score: 0.35
DE  Interaction: Q9UN71; IntAct: EBI-21584146; Score: 0.35
DE  Interaction: Q9Y5G3; IntAct: EBI-21584582; Score: 0.35
DE  Interaction: O43291; IntAct: EBI-21587968; Score: 0.35
DE  Interaction: Q8WWF5; IntAct: EBI-21589535; Score: 0.35
DE  Interaction: Q02297; IntAct: EBI-21594648; Score: 0.35
DE  Interaction: Q8N6K0; IntAct: EBI-21599984; Score: 0.35
DE  Interaction: A2RU67; IntAct: EBI-21694732; Score: 0.35
DE  Interaction: Q8IV01; IntAct: EBI-21748151; Score: 0.35
DE  Interaction: Q96G27; IntAct: EBI-21751108; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-21765755; Score: 0.48
DE  Interaction: Q9UKU6; IntAct: EBI-21773744; Score: 0.35
DE  Interaction: Q14392; IntAct: EBI-21780945; Score: 0.35
DE  Interaction: Q9HBB8; IntAct: EBI-21838749; Score: 0.35
DE  Interaction: Q16586; IntAct: EBI-21845627; Score: 0.35
DE  Interaction: O75106; IntAct: EBI-21896419; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.42
DE  Interaction: P68431; IntAct: EBI-16793336; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: P20339; IntAct: EBI-16798221; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: P62807; IntAct: EBI-25471348; Score: 0.27
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P05771; IntAct: EBI-25390687; Score: 0.35
DE  Interaction: P0DJI4; IntAct: EBI-22303808; Score: 0.35
DE  Interaction: Q9BXT4; IntAct: EBI-25485776; Score: 0.40
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
DE  Interaction: Q01974; IntAct: EBI-32725367; Score: 0.27
DE  Interaction: Q6J9G0; IntAct: EBI-32731895; Score: 0.27
GO  GO:0016021;
GO  GO:0005639;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0031490;
GO  GO:0032926;
GO  GO:0030514;
GO  GO:0030512;
GO  GO:0006998;
GO  GO:1902531;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAAAASAPQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQQQHRSGGRGNKTRNSNNNNTAAATVAAAG
SQ  PAAAAAAGMGVRPVSGDLSYLRTPGGLCRISASGPESLLGGPGGASAAPAAGSKVLLGFSSDESDVEASPRDQAGGGGRK
SQ  DRASLQYRGLKAPPAPLAASEVTNSNSAERRKPHSWWGARRPAGPELQTPPGKDGAVEDEEGEGEDGEERDPETEEPLWA
SQ  SRTVNGSRLVPYSCRENYSDSEEEDDDDVASSRQVLKDDSLSRHRPRRTHSKPLPPLTAKSAGGRLETSVQGGGGLAMND
SQ  RAAAAGSLDRSRNLEEAAAAEQGGGCDQVDSSPVPRYRVNAKKLTPLLPPPLTDMDSTLDSSTGSLLKTNNHIGGGAFSV
SQ  DSPRIYSNSLPPSAAVAASSSLRINHANHTGSNHTYLKNTYNKPKLSEPEEELLQQFKREEVSPTGSFSAHYLSMFLLTA
SQ  ACLFFLILGLTYLGMRGTGVSEDGELSIENPFGETFGKIQESEKTLMMNTLYKLHDRLAQLAGDHECGSSSQRTLSVQEA
SQ  AAYLKDLGPEYEGIFNTSLQWILENGKDVGIRCVGFGPEEELTNITDVQFLQSTRPLMSFWCRFRRAFVTVTHRLLLLCL
SQ  GVVMVCVVLRYMKYRWTKEEEETRQMYDMVVKIIDVLRSHNEACQENKDLQPYMPIPHVRDSLIQPHDRKKMKKVWDRAV
SQ  DFLAANESRVRTETRRIGGADFLVWRWIQPSASCDKILVIPSKVWQGQAFHLDRRNSPPNSLTPCLKIRNMFDPVMEIGD
SQ  QWHLAIQEAILEKCSDNDGIVHIAVDKNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVKYLRLDRYHHRFPQALT
SQ  SNTPLKPSNKHMNSMSHLRLRTGLTNSQGSS
//
ID  Q9WU40;
PN  Inner nuclear membrane protein Man1;
GN  Lemd3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane; Multi-pass membrane protein.
DR  UNIPROT: Q9WU40;
DR  UNIPROT: Q0VGU6;
DR  UNIPROT: Q3USB5;
DR  Pfam: PF03020;
DR  Pfam: PF09402;
DR  PROSITE: PS50954;
DE  Function: Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8VI24; IntAct: EBI-26885060; Score: 0.35
GO  GO:0016021;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0031490;
GO  GO:0001525;
GO  GO:0002044;
GO  GO:0032926;
GO  GO:0030514;
GO  GO:0030512;
GO  GO:0006998;
GO  GO:0006997;
GO  GO:0051726;
GO  GO:1903053;
GO  GO:1902531;
GO  GO:0035914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAATAAAAPQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQQQQQQQQQQQHRAGGRGNKTRNSNNNNT
SQ  ATAMGGRPGSGDLAYLRSPAGLGRLSASAAESPVAGGSGGAAAVPAAGSKVLLGFSSDESDVEASPREQAGGGGGGGARR
SQ  DRAALQYRGLRAPPAPPAAGEVTGGHPGERRKPHSWWGARRPAGPEPQPPAAGSDGAAEDADEELADGEDRDPEAEEPLW
SQ  ASRAVNGSRLLPYSSCREHYSDSEEEEEEGEEDGDVAPARQVLKDDSLARHRPRRSHSKPFSALTAKSGGSRQETSVQGG
SQ  GALAMNDRAAAAGSLDRSRNLEEAAAEPGGGGGGGCGCDPVDSIPRYRAGAKKLAPLLSPPSPDGDSTLESPTGPLLKTN
SQ  NHIGGGAFGVDSPGLYANSLPPGATAAAAPGTLRINHANHTGSNHTYLKTAYGKPKLCEPEEELLQQFKREEVSPTGSFS
SQ  AHYLSMFLLTAACLFFLILGLTYLGMRGTGVPEDGGLIKNPFDETFGKIQESEKNLLMSTLYKLHDRLAQIAGDHECGSS
SQ  SQRMLSVQEAAAYLKNLGPEYEDVFNTSLLWIFKNGKDVGIRCVGYGPEEDLTNITDVQFLQSTRPQMPFWCRFRRAFIT
SQ  VTHRLLLLCLGVVLVCVALRYMRYRWTKEEEETRQMYDMVVKIIDVLRSHNEACQETKDLQPYMPLPHVRDSLIQPQDRK
SQ  KMKKVWDRAVDFLAANESRVRTETRRVGGADFLVWRWIQPSASCDKTLVIPSKVWQGQAFHLDRRNSPPNSLTPCLKIRN
SQ  MFDPVMEIGDHWHLAIQEAILEKCSDNDGIVHIAVDRNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVKYLRLDR
SQ  YHHRFPQALTCNTPLKPANKHMNSLSHLRLRTGLANSQGSS
//
ID  Q5ZIA2;
PN  Ensconsin;
GN  MAP7;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
DR  UNIPROT: Q5ZIA2;
DR  Pfam: PF05672;
DE  Function: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells.
DE  Reference Proteome: Yes;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0048471;
GO  GO:0000226;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEAAGRSGGRRRRAAEGSKTQDKKVASGQSNTGTKPDHPPILKVDDRQRLARERREEREKQLAARETVWLEREERARQH
SQ  YEKHLEERKKKLEEQRLKEEGRRAAVEEKRRQRIEEDKERHEAVVRRTIERSQKPKQKQNRWSWGGALHSRINNSDPDRR
SQ  SVSTMNLSKHVDPVINKRLSSSSATLLNSSDRARRLQLSPWESSIVSRLLTPTHSFLARSKSTAALSGDAASCSPISPLS
SQ  YKTMSCRNSADRAKLFASTDAVGRRRTHLAGTDKKEKERDHLSSNFSANLKGGHFSSNPKARSPAPSPVWHASKSLPSLA
SQ  GTLKQITSPPGSSKVPSTQARPPSPGNIRPVKKDTKPENEKKRAEKEAEKANEERTEGSKETSAGTGESANQEELAVQAE
SQ  DAQAASPSLPPAPPALSPPPAPMKTSAGTTDPEEATRLLSEKRRLAREQREREEQERREREELERQKKEELSQRIAEERA
SQ  RREEEEARRQEAERKRKDAEEEREKEERLRRQAEEREQKEREEMERIQKQKEEEARLREEAERIRLEREKHFQREEQERL
SQ  ERKKRLEEIMKRTRRVEAVDKKPNDQQNGHISKANNTGEAVITSPAPPMEPSGGPQLQHATQSPHSGKPVTCTHTIVSHQ
SQ  PPMNMDSNLNPEKNTEENGMSMQNDNFEEIINLPIGSKPSRLDALNNDGSDSPGIPLNPILAFEDKGTLLPQVDSVQTHQ
SQ  TAEVI
//
ID  Q14244;
PN  Ensconsin;
GN  MAP7;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Basolateral cell membrane. Cytoplasm, cytoskeleton. Note=Colocalized on microtubules. An intracellular redistribution is triggered during induction of keratinocyte terminal differentiation from microtubules with a perinuclear localization to cortical microtubules organized in spike- like bundles facing intercellular contacts.
DR  UNIPROT: Q14244;
DR  UNIPROT: B7Z290;
DR  UNIPROT: B7Z400;
DR  UNIPROT: B7Z5S7;
DR  UNIPROT: B7Z9U7;
DR  UNIPROT: C9JPS0;
DR  UNIPROT: E9PCP3;
DR  UNIPROT: F5H1E2;
DR  UNIPROT: Q7Z6S0;
DR  UNIPROT: Q8TAU5;
DR  UNIPROT: Q9NY82;
DR  UNIPROT: Q9NY83;
DR  Pfam: PF05672;
DR  OMIM: 604108;
DR  DisGeNET: 9053;
DE  Function: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments. {ECO:0000269|PubMed:11719555, ECO:0000269|PubMed:8408219, ECO:0000269|PubMed:9989799}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: O15027; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P59595; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14203; IntAct: EBI-11366138; Score: 0.27
DE  Interaction: Q00005; IntAct: EBI-2210942; Score: 0.46
DE  Interaction: P61457; IntAct: EBI-2688436; Score: 0.00
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: E9QKK1; IntAct: EBI-10995761; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P62714; IntAct: EBI-11056306; Score: 0.35
DE  Interaction: Q8TF05; IntAct: EBI-11056691; Score: 0.35
DE  Interaction: Q9Z2X1; IntAct: EBI-11066678; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079358; Score: 0.35
DE  Interaction: Q2KHM9; IntAct: EBI-11366777; Score: 0.27
DE  Interaction: Q86VQ0; IntAct: EBI-11372448; Score: 0.27
DE  Interaction: Q8N0Z3; IntAct: EBI-11392023; Score: 0.27
DE  Interaction: P54274; IntAct: EBI-11305425; Score: 0.37
DE  Interaction: Q9NUX5; IntAct: EBI-11305435; Score: 0.37
DE  Interaction: Q9Y3M2; IntAct: EBI-12449244; Score: 0.51
DE  Interaction: Q71U36; IntAct: EBI-11897791; Score: 0.35
DE  Interaction: Q8NC26; IntAct: EBI-23690200; Score: 0.56
DE  Interaction: Q6NSX1; IntAct: EBI-23766440; Score: 0.56
DE  Interaction: Q8N3C7; IntAct: EBI-24655058; Score: 0.56
DE  Interaction: A0A0H3JP21; IntAct: EBI-13947943; Score: 0.58
DE  Interaction: Q8XBX8; IntAct: EBI-13947961; Score: 0.59
DE  Interaction: Q9UN74; IntAct: EBI-21510494; Score: 0.35
DE  Interaction: Q9UGM1; IntAct: EBI-21517134; Score: 0.35
DE  Interaction: O60232; IntAct: EBI-21543889; Score: 0.35
DE  Interaction: Q8WVZ9; IntAct: EBI-21562457; Score: 0.35
DE  Interaction: Q96F46; IntAct: EBI-21578337; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21580477; Score: 0.35
DE  Interaction: O14595; IntAct: EBI-21619731; Score: 0.35
DE  Interaction: Q8N6Y1; IntAct: EBI-21628941; Score: 0.35
DE  Interaction: Q9Y5F2; IntAct: EBI-21658599; Score: 0.35
DE  Interaction: Q9Y5G8; IntAct: EBI-21697051; Score: 0.35
DE  Interaction: Q13557; IntAct: EBI-21719478; Score: 0.35
DE  Interaction: Q8N4J0; IntAct: EBI-21736494; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: Q9ULK4; IntAct: EBI-25472850; Score: 0.35
DE  Interaction: Q86V81; IntAct: EBI-21258109; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: O95273; IntAct: EBI-22130147; Score: 0.37
DE  Interaction: Q9ULX6; IntAct: EBI-26451653; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: P0DTC9; IntAct: EBI-27127583; Score: 0.35
DE  Interaction: P15130; IntAct: EBI-27131516; Score: 0.35
DE  Interaction: Q0ZME3; IntAct: EBI-27131755; Score: 0.35
DE  Interaction: Q6Q1R8; IntAct: EBI-27132003; Score: 0.35
DE  Interaction: K9N4V7; IntAct: EBI-27132270; Score: 0.35
DE  Interaction: P33469; IntAct: EBI-27132272; Score: 0.35
DE  Interaction: Q93009; IntAct: EBI-30842225; Score: 0.44
DE  Interaction: Q9UIH9; IntAct: EBI-29019642; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
GO  GO:0030424;
GO  GO:0016323;
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0005875;
GO  GO:0015630;
GO  GO:0048471;
GO  GO:0005102;
GO  GO:0005198;
GO  GO:0007163;
GO  GO:0000226;
GO  GO:0072659;
GO  GO:0006970;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAELGAGGDGHRGGDGAVRSETAPDSYKVQDKKNASSRPASAISGQNNNHSGNKPDPPPVLRVDDRQRLARERREEREKQ
SQ  LAAREIVWLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNRW
SQ  SWGGSLHGSPSIHSADPDRRSVSTMNLSKYVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVNRLLTPTHSFLARS
SQ  KSTAALSGEAASCSPIIMPYKAAHSRNSMDRPKLFVTPPEGSSRRRIIHGTASYKKERERENVLFLTSGTRRAVSPSNPK
SQ  ARQPARSRLWLPSKSLPHLPGTPRPTSSLPPGSVKAAPAQVRPPSPGNIRPVKREVKVEPEKKDPEKEPQKVANEPSLKG
SQ  RAPLVKVEEATVEERTPAEPEVGPAAPAMAPAPASAPAPASAPAPAPVPTPAMVSAPSSTVNASASVKTSAGTTDPEEAT
SQ  RLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQRQAEERALREREE
SQ  AERAQRQKEEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATDKKTSDQRNGDIAKGALTGGTEVS
SQ  ALPCTTNAPGNGKPVGSPHVVTSHQSKVTVESTPDLEKQPNENGVSVQNENFEEIINLPIGSKPSRLDVTNSESPEIPLN
SQ  PILAFDDEGTLGPLPQVDGVQTQQTAEVI
//
ID  O88735;
PN  Ensconsin;
GN  Map7;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:14517216}. Basolateral cell membrane {ECO:0000269|PubMed:14517216}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14517216}. Note=Colocalized on microtubules. An intracellular redistribution is triggered during induction of keratinocyte terminal differentiation from microtubules with a perinuclear localization to cortical microtubules organized in spike- like bundles facing intercellular contacts.
DR  UNIPROT: O88735;
DR  UNIPROT: Q3V0B9;
DR  UNIPROT: Q7TQL9;
DR  UNIPROT: Q80V60;
DR  Pfam: PF05672;
DE  Function: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments. {ECO:0000269|PubMed:14517216}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0030424;
GO  GO:0016323;
GO  GO:0005829;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005102;
GO  GO:0000902;
GO  GO:0008283;
GO  GO:0009566;
GO  GO:0007281;
GO  GO:0006687;
GO  GO:0048872;
GO  GO:0033327;
GO  GO:0001578;
GO  GO:0000226;
GO  GO:0006997;
GO  GO:0035265;
GO  GO:0072659;
GO  GO:0006970;
GO  GO:0032526;
GO  GO:0060009;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEQGAGGDGHRGGDGATHSDPASDGYKVQEKRTAPSRPTSTVSGQTSNHSGNKPDPPPVLRVDDRQRLARERREEREKQ
SQ  LAARETVWLEREERARQHYERHLEARKKKLEDQRLKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPRQKSNRW
SQ  SWGSPLHGSSSIHSGDPDRRSVSTMNLSKHVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVSRLLTPTHSFLARS
SQ  KSTAALSGDTASCSPIIMPFKAAHSRNPVDRPKLFVTPPEGSARRRTIHGLASHKREREREHVPFHVSPGARRTLSPSNL
SQ  KARSPAPARLWLPSKSMPHLPGTPRPASSLPPGSVRAASAQAPSSSPGNIRPFKREVKVEPEKKDPLPAVKSRVPLVKVE
SQ  EVTVEEGTPVKPPEPAAPASAPIATPAPAPATDPAPVPAPSSTVTVGVVPKTSAGTTDPEEATRLLAEKRRLAREQREKE
SQ  ERERKEKEELERQKIEELARRVAEERSRREEEARRLEEEQAREKEELALRLAEEERERWEREEVERVQKQKEEEARAREE
SQ  AERARQEREKHFQKEEQERLERKKRLEEIMRRTRRTETADKKTTEQRNGDIAKGVLTGEPEVPALPCMASSGNGESAESP
SQ  HGVALQQSEVTTESSPDLEKQPNENGMSIQNENFEEVINLPVGSKASRLDVTNENPEIPLKPILAFNDEGTLGPLPQVDG
SQ  VQTQQTAEVI
//
ID  P25491;
PN  Mitochondrial protein import protein MAS5;
GN  YDJ1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Note=Concentrated in a perinuclear ring as well as in the cytoplasm.
DR  UNIPROT: P25491;
DR  UNIPROT: D6W1B6;
DR  PDB: 1NLT;
DR  PDB: 1XAO;
DR  PDB: 5VSO;
DR  Pfam: PF00226;
DR  Pfam: PF01556;
DR  Pfam: PF00684;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DR  PROSITE: PS51188;
DE  Function: Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high-molecular-weight (HMC) complex. {ECO:0000269|PubMed:11689685}.
DE  Reference Proteome: Yes;
DE  Interaction: P06105; IntAct: EBI-3664276; Score: 0.35
DE  Interaction: P06782; IntAct: EBI-3766560; Score: 0.35
DE  Interaction: P38085; IntAct: EBI-785720; Score: 0.35
DE  Interaction: P21147; IntAct: EBI-786767; Score: 0.35
DE  Interaction: P06839; IntAct: EBI-791932; Score: 0.64
DE  Interaction: P00830; IntAct: EBI-813344; Score: 0.27
DE  Interaction: P38737; IntAct: EBI-814203; Score: 0.51
DE  Interaction: P33892; IntAct: EBI-819274; Score: 0.51
DE  Interaction: P18239; IntAct: EBI-820078; Score: 0.27
DE  Interaction: P36046; IntAct: EBI-853933; Score: 0.53
DE  Interaction: P0CG63; IntAct: EBI-7479876; Score: 0.44
DE  Interaction: P02829; IntAct: EBI-863329; Score: 0.62
DE  Interaction: P12866; IntAct: EBI-1637343; Score: 0.35
DE  Interaction: Q12118; IntAct: EBI-1782119; Score: 0.64
DE  Interaction: Q12285; IntAct: EBI-1782144; Score: 0.52
DE  Interaction: P25491; IntAct: EBI-6319619; Score: 0.00
DE  Interaction: Q7LKB1; IntAct: EBI-8411464; Score: 0.54
DE  Interaction: P39743; IntAct: EBI-7317561; Score: 0.31
DE  Interaction: Q08273; IntAct: EBI-2794894; Score: 0.53
DE  Interaction: P25567; IntAct: EBI-2904800; Score: 0.35
DE  Interaction: P0CS82; IntAct: EBI-2904800; Score: 0.35
DE  Interaction: P39101; IntAct: EBI-3654696; Score: 0.35
DE  Interaction: P46997; IntAct: EBI-3658264; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-3663071; Score: 0.35
DE  Interaction: P38009; IntAct: EBI-3663079; Score: 0.35
DE  Interaction: P07244; IntAct: EBI-3663087; Score: 0.35
DE  Interaction: P38972; IntAct: EBI-3663095; Score: 0.35
DE  Interaction: P25376; IntAct: EBI-3663103; Score: 0.35
DE  Interaction: P47019; IntAct: EBI-3663111; Score: 0.35
DE  Interaction: P47771; IntAct: EBI-3663119; Score: 0.35
DE  Interaction: P54115; IntAct: EBI-3663127; Score: 0.35
DE  Interaction: P46682; IntAct: EBI-3663135; Score: 0.35
DE  Interaction: P38328; IntAct: EBI-3663143; Score: 0.35
DE  Interaction: Q12500; IntAct: EBI-3663151; Score: 0.35
DE  Interaction: Q05029; IntAct: EBI-3663159; Score: 0.35
DE  Interaction: P34730; IntAct: EBI-3663167; Score: 0.35
DE  Interaction: P47039; IntAct: EBI-3663175; Score: 0.35
DE  Interaction: Q07457; IntAct: EBI-3663183; Score: 0.35
DE  Interaction: P32639; IntAct: EBI-3663191; Score: 0.35
DE  Interaction: P40096; IntAct: EBI-3663199; Score: 0.35
DE  Interaction: P00812; IntAct: EBI-3663207; Score: 0.35
DE  Interaction: P33322; IntAct: EBI-3663215; Score: 0.35
DE  Interaction: P31384; IntAct: EBI-3663223; Score: 0.53
DE  Interaction: Q03705; IntAct: EBI-3663231; Score: 0.35
DE  Interaction: P19454; IntAct: EBI-3663239; Score: 0.35
DE  Interaction: P53195; IntAct: EBI-3663247; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-3663255; Score: 0.35
DE  Interaction: Q06440; IntAct: EBI-3663263; Score: 0.35
DE  Interaction: P14922; IntAct: EBI-3663271; Score: 0.35
DE  Interaction: P36009; IntAct: EBI-3663279; Score: 0.53
DE  Interaction: Q04216; IntAct: EBI-3663287; Score: 0.35
DE  Interaction: P54858; IntAct: EBI-3663295; Score: 0.35
DE  Interaction: P32461; IntAct: EBI-3663303; Score: 0.35
DE  Interaction: P53911; IntAct: EBI-3663311; Score: 0.35
DE  Interaction: P47169; IntAct: EBI-3663319; Score: 0.35
DE  Interaction: P38241; IntAct: EBI-3663327; Score: 0.35
DE  Interaction: P32324; IntAct: EBI-3663335; Score: 0.35
DE  Interaction: Q04409; IntAct: EBI-3663343; Score: 0.35
DE  Interaction: P00924; IntAct: EBI-3663351; Score: 0.35
DE  Interaction: P38333; IntAct: EBI-3663359; Score: 0.35
DE  Interaction: P43572; IntAct: EBI-3663367; Score: 0.35
DE  Interaction: P32353; IntAct: EBI-3663375; Score: 0.35
DE  Interaction: P39704; IntAct: EBI-3663383; Score: 0.35
DE  Interaction: P38819; IntAct: EBI-3663391; Score: 0.35
DE  Interaction: Q08649; IntAct: EBI-3663399; Score: 0.35
DE  Interaction: P53743; IntAct: EBI-3663407; Score: 0.35
DE  Interaction: Q12178; IntAct: EBI-3663415; Score: 0.35
DE  Interaction: P39730; IntAct: EBI-3663423; Score: 0.35
DE  Interaction: Q08193; IntAct: EBI-3663431; Score: 0.35
DE  Interaction: P41814; IntAct: EBI-3663439; Score: 0.35
DE  Interaction: P12754; IntAct: EBI-3663447; Score: 0.35
DE  Interaction: P43535; IntAct: EBI-3663455; Score: 0.35
DE  Interaction: Q05584; IntAct: EBI-3663463; Score: 0.35
DE  Interaction: Q08220; IntAct: EBI-3663471; Score: 0.35
DE  Interaction: P27472; IntAct: EBI-3663479; Score: 0.35
DE  Interaction: P32190; IntAct: EBI-3663487; Score: 0.35
DE  Interaction: Q12180; IntAct: EBI-3663495; Score: 0.35
DE  Interaction: Q12341; IntAct: EBI-3663503; Score: 0.35
DE  Interaction: P20448; IntAct: EBI-3663511; Score: 0.35
DE  Interaction: P11353; IntAct: EBI-3663519; Score: 0.35
DE  Interaction: Q04458; IntAct: EBI-3663527; Score: 0.35
DE  Interaction: P61830; IntAct: EBI-3663535; Score: 0.35
DE  Interaction: P47171; IntAct: EBI-3663543; Score: 0.35
DE  Interaction: Q03973; IntAct: EBI-3663551; Score: 0.35
DE  Interaction: P32478; IntAct: EBI-3663559; Score: 0.35
DE  Interaction: P04912; IntAct: EBI-3663567; Score: 0.35
DE  Interaction: P07263; IntAct: EBI-3663575; Score: 0.35
DE  Interaction: Q12692; IntAct: EBI-3663583; Score: 0.35
DE  Interaction: P04807; IntAct: EBI-3663591; Score: 0.35
DE  Interaction: P43579; IntAct: EBI-3663599; Score: 0.35
DE  Interaction: P38286; IntAct: EBI-3663607; Score: 0.35
DE  Interaction: P09436; IntAct: EBI-3663615; Score: 0.35
DE  Interaction: P00927; IntAct: EBI-3663623; Score: 0.35
DE  Interaction: P50095; IntAct: EBI-3663631; Score: 0.35
DE  Interaction: P53115; IntAct: EBI-3663639; Score: 0.35
DE  Interaction: P40006; IntAct: EBI-3663647; Score: 0.35
DE  Interaction: Q07821; IntAct: EBI-3663655; Score: 0.35
DE  Interaction: P36132; IntAct: EBI-3663663; Score: 0.35
DE  Interaction: P38217; IntAct: EBI-3663671; Score: 0.35
DE  Interaction: Q08979; IntAct: EBI-3663679; Score: 0.35
DE  Interaction: P22209; IntAct: EBI-3663687; Score: 0.35
DE  Interaction: P40540; IntAct: EBI-3663695; Score: 0.35
DE  Interaction: Q3E840; IntAct: EBI-3663703; Score: 0.35
DE  Interaction: P12695; IntAct: EBI-3663711; Score: 0.35
DE  Interaction: P57743; IntAct: EBI-3663719; Score: 0.35
DE  Interaction: P53905; IntAct: EBI-3663727; Score: 0.35
DE  Interaction: P48570; IntAct: EBI-3663735; Score: 0.35
DE  Interaction: P49367; IntAct: EBI-3663743; Score: 0.35
DE  Interaction: P11914; IntAct: EBI-3663751; Score: 0.35
DE  Interaction: P39677; IntAct: EBI-3663759; Score: 0.35
DE  Interaction: P24719; IntAct: EBI-3663767; Score: 0.35
DE  Interaction: P00958; IntAct: EBI-3663775; Score: 0.35
DE  Interaction: P53128; IntAct: EBI-3663783; Score: 0.35
DE  Interaction: P33441; IntAct: EBI-3663791; Score: 0.35
DE  Interaction: P09440; IntAct: EBI-3663799; Score: 0.35
DE  Interaction: P53141; IntAct: EBI-3663807; Score: 0.35
DE  Interaction: P25847; IntAct: EBI-3663815; Score: 0.35
DE  Interaction: P32335; IntAct: EBI-3663823; Score: 0.35
DE  Interaction: P47047; IntAct: EBI-3663831; Score: 0.35
DE  Interaction: P19524; IntAct: EBI-3663839; Score: 0.35
DE  Interaction: P38205; IntAct: EBI-3663847; Score: 0.35
DE  Interaction: Q08972; IntAct: EBI-3663855; Score: 0.35
DE  Interaction: P53081; IntAct: EBI-3663863; Score: 0.35
DE  Interaction: P06102; IntAct: EBI-3663871; Score: 0.35
DE  Interaction: P53164; IntAct: EBI-3663879; Score: 0.35
DE  Interaction: P31378; IntAct: EBI-3663887; Score: 0.35
DE  Interaction: P35172; IntAct: EBI-3663895; Score: 0.35
DE  Interaction: P39705; IntAct: EBI-3663903; Score: 0.35
DE  Interaction: P54784; IntAct: EBI-3663911; Score: 0.35
DE  Interaction: P50874; IntAct: EBI-3663919; Score: 0.35
DE  Interaction: P38826; IntAct: EBI-3663927; Score: 0.35
DE  Interaction: Q12451; IntAct: EBI-3663935; Score: 0.35
DE  Interaction: Q12447; IntAct: EBI-3663943; Score: 0.35
DE  Interaction: P38254; IntAct: EBI-3663951; Score: 0.35
DE  Interaction: Q04264; IntAct: EBI-3663959; Score: 0.35
DE  Interaction: P42841; IntAct: EBI-3663967; Score: 0.53
DE  Interaction: P47110; IntAct: EBI-3663975; Score: 0.35
DE  Interaction: P39985; IntAct: EBI-3663983; Score: 0.35
DE  Interaction: P23595; IntAct: EBI-3663991; Score: 0.53
DE  Interaction: P32345; IntAct: EBI-3663999; Score: 0.35
DE  Interaction: P53131; IntAct: EBI-3664007; Score: 0.35
DE  Interaction: P28708; IntAct: EBI-3664015; Score: 0.35
DE  Interaction: Q12265; IntAct: EBI-3664023; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-3664031; Score: 0.35
DE  Interaction: Q12335; IntAct: EBI-3664039; Score: 0.35
DE  Interaction: Q12318; IntAct: EBI-3664047; Score: 0.35
DE  Interaction: P09368; IntAct: EBI-3664055; Score: 0.35
DE  Interaction: P06777; IntAct: EBI-3664063; Score: 0.35
DE  Interaction: P32628; IntAct: EBI-3664071; Score: 0.35
DE  Interaction: P32641; IntAct: EBI-3664079; Score: 0.53
DE  Interaction: Q04231; IntAct: EBI-3664095; Score: 0.35
DE  Interaction: P25454; IntAct: EBI-3664103; Score: 0.35
DE  Interaction: P21538; IntAct: EBI-3664111; Score: 0.35
DE  Interaction: P22336; IntAct: EBI-3664119; Score: 0.35
DE  Interaction: P39083; IntAct: EBI-3664127; Score: 0.35
DE  Interaction: Q00453; IntAct: EBI-3664135; Score: 0.35
DE  Interaction: P16664; IntAct: EBI-3664143; Score: 0.35
DE  Interaction: P48565; IntAct: EBI-3664156; Score: 0.35
DE  Interaction: Q07844; IntAct: EBI-3664164; Score: 0.35
DE  Interaction: P21524; IntAct: EBI-3664172; Score: 0.35
DE  Interaction: P32561; IntAct: EBI-3664180; Score: 0.35
DE  Interaction: P17079; IntAct: EBI-3664188; Score: 0.35
DE  Interaction: P53030; IntAct: EBI-3664196; Score: 0.35
DE  Interaction: P32565; IntAct: EBI-3664204; Score: 0.35
DE  Interaction: P40016; IntAct: EBI-3664212; Score: 0.35
DE  Interaction: P40327; IntAct: EBI-3664220; Score: 0.35
DE  Interaction: Q12754; IntAct: EBI-3664228; Score: 0.35
DE  Interaction: P53236; IntAct: EBI-3664236; Score: 0.35
DE  Interaction: Q05543; IntAct: EBI-3664244; Score: 0.35
DE  Interaction: Q03940; IntAct: EBI-3664252; Score: 0.35
DE  Interaction: P32368; IntAct: EBI-3664260; Score: 0.35
DE  Interaction: Q08873; IntAct: EBI-3664268; Score: 0.35
DE  Interaction: P40509; IntAct: EBI-3664284; Score: 0.35
DE  Interaction: P38968; IntAct: EBI-3664292; Score: 0.35
DE  Interaction: O94742; IntAct: EBI-3664300; Score: 0.35
DE  Interaction: P46995; IntAct: EBI-3664308; Score: 0.35
DE  Interaction: P53953; IntAct: EBI-3664316; Score: 0.35
DE  Interaction: P23293; IntAct: EBI-3664324; Score: 0.35
DE  Interaction: P51534; IntAct: EBI-3664332; Score: 0.35
DE  Interaction: P11978; IntAct: EBI-3664340; Score: 0.35
DE  Interaction: Q04195; IntAct: EBI-3664348; Score: 0.35
DE  Interaction: P53327; IntAct: EBI-3664356; Score: 0.35
DE  Interaction: P38989; IntAct: EBI-3664364; Score: 0.35
DE  Interaction: P47037; IntAct: EBI-3664372; Score: 0.35
DE  Interaction: P36048; IntAct: EBI-3664380; Score: 0.35
DE  Interaction: Q04053; IntAct: EBI-3664388; Score: 0.35
DE  Interaction: P38633; IntAct: EBI-3664396; Score: 0.35
DE  Interaction: P38863; IntAct: EBI-3664404; Score: 0.35
DE  Interaction: P23561; IntAct: EBI-3664412; Score: 0.35
DE  Interaction: P05453; IntAct: EBI-3664420; Score: 0.35
DE  Interaction: P53201; IntAct: EBI-3664428; Score: 0.35
DE  Interaction: P09959; IntAct: EBI-3664436; Score: 0.35
DE  Interaction: Q05471; IntAct: EBI-3664444; Score: 0.35
DE  Interaction: Q04175; IntAct: EBI-3664452; Score: 0.35
DE  Interaction: Q12297; IntAct: EBI-3664460; Score: 0.35
DE  Interaction: P33339; IntAct: EBI-3664468; Score: 0.35
DE  Interaction: Q06339; IntAct: EBI-3664476; Score: 0.35
DE  Interaction: P17423; IntAct: EBI-3664484; Score: 0.35
DE  Interaction: P23254; IntAct: EBI-3664492; Score: 0.35
DE  Interaction: P40462; IntAct: EBI-3664500; Score: 0.35
DE  Interaction: P53840; IntAct: EBI-3664508; Score: 0.35
DE  Interaction: Q03280; IntAct: EBI-3664516; Score: 0.35
DE  Interaction: P06786; IntAct: EBI-3664524; Score: 0.35
DE  Interaction: P43637; IntAct: EBI-3664532; Score: 0.35
DE  Interaction: P06244; IntAct: EBI-3664540; Score: 0.35
DE  Interaction: Q00764; IntAct: EBI-3664548; Score: 0.35
DE  Interaction: P38426; IntAct: EBI-3664556; Score: 0.35
DE  Interaction: P38811; IntAct: EBI-3664564; Score: 0.35
DE  Interaction: Q07527; IntAct: EBI-3664572; Score: 0.35
DE  Interaction: P00937; IntAct: EBI-3664580; Score: 0.35
DE  Interaction: P38427; IntAct: EBI-3664588; Score: 0.35
DE  Interaction: Q07381; IntAct: EBI-3664596; Score: 0.35
DE  Interaction: P53378; IntAct: EBI-3664604; Score: 0.35
DE  Interaction: P36164; IntAct: EBI-3664612; Score: 0.35
DE  Interaction: Q08960; IntAct: EBI-3664620; Score: 0.35
DE  Interaction: Q01476; IntAct: EBI-3664628; Score: 0.35
DE  Interaction: P43593; IntAct: EBI-3664636; Score: 0.35
DE  Interaction: P54860; IntAct: EBI-3664644; Score: 0.35
DE  Interaction: P33202; IntAct: EBI-3664652; Score: 0.35
DE  Interaction: P38067; IntAct: EBI-3664660; Score: 0.35
DE  Interaction: P28274; IntAct: EBI-3664668; Score: 0.35
DE  Interaction: P42945; IntAct: EBI-3664676; Score: 0.35
DE  Interaction: Q05946; IntAct: EBI-3664684; Score: 0.35
DE  Interaction: Q06078; IntAct: EBI-3664692; Score: 0.35
DE  Interaction: P53276; IntAct: EBI-3664700; Score: 0.35
DE  Interaction: P32623; IntAct: EBI-3664708; Score: 0.35
DE  Interaction: P53076; IntAct: EBI-3664716; Score: 0.35
DE  Interaction: Q12045; IntAct: EBI-3664724; Score: 0.35
DE  Interaction: Q06685; IntAct: EBI-3664732; Score: 0.35
DE  Interaction: P34110; IntAct: EBI-3664740; Score: 0.35
DE  Interaction: Q12109; IntAct: EBI-3664748; Score: 0.35
DE  Interaction: P39735; IntAct: EBI-3664756; Score: 0.35
DE  Interaction: P46683; IntAct: EBI-3664764; Score: 0.35
DE  Interaction: P38222; IntAct: EBI-3664772; Score: 0.35
DE  Interaction: P38317; IntAct: EBI-3664780; Score: 0.35
DE  Interaction: P25361; IntAct: EBI-3664788; Score: 0.35
DE  Interaction: Q04093; IntAct: EBI-3664796; Score: 0.35
DE  Interaction: Q04431; IntAct: EBI-3664804; Score: 0.35
DE  Interaction: P16521; IntAct: EBI-3664812; Score: 0.35
DE  Interaction: P43594; IntAct: EBI-3664820; Score: 0.35
DE  Interaction: P53262; IntAct: EBI-3664828; Score: 0.35
DE  Interaction: P38829; IntAct: EBI-3664836; Score: 0.35
DE  Interaction: P38833; IntAct: EBI-3664844; Score: 0.35
DE  Interaction: P40533; IntAct: EBI-3664852; Score: 0.35
DE  Interaction: P36114; IntAct: EBI-3664860; Score: 0.35
DE  Interaction: Q05778; IntAct: EBI-3664868; Score: 0.35
DE  Interaction: Q06188; IntAct: EBI-3664876; Score: 0.35
DE  Interaction: Q04847; IntAct: EBI-3664884; Score: 0.35
DE  Interaction: P53970; IntAct: EBI-3664892; Score: 0.35
DE  Interaction: P42842; IntAct: EBI-3664900; Score: 0.35
DE  Interaction: Q08206; IntAct: EBI-3664908; Score: 0.35
DE  Interaction: Q08548; IntAct: EBI-3664916; Score: 0.35
DE  Interaction: Q08822; IntAct: EBI-3664924; Score: 0.35
DE  Interaction: P12688; IntAct: EBI-3664932; Score: 0.35
DE  Interaction: Q08924; IntAct: EBI-3664940; Score: 0.35
DE  Interaction: O13585; IntAct: EBI-3664948; Score: 0.35
DE  Interaction: Q06109; IntAct: EBI-3664956; Score: 0.35
DE  Interaction: Q08245; IntAct: EBI-3664964; Score: 0.35
DE  Interaction: P53303; IntAct: EBI-3664972; Score: 0.35
DE  Interaction: P11412; IntAct: EBI-3664980; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-3664988; Score: 0.35
DE  Interaction: P47138; IntAct: EBI-3664996; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3682766; Score: 0.53
DE  Interaction: P09435; IntAct: EBI-3683827; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3703899; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3719486; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3748847; Score: 0.35
DE  Interaction: P31539; IntAct: EBI-3749791; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3751647; Score: 0.35
DE  Interaction: P32048; IntAct: EBI-3752007; Score: 0.35
DE  Interaction: P06103; IntAct: EBI-3752015; Score: 0.35
DE  Interaction: P04786; IntAct: EBI-3752023; Score: 0.35
DE  Interaction: P53852; IntAct: EBI-3752031; Score: 0.35
DE  Interaction: P15992; IntAct: EBI-3752039; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3752047; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3752055; Score: 0.35
DE  Interaction: P42884; IntAct: EBI-3763499; Score: 0.35
DE  Interaction: P37898; IntAct: EBI-3763507; Score: 0.35
DE  Interaction: Q03266; IntAct: EBI-3763515; Score: 0.35
DE  Interaction: Q00955; IntAct: EBI-3763523; Score: 0.35
DE  Interaction: P21192; IntAct: EBI-3763531; Score: 0.35
DE  Interaction: Q07622; IntAct: EBI-3763539; Score: 0.35
DE  Interaction: P60010; IntAct: EBI-3763547; Score: 0.35
DE  Interaction: Q07732; IntAct: EBI-3763555; Score: 0.35
DE  Interaction: P22136; IntAct: EBI-3763563; Score: 0.35
DE  Interaction: Q12449; IntAct: EBI-3763571; Score: 0.35
DE  Interaction: P03875; IntAct: EBI-3763579; Score: 0.35
DE  Interaction: Q9ZZX1; IntAct: EBI-3763587; Score: 0.35
DE  Interaction: Q12013; IntAct: EBI-3763595; Score: 0.35
DE  Interaction: P47029; IntAct: EBI-3763603; Score: 0.35
DE  Interaction: P22108; IntAct: EBI-3763611; Score: 0.35
DE  Interaction: Q04601; IntAct: EBI-3763619; Score: 0.35
DE  Interaction: P38281; IntAct: EBI-3763627; Score: 0.35
DE  Interaction: P27351; IntAct: EBI-3763635; Score: 0.35
DE  Interaction: P38065; IntAct: EBI-3763643; Score: 0.35
DE  Interaction: Q08951; IntAct: EBI-3763651; Score: 0.35
DE  Interaction: P11076; IntAct: EBI-3763659; Score: 0.35
DE  Interaction: P04076; IntAct: EBI-3763667; Score: 0.35
DE  Interaction: P38116; IntAct: EBI-3763675; Score: 0.35
DE  Interaction: P08566; IntAct: EBI-3763683; Score: 0.35
DE  Interaction: Q04052; IntAct: EBI-3763691; Score: 0.35
DE  Interaction: P34233; IntAct: EBI-3763699; Score: 0.35
DE  Interaction: P53983; IntAct: EBI-3763707; Score: 0.35
DE  Interaction: P39945; IntAct: EBI-3763715; Score: 0.35
DE  Interaction: Q12527; IntAct: EBI-3763723; Score: 0.35
DE  Interaction: P53855; IntAct: EBI-3763731; Score: 0.35
DE  Interaction: Q12142; IntAct: EBI-3763739; Score: 0.35
DE  Interaction: P32453; IntAct: EBI-3763747; Score: 0.35
DE  Interaction: Q08236; IntAct: EBI-3763755; Score: 0.35
DE  Interaction: P47068; IntAct: EBI-3763763; Score: 0.35
DE  Interaction: Q01389; IntAct: EBI-3763771; Score: 0.35
DE  Interaction: P46678; IntAct: EBI-3763779; Score: 0.35
DE  Interaction: Q08347; IntAct: EBI-3763787; Score: 0.35
DE  Interaction: P39960; IntAct: EBI-3763800; Score: 0.35
DE  Interaction: P43583; IntAct: EBI-3763808; Score: 0.35
DE  Interaction: Q08965; IntAct: EBI-3763816; Score: 0.35
DE  Interaction: P47125; IntAct: EBI-3763824; Score: 0.35
DE  Interaction: P41832; IntAct: EBI-3763832; Score: 0.35
DE  Interaction: P40450; IntAct: EBI-3763840; Score: 0.35
DE  Interaction: P38041; IntAct: EBI-3763848; Score: 0.35
DE  Interaction: P39969; IntAct: EBI-3763856; Score: 0.35
DE  Interaction: P25385; IntAct: EBI-3763864; Score: 0.35
DE  Interaction: P25356; IntAct: EBI-3763872; Score: 0.35
DE  Interaction: P33314; IntAct: EBI-3763880; Score: 0.35
DE  Interaction: P41697; IntAct: EBI-3763888; Score: 0.35
DE  Interaction: P48524; IntAct: EBI-3763896; Score: 0.35
DE  Interaction: P53280; IntAct: EBI-3763904; Score: 0.35
DE  Interaction: P29547; IntAct: EBI-3763912; Score: 0.35
DE  Interaction: P28495; IntAct: EBI-3763920; Score: 0.35
DE  Interaction: P53894; IntAct: EBI-3763928; Score: 0.35
DE  Interaction: P38626; IntAct: EBI-3763936; Score: 0.35
DE  Interaction: Q03702; IntAct: EBI-3763944; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-3763952; Score: 0.35
DE  Interaction: P26309; IntAct: EBI-3763960; Score: 0.53
DE  Interaction: P06785; IntAct: EBI-3763968; Score: 0.35
DE  Interaction: P25655; IntAct: EBI-3763976; Score: 0.35
DE  Interaction: P07834; IntAct: EBI-3763984; Score: 0.35
DE  Interaction: Q08032; IntAct: EBI-3763992; Score: 0.35
DE  Interaction: P25694; IntAct: EBI-3764000; Score: 0.35
DE  Interaction: P30665; IntAct: EBI-3764008; Score: 0.35
DE  Interaction: P39525; IntAct: EBI-3764016; Score: 0.35
DE  Interaction: O13297; IntAct: EBI-3764024; Score: 0.35
DE  Interaction: Q12453; IntAct: EBI-3764032; Score: 0.35
DE  Interaction: Q06632; IntAct: EBI-3764040; Score: 0.35
DE  Interaction: P32657; IntAct: EBI-3764048; Score: 0.35
DE  Interaction: P22516; IntAct: EBI-3764056; Score: 0.35
DE  Interaction: P29465; IntAct: EBI-3764064; Score: 0.35
DE  Interaction: P38779; IntAct: EBI-3764072; Score: 0.35
DE  Interaction: P40987; IntAct: EBI-3764080; Score: 0.35
DE  Interaction: P27895; IntAct: EBI-3764088; Score: 0.35
DE  Interaction: P20485; IntAct: EBI-3764096; Score: 0.35
DE  Interaction: P48562; IntAct: EBI-3764104; Score: 0.35
DE  Interaction: Q08685; IntAct: EBI-3764112; Score: 0.35
DE  Interaction: Q03690; IntAct: EBI-3764120; Score: 0.35
DE  Interaction: P06787; IntAct: EBI-3764128; Score: 0.35
DE  Interaction: P23287; IntAct: EBI-3764136; Score: 0.53
DE  Interaction: Q04632; IntAct: EBI-3764144; Score: 0.35
DE  Interaction: P53622; IntAct: EBI-3764152; Score: 0.35
DE  Interaction: P49017; IntAct: EBI-3764160; Score: 0.35
DE  Interaction: Q04935; IntAct: EBI-3764168; Score: 0.35
DE  Interaction: P23285; IntAct: EBI-3764176; Score: 0.35
DE  Interaction: P33307; IntAct: EBI-3764184; Score: 0.35
DE  Interaction: Q12734; IntAct: EBI-3764192; Score: 0.35
DE  Interaction: Q01454; IntAct: EBI-3764200; Score: 0.35
DE  Interaction: P89105; IntAct: EBI-3764208; Score: 0.56
DE  Interaction: P53008; IntAct: EBI-3764216; Score: 0.35
DE  Interaction: P32898; IntAct: EBI-3764224; Score: 0.35
DE  Interaction: P08678; IntAct: EBI-3764232; Score: 0.35
DE  Interaction: P32582; IntAct: EBI-3764240; Score: 0.35
DE  Interaction: Q12389; IntAct: EBI-3764248; Score: 0.35
DE  Interaction: Q06151; IntAct: EBI-3764256; Score: 0.35
DE  Interaction: P06634; IntAct: EBI-3764264; Score: 0.35
DE  Interaction: Q08496; IntAct: EBI-3764272; Score: 0.53
DE  Interaction: P25453; IntAct: EBI-3764280; Score: 0.53
DE  Interaction: P38859; IntAct: EBI-3764288; Score: 0.35
DE  Interaction: Q12675; IntAct: EBI-3764296; Score: 0.35
DE  Interaction: Q12674; IntAct: EBI-3764304; Score: 0.35
DE  Interaction: Q08387; IntAct: EBI-3764312; Score: 0.35
DE  Interaction: P54861; IntAct: EBI-3764320; Score: 0.35
DE  Interaction: Q05610; IntAct: EBI-3764328; Score: 0.35
DE  Interaction: Q03921; IntAct: EBI-3764336; Score: 0.35
DE  Interaction: P24482; IntAct: EBI-3764344; Score: 0.35
DE  Interaction: P53847; IntAct: EBI-3764352; Score: 0.35
DE  Interaction: P38149; IntAct: EBI-3764360; Score: 0.35
DE  Interaction: Q12432; IntAct: EBI-3764368; Score: 0.35
DE  Interaction: Q04110; IntAct: EBI-3764376; Score: 0.35
DE  Interaction: Q04217; IntAct: EBI-3764384; Score: 0.35
DE  Interaction: Q05958; IntAct: EBI-3764392; Score: 0.35
DE  Interaction: P32525; IntAct: EBI-3764400; Score: 0.35
DE  Interaction: Q06673; IntAct: EBI-3764416; Score: 0.35
DE  Interaction: Q03214; IntAct: EBI-3764424; Score: 0.35
DE  Interaction: P40557; IntAct: EBI-3764440; Score: 0.35
DE  Interaction: P10614; IntAct: EBI-3764448; Score: 0.35
DE  Interaction: Q03018; IntAct: EBI-3764456; Score: 0.35
DE  Interaction: Q06163; IntAct: EBI-3764469; Score: 0.35
DE  Interaction: P34756; IntAct: EBI-3764477; Score: 0.35
DE  Interaction: P53971; IntAct: EBI-3764485; Score: 0.35
DE  Interaction: P46671; IntAct: EBI-3764493; Score: 0.35
DE  Interaction: P19097; IntAct: EBI-3764501; Score: 0.35
DE  Interaction: P14540; IntAct: EBI-3764509; Score: 0.35
DE  Interaction: P39521; IntAct: EBI-3764517; Score: 0.35
DE  Interaction: P32785; IntAct: EBI-3764525; Score: 0.35
DE  Interaction: P53848; IntAct: EBI-3764533; Score: 0.35
DE  Interaction: P38911; IntAct: EBI-3764541; Score: 0.35
DE  Interaction: Q12333; IntAct: EBI-3764549; Score: 0.35
DE  Interaction: P31380; IntAct: EBI-3764557; Score: 0.35
DE  Interaction: P46949; IntAct: EBI-3764565; Score: 0.35
DE  Interaction: P38297; IntAct: EBI-3764573; Score: 0.35
DE  Interaction: P09032; IntAct: EBI-3764581; Score: 0.35
DE  Interaction: P32481; IntAct: EBI-3764589; Score: 0.35
DE  Interaction: P32501; IntAct: EBI-3764597; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-3764613; Score: 0.35
DE  Interaction: Q06625; IntAct: EBI-3764621; Score: 0.35
DE  Interaction: P47102; IntAct: EBI-3764629; Score: 0.35
DE  Interaction: P53192; IntAct: EBI-3764637; Score: 0.35
DE  Interaction: Q03016; IntAct: EBI-3764645; Score: 0.35
DE  Interaction: Q12680; IntAct: EBI-3764653; Score: 0.35
DE  Interaction: P08539; IntAct: EBI-3764661; Score: 0.35
DE  Interaction: P41911; IntAct: EBI-3764669; Score: 0.35
DE  Interaction: P00950; IntAct: EBI-3764677; Score: 0.35
DE  Interaction: P25373; IntAct: EBI-3764685; Score: 0.35
DE  Interaction: P32477; IntAct: EBI-3764693; Score: 0.35
DE  Interaction: P48239; IntAct: EBI-3764701; Score: 0.35
DE  Interaction: Q08929; IntAct: EBI-3764714; Score: 0.35
DE  Interaction: Q05775; IntAct: EBI-3764722; Score: 0.35
DE  Interaction: P40012; IntAct: EBI-3764730; Score: 0.35
DE  Interaction: P32874; IntAct: EBI-3764738; Score: 0.35
DE  Interaction: P48362; IntAct: EBI-3764746; Score: 0.35
DE  Interaction: P02309; IntAct: EBI-3764754; Score: 0.35
DE  Interaction: P33734; IntAct: EBI-3764762; Score: 0.35
DE  Interaction: Q08702; IntAct: EBI-3764770; Score: 0.35
DE  Interaction: Q05080; IntAct: EBI-3764778; Score: 0.35
DE  Interaction: P40480; IntAct: EBI-3764786; Score: 0.35
DE  Interaction: Q05787; IntAct: EBI-3764794; Score: 0.35
DE  Interaction: Q05549; IntAct: EBI-3764802; Score: 0.35
DE  Interaction: Q12385; IntAct: EBI-3764810; Score: 0.35
DE  Interaction: P53982; IntAct: EBI-3764818; Score: 0.35
DE  Interaction: P25038; IntAct: EBI-3764826; Score: 0.35
DE  Interaction: P53897; IntAct: EBI-3764834; Score: 0.35
DE  Interaction: Q06706; IntAct: EBI-3764842; Score: 0.35
DE  Interaction: P25605; IntAct: EBI-3764850; Score: 0.35
DE  Interaction: P25642; IntAct: EBI-3764858; Score: 0.35
DE  Interaction: Q06704; IntAct: EBI-3764866; Score: 0.35
DE  Interaction: P47170; IntAct: EBI-3764874; Score: 0.35
DE  Interaction: P50942; IntAct: EBI-3764882; Score: 0.35
DE  Interaction: Q12271; IntAct: EBI-3764890; Score: 0.35
DE  Interaction: Q08227; IntAct: EBI-3764898; Score: 0.35
DE  Interaction: P47056; IntAct: EBI-3764911; Score: 0.35
DE  Interaction: Q07843; IntAct: EBI-3764919; Score: 0.35
DE  Interaction: Q06554; IntAct: EBI-3764927; Score: 0.35
DE  Interaction: P40541; IntAct: EBI-3764935; Score: 0.35
DE  Interaction: P38250; IntAct: EBI-3764943; Score: 0.35
DE  Interaction: P38144; IntAct: EBI-3764951; Score: 0.35
DE  Interaction: P53125; IntAct: EBI-3764959; Score: 0.35
DE  Interaction: Q12358; IntAct: EBI-3764967; Score: 0.35
DE  Interaction: P32767; IntAct: EBI-3764975; Score: 0.35
DE  Interaction: P38853; IntAct: EBI-3764983; Score: 0.35
DE  Interaction: P28742; IntAct: EBI-3764991; Score: 0.35
DE  Interaction: P32350; IntAct: EBI-3764999; Score: 0.35
DE  Interaction: P38873; IntAct: EBI-3765007; Score: 0.35
DE  Interaction: P27810; IntAct: EBI-3765015; Score: 0.35
DE  Interaction: P38130; IntAct: EBI-3765023; Score: 0.35
DE  Interaction: Q08963; IntAct: EBI-3765031; Score: 0.35
DE  Interaction: P53598; IntAct: EBI-3765039; Score: 0.35
DE  Interaction: P53312; IntAct: EBI-3765047; Score: 0.35
DE  Interaction: P07866; IntAct: EBI-3765055; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-3765063; Score: 0.35
DE  Interaction: P40957; IntAct: EBI-3765071; Score: 0.35
DE  Interaction: P29469; IntAct: EBI-3765079; Score: 0.35
DE  Interaction: P24279; IntAct: EBI-3765087; Score: 0.35
DE  Interaction: Q01846; IntAct: EBI-3765095; Score: 0.35
DE  Interaction: P38111; IntAct: EBI-3765103; Score: 0.35
DE  Interaction: P05694; IntAct: EBI-3765111; Score: 0.35
DE  Interaction: P43638; IntAct: EBI-3765119; Score: 0.35
DE  Interaction: P38760; IntAct: EBI-3765135; Score: 0.35
DE  Interaction: P40850; IntAct: EBI-3765143; Score: 0.35
DE  Interaction: Q07980; IntAct: EBI-3765151; Score: 0.35
DE  Interaction: Q12083; IntAct: EBI-3765159; Score: 0.35
DE  Interaction: Q02455; IntAct: EBI-3765167; Score: 0.35
DE  Interaction: P40457; IntAct: EBI-3765175; Score: 0.35
DE  Interaction: P36044; IntAct: EBI-3765183; Score: 0.35
DE  Interaction: P07884; IntAct: EBI-3765191; Score: 0.35
DE  Interaction: P32333; IntAct: EBI-3765199; Score: 0.35
DE  Interaction: Q12404; IntAct: EBI-3765207; Score: 0.35
DE  Interaction: P53159; IntAct: EBI-3765215; Score: 0.35
DE  Interaction: P32829; IntAct: EBI-3765223; Score: 0.35
DE  Interaction: Q06815; IntAct: EBI-3765231; Score: 0.35
DE  Interaction: P38175; IntAct: EBI-3765239; Score: 0.35
DE  Interaction: P36525; IntAct: EBI-3765247; Score: 0.35
DE  Interaction: P36534; IntAct: EBI-3765255; Score: 0.35
DE  Interaction: P21771; IntAct: EBI-3765263; Score: 0.35
DE  Interaction: P48525; IntAct: EBI-3765271; Score: 0.35
DE  Interaction: P25846; IntAct: EBI-3765279; Score: 0.53
DE  Interaction: Q03834; IntAct: EBI-3765287; Score: 0.35
DE  Interaction: P22438; IntAct: EBI-3765303; Score: 0.35
DE  Interaction: P52918; IntAct: EBI-3765312; Score: 0.35
DE  Interaction: P38714; IntAct: EBI-3765320; Score: 0.35
DE  Interaction: P38994; IntAct: EBI-3765328; Score: 0.35
DE  Interaction: Q03151; IntAct: EBI-3765336; Score: 0.35
DE  Interaction: Q03920; IntAct: EBI-3765344; Score: 0.35
DE  Interaction: P40959; IntAct: EBI-3765352; Score: 0.35
DE  Interaction: P08964; IntAct: EBI-3765360; Score: 0.35
DE  Interaction: P36006; IntAct: EBI-3765368; Score: 0.35
DE  Interaction: P27929; IntAct: EBI-3765376; Score: 0.35
DE  Interaction: P25293; IntAct: EBI-3765384; Score: 0.35
DE  Interaction: Q07500; IntAct: EBI-3765392; Score: 0.35
DE  Interaction: P40527; IntAct: EBI-3765400; Score: 0.35
DE  Interaction: P32497; IntAct: EBI-3765408; Score: 0.35
DE  Interaction: P33420; IntAct: EBI-3765416; Score: 0.35
DE  Interaction: P38798; IntAct: EBI-3765424; Score: 0.35
DE  Interaction: Q99207; IntAct: EBI-3765432; Score: 0.35
DE  Interaction: P39683; IntAct: EBI-3765440; Score: 0.35
DE  Interaction: P43124; IntAct: EBI-3765448; Score: 0.35
DE  Interaction: P40064; IntAct: EBI-3765456; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-3765464; Score: 0.35
DE  Interaction: Q00684; IntAct: EBI-3765472; Score: 0.35
DE  Interaction: P50946; IntAct: EBI-3765480; Score: 0.35
DE  Interaction: P53397; IntAct: EBI-3765488; Score: 0.35
DE  Interaction: P16547; IntAct: EBI-3765496; Score: 0.35
DE  Interaction: P21375; IntAct: EBI-3765504; Score: 0.35
DE  Interaction: P40512; IntAct: EBI-3765512; Score: 0.35
DE  Interaction: P40186; IntAct: EBI-3765520; Score: 0.35
DE  Interaction: Q12477; IntAct: EBI-3765528; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-3765536; Score: 0.35
DE  Interaction: P27801; IntAct: EBI-3765544; Score: 0.35
DE  Interaction: P12868; IntAct: EBI-3765552; Score: 0.35
DE  Interaction: P08468; IntAct: EBI-3765560; Score: 0.35
DE  Interaction: P32606; IntAct: EBI-3765568; Score: 0.35
DE  Interaction: P53112; IntAct: EBI-3765576; Score: 0.35
DE  Interaction: P35056; IntAct: EBI-3765584; Score: 0.35
DE  Interaction: P53248; IntAct: EBI-3765592; Score: 0.35
DE  Interaction: P40433; IntAct: EBI-3765600; Score: 0.35
DE  Interaction: P36093; IntAct: EBI-3765608; Score: 0.35
DE  Interaction: Q12252; IntAct: EBI-3765616; Score: 0.35
DE  Interaction: P19881; IntAct: EBI-3765624; Score: 0.35
DE  Interaction: P20052; IntAct: EBI-3765632; Score: 0.35
DE  Interaction: P38264; IntAct: EBI-3765640; Score: 0.35
DE  Interaction: P07271; IntAct: EBI-3765648; Score: 0.35
DE  Interaction: P24583; IntAct: EBI-3765656; Score: 0.35
DE  Interaction: Q03306; IntAct: EBI-3765664; Score: 0.35
DE  Interaction: P32634; IntAct: EBI-3765672; Score: 0.35
DE  Interaction: P33775; IntAct: EBI-3765680; Score: 0.35
DE  Interaction: P21951; IntAct: EBI-3765688; Score: 0.35
DE  Interaction: P39008; IntAct: EBI-3765696; Score: 0.35
DE  Interaction: P40478; IntAct: EBI-3765709; Score: 0.35
DE  Interaction: P27796; IntAct: EBI-3765717; Score: 0.35
DE  Interaction: P07272; IntAct: EBI-3765726; Score: 0.35
DE  Interaction: P09232; IntAct: EBI-3765734; Score: 0.35
DE  Interaction: P21242; IntAct: EBI-3765742; Score: 0.35
DE  Interaction: P23638; IntAct: EBI-3765750; Score: 0.35
DE  Interaction: P54885; IntAct: EBI-3765758; Score: 0.35
DE  Interaction: P24384; IntAct: EBI-3765766; Score: 0.35
DE  Interaction: P33334; IntAct: EBI-3765774; Score: 0.35
DE  Interaction: P31374; IntAct: EBI-3765790; Score: 0.35
DE  Interaction: Q08217; IntAct: EBI-3765798; Score: 0.35
DE  Interaction: P36082; IntAct: EBI-3765806; Score: 0.35
DE  Interaction: P40164; IntAct: EBI-3765814; Score: 0.35
DE  Interaction: Q04373; IntAct: EBI-3765822; Score: 0.35
DE  Interaction: Q08647; IntAct: EBI-3765830; Score: 0.35
DE  Interaction: P52489; IntAct: EBI-3765838; Score: 0.35
DE  Interaction: P40352; IntAct: EBI-3765846; Score: 0.35
DE  Interaction: P14736; IntAct: EBI-3765854; Score: 0.35
DE  Interaction: P32849; IntAct: EBI-3765862; Score: 0.35
DE  Interaction: P12753; IntAct: EBI-3765870; Score: 0.53
DE  Interaction: P53063; IntAct: EBI-3765878; Score: 0.35
DE  Interaction: Q02792; IntAct: EBI-3765886; Score: 0.35
DE  Interaction: P47104; IntAct: EBI-3765894; Score: 0.35
DE  Interaction: P25332; IntAct: EBI-3765902; Score: 0.35
DE  Interaction: P39531; IntAct: EBI-3765910; Score: 0.35
DE  Interaction: P12689; IntAct: EBI-3765918; Score: 0.35
DE  Interaction: P14284; IntAct: EBI-3765926; Score: 0.35
DE  Interaction: Q12090; IntAct: EBI-3765934; Score: 0.35
DE  Interaction: P38629; IntAct: EBI-3765942; Score: 0.35
DE  Interaction: Q06407; IntAct: EBI-3765950; Score: 0.35
DE  Interaction: P19263; IntAct: EBI-3765959; Score: 0.35
DE  Interaction: P40395; IntAct: EBI-3765967; Score: 0.35
DE  Interaction: P29539; IntAct: EBI-3765975; Score: 0.35
DE  Interaction: P32445; IntAct: EBI-3765983; Score: 0.35
DE  Interaction: P43565; IntAct: EBI-3765991; Score: 0.35
DE  Interaction: Q08562; IntAct: EBI-3765999; Score: 0.35
DE  Interaction: Q08961; IntAct: EBI-3766007; Score: 0.35
DE  Interaction: Q03942; IntAct: EBI-3766015; Score: 0.35
DE  Interaction: P53552; IntAct: EBI-3766023; Score: 0.35
DE  Interaction: P39975; IntAct: EBI-3766031; Score: 0.35
DE  Interaction: P32611; IntAct: EBI-3766039; Score: 0.35
DE  Interaction: Q04740; IntAct: EBI-3766047; Score: 0.35
DE  Interaction: P21672; IntAct: EBI-3766055; Score: 0.53
DE  Interaction: P49723; IntAct: EBI-3766063; Score: 0.35
DE  Interaction: P51862; IntAct: EBI-3766071; Score: 0.35
DE  Interaction: P08518; IntAct: EBI-3766079; Score: 0.35
DE  Interaction: P32910; IntAct: EBI-3766087; Score: 0.35
DE  Interaction: P36160; IntAct: EBI-3766095; Score: 0.35
DE  Interaction: P38249; IntAct: EBI-3766103; Score: 0.35
DE  Interaction: P05748; IntAct: EBI-3766111; Score: 0.35
DE  Interaction: P54780; IntAct: EBI-3766119; Score: 0.35
DE  Interaction: P14126; IntAct: EBI-3766127; Score: 0.35
DE  Interaction: P49166; IntAct: EBI-3766135; Score: 0.35
DE  Interaction: P05739; IntAct: EBI-3766143; Score: 0.35
DE  Interaction: P05737; IntAct: EBI-3766151; Score: 0.35
DE  Interaction: Q12213; IntAct: EBI-3766159; Score: 0.35
DE  Interaction: P38764; IntAct: EBI-3766167; Score: 0.35
DE  Interaction: P38886; IntAct: EBI-3766175; Score: 0.35
DE  Interaction: P53196; IntAct: EBI-3766183; Score: 0.35
DE  Interaction: P04050; IntAct: EBI-3766191; Score: 0.35
DE  Interaction: P38786; IntAct: EBI-3766199; Score: 0.35
DE  Interaction: P35271; IntAct: EBI-3766207; Score: 0.35
DE  Interaction: P33442; IntAct: EBI-3766215; Score: 0.35
DE  Interaction: P38701; IntAct: EBI-3766223; Score: 0.35
DE  Interaction: P26786; IntAct: EBI-3766232; Score: 0.35
DE  Interaction: P53549; IntAct: EBI-3766240; Score: 0.35
DE  Interaction: P33297; IntAct: EBI-3766248; Score: 0.35
DE  Interaction: Q01939; IntAct: EBI-3766256; Score: 0.35
DE  Interaction: Q12348; IntAct: EBI-3766264; Score: 0.35
DE  Interaction: P25359; IntAct: EBI-3766272; Score: 0.35
DE  Interaction: Q05022; IntAct: EBI-3766280; Score: 0.35
DE  Interaction: Q02206; IntAct: EBI-3766288; Score: 0.35
DE  Interaction: P13856; IntAct: EBI-3766296; Score: 0.35
DE  Interaction: P38903; IntAct: EBI-3766304; Score: 0.35
DE  Interaction: P40962; IntAct: EBI-3766312; Score: 0.35
DE  Interaction: P53289; IntAct: EBI-3766320; Score: 0.35
DE  Interaction: P46674; IntAct: EBI-3766328; Score: 0.35
DE  Interaction: P10659; IntAct: EBI-3766336; Score: 0.35
DE  Interaction: P50110; IntAct: EBI-3766344; Score: 0.35
DE  Interaction: P53036; IntAct: EBI-3766352; Score: 0.35
DE  Interaction: P53324; IntAct: EBI-3766360; Score: 0.35
DE  Interaction: Q04002; IntAct: EBI-3766368; Score: 0.35
DE  Interaction: Q12334; IntAct: EBI-3766376; Score: 0.35
DE  Interaction: P38072; IntAct: EBI-3766384; Score: 0.35
DE  Interaction: P48415; IntAct: EBI-3766392; Score: 0.35
DE  Interaction: P18759; IntAct: EBI-3766400; Score: 0.35
DE  Interaction: P32844; IntAct: EBI-3766408; Score: 0.35
DE  Interaction: P32855; IntAct: EBI-3766416; Score: 0.35
DE  Interaction: Q04228; IntAct: EBI-3766424; Score: 0.35
DE  Interaction: Q00416; IntAct: EBI-3766432; Score: 0.35
DE  Interaction: P33330; IntAct: EBI-3766440; Score: 0.35
DE  Interaction: P36124; IntAct: EBI-3766448; Score: 0.35
DE  Interaction: Q12369; IntAct: EBI-3766456; Score: 0.35
DE  Interaction: P34223; IntAct: EBI-3766472; Score: 0.35
DE  Interaction: Q07657; IntAct: EBI-3766480; Score: 0.35
DE  Interaction: P53266; IntAct: EBI-3766488; Score: 0.35
DE  Interaction: Q12460; IntAct: EBI-3766496; Score: 0.35
DE  Interaction: P22579; IntAct: EBI-3766504; Score: 0.35
DE  Interaction: P53965; IntAct: EBI-3766512; Score: 0.35
DE  Interaction: Q06315; IntAct: EBI-3766520; Score: 0.35
DE  Interaction: P35207; IntAct: EBI-3766528; Score: 0.35
DE  Interaction: P42843; IntAct: EBI-3766536; Score: 0.35
DE  Interaction: Q02775; IntAct: EBI-3766544; Score: 0.35
DE  Interaction: P32908; IntAct: EBI-3766552; Score: 0.35
DE  Interaction: P12904; IntAct: EBI-3766568; Score: 0.35
DE  Interaction: P32568; IntAct: EBI-3766576; Score: 0.35
DE  Interaction: P25357; IntAct: EBI-3766584; Score: 0.35
DE  Interaction: P53127; IntAct: EBI-3766592; Score: 0.35
DE  Interaction: Q04748; IntAct: EBI-3766600; Score: 0.35
DE  Interaction: P23201; IntAct: EBI-3766608; Score: 0.35
DE  Interaction: P25808; IntAct: EBI-3766616; Score: 0.35
DE  Interaction: P32380; IntAct: EBI-3766624; Score: 0.35
DE  Interaction: P36126; IntAct: EBI-3766632; Score: 0.35
DE  Interaction: Q03868; IntAct: EBI-3766640; Score: 0.35
DE  Interaction: Q03012; IntAct: EBI-3766648; Score: 0.35
DE  Interaction: P08458; IntAct: EBI-3766656; Score: 0.53
DE  Interaction: P32558; IntAct: EBI-3766664; Score: 0.35
DE  Interaction: Q03707; IntAct: EBI-3766672; Score: 0.35
DE  Interaction: Q12020; IntAct: EBI-3766680; Score: 0.35
DE  Interaction: P38688; IntAct: EBI-3766688; Score: 0.35
DE  Interaction: P53599; IntAct: EBI-3766696; Score: 0.53
DE  Interaction: P47821; IntAct: EBI-3766704; Score: 0.35
DE  Interaction: P11972; IntAct: EBI-3766712; Score: 0.35
DE  Interaction: P46679; IntAct: EBI-3766720; Score: 0.35
DE  Interaction: P18851; IntAct: EBI-3766728; Score: 0.53
DE  Interaction: P32597; IntAct: EBI-3766736; Score: 0.35
DE  Interaction: P53101; IntAct: EBI-3766744; Score: 0.35
DE  Interaction: P37297; IntAct: EBI-3766752; Score: 0.35
DE  Interaction: P38198; IntAct: EBI-3766760; Score: 0.35
DE  Interaction: P09064; IntAct: EBI-3766768; Score: 0.35
DE  Interaction: P46676; IntAct: EBI-3766776; Score: 0.35
DE  Interaction: P12385; IntAct: EBI-3766784; Score: 0.35
DE  Interaction: P31376; IntAct: EBI-3766792; Score: 0.35
DE  Interaction: P08153; IntAct: EBI-3766800; Score: 0.35
DE  Interaction: P40528; IntAct: EBI-3766808; Score: 0.35
DE  Interaction: P40468; IntAct: EBI-3766816; Score: 0.35
DE  Interaction: Q06510; IntAct: EBI-3766824; Score: 0.35
DE  Interaction: Q12466; IntAct: EBI-3766832; Score: 0.35
DE  Interaction: Q03640; IntAct: EBI-3766840; Score: 0.35
DE  Interaction: P38228; IntAct: EBI-3766848; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-3766856; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-3766864; Score: 0.35
DE  Interaction: P41903; IntAct: EBI-3766872; Score: 0.35
DE  Interaction: P36145; IntAct: EBI-3766880; Score: 0.35
DE  Interaction: Q02939; IntAct: EBI-3766888; Score: 0.35
DE  Interaction: P32367; IntAct: EBI-3766896; Score: 0.35
DE  Interaction: P14306; IntAct: EBI-3766904; Score: 0.35
DE  Interaction: P10081; IntAct: EBI-3766912; Score: 0.35
DE  Interaction: P34167; IntAct: EBI-3766920; Score: 0.35
DE  Interaction: P40217; IntAct: EBI-3766928; Score: 0.35
DE  Interaction: Q04067; IntAct: EBI-3766936; Score: 0.35
DE  Interaction: P38431; IntAct: EBI-3766944; Score: 0.35
DE  Interaction: Q01852; IntAct: EBI-3766952; Score: 0.35
DE  Interaction: Q02208; IntAct: EBI-3766960; Score: 0.35
DE  Interaction: P35169; IntAct: EBI-3766976; Score: 0.35
DE  Interaction: P40032; IntAct: EBI-3766984; Score: 0.35
DE  Interaction: P40414; IntAct: EBI-3766992; Score: 0.35
DE  Interaction: P48561; IntAct: EBI-3767000; Score: 0.35
DE  Interaction: P12685; IntAct: EBI-3767008; Score: 0.35
DE  Interaction: Q04183; IntAct: EBI-3767016; Score: 0.35
DE  Interaction: P40061; IntAct: EBI-3767024; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-3767032; Score: 0.35
DE  Interaction: P09734; IntAct: EBI-3767040; Score: 0.35
DE  Interaction: P52488; IntAct: EBI-3767048; Score: 0.35
DE  Interaction: P25037; IntAct: EBI-3767056; Score: 0.35
DE  Interaction: Q06682; IntAct: EBI-3767064; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-3767072; Score: 0.35
DE  Interaction: P03962; IntAct: EBI-3767080; Score: 0.35
DE  Interaction: P25386; IntAct: EBI-3767088; Score: 0.35
DE  Interaction: P35194; IntAct: EBI-3767096; Score: 0.35
DE  Interaction: P53254; IntAct: EBI-3767104; Score: 0.35
DE  Interaction: Q06679; IntAct: EBI-3767112; Score: 0.35
DE  Interaction: Q07468; IntAct: EBI-3767120; Score: 0.35
DE  Interaction: P40522; IntAct: EBI-3767128; Score: 0.35
DE  Interaction: Q06337; IntAct: EBI-3767136; Score: 0.35
DE  Interaction: P40157; IntAct: EBI-3767144; Score: 0.35
DE  Interaction: P40547; IntAct: EBI-3767152; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-3767160; Score: 0.35
DE  Interaction: P23643; IntAct: EBI-3767168; Score: 0.35
DE  Interaction: Q03433; IntAct: EBI-3767176; Score: 0.35
DE  Interaction: P40438; IntAct: EBI-3767184; Score: 0.35
DE  Interaction: P40890; IntAct: EBI-3767192; Score: 0.35
DE  Interaction: P33767; IntAct: EBI-3767200; Score: 0.35
DE  Interaction: Q12416; IntAct: EBI-3767208; Score: 0.35
DE  Interaction: P38749; IntAct: EBI-3767216; Score: 0.35
DE  Interaction: O13527; IntAct: EBI-3767224; Score: 0.35
DE  Interaction: P40017; IntAct: EBI-3767232; Score: 0.35
DE  Interaction: P34220; IntAct: EBI-3767240; Score: 0.35
DE  Interaction: P34225; IntAct: EBI-3767248; Score: 0.35
DE  Interaction: Q12491; IntAct: EBI-3767256; Score: 0.35
DE  Interaction: Q12193; IntAct: EBI-3767271; Score: 0.35
DE  Interaction: P38219; IntAct: EBI-3767279; Score: 0.35
DE  Interaction: P38266; IntAct: EBI-3767287; Score: 0.35
DE  Interaction: P38331; IntAct: EBI-3767295; Score: 0.35
DE  Interaction: P38332; IntAct: EBI-3767303; Score: 0.35
DE  Interaction: P39109; IntAct: EBI-3767311; Score: 0.35
DE  Interaction: P25616; IntAct: EBI-3767319; Score: 0.35
DE  Interaction: Q06156; IntAct: EBI-3767327; Score: 0.35
DE  Interaction: Q07349; IntAct: EBI-3767335; Score: 0.35
DE  Interaction: Q12516; IntAct: EBI-3767343; Score: 0.35
DE  Interaction: Q06640; IntAct: EBI-3767351; Score: 0.35
DE  Interaction: Q04411; IntAct: EBI-3767359; Score: 0.35
DE  Interaction: P89887; IntAct: EBI-3767367; Score: 0.35
DE  Interaction: Q3E7X8; IntAct: EBI-3767379; Score: 0.35
DE  Interaction: P40028; IntAct: EBI-3767387; Score: 0.35
DE  Interaction: P40085; IntAct: EBI-3767395; Score: 0.35
DE  Interaction: P43560; IntAct: EBI-3767403; Score: 0.35
DE  Interaction: P43597; IntAct: EBI-3767411; Score: 0.35
DE  Interaction: P53144; IntAct: EBI-3767419; Score: 0.35
DE  Interaction: P53100; IntAct: EBI-3767427; Score: 0.35
DE  Interaction: P53077; IntAct: EBI-3767435; Score: 0.35
DE  Interaction: P53234; IntAct: EBI-3767443; Score: 0.35
DE  Interaction: P53246; IntAct: EBI-3767451; Score: 0.35
DE  Interaction: Q99315; IntAct: EBI-3767459; Score: 0.35
DE  Interaction: P50089; IntAct: EBI-3767474; Score: 0.35
DE  Interaction: P53321; IntAct: EBI-3767482; Score: 0.35
DE  Interaction: Q05900; IntAct: EBI-3767490; Score: 0.35
DE  Interaction: P0C2J7; IntAct: EBI-3767498; Score: 0.35
DE  Interaction: P38842; IntAct: EBI-3767506; Score: 0.35
DE  Interaction: P47024; IntAct: EBI-3767514; Score: 0.35
DE  Interaction: P47101; IntAct: EBI-3767522; Score: 0.35
DE  Interaction: P28320; IntAct: EBI-3767530; Score: 0.35
DE  Interaction: P34246; IntAct: EBI-3767538; Score: 0.35
DE  Interaction: P34248; IntAct: EBI-3767546; Score: 0.35
DE  Interaction: P28273; IntAct: EBI-3767554; Score: 0.35
DE  Interaction: P36158; IntAct: EBI-3767562; Score: 0.35
DE  Interaction: Q07799; IntAct: EBI-3767570; Score: 0.35
DE  Interaction: Q12244; IntAct: EBI-3767578; Score: 0.35
DE  Interaction: Q12177; IntAct: EBI-3767586; Score: 0.35
DE  Interaction: Q07897; IntAct: EBI-3767594; Score: 0.35
DE  Interaction: Q12110; IntAct: EBI-3767602; Score: 0.35
DE  Interaction: Q12288; IntAct: EBI-3767610; Score: 0.35
DE  Interaction: Q06247; IntAct: EBI-3767622; Score: 0.35
DE  Interaction: Q06152; IntAct: EBI-3767630; Score: 0.35
DE  Interaction: Q05867; IntAct: EBI-3767638; Score: 0.35
DE  Interaction: Q06159; IntAct: EBI-3767646; Score: 0.35
DE  Interaction: Q06479; IntAct: EBI-3767654; Score: 0.35
DE  Interaction: Q06409; IntAct: EBI-3767662; Score: 0.35
DE  Interaction: O13577; IntAct: EBI-3767670; Score: 0.35
DE  Interaction: Q04533; IntAct: EBI-3767678; Score: 0.35
DE  Interaction: Q04371; IntAct: EBI-3767686; Score: 0.35
DE  Interaction: P0CF18; IntAct: EBI-3767694; Score: 0.35
DE  Interaction: Q03153; IntAct: EBI-3767709; Score: 0.35
DE  Interaction: Q04471; IntAct: EBI-3767717; Score: 0.35
DE  Interaction: Q03496; IntAct: EBI-3767725; Score: 0.35
DE  Interaction: P40168; IntAct: EBI-3767733; Score: 0.35
DE  Interaction: P53850; IntAct: EBI-3767753; Score: 0.35
DE  Interaction: P53837; IntAct: EBI-3767765; Score: 0.35
DE  Interaction: P53756; IntAct: EBI-3767773; Score: 0.35
DE  Interaction: P53757; IntAct: EBI-3767781; Score: 0.35
DE  Interaction: Q99247; IntAct: EBI-3767789; Score: 0.53
DE  Interaction: Q12496; IntAct: EBI-3767797; Score: 0.35
DE  Interaction: Q08270; IntAct: EBI-3767805; Score: 0.35
DE  Interaction: Q08457; IntAct: EBI-3767813; Score: 0.35
DE  Interaction: Q12275; IntAct: EBI-3767821; Score: 0.35
DE  Interaction: P53049; IntAct: EBI-3767829; Score: 0.35
DE  Interaction: Q12032; IntAct: EBI-3767837; Score: 0.35
DE  Interaction: Q08748; IntAct: EBI-3767845; Score: 0.35
DE  Interaction: Q02754; IntAct: EBI-3767853; Score: 0.35
DE  Interaction: Q02895; IntAct: EBI-3767861; Score: 0.35
DE  Interaction: Q08964; IntAct: EBI-3767869; Score: 0.35
DE  Interaction: Q06813; IntAct: EBI-3767877; Score: 0.35
DE  Interaction: Q06108; IntAct: EBI-3767885; Score: 0.35
DE  Interaction: P01123; IntAct: EBI-3767893; Score: 0.35
DE  Interaction: P51996; IntAct: EBI-3767901; Score: 0.35
DE  Interaction: P36019; IntAct: EBI-3767909; Score: 0.35
DE  Interaction: Q12159; IntAct: EBI-3767917; Score: 0.35
DE  Interaction: P53819; IntAct: EBI-3767925; Score: 0.35
DE  Interaction: P40341; IntAct: EBI-3767933; Score: 0.35
DE  Interaction: P40328; IntAct: EBI-3767941; Score: 0.35
DE  Interaction: P40340; IntAct: EBI-3767949; Score: 0.35
DE  Interaction: P31111; IntAct: EBI-3767957; Score: 0.35
DE  Interaction: P22202; IntAct: EBI-3767965; Score: 0.35
DE  Interaction: A0A023PZA9; IntAct: EBI-3862867; Score: 0.35
DE  Interaction: P22146; IntAct: EBI-6900105; Score: 0.27
DE  Interaction: P04150; IntAct: EBI-9819201; Score: 0.50
DE  Interaction: P40075; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P25367; IntAct: EBI-15790589; Score: 0.44
DE  Interaction: Q08601; IntAct: EBI-15865212; Score: 0.35
DE  Interaction: Q12004; IntAct: EBI-15942387; Score: 0.35
DE  Interaction: Q00776; IntAct: EBI-16263794; Score: 0.35
DE  Interaction: P38153; IntAct: EBI-16263895; Score: 0.35
DE  Interaction: P32381; IntAct: EBI-16264169; Score: 0.35
DE  Interaction: P26448; IntAct: EBI-16264549; Score: 0.35
DE  Interaction: P53323; IntAct: EBI-16264767; Score: 0.35
DE  Interaction: P00546; IntAct: EBI-16265841; Score: 0.35
DE  Interaction: P25656; IntAct: EBI-16266167; Score: 0.35
DE  Interaction: Q00362; IntAct: EBI-16266261; Score: 0.35
DE  Interaction: P06243; IntAct: EBI-16266350; Score: 0.35
DE  Interaction: P04819; IntAct: EBI-16266449; Score: 0.35
DE  Interaction: P38147; IntAct: EBI-16266584; Score: 0.35
DE  Interaction: Q01649; IntAct: EBI-16266663; Score: 0.35
DE  Interaction: P24869; IntAct: EBI-16266949; Score: 0.35
DE  Interaction: P41735; IntAct: EBI-16267444; Score: 0.35
DE  Interaction: P47027; IntAct: EBI-16268315; Score: 0.35
DE  Interaction: P17214; IntAct: EBI-16268957; Score: 0.35
DE  Interaction: P32502; IntAct: EBI-16269661; Score: 0.35
DE  Interaction: P32598; IntAct: EBI-16270070; Score: 0.35
DE  Interaction: P06774; IntAct: EBI-16270452; Score: 0.35
DE  Interaction: P13434; IntAct: EBI-16270569; Score: 0.35
DE  Interaction: Q99181; IntAct: EBI-16271249; Score: 0.35
DE  Interaction: P32464; IntAct: EBI-16271424; Score: 0.35
DE  Interaction: P32581; IntAct: EBI-16271455; Score: 0.35
DE  Interaction: P13902; IntAct: EBI-16271541; Score: 0.35
DE  Interaction: P14681; IntAct: EBI-16272210; Score: 0.35
DE  Interaction: Q12446; IntAct: EBI-16272438; Score: 0.35
DE  Interaction: Q02574; IntAct: EBI-16273337; Score: 0.35
DE  Interaction: P39014; IntAct: EBI-16273553; Score: 0.35
DE  Interaction: P26188; IntAct: EBI-16273684; Score: 0.35
DE  Interaction: P32491; IntAct: EBI-16273903; Score: 0.35
DE  Interaction: Q04149; IntAct: EBI-16274423; Score: 0.35
DE  Interaction: Q02931; IntAct: EBI-16274579; Score: 0.35
DE  Interaction: P40354; IntAct: EBI-16274812; Score: 0.35
DE  Interaction: P39108; IntAct: EBI-16275488; Score: 0.35
DE  Interaction: P16862; IntAct: EBI-16275628; Score: 0.35
DE  Interaction: P25615; IntAct: EBI-16276002; Score: 0.35
DE  Interaction: P23594; IntAct: EBI-16276062; Score: 0.35
DE  Interaction: P30620; IntAct: EBI-16276917; Score: 0.35
DE  Interaction: P34221; IntAct: EBI-16277075; Score: 0.35
DE  Interaction: P25635; IntAct: EBI-16277306; Score: 0.35
DE  Interaction: Q04049; IntAct: EBI-16278245; Score: 0.35
DE  Interaction: Q12223; IntAct: EBI-16278713; Score: 0.35
DE  Interaction: P40348; IntAct: EBI-16279429; Score: 0.35
DE  Interaction: Q12300; IntAct: EBI-16279741; Score: 0.35
DE  Interaction: Q12749; IntAct: EBI-16279839; Score: 0.35
DE  Interaction: P05317; IntAct: EBI-16280656; Score: 0.35
DE  Interaction: P33298; IntAct: EBI-16280713; Score: 0.35
DE  Interaction: P41811; IntAct: EBI-16281700; Score: 0.35
DE  Interaction: P38262; IntAct: EBI-16282437; Score: 0.35
DE  Interaction: P32259; IntAct: EBI-16282486; Score: 0.35
DE  Interaction: P34164; IntAct: EBI-16282515; Score: 0.35
DE  Interaction: P06701; IntAct: EBI-16282584; Score: 0.35
DE  Interaction: P20604; IntAct: EBI-16282774; Score: 0.35
DE  Interaction: Q00772; IntAct: EBI-16283115; Score: 0.35
DE  Interaction: P41808; IntAct: EBI-16283296; Score: 0.35
DE  Interaction: Q00916; IntAct: EBI-16283579; Score: 0.35
DE  Interaction: P53541; IntAct: EBI-16283760; Score: 0.35
DE  Interaction: Q12379; IntAct: EBI-16284692; Score: 0.35
DE  Interaction: P38987; IntAct: EBI-16285008; Score: 0.35
DE  Interaction: P53916; IntAct: EBI-16285181; Score: 0.35
DE  Interaction: P53632; IntAct: EBI-16285647; Score: 0.35
DE  Interaction: P52490; IntAct: EBI-16285898; Score: 0.35
DE  Interaction: P14680; IntAct: EBI-16286565; Score: 0.35
DE  Interaction: P38191; IntAct: EBI-16286723; Score: 0.35
DE  Interaction: P38319; IntAct: EBI-16286900; Score: 0.35
DE  Interaction: Q03899; IntAct: EBI-16287816; Score: 0.35
DE  Interaction: Q03944; IntAct: EBI-16287890; Score: 0.35
DE  Interaction: Q05498; IntAct: EBI-16288251; Score: 0.35
DE  Interaction: P87263; IntAct: EBI-16288516; Score: 0.35
DE  Interaction: P53156; IntAct: EBI-16288834; Score: 0.35
DE  Interaction: P53295; IntAct: EBI-16289121; Score: 0.35
DE  Interaction: P36005; IntAct: EBI-16290101; Score: 0.35
DE  Interaction: P32807; IntAct: EBI-16290244; Score: 0.35
DE  Interaction: Q04437; IntAct: EBI-16290301; Score: 0.35
DE  Interaction: P53877; IntAct: EBI-16291922; Score: 0.35
DE  Interaction: Q12152; IntAct: EBI-16292374; Score: 0.35
DE  Interaction: P0CE41; IntAct: EBI-16401531; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0017053;
GO  GO:0072380;
GO  GO:0005524;
GO  GO:0001671;
GO  GO:0051087;
GO  GO:0030544;
GO  GO:0046872;
GO  GO:0051082;
GO  GO:0006458;
GO  GO:0051131;
GO  GO:0045892;
GO  GO:0042026;
GO  GO:0045047;
GO  GO:0006626;
GO  GO:0009408;
GO  GO:0070482;
GO  GO:0035719;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:1527016};
SQ  MVKETKFYDILGVPVTATDVEIKKAYRKCALKYHPDKNPSEEAAEKFKEASAAYEILSDPEKRDIYDQFGEDGLSGAGGA
SQ  GGFPGGGFGFGDDIFSQFFGAGGAQRPRGPQRGKDIKHEISASLEELYKGRTAKLALNKQILCKECEGRGGKKGAVKKCT
SQ  SCNGQGIKFVTRQMGPMIQRFQTECDVCHGTGDIIDPKDRCKSCNGKKVENERKILEVHVEPGMKDGQRIVFKGEADQAP
SQ  DVIPGDVVFIVSERPHKSFKRDGDDLVYEAEIDLLTAIAGGEFALEHVSGDWLKVGIVPGEVIAPGMRKVIEGKGMPIPK
SQ  YGGYGNLIIKFTIKFPENHFTSEENLKKLEEILPPRIVPAIPKKATVDECVLADFDPAKYNRTRASRGGANYDSDEEEQG
SQ  GEGVQCASQ
//
ID  A7WNB1;
PN  Matrix protein;
GN  M;
OS  666363;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: A7WNB1;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0016020;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MNKMNQLVRFVKDTVAVRKPQSEDKSYLPIPSTIGGHEVNSPFAEPTAPSLGIIQPKCKRADWLIKSHLTITTNYEIKEW
SQ  ETWDRAISDILDLYDGNPVFKPILLFVYYVLAYNARKIPGPSNGVRYGAYFDELTTVWHAIPELMNQEIDYSYNHRVLHR
SQ  KIQYVISFKIQMSSTKRRTSPIESFIEVTSEGLKHTPQFTTILDRARFVYSLTGGRYVIHPF
//
ID  P04888;
PN  Matrix protein;
GN  M;
OS  696863;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: P04888;
DR  UNIPROT: Q91DS1;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0016020;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MSTLRKLFGIKKSKGTPPTYEETLATAPVLMDTHDTHSHSLQWMRYHVELDVKLDTPLKTMSDLLGLLKNWDVDYKGSRN
SQ  KRRFYRLIMFRCALELKHVSGTYSVDGSALYSNKVQGSCYVPHRFGQMPPFKREIEVFRYPVHQHGYNGMVDLRMSICDL
SQ  NGEKIGLNLLKECQVAHPNHFQKYLEEVGLEAACSATGEWILDWTFPMPVDVVPRVPSLFMGD
//
ID  D8V072;
PN  Matrix protein;
GN  M;
OS  1559361;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: D8V072;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0016020;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MLSRIKQGIKTKRSSSSSSSRSKTGDEDSSLMLRWVYDNDPPLKQTDTFQYLMAPTAPTDKASSSYIATTYKVDCKVEII
SQ  SRASIRNFDELINIASCLIDSYDGQLLIKPWIITVYLTIITHLVKEPDTHGVRSSVNRYHNGFNEILTLYINKNFAPENK
SQ  KYSFKKNLSTTHKGNQCNIIISIDLLPTDRKGKSIKDVYEVKMPDNREIPNFQQMLKPYNLKVKEKNGKYLISHKMSSSD
SQ  DSIDVSDSDENEF
//
ID  Q4VKV5;
PN  Matrix protein;
GN  M;
OS  1560034;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: Q4VKV5;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: Yes;
GO  GO:0044200;
GO  GO:0016020;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MLRWFSFGSNEGSEVAGNGWSVKPIGNMSIKKDDPVGFPQGYQCLLKVIIQLEKKDPTKSDVSELIAGWVKRYSGPHLLE
SQ  RLIKALIILTVPKLSRENIDNHVKLGGLFEGQVTFHFSSRDLIPTKYLSYATSIRTTVKGIYSYLSIEAELNPSSHQGTS
SQ  VAKLLRASDVAKYYDNTLQSIFSQFEIKNVTITDDQIIFN
//
ID  P03519;
PN  Matrix protein;
GN  M;
OS  11285;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane; Peripheral membrane protein {ECO:0000269|PubMed:1850035}. Host endomembrane system; Peripheral membrane protein. Host nucleus membrane; Peripheral membrane protein. Host nucleus {ECO:0000269|PubMed:28888655}. Host cytoplasm {ECO:0000269|PubMed:28888655}.
DR  UNIPROT: P03519;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000269|PubMed:16298982, ECO:0000269|PubMed:20943988}. Inhibits mRNA nuclear export through direct interaction with host RAE1-NUP98 complex, thereby preventing interferon signaling and establishment of antiviral state in infected cells (PubMed:15629720, PubMed:33849972). Induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell (PubMed:15629720). Inhibits host transcription, possibly through interaction with host DNA repair factor IIH/TFIIH GTF2H5 subunit (PubMed:28888655). {ECO:0000269|PubMed:15629720, ECO:0000269|PubMed:28888655, ECO:0000269|PubMed:33849972}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9BUJ2; IntAct: EBI-7228130; Score: 0.40
DE  Interaction: P78406; IntAct: EBI-7228174; Score: 0.53
DE  Interaction: P52948; IntAct: EBI-7228174; Score: 0.53
GO  GO:0030430;
GO  GO:0044200;
GO  GO:0016020;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0016310;
GO  GO:0039522;
GO  GO:0039602;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:1850035};
SQ  MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTYDPNQLRYEKFFFTVKMTVRSNRPFRT
SQ  YSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHTHCEGRAYLPHRMGKTPPMLNVPEHFRR
SQ  PFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEKKASGAWVLDSISHFK
//
ID  Q8B0H2;
PN  Matrix protein;
GN  M;
OS  434489;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus {ECO:0000250|UniProtKB:P03519}. Host cytoplasm {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: Q8B0H2;
DR  PDB: 1LG7;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}. Inhibits mRNA nuclear export through direct interaction with host RAE1-NUP98 complex, thereby preventing interferon signaling and establishment of antiviral state in infected cells. Induces cell- rounding, cytoskeleton disorganization and apoptosis in infected cell. Inhibits host transcription, possibly through interaction with host DNA repair factor IIH/TFIIH GTF2H5 subunit (By similarity). {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: No;
GO  GO:0030430;
GO  GO:0044200;
GO  GO:0016020;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039522;
GO  GO:0039602;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTHDPNQLRYEKFFFTVKMTVRSNRPFRT
SQ  YSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADRGQPEYHAHCEGRAYLPHRMGKTPPMLNVPEHFRR
SQ  PFNIGLYKGTVELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEKKASGAWVLDSVSHFK
//
ID  P04876;
PN  Matrix protein;
GN  M;
OS  11278;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus {ECO:0000250|UniProtKB:P03519}. Host cytoplasm {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: P04876;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}. Inhibits mRNA nuclear export through direct interaction with host RAE1-NUP98 complex, thereby preventing interferon signaling and establishment of antiviral state in infected cells. Induces cell- rounding, cytoskeleton disorganization and apoptosis in infected cell. Inhibits host transcription, possibly through interaction with host DNA repair factor IIH/TFIIH GTF2H5 subunit (By similarity). {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: Yes;
GO  GO:0030430;
GO  GO:0044200;
GO  GO:0016020;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039522;
GO  GO:0039602;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTHDPNQLRYEKSFFTVKMTVRSNRPFRT
SQ  YSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHAHCEGRAYLPHRMGKTPPMLNVPEHFRR
SQ  PFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEEEASGAWVLDSVRHSKWASLASSF
//
ID  Q8B0I2;
PN  Matrix protein;
GN  M;
OS  434488;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus {ECO:0000250|UniProtKB:P03519}. Host cytoplasm {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: Q8B0I2;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}. Inhibits mRNA nuclear export through direct interaction with host RAE1-NUP98 complex, thereby preventing interferon signaling and establishment of antiviral state in infected cells. Induces cell- rounding, cytoskeleton disorganization and apoptosis in infected cell. Inhibits host transcription, possibly through interaction with host DNA repair factor IIH/TFIIH GTF2H5 subunit (By similarity). {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: No;
GO  GO:0030430;
GO  GO:0044200;
GO  GO:0016020;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039522;
GO  GO:0039602;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTHDPNQLRYEKFFFTVKLTVRSNRPFRT
SQ  YSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHAHCEGRAYLPHRMGKTPPMLNVPEHFRR
SQ  PFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEKKASGAWILDSVSHFK
//
ID  Q8B0H7;
PN  Matrix protein;
GN  M;
OS  434490;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host nucleus {ECO:0000250|UniProtKB:P03519}. Host cytoplasm {ECO:0000250|UniProtKB:P03519}.
DR  UNIPROT: Q8B0H7;
DR  PDB: 4OWR;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000250|UniProtKB:P03519}. Inhibits mRNA nuclear export through direct interaction with host RAE1-NUP98 complex, thereby preventing interferon signaling and establishment of antiviral state in infected cells. Induces cell- rounding, cytoskeleton disorganization and apoptosis in infected cell. Inhibits host transcription, possibly through interaction with host DNA repair factor IIH/TFIIH GTF2H5 subunit (By similarity). {ECO:0000250|UniProtKB:P03519}.
DE  Reference Proteome: No;
GO  GO:0030430;
GO  GO:0044200;
GO  GO:0016020;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039522;
GO  GO:0039602;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P03519};
SQ  MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTHDPNQLRYEKFFFTVKMTVRSNRPFRT
SQ  YSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHAHCEGRAYLPHRMGKTPPMLNVPEHFRR
SQ  PFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEKKASGAWVLDSVSHFK
//
ID  P08325;
PN  Matrix protein;
GN  M;
OS  11283;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion membrane; Peripheral membrane protein. Host endomembrane system; Peripheral membrane protein. Host nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
DR  UNIPROT: P08325;
DR  PDB: 2W2R;
DR  Pfam: PF06326;
DE  Function: Plays a major role in assembly and budding of virion. Condensates the ribonucleocapsid core during virus assembly. Shut off cellular transcription by inhibiting mRNA nuclear export through direct interaction with host RAE1-NUP98 complex. This shutoff presumably inhibits interferon signaling and thus establishment of antiviral state in virus infected cells. Induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
DE  Interaction: Q12906; IntAct: EBI-15693264; Score: 0.50
DE  Interaction: P07910; IntAct: EBI-15693290; Score: 0.35
GO  GO:0044200;
GO  GO:0016020;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0039660;
GO  GO:0039657;
GO  GO:0039522;
GO  GO:0039702;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSFKKILGLSSKSHKKSKKMGLPPPYDESCPMETQPSAPLSNDFFGMEDMDLYDKDSLRYEKFRFMLKMTVRSNKPFRS
SQ  YDDVTAAVSQWDNSYIGMVGKRPFYKIIAVIGSSHLQATPAVLADLNQPEYYATLTGRCFLPHRLGLIPPMFNVQETFRK
SQ  PFNIGLYKGTLDFTFTVSDDESNEKVPHVWDYMNPKYQSQIQQEGLKFGLILSKKATGTWVLDQLSPFK
//
ID  P52302;
PN  Protein lethal(3)malignant blood neoplasm 1;
GN  l;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:8174791}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8174791}. Note=Mainly around the nucleus.
DR  UNIPROT: P52302;
DR  UNIPROT: Q59E19;
DR  UNIPROT: Q8MS87;
DR  UNIPROT: Q9VRU6;
DR  Pfam: PF00379;
DR  PROSITE: PS51155;
DE  Function: Required for differentiation of the phagocytic blood-cell type, the plasmatocyte. {ECO:0000269|PubMed:8174791}.
DE  Reference Proteome: Yes;
GO  GO:0062129;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0008010;
GO  GO:0040003;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLKLMAFVCALLLLCTLTHVLSAATTVRPYKFGFTIDEQQHRAEKRDERGIIMGEFGFITADGIYHVTVYATDEEGKFR
SQ  IISMKSYPYAGPVGSKSVPVTTTPKVLLPAAPVALPKYNFNSEACSGCFLKKSPPKTEIRTLSQPLAPVQPGKPDGSSDI
SQ  GLNVQLPFRESIAQTVASRLGLLQDTLQTSNTNTNAPNTKTIELGLNIAMSTYYTTKNAVTGHVSTQTSNSQTPSANTKI
SQ  DYNVGVVEKASPPVYRPLNIRLNEDVMRQAITYGNTIPGHVPLPNQPLVETSLLPASQVKIFALDGNAKVPLASNIQSVA
SQ  QHPNAGLNAKVPLASNIQSVAQHPNAGLNAKVPLASNIQSVAQHPNAGLKNINRSGVSSAKTLANTKTRPPHTFNPHQTP
SQ  LLSSATAPGISGVTANTPTGNVPSNGGGIAAGKAPGNPQAGGSGGIIGAGAPGGRKVSAGGIGSGSAIGGVSGGSKASGN
SQ  GGAIGSGSAIGGGATGSKASGFGFGSNIGGGVSGSKPSGFGSESKIGGPDSGSKALGFGSGSKIGGGITGTKASGFGGEI
SQ  GSGRGSASSATGDLYKFKYILDYNGHEETGGRNGDKQGSYFAIGEDAVQRTIEYIANEFGFQPHVSWRKLDAKEALPEEN
SQ  SLKHYEFKWFNQE
//
ID  Q80YF0;
PN  Mitotic spindle assembly checkpoint protein MAD1;
GN  MAD1L1;
OS  10029;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y6D9}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9Y6D9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9Y6D9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9Y6D9}. Note=Detected at the nucleus envelope during interphase. From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody. Detected at kinetochores during prometaphase. Colocalizes with NEK2 at the kinetochore. Colocalizes with IK at spindle poles during metaphase and anaphase. {ECO:0000250|UniProtKB:Q9Y6D9}.
DR  UNIPROT: Q80YF0;
DR  Pfam: PF05557;
DE  Function: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (By similarity). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (By similarity). {ECO:0000250|UniProtKB:Q9Y6D9}.
DE  Reference Proteome: No;
GO  GO:0000776;
GO  GO:1990706;
GO  GO:0005815;
GO  GO:0072686;
GO  GO:1990728;
GO  GO:0097431;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0042802;
GO  GO:0043515;
GO  GO:0051301;
GO  GO:0007094;
GO  GO:0042130;
GO  GO:0090267;
GO  GO:0090235;
GO  GO:0048538;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDLGENTTVLSTLRSLNNFISQRVEGGSGLDVSTAAPGSLQLQYEQSMQLEERAEQIRSKSYLIQMEREKMQMELSHKR
SQ  ARVELERAANTSARNYEREVDRNQELLARIRQLQEREAAAEEKMQEQLERHRLCKQSLDAASQQLREREDGLAAARETIS
SQ  SLKGRVSEMQLNAMDQKVQVKRLESEKQELKEQLELQQRKCQEASQKIQELQASQEERADHEQKIKDLEQKLCLQEQDAA
SQ  VVKNMKSELLRLPRMERELKRLREENTHLREMKETNGLLTEELEGLQRKLGRQEKMQEALVDLELEKEKLLAKLQSWEKL
SQ  DQTMGVNLRTPEDLSRFVVELQQRELTLKEKNNTITSSARGLEKAQQQLQDEVRQVSAQLLEERKKREIHEALARRLQKR
SQ  IVLLTKERDGMRAILGSYDSELTQAEYSAQLTQRMWEAEDMVQKVHAHSSEMETQLSQALEELGVQKQRADTLEMELKML
SQ  RAQTSSAETSFPFCKEEVDALRLKVEELEGERSRLEQEKQALEMQMERLTLQGDYNQSRTKVLHMSLNPASMARKRQQED
SQ  HARLQGECERLRGLVHALERGGPIPADLEVASSLPSSKEVAELRKQVESAELKNQRLKEVFQTKIQEFRKVCYTLTGYQI
SQ  DVTTENQYRLTSRYAEHQSDCLIFKATGPSGSKMQLLETEFSRSVPELIELHLLQQDSIPAFLSALTIELFSRQTSI
//
ID  Q9Y6D9;
PN  Mitotic spindle assembly checkpoint protein MAD1;
GN  MAD1L1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:19010891, ECO:0000269|PubMed:9546394}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14978040, ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:22351768, ECO:0000269|PubMed:29162720}. Nucleus envelope {ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:22351768}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14978040, ECO:0000269|PubMed:9546394}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:9546394}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:22351768}. Note=Co- localizes with TPR at the nucleus envelope during interphase and throughout the cell cycle (PubMed:22351768, PubMed:18981471). From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody (PubMed:9546394). Localizes to kinetochores during prometaphase (PubMed:22351768, PubMed:29162720). Does not localize to kinetochores during metaphase (PubMed:29162720). Colocalizes with NEK2 at the kinetochore (PubMed:14978040). Colocalizes with IK at spindle poles during metaphase and anaphase (PubMed:22351768). {ECO:0000269|PubMed:14978040, ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:22351768, ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:9546394}. [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:19010891}.
DR  UNIPROT: Q9Y6D9;
DR  UNIPROT: B3KR41;
DR  UNIPROT: Q13312;
DR  UNIPROT: Q75MI0;
DR  UNIPROT: Q86UM4;
DR  UNIPROT: Q9UNH0;
DR  PDB: 1GO4;
DR  PDB: 4DZO;
DR  PDB: 7B1F;
DR  PDB: 7B1H;
DR  PDB: 7B1J;
DR  Pfam: PF05557;
DR  OMIM: 602686;
DR  DisGeNET: 8379;
DE  Function: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (PubMed:10049595, PubMed:20133940, PubMed:29162720). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (PubMed:29162720). {ECO:0000269|PubMed:10049595, ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:29162720}. [Isoform 3]: Sequesters MAD2L1 in the cytoplasm preventing its function as an activator of the mitotic spindle assembly checkpoint (SAC) resulting in SAC impairment and chromosomal instability in hepatocellular carcinomas. {ECO:0000269|PubMed:19010891}.
DE  Disease: Note=Defects in MAD1L1 are involved in the development and/or progression of various types of cancer. {ECO:0000269|PubMed:10597320, ECO:0000269|PubMed:11423979}.
DE  Reference Proteome: Yes;
DE  Interaction: P09917; IntAct: EBI-10196727; Score: 0.81
DE  Interaction: P0DTD1; IntAct: EBI-26950100; Score: 0.56
DE  Interaction: P12270; IntAct: EBI-9521828; Score: 0.52
DE  Interaction: Q8IYF3; IntAct: EBI-753268; Score: 0.37
DE  Interaction: Q9Y2I6; IntAct: EBI-753496; Score: 0.37
DE  Interaction: Q15233; IntAct: EBI-755521; Score: 0.37
DE  Interaction: Q96AQ9; IntAct: EBI-758800; Score: 0.37
DE  Interaction: Q14134; IntAct: EBI-759037; Score: 0.78
DE  Interaction: Q9Y2J4; IntAct: EBI-759142; Score: 0.37
DE  Interaction: Q9BVR6; IntAct: EBI-759859; Score: 0.37
DE  Interaction: Q9Y6D9; IntAct: EBI-760381; Score: 0.80
DE  Interaction: Q13257; IntAct: EBI-760453; Score: 0.98
DE  Interaction: P38432; IntAct: EBI-955758; Score: 0.00
DE  Interaction: O43264; IntAct: EBI-1001430; Score: 0.27
DE  Interaction: P11440; IntAct: EBI-2556914; Score: 0.40
DE  Interaction: Q9Z1B5; IntAct: EBI-2560653; Score: 0.56
DE  Interaction: Q9DCX1; IntAct: EBI-2561840; Score: 0.56
DE  Interaction: O46385; IntAct: EBI-8593648; Score: 0.37
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: P06753; IntAct: EBI-8654560; Score: 0.85
DE  Interaction: Q15013; IntAct: EBI-7033350; Score: 0.43
DE  Interaction: P12792; IntAct: EBI-6159029; Score: 0.35
DE  Interaction: Q9UL15; IntAct: EBI-9393211; Score: 0.78
DE  Interaction: Q12834; IntAct: EBI-9519208; Score: 0.35
DE  Interaction: P03410; IntAct: EBI-9676404; Score: 0.49
DE  Interaction: Q63HK5; IntAct: EBI-10171978; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-10175246; Score: 0.72
DE  Interaction: Q9NX65; IntAct: EBI-10178276; Score: 0.56
DE  Interaction: O76041; IntAct: EBI-10190530; Score: 0.78
DE  Interaction: O76064; IntAct: EBI-10190604; Score: 0.78
DE  Interaction: P09493; IntAct: EBI-10196495; Score: 0.72
DE  Interaction: P25786; IntAct: EBI-10202472; Score: 0.56
DE  Interaction: P55081; IntAct: EBI-10214921; Score: 0.72
DE  Interaction: Q3ZCW2; IntAct: EBI-10241431; Score: 0.72
DE  Interaction: Q5VU62; IntAct: EBI-10247900; Score: 0.56
DE  Interaction: Q8TD31; IntAct: EBI-10274974; Score: 0.72
DE  Interaction: Q96CS2; IntAct: EBI-10284116; Score: 0.56
DE  Interaction: Q99576; IntAct: EBI-10294433; Score: 0.56
DE  Interaction: Q9BW85; IntAct: EBI-10300402; Score: 0.56
DE  Interaction: Q9UM82; IntAct: EBI-10324123; Score: 0.56
DE  Interaction: Q9Y4E8; IntAct: EBI-10328242; Score: 0.56
DE  Interaction: Q9P0K8; IntAct: EBI-11318339; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-11013286; Score: 0.35
DE  Interaction: P28004; IntAct: EBI-11525117; Score: 0.56
DE  Interaction: P32502; IntAct: EBI-11526537; Score: 0.56
DE  Interaction: P32571; IntAct: EBI-11526714; Score: 0.56
DE  Interaction: P39976; IntAct: EBI-11530213; Score: 0.56
DE  Interaction: P53933; IntAct: EBI-11533942; Score: 0.56
DE  Interaction: Q03718; IntAct: EBI-11534959; Score: 0.56
DE  Interaction: O00267; IntAct: EBI-11773088; Score: 0.49
DE  Interaction: P08670; IntAct: EBI-11774675; Score: 0.37
DE  Interaction: P14373; IntAct: EBI-11774737; Score: 0.37
DE  Interaction: O00444; IntAct: EBI-11774817; Score: 0.37
DE  Interaction: Q96BZ8; IntAct: EBI-24277408; Score: 0.56
DE  Interaction: Q8TC71; IntAct: EBI-24300923; Score: 0.56
DE  Interaction: O43247; IntAct: EBI-24308960; Score: 0.56
DE  Interaction: Q5T7P8; IntAct: EBI-24327182; Score: 0.56
DE  Interaction: Q07002; IntAct: EBI-24343506; Score: 0.56
DE  Interaction: Q9HAQ2; IntAct: EBI-24353241; Score: 0.56
DE  Interaction: Q96HA8; IntAct: EBI-24355962; Score: 0.56
DE  Interaction: P25800; IntAct: EBI-25247186; Score: 0.56
DE  Interaction: Q86YD7; IntAct: EBI-25258142; Score: 0.56
DE  Interaction: Q9Y4C2; IntAct: EBI-24483937; Score: 0.56
DE  Interaction: Q9H1Y0; IntAct: EBI-24489241; Score: 0.56
DE  Interaction: Q8TAP4; IntAct: EBI-24400928; Score: 0.56
DE  Interaction: Q9BSW7; IntAct: EBI-24413469; Score: 0.56
DE  Interaction: Q4G0R1; IntAct: EBI-24418100; Score: 0.56
DE  Interaction: Q9Y6W3; IntAct: EBI-24422037; Score: 0.56
DE  Interaction: Q16543; IntAct: EBI-24427050; Score: 0.56
DE  Interaction: Q6NYC8; IntAct: EBI-24429971; Score: 0.56
DE  Interaction: O95995; IntAct: EBI-24443410; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-24443653; Score: 0.56
DE  Interaction: Q9BZW7; IntAct: EBI-24446405; Score: 0.56
DE  Interaction: Q92917; IntAct: EBI-24461096; Score: 0.56
DE  Interaction: Q2TAC2; IntAct: EBI-24464910; Score: 0.56
DE  Interaction: Q9Y240; IntAct: EBI-21531678; Score: 0.35
DE  Interaction: Q5SZD1; IntAct: EBI-21545147; Score: 0.35
DE  Interaction: Q9H672; IntAct: EBI-21618657; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-21714606; Score: 0.35
DE  Interaction: Q6NZI2; IntAct: EBI-21738912; Score: 0.35
DE  Interaction: P13497; IntAct: EBI-21764992; Score: 0.35
DE  Interaction: Q8N4Q0; IntAct: EBI-21847953; Score: 0.35
DE  Interaction: O43448; IntAct: EBI-21870954; Score: 0.35
DE  Interaction: Q02224; IntAct: EBI-16169210; Score: 0.59
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: Q96M98; IntAct: EBI-20917716; Score: 0.40
DE  Interaction: Q13077; IntAct: EBI-20934916; Score: 0.40
DE  Interaction: P51114; IntAct: EBI-26510739; Score: 0.37
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:1990706;
GO  GO:0072686;
GO  GO:1990728;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0000922;
GO  GO:0042802;
GO  GO:0043515;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0051220;
GO  GO:1902426;
GO  GO:0007094;
GO  GO:0042130;
GO  GO:0090267;
GO  GO:0090235;
GO  GO:0048538;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKR
SQ  ARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETIN
SQ  ALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAA
SQ  IVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERL
SQ  DQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKR
SQ  VLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKML
SQ  KSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLRED
SQ  HSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQ
SQ  IDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA
//
ID  Q9WTX8;
PN  Mitotic spindle assembly checkpoint protein MAD1;
GN  Mad1l1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y6D9}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9Y6D9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9Y6D9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9Y6D9}. Note=Detected at the nucleus envelope during interphase. From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody. Detected at kinetochores during prometaphase. Colocalizes with NEK2 at the kinetochore. Colocalizes with IK at spindle poles during metaphase and anaphase. {ECO:0000250|UniProtKB:Q9Y6D9}.
DR  UNIPROT: Q9WTX8;
DR  UNIPROT: Q9WTX9;
DR  Pfam: PF05557;
DE  Function: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (By similarity). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (By similarity). {ECO:0000250|UniProtKB:Q9Y6D9}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8CG73; IntAct: EBI-4284701; Score: 0.35
DE  Interaction: Q80Z64; IntAct: EBI-8820601; Score: 0.35
DE  Interaction: Q80YT7; IntAct: EBI-16732484; Score: 0.35
DE  Interaction: Q6P1J9; IntAct: EBI-20726660; Score: 0.35
GO  GO:0005737;
GO  GO:0000776;
GO  GO:1990706;
GO  GO:0005815;
GO  GO:0072686;
GO  GO:1990728;
GO  GO:0097431;
GO  GO:0005635;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0000922;
GO  GO:0042802;
GO  GO:0043515;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0051220;
GO  GO:1902426;
GO  GO:0007094;
GO  GO:0042130;
GO  GO:0090267;
GO  GO:0090235;
GO  GO:1901990;
GO  GO:0048538;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDLGENTTVLSSLRSLNNFISQRMEGTSGLDVSTSASGSLQKQYEYHMQLEERAEQIRSKSYLIQVEREKMQMELSHKR
SQ  ARVELERAASTNARNYEREVDRNQELLARIRQLQECEATAEEKMREQLERHRLCKQNLDAVSQQLREQEDSLASAREMIS
SQ  SLKGRVSELQLSAMDQKVQVKRLESEKQELKEQLELQQRKWQEANQKIQELQASQDERAEHEQKIKDLEQKLCLQEQDAA
SQ  VVKSMKSELMRMPRMERELKRLHEENTHLREMKETNGLLTEELEGLQRKLSRQEKMQEALVDLELEKEKLLAKLQSWENL
SQ  DQTMGLNLRTPEDLSRFVVELQQRELTLKEKNNSITSSARGLEKVQQQLQDEVRQANAQLLEERKKRETHEALARRLQKR
SQ  NALLTKERDGMRAILGSYDSELTQTEYSTQLTQRLWEAEDMVQKVHAHSSEMEAQLSQALEELGVQKQRADTLEMELKML
SQ  KAQTSSAESSFSFCKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQGDYNQSRTKVLHMSLNPISMARQRQHED
SQ  HDRLQEECERLRGLVHALERGGPIPADLEAASSLPSSKEVAELRKQVESAELKNQRLKEVFQTKIQEFRKVCYTLTGYQI
SQ  DVTTESQYRLTSRYAEHQTDCLIFKATGPSGSKMQLLETEFSRSVPELIELHLLQQDSIPAFLSALTIELFSRQTSI
//
ID  P87310;
PN  Mediator of RNA polymerase II transcription subunit 10;
GN  med10;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: P87310;
DR  PDB: 5N9J;
DR  Pfam: PF09748;
DE  Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
DE  Reference Proteome: Yes;
DE  Interaction: Q9P7Y4; IntAct: EBI-1533334; Score: 0.74
DE  Interaction: P87306; IntAct: EBI-1533334; Score: 0.74
DE  Interaction: O14198; IntAct: EBI-1533334; Score: 0.74
DE  Interaction: Q9Y7N2; IntAct: EBI-1533334; Score: 0.66
DE  Interaction: Q09696; IntAct: EBI-1533334; Score: 0.59
DE  Interaction: O94376; IntAct: EBI-1533334; Score: 0.66
DE  Interaction: O14010; IntAct: EBI-1533334; Score: 0.66
DE  Interaction: Q10477; IntAct: EBI-1533334; Score: 0.59
DE  Interaction: Q9Y821; IntAct: EBI-1533334; Score: 0.74
DE  Interaction: Q9US45; IntAct: EBI-1533334; Score: 0.74
DE  Interaction: O60104; IntAct: EBI-1533334; Score: 0.74
DE  Interaction: O94646; IntAct: EBI-1533334; Score: 0.66
DE  Interaction: Q09191; IntAct: EBI-1533334; Score: 0.59
DE  Interaction: Q92399; IntAct: EBI-1533334; Score: 0.40
DE  Interaction: P48011; IntAct: EBI-1533334; Score: 0.40
DE  Interaction: P87123; IntAct: EBI-1533334; Score: 0.40
DE  Interaction: P36594; IntAct: EBI-1533334; Score: 0.59
DE  Interaction: Q02061; IntAct: EBI-1533334; Score: 0.59
DE  Interaction: P37382; IntAct: EBI-1533334; Score: 0.59
DE  Interaction: O74825; IntAct: EBI-1533334; Score: 0.40
DE  Interaction: O14459; IntAct: EBI-1533334; Score: 0.59
DE  Interaction: P36595; IntAct: EBI-1533749; Score: 0.59
DE  Interaction: P68336; IntAct: EBI-1533613; Score: 0.35
DE  Interaction: Q9P6Q0; IntAct: EBI-26372760; Score: 0.52
DE  Interaction: Q10317; IntAct: EBI-26372760; Score: 0.52
DE  Interaction: Q9USH1; IntAct: EBI-26372760; Score: 0.52
DE  Interaction: O13964; IntAct: EBI-26372760; Score: 0.52
GO  GO:0000785;
GO  GO:0005829;
GO  GO:0016592;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0003713;
GO  GO:0003712;
GO  GO:0045944;
GO  GO:0060261;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLPQDDMTDEMKSLASRLEDTTQAFYDLALIVYNLEDTTPSDAIPESLDTLIRDLKSLPDISRKVNNLIPQDVLEYIEQG
SQ  RNPDVYARQFSELVQKDNQYVNGKLYAIEGFQKAFAEEIKQAYPEVSSVVDKILNEGKVESTVS
//
ID  O14770;
PN  Homeobox protein Meis2;
GN  MEIS2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P97367}.
DR  UNIPROT: O14770;
DR  UNIPROT: A6NJI5;
DR  UNIPROT: A8MWD5;
DR  UNIPROT: B3KP98;
DR  UNIPROT: B3KPQ6;
DR  UNIPROT: Q96DI2;
DR  UNIPROT: Q96KI4;
DR  UNIPROT: Q96KI5;
DR  UNIPROT: Q9NRS1;
DR  UNIPROT: Q9NRS2;
DR  UNIPROT: Q9NRS3;
DR  PDB: 3K2A;
DR  PDB: 4XRM;
DR  PDB: 5BNG;
DR  PDB: 5EG0;
DR  Pfam: PF05920;
DR  Pfam: PF16493;
DR  PROSITE: PS50071;
DR  OMIM: 600987;
DR  OMIM: 601740;
DR  DisGeNET: 4212;
DE  Function: Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3 is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3 and isoform 4 can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5 cannot activate DRD1 transcription. {ECO:0000269|PubMed:10764806, ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:21746878}.
DE  Disease: Cleft palate, cardiac defects, and intellectual disability (CPCMR) [MIM:600987]: An autosomal dominant disease characterized by multiple congenital malformations, mild-to-severe intellectual disability with poor speech, and delayed psychomotor development. Congenital malformations include heart defects, cleft lip/palate, distally-placed thumbs and toes, and cutaneous syndactyly between the second and third toes. {ECO:0000269|PubMed:24678003, ECO:0000269|PubMed:25712757, ECO:0000269|PubMed:27225850}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P40424; IntAct: EBI-8025844; Score: 0.68
DE  Interaction: Q5NG24; IntAct: EBI-2804943; Score: 0.00
DE  Interaction: P55347; IntAct: EBI-6390229; Score: 0.37
DE  Interaction: P31314; IntAct: EBI-6390224; Score: 0.51
DE  Interaction: P03363; IntAct: EBI-9676160; Score: 0.56
DE  Interaction: A0A1B0GWI1; IntAct: EBI-10181425; Score: 0.56
DE  Interaction: Q5TZZ9; IntAct: EBI-10181439; Score: 0.56
DE  Interaction: Q6P1W5; IntAct: EBI-10181449; Score: 0.56
DE  Interaction: Q9UJX0; IntAct: EBI-10322586; Score: 0.67
DE  Interaction: O14770; IntAct: EBI-10483276; Score: 0.37
DE  Interaction: Q9HBZ2; IntAct: EBI-21247219; Score: 0.37
DE  Interaction: X5DP20; IntAct: EBI-21248814; Score: 0.37
DE  Interaction: P08563; IntAct: EBI-11477846; Score: 0.40
DE  Interaction: Q93062; IntAct: EBI-11770334; Score: 0.49
DE  Interaction: Q9BYU1; IntAct: EBI-24325661; Score: 0.56
DE  Interaction: A8MTQ0; IntAct: EBI-25245194; Score: 0.56
DE  Interaction: P78424; IntAct: EBI-25257117; Score: 0.56
DE  Interaction: Q3LHN2; IntAct: EBI-24519607; Score: 0.56
DE  Interaction: Q8NCR6; IntAct: EBI-24521509; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-25265493; Score: 0.56
DE  Interaction: Q9NP55; IntAct: EBI-24617898; Score: 0.56
DE  Interaction: Q3LI66; IntAct: EBI-24620047; Score: 0.56
DE  Interaction: Q9BVN2; IntAct: EBI-24627135; Score: 0.56
DE  Interaction: O43482; IntAct: EBI-24629906; Score: 0.56
DE  Interaction: Q16568; IntAct: EBI-24671746; Score: 0.56
DE  Interaction: P17568; IntAct: EBI-24678228; Score: 0.56
DE  Interaction: Q99990; IntAct: EBI-24686169; Score: 0.56
DE  Interaction: Q96C01; IntAct: EBI-24689631; Score: 0.56
DE  Interaction: Q13207; IntAct: EBI-24726892; Score: 0.56
DE  Interaction: Q9BQD7; IntAct: EBI-24753048; Score: 0.56
DE  Interaction: P59942; IntAct: EBI-24764157; Score: 0.56
DE  Interaction: Q3LI64; IntAct: EBI-24764080; Score: 0.56
DE  Interaction: Q8IWZ5; IntAct: EBI-24787203; Score: 0.56
DE  Interaction: P78358; IntAct: EBI-24405116; Score: 0.56
DE  Interaction: Q9BVL2; IntAct: EBI-24450131; Score: 0.56
DE  Interaction: Q16633; IntAct: EBI-24562025; Score: 0.56
DE  Interaction: Q3LI70; IntAct: EBI-24577653; Score: 0.56
DE  Interaction: P18825; IntAct: EBI-24590919; Score: 0.56
DE  Interaction: Q8IUC1; IntAct: EBI-24591528; Score: 0.56
DE  Interaction: P09683; IntAct: EBI-24636392; Score: 0.56
DE  Interaction: P24592; IntAct: EBI-24646860; Score: 0.56
DE  Interaction: Q9Y5J6; IntAct: EBI-24654937; Score: 0.56
DE  Interaction: Q13882; IntAct: EBI-24774645; Score: 0.56
DE  Interaction: Q92567; IntAct: EBI-24803604; Score: 0.56
DE  Interaction: Q13352; IntAct: EBI-24806788; Score: 0.56
DE  Interaction: O60663; IntAct: EBI-21538601; Score: 0.35
DE  Interaction: Q9Y2B2; IntAct: EBI-21552063; Score: 0.35
DE  Interaction: P60709; IntAct: EBI-21552063; Score: 0.35
DE  Interaction: P40426; IntAct: EBI-21552063; Score: 0.35
DE  Interaction: P40425; IntAct: EBI-21552063; Score: 0.35
DE  Interaction: O00470; IntAct: EBI-21552063; Score: 0.35
DE  Interaction: A6NDR6; IntAct: EBI-21552063; Score: 0.35
DE  Interaction: Q8IYS4; IntAct: EBI-21565697; Score: 0.35
DE  Interaction: Q96HB5; IntAct: EBI-21618177; Score: 0.35
DE  Interaction: Q9Y586; IntAct: EBI-21671820; Score: 0.35
DE  Interaction: Q5U5X8; IntAct: EBI-21671625; Score: 0.35
DE  Interaction: Q13394; IntAct: EBI-21671570; Score: 0.35
DE  Interaction: Q9NYL9; IntAct: EBI-21701240; Score: 0.35
DE  Interaction: D3DTS7; IntAct: EBI-25882772; Score: 0.56
DE  Interaction: P48431; IntAct: EBI-26574619; Score: 0.35
DE  Interaction: Q14258; IntAct: EBI-26683485; Score: 0.37
DE  Interaction: Q15649; IntAct: EBI-26685693; Score: 0.37
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: P46937; IntAct: EBI-30845845; Score: 0.44
GO  GO:0000785;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0043565;
GO  GO:1990837;
GO  GO:0008134;
GO  GO:0009887;
GO  GO:0007420;
GO  GO:0009880;
GO  GO:0001654;
GO  GO:0045638;
GO  GO:0000122;
GO  GO:0031016;
GO  GO:0110024;
GO  GO:0008284;
GO  GO:0045931;
GO  GO:0045944;
GO  GO:0006357;
GO  GO:0070848;
GO  GO:0009612;
GO  GO:0008542;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQRYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNHGPPLHATQHYGAHAPHPNVMPASMGSAVNDALKRDKDAI
SQ  YGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELDNLMIQAIQVLRFHLLE
SQ  LEKVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPSSWRDHDDATSTHSAGTPGPSSGGH
SQ  ASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTI
SQ  LQVNNWFINARRRIVQPMIDQSNRAGFLLDPSVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGLQSMPGDYVSQGGPMGM
SQ  SMAQPSYTPPQMTPHPTQLRHGPPMHSYLPSHPHHPAMMMHGGPPTHPGMTMSAQSPTMLNSVDPNVGGQVMDIHAQ
//
ID  P97367;
PN  Homeobox protein Meis2;
GN  Meis2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:9710595}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21059917}.
DR  UNIPROT: P97367;
DR  UNIPROT: O35676;
DR  UNIPROT: O35677;
DR  UNIPROT: P97403;
DR  UNIPROT: P97404;
DR  Pfam: PF05920;
DR  Pfam: PF16493;
DR  PROSITE: PS50071;
DE  Function: Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform Meis2B is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoforms Meis2B and Meis2D can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription. {ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:11438208, ECO:0000269|PubMed:17178831}.
DE  Reference Proteome: Yes;
DE  Interaction: Q62424; IntAct: EBI-925672; Score: 0.00
DE  Interaction: Q04742; IntAct: EBI-26670288; Score: 0.37
DE  Interaction: P41778; IntAct: EBI-26671124; Score: 0.37
DE  Interaction: O35317; IntAct: EBI-26671436; Score: 0.37
DE  Interaction: O35984; IntAct: EBI-26671181; Score: 0.37
DE  Interaction: P15806; IntAct: EBI-26673340; Score: 0.37
DE  Interaction: Q99NE9; IntAct: EBI-26683990; Score: 0.37
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0043565;
GO  GO:1990837;
GO  GO:0008134;
GO  GO:0009887;
GO  GO:0007420;
GO  GO:0009880;
GO  GO:0001654;
GO  GO:0045638;
GO  GO:0031016;
GO  GO:0110024;
GO  GO:0008284;
GO  GO:0045931;
GO  GO:0045944;
GO  GO:0006357;
GO  GO:0070848;
GO  GO:0009612;
GO  GO:0008542;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQRYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNHGPPLHATQHYGAHAPHPNVMPASMGSAVNDALKRDKDAI
SQ  YGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELDNLMIQAIQVLRFHLLE
SQ  LEKVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPSSWRDHDDATSTHSAGTPGPSSGGH
SQ  ASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTI
SQ  LQVNNWFINARRRIVQPMIDQSNRAGFLLDPSVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGLQSMPGDYVSQGGPMGM
SQ  GMAQPSYTPPQMTPHPTQLRHGPPMHSYLPSHPHHPAMVMHGGPPTHPGMTMSAQSPTMLNSVDPNVGGQVMDIHAQ
//
ID  Q18508;
PN  Protein mel-28;
GN  mel;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:27341616}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27341616}. Nucleus envelope {ECO:0000269|PubMed:27341616}. Nucleus inner membrane {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:16950114}. Chromosome {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:27341616}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:27341616}. Note=Has a dynamic expression pattern during the cell cycle (PubMed:16950114, PubMed:27341616). During interphase, localizes to nuclear pore complexes and is also found in the nucleoplasm (PubMed:16950114, PubMed:27341616). During early mitosis, localizes to kinetochores in a hcp-3/CENP-A and hcp-4/CENP-C dependent manner (PubMed:16950114, PubMed:16950115, PubMed:27341616). At later stages of mitosis (anaphase), widely distributed on chromatin (PubMed:16950114, PubMed:27341616). During telophase, localizes again to the reforming nuclear envelope (PubMed:16950114, PubMed:27341616). {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:27341616}.
DR  UNIPROT: Q18508;
DE  Function: Nuclear envelope protein which has essential roles in assembly of nuclear pore complexes and in chromatin maintenance during the cell cycle (PubMed:16950114, PubMed:16950115, PubMed:26166571, PubMed:27341616). Appears to be a stable structural component of the nuclear envelope during interphase (PubMed:16950114, PubMed:16950115). In dividing cells, localizes to kinetochores during early stages of mitosis and then to chromatin during late mitosis (PubMed:16950114, PubMed:27341616). Important for several mitotic processes including chromosome condensation, kinetochore assembly, chromosome segregation and cell-cycle timing (PubMed:16950114, PubMed:16950115, PubMed:26166571, PubMed:27341616). In postmitotic cells, plays a role in the early steps of nuclear pore complex assembly by recruiting the nucleoporins npp-10 and npp-5 to chromatin (PubMed:16950114, PubMed:16950115). Also involved in meiotic chromosome segregation (PubMed:27341616). May function downstream of the Ran GTPase signaling pathway (PubMed:16950115). {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:26166571, ECO:0000269|PubMed:27341616}.
DE  Reference Proteome: Yes;
DE  Interaction: O02101; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q21443; IntAct: EBI-6459403; Score: 0.37
DE  Interaction: P91001; IntAct: EBI-6460881; Score: 0.37
DE  Interaction: G5EDS1; IntAct: EBI-6463292; Score: 0.37
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0003677;
GO  GO:0060090;
GO  GO:0051301;
GO  GO:0051321;
GO  GO:0000070;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDNENSSIFKSYQGYECWRGEKQIILKDSIGRQLPYIVNFKKNTCQIFDIEWERVTHSFVFPEGCALIDADYFPTEEGKL
SQ  GILVGVEDPRQSCGAEHFVLALAVDPDSPAMTITHSLEVPSKITVVKTLFSSADMADETQRTVLKLYHRLMTWQHIVAIG
SQ  CKETQCYLARLVAVETPSSPVITVHSEKKYLINLMNAYVSGSVLQYTLDDGAYREYPTAAVYISALSLMPRSRTLLVGLS
SQ  MGGILAASLNPSNQMMLLELRHERLVRKIAPLEPEDDPDKFEYFIATVDCSPRHPIMIQLWRGSFKTLEDVDGEEKYDRP
SQ  SFSVCLEHKILFGERWLAVNPIVTERDHMMLTRKRGTEDSMHNVSQTFGSTSNRNSVLLAYERKKMVIGTEDPNAEPEYI
SQ  VEAAIFDIDSWYYKRVPGRVSTDGTVLKQCAFLSTIKSNIRSEDVNDIGILTNEATDVSSFSSMVSDADQLFYPSALSFE
SQ  RVFVAKNTRIDWMKIQNIQDTILNKCAVKLPALIRNPEMISSVVMAAGLVRKNILSGSPNSSAAEINELQLSSDQKVLLN
SQ  VIVYYGKIEEFCQLASRPDISDTLKRELAEWALHEAVDYKRTISDKMVSLFQGRSLALSPLAEESIAQGIKLFRVVYEYL
SQ  KACSKALKDDRLRNLAHSVICMRNHTKLTSQFINFAIIPVDPIRQQRMKDLHSKRKNMARKNSSSLPVQSVVRKMNRQAP
SQ  NAQFWNDIPHDEWYPPTPLDLLECLLNVSISESIKRELVVQYVIDWISTSPEDSEHSEKQLALETIKIMTNQMLNVNLEK
SQ  IYYILDQGKKALTSSKTSDDMRALGEKVFSMKDDEISYEKLWGKDAPMTVTIGKHDLQRFEQRMKMQMEGGKVRLPVLDP
SQ  ESEILYQMFLFENEKFEAMSSEAISSNKLLSAFLPGMIKKDGRGRQKTAKEQEIEISVKKMFERKVQNDDEDMPEVFASV
SQ  NDKTERKRKSSQFGEDDESSVSSSQYVPPTAKRIQQWKSAVESVANNSSINSITSPDSHQNAEINMMIATPARYYKRHNE
SQ  EENVQDGFLSPAGNRPPPVSAHNSILKTAKGGQSASRGRIRFRADVPRGADESIEDNGRKGLALNFAILEDEEEETMTIR
SQ  KSRSMGKHDEEKDSEKNVVDEMEEVKDQEQENDECIESEKTFENQDDFEVLEDTSAPEAANTENGSETPPMEDTFEVRDD
SQ  DVMPPTDETYLSHLQTDKTGILEEEGEDEDIWDGVQRSFEVQMDEDCEAVPTIDVADDLESKSEEVNEEEVVESEEVQQD
SQ  AKEPEKTEKRQEEPEPEVMQPVIPEEPQNESLESSIKLQEELQEEPDIVPTGDEDTADKVQEQAVEEDRPPSRNTRSSSV
SQ  QKSTSQVEDRDPKELVEEERPPSRNTRSASVQKSSNQEKTSESGEVTEEDRPPSRNTRSASVQKSSSKVKDQKPEELIEE
SQ  DRPPSRNTRSASAQKTVAANKSVLESEIPSRSASRRTRSTSLRNDTVAEPDETSVAMTTRRRTRATSEVVSKQSSEDDGR
SQ  STPKTGRTPTKKAAASTSSSRAGSVTRGKKSIIQKMPSPLEVTMEVQEEEEEEAEEERPASRSTRSASVKNTTVDPSSSA
SQ  LASTKRTTSRKRGNSETIDFNQDDKSAPTTPKRGRPAKKDAGSPKVGSKARGTKPKSIFENQEDEEDRSSSPDIEQPATP
SQ  TRSSKRTARSRANSESIDDDSKQKTPKKKNAAVNEAGTSKQSRSVTRSRASSIDVQQEVEEPTTPKRGRGRPPKTVLENI
SQ  EEGEEERKETAATPLLRSARRAKQ
//
ID  P35240;
PN  Merlin;
GN  NF2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Cell projection, filopodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=In a fibroblastic cell line, isoform 1 is found homogeneously distributed over the entire cell, with a particularly strong staining in ruffling membranes and filopodia. Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with DCAF1 in the nucleus. The intramolecular association of the FERM domain with the C- terminal tail promotes nuclear accumulation. The unphosphorylated form accumulates predominantly in the nucleus while the phosphorylated form is largely confined to the non-nuclear fractions. [Isoform 7]: Cytoplasm, perinuclear region. Cytoplasmic granule. Note=Observed in cytoplasmic granules concentrated in a perinuclear location. Isoform 7 is absent from ruffling membranes and filopodia. [Isoform 9]: Cytoplasm, perinuclear region. Cytoplasmic granule. Note=Observed in cytoplasmic granules concentrated in a perinuclear location. Isoform 9 is absent from ruffling membranes and filopodia. [Isoform 10]: Nucleus. Cell projection, filopodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, perinuclear region. Cytoplasmic granule. Cytoplasm, cytoskeleton. Note=In a fibroblastic cell line, isoform 10 is found homogeneously distributed over the entire cell, with a particularly strong staining in ruffling membranes and filopodia.
DR  UNIPROT: P35240;
DR  UNIPROT: O95683;
DR  UNIPROT: Q8WUJ2;
DR  UNIPROT: Q969N0;
DR  UNIPROT: Q969Q3;
DR  UNIPROT: Q96T30;
DR  UNIPROT: Q96T31;
DR  UNIPROT: Q96T32;
DR  UNIPROT: Q96T33;
DR  UNIPROT: Q9BTW3;
DR  UNIPROT: Q9UNG9;
DR  UNIPROT: Q9UNH3;
DR  UNIPROT: Q9UNH4;
DR  PDB: 1H4R;
DR  PDB: 3U8Z;
DR  PDB: 4ZRI;
DR  PDB: 4ZRJ;
DR  PDB: 6CDS;
DR  PDB: 7LWH;
DR  Pfam: PF09380;
DR  Pfam: PF00373;
DR  Pfam: PF09379;
DR  PROSITE: PS00660;
DR  PROSITE: PS00661;
DR  PROSITE: PS50057;
DR  OMIM: 101000;
DR  OMIM: 156240;
DR  OMIM: 162091;
DR  OMIM: 607379;
DR  DisGeNET: 4771;
DE  Function: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:20178741, ECO:0000269|PubMed:21167305}.
DE  Disease: Neurofibromatosis 2 (NF2) [MIM:101000]: Genetic disorder characterized by bilateral vestibular schwannomas (formerly called acoustic neuromas), schwannomas of other cranial and peripheral nerves, meningiomas, and ependymomas. It is inherited in an autosomal dominant fashion with full penetrance. Affected individuals generally develop symptoms of eighth-nerve dysfunction in early adulthood, including deafness and balance disorder. Although the tumors of NF2 are histologically benign, their anatomic location makes management difficult, and patients suffer great morbidity and mortality. {ECO:0000269|PubMed:10090912, ECO:0000269|PubMed:10669747, ECO:0000269|PubMed:10790209, ECO:0000269|PubMed:12709270, ECO:0000269|PubMed:20178741, ECO:0000269|PubMed:20445339, ECO:0000269|PubMed:7666400, ECO:0000269|PubMed:7759081, ECO:0000269|PubMed:7913580, ECO:0000269|PubMed:8081368, ECO:0000269|PubMed:8230593, ECO:0000269|PubMed:8566958, ECO:0000269|PubMed:8698340, ECO:0000269|PubMed:9643284}. Note=The disease is caused by variants affecting the gene represented in this entry. Schwannomatosis 1 (SWNTS1) [MIM:162091]: A cancer syndrome in which patients develop multiple non-vestibular schwannomas, benign neoplasms that arise from Schwann cells of the cranial, peripheral, and autonomic nerves. {ECO:0000269|PubMed:18072270}. Note=The disease is caused by variants affecting the gene represented in this entry. Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle-shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos. {ECO:0000269|PubMed:12136076}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P31689; IntAct: EBI-6911783; Score: 0.35
DE  Interaction: Q10728; IntAct: EBI-1014791; Score: 0.52
DE  Interaction: Q9H204; IntAct: EBI-1206136; Score: 0.58
DE  Interaction: O14745; IntAct: EBI-2527605; Score: 0.54
DE  Interaction: Q9BZE4; IntAct: EBI-1388499; Score: 0.61
DE  Interaction: P0DPB4; IntAct: EBI-1397471; Score: 0.51
DE  Interaction: P0DPB3; IntAct: EBI-1397568; Score: 0.40
DE  Interaction: Q4VCS5; IntAct: EBI-2513986; Score: 0.85
DE  Interaction: Q68EM7; IntAct: EBI-3892049; Score: 0.35
DE  Interaction: Q8NI35; IntAct: EBI-3957523; Score: 0.50
DE  Interaction: Q8N3R9; IntAct: EBI-3957573; Score: 0.35
DE  Interaction: Q13153; IntAct: EBI-3957588; Score: 0.40
DE  Interaction: A0A0G2JX94; IntAct: EBI-3892269; Score: 0.40
DE  Interaction: Q8IY63; IntAct: EBI-3957317; Score: 0.64
DE  Interaction: Q9Y2J4; IntAct: EBI-24403805; Score: 0.56
DE  Interaction: Q16584; IntAct: EBI-3990627; Score: 0.65
DE  Interaction: Q14324; IntAct: EBI-5661239; Score: 0.00
DE  Interaction: O60341; IntAct: EBI-8476950; Score: 0.67
DE  Interaction: O60884; IntAct: EBI-6911783; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-6911783; Score: 0.35
DE  Interaction: P34932; IntAct: EBI-6911783; Score: 0.35
DE  Interaction: Q92598; IntAct: EBI-6911783; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-6911783; Score: 0.35
DE  Interaction: P46937; IntAct: EBI-6912563; Score: 0.53
DE  Interaction: O95835; IntAct: EBI-9005158; Score: 0.56
DE  Interaction: P35240; IntAct: EBI-22185197; Score: 0.55
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: O08917; IntAct: EBI-11025136; Score: 0.35
DE  Interaction: Q3UES3; IntAct: EBI-11025889; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: O88952; IntAct: EBI-11079007; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-11095050; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135399; Score: 0.35
DE  Interaction: P46938; IntAct: EBI-11138299; Score: 0.35
DE  Interaction: Q13895; IntAct: EBI-24689238; Score: 0.56
DE  Interaction: Q8N3L3; IntAct: EBI-24702144; Score: 0.56
DE  Interaction: A2BDD9; IntAct: EBI-24715409; Score: 0.56
DE  Interaction: P50402; IntAct: EBI-23824818; Score: 0.56
DE  Interaction: Q96A37; IntAct: EBI-21627270; Score: 0.35
DE  Interaction: Q96S94; IntAct: EBI-21750627; Score: 0.35
DE  Interaction: Q13371; IntAct: EBI-21883365; Score: 0.35
DE  Interaction: Q9UJ04; IntAct: EBI-21883365; Score: 0.35
DE  Interaction: Q13136; IntAct: EBI-21883365; Score: 0.35
DE  Interaction: Q9Y4B6; IntAct: EBI-21912146; Score: 0.35
DE  Interaction: P48668; IntAct: EBI-21912146; Score: 0.35
DE  Interaction: P31431; IntAct: EBI-21912146; Score: 0.35
DE  Interaction: Q9Y2T2; IntAct: EBI-21912201; Score: 0.35
DE  Interaction: Q9UQ35; IntAct: EBI-21912201; Score: 0.35
DE  Interaction: Q9BW61; IntAct: EBI-21912201; Score: 0.35
DE  Interaction: P78347; IntAct: EBI-21912201; Score: 0.35
DE  Interaction: P18827; IntAct: EBI-21912201; Score: 0.35
DE  Interaction: O95218; IntAct: EBI-21912201; Score: 0.35
DE  Interaction: O14646; IntAct: EBI-21912201; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-21912201; Score: 0.35
DE  Interaction: O00468; IntAct: EBI-21912201; Score: 0.35
DE  Interaction: P20719; IntAct: EBI-21912280; Score: 0.35
DE  Interaction: Q9NP74; IntAct: EBI-21912280; Score: 0.35
DE  Interaction: Q9H307; IntAct: EBI-21912280; Score: 0.35
DE  Interaction: Q96HR8; IntAct: EBI-21912280; Score: 0.35
DE  Interaction: Q8TBK6; IntAct: EBI-21912280; Score: 0.35
DE  Interaction: Q3YEC7; IntAct: EBI-21912280; Score: 0.35
DE  Interaction: P98160; IntAct: EBI-21912280; Score: 0.35
DE  Interaction: O00422; IntAct: EBI-21912280; Score: 0.35
DE  Interaction: Q9HCG8; IntAct: EBI-21912397; Score: 0.35
DE  Interaction: Q3L8U1; IntAct: EBI-21912397; Score: 0.35
DE  Interaction: A0A8C0SSK1; IntAct: EBI-16145904; Score: 0.50
DE  Interaction: A0A8I3RSA7; IntAct: EBI-16145960; Score: 0.50
DE  Interaction: Q08345; IntAct: EBI-22227061; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-16795491; Score: 0.27
DE  Interaction: P46663; IntAct: EBI-20803223; Score: 0.37
DE  Interaction: O14964; IntAct: EBI-22184874; Score: 0.63
DE  Interaction: Q9Y6K9; IntAct: EBI-20737021; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: Q8NFZ5; IntAct: EBI-20737410; Score: 0.35
DE  Interaction: P52272; IntAct: EBI-20927432; Score: 0.40
DE  Interaction: Q99613; IntAct: EBI-22185149; Score: 0.37
DE  Interaction: Q01082; IntAct: EBI-25396800; Score: 0.65
DE  Interaction: Q92918; IntAct: EBI-25393102; Score: 0.35
DE  Interaction: P62750; IntAct: EBI-25481947; Score: 0.35
DE  Interaction: Q9H7H0; IntAct: EBI-25481947; Score: 0.35
DE  Interaction: Q969Q0; IntAct: EBI-25481947; Score: 0.35
DE  Interaction: P60896; IntAct: EBI-25878246; Score: 0.56
DE  Interaction: Q15776; IntAct: EBI-25878230; Score: 0.56
DE  Interaction: P17024; IntAct: EBI-25878222; Score: 0.56
DE  Interaction: P40337; IntAct: EBI-25878214; Score: 0.56
DE  Interaction: Q99598; IntAct: EBI-25878206; Score: 0.56
DE  Interaction: P54274; IntAct: EBI-25878198; Score: 0.56
DE  Interaction: O15381; IntAct: EBI-25878188; Score: 0.56
DE  Interaction: O75530; IntAct: EBI-25878294; Score: 0.56
DE  Interaction: O00303; IntAct: EBI-25878286; Score: 0.56
DE  Interaction: O75925; IntAct: EBI-25878278; Score: 0.56
DE  Interaction: Q9UNS2; IntAct: EBI-25878254; Score: 0.56
DE  Interaction: Q14525; IntAct: EBI-25878172; Score: 0.56
DE  Interaction: P48730; IntAct: EBI-25878153; Score: 0.56
DE  Interaction: Q13191; IntAct: EBI-25878145; Score: 0.56
DE  Interaction: Q5H9J7; IntAct: EBI-25878632; Score: 0.56
DE  Interaction: P58304; IntAct: EBI-25878624; Score: 0.56
DE  Interaction: Q6ZR37; IntAct: EBI-25878616; Score: 0.56
DE  Interaction: Q6ZNE9; IntAct: EBI-25878606; Score: 0.56
DE  Interaction: Q8IZU1; IntAct: EBI-25878598; Score: 0.56
DE  Interaction: Q6ZNH5; IntAct: EBI-25878582; Score: 0.56
DE  Interaction: Q86WT6; IntAct: EBI-25878574; Score: 0.56
DE  Interaction: Q96DX5; IntAct: EBI-25878566; Score: 0.56
DE  Interaction: Q96D59; IntAct: EBI-25878550; Score: 0.56
DE  Interaction: Q8NEZ2; IntAct: EBI-25878542; Score: 0.56
DE  Interaction: Q7Z3I7; IntAct: EBI-25878526; Score: 0.56
DE  Interaction: Q8WWB5; IntAct: EBI-25878518; Score: 0.56
DE  Interaction: Q8N594; IntAct: EBI-25878510; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-25878502; Score: 0.56
DE  Interaction: Q8NHS9; IntAct: EBI-25878494; Score: 0.56
DE  Interaction: Q6H8Q1; IntAct: EBI-25878486; Score: 0.56
DE  Interaction: Q9C0F3; IntAct: EBI-25878462; Score: 0.56
DE  Interaction: Q96KP6; IntAct: EBI-25878446; Score: 0.56
DE  Interaction: Q5VYS8; IntAct: EBI-25878438; Score: 0.56
DE  Interaction: Q6GQQ9; IntAct: EBI-25878428; Score: 0.56
DE  Interaction: Q96FW1; IntAct: EBI-25878420; Score: 0.56
DE  Interaction: Q8WVD3; IntAct: EBI-25878412; Score: 0.56
DE  Interaction: Q8WXF7; IntAct: EBI-25878396; Score: 0.56
DE  Interaction: Q5TAQ9; IntAct: EBI-25878388; Score: 0.56
DE  Interaction: Q9BY12; IntAct: EBI-25878378; Score: 0.56
DE  Interaction: Q6X4W1; IntAct: EBI-25878370; Score: 0.56
DE  Interaction: Q8N488; IntAct: EBI-25878352; Score: 0.56
DE  Interaction: Q13573; IntAct: EBI-25878334; Score: 0.56
DE  Interaction: Q9Y6C2; IntAct: EBI-25878318; Score: 0.56
DE  Interaction: O76041; IntAct: EBI-25878310; Score: 0.56
DE  Interaction: Q9UNE7; IntAct: EBI-25878302; Score: 0.56
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P63252; IntAct: EBI-28956270; Score: 0.27
DE  Interaction: O15194; IntAct: EBI-27115784; Score: 0.27
DE  Interaction: P18433; IntAct: EBI-27116377; Score: 0.27
DE  Interaction: P23470; IntAct: EBI-27116482; Score: 0.27
DE  Interaction: P29323; IntAct: EBI-32721290; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
GO  GO:0005912;
GO  GO:0045177;
GO  GO:0044297;
GO  GO:0032154;
GO  GO:0030864;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0031527;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0003779;
GO  GO:0005178;
GO  GO:0030036;
GO  GO:0045216;
GO  GO:0007398;
GO  GO:0021766;
GO  GO:0070306;
GO  GO:0000165;
GO  GO:0001707;
GO  GO:0030336;
GO  GO:0008285;
GO  GO:0022408;
GO  GO:0001953;
GO  GO:0043409;
GO  GO:0033689;
GO  GO:0006469;
GO  GO:0046426;
GO  GO:0010626;
GO  GO:0042532;
GO  GO:0042475;
GO  GO:0033687;
GO  GO:0045597;
GO  GO:0051496;
GO  GO:0042981;
GO  GO:0051726;
GO  GO:0014013;
GO  GO:0035330;
GO  GO:2000177;
GO  GO:1900180;
GO  GO:0031647;
GO  GO:0072091;
GO  GO:0014010;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKK
SQ  VLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKR
SQ  GFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALG
SQ  LHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQ
SQ  MKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQ
SQ  KAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPT
SQ  YPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDI
SQ  LHNENSDRGGSSKHNTIKKLTLQSAKSRVAFFEEL
//
ID  O94756;
PN  Meiotic expression up-regulated protein 14;
GN  meu14;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:12759375}. Nucleus membrane {ECO:0000269|PubMed:12759375}; Peripheral membrane protein {ECO:0000269|PubMed:12759375}; Cytoplasmic side {ECO:0000269|PubMed:12759375}. Prospore membrane {ECO:0000269|PubMed:12759375}.
DR  UNIPROT: O94756;
DR  Pfam: PF13805;
DE  Function: Has a role in nuclear division during meiosis II where it stabilizes the proper segregation of the spindle pole bodies. Also has a role in the formation and extension of the forespore membrane. {ECO:0000269|PubMed:12759375}.
DE  Reference Proteome: Yes;
GO  GO:0036286;
GO  GO:0035974;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0070056;
GO  GO:0070057;
GO  GO:0008289;
GO  GO:0031322;
GO  GO:0070941;
GO  GO:0006897;
GO  GO:0140043;
GO  GO:0006469;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:12759375};
SQ  MPKSSNLKMQRKGSLRENGLVKGLNKNKFSISKLKELSHADDSRKSHRIIRSGKSSGEAYKQAGKGLMNLGNHLSDWGAK
SQ  SSNLSLNDISDKIGVLVSELGETEIEFVKAFNENRIKFKAIRAMEDSIAPSRAHRQRLISSIEREEERDPLSPKLTDLQN
SQ  QLVRTEAENLVGEMQLDNTSREVFKSSFQGLMDAFQLRAQKQMTLSYYASQLAELINDEVAYPGDNPAAYSQKYATQIMH
SQ  QCVESMARLLAPVTSETTEHVGSDCEFTRKSSSSVEFSDHSQDSGDPSQQNILQVKNVQAVLSIPEAESYKAQLLSSIAE
SQ  EQKKKELQAKSTVFL
//
ID  Q0P5M9;
PN  Major facilitator superfamily domain-containing protein 10;
GN  MFSD10;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D2V8}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q0P5M9;
DR  Pfam: PF07690;
DR  PROSITE: PS50850;
DE  Function: Confers cellular resistance to apoptosis induced by the non- steroidal anti-inflammatory drugs indomethacin and diclofenac. May act as an efflux pump (By similarity). {ECO:0000250|UniProtKB:Q14728}.
DE  Reference Proteome: Yes;
GO  GO:0031526;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0022857;
GO  GO:0006915;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGCGAGGSCTPRPPIRQQQAPETRVVAVVFLGLLLDLLAFTLLLPLLPGLLESHGRAHDPLYGSWQRGVDWFAAAIGMPA
SQ  EKRYNSVLFGGLIGSVFSLLQFLSAPLTGALSDCLGRRPGMLLSLAGVATSYAVWAASKSFAAFLASRVIGGISKGNVSL
SQ  CTAIVADLGSPSARSKGMAVIGVAFSLGFTLGPTLGAFLPSETVPWLALLFAVSDLLFIWCFLPETLPPEKRAPSVTLGF
SQ  RAAADLLSPLALLRFSAVARGPDPPTGVRLGSLRGLGLVYFLYLFLFSGLEFTLSFLVHQRFRFSRVEQGKMFFFIGLTM
SQ  ATIQGAYARRIRPGREIAAVKQAILLLIPASLFVGWGHTLPILGLGLLLYSWAAAVVVPCLSSVVAGYGSPGQKGTVMGT
SQ  LRSLGALARAVGPVVAASAYWLAGARVCYTVCAALFLLPFSILRTLSPPARTLKAE
//
ID  Q14728;
PN  Major facilitator superfamily domain-containing protein 10;
GN  MFSD10;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D2V8}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q14728;
DR  UNIPROT: Q07706;
DR  PDB: 6S4M;
DR  Pfam: PF07690;
DR  PROSITE: PS50850;
DR  OMIM: 610977;
DE  Function: Confers cellular resistance to apoptosis induced by the non- steroidal anti-inflammatory drugs indomethacin and diclofenac. May act as an efflux pump. {ECO:0000269|PubMed:17362938}.
DE  Reference Proteome: Yes;
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: H9XIJ5; IntAct: EBI-11514331; Score: 0.37
DE  Interaction: O94886; IntAct: EBI-21566099; Score: 0.35
DE  Interaction: P55085; IntAct: EBI-20806731; Score: 0.37
DE  Interaction: Q6W5P4; IntAct: EBI-20810842; Score: 0.37
DE  Interaction: P19739; IntAct: EBI-25685423; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
DE  Interaction: P16284; IntAct: EBI-25881341; Score: 0.56
DE  Interaction: Q92876; IntAct: EBI-25887528; Score: 0.56
DE  Interaction: P37173; IntAct: EBI-25892796; Score: 0.56
DE  Interaction: P45973; IntAct: EBI-25917360; Score: 0.56
GO  GO:0031526;
GO  GO:0030659;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0008514;
GO  GO:0008493;
GO  GO:0006915;
GO  GO:0043252;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGWGGGGGCTPRPPIHQQPPERRVVTVVFLGLLLDLLAFTLLLPLLPGLLESHGRAHDPLYGSWQGGVDWFATAIGMPVE
SQ  KRYNSVLFGGLIGSAFSVLQFLCAPLTGATSDCLGRRPVMLLCLMGVATSYAVWATSRSFAAFLASRLIGGISKGNVSLS
SQ  TAIVADLGSPLARSQGMAVIGVAFSLGFTLGPMLGASLPLEMAPWFALLFAASDLLFIFCFLPETLPLEKRAPSIALGFR
SQ  DAADLLSPLALLRFSAVARGQDPPSGDRLSSLRRLGLVYFLYLFLFSGLEYTLSFLTHQRFQFSSLQQGKMFFLIGLTMA
SQ  TIQGAYARRIHPGGEVAAVKRALLLLVPAFLLIGWGRSLPVLGLGLLLYSFAAAVVVPCLSSVVAGYGSPGQKGTVMGTL
SQ  RSLGALARAAGPLVAASVYWLAGAQACFTTWSGLFLLPFFLLQKLSYPAQTLKAE
//
ID  Q9D2V8;
PN  Major facilitator superfamily domain-containing protein 10;
GN  Mfsd10;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:31142202}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9D2V8;
DR  UNIPROT: Q3U800;
DR  UNIPROT: Q3UN73;
DR  UNIPROT: Q9D1A7;
DR  Pfam: PF07690;
DR  PROSITE: PS50850;
DE  Function: Confers cellular resistance to apoptosis induced by the non- steroidal anti-inflammatory drugs indomethacin and diclofenac. May act as an efflux pump (By similarity). {ECO:0000250|UniProtKB:Q14728}.
DE  Reference Proteome: Yes;
GO  GO:0031526;
GO  GO:0030659;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0008514;
GO  GO:0006915;
GO  GO:0043252;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGWAGDAGCTPRPPIRPRPASERRVIIVLFLGLLLDLLAFTLLLPLLPGLLERHGREQDPLYGSWQRGVDWFASAIGMPA
SQ  EKRYNSVLFGGLIGSAFSLLQFFSAPLTGAASDYLGRRPVMMLSLTGLAISYAVWATSRSFKAFLASRVIGGISKGNVNL
SQ  STAIVADLGSPPTRSQGMAVIGVAFSLAFTLGPMLGAFLSVEMVPWISLLFAISDMLFIFCFLPETLPQEKRASSVTLGF
SQ  HTAAHLLSPLALLRFAAVTHSQDPPAEHRLRNLRRLGLVYFLYLFLFSGLEYTLSFLAHQRFQFSSLQQGKMFFFIGLTM
SQ  ATIQGTYARRISPGKEAAAVTRAMLLLVPAFLLIGWAHSLPTLGLGLMLYSFAAAVVVPGLSTMVSSYGSPGQKGTIMGI
SQ  LRSLGALGRALGPVVAASVYWLTGAQVCFTVCSALFLLPFLLLWKLKHPAETSKEE
//
ID  Q11068;
PN  Putative alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
GN  gly;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:P26572}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P26572}.
DR  UNIPROT: Q11068;
DR  UNIPROT: O76776;
DR  Pfam: PF03071;
DE  Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0005797;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0003827;
GO  GO:0046872;
GO  GO:0006486;
GO  GO:0006487;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MHAVTKIFIIFIFVFILWTLYVENDITNRTRNTDNIDDLLESANRLERLLKFEAKKIAALAEDVHKIRANRKGKHVIMEE
SQ  MVSQDLKQWKDPIPVLVFSCNRAMAVRDHVEKLIRYRPSQEKFPIIVTQDCDNENVKNEVKKFGDKVEYIKHLAGDKANI
SQ  TIPPSHRQYTAYYRIARHYKLALNHVFVDKGYSSVIITEDDLDISPDFFSYFSSTRYLLENDEKLWCVTAWNDNGKQENI
SQ  DMTAASTLYRSDFFAGLGWMMSSKTWHELEPIWPVGFWDDWMRDPARRKDRQCIRPEISRTGMMSYGKEGASKGQFFSKH
SQ  LAKIKVNDKYINFGKIDLDYLLPANFAKKTNLEVMKEAVELSIDNVASFVLSSENKGKSVRVMYDGNIDYIRKADKLHIM
SQ  HDFKAGVPRTAYDGIVTCFINGIRIYLVPDRTKVSAYNPDWSVPPSFGE
//
ID  P26572;
PN  Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
GN  MGAT1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:30983867}. Note=Co-localizes with BRI3 isoform 1 at the perinuclear region. {ECO:0000269|PubMed:30983867}.
DR  UNIPROT: P26572;
DR  UNIPROT: A8K404;
DR  UNIPROT: B3KRU8;
DR  UNIPROT: D3DWR1;
DR  UNIPROT: Q6IBE3;
DR  Pfam: PF03071;
DR  OMIM: 160995;
DR  DisGeNET: 4245;
DE  Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans. {ECO:0000269|PubMed:1702225}.
DE  Reference Proteome: Yes;
DE  Interaction: O95415; IntAct: EBI-25504004; Score: 0.54
DE  Interaction: O15198; IntAct: EBI-7263379; Score: 0.37
DE  Interaction: Q16659; IntAct: EBI-7211987; Score: 0.37
DE  Interaction: P08563; IntAct: EBI-11478323; Score: 0.40
DE  Interaction: Q9Z1B5; IntAct: EBI-10996176; Score: 0.35
DE  Interaction: Q8R034; IntAct: EBI-11003686; Score: 0.35
DE  Interaction: Q91ZJ0; IntAct: EBI-11131714; Score: 0.35
DE  Interaction: Q8IUW5; IntAct: EBI-21555862; Score: 0.35
DE  Interaction: Q9BRR6; IntAct: EBI-21694151; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-21777303; Score: 0.35
DE  Interaction: Q9BYC5; IntAct: EBI-21833842; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21302175; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-26495719; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
GO  GO:0033116;
GO  GO:0070062;
GO  GO:1903561;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0008375;
GO  GO:0003827;
GO  GO:0030145;
GO  GO:0001701;
GO  GO:0006486;
GO  GO:0006487;
GO  GO:0018279;
GO  GO:0006049;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLKKQSAGLVLWGAILFVAWNALLLLFFWTRPAPGRPPSVSALDGDPASLTREVIRLAQDAEVELERQRGLLQQIGDALS
SQ  SQRGRVPTAAPPAQPRVPVTPAPAVIPILVIACDRSTVRRCLDKLLHYRPSAELFPIIVSQDCGHEETAQAIASYGSAVT
SQ  HIRQPDLSSIAVPPDHRKFQGYYKIARHYRWALGQVFRQFRFPAAVVVEDDLEVAPDFFEYFRATYPLLKADPSLWCVSA
SQ  WNDNGKEQMVDASRPELLYRTDFFPGLGWLLLAELWAELEPKWPKAFWDDWMRRPEQRQGRACIRPEISRTMTFGRKGVS
SQ  HGQFFDQHLKFIKLNQQFVHFTQLDLSYLQREAYDRDFLARVYGAPQLQVEKVRTNDRKELGEVRVQYTGRDSFKAFAKA
SQ  LGVMDDLKSGVPRAGYRGIVTFQFRGRRVHLAPPLTWEGYDPSWN
//
ID  P27808;
PN  Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
GN  Mgat1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:P26572}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P26572}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P26572}. Note=Co-localizes with BRI3 at the perinuclear region. {ECO:0000250|UniProtKB:P26572}.
DR  UNIPROT: P27808;
DR  Pfam: PF03071;
DE  Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans. {ECO:0000269|PubMed:1421759}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0008375;
GO  GO:0003827;
GO  GO:0030145;
GO  GO:0001701;
GO  GO:0006486;
GO  GO:0006487;
GO  GO:0018279;
GO  GO:0006049;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLKKQTAGLVLWGAIIFVGWNALLLLFFWTRPAPGRLPSDSALGDDPASLTREVIHLAEDAEAELERQRGLLQQIKEHYA
SQ  LWRQRWRVPTVAPPAWPRVPVTPSPVQIPILVIACDRSTVRRCLDKLLHYRPSAERFPIIVSQDCGHEETAQVIASYGTA
SQ  VTHIRQPDLSNIAVQPDHRKFQGYYKIARHYRWALGQIFNKFKFPAAVVVEDDLEVAPDFFEYFQATYPLLRTDPSLWCV
SQ  SAWNDNGKEQMVDSSKPELLYRTDFFPGLGWLLLADLWAELEPKWPKAFWDDWMRRPEQRKGRACIRPEISRTMTFGRKG
SQ  VSHGQFFDQHLKFIKLNQQFVPFTQLDLSYLQQEAYDRDFLAQVYGAPQLQVEKVRTNDQKELGEVRVQYTSRDSFKAFA
SQ  KALGVMDDLKSGVPRAGYRGIVTFQFRGRRVHLAPPQTWTGYDPSWN
//
ID  P27115;
PN  Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
GN  MGAT1;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:P26572}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P26572}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P26572}. Note=Co-localizes with BRI3 at the perinuclear region. {ECO:0000250|UniProtKB:P26572}.
DR  UNIPROT: P27115;
DR  PDB: 1FO8;
DR  PDB: 1FO9;
DR  PDB: 1FOA;
DR  PDB: 2AM3;
DR  PDB: 2AM4;
DR  PDB: 2AM5;
DR  PDB: 2APC;
DR  Pfam: PF03071;
DE  Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans. {ECO:0000269|PubMed:1824724}.
DE  Reference Proteome: Yes;
GO  GO:0005797;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0003827;
GO  GO:0030145;
GO  GO:0016262;
GO  GO:0001701;
GO  GO:0006013;
GO  GO:0006487;
GO  GO:0018279;
GO  GO:0006049;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLKKQSAGLVLWGAILFVAWNALLLLFFWTRPVPSRLPSDNALDDDPASLTREVIRLAQDAEVELERQRGLLQQIREHHA
SQ  LWSQRWKVPTAAPPAQPHVPVTPPPAVIPILVIACDRSTVRRCLDKLLHYRPSAELFPIIVSQDCGHEETAQVIASYGSA
SQ  VTHIRQPDLSNIAVQPDHRKFQGYYKIARHYRWALGQIFHNFNYPAAVVVEDDLEVAPDFFEYFQATYPLLKADPSLWCV
SQ  SAWNDNGKEQMVDSSKPELLYRTDFFPGLGWLLLAELWAELEPKWPKAFWDDWMRRPEQRKGRACVRPEISRTMTFGRKG
SQ  VSHGQFFDQHLKFIKLNQQFVPFTQLDLSYLQQEAYDRDFLARVYGAPQLQVEKVRTNDRKELGEVRVQYTGRDSFKAFA
SQ  KALGVMDDLKSGVPRAGYRGIVTFLFRGRRVHLAPPQTWDGYDPSWT
//
ID  Q09325;
PN  Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
GN  Mgat1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane; Single-pass type II membrane protein. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P26572}. Note=Co-localizes with BRI3 at the perinuclear region. {ECO:0000250|UniProtKB:P26572}.
DR  UNIPROT: Q09325;
DR  Pfam: PF03071;
DE  Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
DE  Reference Proteome: Yes;
DE  Interaction: P15127; IntAct: EBI-21297848; Score: 0.35
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0008375;
GO  GO:0003827;
GO  GO:0030145;
GO  GO:0001701;
GO  GO:0006486;
GO  GO:0006487;
GO  GO:0018279;
GO  GO:0006049;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLKKQSAGLVLWGAIIFVGWNALLLLFFWTRPAPGRLPSDSALGDDPASLTREVIHLAEDAEAELERQRGLLQQIKEHYS
SQ  LWRQRWRVPTVAPPAWPRVPGTPSPAVIPILVIACDRSTVRRCLDKLLHYRPSAEHFPIIVSQDCGHEETAQVIASYGTA
SQ  VTHIRQPDLSNIAVQPDHRKFQGYYKIARHYRWALGQIFNKFKFPAAVVVEDDLEVAPDFFEYFQATYPLLKADPSLWCV
SQ  SAWNDNGKEQMVDSSKPELLYRTDFFPGLGWLLLADLWAELEPKWPKAFWDDWMRRPEQRKGRACIRPEISRTMTFGRKG
SQ  VSHGQFFDQHLKFIKLNQQFVPFTQLDLSYLQREAYDRDFLAQVYGAPQLQVEKVRTNDRKELGEVRVQYTSRDSFKAFA
SQ  KALGVMDDLKSGVPRAGYRGIVTFQFRGRRVHLAPPETWNGYDPSWN
//
ID  Q93367;
PN  Messenger RNA-binding inhibitor of apoptosis 1;
GN  mina;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:30728462}.
DR  UNIPROT: Q93367;
DR  PDB: 6FBL;
DR  Pfam: PF00013;
DE  Function: RNA-binding protein which binds to its own mRNA and target mRNAs to negatively regulate gene expression to modulate apoptosis and differentiation in the germline (PubMed:30728462). Negatively regulates the expression of the argonaute protein wago-4, and may thus play a role in RNA-mediated gene silencing (RNAi) in the germline (PubMed:30728462). {ECO:0000269|PubMed:30728462}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0003730;
GO  GO:0043066;
GO  GO:0045814;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDSTPYPVPQELYIPQKMKAFMAEPQGCALVAALEGQFQCSIVVINDHLSVISSADGVAVDINQIEKILRDVWRKRDVQ
SQ  IMIREAALNASCTHICHTLLPRAYCAVVLFFSSDLQRRSRCTDIIIDQFTGKVTMFGTEQAVNKAREMMIECLTEHFGLL
SQ  EMNIPPTQRTTRMGYTNSYNPEIRTHLPPNSFLNSVFPMGEPNAILTSTPPTTSIMDEPLLSASLEKHLLFPSDFSVPPP
SQ  RLSPVQELPLTPPKTCVVEKIKQWIPTTEVGKILGNRAAVKKHIERQFNCVITVHTEVQSSFGATPVEIVAQNKEQCQEA
SQ  RNAVMSLMQSHQDKPASNPPDSGFSTPGSPFTSDSSSTTPEKRGNSRQYHRGSFRDQPKVMLALTPRKLSPSD
//
ID  Q15049;
PN  Membrane protein MLC1;
GN  MLC1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:22328087}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22328087}. Endoplasmic reticulum {ECO:0000269|PubMed:22328087}.
DR  UNIPROT: Q15049;
DR  UNIPROT: B3KW61;
DR  UNIPROT: B7Z659;
DR  UNIPROT: Q5JZ83;
DR  UNIPROT: Q8TAG4;
DR  UNIPROT: Q96RP5;
DR  UNIPROT: Q9UGY8;
DR  OMIM: 604004;
DR  OMIM: 605908;
DR  DisGeNET: 23209;
DE  Function: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx. {ECO:0000269|PubMed:22328087}.
DE  Disease: Leukoencephalopathy, megalencephalic, with subcortical cysts, 1 (MLC1) [MIM:604004]: A syndrome of cerebral leukoencephalopathy and megalencephaly characterized by ataxia, spasticity, seizures, delay in motor development and mild intellectual disability. The brain appears swollen on magnetic resonance imaging, with diffuse white-matter abnormalities and the invariable presence of subcortical cysts in frontal and temporal lobes. {ECO:0000269|PubMed:11254442, ECO:0000269|PubMed:11935341, ECO:0000269|PubMed:12189496, ECO:0000269|PubMed:16652334, ECO:0000269|PubMed:22328087}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O60341; IntAct: EBI-8475314; Score: 0.37
DE  Interaction: Q96LA8; IntAct: EBI-8475351; Score: 0.37
DE  Interaction: P05026; IntAct: EBI-10095331; Score: 0.46
DE  Interaction: P07340; IntAct: EBI-10095479; Score: 0.35
DE  Interaction: Q9ERZ8; IntAct: EBI-10095479; Score: 0.35
DE  Interaction: Q01658; IntAct: EBI-25845761; Score: 0.56
DE  Interaction: P14136; IntAct: EBI-25858220; Score: 0.56
DE  Interaction: Q00403; IntAct: EBI-25865189; Score: 0.56
DE  Interaction: P04792; IntAct: EBI-25870905; Score: 0.56
DE  Interaction: P07196; IntAct: EBI-25877589; Score: 0.56
DE  Interaction: P60891; IntAct: EBI-25886460; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25898357; Score: 0.56
DE  Interaction: Q9Y5Q9; IntAct: EBI-25907076; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25915449; Score: 0.56
DE  Interaction: Q9UBB4; IntAct: EBI-25917631; Score: 0.56
DE  Interaction: Q9Y3C5; IntAct: EBI-25918864; Score: 0.56
DE  Interaction: Q8WXH2; IntAct: EBI-25927809; Score: 0.56
DE  Interaction: Q13148; IntAct: EBI-25984046; Score: 0.56
GO  GO:0016323;
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0045121;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0042802;
GO  GO:0044877;
GO  GO:0072584;
GO  GO:0071397;
GO  GO:0006811;
GO  GO:0032388;
GO  GO:0015031;
GO  GO:0047484;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTQEPFREELAYDRMPTLERGRQDPASYAPDAKPSDLQLSKRLPPCFSHKTWVFSVLMGSCLLVTSGFSLYLGNVFPAEM
SQ  DYLRCAAGSCIPSAIVSFTVSRRNANVIPNFQILFVSTFAVTTTCLIWFGCKLVLNPSAININFNLILLLLLELLMAATV
SQ  IIAARSSEEDCKKKKGSMSDSANILDEVPFPARVLKSYSVVEVIAGISAVLGGIIALNVDDSVSGPHLSVTFFWILVACF
SQ  PSAIASHVAAECPSKCLVEVLIAISSLTSPLLFTASGYLSFSIMRIVEMFKDYPPAIKPSYDVLLLLLLLVLLLQAGLNT
SQ  GTAIQCVRFKVSARLQGASWDTQNGPQERLAGEVARSPLKEFDKEKAWRAVVVQMAQ
//
ID  Q60HE7;
PN  Membrane protein MLC1;
GN  MLC1;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q60HE7;
DE  Function: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016323;
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0045121;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0042802;
GO  GO:0044877;
GO  GO:0072584;
GO  GO:0071397;
GO  GO:0006811;
GO  GO:0032388;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTQEPFREELAYDRMPTLERGRQDPASYAPDTKPSDLQLSKRLPPCFSPKTWVFSVLMGSCLLVTSGFSLYLGNVFPAEM
SQ  DYLRCAAGSCIPSAIVSFTVSRRNANVIPNFQILFVSTFAVTTTCLIWFGCKLILNPSAININFNLILLLLLELLMAATV
SQ  IMSARSSEEYCKKKKGSMSDGTNILGEVPFPARVLKSYSVVEVIAGISAVLGGIIALNVDDSVSGPHLSVTFFWILVACF
SQ  PSAIASHVTAECPSKCLVEVLIAISSLTSPLLFTASGYLSFSVMRIVEMFKDYPPAIKPSYDVLLLLLLLVLLLQAGLNT
SQ  GTAIQCVRFKVSARLQGASWDTQSGPQERLAGEVARSPLKEFDKEKAWRAVVVQMAQ
//
ID  Q8VHK5;
PN  Membrane protein MLC1;
GN  Mlc1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q8VHK5;
DE  Function: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8BIZ1; IntAct: EBI-26595802; Score: 0.35
GO  GO:0016324;
GO  GO:0097450;
GO  GO:0016323;
GO  GO:0005901;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0045121;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0042802;
GO  GO:0044877;
GO  GO:0072584;
GO  GO:0071397;
GO  GO:0006811;
GO  GO:0032388;
GO  GO:0015031;
GO  GO:0047484;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTREGQFREELGYDRMPTLERGRQDAGRQDPGSYTPDSKPKDLQLSKRLPPCFSYKTWVFSVLMGSCLLVTSGFSLYLGN
SQ  VFPSEMDYLRCAAGSCIPSAIVSFAVGRRNVSAIPNFQILFVSTFAVTTTCLIWFGCKLILNPSAININFNLILLLLLEL
SQ  LMAATVIISARSSEEPCKKKKGSISDGSNILDEVTFPARVLKSYSVVEVIAGVSAVLGGVIALNVEEAVSGPHLSVTFFW
SQ  ILVACFPSAIASHVTAECPSKCLVEVLIAISSLTSPLLFTASGYLSFSVMRVVEIFKDYPPAIKSYDVLLLLLLLLLLLQ
SQ  GGLNTGTAIQCVSFKVSARLQAASWDPQSCPQERPAGEVVRGPLKEFDKEKAWRAVVVQMAQ
//
ID  Q5VWP3;
PN  Muscular LMNA-interacting protein;
GN  MLIP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q5FW52}. Nucleus envelope {ECO:0000250|UniProtKB:Q5FW52}. Nucleus, PML body {ECO:0000250|UniProtKB:Q5FW52}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q5FW52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5FW52}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5FW52}.
DR  UNIPROT: Q5VWP3;
DR  UNIPROT: B7Z2N0;
DR  UNIPROT: D6RE05;
DR  UNIPROT: Q96H08;
DR  UNIPROT: Q96NF7;
DR  Pfam: PF15274;
DR  OMIM: 614106;
DR  DisGeNET: 90523;
DE  Function: Required for precocious cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays an important role in protection against cardiac hypertrophy. Acts as a transcriptional cofactor, represses transactivator activity of ISL1 and MYOCD. {ECO:0000250|UniProtKB:A0A096MK47, ECO:0000250|UniProtKB:Q5FW52}.
DE  Disease: Note=Expression is reduced in patients with dilated cardiomyocytes. In murine cardiomyopathy models, deletion of the encoding gene accelerates progress from hypertrophy to heart failure. {ECO:0000269|PubMed:26436652}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-3895433; Score: 0.37
DE  Interaction: P45984; IntAct: EBI-25254847; Score: 0.56
GO  GO:0005635;
GO  GO:0031981;
GO  GO:0005634;
GO  GO:0016605;
GO  GO:0042383;
GO  GO:0005521;
GO  GO:0003714;
GO  GO:0010614;
GO  GO:1903243;
GO  GO:0000122;
GO  GO:0045944;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5FW52};
SQ  MELEKREKRSLLNKNLEEKLTVSAGGSEAKPLIFTFVPTVRRLPTHTQLADTSKFLVKIPEESSDKSPETVNRSKSNDYL
SQ  TLNAGSQQERDQAKLTCPSEVSGTILQEREFEANKLQGMQQSDLFKAEYVLIVDSEGEDEAASRKVEQGPPGGIGTAAVR
SQ  PKSLAISSSLVSDVVRPKTQGTDLKTSSHPEMLHGMAPQQKHGQQYKTKSSYKAFAAIPTNTLLLEQKALDEPAKTESVS
SQ  KDNTLEPPVELYFPAQLRQQTEELCATIDKVLQDSLSMHSSDSPSRSPKTLLGSDTVKTPTTLPRAAGRETKYANLSSPS
SQ  STVSESQLTKPGVIRPVPVKSRILLKKEEEVYEPNPFSKYLEDNSDLFSEQDVTVPPKPVSLHPLYQTKLYPPAKSLLHP
SQ  QTLSHADCLAPGPFSHLSFSLSDEQENSHTLLSHNACNKLSHPMVAIPEHEALDSKEQ
//
ID  Q5FW52;
PN  Muscular LMNA-interacting protein;
GN  Mlip;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:21498514, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26436652}. Nucleus envelope {ECO:0000269|PubMed:21498514}. Nucleus, PML body {ECO:0000269|PubMed:21498514}. Cell membrane, sarcolemma {ECO:0000269|PubMed:26359501}; Peripheral membrane protein {ECO:0000269|PubMed:26359501}; Cytoplasmic side {ECO:0000269|PubMed:26359501}.
DR  UNIPROT: Q5FW52;
DR  UNIPROT: Q9D6X9;
DR  Pfam: PF15274;
DE  Function: Required for precocious cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays an important role in protection against cardiac hypertrophy (PubMed:26359501, PubMed:22343712, PubMed:26436652). Acts as a transcriptional cofactor, represses transactivator activity of ISL1 and MYOCD (PubMed:22343712). {ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26359501, ECO:0000269|PubMed:26436652}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-3895559; Score: 0.44
DE  Interaction: P48678; IntAct: EBI-3895570; Score: 0.49
DE  Interaction: P29590; IntAct: EBI-3895585; Score: 0.32
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0005635;
GO  GO:0031981;
GO  GO:0005634;
GO  GO:0016605;
GO  GO:0042383;
GO  GO:0005521;
GO  GO:0003714;
GO  GO:0010614;
GO  GO:1903243;
GO  GO:0000122;
GO  GO:0006366;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:26359501};
SQ  MEFGKHEPGSSLKRNKNLEEGVTFEYSDHMTFSSESKQERVQRILDYPSEVSGRNSQQKEFNTKEPQGMQKGDLFKAEYV
SQ  FIVDSDGEDEATCRQGEQGPPGGPGNIATRPKSLAISSSLASDVVRPKVRGADLKTSSHPEIPHGIAPQQKHGLALDEPA
SQ  RTESNSKASVLDLPVEHSSDSPSRPPQTMLGSETIKTPTTHPRAAGRETKYANLSSSSSTASESQLTKPGVIRPVPVKSK
SQ  LLLRKDEEVYEPNPFSKYLEDNSGLFSEQ
//
ID  A0A096MK47;
PN  Muscular LMNA-interacting protein;
GN  Mlip;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q5FW52}. Nucleus envelope {ECO:0000250|UniProtKB:Q5FW52}. Nucleus, PML body {ECO:0000250|UniProtKB:Q5FW52}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q5FW52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5FW52}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5FW52}.
DR  UNIPROT: A0A096MK47;
DR  UNIPROT: D4A3C4;
DR  UNIPROT: Q569A0;
DR  Pfam: PF15274;
DE  Function: Required for precocious cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays an important role in protection against cardiac hypertrophy (PubMed:22343712, PubMed:26436652). Acts as a transcriptional cofactor, represses transactivator activity of ISL1 and MYOCD (By similarity). {ECO:0000250|UniProtKB:Q5FW52, ECO:0000269|PubMed:22343712, ECO:0000269|PubMed:26436652}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031981;
GO  GO:0005634;
GO  GO:0016605;
GO  GO:0042383;
GO  GO:0005521;
GO  GO:0003714;
GO  GO:0010614;
GO  GO:1903243;
GO  GO:0045892;
GO  GO:0000122;
GO  GO:0045944;
GO  GO:0006366;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5FW52};
SQ  MEFEKHEQGNALKKNEKLEERVTFEYSDHMTFSCESKEERDQRILDYPSEVSGKNSQRKEFNTKEPQGMQKGDLFKAEYV
SQ  FIVDSDGEDEATCRQGEQGPPGATGNIATRPKSLAISSSLASDVVRPKVRGVDVKVSSHPEIPHGIAPQQKHGQLTSPTT
SQ  SEQLAHKPPAFSFVSPTNQKTPPVPAKVSGTTVLEEFHIRRLDVHGASEEETATYFHTTAHDSPLPAWKGASTLVFSPSA
SQ  QLPGSSLCGSNVADHTRGLAPEAQKKVSTSSALNPREDVRTSPSPASGASLRSPSASYIPVRIVMHSLSPSPKPLTSSSH
SQ  GSLSTVCSQTSSSGNLSKSGLKSPVPSRLSLLTAILKSNPSHQRPLSPASCPTFSLNSLASSTLTLDQKIKQTPSTPKKS
SQ  LSSCSLTTGSTEQEQASAESHQPCHLSFFSKTTPLSQAQPPSPPALASSSYAATDTEKIPGSTLRSSTTPPQSQTDLFSL
SQ  ADVPSVTPGLSPLSSSKGRKDGDLRAPEKNRNICTRPSTLSFIPPINESTALSSSGKCFHPSPALSDLIDRSKRTCSQRH
SQ  SDQRPNPSALPTPPVSRAGSASHPHLGYSILPPESSLTQALQRSPSALHPSCGSATCPSRTGMPDSTASNRSSRVSTPSL
SQ  PVSLTRTKELISPCALSMSAGPENKKPKQYKTKSSYKAFAAIPTNTLLLEQKALDEPARTESNSKASVSDLPVEHSSDSP
SQ  SRPSQTMLGSETIKTPTTHPRAAGRETKYANLSSSSSTTSESQLTKPGVIRPVPIKSKLFLKKEEEVYEPNPFSKYLEDS
SQ  SGLFSEQ
//
ID  Q02455;
PN  Protein MLP1;
GN  MLP1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:14718167, ECO:0000269|PubMed:16027220}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:24152732}. Note=Distributed fairly evenly along a C-shaped portion of the nuclear periphery, where the spindle pole body localizes in 90% of the cases. {ECO:0000269|PubMed:16027220}.
DR  UNIPROT: Q02455;
DR  UNIPROT: D6VXF5;
DR  Pfam: PF07926;
DR  PROSITE: PS51450;
DE  Function: Together with the closely related MLP2, involved in the structural and functional organization of perinuclear chromatin (PubMed:10638763). Together with MLP2, associates with the nuclear pore complex and form filamentous structures along the nuclear periphery (PubMed:10085285, PubMed:24152732). Has a role in the localization of Esc1 to nucleolar regions (PubMed:24152732). Together with MLP2, mediates tethering of the some telomeres to the nuclear periphery, probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and show perinuclear location dependent silencing (PubMed:11862215). MLP1 and MLP2 are involved in telomere length regulation but not silencing or telomere anchoring (PubMed:12490156). Recognizes the 5'-splice site of pre-mRNAs and retains unspliced pre-mRNA in the nucleus without affecting splicing itself (PubMed:12490156, PubMed:12531921, PubMed:14718167). {ECO:0000269|PubMed:10085285, ECO:0000269|PubMed:10638763, ECO:0000269|PubMed:11862215, ECO:0000269|PubMed:12490156, ECO:0000269|PubMed:12531921, ECO:0000269|PubMed:14718167, ECO:0000269|PubMed:24152732}.
DE  Reference Proteome: Yes;
DE  Interaction: P14906; IntAct: EBI-3769967; Score: 0.35
DE  Interaction: P25491; IntAct: EBI-3765167; Score: 0.35
DE  Interaction: P40457; IntAct: EBI-2212926; Score: 0.40
DE  Interaction: P32570; IntAct: EBI-806450; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-808689; Score: 0.56
DE  Interaction: P40024; IntAct: EBI-816662; Score: 0.27
DE  Interaction: Q02336; IntAct: EBI-820587; Score: 0.27
DE  Interaction: P23638; IntAct: EBI-7553011; Score: 0.40
DE  Interaction: Q07622; IntAct: EBI-8225053; Score: 0.22
DE  Interaction: P32505; IntAct: EBI-994908; Score: 0.58
DE  Interaction: Q01560; IntAct: EBI-994992; Score: 0.40
DE  Interaction: P32491; IntAct: EBI-2639782; Score: 0.40
DE  Interaction: P13186; IntAct: EBI-2640329; Score: 0.40
DE  Interaction: P32790; IntAct: EBI-7514515; Score: 0.37
DE  Interaction: Q06677; IntAct: EBI-3758621; Score: 0.35
DE  Interaction: P40564; IntAct: EBI-3760071; Score: 0.35
DE  Interaction: P39102; IntAct: EBI-3761494; Score: 0.35
DE  Interaction: P53863; IntAct: EBI-3769389; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3772409; Score: 0.35
DE  Interaction: P09435; IntAct: EBI-3775414; Score: 0.35
DE  Interaction: P32590; IntAct: EBI-3776763; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3781040; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3787826; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3790511; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3799302; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3806004; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3812463; Score: 0.35
DE  Interaction: P39078; IntAct: EBI-3822418; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3825702; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3829128; Score: 0.35
DE  Interaction: Q04432; IntAct: EBI-3830630; Score: 0.35
DE  Interaction: P22943; IntAct: EBI-3831347; Score: 0.35
DE  Interaction: YGR032W; IntAct: EBI-3952595; Score: 0.35
DE  Interaction: P39523; IntAct: EBI-9976090; Score: 0.35
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0003729;
GO  GO:0140586;
GO  GO:0043021;
GO  GO:0017056;
GO  GO:0006281;
GO  GO:0006406;
GO  GO:1901925;
GO  GO:0071028;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0090204;
GO  GO:0034398;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDHDTPMESIQNGENSDERLNAIASFFGCSLEQVKSFDGDVVKHLNDKLLQFNELKSENLKVTVSFDELKASSLKKIDG
SQ  LKTEMENVIRENDKIRKERNDTFVKFESVENEKMKLSSELEFVKRKLDDLTEEKKETQSNQQRTLKILDERLKEIELVRV
SQ  ENNRSNSECKKLRSTIMDLETKQQGYITNDLNSRTELERKTQELTLLQSNNDWLEKELRSKNEQYLSYRQKTDKVILDIR
SQ  NELNRLRNDFQMERTNNDVLKQKNNELSKSLQEKLLEIKGLSDSLNSEKQEFSAEMSLKQRLVDLLESQLNAVKEELNSI
SQ  RELNTAKVIADDSKKQTPENEDLLKELQLTKEKLAQCEKECLRLSSITDEADEDNENLSAKSSSDFIFLKKQLIKERRTK
SQ  EHLQNQIETFIVELEHKVPIINSFKERTDMLENELNNAALLLEHTSNEKNAKVKELNAKNQKLVECENDLQTLTKQRLDL
SQ  CRQIQYLLITNSVSNDSKGPLRKEEIQFIQNIMQEDDSTITESDSQKVVTERLVEFKNIIQLQEKNAELLKVVRNLADKL
SQ  ESKEKKSKQSLQKIESETVNEAKEAIITLKSEKMDLESRIEELQKELEELKTSVPNEDASYSNVTIKQLTETKRDLESQV
SQ  QDLQTRISQITRESTENMSLLNKEIQDLYDSKSDISIKLGKEKSSRILAEERFKLLSNTLDLTKAENDQLRKRFDYLQNT
SQ  ILKQDSKTHETLNEYVSCKSKLSIVETELLNLKEEQKLRVHLEKNLKQELNKLSPEKDSLRIMVTQLQTLQKEREDLLEE
SQ  TRKSCQKKIDELEDALSELKKETSQKDHHIKQLEEDNNSNIEWYQNKIEALKKDYESVITSVDSKQTDIEKLQYKVKSLE
SQ  KEIEEDKIRLHTYNVMDETINDDSLRKELEKSKINLTDAYSQIKEYKDLYETTSQSLQQTNSKLDESFKDFTNQIKNLTD
SQ  EKTSLEDKISLLKEQMFNLNNELDLQKKGMEKEKADFKKRISILQNNNKEVEAVKSEYESKLSKIQNDLDQQTIYANTAQ
SQ  NNYEQELQKHADVSKTISELREQLHTYKGQVKTLNLSRDQLENALKENEKSWSSQKESLLEQLDLSNSRIEDLSSQNKLL
SQ  YDQIQIYTAADKEVNNSTNGPGLNNILITLRRERDILDTKVTVAERDAKMLRQKISLMDVELQDARTKLDNSRVEKENHS
SQ  SIIQQHDDIMEKLNQLNLLRESNITLRNELENNNNKKKELQSELDKLKQNVAPIESELTALKYSMQEKEQELKLAKEEVH
SQ  RWKKRSQDILEKHEQLSSSDYEKLESEIENLKEELENKERQGAEAEEKFNRLRRQAQERLKTSKLSQDSLTEQVNSLRDA
SQ  KNVLENSLSEANARIEELQNAKVAQGNNQLEAIRKLQEDAEKASRELQAKLEESTTSYESTINGLNEEITTLKEEIEKQR
SQ  QIQQQLQATSANEQNDLSNIVESMKKSFEEDKIKFIKEKTQEVNEKILEAQERLNQPSNINMEEIKKKWESEHEQEVSQK
SQ  IREAEEALKKRIRLPTEEKINKIIERKKEELEKEFEEKVEERIKSMEQSGEIDVVLRKQLEAKVQEKQKELENEYNKKLQ
SQ  EELKDVPHSSHISDDERDKLRAEIESRLREEFNNELQAIKKKSFDEGKQQAMMKTTLLERKLAKMESQLSETKQSAESPP
SQ  KSVNNVQNPLLGLPRKIEENSNSPFNPLLSGEKLLKLNSKSSSGGFNPFTSPSPNKHLQNDNDKRESLANKTDPPTHLEP
SQ  SFNIPASRGLISSSSTLSTDTNDEELTSNNPAQKDSSNRNVQSEEDTEKKKEGEPVKRGEAIEEQTKSNKRPIDEVGELK
SQ  NDEDDTTENINESKKIKTEDEEEKETDKVNDENSI
//
ID  P40457;
PN  Protein MLP2;
GN  MLP2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus, nuclear pore complex {ECO:0000269|PubMed:24152732}. Note=Nuclear periphery, excluded from nuclear envelope adjacent to nucleolus.
DR  UNIPROT: P40457;
DR  UNIPROT: D6VVD8;
DE  Function: Together with the closely related MLP1, involved in the structural and functional organization of perinuclear chromatin (PubMed:10638763). MLP1/MLP2 associate with the nuclear pore complex and form filamentous structures along the nuclear periphery (PubMed:10085285, PubMed:24152732, PubMed:10617624). Has a role in the localization of Esc1 to nucleolar regions (PubMed:24152732). Together with MLP1, mediates tethering of the some telomeres to the nuclear periphery, probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and show perinuclear location dependent silencing (PubMed:11862215). MLP1 and MLP2 are involved in telomere length regulation but not silencing or telomere anchoring (PubMed:12490156). Plays a role in the incorporation of components into the spindle pole body (PubMed:10617624, PubMed:14718167, PubMed:16027220). Involved in double-strand break repair, probably also mediated by the YKU70/YKU80 (HDF1/HDF2) heterodimer (PubMed:10638763, PubMed:14718167, PubMed:16027220). {ECO:0000269|PubMed:10085285, ECO:0000269|PubMed:10617624, ECO:0000269|PubMed:10638763, ECO:0000269|PubMed:11862215, ECO:0000269|PubMed:12490156, ECO:0000269|PubMed:14718167, ECO:0000269|PubMed:16027220, ECO:0000269|PubMed:24152732}.
DE  Reference Proteome: Yes;
DE  Interaction: P06704; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P14906; IntAct: EBI-3769975; Score: 0.35
DE  Interaction: P25491; IntAct: EBI-3765175; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06411; IntAct: EBI-857722; Score: 0.00
DE  Interaction: Q06512; IntAct: EBI-7126570; Score: 0.40
DE  Interaction: P36106; IntAct: EBI-8221031; Score: 0.22
DE  Interaction: Q02455; IntAct: EBI-2212926; Score: 0.40
DE  Interaction: P38863; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P53540; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P33419; IntAct: EBI-2212931; Score: 0.52
DE  Interaction: P36094; IntAct: EBI-2212931; Score: 0.52
DE  Interaction: P39723; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P32380; IntAct: EBI-2212931; Score: 0.52
DE  Interaction: Q12365; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P06787; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P53865; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P53159; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: Q06677; IntAct: EBI-3758629; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3772417; Score: 0.35
DE  Interaction: P09435; IntAct: EBI-3775422; Score: 0.35
DE  Interaction: P32590; IntAct: EBI-3776771; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3781048; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3787834; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3790519; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3794434; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3799310; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3806012; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3812471; Score: 0.35
DE  Interaction: P20081; IntAct: EBI-16269289; Score: 0.35
DE  Interaction: P53916; IntAct: EBI-16285181; Score: 0.35
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0005816;
GO  GO:0043021;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:1901925;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0051300;
GO  GO:0034398;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDKISEFLNVPFESLQGVTYPVLRKLYKKIAKFERSEEEVTKLNVLVDEIKSQYYSRISKLKQLLDESSEQKNTAKEEL
SQ  NGLKDQLNEERSRYRREIDALKKQLHVSHEAMREVNDEKRVKEEYDIWQSRDQGNDSLNDDLNKENKLLRRKLMEMENIL
SQ  QRCKSNAISLQLKYDTSVQEKELMLQSKKLIEEKLSSFSKKTLTEEVTKSSHVENLEEKLYQMQSNYESVFTYNKFLLNQ
SQ  NKQLSQSVEEKVLEMKNLKDTASVEKAEFSKEMTLQKNMNDLLRSQLTSLEKDCSLRAIEKNDDNSCRNPEHTDVIDELI
SQ  DTKLRLEKSKNECQRLQNIVMDCTKEEEATMTTSAVSPTVGKLFSDIKVLKRQLIKERNQKFQLQNQLEDFILELEHKTP
SQ  ELISFKERTKSLEHELKRSTELLETVSLTKRKQEREITSLRQKINGCEANIHSLVKQRLDLARQVKLLLLNTSAIQETAS
SQ  PLSQDELISLRKILESSNIVNENDSQAIITERLVEFSNVNELQEKNVELLNCIRILADKLENYEGKQDKTLQKVENQTIK
SQ  EAKDAIIELENINAKMETRINILLRERDSYKLLASTEENKANTNSVTSMEAAREKKIRELEAELSSTKVENSAIIQNLRK
SQ  ELLIYKKSQCKKKTTLEDFENFKGLAKEKERMLEEAIDHLKAELEKQKSWVPSYIHVEKERASTELSQSRIKIKSLEYEI
SQ  SKLKKETASFIPTKESLTRDFEQCCKEKKELQMRLKESEISHNENKMDFSSKEGQYKAKIKELENNLERLRSDLQSKIQE
SQ  IESIRSCKDSQLKWAQNTIDDTEMKMKSLLTELSNKETTIEKLSSEIENLDKELRKTKFQYKFLDQNSDASTLEPTLRKE
SQ  LEQIQVQLKDANSQIQAYEEIISSNENALIELKNELAKTKENYDAKIELEKKEKWAREEDLSRLRGELGEIRALQPKLKE
SQ  GALHFVQQSEKLRNEVERIQKMIEKIEKMSTIVQLCKKKEMSQYQSTMKENKDLSELVIRLEKDAADCQAELTKTKSSLY
SQ  SAQDLLDKHERKWMEEKADYERELISNIEQTESLRVENSVLIEKVDDTAANNGDKDHLKLVSLFSNLRHERNSLETKLTT
SQ  CKRELAFVKQKNDSLEKTINDLQRTQTLSEKEYQCSAVIIDEFKDITKEVTQVNILKENNAILQKSLKNVTEKNREIYKQ
SQ  LNDRQEEISRLQRDLIQTKEQVSINSNKILVYESEMEQCKQRYQDLSQQQKDAQKKDIEKLTNEISDLKGKLSSAENANA
SQ  DLENKFNRLKKQAHEKLDASKKQQAALTNELNELKAIKDKLEQDLHFENAKVIDLDTKLKAHELQSEDVSRDHEKDTYRT
SQ  LMEEIESLKKELQIFKTANSSSDAFEKLKVNMEKEKDRIIDERTKEFEKKLQETLNKSTSSEAEYSKDIETLKKEWLKEY
SQ  EDETLRRIKEAEENLKKRIRLPSEERIQKIISKRKEELEEEFRKKLKENAGSLTFLDNKGSGEDAEEELWNSPSKGNSER
SQ  PSAVAGFINQKNLKPQEQLKNVKNDVSFNDSQSMVTNKENNIVDSSAAGNKAIPTFSFGKPFFSSNTSSLQSFQNPFTAS
SQ  QSNINTNAPLRTLNIQPEVAVKAAINFSNVTDLTNNSTDGAKITEIGSTSKRPIESGTSSDPDTKKVKESPANDQASNE
//
ID  Q70IA6;
PN  MOB kinase activator 2;
GN  MOB2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:15067004}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15067004}.
DR  UNIPROT: Q70IA6;
DR  UNIPROT: B4DKP3;
DR  UNIPROT: Q96M67;
DR  Pfam: PF03637;
DR  OMIM: 611969;
DR  DisGeNET: 81532;
DE  Function: Stimulates the autophosphorylation and kinase activity of STK38 and STK38L. {ECO:0000269|PubMed:15067004}.
DE  Reference Proteome: Yes;
DE  Interaction: Q91VJ4; IntAct: EBI-2558744; Score: 0.40
DE  Interaction: Q9Y2H1; IntAct: EBI-6912403; Score: 0.84
DE  Interaction: Q9H8S9; IntAct: EBI-8798967; Score: 0.27
DE  Interaction: Q7L9L4; IntAct: EBI-8799069; Score: 0.27
DE  Interaction: P05549; IntAct: EBI-9679119; Score: 0.37
DE  Interaction: Q15208; IntAct: EBI-10104572; Score: 0.53
DE  Interaction: Q96ST8; IntAct: EBI-11396670; Score: 0.27
DE  Interaction: Q96HA8; IntAct: EBI-24519574; Score: 0.56
DE  Interaction: A6NKK0; IntAct: EBI-23725385; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-23741494; Score: 0.56
DE  Interaction: Q6NZ36; IntAct: EBI-23770281; Score: 0.56
DE  Interaction: O95562; IntAct: EBI-23919217; Score: 0.56
DE  Interaction: Q9NT62; IntAct: EBI-24468042; Score: 0.56
DE  Interaction: Q5JXC2; IntAct: EBI-25144811; Score: 0.56
DE  Interaction: Q9GZT6; IntAct: EBI-25152278; Score: 0.56
DE  Interaction: Q70Z53; IntAct: EBI-25181341; Score: 0.56
DE  Interaction: P06493; IntAct: EBI-20304060; Score: 0.35
DE  Interaction: Q96H96; IntAct: EBI-20304156; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-20307233; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-20307902; Score: 0.35
DE  Interaction: Q9NPJ6; IntAct: EBI-25472377; Score: 0.35
DE  Interaction: P10644; IntAct: EBI-25387530; Score: 0.35
DE  Interaction: Q9NRY4; IntAct: EBI-25408519; Score: 0.35
DE  Interaction: Q8K0Q5; IntAct: EBI-25409623; Score: 0.35
DE  Interaction: Q3KRB8; IntAct: EBI-25411814; Score: 0.35
DE  Interaction: A0A024R136; IntAct: EBI-25411916; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q96DG6; IntAct: EBI-25481445; Score: 0.35
DE  Interaction: O15164; IntAct: EBI-25486121; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568044; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0030295;
GO  GO:0001934;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDWLMGKSKAKPNGKKPAAEERKAYLEPEHTKARITDFQFKELVVLPREIDLNEWLASNTTTFFHHINLQYSTISEFCTG
SQ  ETCQTMAVCNTQYYWYDERGKKVKCTAPQYVDFVMSSVQKLVTDEDVFPTKYGREFPSSFESLVRKICRHLFHVLAHIYW
SQ  AHFKETLALELHGHLNTLYVHFILFAREFNLLDPKETAIMDDLTEVLCSGAGGVHSGGSGDGAGSGGPGAQNHVKER
//
ID  Q8VI63;
PN  MOB kinase activator 2;
GN  Mob2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q8VI63;
DR  UNIPROT: Q3UXL5;
DR  UNIPROT: Q9CZJ5;
DR  Pfam: PF03637;
DE  Function: Stimulates the autophosphorylation and kinase activity of STK38 and STK38L. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0044306;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0030295;
GO  GO:0030036;
GO  GO:0010976;
GO  GO:0001934;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDWLMGKSKAKPNGKKPAAEEKKVYLEPEHTKSRITDFEFKELVVLPREIDLNEWLASNTTTFFHHINLQYSTISEFCTG
SQ  ETCQTMAVCNTQYYWYDERGKKVKCTAPQYVDFVMSSVQKLVTDEDVFPTKYGREFPSSFESLVKKICKYLFHVLGHIYW
SQ  AHFKETLALELHGHLNTLYVHFILFAREFNLLDPKETAVMDDLTEVLCSSPGNSGATGDGANSGASGAQNHVKER
//
ID  Q13875;
PN  Myelin-associated oligodendrocyte basic protein;
GN  MOBP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Note=Present in the major dense line of CNS myelin. {ECO:0000250}.
DR  UNIPROT: Q13875;
DR  UNIPROT: A8K2C2;
DR  UNIPROT: G5E945;
DR  UNIPROT: Q13874;
DR  UNIPROT: Q6DHZ6;
DR  UNIPROT: Q8TBJ1;
DR  Pfam: PF02318;
DR  OMIM: 600948;
DR  DisGeNET: 4336;
DE  Function: May play a role in compacting or stabilizing the myelin sheath, possibly by binding the negatively charged acidic phospholipids of the cytoplasmic membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P60370; IntAct: EBI-10230657; Score: 0.56
DE  Interaction: P60409; IntAct: EBI-10230667; Score: 0.56
DE  Interaction: P60411; IntAct: EBI-10230677; Score: 0.72
DE  Interaction: Q6A162; IntAct: EBI-16436101; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-16437155; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-16439621; Score: 0.56
DE  Interaction: Q8WV44; IntAct: EBI-25245181; Score: 0.56
DE  Interaction: P26371; IntAct: EBI-24494434; Score: 0.56
DE  Interaction: P17027; IntAct: EBI-23764765; Score: 0.56
DE  Interaction: P60412; IntAct: EBI-23821872; Score: 0.56
DE  Interaction: A0A087WZT3; IntAct: EBI-23888832; Score: 0.56
DE  Interaction: Q9BYR9; IntAct: EBI-24378588; Score: 0.56
DE  Interaction: P60328; IntAct: EBI-24387401; Score: 0.56
DE  Interaction: P60371; IntAct: EBI-24472391; Score: 0.56
DE  Interaction: O00560; IntAct: EBI-24587332; Score: 0.56
DE  Interaction: P36957; IntAct: EBI-20908424; Score: 0.40
GO  GO:0030864;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0017022;
GO  GO:0007399;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQKPAKEGPRLSKNQKYSEHFSIHCCPPFTFLNSKKEIVDRKYSICKSGCFYQKKEEDWICCACQKTRTSRRAKSPQRP
SQ  KQQPAAPPAVVRAPAKPRSPPRSERQPRSPPRSERQPRSPPRSERQPRSPPRSERQPRPRPEVRPPPAKQRPPQKSKQQP
SQ  RSSPLRGPGASRGGSPVKASRFW
//
ID  Q9D2P8;
PN  Myelin-associated oligodendrocyte basic protein;
GN  Mobp;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Note=Present in the major dense line of CNS myelin. {ECO:0000250}.
DR  UNIPROT: Q9D2P8;
DR  UNIPROT: O35713;
DR  UNIPROT: Q792D7;
DR  UNIPROT: Q792D8;
DR  UNIPROT: Q9JLY4;
DR  UNIPROT: Q9JLY5;
DR  UNIPROT: Q9JLY6;
DR  Pfam: PF02318;
DE  Function: May play a role in compacting or stabilizing the myelin sheath possibly by binding the negatively charged acidic phospholipids of the cytoplasmic membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030864;
GO  GO:0005829;
GO  GO:0005739;
GO  GO:0043209;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0017022;
GO  GO:0019911;
GO  GO:0032289;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQKMAKEGPRLSKNQKFSEHFSIHCCPPFTFLNSKREIVDRKYSICKSGCFYQKKEEDWICCACQKTSRRATSPQRPKH
SQ  QPAASPVVVRAPPAKPKSPLMPAKPRSPPRPAKPRSPSRTERQPRPRPEVRPPPAKQKPPQKSKQPARSSPLRGPGTSRG
SQ  GSPTRAPRFW
//
ID  Q63327;
PN  Myelin-associated oligodendrocyte basic protein;
GN  Mobp;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10537049, ECO:0000269|PubMed:8551331}. Note=Present in the major dense line of CNS myelin. Isoform 5 may be differentially localized in the oligodendrocytes or perinuclear region. Isoform 2, 4, 5 and 6 are highly enriched in myelin. Isoform 1 and 3 are not enriched in mylein.
DR  UNIPROT: Q63327;
DR  UNIPROT: Q63328;
DR  UNIPROT: Q63343;
DR  UNIPROT: Q63519;
DR  UNIPROT: Q64266;
DR  UNIPROT: Q9QZV5;
DR  Pfam: PF02318;
DE  Function: May play a role in compacting or stabilizing the myelin sheath, possibly by binding the negatively charged acidic phospholipids of the cytoplasmic membrane. {ECO:0000269|PubMed:7989345}.
DE  Reference Proteome: Yes;
GO  GO:0030864;
GO  GO:0005739;
GO  GO:0043209;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0017022;
GO  GO:0019911;
GO  GO:0032289;
GO  GO:0007399;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQKVAKEGPRLSKNQKFSEHFSIHCCPPFTFLNSKREIVDRKYSICKSGCFYQKKEEDWICCACQKTSRRATSPQKPKH
SQ  QPAASPVVVRAPPAKPKSPPRPAKPRSPPIPAKPRSPSRTERQPRPRPEVRPPPAKQKPPQKSKQPARSSPLRGPGTSRG
SQ  GSPTRAPRFW
//
ID  Q3ZC61;
PN  MORF4 family-associated protein 1;
GN  MRFAP1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y605}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y605}. Note=Colocalizes with MORF4L1 to cell nuclei. {ECO:0000250|UniProtKB:Q9Y605}.
DR  UNIPROT: Q3ZC61;
DR  Pfam: PF15155;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRPLDIVELAEPEEVEVLEPEEDFEQFLLPVINEMREDIAALSREHGRAYLRNRSKLWEMDNMLIQIKTQVEASEESALN
SQ  HLQNPDDGAEGRGTKRCEKAEEKAKEIAKMAEMLVELVRRIEKSESS
//
ID  Q9Y605;
PN  MORF4 family-associated protein 1;
GN  MRFAP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:11500496, ECO:0000269|PubMed:12397079}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11500496, ECO:0000269|PubMed:12397079}. Note=Colocalizes with MORF4L1 to cell nuclei. {ECO:0000269|PubMed:11500496, ECO:0000269|PubMed:12397079}.
DR  UNIPROT: Q9Y605;
DR  UNIPROT: B3KVT2;
DR  UNIPROT: D3DVT3;
DR  Pfam: PF15155;
DR  OMIM: 616905;
DR  DisGeNET: 93621;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: O14656; IntAct: EBI-25847426; Score: 0.56
DE  Interaction: O75190; IntAct: EBI-25910113; Score: 0.56
DE  Interaction: P01112; IntAct: EBI-25869463; Score: 0.56
DE  Interaction: P0C6X6; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: Q9WMX2; IntAct: EBI-11513238; Score: 0.35
DE  Interaction: Q15014; IntAct: EBI-995721; Score: 0.89
DE  Interaction: Q9UBU8; IntAct: EBI-10319562; Score: 0.85
DE  Interaction: Q9Y4A5; IntAct: EBI-1062613; Score: 0.00
DE  Interaction: Q00975; IntAct: EBI-1065890; Score: 0.00
DE  Interaction: P28749; IntAct: EBI-1070874; Score: 0.00
DE  Interaction: P35244; IntAct: EBI-1075626; Score: 0.00
DE  Interaction: Q5NID2; IntAct: EBI-2804775; Score: 0.00
DE  Interaction: Q5NH45; IntAct: EBI-2804782; Score: 0.00
DE  Interaction: A0A6L8P747; IntAct: EBI-2829622; Score: 0.00
DE  Interaction: Q9H7E9; IntAct: EBI-7109558; Score: 0.37
DE  Interaction: Q9Y3D7; IntAct: EBI-7187220; Score: 0.37
DE  Interaction: Q9GZQ8; IntAct: EBI-7189812; Score: 0.37
DE  Interaction: P04183; IntAct: EBI-7399477; Score: 0.37
DE  Interaction: Q8IZP0; IntAct: EBI-5652758; Score: 0.00
DE  Interaction: O75953; IntAct: EBI-5655989; Score: 0.00
DE  Interaction: P42858; IntAct: EBI-6451449; Score: 0.67
DE  Interaction: Q9H5I1; IntAct: EBI-8475859; Score: 0.51
DE  Interaction: Q8IUH5; IntAct: EBI-9089882; Score: 0.37
DE  Interaction: Q08AF8; IntAct: EBI-10329580; Score: 0.56
DE  Interaction: Q6ZUJ4; IntAct: EBI-10329600; Score: 0.56
DE  Interaction: Q96HT8; IntAct: EBI-10329610; Score: 0.72
DE  Interaction: Q9H972; IntAct: EBI-10329630; Score: 0.56
DE  Interaction: Q9UHG0; IntAct: EBI-10329650; Score: 0.56
DE  Interaction: Q9P2A4; IntAct: EBI-24511853; Score: 0.56
DE  Interaction: Q8IYE0; IntAct: EBI-24522849; Score: 0.56
DE  Interaction: O00560; IntAct: EBI-24523463; Score: 0.56
DE  Interaction: Q2TAY7; IntAct: EBI-24532432; Score: 0.56
DE  Interaction: Q99757; IntAct: EBI-24605994; Score: 0.56
DE  Interaction: Q9HAC8; IntAct: EBI-24608219; Score: 0.56
DE  Interaction: Q9H788; IntAct: EBI-24632647; Score: 0.56
DE  Interaction: Q9H0N5; IntAct: EBI-24632601; Score: 0.56
DE  Interaction: P54646; IntAct: EBI-23754601; Score: 0.56
DE  Interaction: Q9BRT2; IntAct: EBI-24744186; Score: 0.56
DE  Interaction: Q8N720; IntAct: EBI-24747740; Score: 0.56
DE  Interaction: Q9NYB9; IntAct: EBI-24567995; Score: 0.56
DE  Interaction: Q96LD4; IntAct: EBI-23880725; Score: 0.56
DE  Interaction: Q8IYF3; IntAct: EBI-24386836; Score: 0.56
DE  Interaction: Q96NZ9; IntAct: EBI-24419470; Score: 0.56
DE  Interaction: P07951; IntAct: EBI-24534597; Score: 0.56
DE  Interaction: Q9C005; IntAct: EBI-24538323; Score: 0.56
DE  Interaction: Q9BVG8; IntAct: EBI-24563169; Score: 0.56
DE  Interaction: Q969G5; IntAct: EBI-24566551; Score: 0.56
DE  Interaction: O94868; IntAct: EBI-24585786; Score: 0.56
DE  Interaction: Q8WUW1; IntAct: EBI-24633125; Score: 0.72
DE  Interaction: Q9H2K0; IntAct: EBI-25201221; Score: 0.56
DE  Interaction: P10599; IntAct: EBI-25274110; Score: 0.56
DE  Interaction: Q8IVT5; IntAct: EBI-14035152; Score: 0.35
DE  Interaction: Q6VAB6; IntAct: EBI-14036442; Score: 0.35
DE  Interaction: Q9NPJ6; IntAct: EBI-25472377; Score: 0.35
DE  Interaction: P01023; IntAct: EBI-25830269; Score: 0.56
DE  Interaction: Q92870; IntAct: EBI-25831717; Score: 0.56
DE  Interaction: P50570; IntAct: EBI-25845258; Score: 0.56
DE  Interaction: P60891; IntAct: EBI-25886785; Score: 0.56
DE  Interaction: P49768; IntAct: EBI-25888651; Score: 0.56
DE  Interaction: Q86WV8; IntAct: EBI-25893777; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25899748; Score: 0.56
DE  Interaction: O14901; IntAct: EBI-25906063; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25916504; Score: 0.56
DE  Interaction: Q8TB36; IntAct: EBI-25923500; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25933087; Score: 0.56
DE  Interaction: P54253; IntAct: EBI-25978630; Score: 0.56
GO  GO:0005654;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRPLDIVELAEPEEVEVLEPEEDFEQFLLPVINEMREDIASLTREHGRAYLRNRSKLWEMDNMLIQIKTQVEASEESALN
SQ  HLQNPGDAAEGRAAKRCEKAEEKAKEIAKMAEMLVELVRRIEKSESS
//
ID  Q9CQL7;
PN  MORF4 family-associated protein 1;
GN  Mrfap1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y605}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y605}. Note=Colocalizes with MORF4L1 to cell nuclei. {ECO:0000250|UniProtKB:Q9Y605}.
DR  UNIPROT: Q9CQL7;
DR  UNIPROT: Q9CX68;
DR  Pfam: PF15155;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9UBX2; IntAct: EBI-11600705; Score: 0.37
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0042802;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRPLDAVELAEPEEVEVLEPEEDFEQFLLPVIHEMREDIASLTRERGRAPARNRGKLWEMDNMLIQIKTQVEASEESALN
SQ  HLQGAGGAEPRGPRAEKADEKAQEMAKMAEMLVQLVRRIEKSESS
//
ID  Q5RC01;
PN  MORF4 family-associated protein 1;
GN  MRFAP1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y605}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y605}. Note=Colocalizes with MORF4L1 to cell nuclei. {ECO:0000250|UniProtKB:Q9Y605}.
DR  UNIPROT: Q5RC01;
DR  Pfam: PF15155;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042802;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRPLDIDEVEAPEEVEVLEPEEDFEQFLLPVINEMREDIASLIREHGRAYLRTRSKLWEMDNMLIQIKTQVEASEESALN
SQ  HVQHPSGEADERVSELCEKAEEKAKEIAKMAEMLVELVWRIERSESS
//
ID  Q5M820;
PN  MORF4 family-associated protein 1;
GN  Mrfap1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y605}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y605}. Note=Colocalizes with MORF4L1 to cell nuclei. {ECO:0000250|UniProtKB:Q9Y605}.
DR  UNIPROT: Q5M820;
DR  UNIPROT: Q8K3W6;
DR  Pfam: PF15155;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRPLDAVELAEPEEVEVLEPEEDFEQFLLPVIHEMREDIASLTRERGRAPVRNRGKLWEMDNMLIQIKTQVEASEESALN
SQ  HLQGAGGAEPRGPRAEKADEKAQEMAKMAEMLVQLVRRIEKSESS
//
ID  Q32PE2;
PN  Ran guanine nucleotide release factor;
GN  RANGRF;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD47}. Cell membrane {ECO:0000250|UniProtKB:Q9HD47}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HD47}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9HD47}. Note=May shuttle between the nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q9HD47}.
DR  UNIPROT: Q32PE2;
DR  Pfam: PF04603;
DE  Function: May regulate the intracellular trafficking of RAN. Promotes guanine nucleotide release from RAN and inhibits binding of new GTP by preventing the binding of the RAN guanine nucleotide exchange factor RCC1. Regulates the levels of GTP-bound RAN in the nucleus, and thereby plays a role in the regulation of RAN-dependent mitotic spindle dynamics. Enhances the expression of SCN5A at the cell membrane in cardiomyocytes. {ECO:0000250|UniProtKB:Q9HD47}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005085;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9HD47};
SQ  MEPTRDNPLFGGAFSATLPPGAIDVSDLRPVPDHQEVFCHRVTDQSLIVELLELQAHVQGEEAARYHFEDVGGVQEARAV
SQ  QVETVQPLVLEKLALRGCCQEAWILSGQQQVAKENQQVAKYVTLHQALLRLPQYQTDLLLTFNQPPPENRSSLGPENLSI
SQ  PPWSLGDFEQLVTSLTLHDPNIFGPE
//
ID  A3KPP3;
PN  Ran guanine nucleotide release factor;
GN  rangrf;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD47}. Cell membrane {ECO:0000250|UniProtKB:Q9HD47}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HD47}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9HD47}. Note=May shuttle between the nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q9HD47}.
DR  UNIPROT: A3KPP3;
DR  UNIPROT: A7E2J7;
DR  Pfam: PF04603;
DE  Function: May regulate the intracellular trafficking of RAN. Promotes guanine nucleotide release from RAN and inhibits binding of new GTP. Plays a role in the regulation of the levels of GTP-bound RAN in the nucleus (By similarity). Required for normal expression of the ion channel hcn4 and for normal expression of the cardiac transcription factors nkx2.5, gata4 and hand2 during embryonic development. Required for normal embryonic heart development and normal heart rate (PubMed:26903377). {ECO:0000250|UniProtKB:Q9HD47, ECO:0000269|PubMed:26903377}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005085;
GO  GO:0031267;
GO  GO:0017080;
GO  GO:0044325;
GO  GO:0060047;
GO  GO:0001947;
GO  GO:0006606;
GO  GO:0003254;
GO  GO:0042391;
GO  GO:2000649;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9HD47};
SQ  MSRPLFGGALSAVFPSSVMDISELRQIPDNQEVFAHSQTDQSIIIELLEYQSQVQDADAARYHFEDVAGSNKAIENGTWE
SQ  VRVVEQVPQSEISMQECSSAWLLSGAQLVSKFNEEAKNTVNVHQCLFRLPQFTTDILMTFNDPVFINPLSSSAAGNMEAI
SQ  PWTLQDFQGVLQSLRLLDSGVFG
//
ID  Q9HD47;
PN  Ran guanine nucleotide release factor;
GN  RANGRF;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:11290418}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21447824}. Cytoplasm {ECO:0000269|PubMed:11290418, ECO:0000269|PubMed:21447824}. Cell membrane {ECO:0000269|PubMed:21447824}; Peripheral membrane protein {ECO:0000305|PubMed:21447824}; Cytoplasmic side {ECO:0000305|PubMed:21447824}. Note=May shuttle between the nucleus and cytoplasm. {ECO:0000269|PubMed:11290418}.
DR  UNIPROT: Q9HD47;
DR  UNIPROT: D3DTR6;
DR  UNIPROT: Q68DI3;
DR  UNIPROT: Q9BR68;
DR  UNIPROT: Q9HD48;
DR  UNIPROT: Q9NRU9;
DR  UNIPROT: Q9P001;
DR  UNIPROT: Q9P0P2;
DR  PDB: 5YFG;
DR  Pfam: PF04603;
DR  OMIM: 607954;
DR  DisGeNET: 29098;
DE  Function: May regulate the intracellular trafficking of RAN (PubMed:11290418). Promotes guanine nucleotide release from RAN and inhibits binding of new GTP by preventing the binding of the RAN guanine nucleotide exchange factor RCC1 (PubMed:29040603). Regulates the levels of GTP-bound RAN in the nucleus, and thereby plays a role in the regulation of RAN-dependent mitotic spindle dynamics (PubMed:29040603). Enhances the expression of SCN5A at the cell membrane in cardiomyocytes (PubMed:18184654, PubMed:23420830, PubMed:21621375). {ECO:0000269|PubMed:11290418, ECO:0000269|PubMed:18184654, ECO:0000269|PubMed:21621375, ECO:0000269|PubMed:23420830, ECO:0000269|PubMed:29040603}.
DE  Reference Proteome: Yes;
DE  Interaction: P62826; IntAct: EBI-25889861; Score: 0.56
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8IUH5; IntAct: EBI-9089737; Score: 0.37
DE  Interaction: P61769; IntAct: EBI-21675069; Score: 0.35
DE  Interaction: O95976; IntAct: EBI-21725569; Score: 0.35
DE  Interaction: Q8N307; IntAct: EBI-21729950; Score: 0.35
DE  Interaction: Q6PJI9; IntAct: EBI-21755234; Score: 0.35
DE  Interaction: Q08AT0; IntAct: EBI-21833203; Score: 0.35
DE  Interaction: Q15771; IntAct: EBI-21841568; Score: 0.35
DE  Interaction: Q8IYG6; IntAct: EBI-21846955; Score: 0.35
DE  Interaction: P20336; IntAct: EBI-21855745; Score: 0.35
DE  Interaction: Q5SSQ6; IntAct: EBI-21859636; Score: 0.35
DE  Interaction: Q8WW01; IntAct: EBI-21893659; Score: 0.35
DE  Interaction: Q14584; IntAct: EBI-21900281; Score: 0.40
DE  Interaction: P55212; IntAct: EBI-25835212; Score: 0.56
DE  Interaction: P41091; IntAct: EBI-25851912; Score: 0.56
DE  Interaction: P22607; IntAct: EBI-25854264; Score: 0.56
DE  Interaction: Q0VDC6; IntAct: EBI-25855979; Score: 0.56
DE  Interaction: P06396; IntAct: EBI-25864085; Score: 0.56
DE  Interaction: P54652; IntAct: EBI-25869971; Score: 0.56
DE  Interaction: P13473; IntAct: EBI-25873591; Score: 0.56
DE  Interaction: Q06124; IntAct: EBI-27048163; Score: 0.37
DE  Interaction: Q9UHA2; IntAct: EBI-28997391; Score: 0.35
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0014704;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005791;
GO  GO:0005085;
GO  GO:0031267;
GO  GO:0017080;
GO  GO:0044325;
GO  GO:0006888;
GO  GO:0060047;
GO  GO:2000010;
GO  GO:1903078;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0098905;
GO  GO:0098909;
GO  GO:0002027;
GO  GO:0003254;
GO  GO:1900825;
GO  GO:0042391;
GO  GO:0090226;
GO  GO:1902305;
GO  GO:2000649;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:21447824};
SQ  MEPTRDCPLFGGAFSAILPMGAIDVSDLRPVPDNQEVFCHPVTDQSLIVELLELQAHVRGEAAARYHFEDVGGVQGARAV
SQ  HVESVQPLSLENLALRGRCQEAWVLSGKQQIAKENQQVAKDVTLHQALLRLPQYQTDLLLTFNQPPPDNRSSLGPENLSP
SQ  APWSLGDFEQLVTSLTLHDPNIFGPQ
//
ID  Q9JIB0;
PN  Ran guanine nucleotide release factor;
GN  Rangrf;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10811801, ECO:0000269|PubMed:11733047}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm {ECO:0000269|PubMed:18184654}. Cell membrane {ECO:0000250|UniProtKB:Q9HD47}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HD47}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9HD47}. Note=Shuttles between the nucleus and cytoplasm. {ECO:0000269|PubMed:11733047}.
DR  UNIPROT: Q9JIB0;
DR  UNIPROT: Q9CWZ0;
DR  Pfam: PF04603;
DE  Function: May regulate the intracellular trafficking of RAN (PubMed:10811801, PubMed:11733047). Promotes guanine nucleotide release from RAN and inhibits binding of new GTP by preventing the binding of the RAN guanine nucleotide exchange factor RCC1 (PubMed:10811801, PubMed:11733047). Regulates the levels of GTP-bound RAN in the nucleus, and thereby plays a role in the regulation of RAN-dependent mitotic spindle dynamics (By similarity). Enhances the expression of SCN5A at the cell membrane in cardiomyocytes (PubMed:18184654, PubMed:23420830). {ECO:0000250|UniProtKB:Q9HD47, ECO:0000269|PubMed:10811801, ECO:0000269|PubMed:11733047, ECO:0000269|PubMed:18184654, ECO:0000269|PubMed:23420830}.
DE  Reference Proteome: Yes;
DE  Interaction: Q61820; IntAct: EBI-310252; Score: 0.37
DE  Interaction: Q9Z0S9; IntAct: EBI-20974786; Score: 0.37
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0014704;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0005085;
GO  GO:0031267;
GO  GO:0017080;
GO  GO:0044325;
GO  GO:0006888;
GO  GO:0060047;
GO  GO:0006913;
GO  GO:2000010;
GO  GO:1903078;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0098905;
GO  GO:0098909;
GO  GO:0003254;
GO  GO:1900825;
GO  GO:0042391;
GO  GO:0090226;
GO  GO:1902305;
GO  GO:2000649;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9HD47};
SQ  MEPNRNCPLFGGAFSAILPTGAIDVSDLRPVPDNQEVFCHPVTDQSLIIELLELQAHVQGEAAARYHFEDVGRVQGARAV
SQ  HVLSVQPLCLENLSLRGCCQDAWSLSGKQQVAKENQQVAKDVTLHQALLRLPQYQTDLLLTFNQPPCHSRSLGPENLSCP
SQ  PWSLSNFEQLVTSLTLHDPNLFGPQ
//
ID  Q2KHS5;
PN  2-acylglycerol O-acyltransferase 2-A;
GN  mogat2;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3SYC2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q3SYC2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q3SYC2}.
DR  UNIPROT: Q2KHS5;
DR  Pfam: PF03982;
DE  Function: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. {ECO:0000250|UniProtKB:Q3SYC2}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:1990578;
GO  GO:0003846;
GO  GO:0006071;
GO  GO:0006640;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKIQFAPHNVPFERRLQTAAVLQWVFSFLALAQTCILLFFVLLFTRFWIISVVYGVWWFLDWDTPSKGGRRGEWLRRHVI
SQ  WTYMKDYFPITLVKTADLDPQQNYVVGSHPHGVLVAGAFTNFCTEATGFHRLFPGITPYLLMLPLWFRAPFFRDYIMSGG
SQ  LIPSDKDSASYLLKNKAGGNAVVIAVGGAPESLDARPGAFTLLIKNRKGFVRLAILHGASLVPVFSFGENELFDQVDNPR
SQ  GSWLRKIQEKLQKMMGVALPLFHARGVFQYSFGLIPYRKPIATIVGKPIRVEENPNPSSEEVDKLHKIYMEELSKLFEEH
SQ  KTKYNVPADKHLTFV
//
ID  Q5M7F4;
PN  2-acylglycerol O-acyltransferase 2-B;
GN  mogat2;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3SYC2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q3SYC2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q3SYC2}.
DR  UNIPROT: Q5M7F4;
DR  Pfam: PF03982;
DE  Function: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. {ECO:0000250|UniProtKB:Q3SYC2}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:1990578;
GO  GO:0003846;
GO  GO:0006071;
GO  GO:0006640;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MWIHFAPLRIPFSRRLQTVAVLQWAVSFLAMAQCCIALYILLLFSRYWFLALLYGVWLYLDWDTPSKGGRRSNWVRSWIV
SQ  WKYFAEYFPIKLLCTAPLDPKYNYIMGFHPHGVLVVGAFGNFCTEGTGFSRLFPGLTPHLLMLPAWFRVPFFREYIMSGS
SQ  LVSSDRSSAHYLLSQKSGGQALVIAVGGPPEALDAKPGELTLQLLNRTGFIKMALTHGAHLVPVLSFGENDLYNQVNNPR
SQ  GSLLRTTQEKLQKVLGIALPLFHGRGVFQYSWGLLPHRRPIYTVVGSPIPVAKTPCPTQEQISSLHALYVAKLRELYTTH
SQ  KGNYGIPRDRSLVLC
//
ID  Q3SYC2;
PN  2-acylglycerol O-acyltransferase 2;
GN  MOGAT2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12621063, ECO:0000269|PubMed:27184406}; Multi-pass membrane protein {ECO:0000269|PubMed:12621063}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27184406}.
DR  UNIPROT: Q3SYC2;
DR  UNIPROT: A8K7I3;
DR  UNIPROT: Q3SYC1;
DR  UNIPROT: Q6ZQZ2;
DR  UNIPROT: Q86UH6;
DR  UNIPROT: Q9H630;
DR  Pfam: PF03982;
DR  OMIM: 610270;
DR  DisGeNET: 80168;
DE  Function: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705). {ECO:0000269|PubMed:12621063, ECO:0000269|PubMed:27184406, ECO:0000269|PubMed:28420705}.
DE  Reference Proteome: Yes;
DE  Interaction: O60361; IntAct: EBI-21771873; Score: 0.40
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:1990578;
GO  GO:0003846;
GO  GO:0016407;
GO  GO:0006651;
GO  GO:0006071;
GO  GO:0050892;
GO  GO:0006629;
GO  GO:0006640;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLDRDKPRQGGRHIQAIRCWTIW
SQ  KYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFANLCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGL
SQ  VTSEKESAAHILNRKGGGNLLGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSG
SQ  SWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEEVNQLHQRYIKELCNLFEAHK
SQ  LKFNIPADQHLEFC
//
ID  Q80W94;
PN  2-acylglycerol O-acyltransferase 2;
GN  Mogat2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14966132}; Multi-pass membrane protein {ECO:0000269|PubMed:14966132}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q3SYC2}.
DR  UNIPROT: Q80W94;
DR  Pfam: PF03982;
DE  Function: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By similarity). {ECO:0000250|UniProtKB:Q3SYC2, ECO:0000269|PubMed:12576479, ECO:0000269|PubMed:12730219, ECO:0000269|PubMed:14966132}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:1990578;
GO  GO:0003846;
GO  GO:0016407;
GO  GO:0006651;
GO  GO:0006071;
GO  GO:0050892;
GO  GO:0006629;
GO  GO:0006640;
GO  GO:0046462;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVEFAPLLVPWERRLQTFAVLQWVFSFLALAQLCIVIFVGLLFTRFWLFSVLYATWWYLDWDKPRQGGRPIQFFRRLAIW
SQ  KYMKDYFPVSLVKTAELDPSRNYIAGFHPHGVLAAGAFLNLCTESTGFTSLFPGIRSYLMMLTVWFRAPFFRDYIMSGGL
SQ  VSSEKVSADHILSRKGGGNLLAIIVGGAQEALDARPGAYRLLLKNRKGFIRLALMHGAALVPIFSFGENNLFNQVENTPG
SQ  TWLRWIQNRLQKIMGISLPLFHGRGVFQYSFGLMPFRQPITTIVGKPIEVQMTPQPSREEVDRLHQRYIKELCKLFEEHK
SQ  LKFNVPEDQHLEFC
//
ID  Q5M8H5;
PN  2-acylglycerol O-acyltransferase 2;
GN  mogat2;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3SYC2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q3SYC2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q3SYC2}.
DR  UNIPROT: Q5M8H5;
DR  Pfam: PF03982;
DE  Function: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:1990578;
GO  GO:0003846;
GO  GO:0006071;
GO  GO:0006629;
GO  GO:0006640;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MWIHFAPLKIPFSRRLQTGAVLQWAVSFLAMAQCCIALYILLLFSRYWYLAVLYGVWLYIDWDTPSKGGRRSNWVRSWTV
SQ  WKYFAEYFPIKLLCTAPLDPKYNYIMGFHPHGVLVVGAFGNFCTEGTGFSRLFPGLTPHLLMLPAWFRVPFFREYIMSGS
SQ  LVSSDRSSAHHLLSQKSGGQALVIAVGGPPEALDAKPGELTLQLLNRTGFIKMALTHGAHLVPVLSFGENDLYNQVNNPR
SQ  GSLLRATQEKLQKIFGIALPLFHGRGVFQYSWGLLPHRRPIYTVVGSPIHVTKTPCPTREQISSLHSLYIAKLRDLFETH
SQ  KGNYGIPEDRSLVLC
//
ID  Q86VF5;
PN  2-acylglycerol O-acyltransferase 3;
GN  MOGAT3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27184406}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27184406}.
DR  UNIPROT: Q86VF5;
DR  UNIPROT: Q496A6;
DR  UNIPROT: Q496A7;
DR  UNIPROT: Q496A8;
DR  UNIPROT: Q9UDW7;
DR  Pfam: PF03982;
DR  OMIM: 610184;
DR  DisGeNET: 346606;
DE  Function: Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705). {ECO:0000269|PubMed:12618427, ECO:0000269|PubMed:27184406, ECO:0000269|PubMed:28420705}.
DE  Reference Proteome: Yes;
DE  Interaction: P07339; IntAct: EBI-25840151; Score: 0.56
DE  Interaction: G5E9A7; IntAct: EBI-25843901; Score: 0.56
DE  Interaction: P28799; IntAct: EBI-25862183; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25900416; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25933765; Score: 0.56
GO  GO:0005789;
GO  GO:0016021;
GO  GO:1990578;
GO  GO:0003846;
GO  GO:0004144;
GO  GO:0006071;
GO  GO:0006629;
GO  GO:0006640;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGVATTLQPPTTSKTLQKQHLEAVGAYQYVLTFLFMGPFFSLLVFVLLFTSLWPFSVFYLVWLYVDWDTPNQGGRRSEWI
SQ  RNRAIWRQLRDYYPVKLVKTAELPPDRNYVLGAHPHGIMCTGFLCNFSTESNGFSQLFPGLRPWLAVLAGLFYLPVYRDY
SQ  IMSFGLCPVSRQSLDFILSQPQLGQAVVIMVGGAHEALYSVPGEHCLTLQKRKGFVRLALRHGASLVPVYSFGENDIFRL
SQ  KAFATGSWQHWCQLTFKKLMGFSPCIFWGRGLFSATSWGLLPFAVPITTVVGRPIPVPQRLHPTEEEVNHYHALYMTALE
SQ  QLFEEHKESCGVPASTCLTFI
//
ID  Q755A9;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: Q755A9;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MWREEAREQLRRGRCCFAAASVVSTAKHNKSLGNCTHGSGVMTEAEGILNNVWDAVDSKQQGFIYAKDMPDLVGRFGQFL
SQ  AQSLTSRANDEAIAAFASEKPFYKLDKEQFKSTFQTLVGTSLQTAVELAGHGEPRPRLFGAIRRASATGDEQAREELERK
SQ  SAELSRVRDELDEWKSKYQFLEREFLFYQTHHENSVDSTQHEFIISEMKRTIEEQTRMIGQLRRQVQGGTQVLARAGKRA
SQ  SPVDVFMYVSRQGLLLLMRMPKAAFLLLLLGYFVWYTVMGGAVQGPDPSVALPEPPKQPWWEQNNIISALYWYLTDTFEP
SQ  SQRINDTVNDNYNSLFGL
//
ID  Q6FS52;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: Q6FS52;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSEVDVPELLFERVWLQVDRDRDGFIYAKQMPSFITQCEQVIKDTVNTNKTDFHMTRFKNRLKLPLLPKLHMDLIDAFAK
SQ  ETPYYKIYKESFSDMLNKLTGNNFSTVINKIFEDCDGFPASFISALEVKADVKSSPRSKADSLGSPIKVDLLRNLKPQEE
SQ  PETPRRINRKYKSLELQLESMKRELEDKEKTIMNNERNLTELRSTISKLKEKYDLLSEEYEQRHIHGGNNGTAIKHDVVI
SQ  GELKSRLQEQNRLIRILQEQIQFDPQLKRETRVHDNKSKNNTFNGAIAYVIPFLLFIFVIRSLITKEDIGDATMALPWWE
SQ  RNNLASRLAWYFRDVFSNDSAKFLESDAYDKVFGIH
//
ID  Q6CS73;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: Q6CS73;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKQISKSTQYKPSKSTLVSAKLFSMNRTESTRLLDRAWSVLESGSDGYVYAKDIPEIISFIDRELPSKLTTQSNDKVIE
SQ  SWVNNDPMKTLSKEQFLEAFSMLVGTSFDTAVQIAMQSDILTPTRRGASLFGSYRRSSNDLEQVLPAEQIKALKRELQEW
SQ  KDKYTFLEHEFQFFLSQEKKNPEVIDNTKHEFIISELNRKLREQDEAIEDLKSQLDYGLVPELKDKTNWIKALQRKAYNY
SQ  LLPKILICLLLLLLYYCLAAKILFTKSSSTDDVPSFIRQQSWWERNKILSRIQWYFKDRIENNVVRNSSEVIQNYNSVFG
SQ  IH
//
ID  C5E2E7;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  559295;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: C5E2E7;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDTERHATLLLDLVWPEVDEKAQGFIYAKDFPLVVSRMEEILNRGKLERDRAQLVSETGREILRKFGSDQEFFKVYKEDF
SQ  RELFDGLVGTSFKSAVKSCAGDGVLDRLQDSQAVDGIQDEKTSSHALQEEVMRLREQVRVLSSKNDEKDREITARDEIIA
SQ  DLQGKDASPAGSPRSLQRMRTLQARVTSLEDELSFRDEVIREKDRELLNLTKRVGEFKDKYQFLEREFQFYKGHREQKSP
SQ  DSIKEATRHEFIISELRRKITEQSEIIGQMRMQVEAKPGALHPQGIGSTAGLPLNLPLRLVLRLIIGAILAYLAFDIGIR
SQ  SLKAVGGLFGSSSPATLTPKSELSWWEQNTLLSKLLWFFKDLFDTYNLDAGRDEVVSANYDKLFGV
//
ID  B3LHE1;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  285006;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: B3LHE1;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKSKNTEGAGISTSRKKLTESPIKLLSRNNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  C7GW39;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  574961;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: C7GW39;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKSKNTEGAGISTPRKKLTESPIKLLSRNNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  A6ZUA4;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: A6ZUA4;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKSKNTEGAGISTPRKKLTESPIKLLSRNNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  C8Z8H2;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  643680;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: C8Z8H2;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKSKNTEGAGISTPRKKLTESPIKLLSRNNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  E7KCH6;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  764097;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: E7KCH6;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKSKNTEGAGISTPRKKLTESPIKLLSRNNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  E7Q3U9;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  764102;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: E7Q3U9;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKNKNTEGAGISTPRKKLTESPIKLLSRKNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  E7KNG0;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  764098;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: E7KNG0;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKSKNTEGAGISTPRKKLTESPIKLLSRNNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  E7NHN2;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  764101;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: E7NHN2;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKNKNTEGAGISTPRKKLTESPIKLLSRXNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  P53159;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:10397772}; Single-pass membrane protein {ECO:0000269|PubMed:10397772}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10397772}.
DR  UNIPROT: P53159;
DR  UNIPROT: D6VU69;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000269|PubMed:10397772, ECO:0000269|PubMed:10654940, ECO:0000269|PubMed:11952896, ECO:0000269|PubMed:12399372, ECO:0000269|PubMed:16436507, ECO:0000269|PubMed:16923827, ECO:0000269|PubMed:1869587, ECO:0000269|PubMed:9060463}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-3765215; Score: 0.35
DE  Interaction: P40457; IntAct: EBI-2212931; Score: 0.40
DE  Interaction: P47069; IntAct: EBI-2212852; Score: 0.59
DE  Interaction: Q04477; IntAct: EBI-598164; Score: 0.78
DE  Interaction: P47149; IntAct: EBI-599182; Score: 0.37
DE  Interaction: Q12365; IntAct: EBI-1007115; Score: 0.72
DE  Interaction: P53930; IntAct: EBI-1007124; Score: 0.37
DE  Interaction: P36094; IntAct: EBI-2133025; Score: 0.35
DE  Interaction: P52919; IntAct: EBI-2132982; Score: 0.51
DE  Interaction: P14832; IntAct: EBI-2882919; Score: 0.00
DE  Interaction: P32472; IntAct: EBI-2883301; Score: 0.00
DE  Interaction: P38265; IntAct: EBI-2885494; Score: 0.00
DE  Interaction: P27692; IntAct: EBI-2888169; Score: 0.00
DE  Interaction: P11484; IntAct: EBI-3781150; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3799382; Score: 0.35
DE  Interaction: P53159; IntAct: EBI-3870981; Score: 0.37
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0016020;
GO  GO:0106084;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0005816;
GO  GO:0140444;
GO  GO:0005198;
GO  GO:0000741;
GO  GO:1990608;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKNKNTEGAGISTPRKKLTESPIKLLSRNNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  E7LUD2;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  764099;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: E7LUD2;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKSKNTEGAGISTPRKKLTESPIKLLSRNNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  E7QET1;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  764100;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: E7QET1;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHK
SQ  EEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKSKNTEGAGISTPRKKLTESPIKLLSRNNIG
SQ  KALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQ
SQ  KAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL
SQ  AGVLPYIRKYVYAHDTPSQNSRLQLSWWENSGILSKIVWFFEDQTDLETEYRSNANVDDAYSRVFGI
//
ID  C5E006;
PN  Monopolar spindle protein 2;
GN  MPS2;
OS  559307;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000250}.
DR  UNIPROT: C5E006;
DR  Pfam: PF17060;
DE  Function: Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0071988;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDFDKSSSSLVLDLAWNQVDKKNQDFIYAKDFPALIMSIEEILSRGQQTPLAFLSNTGKSVIDTFAREKEFFKIYRDEFK
SQ  EIFHGLVGKTFKDTIEGTNVSRSVLDEQGQEPDVSTTPTRQQRSSPRKVNRLLKNLETRVASMKDELKFKDEILAEKDRE
SQ  LIQLTRKLSDYKDKYEFVQRQFSFYKDHGESPRRNSSESEQLNLEQNASTKHEFIISELKRKLQEQTLAISNLKEQLQRG
SQ  EGAGVLYTNYSKRYNPLHNDGPMVLVLATLVFLTIILLIGSMIWVTGGKDDSNSFSQYSWWENNSLLSRIGWFFRDWSDT
SQ  GVDYVNFEPSSDAYERIMGIRRI
//
ID  P47069;
PN  Spindle pole body assembly component MPS3;
GN  MPS3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:21518795, ECO:0000269|PubMed:22017544, ECO:0000269|PubMed:30141044, ECO:0000269|PubMed:30417519, ECO:0000269|PubMed:34586062}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:12486115, ECO:0000269|PubMed:12493774, ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:22017544, ECO:0000269|PubMed:30141044}. Chromosome, telomere {ECO:0000269|PubMed:32967926}. Note=Localizes to the spindle pole body half bridge throughout the cell cycle (PubMed:15282802). Relocalizes from the spindle pole body to the nuclear envelope in meiosis, via the interaction with HTZ1 (PubMed:22017544, PubMed:21518795). The cohesin component REC8 promotes localization on nuclear envelope in mitotic cells (PubMed:30417519). {ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:21518795, ECO:0000269|PubMed:22017544, ECO:0000269|PubMed:30417519}.
DR  UNIPROT: P47069;
DR  UNIPROT: D6VWG1;
DR  UNIPROT: P47070;
DR  PROSITE: PS51469;
DE  Function: Component of the linker nucleocytoskeleton and cytoskeleton (LINC) complex that regulates telomere movement and meiotic recombination during meiosis (PubMed:17245108, PubMed:18585352, PubMed:32967926). Connects the spindle pole body with the nuclear envelope through its interaction with MPS2 and mediates meiotic bouquet formation and rapid chromosome movements in meiotic prophase (PubMed:16923827, PubMed:17495028, PubMed:22017544). Functions as an integral membrane anchor for telomeres and is a nuclear receptor for the SIR4 pathway of telomere tethering and gene inactivation (PubMed:18039933, PubMed:19390087). Essential for nuclear division and fusion and required for the first step of spindle pole body duplication in G1 (PubMed:12486115, PubMed:12493774). Functions in sister chromatid cohesion establishment (PubMed:15355977, PubMed:16682351). Recruits double-strand breaks (DSBs) to the nuclear periphery for chromosome healing (PubMed:19390086, PubMed:19217407, PubMed:20016273). {ECO:0000269|PubMed:12486115, ECO:0000269|PubMed:12493774, ECO:0000269|PubMed:15355977, ECO:0000269|PubMed:16682351, ECO:0000269|PubMed:16923827, ECO:0000269|PubMed:17245108, ECO:0000269|PubMed:17495028, ECO:0000269|PubMed:18039933, ECO:0000269|PubMed:18585352, ECO:0000269|PubMed:19217407, ECO:0000269|PubMed:19390086, ECO:0000269|PubMed:19390087, ECO:0000269|PubMed:20016273, ECO:0000269|PubMed:22017544, ECO:0000269|PubMed:32967926}.
DE  Reference Proteome: Yes;
DE  Interaction: P06704; IntAct: EBI-2212835; Score: 0.59
DE  Interaction: P40358; IntAct: EBI-1560984; Score: 0.51
DE  Interaction: P17214; IntAct: EBI-390285; Score: 0.57
DE  Interaction: Q12692; IntAct: EBI-390480; Score: 0.67
DE  Interaction: P40857; IntAct: EBI-856594; Score: 0.00
DE  Interaction: P47007; IntAct: EBI-861529; Score: 0.00
DE  Interaction: P43605; IntAct: EBI-1553262; Score: 0.68
DE  Interaction: Q08955; IntAct: EBI-1795681; Score: 0.50
DE  Interaction: Q12366; IntAct: EBI-1795681; Score: 0.50
DE  Interaction: P53159; IntAct: EBI-2212852; Score: 0.59
DE  Interaction: Q06616; IntAct: EBI-2342813; Score: 0.37
DE  Interaction: P32562; IntAct: EBI-2342907; Score: 0.37
DE  Interaction: P47069; IntAct: EBI-2343343; Score: 0.37
DE  Interaction: Q03362; IntAct: EBI-2343676; Score: 0.37
DE  Interaction: P28791; IntAct: EBI-2344047; Score: 0.37
DE  Interaction: P40504; IntAct: EBI-2344203; Score: 0.37
DE  Interaction: P40348; IntAct: EBI-2346227; Score: 0.37
DE  Interaction: Q12743; IntAct: EBI-2347098; Score: 0.37
DE  Interaction: P53966; IntAct: EBI-2347429; Score: 0.37
DE  Interaction: Q12404; IntAct: EBI-2347465; Score: 0.37
DE  Interaction: P06197; IntAct: EBI-2347992; Score: 0.37
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P52919; IntAct: EBI-7042905; Score: 0.35
DE  Interaction: P36049; IntAct: EBI-7064638; Score: 0.60
DE  Interaction: Q08746; IntAct: EBI-7064638; Score: 0.57
DE  Interaction: Q02199; IntAct: EBI-7064868; Score: 0.27
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005825;
GO  GO:0016021;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005816;
GO  GO:0005524;
GO  GO:0043495;
GO  GO:0034087;
GO  GO:0007129;
GO  GO:0000741;
GO  GO:0045141;
GO  GO:0007064;
GO  GO:0006998;
GO  GO:0000743;
GO  GO:0030474;
GO  GO:0031509;
GO  GO:0034398;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNSNEHRREEAGAANEQMPYNKAVKSAYADVLKDKMNREQEISLRAIKKGIYTDGGETDNYDMDKENDSAYEMFKKNLD
SQ  FPLDQHNDDDDDDPYIEDNGQETDGYSDEDYTDEADKSFIEDSDSDSYDLESNSDFEENLESSGEAKKLKWRTYIFYGGL
SQ  FFVFYFFGSFLMTTVKNNDLESHSSGATSSPGKSFSNLQKQVNHLYSELSKRDEKHSSELDKTVKIIVSQFEKNIKRLLP
SQ  SNLVNFENDINSLTKQVETISTSMSELQRRNHKFTVENVTQWQDQLVKQLDTHLPQEIPVVINNSSSLLIIPELHNYLSA
SQ  LISDVIESPGIGTAGSAESRWEYDLNRYVKEILSNELQYIDKDYFIQEMNRRLQSNKQEIWEEITNRLETQQQQQQQQVQ
SQ  QDYSNVPQQYSSILMKRLIHQIYNSNQHQWEDDLDFATYVQGTKLLNHLTSPTWRQGSGVQPIELLTDSKQSSSTYWQCE
SQ  NEPGCSWAIRFKTPLYLTKISYMHGRFTNNLHIMNSAPRLISLYVKLSQTKEIKALQTLANQYGFGQHHKRDRNYIKIAK
SQ  FEYRLTDSRIRQQMYLPPWFIQLKPLVRSIVFQVDENYGNKKFISLRKFIINGVTPQDLQIIENNEFPVLLGDTPEYGVT
SQ  QNTDEGKRKVLLSKPPYASSSTSTKFHPASNVPSFGQDELDQ
//
ID  M9MRD1;
PN  Muscle-specific protein 300 kDa;
GN  Msp300;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:22927463}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22927463}. Note=The recruitment of Msp300 to the Z-disks is mediated by the interaction with sls. {ECO:0000269|PubMed:22927463}.
DR  UNIPROT: M9MRD1;
DR  Pfam: PF00307;
DR  Pfam: PF10541;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS51049;
DE  Function: Component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (By similarity). Collaborates with Klar to promote even spacing of the myonuclei at the periphery of striated muscle fibers by mediating a tight association between a nuclear ring structure of Msp300 and the plus ends of a unique astral MT network (PubMed:22927463). In addition, is essential for anchoring nuclei, mitochondria and endoplasmic reticulum (ER) structures to the Z-disks (PubMed:22927463). {ECO:0000250|UniProtKB:Q8NF91, ECO:0000269|PubMed:22927463}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VZ44; IntAct: EBI-245063; Score: 0.00
DE  Interaction: Q9VNH5; IntAct: EBI-256997; Score: 0.00
DE  Interaction: Q9VYK7; IntAct: EBI-258653; Score: 0.00
DE  Interaction: Q9VGS2; IntAct: EBI-264122; Score: 0.00
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0019901;
GO  GO:0007015;
GO  GO:0016477;
GO  GO:0007303;
GO  GO:0051643;
GO  GO:0008335;
GO  GO:0060361;
GO  GO:0007523;
GO  GO:0040011;
GO  GO:0007498;
GO  GO:0034453;
GO  GO:0051646;
GO  GO:0007097;
GO  GO:0051647;
GO  GO:0006997;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MADSGGPGSKHMDPTTIDAGGGGAGAAGGDDVPPVPAVRRRRAHEQKSSREQVLEEEKSQQLETSTVTRTYMKTITTSLT
SQ  TSSSSNVEEFILGEHAAGAAAAPSPNQQRLRQKVAQYEKVWSDGSSPVKRPAEQSSDELRLTDDQDEYDAENPFEIDVHE
SQ  IERRLRQERQRGLAEAEAAKLAFQQVQLRHTTPPRRVEVTSDQVASPFNVTLRTTSRMSPGAEHGNVEEHLAPFNVTLRT
SQ  TRRTKKKEFKELENFLEGERTVREVPSADGVRTIITSSMTSDGGYAEEKIYRHGEGYVSPRDSPSWSRSSYSSERSSVTP
SQ  PRSVDLTAGGRRILIKLEQESELTEENQTRDETDLSFGRQEVAMATGNIDITVGGSNPRRRLYQQTTVQVGGGNRTSPQD
SQ  STPQRPRDLDLAGTTKTMLTSTPIGTKEQPQTGPKTLVSPAATCQLRGSSTEEPRKIVSHKTITSTTTKSTSSSTSATSS
SQ  SSTSRKLIETSPVVVGKIAQIRTGKSNASDNDIDIDNDSDTEGRPASSIVIVSTPTRPTTPATASVSASAVTPSASISAT
SQ  AAHALSGIGTFSKSLRQDYQTLATQSGRSNESPSDQEYQEFQSTMASINYARSNSQYDSHIKEKREEQERVQKKTFTNWI
SQ  NSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKRIKLVNINPADLVDG
SQ  RPPVVLGLIWTIILYFQIEENSRNLEYLGHGIGGSVSSLDSVGNQKHGDLKAEKWKQGARKTLLNWVTNALPKDSGVEVK
SQ  DFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDVDVPKPDEKSIMTYVAQFLHK
SQ  YPEPKGASRDQSHVQQEADELRRFLVEKTTEYEPMVMMSSFPRDFGEYLLARSEVDAHLAAYNRLKQLIESQSGFLQVSR
SQ  QSWEEINELWQRLQYQMMYWLWLLDSELPGDFGTVGKWLAEAEKLLMDNDIPNAMNEETAAVISRKLEEHKLFFADLPRI
SQ  LAMFDNAKRSPVAQQIPLEQLRNMERRLQEVGPKAAERRIRLKFLEHKCCLIAFLNLVENKMRGWTGKYGHEEKVAQQLE
SQ  QYKNFVSRNKIFQEFQKAFVDMQQVVEEYKRDGNVPRKEINDIDRFMYETEERWKRVSMELKCCQNSLEEVVNCWRSWNQ
SQ  LAPTCEEWLQLAEQKVNQSEDERLDFFQDIPVWKDKFDALASSANYLIASCEEPIAQQLRQRHGALSERFERLFANTKQY
SQ  MHAGDIIRSRQEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQSLIQDLSR
SQ  DEVDKMMKLLKQEKESLVRIRAQLPAKLHLFHQLQIQQESLEAGQKEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKT
SQ  YFSRTVYYRSMLESKNKVFQNLLKAVSSDDKIDTAPASQQMQQLNERFNYVIQNAQQWEQRLDSAAGGWSNFKDNERVVS
SQ  EWLTQAESMLVEKHIESKTTIETQKYFFEQVNDRWMNDLVQSAQQLLTTLPAQEQPAVVHSVEQLQSRWKNVLSQAPLHL
SQ  LKLEFRLDENAFYQSLKDVEKELQLEQQALNRNEDVDSILQRNQQFLLQQDVVPRLERCLQNMQRLAQAHRQQQPGDISL
SQ  DQAYDNAKSQWQLLSNKLGDMRQTLQQIPAQWQGYHLKFNDMVDWMNGVDQSLKNIVNEVNTMEEFEKEKVVFQKICQDA
SQ  DNKREDMKWLVKTLDSLLSYATEDEANLEQKKLEDLIARYKNLIPTIEITMVKTEVFSKCYTYRREVHEVVCLLSKVKDQ
SQ  TANIPAPDSLDRVNRLIEEQQYAINQLDHQRPHIMSMLQRGRDLIKDVHAPAFVNAEVKNLETGWNQAYTETSDKLQALK
SQ  GTQAVWSEFVDQKNDIFSMLQTAETELRSLTPLQTDPKNVSQDLKSKRDLNVQLQQASHQLLPKLHALKSELAPLAAPDK
SQ  RPILEKEVTEVEKMFFNTMEHVKDRVGYLEDYSAKWNNYKTRLAELQEWANKVAPKNIEALQSEDLTPEERVVKVQAFKR
SQ  ILGDRMKQLDLLAADASELAPKEGNIAEAKRLKGEITKLQEVLSAINRNVDHQAQAVQEDLVNWQQFQAGLQQIKPAVEQ
SQ  SEVKVNNVVSKPISLEEAVAMQQNAQQFETQCQEQLDKLHGISNISHKMLCKTNAPDELDAMHSRWTAVHENAKQASAKL
SQ  EKLVANWKSFDADAAKLEDWVGQGEQQMSRRPAVLNTPHIDKLEKELVKLKSFNNEISQQQAKLVTLGQNADQISLHLAP
SQ  EGAAALKDRVNQMKGKLQKLSEATRGHINEVSDAIISRQDFNAKLVNFSNWMEQLRNQVTQVEEINPERVETSLHVIHAL
SQ  LQEHADKKPSFNAIYDEVKQLALGATPEESNALNDAYTALVVNYQNLETNMLQKKAALEKWTELLGWKNDTESHLNYLKH
SQ  QLDKPEGPAAEELSKVIDEIDNLGQGIGYWKGQAKEIDENPAIQLRDALSRRPLIATQIVNDVENKLENLKLRSQSQQQQ
SQ  IQQMTVRKDKFHALEHNFGQALQENRAKLDEILRQHPTLNNIDQIIADLVALNDALKYQADLKNRIHDEGSLLMREDIAS
SQ  MPAIQESLLIMDKNYDSLQNEIADRIQKYNLISQALREYADSKDKFSKELKKAEDLYNAIPQQPRDETELHQASEKTRKT
SQ  MEQLRKSKLSLDELERRGNNVGKLFSAIGEPIPQEVPQEVTAAKQHWQDLHDKTAKNAHVYETEAVIWSQIEDAKKDLLP
SQ  WLSETNQGLCDAADNSIEIEFGPMRLSKYRTELPSYQALKDSIVEKTNDLVKINKGAEIPALSALNKLLSEQFAEVNNNA
SQ  DRLSAITTSFNDQEQELRRRSKEAGERVSKLREQLIKCDDMSGDNNKIMERLQQCRALRGELDNSGNEIDNIKQKVDELR
SQ  NLYPTFSESIIPKELNNVQKRYENVDLYAKKIESSLLQFLKKFHADKVGMLKRIIATQREKVAWCQPESSSDKYNLDVKK
SQ  SSLQEVSKSIDDCKARHAETLKSLEMLKAVESPQNLAELTSDAELLRKDMQALQDSFDQIKGILDENVDLWSQYEQSNEQ
SQ  ISNWLRDVEGRVKAETSSQVNLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEARIGQFVTHLVQRYQAVS
SQ  KALTSYIDKIRGAQLSNANFAKAAKDFNEWFGDAKIEFQELARMGSPGSSSATAQQLQTVKNYIKTFDNGQILLNNAVDI
SQ  GEALYPVVSPDNRERIRADLRQMREKFDYLRDEANAFMQQVEGVLIQKTSIEESYTQVSHYLNESKAKVPTTDELYPTLA
SQ  TKKAALQNYKTQLQEITLHKNALKQLHDKAVTLCDDESERKTDESIQEYNTLSKKISDRITTVGNHVVKHEAYDQVLEKA
SQ  QDWLNTIKSEAIDILNETTFEKEGAEEKLLVVENLLQHKPEGDSIFDTCHKLLETVLTQTHPSGHPALLKGFEEPKQSWE
SQ  DFMTLCQDSLVKLKQLCSKWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQ
SQ  GREIEGETDLNLKLSRLNTRYQTLKNLCKESIAKYVNYVKDHESFDKDFDSFKQNLQSSVDELAKTNEIVGDQSVLQDQQ
SQ  NKLREMSDKRILDSTLFEGLIDRGEKLYGHTSPEGREIIRQQLRALRTLWDNYTDDLNSATQKIDQCLLQFNEFSIAQDQ
SQ  LTKWLKDVDKAMQSHTEPKTTLQEKRAQLQNHKLLHQEITTHNVLVDNVCDKAQILVDQIKDNSLNVYLTSIKQLFQSIV
SQ  QKSDEILHNLDDCVQKHNELNNALSSAKTWISNEKAKLLECDDAYGEKADIKRKIETLGQLAQNKPQAMKIISDIRDLFE
SQ  KVKATTSEKGNEVLDKEIEELETTMKSHFDDIEGIEGKQKDVLAQWDKFEKALEELTKWCRSAEAVFREQQLQSTLHEKV
SQ  EQLEKYKIQRELILQKEKEIDAFGDAAHALLNNCGADRLKTLTTQITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYNE
SQ  VDLWLQPIESQMAKVLLDEPTQSSNILQVLLSEKEQAESLFAALNAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEG
SQ  IRNLEKRQEAQGVQLSSYQDILNQTVNWLDQVEKLIHNENPASWTSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAA
SQ  LLGSAAPANADEISKAVAEVNKRYDQVGQDCAKLVADLDGAFDVYQQFSELQKAQQDYQKNLWDRLTGYSDYSGNKAALQ
SQ  ARLQKINEIQDALPEGVAKLKSLEDHIEQQASNIPARSKEVMARDLANLHADFEKFGASLSDVKSGLENRLQQWNDYEIN
SQ  LDRLITWLGEAENSLKNYNLKSSFEEKEEQLNGFQSLAQNLRQNEADFDKVKDDTSELVQSSGETRIAVNVQQVSSRFQS
SQ  IQATAKEILKKCEQAVQDHGHFNDKYKQCADWLANAQARYDDCCDLSTVASRDDLLKKQVVIQELLAQQPTATQLLNSTV
SQ  ELGEKCYGSTATEGREAIRSQLDDLTFDQLFDNIAITARKIQDKIAKWSGFDEIADSLKSWLDETENALPADIELKTTLD
SQ  EKRNKLQTYRDILNDINNHQVELGNLQEIAANLPEKTELVDQIIKDISDRFGKLQKRAQNYVERYEGIVSAHQQYSKAVM
SQ  DAQEFIDATLNTVHYWGDLDLEQISLHTNLDRLKNLKASLADEFPRVDQVRALGEKVIPGTVDVGQVNIKSQIDTTQQEW
SQ  ESLLTTISSTIEAIEARLQHWSEYEQLRDQCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTE
SQ  KAQTLLKGPSSNRASGPELVTKYQQIFHKVKELNNRWQQYVTSHEDFDNAISDCSSWINEIKEKLDYCSDMSSMSPKELD
SQ  KKLATIQDVILLKDEGSARVLKILEQAQHVLANTAPGGHEAINKELTDLQDLWSGIALRIMDVKSNLDDSITQWSGFLDQ
SQ  VQNVRKFNEWLDGQVKELSEHQTTMTEKRAQLDRVKSTEEKVRVEKIDVDALKIQAKEMIASGQQSQAAFQAQKVLDTFD
SQ  ELFAKTQKLLSHRQDQYRDHRLFKEAYDDLVSWIGRAREKFPSLKQSSLSDKLAIENAVQATEALLNKQAQGELLVEHLV
SQ  HTGEVVLASTSAQGQEIIRNDIRALRDSFEGLFREINQQKENLEVTMVQWRAYKEEYERLMEWLQQIDILVKNHKLNLCP
SQ  NLPEKEKQVADMKEVMSRLEKGKDDIDKFNASAASLLKSHLDTYVNNQLRHLSSVYQVQVNLAKDVLKKVETNRDQHREY
SQ  DANMKSAKDWIANAKATIQSAGEGAGSKEALQRRLEQIQDLIRNRELGQNLVHTAINNGEKIIRNTRSDGRDAINTEMKE
SQ  LQTEWDRLVKKMSTAKVQLETNLLQWADYSSSYSQLQQWITDREAKLQQACEQKIVKSKRGQPGLSSGLSERKANLRQTN
SQ  NIVQDIVSFEPMIQSVTSKASVLQQGAPGTEISDKYENLTKQAKDLYEKQKNTIESYQSLIDAGNEFATWLRNAKERLSK
SQ  CSEPTGDKQALAEKTHQLKILQGELPEGAQKLKNALEQGEIACRSAEPEDCEIIEQEVALLQEEFDAYREALNKAKDYLE
SQ  VGIVKWSDYQDQYTEALEWLSKTEALVQSYNKLQDSLIQKKVVLEQFQGHLQTLFDWQKTLDDLNMKAQVLLETCSDTRI
SQ  SNAIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLSECEQIPGTLNEVQIKLNTVKNLRQGF
SQ  ETGQNKLRYLLELKEKVIMNTEQNGAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEP
SQ  SVKTSDEFLNDLSEKRAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLDLKDFQPGLTKFDDLQTQVNKIIESLENQVN
SQ  SHEKYKQAYNELQDWLRRTRIEVEQCADCHGEKDQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIATSGSEGQDNVA
SQ  QEIKHLTSEWETLQTISRDARSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAEK
SQ  DNVEDLNDNCELLMEQSACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDHTEFLNYKKEMDAWIEKAQQVLDDCST
SQ  DGDAAIIAQKLDTVNSLASRLPEGQHLLALVQDAYSKASNITPEDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQAQN
SQ  RWNDFAANKDKLEKWLNETETTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDLGTEVDAVNRLQSR
SQ  CDKLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLLQISFQLMAHNSLFISNREQTQEQIKQHEALLVEIQKYQTNLDD
SQ  LNAKGQAQIKRYESSTPAIRPTVESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDSIMRNLETYEPIIQTEL
SQ  DAPATSLELAQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRPSSPLETAMQAIPERELIVRAKLEDLLDQKPPP
SQ  KTRSSTGGVSTDDDKDEADVEIQVELSDVNEALLDPIAHERVKNYRRIVRLNSAHVGKLNELVAKVQSHLGGLTASVSEL
SQ  EQQQKQRAELQDWVKKQQSSVSDWMMRPCKLRPEAAQQELVSMNDLLNSIGDKRSQLMLEMTGSLGDEDTDLDDNIDKLE
SQ  SELMDAIAKKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSGLNCAQKMAAINEIKNEYELQGHPKIQELKGKAAQ
SQ  VAEVISNLDGQQVEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQAPKPLGYTPKDAE
SQ  ARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPVEYSQLESALRNLNTENRNLSGVLKAELDRALEASKARKSLEND
SQ  LDKARQWLKTKISEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQAANIMKDCDDADKAALQQILDEI
SQ  AADYQTLKDESSKRGKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKGGLIN
SQ  DVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRLAECSQFLGNIQQKLRELNRP
SQ  IGSRIEDVQDLLGAYEGILKELKDSKSKMGDMQMDDLPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIALINEIIA
SQ  FIMKYTDVIIDIENSPDSLEDKINKYDDVIVKIQECEGVLASANDKGQKIASEGNAADKNSITEQLQSLKNQLQNLRKAV
SQ  ESQRQKHQLQLESHKKMAAELSEILDWLHSHEGAAKSRPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEI
SQ  GMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRLEYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKI
SQ  FFGNEAPIRNLVHKQIQEAADKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKAT
SQ  IERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQ
SQ  RRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTF
SQ  LGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVYDEHIAQTEQ
SQ  LLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEV
SQ  QRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYERFTLVKTNGQLIIENCRNSEEKTLVQTTIDQLAASLAQVRGWL
SQ  DEKKQAVGDSLDAWTRFMNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLNDYVTSVKSIKPIVKHLSEMDKELEHIGQ
SQ  VTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKT
SQ  LADINVQKTKLRLSIEKLEVHFRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQ
SQ  EEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQSSLDGMLHGLKLIQSNLEVHERDAIELK
SQ  NQAKKLPTDPATERLLNDTVDRIDLLLRRTQQGITMIANAMHGQKKRQQEIDEYQQHLLELEQWIIEVSAELASFEPTSD
SQ  SSTDEQVLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQSHPDVSPLADTLMEQLQSIITILREQVTVATKRIFTIEKR
SQ  IVDLRKAKSEEAQRQRVLADSLIKPPTEAPASPEAHESIESNENTIDSSSMPEEEIKPTGVYVETQTSLSLQQPPVQVVT
SQ  TTTVEAQTSFKEPAVETAEVALQTQKERSPTENIMVTQTVHHGQETIQIDTTRNKDVPDEPEDVQIEARYHQRPKGDVDR
SQ  ATELILKNVPQAFETTFVEPDETTTEVIVGPDGTKHIVLKKVTRTRQQVVQQQQISSIETISDSDGNIEVHSTGQINLEN
SQ  VHTTDTKADPEEGSVHTVITQQTRGAVVDSTQPEGVILQEFETEPTIETYEEVIAPGSQAQLIPMQPGDVQTQGTIRAVV
SQ  QQVTRKVIRKTRKIIKRVVIIDGKEHITEEVVEEPEEVEITEEETAPHINVNIVRTVDGKVVSEEEFQRMMQEPGVLIEE
SQ  VATDLQKPTAEPQQEVFDIESTQVTTTTRTTTATTQEQEQPEQQTQPTTTETTKEAPVELPAPQVDVEQPVVVATTSPVH
SQ  VPTADVVEPKDSSPTSTTAAVVDVEAVVEDINEIWPLEHHLKPTNIDFSQHVEELAAPAAVTAETEASMPVEEIWPTSPE
SQ  TGNSLTLEQYEFEPQSPHEESTKSDLVKPQETEPQVVAETKPEGITTGSITITKTTTTITSSTEVPEETLVQNVPADEQQ
SQ  PPANKIKTDIQSFLEAEQTLAAALKEQSSTPTGASVAEDVQTQPEEIVLEERTVEISTIKTEENQQEPVIVEEVKSLPVE
SQ  PEPVEPELEEVAIAIVEQTEEKPEEPVIEKQPASGPIDLRAATQLFISGEAAASTAPQKTFQISAPSLEDNGAGVLKVVL
SQ  GKESTNEEDTAAPTTGKVSMTIIETAAAPAADAKRRRKKKKRRDTKHEEELEQEQETEPEPVAAVKEPEVSSDVPVSPED
SQ  SPRDTVRHESIVEISPDSDLSSIEIDTKVKIVEDAVVSSPSESPRTPMVELVIPTEVVELALVEDEEQQTTPRIPSPTEK
SQ  SEVEQDIKSVQTSPQHQPKLDETAVQTSLEVQPDNQENESQTLIVEITETEAQTTPRSEEQSVAVEISTTEIQTDVSGQP
SQ  AETVEISSQTTVTTTIEKELQTTPKDSPRAPEAGSSDVVESLVQDLVKDMTTDLPVRTSEQSTVTETTTTTETHVQTTTP
SQ  EPREQTEVIKPETAHEETSTVELVQFADGEMQTTPPGDQQPASLDDSSLTATSISVSEPYELEVKTTVAIPADSDTSVAE
SQ  PTVYEYTQTMQLPKQEKKSKKDKKKKQKNVPEVEQQLPEDQQISVTVEIAPELLSESGIVVSTNQQIEDVPHVTPVVDTP
SQ  IESEEVETPKAQRVQLQITKTTVYDEYPDLPVHITEQNKVLIASQQSKRSGAGPTSSAVTIEEVGSPTEELVVPITPGPD
SQ  NLSGEPHNIWFSATTSVDKTPIELSQALIMSESLQHYPGQQKLTQEPILISTKEAIGDRIKQLKQASPQQATPLSNVLHL
SQ  ATLSEQIKELPTEQRILEVNEGLKDLDVAIKNGDKTVIQTTVITVIEKVSTWLETIEYRVYLIRQNSNEGPSEEKLDNYN
SQ  QLNDELSTIKQNVVQLERQLSKAEPEPQLLQCVDSLKEHVDAVEQVTQQNQVQDSNDLDKWHNFEVLLYNVSSVLADLQQ
SQ  SYDLLINQEYPLSAKLAQLDELEQQHEAAQQQLAHLCQNARAFQRDFPGKKMPQDVHNAFETSKNIANNIQAERERVLQL
SQ  QSLAEEYEQTLKEFTKITVLADKLVESPIVSSSLEQLNNEVQKQRKFFVNLSHCRAMLESLEENIDSETREKHSELHKEL
SQ  YNRATSLLDKASERSSKLVQAASRWTVLEKGMRDELQWLQVAQQRVPDLSAVTSADYDQYTTLYQSLSNDISHHYVKMTQ
SQ  LSGIANKLQLLVQAPNLVEETNEALIVLLKLREEVALYLHRLLVFKEIWVQYEQQTDKLEAFVREAEQELRNIQIPSQPT
SQ  HQPIEHMRQFWEIKARFELHNNVRTDTGLSFEKSLQVIPLADEMLQRQFHAQLEDRWQAVAQAIELIQHNIVECLSSEDV
SQ  PADEKLKMVERELQEIYLTMTSMKGVIKNEEELCLYIERVQVLRTRVGFIGNELGRIGLQEPAIEPEKVGELFSLSHKIS
SQ  TQIAEELEGASVLRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEELVISWQEIMRIRQML
SQ  HTLPMRLKMSVSPVKLERDISQLQDDHAFLESKCTNIMAILRSRLAVWLRYERQLELVHGSVQETDFMMELIRVHGQVDY
SQ  ERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIESCDVQIVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELWDK
SQ  YRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTQNDRILELRDIVAKIAADVGLDASALMQGELDALGQRLA
SQ  ECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERH
SQ  QNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQ
SQ  QQLCAIHQNLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAER
SQ  NALQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGF
SQ  LQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISP
SQ  HDMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLEQ
SQ  QVNSELQLRDKEREWLLSTSRELLTLYSEPEVRSQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRA
SQ  WLFEVESQLDKPLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWRTQVNTSGLAASAQNLEQR
SQ  WKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLR
SQ  QLEQIYAKLAMSAGVEPENIQKLTLPTKVMVSMWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNAIQKALEQLP
SQ  SAENQQTSKAEPKAVLQRLESLEKKLQDAQQHVQQADNLAQEAKTRTKQQPQLKQLLELVSAYTTLWQTVQTRIVTLKTT
SQ  WLTRAAQAAASLPVSEAANAAVQVNTLSQRKLRQAQQMQRETSITAKDAYIMELQTAITECQNNLDELQRTVVDKTRKPG
SQ  PQKIAKLLGNAQSSTELVKHLSHLLLTECKADDQAAEVDTVAELTLRFDTLQSQWKARQQHDQNASEVGRLTCPLCTQRN
SQ  WQQIDNDLWRLEQWLQFAESTQKAQSAPPSNIELLEDVTQDHREFLLDLESHKSIISSLNVVGDHLATHTLDTEKARQLR
SQ  SRLEADNERWNNVCINATKWQGLLQTALMGNSEFHQTIGELVEWLQRTEQNIKASEPVDLTEERSVLETKFKKFKDLRAE
SQ  LERCEPRVVSLQDAADQLLRSVEGSEQQSQHTYERTLSRLTDLRLRLQSLRRLSGIYIVKLGAVLGYEGDNLGVPLHMLS
SQ  SELLDNTTLSTSSMQAAAPNTENANNTDGGDAVDGDVINTTVLARGARFLGRVARASLPIQALMLLLLGVATLVPHGEDY
SQ  TCMFSNTFARSLEPMLSYPHGPPPT
//
ID  Q96HJ5;
PN  Membrane-spanning 4-domains subfamily A member 3;
GN  MS4A3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Located in the perinuclear area.
DR  UNIPROT: Q96HJ5;
DR  UNIPROT: A8MTP8;
DR  UNIPROT: Q8NHW2;
DR  Pfam: PF04103;
DR  OMIM: 606498;
DR  DisGeNET: 932;
DE  Function: Hematopoietic modulator for the G1-S cell cycle transition. Modulates the level of phosphorylation of cyclin-dependent kinase 2 (CDK2) through its direct binding to cyclin-dependent kinase inhibitor 3 (CDKN3/KAP). {ECO:0000269|PubMed:11781350}.
DE  Reference Proteome: Yes;
DE  Interaction: Q01628; IntAct: EBI-24801917; Score: 0.56
DE  Interaction: Q8IY26; IntAct: EBI-24595440; Score: 0.56
DE  Interaction: Q9UNK0; IntAct: EBI-24517101; Score: 0.56
DE  Interaction: Q9NRQ5; IntAct: EBI-24520672; Score: 0.56
DE  Interaction: A2RU14; IntAct: EBI-24532611; Score: 0.56
DE  Interaction: Q9Y267; IntAct: EBI-24607353; Score: 0.60
DE  Interaction: P55061; IntAct: EBI-24609547; Score: 0.56
DE  Interaction: Q9Y6I9; IntAct: EBI-24610634; Score: 0.60
DE  Interaction: Q16617; IntAct: EBI-24611877; Score: 0.56
DE  Interaction: P24593; IntAct: EBI-24612958; Score: 0.56
DE  Interaction: Q8WVX3; IntAct: EBI-24614489; Score: 0.56
DE  Interaction: Q9P0B6; IntAct: EBI-24619069; Score: 0.56
DE  Interaction: Q9UKR5; IntAct: EBI-24620954; Score: 0.56
DE  Interaction: P60201; IntAct: EBI-24623326; Score: 0.56
DE  Interaction: Q99437; IntAct: EBI-24639063; Score: 0.56
DE  Interaction: Q15848; IntAct: EBI-24689161; Score: 0.56
DE  Interaction: Q6ZP80; IntAct: EBI-24538049; Score: 0.56
DE  Interaction: O95832; IntAct: EBI-24536228; Score: 0.56
DE  Interaction: Q8N0U8; IntAct: EBI-24537215; Score: 0.56
DE  Interaction: Q96CE8; IntAct: EBI-24540310; Score: 0.56
DE  Interaction: Q6UX40; IntAct: EBI-24543702; Score: 0.56
DE  Interaction: Q8WW34; IntAct: EBI-24544415; Score: 0.56
DE  Interaction: Q12983; IntAct: EBI-24546891; Score: 0.56
DE  Interaction: P19397; IntAct: EBI-24547321; Score: 0.56
DE  Interaction: Q5J8X5; IntAct: EBI-24548625; Score: 0.56
DE  Interaction: Q9NV12; IntAct: EBI-24571283; Score: 0.56
DE  Interaction: O95159; IntAct: EBI-24576289; Score: 0.56
DE  Interaction: P52803; IntAct: EBI-24577069; Score: 0.56
DE  Interaction: Q96EC8; IntAct: EBI-24578834; Score: 0.56
DE  Interaction: Q96IW7; IntAct: EBI-24578812; Score: 0.56
DE  Interaction: Q9BZL3; IntAct: EBI-24596021; Score: 0.56
DE  Interaction: P56747; IntAct: EBI-24596210; Score: 0.56
DE  Interaction: O43765; IntAct: EBI-24596868; Score: 0.56
DE  Interaction: Q9NY91; IntAct: EBI-24602190; Score: 0.56
DE  Interaction: P54852; IntAct: EBI-24639148; Score: 0.56
DE  Interaction: O95393; IntAct: EBI-24800071; Score: 0.56
DE  Interaction: P21854; IntAct: EBI-24807056; Score: 0.56
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0035579;
GO  GO:0007166;
GO  GO:0051726;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASHEVDNAELGSASAHGTPGSEAGPEELNTSVYQPIDGSPDYQKAKLQVLGAIQILNAAMILALGVFLGSLQYPYHFQK
SQ  HFFFFTFYTGYPIWGAVFFCSSGTLSVVAGIKPTRTWIQNSFGMNIASATIALVGTAFLSLNIAVNIQSLRSCHSSSESP
SQ  DLCNYMGSISNGMVSLLLILTLLELCVTISTIAMWCNANCCNSREEISSPPNSV
//
ID  Q03455;
PN  Probable zinc transporter MSC2;
GN  MSC2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: Q03455;
DR  UNIPROT: D6VSI6;
DR  Pfam: PF01545;
DE  Function: Probably act as a zinc ion transporter moving zinc from the nucleus/endoplasmic reticulum to the cytoplasm. Involved in zinc ion homeostasis and cellular distribution. {ECO:0000269|PubMed:11058603}.
DE  Reference Proteome: Yes;
DE  Interaction: P53735; IntAct: EBI-7752340; Score: 0.67
DE  Interaction: P53919; IntAct: EBI-858595; Score: 0.00
DE  Interaction: Q06677; IntAct: EBI-3758653; Score: 0.35
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0046873;
GO  GO:0005385;
GO  GO:0006882;
GO  GO:0030001;
GO  GO:0055085;
GO  GO:1904257;
GO  GO:0006829;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNLQELLAKVPLLLSYPTIILSSNLIVPSHNDLISRAASTSAAEYADEKLIFFSTDHAIRLIFLPTFVASSFNLFAHYFN
SQ  FINYSSRRKYYVLFTAIYFLSILTAIFHPIQSTCITLLIIKLLTTADESSPKIALNFKTILKTFVPFITLTLVILRWDPS
SQ  FDASSGDVNKISTSLAAYALLILTLRYASPLILSTLSSSIGVVSKDTSVAQHSISRNKRFPLILVLPIFSFVLLYLMTIV
SQ  NKTYNIQLLMVFVFFGCLSIFFLSLKDLFTEDGNQKKGGQEDEYCRMFDIKYMISYLWLTRFTILLTGIMAIVVHFLSFN
SQ  EITSSIKTDLLSLLFVVVAEYVSSFSNKQPDSHSHNHAHHHSHLTDSLPLENESMFKQMALNKDTRSIFSFLLLNTAFMF
SQ  VQLLYSFRSKSLGLLSDSLHMALDCTSLLLGLIAGVLTKKPASDKFPFGLNYLGTLAGFTNGVLLLGIVCGIFVEAIERI
SQ  FNPIHLHATNELLVVATLGLLVNLVGLFAFDHGAHDHGGTDNENMKGIFLHILADTLGSVGVVISTLLIKLTHWPIFDPI
SQ  ASLLIGSLILLSALPLLKSTSANILLRLDDKKHNLVKSALNQISTTPGITGYTTPRFWPTESGSSGHSHAHTHSHAENHS
SQ  HEHHHDQKNGSQEHPSLVGYIHVQYVDGENSTIIKKRVEKIFENVSIKAWVQVEPQNSTCWCRATSMNTISANPNSLPLQ
SQ  PIAN
//
ID  Q13330;
PN  Metastasis-associated protein MTA1;
GN  MTA1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: [Isoform Short]: Cytoplasm. [Isoform Long]: Nucleus. Nucleus envelope. Cytoplasm. Cytoplasm, cytoskeleton. Note=Associated with microtubules. Localization at the nuclear envelope is TPR-dependent.
DR  UNIPROT: Q13330;
DR  UNIPROT: A5PLK4;
DR  UNIPROT: Q86SW2;
DR  UNIPROT: Q8NFI8;
DR  UNIPROT: Q96GI8;
DR  PDB: 4BKX;
DR  PDB: 4PBY;
DR  PDB: 4PBZ;
DR  PDB: 4PC0;
DR  PDB: 5FXY;
DR  PDB: 5ICN;
DR  PDB: 6G16;
DR  PDB: 6ZRC;
DR  PDB: 6ZRD;
DR  PDB: 7AO8;
DR  PDB: 7AO9;
DR  PDB: 7AOA;
DR  Pfam: PF01426;
DR  Pfam: PF01448;
DR  Pfam: PF00320;
DR  Pfam: PF17226;
DR  Pfam: PF00249;
DR  PROSITE: PS51038;
DR  PROSITE: PS51156;
DR  PROSITE: PS51293;
DR  OMIM: 603526;
DR  DisGeNET: 9112;
DE  Function: Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone- deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Involved in the epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C, IFI16 and HDAC4/5/6-dependent manner. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK- ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression. Isoform Short binds to ESR1 and sequesters it in the cytoplasm and enhances its non-genomic responses. With TFCP2L1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (By similarity). {ECO:0000250|UniProtKB:Q8K4B0, ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:17922032, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24413532}.
DE  Reference Proteome: Yes;
DE  Interaction: Q07912; IntAct: EBI-28939183; Score: 0.35
DE  Interaction: Q8IXH7; IntAct: EBI-730969; Score: 0.00
DE  Interaction: P32249; IntAct: EBI-731761; Score: 0.00
DE  Interaction: Q9NVP1; IntAct: EBI-736553; Score: 0.00
DE  Interaction: Q16665; IntAct: EBI-8110282; Score: 0.56
DE  Interaction: Q13547; IntAct: EBI-8110375; Score: 0.91
DE  Interaction: Q92769; IntAct: EBI-7911409; Score: 0.85
DE  Interaction: O60341; IntAct: EBI-2461776; Score: 0.53
DE  Interaction: Q99497; IntAct: EBI-2898921; Score: 0.35
DE  Interaction: Q9BTC8; IntAct: EBI-3505128; Score: 0.35
DE  Interaction: A8E1C4; IntAct: EBI-6155797; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6268389; Score: 0.35
DE  Interaction: Q09028; IntAct: EBI-8834818; Score: 0.83
DE  Interaction: Q16576; IntAct: EBI-8835025; Score: 0.64
DE  Interaction: Q5S007; IntAct: EBI-9247259; Score: 0.44
DE  Interaction: O95983; IntAct: EBI-9691985; Score: 0.60
DE  Interaction: O14519; IntAct: EBI-9692524; Score: 0.53
DE  Interaction: P43364; IntAct: EBI-10228839; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-10228851; Score: 0.56
DE  Interaction: Q13422; IntAct: EBI-10228871; Score: 0.56
DE  Interaction: Q5VWX1; IntAct: EBI-10228881; Score: 0.56
DE  Interaction: Q6A162; IntAct: EBI-10228891; Score: 0.67
DE  Interaction: Q6FGM0; IntAct: EBI-10228901; Score: 0.56
DE  Interaction: P21673; IntAct: EBI-10228911; Score: 0.56
DE  Interaction: Q7Z3S9; IntAct: EBI-10228921; Score: 0.56
DE  Interaction: O00505; IntAct: EBI-10228931; Score: 0.56
DE  Interaction: Q9BRK4; IntAct: EBI-10228941; Score: 0.56
DE  Interaction: O14862; IntAct: EBI-9995694; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.59
DE  Interaction: Q96KQ7; IntAct: EBI-10891210; Score: 0.58
DE  Interaction: Q92560; IntAct: EBI-10891522; Score: 0.35
DE  Interaction: P62805; IntAct: EBI-10891522; Score: 0.35
DE  Interaction: Q86YP4; IntAct: EBI-10891522; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-10891522; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-10891522; Score: 0.35
DE  Interaction: P52732; IntAct: EBI-10891522; Score: 0.35
DE  Interaction: Q14839; IntAct: EBI-10891522; Score: 0.53
DE  Interaction: O60315; IntAct: EBI-10891522; Score: 0.61
DE  Interaction: P04004; IntAct: EBI-10891522; Score: 0.35
DE  Interaction: O14744; IntAct: EBI-10891522; Score: 0.35
DE  Interaction: Q8WXI9; IntAct: EBI-10891522; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-11009211; Score: 0.35
DE  Interaction: P83917; IntAct: EBI-11012671; Score: 0.35
DE  Interaction: Q80Y55; IntAct: EBI-11022265; Score: 0.35
DE  Interaction: Q9P253; IntAct: EBI-11047442; Score: 0.35
DE  Interaction: Q17RP2; IntAct: EBI-11051402; Score: 0.35
DE  Interaction: Q9ULU4; IntAct: EBI-11059997; Score: 0.35
DE  Interaction: Q8R5C5; IntAct: EBI-11073047; Score: 0.35
DE  Interaction: P58871; IntAct: EBI-11079678; Score: 0.35
DE  Interaction: P08670; IntAct: EBI-11083342; Score: 0.35
DE  Interaction: O35207; IntAct: EBI-11100498; Score: 0.35
DE  Interaction: Q9Z2E1; IntAct: EBI-11102015; Score: 0.35
DE  Interaction: Q9R190; IntAct: EBI-11126242; Score: 0.35
DE  Interaction: Q96EQ0; IntAct: EBI-11152414; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-11153302; Score: 0.35
DE  Interaction: P46379; IntAct: EBI-11154173; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-24354657; Score: 0.68
DE  Interaction: Q15323; IntAct: EBI-25244418; Score: 0.56
DE  Interaction: Q58EX7; IntAct: EBI-24491299; Score: 0.56
DE  Interaction: P0DPK4; IntAct: EBI-25260576; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-24421172; Score: 0.56
DE  Interaction: Q9NRD5; IntAct: EBI-24459255; Score: 0.56
DE  Interaction: Q99961; IntAct: EBI-24554551; Score: 0.56
DE  Interaction: P26358; IntAct: EBI-12687979; Score: 0.35
DE  Interaction: Q9P2Y4; IntAct: EBI-21687197; Score: 0.35
DE  Interaction: Q8WWY6; IntAct: EBI-21686991; Score: 0.35
DE  Interaction: Q9H3M7; IntAct: EBI-21737601; Score: 0.35
DE  Interaction: Q9HCH3; IntAct: EBI-21757216; Score: 0.35
DE  Interaction: Q8IW50; IntAct: EBI-21781744; Score: 0.35
DE  Interaction: Q9Y242; IntAct: EBI-21794087; Score: 0.35
DE  Interaction: Q86UZ6; IntAct: EBI-21798219; Score: 0.35
DE  Interaction: A8MW92; IntAct: EBI-21803672; Score: 0.35
DE  Interaction: Q969R5; IntAct: EBI-21804164; Score: 0.35
DE  Interaction: Q9H165; IntAct: EBI-21882252; Score: 0.35
DE  Interaction: Q96KM6; IntAct: EBI-21882252; Score: 0.35
DE  Interaction: Q96K83; IntAct: EBI-21882252; Score: 0.35
DE  Interaction: Q96EB6; IntAct: EBI-21882252; Score: 0.35
DE  Interaction: Q63HK5; IntAct: EBI-21882252; Score: 0.35
DE  Interaction: Q2M1K9; IntAct: EBI-21882252; Score: 0.35
DE  Interaction: Q8N726; IntAct: EBI-15926073; Score: 0.40
DE  Interaction: Q17R98; IntAct: EBI-16118426; Score: 0.35
DE  Interaction: P70326; IntAct: EBI-16365383; Score: 0.35
DE  Interaction: P03950; IntAct: EBI-16363232; Score: 0.35
DE  Interaction: P04040; IntAct: EBI-16789632; Score: 0.27
DE  Interaction: Q08379; IntAct: EBI-16793089; Score: 0.27
DE  Interaction: P68431; IntAct: EBI-16794028; Score: 0.27
DE  Interaction: Q12873; IntAct: EBI-16878859; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-20976183; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-20976225; Score: 0.46
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: O15530; IntAct: EBI-25375702; Score: 0.35
DE  Interaction: P46734; IntAct: EBI-25388977; Score: 0.35
DE  Interaction: P14240; IntAct: EBI-26968430; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574619; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-28931531; Score: 0.35
DE  Interaction: P19784; IntAct: EBI-28934542; Score: 0.35
DE  Interaction: P20794; IntAct: EBI-28934658; Score: 0.35
DE  Interaction: P32298; IntAct: EBI-28934990; Score: 0.35
DE  Interaction: Q96KG9; IntAct: EBI-28944481; Score: 0.35
DE  Interaction: P35712; IntAct: EBI-29730925; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016581;
GO  GO:0003682;
GO  GO:0042826;
GO  GO:0046872;
GO  GO:0000978;
GO  GO:0061629;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0006338;
GO  GO:0032922;
GO  GO:0006302;
GO  GO:0043153;
GO  GO:0016575;
GO  GO:0045475;
GO  GO:0045892;
GO  GO:0000122;
GO  GO:0045893;
GO  GO:1902499;
GO  GO:0043161;
GO  GO:0042659;
GO  GO:0040029;
GO  GO:2000736;
GO  GO:0010212;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSTLIALADKHATLSVCYKAGPGADNGEE
SQ  GEIEEEMENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTL
SQ  LADKGEIRVGNRYQADITDLLKEGEEDGRDQSRLETQVWEAHNPLTDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHM
SQ  SAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSL
SQ  TSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNNVKAGVVNGTGAPGQSPGAGRACESCYTTQ
SQ  SYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRSNMSPHGLPARSSGSPKFAMKTRQAFYLHTTKLTR
SQ  IARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQSPLVLKQAVRKPLEAVLRYLETHPRPPKPDPVKSVSSVL
SQ  SSLTPAKVAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGLANHGQARHMGPSRNLLLNGKSYPTKVRLIRGGSL
SQ  PPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPPRPPPPAPVNDEPIVIED
//
ID  Q8K4B0;
PN  Metastasis-associated protein MTA1;
GN  Mta1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus. Nucleus envelope {ECO:0000255|PROSITE- ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with microtubules. Primarily localized in the cytoplasm in embryonic tissues. Localization at the nuclear envelope is TPR-dependent.
DR  UNIPROT: Q8K4B0;
DR  UNIPROT: Q80UI1;
DR  UNIPROT: Q8K4D4;
DR  UNIPROT: Q924K9;
DR  Pfam: PF01426;
DR  Pfam: PF01448;
DR  Pfam: PF00320;
DR  Pfam: PF17226;
DR  Pfam: PF00249;
DR  PROSITE: PS51038;
DR  PROSITE: PS51156;
DR  PROSITE: PS51293;
DE  Function: Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone- deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression. With Tfcp2l1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (PubMed:28982712). {ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:19805145, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:20071335, ECO:0000269|PubMed:20682799, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:28982712}.
DE  Reference Proteome: Yes;
DE  Interaction: Q62421; IntAct: EBI-7674614; Score: 0.68
DE  Interaction: Q96R06; IntAct: EBI-7674732; Score: 0.49
DE  Interaction: Q9CQJ4; IntAct: EBI-1216154; Score: 0.35
DE  Interaction: Q01105; IntAct: EBI-1371815; Score: 0.35
DE  Interaction: P20263; IntAct: EBI-3043810; Score: 0.53
DE  Interaction: P49452; IntAct: EBI-8573213; Score: 0.35
DE  Interaction: Q8BX22; IntAct: EBI-5714013; Score: 0.35
DE  Interaction: Q3UNW5; IntAct: EBI-5738236; Score: 0.35
DE  Interaction: Q9R190; IntAct: EBI-5821664; Score: 0.35
DE  Interaction: O94880; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9UHF7; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: P78368; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: O94776; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9NP66; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q09028; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: F5GWX5; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: P22234; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q86YP4; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: O14519; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: P55197; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: E7EV10; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9UJQ4; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9UBB5; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q8N1G0; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q03468; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q13547; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9NR30; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: P61513; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: P56192; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9UII4; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q12873; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q96N64; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: O95983; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q8WXI9; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9UID6; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9UGU0; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q8N680; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9NWV8; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q16576; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q9ULU4; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q92769; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q7Z5J4; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: O60287; IntAct: EBI-11126052; Score: 0.35
DE  Interaction: Q62233; IntAct: EBI-15649730; Score: 0.54
DE  Interaction: Q64364; IntAct: EBI-15925993; Score: 0.40
DE  Interaction: Q8R1H0; IntAct: EBI-16162578; Score: 0.35
DE  Interaction: P70326; IntAct: EBI-16359962; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885060; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016581;
GO  GO:0003682;
GO  GO:0019899;
GO  GO:0042826;
GO  GO:0046872;
GO  GO:0000978;
GO  GO:0061629;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0006338;
GO  GO:0032922;
GO  GO:0006302;
GO  GO:0043153;
GO  GO:0016575;
GO  GO:0045475;
GO  GO:0045892;
GO  GO:0000122;
GO  GO:0045893;
GO  GO:1902499;
GO  GO:0043161;
GO  GO:0042659;
GO  GO:0040029;
GO  GO:2000736;
GO  GO:0010212;
GO  GO:0033363;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSSLIALADKHATLSVCYRAGPGADTGEE
SQ  GEVEEEVENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTL
SQ  LADKGEIRVGNRYQADITDLLKEGEEDGRDQSKLETKVWEAHNPLVDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHM
SQ  SAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSL
SQ  TSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISASSVKATVVNGTGTPGQSPGAGRACESCYTTQ
SQ  SYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRNNMSPHGIPARSSGSPKFAMKTRQAFYLHTTKLTR
SQ  IARRLCREILRPWHAARHPYMPINSAAIKAECTARLPEASQSPLVLKQVVRKPLEAVLRYLETHPRPPKPDPVKSSSSVL
SQ  SSLTPAKSAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGLANHGQTRHMGPSRNLLLNGKSYPTKVRLIRGGSL
SQ  PPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPLRPPPPAPVNDEPIVIED
//
ID  Q62599;
PN  Metastasis-associated protein MTA1;
GN  Mta1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: [Isoform 1]: Nucleus {ECO:0000269|PubMed:10393810}. Nucleus envelope {ECO:0000255|PROSITE- ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with microtubules. Localization at the nuclear envelope is TPR- dependent (By similarity). {ECO:0000250}. [Isoform 2]: Rough endoplasmic reticulum {ECO:0000269|PubMed:10393810}. Golgi apparatus {ECO:0000269|PubMed:10393810}. Zymogen granule {ECO:0000269|PubMed:10393810}.
DR  UNIPROT: Q62599;
DR  UNIPROT: Q9Z0N8;
DR  Pfam: PF01426;
DR  Pfam: PF01448;
DR  Pfam: PF00320;
DR  Pfam: PF17226;
DR  Pfam: PF00249;
DR  PROSITE: PS51038;
DR  PROSITE: PS51156;
DR  PROSITE: PS51293;
DE  Function: Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone- deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression (By similarity). Isoform 2 may be involved in the sorting of amylase during zymogen granule formation in the pancreas. With Tfcp2l1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (By similarity). {ECO:0000250|UniProtKB:Q13330, ECO:0000250|UniProtKB:Q8K4B0, ECO:0000269|PubMed:10933808}.
DE  Reference Proteome: Yes;
DE  Interaction: P63170; IntAct: EBI-349104; Score: 0.35
DE  Interaction: O35615; IntAct: EBI-7678257; Score: 0.44
DE  Interaction: Q9ET75; IntAct: EBI-15649612; Score: 0.40
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016581;
GO  GO:0005791;
GO  GO:0042588;
GO  GO:0003682;
GO  GO:0019899;
GO  GO:0042826;
GO  GO:0046872;
GO  GO:0000978;
GO  GO:0061629;
GO  GO:0003713;
GO  GO:0003714;
GO  GO:0006338;
GO  GO:0032922;
GO  GO:0006302;
GO  GO:0043153;
GO  GO:0007565;
GO  GO:0016575;
GO  GO:0045475;
GO  GO:0000122;
GO  GO:1902499;
GO  GO:0043161;
GO  GO:0040029;
GO  GO:0010212;
GO  GO:0033363;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSSLIALADKHATLSVCYRAGPGADTGEE
SQ  GEVEEEVENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTL
SQ  LADKGEIRVGNRYQADITDLLKDGEEDGRDQSKLETKVWEAHNPLVDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHM
SQ  SAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSL
SQ  TSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNSVKASVVNGTGTPGQSPGAGRACESCYTTQ
SQ  SYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRNNMSPHGIPARSSGSPKFAMKTRQAFYLHTTKLTR
SQ  IARRLCREILRPWHAARHPYMPINSAAIKAECTARLPEASQSPLVLKQVVRKPLEAVLRYLETHPRPPKPDPVKSSSSVL
SQ  SSLTPAKSAPVINNGSPTILGKRSYEQHNGVDGLANHGQTRHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWID
SQ  APDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPLRPPPPAPVNDEPIVIED
//
ID  A6QLT2;
PN  Myotubularin-related protein 2;
GN  MTMR2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q13614}. Early endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13614}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2D1}. Endosome membrane {ECO:0000250|UniProtKB:Q9Z2D1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Note=Partly associated with membranes (By similarity). Localizes to vacuoles in hypo-osmotic conditions (By similarity). {ECO:0000250|UniProtKB:Q13614, ECO:0000250|UniProtKB:Q9Z2D1}.
DR  UNIPROT: A6QLT2;
DR  Pfam: PF02893;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DR  PROSITE: PS50056;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3- phosphate and phosphatidylinositol 3,5-bisphosphate (By similarity). Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5- phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Stabilizes SBF2/MTMR13 at the membranes. Specifically in peripheral nerves, stabilizes SBF2/MTMR13 protein (By similarity). {ECO:0000250|UniProtKB:Q13614, ECO:0000250|UniProtKB:Q9Z2D1}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005829;
GO  GO:0031901;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005774;
GO  GO:0042802;
GO  GO:0052629;
GO  GO:0004438;
GO  GO:0046855;
GO  GO:0032288;
GO  GO:0031642;
GO  GO:0048666;
GO  GO:0046856;
GO  GO:0060304;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q13614};
SQ  MEKSSSCESLGSQPAVARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSAENFSPDLRVLRESNKLAEMEEPPLLP
SQ  GENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVISRVEKIGGASSRGENSYGLETVCKDIRN
SQ  LRFAHKPEGRTRRSIFENLMKYAFPVSNNLSLFAFEYKEVFPENGWKLYDSLSEYRRQGIPNESWRITKVNERYELCDTY
SQ  PALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFD
SQ  ARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGAL
SQ  RIADRVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVF
SQ  LQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPRRTVSLWSYINSQLEDFTNPLYGSYS
SQ  NHVLYPVASMRHLELWVGYYVRWNPRMKPQEPIHNRYKELLAKRAELQKKVEELQREISNRSTSSSERAGSPAQCVTPVQ
SQ  TVV
//
ID  Q13614;
PN  Myotubularin-related protein 2;
GN  MTMR2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:15998640}. Early endosome membrane {ECO:0000269|PubMed:15998640, ECO:0000269|PubMed:21372139}; Peripheral membrane protein {ECO:0000269|PubMed:15998640, ECO:0000269|PubMed:21372139}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12668758}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2D1}. Endosome membrane {ECO:0000250|UniProtKB:Q9Z2D1}; Peripheral membrane protein {ECO:0000305}. Note=Partly associated with membranes (PubMed:12668758, PubMed:15998640, PubMed:21372139). Localizes to vacuoles in hypo- osmotic conditions (By similarity). {ECO:0000250|UniProtKB:Q9Z2D1, ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:15998640, ECO:0000269|PubMed:21372139}.
DR  UNIPROT: Q13614;
DR  UNIPROT: A6NN98;
DR  UNIPROT: Q9UPS9;
DR  PDB: 1LW3;
DR  PDB: 1M7R;
DR  PDB: 1ZSQ;
DR  PDB: 1ZVR;
DR  PDB: 5GNH;
DR  Pfam: PF02893;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DR  PROSITE: PS50056;
DR  OMIM: 601382;
DR  OMIM: 603557;
DR  DisGeNET: 8898;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3- phosphate and phosphatidylinositol 3,5-bisphosphate (PubMed:11733541, PubMed:12668758, PubMed:21372139, PubMed:14690594). Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5- trisphosphate (By similarity). Stabilizes SBF2/MTMR13 at the membranes (By similarity). Specifically in peripheral nerves, stabilizes SBF2/MTMR13 protein (By similarity). {ECO:0000250|UniProtKB:Q9Z2D1, ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:14690594, ECO:0000269|PubMed:21372139}.
DE  Disease: Charcot-Marie-Tooth disease 4B1 (CMT4B1) [MIM:601382]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie- Tooth disease are designated CMT4. {ECO:0000269|PubMed:10802647, ECO:0000269|PubMed:12398840}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95248; IntAct: EBI-27113582; Score: 0.35
DE  Interaction: P07196; IntAct: EBI-475642; Score: 0.51
DE  Interaction: Q8ZH40; IntAct: EBI-2864099; Score: 0.00
DE  Interaction: Q8D1P8; IntAct: EBI-2864085; Score: 0.00
DE  Interaction: Q7ARD3; IntAct: EBI-2864092; Score: 0.00
DE  Interaction: Q9C0I1; IntAct: EBI-6962705; Score: 0.59
DE  Interaction: O60826; IntAct: EBI-21812182; Score: 0.53
DE  Interaction: Q15303; IntAct: EBI-20980446; Score: 0.37
DE  Interaction: P21860; IntAct: EBI-20981016; Score: 0.37
DE  Interaction: Q01974; IntAct: EBI-20981810; Score: 0.37
DE  Interaction: Q9NQ75; IntAct: EBI-21391292; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-21391280; Score: 0.00
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: A4FU01; IntAct: EBI-27113520; Score: 0.35
DE  Interaction: Q13613; IntAct: EBI-27113582; Score: 0.35
DE  Interaction: P68363; IntAct: EBI-27113582; Score: 0.35
DE  Interaction: Q86WG5; IntAct: EBI-27113582; Score: 0.42
DE  Interaction: P19838; IntAct: EBI-27113582; Score: 0.35
DE  Interaction: Q9NXD2; IntAct: EBI-27113582; Score: 0.35
DE  Interaction: Q96QG7; IntAct: EBI-27113664; Score: 0.35
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0031901;
GO  GO:0070062;
GO  GO:0043231;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0097060;
GO  GO:0008021;
GO  GO:0005774;
GO  GO:0042802;
GO  GO:0052629;
GO  GO:0004438;
GO  GO:0008138;
GO  GO:0097062;
GO  GO:0046855;
GO  GO:0032288;
GO  GO:0045806;
GO  GO:0090394;
GO  GO:0031642;
GO  GO:2000645;
GO  GO:0002091;
GO  GO:0048666;
GO  GO:0006661;
GO  GO:0046856;
GO  GO:2000643;
GO  GO:0006470;
GO  GO:0060304;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEKSSSCESLGSQPAAARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSADNFSPDLRVLRESNKLAEMEEPPLLP
SQ  GENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVINRVEKIGGASSRGENSYGLETVCKDIRN
SQ  LRFAHKPEGRTRRSIFENLMKYAFPVSNNLPLFAFEYKEVFPENGWKLYDPLLEYRRQGIPNESWRITKINERYELCDTY
SQ  PALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFD
SQ  ARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGAL
SQ  RIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVF
SQ  LQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPKRTVSLWSYINSQLEDFTNPLYGSYS
SQ  NHVLYPVASMRHLELWVGYYIRWNPRMKPQEPIHNRYKELLAKRAELQKKVEELQREISNRSTSSSERASSPAQCVTPVQ
SQ  TVV
//
ID  Q9Z2D1;
PN  Myotubularin-related protein 2;
GN  Mtmr2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:14530412, ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}. Early endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14530412}. Cell projection, axon {ECO:0000269|PubMed:23297362}. Endosome membrane {ECO:0000269|PubMed:23297362}; Peripheral membrane protein {ECO:0000305}. Note=Partly associated with membranes (PubMed:14530412, PubMed:23297362). Localizes to vacuoles in hypo-osmotic conditions (PubMed:16399794). {ECO:0000269|PubMed:14530412, ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}.
DR  UNIPROT: Q9Z2D1;
DR  UNIPROT: B8JJF4;
DR  UNIPROT: Q8VHA7;
DR  Pfam: PF02893;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DR  PROSITE: PS50056;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup (PubMed:12045210, PubMed:16399794). Has phosphatase activity towards pho sphatidylinositol 3-phosphate and phosphatidylinositol 3,5- bisphosphate (PubMed:12045210, PubMed:16399794). Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5- trisphosphate (PubMed:12045210, PubMed:16399794). Stabilizes SBF2/MTMR13 at the membranes (PubMed:23297362). Specifically in peripheral nerves, stabilizes SBF2/MTMR13 protein (PubMed:23297362). {ECO:0000269|PubMed:12045210, ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}.
DE  Reference Proteome: Yes;
DE  Interaction: O95248; IntAct: EBI-11064455; Score: 0.35
DE  Interaction: Q86WG5; IntAct: EBI-11064455; Score: 0.35
DE  Interaction: Q9C0I1; IntAct: EBI-11064455; Score: 0.35
DE  Interaction: Q9UHQ1; IntAct: EBI-11064455; Score: 0.35
DE  Interaction: Q9NXD2; IntAct: EBI-11064455; Score: 0.35
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0031901;
GO  GO:0043231;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0097060;
GO  GO:0008021;
GO  GO:0005774;
GO  GO:0042802;
GO  GO:0052866;
GO  GO:0052629;
GO  GO:0004438;
GO  GO:0097062;
GO  GO:0016311;
GO  GO:0046855;
GO  GO:0032288;
GO  GO:0042552;
GO  GO:0045806;
GO  GO:0090394;
GO  GO:0031642;
GO  GO:2000645;
GO  GO:0002091;
GO  GO:0048666;
GO  GO:0046856;
GO  GO:0046488;
GO  GO:2000643;
GO  GO:0060304;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEKSSSCESLGAQLPAARLPSEDSLSSASTSHSENSVHTKSASAISSDSISTSADNFSPDLRVLREANKLAEMEEPALLP
SQ  GENIKDMAKDVTYICPFTGAVRGTLTVTSYRLYFKSMERDPPFVLDASLGVISRVEKIGGASSRGENSYGLETVCKDIRN
SQ  LRFAHKPEGRTRRSIFENLMKYAFPVSNGLPLFAFEYKEVFPENGWKLYDPLLEYRRQGIPNESWRITKINERYELCDTY
SQ  PALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATVTRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFD
SQ  ARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPTIEETHWLSNLESTHWLEHIKLILAGAL
SQ  RIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVF
SQ  LQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPKKTVSLWSYINSQLEDFTNPLYGSYS
SQ  NHVLYPVASMRHLELWVGYYIRWNPRMKPQEPIHSRYKELLAKRAELQRKVEELQREISNRSTSSSERASSPAQCVTPVQ
SQ  TVV
//
ID  Q5REB9;
PN  Myotubularin-related protein 2;
GN  MTMR2;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q13614}. Early endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13614}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2D1}. Endosome membrane {ECO:0000250|UniProtKB:Q9Z2D1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Note=Partly associated with membranes (By similarity). Localizes to vacuoles in hypo-osmotic conditions (By similarity). {ECO:0000250|UniProtKB:Q13614, ECO:0000250|UniProtKB:Q9Z2D1}.
DR  UNIPROT: Q5REB9;
DR  Pfam: PF02893;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DR  PROSITE: PS50056;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3- phosphate and phosphatidylinositol 3,5-bisphosphate (By similarity). Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5- phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Stabilizes SBF2/MTMR13 at the membranes. Specifically in peripheral nerves, stabilizes SBF2/MTMR13 protein (By similarity). {ECO:0000250|UniProtKB:Q13614, ECO:0000250|UniProtKB:Q9Z2D1}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005829;
GO  GO:0031901;
GO  GO:0048471;
GO  GO:0052629;
GO  GO:0004438;
GO  GO:0006661;
GO  GO:0046856;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q13614};
SQ  MEKSSSCESLGSQPAAARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSADNFSPDLRVLRESNKLAEMEEPPLLP
SQ  GENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVINRVEKIGGASSRGENSYGLETVCKDIRN
SQ  LRFAHKPEGRTRRSIFENLMKYAFPVSNNLPLFAFEYKEVFPENGWKLYDPLLEYRRQGIPNESWRITKINERYELCDTY
SQ  PALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHEIFIFD
SQ  ARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGAL
SQ  RIADKVESGKTSVIVHCSDGWDRTAQLTSLAMLMLDGYYRTTRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVF
SQ  LQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPKRTVSLWSYINSQLEDFTNPLYGSYS
SQ  NHVLYPVASMRHLELWVGYYIRWNPRMKPQEPIHNRYKELLAKRAELQKKVEELQREISNRSTSSSERASSPAQCVTPVQ
SQ  TVV
//
ID  O95248;
PN  Myotubularin-related protein 5;
GN  SBF1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:20937701}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12668758}.
DR  UNIPROT: O95248;
DR  UNIPROT: A0A024R4Z9;
DR  UNIPROT: A6PVG9;
DR  UNIPROT: G5E933;
DR  UNIPROT: O60228;
DR  UNIPROT: Q5JXD8;
DR  UNIPROT: Q5PPM2;
DR  UNIPROT: Q96GR9;
DR  UNIPROT: Q9UGB8;
DR  Pfam: PF02141;
DR  Pfam: PF02893;
DR  Pfam: PF06602;
DR  Pfam: PF00169;
DR  Pfam: PF12335;
DR  Pfam: PF03456;
DR  PROSITE: PS50211;
DR  PROSITE: PS50003;
DR  PROSITE: PS51339;
DR  OMIM: 603560;
DR  OMIM: 615284;
DR  DisGeNET: 6305;
DE  Function: Acts as an adapter for the phosphatase MTMR2 to regulate MTMR2 catalytic activity and subcellular location (PubMed:12668758). May function as a guanine nucleotide exchange factor (GEF) activating RAB28 (PubMed:20937701). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (PubMed:20937701). Inhibits myoblast differentiation in vitro and induces oncogenic transformation in fibroblasts (PubMed:9537414). {ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:9537414}.
DE  Disease: Charcot-Marie-Tooth disease 4B3 (CMT4B3) [MIM:615284]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie- Tooth disease are designated CMT4. {ECO:0000269|PubMed:23749797}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NTG7; IntAct: EBI-2322825; Score: 0.40
DE  Interaction: A0A380PK27; IntAct: EBI-2864071; Score: 0.00
DE  Interaction: O15530; IntAct: EBI-7283018; Score: 0.37
DE  Interaction: O14788; IntAct: EBI-7404516; Score: 0.37
DE  Interaction: P04792; IntAct: EBI-6873254; Score: 0.37
DE  Interaction: Q9WMX2; IntAct: EBI-9079822; Score: 0.37
DE  Interaction: Q9Z2D1; IntAct: EBI-11064455; Score: 0.35
DE  Interaction: Q9H8J5; IntAct: EBI-21537025; Score: 0.35
DE  Interaction: O60232; IntAct: EBI-21543889; Score: 0.35
DE  Interaction: Q8TDQ0; IntAct: EBI-21556046; Score: 0.35
DE  Interaction: P52799; IntAct: EBI-21582984; Score: 0.35
DE  Interaction: Q86WV1; IntAct: EBI-21601309; Score: 0.35
DE  Interaction: Q9BRK4; IntAct: EBI-21601734; Score: 0.35
DE  Interaction: P48426; IntAct: EBI-21630443; Score: 0.35
DE  Interaction: Q9HCJ2; IntAct: EBI-21642856; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-21650356; Score: 0.35
DE  Interaction: P37173; IntAct: EBI-21668347; Score: 0.35
DE  Interaction: Q9NXC2; IntAct: EBI-21737700; Score: 0.35
DE  Interaction: Q5T8I9; IntAct: EBI-21755295; Score: 0.35
DE  Interaction: Q6ZWK4; IntAct: EBI-21782601; Score: 0.35
DE  Interaction: P16581; IntAct: EBI-21812353; Score: 0.35
DE  Interaction: Q9NRW1; IntAct: EBI-21812395; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: Q6ZMQ8; IntAct: EBI-20980276; Score: 0.37
DE  Interaction: P03372; IntAct: EBI-21302175; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: Q8TDX7; IntAct: EBI-28943744; Score: 0.35
DE  Interaction: Q13614; IntAct: EBI-27113582; Score: 0.35
DE  Interaction: Q13613; IntAct: EBI-27115175; Score: 0.35
DE  Interaction: Q9H6Y2; IntAct: EBI-27115175; Score: 0.35
DE  Interaction: Q9Y5B9; IntAct: EBI-27115175; Score: 0.35
DE  Interaction: Q9H6T3; IntAct: EBI-27115175; Score: 0.35
DE  Interaction: P17252; IntAct: EBI-27115175; Score: 0.35
DE  Interaction: P08123; IntAct: EBI-27115175; Score: 0.35
DE  Interaction: Q86WG5; IntAct: EBI-27115195; Score: 0.42
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016604;
GO  GO:0048471;
GO  GO:0005085;
GO  GO:0019208;
GO  GO:0008138;
GO  GO:0006470;
GO  GO:0043087;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MARLADYFVLVAFGPHPRGSGEGQGQILQRFPEKDWEDNPFPQGIELFCQPSGWQLCPERNPPTFFVAVLTDINSERHYC
SQ  ACLTFWEPAEPSQQETTRVEDATEREEEGDEGGQTHLSPTAPAPSAQLFAPKTLVLVSRLDHTEVFRNSLGLIYAIHVEG
SQ  LNVCLENVIGNLLTCTVPLAGGSQRTISLGAGDRQVIQTPLADSLPVSRCSVALLFRQLGITNVLSLFCAALTEHKVLFL
SQ  SRSYQRLADACRGLLALLFPLRYSFTYVPILPAQLLEVLSTPTPFIIGVNAAFQAETQELLDVIVADLDGGTVTIPECVH
SQ  IPPLPEPLQSQTHSVLSMVLDPELELADLAFPPPTTSTSSLKMQDKELRAVFLRLFAQLLQGYRWCLHVVRIHPEPVIRF
SQ  HKAAFLGQRGLVEDDFLMKVLEGMAFAGFVSERGVPYRPTDLFDELVAHEVARMRADENHPQRVLRHVQELAEQLYKNEN
SQ  PYPAVAMHKVQRPGESSHLRRVPRPFPRLDEGTVQWIVDQAAAKMQGAPPAVKAERRTTVPSGPPMTAILERCSGLHVNS
SQ  ARRLEVVRNCISYVFEGKMLEAKKLLPAVLRALKGRAARRCLAQELHLHVQQNRAVLDHQQFDFVVRMMNCCLQDCTSLD
SQ  EHGIAAALLPLVTAFCRKLSPGVTQFAYSCVQEHVVWSTPQFWEAMFYGDVQTHIRALYLEPTEDLAPAQEVGEAPSQED
SQ  ERSALDVASEQRRLWPTLSREKQQELVQKEESTVFSQAIHYANRMSYLLLPLDSSKSRLLRERAGLGDLESASNSLVTNS
SQ  MAGSVAESYDTESGFEDAETCDVAGAVVRFINRFVDKVCTESGVTSDHLKGLHVMVPDIVQMHIETLEAVQRESRRLPPI
SQ  QKPKLLRPRLLPGEECVLDGLRVYLLPDGREEGAGGSAGGPALLPAEGAVFLTTYRVIFTGMPTDPLVGEQVVVRSFPVA
SQ  ALTKEKRISVQTPVDQLLQDGLQLRSCTFQLLKMAFDEEVGSDSAELFRKQLHKLRYPPDIRATFAFTLGSAHTPGRPPR
SQ  VTKDKGPSLRTLSRNLVKNAKKTIGRQHVTRKKYNPPSWEHRGQPPPEDQEDEISVSEELEPSTLTPSSALKPSDRMTMS
SQ  SLVERACCRDYQRLGLGTLSSSLSRAKSEPFRISPVNRMYAICRSYPGLLIVPQSVQDNALQRVSRCYRQNRFPVVCWRS
SQ  GRSKAVLLRSGGLHGKGVVGLFKAQNAPSPGQSQADSSSLEQEKYLQAVVSSMPRYADASGRNTLSGFSSAHMGSHGKWG
SQ  SVRTSGRSSGLGTDVGSRLAGRDALAPPQANGGPPDPGFLRPQRAALYILGDKAQLKGVRSDPLQQWELVPIEVFEARQV
SQ  KASFKKLLKACVPGCPAAEPSPASFLRSLEDSEWLIQIHKLLQVSVLVVELLDSGSSVLVGLEDGWDITTQVVSLVQLLS
SQ  DPFYRTLEGFRLLVEKEWLSFGHRFSHRGAHTLAGQSSGFTPVFLQFLDCVHQVHLQFPMEFEFSQFYLKFLGYHHVSRR
SQ  FRTFLLDSDYERIELGLLYEEKGERRGQVPCRSVWEYVDRLSKRTPVFHNYMYAPEDAEVLRPYSNVSNLKVWDFYTEET
SQ  LAEGPPYDWELAQGPPEPPEEERSDGGAPQSRRRVVWPCYDSCPRAQPDAISRLLEELQRLETELGQPAERWKDTWDRVK
SQ  AAQRLEGRPDGRGTPSSLLVSTAPHHRRSLGVYLQEGPVGSTLSLSLDSDQSSGSTTSGSRQAARRSTSTLYSQFQTAES
SQ  ENRSYEGTLYKKGAFMKPWKARWFVLDKTKHQLRYYDHRVDTECKGVIDLAEVEAVAPGTPTMGAPKTVDEKAFFDVKTT
SQ  RRVYNFCAQDVPSAQQWVDRIQSCLSDA
//
ID  Q6ZPE2;
PN  Myotubularin-related protein 5;
GN  Sbf1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O95248}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95248}.
DR  UNIPROT: Q6ZPE2;
DR  UNIPROT: B2RXQ1;
DR  UNIPROT: B2RXX4;
DR  UNIPROT: B7ZWK2;
DR  UNIPROT: Q4QQM2;
DR  UNIPROT: Q8BK68;
DR  UNIPROT: Q8K2Z0;
DR  PDB: 1V5U;
DR  Pfam: PF02141;
DR  Pfam: PF02893;
DR  Pfam: PF06602;
DR  Pfam: PF00169;
DR  Pfam: PF12335;
DR  Pfam: PF03456;
DR  PROSITE: PS50211;
DR  PROSITE: PS50003;
DR  PROSITE: PS51339;
DE  Function: Acts as an adapter for the phosphatase MTMR2 to regulate MTMR2 catalytic activity and subcellular location. May function as a guanine nucleotide exchange factor (GEF) activating RAB28. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. Inhibits myoblast differentiation in vitro and induces oncogenic transformation in fibroblasts. {ECO:0000250|UniProtKB:O95248}.
DE  Reference Proteome: Yes;
DE  Interaction: P62158; IntAct: EBI-911456; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-6271507; Score: 0.35
DE  Interaction: Q7TMB8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: P16056; IntAct: EBI-27118288; Score: 0.35
GO  GO:0005737;
GO  GO:0016604;
GO  GO:0048471;
GO  GO:0005085;
GO  GO:0001691;
GO  GO:0001558;
GO  GO:0043087;
GO  GO:0007286;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MARLADYFVLVAFGPHPRGSGEGQGQILQRFPEKDWEDNPFPQGIELFCQPSGWQLCPERNPPTFFVAVLTDINSERHYC
SQ  ACLTFWEPVESTQEVVCTDNATEKEEEADGGGQARLSSTAPAQPGQLFAPKTLVLVSRLDHAEVFRNSLGLIYAIHVEGL
SQ  NVSLENVIGNLLTCTVPLAGGSQRTISLGAGDRQVIQTPLVDSLPVSRCSVALLFRQLGITNVLSLFCAALTEHKVLFLS
SQ  RSYQRLADACRGLLALLFPLRYSFTYVPILPAQLLEVLSTPTPFIIGVNAAFQAETQELLDVIVADLDGGTVTVPECVHI
SQ  PPLPEPLQSQTHNVLSMVLDPELELADLAFPPPTTSASSLKMQDKELRAVFLRLFAQLLQGYRWCLHIVRIHPEPVIRFH
SQ  KAAFLGQRGLVEDDFLMKVLEGMAFAGFVSERGVPYRATDLFDELVAHEVARMRADESHPHRVLRHVQELAEQLYKNENP
SQ  YPAVAMHKVQRPGEASHLRRTHRPFPRLDEGTIQWIVDQAAAKMQGAPPAVKAERRSTVPSGPPMTAILERCSGPHINSA
SQ  RRLEVVRNCISYVFEGKMLEAKKLLPAVLRALKGRAARRCLAHELHLHVQQNRAVLDHQQFDFVVRMMNCCLQDCTSLDE
SQ  HGIASALLPLVTAFCRKLSPGVTQFAYSCVQEHVVWSTPQFWEAMFYGDVQTHIRALYLEPSDGVSPTQETGEAQSQDDE
SQ  RSALDVASEQRRLWPTLSREKQQELVQKEESTVFSQAIHYANRMSYLLLPLDSSKSRLLRERAGLGDLESASNSLVTNSM
SQ  AGSVAESYDTESGFEDAETCDVAGAVVRFINRFVDKVCTESGVTSDHLKGLHVMVPDIVQMHIETLEAVHRESKRLPPIQ
SQ  KPKLLRPRLLPGEECVLDGLRVYLLPDGREEGVGGSGGGPALLPAEGAVFLTTYRVIFTGMPTDPLVGEQVVVRSFPVAA
SQ  LTKEKRISVQTPVDQLLQDGLQLRSCTFQLLKMAFDEEVGSDSAELFRKQLHKLRYPPDIRATFAFTLGSAHTPGRPPRV
SQ  TKDKGPSFRTLSRNLMKNAKKTIGRQYVTRKKYNPPGWEHRGQPPPEDQEDEISVSEELEPSTLTPSSALKPSDRMTMSS
SQ  LVERACCRDYQRLGLGTLSSSLSRAKSEPFRISPVNRMYAICRSYPGLLIVPQSIQDNALQRVSRCYRQNRFPVVCWRSG
SQ  RSKAVLLRSGGLHGKGVVGLFKAQNTPSPGQAQADSSSLEQEKYLQAVVSSMPRYADSSGRNTLSSFSSAHMGGHGKWSS
SQ  VRASGRSSGLGSDVGSRLAGRDLLSTPHTNGAPPDSGFLRPQRAALYIIGDKAQLKGVRPDPLQQWELVPIEVFEARQVK
SQ  ASFKKLLKACVPGCPATEPSPASFLRSLEDSEWLIQIHKLLQISVLVVELLDSGSSVLVSLEDGWDITTQVVSLVQLLSD
SQ  PFYRTLEGFRLLVEKEWLSFGHRFSHRGAHTLAGQSSGFTPVFLQFLDCVHQVHLQFPMEFEFSQFYLKFLGYHHTSRRF
SQ  RTFLLDSDYERIELGLLYEEKGERRGQLACKSVWEYVDRLSKRTPMFYNYTYAPEDTEVLRPYSNVSNLKVWDFYTEETL
SQ  AEGPPYDWELAQGPPEPPEEERPDGGAPQSRRRVVWPCYDSRPRVQPDAISRLLEELQRLETELGRPSERWKDTWDRVKA
SQ  AQRLESRQDGRGTPSSLLVSAVPHHRRSLGVYLQEGPVGSTLSLSLDSDQSSGSTTSSSRQAARRSTSTLYSQFQTAESE
SQ  NRSYEGILYKKGAFMKPWKARWFVLDKTKHQLRYYDHRMDTECKGVIDLAEVEAVAPGTPTIGAPKTVDEKAFFDVKTTR
SQ  RVYNFCAQDVPSAQQWVDRIQSCLSDA
//
ID  Q9Y217;
PN  Myotubularin-related protein 6;
GN  MTMR6;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:19038970}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:16787938, ECO:0000269|PubMed:19038970}. Endoplasmic reticulum {ECO:0000269|PubMed:19038970}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q8VE11}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19038970}. Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR9 to the perinuclear region (PubMed:19038970). Partially localizes to the endoplasmic reticulum (PubMed:19038970). Co-localizes with RAB1B to the endoplasmic reticulum-Golgi intermediate compartment and to the peri- Golgi region (By similarity). {ECO:0000250|UniProtKB:A0A0G2JXT6, ECO:0000250|UniProtKB:Q8VE11, ECO:0000269|PubMed:19038970}.
DR  UNIPROT: Q9Y217;
DR  UNIPROT: B2RBB5;
DR  UNIPROT: B3KSB4;
DR  UNIPROT: Q5JRG6;
DR  UNIPROT: Q86TB7;
DR  UNIPROT: Q86YH4;
DR  UNIPROT: Q96P80;
DR  PDB: 2YF0;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DR  OMIM: 603561;
DR  DisGeNET: 9107;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup (PubMed:19038970, PubMed:22647598). Dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate (PubMed:19038970, PubMed:22647598) (Probable). Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), phosphatidic acid and phosphatidylserine (PubMed:19038970). Negatively regulates ER-Golgi protein transport (By similarity). Probably in association with MTMR9, plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3-phosphate in membrane ruffles (PubMed:24591580). Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4(+) T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3-phosphate (PubMed:15831468). Negatively regulates proliferation of reactivated CD4(+) T-cells (PubMed:16847315). In complex with MTMR9, negatively regulates DNA damage-induced apoptosis (PubMed:19038970, PubMed:22647598). The formation of the MTMR6-MTMR9 complex stabilizes both MTMR6 and MTMR9 protein levels (PubMed:19038970). {ECO:0000250|UniProtKB:A0A0G2JXT6, ECO:0000269|PubMed:15831468, ECO:0000269|PubMed:16847315, ECO:0000269|PubMed:19038970, ECO:0000269|PubMed:22647598, ECO:0000269|PubMed:24591580, ECO:0000305|PubMed:24591580}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q6ZMQ8; IntAct: EBI-20980286; Score: 0.37
DE  Interaction: Q96QG7; IntAct: EBI-8657967; Score: 0.85
DE  Interaction: P41182; IntAct: EBI-765648; Score: 0.35
DE  Interaction: P13631; IntAct: EBI-3912831; Score: 0.37
DE  Interaction: P14373; IntAct: EBI-10325112; Score: 0.56
DE  Interaction: Q13287; IntAct: EBI-10325124; Score: 0.56
DE  Interaction: Q5JR59; IntAct: EBI-10325134; Score: 0.56
DE  Interaction: Q9Y2J4; IntAct: EBI-10325166; Score: 0.56
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96LK0; IntAct: EBI-11376319; Score: 0.27
DE  Interaction: Q15468; IntAct: EBI-11383475; Score: 0.27
DE  Interaction: Q5SW79; IntAct: EBI-11385552; Score: 0.27
DE  Interaction: P49286; IntAct: EBI-11577362; Score: 0.00
DE  Interaction: Q9NXW9; IntAct: EBI-14032135; Score: 0.37
DE  Interaction: Q8N5Z5; IntAct: EBI-21592259; Score: 0.35
DE  Interaction: P32320; IntAct: EBI-21622979; Score: 0.35
DE  Interaction: P14091; IntAct: EBI-21699601; Score: 0.35
DE  Interaction: O95229; IntAct: EBI-21701899; Score: 0.35
DE  Interaction: P48544; IntAct: EBI-21754197; Score: 0.35
DE  Interaction: O00506; IntAct: EBI-21762390; Score: 0.35
DE  Interaction: Q9Y216; IntAct: EBI-21836819; Score: 0.35
DE  Interaction: Q93088; IntAct: EBI-21899859; Score: 0.35
DE  Interaction: P49789; IntAct: EBI-21901559; Score: 0.40
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q8IWU2; IntAct: EBI-20979922; Score: 0.37
DE  Interaction: Q15303; IntAct: EBI-20980456; Score: 0.37
DE  Interaction: P21860; IntAct: EBI-20981026; Score: 0.37
DE  Interaction: Q01974; IntAct: EBI-20981820; Score: 0.37
DE  Interaction: Q13308; IntAct: EBI-20982464; Score: 0.37
DE  Interaction: Q92878; IntAct: EBI-20927160; Score: 0.40
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P21802; IntAct: EBI-32721907; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0032587;
GO  GO:0052629;
GO  GO:0106018;
GO  GO:0004438;
GO  GO:0004722;
GO  GO:0004725;
GO  GO:0006897;
GO  GO:0006661;
GO  GO:0046856;
GO  GO:0006470;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEHIRTTKVEQVKLLDRFSTSNKSLTGTLYLTATHLLFIDSHQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRTVHF
SQ  IVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDSERLQGWQLIDLAEEYKRMGVPNSHWQLSDANRDYKICETYP
SQ  RELYVPRIASKPIIVGSSKFRSKGRFPVLSYYHQDKEAAICRCSQPLSGFSARCLEDEHLLQAISKANPVNRYMYVMDTR
SQ  PKLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVNGTKGLSVNDFYSGLESSGWLRHIKAVMDAAIF
SQ  LAKAITVENASVLVHCSDGWDRTSQVCSLGSLLLDSYYRTIKGFMVLIEKDWISFGHKFSERCGQLDGDPKEVSPVFTQF
SQ  LECVWHLTEQFPQAFEFSEAFLLQIHEHIHSCQFGNFLGNCQKEREELKLKEKTYSLWPFLLEDQKKYLNPLYSSESHRF
SQ  TVLEPNTVSFNFKFWRNMYHQFDRTLHPRQSVFNIIMNMNEQNKQLEKDIKDLESKIKQRKNKQTDGILTKELLHSVHPE
SQ  SPNLKTSLCFKEQTLLPVNDALRTIEGSSPADNRYSEYAEEFSKSEPAVVSLEYGVARMTC
//
ID  A0A0G2JXT6;
PN  Myotubularin-related protein 6;
GN  Mtmr6;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:23188820}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y217}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q8VE11}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:23188820}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y217}. Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR9 to the perinuclear region (By similarity). Partially localizes to the endoplasmic reticulum (By similarity). Co-localizes with RAB1B to the endoplasmic reticulum-Golgi intermediate compartment and to the peri-Golgi region (PubMed:23188820). {ECO:0000250|UniProtKB:Q8VE11, ECO:0000250|UniProtKB:Q9Y217, ECO:0000269|PubMed:23188820}.
DR  UNIPROT: A0A0G2JXT6;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate. Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), phosphatidic acid and phosphatidylserine (By similarity). Negatively regulates ER-Golgi protein transport (PubMed:23188820). Probably in association with MTMR9, plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3-phosphate in membrane ruffles. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4(+) T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3- phosphate. Negatively regulates proliferation of reactivated CD4(+) T- cells. In complex with MTMR9, negatively regulates DNA damage-induced apoptosis. The formation of the MTMR6-MTMR9 complex stabilizes both MTMR6 and MTMR9 protein levels (By similarity). {ECO:0000250|UniProtKB:Q9Y217, ECO:0000269|PubMed:23188820}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0032587;
GO  GO:0052629;
GO  GO:0106018;
GO  GO:0004438;
GO  GO:0006897;
GO  GO:0046856;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEHIRTTKVEQVKLLDRFSTNNKSLTGTLYLTATHLLFIDAHQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRIVHF
SQ  IVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDTERLNGWQLIDLAAEYERMGVPNANWQLSDANREYKVCETYP
SQ  RELYVPRTASRPVIVGSSNFRSKGRLPVLSYCQQGTEAAICRCSQPLSGFSARCLEDEHLLQAISKANPGNRYMYVVDTR
SQ  PKLRMQSWWDTQKDIGRIIVRISSKIWNDEKIRESDEKKRLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQ
SQ  KLLEVNGSKGLSVNDFYSGLESSGWLRHIKAVLDAAIFLAKAIVVENASVLVHCSDGWDRTSQVCSLGSLLLDSYYRTMK
SQ  GFMVLIEKDWISFGHKFSERCGHLDGDPKEVSPVFTQFLECVWHLTEQFPQAFEFNEAFLLQIHEHIHSCQFGNFLGNCQ
SQ  KEREELRLKEKTYSLWPFLLADKKKYLNPLYSSKSQRLTVLEPNTASFNFKFWRNMYHQFDRTLHPRQSVLNIIMNMNEQ
SQ  NKQLEEDVKDLEAKIKQCKSGILTKDLLHAVHPESPSLKTSLCLKEQSLLPVKDTLRAVEGSSPADNRYCDYTEEFSKSE
SQ  PAVVSLEYGVARMTC
//
ID  Q5F452;
PN  Myotubularin-related protein 8;
GN  MTMR8;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96EF0}.
DR  UNIPROT: Q5F452;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup (By similarity). Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5- bisphosphate (By similarity). {ECO:0000250|UniProtKB:Q96EF0}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0052629;
GO  GO:0106018;
GO  GO:0004438;
GO  GO:0010507;
GO  GO:0046856;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEHITTPKVENVKLLDRYTNRKAASGTLYLTATHLIYVDASAEVRKETWILHHHIATVEKLPLTTAGCPLLIHCKNFHVA
SQ  HFVIGQERDCHEVYTSLLKLSQPVKPEELYAFSYNPKMSKDNREIGWKLIDLKVDYQRMGIPNDYWEITDLNKDYEVCNT
SQ  YPPEIVVPRAASKATVIGSSRFRSRGRIPVLSYLYKENNAAICRCSQPLSGFSARCLEDEQMLQAIREANPGSPFMYVVD
SQ  TRPKLNAMANRAAGKGYENEDNYDNIRFKFIGIENIHVMRSSLQKLLEVCETKSPSMSDFLTGLENSGWLRHIKAVMDAS
SQ  VFLAKAVKDEKASVLVHCSDGWDRTAQVCSLASLLLDPFYRAFKGFMVLIEKEWIAMGHKFSHRCGHLDGDPKEVSPVFT
SQ  QFIECVWQLMQQFPCTFEFNEHFLLEIHDHVYSCQFGNFLGTCHKEREDLKIFEKTHSLWPFLLQKKQELRNPLYRGFTA
SQ  YKELQPNTLPFSFQFWCGMYNRFDKGMHPKQCVLDHLLSCMNQKIKLEDNASELENKLPFLDGPLPNEACFLSKVGCAAS
SQ  KTPMLNTPQDYEGEAPPVLTNGISVGDINVTSDVDQRNKENLANHRDLHLNDSVDVLNSEAKDGKPQHH
//
ID  Q6TEL0;
PN  Myotubularin-related protein 8;
GN  mtmr8;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q96EF0}.
DR  UNIPROT: Q6TEL0;
DR  UNIPROT: Q7SZD1;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup (By similarity). Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5- bisphosphate (By similarity). {ECO:0000250|UniProtKB:Q96EF0}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0004708;
GO  GO:0052629;
GO  GO:0106018;
GO  GO:0004438;
GO  GO:0001568;
GO  GO:0010507;
GO  GO:0014065;
GO  GO:0046856;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEHIITPKVENVKLLNRYTEKKSALGTLYLTATHLIYVEQTSNTRKETWVLHHHILSVEKLLLTASGCPLLIRCKTFQHL
SQ  HLLFQKERDCQDVYQSLLRLFQPVKEEELYAFLYNPHQNEEERRRGWELISVVNDFNRMGLSNDYWEISHINKNFEMCST
SQ  YPSILGLPKSASVATVTGSAKFRSRGRLPVLSYYHKDTKAAICRCSQPLSGLNSRCVEDEQMLQAISQANPNSPFIYVVD
SQ  TRPKLNAMANRAAGKGYENEDNYSNIRFQFQGIENIHVMRSSLQKLLEVCSMKSPSMSDYLTGLENSGWLRHIKSVMDAG
SQ  VFLAKAVCEERASVLVHCSDGWDRTAQVCSLACLLLDPYYRTIKGLMVLIEKEWISFGHKFSHRCGHLDSDPKEASPVFT
SQ  QFLECVWQLSQQFPCVFEFNEHYLIEIHDQVYACQYGNFIGNCQKERLDMRLHEKTFSLWPHLLENQHQYRNPLYRRSLE
SQ  STVLRPSTLPLHFKFWCGMYNHYDRGMHPKQSVLDTLLTLTQRQVEGERTMTELQRQLAVADGVLPDPAGPINTHADQNN
SQ  QSEKMPAPPVVQSNGSCAPLINGNVKEVGPGAENSNQEDREEPAANEHDLSSKDKPVFVETEHSKEEVQESS
//
ID  Q96EF0;
PN  Myotubularin-related protein 8;
GN  MTMR8;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16787938}.
DR  UNIPROT: Q96EF0;
DR  UNIPROT: Q5JT99;
DR  UNIPROT: Q9NXP6;
DR  PDB: 4Y7I;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  PROSITE: PS00383;
DR  OMIM: 301061;
DR  DisGeNET: 55613;
DE  Function: Phosphatase that acts on lipids with a phosphoinositol headgroup (PubMed:22647598, PubMed:26143924). Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5- bisphosphate (PubMed:22647598, PubMed:26143924). In complex with MTMR9, negatively regulates autophagy (PubMed:22647598). {ECO:0000269|PubMed:22647598, ECO:0000269|PubMed:26143924}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6ZMQ8; IntAct: EBI-20980296; Score: 0.37
DE  Interaction: Q96QG7; IntAct: EBI-758404; Score: 0.81
DE  Interaction: P20839; IntAct: EBI-21610062; Score: 0.35
DE  Interaction: Q9Y216; IntAct: EBI-21836819; Score: 0.35
DE  Interaction: Q969Q4; IntAct: EBI-21883664; Score: 0.35
DE  Interaction: P21860; IntAct: EBI-20981036; Score: 0.37
DE  Interaction: Q9BUF5; IntAct: EBI-27113652; Score: 0.35
DE  Interaction: Q8WXG6; IntAct: EBI-27113652; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0032991;
GO  GO:0052629;
GO  GO:0106018;
GO  GO:0004438;
GO  GO:0010507;
GO  GO:0046856;
GO  GO:0016241;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDHITVPKVENVKLVDRYVSKKPANGILYLTATHLIYVEASGAARKETWIALHHIATVEKLPITSLGCPLTLRCKNFRVA
SQ  HFVLDSDLVCHEVYISLLKLSQPALPEDLYAFSYNPKSSKEMRESGWKLIDPISDFGRMGIPNRNWTITDANRNYEICST
SQ  YPPEIVVPKSVTLGTVVGSSKFRSKERVPVLSYLYKENNAAICRCSQPLSGFYTRCVDDELLLEAISQTNPGSQFMYVVD
SQ  TRPKLNAMANRAAGKGYENEDNYANIRFRFMGIENIHVMRSSLQKLLEVCELKTPTMSEFLSGLESSGWLRHIKAIMDAG
SQ  IFITKAVKVEKASVLVHCSDGWDRTAQVCSVASILLDPFYRTFKGLMILIEKEWISMGHKFSQRCGHLDGDSKEVSPIFT
SQ  QFLDCIWQLMEQFPCAFEFNENFLLEIHDHVFSCQFGNFLGNCQKDREDLRVYEKTHSVWPFLVQRKPDFRNPLYKGFTM
SQ  YGVLNPSTVPYNIQFWCGMYNRFDKGLQPKQSMLESLLEIKKQRAMLETDVHELEKKLKVRDEPPEEICTCSQLGNILSQ
SQ  HLGSPLTNPLGFMGINGDLNTLMENGTLSREGGLRAQMDQVKSQGADLHHNCCEIVGSLRAINISGDVGISEAMGISGDM
SQ  CTFEATGFSKDLGICGAMDISEATGISGNLGISEARGFSGDMGILGDTGISKASTKEADYSKHQ
//
ID  A7MB43;
PN  Myotubularin-related protein 9;
GN  MTMR9;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q96QG7}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9Z2D0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96QG7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96QG7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QG7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96QG7}. Note=Localizes to ruffles during EGF- induced macropinocytosis (By similarity). Colocalizes with MTMR6 to the perinuclear region. Partially localizes to the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q96QG7, ECO:0000250|UniProtKB:Q9Z2D0}.
DR  UNIPROT: A7MB43;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DE  Function: Acts as an adapter for myotubularin-related phosphatases. Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5-bisphosphate, and MTMR6 binding affinity for phosphorylated phosphatidylinositols (By similarity). Positively regulates lipid phosphatase MTMR7 catalytic activity (By similarity). Increases MTMR8 catalytic activity towards phosphatidylinositol 3-phosphate. The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels. Stabilizes MTMR8 protein levels. Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles. Negatively regulates autophagy, in part via its association with MTMR8. Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6. Does not bind mono-, di- and tri- phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine (By similarity). {ECO:0000250|UniProtKB:Q96QG7, ECO:0000250|UniProtKB:Q9Z2D0}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0032587;
GO  GO:0030234;
GO  GO:0004438;
GO  GO:0019903;
GO  GO:0010507;
GO  GO:0046856;
GO  GO:0010922;
GO  GO:0050821;
GO  GO:0060304;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q96QG7};
SQ  MEFAELIKTPRVDNVVLHRPFYPAVEGTLCLTGHHLILSSRQDNTEELWLLHSNIDAIDKRFVGPLGTIIIKCKDFRIIQ
SQ  LDIPGMEECLNIASSIEALSTLDSITLMYPFFYRPMFEVIEDGWHSFLPEQEFELYSSTISEWRLSYVNKEFSVCPSYPP
SQ  AVIVPKAIDDDALRKVATFRHGGRFPVLSYYHKKNGMVIMRSGQPLTGTNGRRCKEDEKLINATLRAGKRGYIIDTRPLN
SQ  IAQQARAKGGGFEQEAHYPQWRRIHKSIDRYHILQESLIKLVESCNDQTQNMDRWLSKLEASNWLTHIKEILTTACLAAQ
SQ  CLDREGASILIHGTEGTDSTLQVTSLAQIILEPRSRTIRGFEALIEREWLQAGHPFQQRCAQSAYCNSKQKWESPVFLLF
SQ  LDCVWQILRQFPCSFEFNENFLIMLFEHAYASQFGTFLGNNESERCKLKLQQKTMSLWSWVNRPSELSKFTNPLFEANNL
SQ  VIWPSVAPQSLQLWEGIFLRWNRSSKYLDEAYEEMVNIIEYNKELQAKVNLLRRQLAELETEDGVQESP
//
ID  Q96QG7;
PN  Myotubularin-related protein 9;
GN  MTMR9;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16787938, ECO:0000269|PubMed:19038970}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9Z2D0}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16787938, ECO:0000269|PubMed:19038970}. Endoplasmic reticulum {ECO:0000269|PubMed:19038970}. Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR6 to the perinuclear region (PubMed:19038970). Partially localizes to the endoplasmic reticulum (PubMed:19038970). {ECO:0000250|UniProtKB:Q9Z2D0, ECO:0000269|PubMed:19038970}.
DR  UNIPROT: Q96QG7;
DR  UNIPROT: B7Z291;
DR  UNIPROT: Q52LU3;
DR  UNIPROT: Q8WW11;
DR  UNIPROT: Q96QG6;
DR  UNIPROT: Q9NX50;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DR  OMIM: 606260;
DR  DisGeNET: 66036;
DE  Function: Acts as an adapter for myotubularin-related phosphatases (PubMed:19038970, PubMed:22647598). Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5- bisphosphate and MTMR6 binding affinity for phosphorylated phosphatidylinositols (PubMed:19038970, PubMed:22647598). Positively regulates lipid phosphatase MTMR7 catalytic activity (By similarity). Increases MTMR8 catalytic activity towards phosphatidylinositol 3- phosphate (PubMed:22647598). The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels (PubMed:19038970). Stabilizes MTMR8 protein levels (PubMed:22647598). Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles (PubMed:24591580). Negatively regulates autophagy, in part via its association with MTMR8 (PubMed:22647598). Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6 (PubMed:19038970, PubMed:22647598). Does not bind mono-, di- and tri- phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine (PubMed:19038970). {ECO:0000250|UniProtKB:Q9Z2D0, ECO:0000269|PubMed:19038970, ECO:0000269|PubMed:22647598, ECO:0000269|PubMed:24591580}.
DE  Reference Proteome: Yes;
DE  Interaction: O75140; IntAct: EBI-24656502; Score: 0.56
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P10909; IntAct: EBI-21831285; Score: 0.35
DE  Interaction: Q13614; IntAct: EBI-27113664; Score: 0.35
DE  Interaction: Q6ZMQ8; IntAct: EBI-20980306; Score: 0.37
DE  Interaction: Q96EF0; IntAct: EBI-758404; Score: 0.81
DE  Interaction: Q9Y6C2; IntAct: EBI-754120; Score: 0.88
DE  Interaction: Q96QG7; IntAct: EBI-755452; Score: 0.55
DE  Interaction: Q9NZD8; IntAct: EBI-756217; Score: 0.37
DE  Interaction: Q01844; IntAct: EBI-759352; Score: 0.37
DE  Interaction: Q9Y217; IntAct: EBI-8657967; Score: 0.85
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: O60341; IntAct: EBI-8476194; Score: 0.37
DE  Interaction: P00540; IntAct: EBI-10193386; Score: 0.74
DE  Interaction: Q08AM6; IntAct: EBI-10292953; Score: 0.56
DE  Interaction: Q13287; IntAct: EBI-10292965; Score: 0.72
DE  Interaction: Q8TBB1; IntAct: EBI-10292977; Score: 0.74
DE  Interaction: Q9Y216; IntAct: EBI-10293001; Score: 0.90
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: P26045; IntAct: EBI-24295537; Score: 0.56
DE  Interaction: Q7Z3Y8; IntAct: EBI-24327528; Score: 0.56
DE  Interaction: Q7Z6G3; IntAct: EBI-24331912; Score: 0.56
DE  Interaction: Q9Y6X4; IntAct: EBI-24348015; Score: 0.56
DE  Interaction: Q6IC98; IntAct: EBI-24604921; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-24695190; Score: 0.56
DE  Interaction: Q8N720; IntAct: EBI-24727726; Score: 0.56
DE  Interaction: A8MW99; IntAct: EBI-23821907; Score: 0.56
DE  Interaction: Q86T90; IntAct: EBI-24423707; Score: 0.56
DE  Interaction: Q8N5Z5; IntAct: EBI-21592259; Score: 0.35
DE  Interaction: P32320; IntAct: EBI-21622979; Score: 0.35
DE  Interaction: P14091; IntAct: EBI-21699601; Score: 0.35
DE  Interaction: P05090; IntAct: EBI-21831285; Score: 0.35
DE  Interaction: Q15303; IntAct: EBI-20980466; Score: 0.37
DE  Interaction: P21860; IntAct: EBI-20981046; Score: 0.37
DE  Interaction: Q01974; IntAct: EBI-20981830; Score: 0.37
DE  Interaction: Q13308; IntAct: EBI-20982474; Score: 0.37
DE  Interaction: O43464; IntAct: EBI-27050249; Score: 0.35
DE  Interaction: Q96LU5; IntAct: EBI-27050332; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: P15924; IntAct: EBI-27113664; Score: 0.35
DE  Interaction: Q9UII2; IntAct: EBI-27113664; Score: 0.35
DE  Interaction: P21802; IntAct: EBI-32721907; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0032587;
GO  GO:0030234;
GO  GO:0004438;
GO  GO:0019903;
GO  GO:0006897;
GO  GO:0010507;
GO  GO:0046856;
GO  GO:0010922;
GO  GO:0050821;
GO  GO:0060304;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEFAELIKTPRVDNVVLHRPFYPAVEGTLCLTGHHLILSSRQDNTEELWLLHSNIDAIDKRFVGSLGTIIIKCKDFRIIQ
SQ  LDIPGMEECLNIASSIEALSTLDSITLMYPFFYRPMFEVIEDGWHSFLPEQEFELYSSATSEWRLSYVNKEFAVCPSYPP
SQ  IVTVPKSIDDEALRKVATFRHGGRFPVLSYYHKKNGMVIMRSGQPLTGTNGRRCKEDEKLINATLRAGKRGYIIDTRSLN
SQ  VAQQTRAKGGGFEQEAHYPQWRRIHKSIERYHILQESLIKLVEACNDQTHNMDRWLSKLEASNWLTHIKEILTTACLAAQ
SQ  CIDREGASILIHGTEGTDSTLQVTSLAQIILEPRSRTIRGFEALIEREWLQAGHPFQQRCAQSAYCNTKQKWEAPVFLLF
SQ  LDCVWQILRQFPCSFEFNENFLIMLFEHAYASQFGTFLGNNESERCKLKLQQKTMSLWSWVNQPSELSKFTNPLFEANNL
SQ  VIWPSVAPQSLPLWEGIFLRWNRSSKYLDEAYEEMVNIIEYNKELQAKVNILRRQLAELETEDGMQESP
//
ID  Q9Z2D0;
PN  Myotubularin-related protein 9;
GN  Mtmr9;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:24591580}. Cell projection, ruffle membrane {ECO:0000269|PubMed:24591580}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QG7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96QG7}. Note=Localizes to ruffles during EGF-induced macropinocytosis (PubMed:24591580). Colocalizes with MTMR6 to the perinuclear region (By similarity). Partially localizes to the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q96QG7, ECO:0000269|PubMed:24591580}.
DR  UNIPROT: Q9Z2D0;
DR  UNIPROT: A6H6P1;
DR  UNIPROT: Q80XL4;
DR  Pfam: PF06602;
DR  PROSITE: PS51339;
DE  Function: Acts as an adapter for myotubularin-related phosphatases (PubMed:12890864). Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5-bisphosphate, and MTMR6 binding affinity for phosphorylated phosphatidylinositols (By similarity). Positively regulates lipid phosphatase MTMR7 catalytic activity (PubMed:12890864). The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels (By similarity). Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles (By similarity). Negatively regulates DNA damage- induced apoptosis, in part via its association with MTMR6 (By similarity). Does not bind mono-, di- and tri-phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine (By similarity). {ECO:0000250|UniProtKB:Q96QG7, ECO:0000269|PubMed:12890864}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3UL36; IntAct: EBI-26888124; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0032587;
GO  GO:0030234;
GO  GO:0004438;
GO  GO:0019903;
GO  GO:0006897;
GO  GO:0010507;
GO  GO:0046856;
GO  GO:0010922;
GO  GO:0050821;
GO  GO:0060304;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MEFAELIKTPRVDNVVLHRPFYTAVEGTLCLTGHHLILSSRQDNTEELWLLHSNIDAIDKRFVGSLGTIIIKCKDFRIIQ
SQ  LDIPGMEECLNIASSIEALSTLDSVTLMYPFFYRPMFEVIEDGWHSFLPEQEFEFYSSATSEWRLSYINKDFSICPSYPP
SQ  TVIVPKSVDDEALRKVAAFRHGGRFPVLSYYHKKNGMVIMRSGQPLTGTNGRRCKEDEKLINATLRAGKRGYLIDTRSLN
SQ  VAQQARAKGGGFEQEAHYPQWRRIHKSIERYHVLQESLIKLVEACNEQTHNMDRWLGKLEASNWLTHIKEILTTACLAAQ
SQ  CIDREGASVLIHGTEGTDSTLQVTSLAQIILEPRSRTIRGFEALIEREWLQAGHPFQQRCAQSAYCSSKQKWEAPVFLLF
SQ  LDCVWQILRQFPCSFEFNEHFLIMLFEHAYASQFGTFLGNNESERCKLKLQQKTMSLWSWVNRPGELSKFTNPLFEANNL
SQ  VIWPSVAPQSLQLWEGIFLRWSRSSKYLDEAYEEMVNIIEYNKELQAKVNVLRRQLAELETEDGL
//
ID  Q86WG5;
PN  Myotubularin-related protein 13;
GN  SBF2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15998640}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:E9PXF8}. Membrane {ECO:0000269|PubMed:15998640}; Peripheral membrane protein {ECO:0000269|PubMed:15998640}. Endosome membrane {ECO:0000250|UniProtKB:E9PXF8}; Peripheral membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:E9PXF8}. Note=Associated with membranes (PubMed:15998640). Localizes to vacuoles in hypo-osmotic conditions (By similarity). Membrane localization is likely to be mediated via its interaction with MTMR2 (By similarity). {ECO:0000250|UniProtKB:E9PXF8, ECO:0000269|PubMed:15998640}.
DR  UNIPROT: Q86WG5;
DR  UNIPROT: Q3MJF0;
DR  UNIPROT: Q68DQ3;
DR  UNIPROT: Q6P459;
DR  UNIPROT: Q6PJD1;
DR  UNIPROT: Q7Z325;
DR  UNIPROT: Q7Z621;
DR  UNIPROT: Q86VE2;
DR  UNIPROT: Q96FE2;
DR  UNIPROT: Q9C097;
DR  Pfam: PF02141;
DR  Pfam: PF02893;
DR  Pfam: PF06602;
DR  Pfam: PF00169;
DR  Pfam: PF12335;
DR  Pfam: PF03456;
DR  PROSITE: PS50211;
DR  PROSITE: PS50003;
DR  PROSITE: PS51339;
DR  OMIM: 604563;
DR  OMIM: 607697;
DR  DisGeNET: 81846;
DE  Function: Guanine nucleotide exchange factor (GEF) which activates RAB21 and possibly RAB28 (PubMed:20937701, PubMed:25648148). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (PubMed:20937701, PubMed:25648148). In response to starvation-induced autophagy, activates RAB21 which in turn binds to and regulates SNARE protein VAMP8 endolysosomal transport required for SNARE-mediated autophagosome-lysosome fusion (PubMed:25648148). Acts as an adapter for the phosphatase MTMR2 (By similarity). Increases MTMR2 catalytic activity towards phosphatidylinositol 3,5-bisphosphate and to a lesser extent towards phosphatidylinositol 3-phosphate (By similarity). {ECO:0000250|UniProtKB:E9PXF8, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:25648148}.
DE  Disease: Charcot-Marie-Tooth disease 4B2 (CMT4B2) [MIM:604563]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie- Tooth disease are designated CMT4. {ECO:0000269|PubMed:12554688, ECO:0000269|PubMed:12687498, ECO:0000269|PubMed:15304601, ECO:0000269|PubMed:15477569}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95248; IntAct: EBI-27115195; Score: 0.42
DE  Interaction: Q13614; IntAct: EBI-27113582; Score: 0.42
DE  Interaction: P01100; IntAct: EBI-2683286; Score: 0.00
DE  Interaction: Q93062; IntAct: EBI-10260028; Score: 0.56
DE  Interaction: Q9Z2D1; IntAct: EBI-11064455; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-11152836; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-11153302; Score: 0.35
DE  Interaction: P46379; IntAct: EBI-11154173; Score: 0.35
DE  Interaction: Q99523; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q13643; IntAct: EBI-24546915; Score: 0.56
DE  Interaction: Q00839; IntAct: EBI-20923842; Score: 0.40
DE  Interaction: Q9NRI5; IntAct: EBI-21389904; Score: 0.00
DE  Interaction: Q13613; IntAct: EBI-27115195; Score: 0.42
DE  Interaction: Q9H773; IntAct: EBI-27116778; Score: 0.27
DE  Interaction: O95881; IntAct: EBI-27116778; Score: 0.27
DE  Interaction: O75439; IntAct: EBI-27116778; Score: 0.27
DE  Interaction: P54819; IntAct: EBI-27116778; Score: 0.27
DE  Interaction: P11413; IntAct: EBI-27116778; Score: 0.27
DE  Interaction: Q9C0B1; IntAct: EBI-27116778; Score: 0.27
DE  Interaction: P22314; IntAct: EBI-27116778; Score: 0.27
DE  Interaction: Q9UL15; IntAct: EBI-27116778; Score: 0.27
DE  Interaction: Q9P0M6; IntAct: EBI-27116778; Score: 0.27
GO  GO:0030424;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005774;
GO  GO:0005085;
GO  GO:0042802;
GO  GO:0019902;
GO  GO:0019208;
GO  GO:0035091;
GO  GO:0006914;
GO  GO:0042552;
GO  GO:0043087;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MARLADYFIVVGYDHEKPGSGEGLGKIIQRFPQKDWDDTPFPQGIELFCQPGGWQLSRERKQPTFFVVVLTDIDSDRHYC
SQ  SCLTFYEAEINLQGTKKEEIEGEAKVSGLIQPAEVFAPKSLVLVSRLYYPEIFRACLGLIYTVYVDSLNVSLESLIANLC
SQ  ACLVPAAGGSQKLFSLGAGDRQLIQTPLHDSLPITGTSVALLFQQLGIQNVLSLFCAVLTENKVLFHSASFQRLSDACRA
SQ  LESLMFPLKYSYPYIPILPAQLLEVLSSPTPFIIGVHSVFKTDVHELLDVIIADLDGGTIKIPECIHLSSLPEPLLHQTQ
SQ  SALSLILHPDLEVADHAFPPPRTALSHSKMLDKEVRAVFLRLFAQLFQGYRSCLQLIRIHAEPVIHFHKTAFLGQRGLVE
SQ  NDFLTKVLSGMAFAGFVSERGPPYRSCDLFDELVAFEVERIKVEENNPVKMIKHVRELAEQLFKNENPNPHMAFQKVPRP
SQ  TEGSHLRVHILPFPEINEARVQELIQENVAKNQNAPPATRIEKKCVVPAGPPVVSIMDKVTTVFNSAQRLEVVRNCISFI
SQ  FENKILETEKTLPAALRALKGKAARQCLTDELGLHVQQNRAILDHQQFDYIIRMMNCTLQDCSSLEEYNIAAALLPLTSA
SQ  FYRKLAPGVSQFAYTCVQDHPIWTNQQFWETTFYNAVQEQVRSLYLSAKEDNHAPHLKQKDKLPDDHYQEKTAMDLAAEQ
SQ  LRLWPTLSKSTQQELVQHEESTVFSQAIHFANLMVNLLVPLDTSKNKLLRTSAPGDWESGSNSIVTNSIAGSVAESYDTE
SQ  SGFEDSENTDIANSVVRFITRFIDKVCTESGVTQDHIKSLHCMIPGIVAMHIETLEAVHRESRRLPPIQKPKILRPALLP
SQ  GEEIVCEGLRVLLDPDGREEATGGLLGGPQLLPAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQN
SQ  QLQQNMQEGLQITSASFQLIKVAFDEEVSPEVVEIFKKQLMKFRYPQSIFSTFAFAAGQTTPQIILPKQKEKNTSFRTFS
SQ  KTIVKGAKRAGKMTIGRQYLLKKKTGTIVEERVNRPGWNEDDDVSVSDESELPTSTTLKASEKSTMEQLVEKACFRDYQR
SQ  LGLGTISGSSSRSRPEYFRITASNRMYSLCRSYPGLLVVPQAVQDSSLPRVARCYRHNRLPVVCWKNSRSGTLLLRSGGF
SQ  HGKGVVGLFKSQNSPQAAPTSSLESSSSIEQEKYLQALLNAVSVHQKLRGNSTLTVRPAFALSPGVWASLRSSTRLISSP
SQ  TSFIDVGARLAGKDHSASFSNSSYLQNQLLKRQAALYIFGEKSQLRNFKVEFALNCEFVPVEFHEIRQVKASFKKLMRAC
SQ  IPSTIPTDSEVTFLKALGDSEWFPQLHRIMQLAVVVSEVLENGSSVLVCLEEGWDITAQVTSLVQLLSDPFYRTLEGFQM
SQ  LVEKEWLSFGHKFSQRSSLTLNCQGSGFAPVFLQFLDCVHQVHNQYPTEFEFNLYYLKFLAFHYVSNRFKTFLLDSDYER
SQ  LEHGTLFDDKGEKHAKKGVCIWECIDRMHKRSPIFFNYLYSPLEIEALKPNVNVSSLKKWDYYIEETLSTGPSYDWMMLT
SQ  PKHFPSEDSDLAGEAGPRSQRRTVWPCYDDVSCTQPDALTSLFSEIEKLEHKLNQAPEKWQQLWERVTVDLKEEPRTDRS
SQ  QRHLSRSPGIVSTNLPSYQKRSLLHLPDSSMGEEQNSSISPSNGVERRAATLYSQYTSKNDENRSFEGTLYKRGALLKGW
SQ  KPRWFVLDVTKHQLRYYDSGEDTSCKGHIDLAEVEMVIPAGPSMGAPKHTSDKAFFDLKTSKRVYNFCAQDGQSAQQWMD
SQ  KIQSCISDA
//
ID  E9PXF8;
PN  Myotubularin-related protein 13;
GN  Sbf2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:16750429, ECO:0000269|PubMed:23297362}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16750429}. Membrane {ECO:0000250|UniProtKB:Q86WG5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q86WG5}. Endosome membrane {ECO:0000269|PubMed:23297362}; Peripheral membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:23297362}. Note=Associated with membranes (By similarity). Localizes to vacuoles in hypo-osmotic conditions (PubMed:16399794). Membrane localization is likely to be mediated via its interaction with MTMR2 (PubMed:23297362). {ECO:0000250|UniProtKB:Q86WG5, ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}.
DR  UNIPROT: E9PXF8;
DR  UNIPROT: E9Q305;
DR  UNIPROT: Q8BJ67;
DR  UNIPROT: Q8BJD2;
DR  UNIPROT: Q8BJP4;
DR  UNIPROT: Q91VH0;
DR  Pfam: PF02141;
DR  Pfam: PF02893;
DR  Pfam: PF06602;
DR  Pfam: PF00169;
DR  Pfam: PF12335;
DR  Pfam: PF03456;
DR  PROSITE: PS50211;
DR  PROSITE: PS50003;
DR  PROSITE: PS51339;
DE  Function: Guanine nucleotide exchange factor (GEF) which activates RAB21 and possibly RAB28 (By similarity). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (By similarity). In response to starvation-induced autophagy, activates RAB21 which in turn binds to and regulates SNARE protein VAMP8 endolysosomal transport required for SNARE-mediated autophagosome-lysosome fusion (By similarity). Acts as an adapter for the phosphatase MTMR2 (PubMed:16399794). Increases MTMR2 catalytic activity towards phosphatidylinositol 3,5-bisphosphate and to a lesser extent towards phosphatidylinositol 3-phosphate (PubMed:16399794). {ECO:0000250|UniProtKB:Q86WG5, ECO:0000269|PubMed:16399794}.
DE  Reference Proteome: Yes;
DE  Interaction: P62158; IntAct: EBI-911456; Score: 0.35
GO  GO:0030424;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005774;
GO  GO:0005085;
GO  GO:0042802;
GO  GO:0019902;
GO  GO:0019208;
GO  GO:0035091;
GO  GO:0006914;
GO  GO:0043087;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MARLADYFIVVGYDHEKPAGPGEGLGKIIQRFPQQDWDDTPFPQGIELFCQPGGWHLSRERKQPTFFVVVLTDIDSDRHY
SQ  CSCLTFYEAEINLQGTKKEEIEGEEVSGLIQPAEVFAPKSLVLVSRLDYPEIFRACLGLIYTVYVDSMSVSLESLIANLC
SQ  ACLVPAAGGSQKLFSLGAGDRQLIQTPLHDSLPVTGTSVALLFQQLGIQNVLNLFCAVLTENKVLFHSASFQRLSDACRA
SQ  LESLMFPLKYSYPYIPILPAQLLEVLSSPTPFIIGVHSIFKTDVHELLDVIIADLDGGTIKIPECIHLSSLPEPLLHQTQ
SQ  SALSLILHPDLEVADHAFPPPRTALSHSKMLDKEVRAVFLRLFAQLFQGYRSCLQLIRIHAEPVIHFHKTAFLGQRGLVE
SQ  NDFLTKVLNGMAFAGFVSERGPPYRACDLFDELVAFEVERIKVEEKNPLKMIKHIRELAEQLFKNENPNPHMAFQKVPRP
SQ  TEGSHLRVHILPFPKINEARVQELIQENLAKNQNAPPATRIEKKCVVPAGPPVVSIMEKVITVFNSAQRLEVVRNCISFI
SQ  FENKTLETEKTLPAALRALKGKAARQCLTDELGLHVQQNRAILDHQQFDYIIRMMNCTLQDCSSLEEYNIAAALLPLTSA
SQ  FYRKLAPGVSQFAYTCVQDHPIWTNQQFWETTFYNAVQEQVRSLYLSAKDDNHIPHLKQKLPDGQHQEKTAMDLAAEQLR
SQ  LWPTLSKSTQQELVQHEESTVFSQAIHFANLMVNLLVPLDTSKNKLLRASAPGDWESGSNSIVTNSIAGSVAESYDTESG
SQ  FEDSENSDVANSVVRFIARFIDKVCTESGVTQDHIRSLHCMIPGIVAMHIETLEAVHRESRRLPPIQKPKILRPALLPGE
SQ  EIVCEGLRVLLDPDGREEATGGLLGGPQLLPAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQNQL
SQ  QQSVQEGLQITSASFQLIKVAFDEEVSPEVVDIFKKQLMKFRYPQSIFSTFAFAAGQTTPQIILPKQKEKNTSFRTFSKT
SQ  IVKGAKKAGKMTIGRQYLLKKRTGTIVEERVNRPGWNEEDDISVSDDSELPTSTTLKASEKSTMEQLVEKACFRDYQRLG
SQ  LGTISGNSSRSKPEYFRVTASNRLYSLCRSYPGLLVIPQAVQDSSLPRVARCYRHNRLPVVCWKNSRSGTLLLRSGGFHG
SQ  KGVVGLFKSQNSPQAVSTSSLESSSSIEQEKYLQALLTAVIVHQKLRGSSTLTVRPALALSPVHGYRDKSFTQSNPKSSA
SQ  KEPVHNQGVWASLRSSTRLISSPTSFIDVGARLAGKDHSASFSNSTYLQNQLLKRQAALYIFGEKSQLRSSKVEFAFNCE
SQ  FVPVEFHEIRQVKASFKKLMRACIPSTIPTDSEVTFLKALGDSEWFPQLHRIMQLAVVVSEVLENGSSVWVCLEEGWDIT
SQ  TQVTSLAQLLSDPFYRTIAGFRTLVEKEWLSFGHKFSQRSSLALNSQGGGFAPIFLQFLDCVHQVHNQYPTEFEFNLYYL
SQ  KFLAFHYVSNRFKTFLLDSDYERLEHGTLFDDKGDKHAKKGVCIWECIDKMHTRSPIFFNYLYSPVEVEALKPNVNVSSL
SQ  KKWDYYTEETLSAGPSYDWMMLTPKHFPYEESDVAGGAGPQSQRKTVWPCYDDVTCSQPDALTRLFSEIEKLEHKLNQTP
SQ  ERWHQLWEKVTTDLKEEPRTAHSLRHSAGSPGIASTNVPSYQKRPALHPLHRGLGEDQSTTTAPSNGVEHRAATLYSQYT
SQ  SKNDENRSFEGTLYKRGALLKGWKPRWFVLDVTKHQLRYYDSGEDTSCKGHIDLAEVEMVIPAGPSMGAPKYTSDKAFFD
SQ  LKTSKRVYNFCAQDGQSAQQWMDRIQSCISDA
//
ID  Q3T0F7;
PN  Myotrophin;
GN  MTPN;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q3T0F7;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P79136; IntAct: EBI-2128149; Score: 0.40
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0008290;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0010613;
GO  GO:0030307;
GO  GO:0010557;
GO  GO:0051092;
GO  GO:0051247;
GO  GO:2000812;
GO  GO:0008361;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDKHHITPLLSAVYEGH
SQ  VSCVKLLLSKGADKTVKGPDGLTAFEATDNQAIKALLQ
//
ID  Q863Z4;
PN  Myotrophin;
GN  MTPN;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q863Z4;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0008290;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0010613;
GO  GO:0030307;
GO  GO:0010557;
GO  GO:0051092;
GO  GO:0051247;
GO  GO:2000812;
GO  GO:0008361;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDKHHITPLLSAVYEGH
SQ  VSCVKLLLSKGADKTVKGPDGLTAFEATDNQAIKALLQ
//
ID  Q91955;
PN  Myotrophin;
GN  MTPN;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q91955;
DR  UNIPROT: Q5ZHL6;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0010613;
GO  GO:0030307;
GO  GO:0010557;
GO  GO:0051092;
GO  GO:0051247;
GO  GO:2000812;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDKHNITPLLSAVYEGH
SQ  VSCVKLLLSKGADKTVKGPDGLTAFEATDNQAIKTLLQ
//
ID  Q7T2B9;
PN  Myotrophin;
GN  mtpn;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q7T2B9;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:2000812;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDKELMWALKNGDLDEVKNILVKAEDVNRTLEGGRKPLHYAADCGQAEMLEFLLSKGADVNAPDKHGITPLLSATYEGH
SQ  VTCVKILLEKGADKNRKGPDGLSAFEAAESEAIKALLE
//
ID  P58546;
PN  Myotrophin;
GN  MTPN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: P58546;
DR  PDB: 3AAA;
DR  PDB: 7DF7;
DR  PDB: 7DSA;
DR  PDB: 7DSB;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  OMIM: 606484;
DR  DisGeNET: 136319;
DE  Function: Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. {ECO:0000250, ECO:0000269|PubMed:10329199, ECO:0000269|PubMed:16895918, ECO:0000269|PubMed:20625546}.
DE  Reference Proteome: Yes;
DE  Interaction: P40337; IntAct: EBI-1061855; Score: 0.00
DE  Interaction: Q9UBN6; IntAct: EBI-1065363; Score: 0.00
DE  Interaction: Q9UET6; IntAct: EBI-1070822; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1075309; Score: 0.00
DE  Interaction: P11171; IntAct: EBI-1075573; Score: 0.00
DE  Interaction: Q6XUX3; IntAct: EBI-1080424; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1080482; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-1080813; Score: 0.00
DE  Interaction: Q9Y478; IntAct: EBI-1082502; Score: 0.00
DE  Interaction: Q9H8T0; IntAct: EBI-2340070; Score: 0.37
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: P28482; IntAct: EBI-3443749; Score: 0.00
DE  Interaction: Q96FW1; IntAct: EBI-10770028; Score: 0.35
DE  Interaction: O15078; IntAct: EBI-11365070; Score: 0.27
DE  Interaction: Q9UPV0; IntAct: EBI-11379107; Score: 0.27
DE  Interaction: Q14203; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q5SW79; IntAct: EBI-11385552; Score: 0.27
DE  Interaction: Q66GS9; IntAct: EBI-11386281; Score: 0.27
DE  Interaction: Q6UVJ0; IntAct: EBI-11388172; Score: 0.27
DE  Interaction: Q7Z7A1; IntAct: EBI-11389211; Score: 0.27
DE  Interaction: Q8N0Z3; IntAct: EBI-11392023; Score: 0.27
DE  Interaction: Q8N137; IntAct: EBI-11392655; Score: 0.27
DE  Interaction: Q96Q45; IntAct: EBI-11396533; Score: 0.27
DE  Interaction: O40945; IntAct: EBI-14064147; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-14035152; Score: 0.35
DE  Interaction: Q9NWT6; IntAct: EBI-15602804; Score: 0.44
DE  Interaction: P13127; IntAct: EBI-15865556; Score: 0.54
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25417249; Score: 0.35
DE  Interaction: Q9NRY4; IntAct: EBI-25408519; Score: 0.35
DE  Interaction: Q3KRB8; IntAct: EBI-25411814; Score: 0.35
DE  Interaction: O15164; IntAct: EBI-25486121; Score: 0.35
DE  Interaction: P83105; IntAct: EBI-25745135; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25686340; Score: 0.35
DE  Interaction: O43318; IntAct: EBI-28931001; Score: 0.35
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0008290;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0043565;
GO  GO:0006584;
GO  GO:0071260;
GO  GO:0021707;
GO  GO:0030182;
GO  GO:0010613;
GO  GO:0030307;
GO  GO:0010557;
GO  GO:0051092;
GO  GO:0051247;
GO  GO:2000812;
GO  GO:0008361;
GO  GO:0016202;
GO  GO:0006417;
GO  GO:0043403;
GO  GO:0051146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDKHHITPLLSAVYEGH
SQ  VSCVKLLLSKGADKTVKGPDGLTAFEATDNQAIKALLQ
//
ID  P62774;
PN  Myotrophin;
GN  Mtpn;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: P62774;
DR  UNIPROT: P80144;
DR  UNIPROT: Q543M6;
DR  UNIPROT: Q9DCN8;
DR  PDB: 2KXP;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin- capping protein complex formed by the CAPZA1 and CAPZB heterodimer. {ECO:0000250, ECO:0000269|PubMed:20538588}.
DE  Reference Proteome: Yes;
DE  Interaction: Q62108; IntAct: EBI-2307988; Score: 0.35
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0008290;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0043565;
GO  GO:0006584;
GO  GO:0071260;
GO  GO:0021707;
GO  GO:0010613;
GO  GO:0030307;
GO  GO:0010557;
GO  GO:0051092;
GO  GO:0051247;
GO  GO:2000812;
GO  GO:0008361;
GO  GO:0043403;
GO  GO:0051146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDKHHITPLLSAVYEGH
SQ  VSCVKLLLSKGADKTVKGPDGLTALEATDNQAIKALLQ
//
ID  P62775;
PN  Myotrophin;
GN  Mtpn;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Nucleus. Cytoplasm, perinuclear region.
DR  UNIPROT: P62775;
DR  UNIPROT: P80144;
DR  UNIPROT: Q58HB3;
DR  UNIPROT: Q9DCN8;
DR  PDB: 1MYO;
DR  PDB: 2MYO;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer (By similarity). Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. {ECO:0000250, ECO:0000269|PubMed:17041682, ECO:0000269|PubMed:18693253}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5XI32; IntAct: EBI-2128081; Score: 0.46
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0008290;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0043565;
GO  GO:0006584;
GO  GO:0071260;
GO  GO:0021707;
GO  GO:0030182;
GO  GO:0010613;
GO  GO:0030307;
GO  GO:0010557;
GO  GO:0051092;
GO  GO:0051247;
GO  GO:2000812;
GO  GO:0008361;
GO  GO:0043403;
GO  GO:0051146;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDKHHITPLLSAVYEGH
SQ  VSCVKLLLSKGADKTVKGPDGLTALEATDNQAIKALLQ
//
ID  Q7T0Q1;
PN  Myotrophin;
GN  mtpn;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q7T0Q1;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDKEFMWALKNGDLDAVKEFVAGGVDVNRTLEGGRKPLHYAADCGQDEIVEFLLAKGANINAADKHGITPLLSACYEGH
SQ  RKCVELFVSKGADKNVKGPDGLNAFESTDNQAIKDLLH
//
ID  Q6P1S6;
PN  Myotrophin;
GN  mtpn;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q6P1S6;
DR  Pfam: PF12796;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DE  Function: Regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:2000812;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDKEFVWAIKNGDLDAVKEFVLGGEDVNRTLDGGRKPMHYAADCGQDEVLEFLLSKGANINAADKHGITPLLSACYEGH
SQ  RKCVELLLSKGADKTVKGPDGLNALESTDNQAIKDLLH
//
ID  O13999;
PN  Meiotically up-regulated gene 155 protein;
GN  mug155;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O13999;
DE  Function: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0051321;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRPTSGCSKDDTIQKQNRRHNTVDNKQEKLPLSIEIFLNKQINKISFDTIRSKQNCRLKEIYCRLKIRCRLKKKFIKSLS
SQ  KKIISYHFISFHTIVVLLLLPPFSHLLVLVYPSVFTTAFYHQKWALRLNPCLPTYFFHRQRQCVTLLIRNANENMRARRV
SQ  NSVMLTKPKQFLFLLEFITLFIFTYCL
//
ID  Q9USG8;
PN  Meiotically up-regulated gene 190 protein;
GN  mug190;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single- pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9USG8;
DR  Pfam: PF00168;
DR  PROSITE: PS50004;
DR  PROSITE: PS51847;
DE  Function: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
DE  Reference Proteome: Yes;
GO  GO:0032541;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005816;
GO  GO:0046872;
GO  GO:0005543;
GO  GO:0043495;
GO  GO:0061817;
GO  GO:0006869;
GO  GO:0051321;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSTHSGDSTKQQHYRSSDPYSGRRPIPTIPKFFRDRKQRAEKKEEQQREQTENEKLFDPITQRDVEINDVHFDYAKTYDD
SQ  PSFTVPNQSIQGSSLPSEKPYLSSNQPTNVYKQHQDDLAPPEADNQITRDVPISDEKTNILFFPSPSIDLSYVSKEVKQK
SQ  TGQYSLFAYIFSLVISWFFTHSIIISAVLPLAISSCMYLWMQNIYAVAKDAEWGAEQKRGEYARLNLIPESAEWMNHLLE
SQ  KVWPLINPEMFSSVADQIEDVMQASIPSFVENVRVASLDQGSHPVRVVSIRSLPSGEASESFSEKQASEAEHKDEPEQQR
SQ  KQFYNFELCLAYHAKPVEDATSTSARASNLHLRIVFYPGIKGTVGFPLPIWVEIKGFVARIRFRCELMPEVPFLKNVTFS
SQ  LMGLPELNVSAVPVAEGGVNIFGLPLISKFVNDAISAAANEYVSPKSMTIDLSKTLLGDDIKKEVNALGVIFVHINRAED
SQ  LSKQDVNGLSDAYITVGFHKFGKPLYCTRVVKQDLNPIWNEYAFIPVFPDQVKAGEKISIELWDSDRFSPDDVVGRTKIG
SQ  LHLLIQDSGKMHERCDTLTGISEDTSLPGRVFYEIGYFPRAEFKPSLKTSGHDITIPRSMRDDPAFQNPHGSLDNKEEEA
SQ  AVTTAPDEEYPSGILSFTVHQAVNLQMNHPTGTFGNVSGNYNTSPAQSVGDVTAEEGSELPSSYVCVDLDDTLVYKTRTK
SQ  VFTSNPIYNAGSEKFVKDWRNAMLCFTVRDFKLREHDSILGVVNIPLATTLTTSSQLTKWYPIQGGIGFGSVRISILFRS
SQ  MKLKIPRNLLGWDIGTLEFMDRQIVAEGTGSVSDVSFSSIRVNIAGVKITAKSSTSNSSSTAEYHVRSRHAVIPVNNRYR
SQ  SAVVFEFRKQLQRKHNVFAMVWLVDLEDNVEQNIRVPIFTSSKPAHVLQNMIDFDHPDKESEFKIIGYLSTRICFHRGLD
SQ  DSHEQLVDNDDEAAIFETYRCLKSMGLRRGYVKDMKNPLADQRASLDESRETTTASSKFESDDSVDTEDEETTTDRTPIE
SQ  CTQTVSMVDPNVNGDIQGRNSLGTMNSNERNLEQEFISLGYASKNRPKAHAQEGTNQPGASENVEPVLADDSDAVTIHSN
SQ  ISSDDQKRKLVNADDRELEKRLHRGPYNSKIVRTGEWVKDGAKMGWRNLRRKFALNGRQPDVETEISK
//
ID  O13712;
PN  Meiotically up-regulated gene 61 protein;
GN  mug61;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein.
DR  UNIPROT: O13712;
DR  UNIPROT: Q9USD6;
DR  Pfam: PF12949;
DR  Pfam: PF09402;
DE  Function: Required for correct meiotic chromosome segregation. {ECO:0000269|PubMed:16303567}.
DE  Reference Proteome: Yes;
DE  Interaction: Q09825; IntAct: EBI-1557581; Score: 0.55
DE  Interaction: Q9P7F8; IntAct: EBI-21242229; Score: 0.37
DE  Interaction: O42841; IntAct: EBI-21242375; Score: 0.37
DE  Interaction: Q9UUJ1; IntAct: EBI-21242353; Score: 0.37
DE  Interaction: Q10436; IntAct: EBI-21242310; Score: 0.37
DE  Interaction: Q10169; IntAct: EBI-21242384; Score: 0.37
DE  Interaction: O13787; IntAct: EBI-21242344; Score: 0.37
DE  Interaction: Q9P6P8; IntAct: EBI-21242431; Score: 0.37
DE  Interaction: Q9P6M1; IntAct: EBI-21242440; Score: 0.37
DE  Interaction: Q09835; IntAct: EBI-21242411; Score: 0.37
DE  Interaction: O14223; IntAct: EBI-21242460; Score: 0.37
DE  Interaction: Q9UT35; IntAct: EBI-21242485; Score: 0.37
DE  Interaction: O42901; IntAct: EBI-21242510; Score: 0.37
DE  Interaction: Q9Y806; IntAct: EBI-21242548; Score: 0.37
DE  Interaction: Q9Y7X6; IntAct: EBI-21242557; Score: 0.37
DE  Interaction: P36596; IntAct: EBI-21242602; Score: 0.37
DE  Interaction: P10815; IntAct: EBI-21242593; Score: 0.37
DE  Interaction: O94361; IntAct: EBI-21242584; Score: 0.37
GO  GO:0034506;
GO  GO:0099115;
GO  GO:0005789;
GO  GO:0000792;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0003682;
GO  GO:0062239;
GO  GO:0140698;
GO  GO:0007059;
GO  GO:0051321;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVPSYFDPDYDPSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSKLRRAKNGLISMTELQQKNVPPSSRSPRRRVAGV
SQ  TNNVTARISSKRKINMVDEANDTEISKTSQFEDNVMGMLQDENVQVLNTNTITISEESEFHASKIAKIDSRNEEITHIPF
SQ  ETQTELNAAVVNLDNSMESSFSIVQNLTNKDSSVDTATYDFSAEVGNIVTPASKFLDYDQSYLVNASVSGDPTPVKVLNT
SQ  TSPKSENPLNQSSFLSFLGENLKPKFTSRSSSVYASPIKSSLNSLECNPSNLLSVRKNFQQSSDSYLKSNKSFDQLNNLV
SQ  GLSTGNSENFTPENNSFSWTHPKKNSSSPLPQSQSSSIFVEHLNQLYEANASIHRPVNPAFSTNFGLEASNTSTPEKKKF
SQ  DSQKPDDDSVNEISSDLGLSTTGIDRVEENISLTKDRQPKRPYFSLGSFISLIFSFTKVVNSLWLVLLVVPLLGFVGFWH
SQ  QEVQRVGFCGVPAEPYPSSLYYLQPGVLRSSIESAYSFAHSLGIEASCQPCPENAECGFNRQLFCKEGLKASFPLLADFG
SQ  LKPYPRCIPNTVKVNKVEEMVQAFMSIIGKWYYKAPKEFATFESAKNLNGKSFVDNFKDRYYMYKQDIDNVVGLKDFKVY
SQ  LKTTLNRLYNSKLTRKVLYYLFSPLFTLELWKLRVRGALSKFPTNCLRSVYSHTVSLMKYLTSAVISCWRIYLLIGILAA
SQ  ITGTVVWRIRVYAKKHVVKHGVSVCVSHCIAKLQKTKLKSLTDFSVNPRVEVVQLRSDCFVSGVADDKGLFELVHLPLSI
SQ  QLEIWEKVVSVLEGMVSVKVWDSERLAKNRAWEWIGVFSDDIAL
//
ID  O13965;
PN  Meiotically up-regulated gene 70 protein;
GN  mug70;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus membrane; Multi-pass membrane protein.
DR  UNIPROT: O13965;
DR  UNIPROT: Q9USF6;
DR  Pfam: PF00571;
DR  Pfam: PF00564;
DR  PROSITE: PS51371;
DR  PROSITE: PS51745;
DE  Function: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0051321;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTVGTLSVVSSTASDTASHVSDTRKRQYQRDEALRKKIISELGKKSGNFESPVRKIRRNGEPGTVDSAALDPALTVHMQS
SQ  LVTETAQLMAAKRQNCVLVVDDDEQLAGIVTATDIATRCVGAGLNARQTLIADIMSTSPLCITSDTRFDDALLLMIEHKF
SQ  RHLPVVSDGGPDGSAGDEGDVIGIINMRACLREPLNRIARQQEAAQKLVEALEGAQEEIENKSVSGNTNSSSVSGNHAAE
SQ  FLEYVESLKKKASGLEIMSLIDSSEEPFLVGTRTTVAEATESMARSGVSAVLVMDNGAVSGVFTAHDVVLRVLAAGLDPY
SQ  RSSVIRVMTPHPDCALASLRVSTALERMIEGKFSNLPVVDESDAIIGMLSLFHLATAIEQTPEEEEEVFDQAENDAGIEP
SQ  SNGFEDQQQQLLGNSNEVVENYDVNPPLPLNPLPSNTQQSESTYEYSARQLPKPPVQAWQNENLSSNNKPQEYVGVENDY
SQ  NFSNNPPTAMSEQSFHPSVSQKPMDTPENGSNSFAASPYLQPYNSASQLAPSYVGSLPQYHGNPSFVEQALQDLVQPTDS
SQ  ASQIFPLNPQSPSQFTIKYRSIAGRVHRLRLDGINSVSDLRTAVEEREKEQLVTLTYIDDEGDVVELVSDSDLREAILLA
SQ  RRRGLPRLEVRGVAAFTNHLESSHPPISTVDSSIGSASVVEKGVANSIVDIHQPTAKADKGNSKKPIYIGIVSSSIVILA
SQ  VSMWYLRRKR
//
ID  O94418;
PN  Meiotically up-regulated gene 87 protein;
GN  mug87;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94418;
DR  Pfam: PF04097;
DE  Function: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051321;
GO  GO:0016973;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVASDDSPKEARGIPFLDQKSRKLANELLEPCLPFIQFNLGEIEQRAKHYLNTVPTSKDGNTKAHYLLAGSGINAEQTW
SQ  KKIESLSLQVRPPTTLELSFTDVDMFLKYHREKNVLNSLEALVQNTQIAFDQYLEEEWRSKAAKSRPSFDNILLENKKRV
SQ  SFYPFSVQRSQKFASTLKMCLEEEALHGFQSKLVSSFCEVAREFAHDTKSLLLYESWKLLSSVILDKDSVTVFGNKGIIS
SQ  KAFDIETEDGSVNSRFYQRISDCSRKFLEAQFFEVLNKEIAKTPQAALVGGVPSIRNKIRAYLNIRLLRNGVWINPDLEI
SQ  IQDVPIWAFIFYLLRCGFLKEAVDFTEENRDLFEKVAEKFPFYINAYAKAPNGILPRQLRSQLFSEFNQTIRLQESSDPY
SQ  KYAVYKIIGRCDLSKTSCPSICSVTEDYIWFQLILSREFTEKSVSAHEFFSLEDVQHILLSYGSDYFTNNGSNPVMYFFL
SQ  LMLCGLYERAINFLYPYFPTDAVHFAITCAYYGLLRTAPSSSVVSNEPGKIQSMLVETKSGKPSLEFDRLLIDYTQTCQE
SQ  LSPVMSACYLIPMCKIDKYISMCHKSLCSLVLSTRDYVNLLGDIRGDGERTPSFLENHRSLIGLSSVKEYLSKITLTAAK
SQ  QADDQGLLSDAILLYHLAEDYDAAVTVINRRLGSALLRFLDQFVFPDKLISLTKSMMDVYNRNPSLYAKVDYKNRETTNL
SQ  LLLTVEAFNAYTNKDYEQALSSLQQLEILPLDPLDSDCETFVVRKLAKEFRFLNENLLQNVPGIVLIAMNSLKELYAKQK
SQ  SSSFGNDAISVDKLRLYRQKARRIVMYSFLIEYRMPSQILEQLNRCEIEMT
//
ID  P09513;
PN  Movement protein;
GN  ORF4;
OS  2169986;
SL  Nucleus Position: SL-0415;
SL  Comments: Host nucleus envelope {ECO:0000269|PubMed:15971210}.
DR  UNIPROT: P09513;
DR  Pfam: PF01659;
DE  Function: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding (PubMed:8623554). The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier (PubMed:8623554). Acts as a suppressor of RNA-mediated gene silencing, also known as post- transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs (PubMed:28994713). {ECO:0000269|PubMed:28994713, ECO:0000269|PubMed:8623554}.
DE  Reference Proteome: Yes;
GO  GO:0044199;
GO  GO:0046740;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQEGGAVEQFGQWLWSNPIEQDPDDEMVDAREEEGQILYLDQQAGLRYSYSQLTTLKPTPPGQSNSAPVYRNAQRFQTE
SQ  YSSPTIVTRSQVSELSLSHTRPPIRQALSLLSSTPRASNQPWVATLIPSPSARPPPRPSGQRQLMGRNSRNQR
//
ID  Q14764;
PN  Major vault protein;
GN  MVP;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15133037, ECO:0000269|PubMed:16441665}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:16441665}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16441665}. Note=5% found in the nuclear pore complex (PubMed:15133037). Translocates from the nucleus to the cytoplasm upon EGF treatment (PubMed:16441665).
DR  UNIPROT: Q14764;
DR  UNIPROT: Q96BG4;
DR  UNIPROT: Q9BPW6;
DR  UNIPROT: Q9BQT1;
DR  UNIPROT: Q9UBD1;
DR  PDB: 1Y7X;
DR  Pfam: PF11978;
DR  Pfam: PF01505;
DR  Pfam: PF17794;
DR  Pfam: PF17795;
DR  Pfam: PF17796;
DR  PROSITE: PS51224;
DR  OMIM: 605088;
DR  DisGeNET: 9961;
DE  Function: Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates IFNG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases. {ECO:0000269|PubMed:15133037, ECO:0000269|PubMed:16418217, ECO:0000269|PubMed:16441665}.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-3933015; Score: 0.44
DE  Interaction: O95271; IntAct: EBI-30837957; Score: 0.44
DE  Interaction: P21980; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: Q06787; IntAct: EBI-26509623; Score: 0.37
DE  Interaction: Q07065; IntAct: EBI-3936356; Score: 0.37
DE  Interaction: P63104; IntAct: EBI-7198482; Score: 0.40
DE  Interaction: Q81TT4; IntAct: EBI-2816262; Score: 0.00
DE  Interaction: A0A6L7HH45; IntAct: EBI-2816269; Score: 0.00
DE  Interaction: Q81ME0; IntAct: EBI-2829464; Score: 0.00
DE  Interaction: A0A6L8PQC3; IntAct: EBI-2829450; Score: 0.00
DE  Interaction: A0A5P8YK76; IntAct: EBI-2863891; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: P34913; IntAct: EBI-3929246; Score: 0.37
DE  Interaction: P00738; IntAct: EBI-3930906; Score: 0.37
DE  Interaction: P52292; IntAct: EBI-3931479; Score: 0.37
DE  Interaction: P00156; IntAct: EBI-3932277; Score: 0.37
DE  Interaction: Q14161; IntAct: EBI-3934710; Score: 0.37
DE  Interaction: Q14764; IntAct: EBI-3934720; Score: 0.80
DE  Interaction: Q13423; IntAct: EBI-3938084; Score: 0.37
DE  Interaction: Q9NUX5; IntAct: EBI-3938387; Score: 0.37
DE  Interaction: Q9WMX2; IntAct: EBI-9079726; Score: 0.37
DE  Interaction: Q8NHY2; IntAct: EBI-9698226; Score: 0.35
DE  Interaction: Q6FHY5; IntAct: EBI-21250233; Score: 0.37
DE  Interaction: Q9QWF0; IntAct: EBI-11015136; Score: 0.35
DE  Interaction: Q9D6T1; IntAct: EBI-11015451; Score: 0.35
DE  Interaction: Q6IRU7; IntAct: EBI-11021803; Score: 0.35
DE  Interaction: P51692; IntAct: EBI-11024794; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: Q5SRY7; IntAct: EBI-11073514; Score: 0.35
DE  Interaction: Q3TRR0; IntAct: EBI-11074327; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: Q06180; IntAct: EBI-11091446; Score: 0.35
DE  Interaction: Q08380; IntAct: EBI-11108487; Score: 0.35
DE  Interaction: Q07797; IntAct: EBI-11108624; Score: 0.35
DE  Interaction: P18031; IntAct: EBI-11122129; Score: 0.35
DE  Interaction: H9XIJ5; IntAct: EBI-11514306; Score: 0.37
DE  Interaction: B4URF7; IntAct: EBI-11515262; Score: 0.37
DE  Interaction: Q16656; IntAct: EBI-24734362; Score: 0.56
DE  Interaction: Q86UW9; IntAct: EBI-24736031; Score: 0.56
DE  Interaction: Q8WUN7; IntAct: EBI-23853018; Score: 0.56
DE  Interaction: Q9H0E2; IntAct: EBI-23930246; Score: 0.56
DE  Interaction: Q96HA8; IntAct: EBI-24587066; Score: 0.56
DE  Interaction: Q53EP0; IntAct: EBI-25274658; Score: 0.56
DE  Interaction: P03431; IntAct: EBI-12579142; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12588645; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q9UMR2; IntAct: EBI-21616596; Score: 0.35
DE  Interaction: Q9UKK3; IntAct: EBI-21846379; Score: 0.35
DE  Interaction: Q9P2K3; IntAct: EBI-21846379; Score: 0.35
DE  Interaction: Q9HD26; IntAct: EBI-21846379; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-21846379; Score: 0.35
DE  Interaction: P62136; IntAct: EBI-16370519; Score: 0.35
DE  Interaction: P61417; IntAct: EBI-20817194; Score: 0.37
DE  Interaction: A0A380PIB3; IntAct: EBI-20817905; Score: 0.37
DE  Interaction: Q14254; IntAct: EBI-20913686; Score: 0.40
DE  Interaction: Q16778; IntAct: EBI-20926138; Score: 0.40
DE  Interaction: Q93079; IntAct: EBI-20926130; Score: 0.40
DE  Interaction: P57053; IntAct: EBI-20926122; Score: 0.40
DE  Interaction: P58876; IntAct: EBI-20926146; Score: 0.40
DE  Interaction: Q5QNW6; IntAct: EBI-20936876; Score: 0.40
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: O60496; IntAct: EBI-25390132; Score: 0.35
DE  Interaction: P20339; IntAct: EBI-25391898; Score: 0.35
DE  Interaction: Q8NHP6; IntAct: EBI-25617558; Score: 0.35
DE  Interaction: P02452; IntAct: EBI-26366205; Score: 0.35
DE  Interaction: P51114; IntAct: EBI-26510810; Score: 0.37
DE  Interaction: P51116; IntAct: EBI-26511983; Score: 0.37
DE  Interaction: Q13363; IntAct: EBI-27045766; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-30816432; Score: 0.44
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:1904813;
GO  GO:0016020;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0034774;
GO  GO:0042802;
GO  GO:0019901;
GO  GO:0019903;
GO  GO:0038127;
GO  GO:0051028;
GO  GO:0042059;
GO  GO:0031953;
GO  GO:0061099;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATEEFIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPMRMVTVPPRHYCTVANPVSRDAQGLVLFDVTGQ
SQ  VRLRHADLEIRLAQDPFPLYPGEVLEKDITPLQVVLPNTALHLKALLDFEDKDGDKVVAGDEWLFEGPGTYIPRKEVEVV
SQ  EIIQATIIRQNQALRLRARKECWDRDGKERVTGEEWLVTTVGAYLPAVFEEVLDLVDAVILTEKTALHLRARRNFRDFRG
SQ  VSRRTGEEWLVTVQDTEAHVPDVHEEVLGVVPITTLGPHNYCVILDPVGPDGKNQLGQKRVVKGEKSFFLQPGEQLEQGI
SQ  QDVYVLSEQQGLLLRALQPLEEGEDEEKVSHQAGDHWLIRGPLEYVPSAKVEVVEERQAIPLDENEGIYVQDVKTGKVRA
SQ  VIGSTYMLTQDEVLWEKELPPGVEELLNKGQDPLADRGEKDTAKSLQPLAPRNKTRVVSYRVPHNAAVQVYDYREKRARV
SQ  VFGPELVSLGPEEQFTVLSLSAGRPKRPHARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVNDRKDPQETAK
SQ  LFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARIIRTAVFGFETSEAKGPDGMALPRPRDQAVFPQNGLVVSSVDV
SQ  QSVEPVDQRTRDALQRSVQLAIEITTNSQEAAAKHEAQRLEQEARGRLERQKILDQSEAEKARKELLELEALSMAVESTG
SQ  TAKAEAESRAEAARIEGEGSVLQAKLKAQALAIETEAELQRVQKVRELELVYARAQLELEVSKAQQLAEVEVKKFKQMTE
SQ  AIGPSTIRDLAVAGPEMQVKLLQSLGLKSTLITDGSTPINLFNTAFGLLGMGPEGQPLGRRVASGPSPGEGISPQSAQAP
SQ  QAPGDNHVVPVLR
//
ID  P09922;
PN  Interferon-induced GTP-binding protein Mx1;
GN  Mx1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:21859714}. Nucleus {ECO:0000269|PubMed:21859714}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. Colocalizes with CCHFV protein N in the perinuclear region. {ECO:0000250|UniProtKB:P20591}.
DR  UNIPROT: P09922;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity against influenza A virus, (IAV), influenza B virus (IBV) and Thogoto virus (THOV). Inhibits FLUAV by interfering with the process of primary transcription, probably by affecting the viral polymerase function. {ECO:0000269|PubMed:17652381, ECO:0000269|PubMed:21651940}.
DE  Reference Proteome: No;
DE  Interaction: Q6P1J9; IntAct: EBI-20726660; Score: 0.35
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0008017;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0009615;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P20591};
SQ  MDSVNNLCRHYEEKVRPCIDLIDTLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLRKL
SQ  KEGEEWRGKVSYDDIEVELSDPSEVEEAINKGQNFIAGVGLGISDKLISLDVSSPNVPDLTLIDLPGITRVAVGNQPADI
SQ  GRQIKRLIKTYIQKQETINLVVVPSNVDIATTEALSMAQEVDPEGDRTIGVLTKPDLVDRGAEGKVLDVMRNLVYPLKKG
SQ  YMIVKCRGQQDIQEQLSLTEAFQKEQVFFKDHSYFSILLEDGKATVPCLAERLTEELTSHICKSLPLLEDQINSSHQSAS
SQ  EELQKYGADIPEDDRTRMSFLVNKISAFNRNIMNLIQAQETVSEGDSRLFTKLRNEFLAWDDHIEEYFKKDSPEVQSKMK
SQ  EFENQYRGRELPGFVDYKAFESIIKKRVKALEESAVNMLRRVTKMVQTAFVKILSNDFGDFLNLCCTAKSKIKEIRLNQE
SQ  KEAENLIRLHFQMEQIVYCQDQVYKETLKTIREKEAEKEKTKALINPATFQNNSQFPQKGLTTTEMTQHLKAYYQECRRN
SQ  IGRQIPLIIQYFILKTFGEEIEKMMLQLLQDTSKCSWFLEEQSDTREKKKFLKRRLLRLDEARQKLAKFSD
//
ID  P79135;
PN  Interferon-induced GTP-binding protein Mx1;
GN  MX1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:19951175}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. Colocalizes with CCHFV protein N in the perinuclear region. {ECO:0000250|UniProtKB:P20591}. [Isoform 2]: Nucleus {ECO:0000269|PubMed:19951175}.
DR  UNIPROT: P79135;
DR  UNIPROT: O46623;
DR  UNIPROT: Q17QZ1;
DR  UNIPROT: Q53ZW3;
DR  UNIPROT: Q867D5;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity against rabies virus (RABV), vesicular stomatitis virus (VSV) and murine pneumonia virus (MPV). Isoform 1 but not isoform 2 shows antiviral activity against vesicular stomatitis virus (VSV). {ECO:0000269|PubMed:16202617, ECO:0000269|PubMed:19951175, ECO:0000269|PubMed:22385204}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0140374;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0070106;
GO  GO:0045071;
GO  GO:0034340;
GO  GO:0034342;
GO  GO:0009615;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P20591};
SQ  MVHSDLGIEELDSPESSLNGSEDMESKSNLYSQYEEKVRPCIDLIDSLRSLGVEQDLALPAIAVIGDQSSGKSSVLEALS
SQ  GVALPRGSGIVTRCPLVLRLKKLGNEDEWKGKVSFLDKEIEIPDASQVEKEISEAQIAIAGEGTGISHELISLEVSSPHV
SQ  PDLTLIDLPGITRVAVGNQPPDIEYQIKSLIRKYILRQETINLVVVPANVDIATTEALRMAQEVDPQGDRTIGILTKPDL
SQ  VDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQDIKHRMSLDKALQRERIFFEDHAHFRDLLEEGKATIPCLAERLTSEL
SQ  IMHICKTLPLLENQIKETHQRITEELQKYGKDIPEEESEKMFCLIEKIDTFNKEIISTIEGEEFVEQYDSRLFTKVRAEF
SQ  SKWSAVVEKNFEKGYEAIRKEIKQFENRYRGRELPGFVNYKTFETIIKKQVRVLEEPAVDMLHTVTDIIRNTFTDVSGKH
SQ  FNEFFNLHRTAKSKIEDIRLEQENEAEKSIRLHFQMEQLVYCQDQVYRRALQQVREKEAEEEKNKKSNHYFQSQVSEPST
SQ  DEIFQHLTAYQQEVSTRISGHIPLIIQFFVLRTYGEQLKKSMLQLLQDKDQYDWLLKERTDTRDKRKFLKERLERLTRAR
SQ  QRLAKFPG
//
ID  Q9N0Y3;
PN  Interferon-induced GTP-binding protein Mx1;
GN  MX1;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15767791}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250}.
DR  UNIPROT: Q9N0Y3;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0070382;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0008017;
GO  GO:0051607;
GO  GO:0045087;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVNSQGKITDSNPVPNHVLLNGLTDKAEKNQGIGNSLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKS
SQ  SVLEALSGVALPRGSGIVTRCPLVLKLKKLINEDEWRGKVSYQDTEMEISDPSEVEVEINKAQDAIAGEGQGISHELISL
SQ  EVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQTKQLIRKYILKQETINLVVVPCNVDIATTEALSMAQEVDPDGDRTIG
SQ  ILTKPDLVDRGTEGKVVDVAQNLVCHLKKGYMIVKCRGQQDIQDQVSLAEALQKEKDFFEDHPHFRVLLEEGRATVPNLA
SQ  EKLTSELITHICKTLPLLENQIKENHEKITEELQKYGSDVPEDEHEKMFFLIDKLNAFNQDISSLIQGEESVGEDESRLF
SQ  TKIRNEFHKWSAVIEKKFQRGYKAIYKQMEKFENRYRGRELPGFVNYKTFEIIIKQQIKELEEPAVDMLHTITDMVQVAF
SQ  GDISKANFDEFFNLYRTTKSKIEDIKFELEKEAEKSIRLHFQMEQIVYCQDHVYQRALQRVREKDSDEEKKKKTSSMSHD
SQ  EVSSVNISLSEILEHLLAYRQEATNRISSHIPLIIQYFILQVYGQKLQNGMLQLLQDKDTYSWLLKERSDTSDKRKFLKE
SQ  RLARLAQARRRLAKFPG
//
ID  Q4ADG8;
PN  Interferon-induced GTP-binding protein Mx1;
GN  MX1;
OS  34886;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250}.
DR  UNIPROT: Q4ADG8;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0051607;
GO  GO:0045087;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVNSKGKITDSDPGSSHLLLNGLADKAGKNQDTEPENSLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSG
SQ  KSSVLEALSGVALPRGSGIVTRCPLVLKLKKLLNKDEWRGKVSYQDFEMEISDPSEVEVEINKAQNAIAGEGQGISHELI
SQ  SLEVSSPHVPDLTLIDLPGITRVAVGNQPADIGHQTKKLIKKYILKQETINLVVVPCNVDIATTEALSMAEEVDPDGDRT
SQ  IGILTKPDLVDRGTESKVVDVAQNLVCHLKKGYMIVKCRGQQDIQDQVTLTEALQKERDFFEDHPHFRVLLEEGRATVPC
SQ  LADRLTSELITHICKTLPLLENQIKENYEKITEELQKYGSDVPEEEHEKMFFLIEKINAFNHDITSLTEGEEFVGEDECR
SQ  LFTKIRNEFHKWSLVIEKRFQRGYKAICKQIERFENRYRGRELPGFVNYKTFEIIIKQQIKELEEPAVYMLHTITDMVQA
SQ  AFTDISEANFAEFFNLYRTTKSKIEDIKFELEKEAEKSIRLHFQMEQIVYCQDQVYQCALQRVREESDKGKDRKINSMCS
SQ  KEVSSVNISLSDIFEHLLAYRQEATNRISSHIPLIIQYFILQVYGQKLQKDMLLLLHDKDTHNWLLKERSDTSDKRKLLK
SQ  ERLARLAQARRRLAKFPG
//
ID  Q28379;
PN  Interferon-induced GTP-binding protein Mx1;
GN  MX1;
OS  9796;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P20591}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
DR  UNIPROT: Q28379;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0008017;
GO  GO:0051607;
GO  GO:0045087;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P20591};
SQ  MVHSEAKMTRPDSASASKQQLLNGNADIQETNQKRSIEKNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQS
SQ  SGKSSVLEALSGVALPRGSGIVTRCPLVLKLKRLVKEDEWKGKVSYRDIEVEISNALDVEEQVRKAQNVLAGEGVGISQE
SQ  LVTLEVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQIKTLIRKYIQRQETINLVVVPSNVDIATTEALSMAQEVDPEGD
SQ  RTIGILTKPDLVDKGTEEQVVDVVRNLICHLKKGYMIVKCRGQQDIQDRLSLAEALQREKAFFEENPYFRGLLEEGRASV
SQ  PCLAERLTTELITHISKSLPLLENQIKESYQNLSDELQKYGTDIPEDETEKTFFLIVKITTFNQNITSFVQGEELVGPND
SQ  TRLFNKIRQEFQKWSGVIENNFRKGGEAIRRQIWTFENQYRGRELPGFVNYRTFETIIKQQIQLLEEPAIDMLHRISDLV
SQ  RDTFTKVSEKNFSEFFNLHRTTKSKLEDIKLEQENEAEKSIRLHFQMEKIVYCQDHVYRGTLQKVRENEMEEEKKKKTIN
SQ  VWGQNTSTESSMAEILEHLNAYQHEAGNRLSTHIPLIIQFFVLQTFGQQLQKSMLQLLQDRDTYDWLLKERNDTCDKRKF
SQ  LKERLARLAQARRRLAKFPG
//
ID  P20591;
PN  Interferon-induced GTP-binding protein Mx1, N-terminally processed;
GN  MX1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:21992152, ECO:0000269|PubMed:9060610}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15355513, ECO:0000269|PubMed:16413306, ECO:0000269|PubMed:21992152}; Peripheral membrane protein {ECO:0000269|PubMed:16413306}; Cytoplasmic side. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15047845}. Note=Binds preferentially to negatively charged phospholipids (PubMed:21900240). Colocalizes with CCHFV protein N in the perinuclear region (PubMed:15047845). {ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:21900240}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:20603636}. Nucleus {ECO:0000269|PubMed:20603636}. Note=Translocates into the nuclei of HSV-1 infected cells (PubMed:20603636). {ECO:0000269|PubMed:20603636}.
DR  UNIPROT: P20591;
DR  UNIPROT: B2RDA5;
DR  UNIPROT: B3KU10;
DR  UNIPROT: C9IYV7;
DR  UNIPROT: C9J8D6;
DR  UNIPROT: C9JN19;
DR  UNIPROT: C9JN88;
DR  UNIPROT: C9JUL1;
DR  UNIPROT: C9JZS6;
DR  UNIPROT: D3DSI8;
DR  UNIPROT: Q86YP5;
DR  UNIPROT: Q96CI3;
DR  PDB: 3LJB;
DR  PDB: 3SZR;
DR  PDB: 3ZYS;
DR  PDB: 4P4S;
DR  PDB: 4P4T;
DR  PDB: 4P4U;
DR  PDB: 5GTM;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DR  OMIM: 147150;
DR  DisGeNET: 4599;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity against a wide range of RNA viruses and some DNA viruses. Its target viruses include negative-stranded RNA viruses and HBV through binding and inactivation of their ribonucleocapsid. May also antagonize reoviridae and asfarviridae replication. Inhibits thogoto virus (THOV) replication by preventing the nuclear import of viral nucleocapsids. Inhibits La Crosse virus (LACV) replication by sequestering viral nucleoprotein in perinuclear complexes, preventing genome amplification, budding, and egress. Inhibits influenza A virus (IAV) replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. Enhances ER stress- mediated cell death after influenza virus infection. May regulate the calcium channel activity of TRPCs. {ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:14687945, ECO:0000269|PubMed:14752052, ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:15355513, ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:16202617, ECO:0000269|PubMed:16413306, ECO:0000269|PubMed:17374778, ECO:0000269|PubMed:18668195, ECO:0000269|PubMed:19109387, ECO:0000269|PubMed:21900240, ECO:0000269|PubMed:21992152}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y210; IntAct: EBI-929361; Score: 0.58
DE  Interaction: Q13507; IntAct: EBI-929460; Score: 0.52
DE  Interaction: Q9UBN4; IntAct: EBI-929536; Score: 0.52
DE  Interaction: Q9UL62; IntAct: EBI-929568; Score: 0.40
DE  Interaction: Q9HCX4; IntAct: EBI-929592; Score: 0.40
DE  Interaction: P48995; IntAct: EBI-929688; Score: 0.40
DE  Interaction: A0A6L8PKS7; IntAct: EBI-2829457; Score: 0.00
DE  Interaction: Q81K97; IntAct: EBI-2829443; Score: 0.00
DE  Interaction: A0A5P8YLE8; IntAct: EBI-2863884; Score: 0.00
DE  Interaction: P27958; IntAct: EBI-8788892; Score: 0.27
DE  Interaction: Q8IUQ4; IntAct: EBI-10200608; Score: 0.56
DE  Interaction: Q9H9S4; IntAct: EBI-10309833; Score: 0.56
DE  Interaction: P20591; IntAct: EBI-10484340; Score: 0.87
DE  Interaction: P32502; IntAct: EBI-11525838; Score: 0.56
DE  Interaction: P38340; IntAct: EBI-11528500; Score: 0.56
DE  Interaction: Q02821; IntAct: EBI-11534426; Score: 0.56
DE  Interaction: P59942; IntAct: EBI-24324105; Score: 0.56
DE  Interaction: O75928; IntAct: EBI-24637753; Score: 0.56
DE  Interaction: Q8IVT5; IntAct: EBI-14035152; Score: 0.35
DE  Interaction: Q9Y276; IntAct: EBI-21901591; Score: 0.40
DE  Interaction: Q68D27; IntAct: EBI-21261783; Score: 0.35
DE  Interaction: Q08380; IntAct: EBI-21261783; Score: 0.50
DE  Interaction: P63167; IntAct: EBI-21261783; Score: 0.35
DE  Interaction: P12532; IntAct: EBI-21261783; Score: 0.35
DE  Interaction: O75096; IntAct: EBI-21261783; Score: 0.35
DE  Interaction: Q9ULX6; IntAct: EBI-26451653; Score: 0.35
DE  Interaction: P51114; IntAct: EBI-26510819; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0140374;
GO  GO:0006915;
GO  GO:0006952;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0070106;
GO  GO:0045071;
GO  GO:0034340;
GO  GO:0009615;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16413306};
SQ  MVVSEVDIAKADPAAASHPLLLNGDATVAQKNPGSVAENNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQS
SQ  SGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNAIAGEGMGISHE
SQ  LITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVDIATTEALSMAQEVDPEGD
SQ  RTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFENHPYFRDLLEEGKATV
SQ  PCLAEKLTSELITHICKSLPLLENQIKETHQRITEELQKYGVDIPEDENEKMFFLIDKVNAFNQDITALMQGEETVGEED
SQ  IRLFTRLRHEFHKWSTIIENNFQEGHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLHTVTDMV
SQ  RLAFTDVSIKNFEEFFNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQIVYCQDQVYRGALQKVREKELEEEKKKKSWD
SQ  FGAFQSSSATDSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKR
SQ  KFLKERLARLTQARRRLAQFPG
//
ID  A1E2I4;
PN  Interferon-induced GTP-binding protein Mx1;
GN  MX1;
OS  9544;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P20591}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
DR  UNIPROT: A1E2I4;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0008017;
GO  GO:0051607;
GO  GO:0045087;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P20591};
SQ  MVLSEVDIVKADPAAASQPLLLNGDADVAQKSPGSVAENNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQS
SQ  SGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEDEWRGKVSYQDYEIEILDASEVEKEINKAQNTIAGEGMGISHE
SQ  LITLEISSRDVPDLTLIDLPGITRVAVGNQPPDIGYKIKTLIRKYIQRQETINLVVVPSNVDIATTEALSMAQEVDPEGD
SQ  RTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFEDHPHFRDLLEEGKATI
SQ  PCLAEKLTSELIAHICKSLPLLENQIKESHQGITEELQKYGVDIPEDENEKMFFLIDKINAFNQDITALIQGEETVGEDD
SQ  SRLFTRLRREFHKWGIIIENNLQEGHKITSRKMQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVNMLHTVTDMV
SQ  RLAFTDVSMKNFEELFNLHRTAKSKIEDIRTEQEREGEKLIRLHFQMEQIVYCQDQVYRGALQKVREKELEEEKKKKSWD
SQ  IGTFQPSSTESSMEEIFQHLMAYHQEASKRISSHIPLVIQFFMLQMYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRK
SQ  FLKERLARLTQARRRLAQFPG
//
ID  Q4ADG7;
PN  Interferon-induced GTP-binding protein Mx1;
GN  MX1;
OS  161932;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250}.
DR  UNIPROT: Q4ADG7;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0051607;
GO  GO:0045087;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVNSKGKITDSDPGSSHLLLNGLADKAGKNQDTEPENSLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSG
SQ  KSSVLEALSGVALPRGSGIVTRCPLVLKLKKLLNKDEWRGKVSYQDFEMEISDPSEVEVEINKAQNAIAGEGQGISHELI
SQ  SLEVSSPHVPDLTLIDLPGITRVAVGNQPADIGHQTKKLIKKYILKQETINLVVVPCNVDIATTEALSMAQEVDPDGDRT
SQ  IGILTKPDLVDRGTESKVVDVAQNLVCHLKKGYMIVKCRGQQDIQDQVTLTEALQKERDFFEDHPHFRVLLEEGRATVPC
SQ  LADRLTSELITHICKTLPLLEKQIKENYEKITEELQKYGSDVPEEEHEKMFFLIEKINAFNHDITSLTEGEEFVGEDECR
SQ  LFTKIRNEFHKWSLVIEKRFQQGYKAICKQIERFENRYRGRELPGFVNYKTFEIIIKQQIKELEEPAVYMLHTITDMVQA
SQ  AFTDISEANFAEFFNLYRTTKSKIEDIKFELEKEAEKSIRLHFQMEQIVYCQDQVYQCALQRVREESDKEKDKKINSMCS
SQ  KEVSSVNISLSDIFEHLLAYRQEATNRISSHIPLIIQYFILQVYGQKLQKDMLLLLHDKDTHNWLLKERSDTRDKRKLLK
SQ  ERLARLAQARRRLAKFPG
//
ID  Q4ADG6;
PN  Interferon-induced GTP-binding protein Mx1;
GN  MX1;
OS  9720;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250}.
DR  UNIPROT: Q4ADG6;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0051607;
GO  GO:0045087;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVNSKGEITDSDPGSNHLLLNGLPDKAGKNQDTEPENSLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSG
SQ  KSSVLEALSGVALPRGSGIVTRCPLVLKLKKLLNEDEWRGKVSYQDFEMEISDPSEVEVEISKAQNVIAGEGQGISHELI
SQ  SLEVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQTKQLIRKYILKQETINLVVVPCNVDIATTEALSMAQEVDPSGDRT
SQ  IGILTKPDLVDRGTESKVVDVAQNLVCHLKKGYMIVKCRGQQDIQDQVTLTEALQKERDFFEDHPHFRVLLEEGRATVPC
SQ  LADKLTSELITHICKTLPLLENQIKENHEKITEELKKYGSDVPEEEHEKMFFLIEKINAFNHDINSLIEGEEFVGEDESR
SQ  LFTKIRNEFHKWSCVIEKKFQQGYKAIYKQIEKFENRYRGRELPGFVNYKTFEIIIKQQIKELEEPAVYMLHMVTDMVQA
SQ  AFTDISEANFAEFFNLYRTTKSKIEDIKFELEKEAEKSIRLHFQMEQIVYCQDQVYQRALQRVREKVADEEKNKKINSMS
SQ  SEEVSSVNISLSEIFEHLLAYRQEATNRISSHIPLIIQYFILQAYGQKLQKGMLQLLQDKDTYNWLLKERSDTSDKRKFL
SQ  KERLSRLAQARRRLAKFPG
//
ID  P27594;
PN  Interferon-induced GTP-binding protein Mx1;
GN  MX1;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17203407, ECO:0000269|PubMed:19109387}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
DR  UNIPROT: P27594;
DR  UNIPROT: Q1AHC4;
DR  UNIPROT: Q75PY7;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity against influenza A virus, (IAV). Inhibits IAV replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. {ECO:0000269|PubMed:20167191}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0008017;
GO  GO:0071357;
GO  GO:0051607;
GO  GO:0016197;
GO  GO:1901253;
GO  GO:0045071;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P20591};
SQ  MVYSSCESKEPDSVSASNHLLLNGNDELVEKSHKTGPENNLYSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQS
SQ  SGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEEDEWKGKVSYRDSEIELSDASQVEKEVSAAQIAIAGEGVGISH
SQ  ELISLEVSSPHVPDLTLIDLPGITRVAVGNQPYDIEYQIKSLIKKYICKQETINLVVVPCNVDIATTEALRMAQEVDPEG
SQ  DRTIGILTKPDLVDKGTEDKIVDVARNLVFHLKKGYMIVKCRGQQDIQEQLSLAKALQKEQAFFENHAHFRDLLEEGRAT
SQ  IPCLAERLTSELIMHICKTLPLLENQIKESHQKITEELQKYGSDIPEDESGKMFFLIDKIDAFNSDITALIQGEELVVEY
SQ  ECRLFTKMRNEFCRWSAVVEKNFKNGYDAICKQIQLFENQYRGRELPGFVNYKTFETIIKKQVSVLEEPAVDMLHTVTDL
SQ  VRLAFTDVSETNFNEFFNLHRTAKSKIEDIKLEQEKEAETSIRLHFQMEQIVYCQDQVYRGALQKVREKEAEEEKNRKSN
SQ  QYFLSSPAPSSDPSIAEIFQHLIAYHQEVGKRISSHIPLIIQFFILRTFGQQLQKSMLQLLQNKDQYDWLLRERSDTSDK
SQ  RKFLKERLMRLTQARRRLAKFPG
//
ID  Q5R5G3;
PN  Interferon-induced GTP-binding protein Mx1;
GN  MX1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P20591}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
DR  UNIPROT: Q5R5G3;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0051607;
GO  GO:0045087;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P20591};
SQ  MVLSEVDIAKADPAAASHPVLLNGDANVAQKNLGSVAENNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQS
SQ  SGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNTIAGEGMGISHE
SQ  LITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVDIATTEALSMAQEVDPEGD
SQ  RTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFEDHPYFRDLLEEGKATV
SQ  PCLAEKLTSELITHICKSLPLLENQIRESHQRITEELQKYGVDVPEDENEKMFFLIDKINAFNQDITALIQGEETVGEED
SQ  IRLFTRLRHEFHKWSIIIENNFQEGHKILSRKIQKFENQYRGRGLPGFVNYRTFETIVKQQIKALEEPAVDMLHTVTDMV
SQ  RLAFTDVSIKNFEEFFNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQIVYCQDQVYRGALQKVREKELEEEKKKKSWD
SQ  FGAFQSSSATDSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERGDTSDKR
SQ  KFLKERLARLTQARRRLAQFPG
//
ID  P18588;
PN  Interferon-induced GTP-binding protein Mx1;
GN  Mx1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:2173790}. Cytoplasm {ECO:0000250|UniProtKB:P20591}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
DR  UNIPROT: P18588;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase which has antiviral activity against influenza A virus, (IAV) and Thogoto virus (THOV). Inhibits IAV by interefering with the process of primary transcription, probably by affecting the viral polymerase function (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0140374;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0070106;
GO  GO:0045071;
GO  GO:0009615;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P20591};
SQ  MKERTSACRHGTPQKHPDTSEESQAMESVDNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEA
SQ  LSGVALPRGSGIVTRCPLVLKLKQLKQGEKWSGKVIYKDTEIEISHPSLVEREINKAQNLIAGEGLKISSDLISLEVSSP
SQ  HVPDLTLIDLPGITRVAVGDQPADIEHKIKRLITEYIQKQETINLVVVPSNVDIATTEALKMAQEVDPQGDRTIGILTKP
SQ  DLVDRGTEDKVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRVLLEDGKATVPCLAKRLTM
SQ  ELTSHICKSLPILENQINVNHQIASEELQKYGADIPEDDSKRLSFLMNKINVFNKDILSLVQAQENISWEESRLFTKLRN
SQ  EFLAWNDYIEEHFKKTLGSSEKHSQMEKFESHYRGRELPGFVDYKAFENIIKKEVKALEEPALNMLHRVTTMVKNAFTKV
SQ  SSNNFGDFLNLHSTAKSKIEDIRFNQEKEAEKLIRLHFQMEHIVYCQDQAYKKALQEIREKEAEKEKSTFGAFQHNSPRK
SQ  ELTTTEMTQHLNAYYQECGRNIGRQIPLIIQYSILQTFGQEMEKAMLQLLQDTSKCNWFLTEQSDSREKKKFLKRRLLRL
SQ  DEAQRKLAKFSN
//
ID  P33237;
PN  Interferon-induced GTP-binding protein Mx1;
GN  MX1;
OS  9940;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P20591}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
DR  UNIPROT: P33237;
DR  UNIPROT: Q95MD4;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DE  Function: Interferon-induced dynamin-like GTPase with antiviral activity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0048471;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0045087;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P20591};
SQ  MVLSDLDIKEPDSPESGLNGSDDMVREHETESKGNLYSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSS
SQ  VLEALSGVALPRGSGIVTRCPLVLRLKKLEKEGEWKGKVSFLDREIEISDASQVEKEISEAQIAIAGEGMGISHELISLE
SQ  VSSPHVPDLTLIDLPGITRVAVGNQPHDIEYQIKSLIRKYILRQETINLVVVPANVDIATTEALRMAQDVDPQGDRTIGI
SQ  LTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQHRLSLDKALQRERIFFEDHTHFRDLLEEGRATIPCLAE
SQ  RLTNELIMHICKTLPLLENQIKETHQRITEELQKYGKDIPEEESEKMFSLIEKIDTFNKEIISTIEGEEHVGQYDSRLFT
SQ  KVRAEFCKWSAVVEKNFEKGHEAIRKEIKQFENRYRGRELPGFVNYKTFEIIIKKQVIVLEEPAVDMLHTVTDIIRNTFT
SQ  EVSGKHFSEFFNLHRTAKSKIEDIRLEQENEAEKSIRLHFQMEQLVYCQDQVYRRALQQVREKEAEEEKKKKSNHYYQSE
SQ  DSEPSTAEIFQHLMAYHQEVSTRISSHIPLIIQFFVLRTYGEQLKKSMLQLLQDKDQYDWLLKERTDTRDKRKFLKERLE
SQ  RLSRARQRLAKFPG
//
ID  P20592;
PN  Interferon-induced GTP-binding protein Mx2;
GN  MX2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15184662}. Nucleus {ECO:0000269|PubMed:15184662}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:15184662}. Note=Localization to nuclear pores requires GTP-binding.
DR  UNIPROT: P20592;
DR  UNIPROT: B7Z5D3;
DR  UNIPROT: D3DSI7;
DR  PDB: 4WHJ;
DR  PDB: 4X0R;
DR  PDB: 5UOT;
DR  Pfam: PF01031;
DR  Pfam: PF00350;
DR  Pfam: PF02212;
DR  PROSITE: PS00410;
DR  PROSITE: PS51718;
DR  PROSITE: PS51388;
DR  OMIM: 147890;
DR  DisGeNET: 4600;
DE  Function: Interferon-induced dynamin-like GTPase with potent antiviral activity against human immunodeficiency virus type 1 (HIV-1). Acts by targeting the viral capsid and affects the nuclear uptake and/or stability of the HIV-1 replication complex and the subsequent chromosomal integration of the proviral DNA. Exhibits antiviral activity also against simian immunodeficiency virus (SIV-mnd). May play a role in regulating nucleocytoplasmic transport and cell-cycle progression. {ECO:0000269|PubMed:15184662, ECO:0000269|PubMed:24048477, ECO:0000269|PubMed:24055605, ECO:0000269|PubMed:24121441}.
DE  Reference Proteome: Yes;
DE  Interaction: A2ABF9; IntAct: EBI-10200624; Score: 0.56
DE  Interaction: O75928; IntAct: EBI-10200636; Score: 0.56
DE  Interaction: Q8WXE1; IntAct: EBI-10200646; Score: 0.56
DE  Interaction: Q96KQ7; IntAct: EBI-24422219; Score: 0.56
DE  Interaction: P16749; IntAct: EBI-15832895; Score: 0.41
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0008017;
GO  GO:0006952;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0051726;
GO  GO:0046822;
GO  GO:0035455;
GO  GO:0009615;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKAHKPWPYRRRSQFSSRKYLKKEMNSFQQQPPPFGTVPPQMMFPPNWQGAEKDAAFLAKDFNFLTLNNQPPPGNRSQP
SQ  RAMGPENNLYSQYEQKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLK
SQ  KQPCEAWAGRISYRNTELELQDPGQVEKEIHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRD
SQ  IGLQIKALIKKYIQRQQTINLVVVPCNVDIATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEKSVMNVVRNLTYPLKK
SQ  GYMIVKCRGQQEITNRLSLAEATKKEITFFQTHPYFRVLLEEGSATVPRLAERLTTELIMHIQKSLPLLEGQIRESHQKA
SQ  TEELRRCGADIPSQEADKMFFLIEKIKMFNQDIEKLVEGEEVVRENETRLYNKIREDFKNWVGILATNTQKVKNIIHEEV
SQ  EKYEKQYRGKELLGFVNYKTFEIIVHQYIQQLVEPALSMLQKAMEIIQQAFINVAKKHFGEFFNLNQTVQSTIEDIKVKH
SQ  TAKAENMIQLQFRMEQMVFCQDQIYSVVLKKVREEIFNPLGTPSQNMKLNSHFPSNESSVSSFTEIGIHLNAYFLETSKR
SQ  LANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYRLTQARHALCQFSSKEIH
//
ID  Q8R411;
PN  Myc target protein 1;
GN  Myct1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q8R411;
DR  UNIPROT: Q3UQ11;
DR  UNIPROT: Q8C6M8;
DR  UNIPROT: Q9D182;
DR  Pfam: PF15179;
DE  Function: May regulate certain MYC target genes, MYC seems to be a direct upstream transcriptional activator. Does not seem to significantly affect growth cell capacity. Overexpression seems to mediate many of the known phenotypic features associated with MYC, including promotion of apoptosis, alteration of morphology, enhancement of anchorage-independent growth, tumorigenic conversion, promotion of genomic instability and inhibition of hematopoietic differentiation. {ECO:0000269|PubMed:11909865}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0061484;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MANNTTSLGSPWPENFWEDLIMSFTVSVAIGLAIGGFLWALFVFLSRRRRASAPISQWSPTRRPRSSYNHGLNRTGFYRH
SQ  SGYERRSNLSLASLTFQRQASMELVNSFPRKSSFRASTFHPFLQCPPLPVETESQLMTLSASTTPSTLSTAHSPSRPDFR
SQ  WSSNSLRMGLSTPPPPAYESIIKAFPDS
//
ID  Q0WPU1;
PN  Myosin-15;
GN  XI;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17288617, ECO:0000269|PubMed:17500056}. Nucleus membrane {ECO:0000269|PubMed:23973298}. Note=Colocalizes with peroxisome, cytoplasmic vesicles and/or organelles. Nucleus membrane localization is dependent of the WIT2 association. {ECO:0000269|PubMed:17288617, ECO:0000269|PubMed:17500056}.
DR  UNIPROT: Q0WPU1;
DR  UNIPROT: Q9SMY9;
DR  Pfam: PF01843;
DR  Pfam: PF00612;
DR  Pfam: PF00063;
DR  Pfam: PF02736;
DR  PROSITE: PS51126;
DR  PROSITE: PS50096;
DR  PROSITE: PS51456;
DR  PROSITE: PS51844;
DE  Function: Myosin heavy chain that is required for the cell cycle- regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in trafficking of Golgi stacks and mitochondria. Plays a role in nuclear shape determination. Drives nuclear movement along actin filaments (PubMed:23973298). As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:19369591, ECO:0000269|PubMed:20581304, ECO:0000269|PubMed:21914656, ECO:0000269|PubMed:23973298, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
GO  GO:0015629;
GO  GO:0005737;
GO  GO:0016459;
GO  GO:0031965;
GO  GO:0051015;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0003774;
GO  GO:0000146;
GO  GO:0007015;
GO  GO:0030048;
GO  GO:0007097;
GO  GO:2000769;
GO  GO:0030050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRNCLPMELNLRKGDKVWVEDKDLAWIAADVLDSFDNKLHVETSTGKKVFVSPEKLFRRDPDDEEHNGVDDMTKLTYLHE
SQ  AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS
SQ  GESGAGKTETTKLIMQYLTFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIR
SQ  TYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDEQ
SQ  EGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAVTS
SQ  RDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRK
SQ  EEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSETDFTLSHYAGKVTY
SQ  QTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKPNS
SQ  LNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTEKILSKLGLGNYQLGRT
SQ  KVFLRAGQIGILDSRRAEVLDASARLIQRRLRTFVTHQNFISARASAISIQAYCRGCLSRNAYATRRNAAAAVLVQKHVR
SQ  RWLSRCAFVKLVSAAIVLQSCIRADSTRLKFSHQKEHRAASLIQAHWRIHKFRSAFRHRQSSIIAIQCRWRQKLAKREFR
SQ  KLKQVANEAGALRLAKTKLEKRLEDLEWRLQLEKRLRTSGEEAKSSEISKLQKTLESFSLKLDAARLATINECNKNAVLE
SQ  KQLDISMKEKSAVERELNGMVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSVQSLE
SQ  EKLSHLENENQVLMQKTLITSPERIGQILGEKHSSAVVPAQNDRRSVFETPTPSKHIMPFSHSLSESRRSKLTAERNLEN
SQ  YELLSRCIKENLGFNDDKPLAACVIYKCLLHWRAFESESTAIFNIIIEGINEALKGGDENGVLPYWLSNASALLCLLQRN
SQ  LRSNSFLNASAQRSGRAAYGVKSPFKLHGPDDGASHIEARYPALLFKQQLTACVEKIYGLIRDNLKKELSPLLGSCIQAP
SQ  KASRGIAGKSRSPGGVPQQSPSSQWESILKFLDSLMSRLRENHVPSFFIRKLVTQVFSFINLSLFNSLLLRRECCTFSNG
SQ  EYVKSGISELEKWIANAKEEFAGTSWHELNYIRQAVGFLVIHQKKKKSLDEIRQDLCPVLTIRQIYRISTMYWDDKYGTQ
SQ  SVSSEVVSQMRVLVDKDNQKQTSNSFLLDDDMSIPFSAEDIDKAIPVLDPSEIEPPKFVSEYTCAQSLVKKPSIASTSKQ
SQ  II
//
ID  E1BPK6;
PN  Unconventional myosin-VI;
GN  MYO6;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9UM54}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UM54}. Golgi apparatus {ECO:0000250|UniProtKB:Q9UM54}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q29122}. Cell projection, microvillus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29122}. Note=Also present in endocytic vesicles (By similarity). Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage. Recruited into membrane ruffles from cell surface by EGF-stimulation. Colocalizes with DAB2 in clathrin-coated pits/vesicles (By similarity). Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q9I8D1, ECO:0000250|UniProtKB:Q9UM54}.
DR  UNIPROT: E1BPK6;
DR  Pfam: PF16521;
DR  Pfam: PF00063;
DR  PROSITE: PS51456;
DR  PROSITE: PS51844;
DE  Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (By similarity). Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro- survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (By similarity). Together with TOM1, mediates delivery of endocytic cargo to autophagosomes thereby promoting autophagosome maturation and driving fusion with lysosomes (By similarity). Links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (By similarity). May act as a regulator of F-actin dynamics (By similarity). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (By similarity). May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity). May play a role in the extension and network organization of neurites (By similarity). Required for structural integrity of inner ear hair cells (By similarity). Modulates RNA polymerase II-dependent transcription (By similarity). {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q64331, ECO:0000250|UniProtKB:Q9UM54}.
DE  Reference Proteome: Yes;
GO  GO:0015629;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0005829;
GO  GO:0030139;
GO  GO:0030175;
GO  GO:0005794;
GO  GO:0005902;
GO  GO:0016459;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001726;
GO  GO:0032587;
GO  GO:0051015;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0000146;
GO  GO:0007015;
GO  GO:0006897;
GO  GO:0042491;
GO  GO:0042472;
GO  GO:0015031;
GO  GO:0007605;
GO  GO:0030050;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9UM54};
SQ  MEDGRPVWAPHPTEGFQMGNIVDIGPDSLTIEPLGQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVR
SQ  YSKDRIYTYVANILIAVNPYFDIPKIYSSDSIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTEN
SQ  TKFVLRYLTESYGSGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGK
SQ  EERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKTPEHLKAGSLKDPLLDDHGDFVRM
SQ  CTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSTQSLEYCAELLGLDQDDLRVSLTTRVMLTTAG
SQ  GTKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKL
SQ  QQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEAKLMGILDILDEENRLPQPSDQHFTSAVHQKHKDHFRLSIP
SQ  RKSKLAVHRNIRDDEGFIVRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSF
SQ  ISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHDFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKK
SQ  YMPDKLARLDPRLFCKALFKALGLNEVDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAQLVKRVNHWLICSRWKKVQWCS
SQ  LSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKAEMNKQVKDLEISIDA
SQ  LMAKIKSTMMTREQIQKEYDALVKSSEVLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEQRRRKEEEERRMKLEM
SQ  EAKRKQEEEERKKREDDEKRIQAEVEAQLARQREEESQQQAVLEQERRDRELALRIARSEAELIIDEAQADPAALRSLDF
SQ  HPVTSKINGTRRTMTPEQMAKEMSEILSRGPAVQATKAAAGTKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLK
SQ  VYHAWKSKNKKRNTETEQRAPKSVTDYDFAPFLNNSPQQNPAAQLPARQQEIEMNRQQRFFRIPFIRPADQYKDPQNKKK
SQ  GWWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQSAIESRQ
SQ  ARPTYATAMLQNLLK
//
ID  Q9I8D1;
PN  Unconventional myosin-VI;
GN  MYO6;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11447109}; Peripheral membrane protein {ECO:0000269|PubMed:11447109}. Golgi apparatus {ECO:0000269|PubMed:11447109, ECO:0000269|PubMed:15837803}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, ruffle membrane {ECO:0000269|PubMed:11447109}. Cell projection, microvillus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29122}. Note=Also present in endocyctic vesicles (By similarity). Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage (By similarity). Recruited into membrane ruffles from cell surface by EGF- stimulation (By similarity). Colocalizes with DAB2 in clathrin-coated pits/vesicles (By similarity). Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (PubMed:15837803). {ECO:0000250|UniProtKB:Q9UM54, ECO:0000269|PubMed:15837803}. [Isoform 1]: Cytoplasmic vesicle, clathrin-coated vesicle membrane.
DR  UNIPROT: Q9I8D1;
DR  Pfam: PF16521;
DR  Pfam: PF00063;
DR  PROSITE: PS50096;
DR  PROSITE: PS51456;
DR  PROSITE: PS51844;
DE  Function: Myosins are actin-based motor molecules with ATPase activity (By similarity). Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (By similarity). Has slow rate of actin-activated ADP release due to weak ATP binding (By similarity). Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway (By similarity). Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (By similarity). Together with TOM1, mediates delivery of endocytic cargo to autophagosomes thereby promoting autophagosome maturation and driving fusion with lysosomes (By similarity). Links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (By similarity). May act as a regulator of F-actin dynamics (By similarity). May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity). May play a role in the extension and network organization of neurites (By similarity). Modulates RNA polymerase II- dependent transcription (By similarity). {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q64331, ECO:0000250|UniProtKB:Q9UM54}.
DE  Reference Proteome: Yes;
DE  Interaction: P98082; IntAct: EBI-6307290; Score: 0.37
DE  Interaction: P97318; IntAct: EBI-6307483; Score: 0.40
DE  Interaction: P98078; IntAct: EBI-6307422; Score: 0.40
DE  Interaction: O88797; IntAct: EBI-6307558; Score: 0.27
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0005938;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0030665;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0030139;
GO  GO:0031941;
GO  GO:0030175;
GO  GO:0005794;
GO  GO:0005902;
GO  GO:0016459;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016591;
GO  GO:0001726;
GO  GO:0032587;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0003774;
GO  GO:0000146;
GO  GO:0060002;
GO  GO:0007015;
GO  GO:0030048;
GO  GO:0030330;
GO  GO:0006897;
GO  GO:0042491;
GO  GO:0042472;
GO  GO:0006886;
GO  GO:0045944;
GO  GO:0051046;
GO  GO:0007605;
GO  GO:0030050;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11447109};
SQ  MEDGKPVWAPHPTDGFQMGMIVDIGTDYLTIEPLNQKGKTFQAAINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVR
SQ  YSKDRIYTYVANILIAVNPYFDIPKFYSSDAIKKYQGRSLGTLPPHVFAIADKAYRDMKVLKMSQSIIVSGESGAGKTEN
SQ  TKFVLRYLTESYGTGQDIDDRIVEANPLLEAFGNAKTIRNNNSSRFGKFVEIHFNEKNSVVGGFVSHYLLEKSRICVQGK
SQ  EERNYHIFYRLCAGAPEDIREKLYLSSPDSFRYLNRGCTRYFATKETDKQILQNRKSPEYLKAGSLKDPLLDDHGDFNRM
SQ  CTAMKKIGLDDAEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCTLKAQSQPALECCAALLGLDEEDLRVSLTTRVMLTTAG
SQ  GAKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSFFIGVLDIAGFEYFEHNSFEQFCINYCNEKL
SQ  QQFFNERILKEEQELYQKEGLGVNEVRYVDNQDCIDLIEAKLIGVLDILDEENRLPQPSDQHFTSVVHQKHKDHFRLSIP
SQ  RKSKLAVHRNVRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESKDKFVRQLFESNTNNNKDPKQKAGKLSF
SQ  ISVGNKFKTQLNLLLEKLHSTGSSFIRCIFPNLKMTSHHFEGGQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKK
SQ  YLPEKLARLDPRLFCKALFKALGLNEIDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNHWLICSRWKKVQWCS
SQ  LSVIKLKNKIKYRASACIKIQKTIRMWLCKRKHKPRIDGLIKVRTLKKRLDKFNEVVSALKEGKAETSKQIKELEYSIDA
SQ  SMTKIKTTMMTREQIMKEYDALVRSSEQLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEEEKRRRKEEEERRLKSEI
SQ  EAKRKQEEEERKKREEEEKRIQAEIEAQLAREREEETQHQAILEQERRDRELAMRIAQTGAELSTEETKLDVGLCRANGT
SQ  KLQMTAEQMAKEMSEMLSRGPAVQATKAAAGAKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNK
SQ  KRNAETEQRAPKSVTDYAQQNPTAQLPMRQQEIEINRQQRYFRIPFIRPMDQYKDPQNKKKGWWYAHFDGPWIARQMELH
SQ  PDKAPILLVAGKDDMDMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQNAIESRQARPTYATAMLQNLLK
//
ID  Q9UM54;
PN  Unconventional myosin-VI;
GN  MYO6;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16507995}; Peripheral membrane protein {ECO:0000269|PubMed:16507995}. Golgi apparatus {ECO:0000269|PubMed:16507995}. Nucleus {ECO:0000269|PubMed:16507995, ECO:0000269|PubMed:16949370}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16507995}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:11447109}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:11447109}. Cell projection, filopodium {ECO:0000269|PubMed:9852149}. Cell projection, ruffle membrane {ECO:0000269|PubMed:16507995}. Cell projection, microvillus {ECO:0000269|PubMed:9852149}. Cytoplasm, cytosol {ECO:0000269|PubMed:16949370}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:23023224}. Endosome {ECO:0000269|PubMed:23023224}. Note=Also present in endocyctic vesicles (PubMed:16507995). Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage (PubMed:16507995). Recruited into membrane ruffles from cell surface by EGF-stimulation (PubMed:9852149). Colocalizes with DAB2 in clathrin-coated pits/vesicles (PubMed:11967127). Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (By similarity). Recruited to endosomes by TOM1 and TOM1L2 (PubMed:23023224). {ECO:0000250|UniProtKB:Q9I8D1, ECO:0000269|PubMed:11967127, ECO:0000269|PubMed:16507995, ECO:0000269|PubMed:23023224, ECO:0000269|PubMed:9852149}. [Isoform 3]: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:11447109}. [Isoform 4]: Cytoplasmic vesicle, clathrin-coated vesicle membrane. Cell projection, ruffle membrane {ECO:0000269|PubMed:11447109}.
DR  UNIPROT: Q9UM54;
DR  UNIPROT: A6H8V4;
DR  UNIPROT: E1P540;
DR  UNIPROT: Q5TEM5;
DR  UNIPROT: Q5TEM6;
DR  UNIPROT: Q5TEM7;
DR  UNIPROT: Q9BZZ7;
DR  UNIPROT: Q9UEG2;
DR  PDB: 2N0Z;
DR  PDB: 2N10;
DR  PDB: 2N11;
DR  PDB: 2N12;
DR  PDB: 2N13;
DR  PDB: 6E5N;
DR  PDB: 6J56;
DR  Pfam: PF16521;
DR  Pfam: PF00063;
DR  PROSITE: PS51456;
DR  PROSITE: PS51844;
DR  OMIM: 600970;
DR  OMIM: 606346;
DR  OMIM: 607821;
DR  DisGeNET: 4646;
DE  Function: Myosins are actin-based motor molecules with ATPase activity (By similarity). Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (PubMed:10519557). Has slow rate of actin-activated ADP release due to weak ATP binding (By similarity). Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway (PubMed:16507995). Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (PubMed:11447109). Together with TOM1, mediates delivery of endocytic cargo to autophagosomes thereby promoting autophagosome maturation and driving fusion with lysosomes (PubMed:23023224). Links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (PubMed:31371777). May act as a regulator of F-actin dynamics (By similarity). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (PubMed:29467281). May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity). May play a role in the extension and network organization of neurites (By similarity). Required for structural integrity of inner ear hair cells (By similarity). Modulates RNA polymerase II-dependent transcription (PubMed:16949370). {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q64331, ECO:0000269|PubMed:10519557, ECO:0000269|PubMed:11447109, ECO:0000269|PubMed:16507995, ECO:0000269|PubMed:16949370, ECO:0000269|PubMed:23023224, ECO:0000269|PubMed:29467281, ECO:0000269|PubMed:31371777}.
DE  Disease: Deafness, autosomal dominant, 22 (DFNA22) [MIM:606346]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA22 is progressive and postlingual, with onset during childhood. By the age of approximately 50 years, affected individuals invariably have profound sensorineural deafness. {ECO:0000269|PubMed:11468689}. Note=The disease is caused by variants affecting the gene represented in this entry. Deafness, autosomal recessive, 37 (DFNB37) [MIM:607821]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:12687499}. Note=The disease is caused by variants affecting the gene represented in this entry. Deafness, autosomal dominant 22, with hypertrophic cardiomyopathy (DFNHCM) [MIM:606346]: An autosomal dominant sensorineural deafness associated with hypertrophic cardiomyopathy. {ECO:0000269|PubMed:15060111}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O14976; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: P0C6X7; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: P0DTC1; IntAct: EBI-25509753; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: Q16620; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q86WV6; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q9NQC7; IntAct: EBI-2510419; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-350217; Score: 0.35
DE  Interaction: Q14164; IntAct: EBI-361350; Score: 0.00
DE  Interaction: Q9Y6K9; IntAct: EBI-361545; Score: 0.00
DE  Interaction: Q99759; IntAct: EBI-362292; Score: 0.00
DE  Interaction: Q9Y572; IntAct: EBI-363850; Score: 0.00
DE  Interaction: P19438; IntAct: EBI-364456; Score: 0.00
DE  Interaction: P20333; IntAct: EBI-364705; Score: 0.00
DE  Interaction: Q9Y3C5; IntAct: EBI-7220649; Score: 0.37
DE  Interaction: P62158; IntAct: EBI-734105; Score: 0.00
DE  Interaction: P0CG47; IntAct: EBI-914272; Score: 0.44
DE  Interaction: O14908; IntAct: EBI-15596914; Score: 0.59
DE  Interaction: P51784; IntAct: EBI-2511298; Score: 0.40
DE  Interaction: Q9UHP3; IntAct: EBI-2513469; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-2878124; Score: 0.53
DE  Interaction: P25054; IntAct: EBI-3437237; Score: 0.00
DE  Interaction: P60953; IntAct: EBI-3438570; Score: 0.00
DE  Interaction: P98078; IntAct: EBI-6100356; Score: 0.63
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: P98082; IntAct: EBI-6307391; Score: 0.54
DE  Interaction: P63010; IntAct: EBI-6307454; Score: 0.40
DE  Interaction: P97318; IntAct: EBI-6307499; Score: 0.40
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q9NQW6; IntAct: EBI-11009421; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-11030093; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: Q9JLQ0; IntAct: EBI-11033702; Score: 0.35
DE  Interaction: P21333; IntAct: EBI-11038784; Score: 0.35
DE  Interaction: Q61879; IntAct: EBI-11041929; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062262; Score: 0.35
DE  Interaction: Q9JHJ0; IntAct: EBI-11063313; Score: 0.35
DE  Interaction: P58771; IntAct: EBI-11063826; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: P09497; IntAct: EBI-11081190; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: Q13492; IntAct: EBI-11082344; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-11092730; Score: 0.35
DE  Interaction: Q9WTI7; IntAct: EBI-11093786; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11098811; Score: 0.35
DE  Interaction: Q9NQX4; IntAct: EBI-11100755; Score: 0.35
DE  Interaction: P24941; IntAct: EBI-11106375; Score: 0.35
DE  Interaction: P11688; IntAct: EBI-11109223; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-11142496; Score: 0.35
DE  Interaction: P61160; IntAct: EBI-11156891; Score: 0.35
DE  Interaction: P56945; IntAct: EBI-15099384; Score: 0.35
DE  Interaction: Q9UQK1; IntAct: EBI-14027877; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q562R1; IntAct: EBI-21540493; Score: 0.35
DE  Interaction: Q8TB52; IntAct: EBI-21629478; Score: 0.40
DE  Interaction: Q9NWN3; IntAct: EBI-21629491; Score: 0.35
DE  Interaction: Q9NZR1; IntAct: EBI-21629535; Score: 0.35
DE  Interaction: Q9ULJ8; IntAct: EBI-21832394; Score: 0.35
DE  Interaction: Q9NZN5; IntAct: EBI-21832394; Score: 0.35
DE  Interaction: Q9NWM3; IntAct: EBI-21832394; Score: 0.35
DE  Interaction: Q96D71; IntAct: EBI-21832394; Score: 0.35
DE  Interaction: P0CG38; IntAct: EBI-21832394; Score: 0.35
DE  Interaction: P06396; IntAct: EBI-21832394; Score: 0.35
DE  Interaction: P54645; IntAct: EBI-16361875; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16362252; Score: 0.35
DE  Interaction: Q9Z0G0; IntAct: EBI-15596835; Score: 0.52
DE  Interaction: Q9UM54; IntAct: EBI-15706123; Score: 0.62
DE  Interaction: Q6ZVM7; IntAct: EBI-16015408; Score: 0.48
DE  Interaction: O60784; IntAct: EBI-16015453; Score: 0.37
DE  Interaction: P15311; IntAct: EBI-16791848; Score: 0.27
DE  Interaction: P25786; IntAct: EBI-16797556; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: P27824; IntAct: EBI-16789004; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: Q99714; IntAct: EBI-20306067; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: Q92731; IntAct: EBI-20764888; Score: 0.35
DE  Interaction: Q93079; IntAct: EBI-20927928; Score: 0.40
DE  Interaction: Q12996; IntAct: EBI-20937036; Score: 0.40
DE  Interaction: P11166; IntAct: EBI-20938324; Score: 0.40
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: O75368; IntAct: EBI-25373235; Score: 0.35
DE  Interaction: Q8N5H7; IntAct: EBI-25387159; Score: 0.35
DE  Interaction: Q16637; IntAct: EBI-25484957; Score: 0.35
DE  Interaction: P0DTC2; IntAct: EBI-25509945; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-25510103; Score: 0.35
DE  Interaction: P0DTD2; IntAct: EBI-25510322; Score: 0.35
DE  Interaction: P0DTD3; IntAct: EBI-25510342; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
DE  Interaction: Q6PB30; IntAct: EBI-26354359; Score: 0.35
DE  Interaction: D3ZN21; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: G3V817; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: F1LTH9; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: F1LMK2; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: Q5XI21; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: A2RUW1; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: Q7TP47; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P62755; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P62703; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P49242; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P62909; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P27952; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P19945; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P62425; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P05426; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: O54889; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: Q9EPH8; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P04785; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P13383; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: D4A8M4; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: B2GV98; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: D3ZBH5; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: Q6IMY8; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: Q62826; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P61980; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: M0R7B4; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: Q8VIB1; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: A0A0G2K3H2; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: A0A0G2KAH4; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: Q6AYI1; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: A0A0G2K719; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: A0A096MIX2; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: O88797; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: P60711; IntAct: EBI-26551477; Score: 0.35
DE  Interaction: A7VJC2; IntAct: EBI-26553037; Score: 0.35
DE  Interaction: F1LQ48; IntAct: EBI-26553037; Score: 0.35
DE  Interaction: P14240; IntAct: EBI-26968430; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P63252; IntAct: EBI-27067929; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: Q15884; IntAct: EBI-27118789; Score: 0.37
DE  Interaction: P53355; IntAct: EBI-28938354; Score: 0.35
DE  Interaction: Q02556; IntAct: EBI-29000425; Score: 0.35
DE  Interaction: P23759; IntAct: EBI-29000845; Score: 0.35
DE  Interaction: O60481; IntAct: EBI-29013426; Score: 0.35
DE  Interaction: P78545; IntAct: EBI-29019619; Score: 0.35
DE  Interaction: P01100; IntAct: EBI-29015727; Score: 0.27
DE  Interaction: Q12952; IntAct: EBI-29015877; Score: 0.27
DE  Interaction: P42224; IntAct: EBI-29757172; Score: 0.27
DE  Interaction: Q5JZY3; IntAct: EBI-32717780; Score: 0.35
DE  Interaction: P54756; IntAct: EBI-32720907; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: Q06124; IntAct: EBI-32723738; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: P16234; IntAct: EBI-32724889; Score: 0.27
DE  Interaction: O96017; IntAct: EBI-34581463; Score: 0.35
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0005938;
GO  GO:0005905;
GO  GO:0030665;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0030139;
GO  GO:0070062;
GO  GO:0031941;
GO  GO:0030175;
GO  GO:0005794;
GO  GO:0005765;
GO  GO:0016020;
GO  GO:0005902;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016591;
GO  GO:0001726;
GO  GO:0032587;
GO  GO:0016461;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0003774;
GO  GO:0042802;
GO  GO:0000146;
GO  GO:0060001;
GO  GO:0007015;
GO  GO:0030048;
GO  GO:0030330;
GO  GO:0006897;
GO  GO:0042491;
GO  GO:0042472;
GO  GO:0006886;
GO  GO:0045944;
GO  GO:0051046;
GO  GO:0007605;
GO  GO:0030050;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16507995};
SQ  MEDGKPVWAPHPTDGFQMGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVR
SQ  YSKDRIYTYVANILIAVNPYFDIPKIYSSEAIKSYQGKSLGTRPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTEN
SQ  TKFVLRYLTESYGTGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGK
SQ  EERNYHIFYRLCAGASEDIREKLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEYLKAGSMKDPLLDDHGDFIRM
SQ  CTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSAQSLEYCAELLGLDQDDLRVSLTTRVMLTTAG
SQ  GTKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKL
SQ  QQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEAKLVGILDILDEENRLPQPSDQHFTSAVHQKHKDHFRLTIP
SQ  RKSKLAVHRNIRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSF
SQ  ISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGYPSRASFHELYNMYKK
SQ  YMPDKLARLDPRLFCKALFKALGLNENDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNHWLTCSRWKKVQWCS
SQ  LSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSVLKDGKPEMNKQIKNLEISIDT
SQ  LMAKIKSTMMTQEQIQKEYDALVKSSEELLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEKRRRKEEEERRMKLEM
SQ  EAKRKQEEEERKKREDDEKRIQAEVEAQLARQKEEESQQQAVLEQERRDRELALRIAQSEAELISDEAQADLALRRSLDS
SQ  YPVSKNDGTRPKMTPEQMAKEMSEFLSRGPAVLATKAAAGTKKYDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKV
SQ  YHAWKSKNKKRNTETEQRAPKSVTDYDFAPFLNNSPQQNPAAQIPARQREIEMNRQQRFFRIPFIRPADQYKDPQSKKKG
SQ  WWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQNAIESRQA
SQ  RPTYATAMLQSLLK
//
ID  Q64331;
PN  Unconventional myosin-VI;
GN  Myo6;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9UM54}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UM54}. Golgi apparatus {ECO:0000250|UniProtKB:Q9UM54}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, microvillus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29122}. Note=Also present in endocyctic vesicles (By similarity). Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage (By similarity). Recruited into membrane ruffles from cell surface by EGF- stimulation (By similarity). Colocalizes with DAB2 in clathrin-coated pits/vesicles (By similarity). Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q9I8D1, ECO:0000250|UniProtKB:Q9UM54}.
DR  UNIPROT: Q64331;
DR  PDB: 2KIA;
DR  PDB: 2LD3;
DR  PDB: 3H8D;
DR  PDB: 5V6E;
DR  PDB: 5V6H;
DR  Pfam: PF16521;
DR  Pfam: PF00063;
DR  PROSITE: PS51456;
DR  PROSITE: PS51844;
DE  Function: Myosins are actin-based motor molecules with ATPase activity (PubMed:11906161). Unconventional myosins serve in intracellular movements (PubMed:11906161). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (By similarity). Has slow rate of actin-activated ADP release due to weak ATP binding (By similarity). Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway (By similarity). Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (By similarity). Together with TOM1, mediates delivery of endocytic cargo to autophagosomes thereby promoting autophagosome maturation and driving fusion with lysosomes (By similarity). Links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (By similarity). May act as a regulator of F-actin dynamics (By similarity). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (By similarity). May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (PubMed:11906161). May play a role in the extension and network organization of neurites (PubMed:22039235). Required for structural integrity of inner ear hair cells (PubMed:7493015). Modulates RNA polymerase II-dependent transcription (By similarity). {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q9UM54, ECO:0000269|PubMed:11906161, ECO:0000269|PubMed:22039235, ECO:0000269|PubMed:7493015}.
DE  Disease: Note=Defects in Myo6 are the cause of Snell's waltzer, a condition characterized by circling, head-tossing, deafness and hyperactivity. {ECO:0000269|PubMed:7493015}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q9P2S5; IntAct: EBI-11694751; Score: 0.35
DE  Interaction: Q8BJ03; IntAct: EBI-20313526; Score: 0.35
DE  Interaction: Q9D2G2; IntAct: EBI-20313723; Score: 0.35
DE  Interaction: P35486; IntAct: EBI-20313969; Score: 0.35
DE  Interaction: O08756; IntAct: EBI-20313873; Score: 0.35
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0015629;
GO  GO:0045177;
GO  GO:0030424;
GO  GO:0005903;
GO  GO:0045334;
GO  GO:0005905;
GO  GO:0098683;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0030139;
GO  GO:0031941;
GO  GO:0030175;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005902;
GO  GO:0016459;
GO  GO:0043025;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098871;
GO  GO:0014069;
GO  GO:0098833;
GO  GO:0032991;
GO  GO:0016591;
GO  GO:0001726;
GO  GO:0032587;
GO  GO:0098685;
GO  GO:0045202;
GO  GO:0012506;
GO  GO:0051015;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0042802;
GO  GO:0000146;
GO  GO:0007015;
GO  GO:0071257;
GO  GO:0007268;
GO  GO:0016358;
GO  GO:0030330;
GO  GO:0006897;
GO  GO:0014047;
GO  GO:0042491;
GO  GO:0048839;
GO  GO:0042472;
GO  GO:0007626;
GO  GO:0045944;
GO  GO:0098884;
GO  GO:0006605;
GO  GO:0051046;
GO  GO:0048167;
GO  GO:2000300;
GO  GO:0009410;
GO  GO:0007605;
GO  GO:0007416;
GO  GO:0030050;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9UM54};
SQ  MEDGKPVWAPHPTDGFQMGNIVDIGPDSLTIEPLNQKGKTFGALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNVKVR
SQ  YSKDRIYTYVANILIAVNPYFDIPKIYSSDTIKSYQGKSLGTMPPHVFGIADKAFRDMKVLKMSQSIIVSGESGAGKTEN
SQ  TKFGSKIPDRILWTGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGK
SQ  EERNHHIFYRLCAGASEDIREKLHLSSPDNFRYLNRGCTRFFANKETDKQILQNRKSPEYVKAGSLEGSSIRRPWRFYQD
SQ  VHSHEKNWFGMMKKNFDLFRVVAGVLHLGNIDLEEAGSTSGGCNLKNKSAPSLEYCAELLGLDQDDLRVSLTTRVMLTTA
SQ  GGTKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEK
SQ  LQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIELIEVKLVGILDILDEENRLPQPSDQHFTSVVHQKHKDHFRLTI
SQ  PRKSKLAVHRNLRDDEGFIIRQLCRGRVLRRQPQYGGGKNNDALHMSLESLICESRDKFIRALFESSTNNSKDTKQKAGK
SQ  LSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMASHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNM
SQ  YKKYMPEKLPRLDPRLFCKPLFKALGLNEVDYKFGLTQVFFRPGKFAEFDQIMKSDPDHLAELVKRVNLWLVCSRWKKVQ
SQ  WCSLSVIKLKNKIKYRAEACIKMQKPIRMWLCKRRHNPRIDGLVKVGTLKKRLDKFNEVVSALKDGKPEVNRQIKNLEIS
SQ  IDALMAKFTSTMMTREQIQKEYDALVKSSEDLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEERRRKEEEERRMK
SQ  LEMEPKRKQEEEERKKREDDEKRIQSEVEAQLARQREEESQQQAVLAQECRDRELALRIAQNESELISDEAQGDMALRRG
SQ  PAVQATKAASGTKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKRNTETEQRAPKSVTDYDFA
SQ  PFLNNSPQQNPAAQLPARQQEIDMKRQQRFFRIPFIRPADQYKDPQNKKKGWWYAHFDGPWIARQMELHPDKPPILLVAG
SQ  KDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQSAIESRQARPTYATAMLQNLLK
//
ID  Q29122;
PN  Unconventional myosin-VI;
GN  MYO6;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9UM54}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UM54}. Golgi apparatus {ECO:0000250|UniProtKB:Q9UM54}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, ruffle membrane {ECO:0000269|PubMed:16917816}. Cell projection, microvillus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, cytosol {ECO:0000269|PubMed:7929586}. Note=Also present in endocytic vesicles (PubMed:16917816). Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage (By similarity). Recruited into membrane ruffles from cell surface by EGF- stimulation (By similarity). Colocalizes with DAB2 in clathrin-coated pits/vesicles (By similarity). Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q9I8D1, ECO:0000250|UniProtKB:Q9UM54, ECO:0000269|PubMed:16917816}.
DR  UNIPROT: Q29122;
DR  PDB: 2BKH;
DR  PDB: 2BKI;
DR  PDB: 2V26;
DR  PDB: 2VAS;
DR  PDB: 2VB6;
DR  PDB: 2X51;
DR  PDB: 3GN4;
DR  PDB: 3L9I;
DR  PDB: 4ANJ;
DR  PDB: 4DBP;
DR  PDB: 4DBQ;
DR  PDB: 4DBR;
DR  PDB: 5O2L;
DR  PDB: 6BNP;
DR  PDB: 6BNQ;
DR  PDB: 6BNV;
DR  PDB: 6BNW;
DR  Pfam: PF16521;
DR  Pfam: PF00063;
DR  PROSITE: PS51456;
DR  PROSITE: PS51844;
DE  Function: Myosins are actin-based motor molecules with ATPase activity (By similarity). Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (By similarity). Has slow rate of actin-activated ADP release due to weak ATP binding (PubMed:15944696). Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (PubMed:16917816). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway (By similarity). Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (By similarity). Together with TOM1, mediates delivery of endocytic cargo to autophagosomes thereby promoting autophagosome maturation and driving fusion with lysosomes (By similarity). Links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (By similarity). May act as a regulator of F-actin dynamics (PubMed:7929586). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (By similarity). May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity). May play a role in the extension and network organization of neurites (By similarity). Required for structural integrity of inner ear hair cells (By similarity). Modulates RNA polymerase II-dependent transcription (By similarity). {ECO:0000250|UniProtKB:Q64331, ECO:0000250|UniProtKB:Q9UM54, ECO:0000269|PubMed:15944696, ECO:0000269|PubMed:16917816, ECO:0000269|PubMed:7929586}.
DE  Reference Proteome: Yes;
DE  Interaction: Q96CV9; IntAct: EBI-15804564; Score: 0.60
DE  Interaction: P98082; IntAct: EBI-15804626; Score: 0.52
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0005938;
GO  GO:0030136;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0031941;
GO  GO:0030175;
GO  GO:0005794;
GO  GO:0005902;
GO  GO:0016459;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016591;
GO  GO:0001726;
GO  GO:0032587;
GO  GO:0051015;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0003774;
GO  GO:0000146;
GO  GO:0007015;
GO  GO:0030048;
GO  GO:0030330;
GO  GO:0006897;
GO  GO:0042491;
GO  GO:0042472;
GO  GO:0006886;
GO  GO:0045944;
GO  GO:0051046;
GO  GO:0007605;
GO  GO:0030050;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9UM54};
SQ  MEDGKPVWAPHPTDGFQVGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVR
SQ  YSKDRIYTYVANILIAVNPYFDIPKIYSSETIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKLSQSIIVSGESGAGKTEN
SQ  TKFVLRYLTESYGTGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGK
SQ  EERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEYLKAGSLKDPLLDDHGDFIRM
SQ  CTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSTQALEYCAEKLLGLDQDDLRVSLTTRVMLTTA
SQ  GGAKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEK
SQ  LQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEARLVGILDILDEENRLPQPSDQHFTSAGHQKHKDHFRLSI
SQ  PRKSKLAIHRNIAYDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLS
SQ  FISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHEVYNMYK
SQ  KSLPDKLARLDPRLFCKALFKALGLNEIDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNHWLICSRWKKVQWC
SQ  SLSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKQEMSKQVKDLEISID
SQ  ALMAKIKSTMMTREQIQKEYDALVKSSAVLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEQRRRKEEEERRMKLE
SQ  MEAKRKQEEEERKKREDDEKRIQAEVEAQLARQREEESQQQAVLEQERRDRELALRIAQSEAELISDEAQADPGLRRGPA
SQ  VQATKAAAGTKKYDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKRNTETEQRAPKSVTDYAQQNP
SQ  AVQLPARQQEIEMNRQQRFFRIPFIRSADQYKDPQNKKKGWWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNL
SQ  EETGLTRKRGAEILPRQFEEIWERCGGIQYLQNAIESRQARPTYATAMLQNLLK
//
ID  Q13459;
PN  Unconventional myosin-IXb;
GN  MYO9B;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cell cortex {ECO:0000269|PubMed:8907710}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8907710}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8907710, ECO:0000269|PubMed:9490638}. Note=In undifferentiated cells colocalizes with F-actin in the cell periphery while in differentiated cells its localization is cytoplasmic with the highest levels in the perinuclear region. {ECO:0000269|PubMed:8907710}.
DR  UNIPROT: Q13459;
DR  UNIPROT: O75314;
DR  UNIPROT: Q9NUJ2;
DR  UNIPROT: Q9UHN0;
DR  PDB: 5C5S;
DR  PDB: 5HPY;
DR  Pfam: PF00612;
DR  Pfam: PF00063;
DR  Pfam: PF00788;
DR  Pfam: PF00620;
DR  PROSITE: PS50096;
DR  PROSITE: PS51456;
DR  PROSITE: PS50200;
DR  PROSITE: PS50238;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DR  OMIM: 602129;
DR  OMIM: 609753;
DR  DisGeNET: 4650;
DE  Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions (PubMed:9490638). Also acts as a GTPase activator for RHOA (PubMed:9490638, PubMed:26529257). Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). {ECO:0000269|PubMed:26529257, ECO:0000269|PubMed:9490638}.
DE  Disease: Celiac disease 4 (CELIAC4) [MIM:609753]: A multifactorial, chronic disorder of the small intestine caused by intolerance to gluten. It is characterized by immune-mediated enteropathy associated with failed intestinal absorption, and malnutrition. In predisposed individuals, the ingestion of gluten-containing food such as wheat and rye induces a flat jejunal mucosa with infiltration of lymphocytes. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: D4A631; IntAct: EBI-6251284; Score: 0.40
DE  Interaction: Q15345; IntAct: EBI-735178; Score: 0.00
DE  Interaction: Q9Y3A3; IntAct: EBI-737438; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.35
DE  Interaction: Q5NID9; IntAct: EBI-2804609; Score: 0.00
DE  Interaction: Q16513; IntAct: EBI-7309416; Score: 0.37
DE  Interaction: Q9Y6D6; IntAct: EBI-6251244; Score: 0.56
DE  Interaction: P61586; IntAct: EBI-6251332; Score: 0.44
DE  Interaction: P55316; IntAct: EBI-11320867; Score: 0.35
DE  Interaction: Q12952; IntAct: EBI-11321256; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: Q9Y4Z2; IntAct: EBI-21514441; Score: 0.35
DE  Interaction: O95861; IntAct: EBI-21532230; Score: 0.35
DE  Interaction: Q8TE96; IntAct: EBI-21601615; Score: 0.35
DE  Interaction: Q86WV1; IntAct: EBI-21601309; Score: 0.35
DE  Interaction: Q9NZQ9; IntAct: EBI-21602161; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-21650356; Score: 0.35
DE  Interaction: Q9UBP4; IntAct: EBI-21684976; Score: 0.35
DE  Interaction: Q86XD5; IntAct: EBI-21711466; Score: 0.35
DE  Interaction: Q9BRK5; IntAct: EBI-21763329; Score: 0.35
DE  Interaction: Q96FT9; IntAct: EBI-21792723; Score: 0.35
DE  Interaction: Q9Y6B2; IntAct: EBI-21805551; Score: 0.35
DE  Interaction: Q96EV2; IntAct: EBI-21884250; Score: 0.35
DE  Interaction: Q96BY2; IntAct: EBI-21884195; Score: 0.35
DE  Interaction: Q96JN8; IntAct: EBI-16813376; Score: 0.35
DE  Interaction: Q15293; IntAct: EBI-20911056; Score: 0.40
DE  Interaction: Q15155; IntAct: EBI-20911048; Score: 0.40
DE  Interaction: Q15651; IntAct: EBI-20918980; Score: 0.40
DE  Interaction: P16401; IntAct: EBI-20921894; Score: 0.40
DE  Interaction: P16403; IntAct: EBI-20921886; Score: 0.40
DE  Interaction: Q9H6W3; IntAct: EBI-25476748; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: Q14012; IntAct: EBI-28939656; Score: 0.35
DE  Interaction: P46937; IntAct: EBI-30846798; Score: 0.44
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0016459;
GO  GO:0048471;
GO  GO:0001726;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0043008;
GO  GO:0005516;
GO  GO:0005096;
GO  GO:0000146;
GO  GO:0048495;
GO  GO:0031267;
GO  GO:0008270;
GO  GO:0030048;
GO  GO:0072673;
GO  GO:0035023;
GO  GO:0051056;
GO  GO:0007266;
GO  GO:0035385;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSVKEAGSSGRREQAAYHLHIYPQLSTTESQASCRVTATKDSTTSDVIKDAIASLRLDGTKCYVLVEVKESGGEEWVLDA
SQ  NDSPVHRVLLWPRRAQDEHPQEDGYYFLLQERNADGTIKYVHMQLVAQATATRRLVERGLLPRQQADFDDLCNLPELTEG
SQ  NLLKNLKHRFLQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKRVNQCIVISGE
SQ  SGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVSYLESGIVRGAVVEKYLL
SQ  EKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPEDYFYLNQHNLKIEDGEDLKHDFERLKQAMEMVGFLPATKKQ
SQ  IFAVLSAILYLGNVTYKKRATGREEGLEVGPPEVLDTLSQLLKVKREILVEVLTKRKTVTVNDKLILPYSLSEAITARDS
SQ  MAKSLYSALFDWIVLRINHALLNKKDVEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFNQHIFKLEQEEY
SQ  QGEGITWHNIGYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSQTLLAKFKQQHEDNKYFLGTPVMEPAFIIQHFAGKV
SQ  KYQIKDFREKNMDYMRPDIVALLRGSDSSYVRELIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAAGMSSPGA
SQ  QSHPEELPRGASTPSEKLYRDLHNQMIKSIKGLPWQGEDPRSLLQSLSRLQKPRAFILKSKGIKQKQIIPKNLLDSKSLK
SQ  LIISMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLE
SQ  TVRIRRSGYSAKYTFQDFTEQFQVLLPKDAQPCREVISTLLEKMKIDKRNYQIGKTKVFLKETERQALQETLHREVVRKI
SQ  LLLQSWFRMVLERRHFLQMKRAAVTIQACWRSYRVRRALERTQAAVYLQASWRGYWQRKLYRHQKQSIIRLQSLCRGHLQ
SQ  RKSFSQMISEKQKAEEKEREALEAARAGAEEGGQGQAAGGQQVAEQGPEPAEDGGHLASEPEVQPSDRSPLEHSSPEKEA
SQ  PSPEKTLPPQKTVAAESHEKVPSSREKRESRRQRGLEHVKFQNKHIQSCKEESALREPSRRVTQEQGVSLLEDKKESRED
SQ  ETLLVVETEAENTSQKQPTEQPQAMAVGKVSEETEKTLPSGSPRPGQLERPTSLALDSRVSPPAPGSAPETPEDKSKPCG
SQ  SPRVQEKPDSPGGSTQIQRYLDAERLASAVELWRGKKLVAAASPSAMLSQSLDLSDRHRATGAALTPTEERRTSFSTSDV
SQ  SKLLPSLAKAQPAAETTDGERSAKKPAVQKKKPGDASSLPDAGLSPGSQVDSKSTFKRLFLHKTKDKKYSLEGAEELENA
SQ  VSGHVVLEATTMKKGLEAPSGQQHRHAAGEKRTKEPGGKGKKNRNVKIGKITVSEKWRESVFRQITNANELKYLDEFLLN
SQ  KINDLRSQKTPIESLFIEATEKFRSNIKTMYSVPNGKIHVGYKDLMENYQIVVSNLATERGQKDTNLVLNLFQSLLDEFT
SQ  RGYTKNDFEPVKQSKAQKKKRKQERAVQEHNGHVFASYQVSIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSH
SQ  CSYTYGRKGEPGVEPGHFGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLE
SQ  NFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLAAIYAVLEHLPEANHNSLERLIFHLVKVALLEDVNR
SQ  MSPGALAIIFAPCLLRCPDNSDPLTSMKDVLKITTCVEMLIKEQMRKYKVKMEEISQLEAAESIAFRRLSLLRQNAPWPL
SQ  KLGFSSPYEGVLNKSPKTRDIQEEELEVLLEEEAAGGDEDREKEILIERIQSIKEEKEDITYRLPELDPRGSDEENLDSE
SQ  TSASTESLLEERAGRGASEGPPAPALPCPGAPTPSPLPTVAAPPRRRPSSFVTVRVKTPRRTPIMPTANIKLPPGLPSHL
SQ  PRWAPGAREAAAPVRRREPPARRPDQIHSVYITPGADLPVQGALEPLEEDGQPPGAKRRYSDPPTYCLPPASGQTNG
//
ID  Q9QY06;
PN  Unconventional myosin-IXb;
GN  Myo9b;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q13459}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13459}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13459}. Note=In undifferentiated cells colocalizes with F-actin in the cell periphery while in differentiated cells its localization is cytoplasmic with the highest levels in the perinuclear region. {ECO:0000250|UniProtKB:Q13459}.
DR  UNIPROT: Q9QY06;
DR  UNIPROT: Q9QY07;
DR  UNIPROT: Q9QY08;
DR  UNIPROT: Q9QY09;
DR  Pfam: PF00612;
DR  Pfam: PF00063;
DR  Pfam: PF00788;
DR  Pfam: PF00620;
DR  PROSITE: PS50096;
DR  PROSITE: PS51456;
DR  PROSITE: PS50200;
DR  PROSITE: PS50238;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions. Also acts as a GTPase activator for RHOA. Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA. {ECO:0000250|UniProtKB:Q13459}.
DE  Reference Proteome: Yes;
GO  GO:0005884;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0032433;
GO  GO:0030027;
GO  GO:0016459;
GO  GO:0048471;
GO  GO:0001726;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0043008;
GO  GO:0005516;
GO  GO:0003774;
GO  GO:0005096;
GO  GO:0000146;
GO  GO:0048495;
GO  GO:0031267;
GO  GO:0008270;
GO  GO:0030048;
GO  GO:0033275;
GO  GO:0030010;
GO  GO:0072673;
GO  GO:0048246;
GO  GO:0002548;
GO  GO:0043547;
GO  GO:0035023;
GO  GO:0007266;
GO  GO:0035385;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAHEAGSSGRRQQATYHLHIYPQLSSAGSQTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGGEEWVLDA
SQ  SDSPVHRVLLWPRRAQDEHPQEDGYYFLLQERNADGSIQYLPIQLLAQPTAACRLVERGLLPRPQADFDDLCNLPELTEA
SQ  NLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGE
SQ  SGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLL
SQ  EKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQ
SQ  IFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDS
SQ  MAKSLYSALFDWIVLRINHALLNKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEY
SQ  QGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRV
SQ  KYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAAGISSPAT
SQ  RSHMEELPRGASTPSEKLYRDLHNQIIKSLKGLPWQGEDPRRLLQSLSLLQKPRTSFLKSKGIKQKQIIPKNLLDSKSLR
SQ  LIISMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLE
SQ  TVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQEKLHGEVLRRI
SQ  LQLQSWFRMVLERKHFVQMKHAALTIQACWRSYRVRRALERTQAAVYLQAAWRGYLQRQAYHHQRHSIIRLQSLCRGHLQ
SQ  RRSFSQMVSEKQKAEQAREAAGGKLSEGEPGPVAAGEQLSEHPVEDPESLGVEAETWMNKSPDGMSPKKETPSPEMETAA
SQ  QKTVPAESHEKVSSSREKRESRRQRGLEHVERQNKHIQSCREESSTHREPSRRASLEIGESFPEGTKGPREDGLEAWTET
SQ  TAPSSSKQAQVVGDPPGSPSPVQRPTTLALDSRVSPMLPSSSLESPKDKDKDESSTKAQDKPESPSGSTQIQRYQHPDTE
SQ  RLATAVEIWRGKKLASAVLSQSLDLSEKHRATGAALTPTEERRISFSTSDISKLSPVKTSAEIDGDFSSKKPSIHKKKSG
SQ  DPSAGPDAGLSPGSQGDSKSAFKRLFLHKAKDKKPSLEGVEETESNGGQAAQETPARKTLDVPSSQQHRHTTGEKPLKGK
SQ  KNRNRKVGQITVSEKWRESVFRKITNANELKFLDEFLLNKVNDLRSQKTPIESLFIEATERFRSNIKTMYSVPNGKIHVG
SQ  YKDLMENYQIVVSNLAAERGEKDTNLVLNVFQSLLDEFTRSYNKTDFERAKSKAQKKKRKQERAVQEHNGHVFASYQVNI
SQ  PQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTGRRKSELGAEPGHFGVCVDSLTSDKASVPIVLEKLLEH
SQ  VEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEKQE
SQ  QLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPLTSMKDVLKITTCVEMLIK
SQ  EQMRKYKMKMEEINHLEAAESIAFRRLSLLRQNAPWPLKLGFSSPYEGVRIKSPRTPVVQDLELGALSEEAAGGDEDREK
SQ  EILMERIQSIKEEKEDITYRLPELDPRGSDEENLDSETSASTESLLEERGVRGAVEGPPAPALPCPISPTLSPLPEAAAP
SQ  PRGRPTSFVTVRVKTPRRTPIMPMANIKLPPGLPLHLTSWAPALQEAVVPVKRREPPARRQDQVHSVYIAPGADLPSQST
SQ  LIALDHDTILPGTKRRYSDPPTYCLPPSSGQANG
//
ID  Q63358;
PN  Unconventional myosin-IXb;
GN  Myo9b;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q13459}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13459}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13459}. Note=In undifferentiated cells colocalizes with F-actin in the cell periphery while in differentiated cells its localization is cytoplasmic with the highest levels in the perinuclear region. {ECO:0000250|UniProtKB:Q13459}.
DR  UNIPROT: Q63358;
DR  Pfam: PF00612;
DR  Pfam: PF00063;
DR  Pfam: PF00788;
DR  Pfam: PF00620;
DR  PROSITE: PS50096;
DR  PROSITE: PS51456;
DR  PROSITE: PS50200;
DR  PROSITE: PS50238;
DR  PROSITE: PS00479;
DR  PROSITE: PS50081;
DE  Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions (By similarity). Also acts as a GTPase activator for RHOA (PubMed:7882973). Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (By similarity). {ECO:0000250|UniProtKB:Q13459, ECO:0000269|PubMed:7882973}.
DE  Reference Proteome: Yes;
DE  Interaction: D4A631; IntAct: EBI-6251135; Score: 0.51
DE  Interaction: P35658; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: P78406; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: P51571; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: P28074; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: O14818; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: Q9H3U1; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: Q9NZ01; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: Q6NUK1; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: P28070; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: P49721; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: P25786; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: Q13765; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: P14649; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: P07195; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: P84077; IntAct: EBI-25412031; Score: 0.35
GO  GO:0005884;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0032433;
GO  GO:0030027;
GO  GO:0016459;
GO  GO:0048471;
GO  GO:0001726;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0043008;
GO  GO:0005516;
GO  GO:0005096;
GO  GO:0000146;
GO  GO:0048495;
GO  GO:0031267;
GO  GO:0008270;
GO  GO:0030048;
GO  GO:0030010;
GO  GO:0072673;
GO  GO:0048246;
GO  GO:0002548;
GO  GO:0043547;
GO  GO:0035023;
GO  GO:0007266;
GO  GO:0035385;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAHEAGSSGRRRPATFHLHIYPQLPSAGSQTSCRVTATKDSTTSDVIRDVVASLHLDGSKHYVLVEVKESGGEEWVLDA
SQ  SDSPVHRVLLWPRRAQKEHPREDGYYFLLQERNADGSIQYLHVQLLAQPTAACRLVERGLLPRPQADFDDLCNLPELNEA
SQ  NLLQSLKLRFVQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYTMLRKHVNQCIVISGE
SQ  SGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLESGIVRGAVVEKYLL
SQ  EKSRLVSQEKDERNYHVFYYLLLGVSEEERQEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQ
SQ  IFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTITVNDKLILPYSLSEAITARDS
SQ  MAKSLYSALFDWIVLRINHALLNKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEY
SQ  QGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRV
SQ  KYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAEAGVSSPV
SQ  TRSHVEELPRGANTPSEKLYRDLHNQIIKSLKGLPWQGEDPRRLLQSLSRLQKPRTFFLKSKGIKQKQIIPKNLLDSKSL
SQ  RLIISMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGML
SQ  ETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLKETERQALQERLHGEVLRR
SQ  ILLLQSWFRMVLERRHFVQMKHAALTIQACWRSYRVRRTLERTRAAVYLQAAWRGYLQRQAYHHQRHSIIRLQSLCRGHL
SQ  QRRSFSQMMLEKQKAEQARETAGAEMSEGEPSPVAAGEQPSEHPVEDPESLGVETETWMNSKSPNGLSPKKEIPSPEMET
SQ  PAQKTVPAESHEKVPSSREKRESRRQRGLEHVERQNKHIQSCREENSTLREPSRKASLETGESFPEDTKEPREDGLETWT
SQ  ETAAPSCPKQVPIVGDPPRSPSPLQRPASLDLDSRVSPVLPSSSLESPQDEDKGENSTKVQDKPESPSGSTQIQRYQHPD
SQ  TERLATAVEIWRGKKLASAMLSQSLDLSEKPRTAGAALTPTEERRISFSTSDVSKLSPVKTSTEVDGDLSAKKPAGHKKK
SQ  SEDPSAGPDAGLPTGSQGDSKSAFKRLFLHKAKDKKPSLEGVEETEGSGGQAAQEAPARKTLDVPSSQQHRHTTGEKPLK
SQ  GKKNRNRKVGQITVSEKWRESVFRKITNANELKFLDEFLLNKVNDLRSQKTPIESLFIEATERFRSNIKTMYSVPNGKIH
SQ  VGYKDLMENYQIVVSNLAAERGEKDTNLVLNVFQSLLDEFTRSYNKTDFEPVKGKAQKKKRKQERAVQEHNGHVFASYQV
SQ  NIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTGRRKSELGAEPGHFGVCVDSLTSDKASVPIVLEKLL
SQ  EHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPATVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEK
SQ  QEQLAAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPLTSMKDVLKITTCVEML
SQ  IKEQMRKYKVKMEEINHLEAAESIAFRRLSLLRQNAPWPLKLGFSSPYEGVRTKSPRTPVVQDLEELGALPEEAAGGDED
SQ  REKEILMERIQSIKEEKEDITYRLPELDPRGSDEENLDSETSASTESLLEERAVRGAAEE
//
ID  Q9NZM1;
PN  Myoferlin;
GN  MYOF;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane; Single-pass type II membrane protein. Nucleus membrane; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; Single-pass type II membrane protein. Note=Concentrated at the membrane sites of both myoblast-myoblast and myoblast-myotube fusions. Detected at the plasmalemma in endothelial cells lining intact blood vessels (By similarity). Found at nuclear and plasma membranes. Enriched in undifferentiated myoblasts near the plasma membrane in puncate structures. {ECO:0000250}.
DR  UNIPROT: Q9NZM1;
DR  UNIPROT: B3KQN5;
DR  UNIPROT: Q5VWW2;
DR  UNIPROT: Q5VWW3;
DR  UNIPROT: Q5VWW4;
DR  UNIPROT: Q5VWW5;
DR  UNIPROT: Q7Z642;
DR  UNIPROT: Q8IWH0;
DR  UNIPROT: Q9HBU3;
DR  UNIPROT: Q9NZM0;
DR  UNIPROT: Q9ULL3;
DR  UNIPROT: Q9Y4U4;
DR  PDB: 2DMH;
DR  PDB: 2K2O;
DR  PDB: 6EEL;
DR  Pfam: PF00168;
DR  Pfam: PF08165;
DR  Pfam: PF08150;
DR  Pfam: PF08151;
DR  Pfam: PF16165;
DR  PROSITE: PS50004;
DR  OMIM: 604603;
DR  OMIM: 619366;
DR  DisGeNET: 26509;
DE  Function: Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). {ECO:0000250}.
DE  Disease: Angioedema, hereditary, 7 (HAE7) [MIM:619366]: A form of angioedema, a disorder characterized by episodic local swelling involving subcutaneous or submucous tissue of the upper respiratory and gastrointestinal tracts, face, extremities, and genitalia. HAE7 is an autosomal dominant form characterized by onset of recurrent swelling of the face, lips, and oral mucosa in the second decade. {ECO:0000269|PubMed:32542751}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P03246; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P13285; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-7198973; Score: 0.40
DE  Interaction: Q8BH64; IntAct: EBI-1994435; Score: 0.44
DE  Interaction: P38606; IntAct: EBI-4324466; Score: 0.35
DE  Interaction: P03177; IntAct: EBI-11721652; Score: 0.35
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P03209; IntAct: EBI-11722090; Score: 0.35
DE  Interaction: P03225; IntAct: EBI-11722220; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06461; IntAct: EBI-11723785; Score: 0.35
DE  Interaction: P06463; IntAct: EBI-11724048; Score: 0.35
DE  Interaction: P06927; IntAct: EBI-11724813; Score: 0.35
DE  Interaction: P0CK49; IntAct: EBI-11725356; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: P0CK58; IntAct: EBI-11732874; Score: 0.35
DE  Interaction: P30119; IntAct: EBI-11733103; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: Q2MG95; IntAct: EBI-11733653; Score: 0.35
DE  Interaction: Q2MG96; IntAct: EBI-11733890; Score: 0.35
DE  Interaction: Q69117; IntAct: EBI-11733954; Score: 0.35
DE  Interaction: Q8AZK7; IntAct: EBI-11734159; Score: 0.35
DE  Interaction: Q8AZJ3; IntAct: EBI-11734105; Score: 0.35
DE  Interaction: Q9DUG7; IntAct: EBI-11734217; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: P35278; IntAct: EBI-11012136; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-11027413; Score: 0.35
DE  Interaction: Q9JLQ0; IntAct: EBI-11033702; Score: 0.35
DE  Interaction: P51148; IntAct: EBI-11046231; Score: 0.35
DE  Interaction: P51149; IntAct: EBI-11050319; Score: 0.35
DE  Interaction: Q91YN9; IntAct: EBI-11052510; Score: 0.35
DE  Interaction: Q9ERB0; IntAct: EBI-11068003; Score: 0.35
DE  Interaction: Q14108; IntAct: EBI-11072280; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079358; Score: 0.35
DE  Interaction: Q08380; IntAct: EBI-11108487; Score: 0.35
DE  Interaction: Q07797; IntAct: EBI-11108624; Score: 0.35
DE  Interaction: Q9R0Q3; IntAct: EBI-11111571; Score: 0.35
DE  Interaction: P46379; IntAct: EBI-11154173; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-11155257; Score: 0.35
DE  Interaction: Q6SPF0; IntAct: EBI-11160311; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-16795491; Score: 0.27
DE  Interaction: P21926; IntAct: EBI-20977405; Score: 0.35
DE  Interaction: P49716; IntAct: EBI-21259421; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P09613; IntAct: EBI-21497303; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: Q5NIP8; IntAct: EBI-22298766; Score: 0.37
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25686340; Score: 0.35
DE  Interaction: A0A0F6B1Q8; IntAct: EBI-27034088; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: P42695; IntAct: EBI-28951349; Score: 0.35
GO  GO:0005901;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0046872;
GO  GO:0005543;
GO  GO:0008015;
GO  GO:0061025;
GO  GO:0006936;
GO  GO:0007520;
GO  GO:0007009;
GO  GO:0001778;
GO  GO:0033292;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLRVIVESASNIPKTKFGKPDPIVSVIFKDEKKKTKKVDNELNPVWNEILEFDLRGIPLDFSSSLGIIVKDFETIGQNKL
SQ  IGTATVALKDLTGDQSRSLPYKLISLLNEKGQDTGATIDLVIGYDPPSAPHPNDLSGPSVPGMGGDGEEDEGDEDRLDNA
SQ  VRGPGPKGPVGTVSEAQLARRLTKVKNSRRMLSNKPQDFQIRVRVIEGRQLSGNNIRPVVKVHVCGQTHRTRIKRGNNPF
SQ  FDELFFYNVNMTPSELMDEIISIRVYNSHSLRADCLMGEFKIDVGFVYDEPGHAVMRKWLLLNDPEDTSSGSKGYMKVSM
SQ  FVLGTGDEPPPERRDRDNDSDDVESNLLLPAGIALRWVTFLLKIYRAEDIPQMDDAFSQTVKEIFGGNADKKNLVDPFVE
SQ  VSFAGKKVCTNIIEKNANPEWNQVVNLQIKFPSVCEKIKLTIYDWDRLTKNDVVGTTYLHLSKIAASGGEVEDFSSSGTG
SQ  AASYTVNTGETEVGFVPTFGPCYLNLYGSPREYTGFPDPYDELNTGKGEGVAYRGRILVELATFLEKTPPDKKLEPISND
SQ  DLLVVEKYQRRRKYSLSAVFHSATMLQDVGEAIQFEVSIGNYGNKFDTTCKPLASTTQYSRAVFDGNYYYYLPWAHTKPV
SQ  VTLTSYWEDISHRLDAVNTLLAMAERLQTNIEALKSGIQGKIPANQLAELWLKLIDEVIEDTRYTLPLTEGKANVTVLDT
SQ  QIRKLRSRSLSQIHEAAVRMRSEATDVKSTLAEIEDWLDKLMQLTEEPQNSMPDIIIWMIRGEKRLAYARIPAHQVLYST
SQ  SGENASGKYCGKTQTIFLKYPQEKNNGPKVPVELRVNIWLGLSAVEKKFNSFAEGTFTVFAEMYENQALMFGKWGTSGLV
SQ  GRHKFSDVTGKIKLKREFFLPPKGWEWEGEWIVDPERSLLTEADAGHTEFTDEVYQNESRYPGGDWKPAEDTYTDANGDK
SQ  AASPSELTCPPGWEWEDDAWSYDINRAVDEKGWEYGITIPPDHKPKSWVAAEKMYHTHRRRRLVRKRKKDLTQTASSTAR
SQ  AMEELQDQEGWEYASLIGWKFHWKQRSSDTFRRRRWRRKMAPSETHGAAAIFKLEGALGADTTEDGDEKSLEKQKHSATT
SQ  VFGANTPIVSCNFDRVYIYHLRCYVYQARNLLALDKDSFSDPYAHICFLHRSKTTEIIHSTLNPTWDQTIIFDEVEIYGE
SQ  PQTVLQNPPKVIMELFDNDQVGKDEFLGRSIFSPVVKLNSEMDITPKLLWHPVMNGDKACGDVLVTAELILRGKDGSNLP
SQ  ILPPQRAPNLYMVPQGIRPVVQLTAIEILAWGLRNMKNFQMASITSPSLVVECGGERVESVVIKNLKKTPNFPSSVLFMK
SQ  VFLPKEELYMPPLVIKVIDHRQFGRKPVVGQCTIERLDRFRCDPYAGKEDIVPQLKASLLSAPPCRDIVIEMEDTKPLLA
SQ  SKLTEKEEEIVDWWSKFYASSGEHEKCGQYIQKGYSKLKIYNCELENVAEFEGLTDFSDTFKLYRGKSDENEDPSVVGEF
SQ  KGSFRIYPLPDDPSVPAPPRQFRELPDSVPQECTVRIYIVRGLELQPQDNNGLCDPYIKITLGKKVIEDRDHYIPNTLNP
SQ  VFGRMYELSCYLPQEKDLKISVYDYDTFTRDEKVGETIIDLENRFLSRFGSHCGIPEEYCVSGVNTWRDQLRPTQLLQNV
SQ  ARFKGFPQPILSEDGSRIRYGGRDYSLDEFEANKILHQHLGAPEERLALHILRTQGLVPEHVETRTLHSTFQPNISQGKL
SQ  QMWVDVFPKSLGPPGPPFNITPRKAKKYYLRVIIWNTKDVILDEKSITGEEMSDIYVKGWIPGNEENKQKTDVHYRSLDG
SQ  EGNFNWRFVFPFDYLPAEQLCIVAKKEHFWSIDQTEFRIPPRLIIQIWDNDKFSLDDYLGFLELDLRHTIIPAKSPEKCR
SQ  LDMIPDLKAMNPLKAKTASLFEQKSMKGWWPCYAEKDGARVMAGKVEMTLEILNEKEADERPAGKGRDEPNMNPKLDLPN
SQ  RPETSFLWFTNPCKTMKFIVWRRFKWVIIGLLFLLILLLFVAVLLYSLPNYLSMKIVKPNV
//
ID  Q69ZN7;
PN  Myoferlin;
GN  Myof;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single- pass type II membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Found at nuclear and plasma membranes. Enriched in undifferentiated myoblasts near the plasma membrane in puncate structures (By similarity). Concentrated at the membrane sites of both myoblast-myoblast and myoblast-myotube fusions. Detected at the plasmalemma in endothelial cells lining intact blood vessels. {ECO:0000250, ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744}.
DR  UNIPROT: Q69ZN7;
DR  UNIPROT: Q7TMG0;
DR  UNIPROT: Q80V33;
DR  UNIPROT: Q8BU64;
DR  UNIPROT: Q8BU70;
DR  UNIPROT: Q8BUC1;
DR  UNIPROT: Q8BVY6;
DR  UNIPROT: Q8C0D1;
DR  UNIPROT: Q8R3B4;
DR  Pfam: PF00168;
DR  Pfam: PF08165;
DR  Pfam: PF08150;
DR  Pfam: PF08151;
DR  Pfam: PF16165;
DR  PROSITE: PS50004;
DE  Function: Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR. {ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744, ECO:0000269|PubMed:18502764}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3TBT3; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8BH64; IntAct: EBI-1994351; Score: 0.35
GO  GO:0005901;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0046872;
GO  GO:0005543;
GO  GO:0034605;
GO  GO:0006071;
GO  GO:0061025;
GO  GO:0055001;
GO  GO:0007520;
GO  GO:0007009;
GO  GO:0001778;
GO  GO:0030947;
GO  GO:0033292;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLRVIVESATNIPKTKFGKPDPIVSVIFKDEKKKTKKVDNELNPVWNEILEFDLRGIPLDSSSSLVIVVKDFETIGQNKL
SQ  IGTATVSLKDLIGDQNRSLPYKQTSLLNEKGQDTGATIDLVIGYTPPSAPHPNDPSGTSVPGMGEEEEEDQGDEDRVDGI
SQ  VRGPGPKGPSGTVSEAQLARRITKGKSSRRMLSNKPQDFQIRVRVIEGRQLCGNNIRPVVKVHICGQTHRTRIKRGNNPF
SQ  FDELFFYNVHITPSELMDEIISIRVYNSHSLRADCLMGEFKIDVGFVYDEPGHAVMRKWLLLNDPEDTSSGAKGYMKVSM
SQ  FVLGTGDEPPPEKRDRDNDSDDVESNLLLPAGIALRWVTFMLKIYRAEDIPQMDDAFSQTVKEIFGGNADKKNLVDPFVE
SQ  VSFAGKKVCTNIIERNANPEWNQVVNLQIKFPSMCEKIKLTVYDWDRLTKNDVVGTTYLYLSKIAASGGEVEATTGETEV
SQ  GFVPTFGPCYLNLYGSPREYTGFPDPYDELNSGKGEGVAYRGRIFVELNTFLEKKPPEKKLEPISSDDLLVVEKYQRRRK
SQ  YSLSAVFHSATMLQDVGEAIQFEVSIGNYGNKFDATCKPLASTTQYSRAVFDGNYYYYLPWAHTKPVVTLTSYWEDISHR
SQ  LDAVNTLLVMAERLQSNIEAVKSGIQGKIPANQLAEVWLKLIDEVIEDTRYTLPVTEGKANVTVLDTQIRKLRSRFLSQI
SQ  HEAALRMRSEATDVKSTLLEIEEWLDKLMQLTEEPQNSMPDIIIWMIRGEKRLAYARIPAHQVLYSTSGGNASGKYCGKT
SQ  QTILLKYPQEKTNGPKVPVELRVNIWLGLSAVEKKFNSFAEGTFTVFAEMYENQALVFGKWGTSGLVGRHKFSDVTGKIK
SQ  LKREFFLPPKGWEWEGDWVVDPERSLLTEADAGHTEFTDEVYQNENRYPGGEWKQAEDTYTDANGDKAASPSEMTCPPGW
SQ  EWEDDAWIYDINRAVDEKGWEYGITIPPDNKPKSWVAAEKMYHTHRRRRLVRKRKKDLTQTASSTARAMEELEDREGWEY
SQ  ASLIGWKFHWKQRSSDTFRRRRWRRKMAPSETHGAAAIFKLEGALGADTTEDGEEKGPEKQKHSATTVFGANTPIVSCNF
SQ  DRVYIYHLRCYIYQARNLMALDKDSFSDPYAHVSFLHRSKTTEIIHSTLNPTWDQTIIFDEVEIFGEPQTVLQNPPNVTI
SQ  ELFDNDQVGKDEFLGRSICSPLVKLNSETDITPKLLWHPVMNGDKACGDVLVTAELILRNKDGSNLPILPSQRAPNLYMV
SQ  PQGIRPVVQLTAIEILAWGLRNMKNYQMASVTSPSLVVECGGERVESVVIKSLKKTPNFPSSVLFMKVFLPKEELYMPPL
SQ  VIKVIDHRQFGRKPVVGQCTIDHLDRFRCDPYAGKEDIVPQLKASLMSAPPCREVVIEIEDTKPLLASKLSEKEEEIVDW
SQ  WSKFYASSGEHEKCGQYIQKGYSKLKIYDCELEDVADFEGLTDFSDTFKLYRGKSDENEDPSVVGEFKGSFRIYPLPDDP
SQ  SVPAPPRQFRELPDSVPQECTVRIYIVQGLQLQPQDNNGLCDPYIKITLGKKVIEDRDHYIPNTLNPVFGRMYELSCYLP
SQ  QEKDLKISVYDYDTFTRDEKVGETTIDLENRFLSRFGSHCGIPEQYCVSGVNTWRDQLRPTQLLQNVARFKGFPPPVLSE
SQ  DGSRIRYGGRDYHLDEFEANKILHQHLGAPEERLALHILRTQGLVPEHVETRTLHSTFQPNISQGKLQMWVDVFPKSLGP
SQ  PGPPFNITPRKAKKYYLRVIIWNTKDVILDEKSITGEDMSDIYVKGWISGSEENKQKTDVHYRSLDGEGNFNWRFVFPFD
SQ  YLPAEQLCIVAKKEHFWSIDQTEFRVPPRLIIQIWDNDKFSLDDYLGFLELDLHRTIIPAKTSEKCSLDMIPDLKAMDPL
SQ  KAKTASLFEQRSMKGWWPCYADKDGTRVMAGKVEMTLEVLNEREADERPAGKGRSEPNMNPKLDPPNRPETSFLWFTNPC
SQ  KTMRFIVWRRFKWVIIGLLLLLILLLFVAVLLYSLPNYLSMKIVRPNA
//
ID  B3DLH6;
PN  Myoferlin;
GN  myof;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single- pass type II membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
DR  UNIPROT: B3DLH6;
DR  UNIPROT: A2RRS9;
DR  Pfam: PF00168;
DR  Pfam: PF08165;
DR  Pfam: PF08150;
DR  Pfam: PF08151;
DR  Pfam: PF16165;
DR  PROSITE: PS50004;
DE  Function: May play a role in membrane regeneration and repair. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005901;
GO  GO:0030659;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0046872;
GO  GO:0005543;
GO  GO:0061025;
GO  GO:0007520;
GO  GO:0007009;
GO  GO:0001778;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MISYEPPPSAISNPTDPGGTTIIQGDGENDEEEDRDIVDAGFNPSVPGAPGQTDTQIARRLVKGKKTRRILSNKPQDFQI
SQ  RIRVIEGRQLPGNNIKPVVKVSVGGQTHRTRIKRGNNPYFDEIFFYNVNMTPLELLDESVIFRLFNSGSIRADSLIGEFK
SQ  LDVGYIYDEPGHAVMRKWVLLNDPDDSSSGAKGYLKVSMFVVGTGDEPPVEKRDREMEDDDVESNLLLPAGVALRWVTFF
SQ  LKIYRAEDIPQMDDAFAQTVKEIFGADSDKKNLVDPFVEVSFAGKKVCTNRIEKNANPEWNQAVNLQIKFPSMCENIKLT
SQ  VYDWDRLTKNDAVGTTCLSLSKIAASGGEIEEYDSTGTGSSSLEATTEKEVGFLPTFGPCYLNLYGSPREYTGFPDPYDD
SQ  LNFGKGEGVAYRGRVLVELTTKLDNSSIKKIEDISSDDILVVEKYQRRRKYCLCAVFHSATMIQDIGEAIQFEVSIGNYG
SQ  NKFDSTCKPLASTTQYSRPIFDGNYYYYLPWSFTKPVVTLTSYWEDISHRLDIVNILIAMTDRLQSNISTLKSAIQAKLP
SQ  DVRLAEIWMRLIDQLIEDTMRPMPSLEGKANVTVLDKQRDKLRQTSLKYIQEAAIKMRGEATDVKATLTEIEDWLDRLQQ
SQ  LSEEPQNSMPDVIIWMIRAEKRLAYARVPAHQVLFSKTSEEACGKYCGKTQTVFLQYPLDKTKGLKIPTELRVNIWLGLS
SQ  EVEKKFNSYSEGTFSVYAEMYENQALLLGKWGTTGLLKRHKFSDVTGSIKLKRESFLPPKGWEWEDDWKVDPERSLLTEA
SQ  DAGHTEFTDEIFENEARYPGGEWKKADETFTDANGEKSASPSDLSCPFGWIWDDDGWMRDINRAVDENGWEYGLTIPPDS
SQ  KPKSWVAAEKMYHTNRRRRLVRKRKKDPKVSTTSKAALTPQEQEGWEYAALIGWKFHITPRSSDTFRRRRWRRKMAPSDQ
SQ  HGAAAIFKLEGALGTDMTEDEEKKGSEKQTATNVFGANTPIVSCTFDKFYTYHLRCYIYQARGLTPLDKDSFSDPYAHVS
SQ  FLHRSKTTETIRSTLNPTWDQTLIFNTIDIYGDPHAVAQNPPNVVIEIFDYDQVGKDEFLGRSVCMPMVKLNPEVDIAPK
SQ  LLWYPVMNSNKHCGDLLLAAELIIREKDGSNLPILPSQRAPQIYMVPQGIRPVVQLTAIEILTWGLRNMKSYQLASVTSP
SQ  SLIVECGGEIVETAVIKNLKKTPNFYSSVLFMKVLLPKDEMYVPPIIIKIVDHRPFGRKPVVGQCTIECLEEFRCDPYLT
SQ  KHEDAPELRVARLTSSPLRDVVIEVEDTKPLLANQLQEKEEEVVDWWSKYYASTGETEKCGQYIQKGYTTLKVYKCELEN
SQ  VSEFRGLTDFCDTFKLYRGKAEDSDDPSVVGEFKGSFRIYPLPDDPNIPYPPRQFLELPGTESQECIVRIYIVRGIDLQP
SQ  KDNNGLCDPYIKITLNKKVIEDRDHYIPNTLNPLFGRMYELSCFLPQEKDLKISVYDYDTLTRDEKVGETTIDLENRFLS
SQ  RFGSHCGLPQTYCISGINQWRDQLTPTQILQNFARLKSSPPPVFSDNGTRLTFSSKDYTLEEFENNRKIHQHLGPPNERL
SQ  ALYVLRTQGLVPEHVETRTLYSTFQPNISQGKLEMWVDVFPKSLGPPGPPFNITPRKAKKYVLRVIVWNTKDVILDEKSI
SQ  TGEEMSDIYVKGWIPGNEENKQKTDVHYRSLDGEGNFNWRFVFPFEYLPAEQLCIVSKKEHFWSLDKTEFKLPPKLILQI
SQ  WDNDKFSLDDYLGFVELDLHRTTIPAKVPEKCSFNLLDQDKHSKVASLFEQKSMKGWWPCHAEKDGKRILAGKIEMTLEV
SQ  LNEKDAEERPAGKGRDEPNMNPKLDPPNRPDTSFLWFTNPCKTMKFIIWRRFKWVFIGLIILLLVLLFLGVFFYSLPGYV
SQ  SMKIVKPNL
//
ID  Q6NSJ0;
PN  Myogenesis-regulating glycosidase;
GN  MYORG;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q69ZQ1}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q69ZQ1}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:29910000}; Single- pass type II membrane protein {ECO:0000250|UniProtKB:Q69ZQ1}. Note=Only a minor fraction is present in the peripheral endoplasmic reticulum. {ECO:0000250|UniProtKB:Q69ZQ1}.
DR  UNIPROT: Q6NSJ0;
DR  UNIPROT: Q5T587;
DR  UNIPROT: Q5T588;
DR  UNIPROT: Q9ULQ9;
DR  Pfam: PF01055;
DR  OMIM: 618255;
DR  OMIM: 618317;
DR  DisGeNET: 57462;
DE  Function: Putative glycosidase. Promotes myogenesis by activating AKT signaling through the maturation and secretion of IGF2. {ECO:0000250|UniProtKB:Q69ZQ1}.
DE  Disease: Basal ganglia calcification, idiopathic, 7, autosomal recessive (IBGC7) [MIM:618317]: A form of basal ganglia calcification, a genetically heterogeneous condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas. {ECO:0000269|PubMed:29910000, ECO:0000269|PubMed:30460687, ECO:0000269|PubMed:30589467, ECO:0000269|PubMed:30656188, ECO:0000269|PubMed:30895394, ECO:0000269|PubMed:31009047}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P80370; IntAct: EBI-21555448; Score: 0.35
DE  Interaction: O95274; IntAct: EBI-21607810; Score: 0.35
DE  Interaction: Q9HAT2; IntAct: EBI-21753979; Score: 0.35
DE  Interaction: Q9Y680; IntAct: EBI-21844541; Score: 0.35
DE  Interaction: Q9NQZ7; IntAct: EBI-21844541; Score: 0.35
DE  Interaction: Q99675; IntAct: EBI-21844541; Score: 0.35
DE  Interaction: Q8WW22; IntAct: EBI-21844541; Score: 0.35
DE  Interaction: Q8TDY4; IntAct: EBI-21844541; Score: 0.35
DE  Interaction: Q8NAV1; IntAct: EBI-21844541; Score: 0.35
DE  Interaction: Q8N5K1; IntAct: EBI-21844541; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-21844541; Score: 0.35
DE  Interaction: Q8N3C7; IntAct: EBI-21871349; Score: 0.35
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0004553;
GO  GO:0005975;
GO  GO:0043568;
GO  GO:0051897;
GO  GO:0048741;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLQNPQEKSQAYPRRRRPGCYAYRQNPEAIAAAAMYTFLPDNFSPAKPKPSKDLKPLLGSAVLGLLLVLAAVVAWCYYSV
SQ  SLRKAERLRAELLDLKAGGFSIRNQKGEQVFRLAFRSGALDLDSCSRDGALLGCSLTADGLPLHFFIQTVRPKDTVMCYR
SQ  VRWEEAAPGRAVEHAMFLGDAAAHWYGGAEMRTQHWPIRLDGQQEPQPFVTSDVYSSDAAFGGILERYWLSSRAAAIKVN
SQ  DSVPFHLGWNSTERSLRLQARYHDTPYKPPAGRAAAPELSYRVCVGSDVTSIHKYMVRRYFNKPSRVPAPEAFRDPIWST
SQ  WALYGRAVDQDKVLRFAQQIRLHHFNSSHLEIDDMYTPAYGDFDFDEVKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSS
SQ  RFGEGVERELFVREPTGRLPALVRWWNGIGAVLDFTHPKARDWFQGHLRRLRSRYSVASFKFDAGEVSYLPRDFSTYRPL
SQ  PDPSVWSRRYTEMALPFFSLAEVRVGYQSQNISCFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDMVGGNAVP
SQ  QRTAGGDVPERELYIRWLEVAAFMPAMQFSIPPWRYDAEVVAIAQKFAALRASLVAPLLLELAGEVTDTGDPIVRPLWWI
SQ  APGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKWRSYKGELFDKTPVLLTDYPVDLDEIAYFTWAS
//
ID  Q69ZQ1;
PN  Myogenesis-regulating glycosidase;
GN  Myorg;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19706595}; Single-pass type II membrane protein {ECO:0000269|PubMed:19706595}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19706595}; Single-pass type II membrane protein {ECO:0000269|PubMed:19706595}. Note=Only a minor fraction is present in the peripheral endoplasmic reticulum (PubMed:19706595). {ECO:0000269|PubMed:19706595}.
DR  UNIPROT: Q69ZQ1;
DR  UNIPROT: A2ANN6;
DR  UNIPROT: B2RU42;
DR  Pfam: PF01055;
DE  Function: Putative glycosidase. Promotes myogenesis by activating AKT signaling through the maturation and secretion of IGF2 (PubMed:19706595). {ECO:0000269|PubMed:19706595}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0004553;
GO  GO:0005975;
GO  GO:0043568;
GO  GO:0051897;
GO  GO:0048741;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSQNLQETSQAYPRHRPGSHAGPKSLKVTPRATMYTFLPDNFSPAKPKPTKELRPLLCSAVLGLLLVLAAVVAWCYYSAS
SQ  LRKAERLRAELLDLNRGGFSIRNQKGEQVFRLAFRSGALDLDSCSRDGALLGCSRAADGRPLHFFIQTVRPKDTVMCYRV
SQ  RWEEAVPGRAVEHAMFLGDAAAHWYGGAEMRTQHWPIRLDGQQEPQPFVTSDVYSSDAAFGGILERYWLSSRAAAIKVND
SQ  SVPFHLGWNSTERSMRLQARYHDTSYKPPAGRTAAPELSYRVCVGSDVTSIHKYMVRRYFNKPSRVPASEAFRDPIWSTW
SQ  ALHGRAVDQNKVLQFAQQIRQHRFNSSHLEIDDMYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSS
SQ  FGEGVERELFVREPTGRLPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEVSYLPRDFSTYRPLS
SQ  DPSVWSRRYTEMAEPFFSLAEVRVGYQSQNISCFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDMIGGNAVPE
SQ  RTAGRQDGPGPERELYVRWLEVAAFMPAMQFSIPPWQYDAEVVAIAHKFAALRASLVAPLLLELAGEITDTGDPIVRPLW
SQ  WIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKWRSYKGELFDKTPVLLTDYPVDLDEVAYFTWAS
//
ID  A8T6P4;
PN  Rab effector MyRIP;
GN  myrip;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8K3I4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}.
DR  UNIPROT: A8T6P4;
DR  Pfam: PF02318;
DR  Pfam: PF04698;
DR  PROSITE: PS50916;
DE  Function: May link secretory vesicles to actin filaments (By similarity). May function as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030864;
GO  GO:0048471;
GO  GO:0030133;
GO  GO:0003779;
GO  GO:0046872;
GO  GO:0017022;
GO  GO:0031267;
GO  GO:0006886;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGRKLDLSGLSNNEAEHVLRVVQRDMQLRKKEEERLSEMKQELEEEGSRCLLLSKQQKFNEHCCIRCCSPFTFLLNPKRQ
SQ  CLDCHYNICKSCCSYSQSERGYICAACQKSRHLRTQSLEWFYNNVKSRFKRFGSAKVLKTLYRKHIIERGALSELPEVSA
SQ  HEGSNDNGSICDGSDSTLYKQSEGHSMADTLTVALRVAEEAIEEAIAKAENYKDSLEKQNEARYLHEHKEELIEELATTI
SQ  VQKIIQRGKRPEIQEEYEFVWPQNQKSELPSPTSTQNPLATQNSHSTSQPGAVAQSDISKRSRSAYSSDDSPEKGPEVGM
SQ  APGVPKSTEVETDIQNYSSLRRESRALSLPGWKSVDRLENSSASSVLQSPDGNWIALQSSQHSRPSLLTKRKSLVFSVLE
SQ  KESGVVSAYDEMGSDSDPEDQGGWGAALLQFRRRLSDETYYTDSQHDPEWTFTQHPPITSPSSGQYTNTETLNSDSETSP
SQ  SPSTRARRAPVMKKGPPETHLYPYYRHPADIVALPQLKPDVLDVNFNPHLGGDSSDGEERSEQVKRSRRRRKSKRETSEH
SQ  SRAHNALYSAATAENSTVLLNAMMMRRQQSQENTVPLNHQTPDSVTSPDILTFNNMSPEPEYQNTLAHNSSAASLPLLSQ
SQ  LGSNNPGFAPQDPLLRAFPVNETLEEELKYKLSELIGQVSERDVKSSDFEPISEVGNKQEDRVSEKDSGKLRPKERRESK
SQ  RESKLREMEKQSERQTVKLMDTSDAVRQINIERQMKKERERQRDIERQVERERERQRELEKQIEKDRERRREIEMQVEKK
SQ  QERQKEMEKQLKQEQERQSEIERDLEKKRKSIRMEKRN
//
ID  Q8NFW9;
PN  Rab effector MyRIP;
GN  MYRIP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8K3I4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}. Note=In presynaptic and postsynaptic areas in photoreceptor cells and in the basal microvilli of retinal pigment epithelium cells. Associated with melanosomes. Colocalizes with actin filaments. {ECO:0000250|UniProtKB:Q7TNY7}.
DR  UNIPROT: Q8NFW9;
DR  UNIPROT: B3KWM3;
DR  UNIPROT: B3KWW4;
DR  UNIPROT: B7Z2H1;
DR  UNIPROT: B7Z9V3;
DR  UNIPROT: G3XAI8;
DR  UNIPROT: Q32M41;
DR  UNIPROT: Q32M42;
DR  UNIPROT: Q569F7;
DR  UNIPROT: Q8IUF5;
DR  UNIPROT: Q9Y3V4;
DR  Pfam: PF02318;
DR  Pfam: PF04698;
DR  PROSITE: PS50916;
DR  OMIM: 611790;
DR  DisGeNET: 25924;
DE  Function: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments. Functions as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P62993; IntAct: EBI-1964454; Score: 0.40
DE  Interaction: P16333; IntAct: EBI-1969161; Score: 0.40
DE  Interaction: P27986; IntAct: EBI-1970169; Score: 0.40
DE  Interaction: P31016; IntAct: EBI-7970723; Score: 0.44
DE  Interaction: Q8TAB5; IntAct: EBI-10271494; Score: 0.72
DE  Interaction: O43482; IntAct: EBI-24530905; Score: 0.56
DE  Interaction: O00194; IntAct: EBI-24438904; Score: 0.56
DE  Interaction: P51159; IntAct: EBI-24457942; Score: 0.56
DE  Interaction: Q03135; IntAct: EBI-15800555; Score: 0.40
GO  GO:0030864;
GO  GO:0031045;
GO  GO:0000145;
GO  GO:0042470;
GO  GO:0048471;
GO  GO:0001750;
GO  GO:0045202;
GO  GO:0030133;
GO  GO:0003779;
GO  GO:0017022;
GO  GO:0051018;
GO  GO:0031267;
GO  GO:0008270;
GO  GO:0006886;
GO  GO:0032024;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGRKLDLSGLTDDETEHVLQVVQRDFNLRKKEEERLSELKQKLDEEGSKCSILSKHQQFVEHCCMRCCSPFTFLVNTKRQ
SQ  CGDCKFNVCKSCCSYQKHEKAWVCCVCQQARLLRAQSLEWFYNNVKSRFKRFGSAKVLKNLYRKHRLESGACFDILGGSL
SQ  FESNLENEGSISGSDSTFYRQSEGHSVMDTLAVALRVAEEAIEEAISKAEAYGDSLDKQNEASYLRDHKEELTEELATTI
SQ  LQKIIRKQKSKSEQQVEEEPGWPHPQSCSTKVADEGTSASPGGYRAPAALWRSQSAFSITGEEALKTPPVEAPSRQPRDQ
SQ  GQHPRAESALPSWKSVDRLDETNLAPVLQSPDGNWVALKDGAPPPTRLLAKPKSGTFQALEVASSVASAYDEMGSDSEED
SQ  FDWSEALSKLCPRSRALPRNPQPQPTQAQSSDQGPIAASPSSALSPNPEAMCSDSETSSAGSSREVGHQARLSWLQRKAP
SQ  RNPAAEKMRLHGELDVNFNPQLASRETSDSSEPEEAPHTTDRRARRWRRARLGSEEPSKEPSSPSAQLRDLDTHQVSDDL
SQ  SETDISNEARDPQTLTDTTEEKRRNRLYELAMKMSEKETSSGEDQESEPKTESENQKESLSSEDNSQSVQEELKKKFSAV
SQ  SLCNISTEVLKVINATEELIAGSTGPWESPQVPPDRQKGMFPRGTDQVRLDEQLTSLEENVYLAAGTVYGLETQLTELED
SQ  AARCIHSGTDETHLADLEDQVATAAAQVHHAELQISDIESRISALTIAGLNIAPCVRFTRRRDQKQRTQVQTIDTSRQQR
SQ  RKLPAPPVKAEKIETSSVTTIKTFNHNFILQGSSTNRTKERKGTTKDLMEPALESAVMY
//
ID  Q8K3I4;
PN  Rab effector MyRIP;
GN  Myrip;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12221080}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}. Melanosome {ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:12221080}. Note=In presynaptic and postsynaptic areas in photoreceptor cells and in the basal microvilli of retinal pigment epithelium cells. Associated with melanosomes. Colocalizes with actin filaments. In insulin- secreting cells, associated with dense core secretory granules. {ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:12221080}.
DR  UNIPROT: Q8K3I4;
DR  UNIPROT: A1L320;
DR  UNIPROT: A1L321;
DR  UNIPROT: Q8CFC0;
DR  UNIPROT: Q8K4H5;
DR  Pfam: PF02318;
DR  Pfam: PF04698;
DR  PROSITE: PS50916;
DE  Function: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments. Functions as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release. {ECO:0000269|PubMed:17827149}.
DE  Reference Proteome: Yes;
GO  GO:0015629;
GO  GO:0016324;
GO  GO:0030864;
GO  GO:0031045;
GO  GO:0000145;
GO  GO:0042470;
GO  GO:0048471;
GO  GO:0001750;
GO  GO:0030667;
GO  GO:0045202;
GO  GO:0030133;
GO  GO:0003779;
GO  GO:0046872;
GO  GO:0017022;
GO  GO:0051018;
GO  GO:0031267;
GO  GO:0006886;
GO  GO:0032024;
GO  GO:0030050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGRKLDLSGLTDDETEHVLQVVQRDFNLRKKEEDRLSEMKQRLAEENSKCSILSKHQKFVERCCMRCCSPFTFLVNARRR
SQ  CGECKFSVCKSCCSYQKHEKLWVCCVCQQARLLRTQSLEWFYNNVKSRFKRFGSAKVLKNLYRKHRLESGACFDILGGGL
SQ  FEPNLENEGSISGSDSTFYRQSEGHSMMDTLAVALRVAEEAIEEAISKAESHGDSLDKQNEASYLRDHKQELTEELAGTI
SQ  LQRIIRKQKDKAELRAEEEEPEWPRSQSGSVKARGEGTTAPPGRHKARATFRRSQSAFSFTMEDALKSGSAEAAPRSPKD
SQ  RAQRLLEEAALPSWRSMDGLDGTNLAPLLQSPDGNWMTLKDGSRQPPTRLLTKPKSGTFQALEVASSVTSAYDEIGSDSE
SQ  EDFDYSEALSKLCPPSQSRLKQPQPQPTQAQSSGQGPLATSPSNPEAMCSDSETSSTSSSREAGCRAKLSWLQRKAPKNP
SQ  AVEKMPLQGELDVNFNPQAAGGETSDSSDPEETLRTAERRARRWRRARVGPEESNRGLPSPGAHPRALHTAQVSDNVSET
SQ  DISNETQNSRSSTDSVEEKLRNRLYELAMKMSEKETSSGEDQESESKAEPKNQKGSLSSEENNQGVQEELKKKCSAVSLC
SQ  NISTEVLKVINATEELIAESAGPWEIPPVSTDRENGMFPLGTDQVRLDKQLTSLEENVYLAAGTVYGLEGQLSELEDAAR
SQ  CIHSSTGETELADLEDQVAAAAAQVHHAELQISDIESRISALTIAGLNIAPCVRLTRRRDQKQRSQVQTIDTSRQQRRKL
SQ  PAPPVKAEKIEASSVTPIKTFNRNFLLQGSSTNRPTASTGDTKDLMEPDLESAVMY
//
ID  Q7TNY7;
PN  Rab effector MyRIP;
GN  Myrip;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8K3I4}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17827149}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:17827149}. Melanosome {ECO:0000250|UniProtKB:Q8K3I4}. Note=In presynaptic and postsynaptic areas in photoreceptor cells and in the basal microvilli of retinal pigment epithelium cells. Associated with melanosomes. Colocalizes with actin filaments. {ECO:0000250|UniProtKB:Q8K3I4}.
DR  UNIPROT: Q7TNY7;
DR  Pfam: PF02318;
DR  Pfam: PF04698;
DR  PROSITE: PS50916;
DE  Function: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments (By similarity). Functions as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release. {ECO:0000250, ECO:0000269|PubMed:17827149}.
DE  Reference Proteome: Yes;
GO  GO:0015629;
GO  GO:0016324;
GO  GO:0030864;
GO  GO:0031045;
GO  GO:0000145;
GO  GO:0042470;
GO  GO:0048471;
GO  GO:0001750;
GO  GO:0030667;
GO  GO:0045202;
GO  GO:0030133;
GO  GO:0003779;
GO  GO:0046872;
GO  GO:0017022;
GO  GO:0051018;
GO  GO:0031267;
GO  GO:0006886;
GO  GO:0032024;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGRKLDLSGLTDDETEHVLQVVQRDFNLRKKEEDRLSEMKQRLAEENSKCSILSKHQKFVERCCMRCCSPFTFLVNARRR
SQ  CGECKFSVCKSCCSYQKHEKLWVCCVCQQARLLRTQSLEWFYNNVKTRFKRFGSAKVLKNLYKKHRLESGACFDILGGGL
SQ  YEPNLENEGSISGSDSTFYRQSEGHSMMDTLAVALQVAEEAIEEAISKAESQRDSLDKQNEASYLRDHRQELAEELAGTI
SQ  LQRIIRKQKDKADLHAEEEEPECTRPQSSGVKARGEGTAAPPGRHKARAALWRSQSAFSFTTEDTLKTSSAEAAPRQPKD
SQ  RAQRLLEESALPSWRSMDGLDGKNLVPLLQSPDGNWMTLKDSSRQPPTRLLAKPKSRTFQALEVASSVASAYDELGSDSE
SQ  EDFDYSEALSKLRPPSQGRLKQPQPQPAQAQSSGQGPLATSPSNPEAMCSDSETSSTSSSREAGCRAKLLWLQRKAPKNP
SQ  SAEKTHLQGELDVNFNPQAAGGETSDSSDPEETLHTADRRARRWRRARVGPEESNRGLPSPSAYPPALHTAQVSDNVSET
SQ  DISNEAQNSRSSTDSAEEKLRNRLYELAMKMSEKETSSGEDQESESKTEPKNQKGSLSSEENNQGVQEELKKKCSAVSLC
SQ  NISTEVLKVINATEELIAESAGPWEIPPVSTDRDNGMFPLGTDQRSLDKQLTSLEENVYLAAGTVYGLEGQLSELEDAAR
SQ  CIHSSTGETELADLEDQVAAAAAQVHHAELQISDIESRISALTIAGLNIAPCVRLTRRRDQKQRSQVQTIDTSRQQRRKL
SQ  PAPPVKAEKIEASSVTPIKTFNRNFLLQGSSTNRPTASTSNTKDLMEPVLESAVMY
//
ID  Q9C9T3;
PN  Mitotic-spindle organizing protein 1A;
GN  GIP2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q08AG7}. Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, phragmoplast. Nucleus envelope. Note=Reorganized from the nucleus to the prospindle and the preprophase band in late G2. After nuclear envelope breakdown, localized on spindle and phragmoplast microtubules (MTs) and on the reforming nuclear envelope of daughter cells. Present in mitotic microtubule arrays. In interphase cortical arrays, gamma-tubulin complexes are preferentially recruited to existing microtubules, from which new microtubules are efficiently nucleated.
DR  UNIPROT: Q9C9T3;
DR  Pfam: PF12554;
DE  Function: Required for gamma-tubulin complex recruitment to the microtubule organizing centers (MTOCs) (By similarity). During mitosis, modulates gamma-tubulin complex localization, spindle stability and chromosomal segregation. Necessary for gametophyte development and embryogenesis. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8LAZ7; IntAct: EBI-4512944; Score: 0.37
DE  Interaction: O82230; IntAct: EBI-4512952; Score: 0.37
DE  Interaction: Q56YJ8; IntAct: EBI-4512960; Score: 0.37
DE  Interaction: Q84K16; IntAct: EBI-4512968; Score: 0.37
DE  Interaction: Q8L7I1; IntAct: EBI-4512976; Score: 0.37
GO  GO:0000931;
GO  GO:0031021;
GO  GO:0005874;
GO  GO:0005635;
GO  GO:0009524;
GO  GO:0005819;
GO  GO:0042393;
GO  GO:0034080;
GO  GO:0034508;
GO  GO:0033566;
GO  GO:0051415;
GO  GO:0051418;
GO  GO:0090307;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNQEAAETARESLELVFRMSNILETGLDRHTLSVLIALCDIGLNPEALATLVKELRRDSATTTTTVD
//
ID  Q9M0N8;
PN  Mitotic-spindle organizing protein 1B;
GN  GIP1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q08AG7}. Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, phragmoplast. Nucleus envelope. Note=Reorganized from the nucleus to the prospindle and the preprophase band in late G2. After nuclear envelope breakdown, localized on spindle and phragmoplast microtubules (MTs) and on the reforming nuclear envelope of daughter cells. Present in mitotic microtubule arrays. In interphase cortical arrays, gamma-tubulin complexes are preferentially recruited to existing microtubules, from which new microtubules are efficiently nucleated.
DR  UNIPROT: Q9M0N8;
DR  Pfam: PF12554;
DE  Function: Required for gamma-tubulin complex recruitment to the microtubule organizing centers (MTOCs) (By similarity). During mitosis, modulates gamma-tubulin complex localization, spindle stability and chromosomal segregation. Necessary for gametophyte development and embryogenesis. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P29512; IntAct: EBI-1573933; Score: 0.51
GO  GO:0000930;
GO  GO:0000931;
GO  GO:0031021;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0009524;
GO  GO:0009574;
GO  GO:0005819;
GO  GO:0042393;
GO  GO:0034080;
GO  GO:0034508;
GO  GO:0033566;
GO  GO:0000226;
GO  GO:0051415;
GO  GO:0051418;
GO  GO:0090307;
GO  GO:0007052;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDEEASRTARESLELVFRMSNILDTGLDRHTLSVLIALCDLGVNPEALATVVKELRRESIPDSVTTTPSIH
//
ID  Q80UM3;
PN  N-alpha-acetyltransferase 15, NatA auxiliary subunit;
GN  Naa15;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Mainly cytoplasmic, nuclear in some cases. Present in the free cytosolic and cytoskeleton- bound polysomes, but not in the membrane-bound polysomes. {ECO:0000250}.
DR  UNIPROT: Q80UM3;
DR  UNIPROT: Q811Z9;
DR  UNIPROT: Q9JID5;
DR  Pfam: PF12569;
DR  Pfam: PF13181;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Auxillary subunit of N-terminal acetyltransferase complexes which display alpha (N-terminal) acetyltransferase (NAT) activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. {ECO:0000269|PubMed:10842358, ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:12888564, ECO:0000269|PubMed:15452080}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9GZZ1; IntAct: EBI-2563502; Score: 0.40
DE  Interaction: Q9BXJ9; IntAct: EBI-2563502; Score: 0.40
DE  Interaction: Q9NX55; IntAct: EBI-2563502; Score: 0.40
DE  Interaction: P41227; IntAct: EBI-2563502; Score: 0.40
DE  Interaction: Q6NZM9; IntAct: EBI-26472137; Score: 0.35
DE  Interaction: Q9CQE6; IntAct: EBI-26472808; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0031415;
GO  GO:0016604;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005667;
GO  GO:0016407;
GO  GO:0008080;
GO  GO:0043022;
GO  GO:0001525;
GO  GO:0030154;
GO  GO:0017196;
GO  GO:0006474;
GO  GO:0043066;
GO  GO:0045893;
GO  GO:0050821;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPAVSLPPKENALFKRILRCYEHKQYRNGLKFCKQILSNPKFAEHGETLAMKGLTLNCLGKKEEAYELVRRGLRNDLKSH
SQ  VCWHVYGLLQRSDKKYDEAIKCYRNALKWDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPAQRASWIGYAIAYHL
SQ  LEDYEMAAKILEEFRKTQQTSPDKVDYEYSELLLYQNQVLREAGLYREALEHLCTYEKQICDKLAVEETKGELLLQLCRL
SQ  EDAADVYRGLQERNPGNWAYYKGLEKALKPANMLERLKIYEEAWTKYPRGLVPRRLPLNFLSGEKFKECLDRFLRMNFSK
SQ  GCPPVFNTLRSLYRDKEKVAIVEELVVGYETSLKSCRLFNPNDDGKEEPPTTLLWVQYYLAQHYDKIGQPSIALEYINTA
SQ  IESTPTLIELFLVKAKIYKHAGNIKEAARWMDEAQALDTADRFINSKCAKYVLKANLIKEAEEMCSKFTREGTSAVENLN
SQ  EMQCMWFQTECAQAYKAMNKFGEALKKCHEIERHFIEITDDQFDFHTYCMRKITLRSYVDLLKLEDVLRQHPFYFKAARI
SQ  AIEIYLKLHDNPLTDENKEHEADTANMSDKELKKLRNKQRRAQKKAQIEEEKKNAEKEKQQRNQKKKKDDDDEEIGGPKE
SQ  ELIPEKLAKVETPLEEAIKFLTPLKNLVKNKIETHLFAFEIYFRKEKFLLMLQSVKRAFAIDSGHPWLHECMIRLFHSVC
SQ  ESKDLPETVRTVLKQEMNRLFGATNPKNFNETFLKRNSDSLPHRLSAAKMVYYLDSSSQKRAIELATTLDGSLTNRNLQT
SQ  CMEVLEALCDGSLGDCKEAAEAYRASCHKLFPYALAFMPPGYEEDMKITVNGDSSAETEELANEI
//
ID  P57103;
PN  Sodium/calcium exchanger 3;
GN  SLC8A3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:21959935}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:P70549}. Cell projection, dendrite {ECO:0000250|UniProtKB:P70549}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P70549}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:S4R2P9}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:S4R2P9}. Cell junction {ECO:0000250|UniProtKB:S4R2P9}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:S4R2P9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:S4R2P9}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21959935}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:21959935}; Multi-pass membrane protein {ECO:0000250|UniProtKB:S4R2P9}. Note=Detected at neuromuscular junctions. {ECO:0000250|UniProtKB:S4R2P9}.
DR  UNIPROT: P57103;
DR  UNIPROT: Q5K3P6;
DR  UNIPROT: Q5K3P7;
DR  UNIPROT: Q8IUE9;
DR  UNIPROT: Q8IUF0;
DR  UNIPROT: Q8NFI7;
DR  UNIPROT: Q96QG1;
DR  UNIPROT: Q96QG2;
DR  Pfam: PF03160;
DR  Pfam: PF01699;
DR  Pfam: PF16494;
DR  OMIM: 607991;
DR  DisGeNET: 6547;
DE  Function: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells, both in muscle and in brain. In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A3 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline. Contributes to Ca(2+) transport during excitation-contraction coupling in muscle. In neurons, contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory (By similarity). Required for normal oligodendrocyte differentiation and for normal myelination (PubMed:21959935). Mediates Ca(2+) efflux from mitochondria and contributes to mitochondrial Ca(2+) ion homeostasis (By similarity). {ECO:0000250|UniProtKB:S4R2P9, ECO:0000269|PubMed:21959935}.
DE  Reference Proteome: Yes;
DE  Interaction: P48165; IntAct: EBI-24665899; Score: 0.56
DE  Interaction: Q9H6H4; IntAct: EBI-21868787; Score: 0.35
DE  Interaction: Q9UPR5; IntAct: EBI-21868787; Score: 0.35
DE  Interaction: Q8TCT7; IntAct: EBI-21868787; Score: 0.35
DE  Interaction: Q8N6G5; IntAct: EBI-21868787; Score: 0.35
DE  Interaction: P43304; IntAct: EBI-21868787; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21024514; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005789;
GO  GO:0005887;
GO  GO:0031226;
GO  GO:0016020;
GO  GO:0005741;
GO  GO:0031594;
GO  GO:0043025;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0042383;
GO  GO:0016528;
GO  GO:0045202;
GO  GO:0005432;
GO  GO:0005516;
GO  GO:0099580;
GO  GO:0046872;
GO  GO:0098703;
GO  GO:0070588;
GO  GO:0007154;
GO  GO:0006874;
GO  GO:0071456;
GO  GO:0002244;
GO  GO:0006811;
GO  GO:0007612;
GO  GO:0007611;
GO  GO:0060291;
GO  GO:0007613;
GO  GO:0030001;
GO  GO:0051560;
GO  GO:0006851;
GO  GO:0098815;
GO  GO:0042552;
GO  GO:0071901;
GO  GO:0048709;
GO  GO:1903779;
GO  GO:0014819;
GO  GO:0035725;
GO  GO:0050808;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAWLRLQPLTSAFLHFGLVTFVLFLNGLRAEAGGSGDVPSTGQNNESCSGSSDCKEGVILPIWYPENPSLGDKIARVIVY
SQ  FVALIYMFLGVSIIADRFMASIEVITSQEREVTIKKPNGETSTTTIRVWNETVSNLTLMALGSSAPEILLSLIEVCGHGF
SQ  IAGDLGPSTIVGSAAFNMFIIIGICVYVIPDGETRKIKHLRVFFITAAWSIFAYIWLYMILAVFSPGVVQVWEGLLTLFF
SQ  FPVCVLLAWVADKRLLFYKYMHKKYRTDKHRGIIIETEGDHPKGIEMDGKMMNSHFLDGNLVPLEGKEVDESRREMIRIL
SQ  KDLKQKHPEKDLDQLVEMANYYALSHQQKSRAFYRIQATRMMTGAGNILKKHAAEQAKKASSMSEVHTDEPEDFISKVFF
SQ  DPCSYQCLENCGAVLLTVVRKGGDMSKTMYVDYKTEDGSANAGADYEFTEGTVVLKPGETQKEFSVGIIDDDIFEEDEHF
SQ  FVRLSNVRIEEEQPEEGMPPAIFNSLPLPRAVLASPCVATVTILDDDHAGIFTFECDTIHVSESIGVMEVKVLRTSGARG
SQ  TVIVPFRTVEGTAKGGGEDFEDTYGELEFKNDETVKTIRVKIVDEEEYERQENFFIALGEPKWMERGISALLLSPDVTDR
SQ  KLTMEEEEAKRIAEMGKPVLGEHPKLEVIIEESYEFKTTVDKLIKKTNLALVVGTHSWRDQFMEAITVSAAGDEDEDESG
SQ  EERLPSCFDYVMHFLTVFWKVLFACVPPTEYCHGWACFAVSILIIGMLTAIIGDLASHFGCTIGLKDSVTAVVFVAFGTS
SQ  VPDTFASKAAALQDVYADASIGNVTGSNAVNVFLGIGLAWSVAAIYWALQGQEFHVSAGTLAFSVTLFTIFAFVCISVLL
SQ  YRRRPHLGGELGGPRGCKLATTWLFVSLWLLYILFATLEAYCYIKGF
//
ID  S4R2P9;
PN  Sodium/calcium exchanger 3;
GN  Slc8a3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:14722618, ECO:0000269|PubMed:24101730}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:P70549}. Cell projection, dendrite {ECO:0000250|UniProtKB:P70549}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P70549}. Cell membrane, sarcolemma {ECO:0000269|PubMed:14722618}. Cytoplasm, sarcoplasm {ECO:0000269|PubMed:14722618}. Cell junction {ECO:0000269|PubMed:14722618}. Mitochondrion outer membrane {ECO:0000269|PubMed:24101730}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57103}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24101730}; Multi-pass membrane protein {ECO:0000305}. Note=Detected at neuromuscular junctions. {ECO:0000269|PubMed:14722618}. [Isoform 1]: Cell membrane {ECO:0000269|PubMed:24616101}; Multi-pass membrane protein {ECO:0000305}. [Isoform 2]: Cell membrane {ECO:0000269|PubMed:24616101}; Multi-pass membrane protein {ECO:0000305}.
DR  UNIPROT: S4R2P9;
DR  UNIPROT: Q7TS90;
DR  UNIPROT: Q8VHJ8;
DR  PDB: 2LT9;
DR  Pfam: PF03160;
DR  Pfam: PF01699;
DR  Pfam: PF16494;
DE  Function: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells, both in muscle and in brain (PubMed:14722618, PubMed:21593315). In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A3 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline (PubMed:14722618, PubMed:21593315). Contributes to Ca(2+) transport during excitation-contraction coupling in muscle (PubMed:14722618). In neurons, contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory (PubMed:21593315). Required for normal oligodendrocyte differentiation and for normal myelination (PubMed:21959935). Mediates Ca(2+) efflux from mitochondria and contributes to mitochondrial Ca(2+) ion homeostasis (PubMed:24616101). Isoform 1 displays higher calcium exchanger activity than isoform 2, probably because isoform 1 has a lower threshold for activation by cytoplasmic Ca(2+) (PubMed:24616101). {ECO:0000269|PubMed:14722618, ECO:0000269|PubMed:21593315, ECO:0000269|PubMed:21959935, ECO:0000269|PubMed:24616101}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0042995;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005789;
GO  GO:0005887;
GO  GO:0099055;
GO  GO:0031226;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031594;
GO  GO:0043025;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0042383;
GO  GO:0016528;
GO  GO:0045202;
GO  GO:0015368;
GO  GO:1905060;
GO  GO:0005432;
GO  GO:0005516;
GO  GO:0099580;
GO  GO:0046872;
GO  GO:1990034;
GO  GO:0098703;
GO  GO:0070588;
GO  GO:0060402;
GO  GO:0007154;
GO  GO:0006874;
GO  GO:0071320;
GO  GO:0071456;
GO  GO:0002244;
GO  GO:0007612;
GO  GO:0007611;
GO  GO:0060291;
GO  GO:0007613;
GO  GO:0030001;
GO  GO:0051560;
GO  GO:0006851;
GO  GO:0098815;
GO  GO:0042552;
GO  GO:0071901;
GO  GO:0048709;
GO  GO:0014819;
GO  GO:0035725;
GO  GO:0006814;
GO  GO:0050808;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAWLRLQPLTSAFLHFGLVTFVLFLNCLRAEAGDSGDVPSAGQNNESCSGSSDCKEGVILPIWYPENPSLGDKIARVIVY
SQ  FVALIYMFLGVSIIADRFMASIEVITSQEREVTIKKPNGETSTTTIRVWNETVSNLTLMALGSSAPEILLSLIEVCGHGF
SQ  IAGDLGPSTIVGSAAFNMFIIIGICVYVIPDGETRKIKHLRVFFVTAAWSIFAYIWLYMILAVFSPGVVQVWEGLLTLFF
SQ  FPVCVLLAWVADKRLLFYKYMHKKYRTDKHRGIIIETEGDHPKGIEMDGKMMNSHFLDGNFTPLEGKEVDESRREMIRIL
SQ  KDLKQKHPEKDLDQLVEMANYYALSHQQKSRAFYRIQATRMMTGAGNILKKHAAEQAKKTSSMSEVHTDEPEDFASKVFF
SQ  DPCSYQCLENCGAVLLTVVRKGGDISKTMYVDYKTEDGSANAGADYEFTEGTVVLKPGETQKEFSVGIIDDDIFEEDEHF
SQ  FVRLSNVRVEEEQLAEGMLPAILNSLPLPRAVLASPCVATVTILDDDHAGIFTFECDTIHVSESIGVMEVKVLRTSGARG
SQ  TVIVPFRTVEGTAKGGGEDFEDAYGELEFKNDETVKTIHIKVIDDKAYEKNKNYVIEMMGPRMVDMSVQKALLLSPEVTD
SQ  RKLTVEEEEAKRIAEMGKPVLGEHPKLEVIIEESYEFKSTVDKLIKKTNLALVVGTHSWRDQFMEAITVSAGGDEDEDES
SQ  GEERLPSCFDYVMHFLTVFWKVLFACVPPTEYCHGWACFVVSILIIGMLTAIIGDLASHFGCTIGLKDSVTAVVFVAFGT
SQ  SVPDTFASKAAALQDVYADASIGNVTGSNAVNVFLGIGLAWSVAAIYWAMQGQEFHVSAGTLAFSVTLFTIFAFVCLSVL
SQ  LYRRRPHLGGELGGPRGCKLATTWLFVSLWLLYILFATLEAYCYIKGF
//
ID  P70549;
PN  Sodium/calcium exchanger 3;
GN  Slc8a3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:16914199, ECO:0000269|PubMed:8798769, ECO:0000269|PubMed:9486131}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:16914199}. Cell projection, dendrite {ECO:0000269|PubMed:16914199}. Cell projection, dendritic spine {ECO:0000269|PubMed:16914199}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:S4R2P9}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:S4R2P9}. Cell junction {ECO:0000250|UniProtKB:S4R2P9}. Mitochondrion outer membrane {ECO:0000269|PubMed:16914199}; Multi-pass membrane protein {ECO:0000250|UniProtKB:S4R2P9}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16914199}; Multi-pass membrane protein {ECO:0000250|UniProtKB:S4R2P9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57103}. Note=Detected at neuromuscular junctions. {ECO:0000250|UniProtKB:S4R2P9}.
DR  UNIPROT: P70549;
DR  Pfam: PF03160;
DR  Pfam: PF01699;
DR  Pfam: PF16494;
DE  Function: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes (PubMed:8798769, PubMed:9486131). Contributes to cellular Ca(2+) homeostasis in excitable cells, both in muscle and in brain. In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A3 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline. Contributes to Ca(2+) transport during excitation- contraction coupling in muscle. In neurons, contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory. Required for normal oligodendrocyte differentiation and for normal myelination. Mediates Ca(2+) efflux from mitochondria and contributes to mitochondrial Ca(2+) ion homeostasis. {ECO:0000250|UniProtKB:S4R2P9, ECO:0000269|PubMed:8798769, ECO:0000269|PubMed:9486131}.
DE  Reference Proteome: Yes;
DE  Interaction: P20651; IntAct: EBI-7400767; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0042995;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005789;
GO  GO:0005887;
GO  GO:0099055;
GO  GO:0031226;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031594;
GO  GO:0043025;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0042383;
GO  GO:0016528;
GO  GO:0045202;
GO  GO:0015368;
GO  GO:1905060;
GO  GO:0005432;
GO  GO:0005516;
GO  GO:0099580;
GO  GO:0046872;
GO  GO:1990034;
GO  GO:0098703;
GO  GO:0070588;
GO  GO:0060402;
GO  GO:0007154;
GO  GO:0006874;
GO  GO:0071320;
GO  GO:0071456;
GO  GO:0002244;
GO  GO:0007612;
GO  GO:0007611;
GO  GO:0060291;
GO  GO:0007613;
GO  GO:0030001;
GO  GO:0051560;
GO  GO:0006851;
GO  GO:0098815;
GO  GO:0042552;
GO  GO:0071901;
GO  GO:0048709;
GO  GO:0014819;
GO  GO:0035725;
GO  GO:0006814;
GO  GO:0050808;
GO  GO:0021537;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAWLRLQPLTSAFLHFGLVTFVLFLNGLRAEAGDLRDVPSAGQNNESCSGSSDCKEGVILPIWYPENPSLGDKIARVIVY
SQ  FVALIYMFLGVSIIADRFMASIEVITSQEREVTIKKPNGETSTTTIRVWNETVSNLTLMALGSSAPEILLSLIEVCGHGF
SQ  IAGDLGPSTIVGSAAFNMFIIIGICVYVIPDGETRKIKHLRVFFVTAAWSVFAYIWLYMILAVFSPGVVQVWEGLLTLFF
SQ  FPVCVLLAWVADKRLLFYKYMHKRYRTDKHRGIIIETEGEHPKGIEMDGKMMNSHFLDGNLIPLEGKEVDESRREMIRIL
SQ  KDLKQKHPEKDLDQLVEMANYYALSHQQKSRAFYRIQATRMMTGAGNILKKHAAEQAKKTASMSEVHTDEPEDFASKVFF
SQ  DPCSYQCLENCGAVLLTVVRKGGDISKTMYVDYKTEDGSANAGADYEFTEGTVVLKPGETQKEFSVGIIDDDIFEEDEHF
SQ  FVRLSNVRVEEEQLEEGMTPAILNSLPLPRAVLASPCVATVTILDDDHAGIFTFECDTIHVSESIGVMEVKVLRTSGARG
SQ  TVIVPFRTVEGTAKGGGEDFEDTYGELEFKNDETVKTIRVKIVDEEEYERQENFFIALGEPKWMERGISALLLSPEVTDR
SQ  KLTMEEEEAKRIAEMGKPVLGEHPKLEVIIEESYEFKSTVDKLIKKTNLALVVGTHSWRDQFMEAITVSAAGDEEEDESG
SQ  EERLPSCFDYVMHFLTVFWKVLFACVPPTEYCHGWACFVVSILIIGMLTAIIGDLASHFGCTIGLKDSVTAVVFVAFGTS
SQ  VPDTFASKAAALQDVYADASIGNVTGSNAVNVFLGIGLAWSVAAIYWAMQGQEFHVSAGTLAFSVTLFTIFAFVCLSVLL
SQ  YRRRPHLGGELGGPRGCKLATTWLFVSLWLLYVLFATLEAYCYIKGF
//
ID  E7FDB3;
PN  Nanos homolog 1;
GN  nanos1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11691838}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11691838}.
DR  UNIPROT: E7FDB3;
DR  Pfam: PF05741;
DR  PROSITE: PS51522;
DE  Function: Acts as a translational repressor. Can mediate repression affecting different steps in the translation process: cap-driven, IRES- driven, polyadenylated RNAs or nonpolyadenylated RNAs (By similarity). Essential for the development of primordial germ cells (PGCs) by ensuring their proper migration and survival. {ECO:0000250, ECO:0000269|PubMed:11691838}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0060293;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0030371;
GO  GO:0008270;
GO  GO:0007281;
GO  GO:0008354;
GO  GO:0017148;
GO  GO:0048477;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDFLNHNYLSARASYDYTFNFWNDYLGLSTLVTKNSKHSVPQNPNSITESLKATLGLDDSPPCPCVMGEGDSGGHLDSCC
SQ  CPPPASISILDLKERFSILSPFQNQNQGSLLSSSQEREIGIGGGFAGFDLFGVERKMRKPAARNKQEPKICVFCRNNGAP
SQ  EEVYGSHVLKTPDGRVVCPILRAYTCPLCSANGDNAHTIKYCPLSKDQPAQRVLKGGRAVGGKRVKIF
//
ID  Q8WY41;
PN  Nanos homolog 1;
GN  NANOS1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12690449, ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:19168546}. Cytoplasm {ECO:0000269|PubMed:12690449, ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:19168546}. Note=Colocalizes with SNAPIN and PUM2 in the perinuclear region of germ cells. {ECO:0000269|PubMed:12690449, ECO:0000269|PubMed:19168546}.
DR  UNIPROT: Q8WY41;
DR  PDB: 4CQO;
DR  Pfam: PF05741;
DR  PROSITE: PS51522;
DR  OMIM: 608226;
DR  OMIM: 615413;
DR  DisGeNET: 340719;
DE  Function: May act as a translational repressor which regulates translation of specific mRNAs by forming a complex with PUM2 that associates with the 3'-UTR of mRNA targets. Capable of interfering with the proadhesive and anti-invasive functions of E-cadherin. Up-regulates the production of MMP14 to promote tumor cell invasion. {ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:18223680}.
DE  Disease: Spermatogenic failure 12 (SPGF12) [MIM:615413]: An infertility disorder caused by spermatogenesis defects. It results in decreased sperm motility, concentration, and multiple sperm structural defects. Non-obstructive azoospermia, oligozoospermia and oligo-astheno- teratozoospermia are features observed in SPGF12 patients. {ECO:0000269|PubMed:23315541}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O60716; IntAct: EBI-9639078; Score: 0.52
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0030371;
GO  GO:0008270;
GO  GO:0016477;
GO  GO:0098749;
GO  GO:0010631;
GO  GO:0017148;
GO  GO:0048477;
GO  GO:1900153;
GO  GO:0010608;
GO  GO:0001558;
GO  GO:0001894;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEAFPWAPRSPRRGRAPPPMALVPSARYVSAPGPAHPQPFSSWNDYLGLATLITKAVDGEPRFGCARGGNGGGGSPPSSS
SQ  SSSCCSPHTGAGPGALGPALGPPDYDEDDDDDSDEPGSRGRYLGSALELRALELCAGPAEAGLLEERFAELSPFAGRAAA
SQ  VLLGCAPAAAAAATTTSEATPREERAPAWAAEPRLHAASGAAAARLLKPELQVCVFCRNNKEAMALYTTHILKGPDGRVL
SQ  CPVLRRYTCPLCGASGDNAHTIKYCPLSKVPPPPARPPPRSARDGPPGKKLR
//
ID  Q80WY3;
PN  Nanos homolog 1;
GN  Nanos1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8WY41}. Cytoplasm {ECO:0000250|UniProtKB:Q8WY41}. Note=Colocalizes with SNAPIN and PUM2 in the perinuclear region of germ cells. {ECO:0000250|UniProtKB:Q8WY41}.
DR  UNIPROT: Q80WY3;
DR  UNIPROT: Q3UTS9;
DR  UNIPROT: Q8BIJ9;
DR  Pfam: PF05741;
DR  PROSITE: PS51522;
DE  Function: May act as a translational repressor which regulates translation of specific mRNAs by forming a complex with PUM2 that associates with the 3'-UTR of mRNA targets. Capable of interfering with the proadhesive and anti-invasive functions of E-cadherin. Up-regulates the production of MMP14 to promote tumor cell invasion (By similarity). Not essential for normal development. {ECO:0000250, ECO:0000269|PubMed:12834871}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0030371;
GO  GO:0008270;
GO  GO:0016477;
GO  GO:0098749;
GO  GO:0010631;
GO  GO:0017148;
GO  GO:0048477;
GO  GO:1900153;
GO  GO:0010608;
GO  GO:0001558;
GO  GO:0001894;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEAFPWAPRSPRRARAPAPMALVPSARYVSASGPVHPQPFSSWNDYLGLATLITRASDRGSPHEGPGPTAAGPTMGPPED
SQ  DEDDDGEEPEAGGRYLGGALELRALELCAGPAEPGLLEERFAELNPFAGRAAAVLLGCAPTASTTAAAASTAEVTPREEP
SQ  SPAWAAEPRLHAASGATAARLLKPELQVCVFCRNNKEAVALYTTHILKGPDGRVLCPVLRRYTCPLCGASGDNAHTIKYC
SQ  PLSKVPPPTVRPPPRSNRDSLPSKKLR
//
ID  Q90ZZ5;
PN  Nanos homolog 1;
GN  nanos1;
OS  8354;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=During early cleavage and blastula stages found close to the cell periphery in a germ plasm-like pattern. From gastrula stage on, detected predominantly in a perinuclear region (By similarity). {ECO:0000250}.
DR  UNIPROT: Q90ZZ5;
DR  Pfam: PF05741;
DR  PROSITE: PS51522;
DE  Function: Acts as a translational repressor. Can mediate repression affecting different steps in the translation process: cap-driven, IRES- driven, polyadenylated RNAs or nonpolyadenylated RNAs. Essential for the development of primordial germ cells (PGCs) by ensuring their proper migration and survival (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0060293;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0030371;
GO  GO:0008270;
GO  GO:0007281;
GO  GO:0008354;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDGGLCFDSWSDYLGLSSLISRGLQPRGEGENPSPRWNVSCPAPAEPLPSKEPEGRGYKGCGFCRSNKEAMSLYSSHRLR
SQ  SLDGRVLCPVLRGYTCPLCGANGDWAHTMRYCPLRQLLRNPQSPRNGQ
//
ID  Q07937;
PN  Nanos homolog 1;
GN  nanos1;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21195170}. Note=During early cleavage and blastula stages found close to the cell periphery in a germ plasm-like pattern. From gastrula stage on, detected predominantly in a perinuclear region.
DR  UNIPROT: Q07937;
DR  Pfam: PF05741;
DR  PROSITE: PS51522;
DE  Function: Acts as a translational repressor. Can mediate repression affecting different steps in the translation process: cap-driven, IRES- driven, polyadenylated RNAs or nonpolyadenylated RNAs. Essential for the development of primordial germ cells (PGCs) by ensuring their proper migration and survival. {ECO:0000269|PubMed:21195170}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9DEB9; IntAct: EBI-7812774; Score: 0.54
GO  GO:0005737;
GO  GO:0060293;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0030371;
GO  GO:0008270;
GO  GO:0007281;
GO  GO:0008354;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDGGLCFDSWSDYLGLSSLISRGLQPQREGERPRWDVLSPASAEPLPSNESVGHKGCGFCRSNREALSLYTSHRLRALDG
SQ  RVLCPVLRGYTCPLCGANGDWAHTMRYCPLRRLLRDPQSNSNNPKLRH
//
ID  Q90ZZ6;
PN  Nanos homolog 1;
GN  nanos1;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=During early cleavage and blastula stages found close to the cell periphery in a germ plasm-like pattern. From gastrula stage on, detected predominantly in a perinuclear region (By similarity). {ECO:0000250}.
DR  UNIPROT: Q90ZZ6;
DR  UNIPROT: B7ZTT7;
DR  Pfam: PF05741;
DR  PROSITE: PS51522;
DE  Function: Acts as a translational repressor. Can mediate repression affecting different steps in the translation process: cap-driven, IRES- driven, polyadenylated RNAs or nonpolyadenylated RNAs. Essential for the development of primordial germ cells (PGCs) by ensuring their proper migration and survival (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0060293;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0030371;
GO  GO:0008270;
GO  GO:0007281;
GO  GO:0008354;
GO  GO:0017148;
GO  GO:0048477;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDGGLCFNSWSDYLGLSSLISRGLQPREGGESPRPRWKASSPTPAEPLPSKAAEAHGHKGCGFCRSNREAQSLYSSHRLR
SQ  APDGRVLCPVLRGYTCPLCGANGDWAHTMRYCPLRHFLRHPHSPRDGQ
//
ID  P60321;
PN  Nanos homolog 2;
GN  NANOS2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:19168545}. Cytoplasm, P-body {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19168545}. Note=Localizes at P-bodies during gonocyte development (By similarity). More abundant in perinuclear region of the cytoplasm of the germ cells of the adult testis. {ECO:0000250}.
DR  UNIPROT: P60321;
DR  UNIPROT: Q17R30;
DR  UNIPROT: Q4G0P8;
DR  Pfam: PF05741;
DR  PROSITE: PS51522;
DR  OMIM: 608228;
DR  DisGeNET: 339345;
DE  Function: Plays a key role in the sexual differentiation of germ cells by promoting the male fate but suppressing the female fate. Represses the female fate pathways by suppressing meiosis, which in turn results in the promotion of the male fate. Maintains the suppression of meiosis by preventing STRA8 expression, which is required for premeiotic DNA replication, after CYP26B1 is decreased. Regulates the localization of the CCR4-NOT deadenylation complex to P-bodies and plays a role in recruiting the complex to trigger the degradation of mRNAs involved in meiosis. Required for the maintenance of the spermatogonial stem cell population. Not essential for the assembly of P-bodies but is required for the maintenance of their normal state (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: O95273; IntAct: EBI-10216567; Score: 0.67
DE  Interaction: P43365; IntAct: EBI-10216583; Score: 0.78
DE  Interaction: P60903; IntAct: EBI-24517826; Score: 0.56
DE  Interaction: Q9UIV1; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q9C0C2; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q9UKZ1; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q9UHA7; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q9UFF9; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q9NZN8; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q9HC44; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q9H9A5; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q9H2K2; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q96LI5; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q92600; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q8N4C8; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q14201; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q14192; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: Q14106; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: O95819; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: O75175; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: D6R9H6; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: A5YKK6; IntAct: EBI-21547464; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21024514; Score: 0.35
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0008270;
GO  GO:0030718;
GO  GO:0006402;
GO  GO:0045835;
GO  GO:0017148;
GO  GO:0048477;
GO  GO:1900153;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQLPPFDMWKDYFNLSQVVWALIASRGQRLETQEIEEPSPGPPLGQDQGLGAPGANGGLGTLCNFCKHNGESRHVYSSHQ
SQ  LKTPDGVVVCPILRHYVCPVCGATGDQAHTLKYCPLNGGQQSLYRRSGRNSAGRRVKR
//
ID  P60322;
PN  Nanos homolog 2;
GN  Nanos2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:20133598}. Cytoplasm, P-body {ECO:0000269|PubMed:20133598}. Cytoplasm, perinuclear region {ECO:0000250}. Note=More abundant in perinuclear region of the cytoplasm of the germ cells of the adult testis (By similarity). Localizes at P-bodies during gonocyte development. {ECO:0000250}.
DR  UNIPROT: P60322;
DR  UNIPROT: F8VQ09;
DR  Pfam: PF05741;
DR  PROSITE: PS51522;
DE  Function: Plays a key role in the sexual differentiation of germ cells by promoting the male fate but suppressing the female fate. Represses the female fate pathways by suppressing meiosis, which in turn results in the promotion of the male fate. Maintains the suppression of meiosis by preventing STRA8 expression, which is required for premeiotic DNA replication, after CYP26B1 is decreased. Regulates the localization of the CCR4-NOT deadenylation complex to P-bodies and plays a role in recruiting the complex to trigger the degradation of mRNAs involved in meiosis. Required for the maintenance of the spermatogonial stem cell population. Not essential for the assembly of P-bodies but is required for the maintenance of their normal state. {ECO:0000269|PubMed:12947200, ECO:0000269|PubMed:17138666, ECO:0000269|PubMed:18281459, ECO:0000269|PubMed:19745153, ECO:0000269|PubMed:20133598}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6ZQ08; IntAct: EBI-6507233; Score: 0.54
DE  Interaction: Q8K0V4; IntAct: EBI-6507244; Score: 0.43
DE  Interaction: Q60809; IntAct: EBI-6507244; Score: 0.43
DE  Interaction: Q8VEG6; IntAct: EBI-6507244; Score: 0.35
DE  Interaction: Q9JKY0; IntAct: EBI-6507244; Score: 0.43
DE  Interaction: P97789; IntAct: EBI-6507327; Score: 0.27
DE  Interaction: Q91YD3; IntAct: EBI-6553102; Score: 0.27
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0008270;
GO  GO:0030718;
GO  GO:0006402;
GO  GO:0045835;
GO  GO:0017148;
GO  GO:0048477;
GO  GO:1900153;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLPPFDMWRDYFNLSQVVMDIIQSRKQRQEGEVAEEPNSRPQEKSEQDLEGYPGCLPTICNFCKHNGESRHVYTSHQLK
SQ  TPEGVVVCPILRHYVCPLCGATGDQAHTLKYCPLNSSQQSLYRRSGRNSAGRRVKR
//
ID  Q58CN9;
PN  N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D;
GN  NAPEPLD;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}.
DR  UNIPROT: Q58CN9;
DR  Pfam: PF12706;
DE  Function: D-type phospholipase that hydrolyzes N-acyl- phosphatidylethanolamines (NAPEs) to produce bioactive N- acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (By similarity). Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain (By similarity). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (By similarity). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (By similarity). {ECO:0000250|UniProtKB:Q6IQ20, ECO:0000250|UniProtKB:Q8BH82}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005769;
GO  GO:0031901;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043227;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0032052;
GO  GO:0042802;
GO  GO:0102200;
GO  GO:0070290;
GO  GO:0008270;
GO  GO:0048874;
GO  GO:0070291;
GO  GO:0070292;
GO  GO:0009395;
GO  GO:0090336;
GO  GO:0050729;
GO  GO:0001659;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q6IQ20};
SQ  MDENETNQLLMTSNQYPKEAVRKRQNSRNSGGSDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNPSIPSLL
SQ  RWVITERDHSSVPCSKELDKELPVLKPYFIDDPEEAGVRGAGLRVTWLGHATVMVEMDELILLTDPIFSARASPSQRMGP
SQ  KRFRRAPCTVEELPRIDAVLVSHNHYDHLDCNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHD
SQ  KVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCSAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHV
SQ  DPEEAVKIHIDVQAKKSVAIHWGTFALANEHYLEPPAKLCEALEKYRLKTEDFLVLKHGESRYLNTDDEDVE
//
ID  Q6IQ20;
PN  N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D;
GN  NAPEPLD;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Golgi apparatus membrane {ECO:0000269|PubMed:25684574}; Peripheral membrane protein {ECO:0000305|PubMed:25684574}. Early endosome membrane {ECO:0000269|PubMed:25684574}; Peripheral membrane protein {ECO:0000305|PubMed:25684574}. Nucleus envelope {ECO:0000269|PubMed:25684574}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25684574}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000269|PubMed:25684574}.
DR  UNIPROT: Q6IQ20;
DR  UNIPROT: Q5CZ87;
DR  UNIPROT: Q769K1;
DR  PDB: 4QN9;
DR  Pfam: PF12706;
DR  OMIM: 612334;
DR  DisGeNET: 222236;
DE  Function: D-type phospholipase that hydrolyzes N-acyl- phosphatidylethanolamines (NAPEs) to produce bioactive N- acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (PubMed:14634025, PubMed:16527816, PubMed:27571266, PubMed:25684574). Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain (By similarity). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (By similarity). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (By similarity). {ECO:0000250|UniProtKB:Q8BH82, ECO:0000269|PubMed:14634025, ECO:0000269|PubMed:16527816, ECO:0000269|PubMed:25684574, ECO:0000269|PubMed:27571266}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6IQ20; IntAct: EBI-16143196; Score: 0.62
DE  Interaction: Q9NRI5; IntAct: EBI-21373874; Score: 0.00
GO  GO:0005737;
GO  GO:0005769;
GO  GO:0031901;
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043227;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0042622;
GO  GO:0032052;
GO  GO:0042802;
GO  GO:0102200;
GO  GO:0070290;
GO  GO:0008270;
GO  GO:0048874;
GO  GO:0070291;
GO  GO:0070292;
GO  GO:0009395;
GO  GO:0090336;
GO  GO:0050729;
GO  GO:0001523;
GO  GO:0001659;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:25684574};
SQ  MDENESNQSLMTSSQYPKEAVRKRQNSARNSGASDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNPSIPNV
SQ  LRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGVREAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYM
SQ  GPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPG
SQ  HDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQ
SQ  HVDPEEAVRIHTDVQTKKSMAIHWGTFALANEHYLEPPVKLNEALERYGLNAEDFFVLKHGESRYLNNDDENF
//
ID  Q8BH82;
PN  N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D;
GN  Napepld;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}.
DR  UNIPROT: Q8BH82;
DR  Pfam: PF12706;
DE  Function: D-type phospholipase that hydrolyzes N-acyl- phosphatidylethanolamines (NAPEs) to produce bioactive N- acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (PubMed:14634025, PubMed:15760304, PubMed:17655883, PubMed:21801852). Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain (PubMed:21801852, PubMed:16605240). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (PubMed:31685899). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose (PubMed:25757720). Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (PubMed:14634025). {ECO:0000269|PubMed:14634025, ECO:0000269|PubMed:15760304, ECO:0000269|PubMed:16605240, ECO:0000269|PubMed:17655883, ECO:0000269|PubMed:21801852, ECO:0000269|PubMed:25757720, ECO:0000269|PubMed:31685899}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005769;
GO  GO:0031901;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043227;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0032052;
GO  GO:0042802;
GO  GO:0102200;
GO  GO:0070290;
GO  GO:0004620;
GO  GO:0008270;
GO  GO:0048874;
GO  GO:0070291;
GO  GO:0070292;
GO  GO:1903999;
GO  GO:0009395;
GO  GO:0006644;
GO  GO:0090336;
GO  GO:0050729;
GO  GO:0001659;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q6IQ20};
SQ  MDEYEDSQSPAPSYQYPKETLRKRQNSVQNSGGSVSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNISIPNV
SQ  LRWLIMEKNHSGVPGSKEELDKELPVLKPYFVSDPEDAGVREAGLRVTWLGHATLMVEMDELIFLTDPMFSSRASPSQYM
SQ  GPKRFRRPPCTISELPTIDAVLISHNHYDHLDYGSVLALNERFGSELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPG
SQ  HDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWSRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQ
SQ  HADPEDAVRIHIDLQTKRSVAIHWGTFALANEHYLEPPVKLNEALERYGLSCEDFFILKHGESRYLNTDDRAFEET
//
ID  Q5RCU3;
PN  N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D;
GN  NAPEPLD;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}.
DR  UNIPROT: Q5RCU3;
DR  Pfam: PF12706;
DE  Function: D-type phospholipase that hydrolyzes N-acyl- phosphatidylethanolamines (NAPEs) to produce bioactive N- acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (By similarity). Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain (By similarity). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (By similarity). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (By similarity). {ECO:0000250|UniProtKB:Q6IQ20, ECO:0000250|UniProtKB:Q8BH82}.
DE  Reference Proteome: Yes;
GO  GO:0005769;
GO  GO:0031901;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0102200;
GO  GO:0070290;
GO  GO:0008270;
GO  GO:0048874;
GO  GO:0070292;
GO  GO:0009395;
GO  GO:0090336;
GO  GO:0050729;
GO  GO:0001659;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q6IQ20};
SQ  MDENESNQSLMTSSQYPKEAVRKRQNSARNSGGSDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNHSIPHV
SQ  LRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGVRETGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYM
SQ  GPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPG
SQ  HDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRRFMKYQ
SQ  HVDPEEAVRIHIDVQTKKSMAIHWGTFALANEHYLEPPVKLNEALERYGLNAEDFFVLKHGESRYLNTDDENF
//
ID  Q769K2;
PN  N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D;
GN  Napepld;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}.
DR  UNIPROT: Q769K2;
DR  Pfam: PF12706;
DE  Function: D-type phospholipase that hydrolyzes N-acyl- phosphatidylethanolamines (NAPEs) to produce bioactive N- acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (PubMed:14634025, PubMed:16527816, PubMed:17655883). Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain (By similarity). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (By similarity). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (By similarity). {ECO:0000250|UniProtKB:Q8BH82, ECO:0000269|PubMed:14634025, ECO:0000269|PubMed:16527816, ECO:0000269|PubMed:17655883}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005769;
GO  GO:0031901;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043227;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0032052;
GO  GO:0042802;
GO  GO:0102200;
GO  GO:0070290;
GO  GO:0004620;
GO  GO:0008270;
GO  GO:0007568;
GO  GO:0048874;
GO  GO:0070291;
GO  GO:0070292;
GO  GO:1903999;
GO  GO:0009395;
GO  GO:0006644;
GO  GO:0090336;
GO  GO:0050729;
GO  GO:0035900;
GO  GO:0001659;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q6IQ20};
SQ  MDENENSQSPAPSHQYPKETLRKRQNSVQNSGGSESSRLSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNVSIPNV
SQ  LRWLIMEKDHSSVPGSKEELDKELPVLKPYFISDPEEAGVREAGLRVTWLGHATLMVEMDELILLTDPMFSSRASPSQYM
SQ  GPKRFRRPPCTISELPPIDAVLISHNHYDHLDYGSVLALNERFGSELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPG
SQ  HDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQ
SQ  HADPEDAVRIHIDVQAKRSVAIHWGTFALANEHYLEPPVKLNEALERYGLKSEDFFILKHGESRYLNTDDKAFEET
//
ID  Q5TZ18;
PN  Neuron navigator 3;
GN  nav3;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250}.
DR  UNIPROT: Q5TZ18;
DR  Pfam: PF00004;
DR  Pfam: PF00307;
DR  PROSITE: PS50021;
DE  Function: May be involved in neuron regeneration. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030175;
GO  GO:0005794;
GO  GO:0030027;
GO  GO:0005640;
GO  GO:0003779;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0072576;
GO  GO:0007399;
GO  GO:0022008;
GO  GO:0031016;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHGLAPRSSELRVTESPMLSCQLSFKTEIHDRRTNLVPAPAATLARSSREAEESKICKIYTDWANHYLAKSGCPRLIKD
SQ  LTQDIPDGVLLAEIIQIIANEKIEDINSCPKSHSQMIENVECCLSFLGARGVSVQGLSAEEVCNGNLKSILGLFFILSRY
SQ  KQQQQHQQQYLQSLVELQQHVTHQTTGAAQLSQHKTQDMQSSLTARYTSPPGHSGIAAPQKKNTRLPGPSRVPAAGSGSN
SQ  SSKGSSNLNRRSQSFNSIDKSKPLQYASGNDRGSMNGSGSVPSSTSGQQLASAIPSPTAGKTWRSKSMNMKHSATSSMLA
SQ  TKPPSPTSSPTPPSSSDRLRPPITDASKSAPGNQRSMLEKFRILNPRATSRTSPSVAEMALQEEDDLSEFGDEGTFSPTP
SQ  PCGISKQQGKPSASAFAPPSKSNNCKNHNNKSLPQPKDKEDKNKTKNKASTPPKEEPVIVETSKKGSKIASLIPKGSKTS
SQ  AASVKKESAIPASSSIPKPGLKAPTATSKPAGTQSCVPATTGGEKTKLNKGSQSIYMQRSLGGLENRKTSMVLSTSTSAL
SQ  SASTTSGLGGGCALGGNGAVQLPQQQQHNHPNTATVAPFMYRTYSENDCTTVVPPEPCLSPTKELVYGKTAKQCLEEISG
SQ  EDPETRRMRTVKNIADLRQNLEETMSSLRGTQITHSTLETTFDTTVTTEVNGRGLPALSSRSSPMSWRLGQGSSPRLQAG
SQ  DAPSYTPPRSSAGSTTVRYGEPSRLLYTAPLRRAAASGARGAEPGEKGGISEVGPEVDVTGYGSDGDILAKNVHADDISG
SQ  YHTDGGIYSRNVDLYSRNVGRPAEMTPAREVVQKGVKEMQGEDSWDDSSSVSSGLSDTLDNISTDDLNPAPYSGISSRKS
SQ  KAAQSNKETHRHIEQDASSWAGAEDLKKVDEEMEPGMDPSCKWKTSSPSSSCQGEDISQKTGLPMSQTGSWRRGMSAQVG
SQ  ITPPRTKGTSTSLKTPGKTDDAKASEKGKGSPKSPSIQRSPSDAGKSSGDEGKKPPSGIARPPTTSSFGYKKIPGPAGAL
SQ  ITASGATLTSGSATLGKVPKSACIGKSTGISNGRKTSLDGAQHQDDAVLLGCGGSEVPLQYRSLPRPAKSSSGGSSVVSR
SQ  SGHRSSSSSIDSNVSGKSAGGSGVAVGTPTSTKRRDTGKVGSGRSSPVTINQTDKEKVAGSDQEGTGLPTSPKSSPTSTQ
SQ  SGLRQPGSKYPDIASPTFRRLFGSKASSKPSSPGTPDSGKCPSALGSPHGTLARQASLDSPSSGTGSLGSMGGQSGGSSP
SQ  LYGKTPDLGTDSPASSPASGLSLPSNARPWPPNLSSSSAGSKDTLSCHSMTSLHTSSESIDLPLPHHHGPKVTRTGSVKS
SQ  TLSEGMPLDRNTLPKKGLRQTSHEEGKEWLRSHSTGGLQDTGSPLSPPGTTCANAGKYHYSNLLSPTSMSQYNIPSTSMS
SQ  RSNSIPAQDSFELYGEGHPLGGSATSLEERPRGMSRSGSFRDSTDEVHGSSLSLVSSTSSLYSAQIRKLRRELDASQEKV
SQ  ATLTSQLAANAHLVAAFEKSLANMTCRLQSLTMTAEQKESELAELRETIEALKTQNTDAQTAIQVALNGPDHVHRDLRIR
SQ  RQHSSESMSSINSAASHSSLGSAKDAEDKKKKKKSWLRSSFKQAFSKKKTNKPQSSHDEIEEMTDSSLPSSPKLLHISRQ
SQ  ASSPQPLLSSPSTTELCECTEAEAEIILQLKNELREKELKLTDIRLEALSSAHHLDQIREAMNRMQNEIELLKAENDRLK
SQ  SSGNTTPAATPAKTARPPSETSSTSSSSSRQSLGLSLNNLNITDTIMSDILLDDGYEGNLRKEGRSVRIVVTINSDSNKT
SQ  KAMQKKQYLIGSIGVSGKTKWDVLDGVIRRLFKEYVFRVDPLTSLGMNSDSIVCYRMGDVVRSHASEVPELLPCGYLVGD
SQ  NNVITVTLKGVKEGSIDDLVFDTLIPKPIIQRYLNLLMEHRRIILSGPSGTGKSYLATKLAYFILSKTGREVTDTNLATF
SQ  NVDQKSSKDLRQYLSSLAEQCNTEECEIELPTVVILDNLHHIGSLSDIFNGFLNCKYHKCPYVIGTMNQGVSSSPNLELH
SQ  HNFRWVLCANHTEPVKGFLGRFLRRKLIETEIDKNMRSNDLIKIIDWIPKIWQHLNSFLEAHSSSDVTIGPRLFLSCPMD
SQ  ADGSRVWFTDLWNYSLVPYLLEAVREGLQHEGQSLLQLRPEDVGYDGYSSSKDGAASKQVSQSDTEGDPLMNMLMRLQEA
SQ  ANYSSAQSCDSDSASHHEDLLDSSLESAL
//
ID  Q8IVL0;
PN  Neuron navigator 3;
GN  NAV3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250}.
DR  UNIPROT: Q8IVL0;
DR  UNIPROT: Q8NFW7;
DR  UNIPROT: Q9Y2E7;
DR  Pfam: PF00004;
DR  Pfam: PF00307;
DR  PROSITE: PS50021;
DR  OMIM: 611629;
DR  DisGeNET: 89795;
DE  Function: May regulate IL2 production by T-cells. May be involved in neuron regeneration. {ECO:0000269|PubMed:16166283}.
DE  Disease: Note=A chromosomal aberration disrupting NAV3 has been found in patients with Sezary syndrome (PubMed:16166283). Translocation t(12;18)(q21;q21.2) (PubMed:16166283). {ECO:0000269|PubMed:16166283}.
DE  Reference Proteome: Yes;
DE  Interaction: P25054; IntAct: EBI-3437272; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-3962281; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-11322719; Score: 0.35
DE  Interaction: P84101; IntAct: EBI-20900792; Score: 0.40
GO  GO:0005640;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0008017;
GO  GO:0030336;
GO  GO:0032703;
GO  GO:0007026;
GO  GO:0007399;
GO  GO:0022008;
GO  GO:0031116;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPVLGVASKLRQPAVGSKPVHTALPIPNLGTTGSQHCSSRPLELTETESSMLSCQLALKSTCEFGEKKPLQGKAKEKEDS
SQ  KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS
SQ  AEEIRNGNLKAILGLFFSLSRYKQQQHHQQQYYQSLVELQQRVTHASPPSEASQAKTQQDMQSSLAARYATQSNHSGIAT
SQ  SQKKPTRLPGPSRVPAAGSSSKVQGASNLNRRSQSFNSIDKNKPPNYANGNEKDSSKGPQSSSGVNGNVQPPSTAGQPPA
SQ  SAIPSPSASKPWRSKSMNVKHSATSTMLTVKQSSTATSPTPSSDRLKPPVSEGVKTAPSGQKSMLEKFKLVNARTALRPP
SQ  QPPSSGPSDGGKDDDAFSESGEMEGFNSGLNSGGSTNSSPKVSPKLAPPKAGSKNLSNKKSLLQPKEKEEKNRDKNKVCT
SQ  EKPVKEEKDQVTEMAPKKTSKIASLIPKGSKTTAAKKESLIPSSSGIPKPGSKVPTVKQTISPGSTASKESEKFRTTKGS
SQ  PSQSLSKPITMEKASASSCPAPLEGREAGQASPSGSCTMTVAQSSGQSTGNGAVQLPQQQQHSHPNTATVAPFIYRAHSE
SQ  NEGTALPSADSCTSPTKMDLSYSKTAKQCLEEISGEDPETRRMRTVKNIADLRQNLEETMSSLRGTQISHSTLETTFDST
SQ  VTTEVNGRTIPNLTSRPTPMTWRLGQACPRLQAGDAPSLGAGYPRSGTSRFIHTDPSRFMYTTPLRRAAVSRLGNMSQID
SQ  MSEKASSDLDMSSEVDVGGYMSDGDILGKSLRTDDINSGYMTDGGLNLYTRSLNRIPDTATSRDIIQRGVHDVTVDADSW
SQ  DDSSSVSSGLSDTLDNISTDDLNTTSSVSSYSNITVPSRKNTQLRTDSEKRSTTDETWDSPEELKKPEEDFDSHGDAGGK
SQ  WKTVSSGLPEDPEKAGQKASLSVSQTGSWRRGMSAQGGAPSRQKAGTSALKTPGKTDDAKASEKGKAPLKGSSLQRSPSD
SQ  AGKSSGDEGKKPPSGIGRSTATSSFGFKKPSGVGSSAMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGSQNQ
SQ  DDVVLHVSSKTTLQYRSLPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQTDKE
SQ  KEKVAVSDSESVSLSGSPKSSPTSASACGAQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGVKSSSVMPSPST
SQ  TLARQGSLESPSSGTGSMGSAGGLSGSSSPLFNKPSDLTTDVISLSHSLASSPASVHSFTSGGLVWAANMSSSSAGSKDT
SQ  PSYQSMTSLHTSSESIDLPLSHHGSLSGLTTGTHEVQSLLMRTGSVRSTLSESMQLDRNTLPKKGLRYTPSSRQANQEEG
SQ  KEWLRSHSTGGLQDTGNQSPLVSPSAMSSSAAGKYHFSNLVSPTNLSQFNLPGPSMMRSNSIPAQDSSFDLYDDSQLCGS
SQ  ATSLEERPRAISHSGSFRDSMEEVHGSSLSLVSSTSSLYSTAEEKAHSEQIHKLRRELVASQEKVATLTSQLSANAHLVA
SQ  AFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAIQGALNGPDHPPKDLRIRRQHSSESVSSINSAT
SQ  SHSSIGSGNDADSKKKKKKNWVNSRGSELRSSFKQAFGKKKSTKPPSSHSDIEELTDSSLPASPKLPHNAGDCGSASMKP
SQ  SQSASASPLVWPPKKRQNGPVIYKHRSRICECTEAEAEIILQLKSELREKELKLTDIRLEALSSAHHLDQIREAMNRMQN
SQ  EIEILKAENDRLKAETGNTAKPTRPPSESSSSTSSSSSRQSLGLSLNNLNITEAVSSDILLDDAGDATGHKDGRSVKIIV
SQ  SISKGYGRAKDQKSQAYLIGSIGVSGKTKWDVLDGVIRRLFKEYVFRIDTSTSLGLSSDCIASYCIGDLIRSHNLEVPEL
SQ  LPCGYLVGDNNIITVNLKGVEENSLDSFVFDTLIPKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVITKSGRK
SQ  KTEDAIATFNVDHKSSKELQQYLANLAEQCSADNNGVELPVVIILDNLHHVGSLSDIFNGFLNCKYNKCPYIIGTMNQGV
SQ  SSSPNLELHHNFRWVLCANHTEPVKGFLGRYLRRKLIEIEIERNIRNNDLVKIIDWIPKTWHHLNSFLETHSSSDVTIGP
SQ  RLFLPCPMDVEGSRVWFMDLWNYSLVPYILEAVREGLQMYGKRTPWEDPSKWVLDTYPWSSATLPQESPALLQLRPEDVG
SQ  YESCTSTKEATTSKHIPQTDTEGDPLMNMLMKLQEAANYSSTQSCDSESTSHHEDILDSSLESTL
//
ID  Q80TN7;
PN  Neuron navigator 3;
GN  Nav3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:12062803}.
DR  UNIPROT: Q80TN7;
DR  Pfam: PF00004;
DR  Pfam: PF00307;
DR  PROSITE: PS50021;
DE  Function: May regulate IL2 production by T-cells. May be involved in neuron regeneration. {ECO:0000269|PubMed:12062803}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8BHC1; IntAct: EBI-11568621; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26471532; Score: 0.35
GO  GO:1990752;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0005634;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0008017;
GO  GO:0030336;
GO  GO:0032703;
GO  GO:0007026;
GO  GO:0007399;
GO  GO:0022008;
GO  GO:0031116;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPVLGVASKLRQPAVGPKPVHAALPIPNLGISVSRRCSSRPLEFATPERSMLSCQLTLKSTCEFGEKKALQGTAKEIEDS
SQ  KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS
SQ  AEEIRNGNLKAILGLFFSLSRYKQQQHHQQQYYQSLVELQQRVTHTAPQSEASQAKTQQDMQSSLTARYAAQSKHSGIAT
SQ  SQKKPTRLPGPSRVPAASSSNKAQGASNLNRRSQSFNSIDKNKPPNYANGNEKDSPKGPQPSSGINGNTQPPSTSGQPPA
SQ  SAIPSPSASKPWRSKSMNVKHSATSTMLTVKQPSPATSPTPSSDRLKPPVTEGVKSAPSGQKSMLEKFKLVNARTALRPP
SQ  QAPSSGPNDGGREDDAFSESGEMEGFNSGLNSGGSTNSSPKVSPKLTPPKAGSKNFSNKKSLLQPKEKEEKTRDKNKACA
SQ  EKSGKEEKDQVTTEAAPKKTSKIASLIPKGSKTAAAKKESLIPSSSGIPKPGSKVPTPKQTISPGSAASKESEKFRTSKG
SQ  SSSQAFPKAITAEKASTPSLSTPLDGREAGQASPSSSCVMQVTHSSGQSPGNGAVQLPQQQQHSHPNTATVAPFIYRAHS
SQ  ENEGTSLPPADSCTSPTKMDSSYSKTAKQCLEEISGEDPEARRMRTVKNIADLRQNLEETMSSLRGTQISHSTLETTFDT
SQ  TVTTEVNGRAIPNLTSRPSPMTWRLGQACPRLQAGDAPSMGAGYSRSGTSRFIHTDPSRFMYTTPLRRAAVSRLGNMSQI
SQ  DMSEKASSDLDVSSEVDVGGYMSDGDILGKSLRADDINSGYMTDGGLNLYTRSLNRVPDTATSRDVIQRGVHDVTVDADS
SQ  WDDSSSVSSGLSDTLDNISTDDLNTTSSISSYSNITVPSRKNTQLKTDAEKRSTTDETWDSPEELKKAEGDCDSHGDGAA
SQ  KWKGATSGLAEDSEKTGQKASLSVSQTGSWRRGMSAQGGTPATARQKTSTSALKTPGKTDDAKASEKGKTPLKGSSLQRS
SQ  PSDAGKSSGDEGKKPPSGIGRSTASSSFGYKKPSGVGASTMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGS
SQ  QNQDDVVLHVSSKTTLQYRSLPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQT
SQ  DKEKEKVAVSDSESVSLSGSPKSSPTSASACGTQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGAKSSSVVLS
SQ  PSTSLARQGSLESPSSGTGSMGSAGGLSGSSSPLFNKPSDLTTDVISLSHSLASSPASVHSFTSGGLVWAANLSSSSAGS
SQ  KDTPSYQSMTSLHTSSESIDLPLSHHGSLSGLTTGTHEVQSLLMRTGSVRSTLSESMQLDRNTLPKKGLRYTPSSRQANQ
SQ  EEGKEWLRSHSTGGLQDTGNQSPLVSPSAMSSSATGKYHFSNLVSPTNLSQFNLPAPSMMRSSSIPAQDSSFDLYDDAQL
SQ  CGSATSLEERPRAVSHSGSFRDSMEEVHGSSLSLVSSTSSLYSTAEEKAHSEQIHKLRRELVASQEKVATLTSQLSANAH
SQ  LVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAIQGALNGPDHPPKDLRIRRQHSSESVSSIN
SQ  SATSHSSIGSGNDADSKKKKKKNWLRSSFKQAFGKKKSTKPPSSHSDIEELTDSSLPASPKLPHNAGESGSSSMKPSQSA
SQ  SAICECTEAEAEIILQLKSELREKELKLTDIRLEALSSAHHLDQIREAMNRMQNEIEILKAENDRLKAETGNTAKPARPP
SQ  SDSSSTASSSSSRQSLGLSLNNLNITESVTSDILLDDTGDATGHKDGRSVKIIVSISKGYGRAKDQKSQAYLIGSIGVSG
SQ  KTKWDVLDGVIRRLFKEYVFRIDTSSSLGLSSDCIASYCIGDLIRSHNLEVPELLPCGYLVGDNNIITVNLKGVEENSLD
SQ  SFVFDTLIPKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVITKSGRKKTEDAIATFNVDHKSSKELQQYLANL
SQ  AEQCSADNNGVELPVVIILDNLHHVGSLSDIFNGFLNCKYNKCPYIIGTMNQGVSSSPNLELHHNFRWVLCANHTEPVKG
SQ  FLGRYLRRKLIEMEIERNIRNNDLVKIIDWIPKTWHHLNSFLETHSSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLV
SQ  PYVLEAVREGLQMYGKRAPWEDPSKWVLDTYPWSSASLPQEGPALLQLRPEDVGYEACTSTKEATTSKHIPQTDTEGDPL
SQ  MNMLMKLQEAANYPSTQSCDGDSVSHREDILDTSIESTL
//
ID  O36307;
PN  Nucleoprotein;
GN  N;
OS  1980456;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: O36307;
DR  UNIPROT: Q80DP9;
DR  PDB: 2K48;
DR  PDB: 5E04;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (PubMed:25410857). Inhibits IFN signaling responses directed by the dsRNA sensors DDX58/RIG-I and IFIH1/MDA5, probably by interacting with host E3 ubiquitin ligase TRIM21 (PubMed:24549848). As a consequence, TBK1-directed IRF3 phosphorylation and TBK1 autophosphorylation are inhibited (PubMed:24549848, PubMed:30867297). Also displays sequence- unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000269|PubMed:24549848, ECO:0000269|PubMed:25410857, ECO:0000269|PubMed:30867297, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
GO  GO:0039503;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTLQELQENITAHEQQLVTARQKLKDAEKAVEVDPDDVNKSTLQSRRAAVSTLETKLGELKRQLADLVAAQKLATKPVD
SQ  PTGLEPDDHLKEKSSLRYGNVLDVNSIDLEEPSGQTADWKAIGAYILGFAIPIILKALYMLSTRGRQTVKDNKGTRIRFK
SQ  DDSSFEEVNGIRKPKHLYVSMPTAQSTMKAEEITPGRFRTIACGLFPAQVKARNIISPVMGVIGFGFFVKDWMDRIEEFL
SQ  AAECPFLPKPKVASEAFMSTNKMYFLNRQRQVNESKVQDIIDLIDHAETESATLFTEIATPHSVWVFACAPDRCPPTALY
SQ  VAGVPELGAFFSILQDMRNTIMASKSVGTAEEKLKKKSAFYQSYLRRTQSMGIQLDQKIIILYMLSWGKEAVNHFHLGDD
SQ  MDPELRQLAQSLIDTKVKEISNQEPLKL
//
ID  I7GVL4;
PN  Nucleoprotein;
GN  N;
OS  1980460;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:11160679}. Host Golgi apparatus, host cis-Golgi network {ECO:0000305|PubMed:11160679}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: I7GVL4;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNLKEVQDNITTHEQQLVAARQKLKDAERTVGVDPDDVNKSTLQNRRAAVSALEAKIGELKRQLADLVAAQKLATKSVD
SQ  PTGIEPDDHLKEKSSLRYGNVLDVNSIDLEEPSGQTADWKAIGTYILSFVLPIVLKALYMLSTRGRQTVKENKGTRIRFK
SQ  DDSSYEDVNGIRKPKHLYVSLPTAQSTMKADEITPGRFRTIVCGLFPAQIKARNIISPVMGVIGFSFFVKDWVDKIEDFL
SQ  RAECPFLPKPRAQAESFLSTNGAYFMNRQTQVEESKVQDILDLIDTAESGGATLFDNIASPQSAWIFACAPDRCPPTALY
SQ  VAGVPELGAFFSILQDMRNTIMASKSVGTAEEKLKKKSAFYQSYLRRTQSMGIQLDQKIIILYMINWGKEAVNHFHLGDD
SQ  MDPELRQLAQALVDTKVKEISNQEPLKI
//
ID  Q805Q9;
PN  Nucleoprotein;
GN  N;
OS  1980467;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: Q805Q9;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATLEELQKEINNHEGQLVIARQKVKDAEKQYEKDPDDLNKRALSDRESIAQSIQGKIDELRRQLADRVAAGKNIGKERD
SQ  PTGLDPGDHLKEKSMLSYGNVIDLNHLDIDEPTGQTADWLSIVVYLTSFVVPILLKALYMLTTRGRQTTKDNKGMRIRFK
SQ  DDSSFEDVNGIRKPKHLFLSMPNAQSSMKADEITPGRFRTAICGLYPAQVKARNLISPVMSVIGFLALAKNWTERVEEWL
SQ  DLPCKLLSEPSPTSLTKGPSTNRDYLNQRQGALAKMETKEAQAVRKHAIDAGCNLIDHIDSPSSIWVFAGAPDRCPPTCL
SQ  FIAGMAELGAFFAVLQDMRNTIMASKTIGTSEEKLKKKSSFYQSYLRRTQSMGIQLDQRIIVLFMVDWGKEAVDSFHLGD
SQ  DMDPELRGLAQALIDQKVKEISNQEPLKL
//
ID  P05133;
PN  Nucleoprotein;
GN  N;
OS  11602;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12573574}. Host Golgi apparatus, host cis-Golgi network {ECO:0000269|PubMed:24070985}. Note=Internal protein of virus particle. {ECO:0000305}.
DR  UNIPROT: P05133;
DR  PDB: 4FI5;
DR  PDB: 5FSG;
DR  PDB: 6I2N;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (PubMed:26923588). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (PubMed:30638449). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (PubMed:31091447). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). Suppresses apoptosis probably through the inhibition of nuclear import of NF-kappa-B (PubMed:20227103). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:Q89462, ECO:0000269|PubMed:20227103, ECO:0000269|PubMed:26923588, ECO:0000269|PubMed:30638449, ECO:0000269|PubMed:31091447, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
GO  GO:0019050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATMEELQREINAHEGQLVIARQKVRDAEKQYEKDPDELNKRTLTDREGVAVSIQAKIDELKRQLADRIATGKNLGKEQD
SQ  PTGVEPGDHLKERSMLSYGNVLDLNHLDIDEPTGQTADWLSIIVYLTSFVVPILLKALYMLTTRGRQTTKDNKGTRIRFK
SQ  DDSSFEDVNGIRKPKHLYVSLPNAQSSMKAEEITPGRYRTAVCGLYPAQIKARQMISPVMSVIGFLALAKDWSDRIEQWL
SQ  IEPCKLLPDTAAVSLLGGPATNRDYLRQRQVALGNMETKESKAIRQHAEAAGCSMIEDIESPSSIWVFAGAPDRCPPTCL
SQ  FIAGIAELGAFFSILQDMRNTIMASKTVGTSEEKLRKKSSFYQSYLRRTQSMGIQLGQRIIVLFMVAWGKEAVDNFHLGD
SQ  DMDPELRTLAQSLIDVKVKEISNQEPLKL
//
ID  P22047;
PN  Nucleoprotein;
GN  N;
OS  1980485;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: P22047;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQLREIQEEITRHEQQLVIARQKLKEAERTVEVDPDDVNKSTLQSRRSAVSTLEDKLAEFKRQLADVISRQKMDEKPVD
SQ  PTGIELDDHLKERSSLQYGNVLDVNSIDIEEPSGQTADWLKIGSYIIEFALPIILKALHMLSTRGRQTVKENKGTRIRFK
SQ  DDSSYEDVNGIRRPKHLYVSMPTAQSTMKAEELTPGRFRTIVCGLFPAQIMARNIISPVMGVIGFAFFVKDWADKVKAFL
SQ  DQKCPFLKAEPRPGQPAGEAEFLSSIRAYLMNRQAVLDETHLPDIDALVELAASGDPTLPDSLENPHAAWVFACAPDRCP
SQ  PTCIYIAGMAELGAFFAILQDMRNTIMASKTVGTAEEKLKKKSAFYQSYLRRTQSMGIQLDQRIILMYMIEWGNEVVNHF
SQ  HLGDDMDPELRQLAQALIDQKVKEISNQEPLKI
//
ID  P41267;
PN  Nucleoprotein;
GN  N;
OS  38998;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: P41267;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  LQARQQTVSALEDKIADYKRRMADAVSRKKMDTKPTDPTGIEPDDHLKERSSLRYGNVLDVNAIDIEEPSGQTADWYTIG
SQ  VYVIGFTLPIILKALYMLSTRGRQTVKENKGTRIRFKDDTSFEDINGIRRPKHLYVSMPTAQSTMKAEELTPGRFRTIVC
SQ  GLFPTQIQVRNIMSPVMGVIGFSFFVKDWADRIREFMEKECPFIKPEVKPGTPAQEAEFLKRNKVYFMQRQDVLDKNHVA
SQ  DIDKLIDYAASGDPTSPDNIESPNAPWVFACAPDRCPPTCIYVAGMAELGAFFSILQDMRNTIMASKTVGTAEEKLKKKS
SQ  SFYQSYLRRTQSMGIQLDQRIILLYMLEWGKEMVDH
//
ID  P41268;
PN  Nucleoprotein;
GN  N;
OS  38999;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: P41268;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
DE  Interaction: A0QR10; IntAct: EBI-26883494; Score: 0.32
DE  Interaction: A0QSG5; IntAct: EBI-26884055; Score: 0.50
DE  Interaction: A0A8B4QKV6; IntAct: EBI-26881799; Score: 0.49
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDLTDIQEDITRHEQQLVVARQKLKDAERAVEVDPDDVNKNTLQARQQTVSALEDKLADYKRRMADAVSRKKMDTKPTD
SQ  PTGIEPDDHLKERSSLRYGNVLDVNAIDIEEPSGQTADWYTIGVYVIGFTIPIILKALYMLSTRGRQTVKENKGTRIRFK
SQ  DDTSFEDINGIRRPKHLYVSMPTAQSTMKAEELTPGRFRTIVCGLFPTQIQVRNIMSPVMGVIGFSFFVKDWPERIREFM
SQ  EKECPFIKPEIKPGTPAQEMEMLKRNKIYFMQRQDVLDKNHVADIDKLIDYAASGDPTSPDNIDSPNAPWVFACAPDRCP
SQ  PTCIYVAGMAELGAFFSILQDMRNTIMASKTVGTAEEKLRKKSSFYQSYLRRTQSMGIQLDQRIILLFMLEWGKEMVDHF
SQ  HLGDDMDPELRGLAQALIDQKVKEISNQEPLKI
//
ID  P19475;
PN  Nucleoprotein;
GN  N;
OS  1337063;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: P19475;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDLTDIQEEITRHEQQLVVARQKLKDAERAVEVDPDDVNKSTLQARQQTVSALEDKLADYKRRMADAVSRKKMDTKPTD
SQ  PTGIEPDDHLKERSSLRYGNVLDVNAIDIEEPSGQTADWYTIGVYVIGFTIPIILKALYMLSTRGRQTVKENKGTRIRFK
SQ  DDTSFEDINGIRRPKHLYVSMPTAQSTMKAEELTPGRFRTIVCGLFPTQIQVRNIMSPVMGVIGFSFFVKDWPEKIREFM
SQ  EKECPFIKPEVKPGTPAQEVEFLKRNRVYFMTRQDVLDKNHVADIDKLIDYAASGDPTSPDDIESPNAPWVFACAPDRCP
SQ  PTCIYVAGMAELGAFFSILQDMRNTIMASKTVGTAEEKLKKKSSFYQSYLRRTQSMGIQLDQRIILLYMLEWGREMVDHF
SQ  HLGDDMDPELRGLAQSLIDQKVKEISNQEPLKI
//
ID  P41269;
PN  Nucleoprotein;
GN  N;
OS  39000;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: P41269;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDLTDIQEEITRHEQQLVVARQKLKDAERAVEVYPDDVIKNTLQARQQTVSALEDKLADYKRRMADAVSRKKMDTKPTD
SQ  PTGIEPDDHLKERSSLRYGNVLDVNAIDIEEPSGQTADWYTIGVYVIGFTIPIILKALYMLSTRGRQTVKENKGTRIRFK
SQ  DDTSFEDINGIRRPKHLYVSMPTAQSTMKAEELTPGRFRTIVCGLFPTQIQVRNIMSPVMGVIGFSFFVKDWPEKIREFM
SQ  EKECPFIKPEVKPGTPAQEVEFLKRNRVYFMTRQDVLDKNHVADIDKLIDYAASGDPTSPDDIKSPNAPWVFACAPDRSP
SQ  PTCIYVAGMAELGAFFSILQDMRNTIMASKTVGTAEEKLKRKSSFYQSYLRRTQSMGIQLDQRIILLYMLEWGKEMVDHF
SQ  HLGDDMDPELRGLAQSLIDQKVKEISNQEPLKI
//
ID  P41270;
PN  Nucleoprotein;
GN  N;
OS  39001;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: P41270;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDLTDIQEEITRHEQQLVVARQKLKDAERAVEVYPDDVNKNTLQARQQTVSALEDKLADYKRRMADAVSRKKMDTKPTD
SQ  PTGIEPDDHLKERSSLRYGNVLDVNAIDIEEPSGQTADWYTIGVYVIGFTIPIILKALYMLSTRGRQTVKENKGTRIRFK
SQ  DDTSFEDINGIRRPKHLYVSMPTAQSTMKAEELTPGRFRTIVCGLFPTQIQVRNIMSPVMGVIGFSFFVKDWPEKIREFM
SQ  EKECPFIKPEVKPGTPAQEVEFLKRNRVYFMTRQDVLDKNHVADIDKLIDYAASGDPTSPDDIESPNAPWVFACAPDRCP
SQ  PTCIYVAGMAELGAFFSILQDMRNTIMASKTVGTAEEKLKKKSSFYQSYLRRTQSMGIQLDQRIILLYMLEWGKEMVDHF
SQ  HLGDDMDPELRGLAQSLIDQKVKEISNQEPLKI
//
ID  P27313;
PN  Nucleoprotein;
GN  N;
OS  39002;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:11160679}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: P27313;
DR  UNIPROT: I4EPA2;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDLTDIQEDITRHEQQLIVARQKLKDAERAVEVDPDDVNKNTLQARQQTVSALEDKLADYKRRMADAVSRKKMDTKPTD
SQ  PTGIEPDDHLKERSSLRYGNVLDVNAIDIEEPSGQTADWYTIGVYVIGFTLPIILKALYMLSTRGRQTVKENKGTRIRFK
SQ  DDTSFEDINGIRRPKHLYVSMPTAQSTMKAEELTPGRFRTIVCGLFPTQIQVRNIMSPVMGVIGFSFFVKDWSERIREFM
SQ  EKECPFIKPEVKPGTPAQEIEMLKRNKIYFMQRQDVLDKNHVADIDKLIDYAASGDPTSPDNIDSPNAPWVFACAPDRCP
SQ  PTCIYVAGMAELGAFFSILQDMRNTIMASKTVGTAEEKLKKKSSFYQSYLRRTQSMGIQLDQRIILLFMLEWGKEMVDHF
SQ  HLGDDMDPELRGLAQALIDQKVKEISNQEPLKI
//
ID  Q07513;
PN  Nucleoprotein;
GN  N;
OS  39003;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: Q07513;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDLTDIQEEITRHEQQLVVARQKLKDAERAVEVDPDDVNKNTLQARQQTVSALEDKLADYKRRMADAVSRKKMDTKPTD
SQ  PTGIEPDDHLKERSSLRYGNVLDVNAIDIEEPSGQTADWYTIGVYVIGFTIPIILKALYMLSTRGRQTVKENKGTRIRFK
SQ  DDTSFEDINGIRRPKHLYVSMPTAQSTMKAEELTPGRFRTIVCGLFPTQIQVRNIMSPVMGVIGFSFFVKDWPERIRDFM
SQ  EKECPFIKPEVKPGTPAQEIEFLKRNRVYFMTRQDVLDKNHVADIDKLIDYAASGDPTSPDDIESPNAPWVFACAPDRCP
SQ  PTCIYVVGMAELGAFFSILQDMRNTIMASKTVGTAEEKLKKKSSFYQSYLRRTQSMGIQLDQRIILLYMLEWGKEMVDHF
SQ  HLGDDMDPELRGLAQSLIDQKVKEISNQEPLKI
//
ID  P59595;
PN  Nucleoprotein;
GN  N;
OS  694009;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170, ECO:0000269|PubMed:19106108}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:17210170}. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. {ECO:0000255|HAMAP-Rule:MF_04096}.
DR  UNIPROT: P59595;
DR  UNIPROT: Q7T3Z4;
DR  UNIPROT: Q7TA14;
DR  UNIPROT: Q7TF99;
DR  UNIPROT: Q80E50;
DR  PDB: 1SSK;
DR  PDB: 1X7Q;
DR  PDB: 2CJR;
DR  PDB: 2GIB;
DR  PDB: 2JW8;
DR  PDB: 2OFZ;
DR  PDB: 2OG3;
DR  PDB: 3I6L;
DR  PDB: 6IEX;
DR  PDB: 7LG0;
DR  Pfam: PF00937;
DR  PROSITE: PS51929;
DR  PROSITE: PS51928;
DE  Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication (PubMed:17210170). May modulate transforming growth factor-beta signaling by binding host SMAD3 (PubMed:18055455). {ECO:0000255|HAMAP- Rule:MF_04096, ECO:0000269|PubMed:17210170, ECO:0000269|PubMed:18055455}.
DE  Reference Proteome: Yes;
DE  Interaction: O43709; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O75569; IntAct: EBI-25639357; Score: 0.54
DE  Interaction: P19525; IntAct: EBI-26984718; Score: 0.40
DE  Interaction: P24385; IntAct: EBI-25746873; Score: 0.58
DE  Interaction: P63165; IntAct: EBI-7602710; Score: 0.54
DE  Interaction: P59595; IntAct: EBI-7602801; Score: 0.98
DE  Interaction: P09651; IntAct: EBI-7613676; Score: 0.60
DE  Interaction: P61769; IntAct: EBI-25487169; Score: 0.52
DE  Interaction: P59596; IntAct: EBI-25493215; Score: 0.91
DE  Interaction: P63279; IntAct: EBI-25497306; Score: 0.75
DE  Interaction: Q05639; IntAct: EBI-25498109; Score: 0.69
DE  Interaction: P62937; IntAct: EBI-25499625; Score: 0.68
DE  Interaction: P13645; IntAct: EBI-25635560; Score: 0.35
DE  Interaction: P04264; IntAct: EBI-25635560; Score: 0.35
DE  Interaction: P62333; IntAct: EBI-25635560; Score: 0.56
DE  Interaction: Q9HC16; IntAct: EBI-25641899; Score: 0.40
DE  Interaction: P59637; IntAct: EBI-25668008; Score: 0.57
DE  Interaction: P84022; IntAct: EBI-25682920; Score: 0.40
DE  Interaction: P84025; IntAct: EBI-25683178; Score: 0.52
DE  Interaction: P24941; IntAct: EBI-25746912; Score: 0.35
DE  Interaction: P20248; IntAct: EBI-25746912; Score: 0.35
DE  Interaction: P59594; IntAct: EBI-25823635; Score: 0.27
DE  Interaction: Q9Y3U8; IntAct: EBI-26376911; Score: 0.35
DE  Interaction: Q9HCE1; IntAct: EBI-26376911; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-26376911; Score: 0.35
DE  Interaction: P11940; IntAct: EBI-26376911; Score: 0.53
DE  Interaction: O76021; IntAct: EBI-26376911; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-26376911; Score: 0.74
DE  Interaction: Q9BQ75; IntAct: EBI-26376911; Score: 0.53
DE  Interaction: Q8TAD8; IntAct: EBI-26376911; Score: 0.53
DE  Interaction: Q8NCA5; IntAct: EBI-26376911; Score: 0.53
DE  Interaction: Q86U42; IntAct: EBI-26376911; Score: 0.35
DE  Interaction: Q6PKG0; IntAct: EBI-26376911; Score: 0.53
DE  Interaction: Q13310; IntAct: EBI-26376911; Score: 0.53
DE  Interaction: Q13283; IntAct: EBI-26376911; Score: 0.89
DE  Interaction: P67870; IntAct: EBI-26376911; Score: 0.35
DE  Interaction: P19784; IntAct: EBI-26376911; Score: 0.35
DE  Interaction: P16989; IntAct: EBI-26376911; Score: 0.53
DE  Interaction: O75683; IntAct: EBI-26376911; Score: 0.53
DE  Interaction: O43818; IntAct: EBI-26376911; Score: 0.35
DE  Interaction: Q92831; IntAct: EBI-26971417; Score: 0.44
DE  Interaction: Q92830; IntAct: EBI-26971428; Score: 0.44
DE  Interaction: Q14258; IntAct: EBI-27086792; Score: 0.46
DE  Interaction: P23249; IntAct: EBI-27090990; Score: 0.40
DE  Interaction: Q14011; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8WU68; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q13585; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8TBB5; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y388; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P20719; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NWT1; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: E9PRG8; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96G21; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96EU6; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96P11; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9P2D0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8WY91; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NQV6; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q32NC0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9BY49; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y6Y1; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q86XN8; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NP64; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y3A2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q03188; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: A6NFI3; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8WUQ7; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O15213; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q5T280; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96EZ8; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O14647; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: A8MTY0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8IUH3; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8IYN0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q86Y79; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q15397; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14191; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8TF76; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8NB50; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O95251; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9BY12; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: A0AV96; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q6NUN9; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9P1Y6; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14119; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q6P1M3; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96GY0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q13574; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8NI77; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9UH17; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O75525; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P49759; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q13523; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9HAZ1; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8N567; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q16698; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H7N4; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q12873; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NV31; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8NEF9; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14147; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q149N8; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q02880; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96BK5; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H9Y2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9P0L2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q12986; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9UKM9; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8N5F7; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O95625; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96K58; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NQZ2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96MX3; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96C57; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14CB8; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q15776; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9GZR2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O75330; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q709F0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y3Y2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NUL7; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q5VWQ0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P49761; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H6R4; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NY61; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H8H2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y2P8; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q5BKZ1; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P07305; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q6NZI2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H7B2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O00566; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O94761; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NUQ6; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14680; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P78332; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y4F1; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8WXF0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q5VYS8; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96PU8; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O95453; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9UL40; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q15050; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8NDT2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P49840; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9P275; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14244; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P11388; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H5H4; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9HC36; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H6F5; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H7H0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9ULW3; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8IYB3; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q6PK04; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9UGR2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q49A26; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O94813; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y5J1; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9BXS6; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y3C1; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q6DKI1; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P22492; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q12788; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NWH9; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P49841; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y4C8; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P27448; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H6R0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q3KQU3; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9UN81; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14137; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9BVJ6; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9UNX4; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P38935; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O43663; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q659C4; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NUD5; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q01780; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P46783; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O43660; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9UII4; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P46779; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O60306; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q13151; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14692; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q1KMD3; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14562; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q99729; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62136; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8N9T8; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q13601; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q07666; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P07910; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P42766; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q07020; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62899; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q5SSJ5; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q96E39; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NZB2; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q13206; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P10412; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P84103; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q92522; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9BVI4; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P05455; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62280; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q52LJ0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P08708; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P78316; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P16403; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H2U1; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P40429; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q8TDD1; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9BQ39; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P38159; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y224; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P26368; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62841; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P84098; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9UNX3; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62847; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62244; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9BZE4; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P61254; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q07955; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62277; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q6P158; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62241; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9H6S0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O43390; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P46781; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P39023; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62750; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P18621; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9Y3I0; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P67809; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P62701; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q9NR30; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q08211; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q92499; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: P61247; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q00987; IntAct: EBI-30810851; Score: 0.40
DE  Interaction: Q96CW1; IntAct: EBI-30812690; Score: 0.40
GO  GO:0044172;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:0005886;
GO  GO:1990904;
GO  GO:0019028;
GO  GO:0019013;
GO  GO:0003677;
GO  GO:0042802;
GO  GO:0060090;
GO  GO:0003723;
GO  GO:0019074;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDNGPQSNQRSAPRITFGGPTDSTDNNQNGGRNGARPKQRRPQGLPNNTASWFTALTQHGKEELRFPRGQGVPINTNSG
SQ  PDDQIGYYRRATRRVRGGDGKMKELSPRWYFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVL
SQ  QLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLNQLESKVSGKGQ
SQ  QQQGQTVTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSR
SQ  IGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPKKDKKKKTDEAQPLPQRQKKQPTVTLLPAAD
SQ  MDDFSRQLQNSMSGASADSTQA
//
ID  P17881;
PN  Nucleoprotein;
GN  N;
OS  11610;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:11160679}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: P17881;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATMEEIQREISAHEGQLVIARQKVKDAEKQYEKDPDDLNKRALHDRESVAASIQSKIDELKRQLADRLQQGRTSGQDRD
SQ  PTGVEPGDHLKERSALSYGNTLDLNSLDIDEPTGQTADWLTIIVYLTSFVVPIILKALYMLTTRGRQTSKDNKGMRIRFK
SQ  DDSSYEDVNGIRKPKHLYVSMPNAQSSMKAEEITPGRFRTAVCGLYPAQIKARNMVSPVMSVVGFLALAKDWTSRIEEWL
SQ  GAPCKFMAESLIAGSLSGNPVNRDYIRQRQGALAGMEPKEFQALRQHSKDAGCTLVEHIESPSSIWVFAGAPDRCPPTCL
SQ  FVGGMAELGAFFSILQDMRNTIMASKTVGTADEKLRKKSSFYQSYLRRTQSMGIQLDQRIIVMFMVAWGKEAVDNFHLGD
SQ  DMDPELRSLAQILIDQKVKEISNQEPMKL
//
ID  Q89462;
PN  Nucleoprotein;
GN  N;
OS  1980491;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000250|UniProtKB:P05133}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000250|UniProtKB:P05133}.
DR  UNIPROT: Q89462;
DR  PDB: 2IC6;
DR  PDB: 2IC9;
DR  PDB: 5E05;
DR  PDB: 5E06;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (PubMed:15650206, PubMed:15254200, PubMed:21378500, PubMed:16971445, PubMed:25062117, PubMed:16775315). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (PubMed:20164193). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (PubMed:19047634). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (PubMed:18971945, PubMed:25062117). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (PubMed:20844026, PubMed:20164193, PubMed:25062117). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (PubMed:27261891). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000269|PubMed:15254200, ECO:0000269|PubMed:15650206, ECO:0000269|PubMed:16775315, ECO:0000269|PubMed:16971445, ECO:0000269|PubMed:18971945, ECO:0000269|PubMed:19047634, ECO:0000269|PubMed:20164193, ECO:0000269|PubMed:20844026, ECO:0000269|PubMed:21378500, ECO:0000269|PubMed:25062117, ECO:0000269|PubMed:27261891, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
GO  GO:0006417;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTLKEVQDNITLHEQQLVTARQKLKDAERAVELDPDDVNKSTLQSRRAAVSALETKLGELKRELADLIAAQKLASKPVD
SQ  PTGIEPDDHLKEKSSLRYGNVLDVNSIDLEEPSGQTADWKSIGLYILSFALPIILKALYMLSTRGRQTIKENKGTRIRFK
SQ  DDSSYEEVNGIRKPRHLYVSMPTAQSTMKADEITPGRFRTIACGLFPAQVKARNIISPVMGVIGFSFFVKDWMERIDDFL
SQ  AARCPFLPEQKDPRDAALATNRAYFITRQLQVDESKVSDIEDLIADARAESATIFADIATPHSVWVFACAPDRCPPTALY
SQ  VAGMPELGAFFAILQDMRNTIMASKSVGTSEEKLKKKSAFYQSYLRRTQSMGIQLDQKIIILYMSHWGREAVNHFHLGDD
SQ  MDPELRELAQTLVDIKVREISNQEPLKL
//
ID  Q88918;
PN  Nucleoprotein;
GN  N;
OS  1980494;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12606074}. Host Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal protein of virus particle. {ECO:0000305}.
DR  UNIPROT: Q88918;
DR  Pfam: PF00846;
DE  Function: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). Inhibits the IFN signaling response directed by the dsRNA sensor DDX58/RIG-I (PubMed:33478127). {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462, ECO:0000269|PubMed:33478127, ECO:0000305}.
DE  Reference Proteome: No;
GO  GO:0019029;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:1990904;
GO  GO:0019013;
GO  GO:0004519;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQLKEIQEEITRHEQQIVIARQKLKDVEKTVEADPDDVNKSTLQSRRAAVSALEDKLADFKRQLADLVSSQKMGEKPVD
SQ  PTGLEPDDHLKERSSLRYGNVLDVNAIDIDEPSGQTADWFSIGQYITGFALAIILKALYMLSTRGRQTIKENKGTRIRFK
SQ  DDSSYEEINGIRRPKHLYVSMPTAQSTMKADELTPGRFRTIVCGLFPAQIMYRNIISPVMGVIGFSFFVKDWPEKIEEFL
SQ  IKPCPFLKKSGPSKEEDFLVSNDAYLLGREKALRESHLAEIDDLIDLAASGDPTPPDSIKSPQAPWVFACRPDRCPPTCI
SQ  YIAGMAELGAFFSILQDMRNTIMASKTVGTAEEKLKKKSSFYQSYLRRTQSMGIQLDQRIILLFMTEWGSDIVNHFHLGD
SQ  DMDPELRTLAQSLIDQKVKEISNQEPLKI
//
ID  O14253;
PN  Nuclear cap-binding protein subunit 1;
GN  cbc1;
OS  284812;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P34160}. Nucleus {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O14253;
DR  Pfam: PF02854;
DR  Pfam: PF09088;
DR  Pfam: PF09090;
DE  Function: Component of the CBC complex, which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. {ECO:0000250|UniProtKB:P34160}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005845;
GO  GO:0005846;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0000340;
GO  GO:0000339;
GO  GO:0006406;
GO  GO:0006397;
GO  GO:0000184;
GO  GO:0008380;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSYRGSTRPRKRTREGENYGFRPHRGNSQELLAARIKKDITFLADPRGNSVAADDINYVAMSLSREANDPETISTILDC
SQ  IQTTAFIIPVKIPHLATLIIRASLRVPLILEKAAAYFCLQYFTNLNSFLYYEAKVDLRMLICMSFALQPGTLKPLFSLLA
SQ  DAISKETKPSVWGDNFLRIILINLPYFIAANNDLGKKDFANEILDQCEIYVRHRKSSITLSNPLSIHDNLSEEELDLLYK
SQ  QLILSRENDFTFPYISQPWKFFESDFVHIVPVSPSIPEWTFQPTPQQNELPSFKRFFELFNNFEIRTTPDASDVAASIFR
SQ  DISVDVINHLEFNRVEAAQVLTDLDVYFTYKTFALRGTPVNELPNLDPSESRWKAEDIIVEAVLGELLGSQNTTYKPVYY
SQ  HSLLIECCRIAPKILAPTFGRVIRLMYTMSSDLPLQTLDRFIDWFSHHLSNFNFHWKWNEWIPDVELDDLHPKKVFMRET
SQ  ITRELILSYYTRISDSLPEELRCLLGEQPSGPNFVYENETHPLYQQSSQIIEALRLHKPLEELDIILQSEEIQNSETSAV
SQ  RLVMSCAYSLGSRSFSHALNVFEKHLNTLKHFSRKSLDSEIEVVDELFSFWKLQPFNAVMWLDKMLNYSIISITSIIEWL
SQ  IKQDVTIWSRSYTWSLVNTTFNKLAARLRRSVSNKEDSSLINEANEEKEIVTNLLLSALRALISENAENIWVSHWLNLML
SQ  KYVESNFLSVKKDTIEEANEPVQENTSEEQEDTKMQPVDAVDEQPSENNQTAADATNEEK
//
ID  P34160;
PN  Nuclear cap-binding protein complex subunit 1;
GN  STO1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10733586, ECO:0000269|PubMed:10823828, ECO:0000269|PubMed:8858145}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10823828}. Note=Predominantly nuclear, is able to exit the nucleus in an RNA-dependent manner. {ECO:0000269|PubMed:10823828}.
DR  UNIPROT: P34160;
DR  UNIPROT: D6VZU8;
DR  PDB: 3UKY;
DR  PDB: 6N7P;
DR  Pfam: PF02854;
DR  Pfam: PF09088;
DR  Pfam: PF09090;
DE  Function: Component of the CBC complex, which binds co- transcriptionally to the 5'-cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. The CBC complex is required for efficient pre-mRNA splicing through efficient commitment complex and spliceosome formation. Together with NPL3, the CBC complex is required for export of mRNAs out of the nucleus. The CBC complex is also involved in nuclear mRNA degradation, probably by directing the mRNAs to the sites of degradation. Affects replication of the positive- strand RNA virus BMV. {ECO:0000269|PubMed:10490594, ECO:0000269|PubMed:10733586, ECO:0000269|PubMed:10823828, ECO:0000269|PubMed:12756324, ECO:0000269|PubMed:12897126, ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:1512188, ECO:0000269|PubMed:15753296, ECO:0000269|PubMed:16166263, ECO:0000269|PubMed:8811086, ECO:0000269|PubMed:8846890, ECO:0000269|PubMed:8858145, ECO:0000269|PubMed:9499403}.
DE  Reference Proteome: Yes;
DE  Interaction: P06105; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P20676; IntAct: EBI-7438784; Score: 0.40
DE  Interaction: P40018; IntAct: EBI-784510; Score: 0.35
DE  Interaction: Q07508; IntAct: EBI-786510; Score: 0.35
DE  Interaction: P53207; IntAct: EBI-787143; Score: 0.35
DE  Interaction: Q03782; IntAct: EBI-787666; Score: 0.35
DE  Interaction: P53617; IntAct: EBI-787885; Score: 0.53
DE  Interaction: P28320; IntAct: EBI-788628; Score: 0.35
DE  Interaction: Q00916; IntAct: EBI-789921; Score: 0.35
DE  Interaction: P39935; IntAct: EBI-789934; Score: 0.35
DE  Interaction: P07260; IntAct: EBI-791281; Score: 0.53
DE  Interaction: Q03776; IntAct: EBI-792419; Score: 0.35
DE  Interaction: Q00539; IntAct: EBI-793423; Score: 0.35
DE  Interaction: Q02554; IntAct: EBI-794234; Score: 0.35
DE  Interaction: P38199; IntAct: EBI-796822; Score: 0.35
DE  Interaction: P54999; IntAct: EBI-797802; Score: 0.35
DE  Interaction: P10080; IntAct: EBI-798100; Score: 0.35
DE  Interaction: P40204; IntAct: EBI-798151; Score: 0.35
DE  Interaction: P32639; IntAct: EBI-798593; Score: 0.35
DE  Interaction: P32605; IntAct: EBI-800444; Score: 0.35
DE  Interaction: P32588; IntAct: EBI-801532; Score: 0.35
DE  Interaction: P38996; IntAct: EBI-802165; Score: 0.35
DE  Interaction: P36036; IntAct: EBI-806268; Score: 0.56
DE  Interaction: P39936; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-806268; Score: 0.53
DE  Interaction: Q02821; IntAct: EBI-806268; Score: 0.69
DE  Interaction: P25567; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P43321; IntAct: EBI-806268; Score: 0.35
DE  Interaction: Q06217; IntAct: EBI-806268; Score: 0.35
DE  Interaction: Q02260; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P23293; IntAct: EBI-806268; Score: 0.35
DE  Interaction: Q00416; IntAct: EBI-806268; Score: 0.35
DE  Interaction: Q04693; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P0C0W1; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P53552; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P33334; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P33203; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P40965; IntAct: EBI-806268; Score: 0.35
DE  Interaction: Q06142; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P38697; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P04911; IntAct: EBI-806268; Score: 0.35
DE  Interaction: Q08920; IntAct: EBI-806268; Score: 0.82
DE  Interaction: Q05949; IntAct: EBI-806268; Score: 0.35
DE  Interaction: Q12492; IntAct: EBI-806268; Score: 0.35
DE  Interaction: Q12476; IntAct: EBI-806268; Score: 0.44
DE  Interaction: Q05900; IntAct: EBI-806307; Score: 0.56
DE  Interaction: Q04493; IntAct: EBI-808510; Score: 0.35
DE  Interaction: P32561; IntAct: EBI-808736; Score: 0.35
DE  Interaction: P11633; IntAct: EBI-809930; Score: 0.35
DE  Interaction: Q12046; IntAct: EBI-811587; Score: 0.35
DE  Interaction: P32357; IntAct: EBI-812457; Score: 0.27
DE  Interaction: P33322; IntAct: EBI-817668; Score: 0.27
DE  Interaction: P47130; IntAct: EBI-820453; Score: 0.27
DE  Interaction: Q02159; IntAct: EBI-860110; Score: 0.00
DE  Interaction: P53854; IntAct: EBI-853865; Score: 0.35
DE  Interaction: Q02206; IntAct: EBI-6984951; Score: 0.40
DE  Interaction: P32558; IntAct: EBI-7056803; Score: 0.40
DE  Interaction: P47108; IntAct: EBI-7162654; Score: 0.40
DE  Interaction: Q06677; IntAct: EBI-3652626; Score: 0.35
DE  Interaction: P39101; IntAct: EBI-3654258; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3678092; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3696443; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3702075; Score: 0.35
DE  Interaction: P16474; IntAct: EBI-3705755; Score: 0.35
DE  Interaction: P0CS90; IntAct: EBI-3707131; Score: 0.35
DE  Interaction: P36016; IntAct: EBI-3708011; Score: 0.35
DE  Interaction: P39076; IntAct: EBI-3741611; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3747483; Score: 0.35
GO  GO:0000243;
GO  GO:0005845;
GO  GO:0005846;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0003729;
GO  GO:0000339;
GO  GO:0006370;
GO  GO:0031124;
GO  GO:0006406;
GO  GO:0000398;
GO  GO:0042789;
GO  GO:0000956;
GO  GO:0000184;
GO  GO:0031053;
GO  GO:0006970;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFNRKRRGDFDEDENYRDFRPRMPKRQRIPPVVQLCKEMMPDIRTIGESVKAFEDDIKFLSEAIMNEYGHEDYFNNALLS
SQ  TLNAVVVEQPQKQAAIALLTMVVNSKNNVAGKSIINYFFEELQKWCKQTYNDEFKSTSNETGPWNKIKLILRFLSILSPM
SQ  FLVDELINIYKSLFELSIELNNLDPGNRVPLSEAIYTNTLLNIPYLFFFNRNNDGLRTKVEELLAYVEQNYLVKTTDINL
SQ  LREYNGEPPYEMVELVRVVLPNVKKALINNLEQLNELFPDWNHLLTPQTGDEGFNDALTLPSVDDLKSFVRLNKNFGSVD
SQ  SMWKTPRYAFHVYLPNSAGNFETVVPISTYAGQLFNDIIIDLVESLEFNRKEVARQVITLDLFFKAGIFTEPGESIAQLI
SQ  ATYEENPLAPTFKIEDLAIETILGLIFKLPSVSQPFAYFYTLLVDICQNSPKAIAPVFGRAFRFFYSHLDSLDFELKLRY
SQ  LDWFSIQMSNFNFSWKWNEWEDDSIKFGKYFYNPKVNFAKNLIQKELRLTSNFSEVEDSLPQEFTKYLDTSYIPRDQLIN
SQ  YYQSLFTGYTVEEDSVRKNDLYFRQEGVPMENTVRKILDYTHKANNSREVTELESILGELKNEYGSIISDFNRFVIILLV
SQ  QAVTDSGSRSLSHANKYINDLKEDLKTIFAKIELDIETKEYIIIEAVLTFWNANPQTGFLVADAFKYAGLLTSRTIFTFI
SQ  FNETGLKNNGLIEATAIEAVFRNLSQQISEENESGNNFEFVFERLCTIANSTIDLLDVNADEDIEIPKVNGEMDIDDIED
SQ  DKLDLKWKYFTVIGFIKSILRRYSHEYRELADKFIANIDNAIPHESTRRTISNWIQETKEV
//
ID  Q9P383;
PN  Nuclear cap-binding protein subunit 2;
GN  cbc2;
OS  284812;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9P383;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: Component of the CBC complex, which binds co- transcriptionally to the 5' cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000243;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005846;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000339;
GO  GO:0045292;
GO  GO:0000398;
GO  GO:0051028;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASITRLDAVSPYLIRRFKNDLRALDAVKQSNCVYVGNLSFYTTEEQIYALFSKCGEIRRIIMGVDRFTKTPCGFCFVEY
SQ  FENQDALDSLKYISRTSLDERIIRADLDHGYEEGRQYGRGASGGQVRDEMREEFDPGRGGYAKNRQPTSSRQLANYSGIS
SQ  SAPLGSSLELQSNPRYNRWKKN
//
ID  Q08920;
PN  Nuclear cap-binding protein subunit 2;
GN  CBC2;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm, perinuclear region. Note=Predominantly nuclear, is able to exit the nucleus in an RNA- dependent manner.
DR  UNIPROT: Q08920;
DR  UNIPROT: D6W3J0;
DR  PDB: 6N7P;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: Component of the CBC complex, which binds co- transcriptionally to the cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. The CBC complex is required for efficient pre-mRNA splicing through efficient commitment complex and spliceosome formation. Together with NPL3, the CBC complex is required for export of mRNAs out of the nucleus. The CBC complex is also involved in nuclear mRNA degradation, probably by directing the mRNAs to the sites of degradation. Affects replication of the positive- strand RNA virus BMV. {ECO:0000269|PubMed:10490594, ECO:0000269|PubMed:10823828, ECO:0000269|PubMed:12756324, ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:15753296, ECO:0000269|PubMed:16166263, ECO:0000269|PubMed:8682299, ECO:0000269|PubMed:8811086, ECO:0000269|PubMed:8858145, ECO:0000269|PubMed:9215889}.
DE  Reference Proteome: Yes;
DE  Interaction: P34160; IntAct: EBI-806268; Score: 0.82
DE  Interaction: Q02821; IntAct: EBI-810994; Score: 0.77
DE  Interaction: Q06142; IntAct: EBI-810994; Score: 0.67
DE  Interaction: P40018; IntAct: EBI-784510; Score: 0.35
DE  Interaction: P53207; IntAct: EBI-787143; Score: 0.53
DE  Interaction: Q00539; IntAct: EBI-793423; Score: 0.53
DE  Interaction: P32605; IntAct: EBI-800444; Score: 0.35
DE  Interaction: P38996; IntAct: EBI-802165; Score: 0.53
DE  Interaction: P39936; IntAct: EBI-810994; Score: 0.53
DE  Interaction: P11484; IntAct: EBI-810994; Score: 0.53
DE  Interaction: P10591; IntAct: EBI-810994; Score: 0.53
DE  Interaction: Q03782; IntAct: EBI-810994; Score: 0.53
DE  Interaction: Q00916; IntAct: EBI-810994; Score: 0.53
DE  Interaction: Q06217; IntAct: EBI-810994; Score: 0.53
DE  Interaction: Q04693; IntAct: EBI-810994; Score: 0.53
DE  Interaction: P33334; IntAct: EBI-810994; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-810994; Score: 0.35
DE  Interaction: P53617; IntAct: EBI-810994; Score: 0.64
DE  Interaction: Q01560; IntAct: EBI-810994; Score: 0.53
DE  Interaction: Q03735; IntAct: EBI-810994; Score: 0.53
DE  Interaction: Q07508; IntAct: EBI-810994; Score: 0.53
DE  Interaction: P50094; IntAct: EBI-810994; Score: 0.35
DE  Interaction: P50095; IntAct: EBI-810994; Score: 0.35
DE  Interaction: P32357; IntAct: EBI-812457; Score: 0.27
DE  Interaction: Q12476; IntAct: EBI-814722; Score: 0.27
DE  Interaction: P20448; IntAct: EBI-817592; Score: 0.27
DE  Interaction: P47130; IntAct: EBI-820453; Score: 0.27
DE  Interaction: Q03330; IntAct: EBI-783119; Score: 0.35
DE  Interaction: P38074; IntAct: EBI-855796; Score: 0.00
DE  Interaction: P47108; IntAct: EBI-7162554; Score: 0.40
DE  Interaction: P36036; IntAct: EBI-7892497; Score: 0.40
DE  Interaction: P53316; IntAct: EBI-2345805; Score: 0.37
DE  Interaction: P25303; IntAct: EBI-3658934; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3702299; Score: 0.35
DE  Interaction: P0CS90; IntAct: EBI-3706035; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3709132; Score: 0.35
DE  Interaction: P39078; IntAct: EBI-3739659; Score: 0.35
DE  Interaction: P12612; IntAct: EBI-3740499; Score: 0.35
DE  Interaction: P39076; IntAct: EBI-3740987; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3750519; Score: 0.35
DE  Interaction: P40971; IntAct: EBI-16294329; Score: 0.00
GO  GO:0000243;
GO  GO:0005845;
GO  GO:0005846;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000339;
GO  GO:0031124;
GO  GO:0045292;
GO  GO:0006406;
GO  GO:0000398;
GO  GO:0042789;
GO  GO:0000956;
GO  GO:0000184;
GO  GO:0031053;
GO  GO:0006970;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLEEFDEVKYDHSTKRLDTPSRYLLRKARRNPNGLQELRESMKSSTIYVGNLSFYTSEEQIYELFSKCGTIKRIIMGLD
SQ  RFKFTPCGFCFIIYSCPDEALNALKYLSDTKLDEKTITIDLDPGFEDGRQFGRGKSGGQVSDELRFDFDASRGGFAIPFA
SQ  ERVGVPHSRFDNSSSQSNTNNYIPPPDAMGTFRPGFDEEREDDNYVPQ
//
ID  Q2V8Y7;
PN  Neuronal calcium sensor 1;
GN  NCS1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250|UniProtKB:P62166}. Postsynaptic density {ECO:0000250|UniProtKB:P62166}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62166}. Cytoplasm {ECO:0000250|UniProtKB:P62168}. Cell membrane {ECO:0000250|UniProtKB:P62166}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62166}. Membrane {ECO:0000250|UniProtKB:P62168}; Lipid-anchor {ECO:0000250|UniProtKB:P62166}. Note=Associated with Golgi stacks. Post-synaptic densities of dendrites, and in the pre-synaptic nerve terminal at neuromuscular junctions. {ECO:0000250|UniProtKB:P62166}.
DR  UNIPROT: Q2V8Y7;
DR  Pfam: PF00036;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage- gated calcium channel (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0005509;
GO  GO:0008048;
GO  GO:0005245;
GO  GO:0010975;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P62166};
SQ  MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRI
SQ  EFSEFIQALSVTSRGTLDEKLRWASKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNA
SQ  DGKLTLQEFQEGTKADPSIVQALSLYDGLV
//
ID  P62167;
PN  Neuronal calcium sensor 1;
GN  NCS1;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250|UniProtKB:P62166}. Postsynaptic density {ECO:0000250|UniProtKB:P62166}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62166}. Cytoplasm {ECO:0000250|UniProtKB:P62168}. Cell membrane {ECO:0000250|UniProtKB:P62166}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62166}. Membrane {ECO:0000250|UniProtKB:P62168}; Lipid-anchor {ECO:0000250|UniProtKB:P62166}. Note=Associated with Golgi stacks. Post-synaptic densities of dendrites, and in the pre-synaptic nerve terminal at neuromuscular junctions. {ECO:0000250|UniProtKB:P62166}.
DR  UNIPROT: P62167;
DR  UNIPROT: P36610;
DR  UNIPROT: Q9UK26;
DR  Pfam: PF00036;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0005509;
GO  GO:0008048;
GO  GO:0005245;
GO  GO:0010975;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRI
SQ  EFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNA
SQ  DGKLTLQEFQEGSKADPSIVQALSLYDGLV
//
ID  P62166;
PN  Neuronal calcium sensor 1;
GN  NCS1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:17555535}. Postsynaptic density {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11092894, ECO:0000269|PubMed:17555535}. Cytoplasm {ECO:0000250|UniProtKB:P62168}. Cell membrane {ECO:0000269|PubMed:17555535}; Peripheral membrane protein. Membrane {ECO:0000250|UniProtKB:P62168}; Lipid-anchor {ECO:0000305}. Note=Associated with Golgi stacks. Post-synaptic densities of dendrites, and in the pre-synaptic nerve terminal at neuromuscular junctions. {ECO:0000305, ECO:0000305|PubMed:17555535}.
DR  UNIPROT: P62166;
DR  UNIPROT: E9PAY3;
DR  UNIPROT: P36610;
DR  UNIPROT: Q9UK26;
DR  PDB: 1G8I;
DR  PDB: 2LCP;
DR  PDB: 4GUK;
DR  PDB: 5O9S;
DR  PDB: 6QI4;
DR  Pfam: PF00036;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 603315;
DR  DisGeNET: 23413;
DE  Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage- gated calcium channel (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q86UW9; IntAct: EBI-755530; Score: 0.83
DE  Interaction: P41271; IntAct: EBI-10208658; Score: 0.56
DE  Interaction: Q96ST8; IntAct: EBI-24577721; Score: 0.60
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9UKN5; IntAct: EBI-24326300; Score: 0.56
DE  Interaction: P78358; IntAct: EBI-24337955; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-25256722; Score: 0.56
DE  Interaction: Q9Y336; IntAct: EBI-24516320; Score: 0.56
DE  Interaction: Q7Z698; IntAct: EBI-24527170; Score: 0.56
DE  Interaction: Q96K80; IntAct: EBI-24610735; Score: 0.56
DE  Interaction: Q96C03; IntAct: EBI-24615464; Score: 0.56
DE  Interaction: O75084; IntAct: EBI-24627494; Score: 0.56
DE  Interaction: Q8IWL1; IntAct: EBI-23737805; Score: 0.56
DE  Interaction: O95868; IntAct: EBI-23779627; Score: 0.56
DE  Interaction: Q9BXJ5; IntAct: EBI-24732079; Score: 0.56
DE  Interaction: Q03060; IntAct: EBI-23799744; Score: 0.56
DE  Interaction: P10451; IntAct: EBI-24756404; Score: 0.56
DE  Interaction: O60930; IntAct: EBI-24784574; Score: 0.56
DE  Interaction: Q8TDS5; IntAct: EBI-24635892; Score: 0.56
DE  Interaction: A0A1U9X8X8; IntAct: EBI-25196535; Score: 0.56
DE  Interaction: P05362; IntAct: EBI-21568860; Score: 0.35
DE  Interaction: Q8N5S1; IntAct: EBI-21587332; Score: 0.35
DE  Interaction: Q8NFB2; IntAct: EBI-21757603; Score: 0.35
DE  Interaction: Q9UPU5; IntAct: EBI-21775610; Score: 0.35
DE  Interaction: Q9BV23; IntAct: EBI-21775610; Score: 0.35
DE  Interaction: Q5W0U4; IntAct: EBI-21775610; Score: 0.35
DE  Interaction: P30419; IntAct: EBI-21775610; Score: 0.35
DE  Interaction: P04183; IntAct: EBI-21775610; Score: 0.35
DE  Interaction: O75175; IntAct: EBI-21775610; Score: 0.35
DE  Interaction: O60551; IntAct: EBI-21775610; Score: 0.35
DE  Interaction: P37058; IntAct: EBI-21840509; Score: 0.35
DE  Interaction: P08637; IntAct: EBI-21864671; Score: 0.35
DE  Interaction: Q12933; IntAct: EBI-20736875; Score: 0.35
DE  Interaction: Q9BYM8; IntAct: EBI-20737060; Score: 0.35
DE  Interaction: Q9H0F6; IntAct: EBI-20737150; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: Q8NFZ5; IntAct: EBI-20738016; Score: 0.35
DE  Interaction: P21554; IntAct: EBI-21458304; Score: 0.38
DE  Interaction: Q9BXU9; IntAct: EBI-21458640; Score: 0.27
DE  Interaction: P80192; IntAct: EBI-28938802; Score: 0.35
DE  Interaction: Q5TCX8; IntAct: EBI-28941668; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0005509;
GO  GO:0008048;
GO  GO:0005245;
GO  GO:0010975;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:25255805};
SQ  MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRI
SQ  EFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNA
SQ  DGKLTLQEFQEGSKADPSIVQALSLYDGLV
//
ID  Q8BNY6;
PN  Neuronal calcium sensor 1;
GN  Ncs1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250|UniProtKB:P62166}. Postsynaptic density {ECO:0000250|UniProtKB:P62166}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62166}. Cytoplasm {ECO:0000250|UniProtKB:P62168}. Cell membrane {ECO:0000250|UniProtKB:P62166}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62166}. Membrane {ECO:0000250|UniProtKB:P62166, ECO:0000250|UniProtKB:P62168}; Lipid-anchor {ECO:0000250|UniProtKB:P62166}. Note=Associated with Golgi stacks. Post-synaptic densities of dendrites, and in the pre-synaptic nerve terminal at neuromuscular junctions. {ECO:0000250|UniProtKB:P62166}.
DR  UNIPROT: Q8BNY6;
DR  UNIPROT: A2AJ84;
DR  Pfam: PF00036;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage- gated calcium channel (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P11881; IntAct: EBI-15612731; Score: 0.40
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: P47746; IntAct: EBI-21458724; Score: 0.27
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0044305;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0031045;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0099524;
GO  GO:0014069;
GO  GO:0099523;
GO  GO:0005509;
GO  GO:0008048;
GO  GO:0000287;
GO  GO:0019901;
GO  GO:0005245;
GO  GO:0099626;
GO  GO:0048015;
GO  GO:0045921;
GO  GO:0050806;
GO  GO:0010975;
GO  GO:2000300;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P62166};
SQ  MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRI
SQ  EFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNA
SQ  DGKLTLQEFQEGSKADPSIVQALSLYDGLV
//
ID  Q5RC90;
PN  Neuronal calcium sensor 1;
GN  NCS1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250|UniProtKB:P62166}. Postsynaptic density {ECO:0000250|UniProtKB:P62166}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62166}. Cytoplasm {ECO:0000250|UniProtKB:P62168}. Cell membrane {ECO:0000250|UniProtKB:P62166}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62166}. Membrane {ECO:0000250|UniProtKB:P62166, ECO:0000250|UniProtKB:P62168}; Lipid-anchor {ECO:0000250|UniProtKB:P62166}. Note=Associated with Golgi stacks. Post-synaptic densities of dendrites, and in the pre-synaptic nerve terminal at neuromuscular junctions. {ECO:0000250|UniProtKB:P62166}.
DR  UNIPROT: Q5RC90;
DR  Pfam: PF13405;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage- gated calcium channel (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0005509;
GO  GO:0005245;
GO  GO:0010975;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P62166};
SQ  MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRI
SQ  GFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNA
SQ  DGKLTLQEFQEGSKADPSIVQALSLYDGLV
//
ID  P62168;
PN  Neuronal calcium sensor 1;
GN  Ncs1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:11526106}. Postsynaptic density {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62166}. Cytoplasm {ECO:0000269|PubMed:11526106}. Cell membrane {ECO:0000269|PubMed:11526106}. Membrane {ECO:0000250|UniProtKB:P62166, ECO:0000269|PubMed:10514519}; Lipid-anchor {ECO:0000250|UniProtKB:P62166}. Note=Associated with Golgi stacks. Post-synaptic densities of dendrites, and in the pre-synaptic nerve terminal at neuromuscular junctions. {ECO:0000250|UniProtKB:P62166, ECO:0000269|PubMed:11526106, ECO:0000305}.
DR  UNIPROT: P62168;
DR  UNIPROT: P36610;
DR  UNIPROT: Q9UK26;
DR  PDB: 4OV2;
DR  PDB: 4YRU;
DR  PDB: 5AEQ;
DR  PDB: 5AER;
DR  PDB: 5AFP;
DR  Pfam: PF00036;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin. Stimulates PI4KB kinase activity. Involved in long-term synaptic plasticity through its interaction with PICK1. May also play a role in neuron differentiation through inhibition of the activity of N- type voltage-gated calcium channel. {ECO:0000269|PubMed:17502602}.
DE  Reference Proteome: Yes;
DE  Interaction: P14100; IntAct: EBI-907835; Score: 0.50
DE  Interaction: P84080; IntAct: EBI-907835; Score: 0.50
DE  Interaction: P00829; IntAct: EBI-907835; Score: 0.35
DE  Interaction: Q28115; IntAct: EBI-907835; Score: 0.35
DE  Interaction: P19120; IntAct: EBI-907835; Score: 0.35
DE  Interaction: P20004; IntAct: EBI-907835; Score: 0.35
DE  Interaction: P19483; IntAct: EBI-907835; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0044305;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0099524;
GO  GO:0014069;
GO  GO:0099523;
GO  GO:0005509;
GO  GO:0008048;
GO  GO:0008427;
GO  GO:0000287;
GO  GO:0019901;
GO  GO:0005245;
GO  GO:0099626;
GO  GO:0048015;
GO  GO:0045921;
GO  GO:0010975;
GO  GO:2000300;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10514519};
SQ  MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRI
SQ  EFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNA
SQ  DGKLTLQEFQEGSKADPSIVQALSLYDGLV
//
ID  Q91614;
PN  Neuronal calcium sensor 1;
GN  ncs1;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus {ECO:0000250|UniProtKB:P62166}. Postsynaptic density {ECO:0000250|UniProtKB:P62166}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62166}. Cytoplasm {ECO:0000250|UniProtKB:P62168}. Cell membrane {ECO:0000250|UniProtKB:P62166}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62166}. Membrane {ECO:0000250|UniProtKB:P62168}; Lipid-anchor {ECO:0000250|UniProtKB:P62166}.
DR  UNIPROT: Q91614;
DR  UNIPROT: Q6GQJ0;
DR  Pfam: PF00036;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0005509;
GO  GO:0005245;
GO  GO:0010975;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDATGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRI
SQ  EFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNS
SQ  DGKLTLQEFQEGSKADPSIVQALSLYDGLV
//
ID  Q60M68;
PN  Nucleoporin ndc-1;
GN  npp;
OS  6238;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q60M68;
DR  UNIPROT: A8Y4A5;
DR  UNIPROT: H8WHD0;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0070762;
GO  GO:0030674;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMGENSSAYTTLADNQLYNQFSPSRRKADLIASTSATSSPNLRKSPNRGFSSPRAQQKPITIFDQIVSWFHSEIDVRKKL
SQ  ASFVCGAAVALSFIVTVSILKLSIWAPFSSVQDSLTWWLYPTSWPVTLFIWLSSVAWTFLIIHQFCTVTQVPRIPITDTY
SQ  AWAGAALEFVHRLIFVYTAFTVSESSFFEDFAWIAIAFSVAISSALVIFRSDFHLNFSNVQVNSFKTLIDFAKSLPYGSL
SQ  AETSGVDAAIAYTAAMALTVFGSPLLWGFSAWWLLINIQFHLVLFGVCFAQQFFAKIFMKIVNQIVMKPMKFPFPPPYTV
SQ  HSPTPDQIRTLPNVIETDDPLLKMFALHDLRTVAWEDEKRRVDVFSLSQPGKHPRNWKAVSMPCTRMLDELCSRMTVSAA
SQ  RLVGYSWDDHDVENEEVPRDALMMPRKMREMTYRGAGQSRQQKTIAPIRSNNTQTVGFLAKITRNLGLGKTERLVISRFD
SQ  AQQNAYAAEAVYMLVVDSMGEDRFGVVQKDLKDLITLLCKLIAAIDTYERAKASVADKSDVTYLRLVDASLKSCLQRVVT
SQ  TFGSHLRSLELADEHIRTIKLVCAEEI
//
ID  Q8I4N3;
PN  Nucleoporin ndc-1;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q8I4N3;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P91001; IntAct: EBI-6460861; Score: 0.37
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0030674;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMGDSHSSFTTTTDEHLYNQFSPGRRKNDFPAASSSSSSPNLRRSPNRTVSSPRVQQKPITIFDQIVDWFQAEISVRKRL
SQ  AGAACGYLSTIFFIVTVSILKLTIWAPFSSVQDSLAWWIYPNAWASIIFVGIASVAMSLFSIIKFCKVDQLPRLAATDTF
SQ  ALAGVALEFVTRLTFVYTAFCVADFSFSREFAFVAISLAIAISSALVVFRSDYQLNFSHIQVNSVKTLIDFGTSLPYANI
SQ  SEICGIDAAISYTAAVALILVVGPMVSGFSAWWLLLNIPFHVVLFGLCFTQQFYSKISMKIVNQIVMKPISFPFPPPYTV
SQ  HSPTPEQTRTLPNVIETDDSLLKFFALHDLRTIAWNDEKRRVDVFSLSQPGKHPRNWKAVSLPCVRMLDELCSRMTVSAA
SQ  RLVGYSWDDHDIENEDVPRDALLMPRKMREMAYRGTGQSRQQKSMAPIRSHNTQTVGLLSKISNFLGFGVTEKLVISRFD
SQ  AHMNAYAAEALYMLVVDSMGEDRFGVVQKDLKDLITLLCKLIAAIDTYERAKASVADKSDVTFLRIVDASLKSSLQRVVT
SQ  TFGSHLSSLNLPEEHSRTIRMICLTDEL
//
ID  G0S235;
PN  Nucleoporin NDC1;
GN  NDC1;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P32500}. Nucleus membrane; Multi-pass membrane protein {ECO:0000255}. Note=Central core structure of the nuclear pore complex. {ECO:0000250|UniProtKB:P32500}.
DR  UNIPROT: G0S235;
DR  UNIPROT: G0ZGV7;
DR  Pfam: PF09531;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB), probably by playing a key role in de novo assembly and insertion of both structures in the nuclear envelope. NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000250|UniProtKB:P32500}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAAVRRSPYKDFLQPALQRRFATATLVVLATAYFEALLLARWSSWLWSWFPLGPTGFRAALFFLCGIFVIILRISQYHP
SQ  GIRTSDSPIATLVRYAPRWTTFETLFTYALSAWIFSLVYLGTVPDDAGFERITYFTYDRARLNEKPIFLTTHLVLLGIYQ
SQ  GVRHLYSDIDRLSLGTAQPSNGDSSKATGEDGHVSTQMRRFRDQLPKIVVHSLHQSVMGLLLSASLYPLLLRDLLWRVNM
SQ  TMLRPLYSLPRTNVPPANLPYSPSTLLRCLAASVMVMFAWTAANTAFSLLLVKSPLKNGKPLTADAKDPNGSLLNGLKNK
SQ  KLSIKCFAMWELAYIARDFPDRRKAIFEDMDRKDGPMWSQVYKICLDTLHTLSSNIDAYTAPPAPATTPQQAETALGDKP
SQ  RTSAPPKEDHIFAPLPSNKSAFRTSVSSAFQNAALAGPGGPPASLSPVAKRTLHAARSRLLEAAAPNAEIEVTPSSFFRE
SQ  LALKYVLSSPLAGYPFRQTRRRRLASAVLGSPYGEPSLYVNAASAVSGLAVSSLREDRYGHVQRDVASLIRELTSLGEKL
SQ  NAFVNEGGMGKHWTDVVELEGEDKCEEVEEVVNAVKHALKRVIVAFEPYARDLRLTRGEVKKAREVAGLEQEVEVREVMP
SQ  EMVQIR
//
ID  Q7SZC5;
PN  Nucleoporin NDC1;
GN  ndc1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q7SZC5;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0070762;
GO  GO:0030674;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFSMKQNCWFIRKVVIWRAVASIAWSVLLLPITTAVFVLLSRFSLFHPIQWISDCTNLLTASSTIFSLMVLCAVVLITGF
SQ  FNLEFYTLVPSIPCSRVALLGTVLHPLQCVHSLVYSSMGMLVMWCASVIISGRYSTLGTPCMQNESGDVLTCLNEYHLFL
SQ  LLAGAFMGYSHSFLGVVKNMYYVSFQPIQQYKYPQFKGCLPMLLKCSVIQSLYSTRNFAALYFFFGYVPRAWISSTLNLP
SQ  IDSSLQPLDSLTGLLDFSLLYHLSISGTFLYFTWYLTVLIFRIYATEAYSFPVQSTFSEDAERCLPKVVGEKSTLVMKFL
SQ  ALQDLALLSQHSPSRRQEVFSLSQPGGHPHNWNAISGECLCLLRDLTQRLVAHQDAVASNGRVKSQSASSDTRSASSSSS
SQ  VLSGMEDVPETPRPTVPLRTPGSVFKSSVGGMHSSLTAPFTPDVDSPFCSPAIRRLVGQQDPQSPWFGTVQSPHIMRRGP
SQ  KLWSASTESQSNGSPPASPAIAPSPPAANKKPSFLAQWLQNRKEQVKSFLAKRVLIVYLFNKLPEASSQALFADSQAHIW
SQ  ALQGLSHLVAASFSEDQFGVVQTTLPSILSSLVVLLEAVDRHFKLPHASSKPARTVCSMGDSTYKTLRFALRAALKTAIY
SQ  KITTTFGEHLNAVNISTEHRKRLQQFLEFKE
//
ID  Q9VCG4;
PN  Nucleoporin Ndc1;
GN  Ndc1;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q9VCG4;
DR  UNIPROT: Q3YE69;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VNU3; IntAct: EBI-214976; Score: 0.00
DE  Interaction: Q9VG03; IntAct: EBI-217023; Score: 0.00
DE  Interaction: Q9VWG6; IntAct: EBI-235239; Score: 0.00
DE  Interaction: Q9V564; IntAct: EBI-256452; Score: 0.00
DE  Interaction: Q9VTP5; IntAct: EBI-279434; Score: 0.00
DE  Interaction: O61307; IntAct: EBI-9921261; Score: 0.35
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0030674;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0006999;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSASSSSNACKLLLLGRCLRAVLLSVAIQFLLLTVFLLFVNFQLLHPLAWVTGTLRLVASWYTWFASIPLVASVVLYGVI
SQ  LCQQHLSERRYCPTRYRWLLHYGPRKVLFLFAHLLVGLLTAWLYTGYLHTDYQHLKYKCYGQDCISAYNVYLLGIGMTAG
SQ  CYYFVSVHMRKEISIEFPIVEQSRAEKMRELLYASLAKSLLSSLLPTISYTAVFCLFGPMVCHRLSHILSVDMDERLDGF
SQ  FGVVTNVRLLFYGYLLTAQILSNMHLMRCFYGILLSEDLPLVVTKPRAAFAHEQDITLVAGLGVFNVYVVQCLAAHHFYK
SQ  LALRKNSPQRAEIFQLTEPGNRPASWRSLCDQCLSILGSFTEELTESMQKISILKCAQSLPMPKITESLTTSLMAEKVLL
SQ  RQYNQKHGIRPIVSPSREVAVESPADGIRHFPNWCERVSTQLEQSLQRLLQRVPGIVYLFNEPEGAKTTFLLANSLPVVY
SQ  MTQALAQVCAASLKEDPYGVVQNDLPAIIKAINKLRNELDKLSSVIGNIRISSSSFNVLRCAVRRSLYAICLSFCDYLDD
SQ  LLPPGEELRQLQDLVCQE
//
ID  Q298S5;
PN  Nucleoporin Ndc1;
GN  Ndc1;
OS  46245;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q298S5;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSHLSTINACKLLLFRRCLQAVLLTVGIQFLLLTIFLLFVNFQLLRPLHWISVTLSLVCSMYTWFASIPLVGAVVLYGMI
SQ  LCQQHLAERLYCPTRFRWLVHYAPRKLLFLAAHLLVGYLTAWLYTGYMHTDYRHLWYKCYDQECISAYHVYLLGMGIFAG
SQ  CYYFVSVHMRQEVEIEFPIVNHLWGEKLREVLYSSLARSLIKSLLPTLAYTLLFWLFGGVVCHKLSHIFAVDLDERLEGF
SQ  FGVATNGRLLFYGWLLTSQILSNMHLMRCFYSMFLSEEFPLAITKNRAAFVQEKEVTVVAALGLSNVYVVQCLAAKYLYN
SQ  LVTAGDAEKRSELFQLTEPGNRPANWRSLCDQCLSLFGNFTDELIDSMQKISVLKGSPSSPPLTPISENASASLMAERVL
SQ  TRQYNQMHGIRAIVSPRSNAVIDRPVDRIHRVPDWCERTSMQLEQSLQLLINRIPGIVYMFTEPEGAKTAFLLTHSLPLV
SQ  FVIQALSQICVFSLKEDRYGVVQTDLPDIIRSMSRLKGELDKLSSVASNLRGPGSSFSVLRGAVRRSLFHICVAFGEYLS
SQ  ELIPSGEELHQLQTVINQE
//
ID  Q9BTX1;
PN  Nucleoporin NDC1;
GN  NDC1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Note=Central core structure of the nuclear pore complex.
DR  UNIPROT: Q9BTX1;
DR  UNIPROT: B4DHA3;
DR  UNIPROT: B4DQQ5;
DR  UNIPROT: G3XA81;
DR  UNIPROT: Q8NB76;
DR  UNIPROT: Q9H9T6;
DR  UNIPROT: Q9NSG3;
DR  UNIPROT: Q9NSG4;
DR  UNIPROT: Q9NVZ7;
DR  Pfam: PF09531;
DR  OMIM: 610115;
DR  DisGeNET: 55706;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane. {ECO:0000269|PubMed:16600873, ECO:0000269|PubMed:16702233}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8VCB1; IntAct: EBI-2560113; Score: 0.40
DE  Interaction: Q8WTR4; IntAct: EBI-21566764; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q8IYM1; IntAct: EBI-10819461; Score: 0.37
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11389870; Score: 0.27
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: O00322; IntAct: EBI-21504674; Score: 0.35
DE  Interaction: P30825; IntAct: EBI-21505748; Score: 0.35
DE  Interaction: Q86UE6; IntAct: EBI-21507777; Score: 0.35
DE  Interaction: Q9H8X2; IntAct: EBI-21509881; Score: 0.35
DE  Interaction: Q9Y282; IntAct: EBI-21510632; Score: 0.35
DE  Interaction: P16444; IntAct: EBI-21514808; Score: 0.35
DE  Interaction: Q16581; IntAct: EBI-21515265; Score: 0.35
DE  Interaction: Q6P5W5; IntAct: EBI-21515976; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-21559824; Score: 0.35
DE  Interaction: Q8WWF5; IntAct: EBI-21589535; Score: 0.35
DE  Interaction: P62079; IntAct: EBI-21619035; Score: 0.35
DE  Interaction: Q6UWB1; IntAct: EBI-21703330; Score: 0.35
DE  Interaction: P08754; IntAct: EBI-21709056; Score: 0.35
DE  Interaction: P28908; IntAct: EBI-21750180; Score: 0.35
DE  Interaction: Q9UQC9; IntAct: EBI-21899358; Score: 0.40
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: E7ELX2; IntAct: EBI-20625922; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21272198; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0F6B5H5; IntAct: EBI-27033770; Score: 0.35
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055718; Score: 0.42
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: O15146; IntAct: EBI-32724025; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
GO  GO:0015629;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0005886;
GO  GO:0030674;
GO  GO:0017056;
GO  GO:0007129;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0051664;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATAVSRPCAGRSRDILWRVLGWRIVASIVWSVLFLPICTTVFIIFSRIDLFHPIQWLSDSFSDLYSSYVIFYFLLLSVV
SQ  IIIISIFNVEFYAVVPSIPCSRLALIGKIIHPQQLMHSFIHAAMGMVMAWCAAVITQGQYSFLVVPCTGTNSFGSPAAQT
SQ  CLNEYHLFFLLTGAFMGYSYSLLYFVNNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFLVRNFCILYYFLGYIPKA
SQ  WISTAMNLHIDEQVHRPLDTVSGLLNLSLLYHVWLCGVFLLTTWYVSWILFKIYATEAHVFPVQPPFAEGSDECLPKVLN
SQ  SNPPPIIKYLALQDLMLLSQYSPSRRQEVFSLSQPGGHPHNWTAISRECLNLLNGMTQKLILYQEAAATNGRVSSSYPVE
SQ  PKKLNSPEETAFQTPKSSQMPRPSVPPLVKTSLFSSKLSTPDVVSPFGTPFGSSVMNRMAGIFDVNTCYGSPQSPQLIRR
SQ  GPRLWTSASDQQMTEFSNPSPSTSISAEGKTMRQPSVIYSWIQNKREQIKNFLSKRVLIMYFFSKHPEASIQAVFSDAQM
SQ  HIWALEGLSHLVAASFTEDRFGVVQTTLPAILNTLLTLQEAVDKYFKLPHASSKPPRISGSLVDTSYKTLRFAFRASLKT
SQ  AIYRITTTFGEHLNAVQASAEHQKRLQQFLEFKE
//
ID  Q8VCB1;
PN  Nucleoporin NDC1;
GN  Ndc1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q8VCB1;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9BTX1; IntAct: EBI-2560113; Score: 0.40
GO  GO:0015629;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0005886;
GO  GO:0030674;
GO  GO:0017056;
GO  GO:0007129;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0051664;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATAASGPCAGGSPRDILWRVLGWRIVTSIVWSVVLLPVCITAFIVLSSINLFHPIQWLSDSCNDFYSSQVIFHLLLLAV
SQ  VIIIISIFNVEFYTVVPSISGSRLALIARILHPQQLTHSFIHAAMGMAVAWCAAIMTKGQYSSLVVPCTGTESLDSPAAQ
SQ  TCLNEYHLFFLLSGAFMGYSYSLLYFINNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFMVRNFCIVYYFFGHIPK
SQ  AWISTALDLHTDEQAHRPLDTIGGLLNVSLLYHVWLCGVFLLVTWYSSWILFKIYATEAHVFPVQPPFAEASDECLPKVL
SQ  NSNPPRIVKYLALQDLMLLSQYSPSRRQEVFSLSQPGGHPHNWTAISRECLNLLNDMTQKLVLYQEAAATNGRMYSSYSV
SQ  EPKKLSSAEETAFQTPKPSQTPSVPPLVKTSLFSPKLSTPNVSSPFGTPFGSSVVNRMAGILDVNPFSGSPQSPQLIRRG
SQ  PRLWTHTSDQQVSAISNPSPCASVTAEGKTVRQPSVIYSWIQNKREQIKNFLSKRVLIMYFFSKHPEASIQAVFSDAQMH
SQ  IWALEGLSHLVAASFTEDRFGVVQTTLPAILHTLLTLQEAVDKYFKLPHASSKPPRASGSLVDTSYKTLRFAFRASLKTA
SQ  IYRITTTFGEHLNAVQASAEHQKRLQQFLEFKE
//
ID  Q5RBY5;
PN  Nucleoporin NDC1;
GN  NDC1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q5RBY5;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATAVSGPCAGRSRDILWRVLGWRIVASIIWSVLLLPICTTVFIIFSRIDLFHPIQWLSDSFSDLYSSYVIFYLLLLSVV
SQ  IIIISIFNVEFYAVVPSIPCSRLALIGKIIHPQQLMHSFIHAAMGMVMAWCAAVITQGQYSFLVVPCTGANSFGSPAAQT
SQ  CLNEYHLFFLLAGALMGYSYSLLYFVNNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFLVRNFCILYYFLGYIPKA
SQ  WISTAMNLHIDEQVHRPLDTVSGLLNLSLLYHVWLCGAFLLTTWYVSWILFKIYATEAHVFPVQPPFAEGSDECLPKVLN
SQ  SNPPPIIKYLALQDLMLFSQYSPSRRQEVFSLSQPGGHPHNWTAISRECLNLLNGMTQKLVLYQEAAATNGRVSSSYPVE
SQ  PKKLNSPEETTFQTPKSSQMPRPSVPPLVKTSLFSSKLSTPEVVSPFGTPFGSSVMNRMAGIFDVNTCFGSPQSPQLIRR
SQ  GPRLWTSASDQQMTEFSNPSPSTSISAEGKTMRQPSVIYSWIQNKREQIKNFLSKRVLIMYFFSKHPEASIQAVFSDAQM
SQ  HIWALEGLSHLVAASFTEDRFGVVQTTLPAILNTLLTLQEAVDKYFKLPHASSKPPRISGSLVDTSYKTLRFAFRASLKT
SQ  AIYRITTTFGEHLNAVQASAEHQKRLQQFLEFKE
//
ID  Q6AXN4;
PN  Nucleoporin NDC1;
GN  Ndc1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
DR  UNIPROT: Q6AXN4;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0030674;
GO  GO:0017056;
GO  GO:0007129;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0051664;
GO  GO:0006999;
GO  GO:0015031;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATAASGPCAGGSPRDILWRVLGWRIVTSVVWSVLLLPVCITAFIVFSSIDLFHPIQWLSDSLNEFYSSQVIFYLLLLAV
SQ  VIIIISIFNVEFYTVVPSIPGSRLALIARILHPQQLTHSFIHAVMGMAVAWCAAIMTKGQSRSLVVPCTGTESLDSPAAQ
SQ  TCMNEYHLFFLLSGAFMGYSYSLLYFINNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFMVRNFCIVYYFFGHIPK
SQ  AWISTALDLRTDEQAHRPLDTIGGLLNVSLLYHVWLCGVFLLMTWYISWILFKIYATEAYMFPVQPPFAEESDECLPKVL
SQ  NSNPPLIIKYLALQDLMLLSQYSPSRRQEVFSLSQPGGHPHNWTAISRECLSLLNDMTQKLVLYQEAAATNGRMYSSYSV
SQ  EPKRLSSPEETAFQTPKPSQMPSVPPLVKTSLFSPKLSTPDGSSPFGTPFGSSVVNRMAGIFDVNTCCGSPQSPQLVRRG
SQ  PRLWTHTSDQQVSAVSNPSPCASVTAEGKTVRQPSVLYSWIQNKREQIKNFLSKRVLIMYFFSKHPEASIQAVFSDAQMH
SQ  IWALEGLSHLVAASFTEDRFGVVQTTLPAILNTLLTLQEAVDKYFKLPHASSKPPRTSGSLVDTSYKTLRFAFRASLKTA
SQ  IYRITTTFGEHLNAVQASAEHQKRLQQFLEFKE
//
ID  O13961;
PN  Nuclear envelope protein ndc1;
GN  cut11;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Central core structure of the nuclear pore complex.
DR  UNIPROT: O13961;
DR  UNIPROT: Q9UTH4;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC) and the spindle pole body (SPB), which plays a key role in de novo assembly and insertion of both structures in the nuclear envelope. Involved in the formation of the bipolar mitotic spindle. Anchors the spindle pole body in the nuclear envelope. {ECO:0000269|PubMed:9763447}.
DE  Reference Proteome: Yes;
DE  Interaction: P04689; IntAct: EBI-7633541; Score: 0.27
DE  Interaction: O94385; IntAct: EBI-7633650; Score: 0.27
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0140512;
GO  GO:0140599;
GO  GO:0044732;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0005816;
GO  GO:0030674;
GO  GO:0106166;
GO  GO:1903087;
GO  GO:0140480;
GO  GO:1990608;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0015031;
GO  GO:0070631;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVMLRTSFPSGSRTKAVRYHTLLRPILQQRFLRACFALLCLCCITSYWFSSGPFISLSFWFLSLVRGFVCFFFMFPYFVM
SQ  LKSRMSTQKVTKQSLGAQLFYDFSPKSFFLVYLTFAVSVSCLCLFYIKGHASSIRLQWIASPNAYELPSLNERFVYMTYF
SQ  SHILILALTVEHLYLQRDSPSRPVINVSFFNYIFQNLGWLIRFSFRKSIICCLFTPFSYAILRSYIWRFAALLTSCCRRI
SQ  AYTKTPPKWPLSLRLLLHSFWMAFIVCLTFQIALLIFRVFLYSGPMIRGKLLSARSNDPNGTLVDGMKTKKKPLTECIAT
SQ  EELWFIAKRDPQRIKSIFQDIDRSVSIWQELYSITESRCKELATSLKILQSTGDFSAATSKKSGLTKKTNIPYSPNSNHE
SQ  EINSIPLRNKNIFVPPSQGHSPLLEKIKKQGSLPSTTPVNEGGISDIIPKSLYDQVIRFISTFYKAPVFGIFRKTLRRQN
SQ  EALLPNPWLFCVTVNSLTQLVLKSLKYDTYGVVARDISSILAVYCDTFDVLVSYKRSLVKNHSNSTNLDDDFKNLNSAAN
SQ  ALHCGIIDITEKFQDFFTQLNLSPRIERRCWVLFREYKSNS
//
ID  Q6AX31;
PN  Nucleoporin NDC1;
GN  ndc1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:16600873}. Nucleus membrane {ECO:0000269|PubMed:16600873}; Multi-pass membrane protein {ECO:0000269|PubMed:16600873}. Note=Central core structure of the nuclear pore complex.
DR  UNIPROT: Q6AX31;
DR  PDB: 7WKK;
DR  Pfam: PF09531;
DE  Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane. {ECO:0000269|PubMed:16600873}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTMLGERLVLRWRVAASFAWSVILMPVCCALFIVLSRIQILHPIQWLTDSISDLTSSYTIFCLLLICAILGLQCTFLMEY
SQ  YTVVPSIPCSRLALIGNLLLPHRILHSLAHVAMGVLASWCYAVLSKGKYQLLVVSCTLQSEDEADKPSHCLNESHLFQLL
SQ  CGAFFGYSYSLQYFVHNMNYLSFPSIQQYKYLQFRRFLPLIIKQSVFQSLYFIRSYAILYFCLGNIPRTWIQTALNLHMD
SQ  RQQPSLDTLRGFLNLSLFYQIWLSGTFLLATWYMVWILFRIYTTEARIFPVQTSFAEEAEKCLPFILNSNTLPLVKYLAM
SQ  QDLVLLSQYSPSRRQEVFSLSQPGGHPHNWTSISKECLNLMSSLTSRLIAHQEAAANNGRMRVPSSPKQIRKSSSSSGTS
SQ  LIEDSAEQTQNLSTIPRIGIPSLLKTASLKSSLDIGSPFATPGVKQMSESLDPNTPCHGSVQSPQVTRRGAKLWTSDSDV
SQ  QKNGSEVSPVMHRPVCNGAKQGILHTWFQHKLVQIKNVLSKRGLIMYLFSKHPEASSQDVFADAQIHIWALEALSHLVAA
SQ  SFSEDRMGVVQTSLSSVLAILLTLQEAVEKHFKLPHASSKPARNPGSLLDSSCKTLRFSLRAALKTAIYRITTTFGEHLH
SQ  AVPVSSEHKKKLQQFLDFKE
//
ID  P32500;
PN  Nucleoporin NDC1;
GN  NDC1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Central core structure of the nuclear pore complex. Spindle pole body, central plaque.
DR  UNIPROT: P32500;
DR  UNIPROT: D6VZE3;
DR  Pfam: PF09531;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB), probably by playing a key role in de novo assembly and insertion of both structures in the nuclear envelope. In SPB duplication NDC1 is required for the insertion of the cytoplasmic side of the SPB in the nuclear envelope, thus allowing for the assembly of the nucleoplasmic SPB side. NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11352933, ECO:0000269|PubMed:15075274, ECO:0000269|PubMed:9864355}.
DE  Reference Proteome: Yes;
DE  Interaction: Q05166; IntAct: EBI-390807; Score: 0.67
DE  Interaction: Q03790; IntAct: EBI-390810; Score: 0.55
DE  Interaction: P09232; IntAct: EBI-390993; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: P16521; IntAct: EBI-799689; Score: 0.35
DE  Interaction: P38219; IntAct: EBI-799689; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-799689; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-799689; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-799689; Score: 0.35
DE  Interaction: P46654; IntAct: EBI-799689; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-799689; Score: 0.35
DE  Interaction: P14742; IntAct: EBI-799689; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-799689; Score: 0.35
DE  Interaction: Q05021; IntAct: EBI-7777027; Score: 0.40
DE  Interaction: P48559; IntAct: EBI-7887840; Score: 0.40
DE  Interaction: P41817; IntAct: EBI-7987828; Score: 0.44
DE  Interaction: P06197; IntAct: EBI-6314298; Score: 0.00
DE  Interaction: P32500; IntAct: EBI-6322556; Score: 0.00
DE  Interaction: P34077; IntAct: EBI-6322567; Score: 0.00
DE  Interaction: P53337; IntAct: EBI-6322578; Score: 0.00
DE  Interaction: Q06144; IntAct: EBI-6322600; Score: 0.00
DE  Interaction: P52919; IntAct: EBI-2132952; Score: 0.48
DE  Interaction: Q07457; IntAct: EBI-2882288; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: Q12315; IntAct: EBI-11888204; Score: 0.37
DE  Interaction: P49687; IntAct: EBI-11888586; Score: 0.37
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0005816;
GO  GO:0030674;
GO  GO:0106166;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0030474;
GO  GO:0070631;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIQTPRELLNPRYTYHTIFSDVCKTRFNHLVTRLFFICSIIQTVVISLLALPHSPLWELALAFIPNILALNLVSLLIIVT
SQ  RKNYMHVKNFGFANSLTFILGQLLSVKFLVYQGVYSMGSILLSFVLGVVFGRGGSGWKPYYKLFIWLVVPTIYNLQHHVT
SQ  DADKLSFNCENFFQAPQDYVLERVKRIMEKSVILSVISMFVLPIFTTVFFSRQKSGLFDSFTNGVLAVTNLLIISCIIFI
SQ  TFEFINIAFDAHMSIGCLHKGKLISNLSSTPMETLLSGLSADKPFTRLTAYQELAYRATSLDPSLRAPIYHSKFRSSSGN
SQ  TWSLILNECLKTIQINNEKVVQYLRSVQDLGGSATARHKKKVENLDYMYENGKLTSANERLFGNRPSMMAPLRDNGLLDE
SQ  SPNRLRVRTDDSVLLNRGNKKRHRSSYYDNDLDETTQTFNGSIFTHETTFMTAMRLMLKKLKNSIMSFIFPSYAERQSSD
SQ  ESDNYRLLPNGSNKAQISIIDIWSISKKRQAEKLVPLPICHANSVVALTGLLIRSKTEDPKGGIIASVGDILKTLERSIC
SQ  ALGEFADWDPESMAYTAFQTQRTAQDRVQQDSEDEDSMKDTTDMISVLYQLSTSAFMEIVLEYNVALNDVYLDADVAKLA
SQ  NWFLEVYASGNPNAT
//
ID  P22392;
PN  Nucleoside diphosphate kinase B;
GN  NME2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17532299}. Cell projection, lamellipodium {ECO:0000269|PubMed:11919189}. Cell projection, ruffle {ECO:0000269|PubMed:11919189}. Note=Colocalizes with ITGB1 and ITGB1BP1 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen but not on vitronectin or laminin substrates. {ECO:0000269|PubMed:11919189}. [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:16442775}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16442775}. Nucleus {ECO:0000269|PubMed:16442775}. [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:16442775}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16442775}. Nucleus {ECO:0000269|PubMed:16442775}.
DR  UNIPROT: P22392;
DR  UNIPROT: A8MWA3;
DR  UNIPROT: Q1WM23;
DR  UNIPROT: Q6LCT6;
DR  PDB: 1NSK;
DR  PDB: 1NUE;
DR  PDB: 3BBB;
DR  PDB: 3BBC;
DR  PDB: 3BBF;
DR  PDB: 7KPF;
DR  Pfam: PF00334;
DR  PROSITE: PS00469;
DR  OMIM: 156491;
DR  DisGeNET: 4831;
DR  DisGeNET: 654364;
DE  Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Negatively regulates Rho activity by interacting with AKAP13/LBC (PubMed:15249197). Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752, PubMed:19435876). Binds to both single-stranded guanine- and cytosine-rich strands within the nuclease hypersensitive element (NHE) III(1) region of the MYC gene promoter. Does not bind to duplex NHE III(1) (PubMed:19435876). Has G-quadruplex (G4) DNA-binding activity, which is independent of its nucleotide-binding and kinase activity. Binds both folded and unfolded G4 with similar low nanomolar affinities. Stabilizes folded G4s regardless of whether they are prefolded or not (PubMed:25679041). Exhibits histidine protein kinase activity (PubMed:20946858). {ECO:0000250|UniProtKB:P36010, ECO:0000269|PubMed:15249197, ECO:0000269|PubMed:19435876, ECO:0000269|PubMed:20946858, ECO:0000269|PubMed:25679041, ECO:0000269|PubMed:8392752}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13232; IntAct: EBI-21647179; Score: 0.35
DE  Interaction: Q15435; IntAct: EBI-1059661; Score: 0.00
DE  Interaction: P01615; IntAct: EBI-1061143; Score: 0.00
DE  Interaction: P28222; IntAct: EBI-1061406; Score: 0.00
DE  Interaction: Q12972; IntAct: EBI-1064323; Score: 0.00
DE  Interaction: P52434; IntAct: EBI-1071336; Score: 0.00
DE  Interaction: P62807; IntAct: EBI-1075233; Score: 0.00
DE  Interaction: Q9HB71; IntAct: EBI-1075281; Score: 0.00
DE  Interaction: O00264; IntAct: EBI-1075521; Score: 0.00
DE  Interaction: P63173; IntAct: EBI-1075834; Score: 0.00
DE  Interaction: P54819; IntAct: EBI-1076537; Score: 0.00
DE  Interaction: P61088; IntAct: EBI-1076851; Score: 0.00
DE  Interaction: Q9NPH2; IntAct: EBI-1076944; Score: 0.00
DE  Interaction: Q13283; IntAct: EBI-1076964; Score: 0.00
DE  Interaction: Q01105; IntAct: EBI-1077547; Score: 0.00
DE  Interaction: P25787; IntAct: EBI-1077873; Score: 0.00
DE  Interaction: Q9Y3F4; IntAct: EBI-1077889; Score: 0.00
DE  Interaction: P61086; IntAct: EBI-1077953; Score: 0.00
DE  Interaction: P16152; IntAct: EBI-1078617; Score: 0.00
DE  Interaction: P61626; IntAct: EBI-1078976; Score: 0.00
DE  Interaction: P39019; IntAct: EBI-1078996; Score: 0.00
DE  Interaction: Q15084; IntAct: EBI-1079212; Score: 0.00
DE  Interaction: P62249; IntAct: EBI-1079501; Score: 0.00
DE  Interaction: O00232; IntAct: EBI-1079589; Score: 0.00
DE  Interaction: P05455; IntAct: EBI-1080231; Score: 0.00
DE  Interaction: Q9NQC3; IntAct: EBI-1080716; Score: 0.00
DE  Interaction: P30153; IntAct: EBI-1080986; Score: 0.00
DE  Interaction: Q15365; IntAct: EBI-1081301; Score: 0.00
DE  Interaction: P04844; IntAct: EBI-1082016; Score: 0.00
DE  Interaction: P58107; IntAct: EBI-1082068; Score: 0.00
DE  Interaction: P53396; IntAct: EBI-1082405; Score: 0.00
DE  Interaction: O60518; IntAct: EBI-1082514; Score: 0.00
DE  Interaction: Q9Y333; IntAct: EBI-1082666; Score: 0.00
DE  Interaction: P61326; IntAct: EBI-1082762; Score: 0.00
DE  Interaction: Q9Y2L1; IntAct: EBI-1083038; Score: 0.00
DE  Interaction: P31948; IntAct: EBI-1083082; Score: 0.00
DE  Interaction: Q6FHQ0; IntAct: EBI-1083767; Score: 0.00
DE  Interaction: P54725; IntAct: EBI-1084508; Score: 0.00
DE  Interaction: O14818; IntAct: EBI-1084536; Score: 0.00
DE  Interaction: P50502; IntAct: EBI-1084657; Score: 0.00
DE  Interaction: P68402; IntAct: EBI-1084933; Score: 0.00
DE  Interaction: Q14204; IntAct: EBI-1085083; Score: 0.00
DE  Interaction: P28070; IntAct: EBI-1085900; Score: 0.00
DE  Interaction: Q9NZ23; IntAct: EBI-1085916; Score: 0.00
DE  Interaction: Q9Y230; IntAct: EBI-1086002; Score: 0.00
DE  Interaction: Q7L2H7; IntAct: EBI-1086018; Score: 0.00
DE  Interaction: P31939; IntAct: EBI-1086191; Score: 0.00
DE  Interaction: P33176; IntAct: EBI-1086252; Score: 0.00
DE  Interaction: P63104; IntAct: EBI-7192531; Score: 0.40
DE  Interaction: Q00005; IntAct: EBI-2210942; Score: 0.35
DE  Interaction: O14713; IntAct: EBI-2127350; Score: 0.67
DE  Interaction: P15531; IntAct: EBI-2127719; Score: 0.68
DE  Interaction: P62745; IntAct: EBI-2505928; Score: 0.37
DE  Interaction: P68372; IntAct: EBI-2562208; Score: 0.40
DE  Interaction: O46385; IntAct: EBI-7872718; Score: 0.37
DE  Interaction: A0A380PGZ4; IntAct: EBI-2863406; Score: 0.00
DE  Interaction: Q8ZJJ5; IntAct: EBI-2863413; Score: 0.00
DE  Interaction: Q13363; IntAct: EBI-3907897; Score: 0.37
DE  Interaction: P20339; IntAct: EBI-3911907; Score: 0.37
DE  Interaction: Q14161; IntAct: EBI-3932667; Score: 0.37
DE  Interaction: O00746; IntAct: EBI-3932657; Score: 0.55
DE  Interaction: Q7Z465; IntAct: EBI-3942659; Score: 0.37
DE  Interaction: P22392; IntAct: EBI-3943380; Score: 0.37
DE  Interaction: Q8IZL9; IntAct: EBI-6381092; Score: 0.35
DE  Interaction: Q9Y2J4; IntAct: EBI-8797381; Score: 0.35
DE  Interaction: Q00613; IntAct: EBI-9394221; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-11897791; Score: 0.35
DE  Interaction: Q8NI37; IntAct: EBI-14026943; Score: 0.35
DE  Interaction: Q8TCT1; IntAct: EBI-14027014; Score: 0.35
DE  Interaction: Q9H3S7; IntAct: EBI-14027652; Score: 0.35
DE  Interaction: Q76RH1; IntAct: EBI-14063481; Score: 0.40
DE  Interaction: P50570; IntAct: EBI-16110780; Score: 0.52
DE  Interaction: P62753; IntAct: EBI-16799122; Score: 0.35
DE  Interaction: Q96HJ9; IntAct: EBI-21929593; Score: 0.35
DE  Interaction: O00483; IntAct: EBI-21930681; Score: 0.35
DE  Interaction: O75489; IntAct: EBI-21931040; Score: 0.35
DE  Interaction: Q96FC7; IntAct: EBI-21931532; Score: 0.35
DE  Interaction: Q8N3J5; IntAct: EBI-21931555; Score: 0.35
DE  Interaction: Q9H6K4; IntAct: EBI-21931410; Score: 0.35
DE  Interaction: Q9Y3B1; IntAct: EBI-21931754; Score: 0.35
DE  Interaction: O60260; IntAct: EBI-21135687; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q32Q12; IntAct: EBI-25382283; Score: 0.35
DE  Interaction: Q8N264; IntAct: EBI-25408352; Score: 0.35
DE  Interaction: Q9NRY4; IntAct: EBI-25408519; Score: 0.35
DE  Interaction: Q8NF50; IntAct: EBI-25409278; Score: 0.35
DE  Interaction: Q8K337; IntAct: EBI-25409748; Score: 0.35
DE  Interaction: Q8TCU6; IntAct: EBI-25411141; Score: 0.35
DE  Interaction: Q9H3R0; IntAct: EBI-25479978; Score: 0.35
DE  Interaction: P51114; IntAct: EBI-26510919; Score: 0.37
DE  Interaction: O60303; IntAct: EBI-26582514; Score: 0.35
DE  Interaction: P36507; IntAct: EBI-28935019; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-28955760; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: Q05DH4; IntAct: EBI-34574576; Score: 0.27
DE  Interaction: Q5W0V3; IntAct: EBI-34574999; Score: 0.27
GO  GO:0071944;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:1904813;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001726;
GO  GO:0034774;
GO  GO:0005524;
GO  GO:0003677;
GO  GO:0051880;
GO  GO:0019003;
GO  GO:0046872;
GO  GO:0004550;
GO  GO:0004673;
GO  GO:0003713;
GO  GO:0007155;
GO  GO:0006241;
GO  GO:0006183;
GO  GO:0007229;
GO  GO:0043066;
GO  GO:0006165;
GO  GO:0009142;
GO  GO:0045893;
GO  GO:0050679;
GO  GO:0045618;
GO  GO:0045944;
GO  GO:0042981;
GO  GO:0045682;
GO  GO:0006228;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPFFPGLVKYMNSGPVVAMVWEG
SQ  LNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
//
ID  Q1JPJ0;
PN  NADPH-dependent diflavin oxidoreductase 1;
GN  NDOR1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000255|HAMAP- Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}.
DR  UNIPROT: Q1JPJ0;
DR  UNIPROT: G3MXY0;
DR  Pfam: PF00667;
DR  Pfam: PF00258;
DR  Pfam: PF00175;
DR  PROSITE: PS51384;
DR  PROSITE: PS50902;
DE  Function: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of CISD1 and activate this protein implicated in Fe/S cluster repair (By similarity). In vitro can fully activate methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A (By similarity). {ECO:0000250|UniProtKB:Q9UHB4, ECO:0000255|HAMAP- Rule:MF_03178}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0009055;
GO  GO:0050660;
GO  GO:0010181;
GO  GO:0050661;
GO  GO:0003958;
GO  GO:0016491;
GO  GO:0016731;
GO  GO:0016653;
GO  GO:0008219;
GO  GO:0036245;
GO  GO:0016226;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSARLLVLFGSQTGTAQDVSERLGREARRRQLSCRVEELDSYPVVNLINEPLVIFVCATTGQGDPPDNMKSFWRFIFRR
SQ  SLPSTALRQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGSALLPVCLGDDQHELGPDAAIDPWLQDLWEKVLGPHPVP
SQ  LNLDLSPPGVLWPSKFTLQFLKDTPSSGPEELCAAGTDPQGPPSELQPFLAPMVSNQRVTGPSHFQDVRLIEFDISGSGI
SQ  SFAAGDLVLIQPENTASHVQQFCQALGLDPEQHFTLQPREPGVTCPTRLPQPCSVRRLVSQYLDIASVPRRSFFELLACL
SQ  SPHELEREKLWEFGSARGQEELCEYCTRPRRTALEVLCDFPHTAAAVPPDYLLDLLPLIRPRAFSIASSLRAHPSRLQIL
SQ  VAVVQYQTRLREPRRGLCSSWLASLDPAQGPVRVPLWVRSGGLTFPKTPDVPVIMVGPGTGVAPFRAAIQERVAQGETGN
SQ  VLFFGCRRRDQDFYWEAEWEQLQARGCLTLVTAFSREQEQKVYVQHRLRALGPLVWELLDGRGAHFYLAGNAKYMPADVC
SQ  DTLLSIFREEGGLSDPDAAAYLAQLQRTLRFQTETWA
//
ID  Q6PFP6;
PN  NADPH-dependent diflavin oxidoreductase 1;
GN  ndor1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000255|HAMAP- Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}.
DR  UNIPROT: Q6PFP6;
DR  UNIPROT: Q5RL12;
DR  Pfam: PF00667;
DR  Pfam: PF00258;
DR  Pfam: PF00175;
DR  PROSITE: PS51384;
DR  PROSITE: PS50902;
DE  Function: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of ciapin1, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of cisd1 and activate this protein implicated in Fe/S cluster repair. {ECO:0000255|HAMAP-Rule:MF_03178}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0009055;
GO  GO:0050660;
GO  GO:0010181;
GO  GO:0050661;
GO  GO:0003958;
GO  GO:0016491;
GO  GO:0016731;
GO  GO:0016653;
GO  GO:0008219;
GO  GO:0036245;
GO  GO:0016226;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGHTVLVLYGSQTGTAQDTAERIGRQAQRRRLRVKVEALDTYNVVNLISESLVVFVCATTGQGDPPDNMKKFWRFLFRK
SQ  SLPADSLSRLDCAVLGLGDSSYPKFNFVAKKLHKRLLQLGANMLLPVGLADDQHDLGPDGVIDPWLLSFWQKTLSLYPPP
SQ  AGLAPLREEDKLPPRYIFHFLSEVPNKLTEHLQTVDNKSSPTPLRPFPAPLVFNQRVTHTAHFQDVRHIEFDITGSNIEF
SQ  SAGDTVMMRPCNTSEDVEQLCQLLKLDPESYFTLTPTDSSTEVPARLPQPCSIRFLLEHFLDISAVPRRSFFELLATFAT
SQ  DELEQEKLLEFSSAAGQDTLHSYCNRPRRTALEVLTDFPHTTAELSIGRLLDLFPEIQPRSFSIASSLLEHPNRIQILLA
SQ  VVKYKTMLVKPRKGLCSSWLASLDPSKGDVYVPLWVKKGSLKFPQDPESPVIMVGPGTGVAPFRSAIQERVAQGKMANVL
SQ  FFGCRSESKDFYCGSEWQEKVQAGQMILVTAFSRDQEDKVYVQHRVKEQGKLLWDLIAKKNAFFYIAGNAKQMPTSVCDA
SQ  LKAVFQKEGGMSENQAQEMLDGMEKNGRFQSETWS
//
ID  Q9UHB4;
PN  NADPH-dependent diflavin oxidoreductase 1;
GN  NDOR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000255|HAMAP- Rule:MF_03178, ECO:0000269|PubMed:10625700, ECO:0000269|PubMed:12871939}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178, ECO:0000269|PubMed:12871939}.
DR  UNIPROT: Q9UHB4;
DR  UNIPROT: D3YTG6;
DR  UNIPROT: D3YTH9;
DR  UNIPROT: Q5VSG4;
DR  UNIPROT: Q86US9;
DR  UNIPROT: Q96BC6;
DR  PDB: 4H2D;
DR  Pfam: PF00667;
DR  Pfam: PF00258;
DR  Pfam: PF00175;
DR  PROSITE: PS51384;
DR  PROSITE: PS50902;
DR  OMIM: 606073;
DR  DisGeNET: 27158;
DE  Function: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery (PubMed:10625700, PubMed:28648056, PubMed:23596212, PubMed:20802492, PubMed:15900210). Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA machinery (PubMed:28648056, PubMed:23596212, PubMed:20802492). In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins (PubMed:23596212, PubMed:20802492). It can also reduce the [2Fe-2S] cluster of CISD1 and activate this protein implicated in Fe/S cluster repair (PubMed:28648056). In vitro can fully activate methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A (PubMed:12871938). {ECO:0000255|HAMAP-Rule:MF_03178, ECO:0000269|PubMed:10625700, ECO:0000269|PubMed:12871938, ECO:0000269|PubMed:15900210, ECO:0000269|PubMed:20802492, ECO:0000269|PubMed:23596212, ECO:0000269|PubMed:28648056}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6FI81; IntAct: EBI-10249769; Score: 0.84
DE  Interaction: P15884; IntAct: EBI-10321093; Score: 0.67
DE  Interaction: Q5JR59; IntAct: EBI-10321103; Score: 0.67
DE  Interaction: Q5JST6; IntAct: EBI-10321113; Score: 0.56
DE  Interaction: Q9BT92; IntAct: EBI-10321135; Score: 0.78
DE  Interaction: Q9UMX0; IntAct: EBI-24323853; Score: 0.56
DE  Interaction: Q9UHD9; IntAct: EBI-24367687; Score: 0.56
DE  Interaction: P25791; IntAct: EBI-24528524; Score: 0.56
DE  Interaction: P28072; IntAct: EBI-24684590; Score: 0.56
DE  Interaction: Q96N21; IntAct: EBI-24695401; Score: 0.56
DE  Interaction: Q6NX45; IntAct: EBI-24699274; Score: 0.56
DE  Interaction: Q6ZNG0; IntAct: EBI-24722294; Score: 0.56
DE  Interaction: B2RXF5; IntAct: EBI-24540997; Score: 0.56
DE  Interaction: Q8TAP4; IntAct: EBI-23906101; Score: 0.56
DE  Interaction: Q6ZU52; IntAct: EBI-25282111; Score: 0.56
DE  Interaction: Q86UT8; IntAct: EBI-25288817; Score: 0.56
DE  Interaction: O95995; IntAct: EBI-24394954; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-24398378; Score: 0.56
DE  Interaction: Q15742; IntAct: EBI-24399846; Score: 0.56
DE  Interaction: P14652; IntAct: EBI-24401557; Score: 0.56
DE  Interaction: Q13227; IntAct: EBI-24459411; Score: 0.56
DE  Interaction: P50221; IntAct: EBI-24471396; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-24591651; Score: 0.56
DE  Interaction: Q9UBE8; IntAct: EBI-24799487; Score: 0.56
DE  Interaction: Q53FD0; IntAct: EBI-25269225; Score: 0.56
DE  Interaction: Q8N5R6; IntAct: EBI-22120931; Score: 0.37
DE  Interaction: Q9H3K6; IntAct: EBI-27033149; Score: 0.40
DE  Interaction: O76003; IntAct: EBI-27033155; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0045111;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0009055;
GO  GO:0071949;
GO  GO:0050660;
GO  GO:0010181;
GO  GO:0050661;
GO  GO:0070402;
GO  GO:0003958;
GO  GO:0016491;
GO  GO:0016731;
GO  GO:0016653;
GO  GO:0008219;
GO  GO:0036245;
GO  GO:0022900;
GO  GO:0016226;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSPQLLVLFGSQTGTAQDVSERLGREARRRRLGCRVQALDSYPVVNLINEPLVIFVCATTGQGDPPDNMKNFWRFIFRK
SQ  NLPSTALCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGSALLPVCLGDDQHELGPDAAVDPWLRDLWDRVLGLYPPP
SQ  PGLTEIPPGVPLPSKFTLLFLQEAPSTGSEGQRVAHPGSQEPPSESKPFLAPMISNQRVTGPSHFQDVRLIEFDILGSGI
SQ  SFAAGDVVLIQPSNSAAHVQRFCQVLGLDPDQLFMLQPREPDVSSPTRLPQPCSMRHLVSHYLDIASVPRRSFFELLACL
SQ  SLHELEREKLLEFSSAQGQEELFEYCNRPRRTILEVLCDFPHTAAAIPPDYLLDLIPVIRPRAFSIASSLLTHPSRLQIL
SQ  VAVVQFQTRLKEPRRGLCSSWLASLDPGQGPVRVPLWVRPGSLAFPETPDTPVIMVGPGTGVAPFRAAIQERVAQGQTGN
SQ  FLFFGCRWRDQDFYWEAEWQELEKRDCLTLIPAFSREQEQKVYVQHRLRELGSLVWELLDRQGAYFYLAGNAKSMPADVS
SQ  EALMSIFQEEGGLCSPDAAAYLARLQQTRRFQTETWA
//
ID  A2AI05;
PN  NADPH-dependent diflavin oxidoreductase 1;
GN  Ndor1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000255|HAMAP- Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}.
DR  UNIPROT: A2AI05;
DR  UNIPROT: Q3TQZ6;
DR  UNIPROT: Q80WC5;
DR  Pfam: PF00667;
DR  Pfam: PF00258;
DR  Pfam: PF00175;
DR  PROSITE: PS51384;
DR  PROSITE: PS50902;
DE  Function: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of CISD1 and activate this protein implicated in Fe/S cluster repair (By similarity). In vitro can fully activate methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A (By similarity). {ECO:0000250|UniProtKB:Q9UHB4, ECO:0000255|HAMAP- Rule:MF_03178}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0045111;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0009055;
GO  GO:0071949;
GO  GO:0050660;
GO  GO:0010181;
GO  GO:0050661;
GO  GO:0070402;
GO  GO:0003958;
GO  GO:0016491;
GO  GO:0016731;
GO  GO:0016653;
GO  GO:0008219;
GO  GO:0036245;
GO  GO:0022900;
GO  GO:0016226;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQVPQLLVLFGSQTGTAQDEAERLGREARRRRLGCRVQALDSYSVANLIREPLVIFVCATTGQGDPPDNMKNFWRFIFRK
SQ  SLPSSSLCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGSALLPPCLGDDQHELGPDAAIDPWVGDLWEKIMVMYPVP
SQ  LDIPEIPHGVPLPSKFIFQFLQEVPSIGAEELNIASSAPQTPPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNI
SQ  SFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPGLPQPCTVWNLVSQYLDIASVPRRSFFELLACL
SQ  SQHALEREKLLELSSARGQEELWEYCSRPRRTILEVLCDFPHTAGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQIL
SQ  VAVVKYQTRLKEPRHGLCSSWLASLNPGQAGPVRVPLWVRPGSLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTG
SQ  NFLFFGCRQRDQDFYWQTEWQKLEQKGWLTLVTAFSREQEQKVYVQHRLRELGPLVWELLDGQGAYFYLAGNAKYLPTDV
SQ  SEALMSIFQEEGRLSTADASAYLARLQQTLRFQTETWA
//
ID  Q6NRG5;
PN  NADPH-dependent diflavin oxidoreductase 1;
GN  ndor1;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000255|HAMAP- Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}.
DR  UNIPROT: Q6NRG5;
DR  Pfam: PF00667;
DR  Pfam: PF00258;
DR  Pfam: PF00175;
DR  PROSITE: PS51384;
DR  PROSITE: PS50902;
DE  Function: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of ciapin1, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of cisd1 and activate this protein implicated in Fe/S cluster repair. {ECO:0000255|HAMAP-Rule:MF_03178}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0009055;
GO  GO:0050660;
GO  GO:0010181;
GO  GO:0050661;
GO  GO:0003958;
GO  GO:0016731;
GO  GO:0016653;
GO  GO:0008219;
GO  GO:0036245;
GO  GO:0016226;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPQQNLLILYGSQTGTAEDLAGRLSREAKRHHFNCRTEALDEYRVANLINEHLVIFVCATTGQGDPPDNMKNFWRFIFRR
SQ  NLPHNALCQMDYAVLGLGDSSYPKFNFIAKKLHKRLNQLGACPLLPAALGDDQHELGPDAVVDPWLKDLWSKVLSMFPLR
SQ  PGLEIISEDVLLPPKYSLRLLEEKVGQSELSGDAYERDFISNNTTPPSEIHPFLAPVLSNERVSAHDHFQDVRLIEFNIT
SQ  GSAIQFYPGDVVMVQPRNSLLHVEQFCSLLHLDPLNKVVVEPSDPESPVPMHLAALCSVQQLVERYLDICSIPRRSFFQL
SQ  FCHFSPDEMEREKLKEFSCAAGQEELYSYCNRPRRTILEVLVDFPHTTRCIPATFLLELIPQIRPRAFSIASSMEALPNT
SQ  IQILMAVVQYKTKLIEPRRGLCSTWLASLPPHGTERVPIWVKKGSMKFPCDPDTPVVMVGPGTGVAPFRAAIQERVANGR
SQ  PGNCLFFGCRGKSKDFYFEKEWEDLGNRGYLTLFTAFSRDQEDKIYVQHRIKENSKLLWDLIGTKQGYVYIAGNAKLMPN
SQ  EVTDALKWVLQLEGGMSAPDAEQYLASMEKSCRFQSETWS
//
ID  Q3ZBA8;
PN  Protein NDRG2;
GN  NDRG2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity). {ECO:0000250}.
DR  UNIPROT: Q3ZBA8;
DR  Pfam: PF03096;
DE  Function: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0001818;
GO  GO:0070373;
GO  GO:1904706;
GO  GO:0007399;
GO  GO:0090361;
GO  GO:0010574;
GO  GO:0007165;
GO  GO:1990874;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAELREVQITEEKPLLPGQTPEVAKTHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQPLFQFADMQEIIQN
SQ  FVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCILQYLNFSTIIGIGVGAGAYVLSRYALTHPDTVEGLVLINIDPN
SQ  AKGWMDWAAHKLTGLTSSISEMILGHLFSQEELSGNSELIQKYRNIIAHAPNLDNIELYWNSYNNRRDLNFVRGGDTTLK
SQ  CPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASSCMTRLSRSRTASLT
SQ  SAASIDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC
//
ID  Q9UN36;
PN  Protein NDRG2;
GN  NDRG2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cell projection, growth cone {ECO:0000250}. Note=In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9UN36;
DR  UNIPROT: B3KUE3;
DR  UNIPROT: B4DE86;
DR  UNIPROT: B7WP11;
DR  UNIPROT: B7WPD5;
DR  UNIPROT: D3DS07;
DR  UNIPROT: D3DS10;
DR  UNIPROT: Q567T1;
DR  UNIPROT: Q68DW2;
DR  UNIPROT: Q86U08;
DR  UNIPROT: Q86U46;
DR  UNIPROT: Q96FD3;
DR  UNIPROT: Q96FT0;
DR  UNIPROT: Q96JU0;
DR  UNIPROT: Q96PN0;
DR  UNIPROT: Q9BQH5;
DR  UNIPROT: Q9ULH2;
DR  PDB: 2XMQ;
DR  PDB: 2XMR;
DR  PDB: 2XMS;
DR  Pfam: PF03096;
DR  OMIM: 605272;
DR  DisGeNET: 57447;
DE  Function: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation. {ECO:0000269|PubMed:12845671, ECO:0000269|PubMed:16103061, ECO:0000269|PubMed:21247902}.
DE  Reference Proteome: Yes;
DE  Interaction: P03372; IntAct: EBI-3895740; Score: 0.53
DE  Interaction: Q9UI14; IntAct: EBI-8084498; Score: 0.61
DE  Interaction: P35222; IntAct: EBI-8084686; Score: 0.35
DE  Interaction: Q96Q40; IntAct: EBI-21574933; Score: 0.35
DE  Interaction: Q9UMR2; IntAct: EBI-21616596; Score: 0.35
DE  Interaction: Q92597; IntAct: EBI-21847586; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-21847586; Score: 0.35
DE  Interaction: P30556; IntAct: EBI-20802719; Score: 0.37
DE  Interaction: P51679; IntAct: EBI-20804498; Score: 0.37
DE  Interaction: P10636; IntAct: EBI-20749487; Score: 0.35
DE  Interaction: Q92685; IntAct: EBI-25468455; Score: 0.37
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0001818;
GO  GO:0070373;
GO  GO:1904706;
GO  GO:0090361;
GO  GO:0010574;
GO  GO:0007165;
GO  GO:0021762;
GO  GO:1990874;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAELQEVQITEEKPLLPGQTPEAAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQ
SQ  PLFQFEDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCVLQYLNFSTIIGVGVGAGAYILARYALNHP
SQ  DTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRNIITHAPNLDNIELYWNSYNNR
SQ  RDLNFERGGDITLRCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASS
SQ  CMTRLSRSRTASLTSAASVDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC
//
ID  Q4R4K0;
PN  Protein NDRG2;
GN  NDRG2;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity). {ECO:0000250}.
DR  UNIPROT: Q4R4K0;
DR  Pfam: PF03096;
DE  Function: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0007399;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAELQEVQITEEKPLLPGQTPEAAKIHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQPLFQFGDMQEIIQN
SQ  FVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCVLQYLNFSTVIGVGVGAGAYILSRYALNHPDTVEGLVLINIDPN
SQ  AKGWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRNIITHAPNLDNIELYWNSYNNRRDLNFERGGDITLK
SQ  CPVMLVVGDQAPHEDAVVECNSKLDPTQTSSLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASSCMTRLSRSRTASLT
SQ  SAASIDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC
//
ID  Q9QYG0;
PN  Protein NDRG2;
GN  Ndrg2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:14985363, ECO:0000269|PubMed:16520977}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9QYG0;
DR  UNIPROT: Q3TI48;
DR  UNIPROT: Q3TY42;
DR  UNIPROT: Q3U3T5;
DR  UNIPROT: Q69ZN2;
DR  UNIPROT: Q8C661;
DR  PDB: 2QMQ;
DR  Pfam: PF03096;
DE  Function: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P51637; IntAct: EBI-20565496; Score: 0.35
DE  Interaction: A2AKD7; IntAct: EBI-20566393; Score: 0.35
GO  GO:0005737;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0001818;
GO  GO:0070373;
GO  GO:1904706;
GO  GO:0007399;
GO  GO:0099173;
GO  GO:0090361;
GO  GO:0010574;
GO  GO:0007165;
GO  GO:1990874;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAELQEVQITEEKPLLPGQTPETAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAIFTYHDVGLNYKSCFQ
SQ  PLFRFGDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCILQYLNFSTIIGVGVGAGAYILSRYALNHP
SQ  DTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPDMILGHLFSQEELSGNSELIQKYRGIIQHAPNLENIELYWNSYNNR
SQ  RDLNFERGGETTLKCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASS
SQ  CMTRLSRSRTASLTSAASIDGSRSRSRTLSQSSESGTLPSGPPGHTMEVSC
//
ID  A5A6K6;
PN  Protein NDRG2;
GN  NDRG2;
OS  9598;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity). {ECO:0000250}.
DR  UNIPROT: A5A6K6;
DR  Pfam: PF03096;
DE  Function: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0007399;
GO  GO:0007165;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAELQEVQITEEKPLLPGQTPEAAKTHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQPLFQFEDMQEIIQN
SQ  FVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCVLQYLNFSTIIGVGVGAGAYILARYALNHPDTVEGLVLINIDPN
SQ  AKRWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRNIITHAPNLDNIELYWNSYNNRRDLNFERGGDITLK
SQ  CPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASSCMTRLSRSRTASLT
SQ  SAASVDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC
//
ID  Q5RBN6;
PN  Protein NDRG2;
GN  NDRG2;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5RBN6;
DR  UNIPROT: Q5R695;
DR  UNIPROT: Q5R6V9;
DR  Pfam: PF03096;
DE  Function: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030426;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0007399;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAELQEVQITEEKPLLPGQTPEAAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQ
SQ  PLFQFEDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCVLQYLNFSTIIGVGVGAGAYILARYALNHP
SQ  DTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRNIITHAPNLDNIELYWNSYNNR
SQ  RDLNFERGGDITLKCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASS
SQ  CMTRLSRSRTASLTSAASVDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC
//
ID  Q8VBU2;
PN  Protein NDRG2;
GN  Ndrg2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone. Note=In neurons, seems to concentrate at axonal growth cone.
DR  UNIPROT: Q8VBU2;
DR  UNIPROT: Q8VBW2;
DR  UNIPROT: Q8VI00;
DR  UNIPROT: Q8VI01;
DR  Pfam: PF03096;
DE  Function: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor (By similarity). May be involved in dendritic cell and neuron differentiation. {ECO:0000250, ECO:0000269|PubMed:16039777}.
DE  Reference Proteome: Yes;
DE  Interaction: P19332; IntAct: EBI-26374040; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26440627; Score: 0.35
GO  GO:0005737;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0001818;
GO  GO:0070373;
GO  GO:0048662;
GO  GO:1904706;
GO  GO:0007399;
GO  GO:0099173;
GO  GO:0090361;
GO  GO:0010574;
GO  GO:0007165;
GO  GO:1990874;
GO  GO:0016055;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAELQEVQITEEKPLLPGQTPEAAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAIFTYHDVGLNYKSCFQ
SQ  PLFQFGDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSQDQLADMIPCILQYLNFSTIIGVGVGAGAYILSRYALNHP
SQ  DTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRSLITHAPNLENIELYWNSYNNR
SQ  RDLNFERGGEMTLKCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFVQGMGYMASS
SQ  CMTRLSRSRTASLTSAASIDGSRSRSRTLSQSSESGTLPSGPPGHTMEVSC
//
ID  Q9M9L3;
PN  Nuclear envelope-associated protein 1;
GN  NEAP1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:27630107}; Single-pass membrane protein {ECO:0000255}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27630107}. Note=Colocalized with bZIP18 in the nucleoplasm. {ECO:0000269|PubMed:27630107}.
DR  UNIPROT: Q9M9L3;
DR  UNIPROT: Q56Y98;
DR  UNIPROT: Q9ZRC5;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005654;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSYSEKTTVDPLLRDLDEKKESFRRNVVSLATELKQVRGRLVSQEQSFLKETITRKEAEKRGKNMEMEICKLQKRLEERN
SQ  CQLEASASAADKFIKELEEFRLKLDTTKQTAEASADSAQSTKIQCSMLKQQLDDKTRSLREQEDRMTQLGHQLDDLQRGL
SQ  SLRECSEKQLREEVRRIEREVTEAIAKAGIGGMDSELQKLLEDVSPMKFERMNRLVEVKDEEITKLKDEIRLMSGQWKHK
SQ  TKELESQLEKQRRTDQDLKKKVLKLEFCLQEARSQTRKLQRKGERRDMEIKEIRDLISEKQNLNNESWDKQKFWDNSGFK
SQ  IVVSMSMLMLVVVSKR
//
ID  F4K1B4;
PN  Nuclear envelope-associated protein 2;
GN  NEAP2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:27630107}; Single-pass membrane protein {ECO:0000255}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27630107}.
DR  UNIPROT: F4K1B4;
DR  UNIPROT: Q5PP55;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0043621;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSDSVKTTVDPLLKDLDGKKESFRRNVVSMAAELKQVRGRLVSQEQFFVKESFCRKEAEKKAKNMEMEICKLQKKLEDRN
SQ  CELVASTSAAEKFLEEVDDLRSQLALTKDIAETSAASAQSAQLQCSVLTEQLDDKTRSLREHEDRVTHLGHQLDNLQRDL
SQ  KTRECSQKQLREEVMRIEREITEAVAKSGKGTECELRKLLEEVSPKNFERMNMLLAVKDEEIAKLKDDVKLMSAHWKLKT
SQ  KELESQLERQRRADQELKKKVLKLEFCLQEARSQTRKLQRAGERRDKAIKELSDQITGKQLNESVSGEKQNFWDTSGFKI
SQ  VVSMSMLILVIISKR
//
ID  Q4PT37;
PN  Nuclear envelope-associated protein 3;
GN  NEAP3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:27630107}; Single-pass membrane protein {ECO:0000255}. Nucleus, nucleoplasm {ECO:0000269|PubMed:27630107}.
DR  UNIPROT: Q4PT37;
DR  UNIPROT: O80530;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0043621;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPTSVSLREDDPLLKDLSEKKQSFRRNVVSLATELKEARTRLAEQERSCSKEAMSRQEAETRVKRMEDEMHELAKELNEK
SQ  VEQIRASDVATEKFVKELADIKSQLAATHATAEASALSAESAHSHCRVLSKQLHERTGSLKEHEDQVTRLGEQLENLRKE
SQ  LRVRESSQKQLRDELLKVEGDIMRAVSVVKTKENSEVRNMLNEDTPKNSERINKLLTAKDDEIARLRDELKIISAHWRFK
SQ  TKELEDQVENQRRIDQELKKKVLKLEFCLRETRIQTRKLQKMGERNDVAIQELKEQLAAKKQHEADHSSNQNLWDKSGFK
SQ  IVVSMSMLILVAFSRR
//
ID  O36420;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  654901;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: O36420;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MHKIQKMSCTPSVRSRYTLKRKRLNSAKSATLKKKKVFLSNSEFFAGVSTNYELGKDFLREMDTPICTSNTVFLPVKFSD
SQ  VAPGRCLTLSPYGHSSVLGFHCQECKPDSSSGFTQAQQSAESNELLSVNLCFLNNVEKVVQHKAFYLSLLGHSMNTVKQS
SQ  LGQPSLLYCYTVLKKFYPQIFPIFTANGPMLTMYIIFTSLTLHVSEAVLRILTDNVENHNLSADCYKGHYILSIEPQALE
SQ  ESNLNVCVTKICDLVAQLDFSDELKQEYVNGSTLIANFLN
//
ID  P0CK48;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  82830;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: P0CK48;
DR  UNIPROT: P03183;
DR  UNIPROT: Q777G9;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
DE  Interaction: P0C763; IntAct: EBI-9644957; Score: 0.37
DE  Interaction: K9UT58; IntAct: EBI-9645120; Score: 0.37
DE  Interaction: K9US31; IntAct: EBI-9645332; Score: 0.37
DE  Interaction: A6SZC0; IntAct: EBI-9645372; Score: 0.37
DE  Interaction: P25939; IntAct: EBI-9645347; Score: 0.37
DE  Interaction: P03219; IntAct: EBI-9645357; Score: 0.37
DE  Interaction: P0C6Z6; IntAct: EBI-9645352; Score: 0.37
DE  Interaction: P0CK55; IntAct: EBI-9645362; Score: 0.37
DE  Interaction: K9UT36; IntAct: EBI-9645602; Score: 0.37
DE  Interaction: P0CK49; IntAct: EBI-9645650; Score: 0.37
DE  Interaction: P13285; IntAct: EBI-9645790; Score: 0.37
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPVTPDAVNARQQRPADPALRRLMHPHHRNYTASKASAHSVKSVSRCGKSRSELGRMERVGSVARSICSRHTRHGVDRS
SQ  HFSLRDFFRGISANFELGKDFLREMNTPIHVSEAVFLPLSLCTLSPGRCLRLSPFGHSLTLGSHCEICINRSQVHVPQEF
SQ  SSTQLSFFNNVHKIIPNKTFYVSLLSSSPSAVKAGLSQPSLLYAYLVTGHFCGTICPIFSTNGKGRLIMHLLLQGTSLHI
SQ  PETCLKLLCENIGPTYELAVDLVGDAFCIKVSPRDTVYEKAVNVDEDAIYEAIKDLECGDELRLQIINYTQLILENKQ
//
ID  P0CK47;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  10377;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: P0CK47;
DR  UNIPROT: P03183;
DR  UNIPROT: Q777G9;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-2622485; Score: 0.37
DE  Interaction: P03185; IntAct: EBI-2621663; Score: 0.51
DE  Interaction: Q9UBX5; IntAct: EBI-2622365; Score: 0.37
DE  Interaction: Q8N2S1; IntAct: EBI-2622356; Score: 0.37
DE  Interaction: P28799; IntAct: EBI-2622347; Score: 0.37
DE  Interaction: Q02818; IntAct: EBI-2622405; Score: 0.37
DE  Interaction: Q12805; IntAct: EBI-2622396; Score: 0.37
DE  Interaction: P46379; IntAct: EBI-2622387; Score: 0.37
DE  Interaction: Q8WXE0; IntAct: EBI-2622374; Score: 0.37
DE  Interaction: Q9Y228; IntAct: EBI-2622440; Score: 0.37
DE  Interaction: B2RCM5; IntAct: EBI-2622431; Score: 0.37
DE  Interaction: Q9UEW3; IntAct: EBI-2622419; Score: 0.37
DE  Interaction: A1L0V1; IntAct: EBI-2622449; Score: 0.37
DE  Interaction: Q86V58; IntAct: EBI-2622467; Score: 0.37
DE  Interaction: Q9NSC5; IntAct: EBI-2622503; Score: 0.37
DE  Interaction: P63279; IntAct: EBI-2622494; Score: 0.37
DE  Interaction: P55268; IntAct: EBI-2622476; Score: 0.37
DE  Interaction: Q9UHF1; IntAct: EBI-2622539; Score: 0.37
DE  Interaction: Q6PKC3; IntAct: EBI-2622530; Score: 0.37
DE  Interaction: Q9UBP4; IntAct: EBI-2622521; Score: 0.37
DE  Interaction: Q93062; IntAct: EBI-2622512; Score: 0.37
DE  Interaction: Q96NA8; IntAct: EBI-2622553; Score: 0.37
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPVTPDAVNARQQRPADPALRRLMHPHHRNYTASKASAHSVKSVSRCGKSRSELGRMERVGSVARSICSRHTRHGVDRS
SQ  HFSLRDFFRGISANFELGKDFLREMNTPIHVSEAVFLPLSLCTLSPGRCLRLSPFGHSLTLGSHCEICINRSQVHVPQEF
SQ  SSTQLSFFNNVHKIIPNKTFYVSLLSSSPSAVKAGLSQPSLLYAYLVTGHFCGTICPIFSTNGKGRLIMHLLLQGTSLHI
SQ  PETCLKLLCENIGPTYELAVDLVGDAFCIKVSPRDTVYEKAVNVDEDAIYEAIKDLECGDELRLQIINYTQLILENKQ
//
ID  P28951;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  31520;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: P28951;
DR  UNIPROT: Q6DLI2;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFDGRSDIYDSTSFAAELDDLYSCRSTGRENGRRSRVSTRGVHRDRCGSAAKRRSTKRRCELVARERDRYSLYLDYMASH
SQ  PSDEISAVRELVVPLIKTTSITLPFDLNQTVADNCLSLSGMGYYLGIGGCCPTCTVSGEPRLHRADRAALILAYVQQLNN
SQ  IYEYRGFLASVLAAAAQGDQAGVAASEGVQAERLLENVLAQPELFFAYHVLRDGGIQNVRVLFYRDLSVSGYMMYAVFPT
SQ  KSVHLHYRLIDRLLAACPGYKIIAHVWQTAFVLVVRRDEGQQTDMDIPTVSAGDIYCKMCDLSFDGELLLEYKKLYAVFD
SQ  DFLPPV
//
ID  Q66672;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  82831;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: Q66672;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDRERPRKTREPASPGSVLSKRSKLSRKSLALRSLNKFHPYKAPSSVRSLKKAHTLVSNGDFFNGISLNCEFGKDFLREM
SQ  DTPICTSKVICLPLDVHEIAPGRCLVLSPLGHACNMGFYCEKCTQSGQNSYSQFQGRGGNAKMAAQNSKDDLHSVTLTFY
SQ  NQVSKVVQNKNFYLSLLSHSLTTIKKSFVQPSLLYSYTVLRALCDDVFPIFKDTENGLCMFALFKTDDLHVSETCLRHLV
SQ  DNLIHYRVTLDCVKHTYMLKFSPIRAEANGMTIQEVEICEAITGLDFTDEIKQEIISGQELVSEL
//
ID  Q9E6N8;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  10389;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: Q9E6N8;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTGHTLVRRKSIGRDKRLVGRSRRQWRDMNLPSYGNSKGTNMDIYRAYFEFIAESPADELMLVKDLVTPLIKTTSISLPF
SQ  DMSEAVADNCLSLSGMGYYLGVGGCCPTCVSSGDPRLGRNDRAALILAYVQQINNIYHYRIFLASIIVLGDRLRGDARDK
SQ  DMESILTRIIAIPELFFAYYVLLDSGIKNVKVLFYLDREAGSSEYMMYIVFPGKALHLHYRLIDCMKSACKSYRIIAHVW
SQ  RTNFLLVIRKEYDRQTDSCDVPAVNAEDVYCKLCDLNIDGELLLEYGKLYSAFDEFLPPR
//
ID  P16794;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  10360;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023, ECO:0000269|PubMed:11961254, ECO:0000269|PubMed:25339763, ECO:0000269|PubMed:26511021, ECO:0000269|PubMed:31980459}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP- Rule:MF_04023, ECO:0000269|PubMed:26511021}.
DR  UNIPROT: P16794;
DR  UNIPROT: Q7M6N0;
DR  PDB: 5DOB;
DR  PDB: 5DOC;
DR  PDB: 5DOE;
DR  PDB: 6T3X;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023, ECO:0000269|PubMed:25339763}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSVSGVRTPRERRSALRSLLRKRRQRELASKVASTVNGATSANNHGEPPSPADARPRLTLHDLHDIFREHPELELKYLN
SQ  MMKMAITGKESICLPFNFHSHRQHTCLDISPYGNEQVSRIACTSCEDNRILPTASDAMVAFINQTSNIMKNRNFYYGFCK
SQ  SSELLKLSTNQPPIFQIYYLLHAANHDIVPFMHAEDGRLHMHVIFENPDVHIPCDCITQMLTAAREDYSVTLNIVRDHVV
SQ  ISVLCHAVSASSVKIDVTILQRKIDEMDIPNDVSESFERYKELIQELCQSSGNNLYEEATSSYAIRSPLTASPLHVVSTN
SQ  GCGPSSSSQSTPPHLHPPSQATQPHHYSHHQSQSQQHHHRPQSPPPPLFLNSIRAP
//
ID  F5HFZ4;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  295027;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: F5HFZ4;
DR  PDB: 5D5N;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSVSGVRTPRERRSALRSLLRKRRQRELASKVASTVNGATSANNHGEPPSPADARPRLTLHDLHDIFREHPELELKYLN
SQ  MMKMAITGKESICLPFNFHSHRQHTCLDISPYGNEQVSRIACTSCEDNRILPTASDAMVAFINQTSNIMKNRNFYYGFCK
SQ  SSELLKLSTNQPPIFQIYYLLHAANHDIVPFMHAENGRLHMHVIFENSDVHIPCDCITQMLTAAREDYSVTLNIVRDHVV
SQ  ISVLCHAVSASSVKIDVTILQRKIDEMDIPNDVSESFERYKELIQELCQSSGNNLYEEATSSYAIRSPLTASPLHVVSTN
SQ  GCGPSSSSQSTPPHLHPPSQATQPHHYSHHQSQSQQHHHRPQSPPPPLFLNSIRAP
//
ID  P10215;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  10299;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023, ECO:0000269|PubMed:12163613, ECO:0000269|PubMed:16415024}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP- Rule:MF_04023}.
DR  UNIPROT: P10215;
DR  PDB: 4ZXS;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023, ECO:0000269|PubMed:15140953, ECO:0000269|PubMed:15140956, ECO:0000269|PubMed:24453362}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-7183643; Score: 0.40
DE  Interaction: P10209; IntAct: EBI-15938929; Score: 0.35
DE  Interaction: P10201; IntAct: EBI-15938929; Score: 0.35
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046802;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYDTDPHRRGSRPGPYHGKERRRSRSSAAGGTLGVVRRASRKSLPPHARKQELCLHERQRYRGLFAALAQTPSEEIAIVR
SQ  SLSVPLVKTTPVSLPFCLDQTVADNCLTLSGMGYYLGIGGCCPACNAGDGRFAATSREALILAFVQQINTIFEHRAFLAS
SQ  LVVLADRHNAPLQDLLAGILGQPELFFVHTILRGGGACDPRLLFYPDPTYGGHMLYVIFPGTSAHLHYRLIDRMLTACPG
SQ  YRFVAHVWQSTFVLVVRRNAEKPTDAEIPTVSAADIYCKMRDISFDGGLMLEYQRLYATFDEFPPP
//
ID  P89454;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  10315;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023, ECO:0000269|PubMed:10550666, ECO:0000269|PubMed:11369887}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP- Rule:MF_04023}.
DR  UNIPROT: P89454;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYDIAPRRSGSRPGPGRDKTRRRSRFSAAGNPGVERRASRKSLPSHARRLELCLHERRRYRGFFAALAQTPSEEIAIVRS
SQ  LSVPLVKTTPVSLPFSLDQTVADNCLTLSGMGYYLGIGGCCPACSAGDGRLATVSREALILAFVQQINTIFEHRTFLASL
SQ  VVLADRHSTPLQDLLADTLGQPELFFVHTILRGGGACDPRFLFYPDPTYGGHMLYVIFPGTSAHLHYRLIDRMLTACPGY
SQ  RFAAHVWQSTFVLVVRRNAEKPADAEIPTVSAADIYCKMRDISFDGGLMLEYQRLYATFDEFPPP
//
ID  P28865;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  10370;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: P28865;
DR  UNIPROT: Q69060;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVHKSRIRRSRSLSVTHRIQKRPDHREKTKLYLQLKLHDLHTVFNLFPEYEQKFLAIIKLPITGKEPIDVPFSLSNHHQ
SQ  HTCLEFSPYANEQISKSACLHCESVSVPTSSDAMVAHLNQVNNVMQNRLYFYGFRKDMELIRMSAKQPTIFQIFYIVHNT
SQ  INNIFPIMFERKQKLGMHIVFQSRTLHIPCECIKQIVAVSSGYNVYLDILQESVILTVLCETLDTNTNIHIDIGMLQKKL
SQ  EEMDIPNEISDRLEKYKGHLIGFH
//
ID  Q9WT27;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  36351;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: Q9WT27;
DR  UNIPROT: Q77PU8;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVHKNRFRRSRSLSVTHRIQKRPDHREKTKLYLQLKLHDLHAVFNLFPEYEQKFLAIIKLPITGKEPIDVPFSLSNHHQ
SQ  HTCLEFSPYANEQISKSACLHCESVSVPTSSDAMVAHLNQVTNVMQNRFYFYGFRKDMELIRMSAKQPTIFQIFYIVHNT
SQ  INNIFPIMFEKKQKLGMHIVFQSRTLHIPCECIKQIIAVSSGYNVYLDILQDSVILTVLCETLDTNTNIHIDIGMLQKKL
SQ  EEMDIPNEISDRLEKYKGHLIGFH
//
ID  P52361;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  57278;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: P52361;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAIQSTRRLRRASSLLKKSKPYNKEKTNLSLSLSLKELHSVFKLFPEYELKFLNMMKLPITGKEPIKIPFDLSLHHQHTC
SQ  LDLSPYANEQVSKSACVNCGTTNIPTASDAMVAYMNQISNVMQNRLYYYGFQKKVELIRMSAKQPTLFQIFYILSSIASN
SQ  FLPIMFENNEKLNMYVVFQTRTLHIPCECINQIMTVSSGYTVLLDILHDSIVLHVLCKTIETSNIQIDINVLQRKIEEMD
SQ  VPDEIGDKFEKLKHILPFI
//
ID  F5H982;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  868565;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023, ECO:0000269|PubMed:23365436}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: F5H982;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023, ECO:0000269|PubMed:23365436}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPKSVSSHISLATSTGRSGPRDIRRCLSSRLRSVPPGARSASVSSKHRNGLRKFISDKVFFSILSHRHELGVDFLREMET
SQ  PICTSKTVMLPLDLSTVAPGRCVSLSPFGHSSNMGFQCALCPSTENPTVAQGSRPQTMVGDALKKNNELCSVALAFYHHA
SQ  DKVIQHKTFYLSLLSHSMDVVRQSFLQPGLLYANLVLKTFGHDPLPIFTTNNGMLTMCILFKTRALHLGETALRLLMDNL
SQ  PNYKISADCCRQSYVVKFVPTHPDTASIAVQVHTICEAVAALDCTDEMRDDIQKGTALVNAL
//
ID  Q6UDK0;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  670426;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: Q6UDK0;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDVALKRNSSFFRAKARLTLLKRRDGGVISRSLEHRRSSRRRSSVSAPTRRVSGTLAKLGADDRRQFFDAFFRMTAVSP
SQ  EETVSLLRSMTVPVIQQENISLPYDINAKFAPGDCISLSEMGYTLEMGGCCSLCSYGWSTTTPPELPALELAFMHHLSSV
SQ  VEFKELVTSLRVCAGNSIVGNGAYENEGLLRMIKHLLEQSTLFYAYYTVKGGVSHDFRVLISEDGGGDGGSPAYAMYFVF
SQ  KPGSPLHLGAKLIRQLIFNCPGYKWHADVHEGAFLLVVTRDRCSAIPEPRRVKLDPEDVYRRYCDVLVTEEKVHDYSRLY
SQ  STFSTYCPPASRREQTAAPATAKQV
//
ID  Q01041;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  10383;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: Q01041;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSRSVKSRKSTKSRRHHPYVKLTDKMFFSAISSKKELGTDFLREMDAPICTSKTILLPLDLNSISPGRCIYLSPFGHSS
SQ  NMEFQCEKCTESKNKGSGDVSQNHDLYSVTLVFYKNVDKVVKHKAFYLSLLSHSMENLKKSFTQPELLYAYVVVKEAGHN
SQ  VFPIFFEKDDCLSICLTFKCQTLHIGESCLRMLMDNLPNYKISIDYIKDVYAMTFTQCFAIQRNISIAEDTICESVSTLD
SQ  CTDELREEIVKGINALQIKDI
//
ID  P09283;
PN  Nuclear egress protein 1;
GN  NEC1;
OS  10338;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04023}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
DR  UNIPROT: P09283;
DR  Pfam: PF02718;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04023}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016020;
GO  GO:0046872;
GO  GO:0046765;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MHLKPTRFFHANQPPMPHSYEMEDLCFDDMQYRWSPSNTPYRSMSRRYKSVSRSGPSMRVRSRTPCRRQTIRGKLMSKER
SQ  SVYRHYFNYIARSPPEELATVRGLIVPIIKTTPVTLPFNLGQTVADNCLSLSGMGYHLGLGGYCPTCTASGEPRLCRTDR
SQ  AALILAYVQQLNNIYEYRVFLASILALSDRANMQAASAEPLLSSVLAQPELFFMYHIMREGGMRDIRVLFYRDGDAGGFM
SQ  MYVIFPGKSVHLHYRLIDHIQAACRGYKIVAHVWQTTFLLSVCRNPEQQTETVVPSIGTSDVYCKMCDLNFDGELLLEYK
SQ  RLYALFDDFVPPR
//
ID  O36417;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  654901;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: O36417;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MASGKKLIDQLCSVVSSFLCPSISSLDIDRCAVGPHIFSRGSSQAICTVKLLHGEVYNLEFVYRYWAHILEKYNFPFSPT
SQ  FIICNNGLAVTLKCYVSEPRDLSSRYGQATSMALDVNLQRNSFVVLSQDDFIKFKTPLVFAKDLDITNSMVVCRTYLTSS
SQ  RNSLQFLVVKSKNPRRLENVLDMIKRAVEATGSNLPATREKPLPLEQTEQLESTLPSSGHLRVLQSTSLTGRCPSWGAAC
SQ  ALLLLSLAVGLMAILAAKLMQWP
//
ID  P03185;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10377;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024, ECO:0000269|PubMed:10708440, ECO:0000269|PubMed:15731265}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:10708440, ECO:0000269|PubMed:15731265}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P03185;
DR  UNIPROT: Q777G7;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:15731264, ECO:0000269|PubMed:16406456}.
DE  Reference Proteome: Yes;
DE  Interaction: P0CK47; IntAct: EBI-2621663; Score: 0.51
DE  Interaction: P04275; IntAct: EBI-2622571; Score: 0.37
DE  Interaction: P28799; IntAct: EBI-2622562; Score: 0.37
DE  Interaction: Q9NSC5; IntAct: EBI-2622610; Score: 0.55
DE  Interaction: O75094; IntAct: EBI-2622601; Score: 0.37
DE  Interaction: Q99873; IntAct: EBI-2622580; Score: 0.37
DE  Interaction: Q9NR46; IntAct: EBI-11736344; Score: 0.37
DE  Interaction: O96006; IntAct: EBI-11736334; Score: 0.37
DE  Interaction: O00471; IntAct: EBI-11736369; Score: 0.37
DE  Interaction: O75477; IntAct: EBI-11736364; Score: 0.37
DE  Interaction: Q16611; IntAct: EBI-11736349; Score: 0.37
DE  Interaction: Q13323; IntAct: EBI-11736354; Score: 0.37
DE  Interaction: Q9UEW3; IntAct: EBI-11736359; Score: 0.37
DE  Interaction: Q9BXN2; IntAct: EBI-11736390; Score: 0.37
DE  Interaction: Q8N6L0; IntAct: EBI-11736405; Score: 0.37
DE  Interaction: Q8TD10; IntAct: EBI-11736400; Score: 0.37
DE  Interaction: Q969F0; IntAct: EBI-11736395; Score: 0.37
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0046765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MASPEERLLDELNNVIVSFLCDSGSLEVERCSGAHVFSRGSSQPLCTVKLRHGQIYHLEFVYKFLAFKLKNCNYPSSPVF
SQ  VISNNGLATTLRCFLHEPSGLRSGQSGPCLGLSTDVDLPKNSIIMLGQDDFIKFKSPLVFPAELDLLKSMVVCRAYITEH
SQ  RTTMQFLVFQAANAQKASRVMDMISDMSQQLSRSGQVEDTGARVTGGGGPRPGVTHSGCLGDSHVRGRGGWDLDNFSEAE
SQ  TEDEASYAPWRDKDSWSESEAAPWKKELVRHPIRRHRTRETRRMRGSHSRVEHVPPETRETVVGGAWRYSWRATPYLARV
SQ  LAVTAVALLLMFLRWT
//
ID  P28954;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  31520;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P28954;
DR  UNIPROT: Q6S6P5;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MDSYNYRDFAVGGGLLQRIRLVVSGSLHCGESDATLNDPKHLPARCVFQFSGPDNNSVTFPIEYVLRLMKNWARSQCDPY
SQ  IRIQNTGVSVLFQGFFFAPPNAPMASITSEHNNVILKSTHTTGLALSGIERVKRGGGLDLRPLQAMMQISCFTRMPVVQL
SQ  SFRFMGPEDASRTQRLLERATSFGAMELHQKRTVDSCDRSNGIVSPREHRECRERQKRRPTPKRCASEVFASLASISSAF
SQ  ASERVKRRPVRIAAAILAFVFVAVILAIATKGRLF
//
ID  P84406;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  310273;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P84406;
DR  UNIPROT: Q6S6P5;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: No;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MDSYNYRDFAVGGGLLQRIRLVVSGSLHCGESDATLNDPKHLPARCVFQFSGPDNNSVTFPIEYVLRLMKNWARSQCDPY
SQ  IRIQNTGVSVLFQGFFFAPPNAPMASITSEHNNVILKSTHTTGLALSGIERVKRGGGLDLRPLQAMMQISCFTRMPVVQL
SQ  SFRFMGPEDASRTQRLLERATSFGAMELHQKRTVDSCDRSNGIVSPREHRECRERQKRRPTPKRCASEVFASLASISSAF
SQ  ASERVKRRPVRIAAAILAFVFVAVILAIATKGRLF
//
ID  Q66669;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  82831;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: Q66669;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MNGSKRLVAQLCQVVRSFICQPGTAVDLWQCAAGPHVFAKGSTQPICIVKLVHGQIYNLEFVYKYWCHILQSEKFPYSPV
SQ  FIISNNGLAITLKCFLCEPMDLHSQFGRCLSMDTDVYLPKNTSVVLSQDDFTKFKTNLVFSKDLNVFNSMVVCRTYLTDF
SQ  RQALQFLVVKAKNPKRVTAILGTIAQTLGLTPDTRSGEGGKNSERGEDDMVRRPIRAHRAGDSGGSPGTLPAEPQGAPTP
SQ  PGGGLGLSSGLGLVRRWTRCAFQRYFTVLAVGAVAAATFLAGAKLTG
//
ID  Q9E6N5;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10389;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: Q9E6N5;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MEVIPNINSRRAGLIARIKLIVRGDLTTGNYDPVLAESFSGCIPTRSAFQFSGADGVESAFPVEYVMRMMNDWAKGECNP
SQ  YIKIQNTGVSVLIEGFFDPPINATKAPLCTDKVNVLLNTTESTGIVLSDINKIKQSIGVDCRPFQACLIVNCFVRLPIVQ
SQ  LAFRFVGPSDPGRTTKLLDSAIAAYDAKIRQRRKRNLQIMESKSQDHTSDGCIPIPIIDETHRSGITGESKSLFGMFKNI
SQ  ASGECVTTIRIPRYIVMLWIFSVLLAMVTWGSYRLYS
//
ID  P16791;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10360;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024, ECO:0000269|PubMed:25339763, ECO:0000269|PubMed:26511021, ECO:0000269|PubMed:31980459}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP- Rule:MF_04024}.
DR  UNIPROT: P16791;
DR  UNIPROT: Q7M6N3;
DR  PDB: 5DOB;
DR  PDB: 6T3X;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:25339763}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MEMNKVLHQDLVQATRRILKLGPSELRVTDAGLICKNPNYSVCDAMLKTDTVYCVEYLLSYWESRTDHVPCFIFKNTGCA
SQ  VSLCCFVRAPVKLVSPARHVGEFNVLKVNESLIVTLKDIEEIKPSAYGVLTKCVVRKSNSASVFNIELIAFGPENEGEYE
SQ  NLLRELYAKKAASTSLAVRNHVTVSSHSGSGPSLWRARMSAALTRTAGKRSSRTASPPPPPRHPSCSPTMVAAGGAAAGP
SQ  RPPPPPMAAGSWRLCRCEACMGRCGCASEGDADEEEEELLALAGEGKAAAAAAGQDVGGSARRPLEEHVSRRRGVSTHHR
SQ  HPPSPPCAPSLERTGYRWAPSSWWRARSGPSRPQSGPWLPARFATLGPLVLALLLVLALLWRGHGQSSSPTRSAHRD
//
ID  Q6SW81;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  295027;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: Q6SW81;
DR  UNIPROT: D2K3L8;
DR  PDB: 5D5N;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0019033;
GO  GO:0046765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MEMNKVLHQDLVQATRRILKLGPSELRVTDAGLICKNPNYSVCDAMLKTDTVYCVEYLLSYWESRTDHVPCFIFKNTGCA
SQ  VSLCCFVRAPVKLVSPARHVGEFNVLKVNESLIVTLKDIEEIKPSAYGVLTKCVVRKSNSASVFNIELIAFGPENEGEYE
SQ  NLLRELYAKKAASTSLAVRNHVTVSSHSGSGPSLWRARMSAALTRTAGKRSPRTASPPPPPPRHPSCSPTMVAAGGAAAG
SQ  PRPPPPPMAAGSWRLCRCEACMGRCGCASEGDADEEEEELLALAGEGKAAAAAAGQDIGGSARRPLEEHVSRRRGVSTHH
SQ  RHPPSPPCTPSLERTGYRWAPSSWWRARSGPSRPQSGPWLPARFATLGPLVLALLLVLALLWRGHGQSSSPTRSAHRD
//
ID  P10218;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10299;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024, ECO:0000269|PubMed:12163613, ECO:0000269|PubMed:16415024}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:12163613, ECO:0000269|PubMed:16415024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P10218;
DR  PDB: 4ZXS;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:12805460, ECO:0000269|PubMed:15140953, ECO:0000269|PubMed:15140956}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-7183692; Score: 0.40
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0046802;
GO  GO:0046765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MAGLGKPYTGHPGDAFEGLVQRIRLIVPSTLRGGDGEAGPYSPSSLPSRCAFQFHGHDGSDESFPIEYVLRLMNDWAEVP
SQ  CNPYLRIQNTGVSVLFQGFFHRPHNAPGGAITPERTNVILGSTETTGLSLGDLDTIKGRLGLDARPMMASMWISCFVRMP
SQ  RVQLAFRFMGPEDAGRTRRILCRAAEQAITRRRRTRRSREAYGAEAGLGVAGTGFRARGDGFGPLPLLTQGPSRPWHQAL
SQ  RGLKHLRIGPPALVLAAGLVLGAAIWWVVGAGARL
//
ID  P89457;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10315;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P89457;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:10993927}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
GO  GO:0046765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MAGMGKPYGGRPGDAFEGLVQRIRLIVPATLRGGGGESGPYSPSNPPSRCAFQFHGQDGSDEAFPIEYVLRLMNDWADVP
SQ  CNPYLRVQNTGVSVLFQGFFNRPHGAPGGAITAEQTNVILHSTETTGLSLGDLDDVKGRLGLDARPMMASMWISCFVRMP
SQ  RVQLAFRFMGPEDAVRTRRILCRAAEQALARRRRSRRSQDDYGAVVVAAAHHSSGAPGPGVAASGPPAPPGRGPARPWHQ
SQ  AVQLFRAPRPGPPALLLLAAGLFLGAAIWWAVGARL
//
ID  P52465;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10370;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P52465;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MANVLKEKMYDELLSATCRILKLGSHDYRITERNLLSKNPKFPLCDIILKLDYAYNLEYLLSLWEHVTKQEPRFVFKNTG
SQ  GAVSMSCYLHAPVKVEGHHAVRECNILRVNECLTVRMSDIVAMKPSTFAVFTKCIIRRNRDDTYVVEFVAFGPENESEYI
SQ  SLLKAIFLKKCSMGKQHLESNRFCQGLRRRSSHVLEKGRFESSGKVVNKASAVVTSQESIKQFYEKEKSLLSGVKFWRLS
SQ  ERHCRFALVGICFLLALYFCYVLLKKTPTPASGSVV
//
ID  Q9QJ35;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  36351;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: Q9QJ35;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MANVLKEKMYDELLSATCRILKLGSHDYRMTERNLLSKNPKFPLCDIILKLDYAYNLEYLLSLWEHVTKQEPRFVFKNTG
SQ  GAVSMSCYLHAPVKAEGHHAVRECNILRVNECLTVRMSDIVAMKPSTFAVFTKCIIRRNRDETYVVEFVAFGPENESEYI
SQ  SLLKAIFLKKCSMGKQHLESNRFCQGLRRRSSHVLEKGQLGSSGEIANKASAVVTSQESINQFYEKEKSFLSGVKFSRLS
SQ  ERHCRVAIVSICFLLALYFCYVLLKKTPTPASGPVV
//
ID  P52466;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  57278;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P52466;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MLKEKMYDELILSTCRVLKLGPADFRVTDKNLFSKNPKFPLCDILLKLDFAYSLEYLLSLWEDLTKQEARFIFKNTGGAV
SQ  SMSCYLHAPIKQESQNIVKECNILNVNECLSVCLNDIEAIKPSSSGVLTKCIIRRNRDAAFIVEFVAFGPESESEYIALL
SQ  KAIILKKKFLERQDLEKHRAARHIKKPLRLQLKSVGEMTSFRSINYMGNTKDAAVFPVTVPIFARRNNILCGFLVAALLI
SQ  VCYVIFKEFALSADFSAV
//
ID  F5HA27;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  868565;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024, ECO:0000269|PubMed:23365436, ECO:0000269|PubMed:23623980}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:23365436, ECO:0000269|PubMed:23623980}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: F5HA27;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:23365436, ECO:0000269|PubMed:23623980}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MSVVGKRVVDELCRVVSSYLGQSGQSLDLERCIDGAPVYAKGGATAICTVRMQHGCVYHLEFVYKFWAHLLEEMHYPFSP
SQ  CFVISNNGLSTTLKCFLCRPSDAVSQFGHVLPVESDVYLAKNTSVVLGQDDFTKFKASLVFSKNLGVYNSMVICRTYFTD
SQ  YRQVLQFLVVTPKSHKRLKSLLETVYCLAAPVADSAAQGGAGFPTNGRDARACTSDVTAVYWAGQGGRTVRILGAFQWSL
SQ  GRAVALVRRSWPWISAGIAFLCLGLVWMRPS
//
ID  Q6UDJ7;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  670426;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: Q6UDJ7;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MRSDKYSQLVSVVNAGLGACGTSATLVYIRNNARVAPTGDIITLPARLDGPPIPAEYILEAMTSLLSIRTAWLRIQNTGQ
SQ  AVIVAGCSTQNFHHGDVTWEPPASTVTLTTAKSLWVSASAVREMKVIQRIRTAPLAAMMFMCFYRGGKNEVTVRFAFYKS
SQ  DSEPNLLKISKCVYEAIDAEATRNLPKPRGFDTPPCAVLAQRMRPLGAAEGGDRETSAQTHSPAAQAQHVMQHATATKSW
SQ  GALGRTLKHKKNLGWILFTCALSLAAAFVTAYIK
//
ID  Q01045;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10383;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: Q01045;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MNSTRLVYELCDIVNLYLCQPGVQIDVDRCASGPHVFTKGGTEAICTVKLSHGLVYNIEFVYKFWAHKLESVKYPFSPCF
SQ  IISNNGLATTLKCFLSRPRNVNHFGHVLNIDSDVYLTKNTSVILSQDDFVKFKTNLVFSKDLDVFHSMVVFRTYLIEHRQ
SQ  ALQFLVVKPRSSKRVNSILSSVAKTASQNFILDPPRRSEETRVCIKPWTLSKKNIWTIILSLVAVVAIILKWREL
//
ID  P09280;
PN  Nuclear egress protein 2;
GN  NEC2;
OS  10338;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Nucleus Position: SL-0419;
SL  Comments: Host nucleus inner membrane {ECO:0000255|HAMAP- Rule:MF_04024}; Single-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_04024}. Note=Localizes also at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
DR  UNIPROT: P09280;
DR  Pfam: PF04541;
DE  Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04024}.
DE  Reference Proteome: Yes;
GO  GO:0044201;
GO  GO:0016021;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04024};
SQ  MSRRTYVRSERRRGCGDNLLQRIRLVVPSALQCCDGDLPIFDPQRPPARCVFQFNGEDNVSEAFPVEYIMRLMANWAQVD
SQ  CDPYIKIQNTGVSVLFQGFFFRPTNAPVAEVSIDSNNVILSSTLSTGINLSALESIKRGGGIDRRPLQALMWVNCFVRMP
SQ  YVQLSFRFMGPEDPSRTIKLMARATDAYMYKETGNNLDEYIRWRPSFRSPPENGSPNTSVQMQSDIKPALPDTQTTRVWK
SQ  LALPVANVTYALFIVIVLVVVLGAVLFWK
//
ID  B3H5K9;
PN  Protein NEDD1;
GN  NEDD1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:19383896, ECO:0000269|PubMed:25438942}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19383896}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:19383896}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:25438942}. Note=First detected in prophase on the nuclear envelope, where it appeared to cap the future spindle poles. Later detected along kinetochore microtubules (MTs) of the metaphase spindle, with more prominent signals toward the poles. In anaphase, detected with the shortening kinetochore fibers. In the developing phragmoplast, localized mainly toward the minus end of MTs. {ECO:0000269|PubMed:19383896}.
DR  UNIPROT: B3H5K9;
DR  UNIPROT: B6EUA6;
DR  UNIPROT: Q9FI89;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Regulates microtubules organization in a centrosome- independent manner. Required for the spindle to be positioned correctly and for the function of gamma-tubulin in organizing phragmoplast microtubules (PubMed:19383896). Component of active gamma-tubulin ring complexes (gamma-TuRCs) associated with cortical microtubules in interphase cells (PubMed:25438942). Mediates gamma-TuRC recruitment to the nucleation sites and is important for determining the ratio of branched to parallel nucleation (PubMed:25438942). May mediate the localization of GCP2 and GCP3 to the nuclear envelope (PubMed:19383896). {ECO:0000269|PubMed:19383896, ECO:0000269|PubMed:25438942}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0005828;
GO  GO:0005635;
GO  GO:0009524;
GO  GO:0140496;
GO  GO:0000919;
GO  GO:0009553;
GO  GO:0009555;
GO  GO:0032467;
GO  GO:0010968;
GO  GO:0060236;
GO  GO:2000694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMSNLVEPSWRLLAASGGDTVKLFDVSADSGDPCVLSYTPSPGCAVNSVKWNHTNLVVASTGEDKKISLWRKNGQSLGTV
SQ  PVTGKDGGDSAEECLSAISFSKKGSRYICSGGTGQIVKIWDLQRKLCIKKLKGHTSTITGVMYNCKDEHLASVSVGGDLI
SQ  VHNLASGARATELKDPNGQVLRLLDYSRSSRHLLVTAGDDGTVHLWDTTGRSPKMSWLKQHSAPTAGVCFSPSNEKIIAS
SQ  VGMDKKLYTYDSGSRRSSSCIAYEAPFSSLAFGDNGYILVAGTSNGRVVFYDIRGKPQPVTVLHAFSNSEDVTSLSWQTS
SQ  KPVIVNEKNYTSEMALLGSTVEDSVVIPDPLPSTTPSASQSAMAPGSRGVSASTVNASSVEQTPNRNHLWPSGPLGRLHA
SQ  LRANDSYNDDMGVFSPIIDVSSVEKWADSEGYNNKDHLVVDNKPSSLLFPSSSKGYSFGDNGSKEHPIFDWKPSSTSKQD
SQ  DPRAAFSSFGSITPTASSKSEDSALTPPEAWGGDKFSEKFNQLANEKFSDKFSHLHAPSRLAVSSTGASTSGSMFSSSRD
SQ  FPLSHGQTNFANASLEFPRIRDFSSTFETSSTQTDNNLPSSPLFTKGITAPGNIDSLRLSPNFTRRFSTYAERISTTSSF
SQ  SDGASLSLGGSPKIKKTGSETREEVLNHLLARPETVVATEAGAMPLMNQGGLKQSQTDQQQVMGSSNFTLQLFQRTLEGT
SQ  LDSFQNSIHDDVRNLHIEILRQFHMHEMEMSKVLSSILENQAEQMKELKLLRKENQELRQRL
//
ID  P12480;
PN  Protein Nef;
GN  nef;
OS  11694;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. Virion {ECO:0000250}. Secreted {ECO:0000250}. Note=Predominantly found in the paranuclear area, probably in the TGN. Correct localization requires PACS1. Also associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Also incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved (By similarity). {ECO:0000250}.
DR  UNIPROT: P12480;
DE  Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins (By similarity). {ECO:0000250}. In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network- associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase- ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection) (By similarity). {ECO:0000250}. Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis (By similarity). {ECO:0000250}. Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR- mediated death signals by blocking MAP3K5. Interacts and decreases the half-life of p53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of Bad (By similarity). {ECO:0000250}. Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0019049;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGGKWSKRSVVGWPAVR
//
ID  P12478;
PN  C-terminal core protein;
GN  nef;
OS  11683;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. Virion {ECO:0000250}. Secreted {ECO:0000250}. Note=Predominantly found in the paranuclear area, probably in the TGN. Correct localization requires PACS1. Also associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Also incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved (By similarity). {ECO:0000250}.
DR  UNIPROT: P12478;
DR  PDB: 5EO0;
DR  PDB: 5EO1;
DR  Pfam: PF00469;
DE  Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins (By similarity). {ECO:0000250}. In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network- associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase- ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection) (By similarity). {ECO:0000250}. Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis (By similarity). {ECO:0000250}. Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR- mediated death signals by blocking MAP3K5. Interacts and decreases the half-life of p53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of Bad (By similarity). {ECO:0000250}. Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0005525;
GO  GO:0017124;
GO  GO:0019049;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGGRWSKSSIVGWPAIRERIRRTDPAADGVGAVSRDLEKHGAITSSNTRGTNADCAWLEAQEESEEVGFPVRPQVPLRPM
SQ  TYKGALDLSHFLKEKGG
//
ID  P12481;
PN  Protein Nef;
GN  nef;
OS  11681;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. Virion {ECO:0000250}. Secreted {ECO:0000250}. Note=Predominantly found in the paranuclear area, probably in the TGN. Correct localization requires PACS1. Also associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Also incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved (By similarity). {ECO:0000250}.
DR  UNIPROT: P12481;
DE  Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins (By similarity). {ECO:0000250}. In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network- associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase- ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection) (By similarity). {ECO:0000250}. Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis (By similarity). {ECO:0000250}. Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR- mediated death signals by blocking MAP3K5. Interacts and decreases the half-life of p53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of Bad (By similarity). {ECO:0000250}. Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0019049;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGGKWSKSS
//
ID  Q8AIH4;
PN  Protein Nef;
GN  NEF;
OS  388910;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. Virion {ECO:0000250}. Secreted. Note=Predominantly found in the paranuclear area, probably in the TGN. Correct localization requires PACS1. Also associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Also incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8AIH4;
DR  Pfam: PF00469;
DE  Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins (By similarity). {ECO:0000250}. In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28 and probably other immunity surface molecules. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis (By similarity). {ECO:0000250}. Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0005525;
GO  GO:0017124;
GO  GO:0019049;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGNIFGRWPGARKAIEDLHNTSSEPVGQASQDLQNKGGLTTNTLGTSADVLEYSADHTEEEVGFPVRPAVPMRPMTEKLA
SQ  IDLSWFLKEKGGLDGLFFSPKRAAILDTWMYNTQGVFPDWQNYTPGPGIRYPLCRGWLFKLVPVDPPEDDEKNILLHPAC
SQ  SHGTTDPDGETLIWRFDSSLARRHIARERYPEYFK
//
ID  Q06148;
PN  Non-homologous end-joining protein 1;
GN  NEJ1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: Q06148;
DR  UNIPROT: D6VYR3;
DR  UNIPROT: Q0P6Z6;
DR  UNIPROT: Q0P6Z7;
DR  UNIPROT: Q0P707;
DR  Pfam: PF09302;
DE  Function: Involved in non-homologous end joining (NHEJ). Facilitates the transport of LIF1 into the nucleus, where it can interact with DNA ligase DNL4 to repair double-strand breaks (DSB). Mediates mating-type regulation of NHEJ. Prevents chromosome circularisation by NHEJ in absence of telomerase. {ECO:0000269|PubMed:11676923, ECO:0000269|PubMed:11701889, ECO:0000269|PubMed:11711435, ECO:0000269|PubMed:11740566, ECO:0000269|PubMed:12399380, ECO:0000269|PubMed:12769859}.
DE  Reference Proteome: Yes;
DE  Interaction: P38316; IntAct: EBI-858184; Score: 0.00
DE  Interaction: P42940; IntAct: EBI-7857152; Score: 0.40
DE  Interaction: P50277; IntAct: EBI-8220972; Score: 0.22
DE  Interaction: P53150; IntAct: EBI-1567366; Score: 0.65
DE  Interaction: P25294; IntAct: EBI-3661323; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3712698; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3727166; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3781470; Score: 0.35
DE  Interaction: P12954; IntAct: EBI-15792132; Score: 0.53
GO  GO:0005737;
GO  GO:0032807;
GO  GO:0016021;
GO  GO:0070419;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0045027;
GO  GO:0006303;
GO  GO:0045002;
GO  GO:0035825;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDSELKGQQLSDAEWCVKKINGEGNCLLLFLPMSSPTTIVMIVLVSLERLVPYVFKLSQTQLSQQCQSQGFTDSISLNLI
SQ  KLKLMDILQAPQEINQIGLVDSNLVFSFDVSADITVSINSVPSHVTKDMFYMILQSLCMLLLKLVNLSTQYHYVQRDILN
SQ  EKQKCLDFLLISLRDLDGGSKVISQWAPENSKNYESLQQCTDDDIIKKLLHKGKFQHQEFLADSLKTLLSLRNKFQDVSR
SQ  FEESGELNKKERVRFPAVNHFYNDDFELQADPTNEARPNSRGKIKPKTDFKPKSRESSTSSQLRLENFSESEATPEKTKS
SQ  SSSLVEEYPQKKRKFGKVRIKN
//
ID  Q92832;
PN  Protein kinase C-binding protein NELL1;
GN  NELL1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:21723284}. Nucleus envelope {ECO:0000269|PubMed:21723284}. Secreted {ECO:0000250}. Note=Colocalizes with ATRAID on the nuclear envelope and the perinuclear region.
DR  UNIPROT: Q92832;
DR  UNIPROT: B2CKC1;
DR  UNIPROT: Q4VB90;
DR  UNIPROT: Q4VB91;
DR  UNIPROT: Q6NSY8;
DR  UNIPROT: Q9Y472;
DR  PDB: 6POL;
DR  Pfam: PF12947;
DR  Pfam: PF07645;
DR  Pfam: PF00093;
DR  PROSITE: PS00010;
DR  PROSITE: PS00022;
DR  PROSITE: PS01186;
DR  PROSITE: PS50026;
DR  PROSITE: PS01187;
DR  PROSITE: PS01208;
DR  PROSITE: PS50184;
DR  OMIM: 602319;
DR  DisGeNET: 4745;
DE  Function: Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization. {ECO:0000269|PubMed:21723284}.
DE  Reference Proteome: Yes;
DE  Interaction: O75147; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: P00533; IntAct: EBI-8769968; Score: 0.35
DE  Interaction: P54259; IntAct: EBI-950854; Score: 0.00
DE  Interaction: Q6UW56; IntAct: EBI-7001256; Score: 0.61
DE  Interaction: Q5VTD9; IntAct: EBI-953008; Score: 0.00
DE  Interaction: O15265; IntAct: EBI-3866546; Score: 0.37
DE  Interaction: O00555; IntAct: EBI-3867376; Score: 0.37
DE  Interaction: P23588; IntAct: EBI-7001271; Score: 0.40
DE  Interaction: P68104; IntAct: EBI-7001286; Score: 0.40
DE  Interaction: O60841; IntAct: EBI-7001316; Score: 0.40
DE  Interaction: Q6IN85; IntAct: EBI-7001346; Score: 0.40
DE  Interaction: P19174; IntAct: EBI-7001331; Score: 0.40
DE  Interaction: Q9BSC4; IntAct: EBI-7001400; Score: 0.40
DE  Interaction: Q9NWH9; IntAct: EBI-7001361; Score: 0.40
DE  Interaction: Q08945; IntAct: EBI-7001415; Score: 0.40
DE  Interaction: Q5QJE6; IntAct: EBI-7001430; Score: 0.40
DE  Interaction: Q0ZGT2; IntAct: EBI-7001445; Score: 0.40
DE  Interaction: Q9WMX2; IntAct: EBI-9081118; Score: 0.37
DE  Interaction: Q6FHY5; IntAct: EBI-24468498; Score: 0.56
DE  Interaction: Q8NI29; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q9UHF1; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q9H8K7; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q9C0F1; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q9BXX0; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q96S44; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q96GJ1; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q92626; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q8N2S1; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q6IPR3; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q5BLP8; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q3ZCT1; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: Q01813; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: P55268; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: P35625; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: P23142; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: O14757; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: O00411; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: O00339; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P49639; IntAct: EBI-26512606; Score: 0.37
DE  Interaction: Q9UIS9; IntAct: EBI-26512884; Score: 0.37
DE  Interaction: Q7Z417; IntAct: EBI-26513515; Score: 0.37
GO  GO:0005737;
GO  GO:0005576;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0008201;
GO  GO:0005080;
GO  GO:0030154;
GO  GO:0033689;
GO  GO:0042177;
GO  GO:0007399;
GO  GO:0030501;
GO  GO:0045669;
GO  GO:0010468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPMDLILVVWFCVCTARTVVGFGMDPDLQMDIVTELDLVNTTLGVAQVSGMHNASKAFLFQDIEREIHAAPHVSEKLIQL
SQ  FRNKSEFTILATVQQKPSTSGVILSIRELEHSYFELESSGLRDEIRYHYIHNGKPRTEALPYRMADGQWHKVALSVSASH
SQ  LLLHVDCNRIYERVIDPPDTNLPPGINLWLGQRNQKHGLFKGIIQDGKIIFMPNGYITQCPNLNHTCPTCSDFLSLVQGI
SQ  MDLQELLAKMTAKLNYAETRLSQLENCHCEKTCQVSGLLYRDQDSWVDGDHCRNCTCKSGAVECRRMSCPPLNCSPDSLP
SQ  VHIAGQCCKVCRPKCIYGGKVLAEGQRILTKSCRECRGGVLVKITEMCPPLNCSEKDHILPENQCCRVCRGHNFCAEGPK
SQ  CGENSECKNWNTKATCECKSGYISVQGDSAYCEDIDECAAKMHYCHANTVCVNLPGLYRCDCVPGYIRVDDFSCTEHDEC
SQ  GSGQHNCDENAICTNTVQGHSCTCKPGYVGNGTICRAFCEEGCRYGGTCVAPNKCVCPSGFTGSHCEKDIDECSEGIIEC
SQ  HNHSRCVNLPGWYHCECRSGFHDDGTYSLSGESCIDIDECALRTHTCWNDSACINLAGGFDCLCPSGPSCSGDCPHEGGL
SQ  KHNGQVWTLKEDRCSVCSCKDGKIFCRRTACDCQNPSADLFCCPECDTRVTSQCLDQNGHKLYRSGDNWTHSCQQCRCLE
SQ  GEVDCWPLTCPNLSCEYTAILEGECCPRCVSDPCLADNITYDIRKTCLDSYGVSRLSGSVWTMAGSPCTTCKCKNGRVCC
SQ  SVDFECLQNN
//
ID  Q2VWQ2;
PN  Protein kinase C-binding protein NELL1;
GN  Nell1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. Secreted {ECO:0000250}. Note=Colocalizes with ATRAID on the nuclear envelope and the perinuclear region. {ECO:0000250}.
DR  UNIPROT: Q2VWQ2;
DR  Pfam: PF12947;
DR  Pfam: PF07645;
DR  Pfam: PF02210;
DR  Pfam: PF00093;
DR  PROSITE: PS00010;
DR  PROSITE: PS00022;
DR  PROSITE: PS01186;
DR  PROSITE: PS50026;
DR  PROSITE: PS01187;
DR  PROSITE: PS50025;
DR  PROSITE: PS01208;
DR  PROSITE: PS50184;
DE  Function: Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization. {ECO:0000269|PubMed:16537572}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005615;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0008201;
GO  GO:0042802;
GO  GO:0005080;
GO  GO:0030154;
GO  GO:0033689;
GO  GO:0042177;
GO  GO:0043065;
GO  GO:0030501;
GO  GO:0045778;
GO  GO:0045669;
GO  GO:0010468;
GO  GO:0045667;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPMDVILVLWFCVCTARTVLGFGMDPDLQMDIITELDLVNTTLGVTQVAGLHNASKAFLFQDVQREIHSAPHVSEKLIQL
SQ  FRNKSEFTFLATVQQKPSTSGVILSIRELEHSYFELESSGPREEIRYHYIHGGKPRTEALPYRMADGQWHKVALSVSASH
SQ  LLLHVDCNRIYERVIDPPETNLPPGSNLWLGQRNQKHGFFKGIIQDGKIIFMPNGFITQCPNLNRTCPTCSDFLSLVQGI
SQ  MDLQELLAKMTAKLNYAETRLGQLENCHCEKTCQVSGLLYRDQDSWVDGDNCRNCTCKSGAVECRRMSCPPLNCSPDSLP
SQ  VHISGQCCKVCRPKCIYGGKVLAEGQRILTKTCRECRGGVLVKITEACPPLNCSEKDHILPENQCCRVCRGHNFCAEAPK
SQ  CGENSECKNWNTKATCECKNGYISVQGNSAYCEDIDECAAKMHYCHANTVCVNLPGLYRCDCIPGYIRVDDFSCTEHDDC
SQ  GSGQHNCDKNAICTNTVQGHSCTCQPGYVGNGTVCKAFCEEGCRYGGTCVAPNKCVCPSGFTGSHCEKDIDECAEGFVEC
SQ  HNHSRCVNLPGWYHCECRSGFHDDGTYSLSGESCIDIDECALRTHTCWNDSACINLAGGFDCLCPSGPSCSGDCPHEGGL
SQ  KHNGQVWILREDRCSVCSCKDGKIFCRRTACDCQNPNVDLFCCPECDTRVTSQCLDQSGQKLYRSGDNWTHSCQQCRCLE
SQ  GEADCWPLACPSLSCEYTAIFEGECCPRCVSDPCLADNIAYDIRKTCLDSSGISRLSGAVWTMAGSPCTTCQCKNGRVCC
SQ  SVDLVCLENN
//
ID  Q62919;
PN  Protein kinase C-binding protein NELL1;
GN  Nell1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}. Secreted. Note=Colocalizes with ATRAID on the nuclear envelope and the perinuclear region. {ECO:0000250}.
DR  UNIPROT: Q62919;
DR  Pfam: PF12947;
DR  Pfam: PF07645;
DR  Pfam: PF02210;
DR  Pfam: PF00093;
DR  PROSITE: PS00010;
DR  PROSITE: PS00022;
DR  PROSITE: PS01186;
DR  PROSITE: PS50026;
DR  PROSITE: PS01187;
DR  PROSITE: PS01208;
DR  PROSITE: PS50184;
DE  Function: Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005615;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0008201;
GO  GO:0042802;
GO  GO:0005080;
GO  GO:0030154;
GO  GO:0033689;
GO  GO:0042177;
GO  GO:0043065;
GO  GO:0030501;
GO  GO:0045778;
GO  GO:0045669;
GO  GO:0010468;
GO  GO:0045667;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPMDVILVLWFCVCTARTVLGFGMDPDLQLDIISELDLVNTTLGVTQVAGLHNASKAFLFQDVQREIHSAPHVSEKLIQL
SQ  FRNKSEFTFLATVQQKPSTSGVILSIRELEHSYFELESSGPREEIRYHYIHGGKPRTEALPYRMADGQWHKVALSVSASH
SQ  LLLHIDCNRIYERVIDPPETNLPPGSNLWLGQRNQKHGFFKGIIQDGKIIFMPNGFITQCPNLNRTCPTCSDFLSLVQGI
SQ  MDLQELLAKMTAKLNYAETRLGQLENCHCEKTCQVSGLLYRDQDSWVDGDNCGNCTCKSGAVECRRMSCPPLNCSPDSLP
SQ  VHISGQCCKVCRPKCIYGGKVLAEGQRILTKTCRECRGGVLVKITEACPPLNCSAKDHILPENQCCRVCPGHNFCAEAPK
SQ  CGENSECKNWNTKATCECKNGYISVQGNSAYCEDIDECAAKMHYCHANTVCVNLPGLYRCDCVPGYIRVDDFSCTEHDDC
SQ  GSGQHNCDKNAICTNTVQGHSCTCQPGYVGNGTICKAFCEEGCRYGGTCVAPNKCVCPSGFTGSHCEKDIDECAEGFVEC
SQ  HNYSRCVNLPGWYHCECRSGFHDDGTYSLSGESCIDIDECALRTHTCWNDSACINLAGGFDCLCPSGPSCSGDCPHEGGL
SQ  KHNGQVWILREDRCSVCSCKDGKIFCRRTACDCQNPNVDLFCCPECDTRVTSQCLDQSGQKLYRSGDNWTHSCQQCRCLE
SQ  GEADCWPLACPSLGCEYTAMFEGECCPRCVSDPCLAGNIAYDIRKTCLDSFGVSRLSGAVWTMAGSPCTTCKCKNGRVCC
SQ  SVDLECIENN
//
ID  O59718;
PN  Nuclear envelope morphology protein 1;
GN  nem1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Single- pass membrane protein {ECO:0000250}.
DR  UNIPROT: O59718;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Catalytic component of the nem1-spo7 complex which acts as a phosphatase and may be required for proper nuclear membrane morphology. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0017018;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0019915;
GO  GO:0101026;
GO  GO:0071072;
GO  GO:0071763;
GO  GO:0023052;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSIARLSDEINKAILATPLDDDEADKEKLANARGRASSATLRHYNRRRSSYSASSLSSLSSKPTEKEVPTRNEKPKHAN
SQ  IMRVVVYWIRVFLKRIYTFFVHSARVFLYHFLNEEKEFTLASFFWGLCRFVFFPVLLSYKRREMLPPQPSVRRPRFYSSY
SQ  SYPSSHQDPAYSSFKRHRSSNSYSSSSNGNHVRFQPSIAEEEISFNSFSNSLNSEEDVCVSPMKPKEVSLMGKANSNRSG
SQ  HSHQPQSTQFSPPANDNISKLPSSFTIVNDPLKSPSSSRLRIRNITLCADKIPRPLLNSKLPRKTLVLDLDETLIHSVSR
SQ  GSRTTSGQPIEVHVPGEHPILYYIHKRPHLDYFLSNVSQWFRLILFTASVQPYADPIIDYLERDKKIFAKRYYRQHCALV
SQ  DSSFVKDISICNIHLSRIMIIDNSPASYNAHKENAIPIEGWISDPSDVDLLNLLSFLHALQYVHDVRDLLGLRLAK
//
ID  P38757;
PN  Nuclear envelope morphology protein 1;
GN  NEM1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9822591}; Single-pass membrane protein {ECO:0000269|PubMed:9822591}. Nucleus membrane {ECO:0000269|PubMed:9822591}; Single-pass membrane protein {ECO:0000269|PubMed:9822591}.
DR  UNIPROT: P38757;
DR  UNIPROT: D3DKU7;
DR  Pfam: PF03031;
DR  PROSITE: PS50969;
DE  Function: Catalytic component of the NEM1-SPO7 complex which acts as a phosphatase and dephosphorylates the phosphatidic acid phosphohydrolase PAH1 (PubMed:15889145). Essential for the formation of a spherical nucleus and meiotic division (PubMed:9822591). The NEM1-SPOo7 protein phosphatase is required for efficient mitophagy under prolonged respiration, as well as for reticulophagy and pexophagy (PubMed:29305265). {ECO:0000269|PubMed:15889145, ECO:0000269|PubMed:29305265, ECO:0000269|PubMed:9822591}.
DE  Reference Proteome: Yes;
DE  Interaction: P18410; IntAct: EBI-787710; Score: 0.56
DE  Interaction: P40018; IntAct: EBI-6331360; Score: 0.00
DE  Interaction: P38074; IntAct: EBI-8764817; Score: 0.37
DE  Interaction: P13712; IntAct: EBI-16251536; Score: 0.00
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005739;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0017018;
GO  GO:0004722;
GO  GO:0140042;
GO  GO:0071072;
GO  GO:0006998;
GO  GO:0046889;
GO  GO:1903740;
GO  GO:0008104;
GO  GO:0071071;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNALKYFSNHLITTKKQKKINVEVTKNQDLLGPSKEVSNKYTSHSENDCVSEVDQQYDHSSSHLKESDQNQERKNSVPKK
SQ  PKALRSILIEKIASILWALLLFLPYYLIIKPLMSLWFVFTFPLSVIERRVKHTDKRNRGSNASENELPVSSSNINDSSEK
SQ  TNPKNCNLNTIPEAVEDDLNASDEIILQRDNVKGSLLRAQSVKSRPRSYSKSELSLSNHSSSNTVFGTKRMGRFLFPKKL
SQ  IPKSVLNTQKKKKLVIDLDETLIHSASRSTTHSNSSQGHLVEVKFGLSGIRTLYFIHKRPYCDLFLTKVSKWYDLIIFTA
SQ  SMKEYADPVIDWLESSFPSSFSKRYYRSDCVLRDGVGYIKDLSIVKDSEENGKGSSSSLDDVIIIDNSPVSYAMNVDNAI
SQ  QVEGWISDPTDTDLLNLLPFLEAMRYSTDVRNILALKHGEKAFNIN
//
ID  A7MBC7;
PN  Nuclear envelope integral membrane protein 1;
GN  NEMP1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. Nucleus envelope {ECO:0000250|UniProtKB:Q6ZQE4}. Note=Colocalizes with lamins and RAN-GTP at the nuclear envelope. {ECO:0000250|UniProtKB:Q6ZQE4}.
DR  UNIPROT: A7MBC7;
DR  Pfam: PF10225;
DE  Function: Together with EMD, contributes to nuclear envelope stiffness in germ cells (By similarity). Required for female fertility (By similarity). {ECO:0000250|UniProtKB:O14524, ECO:0000250|UniProtKB:Q6ZQE4}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGGMKVAVLPAVGAGPWSWGAGGCGAVRLLLVLFGCFVCGSAGIDLNVVTLRESEILFMNTSRQSCYKNVLIPKWHDIW
SQ  TRIQIRVNSSKLVRVTQVENEDKLKELEQFSIWNFFSSFLKEKLNDTYINVGLYSTKTCLKVEILEEDTKYSVIVTRRFD
SQ  PKLFLIFLLGLTLFFCGDLLSRSQIFYYSTGMSVGIVASLLIIIFIVSKFMPKKSPIYIILVGGWSFSLYLIQLVFKNLQ
SQ  EIWRCYWQYLLSYVLAVGFMSFAVCYKYGPLENERSINLLTWTLQLLGLCFMYSSIQIPHIALAIVVIALCTKNLDYPIH
SQ  WLYITYRKMCKATEKTVPPRLLTEEEYRLQGEVETRKALEQLREYCNSPDCSAWKTVSRIQSPKRFADFVEGSFHLTPNE
SQ  VSVHEQEYGLGSIIAQDELSEETSSEEEDSDSRYPLVVQQNSFLT
//
ID  E7FE40;
PN  Nuclear envelope integral membrane protein 1;
GN  nemp1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
DR  UNIPROT: E7FE40;
DR  Pfam: PF10225;
DE  Function: Contributes to nuclear envelope stiffness in germ cells (By similarity). Involved in male and female fertility (PubMed:32923640). {ECO:0000250|UniProtKB:O14524, ECO:0000269|PubMed:32923640}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGFMKYKSVSTTIETVRLKLILTAVLFLFPFSQTSGASRPIIEIKDGQEIKVQAAQHFCYNNTIIPGWRETWTRIQVRV
SQ  WSTTKLKVTVVNDEQDLKELEHFSIWKLVQYFVREQTNETTISVSLFNNKTCFRVDPSESRTLYTVQPSRHFDIYLFLVF
SQ  LAGVLLFFYADVLSRSQVFHYSAGMSTGMIASLLILIFIVYRFLPKKSPFYMLVVGGWSFSLYIIQLVFRNLQVILTDHW
SQ  HLAIGYVFVVGFISFAVCYRYGPLVEERSINILSWALQIFGLLLVYAGIQVQQVAFAIMIAAFCSKNLEYPFNTAFMLYH
SQ  KLKPKKLEPRRLLTEEEFQRQSEVETQKALEELRKYCGSPDFNTWKTVSRLQSPKRFADFIEGSPHLLSNEVSVHMQEYG
SQ  LGGSFFEDELFSTDEEDKEEEEDGWETEDDIKPEVTSPRMNNTRGK
//
ID  O14524;
PN  Nuclear envelope integral membrane protein 1;
GN  NEMP1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. Nucleus envelope {ECO:0000250|UniProtKB:Q6ZQE4}. Note=Colocalizes with lamins and RAN-GTP at the nuclear envelope. {ECO:0000250|UniProtKB:Q6ZQE4}.
DR  UNIPROT: O14524;
DR  UNIPROT: Q17R72;
DR  UNIPROT: Q68DH0;
DR  UNIPROT: Q6IQ25;
DR  Pfam: PF10225;
DR  OMIM: 616496;
DR  DisGeNET: 23306;
DE  Function: Together with EMD, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). Required for female fertility (By similarity). {ECO:0000250|UniProtKB:Q6ZQE4, ECO:0000269|PubMed:32923640}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A6H3AKG3; IntAct: EBI-2826538; Score: 0.00
DE  Interaction: Q12952; IntAct: EBI-11318689; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6ZNC8; IntAct: EBI-11121915; Score: 0.35
DE  Interaction: Q9Y6G1; IntAct: EBI-24659878; Score: 0.56
DE  Interaction: Q86UF1; IntAct: EBI-24660066; Score: 0.56
DE  Interaction: Q15848; IntAct: EBI-23677731; Score: 0.56
DE  Interaction: Q96PS8; IntAct: EBI-24670298; Score: 0.56
DE  Interaction: A0PK11; IntAct: EBI-24685606; Score: 0.56
DE  Interaction: P54315; IntAct: EBI-24691337; Score: 0.56
DE  Interaction: Q9BXN2; IntAct: EBI-23735883; Score: 0.56
DE  Interaction: Q5BJF2; IntAct: EBI-24702243; Score: 0.56
DE  Interaction: P01031; IntAct: EBI-24710670; Score: 0.56
DE  Interaction: Q69YG0; IntAct: EBI-23757171; Score: 0.56
DE  Interaction: Q8NBD8; IntAct: EBI-23775909; Score: 0.56
DE  Interaction: Q86Y82; IntAct: EBI-24726194; Score: 0.56
DE  Interaction: Q9Y5U4; IntAct: EBI-24727065; Score: 0.56
DE  Interaction: Q5BVD1; IntAct: EBI-23788982; Score: 0.56
DE  Interaction: O75841; IntAct: EBI-23811148; Score: 0.56
DE  Interaction: Q07325; IntAct: EBI-23826105; Score: 0.56
DE  Interaction: Q9NPR9; IntAct: EBI-24757439; Score: 0.56
DE  Interaction: Q02747; IntAct: EBI-24769561; Score: 0.56
DE  Interaction: Q8TBE1; IntAct: EBI-24778423; Score: 0.56
DE  Interaction: Q8N661; IntAct: EBI-23881612; Score: 0.56
DE  Interaction: Q15836; IntAct: EBI-24784453; Score: 0.56
DE  Interaction: Q14162; IntAct: EBI-25284656; Score: 0.56
DE  Interaction: Q5QGT7; IntAct: EBI-25286161; Score: 0.56
DE  Interaction: Q96IV6; IntAct: EBI-24746528; Score: 0.56
DE  Interaction: P07306; IntAct: EBI-24775456; Score: 0.56
DE  Interaction: Q71RG4; IntAct: EBI-24788045; Score: 0.56
DE  Interaction: P29400; IntAct: EBI-25202447; Score: 0.56
DE  Interaction: P60033; IntAct: EBI-24799557; Score: 0.56
DE  Interaction: Q6PL45; IntAct: EBI-25271145; Score: 0.56
DE  Interaction: Q8N6R1; IntAct: EBI-25271350; Score: 0.56
DE  Interaction: P62826; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: P61769; IntAct: EBI-21675069; Score: 0.35
DE  Interaction: Q9Y2X3; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: Q9NVU7; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: Q99666; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: Q709F0; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P0DJD1; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: Q15398; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P78356; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P50579; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P48426; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P48167; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P46060; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: O60503; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: O14715; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16789004; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: P35712; IntAct: EBI-29730925; Score: 0.27
DE  Interaction: P48436; IntAct: EBI-29732788; Score: 0.27
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGGMKVAVSPAVGPGPWGSGVGGGGTVRLLLILSGCLVYGTAETDVNVVMLQESQVCEKRASQQFCYTNVLIPKWHDIW
SQ  TRIQIRVNSSRLVRVTQVENEEKLKELEQFSIWNFFSSFLKEKLNDTYVNVGLYSTKTCLKVEIIEKDTKYSVIVIRRFD
SQ  PKLFLVFLLGLMLFFCGDLLSRSQIFYYSTGMTVGIVASLLIIIFILSKFMPKKSPIYVILVGGWSFSLYLIQLVFKNLQ
SQ  EIWRCYWQYLLSYVLTVGFMSFAVCYKYGPLENERSINLLTWTLQLMGLCFMYSGIQIPHIALAIIIIALCTKNLEHPIQ
SQ  WLYITCRKVCKGAEKPVPPRLLTEEEYRIQGEVETRKALEELREFCNSPDCSAWKTVSRIQSPKRFADFVEGSSHLTPNE
SQ  VSVHEQEYGLGSIIAQDEIYEEASSEEEDSYSRCPAITQNNFLT
//
ID  Q6ZQE4;
PN  Nuclear envelope integral membrane protein 1;
GN  Nemp1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:25946333}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. Nucleus envelope {ECO:0000269|PubMed:25946333}. Note=Colocalizes with lamins and RAN-GTP at the nuclear envelope. {ECO:0000269|PubMed:25946333}.
DR  UNIPROT: Q6ZQE4;
DR  Pfam: PF10225;
DE  Function: Together with EMD, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). Required for female fertility (PubMed:32923640). {ECO:0000269|PubMed:32923640}.
DE  Reference Proteome: Yes;
DE  Interaction: P62827; IntAct: EBI-12595973; Score: 0.60
DE  Interaction: P63280; IntAct: EBI-12598469; Score: 0.37
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGGIKVSVWSAVGPGPRCWGAGGGGGATWLLLVVAGCVVCGSADVNVVMLQESQVDMNSSQQFCYKNVLIPKWHDIWTR
SQ  IQVRVNSSKLVRVTQVDNEEKLKELEQFSIWNFFSSFLKEKLNDTYVNVGLYSTKTCLKVEMIEKDTTYSVTVTRRFDPK
SQ  LFLVFLLGLTLFFCGDLLSRSQIFYYSTGMSVGIVASLLIVIFMISKFMPKRSPIYVILVGGWSFSLYLIQLVFKNLQEI
SQ  WRSYWHYLLSYILTVGFMSFAVCYKYGPLENERSINLLTWTLQLLGLGLMYSSIQIPHVAFALIVIALCTKNLEYPIHWL
SQ  CSTYRRMCKASGKPVPPRLLTEEEYRIQGEVETQKALQELREFCNSPECSAWKTISRIQSPKRFADFVEGSFHLTPNEVS
SQ  VHEQEYGLGSIFTQDEELSSEEEGSEYPTFTQNNFLT
//
ID  Q5RDB4;
PN  Nuclear envelope integral membrane protein 1;
GN  NEMP1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. Nucleus envelope {ECO:0000250|UniProtKB:Q6ZQE4}. Note=Colocalizes with lamins and RAN-GTP at the nuclear envelope. {ECO:0000250|UniProtKB:Q6ZQE4}.
DR  UNIPROT: Q5RDB4;
DR  Pfam: PF10225;
DE  Function: Together with EMD, contributes to nuclear envelope stiffness in germ cells (By similarity). Required for female fertility (By similarity). {ECO:0000250|UniProtKB:O14524, ECO:0000250|UniProtKB:Q6ZQE4}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGGMKVAVSPAVGPGPWGSGVGGGGTVRLLLILSGCLVYGTAEIDVNVVMLQESQVCEKRASQQFCYTNVLIPKWHDIW
SQ  TRIQIRVNSSKLVRVTQVENEQKLKELEQFSIWNFFSSFLKEKLNDTYVNVGLYSTKTCLKVEIIEKDTKYSVIVIRRFD
SQ  PKLFLVFLLGLMLFFCGDLLSRSQIFYYSTGMSVGIVASLLIIIFILSKFMPKKSPIYVILVGGWSFSLYLIQLVFKNLQ
SQ  EIWRCYWQYLLSYILTVGFMSFAVCYKYGPLENERSIDLLTWTLQLMGLCFMYSGIQIPHIALAIIIIALCTKNLEYPIQ
SQ  WLYITYRKVCKAAEKPVPPRLLTEEEYRIQGEVETRKALEELREFCNSPDCSAWKTVSRIQSPKRFADFVEGSSHLTPNE
SQ  VSVHEQEYGLGSIIAQDEIYEEASSEEEDSYSRCPAITQNNFLT
//
ID  Q28EH9;
PN  Nuclear envelope integral membrane protein 1;
GN  nemp1;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:B9X187}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. Nucleus envelope {ECO:0000250|UniProtKB:B9X187}. Note=Localization in the nuclear membrane is essential for its function. Colocalizes with and lamins and banf1-a/b at the nuclear envelope. {ECO:0000250|UniProtKB:B9X187}.
DR  UNIPROT: Q28EH9;
DR  UNIPROT: Q5BJ84;
DR  Pfam: PF10225;
DE  Function: In concert with ran, required for proper eye development. May be involved in the expression of early eye marker genes. Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (By similarity). {ECO:0000250|UniProtKB:B9X187, ECO:0000250|UniProtKB:O14524}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0001654;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGEVEGEGCRVSWGVLVALLLLPLPSLCSLTAGKQLQVIKLFEGRVVRYNESKNFCYQRTYEPKWSDVWTKIQIRVNST
SQ  KMIRVTQVENEEKLKEMETFNMFDFFSSFLKEKLNDSFIYVDLYNNKTCIKVHVSDTDTYYSVALSRGFDPRLFFVFLCG
SQ  LLLFFYGDTLSRSQIFYYSTGITVGMLASMLILVFMLSKLMPKKSPFVALLLGGWSVSIYVIQLVFKNLQAICTEYWQYL
SQ  LGYLGIVGFVSFAFCYKYGPLENERSINILNWTLQLIGLLLMYISVQIRHIAVTMVVIAFCTKQIEYPVRWIYILYRKIK
SQ  LKRGKPSPPRLLTEEEYRKQGDVETRKALEELRGYCSSPDFAAWKTVSRIQSPKRFADFVEGSSHLTPNEVSVHEHEYGF
SQ  GGSFLEDELFGEDSDVEEEMEIEPVLYQDLR
//
ID  Q5ZJY9;
PN  Nuclear envelope integral membrane protein 2;
GN  NEMP2;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
DR  UNIPROT: Q5ZJY9;
DR  Pfam: PF10225;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGPRRLPWARPGPALGLLLLALAGAVPAAGGSCSLLEEGNTIQKLHEDCFCYVQNRTMHLQYIWSTVQVKINSTRTFRFV
SQ  PTPEKSNCRNSETVFEFAACAVQILWRPETSTETFLKIKQYGEDFCFRIQPFKEELYTVSMTREMLDGKLLFLFAAGIFL
SQ  FHFANSLSRSTNFFYLSGIILGVLALLVFVLLALKRFIPRRSTFWILLSGCWMSSLYLIYCFKENMQWLWSEHRIYVLGY
SQ  FVAVGTLSFATCYQHGPLTSELSITLFTWTLQLTAFVFIYCGVNIPQVAYAIIAVKPSPKGLGYPPAAAWHIGRKMKNHF
SQ  QSKKVVVRCLTEEEYREQGETETVRALEELRSFCKNPDFSSWLAVSKLQSPHRFAGFVLGSPHVSPAETKAHDEEYGIGS
SQ  SFLEEQLFETRTESEQDETTSYIHEGDDENEDEIHEPISFPYATELL
//
ID  F1QYC4;
PN  Nuclear envelope integral membrane protein 2;
GN  nemp2;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
DR  UNIPROT: F1QYC4;
DR  Pfam: PF10225;
DE  Function: Contributes to nuclear envelope stiffness in germ cells (By similarity). Involved in male and female fertility (PubMed:32923640). {ECO:0000250|UniProtKB:O14524, ECO:0000269|PubMed:32923640}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEKLAAFILVLTLLCAYWQSAEGIREYSYADCTDVKGDSAHRYSGSRCFCYSPGTVIKWKDIWSTFKVNVSSNVDVVVVF
SQ  PMETINCHHPDDLLTVMNCFVEHYWPSTVQRETSLEIPLVDVDICFMIKSPRSNTEYTLHVSNKRLNRMCFLLFVCGLIL
SQ  FFGARNICRSSLFFYTTGVSLGIIATFVFLTLLLRNFVPKRGLFLVLLGAGSGLSYMGIQRVLNEWDDIVTEHWMELLAY
SQ  VLISGLFSFAVCYKHGPITNKHTLNFMTCSMQAVGIVLLYYGITFPPAYFVLVAVLLCWKILPLAWSLLMGICSLFYSFL
SQ  ALFRRRRRPTVRLLTEEEYREQGEIHTRASLDELREYCNRPGFPAWETVLRLRSPQRFAEFLRQGSHITQEEHQNHENHY
SQ  GLGGAYYENVIFNNSSSSDTQSHREEAEDNSEDEIVGNSPPVLNNLPSPTIYPPTICPYPPVTYTPQPEPLDPEDQDFF
//
ID  A6NFY4;
PN  Nuclear envelope integral membrane protein 2;
GN  NEMP2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
DR  UNIPROT: A6NFY4;
DR  UNIPROT: B4DYG6;
DR  Pfam: PF10225;
DR  OMIM: 616497;
DR  DisGeNET: 100131211;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P62826; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: Q9Y490; IntAct: EBI-30823757; Score: 0.44
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGPRQGRWWLLLWLPPLATLPVRGEAAAAALSVRRCKALKEKDLIRTSESDCYCYNQNSQVEWKYIWSTMQVKITSPGLF
SQ  RIVYIAERHNCQYPENILSFIKCVIHNFWIPKESNEITIIINPYRETVCFSVEPVKKIFNYMIHVNRNIMDFKLFLVFVA
SQ  GVFLFFYARTLSQSPTFYYSSGTVLGVLMTLVFVLLLVKRFIPKYSTFWALMVGCWFASVYIVCQLMEDLKWLWYENRIY
SQ  VLGYVLIVGFFSFVVCYKHGPLADDRSRSLLMWMLRLLSLVLVYAGVAVPQFAYAAIILLMSSWSLHYPLRACSYMRWKM
SQ  EQWFTSKELVVKYLTEDEYREQADAETNSALEELRRACRKPDFPSWLVVSRLHTPSKFADFVLGGSHLSPEEISLHEEQY
SQ  GLGGAFLEEQLFNPSTA
//
ID  Q8CB65;
PN  Nuclear envelope integral membrane protein 2;
GN  Nemp2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
DR  UNIPROT: Q8CB65;
DR  UNIPROT: Q8C844;
DR  Pfam: PF10225;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLPRLWWLVLWLQPLATLPASAVHDEEAAMSVPRCKSLKETDLIKTSVSDCYCYNQHSQIQWTYMWSTVQVTVTSPGLLN
SQ  IVYITGSHNCQHTESILSFIKCVTHNFWAPEEAEEITIVFSPYGETVCFSVKPVGRLLPYIVSVSRNIVDFKLFLVFVTG
SQ  IFLFLYAKTLSQSPVFYYSSGTVLGILMTLVFVLLMAKKHIPKYSTFGALMIGCWFASVYVLCQLMEDLKWLWYGNRMYI
SQ  LGYVVVVGLCSFAACYSHGPLADEGSRDLLMWTLRLFSLALVYTGVAAPQFAYAVLIVLLFSWSLHYLLRAFSYLRWKMR
SQ  PWFTAEPQVARYLTDDEYREQAEAATARALEELRQACCRPDFPSWLAVSRLQAPKKFAEFVLGASHLSPEEVSTHEKQYG
SQ  LGGAFLEEQLFSLQTDSLPAS
//
ID  P0C8N6;
PN  Nuclear envelope integral membrane protein 2;
GN  Nemp2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
DR  UNIPROT: P0C8N6;
DR  Pfam: PF10225;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPPGSWWLVLWLPPLATLPAGAVPQEEAAMSVPRCKSLKETDLIKTSVSDCYCYNQHSQIEWTYMWSTVQVTVTSPGLLS
SQ  IVYITGRHTCQHTETILSFLKCVTHNFWTAEEAKEVTIVFSPYGETVCFSVKPVGSLLTYAVSVNRNVVDFRLFLVFATG
SQ  IFLFFYAKTLSQSPVFYYSSGTVLGILMTLVFVLLMTKKHIPKYSTFGALMIGCWFASVYVLCQLMENLKWLWCGNRIYV
SQ  LGYVLVVGLCSFSACYSRGPPADEGSRDLLMWALRFLSLVLVYTGMAISQFAYAVMILLLLSWTRHYLLRAFSCLRWKVR
SQ  QWFATRALVVRYLTDDEYREQAEAETASALEELRQACCRPDFPSWLAVSRLQAPKKFAEFVLGASHLSPEEVSTHEKQYG
SQ  LGGAFLEEQLFSLQTESLPAS
//
ID  Q19293;
PN  Nuclear envelope integral membrane protein;
GN  nemp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
DR  UNIPROT: Q19293;
DR  Pfam: PF10225;
DE  Function: Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (PubMed:32923640). {ECO:0000250|UniProtKB:O14524, ECO:0000269|PubMed:32923640}.
DE  Reference Proteome: Yes;
DE  Interaction: O17915; IntAct: EBI-338738; Score: 0.00
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRLLTLALLVAGSLAYKFEDCEQKPAALNQVLRVGAKLYSYNLDFFYQKALPYNAIYAFTDVFLQTNLTNADQYQFYQGT
SQ  NCTTVQQLYDNDNRYFGILRKAALLRSHQLNPFNDTIVGVSTTEPYEISVLIWKVNYFRVGVYVGAIVLFLLASKLVRNV
SQ  VFYYTSGCSFGLLASLLLVAFIVWRVAPKKTIGVPILIGGWSVSLYMLHFAWSNLQSIMIEYQKYVIGYFATVLLISMAV
SQ  CYKRGPPTDARSHDIAQWTLQLVALALIYFSVQMVEVSTGTIGALIIQQICRGFLFAGIRWYFVGLKAVWRKFFPARRRL
SQ  LNEEEYEEQAEKTTKEQLAQLREYCKKEGNRPWKIAGNVRSARRLARFIEGEDDHITEDEIYAHELTGDVLDDEDYDFNE
SQ  DYGLRTPNESHFDLEDDEDGAEEWDEVVVRRRASEYGRDSVQSVRVPRSVSSRLLSPYQGQNHMNRSLGPGIGFRRDSTP
SQ  RHGNFQSEHRPRMPRTEQIYRSRRVEYDVKNGRVEGPSSSTASGMTPSEYMRKARRIDATSKTPTRKSRHPTESEDADE
//
ID  Q9VXD6;
PN  Nuclear envelope integral membrane protein;
GN  Nemp;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:32923640}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}.
DR  UNIPROT: Q9VXD6;
DR  Pfam: PF10225;
DE  Function: Contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). Required for male and female fertility (PubMed:32923640). {ECO:0000269|PubMed:32923640}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O97365; IntAct: EBI-280446; Score: 0.00
DE  Interaction: Q29R10; IntAct: EBI-284034; Score: 0.00
DE  Interaction: P33450; IntAct: EBI-9991526; Score: 0.37
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MHSAGLLMLTVAGYFTSGIPGNTASSDVAYLTPGTYINLSENILGLQTLRTFCYPGKRLTVSSLFETVEFVLAIGSDDYS
SQ  QYGGKTPEEVLQHYKDKQSLFSITLFAQKRQLLQLSPFEQQCIGISSRQAYTVILNSIPLDLWRLAQFAVGILILFSARR
SQ  LAKNSVFYYLVGIVIGICASLLVVIYLAAKLFPRRTMMYGVLIGGWTIGFYVIKQLADNLRLILITYRDHVLGYLVITGL
SQ  ISFLICYRIGPPKNPRSQTIVMWVLQAIGAVMAYFSSWHTSAVIFIMVLVFVAHYFPISWTNQIKFMYRRRFPLKRRMLT
SQ  QEEYEQQTAVETSKSLADLRKYVNSPECKQWAVMGKLRDPLRFASFANGAPHLDDEEIEDHSRTIEESMDAAPEEESVEE
SQ  PEEDKPAELLPLPNSQFRYQQAARNSEPEPESESDDSEEEEFFEQEVDLRQVVQ
//
ID  Q3ZBP2;
PN  Nuclear envelope phosphatase-regulatory subunit 1;
GN  CNEP1R1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Filamentous pattern in the cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q3ZBP2;
DR  Pfam: PF09771;
DE  Function: Forms with the serine/threonine protein phosphatase CTDNEP1 an active complex which dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSLEQAEDLKAFERRLTEYIHCLQPATGRWRMLLIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGL
SQ  FFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ
//
ID  Q9XXN3;
PN  Nuclear envelope phosphatase-regulatory subunit 1 homolog;
GN  nepr;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q8N9A8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8N9A8}. Cytoplasm {ECO:0000250|UniProtKB:Q8N9A8}.
DR  UNIPROT: Q9XXN3;
DR  Pfam: PF09771;
DE  Function: May form with the serine/threonine protein phosphatase scpl-2 an active complex dephosphorylating and activating lipin-like phosphatases. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May play a role in nuclear membrane dynamics being crucial for early development of the embryo. {ECO:0000269|PubMed:22134922}.
DE  Reference Proteome: Yes;
DE  Interaction: O45734; IntAct: EBI-341939; Score: 0.00
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
GO  GO:0051783;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAIQARRMPEDPSTACEDLKFFEKRLTEVITYMGPTCTRWRIAIVIFAVLVGVIGSKYFANEKIEIFQIPMIDMFLTTHL
SQ  DFTLCFFVGLLLFAVFGVHRRIVAPTIVARRCRDALSPFSLSCDHNGKLIVKPAVRNSAP
//
ID  Q561X0;
PN  Nuclear envelope phosphatase-regulatory subunit 1;
GN  cnep1r1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
DR  UNIPROT: Q561X0;
DR  Pfam: PF09771;
DE  Function: May form with the serine/threonine protein phosphatase ctdnep1 an active complex dephosphorylating and activating lipins. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSLEQAEDLKAFERRLTEYVSCLQPATGRWRMILIVVSVCTATGAWNWLIDPDTQKVSFFSSLWNHPFFTISCVTLIGL
SQ  FFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHIQ
//
ID  Q8T0B1;
PN  Nuclear envelope phosphatase-regulatory subunit 1 homolog;
GN  CG8009;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
DR  UNIPROT: Q8T0B1;
DR  UNIPROT: Q9VTA4;
DR  Pfam: PF09771;
DE  Function: May form with the serine/threonine protein phosphatase l(1)G0269 an active complex dephosphorylating and activating lipin-like phosphatases. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VDS3; IntAct: EBI-26746382; Score: 0.49
DE  Interaction: Q6AWP0; IntAct: EBI-26770829; Score: 0.49
GO  GO:0005737;
GO  GO:0030176;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEPSACEDLKAFERRLTEVVSSYRPSTFRWRKLLAVVLSAMSMCTAISAWYWLRDPRTTVVPLTESLWIHPVFTVATLTL
SQ  VVLFILGIQKLVIAPQIITSRTRMVLGDFNMSCDDTGKLILKPRQSNNNST
//
ID  Q8N9A8;
PN  Nuclear envelope phosphatase-regulatory subunit 1;
GN  CNEP1R1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:22134922}; Multi-pass membrane protein {ECO:0000269|PubMed:22134922}. Cytoplasm {ECO:0000269|PubMed:22134922}. Note=Filamentous pattern in the cytoplasm.
DR  UNIPROT: Q8N9A8;
DR  UNIPROT: Q4G1A9;
DR  UNIPROT: Q5H9V0;
DR  UNIPROT: Q8NE06;
DR  Pfam: PF09771;
DE  Function: Forms with the serine/threonine protein phosphatase CTDNEP1 an active complex which dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. {ECO:0000269|PubMed:22134922}.
DE  Reference Proteome: Yes;
DE  Interaction: O95476; IntAct: EBI-5323532; Score: 0.46
DE  Interaction: P03372; IntAct: EBI-21302175; Score: 0.35
DE  Interaction: A2ICZ0; IntAct: EBI-25685386; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSLEQAEDLKAFERRLTEYIHCLQPATGRWRMLLIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGL
SQ  FFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ
//
ID  Q3UJ81;
PN  Nuclear envelope phosphatase-regulatory subunit 1;
GN  Cnep1r1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Filamentous pattern in the cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q3UJ81;
DR  UNIPROT: A7E1Z4;
DR  UNIPROT: Q8VEG8;
DR  UNIPROT: Q9D3Q4;
DR  Pfam: PF09771;
DE  Function: Forms with the serine/threonine protein phosphatase CTDNEP1 an active complex which dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSLEQAEDLKAFERRLTEYIHCLQPATGRWRMLLIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGL
SQ  FFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ
//
ID  Q5R7J7;
PN  Nuclear envelope phosphatase-regulatory subunit 1;
GN  CNEP1R1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Filamentous pattern in the cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q5R7J7;
DR  Pfam: PF09771;
DE  Function: Forms with the serine/threonine protein phosphatase CTDNEP1 an active complex which dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSLEQAEDLKAFERRLTEYIHCLQPATGRWRMLLIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGL
SQ  FFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ
//
ID  Q7ZY85;
PN  Nuclear envelope phosphatase-regulatory subunit 1;
GN  cnep1r1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
DR  UNIPROT: Q7ZY85;
DR  Pfam: PF09771;
DE  Function: May form with the serine/threonine protein phosphatase ctdnep1 an active complex dephosphorylating and activating lipins. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSLEQAEDLKAFERRLTEYVSCLQPTTGRWRMLLIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGL
SQ  FFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ
//
ID  Q5M8F7;
PN  Nuclear envelope phosphatase-regulatory subunit 1;
GN  cnep1r1;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
DR  UNIPROT: Q5M8F7;
DR  Pfam: PF09771;
DE  Function: May form with the serine/threonine protein phosphatase ctdnep1 an active complex dephosphorylating and activating lipins. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0006629;
GO  GO:0035307;
GO  GO:0010867;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSLEQAEDLKAFERRLTEYVSCLQPATGRWRMILIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGL
SQ  FFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ
//
ID  Q66GR8;
PN  Protein NETWORKED 3A;
GN  NET3A;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22840520}. Nucleus membrane {ECO:0000269|PubMed:22840520}.
DR  UNIPROT: Q66GR8;
DR  UNIPROT: Q67ZU6;
DR  UNIPROT: Q9LR76;
DR  Pfam: PF07765;
DR  PROSITE: PS51774;
DE  Function: Plant-specific actin binding protein. May be part of a membrane-cytoskeletal adapter complex. {ECO:0000305|PubMed:22840520}.
DE  Reference Proteome: Yes;
GO  GO:0005856;
GO  GO:0031965;
GO  GO:0005774;
GO  GO:0003779;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVMDSSKWWWIGNHNTTNFSPWLHSTLSELDEKTKEMLRVIDEDADSFAARAEMYYKKRPELIAMVEEFYRSHRSLAERY
SQ  DLLRPSSVHKHGSDSESHEKSSTCDESSWSEACETHEEYAESEIDNGESKWVDESEIDGIVEEIEPSEVVYSEGNGNSEM
SQ  MKIEIERLREENKVYSEMVREKDEEKREAIRQMSVAIQMLKEENSELKKRVTNTVVARRNKEGGDSQRKQQMWKPFEFKK
SQ  IKLEGLWGKGFGNWALPNTDSTSKELMTL
//
ID  Q24568;
PN  Netrin-B;
GN  NetB;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:29513217}. Note=Expressed in the perinuclear region of the oldest most anterior lamina neurons at 24 hours after puparium formation. {ECO:0000269|PubMed:29513217}.
DR  UNIPROT: Q24568;
DR  UNIPROT: Q9VY23;
DR  Pfam: PF00053;
DR  Pfam: PF00055;
DR  Pfam: PF01759;
DR  PROSITE: PS00022;
DR  PROSITE: PS01248;
DR  PROSITE: PS50027;
DR  PROSITE: PS51117;
DR  PROSITE: PS50189;
DE  Function: Netrins control guidance of CNS commissural axons and peripheral motor axons (PubMed:8780645, PubMed:8780646, PubMed:11719202). Its association with either fra or unc-5 receptors will lead to axon attraction or repulsion, respectively (PubMed:11719202). While short-range repulsion requires both fra and unc-5 receptors, long-range repulsion only requires unc-5 (PubMed:11719202). {ECO:0000269|PubMed:11719202, ECO:0000269|PubMed:8780645, ECO:0000269|PubMed:8780646}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A0B4K859; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P20240; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P49021; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q24246; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q94538; IntAct: EBI-6895157; Score: 0.40
DE  Interaction: P31368; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VJA9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V3E7; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VL48; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P05130; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q8IML5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W263; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z7K2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VA23; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VK08; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q960V3; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q7KML4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: M9NE38; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W4Z9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q00174; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P17672; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VH64; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VLC0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VYS3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7K2X1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VH20; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q95R34; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VF72; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VGI8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VGW4; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W3E1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KVD1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q8SX76; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P48608; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VE94; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VEX6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P39770; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q86B49; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VY43; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VZF5; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q8IQ71; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VK35; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9U969; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IQI2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPG1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VZI3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8SWT2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P11046; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V3H9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZBL7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VSA4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9U5L1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W0T1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q8T4D6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VLY7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VZY3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IP51; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P07207; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VQI9; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9I7M8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VCP0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P24014; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z8N1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P48610; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KTL4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VXM5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9XZ21; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VQ08; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPL5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VIJ0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q86BB1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VGI6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V3R1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P00522; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VBF5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P13217; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KTT0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VBL3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z9G1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IMA6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VN57; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VS62; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O16102; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O61366; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9NFV8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P42787; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P18490; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9V769; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O18475; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VSK9; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q7JR82; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W391; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q8T421; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V3Y8; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: A1ZAE2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8INT5; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q4V4S9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VG73; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q86B91; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VZS7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IR22; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P26019; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPW5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VJX4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VKG0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P20659; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VVQ9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IPN1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KNQ9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VS41; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VSG7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VXY2; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P05084; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KT06; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O76464; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O97159; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W5E0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VY05; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VB11; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: A1ZBH5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VWR5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VD51; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P18171; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W5E8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O18388; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IQ27; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VCN1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q8IR12; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P13496; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VZK8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q1EBX4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q0E8J0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8MSU4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VNA1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W1G0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P16568; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VM67; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q01820; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VRX7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9Y105; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VJ14; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VUS0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z8S6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W2I5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VAT1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9V3E9; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VQV3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7JQ32; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W4X4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P04197; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VD22; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q967S0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VWH5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VUH9; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VWC0; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VIP9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W3J0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VSE8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W021; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VDA0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VZ81; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VQ54; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IRL2; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q8INH7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IRR2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9I7F7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VK58; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9I7R5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VVB5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZAH1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W0D3; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VES5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VMS3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W1N6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q86NK9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IR23; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z700; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VUH5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W3H8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P12428; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IRV8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IN06; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VSM1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VA45; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W0X7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPI9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VC62; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VP22; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VCJ9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: X2JDY8; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q86B80; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V4C8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VL65; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q27237; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPS7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q86B52; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P22814; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IRD5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P25439; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P20354; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VN82; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VYW3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8SYD9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPX3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VEX0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9XYA7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KSD3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZAJ8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VKM1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9XYU0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VZT7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VAG2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8MT77; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VJ30; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VB72; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W350; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VRM7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VT19; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W002; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W2N0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VXW9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VQ76; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W0T7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W1H0; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q7KV92; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VU16; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P28750; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VQ79; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VWF2; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P26675; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W484; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q86LG9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W2P0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q95V55; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z7J0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VI17; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KTX4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VXA3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8MS59; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VW51; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P34739; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VA73; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: A1Z7Z9; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P52034; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VW97; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V9Q2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W4H1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W0L7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8I0P1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z9W4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPR0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VFE4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P13677; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VYK6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VP76; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P18502; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q7JQY8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IN10; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VEP3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VG60; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9XZ22; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P25159; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IPV3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9U6R9; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q00449; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VAW1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W4A9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VN28; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q0E9C5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VP05; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P15215; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VUA0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VRV9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KTW9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P22813; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W3B8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P26016; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q95TY8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V9N5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VXD6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VWE6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZBA1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W345; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W3D1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W0E8; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VPH4; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VZ60; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q24113; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: M9PIS3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V410; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VU94; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VBJ2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P28466; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VV61; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q86BR6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q24325; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: C0PUW9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A8WHJ2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q86NV3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZAU8; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W106; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VJ03; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VJJ8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W4F6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VVK6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W4E4; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: O15943; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VXL9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VK06; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VC89; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q59DV6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IPG1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W1L7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VM93; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P54398; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P18106; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VF33; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z7D2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z8J5; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VXW2; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9V4B2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VTU0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPA1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P00967; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KVY9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W1C5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W3J6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VXV3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VC66; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9NB04; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V430; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9I7L9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VHD0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VU43; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VEZ5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPL3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZAL4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VSZ4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VGN4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8WTI8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VF03; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VZM9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P18167; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q6AWJ9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZAN6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W2D5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VK89; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VAQ1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VZX7; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W457; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VT40; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VVK7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VXG1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q59DP9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IR50; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z9J1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VDQ7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W420; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VL71; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VH96; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V3J1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VH71; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VXE6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VW37; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W3R8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VSM7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O61602; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VTV9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VCH5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VYY4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VZ00; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VE08; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7JUN3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W2Y5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q59DP4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VAQ5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VU84; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VQS0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VY54; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W425; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P25455; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q0E996; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q95U58; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W3R9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O46072; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8INC1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8SX24; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZA87; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P54367; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V3Z3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZAV3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VIF5; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P54351; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q24270; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VY10; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W3X0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W1A9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V463; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VQV6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VMN5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VMG8; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VZE8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q86BH1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q7KV70; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8T3J1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VI07; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7JXU4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q24595; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q95SK9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VCX2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VE80; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q04691; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VV79; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VCB7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPC7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9XZ32; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZBN5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VCJ3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z8Q9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W0J2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q5U154; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZAW3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z773; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VLW7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W378; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IPJ5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VWV5; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9V853; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W289; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W2W2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VRJ1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W0R3; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VX18; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1ZAC7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q26307; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VU88; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q0E9G3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W198; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VX80; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q7KN85; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W433; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VPH9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VU91; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q6WV17; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q03042; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q86BY9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P55824; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9TVP3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VQR0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VYK0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9I7T2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VWN1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q1EC46; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VX91; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q86B47; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VIU8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VE86; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VGH5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W1J9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VX63; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P16620; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O76462; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VSS2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VFJ2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8SWU7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KUG5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P22769; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VEN2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VGG5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V3I5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VJB6; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VQP5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P13607; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8MSX1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: O96433; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VZX9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VCE0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q23976; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VIU5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VM08; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q23983; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7JVY0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9XZ25; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8INM3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9NII1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P20028; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VMP4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A8JUV0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W018; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8SX83; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9V3K3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VLB3; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q8MT36; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P05990; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P51406; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V9V7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VE00; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VGY2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9U1H0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z6S0; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9W490; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VRB3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VUZ2; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q24573; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VQE5; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VYT8; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: A1Z8W1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9V460; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q24298; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q59E61; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q0E9C6; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q7KVP6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9W2P1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VCD1; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VB25; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VTZ1; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: P91660; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q8IGR0; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7JUX9; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V3D6; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VC54; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q59DW9; IntAct: EBI-9919289; Score: 0.46
DE  Interaction: Q9VNT3; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7K3W4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q7KSF4; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9V9P7; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VGL0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VRJ0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IQQ7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KV35; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VTK2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VBE1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VUX7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V9E3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9NBD7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P46863; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VDU0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8SWR8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9I7J1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VNP5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VR89; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W0B8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VQZ3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VXG0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VHG1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q24180; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P46150; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A4UZL2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VJE5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V3C5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KNF1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VJ07; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VI63; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1Z6E0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VU30; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8T3L6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VNA0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VEK8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VDK5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8MRL0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9XTP7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VJS8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: B9A0M4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VM04; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VXU6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P40657; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IRG5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VE34; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VMC6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VY98; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VBE6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VIE8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VCV8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VCE7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VEH0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VVU5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P54358; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q27297; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V6Y3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P30432; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VJZ6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VYR9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W2N6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q00168; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q0E919; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8INH6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P54397; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V8Y7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P07666; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VNG2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8SZ63; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P17671; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W117; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IH56; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KV88; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P04052; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VQB6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: O76904; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q0KI87; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VKJ1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P10676; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W201; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9I7S4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8INC0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VFK2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q24478; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VKL9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W0D9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q494G8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q27268; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KMH9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VWE7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VXK9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P13368; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VP47; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VAD3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VNH6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V6B9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W4W4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VM15; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VMN9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VIQ9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9XTN4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1Z7A6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P41073; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VEN1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IPV2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VC81; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VVL7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8I0G5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VA60; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VZ97; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KU82; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W058; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P81923; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VA02; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V466; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VC08; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7K4H4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W2U4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8MLV8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q02748; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VJY4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V9W7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VD37; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VK52; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P27864; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VA30; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q86B55; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VM77; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VVC9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q0KIB3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IQW4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9XZ06; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VVW2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VH97; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VJ35; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P91645; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1Z6Z8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VQJ6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VC90; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VB58; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VRK6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VB05; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W397; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VW85; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VCW7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P10040; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VQ73; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VF10; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8MLN2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q961H1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VKV3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VTE2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VJ47; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1Z6M0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V4P1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VS82; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P45437; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P26308; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VID4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VRY4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VJY3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VSM9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: O16810; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W283; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IMA8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V3C0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8SYS8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V3L1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IN16; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7K7E6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VGG9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1Z8J4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VYN8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VM45; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VPB2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q0E940; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8T4F7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q0E993; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W3H0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VKZ6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7JX95; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q29R10; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IQA6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7K284; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q967D7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VNL6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VUL5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7K4C7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V414; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: O02372; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W594; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8MS38; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q0KHQ1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: O61735; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VBW3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7K4B4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VZP5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1ZBB4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8MV48; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W1G7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VHX9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9Y1T2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VG29; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q95TU2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VPP2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W1D3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1ZAK1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VA35; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q24141; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V6U9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VEF7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VUM0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VNC3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7K0F7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VBR7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q961D3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KRY7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VF20; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8SX64; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VP43; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VS54; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VXU8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VZK2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1Z9I9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V9X8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8MSQ4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q0KHR4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W1S1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9U3W7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VWJ0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W4X1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W205; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VRC8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VVG4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VT32; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: O61307; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VGW1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W3Y7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VU76; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W1A0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VG43; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VS63; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W1U2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W472; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VFG4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8SWW4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W1W0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VHB5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W1A4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VM62; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VRF2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VLN6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VGI5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VN58; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7JR75; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: O46067; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VAE4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P40301; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W0Z5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IPL3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VAU5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KU30; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VCH1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VW47; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W278; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V9W5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VUC7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VLI2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q86B79; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7Z020; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IM95; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VHD1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7JV09; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9U3V5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VQ61; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VFI3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: O77410; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KQM6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VL96; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VSM6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VP16; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W0E3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VW80; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q07886; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VJF6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VAW3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V7P1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VHH2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VY63; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VUE8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W093; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W0S9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VMQ4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VAS7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VLM8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9NFV7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KTX8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VWI5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VAH7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9XZS9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VTC1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VPM5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W592; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q27294; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q5BI50; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VNX1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q0KIF4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V9Z9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1ZAJ2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1Z6W6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VDY9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KTW3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V3X4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VW64; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VPH6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7JVN6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VJ21; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1Z9I3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V9K7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V9T2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q4V5M2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9V895; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VK72; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W1S3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: I0DHL3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VAY6; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VTG7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: P08155; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: O46040; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VY78; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VWQ3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VL52; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VX34; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VHB4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VLP5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IPP9; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VIK0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VU11; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VR59; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VQ36; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1ZB09; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9N6D8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VGU5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q86BS3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VUK7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1Z7L8; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W213; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VKU2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8IN81; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7KNA0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7K2B0; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1Z8R2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W3K5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1ZAD3; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VU57; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W0S2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VD46; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7K3L1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q8MRN4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VNH1; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W0S7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VPT4; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9W3E2; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q86B72; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VX14; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9NGK5; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: A1ZBF7; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VHL1; IntAct: EBI-9944837; Score: 0.35
GO  GO:0044295;
GO  GO:0005604;
GO  GO:0031012;
GO  GO:0005576;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0009887;
GO  GO:0007411;
GO  GO:0048749;
GO  GO:0016358;
GO  GO:0070983;
GO  GO:0008347;
GO  GO:0008045;
GO  GO:2000289;
GO  GO:0007432;
GO  GO:0016200;
GO  GO:0008039;
GO  GO:0009888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRATGTRMGLLLPIILALAIGSSAAGISSNDPCYFEGKPRKCLPSFVNAAYGNPVQASSVCGAQQPERYCELLRDGNAG
SQ  ECRSCEQQRYGPAALTDLNNPSNVTCWRSGAVNVPHDPDSAPPDNVTLTLSLGKKYELTYISLSFCPRSPRPDSLAIFKS
SQ  SDFGQTWQPFQFYSSQCQKFYGRPDRAKISKFNEQEARCINSQHDTGGAAQRFAFNTLEGRPSANDLDSSLVLQDWVTAT
SQ  DIRVVFHRLELPPQLLKVKNANAFSDEMGGSREEDEDDDADLELDGEQDEYDYNLQDNDSADAGYDEYEEPKKHLELDDD
SQ  HLHLDYASDGESVVKRQGKHKGSAYEKHYQSKLAATTPPQQPPKVTPPGKVTPPSTAAPSAAASAVTLPISQHYAVSDFA
SQ  VGGRCKCNGHASECVATVSSGSGTALSDQDDGQDEDTPSAPSLANHFGRSTQMSAKLTMTCACKHNTAGPECERCKPFYF
SQ  DRPWGRATDNDANECKMCQCNGHARRCRFNLELYKLSGRVSGGVCYNCQHDTTGRYCHYCREGYYRDATKPPNHRKVCKR
SQ  CDCHPVGSTGKTCNHLSGQCPCKEGVTGLTCNRCARGYQQTRSHVAPCIKVPTNANMIQAESAGGGGGGGTGDYKDGGGS
SQ  QVEEMKKYCGKCKASPKKLNLNKFCMEDYAILAKVIGHDRASQDISTEKFSIERQNEIYKYEINIQTIFKRNPMSGTTSS
SQ  LLGRGNMMLLVPRKSIECQCPKIKLNKSYLILGRDSEAAPGYLAIGPSSVVLEWKDEWSLRMKRFQRRARKCS
//
ID  O76050;
PN  E3 ubiquitin-protein ligase NEURL1;
GN  NEURL1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11585928, ECO:0000269|PubMed:20847082}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Perikaryon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Localized in the cell bodies of the pyramidal neurons and distributed along their apical dendrites. Colocalized with PSD95 in postsynaptic sites. Colocalized with CPEB3 at apical dendrites of CA1 neurons (By similarity). Colocalized with JAG1 at the cell surface. {ECO:0000250}.
DR  UNIPROT: O76050;
DR  UNIPROT: Q5TDR2;
DR  UNIPROT: Q5TDR3;
DR  UNIPROT: Q8TAN0;
DR  UNIPROT: Q9H463;
DR  Pfam: PF07177;
DR  PROSITE: PS51065;
DR  PROSITE: PS50089;
DR  OMIM: 603804;
DR  DisGeNET: 9148;
DE  Function: Plays a role in hippocampal-dependent synaptic plasticity, learning and memory. Involved in the formation of spines and functional synaptic contacts by modulating the translational activity of the cytoplasmic polyadenylation element-binding protein CPEB3. Promotes ubiquitination of CPEB3, and hence induces CPEB3-dependent mRNA translation activation of glutamate receptor GRIA1 and GRIA2. Can function as an E3 ubiquitin-protein ligase to activate monoubiquitination of JAG1 (in vitro), thereby regulating the Notch pathway. Acts as a tumor suppressor; inhibits malignant cell transformation of medulloblastoma (MB) cells by inhibiting the Notch signaling pathway. {ECO:0000269|PubMed:20847082}.
DE  Reference Proteome: Yes;
DE  Interaction: P62256; IntAct: EBI-2129921; Score: 0.37
DE  Interaction: P61088; IntAct: EBI-2130056; Score: 0.37
DE  Interaction: Q07065; IntAct: EBI-20901648; Score: 0.40
GO  GO:0070161;
GO  GO:0097440;
GO  GO:0043197;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0046872;
GO  GO:0045183;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0007420;
GO  GO:0071230;
GO  GO:0007595;
GO  GO:0008285;
GO  GO:0045746;
GO  GO:0007399;
GO  GO:0007219;
GO  GO:0043065;
GO  GO:0060999;
GO  GO:0045741;
GO  GO:0051491;
GO  GO:0048170;
GO  GO:0090129;
GO  GO:0006513;
GO  GO:0007519;
GO  GO:0007288;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGNNFSSIPSLPRGNPSRAPRGHPQNLKDSIGGPFPVTSHRCHHKQKHCPAVLPSGGLPATPLLFHPHTKGSQILMDLSH
SQ  KAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEE
SQ  FANEGNIIAFWVDKKGRVFHRINDSAVMLFFSGVRTADPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLR
SQ  READDARLSVSLCDLNVPGADGDEAAPAAGCPIPQNSLNSQHSRALPAQLDGDLRFHALRAGAHVRILDEQTVARVEHGR
SQ  DERALVFTSRPVRVAETIFVKVTRSGGARPGALSFGVTTCDPGTLRPADLPFSPEALVDRKEFWAVCRVPGPLHSGDILG
SQ  LVVNADGELHLSHNGAAAGMQLCVDASQPLWMLFGLHGTITQIRILGSTILAERGIPSLPCSPASTPTSPSALGSRLSDP
SQ  LLSTCSSGPLGSSAGGTAPNSPVSLPESPVTPGLGQWSDECTICYEHAVDTVIYTCGHMCLCYACGLRLKKALHACCPIC
SQ  RRPIKDIIKTYRSS
//
ID  Q923S6;
PN  E3 ubiquitin-protein ligase NEURL1;
GN  Neurl1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:22153079}; Peripheral membrane protein {ECO:0000269|PubMed:22153079}. Perikaryon {ECO:0000269|PubMed:22153079}. Cell projection, dendrite {ECO:0000269|PubMed:22153079}. Postsynaptic density {ECO:0000269|PubMed:22153079}. Note=Colocalized with JAG1 at the cell surface (By similarity). Localized in the cell bodies of the pyramidal neurons and distributed along their apical dendrites. Colocalized with PSD95 in postsynaptic sites. Colocalized with CPEB3 at apical dendrites of CA1 neurons. {ECO:0000250}.
DR  UNIPROT: Q923S6;
DR  UNIPROT: Q91ZT6;
DR  UNIPROT: Q9CWF1;
DR  UNIPROT: Q9QWF1;
DR  Pfam: PF07177;
DR  PROSITE: PS51065;
DR  PROSITE: PS50089;
DE  Function: Plays a role in hippocampal-dependent synaptic plasticity, learning and memory. Involved in the formation of spines and functional synaptic contacts by modulating the translational activity of the cytoplasmic polyadenylation element-binding protein CPEB3. Promotes ubiquitination of CPEB3, and hence induces CPEB3-dependent mRNA translation activation of glutamate receptor GRIA1 and GRIA2. Can function as an E3 ubiquitin-protein ligase to activate monoubiquitination of JAG1 (in vitro), thereby regulating the Notch pathway. Acts as a tumor suppressor; inhibits malignant cell transformation of medulloblastoma (MB) cells by inhibiting the Notch signaling pathway. {ECO:0000269|PubMed:18077452, ECO:0000269|PubMed:22153079}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7TN99; IntAct: EBI-5424839; Score: 0.56
DE  Interaction: P11499; IntAct: EBI-5415228; Score: 0.40
DE  Interaction: Q9CZ13; IntAct: EBI-5415228; Score: 0.40
DE  Interaction: P28652; IntAct: EBI-5415228; Score: 0.40
DE  Interaction: P63328; IntAct: EBI-5415228; Score: 0.40
DE  Interaction: Q8CHU3; IntAct: EBI-5415228; Score: 0.40
DE  Interaction: P17710; IntAct: EBI-5415228; Score: 0.40
GO  GO:0070161;
GO  GO:0097440;
GO  GO:0005737;
GO  GO:0043197;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0046872;
GO  GO:0045183;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0007420;
GO  GO:0071230;
GO  GO:0030317;
GO  GO:0007595;
GO  GO:0008285;
GO  GO:0045746;
GO  GO:0007399;
GO  GO:0007219;
GO  GO:0043065;
GO  GO:0060999;
GO  GO:0045741;
GO  GO:0051491;
GO  GO:0048170;
GO  GO:0090129;
GO  GO:0006513;
GO  GO:0007519;
GO  GO:0007288;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:18077452};
SQ  MGNNFSSVSSLQRGNPSRASRGHPQNLKDSIGGSFPVPSHRCHHKQKHCPPTLSGGGLPATPLLFHPHTKGSQILMDLSH
SQ  KAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEE
SQ  FANEGNIIAFWVDKKGRVFYRINESAAMLFFSGVRTVDPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLR
SQ  CEADEARLSVSLCDLNVPGADGDDGAPPAGCPIPQNSLNSQHSRALPAQLDGDLRFHALRAGAHVRILDEQTVARLEHGR
SQ  DERALVFTSRPVRVAETIFIKVTRSGGGRAGALSFGVTTCDPGTLRPADLPFSPEALVDRKEFWAVCRVPGPLHSGDILG
SQ  LVVNADGELHLSHNGAAAGMQLCVDASQPLWMLFSLHGAITQVRILGSTIMTERGGPSLPCSPASTPTSPSALGIRLSDP
SQ  LLSTCGSGPLGGSAGGTAPNSPVSLPESPVTPGLGQWSDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPIC
SQ  RRPIKDIIKTYRSS
//
ID  G0S024;
PN  Nucleoporin NIC96;
GN  NIC96;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P34077}. Nucleus membrane {ECO:0000250|UniProtKB:P34077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P34077}; Cytoplasmic side {ECO:0000250|UniProtKB:P34077}. Nucleus membrane {ECO:0000250|UniProtKB:P34077}; Peripheral membrane protein {ECO:0000250|UniProtKB:P34077}; Nucleoplasmic side {ECO:0000250|UniProtKB:P34077}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P34077}.
DR  UNIPROT: G0S024;
DR  UNIPROT: G0ZGU3;
DR  PDB: 5CWS;
DR  PDB: 5HB2;
DR  PDB: 5HB3;
DR  Pfam: PF04097;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NIC96, which is localized to the core of the NPC and the distal ring of the nuclear basket, is required for de novo assembly of NPCs. {ECO:0000250|UniProtKB:P34077}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S4T0; IntAct: EBI-4325438; Score: 0.73
DE  Interaction: G0SFH5; IntAct: EBI-5238287; Score: 0.52
DE  Interaction: G0S156; IntAct: EBI-4325483; Score: 0.70
DE  Interaction: G0S4X2; IntAct: EBI-16176393; Score: 0.61
DE  Interaction: G0S0R2; IntAct: EBI-16176393; Score: 0.61
DE  Interaction: G0SBQ3; IntAct: EBI-16176393; Score: 0.61
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P34077};
SQ  MSLIGNGPSVPPSSTKASLFSSPTTSANPTGGLFGSTTGGSSLFAPKTAGSTTTSTTQPTSTTGLGTSLFGTSTTANTQN
SQ  TANAARPSLFTAGNSIFGTSTTQPGLGASSLTTAATSNQQAQQQQQQRQQHQQAAPTGALFDSLLARNKKQAEGETALGE
SQ  LPSLQLGLADLRQRLRKLGPSSDRPIEPGKAHYFLAASGVDPGAAVRDLGALGLQAKTERTAASVGPAAGPSGVSTTGFG
SQ  TGLGEVDVDTYLSNLQTKTTLSMIADGLERSARDFDAFLEENVTLEWEAQRKRIYQHFGIKPRDSSVAGTTTAQPTATPS
SQ  KDGQGTFGRSRRKASQPPPGERPAQRMSILGRSTMMRSVIGTPTRIGAHAPEFSDVEARKDSSGAAVASVDDRFLREKQA
SQ  KLAEKIREFNDARQRGTPFYICRDLADLESKSGDRHGPHIVEAYRAVMEMVGEHPDAGEAPRERQFAKMYLDPNTQSANA
SQ  LAMRKQILKGATTFLEKQFWNEVNSLIAKYPQDANLGGLPDVVSKIKAYIRLRIARKTLVPDNVELQQINGEYVWAIVFY
SQ  LLRAGFVTEAAQYVNSNQAHFRAIDRTFSGYINSYASSEERRLKRQMQDRCMSEYNQRIRNAPEGSIDPFRMACYKIIGR
SQ  CDLSNRSLDGLQTDVNDWIWLQFNLARETDRSLELAGESYGLAELQASIREIGLKHFPKTAAEDTNGSFGMFFYLQILAG
SQ  MFEQAIAYLYPFSYVDAVHFAIALTYYGLLRPVDAASAGNELLSHNTRSMPQINFGRMLGYYTRDFRAANPAAAVDYLVL
SQ  ICLNADEAAGGQQAQAALCHEALRELVLESREFSRLIGDIRPDGRRIRGVIEERGPLIALGQEDDFIRTITLQAASFADD
SQ  NGRTTDAVLLYHLAEDYDTVVSIVSRALSEAISLEIGEDPMRLIPVKPRVTNAEGQVEEAAPGSSLSLAAIDDPVELAKA
SQ  MMGMYERDHMFWQKIREPNRVACSVLLQMADIKSLVEQGRWAECLDKIRALDILPLTARGDPGTIRSYAARFPSLAQPVA
SQ  INVPNLLMWTVLCCMRQRERLAGGQFAGNESTARLMMDELKQMTVDLMAYTSQLRYRLPPHLHEALARASAD
//
ID  P34077;
PN  Nucleoporin NIC96;
GN  NIC96;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P34077;
DR  UNIPROT: D6VTN2;
DR  PDB: 2QX5;
DR  PDB: 2RFO;
DR  PDB: 6X07;
DR  PDB: 7N85;
DR  PDB: 7N9F;
DR  PDB: 7WOO;
DR  PDB: 7WOT;
DR  Pfam: PF04097;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NIC96, which is localized to the core of the NPC and the distal ring of the nuclear basket, is required for de novo assembly of NPCs. It is involved in nuclear GSP1 import. {ECO:0000269|PubMed:10428845, ECO:0000269|PubMed:10617624, ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10806080, ECO:0000269|PubMed:11121302, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:12403813, ECO:0000269|PubMed:12496130, ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:7828598, ECO:0000269|PubMed:8682855, ECO:0000269|PubMed:9017593}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-789044; Score: 0.35
DE  Interaction: P32499; IntAct: EBI-6322501; Score: 0.00
DE  Interaction: P32500; IntAct: EBI-6322567; Score: 0.00
DE  Interaction: Q03790; IntAct: EBI-390816; Score: 0.67
DE  Interaction: P53271; IntAct: EBI-390819; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P07259; IntAct: EBI-789044; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-789044; Score: 0.35
DE  Interaction: P48837; IntAct: EBI-789044; Score: 0.84
DE  Interaction: Q02199; IntAct: EBI-789044; Score: 0.62
DE  Interaction: P47054; IntAct: EBI-789044; Score: 0.55
DE  Interaction: P40069; IntAct: EBI-789044; Score: 0.35
DE  Interaction: P53863; IntAct: EBI-797840; Score: 0.35
DE  Interaction: P40066; IntAct: EBI-813993; Score: 0.27
DE  Interaction: Q07953; IntAct: EBI-857992; Score: 0.00
DE  Interaction: Q02630; IntAct: EBI-1269736; Score: 0.00
DE  Interaction: Q02629; IntAct: EBI-1269879; Score: 0.00
DE  Interaction: P51998; IntAct: EBI-2347558; Score: 0.37
DE  Interaction: P23291; IntAct: EBI-2614250; Score: 0.35
DE  Interaction: P26448; IntAct: EBI-2882390; Score: 0.00
DE  Interaction: Q00684; IntAct: EBI-2882792; Score: 0.00
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: P02293; IntAct: EBI-2884858; Score: 0.00
DE  Interaction: P38265; IntAct: EBI-2885494; Score: 0.00
DE  Interaction: P39723; IntAct: EBI-2887969; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P46675; IntAct: EBI-2888241; Score: 0.00
DE  Interaction: P52593; IntAct: EBI-4324997; Score: 0.37
DE  Interaction: P52919; IntAct: EBI-7042849; Score: 0.27
DE  Interaction: Q7Z3B4; IntAct: EBI-11889076; Score: 0.37
DE  Interaction: Q05166; IntAct: EBI-11889154; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044612;
GO  GO:0044615;
GO  GO:0017056;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0000055;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MLETLRGNKLHSGTSKGANKKLNELLESSDNLPSASSELGSIQVSINELRRRVFQLRSKNKASKDYTKAHYLLANSGLSF
SQ  EDVDAFIKDLQTNQFLEPNPPKIIESEELEFYIRTKKEENILMSIEQLLNGATKDFDNFINHNLNLDWAQHKNEVMKNFG
SQ  ILIQDKKTVDHKKSISSLDPKLPSWGNKGNNILNSNESRLNVNENNILREKFENYARIVFQFNNSRQANGNFDIANEFIS
SQ  ILSSANGTRNAQLLESWKILESMKSKDINIVEVGKQYLEQQFLQYTDNLYKKNMNEGLATNVNKIKSFIDTKLKKADKSW
SQ  KISNLTVINGVPIWALIFYLLRAGLIKEALQVLVENKANIKKVEQSFLTYFKAYASSKDHGLPVEYSTKLHTEYNQHIKS
SQ  SLDGDPYRLAVYKLIGRCDLSRKNIPAVTLSIEDWLWMHLMLIKEKDAENDPVYERYSLEDFQNIIISYGPSRFSNYYLQ
SQ  TLLLSGLYGLAIDYTYTFSEMDAVHLAIGLASLKLFKIDSSTRLTKKPKRDIRFANILANYTKSFRYSDPRVAVEYLVLI
SQ  TLNEGPTDVELCHEALRELVLETKEFTVLLGKIGRDGARIPGVIEERQPLLHVRDEKEFLHTITEQAARRADEDGRIYDS
SQ  ILLYQLAEEYDIVITLVNSLLSDTLSASDLDQPLVGPDDNSETNPVLLARRMASIYFDNAGISRQIHVKNKEICMLLLNI
SQ  SSIRELYFNKQWQETLSQMELLDLLPFSDELSARKKAQDFSNLDDNIVKNIPNLLIITLSCISNMIHILNESKYQSSTKG
SQ  QQIDSLKNVARQCMIYAGMIQYRMPRETYSTLINIDVSL
//
ID  P59044;
PN  NACHT, LRR and PYD domains-containing protein 6;
GN  NLRP6;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:12387869, ECO:0000269|PubMed:31932628}. Inflammasome {ECO:0000269|PubMed:12387869, ECO:0000269|PubMed:30674671, ECO:0000269|PubMed:31932628, ECO:0000269|PubMed:34678144}. Cell membrane {ECO:0000250|UniProtKB:Q63035}. Nucleus membrane {ECO:0000250|UniProtKB:Q63035}.
DR  UNIPROT: P59044;
DR  UNIPROT: A8K9F3;
DR  UNIPROT: E9PJZ8;
DR  PDB: 6NCV;
DR  PDB: 6NDJ;
DR  Pfam: PF05729;
DR  Pfam: PF17776;
DR  Pfam: PF17779;
DR  Pfam: PF02758;
DR  PROSITE: PS50824;
DR  PROSITE: PS50837;
DR  OMIM: 609650;
DR  DisGeNET: 171389;
DE  Function: Acts as the sensor component of the NLRP6 inflammasome, which mediates inflammasome activation in response to various pathogen- associated signals, leading to maturation and secretion of IL1B and IL18 (PubMed:30392956, PubMed:34678144). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (PubMed:30674671). Acts as a recognition receptor (PRR): recognizes and binds specific pathogens and other damage-associated signals, such as lipoteichoic acid (LTA), a cell-wall component of Gram-positive bacteria, or double stranded RNA (dsRNA) (PubMed:30392956, PubMed:34678144, PubMed:33377178). May also recognize and bind lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria; however, LPS is probably not a major activator of the NLRP6 inflammasome (PubMed:31932628, PubMed:34678144). Following LTA- or dsRNA-binding, NLRP6 undergoes liquid-liquid phase separation (LLPS), enhancing multivalent interactions, an essential step for the formation of the NLRP6 inflammasome polymeric complex (PubMed:34678144). The NLRP6 inflammasome acts by promoting recruitment of effector pro-inflammatory caspases (CASP1 and/or CASP4) that catalyze maturation and secretion of IL1B and IL18 in the extracellular milieu (PubMed:30674671, PubMed:12387869, PubMed:30392956, PubMed:34678144). The NLRP6 inflammasome plays a central role in the maintenance of epithelial integrity and host defense against microbial infections in the intestine (PubMed:30392956). Required to restrict infection against Gram-positive bacteria by recognizing lipoteichoic acid (LTA), leading to recruitment of CASP4 and CASP1, and subsequent maturation and secretion of IL1B and IL18 (PubMed:30392956, PubMed:33377178). Involved in intestinal antiviral innate immunity together with DHX15: recognizes and binds viral dsRNA to restrict infection by enteric viruses through the interferon pathway and GSDMD-dependent release of IL18 (PubMed:34678144, PubMed:34161762). Required to prevent infection by the apicomplexan parasite Cryptosporidium in enterocytes by promoting GSDMD-dependent release of IL18 (By similarity). The NLRP6 inflammasome may also regulate the gut microbiota composition by acting as a sensor of microbiota-associated metabolites to form a PYCARD/ASC-dependent inflammasome for downstream IL18 release and secretion of antimicrobial peptides (By similarity). Essential for gut mucosal self-renewal and proliferation (By similarity). Regulate mucus secretion in an inflammasome- and autophagy-dependent manner to prevent invasion by enteric bacteria, (By similarity). During systemic bacterial infections, the NLRP6 inflammasome negatively regulates neutrophil recruitment and neutrophil extracellular traps (NETs) formation (By similarity). May promote peripheral nerve recovery following injury via an inflammasome-independent mechanism (By similarity). {ECO:0000250|UniProtKB:Q91WS2, ECO:0000269|PubMed:12387869, ECO:0000269|PubMed:30392956, ECO:0000269|PubMed:30674671, ECO:0000269|PubMed:31932628, ECO:0000269|PubMed:33377178, ECO:0000269|PubMed:34161762, ECO:0000269|PubMed:34678144}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0061702;
GO  GO:0140738;
GO  GO:0043228;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0001530;
GO  GO:0070891;
GO  GO:0140693;
GO  GO:0038187;
GO  GO:0042277;
GO  GO:0005000;
GO  GO:0097202;
GO  GO:0002526;
GO  GO:0002438;
GO  GO:0140374;
GO  GO:0050830;
GO  GO:0051607;
GO  GO:0048874;
GO  GO:0070266;
GO  GO:0070373;
GO  GO:0043124;
GO  GO:0002862;
GO  GO:0032689;
GO  GO:0034122;
GO  GO:0070946;
GO  GO:0140739;
GO  GO:0050729;
GO  GO:2000494;
GO  GO:0051260;
GO  GO:0070269;
GO  GO:0010506;
GO  GO:0050727;
GO  GO:0070255;
GO  GO:0009617;
GO  GO:0042060;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDQPEAPCSSTGPRLAVARELLLAALEELSQEQLKRFRHKLRDVGPDGRSIPWGRLERADAVDLAEQLAQFYGPEPALEV
SQ  ARKTLKRADARDVAAQLQERRLQRLGLGSGTLLSVSEYKKKYREHVLQLHARVKERNARSVKITKRFTKLLIAPESAAPE
SQ  EAMGPAEEPEPGRARRSDTHTFNRLFRRDEEGRRPLTVVLQGPAGIGKTMAAKKILYDWAAGKLYQGQVDFAFFMPCGEL
SQ  LERPGTRSLADLILDQCPDRGAPVPQMLAQPQRLLFILDGADELPALGGPEAAPCTDPFEAASGARVLGGLLSKALLPTA
SQ  LLLVTTRAAAPGRLQGRLCSPQCAEVRGFSDKDKKKYFYKYFRDERRAERAYRFVKENETLFALCFVPFVCWIVCTVLRQ
SQ  QLELGRDLSRTSKTTTSVYLLFITSVLSSAPVADGPRLQGDLRNLCRLAREGVLGRRAQFAEKELEQLELRGSKVQTLFL
SQ  SKKELPGVLETEVTYQFIDQSFQEFLAALSYLLEDGGVPRTAAGGVGTLLRGDAQPHSHLVLTTRFLFGLLSAERMRDIE
SQ  RHFGCMVSERVKQEALRWVQGQGQGCPGVAPEVTEGAKGLEDTEEPEEEEEGEEPNYPLELLYCLYETQEDAFVRQALCR
SQ  FPELALQRVRFCRMDVAVLSYCVRCCPAGQALRLISCRLVAAQEKKKKSLGKRLQASLGGGSSSQGTTKQLPASLLHPLF
SQ  QAMTDPLCHLSSLTLSHCKLPDAVCRDLSEALRAAPALTELGLLHNRLSEAGLRMLSEGLAWPQCRVQTVRVQLPDPQRG
SQ  LQYLVGMLRQSPALTTLDLSGCQLPAPMVTYLCAVLQHQGCGLQTLSLASVELSEQSLQELQAVKRAKPDLVITHPALDG
SQ  HPQPPKELISTF
//
ID  Q91WS2;
PN  NACHT, LRR and PYD domains-containing protein 6;
GN  Nlrp6;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q63035}. Inflammasome {ECO:0000269|PubMed:30248149, ECO:0000269|PubMed:34678144}. [Isoform 1]: Cytoplasm {ECO:0000250|UniProtKB:Q63035}. Inflammasome {ECO:0000250|UniProtKB:P59044}. Cell membrane {ECO:0000250|UniProtKB:Q63035}. Nucleus membrane {ECO:0000250|UniProtKB:Q63035}. [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q63035}. Cell membrane {ECO:0000250|UniProtKB:Q63035}. Note=Predominantly expressed in the cell membrane. {ECO:0000250|UniProtKB:Q63035}.
DR  UNIPROT: Q91WS2;
DR  UNIPROT: C9W978;
DR  UNIPROT: F8UKQ6;
DR  UNIPROT: Q67EY0;
DR  UNIPROT: Q8K0L4;
DR  Pfam: PF05729;
DR  Pfam: PF17776;
DR  Pfam: PF17779;
DR  Pfam: PF02758;
DR  PROSITE: PS50824;
DR  PROSITE: PS50837;
DE  Function: Acts as the sensor component of the NLRP6 inflammasome, which mediates inflammasome activation in response to various pathogen- associated signals, leading to maturation and secretion of IL1B and IL18 (PubMed:21593405, PubMed:30392956, PubMed:32424362, PubMed:34678144). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage- associated signals and play critical roles in innate immunity and inflammation (PubMed:30392956). Acts as a recognition receptor (PRR): recognizes and binds specific pathogens and other damage-associated signals, such as lipoteichoic acid (LTA), a cell-wall component of Gram-positive bacteria, or double stranded RNA (dsRNA) (PubMed:26494172, PubMed:30392956, PubMed:34678144). May also recognize and bind lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria; however, LPS is probably not a major activator of the NLRP6 inflammasome (PubMed:34678144). Following LTA- or dsRNA-binding, NLRP6 undergoes liquid-liquid phase separation (LLPS), enhancing multivalent interactions, an essential step for the formation of the NLRP6 inflammasome polymeric complex (PubMed:34678144). The NLRP6 inflammasome acts by promoting recruitment of effector pro-inflammatory caspases (CASP1 and/or CASP4) that catalyze maturation and secretion of IL1B and IL18 in the extracellular milieu (PubMed:30392956). The NLRP6 inflammasome plays a central role in the maintenance of epithelial integrity and host defense against microbial infections in the intestine (PubMed:21565393, PubMed:22763455, PubMed:23696660, PubMed:26638072, PubMed:28445725, PubMed:30392956). Required to restrict infection against Gram-positive bacteria by recognizing lipoteichoic acid (LTA), leading to recruitment of CASP4 and CASP1, and subsequent maturation and secretion of IL1B and IL18 (PubMed:30392956). Involved in intestinal antiviral innate immunity together with DHX15: recognizes and binds viral dsRNA to restrict infection by enteric viruses through the interferon pathway and GSDMD-dependent release of IL18 (PubMed:26494172, PubMed:34678144). Required to prevent infection by the apicomplexan parasite C.tyzzeri in enterocytes by promoting GSDMD-dependent release of IL18 (PubMed:33372132). The NLRP6 inflammasome may also regulate the gut microbiota composition by acting as a sensor of microbiota-associated metabolites to form a PYCARD/ASC-dependent inflammasome for downstream IL18 release and secretion of antimicrobial peptides (PubMed:21565393, PubMed:22763455, PubMed:26638072, PubMed:33617596). Its role in the regulation of the gut microbiota composition is however subject to discussion (PubMed:29281815, PubMed:29281837, PubMed:28801232). Essential for gut mucosal self-renewal and proliferation (PubMed:21593405, PubMed:21543645, PubMed:21565393). Regulate mucus secretion in an inflammasome- and autophagy-dependent manner to prevent invasion by enteric bacteria (PubMed:24581500, PubMed:27339979). During systemic bacterial infections, the NLRP6 inflammasome negatively regulates neutrophil recruitment and neutrophil extracellular traps (NETs) formation (PubMed:22763455, PubMed:30248149, PubMed:33918100, PubMed:33230225). May promote peripheral nerve recovery following injury via an inflammasome-independent mechanism (PubMed:26253422). {ECO:0000269|PubMed:21543645, ECO:0000269|PubMed:21565393, ECO:0000269|PubMed:21593405, ECO:0000269|PubMed:22763455, ECO:0000269|PubMed:23696660, ECO:0000269|PubMed:24581500, ECO:0000269|PubMed:26253422, ECO:0000269|PubMed:26494172, ECO:0000269|PubMed:26638072, ECO:0000269|PubMed:27339979, ECO:0000269|PubMed:28445725, ECO:0000269|PubMed:28801232, ECO:0000269|PubMed:29281815, ECO:0000269|PubMed:29281837, ECO:0000269|PubMed:30248149, ECO:0000269|PubMed:30392956, ECO:0000269|PubMed:32424362, ECO:0000269|PubMed:33230225, ECO:0000269|PubMed:33372132, ECO:0000269|PubMed:33617596, ECO:0000269|PubMed:33918100, ECO:0000269|PubMed:34678144}.
DE  Reference Proteome: Yes;
DE  Interaction: O35286; IntAct: EBI-16182259; Score: 0.44
DE  Interaction: O43143; IntAct: EBI-16182238; Score: 0.40
DE  Interaction: Q7Z434; IntAct: EBI-16182335; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0061702;
GO  GO:0140738;
GO  GO:0043228;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0001530;
GO  GO:0070891;
GO  GO:0140693;
GO  GO:0038187;
GO  GO:0042277;
GO  GO:0005000;
GO  GO:0097202;
GO  GO:0002526;
GO  GO:0002438;
GO  GO:0140374;
GO  GO:0050830;
GO  GO:0051607;
GO  GO:0048874;
GO  GO:0070266;
GO  GO:0070373;
GO  GO:0043124;
GO  GO:0050777;
GO  GO:0002862;
GO  GO:0032689;
GO  GO:0043409;
GO  GO:0034122;
GO  GO:0070946;
GO  GO:0140739;
GO  GO:0050729;
GO  GO:2000494;
GO  GO:0051260;
GO  GO:0070269;
GO  GO:0010506;
GO  GO:0050727;
GO  GO:0070255;
GO  GO:0009617;
GO  GO:0042060;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDAAGASCSSVDAVARELLMATLEELSQEQLKRFRHKLRDAPLDGRSIPWGRLERSDAVDLVDKLIEFYEPVPAVEMTRQ
SQ  VLKRSDIRDVASRLKQQQLQKLGPTSVLLSVSAFKKKYREHVLRQHAKVKERNARSVKINKRFTKLLIAPGTGAVEDELL
SQ  GPLGEPEPERARRSDTHTFNRLFRGNDEESSQPLTVVLQGPAGIGKTMAAKKILYDWAAGKLYHSQVDFAFFMPCGELLE
SQ  RPGKRSLADLVLDQCPDRAWPVKRILAQPNRLLFILDGADELPTLPSSEATPCKDPLEATSGLRVLSGLLSQELLPGARL
SQ  LVTTRHAATGRLQGRLCSPQCAEIRGFSDKDKKKYFFKFFRDERKAERAYRFVKENETLFALCFVPFVCWIVCTVLQQQL
SQ  ELGRDLSRTSKTTTSVYLLFITSMLKSAGTNGPRVQGELRTLCRLAREGILDHHKAQFSEEDLEKLKLRGSQVQTIFLNK
SQ  KEIPGVLKTEVTYQFIDQSFQEFLAALSYLLEAERTPGTPAGGVQKLLNSDAELRGHLALTTRFLFGLLNTEGLRDIGNH
SQ  FGCVVPDHVKKDTLRWVQGQSHPKGPPVGAKKTAELEDIEDAEEEEEEEEDLNFGLELLYCLYETQEEDFVRQALSSLPE
SQ  IVLERVRLTRMDLEVLNYCVQCCPDGQALRLVSCGLVAAKEKKKKKKSLVKRLKGSQSTKKQPPVSLLRPLCETMTTPKC
SQ  HLSVLILSHCRLPDAVCRDLSEALKVAPALRELGLLQSRLTNTGLRLLCEGLAWPKCQVKTLRMQLPDLQEVINYLVIVL
SQ  QQSPVLTTLDLSGCQLPGVIVEPLCAALKHPKCSLKTLSLTSVELSENSLRDLQAVKTSKPDLSIIYSK
//
ID  Q63035;
PN  NACHT, LRR and PYD domains-containing protein 6;
GN  Nlrp6;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:18413781}. Inflammasome {ECO:0000250|UniProtKB:P59044}. Cell membrane {ECO:0000269|PubMed:18413781}. Nucleus membrane {ECO:0000269|PubMed:18413781}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:18413781}. Cell membrane {ECO:0000269|PubMed:18413781}. Note=Predominantly expressed at the cell membrane.
DR  UNIPROT: Q63035;
DR  UNIPROT: A5X5C9;
DR  UNIPROT: D3ZYC0;
DR  UNIPROT: F1LSH2;
DR  Pfam: PF05729;
DR  Pfam: PF17776;
DR  Pfam: PF17779;
DR  Pfam: PF02758;
DR  PROSITE: PS50824;
DR  PROSITE: PS50837;
DE  Function: Acts as the sensor component of the NLRP6 inflammasome, which mediates inflammasome activation in response to various pathogen- associated signals, leading to maturation and secretion of IL1B and IL18. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Acts as a recognition receptor (PRR): recognizes and binds specific pathogens and other damage-associated signals, such as lipoteichoic acid (LTA), a cell-wall component of Gram-positive bacteria, or double stranded RNA (dsRNA). May also recognize and bind lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria; however, LPS is probably not a major activator of the NLRP6 inflammasome. Following LTA- or dsRNA-binding, NLRP6 undergoes liquid-liquid phase separation (LLPS), enhancing multivalent interactions, an essential step for the formation of the NLRP6 inflammasome polymeric complex. The NLRP6 inflammasome acts by promoting recruitment of effector pro-inflammatory caspases (CASP1 and/or CASP4) that catalyze maturation and secretion of IL1B and IL18 in the extracellular milieu. The NLRP6 inflammasome plays a central role in the maintenance of epithelial integrity and host defense against microbial infections in the intestine. Required to restrict infection against Gram-positive bacteria by recognizing lipoteichoic acid (LTA), leading to recruitment of CASP4 and CASP1, and subsequent maturation and secretion of IL1B and IL18. Involved in intestinal antiviral innate immunity together with DHX15: recognizes and binds viral dsRNA to restrict infection by enteric viruses through the interferon pathway and GSDMD-dependent release of IL18 (By similarity). Required to prevent infection by the apicomplexan parasite Cryptosporidium in enterocytes by promoting GSDMD-dependent release of IL18. The NLRP6 inflammasome may also regulate the gut microbiota composition by acting as a sensor of microbiota-associated metabolites to form a PYCARD/ASC-dependent inflammasome for downstream IL18 release and secretion of antimicrobial peptides. Essential for gut mucosal self-renewal and proliferation. Regulate mucus secretion in an inflammasome- and autophagy-dependent manner to prevent invasion by enteric bacteria,. During systemic bacterial infections, the NLRP6 inflammasome negatively regulates neutrophil recruitment and neutrophil extracellular traps (NETs) formation. May promote peripheral nerve recovery following injury via an inflammasome-independent mechanism (By similarity). {ECO:0000250|UniProtKB:P59044, ECO:0000250|UniProtKB:Q91WS2}.
DE  Disease: Note=Defects in Nlrp6 may be a cause of salt-sensitive hypertension. {ECO:0000305|PubMed:11984003}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0061702;
GO  GO:0140738;
GO  GO:0043228;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0001530;
GO  GO:0070891;
GO  GO:0140693;
GO  GO:0038187;
GO  GO:0042277;
GO  GO:0005000;
GO  GO:0097202;
GO  GO:0002526;
GO  GO:0002438;
GO  GO:0140374;
GO  GO:0050830;
GO  GO:0051607;
GO  GO:0048874;
GO  GO:0070266;
GO  GO:0070373;
GO  GO:0043124;
GO  GO:0050777;
GO  GO:0002862;
GO  GO:0032689;
GO  GO:0043409;
GO  GO:0034122;
GO  GO:0070946;
GO  GO:0140739;
GO  GO:0050729;
GO  GO:2000494;
GO  GO:0051260;
GO  GO:0070269;
GO  GO:0010506;
GO  GO:0050727;
GO  GO:0070255;
GO  GO:0009617;
GO  GO:0042060;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDAAGASCSSSEAVARELLLAALQDLSQEQLKRFRHKLRDAPLDGRSIPWGRLEHSDAVDLTDKLIEFYAPEPAVDVTRK
SQ  ILKKADIRDVSLRLKEQQLQRLGSSSALLTVSEYKKKYREHVLRQHAKVKERNARSVKINKRFTKLLIAPGSGAGEDELL
SQ  GTSGEPEPERARRSDTHTFNRLFRGNDDEGPRPLTVVLQGPAGIGKTMAAKKILYDWAGGKLYHSQVDFAFFMPCGELLE
SQ  RPGTRSLADLILEQCPDRTAPVRRILAQPHRLLFILDGADELPTLAAPEATPCRDPFEATSGLRVLSGLLSQELLPSARL
SQ  LVTSRNATLGRLQGRLCSPQCAEVRGFSDKDKKKYFFKFFRDERKAERAYRFVKENETLYALCFVPFVCWIVCTVLLQQM
SQ  ELGRDLSRTSKTTTSVYLLFITSMLKSAGTNGPRVQGELRMLCRLAREGILKHQAQFSEKDLERLKLQGSQVQTMFLSKK
SQ  ELPGVLETVVTYQFIDQSFQEFLAALSYLLDAEGAPGNSAGSVQMLVNSDAGLRGHLALTTRFLFGLLSTERIRDIGNHF
SQ  GCVVPGRVKQDTLRWVQGQSQPKVATVGAEKKDELKDEEAEEEEEEEEEEEEELNFGLELLYCLYETQEDDFVRQALSSL
SQ  PEMVLERVRLTRMDLEVLSYCVQCCPDGQALRLVSCGLVAAKEKKKKKKSFMNRLKGSQSTGKQPPASLLRPLCEAMITQ
SQ  QCGLSILTLSHCKLPDAVCRDLSEALKVAPSLRELGLLQNRLTEAGLRLLSQGLAWPKCKVQTLRIQMPGLQEVIHYLVI
SQ  VLQQSPVLTTLDLSGCQLPGTVVEPLCSALKHPKCGLKTLSLTSVELTENPLRELQAVKTLKPDLAIIHSKLGTHPQPLK
SQ  G
//
ID  I0J0E7;
PN  Nuclear matrix constituent protein 1;
GN  NMCP1;
OS  4679;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus matrix {ECO:0000269|PubMed:23378381}. Nucleus lamina {ECO:0000269|PubMed:23378381}. Note=Localizes at the nuclear periphery and is associated to the nucleoskeleton. {ECO:0000269|PubMed:23378381}.
DR  UNIPROT: I0J0E7;
DE  Function: Architectural component of nuclear structure that plays different roles in controlling nuclear size and morphology (By similarity). Involved in the organization of multimeric complexes in the peripheral nucleoskeleton (Probable). {ECO:0000250|UniProtKB:Q0JJ05, ECO:0000305|PubMed:23378381}.
DE  Reference Proteome: No;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0043578;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLTPQRSAWSLKSKVSSEKPRSKGKGITKNLDSAATPFPPLGLLNGGDLDRGGEDMEAWKRFKDEGLLDESICYKKDRES
SQ  LASRIIELEKDLHEYQYNMGLLLIEKKEWSSHFEEMKMRLAEAEEILKREQAAHIIALTESEKREDNLRKALGVEKQCVT
SQ  DLEKALREMRSEIAEVKYTAEKKMTEAFALEASIEEKRLDTERKLHSADAKLAEASRKSSEINRKLEDVEDRERKVQREL
SQ  NSINSERKALEKDISEQKEHLREWEKKLQDGQNRLLDGQRHINEREERINEAEGGLKKKEEELEEAKRSIEGTRNTLKRK
SQ  EEDLDVRLRSLVSKEKEIELKMKNLQKKEKDLHEIAEKLDHREREEIQKLLDEHRATLDTKKREFELELESKRKSVDEEL
SQ  KSKFAAVNKAEKEVNRKQGLISEGEKELESKMDKIKIKEKDLETKSKALKKWEESLKSDEKKLVAEKDQIMKDTHELKVS
SQ  INELESLRDALNAEQHQIAEEREKLEISKEEREQYIQKQSELKQEIEKYRNMQEELSKGIESLREEREKFEKEWESLDEK
SQ  KITLQRETKKIHEEKEKLEKWHHKDQERLRNEEANAKADIERQLEDIKLQKEAFENTMKHERLMAQEEVARRLADVTREL
SQ  ELRKHDLEMNMQKKQEEIERKLQGKEREFETRKEAELSRITSLINLNNSKLQKLRIEQDRLDREKEEVELQKKKLQEDQS
SQ  EIQRDVDTLRQLSKNLKNQRAEFIKEKECFLAAAERCKTCQNCGVSISELEMVGIIQSSAEIENADIVLPSLTDDHIEQH
SQ  MKNKGSHVTSPQTGSRVFGSGFLQKCTKIFKFSPGKNAETSATTTPLVFGEELDIAASEDAAANDNNPAADVERVTVNPS
SQ  LVFGEQLDTAASEDAAANDNNPAADVERVTVNPPPLAPVATEQNETEESSLPPENDSPPKQRGGRQSTRRGRGGKTVRRT
SQ  RTMEAVVDDAKAILGDTLIVEEAKESSQQNDEQSQGASVHTGGTSNTRQKRRRAPASEMTNSEHDVEESESQSQSISIGR
SQ  GRRKKRQTSAASEVQAPVVERRYNLRHSTVAKNSVAATLAVSDQAKVQTKASHQASHDNNQISMGDDPALEGSHKVTHTV
SQ  QKTTTASVMEVSSKPAMEETHEENIVVRSVEISEMSASEEAEGEVQGVPPIAEEPATPSSGSSTSGDIGNDDDMDDDDEE
SQ  ERHNASIGKKLWNFFTT
//
ID  A0A166B1A6;
PN  Nuclear matrix constituent protein 1;
GN  NMCP1;
OS  79200;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus matrix {ECO:0000269|PubMed:9141634}. Nucleus lamina {ECO:0000269|PubMed:9141634}. Note=Localizes at the nuclear periphery. {ECO:0000269|PubMed:9141634}.
DR  UNIPROT: A0A166B1A6;
DR  UNIPROT: O04390;
DE  Function: Architectural component of nuclear structure that plays different roles in controlling nuclear size and morphology. {ECO:0000250|UniProtKB:Q0JJ05}.
DE  Reference Proteome: Yes;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0006997;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGRVEDMGLNAKLMKLETELFDYQYNMGLLLIEKKEWTSKFEELQQVYTETKDALKQEQEAHLIAISDAEKREENLTKAL
SQ  GVEKQCVLDLEKALRDMRSDYAEIKFTSDSKLAEASALITKVEEKSLEVESKLHSADAKLAELSRKGSDIERKSHELEAR
SQ  ESALRRERLALNAEREALTDNISRQREDLREWERKLQEDEERLAEVRRLLNQREERANENDRLYQQKQSELDGEQKKIEI
SQ  IMVSLKNKEDDISSRIAKLNIKEKEADAVKHSLEVKEKDLTEFEQKLNAREQSEIQKLLDEHKAILEVKKQSFEMEMDKR
SQ  KNDFENDLQNRAVEVEKKEVEVKHLEAKLAKREHALDQKHEKLKEKEQYLASKLQDLNEREKSMKLEENKIEDERNQLLS
SQ  DKQEMLCLKAEIEKDRASTEEQRLKLSEEIERLKITEEERLELARLQSELKQEIENCRHQRELLLKEEDELKQEKMRFEK
SQ  EWEDLDERRTALMKDLKDITVQKENFEKLKHSEEDRLNNKKLDTESYVQKELDALRLTKDSFAATMEHEKAVLAERTSSE
SQ  KKQMLNDFELWKRELETKLFNEREDMENALRLREKQFDEEREKELNNINYIKEVISKEREDIKLERSRIAKEKQEILMHQ
SQ  KHLDEQHVVMQKDIGQLVSLSEKLKDQREQFFKERECFIRFVESQKSCKNCGEMTSEFVVSDLQSLAELENLKALSVPQL
SQ  AENYLRQDLQGTPDKNLSTVTPGAVGLGSPASGGTKSWLQKCTSKIFIFSASKKNNSPDQNTSRRLHVEASPNKLLNTEV
SQ  IPELPSGVAGETLEMQNMQVSNSNREMESNLNLSGTEQSNIDSKALDVEDSQQSDVRAGNRKPGKRAKGRVRRKRSAKEV
SQ  AEEAKTVLADPIELNENEHSNGLASAYTNESRGDSSLVGKRTRNSRKRNPSQPSQSAAGDVGADSEGHSDSVTAGGRQKR
SQ  RRKVVPAVQAPTGRYNLRRHKTAAPLVANGALSDPNKGKEKEIDDGGGIGEEIPDEVDGNTHLVQVTTLKKRINVVNEFS
SQ  SAGFHGINATSESQDRDAANQLVSDTMLSEEVNGTPEQSRGYQNQGDTSGAEGEDEDGDEVEHPGEVSMRKKVWKFLTT
//
ID  Q0DY81;
PN  Nuclear matrix constituent protein 1a;
GN  NMCP1A;
OS  39947;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus matrix {ECO:0000269|PubMed:15659629}. Nucleus lamina {ECO:0000269|PubMed:15659629}. Note=Forms aggregated foci in the inner nuclear matrix region (PubMed:15659629). Localizes in the nuclear periphery (PubMed:15659629). {ECO:0000269|PubMed:15659629}.
DR  UNIPROT: Q0DY81;
DR  UNIPROT: A0A0P0VNU0;
DR  UNIPROT: Q7XXP7;
DE  Function: Architectural component of nuclear structure that plays different roles in controlling nuclear size and morphology. {ECO:0000250|UniProtKB:Q0JJ05}.
DE  Reference Proteome: Yes;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0006997;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFTPQGKGWTGWSTPAPANQRSGGGAPAASAPLGKGKGTTLRVAELEQELHEYQYNMGLLLIEKKEWTAKLDEINQALTQ
SQ  KEEILKREQAAHLNAISEYERREESMRKALGVEKQCVTDLEKALREIRGEIAEVKFMSEKKITDAQSLEASLEEKRLEIE
SQ  GKLHAADAKLAEANRKKSQADRDLEEVEARQRRLEKEKLYFENERKAGEDRIKRQEDSLRDWDKKLKESQNRILDLQRSL
SQ  NDREERANENDKLFKIKQEELEEAKKALEHTKATLKIKEDDINKRLAELHLQEKEAESKNRKLEEREKKIAEREEKVSAR
SQ  EKVGLQKLLEDHNVKLESKRRDFDLQLENEKKSFDAMLVQKEADLVQREKDVRSSEEKLSKKEQVLNESKKKLEEWQNDL
SQ  DTKSNALKKWEESLQNDEKQLSEQKLQIENERKQAEMYKLELESLKATVVAEKEKILQEQNNLKLTEEERQEHIMLTAQL
SQ  KKEIDEYRMRSNSLSEETEDLRKQRQKFEEEWEQLDEKRTHLEEEAKKLNNEKKNLERWHDNEEKRLKDREDELDIKYKE
SQ  QGENLALKEKSLIDNIDHQRLENEELLKRERADLQRNLQLHRHELEMEMEKKQASKERELEEKENELNRKMDFVENELKR
SQ  AAELNESKIQKILLEKKQLQKEKEVLVEDRQKLETDKADIRRDIDSLNTLSKSLKERREAYNRDRNNLIDIFEKYKVCKN
SQ  CGVIIFEGLDALALKDSTDIEYPSLAVEADDRSPNPDTLAQETGALVNSGGRLSLLQKCSRIFKFSPRKKAEQSSEQQAV
SQ  KNTDFGARLEEASQSDDDYEPTPVYQVAYNSFDAEDLPSESGAFENEESERQDIADDVQMESSLGVADNCVDIHGTQSFD
SQ  GNTDMVVDTTIVDVDQNGKDSAVLPVVDLEPETSKQGRRQQNRKGRAKGGVKRTRSVLAVVEDAKEILGENLEVKKDDGQ
SQ  GDSVTVGGTRKRRFAGATISEQDEDSEAHSESVSLGGQRRKRRQTAAAVTQAPGEKRYNLRRTTVANAATAAQTNKKKAA
SQ  KKGSKQTVEATADDTEGTSKAEEPATGSKGASQSADDASQLPEYSQAEAGDTHGPVEVTSAEGVDIVDGIDAAPDAMPMT
SQ  PSGSELGAEQDDEEDDDSERRNQSIGKKLWSFFTT
//
ID  Q0JJ05;
PN  Nuclear matrix constituent protein 1b;
GN  NMCP1B;
OS  39947;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus matrix {ECO:0000269|PubMed:32129897}. Nucleus lamina {ECO:0000269|PubMed:32129897}. Note=Localizes predominantly at the nuclear periphery. {ECO:0000269|PubMed:32129897}.
DR  UNIPROT: Q0JJ05;
DR  UNIPROT: A0A0P0V8N9;
DR  UNIPROT: Q8LIX8;
DE  Function: Architectural component of nuclear structure that plays different roles in controlling nuclear size and morphology (Probable). Involved in the modification of chromatin accessibility by interacting with SWI3C, a component of the chromatin-remodeling complex, to thus reduce the suppression effect of the complex (PubMed:32129897). Acts as positive regulator of drought resistance and modulates root growth (PubMed:32129897). Positively regulates the expression of genes related to root growth and drought resistance (PubMed:32129897). {ECO:0000269|PubMed:32129897, ECO:0000305|PubMed:32129897}.
DE  Reference Proteome: Yes;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0006997;
GO  GO:1902584;
GO  GO:2000280;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASPRSAGGVGGGGGGGGGSGGAAAGDDAIWSKLREAGFDEESLKRRDKAALIAYISRLESEIYQYQHNLGLVLMERKEL
SQ  TSKHEQLRAASESAEIMHKRERAAQQSALAEARKKEENLKKSLGIQKECVANLEKALHDMRGETAETKVSYESKLAEALQ
SQ  LMEAAHKKFDEAEEKLLLAKSLEAESIRTHNAALRSLHDIDDREDQLRRDRISCELENEAKEKEISLQRKSLNDMKKILH
SQ  EKEEVLLKEQALLNQRDENILERLAYVTHSEKRVEEEKNILEAERKVLLEEKYKLELKMEAIVSREEALIQKESLLDKRE
SQ  SELLILQETIASKERAEIERLNQEQAIALERRKHDFESEMANKQMSFDAAMEVTRNALHQRECALSEQESVVVQRSQNLD
SQ  LQLAELASKEKALAGRSDELKEEEEKLLLHREAIHNELQKEREEIQRIKSDLEKEKAFFEEEKREAIQAQQDLAITQADR
SQ  DELLTLQMKLKEEIDSLRAQKRELMADADRLQAEKERFEIEWELIDEKKEELQKEAIRIAEERRAITEYLKNESDIIKQE
SQ  KDNLRVQFKSNSETLSREHKEFMSKMQQEHASWLSKIQQERQDLKRDIDIQRVELLNSAKARQMEIDSYLREREEEFEQK
SQ  KAKELEHINSQKEMINTKLEHVAVELQKLKDERKEATLERERREQELSEIKGTIEALNNQREKLQEQRKLLHSDREAITV
SQ  QIQQLNVLEELKIDSENKQLSLLQHDKSKLGSDINVKDNHHDNSHSSPKQRFGRKLDLSPVSTPISWVRKCAQVIFKRSP
SQ  EKSASHDQFVQNGVPKKVGDSVDVEDVNLDFAKVGQKRLNHLVSCDQTEVLEPKRKHRRSTIQKVNGGEITSNCLSALEE
SQ  KCSKNEHDEAPLGLSNTCKEHEYGDKGPENLTKPGEPASSVDVPYVNGIVDNSDSVQEEPSVEATVSATETSNVDGPEDN
SQ  NDSDEEDEEEEEEKTSSAKKLWRFLIT
//
ID  B9X187;
PN  Nuclear envelope integral membrane protein 1a;
GN  nemp1a;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}; Multi-pass membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Note=Localization in the nuclear membrane is essential for its function. Colocalizes with lamins and banf1-a/b at the nuclear envelope. {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}.
DR  UNIPROT: B9X187;
DR  UNIPROT: Q0IH41;
DR  Pfam: PF10225;
DE  Function: In concert with ran, required for proper eye development (PubMed:25946333). May be involved in the expression of early eye marker genes (PubMed:19167377). Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (By similarity). {ECO:0000250|UniProtKB:O14524, ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}.
DE  Reference Proteome: Yes;
DE  Interaction: A1L3G9; IntAct: EBI-12597651; Score: 0.40
DE  Interaction: P52301; IntAct: EBI-12596100; Score: 0.40
DE  Interaction: Q66KV4; IntAct: EBI-12596342; Score: 0.46
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0043621;
GO  GO:0001654;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGDVEGGGCRVSWGALLTLLLLPLPSLCTLASGKEPHVIKLYEGKVVRYNESKNFCYQRTYEPKWSDVWTKIQIRVNST
SQ  KMIRVTQVENEEKLKEMETFNMFDLFSSFLKEKLNDTFIYVDLYSNKTCIKVHVIDTDTYYSVALSRGFDPRLCFLFLCG
SQ  LLLFFYGDALSRSQLFFYSTGITIGMLASMLILVFMLSKLMPKKSPFVALLLGGWSVSIYIIQLVFKNLQAICSEYWQYL
SQ  LGYLGIVGFVSFAFCYKYGPLENDRSINILTWTLQLIGLLLMYISVQIQHIAVTMVVIAFCTKQIEYPVQWIYILYRKIK
SQ  RKRAKPSPPRLLTEEEYRKQGEIETRKALEELRGYCSSPDFATWKMISRIQSPKRFADFVEGSSHLTPNEVSVHEHEYGL
SQ  GGSFLEDELFGEDSDIEVEMDIEQPLYLVPRSCF
//
ID  A1L3G9;
PN  Nuclear envelope integral membrane protein 1b;
GN  nemp1b;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Note=Localization in the nuclear membrane is essential for its function. Colocalizes with lamins and banf1-a/b at the nuclear envelope. {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}.
DR  UNIPROT: A1L3G9;
DR  UNIPROT: B9X188;
DR  Pfam: PF10225;
DE  Function: In concert with ran, required for proper eye development (PubMed:25946333). May be involved in the expression of early eye marker genes (PubMed:19167377). Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (By similarity). {ECO:0000250|UniProtKB:O14524, ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}.
DE  Reference Proteome: Yes;
DE  Interaction: P50402; IntAct: EBI-12595918; Score: 0.40
DE  Interaction: B9X187; IntAct: EBI-12597651; Score: 0.40
DE  Interaction: Q7ZTB4; IntAct: EBI-12599203; Score: 0.40
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0043621;
GO  GO:0001654;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGEVEGRGCGFSLGVLVTLLVLPLPSLCTLSTEKELHVIKLYEGRMVRYNESRNFCYQRTYEPKWSDVWTKIQIRINST
SQ  KMIRVTQVDNEEKLKEMETFNMFDFFSSFLKEKLNDTFIYVNLYSNKTCVKVHLTDTDTYYSVALSRGFDPRLFFVFLCG
SQ  LLLFFYGDTLSRSQLFFYSTGITVGMLASMLILVFMLSKLMPKKSPFFALLLGGWSVSIYVIQLVFRNLQAICSEYWQYL
SQ  IVYLGIVGFVSFAFCYIYGPLENERSINILNWTLQLIGLLLMYVSVQIQHIAVTIVVIAFCTKQIEYPVQWIYILYRKIK
SQ  LKRAKPGPPRLLTEEEYRKQADVETRKALEELRECCSSPDFAAWKTISRIQSPKRFADFVEGSSHLTPNEVSVHEHEYGL
SQ  GGSFLEDELFGEDSDVEEEMEIEPPLYPIPRSVF
//
ID  Q0VCN1;
PN  NmrA-like family domain-containing protein 1;
GN  NMRAL1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Note=Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios (By similarity). {ECO:0000250}.
DR  UNIPROT: Q0VCN1;
DR  Pfam: PF05368;
DE  Function: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0042802;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADKKLVVVFGATGAQGGSVARTLLEDGTFRVRVVTRDPGQRAAKQLRLQGAEVVQGDQDDEASMELALSGAHATFIVTN
SQ  YWENCSQEQEVKQGKLLADLAKRLGLRYVVYSGLENIKKLTAGRLTVGHFDGKGEVEEYFRDIGVPMTSVRLPCYFENLL
SQ  SYFLPQKAPDGRSYLLSLPMGDVPIDGMSVADLGPVVLSLLKTPEEYVGRNIGLSTCRHTVEEYAALLTKHTGKAVRDAK
SQ  TSPEDYEKLGFPGAQDLANMFRFYALKPDRNIELTLKLNPKARRLDQWLEQHKEDFAGL
//
ID  Q5ZID0;
PN  NmrA-like family domain-containing protein 1;
GN  NMRAL1;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.
DR  UNIPROT: Q5ZID0;
DR  Pfam: PF05368;
DE  Function: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTSKKLIVVFGATGAQGGSVARALLEDGAFAVRAVTRSPGRKEAAELRRRGAELMRADQDDERSLEEALTGAHGAFVVTN
SQ  FWEHCSKEKEVAQGRRLADLSKRLGLQHVVYSGLENVKQLTKGRLEVLHFDGKGEVEEYFRAVNVPTTTIRLPFYYENFL
SQ  SSFKPQKAPQGDKLLLGLPMGDTPMDGMAVEDLGPIVLSLLKSPEQYIGQVIGLSAGKLTVAEYAAAFSQQTGKTVEDSK
SQ  ITPEEYEKLGFPGAKELADMFRFYALKPDRNVELTMKLNPKARTFQQWLADNKAAF
//
ID  Q9HBL8;
PN  NmrA-like family domain-containing protein 1;
GN  NMRAL1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Note=Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios.
DR  UNIPROT: Q9HBL8;
DR  PDB: 2EXX;
DR  PDB: 2WM3;
DR  PDB: 2WMD;
DR  PDB: 3DXF;
DR  PDB: 3E5M;
DR  Pfam: PF05368;
DR  DisGeNET: 57407;
DE  Function: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer. {ECO:0000269|PubMed:17496144, ECO:0000269|PubMed:18263583, ECO:0000269|PubMed:19254724}.
DE  Reference Proteome: Yes;
DE  Interaction: Q96CV9; IntAct: EBI-25911134; Score: 0.56
DE  Interaction: Q8ZHG0; IntAct: EBI-2862654; Score: 0.00
DE  Interaction: Q8CLT3; IntAct: EBI-2862647; Score: 0.00
DE  Interaction: Q92949; IntAct: EBI-3917340; Score: 0.37
DE  Interaction: Q99623; IntAct: EBI-21879470; Score: 0.35
DE  Interaction: Q9HBL8; IntAct: EBI-15636443; Score: 0.56
DE  Interaction: P00966; IntAct: EBI-15636475; Score: 0.52
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0042802;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDKKLVVVFGGTGAQGGSVARTLLEDGTFKVRVVTRNPRKKAAKELRLQGAEVVQGDQDDQVIMELALNGAYATFIVTN
SQ  YWESCSQEQEVKQGKLLADLARRLGLHYVVYSGLENIKKLTAGRLAAAHFDGKGEVEEYFRDIGVPMTSVRLPCYFENLL
SQ  SHFLPQKAPDGKSYLLSLPTGDVPMDGMSVSDLGPVVLSLLKMPEKYVGQNIGLSTCRHTAEEYAALLTKHTRKVVHDAK
SQ  MTPEDYEKLGFPGARDLANMFRFYALRPDRDIELTLRLNPKALTLDQWLEQHKGDFNLL
//
ID  Q8K2T1;
PN  NmrA-like family domain-containing protein 1;
GN  Nmral1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Note=Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8K2T1;
DR  UNIPROT: Q8BVF0;
DR  UNIPROT: Q9CZP2;
DR  Pfam: PF05368;
DE  Function: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16750831; Score: 0.35
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0042802;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADRKLVVVFGATGAQGGSVARALLEDGTFRIRVVTRNPEQRAAKELKQQGAEVVRGDQDDAASMELALAGAHATFIVTN
SQ  YWETCSQDREVQQPHQWDQVFKQGKLLADLAKRLGLHYVVYSGLENIRKLTAGKLAAGHFDGKGEVEEYFRDIGVPMTSV
SQ  RLPCYFENLLSYFLPQKAADGKSFLLDLPMGDVPMDGMSVSDLGPVVLSLLKKPEEYVGQNIGLSTCRHTAEEYAALLSK
SQ  HTGKAVHHAKTTPEDYEKLGFQGAQDLANMFRFYTLKPDRNIHLTLRLNPKAQTLDQWLEQHKGDFAQL
//
ID  P86172;
PN  NmrA-like family domain-containing protein 1;
GN  Nmral1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Note=Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios (By similarity). {ECO:0000250}.
DR  UNIPROT: P86172;
DR  Pfam: PF05368;
DE  Function: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042802;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  KLVVVFGATGAQGGSVARTLLEDGTFRVRVVTRNPEQKLLADLAKRLGLHYVVYSGLENIKKLAAGHFDGKGEVEEYFRK
SQ  PEEYIGQNVGLSTCRTTPEEYEKLGFQGAQDLANMFRFYALKPDRNIDLTLRAQTLDQWLEQHKGDFAHL
//
ID  Q6NRQ2;
PN  Nucleolar complex protein 4 homolog A;
GN  noc4l;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BVI4}.
DR  UNIPROT: Q6NRQ2;
DR  Pfam: PF03914;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0042254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAARKTKHACRIQDKRSDAERQDLDTKLAAVLESRGNANAVFDILEHLESKKEEVVQAAIRTASKLFEVMLEKRELYIGD
SQ  LPAENGTLPDTYSAEDKYKMWMRHRYNSCAACILDLLQHSSFSNQELALCTLMKFIQLEGKFPLENSEWKDSYRFPRELL
SQ  KFVIDNLLQEEADCTLLITRFQEYLEYDDVRYYTMTVTNDCVSRVQQKNKLVLPPVFQTNVFCLLSSINIPVEESALGNF
SQ  LVTKNVNNEDWKPSKLKDHKRVFERVWMIFLKHQLSVSLYKKVLLILHESILPHMSKPTLMIDFLTAAYDVGGAISLLAL
SQ  NGLFILIHQHNLEYPDFYKKLYSLLEPSIFHVKYRARFFHLANMFLSSTHLPVYLVAAFAKRLARLALTAPPQVLLMIIP
SQ  FICNLIRRHPACRVLIHRPSAGDLATDPYIMEEQDPAKSQALESSLWELEVLQQHYHGDVVRAANVISRPLSAQESDISG
SQ  LLEISSCELYDKEMKKKKFKSVPLEYEPVRGLLGLKSDITAQHFTF
//
ID  Q6NU91;
PN  Nucleolar complex protein 4 homolog B;
GN  noc4l;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BVI4}.
DR  UNIPROT: Q6NU91;
DR  Pfam: PF03914;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0042254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAARKAKHAFRSQATQSDAERQDLDSKLAAVLESRGNANAVFDILEHLESKKEDVVQAAIRTTSKLFEVLLEKRELYIGD
SQ  LPAEDDSPPDTCSAEDKYKMWMRNRYNSCVSCLLDLLQYSSFSVQELVLCTLMKFIQLEGKFPLENSEWRDSYRFPRELL
SQ  KFVVDNLLQEEADCTLLITRFQEYLEYDDVRYYTMTVTTECVSRIQQKNKQVLPPVFQTNVFCLLSSINMPVEESTLGNF
SQ  LVTKNENHEEWKPSKLKEQKRVFERVWMSFLKHQLSVSLYKKVLLILHESILPHMSKPSLMIDFLTAAYDVGGAISLLAL
SQ  NGLFILIHQHNLEYPDFYKKLYSLLEPSVFHVKYRARFFHLANLFLSSTHLPVYLVAAFAKRLARLALTAPPQVLLMIIP
SQ  FICNLIRRHPACRVLIHRPSAGDLVTDPYIMEEQDPAKSQALESCLWELEVLQQHYHGDVVRAANVISRALSAQESDVSG
SQ  LLEMSSCELFDKEMKKKFKSVPLEYEPVRGLLGLKSDITAEHFTF
//
ID  Q5ZJC7;
PN  Nucleolar complex protein 4 homolog;
GN  NOC4L;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BVI4}.
DR  UNIPROT: Q5ZJC7;
DR  Pfam: PF03914;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0030692;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0032040;
GO  GO:0042254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARPALAASLEAVLGDRGNANRVFEILELLAAKEEEDVLCAARTCRRLFAALLRRGELFAGSLPAEEDALRGNYSAEEKY
SQ  KIWMRHRYNDCVESLSELLGHDSFQVKESSLCTLMKFVELEAECPLVAEQWKGSIAFPRHLLKVVVNGLIPIHEDASLLI
SQ  SRFQEYMEYEDVRYFVMKVVTESIGQVMQKIKERPLPFYQQNVFSLISPINMPNKERDMVKFMMKQDNREEWKVSKLQAH
SQ  KQAFERMWLTFLKHQLPSGLYKKVLVILHDSILPYMNEPTLMIDFLTVAYGVGGAISLLALNGLFILIHQHNLEYPDFYK
SQ  KLYSLLDPSIYHVKYRARFFHLADLFLSSSHLPAYLVAAFIKRLSRLALTAPPEALLMVIPFICNLFRRHPACKVLMHRP
SQ  NGPQDLSEDPYIMEQEEPSESRALESSLWELQSLQNHYHPDVAQAAAILNQSLSEIEDDISGLLELSASELFDKEIKKTS
SQ  ANVPLEFEQVRGLFGKKNDIIAEHFALD
//
ID  Q4VBT2;
PN  Nucleolar complex protein 4 homolog;
GN  noc4l;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BVI4}.
DR  UNIPROT: Q4VBT2;
DR  Pfam: PF03914;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0030692;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0032040;
GO  GO:0042254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPSGDSNVKEHNNQVSYKKAINTKTDLILQNKKHANDIFDVIEYLQSEKEKEIIFATNACSKIFCELIERGDLFVGELP
SQ  KEEDLAQGDRSAEEKYHIFMRHRYNSCVELMLENVSHESFQVKETSLCAVMKFVATEGKHPLQNLDWSEHYNFPRELIQA
SQ  LVEHLLSEKEDMSLLISRFQEFMEKDDVRYYVMSSVRYSTATVMERNKKAVIPVFQNNVFNLLTTINIPNQASEMTNFLV
SQ  QQQSKHDDWKAAKLKEHKRAFEQMWLLFLRYKLPGSMYKKILVILHESILPQMSDPKLMMDFLSAAYDIGGAISLSALNG
SQ  LFVPIHEHNLDYPDFYKKLYNLLDPSIFHVKYRARFFHLANIFLSSTHLPVYLVAAFVKRLARLSLTAPPTALLILLPFI
SQ  CNLIRRHPSCRVLIHRPSAADEPCDDPYVMEEEDPAQCHALESSLWEIKTLQNHHHPDVSKAATMINEPLSAQEEDISEL
SQ  LELTTFELMERELKGEKKTVPLEFDMATDLLKSSREVLGVHFTLE
//
ID  Q9BVI4;
PN  Nucleolar complex protein 4 homolog;
GN  NOC4L;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:12429849}; Multi-pass membrane protein {ECO:0000269|PubMed:12429849}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
DR  UNIPROT: Q9BVI4;
DR  UNIPROT: Q8N2S5;
DR  UNIPROT: Q96I14;
DR  Pfam: PF03914;
DR  OMIM: 612819;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-754600; Score: 0.37
DE  Interaction: P59595; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: A0JLT2; IntAct: EBI-394580; Score: 0.35
DE  Interaction: O95084; IntAct: EBI-733373; Score: 0.00
DE  Interaction: Q8N6Y0; IntAct: EBI-760896; Score: 0.51
DE  Interaction: P08670; IntAct: EBI-753421; Score: 0.37
DE  Interaction: Q15038; IntAct: EBI-756433; Score: 0.37
DE  Interaction: P19012; IntAct: EBI-757027; Score: 0.67
DE  Interaction: O60232; IntAct: EBI-758122; Score: 0.37
DE  Interaction: Q9Y3Q8; IntAct: EBI-758386; Score: 0.37
DE  Interaction: P49902; IntAct: EBI-759994; Score: 0.37
DE  Interaction: Q9Y2Q3; IntAct: EBI-1081163; Score: 0.00
DE  Interaction: Q16543; IntAct: EBI-6427827; Score: 0.40
DE  Interaction: O14503; IntAct: EBI-10299708; Score: 0.56
DE  Interaction: Q13422; IntAct: EBI-10299728; Score: 0.56
DE  Interaction: Q96EY1; IntAct: EBI-10299738; Score: 0.56
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: F8VQC1; IntAct: EBI-11054725; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: Q68CZ1; IntAct: EBI-11363154; Score: 0.35
DE  Interaction: Q86VQ0; IntAct: EBI-11363336; Score: 0.35
DE  Interaction: Q9UHD9; IntAct: EBI-24319249; Score: 0.56
DE  Interaction: Q9NRD5; IntAct: EBI-24505850; Score: 0.56
DE  Interaction: Q7L775; IntAct: EBI-24607077; Score: 0.56
DE  Interaction: Q68J44; IntAct: EBI-24701942; Score: 0.56
DE  Interaction: Q9C0E8; IntAct: EBI-24439049; Score: 0.56
DE  Interaction: Q3LI70; IntAct: EBI-24542525; Score: 0.56
DE  Interaction: B2RXF5; IntAct: EBI-24550579; Score: 0.56
DE  Interaction: Q8TDS5; IntAct: EBI-24640251; Score: 0.56
DE  Interaction: C5E526; IntAct: EBI-12584981; Score: 0.35
DE  Interaction: Q86Y82; IntAct: EBI-21524609; Score: 0.35
DE  Interaction: O15400; IntAct: EBI-21528726; Score: 0.35
DE  Interaction: Q6AW86; IntAct: EBI-21553112; Score: 0.35
DE  Interaction: P22492; IntAct: EBI-21580683; Score: 0.35
DE  Interaction: O43159; IntAct: EBI-21627620; Score: 0.35
DE  Interaction: Q96IQ9; IntAct: EBI-21636586; Score: 0.35
DE  Interaction: Q15050; IntAct: EBI-21678544; Score: 0.35
DE  Interaction: Q15020; IntAct: EBI-21678189; Score: 0.35
DE  Interaction: Q5T3I0; IntAct: EBI-21681508; Score: 0.35
DE  Interaction: Q96HE9; IntAct: EBI-21733724; Score: 0.35
DE  Interaction: P62263; IntAct: EBI-21741976; Score: 0.35
DE  Interaction: Q02539; IntAct: EBI-21742951; Score: 0.35
DE  Interaction: Q9BYG3; IntAct: EBI-21743958; Score: 0.35
DE  Interaction: P18124; IntAct: EBI-21745402; Score: 0.35
DE  Interaction: P01127; IntAct: EBI-21779861; Score: 0.35
DE  Interaction: Q13895; IntAct: EBI-21815267; Score: 0.35
DE  Interaction: O94979; IntAct: EBI-21875159; Score: 0.35
DE  Interaction: Q96EB6; IntAct: EBI-15682583; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-16792282; Score: 0.27
DE  Interaction: P62753; IntAct: EBI-16798663; Score: 0.27
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21272198; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.35
DE  Interaction: O60729; IntAct: EBI-27115568; Score: 0.27
DE  Interaction: P0DTC9; IntAct: EBI-27127583; Score: 0.35
DE  Interaction: P15130; IntAct: EBI-27131516; Score: 0.35
DE  Interaction: Q0ZME3; IntAct: EBI-27131755; Score: 0.35
DE  Interaction: Q6Q1R8; IntAct: EBI-27132003; Score: 0.35
DE  Interaction: K9N4V7; IntAct: EBI-27132270; Score: 0.35
DE  Interaction: P33469; IntAct: EBI-27132272; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-30863806; Score: 0.35
GO  GO:0016021;
GO  GO:0030692;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0032040;
GO  GO:0003723;
GO  GO:0006364;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEREPGAAGVRRALGRRLEAVLASRSEANAVFDILAVLQSEDQEEIQEAVRTCSRLFGALLERGELFVGQLPSEEMVMTG
SQ  SQGATRKYKVWMRHRYHSCCNRLGELLGHPSFQVKELALSALLKFVQLEGAHPLEKSKWEGNYLFPRELFKLVVGGLLSP
SQ  EEDQSLLLSQFREYLDYDDTRYHTMQAAVDAVARVTGQHPEVPPAFWNNAFTLLSAVSLPRREPTVSSFYVKRAELWDTW
SQ  KVAHLKEHRRVFQAMWLSFLKHKLPLSLYKKVLLIVHDAILPQLAQPTLMIDFLTRACDLGGALSLLALNGLFILIHKHN
SQ  LEYPDFYRKLYGLLDPSVFHVKYRARFFHLADLFLSSSHLPAYLVAAFAKRLARLALTAPPEALLMVLPFICNLLRRHPA
SQ  CRVLVHRPHGPELDADPYDPGEEDPAQSRALESSLWELQALQRHYHPEVSKAASVINQALSMPEVSIAPLLELTAYEIFE
SQ  RDLKKKGPEPVPLEFIPAQGLLGRPGELCAQHFTLS
//
ID  Q8BHY2;
PN  Nucleolar complex protein 4 homolog;
GN  Noc4l;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BVI4}.
DR  UNIPROT: Q8BHY2;
DR  UNIPROT: Q8R1F7;
DR  Pfam: PF03914;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0030692;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0032040;
GO  GO:0042254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MERHPASASSRQELGRLLEAVLTSRGQANAVFDILAVLQSEEPEEIEEGVRTCSRLFGTLLEREELFVGSLPSEDTALAG
SQ  SQGATYKYKVWIRHRYHSCCNRLEELLAHPTFQVKELALKTLMKFVQLEGAKPLEKPQWESHYLFPRTLFRAVVGGLLTP
SQ  EDDHSLLISHFCEYLEYDDIRYHTMQVATSIMARATSQQPEVSLTLWNNAFTLLSAVSLPLQECELTNFYVKHAQTSDKW
SQ  KVVHLKEHKKAFQEMWLGFLKHKLPLSLYKKVLVAMHDSILPHLAQPTLMIDFLTSACDVGGAISLLALNGLFILIHKHN
SQ  LEYPDFYQKLYGLLDPSIFHVKYRARFFHLADLFLSSSHLPAYLVAAFAKRLARLALTAPPEALLMVLPLICNLLRRHPA
SQ  CRVMVHRPQGPELDADPYDPTEKDPARSRALESCLWELQTLQQHYHPEVSKAASVINQVLSVPEVSIAPLLELTAYEIFE
SQ  QDLKKKMPESVPLEFIPAKGLLGRQDDLCTQFFCLS
//
ID  Q5I0I8;
PN  Nucleolar complex protein 4 homolog;
GN  Noc4l;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BVI4}.
DR  UNIPROT: Q5I0I8;
DR  Pfam: PF03914;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0030692;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0032040;
GO  GO:0042254;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MERQPASTGSRQELGRLLEAVLSNRGRANAVFDILAVLQSEDPEEIKEGVRTCSRLFGTLLEREELFVGSLPCEDMALAG
SQ  SQGATYKYKVWMRHRYHSCCNRLEELLTHPSFQVKELALETLMKFVQLEGAKPLEKPQWESHYLFPRTLFRAVVGGLLTP
SQ  EDDHSLLISQFCEYLEYDDIRYHAMQVATSILARATSRQPEVSLTFWNNAFTLLSAVNLPLQEHELTNFYVKHAQTSSKW
SQ  KVVHLKEQRKAFQEMWLGFLKHKLPLSLYKKVLVAMHDSILPHLAQPTLMIDFLTSACDVGGAISLLALNGLFILIHKHN
SQ  LEYPDFYQRLYGLLDPSIFHVKYRARFFHLADLFLSSSHLPAYLVAAFAKRLARLALTAPPEALLMVLPLICNLLRRHPA
SQ  CRVMVHRPQGPELDADPYDPTEKDPARSRALESCLWELQTLQQHYHPEVSRAASVINQALSVPEVSIAPLLELTAYEIFE
SQ  QDLKKMMPESVPLEFIPAKGLLGRQDDLCTQFFCLS
//
ID  F4IMH3;
PN  Protein NUCLEOLAR COMPLEX ASSOCIATED 4;
GN  NOC4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9BVI4}; Multi-pass membrane protein {ECO:0000255}. Nucleus, nucleolus {ECO:0000269|PubMed:23382868}.
DR  UNIPROT: F4IMH3;
DR  UNIPROT: O22737;
DR  UNIPROT: Q8VZE1;
DR  Pfam: PF03914;
DE  Function: Essential protein required during embryogenesis (PubMed:15266054, PubMed:23382868). Involved in nucleolar processing of ribosomal RNA (rRNA) 40S and 90S ribosomal subunits and ribosome assembly; early in ribosome biogenesis, especially required during the maturation of 5.8S rRNA (PubMed:23382868). Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q06512, ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:23382868}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0030692;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0032040;
GO  GO:0009793;
GO  GO:0006364;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASILSKKQKKNEKYTLKELKSLGHDLLTSRSHINNLPLLLTFVSPESPPQFVVESLLSLQSFFTPLLSQLPPTSSSPSS
SQ  TKTEDPEVVFKAWLRSKFDEFVKLLLDVLVSQQSEDSLRGIVLGTLMEFVKLLNAGRFHSSIYHRLLDAIIHSEVDIEIF
SQ  LDILTSKYFKYIDVRYFTYISMEKFVKTLEASVSADRTVIENNEAESDSKESLELSVRKIYQVLSQIPPPEKQAEKSQHE
SQ  MWSGSDESISEKPTDKKKKTEKGDSTLLSPATISKRMKLKFTKAWISFLRLPLPIDVYKEVLASIHLTVIPHLSNPTMLC
SQ  DFLTKSYDIGGVVSVMALSSLFILMTQHGLEYPFFYEKLYALLVPSVFVAKHRAKFLQLLDACLKSSMLPAYLAASFTKK
SQ  LSRLSLSIPPAGSLVITALIYNLLRRNPTINHLVQEIVENADEANTEAGEHNESQPKTIKKRKLGIDYFNNQESDPKKSG
SQ  ALKSSLWEIDTLRHHYCPPVSRFISSLETNLTIRSKTTEMKIEDFCSGSYATIFGDEIRRRVKQVPLAFYKTVPTSLFAD
SQ  SDFPGWTFTIPQEEGTC
//
ID  Q9UK39;
PN  Nocturnin;
GN  NOCT;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O35710}. Nucleus {ECO:0000250|UniProtKB:O35710}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O35710}. Mitochondrion {ECO:0000269|PubMed:31147539}.
DR  UNIPROT: Q9UK39;
DR  UNIPROT: D3DNY5;
DR  UNIPROT: Q14D51;
DR  UNIPROT: Q9HD93;
DR  UNIPROT: Q9HD94;
DR  UNIPROT: Q9HD95;
DR  PDB: 6BT1;
DR  PDB: 6BT2;
DR  PDB: 6MAL;
DR  PDB: 6NF0;
DR  Pfam: PF03372;
DR  OMIM: 608468;
DR  DisGeNET: 25819;
DE  Function: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (PubMed:31147539). Shows a small preference for NADPH over NADP(+) (PubMed:31147539). Represses translation and promotes degradation of target mRNA molecules (PubMed:29860338). Plays an important role in post-transcriptional regulation of metabolic genes under circadian control (By similarity). Exerts a rhythmic post- transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis (By similarity). Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance (By similarity). Promotes adipogenesis by facilitating PPARG nuclear translocation which activates its transcriptional activity (By similarity). Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone (By similarity). Critical for proper development of early embryos (By similarity). {ECO:0000250|UniProtKB:O35710, ECO:0000269|PubMed:29860338, ECO:0000269|PubMed:31147539}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8TEM1; IntAct: EBI-21901186; Score: 0.40
DE  Interaction: O75953; IntAct: EBI-5655971; Score: 0.00
DE  Interaction: Q92614; IntAct: EBI-11030093; Score: 0.35
DE  Interaction: Q8TBP5; IntAct: EBI-21502646; Score: 0.35
DE  Interaction: Q92930; IntAct: EBI-21503027; Score: 0.35
DE  Interaction: Q15116; IntAct: EBI-21506827; Score: 0.35
DE  Interaction: Q86UE6; IntAct: EBI-21507777; Score: 0.35
DE  Interaction: Q9UK85; IntAct: EBI-21531225; Score: 0.35
DE  Interaction: Q8TDQ0; IntAct: EBI-21556046; Score: 0.35
DE  Interaction: Q13432; IntAct: EBI-21558921; Score: 0.35
DE  Interaction: P11912; IntAct: EBI-21559510; Score: 0.35
DE  Interaction: Q14627; IntAct: EBI-21561326; Score: 0.35
DE  Interaction: P49146; IntAct: EBI-21569349; Score: 0.35
DE  Interaction: Q03405; IntAct: EBI-21577545; Score: 0.35
DE  Interaction: P20309; IntAct: EBI-21598769; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-21684279; Score: 0.35
DE  Interaction: Q86VW1; IntAct: EBI-21721972; Score: 0.35
DE  Interaction: Q9NXH9; IntAct: EBI-21733282; Score: 0.35
DE  Interaction: P40967; IntAct: EBI-21773380; Score: 0.35
DE  Interaction: Q9Y6Y0; IntAct: EBI-21793294; Score: 0.35
DE  Interaction: Q9HBU6; IntAct: EBI-21793294; Score: 0.35
DE  Interaction: Q96BK5; IntAct: EBI-21793294; Score: 0.35
DE  Interaction: P11182; IntAct: EBI-21793294; Score: 0.35
DE  Interaction: O75414; IntAct: EBI-21793294; Score: 0.35
DE  Interaction: Q9NQ79; IntAct: EBI-21819334; Score: 0.35
DE  Interaction: P02746; IntAct: EBI-21828080; Score: 0.35
DE  Interaction: Q8NBA8; IntAct: EBI-21829890; Score: 0.35
DE  Interaction: P36507; IntAct: EBI-21878046; Score: 0.35
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0000175;
GO  GO:0046872;
GO  GO:0003729;
GO  GO:0019178;
GO  GO:0102757;
GO  GO:0004535;
GO  GO:0032922;
GO  GO:0000290;
GO  GO:0048255;
GO  GO:0006739;
GO  GO:0010629;
GO  GO:0045668;
GO  GO:0033962;
GO  GO:0045600;
GO  GO:0042752;
GO  GO:0045995;
GO  GO:0009991;
GO  GO:0032496;
GO  GO:0006366;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFHSPRRLCSALLQRDAPGLRRLPAPGLRRPLSPPAAVPRPASPRLLAAASAASGAARSCSRTVCSMGTGTSRLYSALAK
SQ  TLNSSAASQHPEYLVSPDPEHLEPIDPKELLEECRAVLHTRPPRFQRDFVDLRTDCPSTHPPIRVMQWNILAQALGEGKD
SQ  NFVQCPVEALKWEERKCLILEEILAYQPDILCLQEVDHYFDTFQPLLSRLGYQGTFFPKPWSPCLDVEHNNGPDGCALFF
SQ  LQNRFKLVNSANIRLTAMTLKTNQVAIAQTLECKESGRQFCIAVTHLKARTGWERFRSAQGCDLLQNLQNITQGAKIPLI
SQ  VCGDFNAEPTEEVYKHFASSSLNLNSAYKLLSADGQSEPPYTTWKIRTSGECRHTLDYIWYSKHALNVRSALDLLTEEQI
SQ  GPNRLPSFNYPSDHLSLVCDFSFTEESDGLS
//
ID  O35710;
PN  Nocturnin;
GN  Noct;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:23449310}. Nucleus {ECO:0000269|PubMed:23449310}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20498072}. Mitochondrion {ECO:0000250|UniProtKB:Q9UK39}.
DR  UNIPROT: O35710;
DR  UNIPROT: Q9QZG9;
DR  Pfam: PF03372;
DE  Function: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (By similarity). Shows a small preference for NADPH over NADP(+) (By similarity). Represses translation and promotes degradation of target mRNA molecules (By similarity). Plays an important role in post-transcriptional regulation of metabolic genes under circadian control (PubMed:20685873, PubMed:20498072). Exerts a rhythmic post-transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis (PubMed:20498072, PubMed:22082366, PubMed:21820310, PubMed:22073225, PubMed:22331129). Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance (PubMed:20498072, PubMed:22082366). Promotes adipogenesis by facilitating PPARG nuclear translocation which activates its transcriptional activity (PubMed:20498072). Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone (PubMed:22073225, PubMed:20685873). Critical for proper development of early embryos (PubMed:23449310). {ECO:0000250|UniProtKB:Q9UK39, ECO:0000269|PubMed:20498072, ECO:0000269|PubMed:20685873, ECO:0000269|PubMed:21820310, ECO:0000269|PubMed:22073225, ECO:0000269|PubMed:22082366, ECO:0000269|PubMed:22331129, ECO:0000269|PubMed:23449310}.
DE  Reference Proteome: Yes;
DE  Interaction: P37238; IntAct: EBI-15856114; Score: 0.40
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0000175;
GO  GO:0046872;
GO  GO:0003729;
GO  GO:0019178;
GO  GO:0102757;
GO  GO:0004535;
GO  GO:0032922;
GO  GO:0007623;
GO  GO:0000290;
GO  GO:0048255;
GO  GO:0006739;
GO  GO:0010629;
GO  GO:0045668;
GO  GO:0033962;
GO  GO:0045600;
GO  GO:0042752;
GO  GO:0045995;
GO  GO:0009991;
GO  GO:0032496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYQSPRRLCSALLLRDAPGLRRTLVPGPRRTLAPPVLGSRPKSPQLQAAAASGAARSRPRTVSSMGNGTSRLYSALAKTV
SQ  NSSAAAQHPEYLVSTDPEHLEPIDPKELLEECRAVLHTRPPRYQRDFVDLRTDCSSSHSPIRVMQWNILAQALGEGKDNF
SQ  VQCPVEALKWEERKCLILEEILAYQPDILCLQEVDHYFDTFQPLLSRLGYQGTFFPKPWSPCLDVEHNNGPDGCALFFLQ
SQ  NRFKLISSTNIRLTAMTLKTNQVAIAQTLECKESGRQFCIAVTHLKARTGWERFRSAQGCDLLQNLQNITQGAKIPLIVC
SQ  GDFNAEPTEEVYKHFASSSLNLNSAYKLLSPDGQSEPPYTTWKIRTSGECRHTLDYIWYSRHALSVTSALDLLTEEQIGP
SQ  NRLPSFHYPSDHLSLVCDFSFNEEPHELF
//
ID  Q9ET55;
PN  Nocturnin;
GN  Noct;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O35710}. Nucleus {ECO:0000250|UniProtKB:O35710}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O35710}. Mitochondrion {ECO:0000250|UniProtKB:Q9UK39}.
DR  UNIPROT: Q9ET55;
DR  UNIPROT: G3V7F4;
DR  Pfam: PF03372;
DE  Function: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (By similarity). Shows a small preference for NADPH over NADP(+) (By similarity). Represses translation and promotes degradation of target mRNA molecules (By similarity). Plays an important role in post-transcriptional regulation of metabolic genes under circadian control (By similarity). Exerts a rhythmic post- transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis (By similarity). Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance (By similarity). Promotes adipogenesis by facilitating PPARG nuclear translocation which activates its transcriptional activity (By similarity). Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone (By similarity). Critical for proper development of early embryos (By similarity). {ECO:0000250|UniProtKB:O35710, ECO:0000250|UniProtKB:Q9UK39}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0000175;
GO  GO:0046872;
GO  GO:0003729;
GO  GO:0019178;
GO  GO:0102757;
GO  GO:0004535;
GO  GO:0032922;
GO  GO:0007623;
GO  GO:0000290;
GO  GO:0048255;
GO  GO:0006739;
GO  GO:0010629;
GO  GO:0045668;
GO  GO:0033962;
GO  GO:0045600;
GO  GO:0042752;
GO  GO:0045995;
GO  GO:0009991;
GO  GO:0032496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MYQSPRRLCSALLLRDAPGLRRTLVPGPRRTLAPPVLGSRPASPQLQAAASGAARSRPRTVSPMGNGTSRLYSALAKTIN
SQ  SSAAAQHPEYLVSADPEHLEPIDPKELLEECRAVLHTRPPRYQRDFVDLRTDCSSSHPPIRVMQWNILAQALGEGKDNFV
SQ  QCPVEALKWEERKCLILEEILAYQPDILCLQEVDHYFDTFQPLLSRLGYQGTFFPKPWSPCLDVEHNNGPDGCALFFLQS
SQ  RFKLINSTNIRLTAMTLKTNQVAIAQTLECKESGRQFCIAVTHLKARTGWERFRSAQGCDLLQNLQNITEGAKIPLIVCG
SQ  DFNAEPTEEVYKHFASSSLNLNSAYKLLSPDGQSEPPYTTWKIRTSGECRHTLDYIWYSRHALSVTSALDLLTEEQIGPN
SQ  RLPSFHYPSDHLSLVCDFSFNEEPDELL
//
ID  P79942;
PN  Nocturnin;
GN  noct;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O35710}. Nucleus {ECO:0000250|UniProtKB:O35710}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O35710}. Mitochondrion {ECO:0000250|UniProtKB:Q9UK39}.
DR  UNIPROT: P79942;
DR  Pfam: PF03372;
DE  Function: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (By similarity). Shows a small preference for NADPH over NADP(+) (By similarity). Component of the circadian clock or downstream effector of clock function (PubMed:12573214). Exhibits a high amplitude circadian rhythm with maximal levels in early evening (PubMed:12573214). In constant darkness or constant light, the amplitude of the rhythm decreases (PubMed:12573214). {ECO:0000250|UniProtKB:Q9UK39, ECO:0000269|PubMed:12573214}.
DE  Reference Proteome: Yes;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0019178;
GO  GO:0102757;
GO  GO:0004535;
GO  GO:0032922;
GO  GO:0006739;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDAQLTYTMGLLEQGYLSARVCSMGNSTSRLYSALAKTLSSSAAVSQELLEASQHDQSEPLDPKELLDECQVALQDRPAR
SQ  LHRDFFSLRSESSSQQPRTFRVMQWNILAQALGEGKDNFIMCPMEALKWEERKYLILEEILMYQPDVLCLQEVDHYFDTF
SQ  QPILSRLGYQCTFLAKPWSPCLDVEHNNGPDGCALFFLQDRFQLVNSAKIRLSARTLKTNQVAIAETLQCCETGRQLCFA
SQ  VTHLKARTGWERFRLAQGSDLLDNLESITQGATVPLIICGDFNADPTEEVYKRFASSSLNLNSAYKLLSEDGESEPPYTT
SQ  WKIRTTGESCHTLDYIWYSQHALRVNAALGLPTEEQIGPNRLPSFNYPSDHLSLVCDFSFNEDPARLL
//
ID  O14310;
PN  Nucleoporin npp106;
GN  npp106;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:9372936}.
DR  UNIPROT: O14310;
DR  Pfam: PF04097;
DE  Function: Has a role in promoting mRNA export from the nucleus. {ECO:0000269|PubMed:9372936}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0120290;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESKEAKEKGVNTSDSKGSQIESSISDLREKSQHLFGVLLEPQVPVIQYGLNQLEEKARNLESKVLLTRDGDTKAHYLLA
SQ  ESGMNAEQTRQKIYSIHIHSPWDQLELDKKSLYEQPHTKLYNGQNVVASIENGYQSNVYEFQLRLMKNNGIAWENTKTEF
SQ  MEDVGKLLHSKDNSGLGTSISMSLRPNLARPLLTASSVKSQSVRSLREVGSNLPIPTGSLTKIDGLNNQLSNDLTRSQTT
SQ  NIFGFAEKASSFAAAVHKLNEARIRNQACHVWSLFASVSQMVNTEVIQLFDAWSLLAHMIDETRYGMGDFEARHLALDSS
SQ  SAALAVEKNCIEGSLKYLENQFLSLIDLHLSDAGHITTVNSVEKVIAYSKLRFYKNGSWIKSTVSVVNDVPLWVVLFYLM
SQ  RSGQLDAALQFVNTYSDDFEKLGRSFPLYFYSYAKNPSLPLPKQLRDRLQAEYGQLMKYAPEDPFKHAIYKLLGNCEPHR
SQ  VSLPEVCVTSEDYMWIQLMFCRVNQNDVIDSNGGQSTNSLFNLYQLEKKIVAFGPRYFNPKNNTPTNYFLALLMCGEFER
SQ  AISFLHTNYPVEATHFAVAMAYYGLLRTKNYEKNENILIYEADDVKINFPQLIIAYLKHLEYVDAAVYLDYIACIPLVPA
SQ  YQACSINLTKILLLQSHEFSKFLGDIKPDTERTTGLLDLYLRLIPFDHDSLQKLYLEGAREADDDGRFGDSIILYHLLGD
SQ  YDTVIGVAIKNLSQSIVSRGLWSIDSKESKNMHISSNVVASEAPDALAANLLAMYESNPKKSAKVSATNKKALKVLLKVV
SQ  KVQKLYGQEKWDEVLQLIEHLDLLPINEVQAEFEPNEQIPPISARLRRRAFEFSTFQDEVLSVIPSLMYISMSSIKALYR
SQ  TISKLPVVNEESKKKLQRLQFKGSMLVMFSTMIESRLSPQILEYLQAEQLTLL
//
ID  F4I1T7;
PN  Nuclear pore complex protein NUP214;
GN  NUP214;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4I1T7;
DR  UNIPROT: F4I1T6;
DR  UNIPROT: Q94C88;
DR  UNIPROT: Q9ZVV0;
DE  Function: Required for normal embryogenesis and seed viability. Involved in the first asymmetrical cell division of the zygote. Regulates the number and planes of cell divisions required for generating the normal embryo proper and suspensor, apical-basal axis, cotyledons and meristem. {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:22898497}.
DE  Reference Proteome: Yes;
GO  GO:0005739;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0009793;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0006405;
GO  GO:0010070;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRVEIEEDTEGDRISTNDYYFERIGEPISIKEDDAQYDLENPPSQPLAISERHAVLFVAHSSGFFVGRTNDVISASKNS
SQ  NGNGDKVFIQDLSLVDVPVGDVRILSLSADDSILAVTVAADIHFFSVDSLLKKDAKPSFSYSPDESGFVKDFRWRRNDKH
SQ  SYLVLSNTGKLFHGIDNAPPRHVMDAVDAVEWSSKGSYIAVAQDNSLRIFSSKFNEKRCIALSFDSWIGDSDEDCFVKVD
SQ  SIRWVRNNCILLGCFQLIEGREENYLVQVIRSPDGKISDGSTNLVALSFSDLFPCSMDDLVPVGVGPHLLFSYIDQCKLA
SQ  VTANRKSIDEHIVLLDWSSGDDKSAVSVVDIDRETFLPRIGLQENNDDNTVMGLCIDRVSIEGTVNVRSGDDELKELQPY
SQ  FVLVCLTLEGKLVMFNVASVAGRPASSDTDLASSSDIEDAYTPLIEDDLSKQSSEKHQQLNIAVQNDQKHLNTEKFSTEQ
SQ  RLPNENIFSKEFESVKSSVSGDNNKKQEPYAEKPLQVEDAQQSMIPRLSGTSFGQLPMSLGYDTNKFAGFGPALPVSEKL
SQ  QKDIFAQSNSMHLQANVESKSTAAFFGSPGLQNAILQSPQNTSSQPWSSGKSVSPPDFVSGPFPSMRDTQHKQSVQSGTG
SQ  YVNPPMSIKDKSVQVIETGRVSALSNLSPLLGQNQDTNEGVEKIEPIPSIRASQLSQQVKSSFEKSASHQQHKTPLSTGP
SQ  LRLEHNMSNQPSNINEMAREMDTLLQSIEGPGGFKDSCAFILKSNVEELEQGLESLAGKCQTWKSTIHEQQAEIQHLLDK
SQ  TIQVLAKKTYMEGMYKQTADNQYWQLWNRQKLNPELEAKRQHIMKLNKDLTHQLIELERYFNRLELDRYNEDGGHPVARR
SQ  GVPNRSAPSRRVQSLHSLHNTMSSQLAAAEQLSECLSKQMTYLKIDSPVKKNVKQELFETIGIPYDASFSSPDAVKAKNA
SQ  SSAKNLLLSSIPASINQQSRQRQSSAMKNSDPETARRRRESLDRVIFNWAAFEPPKTTVKRMLLQEQQKTGMNQQTVLSE
SQ  RLRSANNTQDRSLLHVKDHASPVVSSNKGIMESFQQDTSEAQSTPFKTRPPMPQSNSPFTISPISASKPSFNWSGNKSSN
SQ  TTSYAEESAPSQIKDTRTVSQPGGSSFLPKRPVASTVLEQTEKKAGEFKFSEAKANAFVETAAGSVQRLSTTSSGSDFES
SQ  SKGFGAQFSTMSSGAPASSFSSKSLFGFNSSSSIPGDKFTFPAVTAPLSGTPLDSTSTLFTASSAPVSSSSQDPVPASIP
SQ  ISSAPVPQTFSVTSTSTVSATGFNVPFGKPLTSVKVDLNQAAPSTPSPSPGPTAGFTFNLPALSPSSPEMVSSSTGQSSL
SQ  FPPSAPTSQVSSDQASATSSLTDSSRLFSSTSLSSTPPITPPDAFQSPQVSTPSSAVPITEPVSEPKKPEAQSSSILSTQ
SQ  STVDSVANATKTQNEPLPVKSEISNPGTTVTPVSSSGFLSGFSSGTQSSLASMAAPSFSWPGSSQPQQLSSTPAPFPASS
SQ  PTSASPFGEKKDIVDTQEDEMDEEAPEASQTTELSMGSFGGFGLGSTPNPGAPKTNPFGGPFGNATTTTSNPFNMTVPSG
SQ  ELFKPASFNFQNPQPSQPAGFGSFSVTPSQTPAQSGFGQPSQIGGGQQALGSVLGSFGQSRQIGAGLPGATFGSPTGFGG
SQ  SNPGSGLPNAPASGGFAAAGSSATGGFAAMASAGRGFAGASSTPTGGFAALASGSGGFAGAAPGGGGGGFGGLGSGTGGF
SQ  GGFAPQGSSGGFAGAAGGGGFGGFGGQAQGQAGGGGFSAFGGNSGATGKPSELFTQMRK
//
ID  O22224;
PN  Nuclear pore complex protein NUP93A;
GN  NUP93A;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: O22224;
DR  UNIPROT: Q94CF2;
DR  Pfam: PF04097;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q01525; IntAct: EBI-2355182; Score: 0.35
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0009506;
GO  GO:0017056;
GO  GO:0016973;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MANDQEMSGWTDLLHSSSKLLEQAAPSSQFPPLQRNLDQLEALSKKLKAKTLRNEAPSQSIAATRLLAREGINAEQLARD
SQ  LKSFELKTTFEDVFPAEATSVEEYLQQVHEMAMVSAIQEAQKDNVRSFNDYMMKVLEEDWRKEKRDFLQSLSRISMLPKT
SQ  NMIDTSREAHAGQLVPVGSSPRVSSTPGKELVALANIPIHEKKAYVYGEVVKKLNTSRERGMPFRPAMCFKDAYDTLGAE
SQ  VTRGKSVNMQKIWQLVQAITGEDSAVRQGVSKRMALAIGARHHLQHGHEKFIMDTIQTHPTQAALGGSVGNLQRIRAFLR
SQ  IRLRDYGVLDFDSTDARRQPPVDTTWQQIYFCLRTGYYEEAREIARSTRSSQQFAPLLTEWITTDGMVAAESAAIASEEC
SQ  EKMLRMGDRLGRTAYDKKKLLLYTIISGSRRQIERILRDLSTLFNTIEDFLWFKLSCIRDVTGGSSSVVLNDGLAPYSLD
SQ  DLQAYLNKFEPSYYTKNGKDPLVYPYVLLLSVQLLPAIMHLSKEAGDGGYNIDAVHIAISLVDHSVLSEGSGTGHKLSVM
SQ  DSNAEASSMIRQYGSMFLHHGDLQMTVEYYAQAAATVGGGQLAWSGRSNVDQQRQRNLMLKQLLTEILLRERGIYFLLGA
SQ  RGSGEEGQLGRFFPDSRLRQQFLVEAAHQCQEAGLYDKSIELQKRVGAFSAALETINKCLSEAICSLARGRLDGESRTSG
SQ  LILAGNDILETYKYYPEVSLQERERVMEQETILRELEAILSIHKLGRLGNHLDALREIAKLPFLHLDPRMPDATADVFQS
SQ  ASPYFQTCVPDLLKVALTCLDNVPDTDGSIRAMRSKIAGFLASNTHRNWPRDLYEKVARSF
//
ID  Q9NZP6;
PN  Nuclear pore-associated protein 1;
GN  NPAP1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:22694955}. Nucleus inner membrane {ECO:0000269|PubMed:22694955}. Note=Colocalizes with the NPC and nuclear lamins at the nuclear periphery.
DR  UNIPROT: Q9NZP6;
DR  OMIM: 610922;
DR  DisGeNET: 23742;
DE  Function: May be involved in spermatogenesis.
DE  Reference Proteome: Yes;
DE  Interaction: P0DOF2; IntAct: EBI-25607852; Score: 0.35
DE  Interaction: Q93009; IntAct: EBI-30844724; Score: 0.44
GO  GO:0043231;
GO  GO:0005637;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005886;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0030154;
GO  GO:0006606;
GO  GO:0006405;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGNLLSKFRPGCRRRPLPGPGRGAPAPLSRDASPPGRAHSVPTPRPFRGLFRRNARRRPSAASIFVAPKRPCPLPRAAAA
SQ  PLGVLPAVGWGLAIRKTPMLPARNPPRFGHPSSVRIPPPSRMFTLLLPSPREPAVKARKPIPATLLEETEVWAQEGPRRV
SQ  KKDEDPVQIEGEDDEKRTPLSSGEASSTSRSQGTQGDVASFRCSPGPLEGNVYHKFSENSMSEKAQASPASSCLEGPAMP
SQ  STHSQAGCARHLGKPDPDATAPPEPAVGCSLLQQKLAAEVLNEEPPPSSLGLPIPLMSGKRMPDEKPFCIPPRSAAPPRA
SQ  ARNRPCKRKMSIPLLLPLPPSLPLLWDRGELPPPAKLPCLSVEGDLHTLEKSPEYKRNSRILEDKTETMTNSSITQPAPS
SQ  FSQPVQTTDSLPLTTYTSQVSAPLPIPDLADLATGPLILPIPPLSTTPKMDEKIAFTIPNSPLALPADLVPILGDQSNEK
SQ  GGSYNSVVGAAPLTSDPPTPPSSTPSFKPPVTRESPISMCVDSPPPLSFLTLLPVPSTGTSVITSKPMNSTSVISTVTTN
SQ  ASAHLTSQTAVDPEVVNMDTTAPSQVVIFTSSLSSRVSSLPNSQIHCSAEQRHPGKTSVYTSPLPFIFHNTTPSFNQLFG
SQ  KEATPQPKFEAPDGQPQKASLPSACVFLSLPIIPPPDTSTLVNSASTASSSKPPIETNAMHTTPPSKAVILQSASVSKKY
SQ  LPFYLGLPGSGNTQPSGNTASVQGSTSLPAQSVRAPATASNHPLNPGATPQPKFGAPDGPQQKTSLPSAHDFLSLPIMVP
SQ  PDTSTLVSSASAASLSKPAIDTSDMNTTPPSKTVILQSTFVSRKEEYIRFYMGLPGSGNTLHSDSIASAQVSTSFPAQAD
SQ  RRPTTTSSHPLNTGSISHSTLGATDGQQKSDSSFILGNPATPAPVIGLTSPSVQPLSGSIIPPGFAELTSPYTALGTPVN
SQ  AEPVEGHNASAFPNGTAKTSGFRIATGMPGTGDSTLLVGNTIPGPQVIMGPGTPMDGGSIGFSMSAPGPSSTSGELNIGQ
SQ  GQSGTPSTTSVFPFGQAAWDPTGHSMAAAPQGASNIPVFGYTSAAAYIPGLDPPTQNSCSGMGGDGTRSIVGGPCVPAFQ
SQ  QCILQHTWTERKFYTSSTHYYGQETYVRRHVCFQLP
//
ID  Q9UND3;
PN  Nuclear pore complex-interacting protein family member A1;
GN  NPIPA1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11586358}. Nucleus membrane {ECO:0000269|PubMed:11586358}. Note=Colocalizes with nuclear pore complex protein NUP62.
DR  UNIPROT: Q9UND3;
DR  UNIPROT: O15102;
DR  Pfam: PF06409;
DR  OMIM: 606406;
DR  DisGeNET: 642799;
DR  DisGeNET: 9284;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P01100; IntAct: EBI-2692966; Score: 0.00
DE  Interaction: Q99816; IntAct: EBI-30840530; Score: 0.44
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFCCLGYEWLSGGCKTWHSAWVINTLADHRHRGTDFGGSPWLLIITVFLRSYKFAISLCTSYLCVSFLKTIFPSQNGHDG
SQ  STDVQQRARRSNRRRQEGIKIVLEDIFTLWRQVETKVRAKIRKMKVTTKVNRHDKINGKRKTAKEHLRKLSMKEREHGEK
SQ  ERQVSEAEENGKLDMKEIHTYMEMFQRAQALRRRAEDYYRCKITPSARKPLCNRVRMAAVEHRHSSGLPYWPYLTAETLK
SQ  NRMGHQPPPPTQQHSIIDNSLSLKTPSECLLTPLPPSALPSADDNLKTPAECLLYPLPPSADDNLKTPPECLLTPLPPSA
SQ  PPSVDDNLKTPPECVCSLPFHPQRMIISRN
//
ID  A6R538;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  2059318;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A6R538;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAPARPILLRFESRNGQFRLTVNPTDEFPSLLPKVLDNLPKNTAPPSIVLSNKPIGTGGQERNISTLKGVTIQRVGLSHG
SQ  DKLFIGYEEETAVVNGSSSEHPSSISKSQNAPRRLDGVAVRQQEQAPPVPTPTSETLIKNPWEAVKQSPLDDRLDRKDGK
SQ  ISRGLDHKMCRHGPKGMCDYCMPLEPYAPEYLAEKKIKHLSFHSYLRKINSSTNKPELKSSYIPPLSEPDYRVKRDCPSG
SQ  HPAWPEGICTKCQPSAITLQPQPFRMVDHVEFSSPDLINSLLDFWRKSGTQRLGFLYGTYEEYTEVPLGIKAVVQAIYEP
SQ  PQVGEVDGVTLHEWGNEKDVDEVAKFCGLEKIGVIFTDLLDAGAGDEIVFAAQLQARYPKATKWSETGRFGSNFVTCVLS
SQ  GDEDGAISISAYQASNSAVEMVKADIIEPSADPGVMLVQQENHSDDDASKARYIPEVFYRKVNEYGANVQENAKPSFPVE
SQ  YLLVTLTHGFPTDPDVMFNNSTFPIENREVIGESQDLRMLADKLVSHGDPNKTICGVSDFHLLCFLNSLGILNKDEEFLL
SQ  CTVARSHDTADGMQLINTSGWATLVTILQESGERPPKRSWPFQSQTFISSHQRSKHPQAPKSEHPQSDSEQLAKRFKGAS
SQ  LG
//
ID  Q74ZJ1;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q74ZJ1;
DR  Pfam: PF05021;
DR  Pfam: PF11543;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MILRFRSKHGMQRVNCEGSEQFGTVLDRWVKLVHERAPREAMEVGVAERQIETRIAAEMAQKTVEQLGLKHGDMLSVSFK
SQ  ETGGSLAVAAAPERSSELAVDRELAREEGLIRRSHSRLCRHGDRGMCEYCSPLPPWDRGYQQEQNLKHISFHAHVKELNE
SQ  HTNKKASGSTYIPPLSPPDFHVNKHCPAPHEPWPRGICSKCQPSAISLQQQEFRMVDHVEFQHSELVNEFINTWRSTGMQ
SQ  RFGYLYGRYARYDNTPLGIKAVVEAIWEPEQHDEQDGLTMDTVAVRVSVAAVDAIAADMGLMRLGMIFTDLTDSGSGDGS
SQ  VFCKRHKDSFFLSSLEVITAARHQLHHRNACRFSDQGFYSSKFVTCVVSGNLQGEIDVAAYQVSTDAEALVDADIISGST
SQ  HPSMAYINEPSAERYVPEIFYMRRNEYGITIKENAKPAFPVDYLIVSLTHGFPVAADTPPTFQAHTGFPWANRQAMGQSQ
SQ  DYLELRRVLLPSIAAGDYTELHRRLSSFHLLLYLHSLQILDASEWRRLVTVATTPAPRGVEAVYDLISGPGWQTLVMILQ
SQ  EAA
//
ID  A1CS06;
PN  Nuclear protein localization protein 4;
GN  npl4;
OS  344612;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A1CS06;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAATRPIILRFESRNGQFRLSVSPQELFPTLKQKILENLPKDVEPSSITLSNKPIGTGGEERSLDGLEGVSIEQVGLKHG
SQ  DKLFVGYQERKGGETTPAKAHAAADSLRRLNGALVPQTETVTFRPPTSSSATVKNPWEVVQQSPLDDKLDKKDGKIQRPR
SQ  DMKMCKHGPKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYMRKINAATNKAELKSSFMPPLSEPYYRVRHDCPSGHPPWP
SQ  EGICTKCQPSAISLQPQEFRMVDHVEFSSPDLINSLLDFWRKSGSQRLGFLYGTYEEYTEVPLGVKAVVQAIYEPPQVDE
SQ  VDGVTLHEWPNEKEVDEVARLCGLEKVGVIFTDLLDAGRGDGSVVCKRHIDSYYLSSLEIAFASRLQAQYPKTTKWSRTG
SQ  RFGSNFVTCVLSGDEEGAITISSYQASVSAVEMVRADIVEPSAEPSVMLVQSEDDDSDNKSRYIPEVFYRKINEYGVSAQ
SQ  QNAKPSFPVEFLLVTLTHGFPTESNPLFTKSTFPIENREVIGESQDLRSVAKKLVSHRDSNEVIPEVSDFHLLCYLHSLS
SQ  TFSKTNANRLHSKITRTVTTNLMTPQDEEKLLCRVATSHDPTEGLKLINTPGWATLVTILQESGERPPKRPWLNPADPPR
SQ  PLSQQGKRHLSSRPESPKSESEQLAKRFKGASLE
//
ID  Q4WKD7;
PN  Nuclear protein localization protein 4;
GN  npl4;
OS  330879;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q4WKD7;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAAARPIILRFESRNGQFRLSVSPQEQFPFLKEKILENLPKDVEPSSLVLSNKPIGTGGQERQLKDLTGVSIERVGLKHG
SQ  DKLFIGYQDKQASQAAPAQKHVTADVSRRLNGAPVPETETVAFHPPTSPSATIKNPWEVVQQSPLDDMLDKKDGKIYRPR
SQ  DPKMCKHGPKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYMRKVNASTNKAELKSSFMPPLTEPYYRVRRDCPSGHPPWP
SQ  EGICTKCQPSAISLQPQEFRMVDHVEFASPDLINSLLDFWRKSGAQRLGFLYGTYEEYTEVPLGIKAVVQAIYEPPQVDE
SQ  IDGITLHEWPNEKEVDEVARQCGLEKVGVIFTDLLDAGRGDGSVVCKRHIDSYYLSSLEIAFASRMQAKHPKPTKWSRTG
SQ  RFGSNFVTCVLSGDEEGAITVSSYQASISAVEMVRADIIEPSAEPSVMLVQSEDEDTDNKSRYIPEVFYRKINEYGVSAQ
SQ  QNAKPSFPVEYLLVTLTHGFPTEASPIFPASTFPIENREVIGESQELRHVAKKLVSHGDPDKAIREVSDFHLLCFLHSLS
SQ  MFSKEEEALLCRVATTHDPTEGLKLLNTPGWATLVTVLQESGERPPKRPWLNPADPPRPLSQQGKRHLPSRPESPKSESE
SQ  QLAKRFKGASLE
//
ID  A2Q8R9;
PN  Nuclear protein localization protein 4;
GN  npl4;
OS  425011;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A2Q8R9;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MASRPIVLRFESRNGQFRLTVNPQDLFPSLQPQILERLPPNVDPSSITLSNRPIGTGGEERLLNSLDGVGFDKVGLKHGD
SQ  KLFIGYQENQGQQNGTANGHITPSAGDASRRLNGAPVPQSETATIKNPWDVVQQSPLDDMLDKKDGKIKRGLDTKFCRHG
SQ  PKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYLRKINASTNKAELNSSFMPPLSEPYYRVRRDCPSGHPQWPEGICTKCQ
SQ  PSAISLQPQEFRMVDHVEFSSPDLINSLLDFWRKSGAQRLGFLYGTYEEYKEVPLGVKAVVQAIYEPPQVDEVDGVTLHE
SQ  WPNEKEVDEVAHLCGLERIGVIFTDLLDAGRGDGSVICKRHIDSYYLSSLEIAFAARMQAQHPKATKWSRTGRFGSNFVT
SQ  CVLSGDEEGAISVSAYQASVAAVEMVRADIVEPSAEPSVMLVQSEDDDTENKSRYIPEVFYRKINEYGVSAQQNAKPSFP
SQ  VEYLLVTLTHGFPTDASPLFTDSSFPIENREVIGESQELVHVAKKLVTHGDPDKAIQAVSDFHMLCFLHSLSTFNKDEEA
SQ  LLCRVATQRAPADGLQLINTPGWATLVTILQESGERPPKRPWLPTPEPYPPRSVPYNPGKRSLPSSSSSSHLRPESPKSE
SQ  SERLAKRFKGASLE
//
ID  Q2URI8;
PN  Nuclear protein localization protein 4;
GN  npl4;
OS  510516;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q2URI8;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MASRPIVLRFEGRNGQFRLTVSPQELFPSLKQKILEHLPPDTEPSSINLSNKPIGTGGDERLLDTLDGIALGTVGLKHGD
SQ  KLYLGYQEKQSLQDGSANGHITNVSSRRLNGAPVPQTETVSLRPQPTSPTAVIKNPWDVVQQSPLDDALDKKDGKIKRNR
SQ  DMKMCKHGPKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYLRKLNAATNKAELKSSFMPPLSEPYYRVRRDCPSGHPSWP
SQ  EGICTKCQPSAISLQPQEFRTVDHVEFSSPDLINSLLDFWRKSGAQRLGFLYGTYEEYTEVPLGVKAVVQAIYEPPQVDE
SQ  IDGVTLHEWHNEKEVDEVARLCGLEKVGVIFTDLLDAGQGDGSVICKRHIDSYFLSSLEITFAARLQAQYPKATKWSRTG
SQ  RFGSNFVTCVLSGDEEGAISVSAYQASVAAVEMVRADIVEPSAEPSVMLVQSEEDDSENKSRYIPEVFYRKINEYGVSAQ
SQ  QNAKPAFPVEYLLVTLTHGFPTESSPLFVEGNFPIENREVIGESQELRHVAKKLVSHGDPDKAIRAVSDFHLLCFLHSLS
SQ  TFSKDEEALLGRVATKHDPADGVQLISTPGWATLVTILQESGERPPKRPWLSSADSPRAVPQAGKRFFPSRPESPKSESE
SQ  QLAKRFKGASLE
//
ID  Q5AA50;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  237561;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q5AA50;
DR  UNIPROT: A0A1D8PDQ6;
DR  UNIPROT: Q5AAD8;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSIILRFRSKDGMFRITTDSSSNFTLVLEQLIEKLSQSGNNGNGNGNNNKIDLQSLTIANKPQDKGKSSYEFQNQTVNE
SQ  LGLKNGDMLYVNYESVTNDSGPTTTATNTTTNTASGNTIPITGPVPSIPINSVVTSHGPLKVEELPIDQELDKEDGLITR
SQ  PLSSMCRHGPKGMCEYCSPLPPWDENYRKDHAIKHISFHAYLKQQLEKLKSSGGSYFPPLDPVDYSIDLTCNQGHKPYPN
SQ  GICSKCQPSPITLQLQKFRMVDHLEFADSFILNDFINVWRVSGVQRFGYLYGRYAKSEKTPLGIKAIVETIIEPPQHDEL
SQ  DGITLLDWDQQEEKMVDQVANKFGLYKVGIIFTDLTDAGTKNGKVLCKRHKDSYFLTNLEIIMAAKFQLKYPNISKYSTA
SQ  KNNGQFSSKFVTCVISGGLNGEIEPRSYQVSTSAEALVKADIITGCTQPSQIYVNESNNHRYVPDIQYSKINKYGLEVKS
SQ  NAKPTFPGEFLLVSLTDSFPLQPTPIFTNSYVIENREFLGDENHDIQSLKTLHNYLKSNNDQIFNFHFILHLIKTHILND
SQ  QEIDLLIEYIKSKNLEDYLKLVESNGWMTLMTILEQSV
//
ID  Q6FJI2;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q6FJI2;
DR  Pfam: PF05021;
DR  Pfam: PF11543;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MIIRFRSPVGMHRVRCEGSETLGQVLPQLQTILNEHGITPRAIELGKEANGKDKTNVESLLEKTIEALGFRHGDIVYVHY
SQ  QVDSSETKGSANDNNGSVAVNIPNNLVPGKSQKADELEVDKELEKLDGLIPRQKTKLCKHGDRGMCEYCSPLPPWDANYA
SQ  NENNIKHISFHAYLKKLNESTNKRESGSSYIAPLSQPNFKINKHCTNGHEPWPKGICSKCQPSAITLQQQEFRMVDHVEF
SQ  QSSELINQFIEFWRASGTQRFAYLYGKYEKYDATPLGIKACVHAIYEPPQHDEQDGITMDMEQVTQELNTIDLLAKEMGL
SQ  LRVGMIFSDLTDAGNGDGTVLCKRHKDSFFLSSLETIMAAQHQTRHPNVSKFSEQGIFSSKFVTCVVSGNLKEEIDIASY
SQ  QVSIDAEALVSADMIGGSTHPSMAYINDTTEDRYVPEIFYMKKNEYGLTVKENAKPAFPVDYLIVSLTHGFPKDEDTTTQ
SQ  LFNSVTGFPWSNRQAMGYSQDYHELKRYLHSTAASGNFNDLHDKLANFHLLLYIHSLQILSQEEWELLVKGALSQDYQEP
SQ  LYKLSASPGWQTLLMIIESA
//
ID  Q1DY54;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  246410;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q1DY54;
DR  UNIPROT: J3KEP2;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAPPKPLILRFESRNGQFRLTVEPAELFPALLPKILSNLPQNVDPTSIALSNQPIGTGGQERKLSLLDGVSIQQVGLKHG
SQ  DKLFIGYSEQSTLVNGKSSNTSAGNMQHISRRLNGAPVPEQDLPAPPQPSSPTALIKNPWEVVQQSALDDRLDKKDGKIP
SQ  RGRDLKMCRHGPKGMCDYCMPLEPYAPEYLADKKIKHLSFHSYLRKVNSSKNKPELGSSFMPPLTEPYYRVRKDCPSGHP
SQ  AWPEGICTKCQPSAITLQPQEFRMVDHVEFASPDLINSLLDFWRKSGSQRLGFLYGTYEEYSEVPLGVKAVVQAIYEPPQ
SQ  VDEVDGITLREWENERDVDEVAKLCGLEKVGVIFTDLLDSGLGDGTVICRRHIDSYYLSSLEVAFAARLQARYPKPSKWS
SQ  ETGRFGSNFVTCILSGDENGAISISAYQASNSAVEMVRADIVEPSADPSVMLVQRENELENADTGNARYIPEVFYRKVNE
SQ  YGANVQENAKPAFPVEYLFVTLTHGFPTEPSALFADTTFPIENREVIGESQDIRNVAKKLLSRSDPDEAIRAVSNFHLLC
SQ  FMHGLGILSKEEEALLCTVARTHDPADGVQLINTPGWATLVTILQESGEPPPKRSWPFQTESSSSNKNHTRHVPLYPKTL
SQ  TSDSDQLAKRFKGASLE
//
ID  P0CP31;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  283643;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: P0CP31;
DR  UNIPROT: Q55VJ9;
DR  UNIPROT: Q5KKN9;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLLRIRSPAGTARLTVQPETTGEDFAEAILNTIPAADPQPDPATLALSNQPGAAGESVPFHALSGRTVGDMGFSHGDLLF
SQ  LSYKPRAADPDSHPAMQATAPHPQPAQPDPSHPKTHTDPPMPNTIPLRDLSSVQEPEIDQYWEKQTGKIERKRDPAFCRH
SQ  GDKAMCDYCMPLEPYDPKFQSEHQIKHLSYHAYLRKLLSSRPPTASSATDLPPLSPTSLSVITPCPTGAHPSFPDGICST
SQ  CQPSAVTLQSQPFRMVDHIEFASPSIIEGLLSAWRRTGTQRIAFLIGREDKYEKVPMGIKVIVEAVWEPKQEGELDGLTV
SQ  ETPWSDESRVQEIAKWCDKGLSVVGMIYTDLTPSPDDITKTLYKRHAQSYTASSLEMLLSAAYQLSHPLSTRMSPTGHYS
SQ  SRFVTCCLTGDKDGGVDILAWQASEHAEAMVKAGIVEASVDPAVVRVRKPGEGEYVPEVFYSYKNEYGLQVKMPAKPTFP
SQ  VEYLYVNITHGFPLAPSPLFLSNAFPTENRPGLHDQSMQVVITQLAAILKTSDAEIGDAGTWPGRIKKDVEKWLSDWHLV
SQ  TFLCMQGLFSLKEQQILCRAATAHAHPNDTYALEELFASGGWQTLLTIVDSEASANARSNPPPTSSFNNLGIDSPAFAGP
SQ  STESSAPPSGPDSVGAGAGAGPVGGRERVCPHCTFVNEHGGSDCEICGLPLDG
//
ID  P0CP30;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  214684;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: P0CP30;
DR  UNIPROT: Q55VJ9;
DR  UNIPROT: Q5KKN9;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLLRIRSPAGTARLTVQPETTGEDFAEAILNTIPAADPQPDPATLALSNQPGAAGESVPFHALSGRTVGDMGFSHGDLLF
SQ  LSYKPRAADPDSHPAMQATAPHPQPAQPDPSHPKTHTDPPMPNTIPLRDLSSVQEPEIDQYWEKQTGKIERKRDPAFCRH
SQ  GDKAMCDYCMPLEPYDPKFQSEHQIKHLSYHAYLRKLLSSRPPTASSATDLPPLSPTSLSVITPCPTGAHPSFPDGICST
SQ  CQPSAVTLQSQPFRMVDHIEFASPSIIEGLLSAWRRTGTQRIAFLIGREDKYEKVPMGIKVIVEAVWEPKQEGELDGLTV
SQ  ETPWSDESRVQEIAKWCDKGLSVVGMIYTDLTPSPDDITKTLYKRHAQSYTASSLEMLLSAAYQLSHPLSTRMSPTGHYS
SQ  SRFVTCCLTGDKDGGVDILAWQASEHAEAMVKAGIVEASVDPAVVRVRKPGEGEYVPEVFYSYKNEYGLQVKMPAKPTFP
SQ  VEYLYVNITHGFPLAPSPLFLSNAFPTENRPGLHDQSMQVVITQLAAILKTSDAEIGDAGTWPGRIKKDVEKWLSDWHLV
SQ  TFLCMQGLFSLKEQQILCRAATAHAHPNDTHALEELFASGGWQTLLTIVDSEASANARSNPPPTSSFNNLGIDSPAFAGP
SQ  STESSAPPSGPDSVGAGAGAGAGGGRERVCPHCTFVNEHGGSDCEICGLPLDG
//
ID  Q6BRJ9;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  284592;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q6BRJ9;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFRINVDAGSDFLLVLEELVGKLSTNDIQSIYISDKPNSKGEQANSLCGRSVNDLGFKNGDLLFVTYESTGEPPKTESSA
SQ  PLTTAKTTNGANVSINMNDISIPINKGPGPLKVDQLPVDGLLDKEEGMIMRPRSDLCRHGDKGMCEYCSPLPPWDKDYRK
SQ  EKGFKHMSYHAHLNEINESKNNRNNATSYMAPLEEPNYNINLNCPSGSHAPYPKGICSKCQPPVITLQQQQFRMVDHVEY
SQ  ADSTILNKFIDSWRTTGVQRFGILYGRYEQFDKVPLGIKAVVEAIYEPPQSGELDGLTLLPWENERQVDEIAASLGLYKV
SQ  GMTFTDLTDSGAKNGTVLCKRHKNSYFLSCLEVIMAAKYQVSNPNITKHSNSGRFSSKFVTCVISGGMNGEIEPRSYQVS
SQ  NSAEALIKADIITGSTQPSMLYINDSEGKRYVPDVFYSKINEYGLEVKTNAKPAFPVEFLLVSLSDSFPLDPSPMFRENF
SQ  PIENRDFMGDLQDLKSAYNYLNADPGDGSQLFDFHFLTYIAKTGILSHDELKLVLSYVRNKDQTDYLQLVESPGWMTFIT
SQ  ILEQSV
//
ID  Q5BGN5;
PN  Nuclear protein localization protein 4;
GN  npl4;
OS  227321;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q5BGN5;
DR  UNIPROT: C8VUA1;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTSRTIILRFESRNGQFRLNVSPQDMFPSLETKILEHLPPDTEPSSIKLSNKPIGAAGDERFLNTLDGVSFEQVGLRSGH
SQ  GDKLYIGYQSKQDLQDGASNGTAAGSSARRLNGAPINQEITPTSRAQADRVASVTVKNPWDAVRQSALDDRLEKKDGKIH
SQ  RSRDNKMCKHSAKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYLRKINAATNKPELKSSFMPPLSEPYYRVRTDCPSGHP
SQ  PWPEGICTKCQPSAISLQPQEYRMVDHVEFSTPDLINSLLDFWRKSGTQRLGYLYGTYEEYDEVPLGIKAVVQAIYEPPQ
SQ  VDEVDGVTLHEWENEKDVDEIARLCGLEKVGVIFTDLLDAGRGDGSVLCKRHIDSYYLSSLEIAFASRLQMQQPKATRWS
SQ  RTGYFGSNFVTCVLSGDEEGAITISSYQASVAAVEMIRADIIEPSAEPSVMLVQSEDDDTNKSRYIPEVFYRKINEYGVS
SQ  AQVNAKPAFPVEYLLVTLTHGFPTESKPLFIDSTYPIENREVIGEGQEFHSLARKLVSHGDPQKAIRAVSDFHLLCFLRT
SQ  FSTFSKEEEALLCRVATTQNPTDGLQLINTPGWATLVTILQDSGERPPKRPWLDPSHPVPQPGKRYSPSSRHESPRSESE
SQ  QLAKRFKGASLR
//
ID  Q6CLY1;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q6CLY1;
DR  Pfam: PF05021;
DR  Pfam: PF11543;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLLRLRSKLGIHRVSCEGNDNFGSVIEKWANQLRLNVDPDSVSVSTQPGVSKLMTEIAHQGVESLGLRHGDMVTVEFKVL
SQ  DTEEKNVSEKEMTNMTVSASTTSVPISSSHNKGSIRGKVKESALDIELEGETGLIPRSRSSLCRHGEKGMCEYCSPLPPW
SQ  DKGYQDEHSIKHISFHAYLKQLDEVTNKKSSGSSYIPPLSEPNYEINLNCAGGHEPWPKGICSKCQPSAITLQQQSFRMV
SQ  DHVEFQESELINQFIDSWRTTGMQRFGYLYGYYKRYDNVPLGIKAVVEAIWEPPQHDEQDGLTMDMDQVVKEVEDTDKLA
SQ  REMGLERIGMIFTDLTDTGLGDGSVYCKRHKDSFFLSSLEVIMAAKHQLRHPNVSKFSETGLFSSRFVTCCISGNLNQEI
SQ  DIATYQVSIEAEGLVEADLISGSTHPSQAYINETNDKRYVPEIFYTRKNEYNLTVKQNAKPAFPVDYLLVSLTHGFPKET
SQ  DDDSTTTANTTTVFKTVAGFPWTNRQAMGQSQDYTELKRYVYKACTGNDLAELQAKLSNFHFLLYLHSIEVLNQQEWSLL
SQ  IRTVTAPTLHEATEPLLNLINSPGWQTFVMILEQSM
//
ID  A5DX93;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  379508;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A5DX93;
DR  Pfam: PF05021;
DR  Pfam: PF11543;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSLILRFRSKDGMFRVNTDSSSTFQTVVDQLSLKLPTTDYDQITVSDKPNNKNDLGSQAKTLLSILHQTISELQLKNGDL
SQ  LFLNYSNAIPQGTLASTSSTKLQSGSIAINSSGGSSGPATASGANASTIRVSPTTHGPVKVSQLPIDDELDSQDGILSRP
SQ  ISSMCRHGAKGMCEYCSPLPPWDENYRKEHAIKHISYHAYLKQQMAKFNKKELSSSYIAPLENPNYAINLNCNEGHQSYP
SQ  RGICSKCQPLPITLQLQKFRMVDHLEYASHTILNDFINVWRSTGVQRFGYLYGRYEKFDKVPMGIKAVVEAIYEPPQHDE
SQ  LDGLTLLDWEDEPIVDAIAAKLGLQKVGIVFTDLTDSGNRDGTVLCKRHKDSYFLTNLEIIMAAKFQIKNPNITKYANLG
SQ  EFSSKFVTCVISGGLQGEIEPRSYQVSSSAEGLVKADIITGSTQPSQIYVNGNNDTRYVPDIQYSKINEYGLEVKSNAKP
SQ  TFPGEFLLVSLTDSFPIDPKPLFTSKISYVIENREFLGHGDIDGLDHLQNLSSVAKFIKLNDSELFDFHWLVHVAKMGIL
SQ  SEEELSLLCKYVKEKKYDDYLQLMESGGWMTFLTILEQST
//
ID  A4RN19;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  242507;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A4RN19;
DR  UNIPROT: G4MZE9;
DR  UNIPROT: G4MZF0;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0005829;
GO  GO:0000837;
GO  GO:0005783;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLLRLRGPDGMLRIELDPKDTFNKLGQELMGKLPPTVDPATITVSNAPGSQGDKKLLKDIAKYKVEAIGLKHGDLIFVDY
SQ  KHQGAEADGTANSDGASQPLTSTTNRLNGQPVLPTEDLPIDPLPTPAPGATIKNPWEVVRQSPLDDRLDKKDGKIPRKRD
SQ  AMCRHGPKGMCDYCQPLDPFDAKFLAEKKIKYLSMHAHLRKINSATNKPELGSSFIPPLSEPYFRVKHDCPSGHPQWPEG
SQ  ICSKCQPSAITLQPQPFRMVDHVEFASPSIVDSFINTWRRTGGQRYGIMYGKYSEYEEVPLGIKAVVQAIYEPPQVDEVD
SQ  GVSLNSWDNEKDVNQVARLCGLEPVGAIWTDLLDAGAGDGSVVCKRHADSYFLSSLEVCFAARLQAQHPKPSKWSDTGRF
SQ  GSNFVTCIISGNEQGEIAISSYQVSNEAVEMVRADIMEPSADPTVMLVREEEEDDGSTSRTRYIPDVFYRRINEYGANVQ
SQ  ENAKPSFPVEYLFVTLTHGFPDVAKPMFSDEGAFPIENREYMGESQEHSAAAKALKVHEKASSGSSKDGMKVSNFHLLCF
SQ  LHQMSVLSKDEESLLCRVATQHDLADAFQLRSTTGWQTLMAILQSTGERIPKRSRQTDVLAADPAASSYPGRRGIDDSDE
SQ  RLAKRFASVRLNARGDGRNGRDRPSAHET
//
ID  A1D4X8;
PN  Nuclear protein localization protein 4;
GN  npl4;
OS  331117;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A1D4X8;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAAARPIILRFESRNGQFRLSVSPQEQFPLLQEKILENLPKDVEPSSLVLSNKPIGTGGQERQLKDLAGVSIERVGLKHG
SQ  DKLFIGYQDKQASQAAPAHKHVTADVSRRLNGAPVPETETVTFHPPTSPSATIKNPWEVVQQSPLDDMLDKKDGKIYRPR
SQ  DPKMCNHGPKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYMRKVNATTNKAELKSSFMPPLNEPYYRVRRDCPSGHPPWP
SQ  EGICTKCQPSAISLQPQEFRMVDHVEFASPDLINSLLDFWRKSGAQRLGFLYGTYEEYTEVPLGIKAVVQAIYEPPQVDE
SQ  IDGITLHEWPNEKEVDEVARQCGLEKVGVIFTDLLDAGRGDGSVVCKRHIDSYYLSSLEIAFASRMQAKHPKATKWSRTG
SQ  RFGSNFVTCVLSGDEEGAITVSSYQASISAVEMVRADIVEPSAEPSVMLVQSEDDDTDNKSRYIPEVFYRKINEYGVSAQ
SQ  QNAKPSFPVEYLLVTLTHGFPTEASPMFSASTFPIENREVIGESQELRHVAKKLVSHGDPDKAIREVSDFHLLCFLHSLS
SQ  MFSKEEEALLCRVATTHDPTEGLKLLNTPGWATLVTVLQESGERPPKRPWLNPADPPRPLSQQGKRHLSSRPESPKSESE
SQ  QLAKRFKGASLE
//
ID  Q7SH49;
PN  Nuclear protein localization protein 4;
GN  npl4;
OS  367110;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q7SH49;
DR  UNIPROT: V5IQV4;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLLRVRGPDGMLRLTLEKDDTFADLGRQLIPKLPPTVDPKTITFSNHPTGSDAKNLSEVAKFKVGQTGLSHGDLIFVTYK
SQ  HNDAATDGPGNGEATKSSVLSSTNRLNGKPILPAEDLPIDPPPLTSPHEHIKNPWETVRQSPLDDRLDKRDGKIPRGRDH
SQ  KMCRHGPKGMCDYCMPLDPFNAKYLEEKKIKYMSVHAYLRKINSATNKPELGASFIPPLVEPYYRVKRDCPSGHPQWPEG
SQ  ICTKCQPSAITLQPQPFRMVDHVEFATPQIIDKFLNPWRMTGCQRLGILYGKYLEYDVVPLGVKAVVEAIYEPPQVDEID
SQ  GVTLNAWENEKDVNEVARLCGLEPVGVIWTDLLDAGKGDGSAICKRHSDSYFLAAQEICFAARLQAQHPKPTKWSDTGRF
SQ  GSNFVTCVISGNEQGEISISAYQMSNDAVEMVRADIIEPSTDPGQMLVREEEEDDGSVSRTRYIPEVFYRKINEYGANVQ
SQ  ENAKPAFPVEYLFVTLTHGFPESPRPVFTNDGFPIANREFVGEAQEASSVAKILKVNQKSDQFDVSNFHLLCFIRQMSVL
SQ  SKDEEALLCRVATQHDLADAFQLRATEGWRTLHMILESTGERLPKRPRTEDASFPSVDRSYLSHHPLMQRNHNSTDEPLA
SQ  KRFAAVRLNEQRPPPPPPPE
//
ID  P0C7N6;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  321614;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: P0C7N6;
DR  UNIPROT: Q0UV64;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MILRFVSKEGQFRLTVQPDSTFPELLAQIAEKLPKSVDLQSVTVSNRPQGGDARKISELKGVSFKQVGLSHGAQLFLGFE
SQ  DQSTASNGHATAPTGANRLNGKVVEASDMPSVPLGSPTQVIKNPWEVVRQSPLDDKLDRQDGKIHRKRDARMCTHGPKGM
SQ  CDYCMPLEPYAAAYLAEKKIKHLSFHSYLRKVNSAKNRPELGSSYIPPLTEPYYRVRPDCPSGHKPFPAGICTKCQPGAI
SQ  SLKPQEYRMVDHVEFASIQVVDDLINFWRNTGCQRLGFLYGRYEEYTEVPLGTKAVVETIYEPPQVNELDGISLGDWDNE
SQ  KEIDEIAAQCGLQRVGVIFTDLLDADKGDGSVICKRHIDSYYLSSLEIAFAARYQAKYPRPTKWSETGKFGSNFVTCVIS
SQ  GDDQGQIGISSYQASNDAVEMVRADIIEPSAEPSVMLVQSEDDNEALNRARYIPEVFYRRINEHGANVQENAKPDFPVEY
SQ  LFVTLTHGFPTQPNPLFTGGKFPIENREIMGEMPDVSALGKSLNAKANGLALNTTSGLNAISNFHMLCFIHNLGILSKDE
SQ  ESLLFKVASTHDTSEGSALQHTGGWATLLTILKESGERPPKRSYASPSFSATGRGAAHPGEKNRLMRQPSHGSDSDSVQL
SQ  AKRLKGASLKGKE
//
ID  A5DBC9;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  294746;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A5DBC9;
DR  Pfam: PF05021;
DR  Pfam: PF11543;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MCYFCDFASLRVSYFIINFKFQLTQIIRFRTPSGMLRVNATPETAFNDLLNDLGNQMGESDLSSFTFSDKPNDKGSSANT
SQ  FHGKSVADLGLKHGDMLYVTRTATSSSPAVTASVNEPKSGSAVVTKPINTAGIIPIHGPTKVKQLEVDDVLDTQDGMIKR
SQ  KKSNLCRHGEKGMCEYCSPLPSWDKGYREENGIKHMSFHAYVNQINEQKNNRNNSTSYMSPLEEPDYNVNLNCPSGHAPY
SQ  PKGICSKCQPPVITLQQQQFRMVDHVEFADSGILNDFIDVWRQTGVQRFGFMFGRYEVFDKVPLGIKAVVEAIYEPPQAG
SQ  ETDGITLLPWENQELVLKVAEKLNLYPVGIAFTDLTDSGARNGTVLCKRHKDTYFLSCLEVLMAARFQIEHPNITKHSNS
SQ  GRFSSKFVTCVVSGGLEGEIEPRSFQVSTNAEALVRADIITGSTQPSMLYINSSQGKRYVPDVFYSKINEYGLEVKTNAK
SQ  PAFPVDFLLVTLSDAFPLNPTPRFTNGFTIENRDFMGNLQDLRAAYRYINSDPGNGSCLSNFHFIVYLVTLGILGDSELQ
SQ  MVFD
//
ID  A3GFS1;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  322104;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A3GFS1;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSVTLRFRSREGTFRVAANPDADFLLVLEQLLSKISIEDVQNLYLSDKPNSKGELANGLCGKTVTELGLKNGDMLYASYE
SQ  AATGSNPDSTTNITTSTNNHNSGSISIGHISIPTTTSGPRKVTQLPVDDVLEKDEGLIKRPLTKFCRHGAKGMCEFCSPL
SQ  PPWDANYRKENAIKHMSYHAYLKELNELKNSKHNSSSYIAPLEEPNYSILLNCNEGHQPYPKGICSKCQPPPITLQLQKF
SQ  RMVDHVEFATSSIMNNFIDVWRHTGVQRFGVMYGRYEPFDKVPLGIKAVVEAIYEPPQSGELDGITMLPWENEAEVDAIA
SQ  SELGIYKVGVVFTDLTDSGQKNGTVLCKRHKDSYFLSNLEILMAARNQIQHANITKFSSSGQFSSKFVTCVISGGLNGEI
SQ  EPRSYQVSTSAEALVRADIITGSTQPSRLYVNSSNDRRYVPDVAYSELNEYGLEVKSNAKPTFPVDFLLVSLTDSFPVNP
SQ  TPMFDTDSNFVIENRDFFNELQNLHAVSKYLNADTSGKGTSLCNFHFLVYLKRTNILGAQEFDLLLRFVRERQYEDYLHL
SQ  VESPGWMTLITILEQST
//
ID  Q9P780;
PN  Nuclear protein localization protein 4;
GN  npl4;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q9P780;
DR  Pfam: PF05021;
DR  Pfam: PF11543;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0032473;
GO  GO:0005829;
GO  GO:0000836;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990112;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:1990116;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MILRFRSKRGMARAEFQPTDTLAMLSAKILSDILKNDYSPENVSLCQNESDQGVIFSNLNDQTLQDAGLTHGQMLYLRLG
SQ  TPNSDIASSNNEPALTVTGAPKQVSTPDVSEKKPSMPVIQDPIDDSLEKEDGLIRRSMTSLCRHGPKGMCDYCSPLEPYD
SQ  ESYRQENKIKHLSFHAYLRKINSNVNKYASSQSFIPPLEEPSFTVKEKCPSGHPPWPAGICTKCQPSTVMLNLQPFRVID
SQ  HIEFASPGIVDSFLNKWRQSGFQRIGYTYGHFEQYNNVPLGIKGVIEAIYEPPQVSEADGVTLEEWADEALVEQVATACG
SQ  LRRIGIIFTDLTDDGSNSGKVLCKRHSDSYFLSSLEVYNSANFQTKFKNPCKWSRSGYFGSKFVTSVISGNLNGEIEVMS
SQ  YQVSNIGTALYQADLIQPSVDPDRMLVKKEDQTRYVPDVLYRYTDKYGKQVSENAKPAFPVSFLLVTLTDGFPEKPDPLF
SQ  SNNDTSIITTLESTDETGRLRQLAKLFDHNAIANGSLSNFSVLLAIAKLSILGKDDLAALASYATAPTEENEKNLNSRES
SQ  YQTLLAILYSSL
//
ID  A7EGK5;
PN  Nuclear protein localization protein 4;
GN  npl4;
OS  665079;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A7EGK5;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0036266;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0072665;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLLRFRGPDGTVRIAVEANETFGQLGDKLLKLLPENLDPRTLTLSNAPSGGEVKLLMEIARAKVSQIGLKNGDMVFINYK
SQ  LLDNLPNGNSTTSTSTTHSSHLTSSTNRLNGSAVLPESIPVNVPAQAVTSPSEKIKNPWEVVQQSDLDNRLDKKDGKIPR
SQ  KRDTKMCRHGEKGMCDYCMPLEPFNAQYLAEKKIKNLSFHSYLRKINSATNKPELGSSFMPPLTEPYYRVKKNCPSGHPQ
SQ  WPEGICTKCQPSAITLQPQEFRMVDHVEFAQASLVENLLVFWRSTGAQRFGYLYGRYEEYTEVPLGVKAVVEAIYEPPQV
SQ  DELDGITLNKWESEKDVDEMARLCGMERVGVIWTDLLDSGAGDGTVICKRHIDSYYLSSLEIAFAARLQAKHPKPTKWSD
SQ  TGKFGSNFVTCVVTADETGGIAISAYQVSNTAVEMVRADIVEPSADPAVMIVRSEGDDDSDTSARYIPEVFYRKINEYGR
SQ  SVQENAKPSFPVEYLLVTLTHGFPSDPKPAFMAKNSFTIENRLVIGQEQDIKDVGKQLGLDKNGQLTQSSDGVLAVSDFH
SQ  LLCYIYSMGILSKEEMALLCRVATQHDLADGYQLIATPGWANFLAILQSTG
//
ID  A7TTC4;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  436907;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: A7TTC4;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MLLRFRSKIGMNRVSCEATDLFGDVVENWVKEVGLNVDPGTVVVGNDPGSAKEPVSNIAGRSVEEMGLKHGDIVYIEYSD
SQ  SSGSNEGQSVPVNAVGAGSAVISELPVDVLLEKEDGLIKRTRSSLCKHGDKGMCEYCSPLPPWDKEYHAENKLKHISFHS
SQ  YLKKLNEATNKKSSGSSYIPPLSQPDYKINKRCNNGHEPWPRGICSKCQPSAITLQQQEFRMVDHVEIQQSDLINQFIES
SQ  WRATGMQRFGYLYGSYEKYDSTPLGVKAVVHAIYEPPQHDEQDGLTMDLEQVEEEMQKVDQIAMSMGLLRVGLIFSDLTD
SQ  TGNGNGTVFCKRHKDSFFLSSLEIIMAAKHQLAFPNASRFSEQGKFSSKFVTCVVSGNLDSEIDITSYQVSIEAEALVDA
SQ  KMISGSTHPSMAYINETNEEVYVPEIFYMKTNEYGLTVKENAKPAFPVDYLLVSLTHGFITEDSKNQIKFHSTGGFPWAN
SQ  RQAMGLSQDYQELKNYLYSAATGGDYNLLHEKISNFHLLLYIKSLEIFNEKDWSLLITSAISENWEQPLIQLTTTESFNS
SQ  LVLIMEMI
//
ID  Q6C619;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  284591;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. {ECO:0000250}.
DR  UNIPROT: Q6C619;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MILRFRSKKGTLRAEAQPTDLFDVAFKKLTEDLPDIDPATITLATSPTGKQEPASRLLGKTVQKLGLNHGDMLFVSYTDS
SQ  APRAAVEAVTAETAPQMTAAHIRDATKQLPVDDYLEKQDGKIKRQLSALQQRKFGSRGMGEDTLPVDPWDEEYLKEQKIK
SQ  HMSYHAYVKKLNSQANKKNGGGYIAPLNVSDFGVSKSCTGAHAPWPEGICSRCQPSAITLQSQPFRMVDHVEFAESGMIN
SQ  SFIEPWRQSGTQRIGWMYGHYEPYELVPLGIKAVVEAIYEPAQSGEYDGITITEITQADGQPQPPHIATAEACGLVPLGV
SQ  IFTDLVDAGNGDGSVICKRHADSYFLSSLEVAFAGAMQARFPNKSRWSPTSEFSSKFVTAVISGNPKGEIDVSCYQVSEQ
SQ  CEAMARADLIEPSINPSVLLVKEATKTRYVPDVFYKKNNEYGRTVLQGANPQLPVDYMLVTLTHGFPQDPRPLFSSGLSS
SQ  FPVENRELIGVTQSPQALGKALDSGSAGGAVSNFHLLSYIQSMGVLSAEEFQLLAKVATEKKDEDVSRLVASEGWNNLLL
SQ  IIQ
//
ID  P33755;
PN  Nuclear protein localization protein 4;
GN  NPL4;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane.
DR  UNIPROT: P33755;
DR  UNIPROT: D6VQG6;
DR  PDB: 6JWH;
DR  PDB: 6JWI;
DR  PDB: 6JWJ;
DR  PDB: 6OA9;
DR  PDB: 6OAA;
DR  Pfam: PF05021;
DR  Pfam: PF05020;
DR  PROSITE: PS50249;
DE  Function: Substrate-recruiting cofactor of the CDC48-NPL4-UFD1 segregase (PubMed:31249135). Assists CDC48 in the dislocation of misfolded, polyubiquitinated ERAD substrates that are subsequently delivered to the proteasome for degradation (PubMed:11739805, PubMed:11740563, PubMed:11847109). Involved in the import of nuclear- targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus (PubMed:8930904, PubMed:11733065). Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1 (PubMed:11733065). Regulates ubiquitin-mediated mitochondria protein degradation (PubMed:31249135). Involved in spindle disassembly probably by promoting the degradation of spindle assemby factors ASE1 and CDC5 at the end of mitosis (PubMed:14636562). {ECO:0000269|PubMed:11733065, ECO:0000269|PubMed:11739805, ECO:0000269|PubMed:11740563, ECO:0000269|PubMed:11847109, ECO:0000269|PubMed:14636562, ECO:0000269|PubMed:31249135, ECO:0000269|PubMed:8930904}.
DE  Reference Proteome: Yes;
DE  Interaction: P53044; IntAct: EBI-390843; Score: 0.93
DE  Interaction: P32467; IntAct: EBI-792844; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-794304; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-794304; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-794304; Score: 0.35
DE  Interaction: P25694; IntAct: EBI-794304; Score: 0.91
DE  Interaction: Q04228; IntAct: EBI-805595; Score: 0.74
DE  Interaction: P41832; IntAct: EBI-818477; Score: 0.27
DE  Interaction: Q02159; IntAct: EBI-860287; Score: 0.00
DE  Interaction: P39081; IntAct: EBI-861487; Score: 0.00
DE  Interaction: P28707; IntAct: EBI-7671928; Score: 0.40
DE  Interaction: P53899; IntAct: EBI-7872468; Score: 0.40
DE  Interaction: P47113; IntAct: EBI-8221329; Score: 0.22
DE  Interaction: Q05787; IntAct: EBI-1008463; Score: 0.35
DE  Interaction: Q08109; IntAct: EBI-1008463; Score: 0.53
DE  Interaction: P38307; IntAct: EBI-7894018; Score: 0.35
DE  Interaction: Q12743; IntAct: EBI-7894121; Score: 0.35
DE  Interaction: P54860; IntAct: EBI-2343183; Score: 0.55
DE  Interaction: Q05468; IntAct: EBI-6554533; Score: 0.35
DE  Interaction: Q12532; IntAct: EBI-6554563; Score: 0.35
DE  Interaction: Q04311; IntAct: EBI-9510937; Score: 0.40
DE  Interaction: Q03935; IntAct: EBI-16251296; Score: 0.00
DE  Interaction: P04838; IntAct: EBI-21915226; Score: 0.35
GO  GO:0036266;
GO  GO:0005737;
GO  GO:0000837;
GO  GO:0000839;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030894;
GO  GO:1990112;
GO  GO:0034098;
GO  GO:0043130;
GO  GO:0031625;
GO  GO:0071629;
GO  GO:0006274;
GO  GO:0071712;
GO  GO:0072671;
GO  GO:0051228;
GO  GO:0051028;
GO  GO:0051974;
GO  GO:0070651;
GO  GO:1900182;
GO  GO:0043161;
GO  GO:0072665;
GO  GO:0006515;
GO  GO:0030970;
GO  GO:1990116;
GO  GO:0030433;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MLIRFRSKNGTHRVSCQENDLFGTVIEKLVGNLDPNADVDTFTVCEKPGQGIHAVSELADRTVMDLGLKHGDMLILNYSD
SQ  KPANEKDGVNVEIGSVGIDSKGIRQHRYGPLRIKELAVDEELEKEDGLIPRQKSKLCKHGDRGMCEYCSPLPPWDKEYHE
SQ  KNKIKHISFHSYLKKLNENANKKENGSSYISPLSEPDFRINKRCHNGHEPWPRGICSKCQPSAITLQQQEFRMVDHVEFQ
SQ  KSEIINEFIQAWRYTGMQRFGYMYGSYSKYDNTPLGIKAVVEAIYEPPQHDEQDGLTMDVEQVKNEMLQIDRQAQEMGLS
SQ  RIGLIFTDLSDAGAGDGSVFCKRHKDSFFLSSLEVIMAARHQTRHPNVSKYSEQGFFSSKFVTCVISGNLEGEIDISSYQ
SQ  VSTEAEALVTADMISGSTFPSMAYINDTTDERYVPEIFYMKSNEYGITVKENAKPAFPVDYLLVTLTHGFPNTDTETNSK
SQ  FVSSTGFPWSNRQAMGQSQDYQELKKYLFNVASSGDFNLLHEKISNFHLLLYINSLQILSPDEWKLLIESAVKNEWEESL
SQ  LKLVSSAGWQTLVMILQESG
//
ID  Q19131;
PN  Nuclear pore complex protein 5;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P57740}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:22238360}. Nucleus membrane {ECO:0000269|PubMed:22238360}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to nuclear membrane periphery during interphase and to kinetochore during mitosis. {ECO:0000269|PubMed:22238360}.
DR  UNIPROT: Q19131;
DR  Pfam: PF04121;
DE  Function: Involved in kinetochore assembly and chromosome segregation during embryonic mitosis. Required for the localization of the NDC80 complex member him-10, the chromosomal passenger complex component air- 2 and nuclear pore complex proteins npp-23 and npp-15 to kinetochores during metaphase. Required for npp-23 localization to the nuclear envelope during interphase. Recruits mdf-1, a component of the spindle assembly checkpoint, to the nuclear envelope. Appears dispensable for the assembly of the nuclear pore complex and for nuclear protein import. {ECO:0000269|PubMed:22238360}.
DE  Reference Proteome: Yes;
DE  Interaction: O17982; IntAct: EBI-339761; Score: 0.00
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0051382;
GO  GO:0006406;
GO  GO:0002119;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0008104;
GO  GO:0034501;
GO  GO:1900037;
GO  GO:0006355;
GO  GO:0010965;
GO  GO:0097298;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MTDLFASGDNSSNSFDDSNDEIARKNETAFKYTTIFHTNLSEKLYHELCALAFGEFDIPQGQISPLMWTRLHEIYSEVEM
SQ  QTRKLPAGSNYSASSQKYANEAVQIASVLSIYTALAHEYDETVEVSLLSKLVVEDVEFRRIYALLLWSEKAISEQQYEKG
SQ  LGDKVRKLEGIKSSRINSMMALKRPTFGAANAPKDASLDPDAPGTKEDQALEQMAMNVFFQLIRSGETSKAANLAIDLGM
SQ  GAIGAQLQLHSMLRNPLDIPLEASKQNFGEYKRSRRAKYYQMTQKLIEQSQGSEDDAYWMLISAIRGNIQPMLKAGKSVI
SQ  EKVWAYANSAVLARILAAEGAMTQETISTLFNVPLTSKSILDELRSEADRTKEVYILLRVIDDMLNDDIEDLYKFANETV
SQ  GEFVPNDKNCQVNMLALDIFFHLVAVSYASGFEPNDDGNAVIILGFDDLRARSGTSSHKKMAAFYSRFLPEDMKLPEIVE
SQ  TMKAVDSDEEREILAESLKQSDIDFGRCACTLIEQIRKDDKTKVVTLEEQIDHWHWLLIGGEETALAALEECNRLVRKVM
SQ  LSTPIDESVIRQIIRKALHFEVPKLLSQAVENEATVLSLITDGTLFEQKPGSQLAINKIEHAALEFYGLCSFVDVNNFMI
SQ  TIALKLGLMFKYTPITDDELSMIGGVKRLDNTTAADWEASLRVRARAEQTLREEVLKKRAAEHNTRVGMVQQHLDTVLPM
SQ  LRGLVNNIGVRPEYFLSPRANGDPMRVHRKEIQEIRNLFLPQFFILLAQAAVRLDDTTNFNDFFTSFNNDLGLDQEWMVF
SQ  IKAFYAELNLKVE
//
ID  Q32LM8;
PN  Nurim;
GN  NRM;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q32LM8;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q28181; IntAct: EBI-7079722; Score: 0.40
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPALLLIPAALASFILAFGTGVEFVRFTSLRPLLGRISESGSPDARQGWLAALQDQSILVPLVWDLGLLLLFVGQHSLM
SQ  ATETVKEWMSRYFGVLQRSLYVACTALALQLVMRYWEPVPRGPVLWETRTEPWATWVPLLCFVLHVISWLLIFSILLVFD
SQ  YAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLALLLTLYLGLAHGLDQHDLR
SQ  YLRAQLQRKLHLLSRPQDGEAE
//
ID  Q1L911;
PN  Nurim;
GN  nrm;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q1L911;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASVTFRDGFLCVSALITFVFVFVTGADFVRFVSFRAINHNLSGAAPLCRDSVPWSVALRDGVVQKAVAVDVLLLVVFSL
SQ  QHSLLAWTPVKRVCQSVFGVLSRSVYCFTTAAALQILMHYWRPVTSAPCLWSVSSAPWEIWFPLICFIVHFLCWAIICSI
SQ  LLIFDYPELLGIKQVYYECLGLGDPLLLKSERAQRLYSHLRHPVCVELLTVLWLLPSFPLDRLLLAVFLTVYLILAHSLD
SQ  KQDCAYLRHQLRNKLQLFSTPLEGSEQTNDNNKLE
//
ID  Q9VEG9;
PN  Nurim homolog;
GN  nrm;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9VEG9;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9VZB3; IntAct: EBI-214240; Score: 0.00
DE  Interaction: Q9VCT6; IntAct: EBI-232780; Score: 0.00
DE  Interaction: P25724; IntAct: EBI-278580; Score: 0.00
DE  Interaction: Q9VP16; IntAct: EBI-282406; Score: 0.00
DE  Interaction: O61307; IntAct: EBI-9927725; Score: 0.35
DE  Interaction: Q9VRP5; IntAct: EBI-9956565; Score: 0.35
DE  Interaction: Q9I7H9; IntAct: EBI-9961495; Score: 0.35
DE  Interaction: Q9VXY7; IntAct: EBI-9962220; Score: 0.35
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTSIAKSIVLLASLATFAYSLYVVGSLMMFLSTPRSISKAHTWIFNLLDNKSRLQTAYGPVVFDTLYLIGFIFQHSFLKS
SQ  AVVKKLLAKLGLSGAERTIYSLTSSLCLHYLIVNWLPAQSIVLWQIDVEQSAPLWWTFVITHGICWVVIFGGSLVMDLPE
SQ  LLGVKQAYYDLKAYGPPISYKSGELRNLYAHVRHPSFVGLSVILFATNVMSVDRLVMALLLTTYMYLAWSTDQKDVAYQK
SQ  IQLQRKKLELKAK
//
ID  Q296J9;
PN  Nurim homolog;
GN  nrm;
OS  46245;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q296J9;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATFAKVMLLLSSVATFGYTFFVVGKLMLFLSTPRSISKAHTWIFNLLDNKSRLETAYGPIVFDTLYLIGFIFQHSFLKS
SQ  ALVKNLWRKLGLAAAERTIYSLTSSICLHYLLKNWLPAQSIVLWQVDVDESAPLWWTFVVTHGLGWAVIFGGSLIMDLPE
SQ  LLGVKQVYYDLKEYGEPVAYKSSELRNLYSHVRHPSFVGLSVILFATNVMSLDRLLLASLLTVYMYVAWSTDDKDVAYQK
SQ  QQLRNKKHELKAQ
//
ID  Q8IXM6;
PN  Nurim;
GN  NRM;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:10402458, ECO:0000269|PubMed:15542857, ECO:0000269|PubMed:23092226}; Multi-pass membrane protein {ECO:0000269|PubMed:10402458, ECO:0000269|PubMed:15542857, ECO:0000269|PubMed:23092226}.
DR  UNIPROT: Q8IXM6;
DR  UNIPROT: B0S7R0;
DR  UNIPROT: B0S7R1;
DR  UNIPROT: I3XIE2;
DR  UNIPROT: I3XIE3;
DR  UNIPROT: Q5JP57;
DR  UNIPROT: Q5JP58;
DR  UNIPROT: Q5JP59;
DR  UNIPROT: Q5JP60;
DR  UNIPROT: Q8WU45;
DR  UNIPROT: Q9BSX3;
DR  UNIPROT: Q9UN92;
DR  DisGeNET: 11270;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q15125; IntAct: EBI-22753239; Score: 0.56
DE  Interaction: Q5JX71; IntAct: EBI-24729136; Score: 0.56
DE  Interaction: Q8IWR1; IntAct: EBI-10262545; Score: 0.78
DE  Interaction: Q96BA8; IntAct: EBI-10262570; Score: 0.56
DE  Interaction: Q9UH99; IntAct: EBI-10262580; Score: 0.56
DE  Interaction: Q9GZY8; IntAct: EBI-24300342; Score: 0.56
DE  Interaction: Q13323; IntAct: EBI-24267975; Score: 0.56
DE  Interaction: Q96DX8; IntAct: EBI-22747662; Score: 0.56
DE  Interaction: Q96DB2; IntAct: EBI-24267653; Score: 0.56
DE  Interaction: Q9Y5G9; IntAct: EBI-22752666; Score: 0.56
DE  Interaction: Q6NTF9; IntAct: EBI-24268630; Score: 0.56
DE  Interaction: Q8WWF3; IntAct: EBI-24268764; Score: 0.56
DE  Interaction: O95214; IntAct: EBI-22756940; Score: 0.56
DE  Interaction: Q9NP94; IntAct: EBI-22759167; Score: 0.56
DE  Interaction: P41181; IntAct: EBI-22759324; Score: 0.56
DE  Interaction: Q9H2J7; IntAct: EBI-22760321; Score: 0.56
DE  Interaction: A2A2Y4; IntAct: EBI-24623065; Score: 0.56
DE  Interaction: Q9BQA9; IntAct: EBI-24660430; Score: 0.56
DE  Interaction: Q12908; IntAct: EBI-24661936; Score: 0.56
DE  Interaction: Q3KNW5; IntAct: EBI-24678500; Score: 0.56
DE  Interaction: Q6ZVE7; IntAct: EBI-24687195; Score: 0.56
DE  Interaction: O15529; IntAct: EBI-24692000; Score: 0.56
DE  Interaction: Q5T7V8; IntAct: EBI-24694696; Score: 0.56
DE  Interaction: Q8TDV0; IntAct: EBI-23731908; Score: 0.56
DE  Interaction: Q9Y282; IntAct: EBI-24699306; Score: 0.56
DE  Interaction: Q9NR31; IntAct: EBI-24701075; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24706709; Score: 0.56
DE  Interaction: O00623; IntAct: EBI-24731075; Score: 0.56
DE  Interaction: Q9UM44; IntAct: EBI-24734285; Score: 0.56
DE  Interaction: Q9NQQ7; IntAct: EBI-24737125; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-24744570; Score: 0.56
DE  Interaction: P00387; IntAct: EBI-24769607; Score: 0.56
DE  Interaction: P30040; IntAct: EBI-24782717; Score: 0.56
DE  Interaction: P58418; IntAct: EBI-24786973; Score: 0.56
DE  Interaction: P54219; IntAct: EBI-25277809; Score: 0.56
DE  Interaction: Q6IN84; IntAct: EBI-23930500; Score: 0.56
DE  Interaction: Q16623; IntAct: EBI-24388331; Score: 0.56
DE  Interaction: P04000; IntAct: EBI-24598954; Score: 0.56
DE  Interaction: Q9BRI3; IntAct: EBI-24600461; Score: 0.56
DE  Interaction: Q9NPE6; IntAct: EBI-24640159; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-25149744; Score: 0.56
DE  Interaction: O14880; IntAct: EBI-24645409; Score: 0.56
DE  Interaction: O60930; IntAct: EBI-24649436; Score: 0.56
DE  Interaction: P34972; IntAct: EBI-24650435; Score: 0.56
DE  Interaction: O15552; IntAct: EBI-24651833; Score: 0.56
DE  Interaction: P43628; IntAct: EBI-24762668; Score: 0.56
DE  Interaction: Q460N3; IntAct: EBI-24774289; Score: 0.56
DE  Interaction: Q7Z7G2; IntAct: EBI-24789152; Score: 0.56
DE  Interaction: Q4KMG9; IntAct: EBI-24789630; Score: 0.56
DE  Interaction: P16157; IntAct: EBI-24790332; Score: 0.56
DE  Interaction: Q99437; IntAct: EBI-24799041; Score: 0.56
DE  Interaction: Q7Z5P4; IntAct: EBI-24800152; Score: 0.56
DE  Interaction: Q3SXY8; IntAct: EBI-25266505; Score: 0.56
DE  Interaction: Q96TC7; IntAct: EBI-25269247; Score: 0.56
DE  Interaction: Q8TD06; IntAct: EBI-25270864; Score: 0.56
DE  Interaction: Q8TED1; IntAct: EBI-25271666; Score: 0.56
DE  Interaction: Q01814; IntAct: EBI-21599092; Score: 0.35
DE  Interaction: Q9Y278; IntAct: EBI-21845255; Score: 0.35
DE  Interaction: Q9UBG3; IntAct: EBI-21897751; Score: 0.35
DE  Interaction: Q96DA0; IntAct: EBI-21897751; Score: 0.35
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPALLLIPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARQGWLAALQDRSILAPLAWDLGLLLLFVGQHSLM
SQ  AAERVKAWTSRYFGVLQRSLYVACTALALQLVMRYWEPIPKGPVLWEARAEPWATWVPLLCFVLHVISWLLIFSILLVFD
SQ  YAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLAFLLTLYLGLAHGLDQQDLR
SQ  YLRAQLQRKLHLLSRPQDGEAE
//
ID  Q5TM67;
PN  Nurim;
GN  NRM;
OS  9544;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q5TM67;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPALLLVPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARQGWLAALQDRSILAPLAWDLGLLLLFVGQHSLM
SQ  AAERVKAWTSRYFGVLQRSLYVACTALALQLVMRYWEPVPRGPVLWEAQAEPWATWVPLLCFVLHVISWLLIFSILLVFD
SQ  YAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGMDRLLLALLLTLYLGLAHGLDQQDLR
SQ  YLRAQLQRKLHLLSRPQDGEAE
//
ID  Q8VC65;
PN  Nurim;
GN  Nrm;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q8VC65;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005652;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPALLLVPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARHGWLAALQDRSILASLAWDLCLLLLFVVQHSLM
SQ  ATEAVKAWTSRYFGVLQRSLYVACTALALQLVMRYWETTPRGPVLWEARAEPWATWVPLLCFVLHVVSWLLIFSILLVFD
SQ  YAELMGLKQVYYHVLGLGEPLSLKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLALLFTLYLGLAHGLDQQDLR
SQ  YLRSQLQRKLHLLSRPQDGEAE
//
ID  Q1XHX8;
PN  Nurim;
GN  NRM;
OS  9598;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q1XHX8;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPALLLVPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARQGWLAALQDRSILAPLAWDLGLLLLFVGQHSLM
SQ  AAERVKAWTSRYFGVLQRSLYVACTALALQLVMRYWEPIPKGPVLWEARAEPWATWVPLLCFVLHVISWLLIFSILLVFD
SQ  YAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLAFLLTLYLGLAHGLDQQDLR
SQ  YLRAQLQRKLHLLSRPQDGEAE
//
ID  Q767L9;
PN  Nurim;
GN  NRM;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q767L9;
DR  UNIPROT: Q767K5;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPALLLVPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARQGWLAALQDQSILVPLAWDLGLLLLFVGQHSLM
SQ  ATETVKAWMSRYFGVLQRSLYVACTALALQLVMRYWEPVPRGPVLWEAQAEPWATWVPLLCFVLHVISWLLIFSILLVFD
SQ  YAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLALLLTLYLGLAHGLDQQDLR
SQ  YLRAQLQRKLHLLSRPQDGEAE
//
ID  Q6MG14;
PN  Nurim;
GN  Nrm;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6MG14;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPALLLVPAALASFVLAFGTGVEFVRFTSLRPLLGGIPESGGPDARHGWLAALQDRSILASLAWDLCLLLLFVVQHSLM
SQ  ATEAVKAWTSRYFGVLQRSLYVACTALALQLVMRYWEATPRGPVLWEARAEPWATWVPLLCFVLHVVSWLLIFSILLVFD
SQ  YAELMGLKQVYYHVLGLGEPLSLKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLALLFTLYLGLAHGLDQQDLR
SQ  YLRSQLQRKLQLLSRPQDGEAE
//
ID  Q6GNM0;
PN  Nurim;
GN  nrm;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6GNM0;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSANVQVSGQLSSGPSLPACIVLSAVSLLCFVAGFGTGAEFVRFLSFGAIFRNISGGLDGEIPLTWSEAIRNTQFQCCIG
SQ  IDIGLLFLFVLQHSLMAWTAVKKNVLHVFGVLQRSIYILCTALSLQVLMRFWQPCPHGPYLWNVSSDPWSAWLPLLCALV
SQ  HTISWLLIFSVLLIFDYAELMGIKQVYYFCLGMGDPLSHKSPRVARLYAHLRHPIYLELLLILWAVPCLPPDRLILAIFF
SQ  TLYLSLVHRLDVQDYAYLRSQLEKKFLLFSREEASAVGGQIRKNN
//
ID  Q8V3U2;
PN  Non-structural protein 1;
GN  Segment;
OS  652965;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:18304672}. Host cytoplasm {ECO:0000269|PubMed:16202469, ECO:0000269|PubMed:18304672}.
DR  UNIPROT: Q8V3U2;
DE  Function: Plays a role in inhibition of the host innate immune system by counteracting the type I interferon signaling. {ECO:0000269|PubMed:16202469, ECO:0000269|PubMed:18304672}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0039502;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGFNFEVMVPEQGGKVVFSLTETGSCVSFYGDDEPGEGSCELASENMDFPSCPLGNGDDFCLSLALSTMRWSGMTKRNN
SQ  FMDRFIGSFVHCTPVMIWSYGNLSKKSHHKMVCHTCPDEYKFSDKDEMQGYYEECLEASTDIFLDELATVVTGGFFPVGL
SQ  KGSWGGWYLKYVRYAGPLAGSSGFIVNQRFYDRAQNKTGSRVVSMVEMDGDGLSFIYEKPSVYHSDGCTGSAARFWKRDH
SQ  NERAGVELRAGLHFRM
//
ID  P0DTC7;
PN  ORF7a protein;
GN  7a;
OS  2697049;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:33930332}. Virion {ECO:0000250|UniProtKB:P59635}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P59635}; Single-pass membrane protein {ECO:0000250|UniProtKB:P59635}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:P59635}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P59635}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P59635}; Single-pass membrane protein {ECO:0000250|UniProtKB:P59635}.
DR  UNIPROT: P0DTC7;
DR  PDB: 6W37;
DR  PDB: 7CI3;
DR  Pfam: PF08779;
DR  PROSITE: PS51919;
DE  Function: Plays a role as antagonist of host tetherin (BST2), disrupting its antiviral effect. Acts by binding to BST2 and sequestering it to perinuclear region, thereby preventing its antiviral function at cell membrane. {ECO:0000269|PubMed:33930332}.
DE  Reference Proteome: Yes;
DE  Interaction: O15027; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q9NU22; IntAct: EBI-25491332; Score: 0.64
DE  Interaction: Q7Z4Q2; IntAct: EBI-25491332; Score: 0.53
DE  Interaction: P0DTD1; IntAct: EBI-25508859; Score: 0.62
DE  Interaction: P30153; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P06576; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P40939; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q8IXB1; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q9UHI6; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: O95816; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P53007; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q96EY1; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: O43852; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q9H936; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P62195; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P30876; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q99615; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P55786; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P57678; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: O75746; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P34932; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q15008; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q9UNM6; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: O60884; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P62191; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P51665; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P53618; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q9NZ01; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P35998; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q13200; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P53621; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q5H9R7; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q99460; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: O43592; IntAct: EBI-25510184; Score: 0.53
DE  Interaction: Q9NXS2; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P46379; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q16891; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: O95347; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P35606; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q9UBF2; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q9P035; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: O14980; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: Q96CS3; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: O60784; IntAct: EBI-26495729; Score: 0.35
DE  Interaction: Q9Y5K5; IntAct: EBI-26495729; Score: 0.35
DE  Interaction: Q13535; IntAct: EBI-26495729; Score: 0.53
DE  Interaction: Q9Y385; IntAct: EBI-26495729; Score: 0.35
DE  Interaction: Q6NUT2; IntAct: EBI-26495729; Score: 0.35
DE  Interaction: Q13586; IntAct: EBI-26495729; Score: 0.35
DE  Interaction: P14314; IntAct: EBI-26495729; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-26495729; Score: 0.35
DE  Interaction: P48741; IntAct: EBI-26495729; Score: 0.35
DE  Interaction: Q13315; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9H0H0; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q6P9B9; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9Y6D6; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9Y617; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9UI26; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9UI09; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9NVI1; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9HD20; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9HAV4; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9H9P8; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9H7D0; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9H6E5; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9H0V1; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9BXW9; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q9BSE5; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q96JJ3; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q96JB2; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q96HW7; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q96CB8; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q8WTW3; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q8TB37; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q8NCM8; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q8N9R8; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q8N201; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q8N1F8; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q86XI2; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q86UT6; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q75QN2; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q70CQ2; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q6YHU6; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q6P3X3; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q63HN8; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q5UIP0; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q53R41; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q29RF7; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q15386; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q14746; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: Q01813; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P83436; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P42695; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P21359; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P11498; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P04181; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: O95759; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: O94822; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: O75063; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: O60518; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: O43156; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: O14981; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P0DTC7; IntAct: EBI-27121790; Score: 0.37
DE  Interaction: P0DTC5; IntAct: EBI-27121890; Score: 0.37
DE  Interaction: P0DTD8; IntAct: EBI-27121899; Score: 0.37
DE  Interaction: P43353; IntAct: EBI-27127130; Score: 0.40
DE  Interaction: P31639; IntAct: EBI-27128324; Score: 0.27
DE  Interaction: Q10589; IntAct: EBI-28948095; Score: 0.40
GO  GO:0044167;
GO  GO:0044173;
GO  GO:0044178;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0055036;
GO  GO:0039646;
GO  GO:0039587;
GO  GO:0039502;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKIILFLALITLATCELYHYQECVRGTTVLLKEPCSSGTYEGNSPFHPLADNKFALTCFSTQFAFACPDGVKHVYQLRAR
SQ  SVSPKLFIRQEEVQELYSPIFLIVAAIVFITLCFTLKRKTE
//
ID  Q6PFJ7;
PN  Sphingomyelin phosphodiesterase 4;
GN  smpd4;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NXE4}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NXE4}; Single-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NXE4}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q6ZPR5}.
DR  UNIPROT: Q6PFJ7;
DR  Pfam: PF14724;
DE  Function: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. It has a relevant role in the homeostasis of membrane sphingolipids, thereby influencing membrane integrity, and endoplasmic reticulum organization and function. May sensitize cells to DNA damage-induced apoptosis. {ECO:0000250|UniProtKB:Q9NXE4}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0042383;
GO  GO:0046872;
GO  GO:0004767;
GO  GO:0050290;
GO  GO:0071356;
GO  GO:0046513;
GO  GO:0046475;
GO  GO:0006685;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAASALQQPSYLLANLKADWTNKPLHQRCHELCKIIDDYPAKELHAIFPWLVECVFGSLDGILTGWNLRFLQARSAEYSI
SQ  AMEFLDPSGPMMKLVYKLQAEEYKYEFPISYLPGPIKSSIHAGVLPDCPLFHNKIQFPMSGLLFLNPFEYYMFNFASSLI
SQ  APKNYPQGQHGSSSDSAYFVLVDTYLKYFLPTEGNVPPSPFSDTRGTVASPAPRSTNVPYVGYGGHSTSLLKRHITHQSS
SQ  VNADPAAQEIWRSETLLQVFVEMWLHHYSLEMYQKLQSPQVKEPFMPSEEHVLVVRLLVKHLHTFSSSLKPESISSSPSA
SQ  HSHSSPLEELKRVVVQRFVQQKLYVFLQHCFGHWPLDASFRAVLETWLSYIQPWRYTGDKNNTQTDGPNRTVPDKWASFV
SQ  QENLLLYTKLFQGFLNRAMRTDLVNAKNALMVFRVAKVFAQPSLSEMIQKGEQLFLEPEHAILQRHNRVFLTPSHGGSFL
SQ  SARQPMGTDNVFKVKSHVYSLEGQDCQYNLMFGPDQRKNVLKLIQIIAQARQTAKRISDHSTEMAANNSFLSWFGVGSPD
SQ  HNSTFTGGEMDEMGGEGVKKTHEFLDKALDYLCQIFRLNAGQLSQLISNVASVDNNGASKQLPDCIPSENGLVLTDLGRL
SQ  QIINGLRRFEIEYQGDPELQPIRSYENAFLVRLLFQISSFINERLGEHMEVLCSRQDFLGSVGRHYLSSSSAVVEQRRKS
SQ  PVTRQMRDRPQRARLSLRALASYRTLLTLLLLYMLFALLSFGLFSSTGLILIISFLYELLSNFFHEKLKTH
//
ID  Q9NXE4;
PN  Sphingomyelin phosphodiesterase 4;
GN  SMPD4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16517606, ECO:0000269|PubMed:18505924, ECO:0000269|PubMed:31495489}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16517606}; Single-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:31495489}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q6ZPR5}.
DR  UNIPROT: Q9NXE4;
DR  UNIPROT: B1PBA3;
DR  UNIPROT: B4DM23;
DR  UNIPROT: B4DQ31;
DR  UNIPROT: B4DRB8;
DR  UNIPROT: B4DWK7;
DR  UNIPROT: B4E0L6;
DR  UNIPROT: E7ESA2;
DR  UNIPROT: E9PCE6;
DR  UNIPROT: Q6FI76;
DR  UNIPROT: Q6P1P7;
DR  UNIPROT: Q6ZT43;
DR  UNIPROT: Q9H0M2;
DR  UNIPROT: Q9NW20;
DR  UNIPROT: Q9NWL2;
DR  UNIPROT: Q9P2C9;
DR  Pfam: PF14724;
DR  OMIM: 610457;
DR  OMIM: 618622;
DR  DisGeNET: 55627;
DE  Function: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide (PubMed:16517606, PubMed:25180167). It has a relevant role in the homeostasis of membrane sphingolipids, thereby influencing membrane integrity, and endoplasmic reticulum organization and function (PubMed:31495489). May sensitize cells to DNA damage-induced apoptosis (PubMed:18505924). In skeletal muscle, mediates TNF-stimulated oxidant production (By similarity). {ECO:0000250|UniProtKB:Q6ZPR5, ECO:0000269|PubMed:16517606, ECO:0000269|PubMed:18505924, ECO:0000269|PubMed:25180167, ECO:0000269|PubMed:31495489}.
DE  Disease: Neurodevelopmental disorder with microcephaly, arthrogryposis, and structural brain anomalies (NEDMABA) [MIM:618622]: An autosomal recessive disorder characterized by severe global developmental delay, severely impaired intellectual development with poor or absent speech, severe encephalopathy, microcephaly with simplified gyral pattern, hypomyelination, thin corpus callosum, mild cerebellar hypoplasia, brainstem hypoplasia, congenital arthrogryposis, dysmorphic features, and respiratory problems often leading to early demise. {ECO:0000269|PubMed:31495489}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P04626; IntAct: EBI-25368491; Score: 0.37
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8NEF9; IntAct: EBI-20919780; Score: 0.40
DE  Interaction: Q9NPD3; IntAct: EBI-373650; Score: 0.00
DE  Interaction: Q9HAW0; IntAct: EBI-1067955; Score: 0.00
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: P55318; IntAct: EBI-11317309; Score: 0.35
DE  Interaction: Q99853; IntAct: EBI-11317404; Score: 0.35
DE  Interaction: O00358; IntAct: EBI-11317831; Score: 0.35
DE  Interaction: O75593; IntAct: EBI-11318125; Score: 0.35
DE  Interaction: Q12951; IntAct: EBI-11318187; Score: 0.35
DE  Interaction: Q6ZQN5; IntAct: EBI-11318220; Score: 0.35
DE  Interaction: Q12952; IntAct: EBI-11318689; Score: 0.35
DE  Interaction: P58012; IntAct: EBI-11318924; Score: 0.35
DE  Interaction: Q15562; IntAct: EBI-11320344; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11372136; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q1K9H5; IntAct: EBI-12588354; Score: 0.35
DE  Interaction: P05161; IntAct: EBI-16720078; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q9NWW5; IntAct: EBI-20626000; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P59635; IntAct: EBI-25688593; Score: 0.35
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: Q6J9G0; IntAct: EBI-28941708; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
DE  Interaction: O15146; IntAct: EBI-32724025; Score: 0.27
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0042383;
GO  GO:0005802;
GO  GO:0046872;
GO  GO:0004767;
GO  GO:0050290;
GO  GO:0071356;
GO  GO:0046513;
GO  GO:0007029;
GO  GO:0046475;
GO  GO:0006685;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MTTFGAVAEWRLPSLRRATLWIPQWFAKKAIFNSPLEAAMAFPHLQQPSFLLASLKADSINKPFAQQCQDLVKVIEDFPA
SQ  KELHTIFPWLVESIFGSLDGVLVGWNLRCLQGRVNPVEYSIVMEFLDPGGPMMKLVYKLQAEDYKFDFPVSYLPGPVKAS
SQ  IQECILPDSPLYHNKVQFTPTGGLGLNLALNPFEYYIFFFALSLITQKPLPVSLHVRTSDCAYFILVDRYLSWFLPTEGS
SQ  VPPPLSSSPGGTSPSPPPRTPAIPFASYGLHHTSLLKRHISHQTSVNADPASHEIWRSETLLQVFVEMWLHHYSLEMYQK
SQ  MQSPHAKLEVLHYRLSVSSALYSPAQPSLQALHAYQESFTPTEEHVLVVRLLLKHLHAFANSLKPEQASPSAHSHATSPL
SQ  EEFKRAAVPRFVQQKLYLFLQHCFGHWPLDASFRAVLEMWLSYLQPWRYAPDKQAPGSDSQPRCVSEKWAPFVQENLLMY
SQ  TKLFVGFLNRALRTDLVSPKHALMVFRVAKVFAQPNLAEMIQKGEQLFLEPELVIPHRQHRLFTAPTFTGSFLSPWPPAV
SQ  TDASFKVKSHVYSLEGQDCKYTPMFGPEARTLVLRLAQLITQAKHTAKSISDQCAESPAGHSFLSWLGFSSMDTNGSYTA
SQ  NDLDEMGQDSVRKTDEYLEKALEYLRQIFRLSEAQLRQFTLALGTTQDENGKKQLPDCIVGEDGLILTPLGRYQIINGLR
SQ  RFEIEYQGDPELQPIRSYEIASLVRTLFRLSSAINHRFAGQMAALCSRDDFLGSFCRYHLTEPGLASRHLLSPVGRRQVA
SQ  GHTRGPRLSLRFLGSYRTLVSLLLAFFVASLFCVGPLPCTLLLTLGYVLYASAMTLLTERGKLHQP
//
ID  Q6ZPR5;
PN  Sphingomyelin phosphodiesterase 4;
GN  Smpd4;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25180167}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NXE4}; Single-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:31142202}. Cell membrane, sarcolemma {ECO:0000269|PubMed:25180167}.
DR  UNIPROT: Q6ZPR5;
DR  UNIPROT: Q3TPE0;
DR  UNIPROT: Q3TPP1;
DR  UNIPROT: Q8CBJ5;
DR  UNIPROT: Q8CD12;
DR  UNIPROT: Q8CD83;
DR  UNIPROT: Q8R0J3;
DR  UNIPROT: Q9CX74;
DR  Pfam: PF14724;
DE  Function: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide (PubMed:25180167). It has a relevant role in the homeostasis of membrane sphingolipids, thereby influencing membrane integrity, and endoplasmic reticulum organization and function. May sensitize cells to DNA damage-induced apoptosis. In skeletal muscle, mediates TNF-stimulated oxidant production (PubMed:25180167). {ECO:0000250|UniProtKB:Q9NXE4, ECO:0000269|PubMed:25180167}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8QZZ8; IntAct: EBI-11569280; Score: 0.35
DE  Interaction: Q9CZE3; IntAct: EBI-11570633; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0042383;
GO  GO:0005802;
GO  GO:0046872;
GO  GO:0004767;
GO  GO:0050290;
GO  GO:0071356;
GO  GO:0046513;
GO  GO:0007029;
GO  GO:0046475;
GO  GO:0001701;
GO  GO:0006685;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAFPHLQQPSFLLASLKADSINKPFAQRCQDLVKVIEDFPAKELHAVFPWLVESIFGSLDGVLVGWNLRCLQGRVNPVEY
SQ  STAMEFLDPSGPMMKLVYKLQAEDYNFDFPVSCLPGPVKASIQENVLPDSPLYHNKVQFPPTGGLGLNLALNPFEYYMFY
SQ  FALSLISQKPMSMTLHVRTSDCAYFTLVDRYLSWFLPTEGSVPPPLCSSPGGSSPSPAPRTPAMPFASYGLHTSLLKRHI
SQ  SHQTSVNADPASHEIWRSETLLQVFVEMWLHHYSLEMYQKMQSPHAKLEVLHYRLTVSSALHSPAQPSLQALHAYQESFT
SQ  PTEEHVLVVRLLLKHLHAFANSLKPDQASPSAHSHATSPLEEFKRAAVPRFVQQKLYVFLQHCFGHWPLDATFRAVLEMW
SQ  LSYLQPWRYAPEKQAQGSDPQPRCVSEKWAPFIQENLLMYTKLFVSFLNRALRTDLVSPKNALMVFRVAKVFAQPNLAEM
SQ  IQKGEQLFLEPELIIPHRQHRLFTVTTSFLSPWPPVVTDASFKVKSHVYSLEGQDCKYTPMFGPEIRTLVLRLAQLITQA
SQ  KQTAKSISDQYVESPTGRSFLSWLTFGLTDTNSCYPANDLDEIGQDSIRKTDEYLEKALEYLRQIFRLSEAQLAQLTLAL
SQ  GSARDENGKQQLPDCIVGEEGLILTPLGRYQIINGLRRFEIEYQGDLELQPIRSYEITSLVRALFRLSSAINRRFAGQMA
SQ  ALCSRNDFLGSFCRYHLTEPALSNRHLLSPVGRRQVTNPARGPRLSLRFLGSYRTLLLLLMAFFVASLFCIGPLSCSLLL
SQ  VLGYVLYAIAMTLLTERGKLHQL
//
ID  Q5XHG1;
PN  Sphingomyelin phosphodiesterase 4;
GN  smpd4;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NXE4}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NXE4}; Single-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NXE4}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q6ZPR5}.
DR  UNIPROT: Q5XHG1;
DR  UNIPROT: Q4V7Y8;
DR  Pfam: PF14724;
DE  Function: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. It has a relevant role in the homeostasis of membrane sphingolipids, thereby influencing membrane integrity, and endoplasmic reticulum organization and function. May sensitize cells to DNA damage-induced apoptosis. {ECO:0000250|UniProtKB:Q9NXE4}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0042383;
GO  GO:0046872;
GO  GO:0004767;
GO  GO:0050290;
GO  GO:0071356;
GO  GO:0046513;
GO  GO:0006685;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLAGGSPQPSFLLGSLKADCVTKPFLQRCQDLVRVIEDFPAKELHAIFPWLIETVFGSLDGSILGWNLRGLHERINPLE
SQ  FHTALEFLDPSGAMMKLVYKLQAEEYKYDFPVSFLPGPVRASIQERVLPECPLYHNKIQFPASGGVSFNLALNSFEYFMF
SQ  HFAFCLLKQRNYPQGLHFSTADSAYYILVDKYLKWFLPVEGNVPPPHSPNTGGTVPSPAPRSPSLSFTSYGSHTSLLKRH
SQ  ISHQHLVNADPAAQEIWRTETLLQVFVEIWLHHYSLEMYQKMQSPNAKLEALHNRLSVSSAPPIYPALPGSLHSYQELFQ
SQ  PTEEHVLVVRLLVKHLHTFSNSIRPEQVSPSTHSHTASPLEELKRVVVPRFIQQKLYIFLQHCFGHWPLDASFRAVLEMW
SQ  LSYVQPWRYVLERSSPVSGEMQNRNVPEKWSTFVQENLLFYTKLFLRFLSRALRTDLVNPKNALMVFRAAKVFSQLNLPE
SQ  MILNGEQLFLKPEHVIPHRQHRLLLTPNLGGSFLSSWQPPITDTSLKVKSHVFSLEGQDCQYMQMFGPEARNLVLRLAQM
SQ  ISQAKQTAKSISNHSPDSSANQSFLSWFGLGSPDFNGSYNGSDLDEAGYDTIRKTDEHLEKALDYFCQIFRLNPTQLGQL
SQ  TANVDSSQDDDGKNKLPDCIQSEDGVVLTSLGRYQIINGLRKFDIEYQGDPELQPIRSYENAMLVRYLYRLSSVINKRFA
SQ  NSMGALCARKDFLGKLCRHHLTSSSRKCKKSPITSVSPSEPAAPHIRLRFLASYRTLAFLFIFYILGSLLSLGPLICTFL
SQ  LLIGCMFYAIVQTLLSEEQKPHNN
//
ID  B8PYG1;
PN  NMDA receptor synaptonuclear signaling and neuronal migration factor;
GN  nsmf;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Nucleus envelope {ECO:0000250}. Nucleus membrane {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Synapse {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Postsynaptic density {ECO:0000250}. Membrane {ECO:0000250}.
DR  UNIPROT: B8PYG1;
DE  Function: Stimulates outgrowth of olfactory axons and migration of hypophysiotropic gonadotropin-releasing hormone 3 (GnRH3) neurons. May couple NMDA-sensitive glutamate receptor signaling to the nucleus and trigger long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. {ECO:0000269|PubMed:19097186}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0030425;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045773;
GO  GO:2001224;
GO  GO:0048168;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGTVVSKKENLRNDAISSVAAKVRAARAFGEYLSHTRPENRNRSDHLLSDTFIGQETDSPDISRLNNNNSLQPYSQHTLI
SQ  VKPSQEELQQGSQSAPLPTSSKRRLSVERSLSSEDQQNQRRTESSVKPARVYTITRERDMLGGQGSEESLELEVLKRTSE
SQ  PSQINPPTGLRGSHHRGSQHRGNNGPTHQHHYGHAPMAQPLQSSGSTHNIRDWGSRRSRSREDCTPDCVACIRPHCQSQR
SQ  SLDLDTSPHGGGKQHKKLERMYSEDRVSSEDREDHTNSWFPKENMFSFQTATTTMQAISNFRKHLRMVGSRRVKAQTFVD
SQ  RKAKSFSRSWSDPTPVKPDSLHDSRDSGDLQASSGNLDEEDCDDVDWEEERELERVACEGDDFIPPKLMLISSKVPKAEY
SQ  VPNIIRRDDPSIIPILYDHEHATFDDILEEIEKKLTAYRKGCKIWNMLIFCQGGPGHLYLLKNKVATFAKVEKEEGMMQF
SQ  WKKLGRFMSLLNPEPNLIHIMGCYVLGNANGEKLFQNLKRLMKPHGIEFKSPLELSAQGKEMIEMYFDFRLYRLWKTRQH
SQ  SKLHDYDDLL
//
ID  Q6X4W1;
PN  NMDA receptor synaptonuclear signaling and neuronal migration factor;
GN  NSMF;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:20025934}. Nucleus envelope {ECO:0000250}. Nucleus membrane {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:20025934}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:20025934}; Peripheral membrane protein {ECO:0000269|PubMed:20025934}. Cell projection, dendrite {ECO:0000250}. Synapse {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Postsynaptic density {ECO:0000250}. Membrane {ECO:0000250}. Note=Found on the outside of the luteinizing-hormone-releasing hormone (LHRH) cell membrane and axons projecting from the olfactory pit and epithelium. Associates with transcriptionally active chromatin regions. Detected at the nuclear membranes of CA1 neurons. Cortical cytoskeleton. Localized in proximal apical dendrites. Colocalizes with CABP1 in dendrites and dendritic spines. Myristoylation is a prerequisite for extranuclear localization. Translocates from dendrites to the nucleus during NMDA receptor-dependent long-term potentiation (LTP) induction of synaptic transmission at Schaffer collateral/CA1 synapses of hippocampal primary neurons and in a importin-dependent manner (By similarity). {ECO:0000250}.
DR  UNIPROT: Q6X4W1;
DR  UNIPROT: Q2TB96;
DR  UNIPROT: Q6X4V7;
DR  UNIPROT: Q6X4V8;
DR  UNIPROT: Q6X4V9;
DR  UNIPROT: Q8N2M2;
DR  UNIPROT: Q96SY1;
DR  UNIPROT: Q9NPM4;
DR  UNIPROT: Q9NPP3;
DR  UNIPROT: Q9NPS3;
DR  OMIM: 608137;
DR  OMIM: 614838;
DR  DisGeNET: 26012;
DE  Function: Couples NMDA-sensitive glutamate receptor signaling to the nucleus and triggers long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. Part of the cAMP response element-binding protein (CREB) shut-off signaling pathway. Stimulates outgrowth of olfactory axons and migration of gonadotropin-releasing hormone (GnRH) and luteinizing-hormone-releasing hormone (LHRH) neuronal cells. {ECO:0000269|PubMed:20025934}.
DE  Disease: Hypogonadotropic hypogonadism 9 with or without anosmia (HH9) [MIM:614838]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic-pituitary axis. In some cases, it is associated with non-reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:15362570, ECO:0000269|PubMed:21700882, ECO:0000269|PubMed:23643382}. Note=The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in NSMF as well as in other HH-associated genes including FGFR1 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-25874947; Score: 0.56
DE  Interaction: P35240; IntAct: EBI-25878370; Score: 0.56
DE  Interaction: Q5VTD9; IntAct: EBI-953002; Score: 0.00
DE  Interaction: Q9UJV3; IntAct: EBI-24321902; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-24262865; Score: 0.56
DE  Interaction: Q8ND90; IntAct: EBI-25254367; Score: 0.56
DE  Interaction: O75031; IntAct: EBI-24504154; Score: 0.56
DE  Interaction: Q12933; IntAct: EBI-22730042; Score: 0.56
DE  Interaction: Q9BPX5; IntAct: EBI-22734617; Score: 0.56
DE  Interaction: P29377; IntAct: EBI-22734564; Score: 0.56
DE  Interaction: Q5W5X9; IntAct: EBI-22757664; Score: 0.56
DE  Interaction: O14950; IntAct: EBI-24722799; Score: 0.56
DE  Interaction: Q16825; IntAct: EBI-24373467; Score: 0.56
DE  Interaction: Q86Z20; IntAct: EBI-24390896; Score: 0.56
DE  Interaction: Q15654; IntAct: EBI-24392928; Score: 0.56
DE  Interaction: Q9BS40; IntAct: EBI-24413700; Score: 0.56
DE  Interaction: O95273; IntAct: EBI-24439262; Score: 0.56
DE  Interaction: Q9UBB9; IntAct: EBI-24441101; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-24443988; Score: 0.56
DE  Interaction: Q9BVG8; IntAct: EBI-24451566; Score: 0.56
DE  Interaction: P57075; IntAct: EBI-24573458; Score: 0.56
DE  Interaction: P25791; IntAct: EBI-24576651; Score: 0.56
DE  Interaction: O14512; IntAct: EBI-24601500; Score: 0.56
DE  Interaction: Q96SI1; IntAct: EBI-21881639; Score: 0.35
DE  Interaction: Q5XPI4; IntAct: EBI-21881639; Score: 0.35
DE  Interaction: Q5TEU4; IntAct: EBI-21881639; Score: 0.35
DE  Interaction: Q06330; IntAct: EBI-21881639; Score: 0.35
DE  Interaction: G5E9A7; IntAct: EBI-25842713; Score: 0.56
DE  Interaction: P14136; IntAct: EBI-25858284; Score: 0.56
DE  Interaction: P19404; IntAct: EBI-25876878; Score: 0.56
DE  Interaction: P07196; IntAct: EBI-25877605; Score: 0.56
DE  Interaction: P29474; IntAct: EBI-25878762; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25898453; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25915530; Score: 0.56
DE  Interaction: Q9Y3C5; IntAct: EBI-25918897; Score: 0.56
DE  Interaction: Q8WXH2; IntAct: EBI-25927865; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25931866; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25954663; Score: 0.56
GO  GO:0070161;
GO  GO:0097440;
GO  GO:0030863;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0000791;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005635;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045202;
GO  GO:0048306;
GO  GO:0071230;
GO  GO:0071257;
GO  GO:0071371;
GO  GO:2001224;
GO  GO:0035307;
GO  GO:0048814;
GO  GO:0043523;
GO  GO:0048168;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGAAASRRRALRSEAMSSVAAKVRAARAFGEYLSQSHPENRNGADHLLADAYSGHDGSPEMQPAPQNKRRLSLVSNGCYE
SQ  GSLSEEPSIRKPAGEGPQPRVYTISGEPALLPSPEAEAIELAVVKGRRQRHPHHHSQPLRASPGGSREDVSRPCQSWAGS
SQ  RQGSKECPGCAQLAPGPTPRAFGLDQPPLPETSGRRKKLERMYSVDRVSDDIPIRTWFPKENLFSFQTATTTMQAISVFR
SQ  GYAERKRRKRENDSASVIQRNFRKHLRMVGSRRVKAQTFAERRERSFSRSWSDPTPMKADTSHDSRDSSDLQSSHCTLDE
SQ  AFEDLDWDTEKGLEAVACDTEGFVPPKVMLISSKVPKAEYIPTIIRRDDPSIIPILYDHEHATFEDILEEIERKLNVYHK
SQ  GAKIWKMLIFCQGGPGHLYLLKNKVATFAKVEKEEDMIHFWKRLSRLMSKVNPEPNVIHIMGCYILGNPNGEKLFQNLRT
SQ  LMTPYRVTFESPLELSAQGKQMIETYFDFRLYRLWKSRQHSKLLDFDDVL
//
ID  Q99NF2;
PN  NMDA receptor synaptonuclear signaling and neuronal migration factor;
GN  Nsmf;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus. Nucleus envelope {ECO:0000250}. Nucleus membrane {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane; Peripheral membrane protein. Cell projection, dendrite {ECO:0000250}. Synapse {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Postsynaptic density {ECO:0000250}. Membrane {ECO:0000250}. Note=Found on the outside of the luteinizing-hormone- releasing hormone (LHRH) cell membrane and axons projecting from the olfactory pit and epithelium. Associates with transcriptionally active chromatin regions. Detected at the nuclear membranes of CA1 neurons. Cortical cytoskeleton. Localized in proximal apical dendrites. Colocalizes with CABP1 in dendrites and dendritic spines. Myristoylation is a prerequisite for extranuclear localization. Translocates from dendrites to the nucleus during NMDA receptor- dependent long-term potentiation (LTP) induction of synaptic transmission at Schaffer collateral/CA1 synapses of hippocampal primary neurons and in an importin-dependent manner (By similarity). {ECO:0000250}.
DR  UNIPROT: Q99NF2;
DR  UNIPROT: A2AJ93;
DR  UNIPROT: A2AJ94;
DR  UNIPROT: Q8BPT0;
DR  UNIPROT: Q8C9R5;
DR  UNIPROT: Q9DBF4;
DR  UNIPROT: Q9ERZ1;
DE  Function: Couples NMDA-sensitive glutamate receptor signaling to the nucleus and triggers long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. Part of the cAMP response element-binding protein (CREB) shut-off signaling pathway. Stimulates outgrowth of olfactory axons and migration of gonadotropin-releasing hormone (GnRH) and luteinizing-hormone-releasing hormone (LHRH) neuronal cells. {ECO:0000269|PubMed:10898796}.
DE  Reference Proteome: Yes;
DE  Interaction: P27361; IntAct: EBI-6899796; Score: 0.44
DE  Interaction: P83953; IntAct: EBI-15688730; Score: 0.44
DE  Interaction: O88751; IntAct: EBI-15688845; Score: 0.54
GO  GO:0070161;
GO  GO:0097440;
GO  GO:0030863;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0000791;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005635;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0045202;
GO  GO:0048306;
GO  GO:0071230;
GO  GO:0071257;
GO  GO:0071371;
GO  GO:2001224;
GO  GO:0035307;
GO  GO:0099527;
GO  GO:0048814;
GO  GO:0043523;
GO  GO:0048168;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGAAASRRRALRSEAMSSVAAKVRAARAFGEYLSQSHPENRNGADHLLADAYSGHDGSPEMQPAPQNKRRLSLVSNGRYE
SQ  GSISDEAVSGKPAIEGPQPHVYTISREPALLPGSEAEAIELAVVKGRRQRERHPHHHSQPLRASPGSSREDISRPCQSWA
SQ  GSRQGSKECPGCAQLVPGPSSRAFGLEQPPLPEAPGRHKKLERMYSVDGVSDDVPIRTWFPKENLFSFQTATTTMQAISV
SQ  FRGYAERKRRKRENDSASVIQRNFRKHLRMVGSRRVKAQTFAERRERSFSRSWSDPTPMKADTSHDSRDSSDLQSSHCTL
SQ  DEACEDLDWDTEKGLEAMACNTEGFLPPKVMLISSKVPKAEYIPTIIRRDDPSIIPILYDHEHATFEDILEEIEKKLNIY
SQ  HKGAKIWKMLIFCQGGPGHLYLLKNKVATFAKVEKEEDMIHFWKRLSRLMSKVNPEPNVIHIMGCYILGNPNGEKLFQNL
SQ  RTLMTPYKVTFESPLELSAQGKQMIETYFDFRLYRLWKSRQHSKLLDFDDVL
//
ID  Q9EPI6;
PN  NMDA receptor synaptonuclear signaling and neuronal migration factor;
GN  Nsmf;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus. Nucleus envelope. Nucleus membrane. Nucleus matrix. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell projection, dendrite. Synapse. Synapse, synaptosome. Postsynaptic density. Membrane. Note=Found on the outside of the luteinizing-hormone-releasing hormone (LHRH) cell membrane and axons projecting from the olfactory pit and epithelium (By similarity). Associates with transcriptionally active chromatin regions. Detected at the nuclear membranes of CA1 neurons. Cortical cytoskeleton. Localized in proximal apical dendrites. Colocalizes with CABP1 in dendrites and dendritic spines. Myristoylation is a prerequisite for extranuclear localization. Translocates from dendrites to the nucleus during NMDA receptor- dependent long-term potentiation (LTP) induction of synaptic transmission at Schaffer collateral/CA1 synapses of hippocampal primary neurons and in an importin-dependent manner. {ECO:0000250}.
DR  UNIPROT: Q9EPI6;
DR  UNIPROT: Q5PPF6;
DR  UNIPROT: Q7TSC6;
DR  UNIPROT: Q7TSC8;
DR  UNIPROT: Q9EPI4;
DR  UNIPROT: Q9EPI5;
DE  Function: Couples NMDA-sensitive glutamate receptor signaling to the nucleus and triggers long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. Part of the cAMP response element-binding protein (CREB) shut-off signaling pathway. Stimulates outgrowth of olfactory axons and migration of gonadotropin-releasing hormone (GnRH) and luteinizing-hormone-releasing hormone (LHRH) neuronal cells. {ECO:0000269|PubMed:18303947}.
DE  Reference Proteome: Yes;
DE  Interaction: P27361; IntAct: EBI-6899704; Score: 0.56
DE  Interaction: P23565; IntAct: EBI-6899892; Score: 0.57
DE  Interaction: P48039; IntAct: EBI-11578061; Score: 0.00
DE  Interaction: P49286; IntAct: EBI-11578707; Score: 0.00
DE  Interaction: O88751; IntAct: EBI-15688794; Score: 0.59
DE  Interaction: P83953; IntAct: EBI-15688896; Score: 0.40
DE  Interaction: Q5XIE8; IntAct: EBI-26439741; Score: 0.35
GO  GO:0070161;
GO  GO:0097440;
GO  GO:0030863;
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0000791;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005635;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0045202;
GO  GO:0048306;
GO  GO:0071230;
GO  GO:0071257;
GO  GO:0071371;
GO  GO:2001224;
GO  GO:0035307;
GO  GO:0099527;
GO  GO:0048814;
GO  GO:0043523;
GO  GO:0048168;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:18303947};
SQ  MGAAASRRRALRSEAMSSVAAKVRAARAFGEYLSQSHPENRNGADHLLADAYSGHEGSPEMQPAPHNKRRLSLVSNGRYE
SQ  GSISDEAVSGKTATEGPQPRVYTISREPALLPGSEAEAIELAVVKGRRQRERHPHHHSQPLRASPGSSREDISRPCQSWA
SQ  GSRQGSKECPGCAKLVPGPSPRAFGLEQPPLPEASGRHKKLERMYSVDGVSDDVPIRTWFPKENPFSFQTATTTMQAISV
SQ  FRGYAERKRRKRENDSASVIQRNFRKHLRMVGSRRVKAQTFAERRERSFSRSWSDPTPMKADTSHDSRDSSDLQSSHCTL
SQ  DEACEDLDWDTEKGLEATACDTEGFLPPKVMLISSKVPKAEYIPTIIRRDDPSIIPILYDHEHATFEDILEEIEKKLNIY
SQ  HKGAKIWKMLIFCQGGPGHLYLLKNKVATFAKVEKEEDMIHFWKRLSRLMSKVNPEPNVIHIMGCYILGNPNGEKLFQNL
SQ  RTLMTPYKVTFESPLELSAQGKQMIETYFDFRLYRLWKSRQHSKLLDFDDVL
//
ID  G0SBQ3;
PN  Nucleoporin NSP1;
GN  NSP1;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P14907}. Nucleus membrane {ECO:0000250|UniProtKB:P14907}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14907}; Cytoplasmic side {ECO:0000250|UniProtKB:P14907}. Nucleus membrane {ECO:0000250|UniProtKB:P14907}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14907}; Nucleoplasmic side {ECO:0000250|UniProtKB:P14907}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P14907}.
DR  UNIPROT: G0SBQ3;
DR  UNIPROT: G0ZGU1;
DR  PDB: 5CWS;
DR  Pfam: PF05064;
DR  Pfam: PF13634;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NSP1 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, pre-ribosome, signal recognition particle (SRP), and protein transport. {ECO:0000250|UniProtKB:P14907}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S024; IntAct: EBI-16176393; Score: 0.61
DE  Interaction: G0S0R2; IntAct: EBI-16176589; Score: 0.58
DE  Interaction: G0S156; IntAct: EBI-16176459; Score: 0.46
DE  Interaction: G0S4F3; IntAct: EBI-16176539; Score: 0.58
DE  Interaction: G0S4X2; IntAct: EBI-16176513; Score: 0.61
DE  Interaction: G0SBS8; IntAct: EBI-16176539; Score: 0.61
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P14907};
SQ  MSFTFGQPSTSGASGQSNTSTAPASGGLFGSTTGSSTPAFSFGNTSGTQSGSLFGGATTGQKTSLFGNTSSTTPAGTPAT
SQ  SLFGQSTSSSSGPSLFGNASKPSGNLFGNTSTSAAGSSTPAGTPSLFGSKTATTSAGASSTTPAATAGSGSLFGSTTATT
SQ  QGSSTPTSTGLFGGSSTASKSLFGSTTTPATGTSGSQTTPAKPLFGSFGSTTPAGAPPTDATKTAGLFGNLSKPATTGTS
SQ  TPTLFGSTSATTQGQSSTPLFGAKPAETSTTTAASGAATPATSAPASTTPTLFGGATLTSSAPAASTSTSTATASTPAAT
SQ  KPLFGATATTSAPGSSTTTATPGLFSTTPATTAAAGSSTATSTLFGTKPATTTAAAASSTPAATSTPSLFGSKPASTTAP
SQ  ASGTPTTTTAPASTSAPATTTAAPTSGASATASTTTAGQDAKTTTAGLGASTVGPQSQLPRLKNKTMDEIITRWATDLAK
SQ  YQKEFKEQAAKVMEWDRLLVENGEKIQKLYTSTYEAERASNEIERQLSNVESQQEELTAWLDRYERELDELYAKQMGSAA
SQ  GEQAAGPDQERERTYKLAEKLTDQLDEMGKDLAKMIKEINDMSNTLSKGSKPDDPLTQIVRVLNGHLAQLQWIDTNAAAL
SQ  QAKVAAAQKAAGSMGANVPGTETDAAESFYRSYRGGLK
//
ID  Q10168;
PN  Nucleoporin nsp1;
GN  nsp1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:15116432}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Cytoplasmic side {ECO:0000250|UniProtKB:P14907}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Nucleoplasmic side {ECO:0000250|UniProtKB:P14907}.
DR  UNIPROT: Q10168;
DR  Pfam: PF05064;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. Appears to have a role in the formation of the septum. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0017056;
GO  GO:0000917;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0000054;
GO  GO:0006405;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16823372};
SQ  MSFNPGNNQNSGFSFGKPAQPNSAAQGAATPAATGLFGNTNNNTSSTAPSGGLFGSNNASNTSAPSTFSFGKAATTGNST
SQ  NASTSSPFSFGSTNTNNTAGAKPLFGGLGSTGSANSTGDKSKNTASSATGAATTNPSGSTFNFGSSNNSFNFGKPASTTN
SQ  TTTPAAASTGSLFGKPAATGTTSNAPPASSTSTTPATGSGGFSFGKPASLGSTNNASTSTTANSGFSFGKPATTSAPGSN
SQ  TTVTPSSSITGTNDSKPAASNTGSAPTTGFSFGKPAGQAASTATDKGTTTTSSAGTGFSFGKPATTEDTNKPTAPNSAFT
SQ  KPATSTGDNKPTFSFGNTSKPTENTSTTATSAPPLSNNTKPAEGANQTSSGFSFGKPATDTTTSTSKTGPLFGNKPADPS
SQ  AKPGATASTTPSEPPPSSIKHKTLQEILNKWSTDLTTQTEVFNKLCDQVSDWDRTLVDNGALISKLYTETVEAEQMSNRI
SQ  DDGLEYVSSSQQELFKLLDSYETQLETFDGRATSALNVERERAFGVADDILSRLDRLGEDLGTVINQMNDFSKPDDSISE
SQ  IVKVLNAQLASLGWVENRIFQMEEKLDTIKKKNSDVLF
//
ID  P14907;
PN  Nucleoporin NSP1;
GN  NSP1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P14907;
DR  UNIPROT: D6VWE3;
DR  PDB: 1O6O;
DR  PDB: 7N85;
DR  PDB: 7N9F;
DR  PDB: 7WOO;
DR  PDB: 7WOT;
DR  Pfam: PF05064;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NSP1 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, pre-ribosome, signal recognition particle (SRP), and protein transport. {ECO:0000269|PubMed:10889207, ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11352936, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:11739405, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:9017593, ECO:0000269|PubMed:9461539, ECO:0000269|PubMed:9774653, ECO:0000269|PubMed:9843582, ECO:0000269|PubMed:9891088}.
DE  Reference Proteome: Yes;
DE  Interaction: P48837; IntAct: EBI-390867; Score: 0.81
DE  Interaction: P02829; IntAct: EBI-763009; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P34077; IntAct: EBI-789044; Score: 0.35
DE  Interaction: P40368; IntAct: EBI-790236; Score: 0.87
DE  Interaction: Q02630; IntAct: EBI-795280; Score: 0.35
DE  Interaction: P40066; IntAct: EBI-797307; Score: 0.44
DE  Interaction: Q02199; IntAct: EBI-801342; Score: 0.68
DE  Interaction: P40477; IntAct: EBI-805203; Score: 0.59
DE  Interaction: P51998; IntAct: EBI-811019; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-811019; Score: 0.53
DE  Interaction: P22353; IntAct: EBI-811019; Score: 0.35
DE  Interaction: Q06678; IntAct: EBI-811019; Score: 0.35
DE  Interaction: P36516; IntAct: EBI-811019; Score: 0.35
DE  Interaction: P36525; IntAct: EBI-811019; Score: 0.35
DE  Interaction: P36523; IntAct: EBI-811019; Score: 0.35
DE  Interaction: Q04599; IntAct: EBI-811019; Score: 0.35
DE  Interaction: P36161; IntAct: EBI-7438937; Score: 0.44
DE  Interaction: P40005; IntAct: EBI-8464369; Score: 0.56
DE  Interaction: P48363; IntAct: EBI-8464653; Score: 0.56
DE  Interaction: Q14974; IntAct: EBI-1034546; Score: 0.62
DE  Interaction: Q04175; IntAct: EBI-1173446; Score: 0.40
DE  Interaction: Q06142; IntAct: EBI-1173482; Score: 0.72
DE  Interaction: P32499; IntAct: EBI-6322490; Score: 0.00
DE  Interaction: P29295; IntAct: EBI-2612057; Score: 0.35
DE  Interaction: P23291; IntAct: EBI-2614250; Score: 0.35
DE  Interaction: P24869; IntAct: EBI-2617071; Score: 0.35
DE  Interaction: P26448; IntAct: EBI-2882390; Score: 0.00
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q02796; IntAct: EBI-2885546; Score: 0.00
DE  Interaction: P39723; IntAct: EBI-2887969; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P48353; IntAct: EBI-3658592; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3673674; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3691838; Score: 0.35
DE  Interaction: P52553; IntAct: EBI-3739443; Score: 0.35
DE  Interaction: P53900; IntAct: EBI-3739619; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3745755; Score: 0.35
DE  Interaction: P15992; IntAct: EBI-3750055; Score: 0.35
DE  Interaction: P38915; IntAct: EBI-4375569; Score: 0.35
DE  Interaction: P50875; IntAct: EBI-4376349; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-4377624; Score: 0.35
DE  Interaction: Q02336; IntAct: EBI-4378994; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-4379349; Score: 0.35
DE  Interaction: P36160; IntAct: EBI-7433031; Score: 0.35
DE  Interaction: Q8IYF3; IntAct: EBI-11523349; Score: 0.56
DE  Interaction: Q05166; IntAct: EBI-11888294; Score: 0.37
DE  Interaction: P61970; IntAct: EBI-15747989; Score: 0.44
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0060090;
GO  GO:0005543;
GO  GO:0017056;
GO  GO:0007049;
GO  GO:0097064;
GO  GO:0006607;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0006405;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MNFNTPQQNKTPFSFGTANNNSNTTNQNSSTGAGAFGTGQSTFGFNNSAPNNTNNANSSITPAFGSNNTGNTAFGNSNPT
SQ  SNVFGSNNSTTNTFGSNSAGTSLFGSSSAQQTKSNGTAGGNTFGSSSLFNNSTNSNTTKPAFGGLNFGGGNNTTPSSTGN
SQ  ANTSNNLFGATANANKPAFSFGATTNDDKKTEPDKPAFSFNSSVGNKTDAQAPTTGFSFGSQLGGNKTVNEAAKPSLSFG
SQ  SGSAGANPAGASQPEPTTNEPAKPALSFGTATSDNKTTNTTPSFSFGAKSDENKAGATSKPAFSFGAKPEEKKDDNSSKP
SQ  AFSFGAKSNEDKQDGTAKPAFSFGAKPAEKNNNETSKPAFSFGAKSDEKKDGDASKPAFSFGAKPDENKASATSKPAFSF
SQ  GAKPEEKKDDNSSKPAFSFGAKSNEDKQDGTAKPAFSFGAKPAEKNNNETSKPAFSFGAKSDEKKDGDASKPAFSFGAKS
SQ  DEKKDSDSSKPAFSFGTKSNEKKDSGSSKPAFSFGAKPDEKKNDEVSKPAFSFGAKANEKKESDESKSAFSFGSKPTGKE
SQ  EGDGAKAAISFGAKPEEQKSSDTSKPAFTFGAQKDNEKKTEESSTGKSTADVKSSDSLKLNSKPVELKPVSLDNKTLDDL
SQ  VTKWTNQLTESASHFEQYTKKINSWDQVLVKGGEQISQLYSDAVMAEHSQNKIDQSLQYIERQQDELENFLDNFETKTEA
SQ  LLSDVVSTSSGAAANNNDQKRQQAYKTAQTLDENLNSLSSNLSSLIVEINNVSNTFNKTTNIDINNEDENIQLIKILNSH
SQ  FDALRSLDDNSTSLEKQINSIKK
//
ID  Q2PEG7;
PN  Protein NODULATION SIGNALING PATHWAY 2;
GN  NSP2;
OS  34305;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:17244637, ECO:0000269|PubMed:24400899, ECO:0000269|PubMed:25560877}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q5NE24}. Note=Mainly localized to the nuclear envelope. Also found in the endoplasmic reticulum. Upon Nod- factor application, the nuclear envelope localization disappears and the protein accumulates in the nucleus. {ECO:0000250|UniProtKB:Q5NE24}.
DR  UNIPROT: Q2PEG7;
DR  UNIPROT: A1DS15;
DR  Pfam: PF03514;
DR  PROSITE: PS50985;
DE  Function: Transcriptional regulator essential for Nod-factor-induced gene expression (Probable) (PubMed:17244637, PubMed:17071642). Acts downstream of calcium spiking and a calcium/calmodulin-dependent protein kinase required for activation of early nodulation gene expression (PubMed:17244637, PubMed:17071642, PubMed:24329948). Transcription factor involved in the induction of NIN and ENOD40 genes, which are required for rhizobial infection and early nodule development (PubMed:17244637). Does not seem to contribute to the early steps of the arbuscular mycorrhizal fungus infection and colonization processes in roots (PubMed:23926062). Transcription factor involved in the positive regulation of the beta-carotene isomerase D27, which participates in a pathway leading to biosynthesis of strigolactones in roots (PubMed:23926062). {ECO:0000269|PubMed:17071642, ECO:0000269|PubMed:17244637, ECO:0000269|PubMed:23926062, ECO:0000269|PubMed:24329948, ECO:0000305|PubMed:20719766, ECO:0000305|PubMed:23335614}.
DE  Reference Proteome: No;
GO  GO:0005783;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0009877;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEMDIDCIHHLDFSGHSTLTNTPSSDNDNYGCSWNHWSPVVNWDAFTGNQDDFHHLIDSMIDDNNTGPAFSDHTASTTSE
SQ  EEEEEEATTTTMTTTTTTTTTTPEAADDDFKGLRLVHLLMAGAEALTGANKNRELARVILVRLKELVSHTDGTNMERLAA
SQ  YFTEALQGLLEGAGGAYNSSSKHHVIGGPHHEPQNDALAAFQLLQDMSPYVKFGHFTANQAIVEAVAHERRVHIVDYDIM
SQ  EGVQWASLMQALASNPNGPHLRITALSRSGVGRRSMATVQETGRRLTAFATSLGQPFSFHHSRLESDETFRPAGLKLVRG
SQ  EALVFNCMLNLPHLTYRSPNSVASFLTAAKALRPRLVTVVEEEVGSALGGFVERFMDSLHHFSAVFDSLEAGFPMQGRAR
SQ  ALVERVFLGPRIVGSLARIYRTGGGGEERGSWREWLRAAGFSGVAVSSANHCQSNLLLGLFNDGYRVEELGSNKLVLHWK
SQ  TRRLLSASLWTCSSESDCA
//
ID  Q5NE24;
PN  Protein NODULATION SIGNALING PATHWAY 2;
GN  NSP2;
OS  3880;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15961668}. Endoplasmic reticulum {ECO:0000269|PubMed:15961668}. Note=Mainly localized to the nuclear envelope. Also found in the endoplasmic reticulum. Upon Nod-factor application, the nuclear envelope localization disappears and the protein accumulates in the nucleus. {ECO:0000269|PubMed:15961668}.
DR  UNIPROT: Q5NE24;
DR  UNIPROT: G7J334;
DR  Pfam: PF03514;
DR  PROSITE: PS50985;
DE  Function: Transcriptional regulator essential for Nod-factor-induced gene expression (PubMed:15961668). Acts downstream of calcium spiking and DMI3, a calcium/calmodulin-dependent protein kinase (CCaMK) (PubMed:15961668). Transcription factor involved in the control of strigolactone biosynthesis in roots through the activation of the beta- carotene isomerase D27, which participates in a pathway leading to biosynthesis of strigolactones (PubMed:22039214, PubMed:26503135). {ECO:0000269|PubMed:15961668, ECO:0000269|PubMed:22039214, ECO:0000269|PubMed:26503135}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0003700;
GO  GO:0043565;
GO  GO:0009877;
GO  GO:0006355;
GO  GO:0009610;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLMDMDAINDLHFSGHSSLTNTPTSDEDYGCTWNHWSPIVNWDTFTGAPDDFHHLMDTIIEDRTTVLEQLSPSITTTTT
SQ  TTTTTDEEEEEMETTTTTTTTAIKTHEVGDDSKGLKLVHLLMAGAEALTGSTKNRDLARVILIRLKELVSQHANGSNMER
SQ  LAAHFTEALHGLLEGAGGAHNNHHHHNNNKHYLTTNGPHDNQNDTLAAFQLLQDMSPYVKFGHFTANQAIIEAVAHERRV
SQ  HVIDYDIMEGVQWASLIQSLASNNNGPHLRITALSRTGTGRRSIATVQETGRRLTSFAASLGQPFSFHHCRLDSDETFRP
SQ  SALKLVRGEALVFNCMLNLPHLSYRAPESVASFLNGAKTLNPKLVTLVEEEVGSVIGGFVERFMDSLHHYSAVFDSLEAG
SQ  FPMQNRARTLVERVFFGPRIAGSLGRIYRTGGEEERRSWGEWLGEVGFRGVPVSFANHCQAKLLLGLFNDGYRVEEVGVG
SQ  SNKLVLDWKSRRLLSASLWTCSSSDSDL
//
ID  Q80DP8;
PN  Non-structural protein NS-S;
GN  N;
OS  1980456;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0DTK1}.
DR  UNIPROT: Q80DP8;
DE  Function: Antagonizes host MAVS-induced type-I IFN signaling pathway. {ECO:0000269|PubMed:32321811}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0039503;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPRRRWRWTRMTLTRAHYKIDGQLCLHWRPNSGNSRDNLQIWWQLKNWLQNQLIQQGLSLMTI
//
ID  P0DJX5;
PN  Non-structural protein NS-S;
GN  N;
OS  1337063;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0DTK1}. Host cytoplasm {ECO:0000250|UniProtKB:I4EPA3}.
DR  UNIPROT: P0DJX5;
DE  Function: Antagonizes host type-I IFN signaling pathway. {ECO:0000250|UniProtKB:I4EPA3}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0039503;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNNLLLPDKNSRMQREQWKWTRMTLTRAHYKQDNKQCQHWRINSQTTREEWQMLCPGRKWILNLLTRLGLNLMIISRRD
SQ  QALDMEMSLM
//
ID  I4EPA3;
PN  Non-structural protein NS-S;
GN  N;
OS  39002;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0DTK1}. Host cytoplasm {ECO:0000269|PubMed:33478127}.
DR  UNIPROT: I4EPA3;
DE  Function: Antagonizes host type-I IFN signaling pathway. {ECO:0000269|PubMed:17705180, ECO:0000269|PubMed:33478127}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0039536;
GO  GO:0039503;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNSNLLLPDKNLRMQREQWKWTQMTLIKTHCKPGNKQCQHWRTNSQTTREGWQMLCPGKKWILNLLTRLGLNLMTTSRRD
SQ  QALGMEMSLM
//
ID  P0DTK1;
PN  Non-structural protein NS-S;
GN  N;
OS  1980494;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:19956987}. Host cytoplasm {ECO:0000269|PubMed:33478127}. Host nucleus {ECO:0000269|PubMed:33478127}.
DR  UNIPROT: P0DTK1;
DE  Function: Antagonizes host type-I IFN signaling pathway. {ECO:0000269|PubMed:17705180, ECO:0000269|PubMed:33478127}.
DE  Reference Proteome: No;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0039503;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNSKLSLPGKNLKMQKRRWKPTRMMLTRAHYRVDGQLCQHWRTNWQTSRGSLQIWCQVKKWVKSLLTRLGLSRMITSRRD
SQ  QAFDMEMSLM
//
ID  Q9JIY8;
PN  N-acetyltransferase family 8 member 3;
GN  Nat8f3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus membrane {ECO:0000305|PubMed:25123547}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:25123547}. Cytoplasm {ECO:0000305|PubMed:25123547}. Note=C-terminally tagged constructs localize to the nuclear membrane and perinuclear region. N-terminally tagged constructs show a punctate cytoplasmic distribution. {ECO:0000269|PubMed:25123547}.
DR  UNIPROT: Q9JIY8;
DR  UNIPROT: Q8BQW2;
DR  UNIPROT: Q91WM7;
DR  Pfam: PF00583;
DR  PROSITE: PS51186;
DE  Function: Has histone acetyltransferase activity in vitro, with specificity for histone H4. {ECO:0000269|PubMed:25123547}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005793;
GO  GO:0033116;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0047198;
GO  GO:0010485;
GO  GO:0004468;
GO  GO:0008080;
GO  GO:0050435;
GO  GO:0003401;
GO  GO:0001702;
GO  GO:0016573;
GO  GO:0043066;
GO  GO:0007162;
GO  GO:0018003;
GO  GO:0010628;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPYHIRKYQDSDHRSVVDLFRRGMEEHIPATFRHMLLLPRTLLLLLGVPLTLFLASGSWLLVLLSILTLFLSLWFLAKY
SQ  TWEKHVMNCLHTDMADITRTYLSSHSSCFWVAESRGQTVGMVAARPVKDPLLQKKQLQLLHLSVSLQHRREGLGKAMVRT
SQ  VLQFAQMQGFSEVVLSTSMLQYAALALYQGMGFQKTGETFYTYLSRLRKSPMINLKYSLTSREGDL
//
ID  Q9QXS4;
PN  N-acetyltransferase family 8 member 3;
GN  Nat8f3;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9JIY8}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9JIY8}. Cytoplasm {ECO:0000250|UniProtKB:Q9JIY8}. Note=C-terminally tagged constructs localize to the nuclear membrane and perinuclear region. N-terminally tagged constructs show a punctate cytoplasmic distribution. {ECO:0000250|UniProtKB:Q9JIY8}.
DR  UNIPROT: Q9QXS4;
DR  Pfam: PF00583;
DR  PROSITE: PS51186;
DE  Function: Has histone acetyltransferase activity in vitro, with specificity for histone H4. {ECO:0000250|UniProtKB:Q9JIY8}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0010485;
GO  GO:0008080;
GO  GO:0001702;
GO  GO:0016573;
GO  GO:0043967;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPYHIRKYQDSDHRSVVNLFCRGTEEHISASFRYMLLLPGTLLILLGVPLTLFLASGSWLLVLLSTLTLLVSLWLLAKY
SQ  PWEKYTAMCLHSDMADIPRTYLSSHYSCFWVAESRGQMVGIIAVLPVKDPLLQRKQLQLRHLSVSLEHRREGIGRAMVRT
SQ  ALQFAEMQGFSEVVLVTSMLQYAALALYQSMGFQKTGEFFYTFVSRLRNSPMICLKYCLTSALNDLKT
//
ID  Q9FZK4;
PN  Nuclear transport factor 2A, N-terminally processed;
GN  NTF2A;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15610358, ECO:0000269|PubMed:16428596}. Nucleus {ECO:0000269|PubMed:15610358, ECO:0000269|PubMed:16428596}. Nucleus envelope {ECO:0000269|PubMed:16428596}. Note=Accumulates at the nuclear rim. Excluded from the nucleolus. {ECO:0000269|PubMed:16428596}.
DR  UNIPROT: Q9FZK4;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DE  Function: Facilitates protein transport into the nucleus. Interacts with various nucleoporins and with Ran-GDP. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import. {ECO:0000269|PubMed:16428596}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0044613;
GO  GO:0005634;
GO  GO:0031267;
GO  GO:0006913;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDPDAVAKAFVEHYYSTFDANRPGLVSLYQEGSMLTFEGQKIQGSQNIVAKLTGLPFQQCKHNITTVDCQPSGPAGGMLV
SQ  FVSGNLQLAGEQHALKFSQMFHLISNQGNYYVFNDIFRLNYA
//
ID  Q9C7F5;
PN  Nuclear transport factor 2B;
GN  NTF2B;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16428596}. Nucleus {ECO:0000269|PubMed:16428596}. Nucleus envelope {ECO:0000269|PubMed:16428596}. Note=Accumulates at the nuclear rim. Excluded from the nucleolus. {ECO:0000269|PubMed:16428596}.
DR  UNIPROT: Q9C7F5;
DR  UNIPROT: Q1H566;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DE  Function: Facilitates protein transport into the nucleus. Interacts with various nucleoporins and with Ran-GDP. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import. {ECO:0000269|PubMed:16428596}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0044613;
GO  GO:0005634;
GO  GO:0006913;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQMDPDAVSKAFVEHYYSTFDTNRVGLAGLYQEASMLTFEGQKIQGVQSIVAKLTSLPFQQCKHHISTVDCQPSGPASG
SQ  MLVFVSGNLQLAGEEHALKFSQMFHLMPTPQGSFYVFNDIFRLNYA
//
ID  Q32KP9;
PN  Nuclear transport factor 2;
GN  NUTF2;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61970}. Nucleus outer membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P61972}. Nucleus inner membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61970}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000250|UniProtKB:P61970}.
DR  UNIPROT: Q32KP9;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DE  Function: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. {ECO:0000250|UniProtKB:P61970}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0042802;
GO  GO:0031267;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0090204;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDKPIWEQIGSSFIQHYYQLFDNDRTQLGAIYIDASCLTWEGQQFQGKAAIVEKLSSLPFQKIQHSITAQDHQPTPDSC
SQ  IISMVVGQLKADEDPIMGFHQMFLLKNINDAWVCTNDMFRLALHNFG
//
ID  Q86HW7;
PN  Nuclear transport factor 2;
GN  nutf2;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61970}. Nucleus outer membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P61972}. Nucleus inner membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61970}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000250|UniProtKB:P61970}.
DR  UNIPROT: Q86HW7;
DR  UNIPROT: Q551K9;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DE  Function: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. {ECO:0000250|UniProtKB:P61970}.
DE  Reference Proteome: Yes;
DE  Interaction: O76329; IntAct: EBI-922911; Score: 0.40
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0031267;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQSVDPQVVGVGKQFVEHYYGIFDSNRAGLTQIYQQQTTLTWEGKFLSGADAIVKHIVELPFQQTNRKINSIDCQQTYQP
SQ  GIMITVTGTLIIDGEAKNQLKFVQVFNLASNNGSFLLINDFFRLVLD
//
ID  P61970;
PN  Nuclear transport factor 2;
GN  NUTF2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:7744965}. Nucleus outer membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P61972}. Nucleus inner membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10679025}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000269|PubMed:10679025}.
DR  UNIPROT: P61970;
DR  UNIPROT: B2R4G7;
DR  UNIPROT: P13662;
DR  UNIPROT: Q6IB67;
DR  PDB: 1GY5;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DR  OMIM: 605813;
DR  DisGeNET: 10204;
DE  Function: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:7744965}.
DE  Reference Proteome: Yes;
DE  Interaction: P0DTD1; IntAct: EBI-25490898; Score: 0.53
DE  Interaction: P14907; IntAct: EBI-15747989; Score: 0.44
DE  Interaction: P37198; IntAct: EBI-10219209; Score: 0.78
DE  Interaction: P46527; IntAct: EBI-591758; Score: 0.40
DE  Interaction: Q9Y383; IntAct: EBI-732692; Score: 0.00
DE  Interaction: Q9UET6; IntAct: EBI-1063453; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1084678; Score: 0.00
DE  Interaction: Q8WUF5; IntAct: EBI-9688209; Score: 0.35
DE  Interaction: Q13625; IntAct: EBI-9688225; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-9688194; Score: 0.81
DE  Interaction: P61970; IntAct: EBI-10484973; Score: 0.67
DE  Interaction: P12004; IntAct: EBI-24293281; Score: 0.56
DE  Interaction: Q13555; IntAct: EBI-25247788; Score: 0.56
DE  Interaction: Q5T751; IntAct: EBI-25264315; Score: 0.56
DE  Interaction: Q01813; IntAct: EBI-24530859; Score: 0.56
DE  Interaction: Q9BYQ0; IntAct: EBI-24621450; Score: 0.56
DE  Interaction: Q3KNR5; IntAct: EBI-24659751; Score: 0.56
DE  Interaction: Q9H0A9; IntAct: EBI-23671523; Score: 0.56
DE  Interaction: Q9UIL8; IntAct: EBI-24664109; Score: 0.56
DE  Interaction: Q9NSI6; IntAct: EBI-23733567; Score: 0.56
DE  Interaction: Q9C004; IntAct: EBI-24714464; Score: 0.56
DE  Interaction: Q9BYU1; IntAct: EBI-24723781; Score: 0.56
DE  Interaction: Q8IY57; IntAct: EBI-23788279; Score: 0.56
DE  Interaction: Q96I34; IntAct: EBI-24737460; Score: 0.56
DE  Interaction: Q8TDC0; IntAct: EBI-24738439; Score: 0.56
DE  Interaction: Q9Y247; IntAct: EBI-24740716; Score: 0.56
DE  Interaction: Q9P0W2; IntAct: EBI-24742792; Score: 0.56
DE  Interaction: Q8NCX0; IntAct: EBI-24748463; Score: 0.56
DE  Interaction: Q9NP66; IntAct: EBI-24750900; Score: 0.56
DE  Interaction: Q8WTV1; IntAct: EBI-23829247; Score: 0.56
DE  Interaction: Q9BWC9; IntAct: EBI-24756668; Score: 0.56
DE  Interaction: Q14847; IntAct: EBI-24784348; Score: 0.56
DE  Interaction: Q16740; IntAct: EBI-24787087; Score: 0.56
DE  Interaction: Q9NQ35; IntAct: EBI-24797969; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-23916904; Score: 0.56
DE  Interaction: P15531; IntAct: EBI-24551845; Score: 0.56
DE  Interaction: P12532; IntAct: EBI-24557865; Score: 0.56
DE  Interaction: Q9NQG5; IntAct: EBI-24562569; Score: 0.56
DE  Interaction: Q8N7W2; IntAct: EBI-24575519; Score: 0.56
DE  Interaction: Q6NTE8; IntAct: EBI-24579511; Score: 0.56
DE  Interaction: Q7Z3B4; IntAct: EBI-24586864; Score: 0.56
DE  Interaction: Q9BY43; IntAct: EBI-24637248; Score: 0.56
DE  Interaction: O43790; IntAct: EBI-24638929; Score: 0.56
DE  Interaction: O00746; IntAct: EBI-24642247; Score: 0.56
DE  Interaction: Q5T6F2; IntAct: EBI-24642429; Score: 0.56
DE  Interaction: Q96BZ8; IntAct: EBI-25150841; Score: 0.56
DE  Interaction: Q9NX63; IntAct: EBI-25158772; Score: 0.56
DE  Interaction: Q7Z7F0; IntAct: EBI-25186711; Score: 0.56
DE  Interaction: Q5T0J7; IntAct: EBI-25195387; Score: 0.56
DE  Interaction: Q96NC0; IntAct: EBI-25201668; Score: 0.56
DE  Interaction: Q5TCM9; IntAct: EBI-25235321; Score: 0.56
DE  Interaction: Q02629; IntAct: EBI-15747947; Score: 0.44
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q8WTR7; IntAct: EBI-22127900; Score: 0.37
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0042802;
GO  GO:0031267;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0090204;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDKPIWEQIGSSFIQHYYQLFDNDRTQLGAIYIDASCLTWEGQQFQGKAAIVEKLSSLPFQKIQHSITAQDHQPTPDSC
SQ  IISMVVGQLKADEDPIMGFHQMFLLKNINDAWVCTNDMFRLALHNFG
//
ID  P61971;
PN  Nuclear transport factor 2;
GN  Nutf2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61970}. Nucleus outer membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P61972}. Nucleus inner membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61970}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000250|UniProtKB:P61970}.
DR  UNIPROT: P61971;
DR  UNIPROT: P13662;
DR  UNIPROT: Q3TI35;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DE  Function: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. {ECO:0000250|UniProtKB:P61970}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0042802;
GO  GO:0061608;
GO  GO:0031267;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:1904046;
GO  GO:0006913;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0090204;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDKPIWEQIGSSFIQHYYQLFDNDRTQLGAIYIDASCLTWEGQQFQGKAAIVEKLSSLPFQKIQHSITAQDHQPTPDSC
SQ  IISMVVGQLKADEDPIMGFHQMFLLKNINDAWVCTNDMFRLALHNFG
//
ID  Q5R8G4;
PN  Nuclear transport factor 2;
GN  NUTF2;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61970}. Nucleus outer membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P61972}. Nucleus inner membrane {ECO:0000250|UniProtKB:P61972}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61970}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000250|UniProtKB:P61970}.
DR  UNIPROT: Q5R8G4;
DR  UNIPROT: H2NR93;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DE  Function: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. {ECO:0000250|UniProtKB:P61970}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0042802;
GO  GO:0031267;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0090204;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDKPIWEQIGSSFIQHYYQLFDNDRTQLGAIYIDASCLTWEGQQFQGKAAIVEKLSSLPFQKIQHSITAQDHQPTPDSC
SQ  IISMVVGQLKADEDPIMGFHQMFLLKNINDAWVCTNDMFRLALHNFG
//
ID  P61972;
PN  Nuclear transport factor 2;
GN  Nutf2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:9822603}. Nucleus outer membrane {ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:11846560, ECO:0000269|PubMed:15522285, ECO:0000269|PubMed:9822603}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:11846560, ECO:0000269|PubMed:15522285}. Nucleus inner membrane {ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:11846560}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61970}. Note=At steady state it is essentially nucleoplasmic, enriched in nucleoplasmic foci. {ECO:0000250|UniProtKB:P61970}.
DR  UNIPROT: P61972;
DR  UNIPROT: P13662;
DR  PDB: 1A2K;
DR  PDB: 1AR0;
DR  PDB: 1ASK;
DR  PDB: 1GY6;
DR  PDB: 1JB2;
DR  PDB: 1JB4;
DR  PDB: 1JB5;
DR  PDB: 1OUN;
DR  PDB: 1QMA;
DR  PDB: 1U5O;
DR  PDB: 5BXQ;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DE  Function: Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. {ECO:0000269|PubMed:10543952, ECO:0000269|PubMed:9822603}.
DE  Reference Proteome: Yes;
DE  Interaction: P62825; IntAct: EBI-1026859; Score: 0.44
GO  GO:0005829;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0042802;
GO  GO:0061608;
GO  GO:0031267;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:1904046;
GO  GO:0006913;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0090204;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDKPIWEQIGSSFIQHYYQLFDNDRTQLGAIYIDASCLTWEGQQFQGKAAIVEKLSSLPFQKIQHSITAQDHQPTPDSC
SQ  IISMVVGQLKADEDPIMGFHQMFLLKNINDAWVCTNDMFRLALHNFG
//
ID  Q91987;
PN  BDNF/NT-3 growth factors receptor;
GN  NTRK2;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:8287802, ECO:0000269|PubMed:8670834}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250|UniProtKB:Q63604}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63604}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63604}. Postsynaptic density {ECO:0000250|UniProtKB:P15209}. Note=Internalized to endosomes upon ligand-binding. {ECO:0000250|UniProtKB:P15209}.
DR  UNIPROT: Q91987;
DR  UNIPROT: Q91010;
DR  Pfam: PF07679;
DR  Pfam: PF13855;
DR  Pfam: PF16920;
DR  Pfam: PF07714;
DR  PROSITE: PS50835;
DR  PROSITE: PS51450;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS00239;
DE  Function: Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4 (PubMed:8287802, PubMed:8670834). Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation (PubMed:8670834). Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia (By similarity). {ECO:0000250|UniProtKB:P15209, ECO:0000269|PubMed:8287802, ECO:0000269|PubMed:8670834}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0010008;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0043235;
GO  GO:0005524;
GO  GO:0048403;
GO  GO:0060175;
GO  GO:0005004;
GO  GO:0043121;
GO  GO:0005030;
GO  GO:0042803;
GO  GO:0004714;
GO  GO:0005244;
GO  GO:0031547;
GO  GO:1990416;
GO  GO:1990090;
GO  GO:0021954;
GO  GO:0021987;
GO  GO:0048668;
GO  GO:0007612;
GO  GO:0043524;
GO  GO:0030182;
GO  GO:0001764;
GO  GO:0050772;
GO  GO:0008284;
GO  GO:0048672;
GO  GO:0010628;
GO  GO:0033674;
GO  GO:0043410;
GO  GO:0010976;
GO  GO:0014068;
GO  GO:0046777;
GO  GO:1903859;
GO  GO:0043087;
GO  GO:0051896;
GO  GO:0099551;
GO  GO:0007169;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVSWRRRPGPGLARLWGLCCLVLGCWRGALGCPASCRCSSWRIWCSEPVPGITSFPVPQRSTEDDNVTEIYIANQRKLES
SQ  INDNEVGFYVGLKNLTVVDSGLRFVSRQAFVKNINLQYINLSRNKLSSLSKKPFRHLGLSDLILVDNPFKCSCEIMWIKK
SQ  FQETKFYTEAQDIYCVDDNNKRIALMDMKVPNCDLPSANLSNYNITVVEGKSITLYCDTTGGPPPNVSWVLTNLVSNHES
SQ  DTSKNPASLTIKNVSSMDSGLWISCVAENIVGEVQTSAELTVFFAPNITFIESPTPDHHWCIPFTVKGNPKPTLQWFYEG
SQ  AILNESEYICTKIHVINQSEYHGCLQLDNPTHLNNGAYTLLAKNEYGEDEKRVDAHFMSVPGDGSGPIVDPDVYEYETTP
SQ  NDLGDTTNNSNQITSPDVSNKENEDSITVYVVVGIAALVCTGLVIMLIILKFGRHSKFGMKGPSSVISNDDDSASPLHHI
SQ  SNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQ
SQ  DKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNR
SQ  PAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPES
SQ  IMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIH
SQ  SLLQNLAKASPVYLDILG
//
ID  Q16620;
PN  BDNF/NT-3 growth factors receptor;
GN  NTRK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:15494731}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:P15209}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P15209}. Early endosome membrane {ECO:0000250|UniProtKB:P15209}. Cell projection, axon {ECO:0000250|UniProtKB:Q63604}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63604}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63604}. Postsynaptic density {ECO:0000250|UniProtKB:P15209}. Note=Internalized to endosomes upon ligand-binding. {ECO:0000250|UniProtKB:P15209}.
DR  UNIPROT: Q16620;
DR  UNIPROT: B1ANZ4;
DR  UNIPROT: B4DFV9;
DR  UNIPROT: Q16675;
DR  UNIPROT: Q59GJ1;
DR  UNIPROT: Q8WXJ5;
DR  UNIPROT: Q8WXJ6;
DR  UNIPROT: Q8WXJ7;
DR  PDB: 1HCF;
DR  PDB: 1WWB;
DR  PDB: 2MFQ;
DR  PDB: 4ASZ;
DR  PDB: 4AT3;
DR  PDB: 4AT4;
DR  PDB: 4AT5;
DR  PDB: 5MO9;
DR  Pfam: PF07679;
DR  Pfam: PF13855;
DR  Pfam: PF16920;
DR  Pfam: PF01462;
DR  Pfam: PF07714;
DR  PROSITE: PS50835;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS00239;
DR  OMIM: 600456;
DR  OMIM: 613886;
DR  OMIM: 617830;
DR  DisGeNET: 4915;
DE  Function: Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity (By similarity). Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2 (PubMed:7574684, PubMed:15494731). Upon ligand- binding, undergoes homodimerization, autophosphorylation and activation (PubMed:15494731). Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia. {ECO:0000250|UniProtKB:P15209, ECO:0000269|PubMed:15494731, ECO:0000269|PubMed:7574684}.
DE  Disease: Developmental and epileptic encephalopathy 58 (DEE58) [MIM:617830]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE58 is an autosomal dominant condition characterized by onset of refractory seizures in the first days or months of life. {ECO:0000269|PubMed:29100083}. Note=The disease may be caused by variants affecting the gene represented in this entry. Obesity, hyperphagia, and developmental delay (OBHD) [MIM:613886]: A disorder characterized by early-onset obesity, hyperphagia, and severe developmental delay in motor function, speech, and language. {ECO:0000269|PubMed:15494731, ECO:0000269|PubMed:27884935, ECO:0000269|PubMed:29100083}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-9689644; Score: 0.55
DE  Interaction: Q03001; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q10567; IntAct: EBI-3904879; Score: 0.37
DE  Interaction: P62487; IntAct: EBI-3911957; Score: 0.37
DE  Interaction: Q9HAN9; IntAct: EBI-3919655; Score: 0.37
DE  Interaction: Q16620; IntAct: EBI-5650732; Score: 0.49
DE  Interaction: P08238; IntAct: EBI-6424683; Score: 0.40
DE  Interaction: P34130; IntAct: EBI-6590946; Score: 0.41
DE  Interaction: P14618; IntAct: EBI-9354703; Score: 0.44
DE  Interaction: Q99523; IntAct: EBI-9828457; Score: 0.44
DE  Interaction: Q03114; IntAct: EBI-15624658; Score: 0.56
DE  Interaction: P04150; IntAct: EBI-15750128; Score: 0.40
DE  Interaction: P78352; IntAct: EBI-16037188; Score: 0.40
DE  Interaction: Q96QK1; IntAct: EBI-27081124; Score: 0.35
DE  Interaction: P19174; IntAct: EBI-32719199; Score: 0.42
DE  Interaction: Q16543; IntAct: EBI-32719199; Score: 0.42
DE  Interaction: P08754; IntAct: EBI-32719199; Score: 0.35
DE  Interaction: Q8WU20; IntAct: EBI-32719199; Score: 0.42
DE  Interaction: P62158; IntAct: EBI-32719199; Score: 0.35
DE  Interaction: Q16288; IntAct: EBI-32719212; Score: 0.54
DE  Interaction: Q3V6T2; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9UPS8; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9H3R5; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q86YF9; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q92738; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q8IYB1; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q16625; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P50851; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q12923; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q96RT1; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9H3P7; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q5VUB5; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q6WCQ1; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q15334; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q8TEW0; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: A8MVW0; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P27448; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9NNW5; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O00459; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O95487; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9ULH0; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q13480; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9Y6M7; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9H792; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9H2D6; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q99618; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P29317; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q86X29; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P20020; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: A7KAX9; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9Y2I1; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q15643; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q04721; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O14964; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q86W92; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P16333; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q8TDM6; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q15437; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9UM54; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q8TAA9; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9HCM4; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P27986; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9C0B5; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9HD26; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q6ZVF9; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9H2J7; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q02487; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q14254; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P62993; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O95490; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P41743; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q658P3; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O75052; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9HDC5; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9P2D6; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9UKG1; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q6P995; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9UBH6; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q13136; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9BXF6; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9UET6; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9UNF0; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O75886; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9Y5Z9; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q6NSJ2; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O95292; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O15013; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q92569; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9Y4J8; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q99959; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9H8Y8; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P42338; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O14639; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q8N4C8; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q8N350; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q4KWH8; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9C004; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9H0W5; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q9H939; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q8NE01; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q08357; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: P62873; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q6P996; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O95405; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: O00170; IntAct: EBI-32724423; Score: 0.27
DE  Interaction: Q06124; IntAct: EBI-32724423; Score: 0.27
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005769;
GO  GO:0031901;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0043235;
GO  GO:0043195;
GO  GO:0005524;
GO  GO:0048403;
GO  GO:0060175;
GO  GO:0043121;
GO  GO:0005030;
GO  GO:0002020;
GO  GO:0042803;
GO  GO:0004714;
GO  GO:0031547;
GO  GO:0071230;
GO  GO:1990416;
GO  GO:1990090;
GO  GO:0021954;
GO  GO:0021987;
GO  GO:0007623;
GO  GO:0007631;
GO  GO:0014047;
GO  GO:0007612;
GO  GO:0060291;
GO  GO:0042490;
GO  GO:0022011;
GO  GO:1902430;
GO  GO:2000811;
GO  GO:0043524;
GO  GO:0030182;
GO  GO:0001764;
GO  GO:0019227;
GO  GO:0048709;
GO  GO:0018105;
GO  GO:0048935;
GO  GO:0050772;
GO  GO:0008284;
GO  GO:0010628;
GO  GO:0033674;
GO  GO:0043410;
GO  GO:0010976;
GO  GO:0033138;
GO  GO:0014068;
GO  GO:0001934;
GO  GO:0051965;
GO  GO:0046777;
GO  GO:0043087;
GO  GO:0051896;
GO  GO:0046548;
GO  GO:0099183;
GO  GO:0099551;
GO  GO:0007169;
GO  GO:0001570;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSWIRWHGPAMARLWGFCWLVVGFWRAAFACPTSCKCSASRIWCSDPSPGIVAFPRLEPNSVDPENITEIFIANQKRLE
SQ  IINEDDVEAYVGLRNLTIVDSGLKFVAHKAFLKNSNLQHINFTRNKLTSLSRKHFRHLDLSELILVGNPFTCSCDIMWIK
SQ  TLQEAKSSPDTQDLYCLNESSKNIPLANLQIPNCGLPSANLAAPNLTVEEGKSITLSCSVAGDPVPNMYWDVGNLVSKHM
SQ  NETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVKGNPKPALQWFYN
SQ  GAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEKQISAHFMGWPGIDDGANPNYPDVIYEDY
SQ  GTAANDIGDTTNRSNEIPSTDVTDKTGREHLSVYAVVVIASVVGFCLLVMLFLLKLARHSKFGMKGPASVISNDDDSASP
SQ  LHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNL
SQ  CPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMA
SQ  EGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWM
SQ  PPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNI
SQ  KGIHTLLQNLAKASPVYLDILG
//
ID  P15209;
PN  BDNF/NT-3 growth factors receptor;
GN  Ntrk2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:14581459}; Single-pass type I membrane protein {ECO:0000269|PubMed:14581459}. Endosome membrane {ECO:0000269|PubMed:14581459}; Single-pass type I membrane protein {ECO:0000269|PubMed:14581459}. Early endosome membrane {ECO:0000269|PubMed:21849472}. Cell projection, axon {ECO:0000250|UniProtKB:Q63604}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63604}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63604}. Postsynaptic density {ECO:0000269|PubMed:27457814}. Note=Internalized to endosomes upon ligand-binding. {ECO:0000269|PubMed:21849472}.
DR  UNIPROT: P15209;
DR  UNIPROT: Q3TUF9;
DR  UNIPROT: Q80WU0;
DR  UNIPROT: Q91XJ9;
DR  Pfam: PF07679;
DR  Pfam: PF13855;
DR  Pfam: PF16920;
DR  Pfam: PF07714;
DR  PROSITE: PS50835;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS00239;
DE  Function: Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. Isoform GP95-TRKB may also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia. {ECO:0000269|PubMed:10571233, ECO:0000269|PubMed:12367511, ECO:0000269|PubMed:15329723, ECO:0000269|PubMed:15372074, ECO:0000269|PubMed:1645620, ECO:0000269|PubMed:16801538, ECO:0000269|PubMed:21414899, ECO:0000269|PubMed:27457814, ECO:0000269|PubMed:8402890, ECO:0000269|PubMed:9728914}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3UA06; IntAct: EBI-310345; Score: 0.37
DE  Interaction: P35235; IntAct: EBI-8602584; Score: 0.50
DE  Interaction: Q8K4V6; IntAct: EBI-8602608; Score: 0.50
DE  Interaction: P04629; IntAct: EBI-8602726; Score: 0.35
DE  Interaction: Q6PHU5; IntAct: EBI-9663469; Score: 0.64
DE  Interaction: Q61768; IntAct: EBI-9663474; Score: 0.35
DE  Interaction: Q60610; IntAct: EBI-15589790; Score: 0.40
DE  Interaction: P49615; IntAct: EBI-15624677; Score: 0.35
DE  Interaction: P61809; IntAct: EBI-15624695; Score: 0.35
DE  Interaction: Q99LI8; IntAct: EBI-15885565; Score: 0.50
DE  Interaction: Q62108; IntAct: EBI-16037153; Score: 0.50
DE  Interaction: Q9QYY0; IntAct: EBI-16037170; Score: 0.35
DE  Interaction: Q62077; IntAct: EBI-16037170; Score: 0.35
DE  Interaction: Q7TMB8; IntAct: EBI-16727444; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005769;
GO  GO:0031901;
GO  GO:0005768;
GO  GO:0060076;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0005887;
GO  GO:0043025;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0048786;
GO  GO:0043235;
GO  GO:0005791;
GO  GO:0043195;
GO  GO:0005524;
GO  GO:0048403;
GO  GO:0060175;
GO  GO:0043121;
GO  GO:0005030;
GO  GO:0002020;
GO  GO:0042803;
GO  GO:0030971;
GO  GO:0004714;
GO  GO:0031547;
GO  GO:0035584;
GO  GO:0071230;
GO  GO:1990416;
GO  GO:1990090;
GO  GO:0021954;
GO  GO:0021987;
GO  GO:0007623;
GO  GO:0007631;
GO  GO:0014047;
GO  GO:0007612;
GO  GO:0007616;
GO  GO:0060291;
GO  GO:0042490;
GO  GO:0022011;
GO  GO:1902430;
GO  GO:2000811;
GO  GO:0043524;
GO  GO:0030182;
GO  GO:0001764;
GO  GO:0019227;
GO  GO:0048709;
GO  GO:0018105;
GO  GO:0048935;
GO  GO:0050772;
GO  GO:0008284;
GO  GO:0010628;
GO  GO:2000324;
GO  GO:0033674;
GO  GO:0043410;
GO  GO:0010976;
GO  GO:0033138;
GO  GO:0014068;
GO  GO:0051965;
GO  GO:0051968;
GO  GO:0046777;
GO  GO:0050773;
GO  GO:0043087;
GO  GO:0043408;
GO  GO:0019222;
GO  GO:0046928;
GO  GO:0051896;
GO  GO:0060041;
GO  GO:0046548;
GO  GO:0099183;
GO  GO:0099551;
GO  GO:0007169;
GO  GO:0001570;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSPWLKWHGPAMARLWGLCLLVLGFWRASLACPTSCKCSSARIWCTEPSPGIVAFPRLEPNSVDPENITEILIANQKRLE
SQ  IINEDDVEAYVGLRNLTIVDSGLKFVAYKAFLKNSNLRHINFTRNKLTSLSRRHFRHLDLSDLILTGNPFTCSCDIMWLK
SQ  TLQETKSSPDTQDLYCLNESSKNMPLANLQIPNCGLPSARLAAPNLTVEEGKSVTLSCSVGGDPLPTLYWDVGNLVSKHM
SQ  NETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVRGNPKPALQWFYN
SQ  GAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLMAKNEYGKDERQISAHFMGRPGVDYETNPNYPEVLYEDW
SQ  TTPTDIGDTTNKSNEIPSTDVADQSNREHLSVYAVVVIASVVGFCLLVMLLLLKLARHSKFGMKGPASVISNDDDSASPL
SQ  HHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLC
SQ  PEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAE
SQ  GNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMP
SQ  PESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHTRKNIK
SQ  SIHTLLQNLAKASPVYLDILG
//
ID  Q63604;
PN  BDNF/NT-3 growth factors receptor;
GN  Ntrk2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:1645620}; Single-pass type I membrane protein {ECO:0000269|PubMed:1645620}. Endosome membrane {ECO:0000250|UniProtKB:P15209}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P15209}. Early endosome membrane {ECO:0000250|UniProtKB:P15209}. Cell projection, axon {ECO:0000269|PubMed:21775604}. Cell projection, dendrite {ECO:0000269|PubMed:21775604}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21775604}. Postsynaptic density {ECO:0000250|UniProtKB:P15209}. Note=Internalized to endosomes upon ligand-binding. {ECO:0000250|UniProtKB:P15209}.
DR  UNIPROT: Q63604;
DR  UNIPROT: Q63605;
DR  UNIPROT: Q63606;
DR  Pfam: PF07679;
DR  Pfam: PF13855;
DR  Pfam: PF16920;
DR  Pfam: PF07714;
DR  PROSITE: PS50835;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS00239;
DE  Function: Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin-dependent calcium signaling in glial cells. {ECO:0000269|PubMed:10196222, ECO:0000269|PubMed:10985347, ECO:0000269|PubMed:1645620, ECO:0000269|PubMed:9582017}.
DE  Reference Proteome: Yes;
DE  Interaction: P61810; IntAct: EBI-15624622; Score: 0.35
DE  Interaction: Q9Z254; IntAct: EBI-7287661; Score: 0.57
DE  Interaction: P27671; IntAct: EBI-7365310; Score: 0.52
DE  Interaction: Q8K4V6; IntAct: EBI-8602529; Score: 0.52
DE  Interaction: P41499; IntAct: EBI-7443286; Score: 0.40
DE  Interaction: Q99523; IntAct: EBI-9663445; Score: 0.43
DE  Interaction: P54256; IntAct: EBI-9663546; Score: 0.27
DE  Interaction: D3ZWV8; IntAct: EBI-15589773; Score: 0.40
DE  Interaction: Q03114; IntAct: EBI-15624566; Score: 0.52
DE  Interaction: Q04631; IntAct: EBI-15737743; Score: 0.59
DE  Interaction: P53610; IntAct: EBI-15737826; Score: 0.40
DE  Interaction: P06536; IntAct: EBI-15750099; Score: 0.40
DE  Interaction: P10686; IntAct: EBI-15750164; Score: 0.40
DE  Interaction: Q63604; IntAct: EBI-15833544; Score: 0.40
DE  Interaction: P08592; IntAct: EBI-21182891; Score: 0.27
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043197;
GO  GO:0005769;
GO  GO:0031901;
GO  GO:0005768;
GO  GO:0060076;
GO  GO:0098978;
GO  GO:0000139;
GO  GO:0030426;
GO  GO:0005887;
GO  GO:0043025;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0014069;
GO  GO:0045211;
GO  GO:0048786;
GO  GO:0043235;
GO  GO:0005791;
GO  GO:0043195;
GO  GO:0005524;
GO  GO:0048403;
GO  GO:0060175;
GO  GO:0043121;
GO  GO:0005030;
GO  GO:0002020;
GO  GO:0042803;
GO  GO:0004713;
GO  GO:0030971;
GO  GO:0004675;
GO  GO:0004714;
GO  GO:0007568;
GO  GO:0031547;
GO  GO:0035584;
GO  GO:0071230;
GO  GO:1990416;
GO  GO:1990090;
GO  GO:0071356;
GO  GO:0021954;
GO  GO:0021987;
GO  GO:0007623;
GO  GO:0007631;
GO  GO:0014047;
GO  GO:0006954;
GO  GO:0007612;
GO  GO:0007616;
GO  GO:0060291;
GO  GO:0042490;
GO  GO:0022011;
GO  GO:1902430;
GO  GO:2000811;
GO  GO:0043524;
GO  GO:0030182;
GO  GO:0001764;
GO  GO:0019227;
GO  GO:0048709;
GO  GO:0018105;
GO  GO:0048935;
GO  GO:0050772;
GO  GO:0008284;
GO  GO:0010628;
GO  GO:2000324;
GO  GO:0033674;
GO  GO:0043410;
GO  GO:0010976;
GO  GO:0033138;
GO  GO:0014068;
GO  GO:0051965;
GO  GO:0051968;
GO  GO:0046777;
GO  GO:0050773;
GO  GO:0043087;
GO  GO:0043408;
GO  GO:0019222;
GO  GO:0046928;
GO  GO:0051896;
GO  GO:0010996;
GO  GO:0009416;
GO  GO:0060041;
GO  GO:0046548;
GO  GO:0099183;
GO  GO:0099551;
GO  GO:0007169;
GO  GO:0001570;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSPWPRWHGPAMARLWGLCLLVLGFWRASLACPMSCKCSTTRIWCTEPSPGIVAFPRLEPNSIDPENITEILIANQKRLE
SQ  IINEDDVEAYVGLKNLTIVDSGLKFVAYKAFLKNGNLRHINFTRNKLTSLSRRHFRHLDLSDLILTGNPFTCSCDIMWLK
SQ  TLQETKSSPDTQDLYCLNESSKNTPLANLQIPNCGLPSARLAAPNLTVEEGKSVTISCSVGGDPLPTLYWDVGNLVSKHM
SQ  NETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVRGNPKPALQWFYN
SQ  GAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLMAKNEYGKDERQISAHFMGRPGVDYETNPNYPEVLYEDW
SQ  TTPTDIGDTTNKSNEIPSTDVADQTNREHLSVYAVVVIASVVGFCLLVMLLLLKLARHSKFGMKGPASVISNDDDSASPL
SQ  HHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLC
SQ  PEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAE
SQ  GNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMP
SQ  PESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHTRKNIK
SQ  NIHTLLQNLAKASPVYLDILG
//
ID  Q02629;
PN  Nucleoporin NUP100/NSP100;
GN  NUP100;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
DR  UNIPROT: Q02629;
DR  UNIPROT: D6VXL9;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  PROSITE: PS51434;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP100 plays an important role in several nuclear export and import pathways including poly(A)+ RNA and protein transport. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11104765, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:8044840, ECO:0000269|PubMed:8557738}.
DE  Reference Proteome: Yes;
DE  Interaction: P34077; IntAct: EBI-1269879; Score: 0.00
DE  Interaction: P35729; IntAct: EBI-1269846; Score: 0.00
DE  Interaction: P38181; IntAct: EBI-1269835; Score: 0.00
DE  Interaction: P40064; IntAct: EBI-6340320; Score: 0.00
DE  Interaction: P40368; IntAct: EBI-11889216; Score: 0.55
DE  Interaction: P46673; IntAct: EBI-11889530; Score: 0.59
DE  Interaction: P48837; IntAct: EBI-1266728; Score: 0.53
DE  Interaction: P49686; IntAct: EBI-1269516; Score: 0.00
DE  Interaction: P49687; IntAct: EBI-1269780; Score: 0.00
DE  Interaction: P52593; IntAct: EBI-11888868; Score: 0.37
DE  Interaction: P52891; IntAct: EBI-11889422; Score: 0.59
DE  Interaction: P61970; IntAct: EBI-15747947; Score: 0.44
DE  Interaction: Q02199; IntAct: EBI-1269802; Score: 0.00
DE  Interaction: P48562; IntAct: EBI-393057; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.53
DE  Interaction: P53035; IntAct: EBI-854602; Score: 0.00
DE  Interaction: Q02159; IntAct: EBI-859483; Score: 0.00
DE  Interaction: Q02630; IntAct: EBI-1266671; Score: 0.65
DE  Interaction: Q06142; IntAct: EBI-1566666; Score: 0.82
DE  Interaction: Q02629; IntAct: EBI-1269769; Score: 0.00
DE  Interaction: Q05166; IntAct: EBI-1269813; Score: 0.00
DE  Interaction: Q99257; IntAct: EBI-1566656; Score: 0.44
DE  Interaction: P43603; IntAct: EBI-2344068; Score: 0.37
DE  Interaction: P40482; IntAct: EBI-2344542; Score: 0.37
DE  Interaction: P53038; IntAct: EBI-2345945; Score: 0.37
DE  Interaction: P24870; IntAct: EBI-2611503; Score: 0.35
DE  Interaction: P24869; IntAct: EBI-2617071; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: P11484; IntAct: EBI-3781717; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3799829; Score: 0.35
DE  Interaction: P38315; IntAct: EBI-16251716; Score: 0.00
DE  Interaction: P40971; IntAct: EBI-16294029; Score: 0.00
DE  Interaction: P52918; IntAct: EBI-16297131; Score: 0.00
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044614;
GO  GO:0060090;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0006913;
GO  GO:0045893;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006405;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFGNNRPMFGGSNLSFGSNTSSFGGQQSQQPNSLFGNSNNNNNSTSNNAQSGFGGFTSAAGSNSNSLFGNNNTQNNGAFG
SQ  QSMGATQNSPFGSLNSSNASNGNTFGGSSSMGSFGGNTNNAFNNNSNSTNSPFGFNKPNTGGTLFGSQNNNSAGTSSLFG
SQ  GQSTSTTGTFGNTGSSFGTGLNGNGSNIFGAGNNSQSNTTGSLFGNQQSSAFGTNNQQGSLFGQQSQNTNNAFGNQNQLG
SQ  GSSFGSKPVGSGSLFGQSNNTLGNTTNNRNGLFGQMNSSNQGSSNSGLFGQNSMNSSTQGVFGQNNNQMQINGNNNNSLF
SQ  GKANTFSNSASGGLFGQNNQQQGSGLFGQNSQTSGSSGLFGQNNQKQPNTFTQSNTGIGLFGQNNNQQQQSTGLFGAKPA
SQ  GTTGSLFGGNSSTQPNSLFGTTNVPTSNTQSQQGNSLFGATKLTNMPFGGNPTANQSGSGNSLFGTKPASTTGSLFGNNT
SQ  ASTTVPSTNGLFGNNANNSTSTTNTGLFGAKPDSQSKPALGGGLFGNSNSNSSTIGQNKPVFGGTTQNTGLFGATGTNSS
SQ  AVGSTGKLFGQNNNTLNVGTQNVPPVNNTTQNALLGTTAVPSLQQAPVTNEQLFSKISIPNSITNPVKATTSKVNADMKR
SQ  NSSLTSAYRLAPKPLFAPSSNGDAKFQKWGKTLERSDRGSSTSNSITDPESSYLNSNDLLFDPDRRYLKHLVIKNNKNLN
SQ  VINHNDDEASKVKLVTFTTESASKDDQASSSIAASKLTEKAHSPQTDLKDDHDESTPDPQSKSPNGSTSIPMIENEKISS
SQ  KVPGLLSNDVTFFKNNYYISPSIETLGNKSLIELRKINNLVIGHRNYGKVEFLEPVDLLNTPLDTLCGDLVTFGPKSCSI
SQ  YENCSIKPEKGEGINVRCRVTLYSCFPIDKETRKPIKNITHPLLKRSIAKLKENPVYKFESYDPVTGTYSYTIDHPVLT
//
ID  Q8L748;
PN  Nuclear pore complex protein NUP107;
GN  NUP107;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8L748;
DR  UNIPROT: F4JFR3;
DR  UNIPROT: F4JFR5;
DR  UNIPROT: Q84ME0;
DR  UNIPROT: Q9LJH6;
DR  Pfam: PF04121;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P10797; IntAct: EBI-4486896; Score: 0.37
GO  GO:0005635;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDMDMDTSPSYFDPEALSVRDQFRRYRKRHSTSPHEEMLSSNVSENRLLYDGHNIHSPTNTALLLENIKEEVDNFHTDHY
SQ  EGTPTNPISASRRESVGILNDDDEALFRRVESQSLKACKIENDELAESGDTTFALFASLFDSALQGLMSIPNLMLRLEES
SQ  CRNVSQSIRYGSDIRHRAVEDKLMRQKAQLLLGEAASWSLLWNLYGKGTDEVPENLILIPSTSHLEACQFVLNDHTAQLC
SQ  LRIVMWLEELASKSLDLERKVQGSHVGTYLPNAGVWHHTQRYLKKNGSNADTLHHLDFDAPTREHARLLPDDYKQDESVL
SQ  EDVWTLIRAGRIEEACDLCRSAGQSWRAATLCPFSGMDMFPSIEALVKNGENRTLQAIEQESGFGNQLRLWKWASYCASE
SQ  KIAEQDGGKHEVAVFATQCSNLNRMLPICTDWESACWAMAKSWLDVQVDLELAQSKPGLTERFKSCIDESPEATQNGCQA
SQ  SFGPEDWPLHVLNQQPRDLPALLQKLHSGEMVHEAVVRGCKEQHRQIQMNLMLGDISHLLDIIWSWIAPLEDDQSNFRPH
SQ  GDPHMIKFGAHMVLVLRLLFTDEINDSFKEKLNNVGDLILHMYAMFLFSKQHEELVGIYASQLARHRCIELFVHMMELRM
SQ  HSSVHVKYKIFLSAMEYLSFSPVDDLHGNFEEIVDRVLSRSREIKLAKYDPSIDVAEQHRQQSLQKAIAIQWLCFTPPST
SQ  IKDVKDVTSKLLLRSLMHSNILFREFALIAMWRVPATPVGAHTLLSYLAEPLKQLSENPDTLEDYVSENLQEFQDWNEYY
SQ  SCDAKYRNWLKFQLENAEVTELSEEENQKAVVAAKETLDSSLSLLLRQDNPWMTFLEDHVFESEEYLFLELHATAMLCLP
SQ  SGECLRPDATVCAALMSALYSSVSEEVVLDRQLMVNVSISSRDSYCIEVVLRCLAIKGDGLGPHNANDGGILSAVAAAGF
SQ  KGSDIYGTYFSFTYDLPPFSIEIWGCELTRFQAGVTMDISRLDAWYSSKEGSLETPATYIVRGLCRRCCLPELVLRSMQV
SQ  SVSLMESGNPPEDHDELIELVASDETGFLSLFSRQQLQEFMLFEREYRMSQLELQEELSSP
//
ID  Q9V466;
PN  Nuclear pore complex protein Nup107;
GN  Nup107;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:26502056, ECO:0000269|PubMed:31784359}. Nucleus envelope {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:27402967}. Nucleus membrane {ECO:0000269|PubMed:26485283}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18562695}. Chromosome {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:31784359}. Nucleus matrix {ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:31784359}. Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure (By similarity). During syncytial embryo and larval neuroblast mitosis localizes to the nuclear envelope in interphase, accumulates in the nucleus in prometaphase, localizes to the spindle envelope in metaphase and then to condensing chromatin in telophase (PubMed:18562695). In spermatocytes, detected in the nuclear matrix by the nuclear envelope in metaphase I, and in the spindle envelope in premeiotic nuclei and during anaphase I (PubMed:27402967). Colocalizes with type-B lamin Lam throughout meiosis I (PubMed:27402967). Unlike in mammals, does not localize to kinetochore (PubMed:18562695, PubMed:27402967). Can localize to the nuclear lumen proximal to the inner nuclear membrane (PubMed:31784359). {ECO:0000250|UniProtKB:P57740, ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:31784359}.
DR  UNIPROT: Q9V466;
DR  Pfam: PF04121;
DE  Function: Plays a role in nuclear pore complex (NPC) assembly and maintenance (PubMed:20547758). Required for nuclear import of Mad (PubMed:20547758). Mediates the association between the nuclear pore complex and a subset of active chromatin regions adjacent to lamin- associated domains (PubMed:31784359). Plays a role in double strand break repair by relocalizing the heterochromatic double strain breaks (DSBs) to the nuclear periphery as part of the homologous recombination (HR) repair process (PubMed:26502056). Regulates cytokinesis during spermatocyte meiosis by maintaining type-B lamin Lam localization to the spindle envelope (PubMed:27402967). Regulates female gonad development and oogenesis (PubMed:26485283). {ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:26485283, ECO:0000269|PubMed:26502056, ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:31784359}.
DE  Reference Proteome: Yes;
DE  Interaction: P18459; IntAct: EBI-198339; Score: 0.00
DE  Interaction: Q24568; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VWG6; IntAct: EBI-235243; Score: 0.00
DE  Interaction: O44424; IntAct: EBI-239128; Score: 0.00
DE  Interaction: Q95TK5; IntAct: EBI-246466; Score: 0.00
DE  Interaction: P02844; IntAct: EBI-260156; Score: 0.00
DE  Interaction: Q9W2N5; IntAct: EBI-267738; Score: 0.00
DE  Interaction: Q9W4M8; IntAct: EBI-26767641; Score: 0.49
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005819;
GO  GO:0003682;
GO  GO:0017056;
GO  GO:0000724;
GO  GO:0030703;
GO  GO:0008585;
GO  GO:0007112;
GO  GO:0007110;
GO  GO:0006406;
GO  GO:1900182;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0046822;
GO  GO:0048137;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADSPFPRSSRSGLLRTTLNSSMPPQNLSHSLLILEKSNAEQNELSLMEDTGDDLDRGKSRMDVLFPQFFDVLQAQGNGQ
SQ  EAFEVIQSLTQVCRGVVEQLELEIDHGMGGEQGARQRESMLTWLRQEINTWRLLHALFYDRILLQTDRQADDEMQDGPTL
SQ  GGSEKEVIQQLYALNATLREYQLVVDWLEACYDRGEQQNPLHAHDRMMAWENTLFQLENLQGAAFGKGHKIVTRLDPDAP
SQ  VREKRPLHALDEEDNLRLSRAIFELIRAGRVDDGLKLCKHFGQTWRAAILEGWRLHEDPNFEQNVSVLHEKLPIEGNPRR
SQ  DIWKRCAWMLADSKNYDEYSRATAGVFSGHLGSLKTLLHSNWHDLLWAHLKVQIDIRVESEIRGCCLKNYQPMPDDYWNG
SQ  RMTMEQIFEELNVAKDASVRDFAQSQLGIIQRHLILDTCGELIQHMVRWVEKDTSQQSPHQLRFMAHIVLFLRQIGRVEQ
SQ  ERQAEKIVAAYVEALIARGEPQLIAYYTASLSNPLQVQLYSRFLEQVEQKRPRELAVDAALQAGLDVEQITRVTVQNIRL
SQ  AHQPLGEFGEPQSGEISAIDQRKISALEWLIHLPEQRGELLWQANAMIRTYLASSKVECMRQTFRMVPADIVQQLVSLYG
SQ  SVDNIPPREECCLKEYLCYKAYLSGVDSFVEWNRLQQNRPKKPQTSHAASSQDNFTERMASERKEQAHRSEVVRWEHKVK
SQ  EQAKQTIELLYNVLMFPDKGWLVDPFIAKLPENAVQLSWDHRLLQMEKLRSICIPEIALFLNEVMFKSGDFAGCVRLADE
SQ  ISSENRQLYKVYTKHKLAELLAKIADASLELLNSKLDPWGYPITT
//
ID  P57740;
PN  Nuclear pore complex protein Nup107;
GN  NUP107;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:26411495}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:26411495}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11564755}. Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure (PubMed:11564755). During mitosis, localizes to the kinetochores (PubMed:11564755). Dissociates from the dissasembled NPC structure late during prophase of mitosis (PubMed:11564755). {ECO:0000269|PubMed:11564755}.
DR  UNIPROT: P57740;
DR  UNIPROT: B4DZ67;
DR  UNIPROT: Q6PJE1;
DR  PDB: 3CQC;
DR  PDB: 3CQG;
DR  PDB: 3I4R;
DR  PDB: 5A9Q;
DR  PDB: 7PEQ;
DR  Pfam: PF04121;
DR  OMIM: 607617;
DR  OMIM: 616730;
DR  OMIM: 618078;
DR  OMIM: 618348;
DR  DisGeNET: 57122;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:12552102, PubMed:15229283, PubMed:30179222). Required for the assembly of peripheral proteins into the NPC (PubMed:15229283, PubMed:12552102). May anchor NUP62 to the NPC (PubMed:15229283). Involved in nephrogenesis (PubMed:30179222). {ECO:0000269|PubMed:12552102, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:30179222}.
DE  Disease: Nephrotic syndrome 11 (NPHS11) [MIM:616730]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. NPHS11 is an autosomal recessive, steroid-resistant and progressive form with onset in the first decade of life. {ECO:0000269|PubMed:26411495, ECO:0000269|PubMed:30179222}. Note=The disease is caused by variants affecting the gene represented in this entry. Ovarian dysgenesis 6 (ODG6) [MIM:618078]: A form of ovarian dysgenesis, a disorder characterized by lack of spontaneous pubertal development, primary amenorrhea, uterine hypoplasia, and hypergonadotropic hypogonadism as a result of streak gonads. ODG6 is an autosomal recessive condition. {ECO:0000269|PubMed:26485283}. Note=The disease may be caused by variants affecting the gene represented in this entry. Galloway-Mowat syndrome 7 (GAMOS7) [MIM:618348]: A form of Galloway-Mowat syndrome, a severe renal-neurological disease characterized by early-onset nephrotic syndrome associated with microcephaly, central nervous system abnormalities, developmental delays, and a propensity for seizures. Brain anomalies include gyration defects ranging from lissencephaly to pachygyria and polymicrogyria, and cerebellar hypoplasia. Most patients show facial dysmorphism characterized by a small, narrow forehead, large/floppy ears, deep-set eyes, hypertelorism and micrognathia. Additional variable features are visual impairment and arachnodactyly. Most patients die in early childhood. GAMOS7 inheritance is autosomal recessive. {ECO:0000269|PubMed:28117080, ECO:0000269|PubMed:28280135, ECO:0000269|PubMed:30179222}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: A8CG34; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: O15504; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P04406; IntAct: EBI-20910640; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P12270; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P35658; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P46060; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P49454; IntAct: EBI-7329356; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-295747; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-11160436; Score: 0.53
DE  Interaction: Q8WUM0; IntAct: EBI-295708; Score: 0.90
DE  Interaction: Q12769; IntAct: EBI-295747; Score: 0.53
DE  Interaction: Q8BH74; IntAct: EBI-2563157; Score: 0.40
DE  Interaction: Q6PFD9; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: Q9BW27; IntAct: EBI-9032422; Score: 0.56
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.53
DE  Interaction: P55318; IntAct: EBI-11317309; Score: 0.35
DE  Interaction: Q6ZQN5; IntAct: EBI-11318220; Score: 0.35
DE  Interaction: Q01167; IntAct: EBI-11318541; Score: 0.35
DE  Interaction: Q9BZS1; IntAct: EBI-11319193; Score: 0.35
DE  Interaction: Q9C009; IntAct: EBI-11319301; Score: 0.35
DE  Interaction: Q9ULZ3; IntAct: EBI-10687267; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-11133657; Score: 0.35
DE  Interaction: Q96PC2; IntAct: EBI-11138004; Score: 0.35
DE  Interaction: P18754; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: O14715; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: O95373; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: O75083; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q8TEM1; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q9UKX7; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P63165; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P53396; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q14571; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: E9PF10; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q6NUQ4; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P61619; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q8NFH4; IntAct: EBI-11160436; Score: 0.53
DE  Interaction: Q5SRE5; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P78406; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q5JRG1; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q96SK2; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q9NXE4; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q9UKK6; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q6P087; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q53GS7; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q9HC62; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-11160436; Score: 0.64
DE  Interaction: Q9BTX1; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q7Z3B4; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: P04049; IntAct: EBI-11904756; Score: 0.00
DE  Interaction: P03431; IntAct: EBI-12579142; Score: 0.35
DE  Interaction: P0C0U1; IntAct: EBI-12579831; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581451; Score: 0.35
DE  Interaction: C5E519; IntAct: EBI-12583021; Score: 0.35
DE  Interaction: C5E526; IntAct: EBI-12584472; Score: 0.35
DE  Interaction: C5E527; IntAct: EBI-12585653; Score: 0.35
DE  Interaction: Q20MH8; IntAct: EBI-12586007; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12588729; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12587743; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-21512742; Score: 0.35
DE  Interaction: Q8N7X8; IntAct: EBI-21585341; Score: 0.35
DE  Interaction: Q8NBZ7; IntAct: EBI-21638319; Score: 0.35
DE  Interaction: Q9UBP0; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: P15311; IntAct: EBI-16791848; Score: 0.27
DE  Interaction: O14880; IntAct: EBI-16796348; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q13627; IntAct: EBI-26367331; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q9UII6; IntAct: EBI-27115954; Score: 0.27
DE  Interaction: P10071; IntAct: EBI-29000530; Score: 0.35
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0008585;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDRSGFGEISSPVIREAEVTRTARKQSAQKRVLLQASQDENFGNTTPRNQVIPRTPSSFRQPFTPTSRSLLRQPDISCIL
SQ  GTGGKSPRLTQSSGFFGNLSMVTNLDDSNWAAAFSSQRSGLFTNTEPHSITEDVTISAVMLREDDPGEAASMSMFSDFLQ
SQ  SFLKHSSSTVFDLVEEYENICGSQVNILSKIVSRATPGLQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSALEEESVF
SQ  AVTAVNASEKTVVEALFQRDSLVRQSQLVVDWLESIAKDEIGEFSDNIEFYAKSVYWENTLHTLKQRQLTSYVGSVRPLV
SQ  TELDPDAPIRQKMPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLYHDPNVNGGTELEPVEG
SQ  NPYRRIWKISCWRMAEDELFNRYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIQTSVATLDETEELPR
SQ  EYLGANWTLEKVFEELQATDKKRVLEENQEHYHIVQKFLILGDIDGLMDEFSKWLSKSRNNLPGHLLRFMTHLILFFRTL
SQ  GLQTKEEVSIEVLKTYIQLLIREKHTNLIAFYTCHLPQDLAVAQYALFLESVTEFEQRHHCLELAKEADLDVATITKTVV
SQ  ENIRKKDNGEFSHHDLAPALDTGTTEEDRLKIDVIDWLVFDPAQRAEALKQGNAIMRKFLASKKHEAAKEVFVKIPQDSI
SQ  AEIYNQCEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNEWFKHMNSVPQKPALIPQPTFTEKVAHEHKEKKYEMDFG
SQ  IWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAKEDHERTHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLADM
SQ  VSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQL
//
ID  Q8BH74;
PN  Nuclear pore complex protein Nup107;
GN  Nup107;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P57740}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P57740}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P57740}. Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure. During mitosis, localizes to the kinetochores. Dissociates from the dissasembled NPC structure late during prophase of mitosis. {ECO:0000250|UniProtKB:P57740}.
DR  UNIPROT: Q8BH74;
DR  UNIPROT: Q99KH5;
DR  Pfam: PF04121;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. Involved in nephrogenesis. {ECO:0000250|UniProtKB:P57740}.
DE  Reference Proteome: Yes;
DE  Interaction: A8CG34; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: O14524; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: O15504; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: P35658; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: P46060; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: P55735; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: P57740; IntAct: EBI-2563157; Score: 0.40
DE  Interaction: P62826; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: P63165; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: P78406; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q12769; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q14974; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q53GS7; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q7Z3B4; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q08380; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q9BW27; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q96EE3; IntAct: EBI-2563157; Score: 0.40
DE  Interaction: Q8NFH4; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q8NFH3; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: P18754; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9P0U3; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q86Y46; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9Y679; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q5JRG1; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9NXE4; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: B4E3T4; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: E9PF10; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q99666; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q14160; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9UKX7; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: O00505; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q6NUQ4; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q96SK2; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: O14715; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: P61956; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8TEM1; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9HC62; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9BTX1; IntAct: EBI-10997196; Score: 0.35
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0008585;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDRSGFGGMSSPVIRDAEVTRTARKHSAHKRVLIQANQEDNFGTATPRSQIIPRTPSSFRQPFVTPSSRSLLRHPDISYI
SQ  LGTEGRSPRHTQSSGYLGNLSMVTNLDDSNWAAAFSSQRLGLYTNTEHHSMTEDVNLSTVMLREDDPGEAASMSMFSDFL
SQ  HSFLKHSSTTVFDLVEEYENICGSQVNILSKIVSRATPGLQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSSLEEENM
SQ  FAIAGINASEKMVVETLFQRDSLVRQSQLVVDWLESIAKDEIGEFSDNIEFYAKSVYWENTLHSLKQRQLLSHMGSTRPL
SQ  VTELDPDAPIRQKLPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLYHDPNVNGGTELEPVE
SQ  GNPYRRIWKISCWRMAEDELFNKYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIRTSVMTQDDSEELP
SQ  REYMEANWTLEKVFEELQATDKKRVLEENQEHYHIVQKFLILGDVDGLMDEFSKWLSKSGSSLPGHLLRFMTHLILFLRT
SQ  LGLQTKEEVSIEVLKTYIQLLISEKHTSLIAFYTCHLPQDLAVAQYALFLEGVTEFEQRHQCLELAKEADLDVATITKTV
SQ  VENICKKDNGEFSHHDLAPSLDTGTTEEDRLKIDVIDWLVFDPAQRAEALRQGNAIMRKFLALKKHEAAKEVFVKIPQDS
SQ  IAEIYNQWEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNEWFKHMNSAPQKPTLLSQATFTEKVAYEHREKKYEMDH
SQ  NIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAEDDPERTHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLAD
SQ  MVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQS
//
ID  P52590;
PN  Nuclear pore complex protein Nup107;
GN  Nup107;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P57740}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P57740}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P57740}. Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure. During mitosis, localizes to the kinetochores. Dissociates from the dissasembled NPC structure late during prophase of mitosis. {ECO:0000250|UniProtKB:P57740}.
DR  UNIPROT: P52590;
DR  Pfam: PF04121;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. Involved in nephrogenesis. {ECO:0000250|UniProtKB:P57740}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0008585;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0051292;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDRSGFGGMSSPVIRDPEVTRTARKHSAHKRVLIQANQDENFGTTTPRSQIIPRTPSSFRQPFTPPSRSLLRHPDISYIF
SQ  GTEGRSPRHIQSSGYLGNLSMVTNLDDSNWAAAFSSQRLGFYTNTEHHSMTEDINLSTVMLREDDPGEAASMSMFSDFLQ
SQ  SFLKHSSTTVFDLVEEYENICASQVNILSKIVSRATRWDWQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSSLEEENM
SQ  FAIAGINASEKTVVEALFQRDSLVRQSQLVVDWLESIAKDEIGDFSDNIEFYAKSVYWENTLHSLKQRQLLSYIGSTRPL
SQ  VTELDPDAPIRQKMPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLHHDPNVNGGTELEPVE
SQ  GNPYRRIWKISCWRMAEDELFNKYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIRTSVMTLDETEELP
SQ  REYMEANWTLEKVFEELQATDKKRVLEENQEHYHVVQKFLILGDIDGLMDEFSKWLSKSRSSLPGHLLRFMTHLILFFRT
SQ  LGLQTKEEVSIEVLKTYIQLLINEKHTNLIAFYTCHLPQDLAVAQYALFLEGVTECEQRHQCLELAKEADLDVATITKTV
SQ  VENIRKKDNGEFSHHDLAPSLDTATTEEDRLKIDVIDWLVFDPAQRAEALRQGNAIMRKFLALKKHEAAKEVFVKIPQDS
SQ  IAEIYNQWEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNERFKHMNSAPQKPTLLSQATFTEKVAHEHKEKKYEMDH
SQ  NIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAEEDPERAHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLAD
SQ  MVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQS
//
ID  Q10331;
PN  Nucleoporin nup107;
GN  nup107;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:15226438}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11309419, ECO:0000269|PubMed:15226438}.
DR  UNIPROT: Q10331;
DR  UNIPROT: O94351;
DR  Pfam: PF04121;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. {ECO:0000269|PubMed:12618370}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9P797; IntAct: EBI-295778; Score: 0.57
DE  Interaction: Q9UTH0; IntAct: EBI-295786; Score: 0.57
GO  GO:0005829;
GO  GO:0140599;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0006407;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MACCCYSTILTHTRLDFKTMHQNALNNATLNVLGHKKNGSSSIQELIEMDEEEAEMNQNVVCIGPNETAVSVELGDEYEK
SQ  FNIITSLKKDNLFSKDGLLYAYYELCQEKFEKCLKEDDEEWIELWDLESRTWDLIQRLYSFRLSEQQGHIQSHAFSSRAV
SQ  LEEEYYSQNPEAFENNIVFNWARDNSSDPPSIEIRGNRWFYTREDIKMKNRGGSRFSSNISGTIVSNLDPDADIRDDKRL
SQ  DERDDNFERQFFHTAFCLFRSGSFEELLELCRRTGNHWRSASLQGILEYRDNLIDDVLQSETSGNKRKELLRRSCLALTK
SQ  NKRIDSYERALYGALCGDLNSVLDVCTTWEDAMWAYYNSMTQYNLDVYLSSKAPQTETQLPPVDSGLGLTPELIFNSLSN
SQ  SSIASIQEEASHPLIKLQTHIICNKISEILSSAHIQLEAIRTGNAPESGDLVTPPLLRILTHIILFLKISGLAVDEYTSD
SQ  SIIQAYIELLASAKKVNLVPLYIQYLSNQVQYEAYSRFLILVDEESARSEQLQLAKKYSLDINHAALLAVEYVYDEVVSV
SQ  SPEEVHTVYLKSIEEPVEPSYKKLICTLEWLLITSQTDELLRFANLVYRFFLSIGELNSAYDLYTHIPSDALNTLSSSDG
SQ  EPENDSKFRDAYELMNYRALCRALKFYQEWEELSKQEVFEDSAVTKASTSYKVWKKKLNFASRKCVKSFTDLLQANWLHP
SQ  STLELKPDDDPLLYKTLMTIRNLYVPELILGLHNVYFSLEDYDSCFALANEVASEDLKLYHCLIKSGRLVEYVSYLGKAG
SQ  ECSLSTPNGLFSL
//
ID  Q02630;
PN  Nucleoporin NUP116/NSP116;
GN  NUP116;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10891509}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
DR  UNIPROT: Q02630;
DR  UNIPROT: D6VZM2;
DR  PDB: 1O6P;
DR  PDB: 2AIV;
DR  PDB: 3PBP;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  PROSITE: PS51434;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). Plays an important role in several nuclear export and import pathways including poly(A)+ RNA, tRNA, pre-ribosome, and protein transport. By binding ATPase AFG2, promotes AFG2-mediated release of shuttling protein RLP24 from pre-60S ribosomal particles (PubMed:23185031). {ECO:0000269|PubMed:10801828, ECO:0000269|PubMed:10891509, ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11104765, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:23185031, ECO:0000269|PubMed:8044840, ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9463388, ECO:0000269|PubMed:9891088}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-795280; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-2346716; Score: 0.37
DE  Interaction: P34077; IntAct: EBI-1269736; Score: 0.00
DE  Interaction: P35729; IntAct: EBI-1269703; Score: 0.00
DE  Interaction: P38181; IntAct: EBI-1269692; Score: 0.00
DE  Interaction: P40066; IntAct: EBI-795280; Score: 0.61
DE  Interaction: P40368; IntAct: EBI-795280; Score: 0.67
DE  Interaction: P40477; IntAct: EBI-6332418; Score: 0.00
DE  Interaction: P46673; IntAct: EBI-11889546; Score: 0.59
DE  Interaction: P47054; IntAct: EBI-11888348; Score: 0.59
DE  Interaction: P48837; IntAct: EBI-1266691; Score: 0.53
DE  Interaction: P49686; IntAct: EBI-1269505; Score: 0.00
DE  Interaction: P49687; IntAct: EBI-1269637; Score: 0.00
DE  Interaction: P52593; IntAct: EBI-11888884; Score: 0.37
DE  Interaction: P52891; IntAct: EBI-1269725; Score: 0.00
DE  Interaction: P53011; IntAct: EBI-1269890; Score: 0.00
DE  Interaction: Q02199; IntAct: EBI-1269659; Score: 0.00
DE  Interaction: Q02629; IntAct: EBI-1266671; Score: 0.65
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P32589; IntAct: EBI-795280; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-795280; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-795280; Score: 0.35
DE  Interaction: Q12453; IntAct: EBI-7200360; Score: 0.57
DE  Interaction: Q02630; IntAct: EBI-1266651; Score: 0.53
DE  Interaction: Q06142; IntAct: EBI-1566676; Score: 0.67
DE  Interaction: Q05166; IntAct: EBI-1269670; Score: 0.00
DE  Interaction: Q99257; IntAct: EBI-1566634; Score: 0.77
DE  Interaction: P34232; IntAct: EBI-7700798; Score: 0.56
DE  Interaction: Q04934; IntAct: EBI-2345223; Score: 0.37
DE  Interaction: P53038; IntAct: EBI-2345244; Score: 0.37
DE  Interaction: P40054; IntAct: EBI-2345904; Score: 0.37
DE  Interaction: P45819; IntAct: EBI-2346444; Score: 0.37
DE  Interaction: P24870; IntAct: EBI-2611503; Score: 0.35
DE  Interaction: P24869; IntAct: EBI-2617071; Score: 0.35
DE  Interaction: P39723; IntAct: EBI-2887969; Score: 0.00
DE  Interaction: P35177; IntAct: EBI-4384219; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-4385804; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-4388449; Score: 0.35
DE  Interaction: Q01560; IntAct: EBI-7082807; Score: 0.44
DE  Interaction: Q12443; IntAct: EBI-16713770; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044614;
GO  GO:0051117;
GO  GO:0042802;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0006405;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFGVSRGAFPSATTQPFGSTGSTFGGQQQQQQPVANTSAFGLSQQTNTTQAPAFGNFGNQTSNSPFGMSGSTTANGTPFG
SQ  QSQLTNNNASGSIFGGMGNNTALSAGSASVVPNSTAGTSIKPFTTFEEKDPTTGVINVFQSITCMPEYRNFSFEELRFQD
SQ  YQAGRKFGTSQNGTGTTFNNPQGTTNTGFGIMGNNNSTTSATTGGLFGQKPATGMFGTGTGSGGGFGSGATNSTGLFGSS
SQ  TNLSGNSAFGANKPATSGGLFGNTTNNPTNGTNNTGLFGQQNSNTNGGLFGQQQNSFGANNVSNGGAFGQVNRGAFPQQQ
SQ  TQQGSGGIFGQSNANANGGAFGQQQGTGALFGAKPASGGLFGQSAGSKAFGMNTNPTGTTGGLFGQTNQQQSGGGLFGQQ
SQ  QNSNAGGLFGQNNQSQNQSGLFGQQNSSNAFGQPQQQGGLFGSKPAGGLFGQQQGASTFASGNAQNNSIFGQNNQQQQST
SQ  GGLFGQQNNQSQSQPGGLFGQTNQNNNQPFGQNGLQQPQQNNSLFGAKPTGFGNTSLFSNSTTNQSNGISGNNLQQQSGG
SQ  LFQNKQQPASGGLFGSKPSNTVGGGLFGNNQVANQNNPASTSGGLFGSKPATGSLFGGTNSTAPNASSGGIFGSNNASNT
SQ  AATTNSTGLFGNKPVGAGASTSAGGLFGNNNNSSLNNSNGSTGLFGSNNTSQSTNAGGLFQNNTSTNTSGGGLFSQPSQS
SQ  MAQSQNALQQQQQQQRLQIQNNNPYGTNELFSKATVTNTVSYPIQPSATKIKADERKKASLTNAYKMIPKTLFTAKLKTN
SQ  NSVMDKAQIKVDPKLSISIDKKNNQIAISNQQEENLDESILKASELLFNPDKRSFKNLINNRKMLIASEEKNNGSQNNDM
SQ  NFKSKSEEQETILGKPKMDEKETANGGERMVLSSKNDGEDSATKHHSRNMDEENKENVADLQKQEYSEDDKKAVFADVAE
SQ  KDASFINENYYISPSLDTLSSYSLLQLRKVPHLVVGHKSYGKIEFLEPVDLAGIPLTSLGGVIITFEPKTCIIYANLPNR
SQ  PKRGEGINVRARITCFNCYPVDKSTRKPIKDPNHQLVKRHIERLKKNPNSKFESYDADSGTYVFIVNHAAEQT
//
ID  G0S0E7;
PN  Nucleoporin NUP120;
GN  NUP120;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P35729}. Nucleus membrane {ECO:0000250|UniProtKB:P35729}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35729}; Cytoplasmic side {ECO:0000250|UniProtKB:P35729}. Nucleus membrane {ECO:0000250|UniProtKB:P35729}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35729}; Nucleoplasmic side {ECO:0000250|UniProtKB:P35729}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P35729}.
DR  UNIPROT: G0S0E7;
DR  PROSITE: PS00678;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP120 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000250|UniProtKB:P35729}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S9A7; IntAct: EBI-16069336; Score: 0.49
DE  Interaction: G0SAK3; IntAct: EBI-16069336; Score: 0.63
DE  Interaction: G0SER9; IntAct: EBI-16069336; Score: 0.49
DE  Interaction: G0SDQ4; IntAct: EBI-16069336; Score: 0.62
DE  Interaction: G0S2G1; IntAct: EBI-16069427; Score: 0.62
DE  Interaction: G0S2X1; IntAct: EBI-16069404; Score: 0.66
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0043170;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35729};
SQ  MAFDNFEILYKETRLNLEPASPSSVVQLRVAPTNAYGRSSLSSSSSSRPASATADDEKGYRTKNLATASSIYYRKHHSSP
SQ  RGFLWRVLDNNTVLSIRVADVCRQEKVADAPLILNLRFASPLRPACVGFADHEDHDALFVYAIDQSNQLWSIILRPDHFR
SQ  KRSATEGGLGDASRVYSPPGFGFKHPHRLAVVSPDQLIVTMHDGGILKFDRNKNHESHGSPWRESIYNVAGWGQSLRGLV
SQ  PFQRNPTVRYEKINMELTAAASTAVTTMGHAETAFLFTICLDHRMRVWDVRTGQILYTGDILNNTKRDPQEVGKWTVDPS
SQ  QNNLIRILDNGRGQCLVVTYSPVGAGEFKFWKVKANDQGSIHVTDCFPDARLMSPNPTSLDVWTLADFAIAQQPDGPELW
SQ  ALWKNNTSYRVNRLQIIPRNATAPFADGWKAVCVESPGPTPRASGSWNPTDSTEKWLDLIFSPGRFSKSTLETALAMYEK
SQ  GLGTYKETVSRSGKGIAESICSVIGSTTTLDRSSQGGADYDQFRNTSETQWMRFWRLLLELDKQRGEALSLVFDQYDGMV
SQ  WVTCADLLAAVRQCSDLERLYHNLQSPEKKNEDVAALISAGLTFVETFSDSMHQLCKAALRAELYENSALSDRERMQLFL
SQ  DRAGFWVTDEDWAQVLDIVGQNYQMVTSRLYEDLFDLITATSEANSQELREPFTIFGKKVVVRAVQETVELHWQILFSQL
SQ  ILLVNMVDSESEEARPLHTRFDVGSVYRRLIDALRRLEHLRWMTKTELSVSPSKSRSGSSSPTLSKRGQDESYTRTALEE
SQ  LAGHLFGLPESNNMPLLSSITDLVLDLCAPTSTTVLNTWLIQCWLLKEGRPDLALELMPFAEQDPFSTYVQGRVFLALRD
SQ  YDTAAQHFRKAAIGLSIPLKHVDRHSAGLLDDTEWNLLNSGLPNYYAHIVNLYDKQKAYSYVMEFSRLALQFAQTSNQDS
SQ  ASIKTEMLSRLFTASTATSHFEEAHSALLAMDDEALQKSYLRKLLERMCESGQSSELISLPFSGLQNKVDEILAEKCRAT
SQ  RDVLNGVPYHQILYAWRISHNDYRGAAAILLDRLEKLRRSGEGDKLGAEDGENGAGNDALDTQVTRQYLIVINALSCVAP
SQ  QEAYILEDVPPPVPGKGTNDEEYSQTGSKRKLGKLNATSGEEDLDSRIEELARLLDSESAGDKKARPSSSSEEDQQLLER
SQ  MQKFSTAVRQEQGQQTPRRLLRLEDLRKQYQQELDRIVAIQNNQFALTADGEDEDEDMMDIA
//
ID  P35729;
PN  Nucleoporin NUP120;
GN  NUP120;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P35729;
DR  UNIPROT: D6VXN0;
DR  UNIPROT: P35730;
DR  PDB: 3F7F;
DR  PDB: 3H7N;
DR  PDB: 3HXR;
DR  PDB: 4XMM;
DR  PDB: 4XMN;
DR  PDB: 6X06;
DR  PDB: 7N84;
DR  PDB: 7N9F;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP120 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:8557737, ECO:0000269|PubMed:8565072}.
DE  Reference Proteome: Yes;
DE  Interaction: P53691; IntAct: EBI-393135; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P49687; IntAct: EBI-797641; Score: 0.95
DE  Interaction: P52891; IntAct: EBI-800196; Score: 0.91
DE  Interaction: P10592; IntAct: EBI-800487; Score: 0.35
DE  Interaction: P53011; IntAct: EBI-800487; Score: 0.91
DE  Interaction: Q06488; IntAct: EBI-800487; Score: 0.35
DE  Interaction: Q04439; IntAct: EBI-802262; Score: 0.35
DE  Interaction: Q04491; IntAct: EBI-812133; Score: 0.88
DE  Interaction: P32582; IntAct: EBI-815440; Score: 0.27
DE  Interaction: Q99257; IntAct: EBI-8220602; Score: 0.22
DE  Interaction: Q02630; IntAct: EBI-1269703; Score: 0.00
DE  Interaction: Q02629; IntAct: EBI-1269846; Score: 0.00
DE  Interaction: P40368; IntAct: EBI-6325174; Score: 0.00
DE  Interaction: P46673; IntAct: EBI-4325415; Score: 0.95
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P11484; IntAct: EBI-3781725; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3788002; Score: 0.35
DE  Interaction: P53900; IntAct: EBI-3821173; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-11888124; Score: 0.40
DE  Interaction: P35729; IntAct: EBI-11890170; Score: 0.53
DE  Interaction: Q8WUM0; IntAct: EBI-11890181; Score: 0.40
DE  Interaction: P47054; IntAct: EBI-11888914; Score: 0.37
DE  Interaction: P36161; IntAct: EBI-15786270; Score: 0.75
GO  GO:0000781;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0042802;
GO  GO:0017056;
GO  GO:0006302;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0000122;
GO  GO:0051664;
GO  GO:0006913;
GO  GO:0045893;
GO  GO:0045944;
GO  GO:0000973;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0031509;
GO  GO:0034398;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MACLSRIDANLLQYYEKPEPNNTVDLYVSNNSNNNGLKEGDKSISTPVPQPYGSEYSNCLLLSNSEYICYHFSSRSTLLT
SQ  FYPLSDAYHGKTINIHLPNASMNQRYTLTIQEVEQQLLVNVILKDGSFLTLQLPLSFLFSSANTLNGEWFHLQNPYDFTV
SQ  RVPHFLFYVSPQFSVVFLEDGGLLGLKKVDGVHYEPLLFNDNSYLKSLTRFFSRSSKSDYDSVISCKLFHERYLIVLTQN
SQ  CHLKIWDLTSFTLIQDYDMVSQSDSDPSHFRKVEAVGEYLSLYNNTLVTLLPLENGLFQMGTLLVDSSGILTYTFQNNIP
SQ  TNLSASAIWSIVDLVLTRPLELNVEASYLNLIVLWKSGTASKLQILNVNDESFKNYEWIESVNKSLVDLQSEHDLDIVTK
SQ  TGDVERGFCNLKSRYGTQIFERAQQILSENKIIMAHNEDEEYLANLETILRDVKTAFNEASSITLYGDEIILVNCFQPYN
SQ  HSLYKLNTTVENWFYNMHSETDGSELFKYLRTLNGFASTLSNDVLRSISKKFLDIITGELPDSMTTVEKFTDIFKNCLEN
SQ  QFEITNLKILFDELNSFDIPVVLNDLINNQMKPGIFWKKDFISAIKFDGFTSIISLESLHQLLSIHYRITLQVLLTFVLF
SQ  DLDTEIFGQHISTLLDLHYKQFLLLNLYRQDKCLLAEVLLKDSSEFSFGVKFFNYGQLIAYIDSLNSNVYNASITENSFF
SQ  MTFFRSYIIENTSHKNIRFFLENVECPFYLRHNEVQEFMFAMTLFSCGNFDQSYEIFQLHDYPEAINDKLPTFLEDLKSE
SQ  NYHGDSIWKDLLCTFTVPYRHSAFYYQLSLLFDRNNSQEFALKCISKSAEYSLKEIQIEELQDFKEKQHIHYLNLLIHFR
SQ  MFEEVLDVLRLGHECLSDTVRTNFLQLLLQEDIYSRDFFSTLLRLCNAHSDNGELYLRTVDIKIVDSILSQNLRSGDWEC
SQ  FKKLYCFRMLNKSERAAAEVLYQYILMQADLDVIRKRKCYLMVINVLSSFDSAYDQWILNGSKVVTLTDLRDELRGL
//
ID  Q09904;
PN  Nucleoporin nup124;
GN  nup124;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10409764}.
DR  UNIPROT: Q09904;
DR  Pfam: PF08604;
DR  Pfam: PF10599;
DE  Function: Nucleoporins may be involved in both binding and translocation of the proteins during nucleocytoplasmic transport. In S.pombe it is required for the nuclear localization of retrotransposon tf1. {ECO:0000269|PubMed:10409764}.
DE  Reference Proteome: Yes;
GO  GO:0140599;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0000054;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPPVSKNTRTSSKTVKKPYDPPQGSSRPFFTVLKRAFSSVLHPFTSGLDEKASGTASKDRKSGRAGTKSLLTPELTPHYL
SQ  GKSPRIIRVSNRSHVRTIDGIEEKVHTNTFEPRKPKQKQDYTNSPTLFKRHDELSLKSLNSLHPSSALSKKLGSTSQHQI
SQ  ATPKSSASLLNILRSLHDEQKNTLNISSVKQDRITEANPTCEKRKPSRSPSPMLSKKKSVARASENEPSAKQNKSFSGND
SQ  SHKSLTDIRDKENGETEVSAKNHVPHRSSRRRRRHQRLIPIIYETLEQMDLRKPVLVNAEVQTDSNPGNTMFIDKQDIYH
SQ  RLSTPTSRKRQTLEKGHIKAFSAVDEDLDEIFACEDDVHYTALPKQNPKSERILEPIIASPKDNTSDKGLLTKSAPTFEE
SQ  LQASITPKPVKTSPNDTALTLANAEDNKTFEHQPLSKDTEAPKSQFSSSPTKESTTRKSEVEPPSPSKEIKSSHFSVPEF
SQ  KFEPKTEATTDKKLNVPKFEFKPTATADVQTNRLKENEPKPTFFAQLPSKTQETPSITENKPSFFSQLSPKREETEKKDN
SQ  APSAPASTSGFSFGGFAPKTLEEKEETKAPTFNFSLNNASSTQDTTKPTLQFNFGSSFGKPTSNIFNDKKTSENGLASST
SQ  VASESKPSAPESKPSSGFGNTAGSSPFSFNLTKESKEVPPTNSFSFAKKGKDEANDSLSAKASTPFSFAKPNTENVTTTA
SQ  PQFSFNFTKPNTDAKTNLLPEKTFNEEAVKQKETEKEVPPTGPKASEIKDSVSSNNAVPSSTFNFVSPFAAVSEKTNENN
SQ  IPNDTTKTNGNATKRTLEQTEDAKPFAFSFGSTTEQANKKASTSNETTKPQLDTSSKTDGVTANAPFSFASAFNAPKPST
SQ  NTADGKDSASNLTTPSPAFSFGNNSGVKASSNNNPSTNSSTAPFSFGTSNKPAFSFGSATSKTTSEGTAPAASASAPAPT
SQ  TSAFSFGASNSSMNKEENTPMAKDAGDTAPASGFKSGFSFGANNSPQPASMFGTSTPAPSSAFAFGNQSGTNPAAPAGFG
SQ  GITNTATNNPPSTGFTFTPSNAGSTAAPMFGAGNTPNPSGSINNASQAFAFGSGEPSNPASNPPSTGFSFGAATPSAFNA
SQ  SASQSPAPNGIQFNLGSSNSQTNAPPGRKIAVPRSRRKR
//
ID  Q9UTH0;
PN  Nucleoporin nup132;
GN  nup132;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:15226438, ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9UTH0;
DR  UNIPROT: Q9UU23;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
DE  Interaction: Q10331; IntAct: EBI-295786; Score: 0.57
GO  GO:0140599;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0140602;
GO  GO:0017056;
GO  GO:1990426;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0090234;
GO  GO:0031297;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSILGKRKNEEVVSFSPLKRISVEKSLLDSTAYNNSLDWLRSKNFKVSCLLKHFNSKIINDHPLSGSCYTDIGYALINS
SQ  RKACFILSYRQSLGTAEPPTITFPLPEEDSNGFSGQNALTAFVPSDASDKEPGLLIVMPISGRIAYWTSIGNALAQSYIC
SQ  PQGMESLIKLLPKEKCEHLCCSNPMKFIISTNFGRLFSVQLRDPAGQPDVSVQLFASDISTFSTILQKMKIFNYPSIHII
SQ  ALKSPPLFSPYQHLLYVAEASGLLEIYDLKLENKLVSGMNLSPIFKQVLREGCPDASGLEVLDLTICPTNGNLVSFLVCW
SQ  KNSINYRYMIISLDFSDISSPSVMNIHPLYSFSSKSLESSKLHYSSSGNSLFVVLTDAVIIVHVQEDDKDIVSRTSWEEV
SQ  IRMNTNVSGGIFMSTCYKYVLGKYSIPTESCFIATPYSGIAEIEVHSLEHPANNESLVKSKLEEAVFYSFLPGNPIDFSC
SQ  NYLRSIKKPELERIIVDLGMDILNSRSTHLPPLFASLMQHLSCRLNSLNNLVRYIRSMSLDVDRQVLYKLRVMGEKCNSV
SQ  RYLWNTIDTEFSTVSHSLIFQRIIYRLTQSASSDNALREWFLHNIESIDQLIAQAHEFCIDSGSRVQELPLEVLDVIMEA
SQ  NEVILAIQSSALAYRRESQKIYKLSIDTFGEEVPWTSTPETLVLLCRQFELTRSALVQSHQGTSDVENTFKIKDKGVLRN
SQ  VVSNLEVQLVALTEVCFDAYSERIRWIEQRCGKDASEIQDVKEAFAVNRRFWVQTLSDIGKGSSAIRIAEKYSDYRSLVE
SQ  LCYQLYEDNELTDALNNYLDLFGIKFAFILYDYFVENGMALELLNSDRFNKSYLKQFFKSRDYNQISWMHDMRLGDYDAA
SQ  SHRLLQLATKQEKLVDKKESELSLSKLFLYAVPSNSGNIRDLVLVEQKLEQLHIQKMVSKSVMPVVERLRSQGKKYQLVE
SQ  AVVDDLIGAKVAPVIARQVMQRVVKKFIAGQVVEATELLEYLSFSLYRREDLVEGEVTDYYLALRLLLTTRLTDDAKRFY
SQ  ENTIWRRAVLHDNWIQVLDTQGKNDAIIETQFRMSALYRTLEAVTINGLFHEGLIRPGSLSSCKFEGYDPQNLISIYPPA
SQ  RFGDVTEVTKVLNRESVKLDHYLTKTNLNTCYISMCLSCDTI
//
ID  F4IGA5;
PN  Nuclear pore complex protein NUP133;
GN  NUP133;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000305|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4IGA5;
DR  UNIPROT: F4IGA4;
DR  UNIPROT: Q9SJ43;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFSPLTKRAKQSSRNEKTPRNRVPPPDSPVTPATQNRNNFISDRPATGTPAPWAPRLSVLARVSPGNNGDKGVDSDQLKP
SQ  VFVGEFPQLLRDEQSYPGDACVSGGMDKETCLSWFITGSKVFVWSHLTTLPSRKCVVLELPVVVLVNEESGSGLQDGKSW
SQ  LVNVVSWDTSAGAATRASRSRSPVGVVMCNRKTRAVVYWSDIFSGQEAAPAEKARHLIKRQSNGIRSSRAENSDLNSLIT
SQ  TAVAAAERLCIAIACSSNGELWQFTCSPTGVKSNQVQLNISSSSVSEGYPRSLIWRFSQGLARESCWEFLMLTDCDIHCF
SQ  TIEPYPDLTVSEVWQHEIVGTDGDSGIKKDIASQKQIWPLDLQVDDQGKVITVLVATICMDRASSSSYTQYSLLTLQHKS
SQ  EMRFADGREEKVLEKQGPIQVIIPKARVEDKDFLFSMRLRVGGRPPGSAIILSGDGTATVCYCHGSSTRLYKFDLPYDAG
SQ  KVLDASVLSSTDEHEYGAWTVLTEKAGVWAIPEKAVVLGGVEPPERSLSRKNSSNERSTRDETRVTPYGVDRTAGRENSD
SQ  IQNIEDKGNPKMGFTRQTARDEESEALLGQLFEGFLLSGKVDGSLEKLSQSGAFDRDGEANVFARKSKSIVDTLAKHWTT
SQ  TRGAEIVAMTVISSQLVEKQQKHENFLHFLALSKCHEELCSKQRHSLQIILENGEKLAAMIQLRELQNMINQNRSARFGS
SQ  PQAGSEDQVSCALWDLIQFVGERARRNTVLLMDRDNAEVFYSKVSELEEVFYCLNRQLEYIIRADQPLGTQLQRACELSN
SQ  ACVTILQTALDYKNEHQMWYPPLEGLIPWHSQTVVCNGLWCIASFMLHLLTEASRIDISAKSDIYTHLEVLTEVLLEACA
SQ  GSTFAKLEREEENKGLLNEYWTRRDTIFDSLYRQAKEFMEAEIQGIRERTEATDEDIFRNRCSNLISIAKRHAGYKIMWK
SQ  ICYDLNDTGLLRNLMHEGVGPQGGFSYFVFQQLYDMKQFSKLLRLGEEFQDELLIFLKRHSDLVWLHQVFLHQFSSASDT
SQ  LHTLALSQDEESMTTVEERTGPEPEDVQPTFADRKRFLNLSKIAYVADKDADSESKVKRIEADLNLLKLQEEITKALPNG
SQ  EARNRLFRPEELIETCLNIQGRWTAIKAFEVFAWTSSSFRENHRSLLEECWRNAADQDDWDRHHQASTNEGWSEEETLQN
SQ  LRNTALFQASKRCYGPTRVNTFDGDFAQVLPLRRENPEDSTSSVEDVLMSHKDFAEAGKLMLTAIMLGCVEEEGIVAEEF
SQ  SSPME
//
ID  P34343;
PN  Nuclear pore complex protein 15;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16950114}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12937276}. Note=Recruited early during nuclear envelope assembly after mitosis. {ECO:0000269|PubMed:16950114}.
DR  UNIPROT: P34343;
DR  UNIPROT: Q5WRU8;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Important for early nematode development. {ECO:0000269|PubMed:12937276}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGRDLELTLDRVSSIEYPALVKEAFLNNWHASAHRSEVTSNCASLNDRYCWVLSRNQIFIWERAKSSHRAIIPTQLPLP
SQ  TSGLPRSVKCVVVYDGVHRGANKTPCPGILVVSPEGVLRHWTSIESQTYIEEVLDINNEVALRVELTDEPIDGKSASFLL
SQ  TTTSGTVYFLNGKGQDSAKTGALECNKVAGREAHGFRRRLSSIMFGGESKESTSLITNSFQHQSKDLLVVTVSPDVLTVY
SQ  NMYTPCELWSLKTKEFFQPKIASFFEADLKRTPLKVRARLIDAAVFRDGLMILIGGTHEESQSVHMFMVWMSANWQTEQP
SQ  TGVVWSARVPMNEHRALFSKIDDSIYSNLTLCIPKNTAESKKADRTDGIIIINPYFAVSLYLPFDLAKPKKPESLYRHVS
SQ  IPPRDQLLGYAICSQYVYIMMLESGVSTIRLLPRGFADSSIYTHEQVVVPSLSVGTDDWPILSELLSEMVASGLPKTPLY
SQ  QSLHRAFELFAEKHMAESEEELKAIIKMPDQEIARIVSQFLYAIIDYSDAANKTDTELHAKRVLTSRIMLFLKHMGVYER
SQ  IISSPLGISRGGILSLRVGGTMLGEVSERVAASTAIWTWKTSNETNSAVFDAIIEKVLRIPEVQDLGLKDKDALFGRCGL
SQ  VHHIPVVAAQQLEKNVIGKTKSHRFEVFHAVCELLSGIKETIISWRNCRTKVAIPKFPIWWTLETFASCYRDVAEKIIEE
SQ  LKNGSSTDSERARLLMYILSIYDFYLSESDSQPDNDKVLQEMIALGKPADAMELAEKHKDFGTLVKNYLTTDVGTRQKTF
SQ  ERYKKMFEKDDFEMYLCDYLKEHGRNDVLLQQGGSRVDAYLDNFKELRYSREIANKQFGKAALTLMSLADAETKSFSKFV
SQ  EFLTRAYYCACSSIDGTDVSEVLDFYKRRYPEMKHRKRIPTEILKICFGNDLDAMMSVEDMLEWNMAVQPNDEASVEGFA
SQ  RAFHLLADLLAVHPDSDELKKKIDKTWKALVDYDEWNRVRSKEDVEKKTIFGKFCNYLINSYPADKGDSFPIWMPISRRL
SQ  IFPTDIDTVLDECIANTTGNHLSWIKGHLKWIGEQLCKQALLPKSAFFRPDMKQVGSISQAALEAFGPILQRREQRFIDQ
SQ  LNRDSMMET
//
ID  G0S9A7;
PN  Nucleoporin NUP133;
GN  NUP133;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P36161}. Nucleus membrane {ECO:0000250|UniProtKB:P36161}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36161}; Cytoplasmic side {ECO:0000250|UniProtKB:P36161}. Nucleus membrane {ECO:0000250|UniProtKB:P36161}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36161}; Nucleoplasmic side {ECO:0000250|UniProtKB:P36161}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P36161}.
DR  UNIPROT: G0S9A7;
DR  UNIPROT: G3EQ74;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP133 is involved in nuclear poly(A)+ RNA, tRNA and pre- ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000250|UniProtKB:P36161}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S0E7; IntAct: EBI-16069336; Score: 0.49
DE  Interaction: G0S2G1; IntAct: EBI-16069540; Score: 0.49
DE  Interaction: G0SER9; IntAct: EBI-16069694; Score: 0.44
DE  Interaction: G0SDQ4; IntAct: EBI-16069651; Score: 0.35
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P36161};
SQ  MFSSTLHEDGPATRTRSSRRRQRPVASDSSLQTQPKAKRQRVPLTESNTAPTPTPADADAPPEMFEVKPDPVLAKRERDG
SQ  IGIENIENLGPRRELSLRSKKPKSGERTSKGDGSIILTTNNAFTVSKLPALPDRLRAEPTSRQHGAIFSSGYALALTHTH
SQ  AFVWPYTATTASPETFTFALPYPSKHASDPLPLGALVPPSASSDDPGLVVVMPVSGRVVYWESISSAATLDFIRQQRTGI
SQ  EDAISGMYSSEHITQLVSAESAGFVLVFSSGRIAYMSVRDPHGRPGITVQYLRSPFGGASLGFLSTLRHALSGSSRGDIA
SQ  AAHANHGPRVGERVVIAASSKGRLQAWKIHRGGHHEPVAEADVRERLVEAVNEADAKTQAFPSESFEVLDFAFVPRGLEP
SQ  KYVNASRLSEALTHEEDSLQHMLLLVGFSRGHQARYSLVETVLAPEGARIGTVRPITSYTSPVRPGALEKPRLYLPRPAL
SQ  VAFVVFDRAVVVASMVAPPDSPDSQLQEDSHILPPTFEDVVDFRDDDTLQVVGSGSEEPGAGTSSEDVRPHRHKTKNPTA
SQ  VLLLPGVGIVRVAITDIERFASDAPPRVTAKSKLEQAVFFGIKSDNPLVFQGRRALPFSDREVCDAAVELSHEIVNSKTP
SQ  FIPSVPASLEGNMKSRSAYLDALITFLNACKVNMDERTRWMLLYDAEKMAVATWIWQKHEQFLAERPRADKKTLISEAAV
SQ  FINENQKTELNVAAGQVDPVRHWFIHDIFRLDIFVAWAYQIIKYHYTQKLSDEPGLNRLVWEAVTINNGALLEARQFRLD
SQ  KAAQYGVDPAVVPTGNGLPEPWTSTYFITNNLKRLTEFCHQWLAKHDAQPSADPRFDARLLDTVRERLPSLTSQYFTSLS
SQ  EYITWAASSTDPETQDRCRAYQAAYAEDVYKKIVKLKEFDLWEEAVELAREFEAFDALADVVVGQILMLEAAAADPTTTE
SQ  SKAQENAALAQVKKQRLGRLMEEFGEGFASRAYEVLLDAAGVQAVLEFAFDRKGFITKWLRGKPELARISWVNEVLREGD
SQ  VGGAAETLLGLGMSREVQVWNKKVELSLGKLALLAEGGGSDDEAGKGEVGGTIKKIDAELEVVKVQDLLYQWILASVHEA
SQ  VDSSAEVELAVKQFGGLIPRRQKALLQIFEDGIARLLKHEVLDPLTLIDLLTLSSLGPGHYEGMGDQFFLALKVAHYAAL
SQ  ENAEEVRRLIWRRCLVRDDWRQVNETNLKGDEEALEAVGETAAYRTLFACFDEESSTPTFRPHHTLKPSDCLGVYTEPEQ
SQ  LDSRFAAMDDSFRGKLVEAMRAEDRLLRGFVEKAQLDEWWRATRETAERMVGVAAQKGHRRVNSGSVGNGGVNGLSLNGR
SQ  VKMY
//
ID  F1QNV4;
PN  Nuclear pore complex protein Nup133;
GN  nup133;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8WUM0}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8WUM0}. Note=Located on both the cytoplasmic and nuclear sides of the nuclear pore. During mitosis, localizes to the kinetochores. {ECO:0000250|UniProtKB:Q8WUM0}.
DR  UNIPROT: F1QNV4;
DR  UNIPROT: Q7SZE9;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Involved in poly(A)+ RNA transport (By similarity). Involved in nephrogenesis (PubMed:30427554). {ECO:0000250|UniProtKB:Q8WUM0, ECO:0000269|PubMed:30427554}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFSPRGTPGSGRRQAPRTGGRRSVSAVQPGLLFSPRRSAVTARSTPTRVQSHAVVESYNFDVQTFGSSLPVKVMEALTMA
SQ  DVDDQISVKVEASGWAWMVCGERLIVWKVSQTSVAKLSVCKDLQLPSSEFAYSADLVSISSSGPLDLAPIQSISVLAVSP
SQ  DGLVRFWPSLAHEGSYTEISLDLSGHLSNYVAAVKGGSFIVSSYRGHLLRLSADSSGKLHHRPVQQGQGMLSGIGRRVSS
SQ  LFGIRGQPADLSVFSVLWVKASSCLYSLSSCGLSKWEVDENSETQVLSWSTNQIITDSITDAIWDSESNYSEIKKGVNVL
SQ  YLDMQPSNAGLVVLAAAWYPGDTPCVAYFCLVTLAESIVPSPDLLTVEVTKYNPPFQSEEELLKTRLVLPDPSSPAAYLY
SQ  NEELVFACSTGAGRGGLAEEKILFSSPGDRVRGGGVCADLPVFFSQNSGLVAVLARETASLLPETMEDSLCTSVAGPGPE
SQ  GTPLETPPKIDMVAQEDKTKLLKQAFLQFCRHDLVGAQSMVDELFPSDGEGSADLDTVVTQIDLDLVDDYPACDPRWAES
SQ  VPDEGAGFTLTSLILLHQLEDKMKAHRCLMDFLLQTGLLDRLTSTKVRSCPMATRLLLCEHAEKLSAAIVLKNHHAKHPE
SQ  LVNTAIQTALKKNSTDTPTNLTPADVFFREVSQISSIFECLLDEEEKALKEHPDAARWGEVVLSVNDIIKDMLQAAAQYR
SQ  ETKASLYRAPENCSPEPEYIPWTASGGVGGVRSVISRQHELILRAAYPHADAELRSVLCEQLVALLDSLLSGYVAQLTSL
SQ  RRGGQQERYDTLENEYTQKRSELLKPLLELGQHQWVAALAEKYCDFDILVQLCERTDNQSRLQQYMVKFADQNFADFLFR
SQ  WYMEKGKRGKLLSQPMATHQQLASFLQAHDHLSWLHDIHVQDYQRAHRTLYNQANMETRYFSKKKTLLALSKLTALASDM
SQ  PEPVHRRQLNDIVEQERFLLHQETLPKQLLEEKQLNPDSMPLLSPQNLISLYICDENRGANEYDFKKALDLLEYFEEENG
SQ  IDVDALKREIFSKALKKDWKESWSSSDDNDDPLEAARDSTFVKILQKLIQERVSLQTYLPDIKDLLQEDELESLKSKPYF
SQ  EFLLRANYEHYLKVQI
//
ID  Q9VCW3;
PN  Nuclear pore complex protein Nup133;
GN  Nup133;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8WUM0}. Note=Located on both the cytoplasmic and nuclear sides of the nuclear pore. {ECO:0000250|UniProtKB:Q8WUM0}.
DR  UNIPROT: Q9VCW3;
DR  UNIPROT: Q86PB8;
DR  UNIPROT: Q961A9;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Probable component of the nuclear pore complex (NPC) (Probable). Plays a role in NPC assembly and/or maintenance (PubMed:20547758). {ECO:0000269|PubMed:20547758, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VJ00; IntAct: EBI-206094; Score: 0.00
DE  Interaction: Q24564; IntAct: EBI-235723; Score: 0.00
DE  Interaction: P05812; IntAct: EBI-272655; Score: 0.00
DE  Interaction: A1Z8Z7; IntAct: EBI-281990; Score: 0.00
DE  Interaction: Q95TK6; IntAct: EBI-505273; Score: 0.00
DE  Interaction: Q9VZU6; IntAct: EBI-505280; Score: 0.00
DE  Interaction: Q9VKQ7; IntAct: EBI-505287; Score: 0.00
DE  Interaction: O17144; IntAct: EBI-505294; Score: 0.00
DE  Interaction: Q8SY59; IntAct: EBI-505301; Score: 0.00
DE  Interaction: Q867V1; IntAct: EBI-505308; Score: 0.37
DE  Interaction: A1Z6E0; IntAct: EBI-505315; Score: 0.37
DE  Interaction: Q9W5Y0; IntAct: EBI-505322; Score: 0.00
DE  Interaction: P55841; IntAct: EBI-505329; Score: 0.37
DE  Interaction: Q8IMH4; IntAct: EBI-505336; Score: 0.37
DE  Interaction: P51123; IntAct: EBI-505343; Score: 0.00
DE  Interaction: O97143; IntAct: EBI-505350; Score: 0.37
DE  Interaction: Q9VME5; IntAct: EBI-505357; Score: 0.37
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERNLQKQLYGISRESSPGARRYSMPAASADSTRKSIFGGSASCAQMSGSLKRTALTNSRLSLSVRSTQSIAGIRSDYNS
SQ  VESFGCPLPVVVNEALTFAGPGAGTVTAKVTQNGWAWVVQGRRLLIWQYKDTAKSGSPPRVGKLARRGGGLAQCRELTLP
SQ  YSDLGHKSDLISVFQTEGQQMASCIAVSATGEVRYWSSIAHDGNSVDLSILTGQEFVQLLSLPTQQGYLAVTTTCNLVFL
SQ  RVGLTNGRYTLHHKTIKPATSFLGGFGKKFASILIGMNTGADKDQTLVGMCCESNLESGETIVAVLSDRAIQRWSLSNNG
SQ  NTENLLYEDADMLRRIREEFITNFWKFRLPADSLEIDLHLLDFHVVKNKAYILAGAVNAAHAPQMCYALVTGTAQAERML
SQ  LESFTPLNMNKFFSAKTEEDCLSVRFVVGSSHIYLYTSKVVYPLHLTNSVPTAELEAEKIEFHQHDDRILSAVICSQLPL
SQ  FFSRTHGLVSITPGDFDGTEMMNMSSCNTPDLYAPNSCNASFAVADHSALTNSTNNLHLFELDPDEMYNELSDEVGQLKA
SQ  AFLYHMKRNSNMVKTIVDELLRNVTAADPSGAPMDAYKLDRIVITIAEDLAEDIPIADPRWEEALADQEMNRHAIGSSRS
SQ  MQIINQLRDKIIAFQHFITFLHSSLVWDKLNVIPCGSHSLKPTGCILADISEKIVAAMALRSIQTKLPKLIEEAIDATVA
SQ  LWHEEPQGSLTYQDIFYVKLSRFQNVFEALADIADDRIAAQNQTTISVAHFVNEINSIVLDVLGQVFKYRKQHASSFRLS
SQ  HEKLPSYENLPWTAMAGSAGVRDTLTRLIDISVRYGSHCVSETELKQQLYQQIFELIDLVLDGRKTYLKSVRDTEKFNVL
SQ  QQQFEAQRRELISVLIKDRQYEYAAKIAEKYLDFQSLVLICDETQDKERLEDYTRKYEEYDFSQFAINWHLRQNRHGEVF
SQ  ERFKGNQTALAQFMRDHPSLGWIQLIFNGDFERAAKVLYELAQCETEFVARKKSMLSLAKLAAFAAAESDLTAQVEKINA
SQ  DLTLVEYQSQLGHDVLESFGFDPAEQKVLKAEEIISLYIAEENETASETEFRKALELLSYVEQPYDMRHKIWCAAIKRDN
SQ  WTDYDPNNAVHYMQKLLFYKIIEISQLMGNDSENVLPPMEDFLESVELGDLPQQKPFQYLLKLTYEYVADMFKQPDDMEL
//
ID  Q8WUM0;
PN  Nuclear pore complex protein Nup133;
GN  NUP133;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11564755}. Note=Located on both the cytoplasmic and nuclear sides of the nuclear pore (PubMed:11564755). During mitosis, localizes to the kinetochores (PubMed:11564755). {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
DR  UNIPROT: Q8WUM0;
DR  UNIPROT: B2RAZ8;
DR  UNIPROT: Q5T8N0;
DR  UNIPROT: Q9H9W2;
DR  UNIPROT: Q9NV71;
DR  UNIPROT: Q9NVC4;
DR  PDB: 1XKS;
DR  PDB: 3CQC;
DR  PDB: 3CQG;
DR  PDB: 3I4R;
DR  PDB: 5A9Q;
DR  PDB: 7PEQ;
DR  Pfam: PF03177;
DR  OMIM: 607613;
DR  OMIM: 618177;
DR  OMIM: 618349;
DR  DisGeNET: 55746;
DE  Function: Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222). {ECO:0000269|PubMed:11684705, ECO:0000269|PubMed:30179222}.
DE  Disease: Nephrotic syndrome 18 (NPHS18) [MIM:618177]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form that progresses to end-stage renal failure. NPHS18 is an autosomal recessive, steroid-resistant progressive form with onset in the first decade of life. {ECO:0000269|PubMed:30179222}. Note=The disease is caused by variants affecting the gene represented in this entry. Galloway-Mowat syndrome 8 (GAMOS8) [MIM:618349]: A form of Galloway-Mowat syndrome, a severe renal-neurological disease characterized by early-onset nephrotic syndrome associated with microcephaly, central nervous system abnormalities, developmental delays, and a propensity for seizures. Brain anomalies include gyration defects ranging from lissencephaly to pachygyria and polymicrogyria, and cerebellar hypoplasia. Most patients show facial dysmorphism characterized by a small, narrow forehead, large/floppy ears, deep-set eyes, hypertelorism and micrognathia. Additional variable features are visual impairment and arachnodactyly. Most patients die in early childhood. GAMOS8 inheritance is autosomal recessive. {ECO:0000269|PubMed:30427554}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P11802; IntAct: EBI-11132267; Score: 0.35
DE  Interaction: P35729; IntAct: EBI-11890181; Score: 0.40
DE  Interaction: P46673; IntAct: EBI-11890201; Score: 0.51
DE  Interaction: P49454; IntAct: EBI-7328986; Score: 0.48
DE  Interaction: P49790; IntAct: EBI-7329388; Score: 0.53
DE  Interaction: P52891; IntAct: EBI-11890201; Score: 0.40
DE  Interaction: P52948; IntAct: EBI-295755; Score: 0.35
DE  Interaction: P53011; IntAct: EBI-11890201; Score: 0.40
DE  Interaction: P55735; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-295708; Score: 0.90
DE  Interaction: P78406; IntAct: EBI-11889630; Score: 0.37
DE  Interaction: Q12769; IntAct: EBI-295755; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q7Z3B4; IntAct: EBI-11889088; Score: 0.37
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q8NFH3; IntAct: EBI-21865034; Score: 0.53
DE  Interaction: Q8NFH4; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.56
DE  Interaction: Q5EWX9; IntAct: EBI-8070469; Score: 0.35
DE  Interaction: O15273; IntAct: EBI-5665154; Score: 0.00
DE  Interaction: Q9UBU9; IntAct: EBI-6262548; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: Q9BW27; IntAct: EBI-9032422; Score: 0.57
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.69
DE  Interaction: Q6ZQN5; IntAct: EBI-11318220; Score: 0.35
DE  Interaction: Q12952; IntAct: EBI-11318689; Score: 0.35
DE  Interaction: Q9BZS1; IntAct: EBI-11319193; Score: 0.35
DE  Interaction: Q9C009; IntAct: EBI-11319301; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: P08670; IntAct: EBI-11083342; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q80YV4; IntAct: EBI-11095972; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: Q9NRG9; IntAct: EBI-11888192; Score: 0.37
DE  Interaction: P04049; IntAct: EBI-11904819; Score: 0.00
DE  Interaction: Q68CZ1; IntAct: EBI-11917110; Score: 0.00
DE  Interaction: P06821; IntAct: EBI-12577493; Score: 0.35
DE  Interaction: P0C0U1; IntAct: EBI-12579809; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-12579395; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581451; Score: 0.35
DE  Interaction: C5E526; IntAct: EBI-12584472; Score: 0.35
DE  Interaction: C5E527; IntAct: EBI-12585279; Score: 0.35
DE  Interaction: Q20MH8; IntAct: EBI-12586007; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12588098; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12588729; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-14035664; Score: 0.35
DE  Interaction: Q9UBP0; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q6XPS3; IntAct: EBI-21801323; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: P10412; IntAct: EBI-20930728; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: Q9Y275; IntAct: EBI-21266480; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC5; IntAct: EBI-26495256; Score: 0.35
DE  Interaction: Q13936; IntAct: EBI-26508997; Score: 0.37
DE  Interaction: P52298; IntAct: EBI-26399642; Score: 0.35
DE  Interaction: Q8NI60; IntAct: EBI-28943519; Score: 0.35
DE  Interaction: Q9Y6S9; IntAct: EBI-28948011; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q8WUK0; IntAct: EBI-27114632; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0021915;
GO  GO:0022008;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0048339;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0061053;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFPAAPSPRTPGTGSRRGPLAGLGPGSTPRTASRKGLPLGSAVSSPVLFSPVGRRSSLSSRGTPTRMFPHHSITESVNYD
SQ  VKTFGSSLPVKVMEALTLAEVDDQLTINIDEGGWACLVCKEKLIIWKIALSPITKLSVCKELQLPPSDFHWSADLVALSY
SQ  SSPSGEAHSTQAVAVMVATREGSIRYWPSLAGEDTYTEAFVDSGGDKTYSFLTAVQGGSFILSSSGSQLIRLIPESSGKI
SQ  HQHILPQGQGMLSGIGRKVSSLFGILSPSSDLTLSSVLWDRERSSFYSLTSSNISKWELDDSSEKHAYSWDINRALKENI
SQ  TDAIWGSESNYEAIKEGVNIRYLDLKQNCDGLVILAAAWHSADNPCLIYYSLITIEDNGCQMSDAVTVEVTQYNPPFQSE
SQ  DLILCQLTVPNFSNQTAYLYNESAVYVCSTGTGKFSLPQEKIVFNAQGDSVLGAGACGGVPIIFSRNSGLVSITSRENVS
SQ  ILAEDLEGSLASSVAGPNSESMIFETTTKNETIAQEDKIKLLKAAFLQYCRKDLGHAQMVVDELFSSHSDLDSDSELDRA
SQ  VTQISVDLMDDYPASDPRWAESVPEEAPGFSNTSLIILHQLEDKMKAHSFLMDFIHQVGLFGRLGSFPVRGTPMATRLLL
SQ  CEHAEKLSAAIVLKNHHSRLSDLVNTAILIALNKREYEIPSNLTPADVFFREVSQVDTICECLLEHEEQVLRDAPMDSIE
SQ  WAEVVINVNNILKDMLQAASHYRQNRNSLYRREESLEKEPEYVPWTATSGPGGIRTVIIRQHEIVLKVAYPQADSNLRNI
SQ  VTEQLVALIDCFLDGYVSQLKSVDKSSNRERYDNLEMEYLQKRSDLLSPLLSLGQYLWAASLAEKYCDFDILVQMCEQTD
SQ  NQSRLQRYMTQFADQNFSDFLFRWYLEKGKRGKLLSQPISQHGQLANFLQAHEHLSWLHEINSQELEKAHATLLGLANME
SQ  TRYFAKKKTLLGLSKLAALASDFSEDMLQEKIEEMAEQERFLLHQETLPEQLLAEKQLNLSAMPVLTAPQLIGLYICEEN
SQ  RRANEYDFKKALDLLEYIDEEEDININDLKLEILCKALQRDNWSSSDGKDDPIEVSKDSIFVKILQKLLKDGIQLSEYLP
SQ  EVKDLLQADQLGSLKSNPYFEFVLKANYEYYVQGQI
//
ID  Q8R0G9;
PN  Nuclear pore complex protein Nup133;
GN  Nup133;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8WUM0}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8WUM0}. Note=Located on both the cytoplasmic and nuclear sides of the nuclear pore. During mitosis, localizes to the kinetochores. {ECO:0000250|UniProtKB:Q8WUM0}.
DR  UNIPROT: Q8R0G9;
DR  UNIPROT: E9QLJ8;
DR  Pfam: PF03177;
DE  Function: Involved in poly(A)+ RNA transport. Involved in nephrogenesis. {ECO:0000250|UniProtKB:Q8WUM0}.
DE  Reference Proteome: Yes;
DE  Interaction: P49452; IntAct: EBI-8573213; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0000940;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0021915;
GO  GO:0022008;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0048339;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0061053;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFPSVSSPRTPGPGTRRGPLVGIGPTSTPRASRRGLSLGSAVNSPVLFSPAGRRSSVSSRGTPTRIFPHHSISESVNYDV
SQ  RVFGSSLPVKIMEALTMAEADEQLSVHVDEGGWACLVCTEKLLIWKIAVSPVTKLSVCKELQLPPSDFHGSADLVALSYA
SQ  ATSGEVHSVQAVSVMVATKEGSIRYWPSLAREDTYSDTCVDLGGEKMCRFLTAVQGGSFILSSVGSQLVRLIPESSGKIH
SQ  QHVLPQGQGMLSGIGRRVSSLFGILSPTSDLMLASVLWDRGGSSFYTLTSSNISKWELDDSSEKQVHSWDVHRTLKESIT
SQ  DAVWGSESNYEAIKEGVNIQYLDLKQNCDGLLILAAAWHLGDSPCLVYYSVITVEDNGNQMSDAVTVEVTQYNPPFQSED
SQ  LIACRLMVPNFSSQMTYLYMENAVFVCSTGTGKFSLPQEKIVFDTQGDGILGAGSCAGVPILFSRNSGLVSVTPRENVSL
SQ  LAEDLEESLTSSVGGRGSESMVFETTTKNETVAHEDKTKLLKAAFLQYCRKDLGRAQIMADELFSSHTDLDSDPELDKAV
SQ  TQISVDLIDDYPASDPRWAESVPQEAPGLSNTSLIILHQLEDKMKAHCLLVDFLHQVGLFRRLSSYPIRGTPMSTRLLLC
SQ  EHAEKLSAAITLKNHHSRLPDLVNSAILLALNKRECEVPNSLTPADVFFREVSQVDTICECLLEHEEQVLREVALVSQEW
SQ  AEVAIDVNTVLKDMLQAATHYRLNKSSMYSQEEVLGKEPEYVPWTATSGPSGIRTAVMRQHGIILKMVYPQADSKLRNVV
SQ  MEQLVALIDCFLDSYVSQLKSLEKSSDQERYSSLEVEYLQKRSELLSPLLTLGQYPWAASLAEKYCDFDILVQMCEQTDN
SQ  QARLQRYMTQFADQNFSDFLFRWYLEKGKRGKLLSQPISQHGQLANFLQAHEHLSWLHEINSQELEKAHTTLLGLANMET
SQ  RYFAKKKTLLGLSKLAALASDISEDRLQEKIEAMAEQERFLLHQETLPEQLLTERQLSLSAMPVLTAPQLISLYICDENR
SQ  RANEYDFKKALDLLEYIDEEEDVSIDDLKLEILCRALQRDDWSGSDGKDDPIEVSKDSVFVKILQKLIKDGIQLSEYLPE
SQ  VTDLLRAEQLGSLKSNSYFEFVLKANYEYYVQGQM
//
ID  P36161;
PN  Nucleoporin NUP133;
GN  NUP133;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P36161;
DR  UNIPROT: D6VXE2;
DR  PDB: 3KFO;
DR  PDB: 6X02;
DR  PDB: 6X03;
DR  PDB: 6X04;
DR  PDB: 6X05;
DR  PDB: 7N84;
DR  PDB: 7N9F;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP133 is involved in nuclear poly(A)+ RNA, tRNA and pre- ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:7813444, ECO:0000269|PubMed:7862658, ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9049242}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-7438937; Score: 0.44
DE  Interaction: P35729; IntAct: EBI-15786270; Score: 0.75
DE  Interaction: P46673; IntAct: EBI-295762; Score: 0.55
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P16140; IntAct: EBI-787098; Score: 0.35
DE  Interaction: P0CS90; IntAct: EBI-787098; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-787098; Score: 0.35
DE  Interaction: P22515; IntAct: EBI-7101777; Score: 0.40
DE  Interaction: Q06440; IntAct: EBI-7438922; Score: 0.40
DE  Interaction: P40477; IntAct: EBI-7439043; Score: 0.40
DE  Interaction: P40368; IntAct: EBI-8466646; Score: 0.40
DE  Interaction: Q02647; IntAct: EBI-8466751; Score: 0.40
DE  Interaction: P52891; IntAct: EBI-7700705; Score: 0.55
DE  Interaction: Q04439; IntAct: EBI-7454093; Score: 0.37
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P11484; IntAct: EBI-3691902; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3712954; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3727430; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-3734627; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3745787; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3750959; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3799837; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3812927; Score: 0.35
DE  Interaction: P48363; IntAct: EBI-3817414; Score: 0.35
DE  Interaction: P47079; IntAct: EBI-3823897; Score: 0.35
DE  Interaction: P31539; IntAct: EBI-3827376; Score: 0.35
DE  Interaction: Q04432; IntAct: EBI-3830694; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-4392409; Score: 0.37
DE  Interaction: P39523; IntAct: EBI-9976090; Score: 0.35
DE  Interaction: Q04491; IntAct: EBI-16281671; Score: 0.35
GO  GO:0000781;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0006302;
GO  GO:0031990;
GO  GO:0000122;
GO  GO:0051664;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0045893;
GO  GO:0045944;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0030466;
GO  GO:0031509;
GO  GO:0034398;
GO  GO:0000972;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSEKKVHLRLRKELSVPIAVVENESLAQLSYEEESQASLMDISMEQQQLRLHSHFDNSKVFTENNRYIVKTLQTDYSSGF
SQ  SNDDELNGYIDMQIGYGLVNDHKKVYIWNIHSTQKDTPYITVPFRSDDNDEIAVAPRCILTFPATMDESPLALNPNDQDE
SQ  TGGLIIIKGSKAIYYEDINSINNLNFKLSEKFSHELELPINSSGGEKCDLMLNCEPAGIVLSTNMGRIFFITIRNSMGKP
SQ  QLKLGKLLNKPFKLGIWSKIFNTNSSVVSLRNGPILGKGTRLVYITTNKGIFQTWQLSATNSHPTKLIDVNIYEAILESL
SQ  QDLYPFAHGTLKIWDSHPLQDESSQLFLSSIYDSSCNETYYILSTIIFDSSSNSFTIFSTYRLNTFMESITDTKFKPKIF
SQ  IPQMENANDTNEVTSILVMFPNAVVITQVNSKLDSSYSMRRKWEDIVSLRNDIDIIGSGYDSKSLYVLTKQMGVLQFFVK
SQ  ENEETNSKPEVGFVKSHVDQAVYFSKINANPIDFNLPPEISLDQESIEHDLKLTSEEIFHSNGKYIPPMLNTLGQHLSVR
SQ  KEFFQNFLTFVAKNFNYKISPELKLDLIEKFEILNCCIKFNSIIRQSDVLNDIWEKTLSNYNLTQNEHLTTKTVVINSPD
SQ  VFPVIFKQFLNHVVFVLFPSQNQNFKLNVTNLINLCFYDGILEEGEKTIRYELLELDPMEVDTSKLPWFINFDYLNCINQ
SQ  CFFDFTFACEEEGSLDSYKEGLLKIVKILYYQFNQFKIWINTQPVKSVNANDNFININNLYDDNHLDWNHVLCKVNLKEQ
SQ  CIQIAEFYKDLSGLVQTLQTLDQNDSTTVSLYETFFNEFPKEFSFTLFEYLIKHKKLNDLIFRFPQQHDVLIQFFQESAP
SQ  KYGHVAWIQQILDGSYADAMNTLKNITVDDSKKGESLSECELHLNVAKLSSLLVEKDNLDINTLRKIQYNLDTIDAEKNI
SQ  SNKLKKGEVQICKRFKNGSIREVFNILVEELKSTTVVNLSDLVELYSMLDDEESLFIPLRLLSVDGNLLNFEVKKFLNAL
SQ  VWRRIVLLNASNEGDKLLQHIVKRVFDEELPKNNDFPLPSVDLLCDKSLLTPEYISETYGRFPIDQNAIREEIYEEISQV
SQ  ETLNSDNSLEIKLHSTIGSVAKEKNYTINYETNTVEY
//
ID  G0SAK3;
PN  Nucleoporin NUP145C;
GN  NUP145;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: [Nucleoporin NUP145C]: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49687}; Cytoplasmic side {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49687}; Nucleoplasmic side {ECO:0000250|UniProtKB:P49687}. Note=Symmetrically distributed on the cytoplasmic and nucleoplasmic side of nuclear envelope. {ECO:0000250|UniProtKB:P49687}. [Nucleoporin NUP145N]: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49687}; Nucleoplasmic side {ECO:0000250|UniProtKB:P49687}. Note=Biased towards the nucleoplasmic side, nuclear pore complex. {ECO:0000250|UniProtKB:P49687}.
DR  UNIPROT: G0SAK3;
DR  UNIPROT: G3EQ75;
DR  UNIPROT: G3EQ76;
DR  PDB: 5CWW;
DR  PDB: 5HB0;
DR  PDB: 5HB5;
DR  PDB: 5HB6;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export. {ECO:0000250|UniProtKB:P49687}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S0E7; IntAct: EBI-16069336; Score: 0.63
DE  Interaction: G0S156; IntAct: EBI-16176459; Score: 0.46
DE  Interaction: G0S2G1; IntAct: EBI-16069540; Score: 0.58
DE  Interaction: G0S4F3; IntAct: EBI-16176900; Score: 0.44
DE  Interaction: G0S4T0; IntAct: EBI-16176802; Score: 0.52
DE  Interaction: G0S7B6; IntAct: EBI-16176781; Score: 0.44
DE  Interaction: G0SA60; IntAct: EBI-16069606; Score: 0.44
DE  Interaction: G0SER9; IntAct: EBI-16069356; Score: 0.44
DE  Interaction: G0SDQ4; IntAct: EBI-16069488; Score: 0.52
DE  Interaction: G0RZB7; IntAct: EBI-16160305; Score: 0.40
DE  Interaction: G0SGZ5; IntAct: EBI-16160383; Score: 0.40
DE  Interaction: G0SG92; IntAct: EBI-16160592; Score: 0.35
DE  Interaction: G0SET4; IntAct: EBI-16160592; Score: 0.35
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0016787;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P49687};
SQ  MSFGFGSGGFGQNNNSSTFGGFGSTPTTNTGFGSTGTTAFGSTSNTTGGGLFGGGGGGFGSGNTFGSGFGSKPAFGTPAT
SQ  TSSTSLFGSTTTTAGGTGFGSGGFGSTNTSSPFGGGGTSLFGNKTTTGFGSGTSTFGSNTGGGLFGGGSTTTGFGATNNP
SQ  GIGTNVGDPPGTAVVPFSPTVEKEVNNPSQSNSYQNILFMDAYKKWSAEELRLADYNQGRKTAAPGGTGAFGSSGFGGFG
SQ  TTSNTGGFGSNTGGGLFGNTQQNTGGFGTTNTTGSAFGSGGGLFGNKPATGGLFGTSSSQPAQSGGLFGSGTASTFGSSN
SQ  TGTTSTFGSNNNTGGGLFGSNNTSSKPAFSFGTSNTSTPGFGTATTGSGFGTGTTTNTGGGLFGNTAQNTNTGGGLFGNQ
SQ  QQSGSAFGSGTGFGQQNQSTGTSLFGNTQQKPGGLFGSTTTNTSGGLFGSTNTGTSTFGQTPATQNTGGGLFGSKPAGTG
SQ  GLFGSTATNQPASTGGLFGNLNTNAQTQQPATGGLFGNLGQNNQAKPSLFGTSTTTGGGLFGNTNAQQQTGSLFGTSTAQ
SQ  QQPQTGLGASLFGSSQQQQQQPQTFSTSITDISAYGATTLFSGLPDDKIQNPGPLATPLSGKAKVKSRSILPMYKLSPAN
SQ  ASRLVTTPQKRAYGFSFSAYGSPTSPSSSASSTPGAFGQSILSSSINRGLNKSISASNLRRSLNVEDSILQPGAFSANSS
SQ  MRLLGGPGSHKKLVINKDMRTDLFSPPNKDKQPQEDGTAARKTVTKRVSFDTSNVETPEKTIESSIPATDDSGYLKPDAR
SQ  STANGTNGANGAKSSPVAAASPPEMEQVKGKELAVVHEEESPAPAQTDKPRGSQIEPGAYWMSPTADDIRAMNRMQRQRV
SQ  VGFTVGRENVGSVQFKVPVDLSNINLDDLFGTIVILEPRSATVYPNAAKKPPMGKGLNVPALISLEHSWPRGGPTIKGRR
SQ  LERHIERLKSIPDTTFESYDPETGVWAFSVEHFTTYGLGDDDDYDDDDYETEPESAVKSTPRPVTSPSISKSSTSPIDPD
SQ  DTFEFRRSRRALPGAFDDAALSDTDEVANHAQRQGTLSPEPQDADTPLPSREWPEDESMADGLDEYQLEAYEEASQQGSV
SQ  DEQEDFLPSRFAADNDAPQVPAGIMRARMRAVKKLNAPTKIEVAGGDDWTQILQASVKAPRTMDRATLRALNESGAVWEM
SQ  KDRGSPPPQATATVSDGMGFATSIDLMKSLFEQAKAPTQPALTTSGKGFVKWPYEQRSKTDTEENLAVPRTNWGPNELLI
SQ  STQHNEPNLLPVDAADDSATSPSTLARLQQYINLVSSKKQLQRVAGPEFRELAQGDSVWELAALLFDDNGEGVSQFWQQL
SQ  VSEATDRALSFTAGLEEKAIICLAGNRVDEACRHLLAAGNFRLATLVSTIGKVDNKDIRAQLKDWRESNVLAEFSEPIRA
SQ  IYELLAGNASVCAGVKNVPIENRVNSFTISQRFGLDWMRSFGLRLWYTSGVIPDVAAAVRSFQEDIEQDREPEPDSALWT
SQ  LLKAFASREYDWSDTRLGWLLTKAIYTTGKVSFGEDALQKLDKASVTFASALTAASHWVPATFVLLQLSDPASREAAVRD
SQ  HLGRHAHRIGSPRNLMSPFFTLQKFGVPEAWIWEAKALDYRSRQDSQQEFLALIWAQNYAEANRTFVTRVGPDLVIERNL
SQ  PRLFAFAQLLFKVKKHLPNWERSAAVYLLYPMAVMQNQGSGKLDRFDNQLIDGLVALHSQTHGDIRQEAAIADMAEELIK
SQ  CKGAAAASDPRLLQLLPQDVRGKYLRAQVLEAF
//
ID  P49687;
PN  Nucleoporin NUP145C;
GN  NUP145;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: [Nucleoporin NUP145C]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetrically distributed on the cytoplasmic and nucleoplasmic side of nuclear envelope. [Nucleoporin NUP145N]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards the nucleoplasmic side, nuclear pore complex.
DR  UNIPROT: P49687;
DR  UNIPROT: D6VU53;
DR  PDB: 3BG0;
DR  PDB: 3BG1;
DR  PDB: 3IKO;
DR  PDB: 3JRO;
DR  PDB: 3JRP;
DR  PDB: 3KEP;
DR  PDB: 3KES;
DR  PDB: 4XMM;
DR  PDB: 4XMN;
DR  PDB: 7N84;
DR  PDB: 7N9F;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export. It is also required for normal NPC distribution (probably through interactions with MLP1 and MLP2) and NPC assembly, as well as for normal nuclear envelope organization. {ECO:0000269|PubMed:10542288, ECO:0000269|PubMed:10638763, ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:8044840, ECO:0000269|PubMed:8195299, ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9305650}.
DE  Reference Proteome: Yes;
DE  Interaction: P32500; IntAct: EBI-11888586; Score: 0.37
DE  Interaction: P35729; IntAct: EBI-797641; Score: 0.95
DE  Interaction: P38181; IntAct: EBI-4421662; Score: 0.59
DE  Interaction: P40368; IntAct: EBI-11889248; Score: 0.37
DE  Interaction: P46673; IntAct: EBI-797641; Score: 0.92
DE  Interaction: P47054; IntAct: EBI-11888900; Score: 0.59
DE  Interaction: P48837; IntAct: EBI-1269934; Score: 0.00
DE  Interaction: P49686; IntAct: EBI-1269527; Score: 0.00
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P10592; IntAct: EBI-797641; Score: 0.35
DE  Interaction: P53011; IntAct: EBI-797641; Score: 0.81
DE  Interaction: Q04491; IntAct: EBI-797641; Score: 0.97
DE  Interaction: P52891; IntAct: EBI-797641; Score: 0.95
DE  Interaction: P32582; IntAct: EBI-815440; Score: 0.27
DE  Interaction: Q03718; IntAct: EBI-853738; Score: 0.35
DE  Interaction: P53230; IntAct: EBI-853809; Score: 0.35
DE  Interaction: Q06411; IntAct: EBI-853826; Score: 0.35
DE  Interaction: P47077; IntAct: EBI-854045; Score: 0.35
DE  Interaction: P32599; IntAct: EBI-7439550; Score: 0.40
DE  Interaction: Q06440; IntAct: EBI-8467290; Score: 0.40
DE  Interaction: Q99257; IntAct: EBI-8220602; Score: 0.22
DE  Interaction: Q06142; IntAct: EBI-1269395; Score: 0.00
DE  Interaction: Q02630; IntAct: EBI-1269637; Score: 0.00
DE  Interaction: Q02629; IntAct: EBI-1269780; Score: 0.00
DE  Interaction: P55735; IntAct: EBI-1580653; Score: 0.70
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P10591; IntAct: EBI-3673738; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3691910; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-3762846; Score: 0.35
DE  Interaction: Q02199; IntAct: EBI-11888836; Score: 0.37
DE  Interaction: P49687; IntAct: EBI-11888852; Score: 0.37
GO  GO:0000781;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0031080;
GO  GO:0016787;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0006302;
GO  GO:0006607;
GO  GO:0051664;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0045893;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0046822;
GO  GO:0031509;
GO  GO:0034398;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFNKSVNSGFTFGNQNTSTPTSTPAQPSSSLQFPQKSTGLFGNVNVNANTSTPSPSGGLFNANSNANSISQQPANNSLFG
SQ  NKPAQPSGGLFGATNNTTSKSAGSLFGNNNATANSTGSTGLFSGSNNIASSTQNGGLFGNSNNNNITSTTQNGGLFGKPT
SQ  TTPAGAGGLFGNSSSTNSTTGLFGSNNTQSSTGIFGQKPGASTTGGLFGNNGASFPRSGETTGTMSTNPYGINISNVPMA
SQ  VADMPRSITSSLSDVNGKSDAEPKPIENRRTYSFSSSVSGNAPLPLASQSSLVSRLSTRLKATQKSTSPNEIFSPSYSKP
SQ  WLNGAGSAPLVDDFFSSKMTSLAPNENSIFPQNGFNFLSSQRADLTELRKLKIDSNRSAAKKLKLLSGTPAITKKHMQDE
SQ  QDSSENEPIANADSVTNIDRKENRDNNLDNTYLNGKEQSNNLNKQDGENTLQHEKSSSFGYWCSPSPEQLERLSLKQLAA
SQ  VSNFVIGRRGYGCITFQHDVDLTAFTKSFREELFGKIVIFRSSKTVEVYPDEATKPMIGHGLNVPAIITLENVYPVDKKT
SQ  KKPMKDTTKFAEFQVFDRKLRSMREMNYISYNPFGGTWTFKVNHFSIWGLVNEEDAEIDEDDLSKQEDGGEQPLRKVRTL
SQ  AQSKPSDKEVILKTDGTFGTLSGKDDSIVEEKAYEPDLSDADFEGIEASPKLDVSKDWVEQLILAGSSLRSVFATSKEFD
SQ  GPCQNEIDLLFSECNDEIDNAKLIMKERRFTASYTFAKFSTGSMLLTKDIVGKSGVSIKRLPTELQRKFLFDDVYLDKEI
SQ  EKVTIEARKSNPYPQISESSLLFKDALDYMEKTSSDYNLWKLSSILFDPVSYPYKTDNDQVKMALLKKERHCRLTSWIVS
SQ  QIGPEIEEKIRNSSNEIEQIFLYLLLNDVVRASKLAIESKNGHLSVLISYLGSNDPRIRDLAELQLQKWSTGGCSIDKNI
SQ  SKIYKLLSGSPFEGLFSLKELESEFSWLCLLNLTLCYGQIDEYSLESLVQSHLDKFSLPYDDPIGVIFQLYAANENTEKL
SQ  YKEVRQRTNALDVQFCWYLIQTLRFNGTRVFSKETSDEATFAFAAQLEFAQLHGHSLFVSCFLNDDKAAEDTIKRLVMRE
SQ  ITLLRASTNDHILNRLKIPSQLIFNAQALKDRYEGNYLSEVQNLLLGSSYDLAEMAIVTSLGPRLLLSNNPVQNNELKTL
SQ  REILNEFPDSERDKWSVSINVFEVYLKLVLDNVETQETIDSLISGMKIFYDQYKHCREVAACCNVMSQEIVSKILEKNNP
SQ  SIGDSKAKLLELPLGQPEKAYLRGEFAQDLMKCTYKI
//
ID  G0SDP9;
PN  Nucleoporin NUP152;
GN  NUP152;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P32499}. Nucleus membrane {ECO:0000250|UniProtKB:P32499}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32499}; Nucleoplasmic side {ECO:0000250|UniProtKB:P32499}.
DR  UNIPROT: G0SDP9;
DR  UNIPROT: G3EQ77;
DR  Pfam: PF13634;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000250|UniProtKB:P32499}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046907;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P32499};
SQ  MDPPSKKRSIFGGITSLFRSSTAPPEDRKGKSTNSNSVTANAPSLPPPQPESNGASSPFSPAKRASEAQLSVRKIIPKPQ
SQ  GPSSKLSQSVSASEIAHRPAPSTPAPAAATPVPKRRPGDNPHKLAASTSTPALQNLPNPPAPATSSKATSFSGAPSTPRP
SQ  SIFRNSLYARPAPATTYTQRVSSHPLTQSFPPVTPGRPGRAANVDINNRILSNTASTELFPMKIPEPPRHLTGEMLAKEV
SQ  PEDPNRAGSIYADEYLAHLCPPEFDDLQRRQFFCILDLRRLKYAADEVFLKKDWKINILNFAKEYEKSRSLIMLRYGLYE
SQ  FKTVRASEAVKREWKLKHGIPDSDDESGAPAKTNGGGKRKAEEDLEPSSSTFTHTASPNKRARATEAPATNKRKANDELE
SQ  EESQPSKLQKPGSPSPAKTPSATKSVFESIANKTASPQTAPKSSLFSSSTAAKPNGSIFDNAQKTPATSSNIFGHLSDAS
SQ  KDEDNESDTGSEAEAEDETPAKKKKKTTVNGASSSAPSEGGESTQSRSIFDRITRDANGQPVRQLPEGGLFSGESRKRSL
SQ  SPVKELPANNTWNASAGIKFATPGTSSIFGSSNPKPPATTDTIDFAASTTKKPEEAAAPAEAPKEATPTTNLFGAQTKAT
SQ  EEAPKPAATNIFGSTTNPTETSIPAGSLFSAKPATSTTNSLFGATTSAAGQKKDEESKPTEAAPAPAPATSTLFGAKPAT
SQ  TESPKTNLFQFGTPNKTETAPATQPQFGGLFGKPPSTETPTEKPATTSLFGTDASKPATTSSLFGSATTAADKPAATNLF
SQ  GSTTTPADKPTTTNLFGSTSTQATSGSDEPTAKKFAFGGTTESKPTTSLFGSTTPAPATSTENKGGLFGATTTSATPATN
SQ  TKPLFGSTPAPAQENKPLFGSSTTTAAPVFQFGSTPASTSTEQKPLFGATAATDSKPLFGSTSATSTEQKPLFGSSTTMT
SQ  EQKPLFGSISTTATEQKPLFGSTSTTEAKPLFGAAPASTEQKSLFGITPSTTENNPASIFGNSSTSTEQKPLFGSAPAST
SQ  EQKPLFGSTPSTTENKPAGLFGNTSTTSTSTPLFNFGSQNTTASQPSTTGSIFGSASASFTFTAGGSDGTIKNPFASDGS
SQ  YSAPTSFNFGSGDSQSSSAPFTFGAGGGTPSFTFGASSDSSNASNNASSAPIFSFGASQPSSTPLFGQNNPPAASNIFAS
SQ  SLAPVGGTSTGTSKHVPSFLESENKASAYSSLDSPFTFGGASSLATTPAASTPEPSAANAAAAGEDQGASADADEQPQEQ
SQ  ISLTDGGPGEEDESVVHEVRAKAVKLVTAADSSADSSNGSGEKPAEKKSNSPWKVMGVGPLRLLKHKQTGAVRMLLRAEP
SQ  RGNIALNKLVLPQFTYKPDAATPKFIKFAAARDDGKGLETWMIQVKTPQLAQELAAALEEHKKANEKKDGEKNEESEKKD
SQ  EKQEEKKNEEKKDEKEEKKDEKK
//
ID  Q9VXE6;
PN  Nuclear pore complex protein Nup153;
GN  Nup153;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:17682050}. Nucleus membrane {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:18562695}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. Chromosome {ECO:0000269|PubMed:20174442}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18562695}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket (PubMed:17682050). Localized at the spindle in mitotic syncytial embryos (PubMed:18562695). Associates with chromatin (PubMed:20174442). {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:20174442, ECO:0000303|PubMed:17682050}.
DR  UNIPROT: Q9VXE6;
DR  UNIPROT: Q1LZ48;
DR  Pfam: PF00641;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (PubMed:17682050). Functions as a scaffolding element in the nuclear phase of the NPC (PubMed:17682050). Essential for the nuclear import of nuclear localization signal (NLS)-containing proteins in a Importin alpha/Importin beta receptor-dependent manner (PubMed:17682050). Required for nuclear import of Mad (PubMed:20547758). Plays a role in chromosomal organization and gene expression regulation; stimulates transcription by promoting the formation of an open chromatin environment (PubMed:20174442). Binds chromatin to nucleoporin- associated regions (NARs) that define transcriptionally active regions of the genome (PubMed:20174442). Associates with extended chromosomal regions that alternate between domains of high density binding with those of low occupancy (PubMed:20174442). Preferentially binds to NARs of the male X chromosome (PubMed:20174442). In males, together with Mtor, required for the localization of the male-specific lethal (MSL) histone acetyltransferase complex to the X chromosome and therefore for the transcription of dosage compensation genes (PubMed:16543150). May play a role in double strand break DNA repair (PubMed:26502056). {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:26502056}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: P40798; IntAct: EBI-270193; Score: 0.00
DE  Interaction: Q9VPG5; IntAct: EBI-273901; Score: 0.00
DE  Interaction: Q9VVQ1; IntAct: EBI-273906; Score: 0.00
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: Q9VH81; IntAct: EBI-9922589; Score: 0.35
DE  Interaction: P07207; IntAct: EBI-9924105; Score: 0.46
DE  Interaction: P18431; IntAct: EBI-9925534; Score: 0.35
DE  Interaction: Q9VJ30; IntAct: EBI-9932245; Score: 0.35
DE  Interaction: Q9W258; IntAct: EBI-9932835; Score: 0.35
DE  Interaction: M9NFI9; IntAct: EBI-9933573; Score: 0.46
DE  Interaction: Q9GQR5; IntAct: EBI-9935575; Score: 0.35
DE  Interaction: Q9VXY7; IntAct: EBI-9936142; Score: 0.35
DE  Interaction: Q9VDW6; IntAct: EBI-9940412; Score: 0.35
GO  GO:0005737;
GO  GO:0000791;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0031490;
GO  GO:0046872;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0006974;
GO  GO:0006325;
GO  GO:0006338;
GO  GO:0007549;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0045944;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDAQEQRESSQAELAKKHPLTPLKELPEESEEEEEEEDESSAGALRESDSNNSIMGKMKMRVSSILPASLSGWFSPSSK
SQ  DGNDALSSPANLRQSQPRQSNGRLTTKRKRGRRRIMLAEVDADAADDLDDGSDAKGLNYEEVALADNIAEHDLAAEDEQT
SQ  RRSEYNVFLLRKRAGAVAAAGGDEDEAEEDELEEDDEDGDEEDDDEEQENLQQSAAVQTKRRRLELETPVNLPNMRRLPL
SQ  LSSTPAAPLAAATSSSSSQMYKGVSHIAPHRRNHLNLYGSQRQREPAYNFFTGNEAAEGSTGDLPHSIRRSLNIPFGGSS
SQ  TATSYNNSLSSLPNHKRPSLIGKQTHRRDLTMDETGTGPAMSSEEHLNHLLRISRTNNNTSNNNNNNNNNNNVIETKTRR
SQ  SELSAAAGGCGDSQSESDMNEYHDNGEGHDGLRPSHYNSNSNLEFYGNLQSSKSIFNRSNTAAQQSHRNSTWSLNSLTQR
SQ  RRFNASIYGSTSALSDSRLLSGSASNSGSASASSSPFYQGRTTFGGNSGNNRLFSRSNLSSSAASSMLGLNSAGSSPAHQ
SQ  LHASMTGGIGYGMKAVDMRPSDSGSLAETSVGQGGSKKPGTGLSNTTMRILNLLESYSTPLIDAKRMGSSIKEHQSSRQQ
SQ  RQGTPATPYLRSTSASRNVSVPNHINELAELRSNKLLVPTMQQLLERRRLHRVTQNSRDVVHSQNVRAGGENNQEKPKPT
SQ  APYVAPIDQSANHTQHTNKMRSRLSHQTRNKETRTAEEEAPPPLDLPQISFPDMASAPKFDLIIKPTVPVVSKPSTTDPI
SQ  QSSKSSNTNLSTTNSKQMPNFLANPQPAAPIVNFAANGNVSAISKPSKRTFTFSEPTPLSNFQENCIPKPKINRKYTFSA
SQ  PAPLDDLRITNKQSQPTINGTPSSKEWECDTCMVRNKPEINKCVACETAKPVASAAPVQAPLPPSTAAIDTQSFVGFGDR
SQ  FKKSTTAWECDACMLSNKAEASKCIACETPRKTVAPKVNNFSPLITNAKSNEWECSVCLVRNKVEVSKCVACESAKPGAT
SQ  MALPATSNIAVATPSIITDGFGDRFKKSATAWECDACMLSNKAEASKCIACETPRKSSTPIANSSYPSINNNLPAGSGFD
SQ  ISFTRKANMWECQTCLVMNKSSDEECIACQTPNSQARNSNSESALISSISSSSASFSGSLSRPSSRSSSGSTSTCGSVCS
SQ  GSIVSISSTTESAKALSAKKVPPKPDAGFQQLVAAQKTSTWECEACLAKNDMSRKTCICCEQMMPEAFNPAATTANSAAS
SQ  SVPKFRFGFSHVKEVVKPSVETTTTPAPTSAQFSFGFGQSNQGKDVADSKKTEAPKTFMFGVSKVEEPKTVSFGTGIKET
SQ  TATSSTEATAPTPAAAAPAPVQFVFKAPTTATTASSLTTTISTTSNAPALGGFSFGAPSSSSTVSSSTTSTSANPAAVKP
SQ  MFSWSGAGSAVSSTSSSQQPVAKAPTLGFGVSSSTVTTTTTSTKVFAFTPASGLDPAAATSAPAAGAGFSFGSQSKPATT
SQ  QNTGTFFFGQPTAVAPATPTNPSVSSIFGAPATSTTASTSVSATTSTSTANAIASSFAPTSTPQLFGNWGEKKTDLTTFG
SQ  ASSGSGTTTTPSFGWSSNGDAAKSNSAAVGSAAVPSSSASTMATPIFGSSSMFGPSSSSNNTTSTSTTSLPFGSAATTAA
SQ  TTPAGGNAALTGLFGNVGNSLAGVGAPVATTPAATAAAPLTNIFGNPTPVAAAAPVFGSGSTIPSAGFGAPAAAAPLAAP
SQ  ALPGAFNFGGATAATPAASSAPFVFGSSTNEPLAKPSFNFTGSAASSTAPAPAFNFTANTAATNNPSGGDSTPNANALFQ
SQ  FSATSTAPANIFAFNPPAAGNSAQSSQTARRKIRAPVRRLPPR
//
ID  P49790;
PN  Nuclear pore complex protein Nup153;
GN  NUP153;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus. Nucleus membrane. Nucleus, nuclear pore complex. Note=Tightly associated with the nuclear membrane and lamina (By similarity). Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Dissociates from the NPC structure early during prophase of mitosis. Integrated in the newly assembled nuclear envelope of postmitotic cells early in G1. Colocalized with NUP98 and TPR to the nuclear basket at the nucleoplasmic side of the NPC. Detected in diffuse and discrete intranuclear foci. Remained localized to the nuclear membrane after poliovirus (PV) infection. {ECO:0000250}.
DR  UNIPROT: P49790;
DR  UNIPROT: B4DIK2;
DR  UNIPROT: E7EPX5;
DR  UNIPROT: F6QR24;
DR  UNIPROT: Q4LE47;
DR  UNIPROT: Q5T9I7;
DR  UNIPROT: Q7Z743;
DR  PDB: 2EBQ;
DR  PDB: 2EBR;
DR  PDB: 2EBV;
DR  PDB: 2GQE;
DR  PDB: 4U0C;
DR  PDB: 4U0D;
DR  PDB: 5TSV;
DR  PDB: 5TSX;
DR  PDB: 6AYA;
DR  Pfam: PF08604;
DR  Pfam: PF10599;
DR  Pfam: PF00641;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DR  OMIM: 603948;
DR  DisGeNET: 9972;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:22253824}. (Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro). {ECO:0000269|PubMed:23523133, ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:29997211}. (Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro). {ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:31913756}.
DE  Reference Proteome: Yes;
DE  Interaction: A8CG34; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: O15504; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-8034338; Score: 0.45
DE  Interaction: P12270; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P35658; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P46060; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-7193245; Score: 0.76
DE  Interaction: P29323; IntAct: EBI-7234474; Score: 0.54
DE  Interaction: Q16539; IntAct: EBI-7234526; Score: 0.54
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-7329388; Score: 0.53
DE  Interaction: Q8IY92; IntAct: EBI-2371263; Score: 0.35
DE  Interaction: P51784; IntAct: EBI-2511298; Score: 0.40
DE  Interaction: Q9Y2K6; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q9QWT9; IntAct: EBI-2558911; Score: 0.40
DE  Interaction: E9PVX6; IntAct: EBI-2561030; Score: 0.40
DE  Interaction: A0A6L7HHZ0; IntAct: EBI-2815987; Score: 0.00
DE  Interaction: A0A6L8PGJ0; IntAct: EBI-2816005; Score: 0.00
DE  Interaction: Q9ZC54; IntAct: EBI-2846253; Score: 0.00
DE  Interaction: P03372; IntAct: EBI-2878124; Score: 0.35
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-3437314; Score: 0.00
DE  Interaction: Q05322; IntAct: EBI-6159823; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6515052; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-8232524; Score: 0.60
DE  Interaction: Q8WUF5; IntAct: EBI-9688209; Score: 0.35
DE  Interaction: Q13625; IntAct: EBI-9688225; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-9688194; Score: 0.64
DE  Interaction: P03367; IntAct: EBI-9872771; Score: 0.40
DE  Interaction: O14862; IntAct: EBI-9995694; Score: 0.35
DE  Interaction: P06428; IntAct: EBI-11722493; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: P18754; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q92973; IntAct: EBI-11076796; Score: 0.53
DE  Interaction: O00629; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q8TEM1; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9H9A5; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q53GS7; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P78406; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q8IXQ5; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9NXE4; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: J3KMX2; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P52292; IntAct: EBI-11076796; Score: 0.53
DE  Interaction: P63165; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q69YH5; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P61956; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q96HA1; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9UKX7; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P33991; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P62136; IntAct: EBI-11076796; Score: 0.53
DE  Interaction: O14715; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: O00505; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9BW27; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q03188; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q8NFH4; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q969G3; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: O60684; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: O95373; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q86XI6; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9BTX1; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9HC62; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q96SK2; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P52294; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q8TAQ2; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11076796; Score: 0.77
DE  Interaction: Q92621; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9P0U3; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q12769; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9BW19; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: E9PF10; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q6NUQ4; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: Q9GZY0; IntAct: EBI-21528397; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-21564320; Score: 0.35
DE  Interaction: Q9BXS6; IntAct: EBI-21691494; Score: 0.35
DE  Interaction: Q8N9Q2; IntAct: EBI-21723640; Score: 0.35
DE  Interaction: Q2NL82; IntAct: EBI-21815364; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-21866171; Score: 0.35
DE  Interaction: P70168; IntAct: EBI-15732587; Score: 0.52
DE  Interaction: P35408; IntAct: EBI-20811254; Score: 0.37
DE  Interaction: Q9UPY3; IntAct: EBI-20621330; Score: 0.50
DE  Interaction: O96013; IntAct: EBI-26962273; Score: 0.35
DE  Interaction: Q8WVM7; IntAct: EBI-24811291; Score: 0.35
DE  Interaction: Q8N3U4; IntAct: EBI-24811308; Score: 0.35
DE  Interaction: Q8WUY9; IntAct: EBI-25411615; Score: 0.35
DE  Interaction: A0A0H3LH51; IntAct: EBI-25401350; Score: 0.35
DE  Interaction: Q7RTV0; IntAct: EBI-25482472; Score: 0.35
DE  Interaction: P83105; IntAct: EBI-25745135; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-26396507; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-26397631; Score: 0.35
DE  Interaction: K9N643; IntAct: EBI-26375164; Score: 0.35
DE  Interaction: Q16566; IntAct: EBI-28941485; Score: 0.35
DE  Interaction: Q05D32; IntAct: EBI-27113232; Score: 0.35
DE  Interaction: O15297; IntAct: EBI-27113880; Score: 0.35
DE  Interaction: Q9H9E1; IntAct: EBI-30814700; Score: 0.44
DE  Interaction: Q93009; IntAct: EBI-30841851; Score: 0.44
DE  Interaction: P23771; IntAct: EBI-34580747; Score: 0.35
GO  GO:0005829;
GO  GO:0043657;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0003677;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0008139;
GO  GO:0043495;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0046832;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0006405;
GO  GO:0046718;
GO  GO:0075732;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASGAGGVGGGGGGKIRTRRCHQGPIKPYQQGRQQHQGILSRVTESVKNIVPGWLQRYFNKNEDVCSCSTDTSEVPRWPE
SQ  NKEDHLVYADEESSNITDGRITPEPAVSNTEEPSTTSTASNYPDVLTRPSLHRSHLNFSMLESPALHCQPSTSSAFPIGS
SQ  SGFSLVKEIKDSTSQHDDDNISTTSGFSSRASDKDITVSKNTSLPPLWSPEAERSHSLSQHTATSSKKPAFNLSAFGTLS
SQ  PSLGNSSILKTSQLGDSPFYPGKTTYGGAAAAVRQSKLRNTPYQAPVRRQMKAKQLSAQSYGVTSSTARRILQSLEKMSS
SQ  PLADAKRIPSIVSSPLNSPLDRSGIDITDFQAKREKVDSQYPPVQRLMTPKPVSIATNRSVYFKPSLTPSGEFRKTNQRI
SQ  DNKCSTGYEKNMTPGQNREQRESGFSYPNFSLPAANGLSSGVGGGGGKMRRERTRFVASKPLEEEEMEVPVLPKISLPIT
SQ  SSSLPTFNFSSPEITTSSPSPINSSQALTNKVQMTSPSSTGSPMFKFSSPIVKSTEANVLPPSSIGFTFSVPVAKTAELS
SQ  GSSSTLEPIISSSAHHVTTVNSTNCKKTPPEDCEGPFRPAEILKEGSVLDILKSPGFASPKIDSVAAQPTATSPVVYTRP
SQ  AISSFSSSGIGFGESLKAGSSWQCDTCLLQNKVTDNKCIACQAAKLSPRDTAKQTGIETPNKSGKTTLSASGTGFGDKFK
SQ  PVIGTWDCDTCLVQNKPEAIKCVACETPKPGTCVKRALTLTVVSESAETMTASSSSCTVTTGTLGFGDKFKRPIGSWECS
SQ  VCCVSNNAEDNKCVSCMSEKPGSSVPASSSSTVPVSLPSGGSLGLEKFKKPEGSWDCELCLVQNKADSTKCLACESAKPG
SQ  TKSGFKGFDTSSSSSNSAASSSFKFGVSSSSSGPSQTLTSTGNFKFGDQGGFKIGVSSDSGSINPMSEGFKFSKPIGDFK
SQ  FGVSSESKPEEVKKDSKNDNFKFGLSSGLSNPVSLTPFQFGVSNLGQEEKKEELPKSSSAGFSFGTGVINSTPAPANTIV
SQ  TSENKSSFNLGTIETKSASVAPFTCKTSEAKKEEMPATKGGFSFGNVEPASLPSASVFVLGRTEEKQQEPVTSTSLVFGK
SQ  KADNEEPKCQPVFSFGNSEQTKDENSSKSTFSFSMTKPSEKESEQPAKATFAFGAQTSTTADQGAAKPVFSFLNNSSSSS
SQ  STPATSAGGGIFGSSTSSSNPPVATFVFGQSSNPVSSSAFGNTAESSTSQSLLFSQDSKLATTSSTGTAVTPFVFGPGAS
SQ  SNNTTTSGFGFGATTTSSSAGSSFVFGTGPSAPSASPAFGANQTPTFGQSQGASQPNPPGFGSISSSTALFPTGSQPAPP
SQ  TFGTVSSSSQPPVFGQQPSQSAFGSGTTPNSSSAFQFGSSTTNFNFTNNSPSGVFTFGANSSTPAASAQPSGSGGFPFNQ
SQ  SPAAFTVGSNGKNVFSSSGTSFSGRKIKTAVRRRK
//
ID  P49791;
PN  Nuclear pore complex protein Nup153;
GN  Nup153;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus. Nucleus membrane. Nucleus, nuclear pore complex. Note=Dissociates from the NPC structure early during prophase of mitosis. Integrated in the newly assembled nuclear envelope of postmitotic cells early in G1 (By similarity). Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Tightly associated with the nuclear membrane and lamina. Colocalized with NUP98 and TPR to the nuclear basket at the nucleoplasmic side of the NPC. Detected in diffuse and discrete intranuclear foci. {ECO:0000250}.
DR  UNIPROT: P49791;
DR  PDB: 2K0C;
DR  PDB: 3CH5;
DR  PDB: 3GJ3;
DR  PDB: 3GJ4;
DR  PDB: 3GJ5;
DR  PDB: 3GJ6;
DR  PDB: 3GJ7;
DR  PDB: 3GJ8;
DR  Pfam: PF08604;
DR  Pfam: PF10599;
DR  Pfam: PF00641;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC (By similarity). The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q53FT3; IntAct: EBI-6140559; Score: 0.44
DE  Interaction: P62826; IntAct: EBI-15714795; Score: 0.67
DE  Interaction: P08922; IntAct: EBI-22248889; Score: 0.35
DE  Interaction: P35968; IntAct: EBI-22252650; Score: 0.35
GO  GO:0005642;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:1990875;
GO  GO:0032991;
GO  GO:0003682;
GO  GO:0003690;
GO  GO:0042802;
GO  GO:0008139;
GO  GO:0043495;
GO  GO:0031267;
GO  GO:0017056;
GO  GO:0008270;
GO  GO:0000278;
GO  GO:0051028;
GO  GO:0046832;
GO  GO:0051292;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASGAGGIGGGGGGGKIRTRRCHQGPVKPYQQGRPQHQGILSRVTESVKNIVPGWLQRYFNKSENACSCSVNADEVPRWP
SQ  ENREDEREIYVDENTNTDDGRTTPEPTGSNTEEPSTTSTASNYPDVLTRPSLHRSHLNFSVLESPALHCQPSTSSAFPIG
SQ  SSGFSLVKEIKDSTSQHDDDNISTTSGFSSRASEKDIAVSKNTSLPPLWSPEAERSHSLSQHTAISSKKPAFNLSAFGTL
SQ  STSLGNSSILKTSQLGDSPFYPGKTTYGGAAAAVRQNKVRSTPYQAPVRRQMKAKQLNAQSYGVTSSTARRILQSLEKMS
SQ  SPLADAKRIPSAVSSPLNSPLDRSGIDSTVFQAKKEKVDSQYPPVQRLMTPKPVSIATNRTVYFKPSLTPSGDLRKTNQR
SQ  IDKKNSTVDEKNISRQNREQESGFSYPNFSIPAANGLSSGVGGGGGKMRRERTTHFVASKPSEEEEVEVPLLPQISLPIS
SQ  SSSLPTFNFSSPAISAASSSSVSPSQPLSNKVQMTSLGSTGNPVFTFSSPIVKSTQADVLPPASIGFTFSVPLAKTELSG
SQ  PNSSSETVLSSSVTAQDNTVVNSSSSKKRSAPCEDPFTPAKILREGSVLDILKTPGFMSPKVDSPALQPTTTSSIVYTRP
SQ  AISTFSSSGVEFGESLKAGSSWQCDTCLLQNKVTDNKCIACQAAKLPLKETAKQTGIGTPSKSDKPASTSGTGFGDKFKP
SQ  AIGTWDCDTCLVQNKPEAVKCVACETPKPGTGVKRALPLTVASESPVTASSSTTVTTGTLGFGDKFKRPVGSWECPVCCV
SQ  SNKAEDSRCVSCTSEKPGLVSASSSNSVPVSLPSGGCLGLDKFKKPEGSWDCEVCLVQNKADSTKCIACESAKPGTKSEF
SQ  KGFGTSSSLNPAPSAFKFGIPSSSSGLSQTFTSTGNFKFGDQGGFKLGTSSDSGSTNTMNTNFKFPKPTGDFKFGVLPDS
SQ  KPEEIKNDSKNDNFQFGPSSGLSNPASSAPFQFGVSTLGQQEKKEELPQSSSAGFSFGAGVANPSSAAIDTTVTSENKSG
SQ  FNFGTIDTKSVSVTPFTYKTTEAKKEDASATKGGFTFGKVDSAALSSPSMFVLGRTEEKQQEPVTSTSLVFGKKADNEEP
SQ  KCQPVFSFGNSEQTKDESSSKPTFSFSVAKPSVKESDQLAKATFAFGNQTNTTTDQGAAKPAFSFLNSSSSSSSTPATSS
SQ  SASIFGSSTSSSSPPVAAFVFGQASNPVSSSAFGNSAESSTSQPLLFPQDGKPATTSSTASAAPPFVFGTGASSNSTVSS
SQ  GFTFGATTTSSSSGSFFVFGTGHSAPSASPAFGANQTPTFGQSQGASQPNPPSFGSISSSTALFSAGSQPVPPPTFGTVS
SQ  SSSQPPVFGQQPSQSAFGSGTANASSVFQFGSSTTNFNFTNNNPSGVFTFGASPSTPAAAAQPSGSGGFSFSQSPASFTV
SQ  GSNGKNMFSSSGTSVSGRKIKTAVRRKK
//
ID  Q640Z6;
PN  Nuclear pore complex protein Nup153;
GN  nup153;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:9531546}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:9531546}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Colocalizes with tpr at the nuclear pore complex.
DR  UNIPROT: Q640Z6;
DR  Pfam: PF08604;
DR  Pfam: PF00641;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. May be involved in the retention of unspliced mRNAs in the nucleus. Probably mediates tpr anchoring to the nuclear membrane at NPC. Possible DNA- binding subunit of the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0003677;
GO  GO:0046872;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAGGGGPGGPGTGGKIRSRRYHLSSGRTPYSKSRQQQQGIISRVTDTVKSIVPGWLQKYFNKQEEEHDRVHSASEVIV
SQ  NDTEARENNAEHHIYVVDDDDDEEGNSPTDGRVTPEPIINVDEEVPSTSQSAINNTDALTRPSLHRASLNFNIFDSPALN
SQ  CQPSTSSAFPIGTSGFSLIKEIKDSTSQHDDDNISTTSGFSSRASDKDLAVSKNVSVPPLWSPEVDRSQSLSHNSSMTSK
SQ  KPTFNLSAFGSLSPSLGNASILNRQLGDSPFYPGKTTYQGAAAVRSSRVRATPYQAPLRRQVKAKPAAHSQQCGVTSSAA
SQ  RRILQSLEKMSSPLADAKRIPSNSSLSHTPEKNVMDIPENPSKRKKVESPFPPVQRLVTPKSISVSANRSLYIKPSLTPS
SQ  AVSNTNSRRIQPDKHNESRKNNLQTTSQSHSFSYPKFSTPASNGLSSGTGGGKMMREKGSHYSTKPANEELDGPVLPEIP
SQ  LPLSTAALPSFQFSTLSGSATSPISVTKPANSTTCRLTSSSPSFTFSSPIVKSTESNAQSPGSSVDFTFSVPAAKASSAT
SQ  SDESKVSAVSRAAKTHAAVSSAKNTDDEQLGFCKPAKTLKEGSVLDMLRSPGFSSSPSLLTSASSLNRSTPTLSKTVGNT
SQ  FSPANVSLGVGSKQAFGLWQCSACFHENMSSDSNCISCSALKPRPTETSKKLPASPPSSNTKSTVPLSSTPGLGDIFKKP
SQ  AGMWDCDTCLVQNKAEVTKCVACETPKPGTGMKATLLIPSTTKSTNPATNTLAFASCSASIPNEEMFKKPMGSWECTVCH
SQ  MQNKTEDNTCVGCKAEKPGTVKSVPTAAPSGLLGLLDQFKKPTGSWDCDVCLIQNKPEANKCIACESAKPGTKAELKGTF
SQ  DTVKNSVSVAPLSSGQLGLLDQFKKSAGSWDCDVCLVENKPEATKCVACETSKPGTKAELKGFGTSTFSSGTAAPTFKFG
SQ  VQSSDSTAELKSGASTSGFAKSIGNFKFGLASASTTTEETGKKSFTFGSSTTNEVSAGFKFGIAGSAQTKPDTLSQSTTS
SQ  GFTFGSVSNTVSLAPTATSSGSTGLQVAAVIADSNLATTATLKSAEEKKAEAPTITPFSFGKTDQNKETASTSFVFGKKD
SQ  EKTDSAPTGSSFAFGLKKDGEESKQFLFGKPEPTKVDGSAASAGFAFGVTNPTEKKDIEQPGKSVFAFGAQTSITDAGAS
SQ  KQPFSFLTNVSSTAASSSTCGVSSSVFGSVTQSSTPATPSNVFGSAISANAPAPSSGVFGNLTPSNAPAASSTLFGNVAP
SQ  SSTPSGSSGLFGTAAASSTPATSTSLFGSAAKLSAPASSGGVFNSAAPAAPASTASSVFGSVASSTNTSANSANIFGSSG
SQ  GAATAPGAFVFGQPASTASTVFGNSSESKSTFVFSGQENKPVTSASTSVTPFLFGAVSASTTPAAPGFNFGRTITSNTTG
SQ  TSSSPFIFGAGASGSASSSITAQANPVPAFGQSSNPSTAPAFGSSTSVPVFPAGNSQQVPAFGSSSAQPPVFGQQATQPS
SQ  FGSPAAPSAGSGFPFGNNANFNFNSTNSSGGVFTFNANSGSTTQPPPPGYMFNAAAPGFNMGTNGRTTPASTISTRKIKT
SQ  ARRRK
//
ID  Q9V463;
PN  Nuclear pore complex protein Nup154;
GN  Nup154;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17410542}. Chromosome {ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:9732281}. Nucleus {ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:9732281}. Nucleus membrane {ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:9732281}; Peripheral membrane protein {ECO:0000269|PubMed:17410542}; Cytoplasmic side {ECO:0000269|PubMed:17410542}. Nucleus membrane {ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:9732281}; Peripheral membrane protein {ECO:0000269|PubMed:17410542}; Nucleoplasmic side {ECO:0000269|PubMed:17410542}. Cytoplasm {ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:22718353}. Note=Increased localization to chromatin before interphase (PubMed:22718353). Distributed along filamentous structures that extend radially on the nuclear side of the pore complex (PubMed:17410542). {ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:22718353}.
DR  UNIPROT: Q9V463;
DR  UNIPROT: O62536;
DR  UNIPROT: O62610;
DR  UNIPROT: O62613;
DR  UNIPROT: Q9VKL5;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Component of the nuclear pore complex (PubMed:17410542). Has a role in the organization of the inner nuclear membrane proteins at the nuclear envelope (PubMed:22718353). In germ cells, plays a role in the nuclear localization of components of the dpp signaling pathways, such as Medea and phosphorylated Mad (PubMed:21696798). Binds to chromatin, and together with Nup62 and Nup93-1, contributes to karyosome morphology and chromatin organization including attachment to the nuclear envelope in oocytes and nurse cells (PubMed:22718353, PubMed:26341556). Has a role in female fertility including egg chamber development; in nurse cells, has a role in the organization of F-actin in subcortical and cytoplasmic actin filaments important for the transfer of cytoplasm from nurse cells to the growing oocytes (PubMed:9732281, PubMed:10511559, PubMed:17410542, PubMed:17277377). Has a role in male spermatogenesis and fertility (PubMed:9732281, PubMed:10511559). Has a role in germ line cell proliferation (PubMed:21696798). {ECO:0000269|PubMed:10511559, ECO:0000269|PubMed:17277377, ECO:0000269|PubMed:17410542, ECO:0000269|PubMed:21696798, ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:26341556, ECO:0000269|PubMed:9732281, ECO:0000303|PubMed:17410542}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VTU4; IntAct: EBI-274219; Score: 0.00
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: P18431; IntAct: EBI-9925534; Score: 0.35
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0005634;
GO  GO:0003682;
GO  GO:0017056;
GO  GO:0007015;
GO  GO:0055050;
GO  GO:0007303;
GO  GO:0001654;
GO  GO:0007281;
GO  GO:0007295;
GO  GO:0007140;
GO  GO:0051028;
GO  GO:0001555;
GO  GO:0030715;
GO  GO:0030717;
GO  GO:0048477;
GO  GO:1905938;
GO  GO:0042307;
GO  GO:1900182;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0045477;
GO  GO:1905879;
GO  GO:1905475;
GO  GO:0006405;
GO  GO:0007283;
GO  GO:0000972;
GO  GO:0035220;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17410542};
SQ  MTLPQAQLDFFTTATSMLEWHYNLERNKPGLLELTGVSQHGRATMSGLNDYDYQSLSFLKSDRTHNLQQMRTVTKSAIPN
SQ  EILEHFKHIKCHCTMGLFPEIGRAWLTIDSEIYIWTFNQTRDVAYYDGLSHLIVSVGLVKPKPGVFVQDVKYLLVLTTPI
SQ  EVIVLGVTFGESSYNEMQLMNRPVFVIGTDNVSISVIKGTDDGRIFLGGRDGCLYEIYYQAESSWFGKRCKKINLSQGLV
SQ  SYMVPSFLKVFSEVDPIEHIEIDNSRKLLYVLTEKGVIEAWDISTSYTTARRLGRITQNDITNQAVSLITTVDPSIFKSV
SQ  KAICPLSADDADKLHLVAVTQCGVRLFFSTTSLNVKQQFGPAVPCSPGENTGFGQPAVQPPLSPNAEAPKGLYLLHVRLP
SQ  PGYTPNATTNKPKQVHAAHYTEGTMLMITTQQHEQDLLWSLSSAPSVNFTYLVESTALESLDGVVWGLAEVHEPSTPQRK
SQ  SPLNSARHARKVALLTNQGTHIIEVLKMVDVLRQILLSCNGPHHEEVKMFFQSQNQREACVTALLLATSDTYRGSDVALW
SQ  AAQAFMLYGGEPCYQHQKFLNASNRNMANQTLGPNTTNVRERQSMFMSTPMPNSVANSPVGFPGSQFNQPISPIGNMQPP
SQ  QVAVSNENSPIVFSAKHDGLYMYVSRMLHSVWQMRCVNEQFCSNLSQSECALLLSDLRSLRSFLEVHSVHDISSTTRVSF
SQ  DNHLDRTNSYNTIMMGNTLLPIPEQRVLSEQAQVEETRSLSALNLFVKHACEVISLWNILNSHSFQLICVQLSPEHQKLL
SQ  TCSTFRDLLITRSEVCAFLIISLINLYLKDAAGVSEVSKNLRENCPNLYRHEDDVTYKATELLMNAKNCTSATEKEHMLR
SQ  TTLHMCKEAAPTLPLHSICMQFISADFFEGVIELSAVCASKSDPEEVGVHFYNNGEPADDREGYTCFATRMAYYKEVQLM
SQ  LDHIYQRVCNKTHVQDKSINPLKGTAKASDAKNGATQTIPKIVAHTLKVKDPLIHITLYEWLLAHDMLKELLDVVEPSLG
SQ  EFLRRSVSQNVDNVVLIDLLWKYYEKNSHHSQAAHILDNLAMTRSENINLEQRIEYLVRAVMCMRNGNVGSSLSNGIFLK
SQ  ELEDKLDIARVQKSVLAAMTELASDKLEAATAVKELNYALYDITQLYQHFAEPFDLWECQLSILNCSHHNDPLLIESVWG
SQ  QIINSVVDKPGTTSERCNRLFTKIEILVREYGESGVCFPFAFLIRELEVKACQLRFPEGIVPEKLVSMNLDIELLLEYYS
SQ  RMISMNERVWANEGNEWHLIQSVIRVVSLLADNAQSIWYRSKRRIVGKAQDIVAGCLNICYQKPDTNRLQHSLKELQSQL
SQ  QRLLI
//
ID  F4HXV6;
PN  Nuclear pore complex protein NUP155;
GN  NUP155;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4HXV6;
DR  UNIPROT: Q9LQU6;
DR  Pfam: PF08801;
DE  Function: Major component of the nuclear pore complex (NPC). {ECO:0000305|PubMed:12034489}.
DE  Reference Proteome: Yes;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0005730;
GO  GO:0005886;
GO  GO:0009506;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQDDEIVMRDVTSAGICIGDRIGREAASQLDLEEALEASRYASHPYSTHPREWPPLIEVGETWELPSVLIERYNTAGGE
SQ  GTALCGIFPEIRRAWASVDNSLFLWRFDKRDGQCPEYSGEEQAICAVGLAKCRPGVFVEAIQYLLVLATPVELVLVGVCC
SQ  TEGPDGRDPYAEISVQPLPDYTISSDGVTMTCVTCTNKGRIFMAGRDGHIYELLYTTGSGWNKRCRKVCLTAGVGSMISR
SQ  WVVPNVFKFGAVDPVVEMVVDNERQILYARTEEMKLQAYVSGPNGEGPLKKVAEERNLLNQKDLSQGNRQSAVAGRSNKP
SQ  SIVSISPLSMLESKWLHLVAALSDGRRMYLSTSSSGSGSTISFSGFNNHRQTPNCLKVVSTRPSPPLGVGVGLGFGAASV
SQ  AGRTQNDDLSMKIETAYYSVGTLVLSDSSPPAMSSLLVVSRDSSVHSQAGSSSGPSSRSSRALREVVSSLPIEGRMLFVA
SQ  DVLPSPDTAATIQSLYSELEYCGVEVSGESYEKACGKLWARSDLSTQHILPRRKIVVFTTMGMMELVFNRPVDILRRLLE
SQ  SNSPRSLLEDFFTRFGVGEAAAMCLMLAARIINFEDLISNIVADKAAEAFEDPRIVGMPQFDGSSGLSNTRTATGGFSMG
SQ  QVVQEAEPIFSGAHEGLCLCTSRLLFPLWELPVMSKKTSSDTMSEDGVVICRLSTSAMHVLESKIRSLEKFLRSRRNQRR
SQ  GLYGCVAGLGDVTGSILYGTGSELGATERNMVRNLFGAYSNGGESANKRQRLPYSPAELAATEVRAMECIRQLLLRSAEA
SQ  LFLLQLLSQHHVARLVQELDANLKQALVQLTFHQLVCSEEGDQIATRLISAVMEYYTGSDGRGTVDDISPRLREGCPSYF
SQ  KESDYKFYLAVERLERAALTSDAEEKENVAREAFSFLSKVPGSADLQTVCKRFEDLRFYEAVVCLPLQKAQALDPAGDAF
SQ  NDQLDASIREHALAQRKQCYEIIANALRSLASPLASPTLDEASRSQYICQIVHLGVQSTDRAFREYLYKAMIELHLENEL
SQ  LEYGGPDLVPFLQNAGSHSESQVGAVSTGSSPLGHSGTQISSDQAKYFDLLAKYYVSKRQHVLAAHVFLRLAERRAISLG
SQ  DSPTLERRRDDLSQAVLQAKNASNSDGLVGSAQGVSDSGLLDLLEGKLAVLQFQIKIRDKLEAIASNFESSVAMQDSDQN
SQ  GQVLDGDSSDDTNLANAANEMAMEVSSELKSVTQLYNEYAVPFELWEICLEMLYFANYSGDADSSIIRETWARLIDQALS
SQ  QGGIREACAVLKRVGSHIYPGDGVVLPLDVLCLHLERAALERSERIENVRDEDIAKALLAACKGAAEPVLNAYDRLLSNA
SQ  AVVPSPNLRIRLLRSVLVVLREWAMSVLSDRMGSSPTRSSLILGGSFALENKAALNQGARDKIANAANRYMTEVRRLALP
SQ  PNKTDGVYAGFKELDESLLSPFSF
//
ID  O75694;
PN  Nuclear pore complex protein Nup155;
GN  NUP155;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Cytoplasmic side {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Nucleoplasmic side {ECO:0000250|UniProtKB:P37199}. Note=In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis. {ECO:0000250|UniProtKB:P37199}.
DR  UNIPROT: O75694;
DR  UNIPROT: Q9UBE9;
DR  UNIPROT: Q9UFL5;
DR  PDB: 5A9Q;
DR  PDB: 5IJN;
DR  PDB: 5IJO;
DR  PDB: 7PER;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DR  OMIM: 606694;
DR  OMIM: 615770;
DR  DisGeNET: 9631;
DE  Function: Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. {ECO:0000250|UniProtKB:Q99P88}.
DE  Disease: Atrial fibrillation, familial, 15 (ATFB15) [MIM:615770]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:19070573}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95405; IntAct: EBI-7255490; Score: 0.37
DE  Interaction: P40337; IntAct: EBI-1062521; Score: 0.00
DE  Interaction: P11802; IntAct: EBI-1065754; Score: 0.00
DE  Interaction: P19532; IntAct: EBI-1070952; Score: 0.00
DE  Interaction: P23508; IntAct: EBI-1072074; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-1075999; Score: 0.00
DE  Interaction: P11171; IntAct: EBI-1078988; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1085884; Score: 0.00
DE  Interaction: Q8IY92; IntAct: EBI-2371120; Score: 0.35
DE  Interaction: Q6GQQ9; IntAct: EBI-2510717; Score: 0.40
DE  Interaction: Q09019; IntAct: EBI-2515767; Score: 0.40
DE  Interaction: Q99P88; IntAct: EBI-2558136; Score: 0.40
DE  Interaction: A0A2U2H2G3; IntAct: EBI-2862410; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.55
DE  Interaction: Q5EWX9; IntAct: EBI-8070469; Score: 0.35
DE  Interaction: Q8WVZ9; IntAct: EBI-3232144; Score: 0.35
DE  Interaction: O95758; IntAct: EBI-7850130; Score: 0.35
DE  Interaction: P98078; IntAct: EBI-6100356; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q15843; IntAct: EBI-21328206; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q53GS7; IntAct: EBI-8873568; Score: 0.37
DE  Interaction: Q8WYP5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: O43281; IntAct: EBI-10189017; Score: 0.56
DE  Interaction: Q15637; IntAct: EBI-11299723; Score: 0.00
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q68CZ1; IntAct: EBI-11363154; Score: 0.35
DE  Interaction: Q86VQ0; IntAct: EBI-11363336; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q66GS9; IntAct: EBI-11386281; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11389870; Score: 0.27
DE  Interaction: Q8IVT5; IntAct: EBI-14035520; Score: 0.35
DE  Interaction: P43353; IntAct: EBI-21500028; Score: 0.35
DE  Interaction: P09067; IntAct: EBI-21543288; Score: 0.35
DE  Interaction: Q9H813; IntAct: EBI-21593240; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.67
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q8IY21; IntAct: EBI-21259607; Score: 0.35
DE  Interaction: Q9Y586; IntAct: EBI-21261050; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: P51159; IntAct: EBI-21264064; Score: 0.35
DE  Interaction: Q9Y275; IntAct: EBI-21266480; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC5; IntAct: EBI-26495256; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-26588212; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: A0A0H3NG92; IntAct: EBI-27055968; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P51617; IntAct: EBI-28935882; Score: 0.35
DE  Interaction: Q99952; IntAct: EBI-27114698; Score: 0.35
DE  Interaction: Q92932; IntAct: EBI-27116679; Score: 0.27
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
DE  Interaction: Q8WUM4; IntAct: EBI-30834760; Score: 0.44
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P54756; IntAct: EBI-32720907; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P04626; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P35968; IntAct: EBI-32723270; Score: 0.27
DE  Interaction: Q12866; IntAct: EBI-32723870; Score: 0.27
DE  Interaction: P04629; IntAct: EBI-32724282; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
DE  Interaction: Q01973; IntAct: EBI-32725295; Score: 0.27
DE  Interaction: Q6J9G0; IntAct: EBI-32731895; Score: 0.27
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0086014;
GO  GO:0035196;
GO  GO:0006406;
GO  GO:0006998;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P37199};
SQ  MPSSLLGAAMPASTSAAALQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNNPTVSGMSDMDYPLQGPGLLSVPNLPE
SQ  ISSIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPH
SQ  VRHLLVLATPVDIVILGLSYANLQTGSGVLNDSLSGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAY
SQ  QAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPILQIAIDNSRNILYTRSEKGVIQVYDLGQDGQGMSRVASVSQ
SQ  NAIVSAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASS
SQ  TVEKPSKVHRALYSKGILLMAASENEDNDILWCVNHDTFPFQKPMMETQMTAGVDGHSWALSAIDELKVDKIITPLNKDH
SQ  IPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAA
SQ  CDREVSAWATRAFFRYGGEAQMRFPTTLPPPSNVGPILGSPVYSSSPVPSGSPYPNPSFLGTPSHGIQPPAMSTPVCALG
SQ  NPATQATNMSCVTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERIFKSGNREITAIESSVPCQLLESVLQELKGLQEF
SQ  LDRNSQFAGGPLGNPNTTAKVQQRLIGFMRPENGNPQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALALWKLLCE
SQ  HQFTIIVAELQKELQEQLKITTFKDLVIRDKELTGALIASLINCYIRDNAAVDGISLHLQDICPLLYSTDDAICSKANEL
SQ  LQRSRQVQNKTEKERMLRESLKEYQKISNQVDLSNVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDIV
SQ  GLQAFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLSQRSKDELFSIALY
SQ  NWLIQVDLADKLLQVASPFLEPHLVRMAKVDQNRVRYMDLLWRYYEKNRSFSNAARVLSRLADMHSTEISLQQRLEYIAR
SQ  AILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAVSQLDSELMDITKLYGEFADPFKLAE
SQ  CKLAIIHCAGYSDPILVQTLWQDIIEKELSDSVTLSSSDRMHALSLKIVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNW
SQ  DVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRMKKPLHLLDCIHVLLIRYVENPSQVLNCERRRFTNLCLDAVCGY
SQ  LVELQSMSSSVAVQAITGNFKSLQAKLERLH
//
ID  Q99P88;
PN  Nuclear pore complex protein Nup155;
GN  Nup155;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Cytoplasmic side {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Nucleoplasmic side {ECO:0000250|UniProtKB:P37199}. Note=In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis. {ECO:0000250|UniProtKB:P37199}.
DR  UNIPROT: Q99P88;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. {ECO:0000250|UniProtKB:P37199, ECO:0000269|PubMed:19070573}.
DE  Reference Proteome: Yes;
DE  Interaction: O75694; IntAct: EBI-2558136; Score: 0.40
DE  Interaction: P35658; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: P46060; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: P63165; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q96SK2; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q9P2N6; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q2M296; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q15388; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: O15446; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: O00203; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q9BTX1; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: P05165; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: O35963; IntAct: EBI-11566169; Score: 0.35
DE  Interaction: P35294; IntAct: EBI-11567325; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0086014;
GO  GO:0035196;
GO  GO:0006406;
GO  GO:0006998;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0034504;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P37199};
SQ  MPSVLGSMMVASTSAAASLQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNSPTVSGMSDMDYPLQGPGLLSVPSLPE
SQ  ISTIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPH
SQ  VRHLLVLATPVDIVILGLSYANVQTGSGILNDSMCGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAY
SQ  QAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPIVQIEIDNSRNILYTRSEKGVIQVYDLGHDGQGMSRVASVSQ
SQ  NAIVSAAGNIARTIDRSVFKPIVQIAVIESSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASS
SQ  TVEKPSKVHKALYSKGILLMTASENEDNDILWCVNHDTFPFQKPMMETQMTTRVDGHSWALSAIDELKVDKIITPLNKDH
SQ  IPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAA
SQ  CDREVSAWATRAFFRYGGEAQMRFPATLPTPSNVGPILGSPMYSSSPVPSGSPYPNPSSLGTPSHGAQPPTMSTPMCAVG
SQ  SPAMQAASMSGLTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERVFKSSNREITAIESSVPVQLLESVLQELKGLQEF
SQ  LDRNSQFSGGPLGNPNTTARVQQRLVGFMRPENGNTQQMQQELQRKFQEAQLSEKISLQAIQQLVRKSYQALALWKLLCE
SQ  HQFSVIVGELQKEFQEQLKITTFKDLVIRDKEVTGALIASLINCYIRDNAAVDGISLHLQDTCPLLYSTDDAVCSKANEL
SQ  LQRSRQVQSKTERERMLRESLKEYQKISNQVDLPSVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDVV
SQ  GLQTFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLAQRSKDELFSIALY
SQ  NWLIQADLADKLLQIASPFLEPHLVRMARVDQNRVRYMDLLWRYYEKNRSFSSAARVLSKLADMHSTEISLQQRLEYIAR
SQ  AILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAISQLDSELMDITKLYGEFADPFKLAE
SQ  CKLAVIHCAGYSDPILVHTLWQDIIEKELNDSVALSSSDRMHALSLKLVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNW
SQ  DVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRVKSPLHLLDCIHVLLTRYVENPSLVLNCERRRFTNLCLDAVCGY
SQ  LVELQSMSSSVAVQAITGNFKSLQAKLERLH
//
ID  P37199;
PN  Nuclear pore complex protein Nup155;
GN  Nup155;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:15703211}. Nucleus membrane {ECO:0000269|PubMed:15703211}; Peripheral membrane protein {ECO:0000269|PubMed:15703211}; Cytoplasmic side {ECO:0000269|PubMed:15703211}. Nucleus membrane {ECO:0000269|PubMed:15703211}; Peripheral membrane protein {ECO:0000269|PubMed:15703211}; Nucleoplasmic side {ECO:0000269|PubMed:15703211}. Note=In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis.
DR  UNIPROT: P37199;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Essential component of nuclear pore complex. Could be essessential for embryogenesis (By similarity). Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. {ECO:0000250|UniProtKB:Q99P88}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0086014;
GO  GO:0035196;
GO  GO:0006406;
GO  GO:0006998;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0034504;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:15703211};
SQ  MPSMLGSMMVASTSAPSLQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNSPTVSGMSDMDYPLQGPGLLSVPSLPEI
SQ  STIRRVPLRLSWLNSLDTCSVTAMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHV
SQ  RHLLVLATPVDIVILGLSYANVQTGSGILNDSVCGGLQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQ
SQ  AEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPIVQIEIDNSRNILYTRSEKGVIQVYDLGHDGQGMSRVASVSQN
SQ  AIVCAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASST
SQ  VEKPSKVHKALYSKGILLMTASENEDNDILWCVNHDTFPFQKPMMETQMTTRVDGHSWALSAIDELKVDKIITPLNKDHI
SQ  PITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAAC
SQ  DREVSAWATRAFFRYGGEAQMRFPATLPTPSNVGPILGSPMYSSSPVPTGSPYPNPSSLGTPSHGAQPPTMSTPMSAVGN
SQ  PAMQAASLSGLTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERVFKSSNREITAIESSVPIQLLESVLQELKGLQEFL
SQ  DRNSQFSGGPLGNPNTTAKVQQRLLGVMRPENGNTQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALALWKLLCEH
SQ  QFTVIVGELQKEFQEQLKITTFKDLVIREKEVTGALIASLINCYIRDNAAVDGISLHLQDTCPLLYSTDDAVCSKANELL
SQ  QRSRQVQSKSERERMLRESLKEYQKISNQVDLPSVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDVVG
SQ  LQTFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLAQRSKDELFSIALYN
SQ  WLIQADLADKLLQIASPFLEPHLVRMAKVDQNRVRYMDLLWRYYEKNRSFSSAARVLSKLADMHSTEISLQQRLEYIARA
SQ  ILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAISQLDSELMDITKLYGEFADPFKLAEC
SQ  KLAIIHCAGYSDPILVHTLWQDIIEKELSDSVTLSSSDRMHALSLKLVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNWD
SQ  VGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRVKSPLHLLDCIHVLLTRYVENPSLVLNCERRRFTNLCLDAVCGYL
SQ  VELQSMSSSVAVQAITGNFKSLQAKLERLH
//
ID  P40064;
PN  Nucleoporin NUP157;
GN  NUP157;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P40064;
DR  UNIPROT: D3DM12;
DR  PDB: 4MHC;
DR  PDB: 7N85;
DR  PDB: 7N9F;
DR  PDB: 7WOO;
DR  PDB: 7WOT;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:12473689}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-3765456; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-4325343; Score: 0.37
DE  Interaction: P30657; IntAct: EBI-698282; Score: 0.37
DE  Interaction: P23724; IntAct: EBI-698381; Score: 0.37
DE  Interaction: P40958; IntAct: EBI-390855; Score: 0.37
DE  Interaction: Q03790; IntAct: EBI-390858; Score: 0.55
DE  Interaction: P39998; IntAct: EBI-390861; Score: 0.37
DE  Interaction: P30283; IntAct: EBI-393078; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P39081; IntAct: EBI-858214; Score: 0.00
DE  Interaction: P47007; IntAct: EBI-861577; Score: 0.00
DE  Interaction: Q08817; IntAct: EBI-861604; Score: 0.00
DE  Interaction: P40477; IntAct: EBI-6332396; Score: 0.00
DE  Interaction: Q02629; IntAct: EBI-6340320; Score: 0.00
DE  Interaction: P53739; IntAct: EBI-2611855; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3673746; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3781733; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3806428; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3812935; Score: 0.35
DE  Interaction: P11978; IntAct: EBI-6879814; Score: 0.40
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0003677;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MYSTPLKKRIDYDRETFTASASLGGNRLRNRPRDDQNNGKPNLSSRSFLSERKTRKDVLNKYGEAGNTIESELRDVTTHV
SQ  KISGLTSSEPLQLASEFVQDLSFRDRNTPILDNPDYYSKGLDYNFSDEVGGLGAFTPFQRQQVTNIPDEVLSQVSNTEIK
SQ  SDMGIFLELNYCWITSDNKLILWNINNSSEYHCIDEIEHTILKVKLVKPSPNTFVSSVENLLIVATLFDIYILTISFNDR
SQ  THELNIFNTGLKVNVTGFNVSNIISYERTGQIFFTGATDGVNVWELQYNCSENLFNSKSNKICLTKSNLANLLPTKLIPS
SQ  IPGGKLIQKVLEGDAGTEEETISQLEVDQSRGVLHTLSTKSIVRSYLITSNGLVGPVLIDAAHIRRGMNALGVKNSPLLS
SQ  NRAFKIAKIVSISMCENNDLFLAVITTTGVRLYFKGSISRRSIGSLKLDSVKFPPTSISSSLEQNKSFIIGHHPLNTHDT
SQ  GPLSTQKASSTYINTTCASTIISPGIYFTCVRKRANSGELSKGITNKALLENKEEHKLYVSAPDYGILKNYGKYVENTAL
SQ  LDTTDEIKEIVPLTRSFNYTSTPQGYANVFASQYSAEPLKVAVLTSNALEIYCYRTPDEVFESLIENPLPFIHSYGLSEA
SQ  CSTALYLACKFNKSEHIKSSALAFFSAGIPGVVEIKPKSSRESGSVPPISQNLFDKSGECDGIVLSPRFYGSALLITRLF
SQ  SQIWEERVFVFKRASKTEKMDAFGISITRPQVEYYLSSISVLADFFNIHRPSFVSFVPPKGSNAITASDAESIAMNALIL
SQ  LINSIKDALSLINVFYEDIDAFKSLLNTLMGAGGVYDSKTREYFFDLKFHDLFTPNAKTKQLIKEILIEVVNANIASGTS
SQ  ADYIVNVLKERFGSFCHSADILCYRAGEHLEAAQKFEMIDSKISRNHLDTAIDLYERCAENIELCELRRVVDIMVKLNYQ
SQ  PKTVGFLLRFADKIDKGNQAQEYVSRGCNTADPRKVFYDKRINVYTLIFEIVKSVDDYTSIEQSPSIANISIFSPASSLK
SQ  KRVYSVIMNSNNRFFHYCFYDWLVANKRQDYLLRLDSQFVLPYLKERAEKSLEISNLLWFYLFKEEHFLEAADVLYALAS
SQ  SDFDLKLSERIECLARANGLCDSSTSFDQKPALVQLSENIHELFDIASIQDDLLNLVRNETRIDEDYRKQLTLKLNGRVL
SQ  PLSDLFNDCADPLDYYEIKLRIFKVSQFKDEKVIQGEWNRLLDSMKNAPSPDVGSVGQESFLSSISNTLIRIGKTTRDTD
SQ  VVFPVHFLMNKILESFIDKSSAADGSVCSMFLLAGVSHLKLYYILSRIIENSEGNVELAKKEMVWLIKDWYQSDSDLRGS
SQ  IAPEQIKKLEKYDPNTDPVQDYVKDRHHGLK
//
ID  G0SBS8;
PN  Nucleoporin NUP159;
GN  NUP159;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P40477}. Nucleus membrane {ECO:0000250|UniProtKB:P40477}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40477}; Cytoplasmic side {ECO:0000250|UniProtKB:P40477}.
DR  UNIPROT: G0SBS8;
DR  UNIPROT: G0ZGT8;
DR  PDB: 5CWW;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre- ribosome, and protein export. {ECO:0000250|UniProtKB:P40477}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S156; IntAct: EBI-16176459; Score: 0.46
DE  Interaction: G0S4F3; IntAct: EBI-16176971; Score: 0.35
DE  Interaction: G0SBQ3; IntAct: EBI-16176539; Score: 0.61
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P40477};
SQ  MAFSFGNAGGGGGGVTQGKDLEVIQTEGLGFLALAGDAKVQLTSKWSPPPAPTASLLSIASRKGLVAAAGPDAVHVATTE
SQ  SVRKAFLAEKNGDSEVRPFNPEAKLPLPLRISQLAFTADEQYLVLSAETGGGLRAYDVNSLTQGNTQSAFELATNGETLR
SQ  QLAPNPMPESAAFCAIVTTNGNLYMANLAERTLVSGPNGPTLRSQVSCAAWSTKGKQLVAGMADGSIYQMTPDGTEKAHI
SQ  PKPPNLGDYHVSSVVWLENNVFLTIHNPTNSTNPDDKTVYHVITRQQSSGSPPNFTFQKLNDPVEPFVADKTPHHTVLRL
SQ  KDFPPNLQDLLLVSSTAVETIGLLTRSKTPLATDKPADAITNVFTTTELADDSRRAQLPMSEDMMETYPIGVALDLSSKE
SQ  KVYKPIPTDEEIEYSPGPLPGLWVLNNEGVLASWWVVYNESIRAGTTYSGIGGSSEVIPASPAPALASSTAPVPAFASPV
SQ  SKPTFGSPSPATPAFGGPSALGTKASPWATAGGAASSTPTFGQPSFGKPAAPAFGQASFPGLGQKVSPWATGSTTSAAPA
SQ  FGQSGFASAGTAPGKVFGSSFTAPSSGGFASFATKSGFASLSAPSGGSSIFSSKPGAPLTSAAPEVSMDTDTAFPPPSTK
SQ  TDKPAFGSSPFVLGSTFKADPTAAHDIEKPKEGESKSLFDTGFGLSLEDAAKQPASAAESKDEEMRSTTPPLPPPTETKP
SQ  KSIFESTTPTTTPAPQKFEFKTTTPSGFSTLLGSTKPVASSMPNIFATPKPTSAEKPKSIFDTLKPKEESKENLLKASEP
SQ  PLPPDTTSKAVFQPGSSSSESAESSPGAAAKAAFKVGNDETPKPQKELAPKPEAVPLPPDFVKAKPKTEAKETKAEEPAV
SQ  SPNLPVKPLAKKAEPIPAVPESASEEEQGQAEEEEAESGEEEEEEEEEGEGEEEEEEEEEEEEEEEEGEEGEEQSEAGSE
SQ  GSGVDVAKDLSPTAKFGSMTPGYTPHTSLGGMAESTFSTISRSEVAEQSRPLFGEITKNAPPLFPAAGPLPVSPRSPSPV
SQ  RGVVRSSILRPTETPRPVDTTPVPSRKGLLQKTASFGMSTGQKPAVDPNVKAQRKLAEKLKAEEQVLVDPEDEGIQQILQ
SQ  SKVEPTLRMNEFLAVDTKLAPMKPGRDDVPNACETLWRDINRMIDRLGLNSRSLQSFILGHTSHGKPGGRQKDDLEKPDD
SQ  WVLIEAYDLGDMIDNKLARELEAGRIKDVEGTMAAIHNLGRDLAKLRAKEEDLRKLFNAQVDPDQIALTKALPLSAEQLA
SQ  QQNELRRSYASFSKLLTEAEEALTVLKAKLASANAARGRRGAGAAQVPTVDAIIRTINKMTSMAEKRSGDIDVLESQMRK
SQ  LRIGSLGPAGTPNGNGVGAGTVVPATPGGGGRSRESSPFVTPQSSRRAMFMSPGSVGTATPRGLLAATGTPSPTKKKLSM
SQ  YTAEEKRELRAREAKRKATLRMLRESLARVGPNVVRLRDDD
//
ID  P40477;
PN  Nucleoporin NUP159;
GN  NUP159;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:17546040, ECO:0000269|PubMed:23223634, ECO:0000269|PubMed:25646085}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
DR  UNIPROT: P40477;
DR  UNIPROT: D6VVH2;
DR  PDB: 1XIP;
DR  PDB: 3PBP;
DR  PDB: 3RRM;
DR  PDB: 3TKN;
DR  PDB: 4DS1;
DR  PDB: 7N9F;
DR  Pfam: PF16755;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre- ribosome, and protein export. {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10801828, ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:11739405, ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:9736720, ECO:0000269|PubMed:9843582, ECO:0000269|PubMed:9891088}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-805203; Score: 0.59
DE  Interaction: P20449; IntAct: EBI-7266119; Score: 0.66
DE  Interaction: P36161; IntAct: EBI-7439043; Score: 0.40
DE  Interaction: P40064; IntAct: EBI-6332396; Score: 0.00
DE  Interaction: P40066; IntAct: EBI-797307; Score: 0.44
DE  Interaction: P40368; IntAct: EBI-790236; Score: 0.81
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P11484; IntAct: EBI-805203; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-805203; Score: 0.35
DE  Interaction: Q12046; IntAct: EBI-854174; Score: 0.00
DE  Interaction: P16521; IntAct: EBI-7151928; Score: 0.40
DE  Interaction: Q04175; IntAct: EBI-1173457; Score: 0.40
DE  Interaction: Q06142; IntAct: EBI-1173489; Score: 0.61
DE  Interaction: Q02630; IntAct: EBI-6332418; Score: 0.00
DE  Interaction: P24870; IntAct: EBI-2611503; Score: 0.35
DE  Interaction: P29295; IntAct: EBI-2612057; Score: 0.35
DE  Interaction: P23291; IntAct: EBI-2614250; Score: 0.35
DE  Interaction: P24869; IntAct: EBI-2617071; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: P39076; IntAct: EBI-3741411; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3750967; Score: 0.35
DE  Interaction: P47138; IntAct: EBI-3760963; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3772650; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3788010; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3790791; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3799845; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3806436; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3812943; Score: 0.35
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0000774;
GO  GO:0060090;
GO  GO:0017056;
GO  GO:0003714;
GO  GO:0097064;
GO  GO:0006607;
GO  GO:0051664;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0006611;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0061912;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSSLKDEVPTETSEDFGFKFLGQKQILPSFNEKLPFASLQNLDISNSKSLFVAASGSKAVVGELQLLRDHITSDSTPLTF
SQ  KWEKEIPDVIFVCFHGDQVLVSTRNALYSLDLEELSEFRTVTSFEKPVFQLKNVNNTLVILNSVNDLSALDLRTKSTKQL
SQ  AQNVTSFDVTNSQLAVLLKDRSFQSFAWRNGEMEKQFEFSLPSELEELPVEEYSPLSVTILSPQDFLAVFGNVISETDDE
SQ  VSYDQKMYIIKHIDGSASFQETFDITPPFGQIVRFPYMYKVTLSGLIEPDANVNVLASSCSSEVSIWDSKQVIEPSQDSE
SQ  RAVLPISEETDKDTNPIGVAVDVVTSGTILEPCSGVDTIERLPLVYILNNEGSLQIVGLFHVAAIKSGHYSINLESLEHE
SQ  KSLSPTSEKIPIAGQEQEEKKKNNESSKALSENPFTSANTSGFTFLKTQPAAANSLQSQSSSTFGAPSFGSSAFKIDLPS
SQ  VSSTSTGVASSEQDATDPASAKPVFGKPAFGAIAKEPSTSEYAFGKPSFGAPSFGSGKSSVESPASGSAFGKPSFGTPSF
SQ  GSGNSSVEPPASGSAFGKPSFGTPSFGSGNSSAEPPASGSAFGKPSFGTSAFGTASSNETNSGSIFGKAAFGSSSFAPAN
SQ  NELFGSNFTISKPTVDSPKEVDSTSPFPSSGDQSEDESKSDVDSSSTPFGTKPNTSTKPKTNAFDFGSSSFGSGFSKALE
SQ  SVGSDTTFKFGTQASPFSSQLGNKSPFSSFTKDDTENGSLSKGSTSEINDDNEEHESNGPNVSGNDLTDSTVEQTSSTRL
SQ  PETPSDEDGEVVEEEAQKSPIGKLTETIKKSANIDMAGLKNPVFGNHVKAKSESPFSAFATNITKPSSTTPAFSFGNSTM
SQ  NKSNTSTVSPMEEADTKETSEKGPITLKSVENPFLPAKEERTGESSKKDHNDDPKDGYVSGSEISVRTSESAFDTTANEE
SQ  IPKSQDVNNHEKSETDPKYSQHAVVDHDNKSKEMNETSKNNERSGQPNHGVQGDGIALKKDNEKENFDSNMAIKQFEDHQ
SQ  SSEEDASEKDSRQSSEVKESDDNMSLNSDRDESISESYDKLEDINTDELPHGGEAFKAREVSASADFDVQTSLEDNYAES
SQ  GIQTDLSESSKENEVQTDAIPVKHNSTQTVKKEAVDNGLQTEPVETCNFSVQTFEGDENYLAEQCKPKQLKEYYTSAKVS
SQ  NIPFVSQNSTLRLIESTFQTVEAEFTVLMENIRNMDTFFTDQSSIPLVKRTVRSINNLYTWRIPEAEILLNIQNNIKCEQ
SQ  MQITNANIQDLKEKVTDYVRKDIAQITEDVANAKEEYLFLMHFDDASSGYVKDLSTHQFRMQKTLRQKLFDVSAKINHTE
SQ  ELLNILKLFTVKNKRLDDNPLVAKLAKESLARDGLLKEIKLLREQVSRLQLEEKGKKASSFDASSSITKDMKGFKVVEVG
SQ  LAMNTKKQIGDFFKNLNMAK
//
ID  Q9C811;
PN  Nuclear pore complex protein NUP160;
GN  NUP160;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:17030626, ECO:0000269|PubMed:21189294, ECO:0000269|PubMed:22902705}; Peripheral membrane protein {ECO:0000269|PubMed:17030626}; Nucleoplasmic side {ECO:0000269|PubMed:17030626}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:17030626}.
DR  UNIPROT: Q9C811;
DR  UNIPROT: F4HR72;
DR  UNIPROT: F4HR73;
DR  Pfam: PF17238;
DE  Function: Contributes to the transfer of mature mRNA from the nucleus to the cytosol. Required for both R gene-mediated and basal disease resistance. RNA export seems to play a critical role in stress responses and regulation of plant growth and development. Required for proper expression of factors associated with auxin signaling. {ECO:0000269|PubMed:16751346, ECO:0000269|PubMed:17030626, ECO:0000269|PubMed:20872268, ECO:0000269|PubMed:22238449, ECO:0000269|PubMed:22288649, ECO:0000269|PubMed:22902705}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0006952;
GO  GO:0032502;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0048510;
GO  GO:0009733;
GO  GO:0009409;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17030626};
SQ  MEENRRNPSAGMEVPVAGGGNVVKWIEISVPSPSVSSSSIGANSSEDNECVQLPLSEDYASSSVIGEPSISFVWRINKTS
SQ  PNALELLQLSAKSGFPITGLRFVFAQTLSPFAFVYADEGGDSGRLVYFLYSLTPSGVVYVLKLSNTLAYKSGSVFPLDHL
SQ  IHLDVRPYLNESRVTSVAASPGFIFLGRSDGCVSCFQPIVYFQKSSGFHQELRDDTGFGRLGTVVAAVQDLFISEVHGRN
SQ  YLCVLHADGALRVWDILTYSRVLCQSIAAKNLEGVMCVRLWLGKADYDSGIIPLAVLYRKSMNDSMDVITVYGLHFSSAE
SQ  GIALSLDSGLQNIPLEEGELRDVRFTSDKIWTLKANELTSYMLCQKSSTMEAQSYTLQEDYISEQLFLSSRSSSHDLLLT
SQ  THSLFSSAKDQIMGFISSIFLRRLLCPGIFHNVALRLTLLDHNKNWTDSEFQSLSLDELTSEILLLVEHEVTAETSISVF
SQ  HWWKNFCTSYLHHWCSNNEPRTLLVQSDVIGLVRNNSVSLFFRLENAEHSLGGSSSEHSNLTSLDLGVSHSDHEILAEVL
SQ  RCTSKISKQWGGAPYAMYYESITGRPIISSDEIVPRLVNILESGYSTTIGQRTWSDLGADRAWEKELEAHKNLRTFSIDM
SQ  LLSLSALCQRAGSWEKVFTIMEHYLQYLVPKKSMQKNDGEALSDICSSILVQATSQFVKVMFESAFDIFLLISYLLNIAG
SQ  QVNMSQQDICKLRLELLPMIQDIVSEWLIILFFVTTPAESTSMEDFSLKLSSLQIDSSIDKRSWNAMLGKCGFSLAFILL
SQ  FSDRSCIVDGRFNLRYLPSSQIITSLVQNFISWIRYSKTGDDSSSLLRRSTELSLRLIRNGQSDAVERILVVVEASLRGE
SQ  KTFGCSQDTSGDWCLLQHLRGCCLLDQVQRGASGILRERKIIDAIRCFFRASSGEGSWKALHSLSKEAGFSPATTGPSIL
SQ  DGSTSSAAWKLHYYEWAMQIFERYNISEGACQFAYAALEQVDDAYNFIEMTEEFDPTKAATYTRGRLWANVFKFTLDLNL
SQ  LNDAYCAIISNPDEEIKRICLRRFIIVLFECGKTKILSDGHLPFIGLTEKITQELFWKAGRSDIMMKPNPYKLLYAYEMR
SQ  RHNWRMAASYMYQFSARLRSEGACKDYKHMSLVLQERLNGLSAAMNALALVHPGYAWIDPVPEETTRYPVKKARRAEEEQ
SQ  LRSNDQPKGEKSCIDIEKLQNEFVFTTAEYMLSLKNFGWTYSGLEKPPSDLVDLLVQANLYDMAFTVVLKFWRGSALKRE
SQ  LEKIFENMAIKCCPAKGTLWSSPNLMLTSNDEEVTHSPDRSPADQGSKLAGDWEILEVYLKRYIDIHARLPVSVASTLLQ
SQ  ADSCIELPLWLIQMFKDGQKEKALGMAGQEASPASLFQLYVDYGRLTEATNLLLEYMESFASSKPAEVLKRKKVSGVWFP
SQ  YTTVERLWWELEKTMNSGRMVEQCHKLKEQLHHALLNHLKLLKVDSNDAVSSATG
//
ID  Q9VKJ3;
PN  Nuclear pore complex protein Nup160 homolog;
GN  Nup160;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:19197064}.
DR  UNIPROT: Q9VKJ3;
DR  UNIPROT: C0KG65;
DR  UNIPROT: C0KG66;
DR  UNIPROT: C0KG67;
DR  UNIPROT: C0KG68;
DR  UNIPROT: C0KG69;
DR  UNIPROT: C0KG70;
DR  UNIPROT: C0KG71;
DR  UNIPROT: C0KG74;
DR  UNIPROT: C0KG75;
DR  UNIPROT: Q6AWI7;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (PubMed:19197064). Involved in poly(A)+ RNA transport (By similarity). Required for nuclear import of Mad (PubMed:20547758). May play a role in double strand break DNA repair (PubMed:26502056). Essential for nephrocyte development (PubMed:30910934). {ECO:0000250|UniProtKB:Q12769, ECO:0000269|PubMed:19197064, ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:26502056, ECO:0000269|PubMed:30910934}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8IGE8; IntAct: EBI-503712; Score: 0.37
DE  Interaction: Q9VAY6; IntAct: EBI-26745122; Score: 0.49
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0000724;
GO  GO:0006406;
GO  GO:0006606;
GO  GO:0046822;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTSKLQANMSYREVIPRNLSPAEWIEVKINTGTQSTLQDLKTFETSGGYCYKNTKNVQTRNRFIYWRTYQDVLELSEVS
SQ  LDISLQRNHLRLRFTDSAVLNVSLTEQGTSVTLLVVTVSSVHRYVFPLKVAGQEGGAASPEDLLSQSIFYDVNDKINDPS
SQ  TYYVTDGFGTMPNAAVSYLTQDSQSAYFAVAYQSKLLLHVMKCSTGHTITHEIKEPKLMPWFLSNLKGALTGRSETLEAA
SQ  TSMAFSEIGGEIFILVLYRNNELRLWSVDNLQTVASINCSTELGQDSAAQGPQNSQLRKISDQNFCLFLSHNSRAEFICV
SQ  SIMPDADDASVINLVQNMVPAPQTDLVDFDATSSHIWALWSNAEGDFHVSAAYFASNNAIKWVSAALEPPPDRYCLTMEQ
SQ  GVDPRETYCSYIFHPGRFDRNVIAKALYMFRRVNLQFDVKQLSMSVLKEQVCQAVEDEIQNELKDFVVTDEEYLEISTRL
SQ  WDRFYSCCEQYHIKLSEPTGLAVLGGMDAVCLVRRQSFALLRPCEVLEHLLLIGEHNDEVATYVAPLFRNDPEMAKGFVE
SQ  LMNVVTLLDKLISEDIKIELDKQLYQRESPVEVISKLVARISMIDDNGPILPSNCVRQIQQKLQNIPNLEPALEMLLDVL
SQ  CMIDPDEPPHDYSLSTRFLQSSGALMGSEYGLSILSETVKQMAMIRFSVCRNLLVLQYMAYGQNEMESENVLTNLNYLNS
SQ  YYTLVWIAETPISSSTPAGFEASIQRLSRAQLFSGYNRPYSSHLKHNGNDQTTLLRLFLESKGLFSALTMLLKHDSLSLD
SQ  SEQLNLRQSLLQLVGYINKMLWPGSPIYVFPEWLFGTCHHIIVQDYVRILSNWCSVQKHARRFMLAVSLLDCGEAHKAVH
SQ  LFHEAESGIVEDDFLFEHVLKNTPLYGKLQNSVSRGDTISPEDTKLAIVHYYLKVIQLFEQHSALDYIIQLADMAIRVLQ
SQ  PDDPQLPMFQSIVFNNHLQLGHYVEAYTALVNNADISRRKDCLRQLVITLFQNKCLPLLMQFSYIGLQDEFESIVESRAR
SQ  SMSIDQNEVYNFLYAFHTNKGNMRKASTVMYEQAMRFQVDSDAPNALEKRCSSLLICLNCLHLVDSRYRWIAKPVLGDEQ
SQ  VITIDQDNDDGEPKCDEDKRGQEVVVLELADIRRELVHAEALRELSFYRKDTAAYERATPEELSYLLASSGLYTAALKLS
SQ  RGHSFSVLPIFESLTSACVAATEDKSSDAWNWLQNNDMADLPHRSNAADMAWTLLQKLVVDNEAKDSTLIRKSVVQRLLG
SQ  LNAFLPQWLINSYKLSHSRELLHLLVKHNRLLEAADLGCEIIAGMLGAGSEYFEFKHAVNIANPQLCFPISTIDLLLHGL
SQ  KINGKDDLDYEMAYFKLEEEVQRYIETIKRTTDDKMSMAVLQMRTDLQEER
//
ID  Q12769;
PN  Nuclear pore complex protein Nup160;
GN  NUP160;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
DR  UNIPROT: Q12769;
DR  UNIPROT: B4DYE8;
DR  UNIPROT: B4E2J9;
DR  UNIPROT: Q08AD3;
DR  UNIPROT: Q7Z5X6;
DR  UNIPROT: Q96GB3;
DR  UNIPROT: Q9H660;
DR  PDB: 5A9Q;
DR  PDB: 7PEQ;
DR  OMIM: 607614;
DR  OMIM: 618178;
DR  DisGeNET: 23279;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (PubMed:11564755, PubMed:11684705). Involved in poly(A)+ RNA transport. {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
DE  Disease: Nephrotic syndrome 19 (NPHS19) [MIM:618178]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form that progresses to end-stage renal failure. NPHS19 is an autosomal recessive, steroid-resistant form with onset in the first or second decade of life, resulting in chronic kidney disease. {ECO:0000269|PubMed:30179222, ECO:0000269|PubMed:30910934}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-295747; Score: 0.53
DE  Interaction: Q8WUM0; IntAct: EBI-295755; Score: 0.35
DE  Interaction: Q9Y3B2; IntAct: EBI-373740; Score: 0.00
DE  Interaction: Q9Y5V3; IntAct: EBI-1066277; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-1106154; Score: 0.00
DE  Interaction: O75317; IntAct: EBI-2511514; Score: 0.40
DE  Interaction: O94966; IntAct: EBI-2511876; Score: 0.40
DE  Interaction: Q8BH74; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q6PFD9; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q9P2Y5; IntAct: EBI-3622729; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q7TSJ6; IntAct: EBI-8800022; Score: 0.27
DE  Interaction: Q8WYP5; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: Q9BW27; IntAct: EBI-9032422; Score: 0.59
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.53
DE  Interaction: P62508; IntAct: EBI-10219724; Score: 0.56
DE  Interaction: Q99853; IntAct: EBI-11317404; Score: 0.35
DE  Interaction: Q6ZQN5; IntAct: EBI-11318220; Score: 0.35
DE  Interaction: Q9BZS1; IntAct: EBI-11319193; Score: 0.35
DE  Interaction: Q9C009; IntAct: EBI-11319301; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: P04049; IntAct: EBI-11904774; Score: 0.00
DE  Interaction: P0C0U1; IntAct: EBI-12579831; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581451; Score: 0.35
DE  Interaction: C5E526; IntAct: EBI-12584472; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-21512742; Score: 0.35
DE  Interaction: Q8N7X8; IntAct: EBI-21585341; Score: 0.35
DE  Interaction: Q9H813; IntAct: EBI-21593240; Score: 0.35
DE  Interaction: A8K8V0; IntAct: EBI-21612043; Score: 0.35
DE  Interaction: Q8NBZ7; IntAct: EBI-21638319; Score: 0.35
DE  Interaction: Q6EMK4; IntAct: EBI-21651359; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-21865034; Score: 0.35
DE  Interaction: Q9BTM9; IntAct: EBI-15902832; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P63000; IntAct: EBI-25375986; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q8NFH4; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: Q9NRH2; IntAct: EBI-28946434; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLHLSAAPPAPPPEVTATARPCLCSVGRRGDGGKMAAAGALERSFVELSGAERERPRHFREFTVCSIGTANAVAGAVKYS
SQ  ESAGGFYYVESGKLFSVTRNRFIHWKTSGDTLELMEESLDINLLNNAIRLKFQNCSVLPGGVYVSETQNRVIILMLTNQT
SQ  VHRLLLPHPSRMYRSELVVDSQMQSIFTDIGKVDFTDPCNYQLIPAVPGISPNSTASTAWLSSDGEALFALPCASGGIFV
SQ  LKLPPYDIPGMVSVVELKQSSVMQRLLTGWMPTAIRGDQSPSDRPLSLAVHCVEHDAFIFALCQDHKLRMWSYKEQMCLM
SQ  VADMLEYVPVKKDLRLTAGTGHKLRLAYSPTMGLYLGIYMHAPKRGQFCIFQLVSTESNRYSLDHISSLFTSQETLIDFA
SQ  LTSTDIWALWHDAENQTVVKYINFEHNVAGQWNPVFMQPLPEEEIVIRDDQDPREMYLQSLFTPGQFTNEALCKALQIFC
SQ  RGTERNLDLSWSELKKEVTLAVENELQGSVTEYEFSQEEFRNLQQEFWCKFYACCLQYQEALSHPLALHLNPHTNMVCLL
SQ  KKGYLSFLIPSSLVDHLYLLPYENLLTEDETTISDDVDIARDVICLIKCLRLIEESVTVDMSVIMEMSCYNLQSPEKAAE
SQ  QILEDMITIDVENVMEDICSKLQEIRNPIHAIGLLIREMDYETEVEMEKGFNPAQPLNIRMNLTQLYGSNTAGYIVCRGV
SQ  HKIASTRFLICRDLLILQQLLMRLGDAVIWGTGQLFQAQQDLLHRTAPLLLSYYLIKWGSECLATDVPLDTLESNLQHLS
SQ  VLELTDSGALMANRFVSSPQTIVELFFQEVARKHIISHLFSQPKAPLSQTGLNWPEMITAITSYLLQLLWPSNPGCLFLE
SQ  CLMGNCQYVQLQDYIQLLHPWCQVNVGSCRFMLGRCYLVTGEGQKALECFCQAASEVGKEEFLDRLIRSEDGEIVSTPRL
SQ  QYYDKVLRLLDVIGLPELVIQLATSAITEAGDDWKSQATLRTCIFKHHLDLGHNSQAYEALTQIPDSSRQLDCLRQLVVV
SQ  LCERSQLQDLVEFPYVNLHNEVVGIIESRARAVDLMTHNYYELLYAFHIYRHNYRKAGTVMFEYGMRLGREVRTLRGLEK
SQ  QGNCYLAALNCLRLIRPEYAWIVQPVSGAVYDRPGASPKRNHDGECTAAPTNRQIEILELEDLEKECSLARIRLTLAQHD
SQ  PSAVAVAGSSSAEEMVTLLVQAGLFDTAISLCQTFKLPLTPVFEGLAFKCIKLQFGGEAAQAEAWAWLAANQLSSVITTK
SQ  ESSATDEAWRLLSTYLERYKVQNNLYHHCVINKLLSHGVPLPNWLINSYKKVDAAELLRLYLNYDLLEEAVDLVSEYVDA
SQ  VLGKGHQYFGIEFPLSATAPMVWLPYSSIDQLLQALGENSANSHNIALSQKILDKLEDYQQKVDKATRDLLYRRTL
//
ID  Q9Z0W3;
PN  Nuclear pore complex protein Nup160;
GN  Nup160;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
DR  UNIPROT: Q9Z0W3;
DR  UNIPROT: Q3TBI7;
DR  UNIPROT: Q3TP11;
DR  UNIPROT: Q3U250;
DR  UNIPROT: Q6A0A7;
DR  UNIPROT: Q7TME1;
DR  UNIPROT: Q9CZD9;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (PubMed:11564755, PubMed:11684705). Involved in poly(A)+ RNA transport (PubMed:11684705). {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6AXH7; IntAct: EBI-6876709; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAGSLERSFVELSGAERERPRHFREFTVCDIGTASAAFGTVKYSESAGGFYYVESGKLFSITRNRFIHWKTSGDTLEL
SQ  VEESLDLNLLNNAVRLKFQNYNILPGGVHVSETQNHVIILILTNQTVHRLILPHPSRMYRSELVTESQMQSIFTDIGKVD
SQ  FRDPCNSQLIPSVPGLSPGSTTSAAWLSSDGEALFALPSASGGIFVLKLPPYDVPGIASVVELKQSSVMQRLLTGWMPTA
SQ  IRGDHGPSDRALSLAVHCVEHDAFIFALCQDHKLRMWSYKDQMCLMVADMLEYVPVNKDLRLTAGTGHKLRLAYSPSMGL
SQ  YLGIYMHAPKRGQFCVFQLVSTENNRYSLDHISSLFTSQETLVDFALTSTDIWALWHDAENQTIVKYINFEHNVAGQWNP
SQ  VFMQPLPEEEIVIRDDQDPREMYLRSLFTPGHFINAALCKALQIFCRGTERNLDLSWNELKKEITLAVENELQGSVTEYE
SQ  FSQDEFRTLQQEFWCKFYACVLQYQEALSHPLALHLNPVTNMVCLLKKGYLSFLVPSSLVDHLYLLPDEHLLTEDETTIS
SQ  DDADVARDVLCLIKCLRMIGESVTMDMAVLMETSCYNLQSPEKAAEHILEDLITIDVENVMEDICSKLQEIRNPVHAIGL
SQ  LIREMDYETEVEMEKGFDPAQPLNVRMNLSQLYGSSTAGYIVCRGVYKIASTRFLICRDLLILQQLLTRLGDAVILGAGQ
SQ  LFQAQQDLLHRTAPLLLSYYLIKWASQCLATDVPVDTLESNLQHLSVLELTDSGALMANKLVSSPQTIMELFFQEVARKQ
SQ  IISHLFSQPKAPLSQTGLNWPEMITAVTGYLLQLLWPSNPGCLFLECLMGNCQYVQLQDYIQLLHPWCQVNVGSCRFMLG
SQ  RCYLVTGEVQKALECFCQAASEVGKEEFLDRLIRSEDGEIVSTPKLQYYDKVLRLLDVVGLPELVIQLATSAITEAGDDW
SQ  KSQATLRTCIFKHHLDLGHNSQAYEALTQIPDSSRQLDCLRQLVVVLCERSQLQDLVEFPYVNLHNEVVGIIESRARAVD
SQ  LMTHNYYELLYAFHIYRHNYRKAGTVMFEYGMRLGREVRTLRGLEKQGNCYLAAINCLRLIRPEYAWIVQPASGAVSDRP
SQ  GASPKRNHDGECTAAPTNRQIEILELEDLEKEYSLARIRLTLARHDPSVIAIAGSSSAKEMSALLVQAGLFDTAISLCQT
SQ  FTLPLTPVFEGLAFKCIKLQFGGEAAQGEAWSWLATNQLSSVITTKESSATDEAWRLLSTYLERYKVQNNLYHHCVINKL
SQ  LSHGVPLPNWLINSYKKVDAAELLRLYLNYDLLEEAVDLVSEYVDAVLGKGHQYFGIEFPLSATAPMVWLPYSSIDQLLQ
SQ  ALGENSANSHNIILSQKILDKLEDYQQKVDKATRDLLYRRDL
//
ID  P83722;
PN  Nuclear pore complex protein Nup160;
GN  nup160;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11684705}. Cytoplasm {ECO:0000269|PubMed:11684705}.
DR  UNIPROT: P83722;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (PubMed:11684705). Involved in poly(A)+ RNA transport (PubMed:11684705). {ECO:0000269|PubMed:11684705, ECO:0000303|PubMed:11684705}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5EWX9; IntAct: EBI-8070373; Score: 0.35
GO  GO:0005737;
GO  GO:0031080;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  PVNIYVIMADQGPAHLPVSLAVHTDMLEYVPVSKDEYFQKLKKA
//
ID  G0S7B6;
PN  Nucleoporin NUP170;
GN  NUP170;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P38181}. Nucleus membrane {ECO:0000250|UniProtKB:P38181}; Peripheral membrane protein {ECO:0000250|UniProtKB:P38181}; Cytoplasmic side {ECO:0000250|UniProtKB:P38181}. Nucleus membrane {ECO:0000250|UniProtKB:P38181}; Peripheral membrane protein {ECO:0000250|UniProtKB:P38181}; Nucleoplasmic side {ECO:0000250|UniProtKB:P38181}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P38181}.
DR  UNIPROT: G0S7B6;
DR  UNIPROT: G0ZGU4;
DR  PDB: 5HAX;
DR  PDB: 5HAY;
DR  PDB: 5HAZ;
DR  PDB: 5HB0;
DR  PDB: 5HB1;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP170 probably plays an important role in NPC assembly and organization. {ECO:0000250|UniProtKB:P38181}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S156; IntAct: EBI-4325495; Score: 0.68
DE  Interaction: G0S4T0; IntAct: EBI-4325530; Score: 0.53
DE  Interaction: G0SFH5; IntAct: EBI-4325560; Score: 0.35
DE  Interaction: G0SAK3; IntAct: EBI-16176781; Score: 0.44
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P38181};
SQ  MEPMTPMRPIPGAYVNTPAPPTANPARRRLFTEASSSGAAATTQLGAAPAPLASTMAPGPEINSGLMTPQAREDLPPVAK
SQ  AAQVVNQTLQLDDSYPDLDSYCRPGASSDYEMQSSDSSWAPFHVVRHHNIPDKVFEHLNAGEVFTKLGLFAEIGYAWASI
SQ  DSSLFLWDYTHPNPELIGYEEATHTITAVALVPPKPGVFVKTITHVLVVATTSEIILLGVSATPTPSGSKSLTLYSTRMS
SQ  VHRGGSDVSFIVGTKDGRIFLGGESDTDIHEIFYQQEERWFSSRCGKINHSHPGWSAVVPSLAGLPFGSRQQEWLRGLYV
SQ  DDTRNLLYSLSNRSTIRTYHMEGPEKLTKVIEKDKTSCLRDFAHMADSSPLFTDKTNIVALSPIPATEASKLHLMALTDT
SQ  GCRLFLSATSSASYTMGGATSLAPQSMQLQFVKFPPRESPTRIRTLNGQIIDSQLDKTSRALDPSALGFRFSPGYFFDVV
SQ  RKHPNQDMLFVSAPDTGRIKVTQPASALKYFEQGTWIELENGNRTIEIGLTTAPFAAAKQPLGFGNELAVQFDQVPGEFA
SQ  VLTNTGVHIVRRRRLVDIFAKALGNCVSASDDALEREVRKFINQYGRVETIAAALAVACGQGSDLRTGTGRGMDRNTENL
SQ  ARAAFIEYGGQPRLAESDGKQSVSESVRLSSRHDALALYLTRLVRTLWKAKVVQVGSGSDISSTIPTSKLVTIQENVERL
SQ  RNFLEANKSTIQGLAPPSERLFGRQEDIANQKEHQALHALQKLMESISEGISFVLMLFDERVSDIYARLDAVSQQQLKDL
SQ  TYEQLFSQTPGKELAKVLVKAIVNRNIASGANVETVADALRRRCGSFCSPDDVVTFKAQEQLQRASEQAHNSPVLRALLA
SQ  ESLRLFEQVAGSLTPANLTTAVEQYISLKYYAGAIQLCLTVAQQKDRGNTALSWVNDGKPANDSRKKAFDERKICYNLIH
SQ  QVLDKLESDFAGEPELVDGRPTLAATKRMEAYNVVNDSSDEVFHFDLYEWYIEKGWTDRILSIDSPHVITYLQRLAETDF
SQ  RHAELLCRFYTTRSRFFEAAQVQTNLAKSDLNISLKDRIILLSRAKGNASVNTIGISRQQQQQLNHEASELLEIAHIQDD
SQ  LLERLVADPRIPEERKAEIEEFLDGPIRTLTDLFNDYADQANYYDLCLLIFHAADFHNPRTILDTWNNLINQSHFEAEQR
SQ  REYWEIVQAGGDLPAGVIAPIAEPPLPYVYVSQQIQLIAHRTSLDSLIFPVNSLLPVVCAYAINNGQDASIGADPCWPIQ
SQ  LFLNLGVPHALVVQVLENVLDTQEAPFTGRRRKLVVQWIAMAVDMWVREVERRGAMAAAAASGASGSEAVMGSWVSELLG
SQ  RADQVLTQIAGTGATLRGGAASDAEEIASLRRTVKGLKRSVDMLLGGEMARMSFFR
//
ID  P38181;
PN  Nucleoporin NUP170;
GN  NUP170;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution. {ECO:0000269|PubMed:10684247}.
DR  UNIPROT: P38181;
DR  UNIPROT: D6VPS4;
DR  PDB: 3I5P;
DR  PDB: 3I5Q;
DR  PDB: 7N85;
DR  PDB: 7N9F;
DR  PDB: 7WOO;
DR  PDB: 7WOT;
DR  Pfam: PF03177;
DR  Pfam: PF08801;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP170 probably plays an important role in NPC assembly and organization. In addition it is required for chromosome transmission fidelity. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11290711, ECO:0000269|PubMed:12403813, ECO:0000269|PubMed:12473689, ECO:0000269|PubMed:14697200, ECO:0000269|PubMed:9864357}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-3765464; Score: 0.35
DE  Interaction: P32499; IntAct: EBI-1270066; Score: 0.00
DE  Interaction: P36161; IntAct: EBI-4392409; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: Q03790; IntAct: EBI-805269; Score: 0.72
DE  Interaction: Q06440; IntAct: EBI-7439664; Score: 0.40
DE  Interaction: P31787; IntAct: EBI-7895309; Score: 0.44
DE  Interaction: P53141; IntAct: EBI-8467427; Score: 0.40
DE  Interaction: Q02630; IntAct: EBI-1269692; Score: 0.00
DE  Interaction: Q02629; IntAct: EBI-1269835; Score: 0.00
DE  Interaction: P48837; IntAct: EBI-1269978; Score: 0.00
DE  Interaction: P53233; IntAct: EBI-2611781; Score: 0.35
DE  Interaction: P23291; IntAct: EBI-2614250; Score: 0.35
DE  Interaction: P29366; IntAct: EBI-7311861; Score: 0.31
DE  Interaction: Q00684; IntAct: EBI-2882792; Score: 0.00
DE  Interaction: P14832; IntAct: EBI-2882919; Score: 0.00
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P40358; IntAct: EBI-3657508; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3772658; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3781749; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-4325351; Score: 0.37
DE  Interaction: P40064; IntAct: EBI-4325343; Score: 0.37
DE  Interaction: P49687; IntAct: EBI-4421662; Score: 0.59
DE  Interaction: P32597; IntAct: EBI-6879758; Score: 0.50
DE  Interaction: P11938; IntAct: EBI-6879805; Score: 0.35
DE  Interaction: P11978; IntAct: EBI-6879786; Score: 0.50
DE  Interaction: P39929; IntAct: EBI-10052681; Score: 0.44
DE  Interaction: Q03281; IntAct: EBI-10052697; Score: 0.44
DE  Interaction: Q03707; IntAct: EBI-10052689; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0003682;
GO  GO:1990841;
GO  GO:0044877;
GO  GO:0017056;
GO  GO:0007059;
GO  GO:0031507;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006405;
GO  GO:0034398;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFQSFFHNNGPAAAGETFSDSRSYPLTNHQEVPRNGLNELASSATKAQQQPTHILNSYPITGSNPLMRASAMGATSGSIN
SQ  PNMSNMNEHIRVSGMGTSKPLDLAGKYIDHLQHKDSNTPVLDERSYYNSGVDYNFSREKNGLGAFTPFEKQDVFNIPDEI
SQ  LHEFSTSQTKTDMGIFPELNRCWITIDNKLILWNINNDNEYQVVDDMKHTIQKVALVRPKPNTFVPAVKHLLLISTTMEL
SQ  FMFAISLDKATNELSVFNTHLSVPVQGIDVIDIVSHERSGRIFFAGQASGLNIWELHYSGSDDWFNSKCSKVCLTKSALL
SQ  SLLPTNMLSQIPGVDFIQALFEDNSNGNGGFSQETITQLTIDQQRGIIYSLSSKSTIRAYVITEKSLEGPMSIEPAYISR
SQ  IIGTTTARAAPILGPKYLKIVKISSVAPEENNNLFLVALTVGGVRLYFNGSMGRFNIEALRLESIKFPPSSVTPEVIQQE
SQ  LLHQQQEQAKRSFPFFSNLMSSEPVLLKFQKKSSVLLETTKASTIISPGIFFSAVIKSSQQTHQQEKKENSSVTGTTATA
SQ  GSKTVKQQPVTLQHKLFVSVPDYGILKTHGKYVENATFLETAGPVQQIIPLSGLFNATTKPQGFANEFATQYTSETLRVA
SQ  VLTSTSIEIYKYRTPDEIFEDLIDNPLPFVLNYGAAEACSTALFVTCKSNKSEKLRSNALTFLTMGIPGVVDIKPVYNRY
SQ  SVSTVSSLLSKPTLSTATTNLQQSITGFSKPSPANKEDFDLDDVILSPRFYGIALLITRLLRDIWGRHVFMTFTDNRVTS
SQ  HAFISSSDPITPSINNLKSDEISQNRNIISKVSISKDCIEYYLSSINILNEFFITYGDSISQISAPYVLANNSNGRVIDK
SQ  TEEVANQAESIAINAMIKMVQSIKEGLSFLNVLYEESEVEGFDNQYLGFKDIISFVSLDVQKDLVKLDFKDLFAPNDKTK
SQ  SLIREILLSIINRNITKGASIEYTATALQERCGSFCSASDILGFRAIEHLRRAKEIGLRNYDSLNYHLKNATALLEQIVD
SQ  DLSIEKLKEAVSMMLSVNYYPKSIEFLLNIANSMDKGKLACQYVANGFLENDDRKQYYDKRILVYDLVFDTLIKVDELAE
SQ  KKQSSKTQNQISISNDDEVKLRQKSYEAALKYNDRLFHYHMYDWLVSQNREEKLLDIETPFILPYLMEKAGSSLKISNIL
SQ  WVYYSRRSKFFESAEILYRLATSNFDITLFERIEFLSRANGFCNSVSPLSQKQRIVQLASRIQDACEVAGIQGDILSLVY
SQ  TDARIDSAIKDELIKTLDGKILSTSELFNDFAVPLSYHEIALFIFKIADFRDHEVIMAKWDELFQSLRMEFNNTGKKEDS
SQ  MNFINLLSNVLIKIGKNVQDSEFIFPIFELFPIVCNFFYETLPKEHIVSGSIVSIFITAGVSFNKMYYILKELIETSDSD
SQ  NSVFNKEMTWLIHEWYKSDRKFRDIISYNDIIHLKEYKIDNDPIEKYVKNSGNNLGICFYKE
//
ID  Q9P7M8;
PN  Nucleoporin nup184;
GN  nup184;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10388805}.
DR  UNIPROT: Q9P7M8;
DR  UNIPROT: Q9Y8G4;
DR  Pfam: PF10487;
DR  Pfam: PF18378;
DE  Function: Interacts with pom152 in the core structure of the nuclear pore complex (NPC). Involved in the export of mRNA. {ECO:0000269|PubMed:10388805}.
DE  Reference Proteome: Yes;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0006607;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDYLLSWSWILDAFETSDENLSQNKFEELLDARIAAFQQIESPVTGTLNSNKTTEGEEAKLSIYDSSHSISKSQLESVK
SQ  KISDITGYNEAQVAYVLLVHQYELNTQYFSQLDNDSVLAQEFQRRYYAEIISCWKVLAFLLQACTDADSKWHKMATRLIV
SQ  SIFQTAQRSGENAQSTTPSIFCVRIIDYLSKMTSQAAPASLTFNGEEAISQWYFFHFNLQLQLLRVIFLSTYSLVVCNSE
SQ  MAISWFNCMKKTRYLHDQEFMHLDIDTGFSMCKEITNVAIIISINFISLEKQVLSFKDNPSFFMLSGNTIISLHDMITQL
SQ  SNDSIGAAVSLTWGIALHLLSNSPDNIPLIQNSSVVSSKILQNPQNSFQALIIAALKYDPFTLIHRIISSLEDDPYIDGY
SQ  SKIMATLFSSAVSYVKFSDSTMLCATTLFKTPQVYQLFENNDSVTRLLNFARARFPFEYSQFVLLLIPTFACLTSKQLVS
SQ  SELLHMTTFTQSLPSGFKAYEIIPEPNVTGNALIELQESLHLDSYGFFFPNAERSLPKGTRGRIVSVDTYPPVVMWDLNY
SQ  SLWEAVGISLNYIVRNGLINSHKSFVLTVLSSSVPLFQTDVSGACELVHLASEGLDGELDFINVICDLLDYFLSLSVIED
SQ  ADYQICVSSLRLLREFTRFAATDVWAYVTRSLVCVGSEKGISLEDVIFDYESINGVYDFTLAFFDLYEILLDNCISTSVV
SQ  PDDFSIRLKTDFVKRAMRFLCEVFANYLDWKYARIIQQYQIGHRFASLITKLLNVTFGIEYFNPKTTVNKKTLPLRELSH
SQ  YIVQRFLVQQDSNRYLHPLLSVMDLINLLYTDIFSTISSPRAKAAKMWLISSFCAMKTLICLRGFLNLKPSELERELFSR
SQ  SPDLFNCLPRLLCCIAPILQLLSALILAPWPSETPSLLAYMINSTDIVGRVCIQILTNPIQSTNIEGSVWKFLSSIMKGQ
SQ  QQGLAVLLFSGKKFPLDRMKSLNHNVDVQLTSKSLISLAEKRLDSFSINDILSQVPVFEFIFLSRNFWTASLGNLQQEAN
SQ  FWNRIVDAIKLPLTVKLDGLSSVAQADLYILAAHATRITAIQLHMSKLNKSNSSKKIIIDPLKDSMKDLVQHAFTITAYD
SQ  SNIHNALTRAFKHENGDLHISDLRNTGLFPLRYGDNYFYNIKLAKNMLLNTEDTSFKISMMMSANENLSLLDAQAALLRS
SQ  WSIFICAFVEFVKEDATLSILELKIMKWVLKSLAEDTIDVNVVQELSAERAALVFRISQQTLAIPISNEVKEHLQSILLL
SQ  TWKAITTTKFSIYEDSNGEMAYYRPLLHVLYNTLNRLLSEEKENLSLSVGFVSGLLQLCHRKLSQLFEKAVINPTIEVYG
SQ  DIVLLNSLHKCIVNSHLIRGLQSLYISYINDSFSVDNCLRLFSWSHSLLVDGQPYFADAALSFLLICSSSPAGAEQIVMN
SQ  GFFYSIMESPLSTALSTGGLGLDGSSIQYKIWIRGILPLLFNIVKFLGNRIMNDMREFVLLAFPQIQYALLNWCQPPSSI
SQ  SLASIDESFMIVLLFDLLQQFNPALLQEIRLAELKIEMLEASTI
//
ID  G0SFH5;
PN  Nucleoporin NUP188;
GN  NUP188;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P52593}. Nucleus membrane {ECO:0000250|UniProtKB:P52593}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52593}; Cytoplasmic side {ECO:0000250|UniProtKB:P52593}. Nucleus membrane {ECO:0000250|UniProtKB:P52593}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52593}; Nucleoplasmic side {ECO:0000250|UniProtKB:P52593}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P52593}.
DR  UNIPROT: G0SFH5;
DR  UNIPROT: G0ZGU5;
DR  PDB: 5CWU;
DR  Pfam: PF10487;
DR  Pfam: PF18378;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP188 probably plays an important role in NPC assembly and organization. {ECO:0000250|UniProtKB:P52593}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S024; IntAct: EBI-5238287; Score: 0.52
DE  Interaction: G0S156; IntAct: EBI-4325546; Score: 0.52
DE  Interaction: G0S4T0; IntAct: EBI-4325472; Score: 0.35
DE  Interaction: G0S7B6; IntAct: EBI-4325560; Score: 0.35
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P52593};
SQ  MATLTDRTYLPPLEDCLTGRTVILSWRLVASALEDADLARLTSPALSTFLRDGFVHELLKHPARVFEPKDLKQEFETKTS
SQ  SIQTVAPGVDTIKKDALWLADAVAINQVAALRIVLIEYQTRAHSHLVLPLSTQDVANIQEAAGVGDAHASSILSLLNPAS
SQ  AVDAETMWCDFETEARRRERILATYLSERRSFTAAVDALVTFLLHSAPGQHKDLDSLRRALLKDAFAFDEDLDVPDRSKL
SQ  LTMAPTYMNLVEDCIARAQALPAKLGESFKTEAFELDWLRTAITEAVHSLSIAFQALDLDTPYFAPHELLSEWFELMNSS
SQ  LFLESILGFEVVADLAMPARSLVSAICLKMLNIDRTIQFLHDFDYPDGEEPYLLSSQTLNKIHTAVTNAVNSGVAASLPV
SQ  AFAWSLIVHQMHLGYQERAERRDLLVNQRAQAGFELEFQPSASTPNRRRRNSAGSIVSLEASPYDDFLREQRLDNDIAPV
SQ  EQIAMLATSRGQVYQVMSEMALCLGTTHEAAFRPAVGARARLVFQDLLKRSAYLIPYQDEPVFSLLAILATGRQYWDVTD
SQ  ALSASSLNQVYTDMLDDETLFTQFTMQAINRFPYEFNPFSVLCRVLAAALITNKDKADVVTGWLWRTPTLTVDWNPAWDR
SQ  SYELCFEDENTNSFRLTRDVDLFGSASPARPRHLAAEERFIIPEGTLGRFVTDVGRTARLEFEHSALALLGKRLEVKAAE
SQ  EICDSGMAPLDVDEQAEAVAMLATVLRAESLKSTAKGGDPEAPLKFLKEASRLLPHNKDILTVISDTIDGLVEKELLELD
SQ  GPQIAVLASCLQFLHAALAVCPGRVWAYMSRCALIAGDARPGRLSRITGSLDMYAERFDLLSSAVKLFAALIDSAACSAV
SQ  QRRAGSTALVSVRSAVENPWLGTSEKILSRVALAIAQAALDVYESTTTWRFRSELDRSILVRDVVGLMHKLVVHAHTLSS
SQ  HLTSTLSPAAAHIISSFLTPPPSASSLRFQPLLGTLLVALITPRATLYPGQSRILAERVTSVLAFCTSLLRAADFLGQTH
SQ  IPLQTHLFQSACLLARLPAANAVYRAPVLELLRALVEVAGRAANGSGEPPSLLGYLGSHAARSFISLVEGIDKPFGRVEH
SQ  AVVTWRFFAAVIRNRQQWMAGCLLTGRTPREALKGGGEQKIERKVGEGSVLAAAMERLREVKSLDVQEAVAVMDFVVSAQ
SQ  NYWPWTIFAVRKEKEVVDALRGYVRGLKAPGMVMKTDGAAAAAFQARIAAYVAETFAMQLYHMRQMRQAEKFAGELVADL
SQ  DYFLREGVMVWGYNASLHGNFARNFAKRFPGVEVDDFKRTMWLPRELGKGYYYALEVAEQMLGFDAGWGGVKQSGFRKEM
SQ  ETANLNLSLVEAQVSLFHAWEYLLLELTLSLLPKKENAAFARQVLQVVEQCLEANQRSQPPENIFVVLGHARAGLALTLL
SQ  QRLADANQLPRDVTHLLALVSSAIHAVENPFGANDLPYFRTLLKILFVVLRAAKQGTAKPGESNVAITQQVLTILDRVVA
SQ  RCFRALAALVHEQQQNATDGTTTAPEDLALITAILQACLSVPGIEQCQVQVLNIMAAHDVFQVAVALFSWADRLLPANPS
SQ  PASSSTSTSATNPASGDPVYGELALLFLLELSALPALAEHLACDGLLGHLAAARLAGYMRRTNVGPFAENAGAARCYAIW
SQ  AKCLLPLLLNILAALGSTVAPEVAWVLNQFPNLLQSSVERIEPPGFSRPTLSLASTPPRQKFISLLEISEIHSLALLTRV
SQ  LAACRAQNARDVPEVTWDGAKVLECVEYWLRGRKVLRERLVPLGPREVEWRGMVATGGVVGVAGDGGEGCENRLEEKAVG
SQ  LLVGVREVLEGGLEGEGE
//
ID  A0A0B4K859;
PN  Nucleoporin Nup188;
GN  Nup188;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q5SRE5}.
DR  UNIPROT: A0A0B4K859;
DR  UNIPROT: A1Z945;
DR  Pfam: PF10487;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Required for proper protein transport into the nucleus. {ECO:0000250|UniProtKB:Q5SRE5}.
DE  Reference Proteome: Yes;
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: Q9VH81; IntAct: EBI-9922589; Score: 0.35
DE  Interaction: P18431; IntAct: EBI-9925534; Score: 0.35
DE  Interaction: Q24568; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: O61307; IntAct: EBI-9946542; Score: 0.35
DE  Interaction: M9NFI9; IntAct: EBI-9959939; Score: 0.35
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPAVEKSVITDWKRLWPMVSGIHYETPQDTVREELMNVASELQAGVLQFKPKNASSLELGTLLKEKKQEKLLPFTERLQD
SQ  LLDLESAQCWEILCYYLTQEYRGSASLLTQLISTETNMAKLHEDIRHYYSLERMVVLKIVKNLIVFHQVPNHPYHREYRA
SQ  VVEKITIPRLRDSYLDQLESLICEVPPRKLMAGECFHSAERLVAWSERNAREINEVLHILLVLAEHLPMGLEQIKRIFAA
SQ  CKQHSFGKMQSYLDDSQPYHQEIIRSLSYSELMLVLKCLDFEKPEKHSDLIEKLIEDLQVDIASMYHRPEHGPLLLAWML
SQ  LRLRGTNDADDASSLLRCRQLGKRAVDLKCFVQLHLIARHSMYADDSMLSRIVRRTIYNQVGYLCDLFDGDGSCARYEGI
SQ  YELLCELVSWPHLAKDFCSREDDGPCSLYKTLLENFPLELTHLSKLALSLTKAGQGNYVKSQLEALPILALRYDESQHKL
SQ  REVDTNEFELLASVQPFQQIDFTIPAGTSCTAIQHPSGCFMHFRFPVNYFDALHHEINCLLRETGHLHGDFESSERIRNV
SQ  EAGLRFLESAVKLSQSISGISAEMVHPTEMCVDLLHTFKSVQYPPVGLLSSCLNVCTALLPLVDEEIFSRISNLHILPTV
SQ  SPGSHYDFKMYANANGVGFESRFLGSVIDNVEKKRERYEFLLSYIGFLRAYSNLKRNRQIQMEIPGLIFLLKDVFPHLHT
SQ  WHFSSQVERNKIYFEILSFICDILDLFNTAKESNCKQRELLVKVCVYSLLNLENGLILLRFVGVGNAYVQYTMELETNWM
SQ  QQQPHGLMMLVRLSMRILMQLLRLKEEVYGNSETLSPLEALIYTQPKQRDTLRIIPTVCSYMSNIFDRWLPILSCRLLKR
SQ  IALQFNMSLLACLDMEADQIRLTFMQKLPDELESDSIKIAILELVDACIAKQPGVTEAFFKVNYALDKRSRSFFSKDCVP
SQ  NIGESIVTYMRDFLDALQVDPLTIQQALPAKIMTIFHSMWKHNLQMLVDDLVKDKQFWKKLCSPLFSELQPNLRIYTQLL
SQ  NIISIEVYTGNGNNAALLDVMNKFFEQKNFGPWLNYVFNMPKVPAVKNLSSSDHLPDWICCLQAFKDLIVILLKKQPKFV
SQ  TIPESQFKLMAQKCLVVLVDRSNYLEDMRPFIILAELYVFILLEFKHAYTDSLEEEQTLMDLLLQLMNRICACYEDQHVR
SQ  AKEACLAIVTKCTHLYTDLLIRDSSIALRFLNSVVGIICSELQHMENSVSLEKSQGLNNSDSSDSKTSTNSLILCLNLLK
SQ  AVATIFHNDGPGNWDLPFVSVRLFQRLVRCVSRTLPLFSKQVLSVQLLDVLIVFAKGHCSVEFLHCDVGEYLWLKLLPPR
SQ  ELLQSKHEFTKTTAADAEGWTVEQWWPVYARGIELVTIIYEKHKKCFLEDAFQFVGIHAVFLEDALLLSKQSLEPSAMYL
SQ  IKAAVNLVASLTEHHKEWKQDSDLSLANLMRAVQSLLCHTSSLFHQQKNLKCLLAGRRSQLEILRSTEALIVDDELISAC
SQ  NDLTDIIISCVKALLRFSPDLMELLCCSAYEPSKHSILLDVKFGAPKLNEENLTLTFGIVLNLVNIYVKALNMQNHGFSE
SQ  VPLNSLPNVEHSGDNDDPEVCVGNQTNRTFSKPLSNVSISTGTCPASELLSNMDGQLCLLALEHLLMLVASQAICIIRSP
SQ  NLETLWKQIVRRDISNELLIFNEFVRRKVILDYKENRSPWLRRKHGLCKLKCVDPVRSSSSSSRSSEIVRRSNTNNELRV
SQ  NVVRRLHLQQQQRTPPPQNFDMSSDLSPIAAAQGAAMTTSLDGRKRLYPAQQAGDAFLEDELAAIELQYFPPPTEPGYCE
SQ  LSQVQVVEEDYLQLMSALFNVMPHCD
//
ID  Q5SRE5;
PN  Nucleoporin NUP188;
GN  NUP188;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000305|PubMed:32275884}.
DR  UNIPROT: Q5SRE5;
DR  UNIPROT: Q14675;
DR  UNIPROT: Q2TA87;
DR  UNIPROT: Q7Z3K8;
DR  UNIPROT: Q8IWF1;
DR  PDB: 5IJO;
DR  Pfam: PF10487;
DR  OMIM: 615587;
DR  OMIM: 618804;
DR  DisGeNET: 23511;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (Probable). Required for proper protein transport into the nucleus (PubMed:32275884). {ECO:0000269|PubMed:32275884, ECO:0000305|PubMed:32275884}.
DE  Disease: Note=Copy number variations of NUP188 gene may be a cause of heterotaxy, a congenital heart disease resulting from abnormalities in left-right (LR) body patterning. {ECO:0000269|PubMed:21282601}. Sandestig-Stefanova syndrome (SANDSTEF) [MIM:618804]: An autosomal recessive syndrome characterized by pre- and postnatal microcephaly, trigonocephaly, congenital bilateral cataract, microphthalmia, cleft lip and palate or high-arched palate, camptodactyly, rocker-bottom feet, heart anomalies, specific brain changes such as loss of periventricular white matter, thin corpus callosum, and delayed myelinization. {ECO:0000269|PubMed:32021605, ECO:0000269|PubMed:32275884}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: P0DTC7; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P53671; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-1062503; Score: 0.00
DE  Interaction: O75365; IntAct: EBI-1068582; Score: 0.00
DE  Interaction: Q8IY92; IntAct: EBI-2370766; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-2514311; Score: 0.40
DE  Interaction: P24386; IntAct: EBI-2515120; Score: 0.40
DE  Interaction: Q80U93; IntAct: EBI-2555228; Score: 0.56
DE  Interaction: Q6ZQH8; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: Q15051; IntAct: EBI-4286917; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6191076; Score: 0.53
DE  Interaction: Q8NE63; IntAct: EBI-6381132; Score: 0.35
DE  Interaction: Q9UPZ9; IntAct: EBI-6381514; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P62700; IntAct: EBI-11010796; Score: 0.35
DE  Interaction: Q99JI4; IntAct: EBI-11026623; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q8R344; IntAct: EBI-11048683; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q8NBT2; IntAct: EBI-11147438; Score: 0.35
DE  Interaction: P06821; IntAct: EBI-12577493; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-12578833; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581451; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P22087; IntAct: EBI-16792282; Score: 0.27
DE  Interaction: P62753; IntAct: EBI-16798663; Score: 0.27
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9Y275; IntAct: EBI-21266480; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: P19419; IntAct: EBI-25378580; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
DE  Interaction: P59635; IntAct: EBI-25688593; Score: 0.35
DE  Interaction: O14733; IntAct: EBI-28930089; Score: 0.35
DE  Interaction: P11274; IntAct: EBI-28931791; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-28935882; Score: 0.35
DE  Interaction: Q16654; IntAct: EBI-28941523; Score: 0.35
DE  Interaction: Q86UX6; IntAct: EBI-28942129; Score: 0.35
DE  Interaction: Q8TDX7; IntAct: EBI-28943744; Score: 0.35
DE  Interaction: Q96GD4; IntAct: EBI-28944360; Score: 0.35
DE  Interaction: Q96QS6; IntAct: EBI-28944559; Score: 0.35
DE  Interaction: Q9NRM7; IntAct: EBI-28946455; Score: 0.35
DE  Interaction: Q9Y6S9; IntAct: EBI-28948011; Score: 0.35
DE  Interaction: Q9H5K3; IntAct: EBI-28948637; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-32719716; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
DE  Interaction: O75771; IntAct: EBI-34582077; Score: 0.35
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAAGGPCVRSSRELWTILLGRSALRELSQIEAELNKHWRRLLEGLSYYKPPSPSSAEKVKANKDVASPLKELGLRISK
SQ  FLGLDEEQSVQLLQCYLQEDYRGTRDSVKTVLQDERQSQALILKIADYYYEERTCILRCVLHLLTYFQDERHPYRVEYAD
SQ  CVDKLEKELVSKYRQQFEELYKTEAPTWETHGNLMTERQVSRWFVQCLREQSMLLEIIFLYYAYFEMAPSDLLVLTKMFK
SQ  EQGFGSRQTNRHLVDETMDPFVDRIGYFSALILVEGMDIESLHKCALDDRRELHQFAQDGLICQDMDCLMLTFGDIPHHA
SQ  PVLLAWALLRHTLNPEETSSVVRKIGGTAIQLNVFQYLTRLLQSLASGGNDCTTSTACMCVYGLLSFVLTSLELHTLGNQ
SQ  QDIIDTACEVLADPSLPELFWGTEPTSGLGIILDSVCGMFPHLLSPLLQLLRALVSGKSTAKKVYSFLDKMSFYNELYKH
SQ  KPHDVISHEDGTLWRRQTPKLLYPLGGQTNLRIPQGTVGQVMLDDRAYLVRWEYSYSSWTLFTCEIEMLLHVVSTADVIQ
SQ  HCQRVKPIIDLVHKVISTDLSIADCLLPITSRIYMLLQRLTTVISPPVDVIASCVNCLTVLAARNPAKVWTDLRHTGFLP
SQ  FVAHPVSSLSQMISAEGMNAGGYGNLLMNSEQPQGEYGVTIAFLRLITTLVKGQLGSTQSQGLVPCVMFVLKEMLPSYHK
SQ  WRYNSHGVREQIGCLILELIHAILNLCHETDLHSSHTPSLQFLCICSLAYTEAGQTVINIMGIGVDTIDMVMAAQPRSDG
SQ  AEGQGQGQLLIKTVKLAFSVTNNVIRLKPPSNVVSPLEQALSQHGAHGNNLIAVLAKYIYHKHDPALPRLAIQLLKRLAT
SQ  VAPMSVYACLGNDAAAIRDAFLTRLQSKIEDMRIKVMILEFLTVAVETQPGLIELFLNLEVKDGSDGSKEFSLGMWSCLH
SQ  AVLELIDSQQQDRYWCPPLLHRAAIAFLHALWQDRRDSAMLVLRTKPKFWENLTSPLFGTLSPPSETSEPSILETCALIM
SQ  KIICLEIYYVVKGSLDQSLKDTLKKFSIEKRFAYWSGYVKSLAVHVAETEGSSCTSLLEYQMLVSAWRMLLIIATTHADI
SQ  MHLTDSVVRRQLFLDVLDGTKALLLVPASVNCLRLGSMKCTLLLILLRQWKRELGSVDEILGPLTEILEGVLQADQQLME
SQ  KTKAKVFSAFITVLQMKEMKVSDIPQYSQLVLNVCETLQEEVIALFDQTRHSLALGSATEDKDSMETDDCSRSRHRDQRD
SQ  GVCVLGLHLAKELCEVDEDGDSWLQVTRRLPILPTLLTTLEVSLRMKQNLHFTEATLHLLLTLARTQQGATAVAGAGITQ
SQ  SICLPLLSVYQLSTNGTAQTPSASRKSLDAPSWPGVYRLSMSLMEQLLKTLRYNFLPEALDFVGVHQERTLQCLNAVRTV
SQ  QSLACLEEADHTVGFILQLSNFMKEWHFHLPQLMRDIQVNLGYLCQACTSLLHSRKMLQHYLQNKNGDGLPSAVAQRVQR
SQ  PPSAASAAPSSSKQPAADTEASEQQALHTVQYGLLKILSKTLAALRHFTPDVCQILLDQSLDLAEYNFLFALSFTTPTFD
SQ  SEVAPSFGTLLATVNVALNMLGELDKKKEPLTQAVGLSTQAEGTRTLKSLLMFTMENCFYLLISQAMRYLRDPAVHPRDK
SQ  QRMKQELSSELSTLLSSLSRYFRRGAPSSPATGVLPSPQGKSTSLSKASPESQEPLIQLVQAFVRHMQR
//
ID  Q6ZQH8;
PN  Nucleoporin NUP188;
GN  Nup188;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q5SRE5}.
DR  UNIPROT: Q6ZQH8;
DR  UNIPROT: Q4VA15;
DR  UNIPROT: Q80UL4;
DR  UNIPROT: Q8C7A1;
DR  UNIPROT: Q8R3F1;
DR  Pfam: PF10487;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Required for proper protein transport into the nucleus. {ECO:0000250|UniProtKB:Q5SRE5}.
DE  Reference Proteome: Yes;
DE  Interaction: P35658; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: P62826; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: P78406; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: Q5SRE5; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: O15294; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: Q8WYU3; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: B4DYZ6; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: Q99567; IntAct: EBI-2563113; Score: 0.56
DE  Interaction: O14980; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: P14618; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: Q8N1F7; IntAct: EBI-2563113; Score: 0.56
DE  Interaction: O55222; IntAct: EBI-6914965; Score: 0.35
DE  Interaction: Q92878; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: P62847; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: Q9BRJ2; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: E9PJN9; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: Q567V2; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: Q5T0N5; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: O95373; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: Q9BXS6; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: Q9HCN8; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: Q9H5Q4; IntAct: EBI-10997801; Score: 0.35
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAAGGPCVRSSRELWTILLGRSALRELNQIEAELNKYWQRLLEGLSYYKPPSPSSAERVKANKDVASPLKELGLRVSK
SQ  FLGLDEEQSVQLLQCYLQEDYRGTRDSLKTVLQDERQSQALTLKIADYYYEERTCILRCVLHLLTYFQDERHPYRAEYAD
SQ  CVDKLEKELVLKYRQQFEELYRTEAPTWETHGNLMTERQVSRWLVQCLREQSMLLEIIFLYYAYFEMAPSDLLVLTKMFK
SQ  EQGFGSRQTSRHLVGGTMDPFVDRIGYFSALILVEGMDIESLHKYALDDRRELHQFAQDGLICQDMDRAMLTLGDIPHHA
SQ  PVLLAWALLRHTLSPEETSSVVRKIGGTAIQLNVFQYLTRLLRSLASGGNDCTTSTACMCVYGLLSFALTSLELHTLGNQ
SQ  QDVIDTACEVLADPSLPELFWGTEPTSGLGIILDSVCGMFPHLLSPLLQLLRALVSGKSTAKKVYSFLDKMSFYNELHKH
SQ  KPHDVLSHEDGTLWRRQTPKLLYPLGGQTNLRIPQGTVGQVMLDDRAYLVRWEYSYSSWTLFTCEIEMLLHVVSTADVIQ
SQ  HCQRVKPIIDLVHKVISTDLSIADCLLPITSRIYMLLQRLTTVISPPVNVIASCVNCLTVLAARNPAKVWTDLRHTGFLP
SQ  FVAHPVSNMTQMISAEGMNAGGYGSLLMNSEQPQGEYGVTIAFLRLVTTLVKGQLGSTQSQGLVPCVMFVLKEMLPSYHK
SQ  WRYNSHGVRELIGCLILELIHAILNLCQETELHSSHTPSLPSLCICSLAYTEAGQTVISIMGIGVDTIDMVMAAQPRSDG
SQ  PEGQGQGQLLIKTVKLAFSVTNNVIRLKPPSNVVSPLEQALTQHGAHGNNLIAVLAKYIYHRHDPALPRLAIQLLKRLAT
SQ  VAPMSVYACLGSDAAAIRDAFLTRLQSKIEDMRIKVMILEFLTVAVETQPGLIELFLNLEVKDGSNGSKEFSLGVWSCLH
SQ  VVLELIDSQQQDRYWCPPLLHRAAIAFLHALWQDRRDSAMLVLRTKPKFWENLTSPLFGTLSPPSETSEPSVLETCALIM
SQ  KIICLEIYYVVKGSLDQSLKDTLKKFSSEKRFAYWSGYVKSLAVYMADTEGSSCTSLLEYQMLVSAWRILLIIAASHADV
SQ  MHLTDMAVRRQLFLDVLDGTKALLLVAASVNCLRLGSMMCTLLLILLRQWKRELGAVEKILGPLTEILEGVLQADQQLME
SQ  KTKAKVFSAFITVLQMKELRVGDIPQYSQLVLNVCETLQEEVIALFDQTRHSLASDSAAEDKDSMETDDCPRPRHKDQRD
SQ  GVCVLGLHLAKELCEVDEDGDSWLQVTRRLPILPTLLTTLEVSLRMKQNLHFTEAALHLLLTLARTQQGATAVAGAGITQ
SQ  SICLPLLSVYQLSSNGTGQTPSTSRKSLDAPSWPGVYRLSMSLMERLLKTLRYNFLTEALDFVGVHQERTLQCLNAVKTV
SQ  QSLACLEEADHTVGFILQLSHFRKEWHFHLPQLMRDVQVNLGYLCQACTSLLHSRKMLQHYLQNKNGDGLPSAVTPRAQR
SQ  PSTTTTTTTTTTALATPAGCSSKQPTADTEASEQRALHTVQYGLLKILSRTLAALRHFTPDVCQILLDQSLDLAEYNFLF
SQ  ALSFTTPTFDSEVAPSFGTLLATVNVALNMLGELDKKKESLTQAVGLSTQAEGTRTLKSLLMFTMENCFYLLISQAVRYL
SQ  RDPAVHPRDKQRMKQELSSELSTLLSSLSRYFRRGAPSSPAAGVLPSPQGKATSLSKASPESQEPLIQLVQAFVRHVQR
//
ID  F6WXT2;
PN  Nucleoporin NUP188;
GN  nup188;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q5SRE5}.
DR  UNIPROT: F6WXT2;
DR  UNIPROT: A9JRJ6;
DR  Pfam: PF10487;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Required for proper protein transport into the nucleus. {ECO:0000250|UniProtKB:Q5SRE5}.
DE  Reference Proteome: Yes;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAGCLYRRTSRELWTILLGRSSMKDGHQIKAELDRYGDRLLQGLAYYRPPSTSSTGKVKANKNLSPALQELGLRLSKF
SQ  LGLDEEQSVELLQTYLLYDYRGTQESVKGVPQDERQSQALMLKASMVDYYYEERISLLRCVLYILNYFQDDKHPYSAEFS
SQ  KCVEMMEQKELFGKYLKQFESLCREEAPTWETHGNFMTERQVSRWFVQRLREQAMLLEIIFLYFACFAASPSDLLALTKL
SQ  FKEQGFGCRLQNRHLVEPSMDPLVERIGYFSVLIFLEALDIETLMTCSLSDKTEQHPFSSEEQVCKEMDSVLVTLGDAPH
SQ  HGPVLLAWALLRFALNADKVTPTVRKMGSTAIQLHIFQYLTRMLQSLRSGENNCTTSTACLCVYTFLTFVLTNLEEQVLQ
SQ  SQQDLVDTAFQVFAAPNLPDLFWNMEPTAGLGILLDSVVGMFPFHLSPLLKLFTALVSKSSAKKVYSFLDRMSSYTEHYR
SQ  HKPHDILSHEDETLWKRQTPKVLYALGLGQTNLRIPQGTIGQVMADEHGFLVRWEYSYSCWTLFTCEIEMLLHVVSTADV
SQ  IHQCQRVKPIIDLVHKVISTDLSIADCLLPITSRIYMLLQRLTTVMNPPMDFLSSCVDCLAALATRMPAKVWIDLRHTGF
SQ  LPFAANPVSGHIISTEGMNAGGYGSLFGIEQSQGEYSITLSFLRLVTTLVKGQLGSTQSQGLVPCILFVLREMLPNYHRW
SQ  RYNSHGVREQLGFQILSLIHAILNLSPEEEESTSTPNLQSLCIFSLTNTEAGQAVINIMGVGVDTLNAVMLTQAGSSGTE
SQ  GQGQMLMQTIKLAFSITNNVIRLKPLSSAISPLEHALTQHGAHGNNLIAVLAKYIYHKYDPSLPRLAIQLLKRLAMVAPM
SQ  SVYACLGSDAAAIRDAFLSRLRDNIEDMQIKIMILEFLTVAVETQPGLIELFLNLEVKDTNEGSKEYSLGEWSCLQVVLK
SQ  LIDSQDPESSWGAPLLHRSAIAFLHALWQDRRDSAMTVLRTKPNFWENLTSPLFGTLAFPSESSELSILETCAFIMKIIC
SQ  LEIYYAVRGSLGDSLKKILKKFSEEERFTYWSNYVHSLVCQVAESEGACNSLTEYQQLLSAWRMFLMVATHNADVMHLTN
SQ  PEVRQKLFKDVLGGTQALLLVPRSMTCLHLGSMLCTVMIILLRRWKSDLAAPEDILSSLTQILEGVLQKDQQLVEKTKAR
SQ  VFAALISALEIKPMKASEIPQYPQLVLNVCETLQEEVVFLVDHTRQEVPANDASEDKDSMETEDTGRIRQKDQRDGVCVL
SQ  GLHLAKGLCEADEEGDQWQQVLRKLPVLPMLFSALEVSLRIKQNLHFCEAILHFLFTLAKTHQGAAAMAGAGVTQTVCLP
SQ  LLSVYQLSSNGASTAQPALSLRKSLDAPSWPGVYRLTVSLMERLLKTLRYNFLTEALDFVGVHQERILQCLGAVRTVPSL
SQ  ACLEEADHTVGFLLQLSNFTKEWHFHLPQLIKDVQVNLCYLCQACTSLLHSRKMLQHYLQIKNGETMSSTATPRGQRTPQ
SQ  TPSKQPTAESEALELRQLRSVQHSLLKILGKTLATLRAFTPDLCQILQPLDLAQYNLLFALSFTTPAFDADVTPSFGTLL
SQ  ATVNVTLSMLGEMDKKKDHPLGQVLGETNSTVDNKNIKSLLLFIMENCFYLLISQAVRYLRDPSVHPRDKQRMKQELSSE
SQ  LSTLLSSLSRYFRRGGPSSPAGGLMPSPQPKGASAAKVVPEAQEPLIQLVQAFVRHVQR
//
ID  P52593;
PN  Nucleoporin NUP188;
GN  NUP188;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P52593;
DR  UNIPROT: D6W0I1;
DR  PDB: 7N84;
DR  PDB: 7N85;
DR  PDB: 7N9F;
DR  PDB: 7WO9;
DR  PDB: 7WOO;
DR  PDB: 7WOT;
DR  Pfam: PF10487;
DR  Pfam: PF18378;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP188 probably plays an important role in NPC assembly and organization. {ECO:0000269|PubMed:10684247}.
DE  Reference Proteome: Yes;
DE  Interaction: P30822; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P34077; IntAct: EBI-4324997; Score: 0.37
DE  Interaction: P40069; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: Q08959; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P38708; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-809801; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-809801; Score: 0.53
DE  Interaction: P32905; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P05317; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P23641; IntAct: EBI-809801; Score: 0.35
DE  Interaction: Q12134; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-809801; Score: 0.35
DE  Interaction: P53201; IntAct: EBI-853752; Score: 0.35
DE  Interaction: P53877; IntAct: EBI-854143; Score: 0.35
DE  Interaction: P04912; IntAct: EBI-7352971; Score: 0.40
DE  Interaction: Q02486; IntAct: EBI-8221624; Score: 0.22
DE  Interaction: P23291; IntAct: EBI-2614250; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P46988; IntAct: EBI-3738147; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3750975; Score: 0.35
DE  Interaction: Q06677; IntAct: EBI-3758709; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3799853; Score: 0.35
DE  Interaction: Q02629; IntAct: EBI-11888868; Score: 0.37
DE  Interaction: Q02630; IntAct: EBI-11888884; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0031990;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MATPSFGNSSPQLTFTHVANFMNDAAADVSAVDAKQLAQIRQFLKANKTNLIESLNTIRQNVTSSGDHNKLRSTIANLLQ
SQ  INVDNDPFFAQSEDLSHAVEFFMSERSSRLHIVYSLLVNPDIDLETYSFIDNDRFNVVGKLISIISSVIQNYDIITASSL
SQ  AHDYNNDQDMFTIVSLVQLKKFSDLKFILQILQILNLMILNTKVPVDIVNQWFLQYQNQFVEFCRNINSTDKSIDTSSLQ
SQ  LYKFQNFQDLSYLSETLISRISSLFTITTILILGLNTSIAQFDIQSPLYMDTETFDTVNSALENDVATNIVNEDPIFHPM
SQ  IHYSWSFILYYRRALQSSESFDDSDITKFALFAESHDVLQKLNTLSEILSFDPVYTTVITVFLEFSLNFIPITASTSRVF
SQ  AKIISKAPEQFIENFLTNDTFEKKLSIIKAKLPLLNESLIPLINLALIDTEFANFELKDICSFAVTKSSLNDLDYDLIAD
SQ  TITNSSSSSDIIVPDLIELKSDLLVAPPLENENSNCLLSIPKSTKGKILTIKQQQQQQQQQNGQQPPTTSNLIIFLYKFN
SQ  GWSLVGRILQNLLHSYMEKGTQLDDLQHELMISIIKLVTNVVDPKTSIEKSSEILSYLSNSLDTSASTINGASIIQVIFE
SQ  IFEISLQRKDYTSIVQCCEFMTMLTPNYLHLVSSYLNKSDLLDKYGKTGLSNMILGSVELSTGDYTFTIQLLKLTKVFIR
SQ  ESLSLKNIHISKRSKIDIINKLILHAIHIFESYYNWKYNNFLQKFEIAFHLTLIFYDVLHDVFTINPHQKDQLIISSSAN
SQ  KLLQLFLTPMDSIDLAPNTLTNILISPLNTTTKILGDKILGNLYSKVMNNSFKLCTLLIAIRGSNRDLKPSNLEKLLFIN
SQ  SSKLVDVYTLPSYVHFKVQIIELLSYLVEAPWNDDYPFLLSFLGEAKSMAFLKEVLSDLSSPVQDWNLLRSLYIFFTTLL
SQ  ESKQDGLSILFLTGQFASNKKINDESSIDKKSSILTVLQKNSLLLDSTPEEVSCKLLETITYVLNTWTNSKIFIKDPKFV
SQ  NSLLAKLKDSKKLFQKKENLTRDETVSLIKKYKLISRIVEIFALCIYNSTDSNSEILNFLNQEDLFELVHHFFQIDGFNK
SQ  TFHDELNLKFKEKWPSLELQSFQKIPLSRINENENFGYDIPLLDIVLKADRSWNEPSKSQTNFKEEITDASLNLQYVNYE
SQ  ISTAKAWGALITTFVKRSTVPLNDGFVDLVEHFLKLNIDFGSDKQMFTQIYLERIELSFYILYSFKLSGKLLKEEKIIEL
SQ  MNKIFTIFKSGEIDFIKNIGKSLKNNFYRPLLRSVLVLLELVSSGDRFIELISDQLLEFFELVFSKGVYLILSEILCQIN
SQ  KCSTRGLSTDHTTQIVNLEDNTQDLLLLLSLFKKITNVNPSKNFNVILASSLNEVGTLKVILNLYSSAHLIRINDEPILG
SQ  QITLTFISELCSIEPIAAKLINSGLYSVLLESPLSVAIQQGDIKPEFSPRLHNIWSNGLLSIVLLLLSQFGIKVLPETCL
SQ  FVSYFGKQIKSTIYNWGDNKLAVSSSLIKETNQLVLLQKMLNLLNYQELFIQPKNSDDQQEAVELVIGLDSEHDKKRLSA
SQ  ALSKFLTHPKYLNSRIIPTTLEEQQQLEDESSRLEFVKGISRDIKALQDSLFKDV
//
ID  Q9UTK4;
PN  Nucleoporin nup96;
GN  nup189;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: [Nucleoporin nup98]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:26137436}. [Nucleoporin nup96]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:26137436}.
DR  UNIPROT: Q9UTK4;
DR  UNIPROT: A0A0E3VYD1;
DR  UNIPROT: A0A0E4FZX7;
DR  UNIPROT: P78796;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (PubMed:15116432). Nup189 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC (PubMed:26137436). Nup98 as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. Nup96 as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export (By similarity). {ECO:0000250|UniProtKB:P49687, ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:26137436}.
DE  Reference Proteome: Yes;
DE  Interaction: Q10099; IntAct: EBI-1563788; Score: 0.35
DE  Interaction: O74910; IntAct: EBI-904930; Score: 0.37
DE  Interaction: Q9UUE5; IntAct: EBI-1563817; Score: 0.40
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0008233;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0006407;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGQNNSSGFGGGTGAFGQNNQQTGGLFGSNSNTPGNTLFGSQNTSTTGFGQNTTQPLFGSNTNGGLFGNRNNTTTTGGT
SQ  GFGMSSGTGMFGQSNTPAFGGTNNATNPSGGGLFGSNTANNNANTGTSFSFGSNAGSTGFGNTASNTGTGGGLFGSQNNA
SQ  GNTAGNTGFGSQGTGGGLFGSSTTPATTNAFGTSGFVSSNANAVNGTANPPYAVTSEKDPQTNGTSVFQSITCMPAYRSY
SQ  SFEELRLQDYNQGRRFGNASSTNTTSAFGSTPAFGASTTPFGQNLSGTTNNATPFGTSNATNTTPGSGLFGGGSAFGSNT
SQ  TNTGFGSGTNNASGGLFGQNNNTTSTPSTGLFGGSTFNQQKPAFSGFGSTTNTTNTGTGTGLFGSNNATNTGTGQTTGGL
SQ  FGGAATGTGTGFGSSTGGFGSNTNNQPNSGTMGTGLFGFGANNNTANNNTAPTSTFGGNNSSNFSFGANNNAATKPSGFG
SQ  FGSTTTTPASGGFSFGQNANNAPKPAFGSTATTAPKPAGTGLFGGLGAGANTNTATNATGTGGSLFGNANTAGSNMFGSA
SQ  NSSTPGTGLFGSTQTNNATSNTGTGLFGSNNANTTNTGGSLFNKPSTTTGGLFGNTTAQQPSTTTSGLFGASNTNNQAQT
SQ  SNFGTGLFGGSQAGQQQQPLQASIDQNPYGNNPLFSSTTSQVAPTSIQEPIASPLTSKPTPKKAASLPQFWLSPRSHNTA
SQ  RLASISSFAKSAVMNSTSASGKPKSLHLFDSLNDDVLLSADAFTPRQNIKKLVITHKISKDDILQNGVKNGNDAKSDSKV
SQ  QEKAPQNEADGSLKKDEHVVLSDDYWMKPSIEELSKYPKEKLCSVHQFSVGRTGYGQVAFLKPVDLSGFEKLEDIPGKVV
SQ  VFERKICAVYPVEGSSPPLGEGLNVPAIITLEKTWPLSRETREPIKDPQNPRYIQHVKRLHRIKDTEFIDFNDGKWIFKV
SQ  QHFSRYGLLDDEEEENDMSSTSNEAGNLKKYDQPNLKVSGKNDSFVTHHTPGAFPNDSKNKELNRHFLKVDDSAPLDDTF
SQ  MSKKVKLDFSSDSNVSERGDYDDNAKKVDEVISIEKVDGYSKENNVPLSEDDLSNSSESSNESVYSLVEESDASLAADNM
SQ  DIEDISEESDREELSSMRFGAQDFHGLVVTDNWRDQLNLSVQRSALIKAAFPESQSNANLKNSRGIYYNEHDLVTDIFGN
SQ  QNLDTDRPWQSLDKPGAFIPSKFHFTANGSCIYVLKSSDVKIRSIYDFIPTKDPNGTKLLEYQLDQTEVYLDLSGTHAAS
SQ  PRSSMTVKPLSLCSSGYESIVWDLTSILFDPKNYSLPSELSSEAREVLYQKLVRESLSEWITKTLEHETTTLAKEAETSE
SQ  ERIYILLTGNLIGQACEEAVQSQNNRLSTLIPLVNSDVDIQQEVKQQLEEWRKHGDLPFINKFTRLIFELLSGNTDIAEG
SQ  CGTKGDEDYVQSIPITKNMTWLRAFGLKLWYNTDISIGEAMQLYVESLQKFPEIMQKPIATSAVQGIEVYDIIYLLLKAY
SQ  AMGTSLEELTIPESAKCSPLNYRVVWQLAIYLSKARSLCDFSDRVVDINMAEDLKPISVHSDQLTLAYASQLEASGQWLW
SQ  SLFVLLHLENVETRTSTITSCLARNLRGGLGAGAVEMIEKLCIPESWLNEAKALYARYVGDHLNELYFLQEAALYEDAHK
SQ  VLLDTLAPQAVISGNKTQLKKALEGFNGQTDGLASWRFGGQIYSDYLDLLEGNFDANQELKLFTLRKISVALKELNATNL
SQ  LQKAALHKISRFVNALCNEESLTDAICNLPLPLADSLANLQNISVQF
//
ID  G0S4T0;
PN  Nucleoporin NUP192;
GN  NUP192;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P47054}. Note=Cytoplasmic and nucleoplasmic side of the nuclear pore complex in the nuclear envelope (symmetric distribution). {ECO:0000250|UniProtKB:P47054}.
DR  UNIPROT: G0S4T0;
DR  UNIPROT: G0ZGU6;
DR  PDB: 4KNH;
DR  PDB: 5CWV;
DR  PDB: 5HB4;
DR  Pfam: PF11894;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP192 is located to the NPC core at the nuclear membrane and is essential for de novo assembly of NPCs. {ECO:0000250|UniProtKB:P47054}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S024; IntAct: EBI-4325438; Score: 0.73
DE  Interaction: G0S156; IntAct: EBI-4325530; Score: 0.68
DE  Interaction: G0SFH5; IntAct: EBI-4325472; Score: 0.35
DE  Interaction: G0S7B6; IntAct: EBI-4325530; Score: 0.53
DE  Interaction: G0SAK3; IntAct: EBI-16176802; Score: 0.52
DE  Interaction: G0S4X2; IntAct: EBI-16176870; Score: 0.35
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTDLRKLEALQALHAELVAVRQHRFEGLQVLETLLEEQTDAFKALIAKPARDTKDREALGKEPKKLKIGEEEYSLNEDFV
SQ  NDCLKLADELDLNEKESARILIDCDAEGDVETQSRPLWECGVIRFHQERKYLLDCMRLILEIAADEDIDAGLQESFGVAA
SQ  EDKIFGIPPPWERNKENQPTQVKKFIPRCMEAMKGVRSMLQCMADKANARNMLQQASLVRPLDNQETLDFSRLSLVEQHE
SQ  CLASILHAAVQRHHATIADFQDFIKILRKWDKYDHFLIHLIPVLAAYITEFGSPEGMGDLQQARRLNDFICKGGDEDSWA
SQ  LPVLGAAVRAWWIAEHNGFYLDDTVQDLRGINLDEEDEQRTKQFLDALKEGAFDFILSVAADCKAQEWQDPSQLGARQWL
SQ  QRKIPSLPSEPFPFSHFLQHSLMVHLEGFVDATISNLPDVLRKLRTEEDEQRQLRPNHEQDMDLERFLIIISYAYEGRPD
SQ  AAMSFWEDPDSNLAGFLQWASRRASTPLVSAFCEMLRCLADNEECATAAHNFLLDEGHQASGKMKRSQSLTWSQIFKELE
SQ  YFTTKVCSERPNPPQASMHRPGRPGADPAEIEPESALMLECYLRLIAKLATESEIARKRLIMDEDFNLVDTILKLSVGVI
SQ  PHRLRACIFYVLKALMIRKTHEELDAMWRWVEAWMTNPFSSLPGSQGAPQRISFLGQTPGPQECMEMMFREFGTGFEQSN
SQ  AFIQLLTTLLVPPEGLNSLNDSVPFPEWLGSSIRTLGIEPYVDFVFDVFANRTKDISDPSQLRILRLSCLDFVMVCLVTF
SQ  NEDLIVLGHESNISIDDAMAATNLATYVRLHPFSRVMEWLFNEKVITSLINTIHQDPISLGSASPDSPLVVSILRAIQVM
SQ  IKALELQETYLHLVRPEVLRYQGEAGVRRKPVANAAYSAFEDGILSHLSLVVDLGKYCNLGHAELTLACLKLLEKISTSS
SQ  RILSAWSPDSGRLGHRNKAIVQLERNGEGETISASLSASIMATLDPALAASGENYRVKLAILDFLYACLRATPDQPTIAH
SQ  QLLGFHCELSKLGIEPKGPFDMQKSLFHSLLNVLITLTVSEEEQGMRGYLVTLKYRVLRILQLLWKSPLSASLVMDELRA
SQ  TNFLFHMLLREVQIQPQLPWDGQLVTGCEFLLSDASLAYIDYLASRAAIFEYIGKELCSVSQNRIPSIKRQIFDALNGQI
SQ  FVDEEAPLTIPSIFDFFDFINTDYKWEEIPSPHFTYLKDLDLGPCILEHKYAGVHYDIRKAQEILALKRKEYEHSQLATP
SQ  EFLETVELEEKVLIEWLTVRNRANLLLTARLNLLQAWANLLLVMIESNDFKSTPKMAFLLQALQAILPTLEAFSSLKSDE
SQ  AFELARVAKVLLWKLDFSQDSDAGLDREQFTVGNLIGDKLFQLFQLCLSAISQCSGTPELRSLYYSICYRYLTAVVDNDA
SQ  TVAATPASSTIGPTRSVTNARARTLKAITLYGDRLLNVICDDAYGSDTTCQTAAMILLNALVHTSRASSAAGVSPADVDC
SQ  PIIDALNRLNFIGVLVDSLKEILNEWLAPSSTFDPSLSTNASPSLPIPASPSQQYTSAKLALLLQLCQTRQGAKYVLQAN
SQ  LFRALEQSGVFAADPELVEVDSESGVPRVVALERHYALLVALARVVGAAVTARGAHNIVQGRKFLTQHRGLVVHVLKKNA
SQ  GIGGGVVGNSLASSINGGSTATMTRRDEILAQQALEERIEELAEAFMLLITATGFLEYESEQVPSEQPRAHTTFFH
//
ID  P47054;
PN  Nucleoporin NUP192;
GN  NUP192;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Note=Cytoplasmic and nucleoplasmic side of the nuclear pore complex in the nuclear envelope (symmetric distribution).
DR  UNIPROT: P47054;
DR  UNIPROT: D6VWE4;
DR  PDB: 4IFQ;
DR  PDB: 7N85;
DR  PDB: 7N9F;
DR  PDB: 7WOO;
DR  PDB: 7WOT;
DR  Pfam: PF11894;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP192 is located to the NPC core at the nuclear membrane and is essential for de novo assembly of NPCs. {ECO:0000269|PubMed:10428845, ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11121302}.
DE  Reference Proteome: Yes;
DE  Interaction: P32499; IntAct: EBI-6322512; Score: 0.00
DE  Interaction: P34077; IntAct: EBI-789044; Score: 0.55
DE  Interaction: P35729; IntAct: EBI-11888914; Score: 0.37
DE  Interaction: P40066; IntAct: EBI-813993; Score: 0.27
DE  Interaction: P40069; IntAct: EBI-809765; Score: 0.35
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P23641; IntAct: EBI-787315; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-809765; Score: 0.35
DE  Interaction: P38708; IntAct: EBI-809765; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-809765; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-809765; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-809765; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-809765; Score: 0.53
DE  Interaction: P41940; IntAct: EBI-809765; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-809765; Score: 0.35
DE  Interaction: P38737; IntAct: EBI-814203; Score: 0.27
DE  Interaction: Q06625; IntAct: EBI-818204; Score: 0.27
DE  Interaction: P43587; IntAct: EBI-853569; Score: 0.35
DE  Interaction: P47087; IntAct: EBI-854119; Score: 0.35
DE  Interaction: P23291; IntAct: EBI-2614250; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: P32472; IntAct: EBI-2883301; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P10591; IntAct: EBI-3772666; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3790799; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3799861; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3806444; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3812951; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3829248; Score: 0.35
DE  Interaction: Q05166; IntAct: EBI-4392356; Score: 0.55
DE  Interaction: Q02630; IntAct: EBI-11888348; Score: 0.59
DE  Interaction: P49687; IntAct: EBI-11888900; Score: 0.59
DE  Interaction: Q03790; IntAct: EBI-11889050; Score: 0.37
DE  Interaction: P38346; IntAct: EBI-16252276; Score: 0.00
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0046822;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKWSAIPFQTLYRSIESGEFDFDLFKEVLPDLQNLNLNTDKLKNNASRSQLEKGEIELSDGSTFKVNQEFIFEAISLSDE
SQ  LNLDEIVACELILSGDTTANNGKVQYFLRRQYILQIVSFIVNCFHEDTELYQELIKNGALVSNILSAFKFIHTQLSEIKQ
SQ  QINKAQILENYNALFQQNIKFRRDFLLREYDILSQILYGLVDKGAIMKNKDFILSLLHHVSELDSNDFFIIYYTPAFFHL
SQ  FASLRVLPDADVKLLHSQFMKDLKDDSIYTKPVKVALIFIFFAYFIGWCKEDPKRRADTMDFKTDVDEPMTSAVELGAIE
SQ  QILIFAADTSIVEQDKSMELFYDIRSLLERHIPRLIPKQLLDDEKIFSQTTNSTYNPASATDNMSGRGLWNPSYPGMMST
SQ  TGTARLNSMPNNVNEYSYTTIVLSDQTQEFFLSSFDDVLQTIITDCAFLLTKIKDAEEDSLLSGEDLTLDDISLKADLER
SQ  FFLSIYFFYASRPEYSCTFWSDKESNAYGFIEWCSRCNDNLMRSCFYLMVSSLSFGPENALNVYHYFGENSSISWKNIAQ
SQ  CLSDYTKKISNFNSSLHKRQQFSESTHNDIDSTAVALEEGLNEEAVIFLSSLLTLVGSVTYQVDEDVKSSLSKVFSDVLF
SQ  EFTKINTPLVGAAFKVISNLVPKLESSRTKFWSFLDSLIFKDSSLNYSSESYRNAFTNVLTKYSDVLGFLQLFHNLISIH
SQ  SRENNSEYMVFGKLAFPTRLGQGYRKVGIWPYFDYIFNDILAHVDQIVDIRNKRAVQLPILKIIYTGLCSFDYSVILNSI
SQ  PAAANLDALVDCENFFNYVQECPAIPIFNYIFTEKIYKSIFNVVDVGVDQLSIELEGGKNQAELLQLAVKIINKVLDYQE
SQ  TYVEELFPIVKKHGKTDYFLPKNYSLHGLRSFYDAIFFNIPLVAHLGLYVGVDDQILATNSLRILAKLSERSNGSVASLS
SQ  KRNKLLTIFDSVDESARIKDAFITQLESSITDAGVLALKLELLDFLTSNLSNYSRTMTISHLLLGFQVSNVISLGPNLAT
SQ  FISSGTSLLDSLISVLEASLNSITKDNIDYAPMRLATAALEIILKLCRNPLTSGLLYSYLIKENFFERIMILDPQVTRFT
SQ  TWNGSPFDNSTEEKCKNFIESESVGAFLSFLAYRNYWTQYLGLFIHKISFSGTKSEVLTYVNYLISNTMYSVRLFSFLDP
SQ  LNYGNICEPKETLSIFTNVPLNLEQVTLNKYCSGNIYDFHKMENLMRLIKRVRAESLHSNSFSLTVSKEQFLKDADVECI
SQ  KAKSHFTNIISRNKALELNLSVLHSWVQLVQIIVTDGKLEPSTRSNFILEVFGTIIPKISDYIEFNITFSEELVSLAVFL
SQ  FDIYNRDRKLITDKGTVDGRLYQLFKTCIQGINSPLSSVALRSDFYILANHYLSRVLSDQVGSEKVLQDLRLGSKKLVEI
SQ  IWNDVVYGEGTSRVTGILLLDSLIQLANRSKENFILDSLMKTTRLLLIIRSLKNTDALLNSTTEHINIDDLLYELTAFKA
SQ  TVFFLIRVAETRGGASALIENNLFRIIAELSFLKVDPDLGLDLMFDEVYVQNSKFLKVNVTLDNPLLVDKDANGVSLFEL
SQ  IVPIFQLISAVLVSMGSSNKAVVQTVKGLLNTYKRLVIGIFKRDLLREKEDKKNSSDPNNQSLNEMVKLIVMLCTLTGYQ
SQ  NND
//
ID  F4KBW6;
PN  Nuclear pore complex protein NUP205;
GN  NUP205;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4KBW6;
DR  UNIPROT: Q9LU53;
DR  Pfam: PF11894;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0032922;
GO  GO:0009682;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0009617;
GO  GO:0009862;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVSPKDLVAIVHSSLLGTSRPTPTQRIELTHAIRNSFPSLQNLLSFPPPKPSDRAQVQSKEIRLPDSLPISLDDQDIAIS
SQ  LKLSDELHLNEIDSVRLLVSSNQEWGLMGRDPLEIQRLATGLWYTGRRDLTSTLYTLLRAVVLDEGLEPDLIADIQGLLE
SQ  ELIEAGLRQRLITLIKELNREDPTGLGGPLCERYLIDSRGALVERRAVVQRERLILGHCLVLSILVDRPGSKDVKDIYYI
SQ  LKDNAAQLTEGNDTISSQITFSLLFSLIITFVSDAISRLSDKSSMISQDASFRTDFQDIVMASGSDPTADGFIGGIRLAW
SQ  AVHLMLIHDGISGMDTISTASTTDMGHICSCLESIFSKNVFQFLLDNVLRTAAYQNDEEDIIYIYNAYLHKLASCFLSHP
SQ  IARDKVKESKDMAMSVLNSYRTSDPLDGSMQTEESDRPLPFISLMEFKEPELLSGNDVLWTFVNFAGEDHTNFKTLVAFL
SQ  EMLCTLASTQEGASKVYELLRGTSFRSIGWPTLFDCIRIYDEKFKQSLQTAGAMMPEFLEGDAKALVAYLNVLQKVVENG
SQ  NPTERKNWFPDIEPFFKLLGYENIPPYLKGALRKTIAAFVNVFPEMRDSIWAFLEQYDLPVVVGSQVGKSDQSSQVYDMQ
SQ  FELNEVEARREQYPSTISFLNLINALIAGEKDVNDRGRRAYSDPCEKWQLVVACLQHFHMILSMYDIQEEDLDGFTEHPH
SQ  FLVSLETSSLQTQLPIIELLKDFMSGKALYRNLMGILQVGVNSIISERLSKTYGKILEKAVQLSLEILLLVFEKDLLVSD
SQ  VWRPLYQPLDIILSQDHNQIIALLEYVRYDSLPQIQRSSIKIMNILRCSRLVGLVPMLIKIDAANSLIEDYAACLEGRLE
SQ  EGEVVENSCDDLGVLIMQLLVDNINRPAPSITHLLLKFDLDAPVEGTVLQPKFHYSCLKVILEMLEKLPNPDINFLLFEF
SQ  GFQLLCELNLDPLTSGPTMDLLSSKKYQFFLQHLDTIGVATLPKRSGSQALRISSLHQRAWLLKLLAIALHTGSGSSSAH
SQ  LEACQSILSHLFGREVTEAANEPFSSSTYPQDGLDYAGTSSISKSKALALLEILQFRSPDASMQLPQIVSSLKYDSLVED
SQ  ILGNRDTSVSGSIYYYSERGDRLIDLSSFSNKLWQKLHSGFPLVDSFPNVAELSEVRETIQQLLKWGWKYNRNLEEQAAQ
SQ  LHMLAGWSQIVEVSACRRISSLDNRSEILYRILDASLSASASPDCSLKMAFVLTQVALTCIAKLRDDRFSFQGALSSDTV
SQ  TCLDVMMVKHLSTGACHSVLFKLVMAILRHESSESLRRRQYALLLSYFQYCQHMIALDVPTSVVQFLLLNEQDGEDLDIQ
SQ  KIDKEQADLARANFFIIKKEAQGILDLVIKDASQGSEFGKTISLYVLEALVCIDHERYFLSQLQSRGFIRSCLGSISNIS
SQ  YQDGTHLLESQQRACTLEAELALLLRISHKYGKSGGQVLFSMGALEHIASCRAISFKGNMRRVDMKLQSDVGYNVQKQRT
SQ  IITAVLRLVFALTSLVETSEFFEGRNKIVRDVVEFIKGHQSLFDQLLREDFTQADDLLMEQIILAVGILSKVWPFEENDG
SQ  YGFVQGLFDMMSKLFIASPIKSILSQGSELKLSQLRFSLTSYLYFLVTKNSLRLQVSDDSLDSSTKLRQPTLLLLASLLS
SQ  HVTDSLERAAEKKSLLLHKIRDINELSRQDVDAIIKICDSQEYVTPSDNIHKRRYIAMVEMCQIVGNRDQLITLLLQLAE
SQ  HVLNIILIHLQDRSVSSNERGSYGSKSHIQQEVTDLCGKLSPTIDRLALLNEGKVGHNLKVFQRLATTVKEMAIQKCV
//
ID  Q8IQV9;
PN  Nuclear pore complex protein Nup205;
GN  Nup205;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q92621}.
DR  UNIPROT: Q8IQV9;
DR  UNIPROT: B6IDH1;
DR  UNIPROT: Q3YMV0;
DR  UNIPROT: Q8MSV6;
DR  UNIPROT: Q9VWB8;
DR  Pfam: PF11894;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and maintenance, but with limited role in NPC permeability. Required for specific nuclear import pathways such as Mad import. {ECO:0000269|PubMed:20547758}.
DE  Reference Proteome: Yes;
DE  Interaction: Q960X8; IntAct: EBI-509966; Score: 0.37
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: O97159; IntAct: EBI-9918568; Score: 0.35
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0042332;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDGECLANEQMCVGRQITNATHASTAVIEDMWTPYKHLYNTFQTAVSNRSGFTSDLEQCLKKYKHNFSNLLRNPPRSEKS
SQ  RNLLRNALNEGVPMQGHSRKTKMSQDLADEAVILSDMFDLDEGFAVELLCTAQRQQKHHPGLSRGLVAVLLYYDGRKAIS
SQ  CTLRDMFQVVSGVSWNTELPKEITGLVTNYAESLVDGSGILGRLLQLLEEMDVDKECAMLTTNRAFGSKKHQNQVLGLYE
SQ  DIQQALAMALFNWSAQRGLPRHIAIRLMHQLANRKNHDAGGNMDDVTLIMLMALLYAYDTSMLLVTEEPNEHTTRLPIFS
SQ  DREFAECFLEELYAQSSWQAPRLNAIIAYSFGLTLASLRHAPLQLQATAISIINRDEMLIDEALGAQVFVFFHSLLLEKD
SQ  LVYSTQFFYRRVHLLITDFIDFMNSKVSELRGRADESSHTIISFLNEGLEPPPNLDSNFELLMLCVAKMHGDPRVTIRLC
SQ  NEYWGPGDPNGSTAFKNTSRSVSLFKFISLASDLLPQTLFKAYLKMISGLTRTDFSARCAFNMLRVPQMATGGKYAVSWD
SQ  HFFTTLGNYYTSMRNDFNTNIGMSGETIYRTRSTPKAITQREAEHLVAVMGIIQAVAEHDEVSRIMICDHPNWQTPQVLL
SQ  GLVACATPLFLKAEILHTLAALAKSKETARVIWFHLEASQIIPTVPVSRSYAQCSLLEEMEQIESRSEQYNLTRGILQLL
SQ  YTLMTTNLPKSLGAGQRTPAYEGYLKSMINSVLLKFYNRAYKVPSEKWQVGAQCLKLLYYLLATYRPSAMDFLETVDEPP
SQ  YPGFHVMMQLQLKSEMLQLLLCIVEEVRERLDNYNRFQGKKLLEECSLYALLILEAALAKQNAFFEAHSAANCPILLSGL
SQ  NRMLLDLNPRSRKPDHVLNIIKYVTYNSWLPRHALAAIKILASVTQLPNVSTQILSMYGQGSNEKLEIRQGFVECLEMEV
SQ  CVGKHDDDLLDQLALNNHVPYLGFGDDLDNEREMSGEREYSTIESQLELQAGDGALESKPASIELQLKEAIIKLFEMNLS
SQ  QQLPNFVYFLLGVDVLREFMANGRQHLAIEMQSSCVNSVVLLLEKYMDKQRHSDKYCEHTARIVERIYHLFHGLCANRRT
SQ  AETILRYFRLTCSDFLLRHLRSLPFRQHREDHVLHAMGHLLNCVSIDVKLAAKHGQMTRFNQMCDILLIGNGMERSSHGL
SQ  SMELGHSLISQPSSSFLAMDVLPAGGSISAVAHGAGSASLGAPNTGVKSLKPSLLQETSQGLHVTRLLDILVLEAGTLSQ
SQ  PQLEFFDGHLITQLLRDCEASAEAGANSRANLINVRKLYYILTDELYMVQSIIASGQRKAISTEIMLLLNHAVNINRVRT
SQ  QRCATLAFMAAWGQLVQVLFSNMPDAVLPATQRRQHIIDIVEKVLIKVQPIQPIIEISVQVSETVLLLLANLRYCCYQAE
SQ  DQSPEDLAAEDSLSNGNGNAIGNDSQVNALCLGQRAIGTGSDGGSGGGRDIGSGGNSSNLRFILKNLVQWIMISEVKSQK
SQ  LRINLYSSLLNCLRIAKRLRTDEHLEYQETLISRQESARTYNKEQRRDDRLRLKAMAAEVIGTFGEKLIDTICHDAVTGH
SQ  DVCRMLALACLDMISELQAVSTLCDFVASRGYLKHILESLDQSSTALCGILQPVPDHLRPLYVYESRMAFLTRMANSNVG
SQ  ARLLLTEQALGVLSNMKVYDQQPDLKSSELNRNEPQTFLPSIDDRFRSILLPALSLCDAIVNSLGPRNNSAAVQVLNFLF
SQ  AHIDMVEAMLRSATPYMDLGHLQQVAVISNLFARASTHELTALEDSVQLDLRNRLGRVQQLMIVVFGRFCVSEPTIRRML
SQ  QQDEEQQTNPTDDSKRLRVKYFLDIAANVSLYCRNVVTSHSKDSMTSKYLLTTVINDVTLLTGKMSSKKLTTIMHTILNQ
SQ  LKGSIGYYLSQKSIADNLLQQRASLPNISFGPNGKQSYIELSQRYNEKRSELRQAVFIAEQNLYLLWIHLDFYLRNTIDY
SQ  ANENRNAINESNMDDDNDMSVLNASQEEIVQLKQLLISTFNETFCTQLINASEDYSIKCKGFNGSLLRRIKALVQFAPIT
SQ  ANDVNSSFDS
//
ID  Q92621;
PN  Nuclear pore complex protein Nup205;
GN  NUP205;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283}; Peripheral membrane protein {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:9348540}. Note=Localized near the center, on both the cytoplasmic and nuclear side, of the NPC core structure. {ECO:0000269|PubMed:15229283}.
DR  UNIPROT: Q92621;
DR  UNIPROT: A6H8X3;
DR  UNIPROT: Q86YC1;
DR  PDB: 5IJN;
DR  PDB: 5IJO;
DR  PDB: 7PER;
DR  Pfam: PF11894;
DR  OMIM: 614352;
DR  OMIM: 616893;
DR  DisGeNET: 23165;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:9348540). May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC (PubMed:15229283). {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:9348540}.
DE  Disease: Nephrotic syndrome 13 (NPHS13) [MIM:616893]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. {ECO:0000269|PubMed:26878725}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O40955; IntAct: EBI-6378072; Score: 0.35
DE  Interaction: O75694; IntAct: EBI-26588212; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P50613; IntAct: EBI-16789709; Score: 0.27
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: P01106; IntAct: EBI-1062401; Score: 0.00
DE  Interaction: Q13418; IntAct: EBI-1065563; Score: 0.00
DE  Interaction: Q9Y5V3; IntAct: EBI-1070012; Score: 0.00
DE  Interaction: Q99623; IntAct: EBI-1071721; Score: 0.00
DE  Interaction: Q9Y5J5; IntAct: EBI-1072662; Score: 0.00
DE  Interaction: Q70EL3; IntAct: EBI-2512984; Score: 0.40
DE  Interaction: Q92731; IntAct: EBI-2880601; Score: 0.53
DE  Interaction: Q13286; IntAct: EBI-3248480; Score: 0.35
DE  Interaction: Q9NYD6; IntAct: EBI-3917475; Score: 0.37
DE  Interaction: P09651; IntAct: EBI-6081585; Score: 0.35
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6190694; Score: 0.53
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P20963; IntAct: EBI-9512492; Score: 0.35
DE  Interaction: Q99853; IntAct: EBI-11317404; Score: 0.35
DE  Interaction: Q6ZQN5; IntAct: EBI-11318220; Score: 0.35
DE  Interaction: Q12952; IntAct: EBI-11318689; Score: 0.35
DE  Interaction: P58012; IntAct: EBI-11318924; Score: 0.35
DE  Interaction: Q9C009; IntAct: EBI-11319301; Score: 0.35
DE  Interaction: P55316; IntAct: EBI-11320867; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q6ZU80; IntAct: EBI-11370150; Score: 0.27
DE  Interaction: Q7Z7A1; IntAct: EBI-11371427; Score: 0.27
DE  Interaction: Q2MV58; IntAct: EBI-11384104; Score: 0.27
DE  Interaction: Q9UPV0; IntAct: EBI-11399201; Score: 0.27
DE  Interaction: P27105; IntAct: EBI-12452286; Score: 0.51
DE  Interaction: P06821; IntAct: EBI-12577493; Score: 0.35
DE  Interaction: P0C0U1; IntAct: EBI-12579831; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-12579395; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581451; Score: 0.35
DE  Interaction: C5E519; IntAct: EBI-12583021; Score: 0.35
DE  Interaction: C5E526; IntAct: EBI-12584472; Score: 0.35
DE  Interaction: C5E527; IntAct: EBI-12585279; Score: 0.35
DE  Interaction: Q20MH8; IntAct: EBI-12586007; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12588098; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12588729; Score: 0.35
DE  Interaction: P56180; IntAct: EBI-14025693; Score: 0.35
DE  Interaction: P36876; IntAct: EBI-16121020; Score: 0.35
DE  Interaction: Q6VGT1; IntAct: EBI-16121020; Score: 0.50
DE  Interaction: P04618; IntAct: EBI-16121072; Score: 0.40
DE  Interaction: Q99152; IntAct: EBI-16121180; Score: 0.40
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-16786806; Score: 0.27
DE  Interaction: Q96GD4; IntAct: EBI-16787973; Score: 0.27
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P49336; IntAct: EBI-16790360; Score: 0.27
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: P22087; IntAct: EBI-16792282; Score: 0.27
DE  Interaction: P49841; IntAct: EBI-16793176; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: P62491; IntAct: EBI-16797971; Score: 0.27
DE  Interaction: P20339; IntAct: EBI-16798221; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: P62753; IntAct: EBI-16798663; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: Q71U36; IntAct: EBI-16799955; Score: 0.27
DE  Interaction: P37268; IntAct: EBI-20916624; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: Q14CB8; IntAct: EBI-25409097; Score: 0.35
DE  Interaction: Q86YR7; IntAct: EBI-25410124; Score: 0.35
DE  Interaction: Q6ZRI8; IntAct: EBI-25410669; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P59635; IntAct: EBI-25688593; Score: 0.35
DE  Interaction: Q997F1; IntAct: EBI-25747061; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-26399642; Score: 0.35
DE  Interaction: Q8TB24; IntAct: EBI-26518569; Score: 0.35
DE  Interaction: Q96QK1; IntAct: EBI-27081124; Score: 0.35
DE  Interaction: Q6J9G0; IntAct: EBI-28941708; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
DE  Interaction: Q8TDD2; IntAct: EBI-29000537; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P21709; IntAct: EBI-32720516; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
DE  Interaction: P35968; IntAct: EBI-32723270; Score: 0.27
DE  Interaction: Q12866; IntAct: EBI-32723870; Score: 0.27
DE  Interaction: P08922; IntAct: EBI-32731758; Score: 0.27
DE  Interaction: Q02763; IntAct: EBI-32732012; Score: 0.35
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MATPLAVNSAASLWGPYKDIWHKVGNALWRRQPEAVHLLDKILKKHKPDFISLFKNPPKNVQQHEKVQKASTEGVAIQGQ
SQ  QGTRLLPEQLIKEAFILSDLFDIGELAAVELLLAGEHQQPHFPGLTRGLVAVLLYWDGKRCIANSLKALIQSRRGKTWTL
SQ  ELSPELASMTTRFTDELMEQGLTYKVLTLVSQIDVNNEFEKLQRERGLGSEKHRKEVSDLIKECRQSLAESLFAWACQSP
SQ  LGKEDTLLLIGHLERVTVEANGSLDAVNLALLMALLYCFDISFIEQSTEERDDMIHQLPLLTEKQYIATIHSRLQDSQLW
SQ  KLPGLQATVRLAWALALRGISQLPDVTALAEFTEADEAMAELAIADNVFLFLMESVVVSEYFYQEEFYIRRVHNLITDFL
SQ  ALMPMKVKQLRNRADEDARMIHMSMQMGNEPPISLRRDLEHLMLLIGELYKKNPFHLELALEYWCPTEPLQTPTIMGSYL
SQ  GVAHQRPPQRQVVLSKFVRQMGDLLPPTIYIPYLKMLQGLANGPQCAHYCFSLLKVNGSSHVENIQGAGGSPVSWEHFFH
SQ  SLMLYHEHLRKDLPSADSVQYRHLPSRGITQKEQDGLIAFLQLTSTIITWSENARLALCEHPQWTPVVVILGLLQCSIPP
SQ  VLKAELLKTLAAFGKSPEIAASLWQSLEYTQILQTVRIPSQRQAIGIEVELNEIESRCEEYPLTRAFCQLISTLVESSFP
SQ  SNLGAGLRPPGFDPYLQFLRDSVFLRFRTRAYRRAAEKWEVAEVVLEVFYKLLRDYEPQLEDFVDQFVELQGEEIIAYKP
SQ  PGFSLMYHLLNESPMLELALSLLEEGVKQLDTYAPFPGKKHLEKAVQHCLALLNLTLQKENLFMDLLRESQLALIVCPLE
SQ  QLLQGINPRTKKADNVVNIARYLYHGNTNPELAFESAKILCCISCNSNIQIKLVGDFTHDQSISQKLMAGFVECLDCEDA
SQ  EEFVRLEEGSELEKKLVAIRHETRIHILNLLITSLECNPPNLALYLLGFELKKPVSTTNLQDPGVLGCPRTCLHAILNIL
SQ  EKGTEGRTGPVAVRESPQLAELCYQVIYQLCACSDTSGPTMRYLRTSQDFLFSQLQYLPFSNKEYEISMLNQMSWLMKTA
SQ  SIELRVTSLNRQRSHTQRLLHLLLDDMPVKPYSDGEGGIEDENRSVSGFLHFDTATKVRRKILNILDSIDFSQEIPEPLQ
SQ  LDFFDRAQIEQVIANCEHKNLRGQTVCNVKLLHRVLVAEVNALQGMAAIGQRPLLMEEISTVLQYVVGRNKLLQCLHAKR
SQ  HALESWRQLVEIILTACPQDLIQAEDRQLIIRDILQDVHDKILDDEAAQELMPVVAGAVFTLTAHLSQAVLTEQKETSVL
SQ  GPAEAHYAFMLDSCFTSPPPEENPLVGFASIGDSSLYIILKKLLDFILKTGGGFQRVRTHLYGSLLYYLQIAQRPDEPDT
SQ  LEAAKKTMWERLTAPEDVFSKLQRENIAIIESYGAALMEVVCRDACDGHEIGRMLALALLDRIVSVDKQQQWLLYLSNSG
SQ  YLKVLVDSLVEDDRTLQSLLTPQPPLLKALYTYESKMAFLTRVAKIQQGALELLRSGVIVRLAQCQVYDMRPETDPQSMF
SQ  GMRDPPMFIPTPVDRYRQILLPALQLCQVILTSSMAQHLQAAGQVLQFLISHSDTIQAILRCQDVSAGSLQELALLTGII
SQ  SKAALPGILSELDVDVNEGSLMELQGHIGRFQRQCLGLLSRFGGSDRLRQFKFQDDNVEGDKVSKKDEIELAMQQICANV
SQ  MEYCQSLMLQSSPTFQHAVCLFTPSLSETVNRDGPRQDTQAPVVPYWRLPGLGIIIYLLKQSANDFFSYYDSHRQSVSKL
SQ  QNVEQLPPDEIKELCQSVMPAGVDKISTAQKYVLARRRLVKVINNRAKLLSLCSFIIETCLFILWRHLEYYLLHCMPTDS
SQ  QDSLFASRTLFKSRRLQDSFASETNLDFRSGLAIVSQHDLDQLQADAINAFGESLQKKLLDIEGLYSKVRSRYSFIQALV
SQ  RRIRGLLRISRN
//
ID  Q17602;
PN  Nuclear pore complex protein 14;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P35658}. Nucleus membrane {ECO:0000269|PubMed:27723735}; Peripheral membrane protein {ECO:0000305|PubMed:27723735}. Note=Cytoplasmic side of the nuclear pore complex (By similarity). Co-localizes with caspase ced-3 to the perinuclear region in germ cells. {ECO:0000250|UniProtKB:P35658, ECO:0000269|PubMed:27723735}.
DR  UNIPROT: Q17602;
DE  Function: May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex (By similarity). Plays a role in apoptosis by tethering caspase ced-3 to the nuclear membrane preventing its autoprocessing in absence of ced-4. {ECO:0000250|UniProtKB:P35658, ECO:0000269|PubMed:27723735}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0089720;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:1990001;
GO  GO:0051028;
GO  GO:1900118;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:27723735};
SQ  MSNEDVAEDVSQVTDFHFHTCRKFRLFSSKSDGYSQNEINIRNRVATSSQLGVTFVTVNSNQLSCFHTKSLLGYKITREN
SQ  MNVEVTDLPIKTIRLHGVVLINDMGVNSDGTVLGVLHTKNNDVSVDVFDIKKICTSSSIEPFKPLCTTRVGTEQINQGSC
SQ  LEWNPAFPDTFAASSTDRSILVAKINVQSPANQKLVGIGKFGAVTTAISWSPKGKQLTIGDSLGKIVQLKPELEVVRSQH
SQ  GPENKPNYGRITGLCWLATTEWLVSLENGTDQDAYLMRCKKDKPTEWIQFHELSYSSSKWPLPPQLFPATQLLVDWNVVI
SQ  VGNSKTSEISTVGKRDDWQTWVPVEGESIYLPTTSSGKDTVPIGVAVDRSMTDEVLLNPDGSQRHRPSPLVLCLTNDGIL
SQ  TAHHIISTFAAHIPCQMSSQNLAINDLKKLQFDSQKPISAPPSDQTPVTKPSTVFGQKPEAETLKSSLVGSPSSVQTPKP
SQ  SSSLFNPKSIASNIETSQLTESKPSTPAAPSSQPKIASTPKSEAIPKISDKTLEHKKAELIATKKQVLIERMDKINDSMA
SQ  GAKDATMKLSFAVGKVKTTIMECADVVRASLGDSKEVMDELKNLILSIERMSDRTQHTVKEMDFEIDEKMELVAGVEDGN
SQ  QVLEKLRNMSETEKLMRFNKLETAADLLNGKYEECSDLIKKLRMSLSEKESLRKQAILSPLRLSSNLNQLRSGSETELAL
SQ  KVMRNVSKIIMDTREQIQRTELEFVRFQRDVKFQNFKKGKENLNFTQPLEMSSLDGDAPQGKSLTDAESIKVRQALVNQI
SQ  QKRGIVKTRNVIVESYKKSENSAAMKNDLLDTSNLSNAILKLSMTPRRVMPSSSLFSASPSTPSTKSDAATQADEPPIVK
SQ  TVVVTVESPAKPIASAPAVSSPLIKLNTTTATTTMTTPKVTVPKEEANKTQDQKPIISTPASSSIFSSGSLFGTKTQTPL
SQ  VSKEESTLTTGVPSLINSSLSISPQEIEKASSKVETLNKTEEVKDEKSENEVTPDLKSEEPKSLETKVKEEPKPAVQTPV
SQ  KEEETGSNIQKTPSFSFNSTTTPKSTSSTSSIFGGGLKTQTPSSSNSTNIFGARTTTTATPTPASNTSSIFGGGSKAASS
SQ  PFGSFGQAGCQPAKTSNPATSTASVTFSFNTGATSASAKPAGFGSFGAGASAKPSSVFGGSVTAPTVPNVDDGMEDDSMA
SQ  NGGGSGGFMSGLGNARTSNTSGGNNPFAPKTSTGTSASSSSWLFGGGGNQQQQQQQKPSFSFNTAGSSAQQASAPATGTS
SQ  SVFGGAPKFGSQPAFGAKPFGGGANAGLSKNASIFGGATSSTTNNPATGGFAQFASGQKTSSLFGGGATPQTNTSIFGGG
SQ  ANTTPAPTSSVFGGGASANANKPTSFTSWR
//
ID  Q9W1X4;
PN  Nuclear pore complex protein Nup214;
GN  Nup214;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:20547758}. Nucleus membrane {ECO:0000269|PubMed:17032737}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:20547758}. Note=Localization to the nucleus membrane depends on mbo/Nup88. {ECO:0000269|PubMed:17032737}.
DR  UNIPROT: Q9W1X4;
DR  UNIPROT: Q8T3K4;
DE  Function: Part of the nuclear pore complex (PubMed:14638854). Serves as a docking site in the receptor-mediated import of substrates across the nuclear pore complex including emb, RanGAP and phosphorylated Mad (PubMed:17682050, PubMed:20547758, PubMed:17032737). Protects mbo/Nup88 from proteasomal degradation at the nuclear pore (PubMed:17032737). Together with mbo/Nup88, sequesters emb in the cytoplasm and thereby attenuates nuclear export signal (NES)-mediated nuclear export (PubMed:17032737). Together with mbo/Nup88, required for the nuclear import of the Rel family transcription factors dorsal (dl) and Dorsal- related immunity factor (Dif) and the activation of an immune response (PubMed:17032737). {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:20547758}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VT59; IntAct: EBI-206919; Score: 0.00
DE  Interaction: P19339; IntAct: EBI-268108; Score: 0.00
DE  Interaction: P40798; IntAct: EBI-270189; Score: 0.00
DE  Interaction: Q9XTM1; IntAct: EBI-510204; Score: 0.37
DE  Interaction: P22469; IntAct: EBI-7377284; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0046826;
GO  GO:0046833;
GO  GO:0006606;
GO  GO:0090204;
GO  GO:0006405;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAQNAPDCEDTQDFQFKLHHKIVAFKKCGEPRSNVNLLAVSSSRGLLFAGSPTQPELKVIIVKDLVNAKSTAQQPQARLV
SQ  PLPSIPNYIACSSDGNLLAVNHTQNGTSLLSIYAVLSFMTPDVRPVYNIRLAAEDHVHGVQLLWNPVLPNSLAVVLSNGA
SQ  LAMYALKEGGNFEMHSLDKNQQVKCGCWSPKGKQIVLGFPGGTVKQFKPDLTLAKTLLCPPNIHDAPFDTIAIQWLSTFQ
SQ  FAVIFLQHGEDCSPSLYILNAPKAGAPSYINYYDICYSMNGPRNHQFVFSHVPQWNLLLVVSANGVEVGIMRSTEAGDTP
SQ  AWQQLTLLDEARIEMPLSEDKDETFPLGFAFDTSTTHQLTINEKKLQTMPMVHVLSSDGELLSFNFLNVLPTAVSVCSPP
SQ  PPVADTSGQFKPLNMLLASEEEEQPAWAASPSKAPAATPAASSDISFAFTPNTVTSTPAPSKDKQPSLFSGFGAAAAKAP
SQ  APQLSFGTAPTSSPVSFGAPTTNAAKPTTPFGGFGTQATTTAMGSMFSASGANAFGGMALNKPAIASVTPRTAAPGSTVP
SQ  ATPASAPANKPLYTVPLTFTPVDTKPATSAPPQIADESLKPDDTEPIIKDMIALQIEAFSKDIQKQKEQTKELLKGIAAP
SQ  SALRAYAKRLDDLQELNEQAKDVEFELDVQGLRQGLNEAYAIVAECRGKLEIYRKPEITRLMNSSSCDPSGRRMLARLQS
SQ  YVAANEAQLRLAQQHVDLQWEQFQDVVRRNSKSRMHMPCLEGIYQRLTRLQNLTSNQRIVQNNIKSKLKERGLLQAALLD
SQ  QEKSRTRTNEAVDTLTDSILTMSLSQVVDSNAAKLTRERLQKIRNIVQLQKINVICPQRPDRVGLKSEVILETKRRAEQI
SQ  KRAAAKPATANKYTQAAVAPPSPPDVAPTPAVAPMPQATVTVAPPLPKPMPSIPSVVEKPGVPTHPTTPVATPFSFSQSI
SQ  PFVKTSTVTPTTNTVTPGEAAKPGLSIFGGSTISSFSFGGGAAKSALSFGTGSPAVAAPTPKPNPLSAVEKPTPEPTKPK
SQ  EQKAAESKEFKAVQPETEESKVPQKPKAETENKSFGFGGFTGTGGTVGNTSSSPFSFGGLGSSLGFGGTAAAVPKSEPSS
SQ  TATTSVATSASTAPFGIFSAALAKPSNSEPITTVTSNTTTITSKPTNVIASSSVTDAPSVTTTNAVTSSTDPIGGLFSSV
SQ  TICKPNTPADTTKPANIFGGGLSAGSFSFGGTIDASKGLFGSTKPVATAPTSVTEANNKTDPISTTPSAISTTTATTTVS
SQ  SPAVVPAAVTAAVPATSSTTVTSSTAVPGSAFSFSNAFSTLSAGGAAAPTTSASAPLAAKSPTATSTGNNSSNSVFGGGF
SQ  AVATSTAAPVASPFQSAAKSPVSSANIFGSIPKAETSVFGGATTAPSNTTAAATPDAPPAGLFASAAISNPSPFGSPTTR
SQ  APASGGNIFGQAVKPSVFGQPAQAGDSGGSIFGGGSASTPFGSSSIFGGGNTQGAVGAPAAGSTSIFGQKVFGQSSAAAP
SQ  AAGGNIFSNPVGSPQASPFGGGGNSIFGSPATAPPASGGSIFGGGSSSGGFGSFTQTTPAQGGFGGGFGQGGGGSVAQTG
SQ  FGSPQAPQQQTTTPGGFGAKPVFGGSPAFGASPTFGGGATFGSPKGFGGFGGASPVASPPPFGAAAKPAQGNIFETLGGQ
SQ  ESGLSFGNLAQTGNSNAQKPAFGGSSFMNYR
//
ID  P35658;
PN  Nuclear pore complex protein Nup214;
GN  NUP214;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:8108440}. Note=Cytoplasmic side of the nuclear pore complex. {ECO:0000269|PubMed:8108440}.
DR  UNIPROT: P35658;
DR  UNIPROT: A6NFQ0;
DR  UNIPROT: Q15010;
DR  UNIPROT: Q3KQZ0;
DR  UNIPROT: Q5JUP7;
DR  UNIPROT: Q75R47;
DR  UNIPROT: Q86XD3;
DR  PDB: 2OIT;
DR  PDB: 3FHC;
DR  PDB: 3FMO;
DR  PDB: 3FMP;
DR  PDB: 5DIS;
DR  Pfam: PF18617;
DR  OMIM: 114350;
DR  OMIM: 618426;
DR  DisGeNET: 8021;
DE  Function: Part of the nuclear pore complex (PubMed:9049309). Has a critical role in nucleocytoplasmic transport (PubMed:31178128). May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex (PubMed:31178128, PubMed:8108440). {ECO:0000269|PubMed:31178128, ECO:0000269|PubMed:9049309, ECO:0000303|PubMed:8108440}. (Microbial infection) Required for capsid disassembly of the human adenovirus 5 (HadV-5) leading to release of the viral genome to the nucleus (in vitro). {ECO:0000269|PubMed:25410864}.
DE  Disease: Note=A chromosomal aberration involving NUP214 is found in a subset of acute myeloid leukemia (AML); also known as acute non- lymphocytic leukemia. Translocation t(6;9)(p23;q34) with DEK. It results in the formation of a DEK-CAN fusion gene. {ECO:0000269|PubMed:1549122}. Note=A chromosomal aberration involving NUP214 is found in some cases of acute undifferentiated leukemia (AUL). Translocation t(6;9)(q21;q34.1) with SET. {ECO:0000269|PubMed:1630450}. Encephalopathy, acute, infection-induced, 9 (IIAE9) [MIM:618426]: An autosomal recessive disorder characterized by infancy- onset of episodic neurodevelopmental regression in association with infection-induced febrile illness. Clinical features include poor overall growth, seizures, myoclonic jerks, microcephaly, ataxia, and cerebellar atrophy. {ECO:0000269|PubMed:30758658, ECO:0000269|PubMed:31178128}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Note=Chromosomal aberrations involving NUP214 are found in acute lymphoblastic leukemia (PubMed:20851865, PubMed:15361874). Translocation t(9;9)(q34;q34) with ABL1 (PubMed:15361874). Translocation t(5;9)(q35;q34) with SQSTM1 (PubMed:20851865). {ECO:0000269|PubMed:15361874, ECO:0000269|PubMed:20851865}.
DE  Reference Proteome: Yes;
DE  Interaction: P0DTD1; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: Q9UBU9; IntAct: EBI-7193202; Score: 0.69
DE  Interaction: P01857; IntAct: EBI-1222317; Score: 0.35
DE  Interaction: Q6UXB4; IntAct: EBI-2117445; Score: 0.00
DE  Interaction: Q9UN86; IntAct: EBI-2514381; Score: 0.40
DE  Interaction: Q13283; IntAct: EBI-2514311; Score: 0.56
DE  Interaction: P24386; IntAct: EBI-2515120; Score: 0.40
DE  Interaction: Q80U93; IntAct: EBI-2555228; Score: 0.40
DE  Interaction: Q07832; IntAct: EBI-2560950; Score: 0.40
DE  Interaction: Q5NFS5; IntAct: EBI-2797276; Score: 0.00
DE  Interaction: Q5NGV7; IntAct: EBI-2804214; Score: 0.00
DE  Interaction: A0A2P0HLN8; IntAct: EBI-2812754; Score: 0.00
DE  Interaction: Q81KT8; IntAct: EBI-2828524; Score: 0.00
DE  Interaction: A0A0H2W2I9; IntAct: EBI-2846236; Score: 0.00
DE  Interaction: Q8D1L8; IntAct: EBI-2862398; Score: 0.00
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-3437321; Score: 0.00
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q9J0X9; IntAct: EBI-10766007; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q6ZQH8; IntAct: EBI-10997801; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-30827243; Score: 0.44
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q67020; IntAct: EBI-11514526; Score: 0.37
DE  Interaction: P03508; IntAct: EBI-11521091; Score: 0.37
DE  Interaction: Q0A2H1; IntAct: EBI-11521490; Score: 0.37
DE  Interaction: Q2PJP1; IntAct: EBI-11521674; Score: 0.37
DE  Interaction: Q6DP94; IntAct: EBI-11521853; Score: 0.37
DE  Interaction: Q20P38; IntAct: EBI-11521948; Score: 0.37
DE  Interaction: Q3SBS5; IntAct: EBI-11522027; Score: 0.37
DE  Interaction: E5LBS6; IntAct: EBI-14062727; Score: 0.35
DE  Interaction: Q9GZY0; IntAct: EBI-21528397; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: Q9Y6C2; IntAct: EBI-21562772; Score: 0.35
DE  Interaction: Q9NUU7; IntAct: EBI-21587900; Score: 0.35
DE  Interaction: P51116; IntAct: EBI-21628052; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-20936668; Score: 0.40
DE  Interaction: P05120; IntAct: EBI-21713063; Score: 0.35
DE  Interaction: Q9UMR2; IntAct: EBI-15757014; Score: 0.78
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q9GZM8; IntAct: EBI-21389370; Score: 0.00
DE  Interaction: Q3KR16; IntAct: EBI-25408244; Score: 0.35
DE  Interaction: Q9Y4F1; IntAct: EBI-25408475; Score: 0.35
DE  Interaction: Q15811; IntAct: EBI-25410025; Score: 0.35
DE  Interaction: Q63358; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: A0A0H3LN59; IntAct: EBI-25401114; Score: 0.35
DE  Interaction: P0DTC6; IntAct: EBI-26495724; Score: 0.35
DE  Interaction: Q13627; IntAct: EBI-26367331; Score: 0.35
DE  Interaction: P59634; IntAct: EBI-26377272; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574619; Score: 0.35
DE  Interaction: Q96LU5; IntAct: EBI-27050332; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P11274; IntAct: EBI-28931791; Score: 0.35
DE  Interaction: P42680; IntAct: EBI-28935138; Score: 0.35
DE  Interaction: P43405; IntAct: EBI-28935283; Score: 0.35
DE  Interaction: Q8TAS1; IntAct: EBI-28943630; Score: 0.35
DE  Interaction: Q8TDX7; IntAct: EBI-28943744; Score: 0.35
DE  Interaction: Q96GD4; IntAct: EBI-28944360; Score: 0.35
DE  Interaction: Q9BUB5; IntAct: EBI-28944975; Score: 0.35
DE  Interaction: Q9NRM7; IntAct: EBI-28946455; Score: 0.35
DE  Interaction: Q9UQM7; IntAct: EBI-28947140; Score: 0.35
DE  Interaction: Q9Y6S9; IntAct: EBI-28948011; Score: 0.35
DE  Interaction: P31947; IntAct: EBI-30814589; Score: 0.44
DE  Interaction: Q99816; IntAct: EBI-30839125; Score: 0.44
DE  Interaction: P46937; IntAct: EBI-30846427; Score: 0.44
DE  Interaction: P41212; IntAct: EBI-29015445; Score: 0.27
GO  GO:1990876;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005049;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0000278;
GO  GO:0006406;
GO  GO:0006913;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0051726;
GO  GO:0046822;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDEMDAMIPEREMKDFQFRALKKVRIFDSPEELPKERSSLLAVSNKYGLVFAGGASGLQIFPTKNLLIQNKPGDDPNKI
SQ  VDKVQGLLVPMKFPIHHLALSCDNLTLSACMMSSEYGSIIAFFDVRTFSNEAKQQKRPFAYHKLLKDAGGMVIDMKWNPT
SQ  VPSMVAVCLADGSIAVLQVTETVKVCATLPSTVAVTSVCWSPKGKQLAVGKQNGTVVQYLPTLQEKKVIPCPPFYESDHP
SQ  VRVLDVLWIGTYVFAIVYAAADGTLETSPDVVMALLPKKEEKHPEIFVNFMEPCYGSCTERQHHYYLSYIEEWDLVLAAS
SQ  AASTEVSILARQSDQINWESWLLEDSSRAELPVTDKSDDSLPMGVVVDYTNQVEITISDEKTLPPAPVLMLLSTDGVLCP
SQ  FYMINQNPGVKSLIKTPERLSLEGERQPKSPGSTPTTPTSSQAPQKLDASAAAAPASLPPSSPAAPIATFSLLPAGGAPT
SQ  VFSFGSSSLKSSATVTGEPPSYSSGSDSSKAAPGPGPSTFSFVPPSKASLAPTPAASPVAPSAASFSFGSSGFKPTLEST
SQ  PVPSVSAPNIAMKPSFPPSTSAVKVNLSEKFTAAATSTPVSSSQSAPPMSPFSSASKPAASGPLSHPTPLSAPPSSVPLK
SQ  SSVLPSPSGRSAQGSSSPVPSMVQKSPRITPPAAKPGSPQAKSLQPAVAEKQGHQWKDSDPVMAGIGEEIAHFQKELEEL
SQ  KARTSKACFQVGTSEEMKMLRTESDDLHTFLLEIKETTESLHGDISSLKTTLLEGFAGVEEAREQNERNRDSGYLHLLYK
SQ  RPLDPKSEAQLQEIRRLHQYVKFAVQDVNDVLDLEWDQHLEQKKKQRHLLVPERETLFNTLANNREIINQQRKRLNHLVD
SQ  SLQQLRLYKQTSLWSLSSAVPSQSSIHSFDSDLESLCNALLKTTIESHTKSLPKVPAKLSPMKQAQLRNFLAKRKTPPVR
SQ  STAPASLSRSAFLSQRYYEDLDEVSSTSSVSQSLESEDARTSCKDDEAVVQAPRHAPVVRTPSIQPSLLPHAAPFAKSHL
SQ  VHGSSPGVMGTSVATSASKIIPQGADSTMLATKTVKHGAPSPSHPISAPQAAAAAALRRQMASQAPAVNTLTESTLKNVP
SQ  QVVNVQELKNNPATPSTAMGSSVPYSTAKTPHPVLTPVAANQAKQGSLINSLKPSGPTPASGQLSSGDKASGTAKIETAV
SQ  TSTPSASGQFSKPFSFSPSGTGFNFGIITPTPSSNFTAAQGATPSTKESSQPDAFSSGGGSKPSYEAIPESSPPSGITSA
SQ  SNTTPGEPAASSSRPVAPSGTALSTTSSKLETPPSKLGELLFPSSLAGETLGSFSGLRVGQADDSTKPTNKASSTSLTST
SQ  QPTKTSGVPSGFNFTAPPVLGKHTEPPVTSSATTTSVAPPAATSTSSTAVFGSLPVTSAGSSGVISFGGTSLSAGKTSFS
SQ  FGSQQTNSTVPPSAPPPTTAATPLPTSFPTLSFGSLLSSATTPSLPMSAGRSTEEATSSALPEKPGDSEVSASAASLLEE
SQ  QQSAQLPQAPPQTSDSVKKEPVLAQPAVSNSGTAASSTSLVALSAEATPATTGVPDARTEAVPPASSFSVPGQTAVTAAA
SQ  ISSAGPVAVETSSTPIASSTTSIVAPGPSAEAAAFGTVTSGSSVFAQPPAASSSSAFNQLTNNTATAPSATPVFGQVAAS
SQ  TAPSLFGQQTGSTASTAAATPQVSSSGFSSPAFGTTAPGVFGQTTFGQASVFGQSASSAASVFSFSQPGFSSVPAFGQPA
SQ  SSTPTSTSGSVFGAASSTSSSSSFSFGQSSPNTGGGLFGQSNAPAFGQSPGFGQGGSVFGGTSAATTTAATSGFSFCQAS
SQ  GFGSSNTGSVFGQAASTGGIVFGQQSSSSSGSVFGSGNTGRGGGFFSGLGGKPSQDAANKNPFSSASGGFGSTATSNTSN
SQ  LFGNSGAKTFGGFASSSFGEQKPTGTFSSGGGSVASQGFGFSSPNKTGGFGAAPVFGSPPTFGGSPGFGGVPAFGSAPAF
SQ  TSPLGSTGGKVFGEGTAAASAGGFGFGSSSNTTSFGTLASQNAPTFGSLSQQTSGFGTQSSGFSGFGSGTGGFSFGSNNS
SQ  SVQGFGGWRS
//
ID  Q80U93;
PN  Nuclear pore complex protein Nup214;
GN  Nup214;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P35658}. Note=Cytoplasmic side of the nuclear pore complex. {ECO:0000250|UniProtKB:P35658}.
DR  UNIPROT: Q80U93;
DR  UNIPROT: A2ATN2;
DE  Function: Part of the nuclear pore complex. Has a critical role in nucleocytoplasmic transport. May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex. {ECO:0000250|UniProtKB:P35658}.
DE  Reference Proteome: Yes;
DE  Interaction: P35658; IntAct: EBI-2555228; Score: 0.40
DE  Interaction: P37198; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: P46060; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-2555228; Score: 0.40
DE  Interaction: P57740; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: P78406; IntAct: EBI-2555228; Score: 0.56
DE  Interaction: Q12769; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-2555228; Score: 0.56
DE  Interaction: Q99567; IntAct: EBI-2555228; Score: 0.56
DE  Interaction: Q8N1F7; IntAct: EBI-2555228; Score: 0.56
DE  Interaction: Q8WYU3; IntAct: EBI-2555228; Score: 0.40
DE  Interaction: O15294; IntAct: EBI-2555228; Score: 0.40
DE  Interaction: P07686; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q9BW27; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q14151; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: P52630; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q15438; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: O95678; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8TEM1; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q02388; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q13277; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: E9PF10; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q9NPJ6; IntAct: EBI-11014856; Score: 0.35
GO  GO:1990876;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005049;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0000278;
GO  GO:0006406;
GO  GO:0006913;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0051726;
GO  GO:0046822;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDEMDAMIPEREMKDFQFRALKKVRIFDSPEELPKERSSVLTISNKYGMLFAGGTNGLNVFPTKSLLIQNKPGDDPNKI
SQ  VDTIQGLNVPMKFPVHHLALSCDSLTLSACMMSSEYGSIIAFFDVRTFSNQAKPLKRPFTYHKVSNDASGMVNDMKWNPT
SQ  VPSMVAVCLADGSISVLQVTDVVKVCATLPPSTGVTCVCWSPKGKQLAVGKQNGTVVQYLPTLQEKKVIPCPPFYESDHP
SQ  VRVLDVLWIGTYVFTIVYAGADGTLETCPDVVMALLPKKEEKHPEIFVNFMEPCYSSCTERQHHYYLSYIEEWDLVLAAS
SQ  AASTEVSILARQNDQTNWESWLLEDSSRAELPVTDKSDDSLPMGVAIDYTNEVEVTINEEKTLPPAPVLLLLSTDGVLCP
SQ  FYMINQNPGVRSLIKTLELISTEGERQPKSSGSFPGTPSSPQAPQNLDAPATASSPLPPVSAAPTSTFPMPSAAGSPSVF
SQ  SFGPSSFKSSASVTGEPPLYPTGSDSSRAAPGSGTSTFSFAPPSKGSLASTPAVAPVATSAAPFTFGFKPTLESTPMSST
SQ  PNTGMKPSFPPSASSVKVNLNEKFTAVASSAPVHSSTSTPSVLPFSSSPKPTASGPLSHPTPLPASSSSMPLKSSVSPSP
SQ  AAGRSTQTAPSSAPSTGQKSPRVNPPVPKSGSSQAKALQPPVTEKQRPQWKDSDPVLAGIGEEIAHFQKELEELKARTAK
SQ  ACLQVGTSEEMKMLRTESDDLHTFLFEIRETTESLHGDISTLKTTLLEGFAGVEEAREQHGRNHDSGYLHLLYKRPLDPK
SQ  SEAQLQEIRRLHQYVKFAVQDVNDVLDLEWDRHLEQKKRQRRLIVPERETLFNTLANNREIINQQRKRLNQLVDSLQQLR
SQ  LYNHTAPWSLPSALSTQSNSHSFDSDLECLLKTTIESHTKPSPRVPGKLSPAKQAQLRNFLAKRKTPPVRSTAPASLSRS
SQ  AFLSQRYYEDLDEGSSASSVAQPLEGEDARPTCTSVAQPLEGEDAQPICKEEEAVVPVPRHAPVVRTPSIQPSLLPQSMP
SQ  FAKPHLIHSSSPAVMSSAVSTSATKVIPQGADSTMLATKTVKHGAPGPSHTVAAPQAAAAAALRRQMASQAPAMSTLTES
SQ  TLKTVPQVVNVQELRSNPSPPSAAMGSAVQHSAAKTPHAVLTPVANSQAKQGSLINSFKPSGPTAASCQLSSGDKAVGQG
SQ  TAKTESAATSTPSAAGQLNKPFSFASPGTFTFGTITPTPSSSFTATPGAGPPTKEPTQLEAFSFGGGGKPFSEAIPGNSP
SQ  ATGATSAPSTSVTAASLEDSAPSSSKPAAPPETTVSSASSKLETPPSKLGELLFPSSLAGETLGSFSGLRVGQAEDSTKP
SQ  VSKASSTNLAGAQPAKPSGVSFPNTSVLGKPVEPAVTSSVSPAPAAPASALNVSTSSSSATVFGSVPLTSAGPPGLISFG
SQ  GAALASSKASFSFGNQQTSSSTASSATPTSTSVAPSLPASFPTLSFGGLLSSPSASSLPVSSGKSTEEAAPPAVPDKSDS
SQ  SEVSATTPSLPVQPQSTQASLQTSDPVKKEPVLVQTTDSSPSRPASSASFVASTESMPVTLGAPDSKIEAVSPASTFAGP
SQ  GQAAVATAVLPGAGSAATEASGTPTTSTVSSSSPTSATETAVFGTATSGSSVFTQPPAASSSSAFSQLSSNTATAPSATP
SQ  VFGQVAASITSTAAATPQASSSGFGSPAFGASAPGVFGQTAFGQTPAFGQATSSPASGFSFSQPGFSSVPAFGQSVSSTP
SQ  ASTSANVFGATSSTSSPGSFSFGQASTNTGGTLFGQNNPPAFGQSPGFGQGSSVFGGTSATTSTAAPSGFSFCQASGFGS
SQ  SNTGSVFGQAANTGGSVFGQSSTSSGGVFGSGNATRGGGFFSGLGGKPSQDAANKNPFSSAGGGFGSTAAPNTSNLFGNS
SQ  GAKTFGGFGSSSFGEQKPAGTFSSGGGSVASQGFGFSTPNKTGGFGAAPVFGSPPTFGGSPGFGGVPAFGSAPAFTSPLG
SQ  STGGKVFGEGTAAASAGGFGFGSSGNTASFGTLASQNAPTFGSLSQQTSGFGTPSSGFAGFGSGTGAFTFGSSNSSVQGF
SQ  GGWRS
//
ID  Q9C829;
PN  Nuclear pore complex protein NUP50A;
GN  NUP50A;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q9C829;
DR  UNIPROT: Q8L6Y2;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Probably involved in nucleocytoplasmic transport via its interactions with importins and Ran, rather than by forming part of the nuclear pore complex (NPC) scaffolding. {ECO:0000305|PubMed:21189294}.
DE  Reference Proteome: Yes;
DE  Interaction: F4JL11; IntAct: EBI-4512448; Score: 0.37
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0046907;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0050790;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDSENVQQPSKKRGALKQLSRDNPGLDDDDDSAELESGTFKKASDEVLASRRIVRVKRKEPSAAPVAASNPFAGIQLVP
SQ  TTAPASTPVGTNAPLAESKLAPAEAVVEDNQKASDIEEGDEVDSKKVDVKDAVGEETEKTKDKDDNHCGKSADVQVAATE
SQ  VAQMVSCDTNVCNNAVEGTDQTDFPLEKDSGGDQAEKKEKEGNGIEEADKNGDNGAFSSFQQHSSNKNAFTGLASTEASG
SQ  SSFSFGLVSQDGSTGTGSLFGFGLPSSNSSSIFGATGSSIIKKSEGSGFPPKQEVSTETGEENEKVAFSADSIMFEYLDG
SQ  GWKERGKGELKVNVSSNDGKARLVMRAKGNYRLILNASLYPEMKLANMDKKGITFACVNSVSEGKEGLSTFALKFKDPTI
SQ  VEEFRVAIDKHKDSKPMEKAAEKSALPLKTPENSPTATDT
//
ID  Q9LW88;
PN  Nuclear pore complex protein NUP50B;
GN  NUP50B;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q9LW88;
DR  UNIPROT: Q8GXC8;
DR  UNIPROT: Q8LG62;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Probably involved in nucleocytoplasmic transport via its interactions with importins and Ran, rather than by forming part of the nuclear pore complex (NPC) scaffolding. {ECO:0000305|PubMed:21189294}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9LU93; IntAct: EBI-2131492; Score: 0.00
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0046907;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0050790;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDSDNAIPFSRKRTALKELSRDNPGLDDDDEDTSALESGTFNTASKEVLASRRIIRVRRTDRSATAPPASNPFTGIRLV
SQ  PFTAPAPSTAAAETTKPLSAGKQETLADGRSDATKETDGDSKEKSDAIDAVGKQETQGDEISAKTKDIIDGGEKEMSEAV
SQ  NSVEGGGAVNKNEDEIKTTMVTEVAAGEETVKDDNNNSNTVEGSDCVVKDTGGNQTEKEGKEGDGNEDTEKNGDSGALSS
SQ  FHQHSSSKNAFTGLASTGFSASSFSFGLVPQEGSTGSGSEQSSFSFGQANNGNSSLFGASVATSITTKSTETTTAFPSKQ
SQ  DVSVETGEENEKAAFTADSVMFEYLEGGWKERGKGELKVNISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMDKKG
SQ  ITFACVNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEEHKDSKPSVAEAAAPLKTPENSPSAEDA
//
ID  Q9XZ06;
PN  Nuclear pore complex protein Nup93-1;
GN  Nup93;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q8N1F7}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:31784359}. Nucleus, nucleoplasm {ECO:0000269|PubMed:31784359}. Note=When not in the nuclear pore complex, can localize to the nuclear lumen proximal to the inner nuclear membrane. {ECO:0000269|PubMed:31784359}.
DR  UNIPROT: Q9XZ06;
DR  Pfam: PF04097;
DE  Function: Required for nuclear pore complex assembly, maintenance and function (PubMed:20547758, PubMed:22718353). Required for nuclear import of phosphorylated Mad via importin msk (PubMed:20547758). Has no role in classical nuclear localization signal (cNLS)-dependent nuclear import via importin-beta (PubMed:20547758). Mediates the association between the nuclear pore complex and a subclass of silenced regions bound by Polycomb group (PcG) proteins, enables long-range interactions between Polycomb loci and contributes to repression of polycomb targets (PubMed:31784359). Together with Nup62 and Nup154, contributes to karyosome morphology and chromatin organization including attachment to the nuclear envelope in oocytes and nurse cells (PubMed:26341556). {ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:22718353, ECO:0000269|PubMed:26341556, ECO:0000269|PubMed:31784359}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VWS2; IntAct: EBI-26744845; Score: 0.49
DE  Interaction: Q9VYS8; IntAct: EBI-202060; Score: 0.00
DE  Interaction: P54360; IntAct: EBI-207600; Score: 0.00
DE  Interaction: Q9W215; IntAct: EBI-209296; Score: 0.00
DE  Interaction: Q9VH87; IntAct: EBI-209300; Score: 0.00
DE  Interaction: P84029; IntAct: EBI-209304; Score: 0.00
DE  Interaction: A1Z6Z9; IntAct: EBI-209308; Score: 0.00
DE  Interaction: Q9VHK1; IntAct: EBI-209312; Score: 0.00
DE  Interaction: Q9VQE0; IntAct: EBI-209316; Score: 0.00
DE  Interaction: Q9VRS2; IntAct: EBI-209320; Score: 0.00
DE  Interaction: P35381; IntAct: EBI-209324; Score: 0.00
DE  Interaction: Q9Y119; IntAct: EBI-209328; Score: 0.00
DE  Interaction: Q9VQ61; IntAct: EBI-209332; Score: 0.00
DE  Interaction: P07909; IntAct: EBI-209365; Score: 0.00
DE  Interaction: P19538; IntAct: EBI-502459; Score: 0.37
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: Q9VH81; IntAct: EBI-9922589; Score: 0.46
DE  Interaction: P18431; IntAct: EBI-9925534; Score: 0.35
DE  Interaction: P53034; IntAct: EBI-15160117; Score: 0.49
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0003682;
GO  GO:0031490;
GO  GO:0017056;
GO  GO:0097240;
GO  GO:0045814;
GO  GO:0006999;
GO  GO:0030717;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0097298;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLMELLKQAQRLTNETNTDTEVPGVERTMSQVLQATKEFHSRVTQMGTNDLQAHILLGSKGVDLPKLTQKLESLSARQT
SQ  FEPIDPVTETNVQAYLKNERENAILSVIDETNRSIFKSVERQKWRCIYSEWGEEKEALLNALVGPNQQDFPDVQFQIVPT
SQ  AMADEPTPYSQLNGHEQMYAEQIAIHNQSIILGRRPNLLSTLAHVVQDSFNDESVAEMWNVLQFMTALPPVSSTIDPIKN
SQ  RQTSPQFVEQARTYLERRYRTYMRKFIVANLAKARRGGIPSVYHMVRSYVGVTLQGQRALYGLHDVNNGQPLWPHVYYSL
SQ  RSGDMDAAALYLKESGTCPDLLTLLTLRKNGDRDNLMVKLEGQLKLEYNSRLRACTDPYKKAVYVVLLACDPHFTHVELM
SQ  RSIDDFLWMQLSILRRSDQSDSNTEQLTFSGLQSLILEKYGENYFNAREKAALYFQVLTLTGQFEAAIEFLARTEKNRTH
SQ  AIHMAIALNEISMLGTPRSVEQSLLSSDPDDPKPMKRLNLVRLIVMYTKCFERTDTTQALHYYYLLRNFKSENGRGNVML
SQ  TCVCDLLVEKCDDEMLELIFGTEDKKNGLRYGGIYAEFQIHECDKYSLAEMVGDELSKRGDYELAIELYFIGGQLDKALR
SQ  LVNSLLAQVVHQPTQNGSVRNRLGDIINRLDAALVVRKSDVEVQVVVTYTVLTKVMKFFDHYHEGALRSALEILTNNHLI
SQ  PASSLEVDECVTNIKRMGPEVIKVLPDILLASMDIVYQEYVKLMDSNETASGFFDESKCVNKEPAVKHLRDRAKAFTNMA
SQ  ASVPYRMPSTTNQRLVQLEILMH
//
ID  F4J284;
PN  Nuclear pore complex protein NUP93B;
GN  NUP93B;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305}.
DR  UNIPROT: F4J284;
DR  UNIPROT: Q9M2L2;
DR  Pfam: PF04097;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0016973;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MANDQEMSGWTDLLHSSTKLLEQAAPSSQFPPLQRNLDQLEALSRKLKAKTLRNEAPSQSIAATRLLAREGINADQLSRD
SQ  LKSFELKTTFEDVFPAETTSVEEYLQQVHEMAMVSAIQEAQKDNVRSFNNYMLKVLEEDCIKEKRDFLHSLSKTSMLPKT
SQ  KMINSSRGSHAGSLVPLSPQVSSKPGTELVSMTNKPIHEKKAYVYAEVVKKLNSARERGLPFKLATLFNGAYESLEIDLT
SQ  RGKSVNMQKLWQLIQGMTGEESAVQHGVSKRMALVIGARRHLECGHGKHIMDTIQSHPTQAALGGSVGNLQRIRAFLRIR
SQ  LRDYGSLDFDSVDARRQPPVDTTWQQIYFCLRTGYYEEAREIAQSSRSSQQQFAPLLTEWITTGGTVAAQTAATASEECE
SQ  KLLRMGDRFGQTTYDKKKLLLYTIISGSRRQIDRIMRDFSTLFNTIEDFLWFKLSCVRDVAGGSSSMIVNDGLVPYSLDD
SQ  LQAYLNKFEPSYYTKNGKDPLVYPYVLLLSIQLLPAIMHMSNEAGDEGYNIDAVHVAISLVDHSILSEGSGTGRKLSVMD
SQ  ANAEASSMIRQYGSMYLHHGDLQMTLEYYAQAAIAVGGGQQAWSGRSNVDQQRQRNLMLKQLLTEILSQEDGIHFLLGAR
SQ  GSGEEGELGRFLPDIKLRQQFLIEAAHQFQEAGLYDKSIELQKRVGAFSSALETINKCLSEAICSLVRGRPDGESRTEGL
SQ  VLSGNDILNSYKYHPDVSAQERHLVMEQETILRELEAILSIHKLARLNKHLDAIREVAKLPFLHLDPRQPDTTSDEFQKA
SQ  SSYFQTCVPDLLKVALTCLDNVADTDGSIRGMRSKIAGFLASNTQRNWPRDLYEKIARSF
//
ID  Q8RY25;
PN  Nuclear pore complex protein NUP98A;
GN  NUP98A;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8RY25;
DR  UNIPROT: Q9SY83;
DR  Pfam: PF04096;
DR  PROSITE: PS51434;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P94077; IntAct: EBI-20795895; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0048573;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:1902446;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGSSNPFGQSSGTSPFGSQSLFGQTSNTSSNNPFAPATPFGTSAPFAAQSGSSIFGSTSTGVFGAPQTSSPFASTPTFG
SQ  ASSSPAFGNSTPAFGASPASSPFGGSSGFGQKPLGFSTPQSNPFGNSTQQSQPAFGNTSFGSSTPFGATNTPAFGAPSTP
SQ  SFGATSTPSFGASSTPAFGATNTPAFGASNSPSFGATNTPAFGASPTPAFGSTGTTFGNTGFGSGGAFGASNTPAFGASG
SQ  TPAFGASGTPAFGASSTPAFGASSTPAFGASSTPAFGGSSTPSFGASNTSSFSFGSSPAFGQSTSAFGSSAFGSTPSPFG
SQ  GAQASTPTFGGSGFGQSTFGGQQGGSRAVPYAPTVEADTGTGTQPAGKLESISAMPAYKEKNYEELRWEDYQRGDKGGPL
SQ  PAGQSPGNAGFGISPSQPNPFSPSPAFGQTSANPTNPFSSSTSTNPFAPQTPTIASSSFGTATSNFGSSPFGVTSSSNLF
SQ  GSGSSTTTSVFGSSSAFGTTTPSPLFGSSSTPGFGSSSSIFGSAPGQGATPAFGNSQPSTLFNSTPSTGQTGSAFGQTGS
SQ  AFGQFGQSSAPAFGQNSIFNKPSTGFGNMFSSSSTLTTSSSSPFGQTMPAGVTPFQSAQPGQASNGFGFNNFGQNQAANT
SQ  TGNAGGLGIFGQGNFGQSPAPLNSVVLQPVAVTNPFGTLPAMPQISINQGGNSPSIQYGISSMPVVDKPAPVRISSLLTS
SQ  RHLLHRRVRLPARKYRPGENGPKVPFFTDDEESSSTPKADALFIPRENPRALVIRPVQQWSSRDKSILPKEQRPTAPLHD
SQ  NGKSPDMATDAANHDRNGNGELGATGERIHTSVNANQKPNGTTRSDQASEKERPYKTLSGHRAGEAAIVYEHGADIEALM
SQ  PKLRQSDYFTEPRIQELAAKERADPGYCRRVRDFVVGRHGYGSIKFMGETDVRRLDLESLVQFNTREVIVYMDESKKPAV
SQ  GQGLNKPAEVTLLNIKCIDKKTGKQFTEGERVEKYKMMLKKKAEAQGAEFVSFDPVKGEWKFRVEHFSSYKLGDEDEEDG
SQ  V
//
ID  F4ID16;
PN  Nuclear pore complex protein NUP98B;
GN  NUP98B;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: F4ID16;
DR  UNIPROT: Q9LQ50;
DR  Pfam: PF04096;
DR  PROSITE: PS51434;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0044614;
GO  GO:0017056;
GO  GO:0071456;
GO  GO:0051028;
GO  GO:0048573;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGSSNNNPFGQSSISSPFGTQTHSLFGQTNNNASNNPFATKPFGTSTPFGAQTGSSMFGGTSTGVFGAPQTSSPFGASP
SQ  QAFGSSTQAFGASSTPSFGSSNSPFGGTSTFGQKSFGLSTPQSSPFGSTTQQSQPAFGNSTFGSSTPFGASTTPAFGASS
SQ  TPAFGVSNTSGFGATNTPGFGATNTTGFGGSSTPGFGASSTPAFGSTNTPAFGASSTPLFGSSSSPAFGASPAPAFGSSG
SQ  NAFGNNTFSSGGAFGSSSTPTFGASNTSAFGASSSPSFNFGSSPAFGQSTSAFGSSSFGSTQSSLGSTPSPFGAQGAQAS
SQ  TSTFGGQSTIGGQQGGSRVIPYAPTTDTASGTESKSERLQSISAMPAHKGKNMEELRWEDYQRGDKGGQRSTGQSPEGAG
SQ  FGVTNSQPSIFSTSPAFSQTPVNPTNPFSQTTPTSNTNFSPSFSQPTTPSFGQPTTPSFRSTVSNTTSVFGSSSSLTTNT
SQ  SQPLGSSIFGSTPAHGSTPGFSIGGFNNSQSSPLFGSNPSFAQNTTPAFSQTSPLFGQNTTPALGQSSSVFGQNTNPALV
SQ  QSNTFSTPSTGFGNTFSSSSSLTTSISPFGQITPAVTPFQSAQPTQPLGAFGFNNFGQTQIANTTDIAGAMGTFSQGNFK
SQ  QQPALGNSAVMQPTPVTNPFGTLPALPQISIAQGGNSPSIQYGISSMPVVDKPAPVRVSPLLTSRHLLQRRVRLPTRKYR
SQ  PSDDGPKVPFFSDEEENSSTPKADAFFIPRENPRALFIRPVERVKSEHPKDSPTPLQENGKRSNGVTNGANHETKDNGAI
SQ  REAPPVKVNQKQNGTHENHGGDKNGSHSSPSGADIESLMPKLHHSEYFTEPRIQELAAKERVEQGYCKRVKDFVVGRHGY
SQ  GSIKFLGETDVCRLDLEMVVQFKNREVNVYMDESKKPPVGQGLNKPAVVTLLNIKCMDKKTGTQVMEGERLDKYKEMLKR
SQ  KAGEQGAQFVSYDPVNGEWTFKVEHFSSYKLGDEYDV
//
ID  A4GSN8;
PN  Nuclear-pore anchor;
GN  NUA;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:19704557, ECO:0000269|PubMed:21189294}. Nucleus membrane {ECO:0000269|PubMed:19704557}; Peripheral membrane protein {ECO:0000269|PubMed:19704557}; Nucleoplasmic side {ECO:0000269|PubMed:19704557}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:19704557}. Note=Located at the inner surface of the nuclear envelope during interphase and in the vicinity of the spindle during prometaphase. {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:19704557}.
DR  UNIPROT: A4GSN8;
DR  UNIPROT: F4IDK8;
DR  UNIPROT: F4IDK9;
DR  UNIPROT: O64521;
DR  UNIPROT: O64522;
DR  UNIPROT: O64524;
DR  UNIPROT: O64525;
DR  UNIPROT: Q8H7F1;
DR  Pfam: PF07926;
DE  Function: Component of the nuclear pore complex. Acts as a docking site for activities required for desumoylation and mRNA export. Required for the proper expression or localization of a subset of miRNAs. Plays a role in meristematic cell division by interacting with spindle assembly checkpoint proteins. {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:17535820, ECO:0000269|PubMed:19704557, ECO:0000269|PubMed:19704774, ECO:0000303|PubMed:20872268}.
DE  Reference Proteome: Yes;
DE  Interaction: A4GSN8; IntAct: EBI-1545667; Score: 0.37
DE  Interaction: Q94F30; IntAct: EBI-1545682; Score: 0.37
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0009506;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0009910;
GO  GO:0033234;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0048443;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:19704557};
SQ  MPLFMPDEELARLSSDAASVVAERADEYIRKIYAELDSVRAKADAASITAEQTCSLLEQKYLSLSQDFSSLESQNAKLQS
SQ  DFDDRLAELAQSQAQKHQLHLQSIEKDGEVERMSTEMSELHKSKRQLMELLEQKDAEISEKNSTIKSYLDKIVKLTDTSS
SQ  EKEARLAEATAELARSQAMCSRLSQEKELTERHAKWLDEELTAKVDSYAELRRRHSDLESEMSAKLVDVEKNYIECSSSL
SQ  NWHKERLRELETKIGSLQEDLSSCKDAATTTEEQYTAELFTANKLVDLYKESSEEWSRKAGELEGVIKALEARLSQVESS
SQ  YKERLDKEVSTKQLLEKENGDLKQKLEKCEAEIEKTRKTDELNLIPFSNFTRRVDNSGTSNMIEESQAVISKVPAGVSGT
SQ  ALAASLLRDGWSLAKIYEKYQEAVDAMRHEQLGRKEAEMILQRVLSELEEKAGFIQEERGEYERVVEAYCLVNQKLQDSV
SQ  SEQSNMEKFIMELKADLRRRERENTLLQKDISDLQKQVTILLKECRDVQLRCGAARDDDEDDYPLLSDVEMEMESEADKI
SQ  ISEHLLKFKDINGLVEQNVKLRNLVRSLSEQIESRETELKETFEVDLKNKTDEASAKVATVLKRAEEQGQMIESLHTSVA
SQ  MYKRLYEEEQKLHSSDSRSSDLSPAVVPGRKNFLHLLEDSEEATKRAQEKAFERIRILEEDFAKARSEVIAIRSERDKLA
SQ  MEANFAREKLEGIMKESERKREEMNSVLARNIEFSQLIIDHQRKLRESSESLHAAEEISRKLSMEVSVLKQEKELLSNAE
SQ  KRASDEVSALSQRVYRLQATLDTVQSTEEVREETRAAERRKQEEHIKQLQREWAEAKKELQEERSNARDFTSDRNQTLNN
SQ  AVMQVEEMGKELANALKAVSVAESRASVAEARLSDLEKKIRSSDPKTLDMDSGGIVSLSDKEMSIELRTAKEEIEKLRGE
SQ  VESSKSHMLQYKSIAQVNETALKQMESAHENFRLEAEKRQRSLEAELVSLRERVSELENDCIQKSEQLATAAAGKEDALL
SQ  SASAEIASLREENLVKKSQIEAMNIQMSTLKNDLETEHEKWRVAQRNYERQVILLSETIQELTKTSQALAALQEEASELR
SQ  KLADARGIENSELNAKWSEEKLMLEQQKNLAEKKYHELNEQNKLLHSRLEAKHLNSAEKNSRSGTISSGSTDSDHLEDSG
SQ  LQRVVHYLRRTKEIAETEISLMRQEKLRLQSQLESALKMAESARGSLTAERASTRASLLTDDGIKSLQLQVSEMNLLRES
SQ  NMQLREENKHNFEKCQEMREVAQKARMESENFENLLKTKQTELDLCMKEMEKLRMETDLHKKRVDELRETYRNIDIADYN
SQ  RLKDEVRQLEEKLKAKDAHAEDCKKVLLEKQNKISLLEKELTNCKKDLSEREKRLDDAQQAQATMQSEFNKQKQELEKNK
SQ  KIHYTLNMTKRKYEKEKDELSKQNQSLAKQLEEAKEEAGKRTTTDAVVEQSVKEREEKEKRIQILDKYVHQLKDEVRKKT
SQ  EDLKKKDEELTKERSERKSVEKEVGDSLTKIKKEKTKVDEELAKLERYQTALTHLSEELEKLKHADGNLPEGTSAVQVLS
SQ  GSILNDQAAAYVSAVEYFERVARSIASNSQVSTKPTDMVTEPSSGIPAAEPSTMTRVPSSTPLIKSPVATTQQLPKVASD
SQ  NKEKRLISQKPSTEFRRPSGRRIVRPQLVKPEESPKVDVDMPEAEGTGDEGKQPAAHEPESQVTTSVRPVQTLVRKRQAD
SQ  SLVSEPQQDSLTQGETSSEIAPPASKKAKGSESHPDTSEGENLAKEPAIDELMDATTTTDGDNEETEAENAEEKTEEYVE
SQ  AQQDNEADEPVEESPTETETIPTEEESRDQTEEENQEPLTDMESDKEEGELDLDTLEDLEEGTDVASMMRSPEKEEVQPE
SQ  TLATPTQSPSRMETAMEEAETTIETPVEDDKTDEGGDAAEEAADIPNNANDQQEAPETDIKPETSAATTSPVSTAPTTSS
SQ  TLASAITSSGAPETEDPKRAPSPGGGSSTIVTLADRAQMKRRERIANIVVSRAPNPATRGARGRTVNLRGGGRLLPRGGR
SQ  APRGGRGQSPSPP
//
ID  P80303;
PN  Nesfatin-1;
GN  NUCB2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Golgi apparatus {ECO:0000269|PubMed:11749975}. Membrane {ECO:0000269|PubMed:11749975}; Peripheral membrane protein {ECO:0000269|PubMed:11749975}. Cytoplasm {ECO:0000269|PubMed:11749975}. Secreted {ECO:0000269|PubMed:11749975}. Endoplasmic reticulum {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Golgi retention is mediated by its N-terminal region. [Nesfatin-1]: Secreted.
DR  UNIPROT: P80303;
DR  UNIPROT: A8K642;
DR  UNIPROT: D3DQX5;
DR  UNIPROT: Q8NFT5;
DR  UNIPROT: V9HW75;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  OMIM: 608020;
DR  DisGeNET: 4925;
DE  Function: Calcium-binding protein which may have a role in calcium homeostasis (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein (G-protein) alpha subunit GNAI3 (By similarity). {ECO:0000250|UniProtKB:P81117, ECO:0000250|UniProtKB:Q9JI85}. [Nesfatin-1]: Anorexigenic peptide, seems to play an important role in hypothalamic pathways regulating food intake and energy homeostasis, acting in a leptin-independent manner. May also exert hypertensive roles and modulate blood pressure through directly acting on peripheral arterial resistance. {ECO:0000250|UniProtKB:Q9JI85}.
DE  Reference Proteome: Yes;
DE  Interaction: Q14790; IntAct: EBI-7740879; Score: 0.44
DE  Interaction: P55212; IntAct: EBI-7740930; Score: 0.44
DE  Interaction: P55210; IntAct: EBI-7740913; Score: 0.44
DE  Interaction: P42574; IntAct: EBI-7740963; Score: 0.44
DE  Interaction: Q3KSU8; IntAct: EBI-2623010; Score: 0.37
DE  Interaction: P24522; IntAct: EBI-3928733; Score: 0.51
DE  Interaction: P08754; IntAct: EBI-3930095; Score: 0.37
DE  Interaction: P84996; IntAct: EBI-3930125; Score: 0.37
DE  Interaction: Q96GM5; IntAct: EBI-3932795; Score: 0.37
DE  Interaction: O14980; IntAct: EBI-3932805; Score: 0.37
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q99IB8; IntAct: EBI-6927977; Score: 0.37
DE  Interaction: Q2MV58; IntAct: EBI-11366929; Score: 0.27
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q9H8J5; IntAct: EBI-21537025; Score: 0.35
DE  Interaction: P17275; IntAct: EBI-21713262; Score: 0.35
DE  Interaction: Q9Y6Z7; IntAct: EBI-21859525; Score: 0.35
DE  Interaction: P48788; IntAct: EBI-21878883; Score: 0.35
DE  Interaction: P59817; IntAct: EBI-21878952; Score: 0.35
DE  Interaction: O75489; IntAct: EBI-21931040; Score: 0.35
DE  Interaction: Q9NQH7; IntAct: EBI-21937834; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27049069; Score: 0.27
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: Q5JZY3; IntAct: EBI-32720634; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0070062;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0005509;
GO  GO:0003677;
GO  GO:0001965;
GO  GO:0005085;
GO  GO:0032099;
GO  GO:0007264;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11749975};
SQ  MRWRTILLQYCFLLITCLLTALEAVPIDIDKTKVQNIHPVESAKIEPPDTGLYYDEYLKQVIDVLETDKHFREKLQKADI
SQ  EEIKSGRLSKELDLVSHHVRTKLDELKRQEVGRLRMLIKAKLDSLQDIGMDHQALLKQFDHLNHLNPDKFESTDLDMLIK
SQ  AATSDLEHYDKTRHEEFKKYEMMKEHERREYLKTLNEEKRKEEESKFEEMKKKHENHPKVNHPGSKDQLKEVWEETDGLD
SQ  PNDFDPKTFFKLHDVNSDGFLDEQELEALFTKELEKVYDPKNEEDDMVEMEEERLRMREHVMNEVDTNKDRLVTLEEFLK
SQ  ATEKKEFLEPDSWETLDQQQFFTEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKK
SQ  LQQGIPPSGPAGELKFEPHI
//
ID  P81117;
PN  Nesfatin-1;
GN  Nucb2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10915798}. Perikaryon {ECO:0000269|PubMed:10915798}. Endoplasmic reticulum {ECO:0000269|PubMed:10915798}. Golgi apparatus {ECO:0000250}. Nucleus envelope {ECO:0000269|PubMed:10915798}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Secreted {ECO:0000269|PubMed:10915798}. Note=In dendrites and perikarya of brain neurons. Abundant in the ER cisternae and nuclear envelope, but not detected in Golgi, mitochondria or nucleoplasm in neurons. In cell culture, cytoplasmic and secreted. [Nesfatin-1]: Secreted {ECO:0000250}.
DR  UNIPROT: P81117;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Calcium-binding protein which may have a role in calcium homeostasis (PubMed:10915798). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein (G-protein) alpha subunit GNAI3 (By similarity). {ECO:0000250|UniProtKB:Q9JI85, ECO:0000269|PubMed:10915798}. [Nesfatin-1]: Anorexigenic peptide, seems to play an important role in hypothalamic pathways regulating food intake and energy homeostasis, acting in a leptin-independent manner. May also exert hypertensive roles and modulate blood pressure through directly acting on peripheral arterial resistance. {ECO:0000250|UniProtKB:Q9JI85}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0005797;
GO  GO:0005640;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0005509;
GO  GO:0003677;
GO  GO:0001965;
GO  GO:0005085;
GO  GO:0005164;
GO  GO:0006874;
GO  GO:1901142;
GO  GO:0032099;
GO  GO:0043951;
GO  GO:0045599;
GO  GO:0070093;
GO  GO:0046627;
GO  GO:0046321;
GO  GO:2000845;
GO  GO:0007264;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MRWRIIQVQYCFLLVPCMLTALEAVPIDVDKTKVHNTEPVENARIEPPDTGLYYDEYLKQVIEVLETDPHFREKLQKADI
SQ  EEIRSGRLSQELDLVSHKVRTRLDELKRQEVGRLRMLIKAKLDALQDTGMNHHLLLKQFEHLNHQNPNTFESRDLDMLIK
SQ  AATADLEQYDRTRHEEFKKYEMMKEHERREYLKTLSEEKRKEEESKFEEMKRKHEDHPKVNHPGSKDQLKEVWEETDGLD
SQ  PNDFDPKTFFKLHDVNNDGFLDEQELEALFTRELEKVYNPQNAEDDMIEMEEERLRMREHVMSEIDNNKDRLVTLEEFLR
SQ  ATEKKEFLEPDSWETLDQQQLFTEDELKEYESIIAIQENELKKRAEELQKQKEDLQRQHDHLEAQKQEYHQAVQHLEQKK
SQ  LQQGIAPSGPAGELKFEPHT
//
ID  Q9JI85;
PN  Nesfatin-1;
GN  Nucb2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Golgi apparatus {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Nucleus envelope {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. [Nesfatin-1]: Secreted.
DR  UNIPROT: Q9JI85;
DR  Pfam: PF13499;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: Calcium-binding protein which may have a role in calcium homeostasis (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein (G-protein) alpha subunit GNAI3 (PubMed:21653697). {ECO:0000250|UniProtKB:P81117, ECO:0000269|PubMed:21653697}. [Nesfatin-1]: Anorexigenic peptide, seems to play an important role in hypothalamic pathways regulating food intake and energy homeostasis, acting in a leptin-independent manner. May also exert hypertensive roles and modulate blood pressure through directly acting on peripheral arterial resistance. {ECO:0000269|PubMed:17036007, ECO:0000269|PubMed:22293188}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P08922; IntAct: EBI-22248889; Score: 0.35
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0005615;
GO  GO:0005797;
GO  GO:0005640;
GO  GO:0005634;
GO  GO:0005509;
GO  GO:0003677;
GO  GO:0001965;
GO  GO:0005085;
GO  GO:0005164;
GO  GO:1901142;
GO  GO:0032099;
GO  GO:0043951;
GO  GO:0045599;
GO  GO:0070093;
GO  GO:0046627;
GO  GO:0046321;
GO  GO:2000845;
GO  GO:0009749;
GO  GO:0044752;
GO  GO:1990680;
GO  GO:0042594;
GO  GO:0007264;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MRWRTIQARYCFLLVPCVLTALEAVPIDVDKTKVHNVEPVESARIEPPDTGLYYDEYLKQVIEVLETDPHFREKLQKADI
SQ  EEIRSGRLSQELDLVSHKVRTRLDELKRQEVGRLRMLIKAKLDALQDTGMNHHLLLKQFEHLNHQNPDTFESKDLDMLIK
SQ  AATADLEQYDRTRHEEFKKYEMMKEHERREYLKTLSEEKRKEEEAKFAEMKRKHEDHPKVNHPGSKDQLKEVWEETDGLD
SQ  PNDFDPKTFFKLHDVNNDGFLDEQELEALFTKELDKVYNPQNAEDDMIEMEEERLRMREHVMNEIDNNKDRLVTLEEFLR
SQ  ATEKKEFLEPDSWETLDQQQLFTEEELKEYESIIAIQESELKKKADELQKQKEELQRQHDHLEAQKQEYQQAVQQLEQKK
SQ  FQQGIAPSGPAGELKFEPHT
//
ID  P32336;
PN  Protein NUD1;
GN  NUD1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10330408}. Nucleus envelope {ECO:0000269|PubMed:10330408}. Note=Localizes to the meiotic outer plaque of the SPB, at the end of the meiotic spindles.
DR  UNIPROT: P32336;
DR  UNIPROT: D6W366;
DR  UNIPROT: Q08895;
DR  PROSITE: PS51450;
DE  Function: Involved in astral microtubule organization by binding SCP72 to the outer plaque in a cell-cycle dependent manner. Required for the mitotic exit by facilitating the binding of TEMP1 to CDC15. Also involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. {ECO:0000269|PubMed:11101520}.
DE  Reference Proteome: Yes;
DE  Interaction: P30822; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32337; IntAct: EBI-811610; Score: 0.35
DE  Interaction: Q02159; IntAct: EBI-861139; Score: 0.00
DE  Interaction: Q07732; IntAct: EBI-1566966; Score: 0.55
DE  Interaction: P32336; IntAct: EBI-1566998; Score: 0.37
DE  Interaction: Q12411; IntAct: EBI-1567013; Score: 0.55
DE  Interaction: Q05955; IntAct: EBI-2133813; Score: 0.37
DE  Interaction: Q08550; IntAct: EBI-2256202; Score: 0.51
DE  Interaction: P54199; IntAct: EBI-2612619; Score: 0.35
DE  Interaction: P38990; IntAct: EBI-2613532; Score: 0.35
DE  Interaction: Q07457; IntAct: EBI-2882228; Score: 0.00
DE  Interaction: P26448; IntAct: EBI-2882390; Score: 0.00
DE  Interaction: Q00684; IntAct: EBI-2882792; Score: 0.00
DE  Interaction: P14832; IntAct: EBI-2882919; Score: 0.00
DE  Interaction: P53865; IntAct: EBI-2882903; Score: 0.00
DE  Interaction: P32472; IntAct: EBI-2883301; Score: 0.00
DE  Interaction: Q02796; IntAct: EBI-2885546; Score: 0.00
DE  Interaction: P38265; IntAct: EBI-2885494; Score: 0.00
DE  Interaction: P38890; IntAct: EBI-2887466; Score: 0.00
DE  Interaction: P39723; IntAct: EBI-2887969; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P39101; IntAct: EBI-3653621; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-3661387; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3673714; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3702827; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3712922; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3781701; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0061499;
GO  GO:0043014;
GO  GO:0045504;
GO  GO:0035591;
GO  GO:0030953;
GO  GO:0051301;
GO  GO:0051293;
GO  GO:0000073;
GO  GO:0045132;
GO  GO:0031536;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDMDTQEAELSSQLENLTINSPRKLRSNAHSNSGKVFKEYESNHDFQDSNFTSQVVEPAISDSVKKPPTMTVLNNYSTVH
SQ  QKVPSGFSGTTATSHQEAQWKQYFPGIGSGGGTNFGGAVGTANKVPESDLIVSDLVKDLSGVLETNTFKRHLDMKNKTTT
SQ  MQTHENHDTISISHSKDFFNAEKVSSSFSDDSDSGPAAEAHDVFDGILQKQKSNYLVGSYPSNSNNKNNNNNNNNNNNNS
SQ  ININNKDNARTKEEDEEDTSNSFEFSSSSSMSSSQTQSGRKSKVLKKPPLNTISPGQLGYQFNHTHGAWDPPLNQGLDVS
SQ  SSHSLDNTSSNQSQFATMVPTGDNHTNGKAPSILDKKAYELTSTKPGDVGYRQKKIQEEENLANSDDTPLDTPKFNDLFT
SQ  KNGTRAKVKGQMRTSRSISNSNLLEAHKKLKTFPAERVEDITSISEVNTSFNETEKQLISILTSKLSGSPSYDSDWEKIL
SQ  KVDLSRGKLKNMFGMQRLLPNVLVLNLSDNEMNTLEGIPSNVVQLFCSNNKITSAHCSLAGFHDLECLDLSYNLLNTSLK
SQ  FLSLCHHLQEVNLSYNSIQSLEGIGSSRMKKLNLSNNEINGIIDFEQLILTNNSVVGGWLTVEVLDLSNNNIIGVRNINC
SQ  LPRLKVLNLNGNPLVSIVESSKMENGTLRALSIKNTGGALSKLQNYKLDDQFTFPYQNLKILKLDGFAQLSKWQKWPATL
SQ  QILEINGGLASSLPRFSSLKSTNLYSLTIANVRDFTHLPVDLSKELPFLQELHLPGNNLQNAHKLTKTLPRQSVKFLDLR
SQ  NNPITTPRHDRASTSLHYRQLLQLAGLCQQQCPALATLWLDDTPAPTATNL
//
ID  O45717;
PN  Protein nud-2;
GN  nud;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:20005871}. Note=Recruited to the nuclear envelope by unc-83. {ECO:0000269|PubMed:20005871}.
DR  UNIPROT: O45717;
DE  Function: Part of a complex with lis-1, which is recruited to the nuclear envelope by unc-83, where, in turn, it recruits dynein to the nuclear surface and regulates nuclear migration in hypodermal precursor cells (PubMed:20005871, PubMed:27697906). Plays a role in GABAergic synaptic vesicle localization in the ventral nerve cord (PubMed:16996038). {ECO:0000269|PubMed:16996038, ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:27697906}.
DE  Reference Proteome: Yes;
DE  Interaction: O76447; IntAct: EBI-340082; Score: 0.37
DE  Interaction: O44139; IntAct: EBI-2414977; Score: 0.49
DE  Interaction: O01738; IntAct: EBI-2416423; Score: 0.49
DE  Interaction: Q20398; IntAct: EBI-2417587; Score: 0.49
DE  Interaction: Q94420; IntAct: EBI-2420029; Score: 0.49
DE  Interaction: Q23064; IntAct: EBI-2905337; Score: 0.60
GO  GO:0005813;
GO  GO:0005871;
GO  GO:0000776;
GO  GO:0005875;
GO  GO:0005635;
GO  GO:0045202;
GO  GO:0008017;
GO  GO:0016477;
GO  GO:0051642;
GO  GO:0007059;
GO  GO:0051303;
GO  GO:0000132;
GO  GO:0007020;
GO  GO:0007100;
GO  GO:0007097;
GO  GO:0031022;
GO  GO:0051932;
GO  GO:0048489;
GO  GO:0047496;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLSEDQIRGLPHHELLGHFLQMREEFNEFQTSSAEIEKMMDSELDDLKTQLKKAETRVQQMTTEQIRNKDRQDDSRVQF
SQ  AQVEEQLRRENSHLHEQCESQRERIRKLEQRNDVLETSERNKEYLASDLGSKLDHAIEKIAMLESELYERQVAAEEMHRL
SQ  REEQLRTTERPRLIVEPLRNDPEILPDEPSPGPSKEEFKMSSEDVFMEDVQHHEDVRMEETIAKIDEVRIDDNKNIQEKS
SQ  QRVSTGTGAGACINRIVKDLMTKVERLDSILSTIRVSNNSSNNNSSHLTTTRA
//
ID  Q9CAF4;
PN  Nuclear pore complex protein NUP1;
GN  NUP1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:19843313, ECO:0000269|PubMed:21189294, ECO:0000269|PubMed:25081480}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:21189294}. Cytoplasm, cytosol {ECO:0000269|PubMed:21189294}. Note=Interacts dynamically with the NPC and localizes to the cytosolic pool following nuclear envelope breakdown during mitosis. {ECO:0000269|PubMed:21189294}.
DR  UNIPROT: Q9CAF4;
DR  UNIPROT: Q9LPN4;
DE  Function: Nucleoporin required for nuclear mRNA export. Functions as an adapter and/or regulator molecule in the periphery of the nuclear pore complex (NPC). May interact with importin proteins and mediate active nucleocytoplasmic transport through the NPC. Involved in regulation of nuclear morphology. {ECO:0000269|PubMed:19843313, ECO:0000269|PubMed:21818409, ECO:0000305|PubMed:21189294}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GWE6; IntAct: EBI-2619719; Score: 0.49
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0071763;
GO  GO:0006997;
GO  GO:0016973;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASAARGESSNPYGGGLGTGGKFRKPTARRSQKTPYDRPTTSVRNAGLGGGDVRGGGWLSKLVDPAQRLITYSAQRLFGS
SQ  LSRKRLGSGETPLQSPEQQKQLPERGVNQETKVGHKEDVSNLSMKNGLIRMEDTNASVDPPKDGFTDLEKILQGKTFTRS
SQ  EVDRLTTLLRSKAADSSTMNEEQRNEVGMVVRHPPSHERDRTHPDNGSMNTLVSTPPGSLRTLDECIASPAQLAKAYMGS
SQ  RPSEVTPSMLGLRGQAGREDSVFLNRTPFPQKSPTMSLVTKPSGQRPLENGFVTPRSRGRSAVYSMARTPYSRPQSSVKI
SQ  GSLFQASPSKWEESLPSGSRQGFQSGLKRRSSVLDNDIGSVGPVRRIRQKSNLSSRSLALPVSESPLSVRANGGEKTTHT
SQ  SKDSAEDIPGSSFNLVPTKSSEMASKILQQLDKLVSTREKSPSKLSPSMLRGPALKSLQNVEAPKFLGNLPEKKANSPDS
SQ  SYQKQEISRESVSREVLAQSEKTGDAVDGTSKTGSSKDQDMRGKGVYMPLTNSLEEHPPKKRSFRMSAHEDFLELDDDLG
SQ  AASTPCEVAEKQNAFEVEKSHISMPIGEKPLTPSEAMPSTSYISNGDASQGTSNGSLETERNKFVAFPIEAVQQSNMASE
SQ  PTSKFIQGTEKSSISSGKPTSEEKRIPLEEPKKPAAVFPNISFSPPATGLLNQNSGASADIKLEKTSSTAFGVSEAWAKP
SQ  TESKKTFSNSASGAESSTSAAPTLNGSIFSAGANAVTPPPSNGSLTSSPSFPPSISNIPSDNSVGDMPSTVQSFAATHNS
SQ  SSIFGKLPTSNDSNSQSTSASPLSSTSPFKFGQPAAPFSAPAVSESSGQISKETEVKNATFGNTSTFKFGGMASADQSTG
SQ  IVFGAKSAENKSRPGFVFGSSSVVGGSTLNPSTAAASAPESSGSLIFGVTSSSTPGTETSKISASSAATNTGNSVFGTSS
SQ  FAFTSSGSSMVGGVSASTGSSVFGFNAVSSASATSSQSQASNLFGAGNAQTGNTGSGTTTSTQSIPFQFGSSPSAPSFGL
SQ  SGNSSLASNSSPFGFSKSEPAVFTSVSTPQLSSTNSSASSSSTMSSPLFGTSWQAPNSSPNSGPVFSSSFTTSSTPTTFS
SQ  FGGSSAATVSSTTTPIFGASTNNTPSPSPIFGFGSTPPTTPQQPVFGNSGTPSQSLFGNSTPGFAFGAPNNGNGINNNQQ
SQ  VSMEDSMAEDTDQANRASMVAPMFGQAAVSMPQPNFAFGGGAATQPPSMANPFQFGGQPMASTLQNASPFQASQSLEFQG
SQ  GGSFSLGSTGGGDKSGRRIFKAKKSTRKK
//
ID  P20676;
PN  Nucleoporin NUP1;
GN  NUP1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side.
DR  UNIPROT: P20676;
DR  UNIPROT: D6W2F9;
DR  PDB: 4C31;
DR  PDB: 4MBE;
DR  PDB: 5OWU;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP1 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP2 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1- KAP95-cargo complex in the nucleus, NUP1 binds through its C-terminus to KAP95, thus accelerating the release of KAP95 and, indirectly, of the nuclear localization signal (NLS)-containing cargo from the SRP1- KAP95-cargo complex. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11046143, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11535617, ECO:0000269|PubMed:11867631, ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401, ECO:0000269|PubMed:15039779}.
DE  Reference Proteome: Yes;
DE  Interaction: Q05911; IntAct: EBI-393543; Score: 0.37
DE  Interaction: Q03818; IntAct: EBI-393546; Score: 0.37
DE  Interaction: P38696; IntAct: EBI-393549; Score: 0.37
DE  Interaction: P54861; IntAct: EBI-393552; Score: 0.37
DE  Interaction: P38791; IntAct: EBI-393555; Score: 0.37
DE  Interaction: Q05080; IntAct: EBI-393558; Score: 0.52
DE  Interaction: P32864; IntAct: EBI-393561; Score: 0.37
DE  Interaction: P19524; IntAct: EBI-393564; Score: 0.37
DE  Interaction: P20435; IntAct: EBI-393567; Score: 0.37
DE  Interaction: P34223; IntAct: EBI-393570; Score: 0.37
DE  Interaction: Q03148; IntAct: EBI-393573; Score: 0.37
DE  Interaction: P35497; IntAct: EBI-393576; Score: 0.37
DE  Interaction: P35210; IntAct: EBI-393579; Score: 0.37
DE  Interaction: Q00764; IntAct: EBI-393582; Score: 0.37
DE  Interaction: P30402; IntAct: EBI-393585; Score: 0.37
DE  Interaction: Q12206; IntAct: EBI-393588; Score: 0.37
DE  Interaction: P39718; IntAct: EBI-393591; Score: 0.37
DE  Interaction: P25651; IntAct: EBI-393594; Score: 0.37
DE  Interaction: Q03900; IntAct: EBI-393597; Score: 0.37
DE  Interaction: P53184; IntAct: EBI-393600; Score: 0.37
DE  Interaction: P35727; IntAct: EBI-393603; Score: 0.37
DE  Interaction: P36023; IntAct: EBI-393606; Score: 0.37
DE  Interaction: Q08229; IntAct: EBI-393609; Score: 0.37
DE  Interaction: Q06608; IntAct: EBI-393612; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P11484; IntAct: EBI-789997; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-789997; Score: 0.35
DE  Interaction: Q02821; IntAct: EBI-789997; Score: 0.69
DE  Interaction: Q06142; IntAct: EBI-789997; Score: 0.77
DE  Interaction: P10081; IntAct: EBI-805439; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-805439; Score: 0.35
DE  Interaction: P00560; IntAct: EBI-805439; Score: 0.35
DE  Interaction: P06168; IntAct: EBI-805439; Score: 0.35
DE  Interaction: P00950; IntAct: EBI-805439; Score: 0.35
DE  Interaction: P14540; IntAct: EBI-805439; Score: 0.35
DE  Interaction: P00925; IntAct: EBI-805439; Score: 0.35
DE  Interaction: P32324; IntAct: EBI-805439; Score: 0.35
DE  Interaction: P41832; IntAct: EBI-805439; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-805439; Score: 0.35
DE  Interaction: P28003; IntAct: EBI-815383; Score: 0.27
DE  Interaction: Q03771; IntAct: EBI-817249; Score: 0.27
DE  Interaction: P34160; IntAct: EBI-7438784; Score: 0.40
DE  Interaction: P13259; IntAct: EBI-7438800; Score: 0.40
DE  Interaction: Q04175; IntAct: EBI-1173466; Score: 0.40
DE  Interaction: Q99257; IntAct: EBI-2124355; Score: 0.40
DE  Interaction: P34232; IntAct: EBI-2124355; Score: 0.40
DE  Interaction: P46674; IntAct: EBI-2124372; Score: 0.40
DE  Interaction: P10591; IntAct: EBI-3673730; Score: 0.35
DE  Interaction: P16474; IntAct: EBI-3705579; Score: 0.35
DE  Interaction: P36016; IntAct: EBI-3707779; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3721414; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3750951; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-4383599; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-4388449; Score: 0.35
DE  Interaction: P52297; IntAct: EBI-6285121; Score: 0.44
DE  Interaction: Q08379; IntAct: EBI-11523930; Score: 0.56
DE  Interaction: P51116; IntAct: EBI-11523941; Score: 0.56
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0006607;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSSNTSSVMSSPRVEKRSFSSTLKSFFTNPNKKRPSSKKVFSSNLSYANHLEESDVEDTLHVNKRKRVSGTSQHSDSLTQ
SQ  NNNNAPIIIYGTENTERPPLLPILPIQRLRLLREKQRVRNMRELGLIQSTEFPSITSSVILGSQSKSDEGGSYLCTSSTP
SQ  SPIKNGSCTRQLAGKSGEDTNVGLPILKSLKNRSNRKRFHSQSKGTVWSANFEYDLSEYDAIQKKDNKDKEGNAGGDQKT
SQ  SENRNNIKSSISNGNLATGPNLTSEIEDLRADINSNRLSNPQKNLLLKGPASTVAKTAPIQESFVPNSERSGTPTLKKNI
SQ  EPKKDKESIVLPTVGFDFIKDNETPSKKTSPKATSSAGAVFKSSVEMGKTDKSTKTAEAPTLSFNFSQKANKTKAVDNTV
SQ  PSTTLFNFGGKSDTVTSASQPFKFGKTSEKSENHTESDAPPKSTAPIFSFGKQEENGDEGDDENEPKRKRRLPVSEDTNT
SQ  KPLFDFGKTGDQKETKKGESEKDASGKPSFVFGASDKQAEGTPLFTFGKKADVTSNIDSSAQFTFGKAATAKETHTKPSE
SQ  TPATIVKKPTFTFGQSTSENKISEGSAKPTFSFSKSEEERKSSPISNEAAKPSFSFPGKPVDVQAPTDDKTLKPTFSFTE
SQ  PAQKDSSVVSEPKKPSFTFASSKTSQPKPLFSFGKSDAAKEPPGSNTSFSFTKPPANETDKRPTPPSFTFGGSTTNNTTT
SQ  TSTKPSFSFGAPESMKSTASTAAANTEKLSNGFSFTKFNHNKEKSNSPTSFFDGSASSTPIPVLGKPTDATGNTTSKSAF
SQ  SFGTANTNGTNASANSTSFSFNAPATGNGTTTTSNTSGTNIAGTFNVGKPDQSIASGNTNGAGSAFGFSSSGTAATGAAS
SQ  NQSSFNFGNNGAGGLNPFTSATSSTNANAGLFNKPPSTNAQNVNVPSAFNFTGNNSTPGGGSVFNMNGNTNANTVFAGSN
SQ  NQPHQSQTPSFNTNSSFTPSTVPNINFSGLNGGITNTATNALRPSDIFGANAASGSNSNVTNPSSIFGGAGGVPTTSFGQ
SQ  PQSAPNQMGMGTNNGMSMGGGVMANRKIARMRHSKR
//
ID  P32499;
PN  Nucleoporin NUP2;
GN  NUP2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side.
DR  UNIPROT: P32499;
DR  UNIPROT: D6VYX5;
DR  UNIPROT: Q06130;
DR  PDB: 1UN0;
DR  PDB: 2C1T;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP2 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP1 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1- KAP95-cargo complex in the nucleus, NUP2 binds through its N-terminus to the SRP1 nuclear localization signal (NLS) binding site, thus accelerating the release of the NLS-cargo. SRP1 in turn is released from NUP2 by binding of the GSP1-GTP associated export factor CSE1. NUP2 may also have a chromatin boundary/insulator activity through indirect interaction with genomic DNA via CSE1 and blocking of heterochromatin spreading. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11046143, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11425876, ECO:0000269|PubMed:11535617, ECO:0000269|PubMed:11867631, ECO:0000269|PubMed:12062099, ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401, ECO:0000269|PubMed:14514698, ECO:0000269|PubMed:15039779}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-6322490; Score: 0.00
DE  Interaction: P38910; IntAct: EBI-390864; Score: 0.37
DE  Interaction: Q06142; IntAct: EBI-784458; Score: 0.78
DE  Interaction: P32799; IntAct: EBI-792386; Score: 0.35
DE  Interaction: P53833; IntAct: EBI-799459; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-801825; Score: 0.35
DE  Interaction: P09734; IntAct: EBI-801825; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-801825; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-801825; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-801825; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-801825; Score: 0.53
DE  Interaction: Q02821; IntAct: EBI-801825; Score: 0.78
DE  Interaction: P10659; IntAct: EBI-801825; Score: 0.35
DE  Interaction: P39705; IntAct: EBI-801825; Score: 0.70
DE  Interaction: P40069; IntAct: EBI-801825; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-801825; Score: 0.35
DE  Interaction: P00830; IntAct: EBI-801825; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-801825; Score: 0.35
DE  Interaction: P28003; IntAct: EBI-815383; Score: 0.27
DE  Interaction: P19414; IntAct: EBI-819202; Score: 0.27
DE  Interaction: Q02159; IntAct: EBI-861199; Score: 0.00
DE  Interaction: Q12453; IntAct: EBI-7200346; Score: 0.27
DE  Interaction: P32499; IntAct: EBI-1270044; Score: 0.00
DE  Interaction: P46673; IntAct: EBI-1270055; Score: 0.00
DE  Interaction: P38181; IntAct: EBI-1270066; Score: 0.00
DE  Interaction: P34077; IntAct: EBI-6322501; Score: 0.00
DE  Interaction: P47054; IntAct: EBI-6322512; Score: 0.00
DE  Interaction: P48837; IntAct: EBI-6322523; Score: 0.00
DE  Interaction: Q02199; IntAct: EBI-6322534; Score: 0.00
DE  Interaction: Q12306; IntAct: EBI-2346559; Score: 0.37
DE  Interaction: P39101; IntAct: EBI-3653629; Score: 0.35
DE  Interaction: P40358; IntAct: EBI-3657516; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3673762; Score: 0.35
DE  Interaction: P16474; IntAct: EBI-3705587; Score: 0.35
DE  Interaction: P0CS90; IntAct: EBI-3706579; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3721422; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3727438; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-3734635; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3745795; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3750983; Score: 0.35
DE  Interaction: P09435; IntAct: EBI-3775534; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3790807; Score: 0.35
DE  Interaction: P50875; IntAct: EBI-4376349; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-4380099; Score: 0.35
DE  Interaction: P38129; IntAct: EBI-4389629; Score: 0.35
DE  Interaction: P32835; IntAct: EBI-11888940; Score: 0.37
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0042564;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0044615;
GO  GO:0061676;
GO  GO:0031267;
GO  GO:0017056;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006611;
GO  GO:0036228;
GO  GO:0050790;
GO  GO:0030466;
GO  GO:0031509;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQ
SQ  VDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKS
SQ  SDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKT
SQ  ETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTF
SQ  GSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQ
SQ  EDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINT
SQ  NTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKG
SQ  SQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKK
SQ  DDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK
//
ID  O04326;
PN  Nuclear pore complex protein NUP35;
GN  NUP35;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: O04326;
DR  UNIPROT: Q8VYL9;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: O22690; IntAct: EBI-4483168; Score: 0.37
DE  Interaction: O48741; IntAct: EBI-4484304; Score: 0.37
DE  Interaction: O65397; IntAct: EBI-4485024; Score: 0.37
DE  Interaction: O80594; IntAct: EBI-4485424; Score: 0.37
DE  Interaction: O80895; IntAct: EBI-4485688; Score: 0.37
DE  Interaction: O81062; IntAct: EBI-4485920; Score: 0.37
DE  Interaction: O82174; IntAct: EBI-4486168; Score: 0.37
DE  Interaction: O82219; IntAct: EBI-4486216; Score: 0.37
DE  Interaction: P26587; IntAct: EBI-4487248; Score: 0.37
DE  Interaction: P27202; IntAct: EBI-4487288; Score: 0.37
DE  Interaction: P30302; IntAct: EBI-4487472; Score: 0.37
DE  Interaction: P42813; IntAct: EBI-4487936; Score: 0.37
DE  Interaction: P47192; IntAct: EBI-4488256; Score: 0.37
DE  Interaction: P53799; IntAct: EBI-4488704; Score: 0.37
DE  Interaction: P82874; IntAct: EBI-4489032; Score: 0.37
DE  Interaction: P92941; IntAct: EBI-4489112; Score: 0.37
DE  Interaction: Q147J7; IntAct: EBI-4490232; Score: 0.37
DE  Interaction: Q38935; IntAct: EBI-4490872; Score: 0.37
DE  Interaction: Q41975; IntAct: EBI-4491832; Score: 0.37
DE  Interaction: Q42328; IntAct: EBI-4491888; Score: 0.37
DE  Interaction: Q42342; IntAct: EBI-4491936; Score: 0.37
DE  Interaction: Q5XF13; IntAct: EBI-4492424; Score: 0.37
DE  Interaction: Q5XF36; IntAct: EBI-4492504; Score: 0.37
DE  Interaction: Q6IDC5; IntAct: EBI-4492944; Score: 0.37
DE  Interaction: Q6NLF5; IntAct: EBI-4493104; Score: 0.37
DE  Interaction: Q7XA86; IntAct: EBI-4494128; Score: 0.37
DE  Interaction: Q84WI4; IntAct: EBI-4495504; Score: 0.37
DE  Interaction: Q8GWH4; IntAct: EBI-4496464; Score: 0.37
DE  Interaction: Q8GWM8; IntAct: EBI-4496504; Score: 0.37
DE  Interaction: Q8GWT5; IntAct: EBI-4496664; Score: 0.37
DE  Interaction: Q8GX78; IntAct: EBI-4496984; Score: 0.37
DE  Interaction: Q8GYN0; IntAct: EBI-4497896; Score: 0.37
DE  Interaction: Q8L586; IntAct: EBI-4499328; Score: 0.37
DE  Interaction: Q8LB17; IntAct: EBI-4501032; Score: 0.37
DE  Interaction: Q8LF05; IntAct: EBI-4501592; Score: 0.37
DE  Interaction: Q8RXL7; IntAct: EBI-4502608; Score: 0.37
DE  Interaction: Q8RY62; IntAct: EBI-4502912; Score: 0.37
DE  Interaction: Q93VN2; IntAct: EBI-4505896; Score: 0.37
DE  Interaction: Q93XX0; IntAct: EBI-4506336; Score: 0.37
DE  Interaction: Q93Z42; IntAct: EBI-4506704; Score: 0.37
DE  Interaction: Q93ZQ3; IntAct: EBI-4507008; Score: 0.37
DE  Interaction: Q93ZW4; IntAct: EBI-4507128; Score: 0.37
DE  Interaction: Q946Y7; IntAct: EBI-4508064; Score: 0.37
DE  Interaction: Q94A32; IntAct: EBI-4508296; Score: 0.37
DE  Interaction: Q94A99; IntAct: EBI-4508416; Score: 0.37
DE  Interaction: Q94CH8; IntAct: EBI-4509944; Score: 0.37
DE  Interaction: Q94JU2; IntAct: EBI-4510240; Score: 0.37
DE  Interaction: Q9C933; IntAct: EBI-4512656; Score: 0.37
DE  Interaction: Q9CAN1; IntAct: EBI-4513208; Score: 0.37
DE  Interaction: Q9FI47; IntAct: EBI-4515080; Score: 0.37
DE  Interaction: Q9FZ98; IntAct: EBI-4518152; Score: 0.37
DE  Interaction: Q9LJU6; IntAct: EBI-4519584; Score: 0.37
DE  Interaction: Q9LQ32; IntAct: EBI-4520368; Score: 0.37
DE  Interaction: Q9LSW5; IntAct: EBI-4520960; Score: 0.37
DE  Interaction: Q9LVD9; IntAct: EBI-4522072; Score: 0.37
DE  Interaction: Q9LXV1; IntAct: EBI-4522872; Score: 0.37
DE  Interaction: Q9LYP1; IntAct: EBI-4523096; Score: 0.37
DE  Interaction: Q9M1J1; IntAct: EBI-4523968; Score: 0.37
DE  Interaction: Q9M1J7; IntAct: EBI-4524024; Score: 0.37
DE  Interaction: Q9M2J9; IntAct: EBI-4524480; Score: 0.37
DE  Interaction: Q9M9S6; IntAct: EBI-4525160; Score: 0.37
DE  Interaction: Q9SA23; IntAct: EBI-4526056; Score: 0.37
DE  Interaction: Q9SD04; IntAct: EBI-4526664; Score: 0.37
DE  Interaction: Q9SHG7; IntAct: EBI-4527224; Score: 0.37
DE  Interaction: Q9SIH4; IntAct: EBI-4527504; Score: 0.37
DE  Interaction: Q9SIQ8; IntAct: EBI-4527608; Score: 0.37
DE  Interaction: Q9SRE4; IntAct: EBI-4529352; Score: 0.37
DE  Interaction: Q9SRT3; IntAct: EBI-4529576; Score: 0.37
DE  Interaction: Q9STW3; IntAct: EBI-4529896; Score: 0.37
DE  Interaction: Q9XI60; IntAct: EBI-4531808; Score: 0.37
DE  Interaction: Q9ZSD4; IntAct: EBI-4532304; Score: 0.37
DE  Interaction: Q9ZV66; IntAct: EBI-4532744; Score: 0.37
GO  GO:0031965;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAAAHRTPKSGRQSLLFQDLASPVSARRGKFSSPGQAAAVSALWRENFGGSDLPPPPMYTLDDRSDFSPESGIADYSAS
SQ  PDAKSDRRTPFQSSGKNIVTPGKGKLEASPSFSLLNAQQSQQVSGSPSWWSQSKAGSSTEQDDKGKGSPVEGVVQPGALV
SQ  TLPPPREVARPEVQRQIIPTGNLDEEEWVTVYGFSPGDTNLVLREFEKCGMVLKHVPGPRNANWMHILYQNRSDAHKALN
SQ  KAGMMINGVVIVGVKPVDPIQKQALNERLNNQGFMPLPPPSSTRNTARPLSRPQYLQNGSAFSPQPSGGAMASPSKSMVS
SQ  KFFDLMFGV
//
ID  Q09601;
PN  Nucleoporin NUP35;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane {ECO:0000269|PubMed:12937276}.
DR  UNIPROT: Q09601;
DR  UNIPROT: O62340;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (By similarity). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). Required for the proper organization of chromosomes on the mitotic spindle during anaphase (PubMed:28122936). {ECO:0000250|UniProtKB:Q8NFH5, ECO:0000269|PubMed:28122936}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9BKT9; IntAct: EBI-6455766; Score: 0.37
DE  Interaction: O45599; IntAct: EBI-6455990; Score: 0.37
DE  Interaction: Q8ITV6; IntAct: EBI-6458240; Score: 0.37
DE  Interaction: G5ECY0; IntAct: EBI-6458611; Score: 0.37
DE  Interaction: Q9XVU8; IntAct: EBI-6459588; Score: 0.37
DE  Interaction: Q21443; IntAct: EBI-6460126; Score: 0.37
DE  Interaction: P90925; IntAct: EBI-6460291; Score: 0.37
DE  Interaction: Q18025; IntAct: EBI-6460356; Score: 0.37
DE  Interaction: Q09601; IntAct: EBI-6460761; Score: 0.37
DE  Interaction: P91001; IntAct: EBI-6460931; Score: 0.37
DE  Interaction: Q95Y13; IntAct: EBI-6461344; Score: 0.37
DE  Interaction: G5EGG0; IntAct: EBI-6461649; Score: 0.37
DE  Interaction: P18948; IntAct: EBI-6461689; Score: 0.37
DE  Interaction: O76447; IntAct: EBI-6462243; Score: 0.37
DE  Interaction: Q19749; IntAct: EBI-6462303; Score: 0.37
DE  Interaction: P34331; IntAct: EBI-6463029; Score: 0.37
DE  Interaction: Q19890; IntAct: EBI-6463704; Score: 0.37
DE  Interaction: Q22866; IntAct: EBI-6463711; Score: 0.37
DE  Interaction: P34604; IntAct: EBI-6463725; Score: 0.37
DE  Interaction: H2KYA1; IntAct: EBI-11469945; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0009792;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006997;
GO  GO:0006355;
GO  GO:0007096;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFSHLNQNTSGRHNSMDLNNSSISNFGTPVEQSTPALLFGKRKATVPSSYTASPLNTASAPCSDIFAVSAPAVPQHLKDT
SQ  PGSKSVHWSPSLVQSGEKSAAQTQNTPANLSFGGNSSFSAPTKPAPQSIQTSSFGGQAMHAPPLRSLRDKVEPAKKISRR
SQ  NTFTARSTPLSTPITQRVTSRLAEAEEQPMEEEADAADTWVTVFGFQPSQVSILLNLFSRHGEVVSHQTPSKGNFIHMRY
SQ  SCVTHAQQAISRNGTLLDQDTFIGVVQCTNKDVINGSASGIVARSSNIAAAANRSASMYNSFVENDMADQSVNHNENSVL
SQ  NSSNVFDANNSLNSSRISVRSGVGMRPLAADQRTNILQGTPSVRKAPDGLLNKFWNTIGLN
//
ID  Q6P6X9;
PN  Nucleoporin NUP35;
GN  nup35;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}.
DR  UNIPROT: Q6P6X9;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEIQSCIEPMTLGSPTSPKPGAQFLPGFLMGDLPAPVTPQPRSFGLTGGAEIRSPLLAGGSPPQPVVPTPKDKSGAPPVR
SQ  SIYDDLNGSAVGMSPLAARKQPFAGVHTPLSGLQGTPGTVSNFFSPVSQQRKTTLSPAQVDPFFTQGDALSSEDQLDDTW
SQ  ITVFGFPPASASYILLQFAQYGNILKHVMSNTGNWMHVQYQSKLQARKALSKDGKIFGEAIMIGVKPCIDKSVMESLDKG
SQ  STSSSVFTPPVKAPCTPSHPLSTPRSVMRPLSAAYKASSSDYQVVSDQQTPKKDESFVSKAMEYMFGW
//
ID  Q9VWS2;
PN  Nucleoporin Nup35;
GN  Nup35;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000255|PIRNR:PIRNR038119}.
DR  UNIPROT: Q9VWS2;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (By similarity). May have a role in the organization of the inner nuclear membrane proteins at the nuclear envelope together with Nup154 (PubMed:22718353). {ECO:0000250|UniProtKB:Q8NFH5, ECO:0000269|PubMed:22718353}.
DE  Reference Proteome: Yes;
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: Q9VH02; IntAct: EBI-9964836; Score: 0.35
DE  Interaction: O46339; IntAct: EBI-9966612; Score: 0.35
DE  Interaction: Q8STG9; IntAct: EBI-9966894; Score: 0.35
DE  Interaction: Q9W0N3; IntAct: EBI-15174078; Score: 0.49
DE  Interaction: Q9VMY2; IntAct: EBI-26744855; Score: 0.49
DE  Interaction: Q9XZ06; IntAct: EBI-26744845; Score: 0.49
DE  Interaction: Q9VWS2; IntAct: EBI-26744835; Score: 0.49
GO  GO:0031965;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEPMNLGSPVNSPGSNQTQYLPPFLLGDPQGITPHKNTLSPKTGRSNISFATSPGGSSPHELNRSALSTRTLFAAQGGAH
SQ  TAVGANSSTTAHGQTHSHHQTGPPTQGLFDSLREQSVTPKKKNHLGMLQLQSPNQSYQSSYHTNDSFAPGAPNAINASMR
SQ  ALCSPLGATASPAGGLGTSVTTGGNSRLSDFWVTIFGFPPGAGSMVLQHFTVCGTIVDVVHAPQNGNWMYVRYSSRIESD
SQ  KALNYNEKIIAGNVMVGVSRCTDRSVIDKENIGSVPNAEIGDPPTSPSAIRPFSQQSYKLARKDNIISPQKDVPQKSSGL
SQ  MDKAMDLIFGW
//
ID  Q8NFH5;
PN  Nucleoporin NUP35;
GN  NUP35;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12196509}. Nucleus membrane {ECO:0000269|PubMed:15703211}; Peripheral membrane protein {ECO:0000269|PubMed:15703211}. Note=Tightly associated with the nuclear membrane and lamina. {ECO:0000269|PubMed:15703211}.
DR  UNIPROT: Q8NFH5;
DR  UNIPROT: B4DP57;
DR  UNIPROT: B4DYB4;
DR  UNIPROT: Q4ZFZ9;
DR  UNIPROT: Q53S95;
DR  UNIPROT: Q8TDJ1;
DR  PDB: 4LIR;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DR  OMIM: 608140;
DR  DisGeNET: 129401;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC. {ECO:0000269|PubMed:15703211}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-16796036; Score: 0.27
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-11889606; Score: 0.37
DE  Interaction: Q8WYP5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: P14618; IntAct: EBI-9355861; Score: 0.44
DE  Interaction: P89884; IntAct: EBI-9639903; Score: 0.37
DE  Interaction: Q7L273; IntAct: EBI-10256086; Score: 0.78
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q13526; IntAct: EBI-25252486; Score: 0.56
DE  Interaction: Q8WVK2; IntAct: EBI-21500567; Score: 0.35
DE  Interaction: Q96HA8; IntAct: EBI-21531905; Score: 0.35
DE  Interaction: P09067; IntAct: EBI-21543288; Score: 0.35
DE  Interaction: Q96C01; IntAct: EBI-21554623; Score: 0.35
DE  Interaction: Q9BSU1; IntAct: EBI-21632268; Score: 0.35
DE  Interaction: P48544; IntAct: EBI-21754197; Score: 0.35
DE  Interaction: Q96K76; IntAct: EBI-21756437; Score: 0.35
DE  Interaction: P23416; IntAct: EBI-21770176; Score: 0.35
DE  Interaction: P04798; IntAct: EBI-21774067; Score: 0.35
DE  Interaction: Q9NQA5; IntAct: EBI-21851282; Score: 0.35
DE  Interaction: Q9Y6H3; IntAct: EBI-21893119; Score: 0.35
DE  Interaction: Q9BV10; IntAct: EBI-21896207; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-21302175; Score: 0.35
DE  Interaction: Q8N5V2; IntAct: EBI-25408394; Score: 0.35
DE  Interaction: Q9P107; IntAct: EBI-25408937; Score: 0.35
DE  Interaction: Q8IW93; IntAct: EBI-25410221; Score: 0.35
DE  Interaction: Q9NR80; IntAct: EBI-25411315; Score: 0.35
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0005886;
GO  GO:0042802;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:1990830;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006355;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:15703211};
SQ  MAAFAVEPQGPALGSEPMMLGSPTSPKPGVNAQFLPGFLMGDLPAPVTPQPRSISGPSVGVMEMRSPLLAGGSPPQPVVP
SQ  AHKDKSGAPPVRSIYDDISSPGLGSTPLTSRRQPNISVMQSPLVGVTSTPGTGQSMFSPASIGQPRKTTLSPAQLDPFYT
SQ  QGDSLTSEDHLDDSWVTVFGFPQASASYILLQFAQYGNILKHVMSNTGNWMHIRYQSKLQARKALSKDGRIFGESIMIGV
SQ  KPCIDKSVMESSDRCALSSPSLAFTPPIKTLGTPTQPGSTPRISTMRPLATAYKASTSDYQVISDRQTPKKDESLVSKAM
SQ  EYMFGW
//
ID  Q8R4R6;
PN  Nucleoporin NUP35;
GN  Nup35;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane {ECO:0000250|UniProtKB:Q8NFH5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NFH5}. Note=Tightly associated with the nuclear membrane and lamina. {ECO:0000250|UniProtKB:Q8NFH5}.
DR  UNIPROT: Q8R4R6;
DR  UNIPROT: A2ATJ3;
DR  UNIPROT: Q9D7J2;
DR  PDB: 1WWH;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0005886;
GO  GO:0042802;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:1990830;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006355;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8NFH5};
SQ  MAAFAVDPQAPTLGSEPMMLGSPTSPKTGANAQFLPGFLMGDLPAPVTPQPRSISGPSVGVMEMRSPLLAGGSPPQPVVP
SQ  AHKDKSGAPPVRSIYDDISSPGLGSTPLTSRRQANISLLQSPLVGATTPVPGQSMFSPANIGQPRKTTLSPAQLDPFYTQ
SQ  GDSLTSEDHLDDTWVTVFGFPQASASYILLQFAQYGNILKHVMSNTGNWMHIRYQSKLQARKALSKDGRIFGESIMIGVK
SQ  PCIDKNVMENSDRGVLSSPSLAFTTPIRTLGTPTQSGSTPRVSTMRPLATAYKASTSDYQVISDRQTPKKDESLVSRAME
SQ  YMFGW
//
ID  Q68FY1;
PN  Nucleoporin NUP35;
GN  Nup35;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane {ECO:0000250|UniProtKB:Q8NFH5, ECO:0000269|PubMed:15703211}; Peripheral membrane protein {ECO:0000269|PubMed:15703211}. Note=Tightly associated with the nuclear membrane and lamina. {ECO:0000250|UniProtKB:Q8NFH5}.
DR  UNIPROT: Q68FY1;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005652;
GO  GO:0031965;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0042802;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:1990830;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:15703211};
SQ  MAAFAVDPQAPTLGSEPMMLGSPTSPKPGANAQFLPGFLMGDLPAPVTPQPRSISGPSVGVMEMRSPLLAGGSPPQPVVP
SQ  AHKDKSGAPPVRSIYDDISSPGLGSTPLPSRRQANISVLQSPLVGVTTPVTGQSMFSPANIGQPRKTTLSPAQLDPFYTQ
SQ  GDSLTSEDHLDDTWVTVFGFPQASASYILLQFAQYGNILKHVMSNTGNWMHIRYQSKLQARKALSKDGRIFGESIMIGVK
SQ  PCIDKNVMENSDRGVLSSPSLAFTPPIRTLGTPTQPGSTPRVSTMRPLATAYKASTSDYQVISDRQTPKKDESLVSRAME
SQ  YMFGW
//
ID  Q66IJ0;
PN  Nucleoporin NUP35;
GN  nup35;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}.
DR  UNIPROT: Q66IJ0;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAFSMEPMGAEPMALGSPTSPKPSAGAQFLPGFLLGDIPTPVTPQQRPSIGVMEMRSPLLSGGSPPQPVVPTHKDKSGA
SQ  PPVRSIYDDIASPGLGSTPLNPRKTASFSVLHTPLSGVIPSSPECKNISGSRKRPASSVFSPATIGHSRKTTLSPAQMDP
SQ  FYTQGDALTSDDQLDDTWVTVFGFPQASASYILLQFAQYGNIIKHVMSNNGNWMHIQYQSKLQARKALSKDGRIFGESIM
SQ  IGVKPCIDKSVMEATEKVSTPTVSSVFTPPVKNIGTPTQSVGTPRAASMRPLAATYKTPASADYQVVADKQAPRKDESIV
SQ  SKAMEYMFGW
//
ID  G0S2X1;
PN  Nucleoporin NUP37;
GN  NUP37;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH4}.
DR  UNIPROT: G0S2X1;
DR  UNIPROT: G0ZGV1;
DR  PROSITE: PS00678;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: G0S0E7; IntAct: EBI-16069404; Score: 0.66
DE  Interaction: G0S2G1; IntAct: EBI-16069404; Score: 0.56
DE  Interaction: G0SDQ4; IntAct: EBI-16069488; Score: 0.35
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALQPVPRMRRTLQNTQHTYSLGRRIYDVKTYPVQSPQGATILIYGHENGATVVWRGGRRLKPPKPQTNEKRNGTKPEDA
SQ  VMIIDSDDETGPTFVDKPEFEDSPSVADGSVAEIIQTLDLALGTAVNHIAVLPMPPCAAEDASWNGANILKTKIVFAVTC
SQ  ATNDVYVITLPLTPPSHEAKARPELRKSLLAGNAGKGVWGETLTLLTGPSRSCNGVAISLVKHRSSSRSRSSERSAAQAA
SQ  PITRVVVAAHSREASGTLRLWDVPLEAKPGTINRVEPFQTEYLPSPLTSISFNPVNLTQLLTVASPHAVRIYDYATASLP
SQ  SDDTSEGPFPSQGSWLISLYPPFARGPAMSTSRKPIVAAEWIARGRAILTLLADGQWGIWDLDGASPTAAGGGSNLFSKT
SQ  SAGLRGTAITAFSVTGHLEGTSPLRNPTTQKASSSSSGEFVPMTPHTRRDAIATAFGGSPEKLAAVRGGITVAQLPSTLT
SQ  SGAGDESAVLFLGGADPIVCVIPVLSKFWDSQLRRAAGGGVNLWSGAQPTRMIRLTDLSAGLLGERCTGAVAITKAVRAN
SQ  ASTNGILKEDDNSGSQGLPIEVLLQGESRLVIVHENGDAPTSSLTSRLLGARKKQRDEFKSVNAIVAYPPLEKPSVSFNL
SQ  NLTQRPEKPGTLFAPRSRHSKSLFEQSIDTIPSTDAGDEETIPATSAPSSQQGFMFATDLELAADLPDDEADAEGRDVEQ
SQ  ELLDIMEIDRELEQLEQARERGRKRVFFEEG
//
ID  Q9VBU8;
PN  Nucleoporin Nup37;
GN  Nup37;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH4}.
DR  UNIPROT: Q9VBU8;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: As part of the nuclear pore complex (NPC), has a role in its assembly and function. {ECO:0000250|UniProtKB:Q8NFH4}. (Microbial infection) Required for optimal replication of E.chaffeensis. {ECO:0000269|PubMed:22851751}.
DE  Reference Proteome: Yes;
GO  GO:0031080;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRSVIEPDHSIQLNEAIYCYDICTNDFAYNLIAVAFRKHLSLLLVGLPEESGEFGYTRLQDMDLGEKEQRSVSALAFSPD
SQ  TSLNCTPNNVTLCAANGSQLKLYRTDLGQFTSLQVLRGHGDYVNDVSWVCDGELLASVSDDFTCRFWTTTGGGENVITFG
SQ  LSSAGMSVKSHPEDPNKVLVAEKKGIIHLYNVTLKQTVISVESPKFPLMSADWAHSNRLFITSLAGGDVVTWDLNRPYVP
SQ  ADVKQVHEDCGRVVRFAPGSSEMVIAMVIGLTLKVFAAKSTVPLLEASLKSYGGMAWHQRLPYISAVSDRKLLFWKVQMK
//
ID  Q8NFH4;
PN  Nucleoporin Nup37;
GN  NUP37;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore. Nucleus, nuclear pore complex.
DR  UNIPROT: Q8NFH4;
DR  UNIPROT: Q9H644;
DR  PDB: 5A9Q;
DR  PDB: 7PEQ;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 609264;
DR  OMIM: 618179;
DR  DisGeNET: 79023;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. {ECO:0000269|PubMed:17363900, ECO:0000269|PubMed:30179222}.
DE  Disease: Microcephaly 24, primary, autosomal recessive (MCPH24) [MIM:618179]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH24 patients additionally manifest mildly impaired intellectual development, cerebellar vermis hypoplasia, and fifth finger clinodactyly. {ECO:0000269|PubMed:30179222}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P12270; IntAct: EBI-11888966; Score: 0.37
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-11888954; Score: 0.66
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.53
DE  Interaction: Q12769; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q60952; IntAct: EBI-11075169; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q8BH74; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q8NFH3; IntAct: EBI-21865034; Score: 0.53
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-9050503; Score: 0.62
DE  Interaction: Q9BW27; IntAct: EBI-9032422; Score: 0.56
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8R023; IntAct: EBI-11034239; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: O88952; IntAct: EBI-11079007; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q8WXG6; IntAct: EBI-20934860; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q13242; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: O75494; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: Q86U42; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: P62987; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: Q8ND56; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: P55212; IntAct: EBI-25835597; Score: 0.56
DE  Interaction: P13473; IntAct: EBI-25873962; Score: 0.56
DE  Interaction: O43464; IntAct: EBI-27050249; Score: 0.35
DE  Interaction: Q96LU5; IntAct: EBI-27050332; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKQDASRNAAYTVDCEDYVHVVEFNPFENGDSGNLIAYGGNNYVVIGTCTFQEEEADVEGIQYKTLRTFHHGVRVDGIAW
SQ  SPETRLDSLPPVIKFCTSAADMKIRLFTSDLQDKNEYKVLEGHTDFINGLVFDPKEGQEIASVSDDHTCRIWNLEGVQTA
SQ  HFVLHSPGMSVCWHPEETFKLMVAEKNGTIRFYDLLAQQAILSLESEQVPLMSAHWCLKNTFKVGAVAGNDWLIWDITRS
SQ  SYPQNKRPVHMDRACLFRWSTISENLFATTGYPGKMASQFQIHHLGHPQPILMGSVAVGSGLSWHRTLPLCVIGGDHKLL
SQ  FWVTEV
//
ID  Q9CWU9;
PN  Nucleoporin Nup37;
GN  Nup37;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q9CWU9;
DR  UNIPROT: Q9CZ80;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKQDATRNAAYTVDCEDYVHVVEFNPFESGDSGNLIAYGGSNYVVVGMCTFQEEETDIEGIQYKTLRTFHHGVRVDGIAW
SQ  SPETKLDSLPPVIKFCTSAADLKIRLFTSDLQDKNEYKVLEGHSDFINDLVFHPKEGQELASVSDDHTCRIWNLEGKQTA
SQ  HFLLHSPGMSVCWHPEETFKLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHWCLKNTFKVGAVAGNDWIIWDITRS
SQ  SYPQETRPVHMDRAHLFRWSAISENLFATTGYPGKMASQFQIHHLGHSQPVLIGSVAVGSGLSWHRTLPLCAVGGDHKLL
SQ  FWVTEI
//
ID  O13838;
PN  Nucleoporin nup40;
GN  nup40;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
DR  UNIPROT: O13838;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006355;
GO  GO:0006407;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSFGGSGSITNRSTLKPLSVDDLRSPSPQKEYRGFRTSVSNIPQEKKFVPSHLSHFGSSQQRRFAPEVSSPLAEPYESSS
SQ  SFRLSLSSPPSSKFGGPSFGTPKPFLHTNRLGTGSLIEDAPPTQSIYDFSSSRQINALNVGQSSSPFSPVSEKVYDPSFT
SQ  MSGAPQDSNTSVIVFGFPPELTNQVIAEFSRFGTIISENSLTASSAGFTPSKGPISGNWLQLTYAEPSSAAKAVLSNGML
SQ  INDSFMVGCIYSPAEAKEHVPKTLRNSNKDLEMTDASSSETSMSIPVHADAHFQSQSGLGKKVIVQHKNDIFKSSQKHQP
SQ  RNWLFHYLFGFGSTEPIDEEEKSKTASDNTSLQTSLFGKIVQVVLHTLFGF
//
ID  Q5ZI22;
PN  Nucleoporin NUP42;
GN  NUP42;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
DR  UNIPROT: Q5ZI22;
DR  PROSITE: PS50103;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046872;
GO  GO:0005049;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTICQFFLQGRCRFGDRCWNEHPRGGGGRPHSAGPVRGAGGGWGAASQRYANVIQPPIFKHSTWGGSGDGGGFSGASDFG
SQ  SPGNKSAVFSQNRFSALSSAHPADGFSDEEQRLLDCVAKDMATWESSGQWMFSCYSPEAGKPNVSGFREFSAEEVRLEYY
SQ  NCSANNNTENYINSVNQLVQERRNRLQELKALNASGKESLLSQLKNAVTQPLPSLGFGGQQASSFGFPSFPVSSSSGAAS
SQ  FSFKANPSVPPGNAAAVGSSAAASNPPTFGVTSSPSVPNPVGSGNSSAPSAASFSFKTSGTTSGCGTSGLSGFGSSAAAN
SQ  SSSTAPLPVSATPSAATGTSQSGASSASAAQTAGASGHNVTSAPSAVPNGIASDKLYTPRSELTAEELEQFEAKRFTLGK
SQ  IPLKPPPIDLLYL
//
ID  Q6P0U9;
PN  Nucleoporin NUP42;
GN  nup42;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15504}. Nucleus membrane {ECO:0000250|UniProtKB:O15504}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15504}; Cytoplasmic side {ECO:0000250|UniProtKB:O15504}.
DR  UNIPROT: Q6P0U9;
DR  PROSITE: PS50103;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046872;
GO  GO:0005049;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O15504};
SQ  MPVCNFFLQGRCRYGDTCWNEHPTGGRGGDYRGNQQPSNRGGFGNRVWINPSQRGGGGSSSAGGSNEWGRGAASARDVQS
SQ  SEFSFSQNRFSALETQRAGAEDTHTTLDTIQKEMEVWQTSGQWPFSCYSAVNRQISGFIELCPEELRLEYYTSRASGDIQ
SQ  PYINSVQQLANQWRSRVQELRNMSSSTQISVIAELKSSSPPASAPGFGSPGPGFGSATSGFGNTSLSSPPAGFGGAGFGS
SQ  GPQSSSTFSFAQSKTDFGASNTQQASGFGSSAFAQPSSGFGNPAPSAASFSFAAADSESKPSAGGFGSASGFSFKTATAG
SQ  QGSGFGSGFGSSSGFGSSSGFGSSSGFGSAFGSAAPAQSSSFGSTGGAADTQSGHGLFTANSELTPEELKEFMAKRFTLG
SQ  QIPLRPPPADLLMI
//
ID  O15504;
PN  Nucleoporin NUP42;
GN  NUP42;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12228227, ECO:0000269|PubMed:16000379}. Nucleus membrane {ECO:0000269|PubMed:12228227, ECO:0000269|PubMed:16000379}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:12228227}. Note=Excluded from the nucleolus. {ECO:0000269|PubMed:10358091}.
DR  UNIPROT: O15504;
DR  UNIPROT: A4D143;
DR  UNIPROT: B4DP42;
DR  UNIPROT: Q49AE7;
DR  UNIPROT: Q9BS49;
DR  PDB: 6B4F;
DR  PDB: 6B4I;
DR  PDB: 6B4J;
DR  PROSITE: PS50103;
DR  DisGeNET: 11097;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:16000379}. (Microbial infection) In case of infection by HIV-1, it may participate in the docking of viral Vpr at the nuclear envelope. {ECO:0000269|PubMed:12228227}.
DE  Reference Proteome: Yes;
DE  Interaction: Q03518; IntAct: EBI-8550622; Score: 0.37
DE  Interaction: P24386; IntAct: EBI-2515120; Score: 0.40
DE  Interaction: A0A6L8P1I1; IntAct: EBI-2828503; Score: 0.00
DE  Interaction: Q81KT8; IntAct: EBI-2828510; Score: 0.00
DE  Interaction: Q9H0R8; IntAct: EBI-3623653; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-3437356; Score: 0.00
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q7KZI7; IntAct: EBI-11002856; Score: 0.35
DE  Interaction: A5YKK6; IntAct: EBI-11005861; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-11060556; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-11888324; Score: 0.37
DE  Interaction: O76011; IntAct: EBI-24510043; Score: 0.56
DE  Interaction: E5LBS6; IntAct: EBI-14062727; Score: 0.35
DE  Interaction: Q9GZY0; IntAct: EBI-21528397; Score: 0.35
DE  Interaction: Q8N4J0; IntAct: EBI-21736494; Score: 0.35
DE  Interaction: Q13158; IntAct: EBI-20736966; Score: 0.35
DE  Interaction: Q8IW93; IntAct: EBI-25410221; Score: 0.35
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0046872;
GO  GO:0005049;
GO  GO:0003723;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006611;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAICQFFLQGRCRFGDRCWNEHPGARGAGGGRQQPQQQPSGNNRRGWNTTSQRYSNVIQPSSFSKSTPWGGSRDQEKPYF
SQ  SSFDSGASTNRKEGFGLSENPFASLSPDEQKDEKKLLEGIVKDMEVWESSGQWMFSVYSPVKKKPNISGFTDISPEELRL
SQ  EYHNFLTSNNLQSYLNSVQRLINQWRNRVNELKSLNISTKVALLSDVKDGVNQAAPAFGFGSSQAATFMSPGFPVNNSSS
SQ  DNAQNFSFKTNSGFAAASSGSPAGFGSSPAFGAAASTSSGISTSAPAFGFGKPEVTSAASFSFKSPAASSFGSPGFSGLP
SQ  ASLATGPVRAPVAPAFGGGSSVAGFGSPGSHSHTAFSKPSSDTFGNSSISTSLSASSSIIATDNVLFTPRDKLTVEELEQ
SQ  FQSKKFTLGKIPLKPPPLELLNV
//
ID  Q8CIC2;
PN  Nucleoporin NUP42;
GN  Nup42;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15504}. Nucleus membrane {ECO:0000250|UniProtKB:O15504}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15504}; Cytoplasmic side {ECO:0000250|UniProtKB:O15504}. Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:O15504}.
DR  UNIPROT: Q8CIC2;
DR  UNIPROT: Q8BJX3;
DR  UNIPROT: Q8BVP7;
DR  UNIPROT: Q924S0;
DR  PROSITE: PS50103;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250|UniProtKB:O15504}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0001750;
GO  GO:0046872;
GO  GO:0005049;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006611;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O15504};
SQ  MTICQFFLQGRCRFGDRCWNEHPGARGAGGARQPPPQQQPPSGNNRRGWNASSQRYSNVIQPSSFPKSTPWGGSRDQDKP
SQ  PFGSFDSGASTSRGFGSSQNPFASPLSDEQKDEKKLLEGIVKDVEVWESSGQWMFSVYSPVRKKPNISGFTDISPEELRL
SQ  EYHNFLTSNNLQSYLNSVQQLVSQWRNRINELKNLTMSTKGALLSDVKDGVSQAVPAFGFGSKQAGSFGSPGFPVNNSSS
SQ  STVQNFSFKTSPGLATPPSGSTSVFGSHPAFGAGPSAGSSISSSTPAFGLGKPEATSAASFSFKSPEASSFASPGFSGFP
SQ  ASMAASPSGSTTAPPLRSGSSVVGFGSPSPHSQAVFAKPSTDVFGGSGISTSVLASGAADNALFTPRDQLMKEELEQFQS
SQ  QRFTLGKIPLKPPPVELLTV
//
ID  Q5RB98;
PN  Nucleoporin NUP42;
GN  NUP42;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15504}. Nucleus membrane {ECO:0000250|UniProtKB:O15504}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15504}; Cytoplasmic side {ECO:0000250|UniProtKB:O15504}. Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:O15504}.
DR  UNIPROT: Q5RB98;
DR  PROSITE: PS50103;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250|UniProtKB:O15504}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046872;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O15504};
SQ  MAICQFFLQGRCRFGDRCWNEHPGARGAGGGRQQPQLQPSGNNRRGWNTTSQRYSNVIQSSSFSKSTPWGGSRDQEKPSF
SQ  GSFDSGASTNRKEGFGLSENPFASLSPDEQKDEKKLLEGIVKDMEVWESSGQWMFSVYSPVKKKPNISGFTDISPEELRL
SQ  EYHNFLTSNNLQSYLNSVQRLINQWRNRVNELKSLNISTKVALLSDVKDGVNQAAPAFGFGSSQAATFVSPGFPVNNSSS
SQ  DNAQNFSFKTNSGFAAASSGSPAGFRSSPAFGAAASTSSAISTSAPAFGFGKPEVTSAASFSFKSPAASSFGSPGFSGLP
SQ  ASLATGPVRAPVAPAFGGGSSVAGFGSLGSHSHAAFSKPSSDTFGNSSISTSLSASSSIIATDNVLFTPRDKLTVEELEQ
SQ  FQSKKFTLGKIPLKPPPLELLNI
//
ID  Q5XGN1;
PN  Nucleoporin NUP42;
GN  nup42;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15504}. Nucleus membrane {ECO:0000250|UniProtKB:O15504}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15504}; Cytoplasmic side {ECO:0000250|UniProtKB:O15504}.
DR  UNIPROT: Q5XGN1;
DR  UNIPROT: Q4QQY9;
DR  PROSITE: PS50103;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046872;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O15504};
SQ  MAICNFFLQGRCRYGEKCWNEHPRGGGGGGGNRYQSQNRYQEQSRYQEQSRYPEQSRYPEQNRYQEPAGNAKGTWGASSQ
SQ  RYVQPSNFSKSTTWINRDSEKPSAGSFSGFGSRNVKSTAATGLPSTQNRFAALSSQDNSRDGQTDKGNILDDIMKDMEIW
SQ  ESSGQWMFSVYSMLKEKKNISGFTDFSPEELRLEYSVCQAEGNPLKYINAVQQLGSKWKQRILELKNPNPSIKTALLNEL
SQ  NSPSPDVTPGYSGQQNSAFGALSFPTSNTAPTAVTFSFKADTTTAAKPAVPNALAGSDFSAFGNKPTSAPSFGSGVAAAA
SQ  ASFSFAPSTISGFGSTASNSGFGAASNAAGFQGAANIAAAPAFGVASSTAPASGFGGGFGTTVNTGAKTSSVRDLFSAGT
SQ  AVPVQTTLLFGQATGSLNTTASSTSLAGQPFKASTSATAVSGSFTSDNTSNPLFTPRNELSVEDLAQFEAKQFTLGKTPI
SQ  KPPSADLLKVT
//
ID  Q5FVW4;
PN  Nucleoporin NUP42;
GN  nup42;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15504}. Nucleus membrane {ECO:0000250|UniProtKB:O15504}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15504}; Cytoplasmic side {ECO:0000250|UniProtKB:O15504}.
DR  UNIPROT: Q5FVW4;
DR  PROSITE: PS50103;
DE  Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046872;
GO  GO:0005049;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O15504};
SQ  MAICSFFLQGRCRYGEKCWNEHPRGGSSRYQSQNRYQEPPGNAKGTWGSSSQRYVQPSSFSRSTTWVNRDNEKPSSGSHS
SQ  GFDNRNVKFTAATGFPSSQNRFAALSSQDNSRDAQTDKGNIIDDITNDMEIWESSGQWMFSVYSMLREKKNISGFADFSP
SQ  EELRLEYYACQAEGNPLKYINAVQQLGSKWKQRILELKNLNPSSKMALFNELSSPSSDMTSGYNGQQKPAFGSSSFPTNN
SQ  TAPTAATFSFKADAANAAKAGATNSLAGSNVPAFGNKPTSAPSFGSGGAATAASFSFAPSSSSNFGATTSTSGFGNASNT
SQ  ASFQGTANSAAAPAFGVASSSTAATGFGGGFSTTGAMNTGVRDLFSAGTVGPGPVTSLFVQTTGPLHATASSTSLDGQSF
SQ  RPSALNTTNSLFTPQNELSAEELAQFKAQRFTLGKIPLKPPPADLLNVS
//
ID  P49686;
PN  Nucleoporin NUP42;
GN  NUP42;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
DR  UNIPROT: P49686;
DR  UNIPROT: D6VSH5;
DR  PDB: 6B4E;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP42 is specifically important for nuclear protein and mRNA export. {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10805742, ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401, ECO:0000269|PubMed:15039779}.
DE  Reference Proteome: Yes;
DE  Interaction: P48837; IntAct: EBI-1269538; Score: 0.00
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.74
DE  Interaction: Q04964; IntAct: EBI-7718134; Score: 0.40
DE  Interaction: P32858; IntAct: EBI-8223518; Score: 0.22
DE  Interaction: Q06142; IntAct: EBI-1266067; Score: 0.00
DE  Interaction: P49686; IntAct: EBI-1269494; Score: 0.00
DE  Interaction: Q02630; IntAct: EBI-1269505; Score: 0.00
DE  Interaction: Q02629; IntAct: EBI-1269516; Score: 0.00
DE  Interaction: P49687; IntAct: EBI-1269527; Score: 0.00
DE  Interaction: Q02199; IntAct: EBI-1269549; Score: 0.00
DE  Interaction: Q05166; IntAct: EBI-1269560; Score: 0.00
DE  Interaction: P52891; IntAct: EBI-1269571; Score: 0.00
DE  Interaction: P53266; IntAct: EBI-7612855; Score: 0.35
DE  Interaction: P39103; IntAct: EBI-7612881; Score: 0.35
DE  Interaction: P07256; IntAct: EBI-7612943; Score: 0.35
DE  Interaction: P50111; IntAct: EBI-2132804; Score: 0.37
DE  Interaction: Q03330; IntAct: EBI-4385804; Score: 0.35
DE  Interaction: P69718; IntAct: EBI-16211283; Score: 0.40
DE  Interaction: Q12128; IntAct: EBI-16295069; Score: 0.00
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0003714;
GO  GO:0071472;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSAFGNPFTSGAKPNLSNTSGINPFTNNAASTNNMGGSAFGRPSFGTANTMTGGTTTSAFGMPQFGTNTGNTGNTSISAF
SQ  GNTSNAAKPSAFGAPAFGSSAPINVNPPSTTSAFGAPSFGSTGFGAMAATSNPFGKSPGSMGSAFGQPAFGANKTAIPSS
SQ  SVSNSNNSAFGAASNTPLTTTSPFGSLQQNASQNASSTSSAFGKPTFGAATNTQSPFGTIQNTSTSSGTGVSPFGTFGTN
SQ  SNNKSPFSNLQSGAGAGSSPFGTTTSKANNNNNVGSSAFGTTNNQSPFSGGSGGTFGSASNLNKNTNGNFQSSFGNKGFS
SQ  FGITPQNDANKVSQSNPSFGQTMPNTDPNISLKSNGNATSFGFGQQQMNATNVNANTATGKIRFVQGLSSEKDGILELAD
SQ  LAEETLKIFRANKFELGLVPDIPPPPALVA
//
ID  Q24JJ9;
PN  Nuclear pore complex protein NUP43;
GN  NUP43;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q24JJ9;
DR  UNIPROT: O65565;
DR  UNIPROT: Q8LCD6;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031080;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEMMQDSFQVHRIPQSKYVDGVRWLPQASALNRFFATASYDADCDSSSIEIQSLDPNPRGNHNTNPLIESLSSWTSPSRV
SQ  SSLEVAGNGGGGGSFKPMVSAATSSGSLHVLMIDLVEGAAIEEFYAAEGERFHVGRVEGVDWREGGECVTVGEDGRVNVV
SQ  KIVNGEGLRYRKVFDGNGLVAYRAVKWASPTEFVTGGYGFGLQLWDQRKSGEAVSQLKGNWFQGKTSAIVHSIDIHPSRK
SQ  HTCIAGGSSGTVFAWDLRWPQQPIVLSGVGASENINNPLSESEVWEVQYDSYTKSNVSSSRILPVMTCSEDGILGIIEQG
SQ  EEPIELLAEPCAINSFDIDRQNPQDVICSLEWESIAVFSRP
//
ID  Q54Z22;
PN  Nuclear pore complex protein nup43;
GN  nup43;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}.
DR  UNIPROT: Q54Z22;
DR  PROSITE: PS50294;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSVSVHYSTHKINKVRFLNRNFHNDTSLFVTGTNHPVLSKNKISVWGLESRQNSDEIEELASVPIDGIVTELKVIEINN
SQ  KPMIIGSTSKGSIFMYSIFNLPNKFEYIGYDGLLDKKYENYNNINNINDTYDTCNLLKERIWFNSSSNNNNVNSNNINNN
SQ  NYNNNNNNYNNNNNNNNNNNNNNNNNNNNGSCINSFDISYDQHSLVTVGNDGVMNLLSIENLIPIYTNRYIDGLSVNVVK
SQ  SITSNQIITSGELGRYIKFWDIRSNSSQPVKTIKTQCPRIFSLAIHKDEQHIIAAGSSDGQVNLFDIRNDYSIDQNKTHN
SQ  SNVWELSFSKSNPNQLYSCSEDGFIYQYSYNKDNLGGGGMMTLPNQINNTFDIYSKEVSLLQLPTSIGSIDSFDINSNIN
SQ  RLICCSTSSQCLIVKSL
//
ID  Q8NFH3;
PN  Nucleoporin Nup43;
GN  NUP43;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore. Nucleus, nuclear pore complex.
DR  UNIPROT: Q8NFH3;
DR  UNIPROT: B4E2F0;
DR  UNIPROT: Q9H8S0;
DR  PDB: 4I79;
DR  PDB: 5A9Q;
DR  PDB: 7PEQ;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 608141;
DR  DisGeNET: 348995;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. {ECO:0000269|PubMed:17363900}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-21865034; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-21865034; Score: 0.53
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.64
DE  Interaction: Q12769; IntAct: EBI-21865034; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: P01889; IntAct: EBI-1083368; Score: 0.00
DE  Interaction: Q96S44; IntAct: EBI-6256589; Score: 0.53
DE  Interaction: Q8WYP5; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: Q9BW27; IntAct: EBI-9032422; Score: 0.76
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.67
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: Q8IVT5; IntAct: EBI-14035152; Score: 0.35
DE  Interaction: Q9NPF4; IntAct: EBI-21527449; Score: 0.35
DE  Interaction: Q9UBP0; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: P23025; IntAct: EBI-21837437; Score: 0.35
DE  Interaction: Q9Y3C4; IntAct: EBI-21865034; Score: 0.35
DE  Interaction: Q9NSK0; IntAct: EBI-21865034; Score: 0.35
DE  Interaction: Q9H0B6; IntAct: EBI-21865034; Score: 0.35
DE  Interaction: Q92526; IntAct: EBI-21865034; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-21865034; Score: 0.53
DE  Interaction: Q8NFH4; IntAct: EBI-21865034; Score: 0.53
DE  Interaction: Q14657; IntAct: EBI-21865034; Score: 0.35
DE  Interaction: P33176; IntAct: EBI-21865034; Score: 0.35
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: Q9Y6K9; IntAct: EBI-20737021; Score: 0.35
DE  Interaction: Q8IY21; IntAct: EBI-21259607; Score: 0.35
DE  Interaction: P37802; IntAct: EBI-25482076; Score: 0.35
DE  Interaction: P57721; IntAct: EBI-25482076; Score: 0.35
DE  Interaction: P55212; IntAct: EBI-25836238; Score: 0.56
DE  Interaction: P06307; IntAct: EBI-25837221; Score: 0.56
DE  Interaction: P07686; IntAct: EBI-25867165; Score: 0.56
DE  Interaction: P13473; IntAct: EBI-25874611; Score: 0.56
DE  Interaction: P02766; IntAct: EBI-25894354; Score: 0.56
DE  Interaction: Q99497; IntAct: EBI-25913824; Score: 0.56
DE  Interaction: O75400; IntAct: EBI-25924971; Score: 0.56
DE  Interaction: P54252; IntAct: EBI-25974688; Score: 0.56
DE  Interaction: P54253; IntAct: EBI-25977247; Score: 0.56
DE  Interaction: Q13148; IntAct: EBI-25984820; Score: 0.56
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEIYAKFVSQKISKTRWRPLPPGSLQTAETFATGSWDNEENYISLWSIGDFGNLDSDGGFEGDHQLLCDIRHHGDVMDL
SQ  QFFDQERIVAASSTGCVTVFLHHPNNQTLSVNQQWTTAHYHTGPGSPSYSSAPCTGVVCNNPEIVTVGEDGRINLFRADH
SQ  KEAVRTIDNADSSTLHAVTFLRTPEILTVNSIGQLKIWDFRQQGNEPSQILSLTGDRVPLHCVDRHPNQQHVVATGGQDG
SQ  MLSIWDVRQGTMPVSLLKAHEAEMWEVHFHPSNPEHLFTCSEDGSLWHWDASTDVPEKSSLFHQGGRSSTFLSHSISNQA
SQ  NVHQSVISSWLSTDPAKDRIEITSLLPSRSLSVNTLDVLGPCLVCGTDAEAIYVTRHLFS
//
ID  P59235;
PN  Nucleoporin Nup43;
GN  Nup43;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: P59235;
DR  UNIPROT: E9QPN3;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: P61021; IntAct: EBI-11567757; Score: 0.35
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEIYAKFVSQKISKTRWRPVPSGSLQTTETFATGSWDNEENCVSLWSIGDFGNLDSDGGFEGDHQLLCDIRHHGDVMDL
SQ  QFFDQERIVAASSTGCVTVFLHHPNNQTLSVNQQWPAAHYHTGPSSPSYSSAPCTGIVCDNPEIVTVGEDGRINLFRVDH
SQ  KEAVRTIDNADSSTLHAVTFLRTPEIVTVNSIGQLKIWDFRQQGSEPCQILSLTGDRVPLHCVDRHPDQQHVVATGGQDG
SQ  MLSIWDVRQGTMPVSLLKAHEAEMWEVHFHPSNPDHLFTCSEDGSLWHWDASTDAPEKSSLFHQGGRSSTFLSHSLSNQA
SQ  GVHQSLVSSWLSTDPAKDRIEITSLLPSRTLSVNSLDVLGPCLVCGTDAEAIYVTRQLFS
//
ID  Q09793;
PN  Nucleoporin nup45;
GN  nup45;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm. Nucleus, nuclear pore complex.
DR  UNIPROT: Q09793;
DR  Pfam: PF13634;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGLNKTPSFGSTGTQNQNTGTSAGTGLFSSNTFGNNTQANTPASTGFGGVTGGAFGQTKPQTGGSLFGNKPNATSTTPG
SQ  LNLFGQNPQAAPGGSLFGASTTKPQAPGGLFNQNQTQAQPAQAAPTGGLFGLSGQNQTQSQTQPAQANTSLFGQSNIGTT
SQ  GGLFDQNRPNTSTFGQFSTQPASAGLFGQSTQPSGSTGFGLSNNTQTTPFFSAAQQQPSTTQLPSNPAINATTRYSSLNA
SQ  NTQKFLDDLDKEIFSQIQLAEELQTKLGTVSELVESVPNDVAEVQRRLSSVSTALLIDSDEIETTKRVVDEDTSNARISS
SQ  RILDVFKTPGATYPFASNDPLMNYFEQFTENAKKRTDLYAATIGELEQHLEQVETTPQNNSPEALLKTIKEEHKLFMALS
SQ  NRFAQVHDEVKRLQVNTSTSLPFIS
//
ID  G0S4X2;
PN  Nucleoporin NUP49;
GN  NUP49;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q02199}. Nucleus membrane {ECO:0000250|UniProtKB:Q02199}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q02199}; Cytoplasmic side {ECO:0000250|UniProtKB:Q02199}. Nucleus membrane {ECO:0000250|UniProtKB:Q02199}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q02199}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q02199}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:Q02199}.
DR  UNIPROT: G0S4X2;
DR  UNIPROT: G3EQ72;
DR  PDB: 5CWS;
DR  Pfam: PF13634;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP49 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport. {ECO:0000250|UniProtKB:Q02199}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S024; IntAct: EBI-16176393; Score: 0.61
DE  Interaction: G0S0R2; IntAct: EBI-16176513; Score: 0.35
DE  Interaction: G0S156; IntAct: EBI-16176750; Score: 0.35
DE  Interaction: G0S4T0; IntAct: EBI-16176870; Score: 0.35
DE  Interaction: G0SBQ3; IntAct: EBI-16176513; Score: 0.61
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q02199};
SQ  MSLFGTNTTSQTPAGGGLFGTTTSQSAQTGSLFGTATSQPQQTGGLFGSTATQTPSSQLQSTGLFGSTTATSQPQQTGGL
SQ  FGSTTTTTSQPQQTGGLFGATATSQPQSTGGLFGNTTTTSQPAQTVGLFGTTTQPQPAQSGGLFGSATQQKPATGGLFGS
SQ  TTTNTGAGLFGNTSNTIGGGGLFGQTAKPATGGLFGQSTTQPQQQQNATPGLTMGQSTNTQQQVVPGVRIDLSNIKSTTR
SQ  FNDLTEALQQEIAKIDEEIQKCIRDKEAVDAFLPAHGEQLAAIPTDVNFVTRKSEGAHNALSSDILAIDQLRELVKQDAD
SQ  NARLSFKAIDNLKLPMQYHQAGLWSKQMGGAGTAGASGASADADGQSNADLISYFSKTADEMEEMMKKFEKTITEIEAHL
SQ  TGVEAHAMAMQNVAAQSRNAAQGGVDERVYELAAVLREFEESILKVAGVVGGVKEGVTELQLRDFMGHGS
//
ID  Q02199;
PN  Nucleoporin NUP49/NSP49;
GN  NUP49;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: Q02199;
DR  UNIPROT: D6VTY0;
DR  PDB: 7N85;
DR  PDB: 7N9F;
DR  PDB: 7WOO;
DR  PDB: 7WOT;
DR  Pfam: PF13634;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP49 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:7813444, ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9017593, ECO:0000269|PubMed:9971735}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-801342; Score: 0.68
DE  Interaction: P32499; IntAct: EBI-6322534; Score: 0.00
DE  Interaction: P34077; IntAct: EBI-789044; Score: 0.62
DE  Interaction: P40368; IntAct: EBI-11889308; Score: 0.37
DE  Interaction: P47069; IntAct: EBI-7064868; Score: 0.27
DE  Interaction: P48837; IntAct: EBI-390870; Score: 0.90
DE  Interaction: P49686; IntAct: EBI-1269549; Score: 0.00
DE  Interaction: P49687; IntAct: EBI-11888836; Score: 0.37
DE  Interaction: P23639; IntAct: EBI-698324; Score: 0.37
DE  Interaction: P39731; IntAct: EBI-390798; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P07259; IntAct: EBI-801342; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-801342; Score: 0.35
DE  Interaction: P16861; IntAct: EBI-801342; Score: 0.35
DE  Interaction: Q06411; IntAct: EBI-857689; Score: 0.00
DE  Interaction: Q06142; IntAct: EBI-1269417; Score: 0.00
DE  Interaction: Q02630; IntAct: EBI-1269659; Score: 0.00
DE  Interaction: Q02629; IntAct: EBI-1269802; Score: 0.00
DE  Interaction: Q02199; IntAct: EBI-8276157; Score: 0.69
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: P38265; IntAct: EBI-2885494; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: Q00416; IntAct: EBI-5235312; Score: 0.37
DE  Interaction: Q05166; IntAct: EBI-11889036; Score: 0.37
DE  Interaction: Q7Z3B4; IntAct: EBI-11889006; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0042802;
GO  GO:0017056;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0000055;
GO  GO:0006409;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFGLNKASSTPAGGLFGQASGASTGNANTGFSFGGTQTGQNTGPSTGGLFGAKPAGSTGGLGASFGQQQQQSQTNAFGGS
SQ  ATTGGGLFGNKPNNTANTGGGLFGANSNSNSGSLFGSNNAQTSRGLFGNNNTNNINNSSSGMNNASAGLFGSKPAGGTSL
SQ  FGNTSTSSAPAQNQGMFGAKPAGTSLFGNNAGNTTTGGGLFGSKPTGATSLFGSSNNNNNNNNSNNIMSASGGLFGNQQQ
SQ  QLQQQPQMQCALQNLSQLPITPMTRISELPPQIRQEIEQLDQYIQKQVQISHHLKADTIDHDELIDSIPRDVAYLLKSES
SQ  ATSQYLKQDLKKISSFKSLIDEDLLDTQTFSVLLQQLLTPGSKISSNDLDKFFQKKIHLYEKKLEDYCRILSDIETAVNG
SQ  IDTDLFGAPNNPNSTAITADLGSSEAENLLQLKTGLAAIVSTVIEEFTLFMDIAERIAVLHQKTKTLASLSI
//
ID  Q7K0D8;
PN  Nuclear pore complex protein Nup50;
GN  Nup50;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:20144760}. Nucleus envelope {ECO:0000269|PubMed:20144760}. Chromosome {ECO:0000269|PubMed:20144760}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O08587}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side {ECO:0000250|UniProtKB:O08587}. Note=Associates with chromatin (PubMed:20144760).
DR  UNIPROT: Q7K0D8;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DE  Function: Component of the nuclear pore complex that has a direct role in nuclear protein import (By similarity). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta- cargo complex and importin recycling (By similarity). Binds to transcriptionally active chromatin sites when located in the nucleoplasm and is involved in transcriptional activation (PubMed:20144760). {ECO:0000250|UniProtKB:Q9JIH2, ECO:0000250|UniProtKB:Q9UKX7, ECO:0000269|PubMed:20144760}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VD47; IntAct: EBI-229995; Score: 0.00
DE  Interaction: Q9VJ53; IntAct: EBI-242068; Score: 0.00
DE  Interaction: Q9VSK1; IntAct: EBI-257394; Score: 0.00
DE  Interaction: P40798; IntAct: EBI-257398; Score: 0.00
DE  Interaction: P52295; IntAct: EBI-257405; Score: 0.00
DE  Interaction: Q9W0Y8; IntAct: EBI-257409; Score: 0.00
DE  Interaction: Q9VWE4; IntAct: EBI-510498; Score: 0.37
DE  Interaction: P22469; IntAct: EBI-7377202; Score: 0.37
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: Q4V5M2; IntAct: EBI-15155009; Score: 0.49
DE  Interaction: Q9NHD5; IntAct: EBI-26734134; Score: 0.49
GO  GO:0000785;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005704;
GO  GO:0031490;
GO  GO:0035080;
GO  GO:0051028;
GO  GO:0045944;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAGKRQATSNLNHENWDLEEEPEERGTFRTATEEELKTRVIKKARRKIAGGSSAAEEDGAEEKTAEPKSVFSGFSGFGKP
SQ  AASPAAGSPFSFLANVTAPATTSSSEPKKSAFSFGFSSSSSSADRPVSTSICGTASTSSTAPSPLPAKESTSTVDGAKPT
SQ  TSIFGNISAAKKESSEAKTSSSSTSLTSTMETSEYRESVADLNRSVIKFLQDQMGKSPYCILTPVFKNYDEHLKDLQDEE
SQ  SARTNSTKSKTAQARSQEPVAKVSRASSPPKAATTFTFGKPSAPIGASVSPLAKKPNCTITSGGTTTTTATPLVSFGSTA
SQ  SFTAPVPSSSSIFSLTAKPTGEAKSDDTPKSSIFSFGAKDTTTKKDEPNFSAPKTNGFSFGLKSNNDDKPSTSLFAGFGK
SQ  APGGAGDGAKGFSFTNSATPFSLGNIHPPAAAAAPAEEEKEEDTPPKVEFKQVVEDDAIYSKRCKVFIKKDKDFGDRGVG
SQ  TLYLKPVKDSEKIQLLVRADTNLGNILVNLILSKGIPCQRMGKNNVLMVCVPTPEDSKATSLLLRVKTGDEADDLLEKIK
SQ  EHIK
//
ID  Q9UKX7;
PN  Nuclear pore complex protein Nup50;
GN  NUP50;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12802065}. Nucleus membrane {ECO:0000250|UniProtKB:O08587}; Peripheral membrane protein {ECO:0000250|UniProtKB:O08587}; Nucleoplasmic side {ECO:0000250|UniProtKB:O08587}. Note=Localizes to the nucleoplasmic fibrils of the nuclear pore complex (By similarity). Dissociates from the NPC structure early during prophase of mitosis (PubMed:12802065). Associates with the newly formed nuclear membrane during telophase (PubMed:12802065). In the testis, the localization changes during germ cell differentiation from the nuclear surface in spermatocytes to the whole nucleus (interior) in spermatids and back to the nuclear surface in spermatozoa (By similarity). {ECO:0000250|UniProtKB:O08587, ECO:0000269|PubMed:12802065}.
DR  UNIPROT: Q9UKX7;
DR  UNIPROT: B1AHA4;
DR  UNIPROT: B2RB15;
DR  UNIPROT: O75644;
DR  UNIPROT: Q8N6V5;
DR  UNIPROT: Q9NPM9;
DR  UNIPROT: Q9NPR6;
DR  UNIPROT: Q9P1K5;
DR  PDB: 2EC1;
DR  PDB: 3TJ3;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DR  OMIM: 604646;
DR  DisGeNET: 10762;
DE  Function: Component of the nuclear pore complex that has a direct role in nuclear protein import (PubMed:20016008). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin- alpha:beta-cargo complex and importin recycling (PubMed:20016008). Interacts with regulatory proteins of cell cycle progression including CDKN1B (By similarity). This interaction is required for correct intracellular transport and degradation of CDKN1B (By similarity). {ECO:0000250|UniProtKB:Q9JIH2, ECO:0000269|PubMed:20016008}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.42
DE  Interaction: P29991; IntAct: EBI-8828330; Score: 0.37
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8IY92; IntAct: EBI-2370766; Score: 0.35
DE  Interaction: Q9QWT9; IntAct: EBI-2558911; Score: 0.40
DE  Interaction: E9PVX6; IntAct: EBI-2561030; Score: 0.40
DE  Interaction: O95758; IntAct: EBI-7850130; Score: 0.35
DE  Interaction: P78362; IntAct: EBI-6659073; Score: 0.44
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6515052; Score: 0.35
DE  Interaction: Q9UBN7; IntAct: EBI-6597993; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-6911905; Score: 0.57
DE  Interaction: O00629; IntAct: EBI-10323292; Score: 0.72
DE  Interaction: O15131; IntAct: EBI-10323304; Score: 0.78
DE  Interaction: O60684; IntAct: EBI-10323314; Score: 0.72
DE  Interaction: P52292; IntAct: EBI-10323326; Score: 0.72
DE  Interaction: P52294; IntAct: EBI-10323338; Score: 0.83
DE  Interaction: Q7Z726; IntAct: EBI-10323366; Score: 0.56
DE  Interaction: O00505; IntAct: EBI-10323376; Score: 0.72
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q5JU00; IntAct: EBI-11367780; Score: 0.27
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: Q14145; IntAct: EBI-25252050; Score: 0.56
DE  Interaction: P42694; IntAct: EBI-11908106; Score: 0.00
DE  Interaction: Q504Q3; IntAct: EBI-11915899; Score: 0.00
DE  Interaction: Q9NRA8; IntAct: EBI-11938210; Score: 0.00
DE  Interaction: Q2M3V2; IntAct: EBI-11938201; Score: 0.00
DE  Interaction: Q9Y2I1; IntAct: EBI-11940278; Score: 0.00
DE  Interaction: Q9Y4F3; IntAct: EBI-11941887; Score: 0.00
DE  Interaction: Q68CP9; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: O75717; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q9P0U4; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q9NVF7; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q9NPI1; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q9BW19; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q9BQE9; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q96GM5; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q92925; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q8WUB8; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q8TAQ2; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q8NFC6; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q8IXQ5; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q86Y91; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q86U86; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q6STE5; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q69YH5; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: Q12888; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: O60942; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: O43791; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: O15047; IntAct: EBI-21683766; Score: 0.35
DE  Interaction: P15659; IntAct: EBI-25769043; Score: 0.37
DE  Interaction: P03430; IntAct: EBI-25769263; Score: 0.37
DE  Interaction: P03427; IntAct: EBI-25769858; Score: 0.37
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: P16403; IntAct: EBI-20919740; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-20923986; Score: 0.40
DE  Interaction: P58876; IntAct: EBI-20923978; Score: 0.40
DE  Interaction: Q16778; IntAct: EBI-20923970; Score: 0.40
DE  Interaction: Q99880; IntAct: EBI-20923962; Score: 0.40
DE  Interaction: Q93079; IntAct: EBI-20923954; Score: 0.40
DE  Interaction: Q13547; IntAct: EBI-20935412; Score: 0.40
DE  Interaction: P17813; IntAct: EBI-22197897; Score: 0.35
DE  Interaction: Q8IW93; IntAct: EBI-25410221; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-25481539; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-26396507; Score: 0.35
DE  Interaction: K9N643; IntAct: EBI-26375164; Score: 0.35
DE  Interaction: P17706; IntAct: EBI-27114740; Score: 0.35
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O08587};
SQ  MAKRNAEKELTDRNWDQEDEAEEVGTFSMASEEVLKNRAIKKAKRRNVGFESDTGGAFKGFKGLVVPSGGGRFSGFGSGA
SQ  GGKPLEGLSNGNNITSAPPFASAKAAADPKVAFGSLAANGPTTLVDKVSNPKTNGDSQQPSSSGLASSKACVGNAYHKQL
SQ  AALNCSVRDWIVKHVNTNPLCDLTPIFKDYEKYLANIEQQHGNSGRNSESESNKVAAETQSPSLFGSTKLQQESTFLFHG
SQ  NKTEDTPDKKMEVASEKKTDPSSLGATSASFNFGKKVDSSVLGSLSSVPLTGFSFSPGNSSLFGKDTTQSKPVSSPFPTK
SQ  PLEGQAEGDSGECKGGDEEENDEPPKVVVTEVKEEDAFYSKKCKLFYKKDNEFKEKGIGTLHLKPTANQKTQLLVRADTN
SQ  LGNILLNVLIPPNMPCTRTGKNNVLIVCVPNPPIDEKNATMPVTMLIRVKTSEDADELHKILLEKKDA
//
ID  Q9JIH2;
PN  Nuclear pore complex protein Nup50;
GN  Nup50;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250|UniProtKB:O08587}; Peripheral membrane protein {ECO:0000250|UniProtKB:O08587}; Nucleoplasmic side {ECO:0000250|UniProtKB:O08587}. Note=Localizes to the nucleoplasmic fibrils of the nuclear pore complex. Dissociates from the NPC structure early during prophase of mitosis. Associates with the newly formed nuclear membrane during telophase. In the testis, the localization changes during germ cell differentiation from the nuclear surface in spermatocytes to the whole nucleus (interior) in spermatids and back to the nuclear surface in spermatozoa. {ECO:0000250|UniProtKB:O08587, ECO:0000250|UniProtKB:Q9UKX7}.
DR  UNIPROT: Q9JIH2;
DR  UNIPROT: Q3TG43;
DR  UNIPROT: Q3TN17;
DR  UNIPROT: Q6P1F4;
DR  UNIPROT: Q6PAL4;
DR  UNIPROT: Q8C2Y6;
DR  UNIPROT: Q9CU02;
DR  UNIPROT: Q9JK85;
DR  PDB: 2C1M;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Component of the nuclear pore complex that has a direct role in nuclear protein import (PubMed:10811608). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin- alpha:beta-cargo complex and importin recycling (PubMed:16222336). Interacts with regulatory proteins of cell cycle progression including CDKN1B (PubMed:10891500, PubMed:10811608). This interaction is required for correct intracellular transport and degradation of CDKN1B (PubMed:10811608). {ECO:0000269|PubMed:10811608, ECO:0000269|PubMed:10891500, ECO:0000269|PubMed:16222336}.
DE  Reference Proteome: Yes;
DE  Interaction: P49452; IntAct: EBI-8573213; Score: 0.35
DE  Interaction: P52294; IntAct: EBI-15710711; Score: 0.44
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:1990904;
GO  GO:0051028;
GO  GO:0001841;
GO  GO:0006913;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O08587};
SQ  MAKRVAEKELTDRNWDEEDEVEEMGTFSVASEEVMKNRAVKKAKRRNVGFESDSGGAFKGFKGLVVPSGGGGFSGFGGSG
SQ  GKPLEGLTNGNSTDNATPFSNVKTAAEPKAAFGSFAVNGPTTLVDKKISSPKCNNSNQPPSSGPASSTACPGNAYHKQLA
SQ  GLNCSVRDWIVKHVNTNPLCDLTPIFKDYERYLATIEKQLENGGGSSSESQTDRATAGMEPPSLFGSTKLQQESPFSFHG
SQ  NKAEDTSEKVEFTAEKKSDAAQGATSASFSFGKKIESSALGSLSSGSLTGFSFSAGSSSLFGKDAAQSKAASSLFSAKAS
SQ  ESPAGGGSSECRDGEEEENDEPPKVVVTEVKEEDAFYSKKCKLFYKKDNEFKEKGVGTLHLKPTATQKTQLLVRADTNLG
SQ  NILLNVLIAPNMPCTRTGKNNVLIVCVPNPPLDEKQPTLPATMLIRVKTSEDADELHKILLEKKDA
//
ID  O08587;
PN  Nuclear pore complex protein Nup50;
GN  Nup50;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10891499}. Nucleus membrane {ECO:0000269|PubMed:10891499}; Peripheral membrane protein {ECO:0000269|PubMed:10891499}; Nucleoplasmic side {ECO:0000269|PubMed:10891499}. Note=Dissociates from the NPC structure early during prophase of mitosis (By similarity). Associates with the newly formed nuclear membrane during telophase (By similarity). Localizes to the nucleoplasmic fibrils of the nuclear pore complex (PubMed:10891499). In the testis, the localization changes during germ cell differentiation from the nuclear surface in spermatocytes to the whole nucleus (interior) in spermatids and back to the nuclear surface in spermatozoa (PubMed:9073512). {ECO:0000250|UniProtKB:Q9UKX7, ECO:0000269|PubMed:10891499, ECO:0000269|PubMed:9073512}.
DR  UNIPROT: O08587;
DR  UNIPROT: Q4QR93;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Component of the nuclear pore complex that has a direct role in nuclear protein import. Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling. Interacts with regulatory proteins of cell cycle progression including CDKN1B. This interaction is required for correct intracellular transport and degradation of CDKN1B. {ECO:0000250|UniProtKB:Q9JIH2}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0001841;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10891499};
SQ  MAKRVAEKELTDRNWDEEDEVEEMGTFSVASEEVMKNRAVKKAKRRNIGFESDSGGAFKGFKGLVVPSGGGGFSGFGGGS
SQ  GGKPLEGLTNGNSTDSATPFSSAKTAAEPKAAFGSFAVNGPTTLVDKKISSPKCNSSNQPPSSGPASSTSCTGNTYHKQL
SQ  AGLNCSVRDWIVKHVNTNPLCDLTPIFKDYERYLATIEKQLENGGSSSSERQTDRATAAMEPPSLFGSTKLQQDSPFSFH
SQ  GNKAEDTSEKLEFTAEKKSDAAQGATSASFNFGKKIESSVLGSLSSGSLTGFSFSPGNSSLFGKDAAQSKAASSPFSAKA
SQ  SESQAGGSSSECRDGEEEESDEPPKVVVTEVKEEDAFYSKKCKLFYKKDNEFKEKGVGTLHLKPTATQKTQLLVRADTNL
SQ  GNILLNVLIPPNMPCTRTGKNNVLIVCVPNPPLDEKQPTLPVTMLIRVKTSEDADELHKILLQKKDV
//
ID  G0S156;
PN  Nucleoporin NUP53;
GN  NUP53;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q03790}. Nucleus membrane {ECO:0000250|UniProtKB:Q03790}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03790}; Cytoplasmic side {ECO:0000250|UniProtKB:Q03790}. Nucleus membrane {ECO:0000250|UniProtKB:Q03790}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03790}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q03790}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:Q03790}.
DR  UNIPROT: G0S156;
DR  UNIPROT: G3EQ73;
DR  PDB: 5HAX;
DR  PDB: 5HB3;
DR  PDB: 5HB7;
DR  PDB: 5HB8;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000250|UniProtKB:Q03790}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S024; IntAct: EBI-4325483; Score: 0.70
DE  Interaction: G0S4T0; IntAct: EBI-4325530; Score: 0.68
DE  Interaction: G0SFH5; IntAct: EBI-4325546; Score: 0.52
DE  Interaction: G0S7B6; IntAct: EBI-4325495; Score: 0.68
DE  Interaction: G0SBQ3; IntAct: EBI-16176459; Score: 0.46
DE  Interaction: G0SBS8; IntAct: EBI-16176459; Score: 0.46
DE  Interaction: G0S4F3; IntAct: EBI-16176459; Score: 0.46
DE  Interaction: G0SAK3; IntAct: EBI-16176459; Score: 0.46
DE  Interaction: G0S4X2; IntAct: EBI-16176750; Score: 0.35
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q03790};
SQ  MPPLILHNVPDDELYVGDDGIQRPFAMVFPQQDGSLRSRKANLETGAFGKSTRRTRSKAATPAKREDPTIAAADKIFSNW
SQ  LASQNQSAPQTSVPAPAQRKPNLIPSSSSQNLAQGHDESSAPSQTRFFRKQEPTEVILRGYRNAQHQYAAINHYEQIAGR
SQ  ICEDYPREPPVESRRYKSELRDPAFTHRRALTPEERAKVNRAMSGEHWVKVTFESAEAADKAVYSSPQLIQGHLVYAEYY
SQ  KGVPPAQDEAIPDPSVAAFGAALSRTQTLRQRNRGSFSLSGTQEAGGPDASPTSSLTADTGTLASGVEISTSTSNTLNGG
SQ  AAAGGAEKSQDDEFCRVIPTVRKAKLLPMEEALLPAPTFTQRIANHIPFLRWFNGAMIGSEVPRTETGEFDWVRASLFWK
SQ  LMWWLDFLLGLFGGDIRDAEKDDKED
//
ID  Q03790;
PN  Nucleoporin NUP53;
GN  NUP53;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: Q03790;
DR  UNIPROT: D6VZX4;
DR  PDB: 3W3Y;
DR  PDB: 5UAZ;
DR  PDB: 7N85;
DR  PDB: 7N9F;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP53 may play an important role in cell cycle regulation by inhibiting PSE1 transport functions during mitosis and sequestration of MAD1-MAD2 in a cell cycle-dependent manner. It also seems to play an important role in de novo NPC assembly by associating with nuclear membranes and driving their proliferation. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11352933, ECO:0000269|PubMed:12403813, ECO:0000269|PubMed:12473689, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:14697200, ECO:0000269|PubMed:9864357}.
DE  Reference Proteome: Yes;
DE  Interaction: P32500; IntAct: EBI-390810; Score: 0.55
DE  Interaction: P34077; IntAct: EBI-390816; Score: 0.67
DE  Interaction: P38181; IntAct: EBI-805269; Score: 0.72
DE  Interaction: P39685; IntAct: EBI-390975; Score: 0.37
DE  Interaction: P40064; IntAct: EBI-390858; Score: 0.55
DE  Interaction: P40368; IntAct: EBI-11889264; Score: 0.37
DE  Interaction: P46673; IntAct: EBI-4325410; Score: 0.37
DE  Interaction: P47054; IntAct: EBI-11889050; Score: 0.37
DE  Interaction: Q08227; IntAct: EBI-393408; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P16140; IntAct: EBI-805269; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-805269; Score: 0.53
DE  Interaction: Q12398; IntAct: EBI-805269; Score: 0.35
DE  Interaction: P00925; IntAct: EBI-805269; Score: 0.35
DE  Interaction: Q06142; IntAct: EBI-1269428; Score: 0.00
DE  Interaction: P38265; IntAct: EBI-2885494; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P10591; IntAct: EBI-3673770; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3691918; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3727446; Score: 0.35
DE  Interaction: Q03790; IntAct: EBI-4325327; Score: 0.67
DE  Interaction: P32597; IntAct: EBI-6879758; Score: 0.35
DE  Interaction: P11938; IntAct: EBI-6879805; Score: 0.35
DE  Interaction: P43583; IntAct: EBI-9117313; Score: 0.44
DE  Interaction: Q05359; IntAct: EBI-16713590; Score: 0.37
DE  Interaction: Q06644; IntAct: EBI-16295791; Score: 0.00
DE  Interaction: P38987; IntAct: EBI-16284883; Score: 0.35
DE  Interaction: Q05166; IntAct: EBI-21318430; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0042802;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:0034501;
GO  GO:0006355;
GO  GO:0007088;
GO  GO:0060188;
GO  GO:0072417;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MADLQKQENSSRFTNVSVIAPESQGQHEQQKQQEQLEQQKQPTGLLKGLNGFPSAPQPLFMEDPPSTVSGELNDNPAWFN
SQ  NPRKRAIPNSIIKRSNGQSLSPVRSDSADVPAFSNSNGFNNVTFGSKKDPRILKNVSPNDNNSANNNAHSSDLGTVVFDS
SQ  NEAPPKTSLADWQKEDGIFSSKTDNIEDPNLSSNITFDGKPTATPSPFRPLEKTSRILNFFDKNTKTTPNTASSEASAGS
SQ  KEGASTNWDDHAIIIFGYPETIANSIILHFANFGEILEDFRVIKDFKKLNSKNMSKSPSLTAQKYPIYTGDGWVKLTYKS
SQ  ELSKSRALQENGIIMNGTLIGCVSYSPAALKQLASLKKSEEIINNKTSSQTSLSSKDLSNYRKTEGIFEKAKAKAVTSKV
SQ  RNAEFKVSKNSTSFKNPRRLEIKDGRSLFLRNRGKIHSGVLSSIESDLKKREQASKSKKSWLNRLNNWLFGWNDL
//
ID  Q8GYF7;
PN  Nuclear pore complex protein NUP54;
GN  NUP54;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8GYF7;
DR  UNIPROT: O48698;
DR  Pfam: PF13874;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q8W4D8; IntAct: EBI-4505328; Score: 0.37
GO  GO:0005635;
GO  GO:0044613;
GO  GO:0005730;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0036228;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGTPSSSPSFGTPSSTPAFGTSSPAFGTPSATPAFGTPSNPSFSSGGFGSSLFSSPFSSQQPQQQQQQQQQQQPSSLFQ
SQ  QQPSSNFGFQSPFNNTAQQQQQTPFPNAQLTTQMAPVAPIPYSLADRDVQAIIEAYKEDPTNPKYAFQHLLFSVTEPQYR
SQ  VKPAAVSDIMWAEAMSKLEGMDSTERERLWPQLVQGFKDLSQRLKLQDEVLVSDRDRIKTTQSNVKMLQRHLQASTFPSI
SQ  ERLRQKEQSLQRRMLRVMRIIEGLEGKGFRLPLTKGEAELSEKLTAITRQVKGPGAELSRRVQSLQTISRAQANSIAAGS
SQ  SLYLPGSTKIDEQSLIDMQEVLQQETEAIGRLGNVLKRDMRDMEIMVAEDTEMALDS
//
ID  Q55BX5;
PN  Nuclear pore complex protein nup54;
GN  nup54;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70582}.
DR  UNIPROT: Q55BX5;
DR  Pfam: PF13634;
DR  Pfam: PF13874;
DE  Function: Probable component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P70582}.
DE  Reference Proteome: Yes;
GO  GO:0044613;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0036228;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLFGNTTTGGGGLFGNTTTPTQTTGGGLFGNTTTGGGLFGNTATPTTGGGGLFGNTATPTLTTGGGGGLFGNTTAPTTG
SQ  GGGLFGNTPTQTTGGGLFGNTATGGGGLFGNTQQQQQQQQQQQQQQQQQQQQQPSTSLFSQSSLGSQSSLGSQSSLGSQS
SQ  SLGSQSSLGSFGQTQQPQTSSLFGNLQQQQQLQQPQRSIIEQKLYDFMQSISPNSLNCRFLYWFYNYQANGQLVDPNSIP
SQ  KPPNVTVDQWAYALSNNPDPSILIPVAAKSFDDLINRRMKQEETIIALDQNTQEALKRMRDLENHLNFHIHTQLEMMRKK
SQ  QIELIQRYIEVWSNLEIYQSKGKTFTTSEERIMKKIYELFEEINQPNSIKSKVEEISNQLKLGSMEKEKIKYEISPEAVE
SQ  PLYNLLKNMTISIERITNELEIAVKDAQILKNELYQLKKC
//
ID  Q9V6B9;
PN  Probable nucleoporin Nup54;
GN  Nup54;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17682050}.
DR  UNIPROT: Q9V6B9;
DR  Pfam: PF13874;
DR  Pfam: PF18437;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (PubMed:17682050). Essential for the nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner (PubMed:17682050). Together with Nup58, required for transposable element silencing regulation in ovarian follicle cells (PubMed:33856346). By interacting with the nuclear (Nxf1/Nxt1) and cytosolic (fs(1)Yb) components of the flamenco (flam) transcripts processing pathway, enables export and subsequent piRNA production (PubMed:33856346). {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:33856346}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q7JXF5; IntAct: EBI-280221; Score: 0.00
DE  Interaction: Q9VYL7; IntAct: EBI-210131; Score: 0.00
DE  Interaction: Q9W1H7; IntAct: EBI-211333; Score: 0.00
DE  Interaction: Q9VRQ6; IntAct: EBI-229016; Score: 0.00
DE  Interaction: Q9VTC2; IntAct: EBI-26758035; Score: 0.62
DE  Interaction: Q9VWG2; IntAct: EBI-235591; Score: 0.00
DE  Interaction: O46085; IntAct: EBI-239628; Score: 0.00
DE  Interaction: Q9VS32; IntAct: EBI-239804; Score: 0.00
DE  Interaction: Q8T965; IntAct: EBI-245172; Score: 0.00
DE  Interaction: Q8MRM0; IntAct: EBI-247382; Score: 0.00
DE  Interaction: A1Z6W6; IntAct: EBI-254610; Score: 0.00
DE  Interaction: Q24337; IntAct: EBI-255366; Score: 0.00
DE  Interaction: Q9V9V0; IntAct: EBI-258334; Score: 0.00
DE  Interaction: Q868Z9; IntAct: EBI-268388; Score: 0.00
DE  Interaction: Q9VLA6; IntAct: EBI-270817; Score: 0.00
DE  Interaction: Q9W1A4; IntAct: EBI-272165; Score: 0.00
DE  Interaction: Q9VGW6; IntAct: EBI-272342; Score: 0.00
DE  Interaction: Q9XZS4; IntAct: EBI-15179362; Score: 0.62
DE  Interaction: Q9VF05; IntAct: EBI-278296; Score: 0.00
DE  Interaction: Q9VTU4; IntAct: EBI-278648; Score: 0.00
DE  Interaction: Q9VM05; IntAct: EBI-280628; Score: 0.00
DE  Interaction: Q9VVT5; IntAct: EBI-281753; Score: 0.00
DE  Interaction: Q7KLE5; IntAct: EBI-284881; Score: 0.00
DE  Interaction: Q7JZJ3; IntAct: EBI-285067; Score: 0.00
DE  Interaction: Q8MQZ0; IntAct: EBI-501710; Score: 0.00
DE  Interaction: Q9VSJ8; IntAct: EBI-507431; Score: 0.37
DE  Interaction: P22469; IntAct: EBI-7377238; Score: 0.37
DE  Interaction: Q7KKI9; IntAct: EBI-2109600; Score: 0.37
DE  Interaction: Q6WAR0; IntAct: EBI-2109779; Score: 0.37
DE  Interaction: Q86B83; IntAct: EBI-2110644; Score: 0.37
DE  Interaction: P18824; IntAct: EBI-9923731; Score: 0.35
DE  Interaction: Q8I942; IntAct: EBI-15179462; Score: 0.49
DE  Interaction: Q8IR83; IntAct: EBI-15179442; Score: 0.49
DE  Interaction: Q95RR8; IntAct: EBI-15179422; Score: 0.49
DE  Interaction: Q9VZV3; IntAct: EBI-15179382; Score: 0.49
DE  Interaction: O97420; IntAct: EBI-26758013; Score: 0.49
DE  Interaction: Q9VPX6; IntAct: EBI-26758023; Score: 0.49
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0036228;
GO  GO:0006605;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFFGSNTSLGATSTPAKTTGGLFGSPFGGTAATSQPAPAFGAQATSTPAFGAQPATSAFGAGSAFGATAAAPAFGAATG
SQ  TSAFGGSAFGSTPAFGAATTTTAGTGLGGGGFGGFGAAPATSQAGLFGAPATSAAPPAFSGFGQQAAASTAPASGFSGFG
SQ  TTTTSAPAFGGFGTSQSTGFGGGAFGSTFGKPANTTVTPGFGGFGGTSFMLGQPQQQPAPISADEAFAQSILNVSIFGDE
SQ  RDKIVAKWNYLQATWGTGKMFYSQSAAPVDITPENVMCRFKAIGYSRMPGKDNKLGLVALNFCRELSAVKPHQQQVIQTL
SQ  HSLFGSKPNMLVHIDSIKELENKKCQIVIYVEEKLQHAPNESKRILATELSNYLNQATLKPQLNNLGVVEALALVLPDED
SQ  QLREYLENPPRGVDPRMWRQANSDNPDPTLYIPVPMVGFNDLKWRVKCQEQETDTHALYIKKVESELTELKKRHATATAK
SQ  ILEHKRKLAELSHRILRIIVKQECTRKVGTSLTPEEEALRTKLQNMLAVVSAPTQFKGRLSELLSQMRMQRNQFAANGGA
SQ  EYALDKEAEDEMKTFLTMQQRAMEVLSDTVNKDLRALDVIIKGLPELRQS
//
ID  Q7Z3B4;
PN  Nucleoporin p54;
GN  NUP54;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70582}. Nucleus membrane {ECO:0000250|UniProtKB:P70582}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70582}; Cytoplasmic side {ECO:0000250|UniProtKB:P70582}. Nucleus membrane {ECO:0000250|UniProtKB:P70582}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70582}; Nucleoplasmic side {ECO:0000250|UniProtKB:P70582}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. {ECO:0000250|UniProtKB:P70582}.
DR  UNIPROT: Q7Z3B4;
DR  UNIPROT: B2RCK7;
DR  UNIPROT: B4DT35;
DR  UNIPROT: Q96EA7;
DR  UNIPROT: Q9NVL5;
DR  UNIPROT: Q9P0I1;
DR  PDB: 4JNU;
DR  PDB: 4JNV;
DR  PDB: 4JO7;
DR  PDB: 4JO9;
DR  PDB: 5IJN;
DR  PDB: 5IJO;
DR  PDB: 7PER;
DR  Pfam: PF13874;
DR  Pfam: PF18437;
DR  OMIM: 607607;
DR  DisGeNET: 53371;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P70582}.
DE  Reference Proteome: Yes;
DE  Interaction: O60711; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: P34077; IntAct: EBI-11889076; Score: 0.37
DE  Interaction: P37198; IntAct: EBI-752836; Score: 0.90
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P61970; IntAct: EBI-24586864; Score: 0.56
DE  Interaction: P62826; IntAct: EBI-25889945; Score: 0.56
DE  Interaction: Q02199; IntAct: EBI-11889006; Score: 0.37
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-24314853; Score: 0.56
DE  Interaction: Q15834; IntAct: EBI-760093; Score: 0.37
DE  Interaction: P25054; IntAct: EBI-3437328; Score: 0.00
DE  Interaction: O14964; IntAct: EBI-10256852; Score: 0.78
DE  Interaction: P19012; IntAct: EBI-10256862; Score: 0.67
DE  Interaction: Q8IY31; IntAct: EBI-10256884; Score: 0.56
DE  Interaction: Q96CS2; IntAct: EBI-10283794; Score: 0.56
DE  Interaction: Q9BVL2; IntAct: EBI-10299822; Score: 0.92
DE  Interaction: Q14129; IntAct: EBI-21248884; Score: 0.37
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9WTX6; IntAct: EBI-11016744; Score: 0.35
DE  Interaction: Q17RP2; IntAct: EBI-11051402; Score: 0.35
DE  Interaction: Q9ERZ6; IntAct: EBI-11111345; Score: 0.35
DE  Interaction: P35611; IntAct: EBI-11118761; Score: 0.35
DE  Interaction: Q8NHV4; IntAct: EBI-11157526; Score: 0.35
DE  Interaction: Q96NL6; IntAct: EBI-11376636; Score: 0.27
DE  Interaction: P25299; IntAct: EBI-11524187; Score: 0.56
DE  Interaction: B2BTY8; IntAct: EBI-11510518; Score: 0.40
DE  Interaction: P03433; IntAct: EBI-11514636; Score: 0.37
DE  Interaction: Q67020; IntAct: EBI-11514758; Score: 0.51
DE  Interaction: Q1K9H5; IntAct: EBI-11514868; Score: 0.40
DE  Interaction: Q8WUM0; IntAct: EBI-11889088; Score: 0.37
DE  Interaction: Q7Z3B4; IntAct: EBI-11889112; Score: 0.37
DE  Interaction: Q96HA1; IntAct: EBI-11889100; Score: 0.37
DE  Interaction: Q9NWQ9; IntAct: EBI-24312711; Score: 0.56
DE  Interaction: Q10567; IntAct: EBI-24338598; Score: 0.56
DE  Interaction: P06753; IntAct: EBI-24345511; Score: 0.56
DE  Interaction: Q9Y6A5; IntAct: EBI-25258287; Score: 0.56
DE  Interaction: Q7Z3Y8; IntAct: EBI-24491173; Score: 0.56
DE  Interaction: Q9UJW9; IntAct: EBI-22733542; Score: 0.56
DE  Interaction: O95994; IntAct: EBI-24266008; Score: 0.56
DE  Interaction: Q9H7B4; IntAct: EBI-24266381; Score: 0.56
DE  Interaction: Q86YM7; IntAct: EBI-24266885; Score: 0.56
DE  Interaction: Q969V4; IntAct: EBI-24511616; Score: 0.56
DE  Interaction: Q9H3R5; IntAct: EBI-24529403; Score: 0.56
DE  Interaction: Q9NP55; IntAct: EBI-24529621; Score: 0.56
DE  Interaction: Q9NZD8; IntAct: EBI-24617401; Score: 0.56
DE  Interaction: Q96KN3; IntAct: EBI-24629153; Score: 0.56
DE  Interaction: Q9NYK6; IntAct: EBI-23693027; Score: 0.56
DE  Interaction: Q9BXU0; IntAct: EBI-23732412; Score: 0.56
DE  Interaction: Q8NI38; IntAct: EBI-25281366; Score: 0.56
DE  Interaction: Q9NV70; IntAct: EBI-24426768; Score: 0.67
DE  Interaction: Q9NX04; IntAct: EBI-24428608; Score: 0.56
DE  Interaction: A5D8V6; IntAct: EBI-24536781; Score: 0.56
DE  Interaction: Q14525; IntAct: EBI-24539102; Score: 0.56
DE  Interaction: Q9BT92; IntAct: EBI-24553403; Score: 0.56
DE  Interaction: Q8IYI6; IntAct: EBI-24565174; Score: 0.56
DE  Interaction: Q5JUK2; IntAct: EBI-24570174; Score: 0.56
DE  Interaction: Q8TD31; IntAct: EBI-24572589; Score: 0.56
DE  Interaction: Q5JVL4; IntAct: EBI-24585567; Score: 0.56
DE  Interaction: Q9UJX2; IntAct: EBI-24594466; Score: 0.56
DE  Interaction: Q9BT25; IntAct: EBI-24598735; Score: 0.56
DE  Interaction: O00303; IntAct: EBI-24639350; Score: 0.56
DE  Interaction: O75935; IntAct: EBI-24640014; Score: 0.56
DE  Interaction: O95229; IntAct: EBI-24762391; Score: 0.56
DE  Interaction: O43482; IntAct: EBI-24800025; Score: 0.56
DE  Interaction: Q9GZM8; IntAct: EBI-21504131; Score: 0.35
DE  Interaction: Q96P53; IntAct: EBI-21607501; Score: 0.35
DE  Interaction: Q96A37; IntAct: EBI-21627270; Score: 0.35
DE  Interaction: Q9NXR1; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: Q9UBG3; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: Q9NSC5; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: Q9H9E3; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: Q9BV73; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: Q6PJI9; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: Q12934; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: Q00536; IntAct: EBI-21639232; Score: 0.35
DE  Interaction: Q9H1M0; IntAct: EBI-22125790; Score: 0.37
DE  Interaction: Q96FN4; IntAct: EBI-21659658; Score: 0.35
DE  Interaction: Q9NQW5; IntAct: EBI-20935108; Score: 0.40
DE  Interaction: P55212; IntAct: EBI-25835327; Score: 0.56
DE  Interaction: P06307; IntAct: EBI-25836999; Score: 0.56
DE  Interaction: P30519; IntAct: EBI-25868484; Score: 0.56
DE  Interaction: P13473; IntAct: EBI-25873707; Score: 0.56
DE  Interaction: O14901; IntAct: EBI-25905512; Score: 0.56
DE  Interaction: Q7TLC7; IntAct: EBI-26377368; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
DE  Interaction: P41212; IntAct: EBI-29015445; Score: 0.27
DE  Interaction: Q96Q04; IntAct: EBI-32723651; Score: 0.27
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0042802;
GO  GO:0044877;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0036228;
GO  GO:0006605;
GO  GO:0042306;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P70582};
SQ  MAFNFGAPSGTSGTAAATAAPAGGFGGFGTTSTTAGSAFSFSAPTNTGTTGLFGGTQNKGFGFGTGFGTTTGTSTGLGTG
SQ  LGTGLGFGGFNTQQQQQTTLGGLFSQPTQAPTQSNQLINTASALSAPTLLGDERDAILAKWNQLQAFWGTGKGYFNNNIP
SQ  PVEFTQENPFCRFKAVGYSCMPSNKDEDGLVVLVFNKKETEIRSQQQQLVESLHKVLGGNQTLTVNVEGTKTLPDDQTEV
SQ  VIYVVERSPNGTSRRVPATTLYAHFEQANIKTQLQQLGVTLSMTRTELSPAQIKQLLQNPPAGVDPIIWEQAKVDNPDSE
SQ  KLIPVPMVGFKELLRRLKVQDQMTKQHQTRLDIISEDISELQKNQTTSVAKIAQYKRKLMDLSHRTLQVLIKQEIQRKSG
SQ  YAIQADEEQLRVQLDTIQGELNAPTQFKGRLNELMSQIRMQNHFGAVRSEERYYIDADLLREIKQHLKQQQEGLSHLISI
SQ  IKDDLEDIKLVEHGLNETIHIRGGVFS
//
ID  Q8BTS4;
PN  Nuclear pore complex protein Nup54;
GN  Nup54;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70582}. Nucleus membrane {ECO:0000250|UniProtKB:P70582}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70582}; Cytoplasmic side {ECO:0000250|UniProtKB:P70582}. Nucleus membrane {ECO:0000250|UniProtKB:P70582}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70582}; Nucleoplasmic side {ECO:0000250|UniProtKB:P70582}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. {ECO:0000250|UniProtKB:P70582}.
DR  UNIPROT: Q8BTS4;
DR  UNIPROT: Q3TSI2;
DR  UNIPROT: Q8BU42;
DR  Pfam: PF13874;
DR  Pfam: PF18437;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P70582}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0032991;
GO  GO:0042802;
GO  GO:0044877;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0036228;
GO  GO:0006605;
GO  GO:0042306;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P70582};
SQ  MAFNFGAPSGTSGTSTATAAPAGGFGGFGTTTTTAGSAFSFSAPTNTGSTGLLGGTQNKGFGFGTGFGTTTGTGTGLGTG
SQ  LGTGLGFGGFNTQQQQQQQQTSLGGLFSQPTQAPAQSTQLINTASALSAPTLLGDERDAILAKWNQLQAFWGTGKGYFNN
SQ  NIPPVEFTQENPFCRFKAVGYSCMPNNKDEDGLVVLIFNKKETDIRSQQQQLVESLHKVLGGNQTLTVNVEGIKTLPDDQ
SQ  TEVVIYVVERSPNGTSRRVPATTLYAHFEQANIKAQLQQLGVTLSMTRTELSPAQIKQLLQNPPAGVDPIIWEQAKVDNP
SQ  DSEKLIPVPMVGFKELLRRLKVQDQMTKQHQTRLDIISEDISELQKNQTTTMAKIAQYKRKLMELSHRTLQVLIKQEIQR
SQ  KSGYAIQADEEQLRVQLDTIQGELNAPTQFKGRLNELMSQIRMQNHFGAVKSEEKYYIDADLLREIKQHLKQQQEGLSHL
SQ  ISIIKDDLEDIKLVEHGLNETIHSRGGVFS
//
ID  P70582;
PN  Nuclear pore complex protein Nup54;
GN  Nup54;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:8707840}. Nucleus membrane {ECO:0000269|PubMed:8707840}; Peripheral membrane protein {ECO:0000269|PubMed:8707840}; Cytoplasmic side {ECO:0000269|PubMed:8707840}. Nucleus membrane {ECO:0000269|PubMed:8707840}; Peripheral membrane protein {ECO:0000269|PubMed:8707840}; Nucleoplasmic side {ECO:0000269|PubMed:8707840}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter.
DR  UNIPROT: P70582;
DR  PDB: 3T97;
DR  PDB: 3T98;
DR  PDB: 4J3H;
DR  Pfam: PF13874;
DR  Pfam: PF18437;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000269|PubMed:8707840}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0032991;
GO  GO:0042802;
GO  GO:0044877;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0036228;
GO  GO:0006605;
GO  GO:0042306;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8707840};
SQ  MAFNFGAPSGTSGTSTATAAPAGGFGGFGTTTTTAGSAFSFSAPTNTGSTGLLGGTQNKGFGFGTGFGTSTGTGTGLGTG
SQ  LGTGLGFGGFNTQQQQQQQQTSLGGLFSQPAQAPAQSNQLINTASALSAPTLLGDERDAILAKWNQLQAFWGTGKGYFNN
SQ  NIPPVEFTQENPFCRFKAVGYSCMPNNKDEDGLVVLIFNKKETDIRSQQQQLVESLHKVLGGNQTLTVNVEGIKTLPDDQ
SQ  TEVVIYIVERSPNGTSRRVPATTLYAHFEQANIKTQLQQLGVTLSMTRTELSPAQIKQLLQNPPAGVDPIIWEQAKVDNP
SQ  DSEKLIPVPMVGFKELLRRLKVQDQMTKQHQTRLDIISEDISELQKNQTTTMAKIAQYKRKLMDLSHRTLQVLIKQEIQR
SQ  KSGYAIQAEEEQLRVQLDTIQGELNAPTQFKGRLNELMSQIRMQNHFGAVKSEEKYYIDADLLREIKQHLKQQQEGLSHL
SQ  ISIIKDDLEDIKLVEHGLNETIHSRGGVFS
//
ID  G0S8I1;
PN  Nucleoporin NUP56;
GN  NUP56;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P32499}. Nucleus membrane {ECO:0000250|UniProtKB:P32499}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32499}; Nucleoplasmic side {ECO:0000250|UniProtKB:P32499}.
DR  UNIPROT: G0S8I1;
DR  UNIPROT: G0ZGV9;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000250|UniProtKB:P32499}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046907;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P32499};
SQ  MADDPHNTSTSDVSELVPDNTEPSAANVKEDAETTAARRELKQTTISDKAKRDSAQLSQEDDKSASEEDDNKSDAGEPEK
SQ  KKPRTSRGLTPEVQLAAPKQEVPKETVASPKKRTHDELEQDGKEEEEKKEGEKPSSQNRAERDEPEKKRPRDRQASLSVE
SQ  RDGQKEVEPLSAQESRPSSAEKPKIEEKKDESKDTKVDKPQTSSSAFANSSMAKFASSTTSPFGAFGAAAAGKTNLFGLP
SQ  ATSSNIFGSKSADASAAPAGPPKLSFGSASAASPFASLNGQAGGMSSLFKSPFASAFSGGSSALKTAGATGFGKPGEPLK
SQ  TGKSAKPFGAPESDEEDEGEGEEGEENKSENGEGEEKEEEEKEEKASGEEKKKFKLQKVHIDDGEGNETTLLSVRAKMYV
SQ  MEKGVGWKERGAGMLKVNVPKQAVEVEEGNQPDADSFDPAALDDAARKLVRLIMRQDSTLRVILNTPILPAMKFQVNHKL
SQ  KAATVLFTAFEGGEARQVQMKMSQANATQFSNMVEKIKEKLAAA
//
ID  G0S0R2;
PN  Nucleoporin NUP57;
GN  NUP57;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P48837}. Nucleus membrane {ECO:0000250|UniProtKB:P48837}; Peripheral membrane protein {ECO:0000250|UniProtKB:P48837}; Cytoplasmic side {ECO:0000250|UniProtKB:P48837}. Nucleus membrane {ECO:0000250|UniProtKB:P48837}; Peripheral membrane protein {ECO:0000250|UniProtKB:P48837}; Nucleoplasmic side {ECO:0000250|UniProtKB:P48837}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P48837}.
DR  UNIPROT: G0S0R2;
DR  UNIPROT: G0ZGU2;
DR  PDB: 5CWS;
DR  PDB: 5CWT;
DR  Pfam: PF13874;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP57 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport. {ECO:0000250|UniProtKB:P48837}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S024; IntAct: EBI-16176393; Score: 0.61
DE  Interaction: G0S4X2; IntAct: EBI-16176513; Score: 0.35
DE  Interaction: G0SBQ3; IntAct: EBI-16176589; Score: 0.58
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P48837};
SQ  MFSSLNTRPAGQSLFGANTGGGLFGQSLANQPQQQQQPLQQQQQQAAPALGQSQINQNQQLGGSLWQPGSLTAYQKPIPE
SQ  QIKLIVDKWNPNHPNCAFKTYLYNKVDEHTVPLYGPGPNEDPKEWEEALQRKPAPNFIPVLCSGFPSIVARLMLQRRVIT
SQ  EFNNKLHQINASLDAILSRHDLDHTVRAFNARRRHAELSRRCLHLAARVQVLRNRGYALSGDEDELKQKLQQIDKTLNDP
SQ  AQGSRLEELWSRLIVLRGYAEDLKDQINQAGITESDGLGEEIEAKAKKILEDYDKQLQHLKKQVEEAKKDFEEWEKQHNP
SQ  APAPAR
//
ID  P48837;
PN  Nucleoporin NUP57;
GN  NUP57;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P48837;
DR  UNIPROT: D6VUQ0;
DR  PDB: 7N85;
DR  PDB: 7N9F;
DR  PDB: 7WOO;
DR  PDB: 7WOT;
DR  Pfam: PF13634;
DR  Pfam: PF13874;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP57 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:9017593, ECO:0000269|PubMed:9725905}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-390867; Score: 0.81
DE  Interaction: P32499; IntAct: EBI-6322523; Score: 0.00
DE  Interaction: P34077; IntAct: EBI-789044; Score: 0.84
DE  Interaction: P37198; IntAct: EBI-11532748; Score: 0.56
DE  Interaction: P38181; IntAct: EBI-1269978; Score: 0.00
DE  Interaction: P40066; IntAct: EBI-813993; Score: 0.27
DE  Interaction: Q02199; IntAct: EBI-390870; Score: 0.90
DE  Interaction: Q05027; IntAct: EBI-390873; Score: 0.37
DE  Interaction: P32337; IntAct: EBI-391032; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P10592; IntAct: EBI-809795; Score: 0.53
DE  Interaction: P02829; IntAct: EBI-864098; Score: 0.00
DE  Interaction: Q02630; IntAct: EBI-1266691; Score: 0.53
DE  Interaction: Q02629; IntAct: EBI-1266728; Score: 0.53
DE  Interaction: P48837; IntAct: EBI-1266737; Score: 0.65
DE  Interaction: Q06142; IntAct: EBI-1269406; Score: 0.00
DE  Interaction: P49686; IntAct: EBI-1269538; Score: 0.00
DE  Interaction: P49687; IntAct: EBI-1269934; Score: 0.00
DE  Interaction: P52891; IntAct: EBI-1269989; Score: 0.00
DE  Interaction: Q06410; IntAct: EBI-2344095; Score: 0.37
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q02959; IntAct: EBI-2884580; Score: 0.00
DE  Interaction: P38265; IntAct: EBI-2885494; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P10591; IntAct: EBI-3673778; Score: 0.53
DE  Interaction: P09435; IntAct: EBI-3683222; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3691926; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3727454; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-4374839; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-4385804; Score: 0.35
DE  Interaction: Q6WNK7; IntAct: EBI-4388219; Score: 0.35
DE  Interaction: P53165; IntAct: EBI-4388914; Score: 0.35
DE  Interaction: P13196; IntAct: EBI-11532730; Score: 0.56
DE  Interaction: Q7Z6G3; IntAct: EBI-11532719; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-11532708; Score: 0.56
DE  Interaction: Q9NPJ6; IntAct: EBI-11532784; Score: 0.56
DE  Interaction: Q8N6Y0; IntAct: EBI-11532775; Score: 0.56
DE  Interaction: Q5JR59; IntAct: EBI-11532766; Score: 0.56
DE  Interaction: P43365; IntAct: EBI-11532757; Score: 0.56
DE  Interaction: P19012; IntAct: EBI-11532739; Score: 0.56
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0042802;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0036228;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFGFSGSNNGFGNKPAGSTGFSFGQNNNNTNTQPSASGFGFGGSQPNSGTATTGGFGANQATNTFGSNQQSSTGGGLFGN
SQ  KPALGSLGSSSTTASGTTATGTGLFGQQTAQPQQSTIGGGLFGNKPTTTTGGLFGNSAQNNSTTSGGLFGNKVGSTGSLM
SQ  GGNSTQNTSNMNAGGLFGAKPQNTTATTGGLFGSKPQGSTTNGGLFGSGTQNNNTLGGGGLFGQSQQPQTNTAPGLGNTV
SQ  STQPSFAWSKPSTGSNLQQQQQQQIQVPLQQTQAIAQQQQLSNYPQQIQEQVLKCKESWDPNTTKTKLRAFVYNKVNETE
SQ  AILYTKPGHVLQEEWDQAMEKKPSPQTIPIQIYGFEGLNQRNQVQTENVAQARIILNHILEKSTQLQQKHELDTASRILK
SQ  AQSRNVEIEKRILKLGTQLATLKNRGLPLGIAEEKMWSQFQTLLQRSEDPAGLGKTNELWARLAILKERAKNISSQLDSK
SQ  LMVFNDDTKNQDSMSKGTGEESNDRINKIVEILTNQQRGITYLNEVLEKDAAIVKKYKNKT
//
ID  Q8RWH9;
PN  Nuclear pore complex protein NUP58;
GN  NUP58;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294, ECO:0000269|PubMed:23840761}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8RWH9;
DR  UNIPROT: O23173;
DE  Function: Involved in nucleocytoplasmic trafficking. May have regulatory roles in the gibberellin pathway, in auxin signaling and in light perception. {ECO:0000269|PubMed:23840761}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFFPPQQQQTPQPLFQTQQTSLFQPQQTNSIFSQSQPQQTNSIFSQSQPQQTNSIFSQPQQQQQTSLFQPQQFQQQQQQ
SQ  LNQQQQQQVQQQLYLFTNDKAPANYSTKWADLHPDSQKLLLQIEEKILEHRSESQRLDQCSRLYDSSVSSEGFEFDASRI
SQ  VQELGGINTAMDRQKAVLHELMIVAKDMLRNAEIAVRSFMMLQPRFPHWKQGGGVVSVGSQPSQGQGTNPAPASSGQQQA
SQ  VTTTVQVSDFYRGIPKKPTAFLLQTVVRFEKYLNECRQWVEELEQLLALDSDKYSRHASLLESLPKVMSNVHDFFVHVAA
SQ  KVESIHQYIESMRTSYLADQRRRGECHDPFLEADRRETAKQEAAAKRVHPTLHLPASTTSTQPSTQVAGLIASSATPGGS
SQ  NPPQTSVPTSNPSSGAGFSFLNTPASGPSSSLFATPSSTAPTSSLFGPSPTPTQTPLFGSSPASTFGSTQSLFGQTTPSL
SQ  TMPSQFGGATPGSGASFGSMTKSSRPKSRTTRR
//
ID  Q9VDV3;
PN  Nuclear pore complex protein Nup58;
GN  Nup58;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:15086791}. Note=Present also in annulate lamellae pore complexes (ALPCs). {ECO:0000269|PubMed:15086791}.
DR  UNIPROT: Q9VDV3;
DR  UNIPROT: Q8SYM7;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane (PubMed:15086791). Together with Nup54, required for transposable element silencing regulation in ovarian follicle cells (PubMed:33856346). By interacting with the nuclear (Nxf1/Nxt1) and cytosolic (fs(1)Yb) components of the flamenco (flam) transcripts processing pathway, enables export and subsequent piRNA production (PubMed:33856346). {ECO:0000269|PubMed:15086791, ECO:0000269|PubMed:33856346}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VJ62; IntAct: EBI-201971; Score: 0.00
DE  Interaction: Q9VT59; IntAct: EBI-206923; Score: 0.00
DE  Interaction: Q9W1H5; IntAct: EBI-211350; Score: 0.00
DE  Interaction: Q9W0R9; IntAct: EBI-221208; Score: 0.00
DE  Interaction: Q9VL73; IntAct: EBI-227768; Score: 0.00
DE  Interaction: P19339; IntAct: EBI-268179; Score: 0.00
DE  Interaction: P40798; IntAct: EBI-270201; Score: 0.00
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFTPTTNNAIGGATAATGAFAFGARPATTTAPPPSFGAATSTPTFGAAPATTSLFAAPAATPAFGAPAATPAFGAPASTP
SQ  GFGATSTAAPAFGTAAATPAFGIPAATSAFGAPAATPAFGAAAATPAFGAPAATPAFGAPAATSAFGAPAATTAFGAPAS
SQ  TQASAFGAPAPAVGTVAPTFSFATPATSAPTTAPPAFGFGTTATTAAAAMPASLSSGIGSFSFPKPQATTAASLNFNTTT
SQ  TTATAQPFNTGLKLGTTNATTTLGGGGIFSKPAGQAAAPAASTFVGLGGIDVTATQPKLGDNKQDGIKIKETQVPDEIIK
SQ  TVDGLKAYIKQQKTISSDIGRTSTSKFTNVSHEITNLKWALQNMATLVEGSNQQIRLMRQETVKAIQSLEMAQRTQDTPA
SQ  GLQFENNAPFQYFQCLVAKYEQDLIAFRQQIALTERHMHAISNPQSISPDDLKRGFRQLNESFISLAGRLHEVHQRVEEH
SQ  KEHYLNLRRYRLRDTTNVFERIDNPPLPTVEPQRISSGPTPFSNISALMNKSYAAAASSASNATGN
//
ID  Q9BVL2;
PN  Nucleoporin p58/p45;
GN  NUP58;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Cytoplasmic side {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Nucleoplasmic side {ECO:0000250|UniProtKB:P70581}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. {ECO:0000250|UniProtKB:P70581}.
DR  UNIPROT: Q9BVL2;
DR  UNIPROT: A6NI12;
DR  UNIPROT: B4DZJ1;
DR  UNIPROT: O43160;
DR  UNIPROT: Q5JRG2;
DR  UNIPROT: Q5JRG5;
DR  PDB: 4JO7;
DR  PDB: 4JO9;
DR  PDB: 4JQ5;
DR  PDB: 5IJN;
DR  PDB: 5IJO;
DR  PDB: 7PER;
DR  OMIM: 607615;
DR  DisGeNET: 9818;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P70581}.
DE  Reference Proteome: Yes;
DE  Interaction: A1KXE4; IntAct: EBI-25908575; Score: 0.56
DE  Interaction: O14770; IntAct: EBI-24450131; Score: 0.56
DE  Interaction: O15504; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: P20749; IntAct: EBI-25907809; Score: 0.56
DE  Interaction: P35658; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-8635195; Score: 0.80
DE  Interaction: P49792; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q7Z3B4; IntAct: EBI-10299822; Score: 0.92
DE  Interaction: Q8N1F7; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q8WUX9; IntAct: EBI-25908519; Score: 0.56
DE  Interaction: Q92621; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q99598; IntAct: EBI-25907995; Score: 0.56
DE  Interaction: Q9BTX1; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: A0A6L8PKS7; IntAct: EBI-2811590; Score: 0.00
DE  Interaction: P25054; IntAct: EBI-3437349; Score: 0.00
DE  Interaction: Q9P2A4; IntAct: EBI-8635212; Score: 0.78
DE  Interaction: P27361; IntAct: EBI-7201994; Score: 0.37
DE  Interaction: P42858; IntAct: EBI-6451221; Score: 0.74
DE  Interaction: Q13077; IntAct: EBI-10299812; Score: 0.84
DE  Interaction: Q9UMX0; IntAct: EBI-10299842; Score: 0.56
DE  Interaction: Q99988; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q969P6; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q9BSD7; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: P11532; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: O15440; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q96A73; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q96BD5; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q14746; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: Q96NL6; IntAct: EBI-11396361; Score: 0.27
DE  Interaction: Q96JB2; IntAct: EBI-24514268; Score: 0.72
DE  Interaction: Q7Z3Y7; IntAct: EBI-24531449; Score: 0.56
DE  Interaction: Q9NYP9; IntAct: EBI-24615263; Score: 0.72
DE  Interaction: O95994; IntAct: EBI-24618865; Score: 0.56
DE  Interaction: Q96KN3; IntAct: EBI-24406190; Score: 0.56
DE  Interaction: Q9Y2V7; IntAct: EBI-24474216; Score: 0.56
DE  Interaction: Q7Z3Y8; IntAct: EBI-24474479; Score: 0.56
DE  Interaction: Q9UHD9; IntAct: EBI-24475280; Score: 0.56
DE  Interaction: Q14525; IntAct: EBI-24599138; Score: 0.72
DE  Interaction: P55347; IntAct: EBI-24638583; Score: 0.72
DE  Interaction: Q96P53; IntAct: EBI-21607501; Score: 0.35
DE  Interaction: Q96A37; IntAct: EBI-21627270; Score: 0.35
DE  Interaction: Q5VX52; IntAct: EBI-21635815; Score: 0.35
DE  Interaction: Q9NVF7; IntAct: EBI-21639380; Score: 0.35
DE  Interaction: Q9HD26; IntAct: EBI-21639380; Score: 0.35
DE  Interaction: Q9BZF3; IntAct: EBI-21639380; Score: 0.35
DE  Interaction: Q96AX9; IntAct: EBI-21639380; Score: 0.35
DE  Interaction: Q15075; IntAct: EBI-21639380; Score: 0.35
DE  Interaction: O75150; IntAct: EBI-21639380; Score: 0.35
DE  Interaction: Q9H1M0; IntAct: EBI-21639380; Score: 0.35
DE  Interaction: Q96FN4; IntAct: EBI-21659658; Score: 0.35
DE  Interaction: O75830; IntAct: EBI-20916376; Score: 0.40
DE  Interaction: Q9BYV2; IntAct: EBI-22024904; Score: 0.00
DE  Interaction: Q6P1K2; IntAct: EBI-25907819; Score: 0.56
DE  Interaction: O75886; IntAct: EBI-25908093; Score: 0.56
DE  Interaction: Q99996; IntAct: EBI-25908085; Score: 0.56
DE  Interaction: O60636; IntAct: EBI-25908077; Score: 0.56
DE  Interaction: Q14154; IntAct: EBI-25908069; Score: 0.56
DE  Interaction: Q6ZU52; IntAct: EBI-25908059; Score: 0.56
DE  Interaction: A1A512; IntAct: EBI-25908051; Score: 0.56
DE  Interaction: Q13503; IntAct: EBI-25908043; Score: 0.56
DE  Interaction: Q52LW3; IntAct: EBI-25908035; Score: 0.56
DE  Interaction: O00303; IntAct: EBI-25908027; Score: 0.56
DE  Interaction: Q92783; IntAct: EBI-25908019; Score: 0.56
DE  Interaction: Q8WUW1; IntAct: EBI-25908011; Score: 0.56
DE  Interaction: P49459; IntAct: EBI-25908003; Score: 0.56
DE  Interaction: Q86WV8; IntAct: EBI-25907987; Score: 0.56
DE  Interaction: Q14765; IntAct: EBI-25907979; Score: 0.56
DE  Interaction: Q96GM5; IntAct: EBI-25907971; Score: 0.56
DE  Interaction: P47804; IntAct: EBI-25907963; Score: 0.56
DE  Interaction: P35998; IntAct: EBI-25907955; Score: 0.56
DE  Interaction: Q9BR81; IntAct: EBI-25907939; Score: 0.56
DE  Interaction: Q13562; IntAct: EBI-25907931; Score: 0.56
DE  Interaction: P02795; IntAct: EBI-25907923; Score: 0.56
DE  Interaction: P27338; IntAct: EBI-25907915; Score: 0.56
DE  Interaction: P80217; IntAct: EBI-25907899; Score: 0.56
DE  Interaction: Q06547; IntAct: EBI-25907891; Score: 0.56
DE  Interaction: O15287; IntAct: EBI-25907875; Score: 0.56
DE  Interaction: P41970; IntAct: EBI-25907867; Score: 0.56
DE  Interaction: H3BUJ7; IntAct: EBI-25907859; Score: 0.56
DE  Interaction: Q14117; IntAct: EBI-25907851; Score: 0.56
DE  Interaction: P24310; IntAct: EBI-25907843; Score: 0.56
DE  Interaction: Q86WV5; IntAct: EBI-25907835; Score: 0.56
DE  Interaction: Q13887; IntAct: EBI-25907827; Score: 0.56
DE  Interaction: Q9NP70; IntAct: EBI-25907801; Score: 0.56
DE  Interaction: Q9BQS8; IntAct: EBI-25908407; Score: 0.56
DE  Interaction: O75934; IntAct: EBI-25908101; Score: 0.56
DE  Interaction: Q9BV99; IntAct: EBI-25908389; Score: 0.56
DE  Interaction: Q9BRX5; IntAct: EBI-25908381; Score: 0.56
DE  Interaction: Q969X5; IntAct: EBI-25908373; Score: 0.56
DE  Interaction: Q6GQQ9; IntAct: EBI-25908363; Score: 0.56
DE  Interaction: Q9NS71; IntAct: EBI-25908355; Score: 0.56
DE  Interaction: Q9BXU0; IntAct: EBI-25908347; Score: 0.56
DE  Interaction: Q96FT7; IntAct: EBI-25908331; Score: 0.56
DE  Interaction: Q96EP0; IntAct: EBI-25908313; Score: 0.56
DE  Interaction: Q96EN9; IntAct: EBI-25908305; Score: 0.56
DE  Interaction: Q6NXG1; IntAct: EBI-25908297; Score: 0.56
DE  Interaction: Q9ULW8; IntAct: EBI-25908271; Score: 0.56
DE  Interaction: Q8IXH7; IntAct: EBI-25908263; Score: 0.56
DE  Interaction: P57682; IntAct: EBI-25908255; Score: 0.56
DE  Interaction: Q9BPZ3; IntAct: EBI-25908247; Score: 0.56
DE  Interaction: P57054; IntAct: EBI-25908237; Score: 0.56
DE  Interaction: Q9BT78; IntAct: EBI-25908229; Score: 0.56
DE  Interaction: Q9H347; IntAct: EBI-25908221; Score: 0.56
DE  Interaction: Q9BY12; IntAct: EBI-25908211; Score: 0.56
DE  Interaction: Q9NNX6; IntAct: EBI-25908203; Score: 0.56
DE  Interaction: Q8N490; IntAct: EBI-25908187; Score: 0.56
DE  Interaction: Q6PID6; IntAct: EBI-25908179; Score: 0.56
DE  Interaction: Q13352; IntAct: EBI-25908169; Score: 0.56
DE  Interaction: Q8TBE0; IntAct: EBI-25908153; Score: 0.56
DE  Interaction: O43482; IntAct: EBI-25908145; Score: 0.56
DE  Interaction: O75935; IntAct: EBI-25908137; Score: 0.56
DE  Interaction: Q99871; IntAct: EBI-25908127; Score: 0.56
DE  Interaction: O95229; IntAct: EBI-25908119; Score: 0.56
DE  Interaction: O75528; IntAct: EBI-25908109; Score: 0.56
DE  Interaction: Q0VDD7; IntAct: EBI-25908397; Score: 0.56
DE  Interaction: Q86TI2; IntAct: EBI-25908509; Score: 0.56
DE  Interaction: Q8IY31; IntAct: EBI-25908493; Score: 0.56
DE  Interaction: Q8NE08; IntAct: EBI-25908475; Score: 0.56
DE  Interaction: Q86U90; IntAct: EBI-25908417; Score: 0.56
DE  Interaction: Q9BV20; IntAct: EBI-25908459; Score: 0.56
DE  Interaction: Q8IUR5; IntAct: EBI-25908451; Score: 0.56
DE  Interaction: Q9H410; IntAct: EBI-25908435; Score: 0.56
DE  Interaction: B7Z3E8; IntAct: EBI-25908427; Score: 0.56
DE  Interaction: Q96MW5; IntAct: EBI-25908467; Score: 0.56
DE  Interaction: A1L190; IntAct: EBI-25908655; Score: 0.56
DE  Interaction: Q6DKI2; IntAct: EBI-25908663; Score: 0.56
DE  Interaction: Q7Z6I5; IntAct: EBI-25908639; Score: 0.56
DE  Interaction: Q8IWT0; IntAct: EBI-25908631; Score: 0.56
DE  Interaction: P58304; IntAct: EBI-25908623; Score: 0.56
DE  Interaction: Q8N6F8; IntAct: EBI-25908615; Score: 0.56
DE  Interaction: Q6P597; IntAct: EBI-25908607; Score: 0.56
DE  Interaction: Q86WT6; IntAct: EBI-25908599; Score: 0.56
DE  Interaction: Q96DX5; IntAct: EBI-25908591; Score: 0.56
DE  Interaction: Q8NEZ2; IntAct: EBI-25908583; Score: 0.56
DE  Interaction: Q8NDH6; IntAct: EBI-25908567; Score: 0.56
DE  Interaction: Q6ZMI0; IntAct: EBI-25908559; Score: 0.56
DE  Interaction: Q96A04; IntAct: EBI-25908551; Score: 0.56
DE  Interaction: Q96MN9; IntAct: EBI-25908543; Score: 0.56
DE  Interaction: Q96CS2; IntAct: EBI-25908535; Score: 0.56
DE  Interaction: Q9UII2; IntAct: EBI-25908527; Score: 0.56
DE  Interaction: Q8N4C7; IntAct: EBI-25908647; Score: 0.56
DE  Interaction: Q93009; IntAct: EBI-30844216; Score: 0.44
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0042802;
GO  GO:0008139;
GO  GO:0044877;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0042306;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P70581};
SQ  MSTGFSFGSGTLGSTTVAAGGTSTGGVFSFGTGASSNPSVGLNFGNLGSTSTPATTSAPSSGFGTGLFGSKPATGFTLGG
SQ  TNTGIATTITTGLTLGTPATTSAATTGFSLGFNKPAASATPFALPITSTSASGLTLSSALTSTPAASTGFTLNNLGGTTA
SQ  TTTTASTGLSLGGALAGLGGSLFQSTNTGTSGLGQNALGLTLGTTAATSTAGNEGLGGIDFSSSSDKKSDKTGTRPEDSK
SQ  ALKDENLPPVICQDVENLQKFVKEQKQVQEEISRMSSKAMLKVQEDIKALKQLLSLAANGIQRNTLNIDKLKIETAQELK
SQ  NAEIALRTQKTPPGLQHEYAAPADYFRILVQQFEVQLQQYRQQIEELENHLATQANNSHITPQDLSMAMQKIYQTFVALA
SQ  AQLQSIHENVKVLKEQYLGYRKMFLGDAVDVFETRRAEAKKWQNTPRVTTGPTPFSTMPNAAAVAMAATLTQQQQPATGP
SQ  QPSLGVSFGTPFGSGIGTGLQSSGLGSSNLGGFGTSSGFGCSTTGASTFGFGTTNKPSGSLSAGFGSSSTSGFNFSNPGI
SQ  TASAGLTFGVSNPASAGFGTGGQLLQLKKPPAGNKRGKR
//
ID  Q8R332;
PN  Nucleoporin p58/p45;
GN  Nup58;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Cytoplasmic side {ECO:0000250|UniProtKB:P70581}. Nucleus membrane {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70581}; Nucleoplasmic side {ECO:0000250|UniProtKB:P70581}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. {ECO:0000250|UniProtKB:P70581}.
DR  UNIPROT: Q8R332;
DR  UNIPROT: Q3UJF4;
DR  UNIPROT: Q8BUA7;
DR  UNIPROT: Q8BVG7;
DR  UNIPROT: Q8C0W3;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P70581}.
DE  Reference Proteome: Yes;
DE  Interaction: P39428; IntAct: EBI-657695; Score: 0.37
DE  Interaction: P63085; IntAct: EBI-657764; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0032991;
GO  GO:0042802;
GO  GO:0008139;
GO  GO:0044877;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0042306;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P70581};
SQ  MATGFSFGSGTLGSTTVAPGGTGAGSGFSFGTVASSTPSVGLNFGSLGSSVTPASTSASAGGFGTGLFGSKPATGFTLGG
SQ  TSAGTAATTSASTTGFSLGFSKPAASATPFALPVTSTSASGLTLSSALTSTPAASTGFTLNNLGATPATTTTASTGLSLG
SQ  GALAGLGGSLFQSGNTATSGLGQNALSLSLGTTAPTSAASNEGLGGIDFSTSSDKKSDKTGTRPEDSKALKDENLPPVIC
SQ  QDVENLQKFVKEQKQVQEEISRMSSKAMLKVQEDIKALKQLLSLAASGLQRNTLNIDKLKLETAQELKNAEIALRTQKTP
SQ  PGLQHENTAPADYFRILVQQFEVQLQQYRQQIEELENHLATQASNSHITPQDLSMAMQKIYQTFVALAAQLQSIHENVKV
SQ  LKEQYLGYRKMFLGDAVDVFEARRTEAKKWQNAPRVTTGPTPFSTMPNAAAVAMAATLTQQQQPATGPQPSLGVSFGTPF
SQ  GSGIGTGLQSSGLGSSNLGGFGTSSGFGCGTTGASTFGFGTTDKPSGSLSAGFGSSSTSGFNFSNPGITASAGLTFGVSN
SQ  PASAGFGTGGQLLQLKRPPAGNKRGKR
//
ID  P70581;
PN  Nucleoporin p58/p45;
GN  Nup58;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:8707840}. Nucleus membrane {ECO:0000269|PubMed:8707840}; Peripheral membrane protein {ECO:0000269|PubMed:8707840}; Cytoplasmic side {ECO:0000269|PubMed:8707840}. Nucleus membrane {ECO:0000269|PubMed:8707840}; Peripheral membrane protein {ECO:0000269|PubMed:8707840}; Nucleoplasmic side {ECO:0000269|PubMed:8707840}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter.
DR  UNIPROT: P70581;
DR  UNIPROT: Q9JHE1;
DR  UNIPROT: Q9QWK7;
DR  UNIPROT: Q9Z2W7;
DR  PDB: 2OSZ;
DR  PDB: 3T98;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000269|PubMed:8707840}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0032991;
GO  GO:0042802;
GO  GO:0008139;
GO  GO:0044877;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0042306;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8707840};
SQ  MATGFSFGSGTLGSTTVAPGGTGTGSGFSFGASSTPSVGLNFGTLGSSATPASTSTSASGFGTGLFGSKPGTGFTLGGTS
SQ  AGTTATTSASTTGFSLGFSKPAASATPFALPVTSTTASGLTLSSALTSAPAASTGFTLNNLGATPATTTAASTGLSLGGA
SQ  LAGLGGSLFQSGNTATSGLGQNALSLSLGTATPTSAASSEGLGGIDFSTSSDKKSDKTGTRPEDSKALKDENLPPVICQD
SQ  VENLQKFVKEQKQVQEEISRMSSKAMLKVQEDIKALKQLLSLAASGLQRNTLNIDKLKLETAQELKNAEIALRTQKTPPG
SQ  LQHENTAPADYFRVLVQQFEVQLQQYRQQIEELENHLATQANNSHITPQDLSMAMQKIYQTFVALAAQLQSIHENVKVLK
SQ  EQYLSYRKMFLGDAGDVFEARRTEAKKWQNAPRVTTGPTPFSTMPNAAAVAMAATLTQQQQPATGPQPSLGVSFGTPFGS
SQ  GIGTGLQSSGLGSSNLGGFGTSSGFGCGTTGASTFGFGTTDKPSGSLSAGFGSSSTSGFNFSNPGITASAGLTFGVSNPA
SQ  SAGFGTGGQLLQLKRPPAGNKRGKR
//
ID  Q05166;
PN  Nucleoporin ASM4;
GN  ASM4;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: Q05166;
DR  UNIPROT: D6VRR0;
DR  UNIPROT: E9P903;
DR  UNIPROT: Q12456;
DR  PDB: 7N85;
DR  PDB: 7N9F;
DR  Pfam: PF05172;
DR  PROSITE: PS51472;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). May have a mitosis control function (By similarity). {ECO:0000250, ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:9864357}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-11888294; Score: 0.37
DE  Interaction: P32500; IntAct: EBI-390807; Score: 0.67
DE  Interaction: P34077; IntAct: EBI-11889154; Score: 0.37
DE  Interaction: P46673; IntAct: EBI-4325425; Score: 0.37
DE  Interaction: P47054; IntAct: EBI-4392356; Score: 0.55
DE  Interaction: P49686; IntAct: EBI-1269560; Score: 0.00
DE  Interaction: P52891; IntAct: EBI-4325387; Score: 0.37
DE  Interaction: Q02199; IntAct: EBI-11889036; Score: 0.37
DE  Interaction: Q02629; IntAct: EBI-1269813; Score: 0.00
DE  Interaction: Q02630; IntAct: EBI-1269670; Score: 0.00
DE  Interaction: Q03790; IntAct: EBI-21318430; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: Q03718; IntAct: EBI-858301; Score: 0.00
DE  Interaction: Q06344; IntAct: EBI-854084; Score: 0.35
DE  Interaction: Q06142; IntAct: EBI-1269439; Score: 0.00
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q04947; IntAct: EBI-16714417; Score: 0.37
DE  Interaction: Q05166; IntAct: EBI-16714405; Score: 0.37
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005543;
GO  GO:0003697;
GO  GO:0017056;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006355;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFGIRSGNNNGGFTNLTSQAPQTTQMFQSQSQLQPQPQPQPQQQQQHLQFNGSSDASSLRFGNSLSNTVNANNYSSNIGN
SQ  NSINNNNIKNGTNNISQHGQGNNPSWVNNPKKRFTPHTVIRRKTTKQNSSSDINQNDDSSSMNATMRNFSKQNQDSKHNE
SQ  RNKSAANNDINSLLSNFNDIPPSVTLQDWQREDEFGSIPSLTTQFVTDKYTAKKTNRSAYDSKNTPNVFDKDSYVRIANI
SQ  EQNHLDNNYNTAETNNKVHETSSKSSSLSAIIVFGYPESISNELIEHFSHFGHIMEDFQVLRLGRGINPNTFRIFHNHDT
SQ  GCDENDSTVNKSITLKGRNNESNNKKYPIFTGESWVKLTYNSPSSALRALQENGTIFRGSLIGCIPYSKNAVEQLAGCKI
SQ  DNVDDIGEFNVSMYQNSSTSSTSNTPSPPNVIITDGTLLREDDNTPAGHAGNPTNISSPIVANSPNKRLDVIDGKLPFMQ
SQ  NAGPNSNIPNLLRNLESKMRQQEAKYRNNEPAGFTHKLSNWLFGWNDL
//
ID  O74500;
PN  Nucleoporin nup60;
GN  nup60;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}.
DR  UNIPROT: O74500;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0140512;
GO  GO:0140599;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0017056;
GO  GO:0008298;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0016973;
GO  GO:0034398;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSSGPIRTLHKGKAARNRTPYDRIAASKDGNHSNGPQTPSKSIFQRAKEWLTPSSWKKAISIFSSPVVNKHEDSFDSKTD
SQ  EEYLQNVSTTTEDVSMLINTPVTEKYEQEHRDTSAQATPSIVEQSPNQMLANFFSKKGKTPLNEIEKEGIISILNKSASP
SQ  SSSVISPAASLNRFQTPRAAAISKRESGVSSEPRARTSSLTPGNTPNSAKQWSAFRSTFSPLREQDQLSTISPNSLLPAQ
SQ  RLSYYGPTLSTPYNRRLRHKRHSTTPISLSNSIAPSLSFQPKKARYESANVSFNDTSFTNVPTSSPLHQSTTANHPEKTP
SQ  SRAAASLLSILDSKEKNTPSITAKAGSPQSAPSKASYISPYARPGITTSRRRHDQIRPSSEKSEPEKKEPSAFETLEKSS
SQ  NVQTYKPSLMPEFLEKASTHGSFAKQKEGEQTSLSEKTALSEPENKTPVFSFKAPSATTDKPSPPVSSIFSFNAPSAAST
SQ  KPSPAVSSTFSFNAPTTTPSATSFSIINKEKPARSPNETIDVDLEEEGSGISAEVEVANEGEDLQKNATEVKASTSEKPV
SQ  FRFEAVTDEKNSEVSSSNQASSSTMISQPNTGFSFGSFNKPAGQEEKPQQRSLFSASFTTQKPELPAAKIEPEVQMTNVA
SQ  IDQRSFEQAEKSPISVSESTSLVEVEKPSAEGTNEHKQDATMTLEKTDKQGSLEEEPFPKFSFTVLPKENGENLSTMEST
SQ  QELPKFSFSVLKEEKN
//
ID  P39705;
PN  Nucleoporin NUP60;
GN  NUP60;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Nuclear basket.
DR  UNIPROT: P39705;
DR  UNIPROT: D6VPL6;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11535617, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-3663903; Score: 0.35
DE  Interaction: P32499; IntAct: EBI-801825; Score: 0.70
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: Q02821; IntAct: EBI-802293; Score: 0.69
DE  Interaction: Q06142; IntAct: EBI-802293; Score: 0.77
DE  Interaction: P40069; IntAct: EBI-810484; Score: 0.67
DE  Interaction: P28003; IntAct: EBI-815383; Score: 0.27
DE  Interaction: Q12449; IntAct: EBI-818622; Score: 0.27
DE  Interaction: P40433; IntAct: EBI-7452404; Score: 0.35
DE  Interaction: P34232; IntAct: EBI-2124365; Score: 0.40
DE  Interaction: Q99257; IntAct: EBI-2124365; Score: 0.40
DE  Interaction: P11710; IntAct: EBI-7313261; Score: 0.31
DE  Interaction: P40358; IntAct: EBI-3657524; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3673786; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3691934; Score: 0.35
DE  Interaction: P36016; IntAct: EBI-3707787; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3712986; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3825819; Score: 0.35
DE  Interaction: Q02336; IntAct: EBI-4379269; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-4380099; Score: 0.35
DE  Interaction: Q01560; IntAct: EBI-7082733; Score: 0.40
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0005543;
GO  GO:0017056;
GO  GO:0051276;
GO  GO:0006302;
GO  GO:0008298;
GO  GO:0031990;
GO  GO:0006607;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006611;
GO  GO:0060188;
GO  GO:0030466;
GO  GO:0034398;
GO  GO:0000972;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MHRKSLRRASATVPSAPYRKQIISNAHNKPSLFSKIKTFFTQKDSARVSPRNNVANKQPRNESFNRRISSMPGGYFHSEI
SQ  SPDSTVNRSVVVSAVGEARNDIENKEEEYDETHETNISNAKLANFFSKKGNEPLSEIEIEGVMSLLQKSSKSMITSEGEQ
SQ  KSAEGNNIDQSLILKESGSTPISISNAPTFNPKYDTSNASMNTTLGSIGSRKYSFNYSSLPSPYKTTVYRYSAAKKIPDT
SQ  YTANTSAQSIASAKSVRSGVSKSAPSKKISNTAAALVSLLDENDSKKNNAASELANPYSSYVSQIRKHKRVSPNAAPRQE
SQ  ISEEETTVKPLFQNVPEQGEEPMKQLNATKISPSAPSKDSFTKYKPARSSSLRSNVVVAETSPEKKDGGDKPPSSAFNFS
SQ  FNTSRNVEPTENAYKSENAPSASSKEFNFTNLQAKPLVGKPKTELTKGDSTPVQPDLSVTPQKSSSKGFVFNSVQKKSRS
SQ  NLSQENDNEGKHISASIDNDFSEEKAEEFDFNVPVVSKQLGNGLVDENKVEAFKSLYTF
//
ID  Q9USL4;
PN  Nucleoporin nup61;
GN  nup61;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9USL4;
DR  UNIPROT: Q9UTW5;
DR  Pfam: PF08911;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. May play a role in mitotic spindle formation and/or function. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0140599;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0050790;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKRGADHQLTKDQDDSDDDRHGPVEVPKEASADVMATRKIAKPKSRKRPTSGVSSPGIFANLAAKPVSLPASTTQFTFG
SQ  KPAVTANNDSDIHLKKRGLNKSFIDAVIKSVDNNPFGNLSPLFDEYRQHFSSIEKKPAEEQPTSNAVVSEVNPQQQKSQD
SQ  SSSFVTEKPASSEKEDKEKPLVPPGAPRFGFSAPALGSSFQFNSSAFTPKGSFGEKSATEAEAKEKETSSNQTATGTAAT
SQ  TTNQFSFNTAANPFAFAKKENEESKPLTPVFSFSTTMASADASKETKQTHETKDSKSEESKPSNNEKSENAVEPAKGNTM
SQ  SFSWTPDKPIKFDTPEKKFTFTNPLSSKKLPASSDVKPPSAAAVGFSFGTTTNPFSFAAPKSSFPTSSTPASVGAEKSEE
SQ  TSNGNKSEQEEKENGNDETRSNDSLVSGKGKGEENEDSVFETRAKIYRFDATSKSYSDIGIGPLKINVDRDTGSARILAR
SQ  VEGSGKLLLNVRLCQDFEYSLAGKKDVKVPAASTDGKSIEMYLIRVKEPSTAEKLLAELNEKKVSKSEN
//
ID  Q8L7F7;
PN  Nuclear pore complex protein NUP62;
GN  NUP62;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8L7F7;
DR  UNIPROT: Q9SHD8;
DR  Pfam: PF05064;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9FFV8; IntAct: EBI-4514080; Score: 0.37
DE  Interaction: Q9SB65; IntAct: EBI-4526544; Score: 0.37
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0044613;
GO  GO:0005543;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0010930;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGFPFGQSNSVGGFSFGSSSATNSSSASSTTSPLSFSFNQSSNPSSTGFGFGSSVSSTPASSTTPSFGFGASSTPSFGF
SQ  GSSASSSTPSFGFGSSASVTPASTTPSFGFGTAASSSAPAPSLFGSSTTNASSAAPGSSPFGFVTSSASSTATPSSSLFG
SQ  APASSAATPSSSPFGAAPASGSTPLFGSSPSLFSAPSSASASNSSLFGASSSAATSTSPLFGAPSSATGATPSFSVASSA
SQ  PGSSSSIFGATGSSPSFSVASSASGSSPSIFGATGSSPFFGSSSSAGSTPSLFASSSSGATTSSPSPFGVSTFNSSSTSN
SQ  TSNASASPFSASTGFSFLKSTASSTTSSTTPSAPPQTASSSSSFSFGTSANSGFNLSTGSSAAPASSTSGAVFSIATTTT
SQ  TSSSTPAATSAPASSAPASTMAFPSFGVTSSATNTTPASSAATFSTTGFGLASSTPATGSTNSFTGFAVPKTSTPASSSQ
SQ  PQTTSPAFSFSLPSSTSTTAPATSSATTTQTTLVVPSSSGTSTAVAPVAGSPKLPSEITGKTVEEIIKEWNTELQERTGR
SQ  FRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVDKALQSMEEEAERIYNDERKSLLDDEA
SQ  ASTRDAMYEQSELVERELEHMTEQIRSIIQSVNANQGGELEAIDGMSPLDVVVRILNNQLSSLMWIDEKAEEFSSRIQKI
SQ  ALQGSGGDRELMAPKHWMS
//
ID  Q7JXF5;
PN  Nuclear pore glycoprotein p62;
GN  Nup62;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:26341556}. Chromosome {ECO:0000269|PubMed:20144760}. Nucleus envelope {ECO:0000269|PubMed:26341556}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:7641726}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P37198}. Note=Central region of the nuclear pore, within the transporter (By similarity). Associates with chromatin (PubMed:20144760). {ECO:0000250|UniProtKB:P37198, ECO:0000269|PubMed:20144760}.
DR  UNIPROT: Q7JXF5;
DR  Pfam: PF05064;
DE  Function: Essential component of the nuclear pore complex (By similarity). The N-terminal is probably involved in nucleocytoplasmic transport (By similarity). The C-terminal is involved in protein- protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of Nup62 to the pore complex (By similarity). Binds to transcriptionally active genes (PubMed:20144760). Negatively regulates chromatin attachment to the nuclear envelope, probably by preventing chromatin tethering by Nup154 (PubMed:26341556). {ECO:0000250|UniProtKB:P37198, ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:26341556}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VP67; IntAct: EBI-203693; Score: 0.00
DE  Interaction: Q9VIY1; IntAct: EBI-206585; Score: 0.00
DE  Interaction: Q9VYT1; IntAct: EBI-218220; Score: 0.00
DE  Interaction: Q9VBJ9; IntAct: EBI-237562; Score: 0.00
DE  Interaction: Q9VBH0; IntAct: EBI-237744; Score: 0.00
DE  Interaction: Q8T414; IntAct: EBI-243648; Score: 0.00
DE  Interaction: Q9W4H1; IntAct: EBI-243672; Score: 0.00
DE  Interaction: P17886; IntAct: EBI-264757; Score: 0.00
DE  Interaction: Q9W053; IntAct: EBI-266212; Score: 0.00
DE  Interaction: Q7KW14; IntAct: EBI-267509; Score: 0.00
DE  Interaction: Q9VDS5; IntAct: EBI-274820; Score: 0.00
DE  Interaction: Q9VBM3; IntAct: EBI-276094; Score: 0.00
DE  Interaction: Q9VDK2; IntAct: EBI-278088; Score: 0.00
DE  Interaction: Q9VG59; IntAct: EBI-278552; Score: 0.00
DE  Interaction: Q9VF74; IntAct: EBI-279954; Score: 0.00
DE  Interaction: Q9GYU8; IntAct: EBI-280213; Score: 0.00
DE  Interaction: Q9VSF3; IntAct: EBI-280217; Score: 0.00
DE  Interaction: Q9V6B9; IntAct: EBI-280221; Score: 0.00
DE  Interaction: Q9VVB4; IntAct: EBI-280225; Score: 0.00
DE  Interaction: Q9VYX1; IntAct: EBI-2550835; Score: 0.46
DE  Interaction: O76216; IntAct: EBI-2550846; Score: 0.46
DE  Interaction: Q9U3V9; IntAct: EBI-2554458; Score: 0.46
DE  Interaction: Q8I8V0; IntAct: EBI-2550868; Score: 0.27
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005815;
GO  GO:0005635;
GO  GO:0044613;
GO  GO:0000922;
GO  GO:0031490;
GO  GO:0005543;
GO  GO:0017056;
GO  GO:0097240;
GO  GO:0051028;
GO  GO:0030717;
GO  GO:0006606;
GO  GO:0097298;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVFQLPTTTAAPTGGATSSFSFGLSTGTPAAAPASGAATTAPATKTTFSFGTPAPTAGIGGGDADNSKAQAPPAFGFGLG
SQ  SGTASAPLTLGTQAAANPASTTSATATGTSAAPPAFGGFTAQPAASVVPTIATSAPNTAATTTGLLGGSGLGAPKTTAAA
SQ  STTLTAAPSAIASTQGAAPAPTLSTGGAFANLTTETKTTDSSAVSTASQLSYHQLEEHINKWTLEFEEQEKVFTEQATQI
SQ  NAWDKLLISNNGKIVELNDAVKKVKTDQQVLDQELEFIATQQKELEDSLGPLEKEFVNLPRVDMERSQTYLMVENLDTQL
SQ  KQMSEDLKEIIDNLNEANKGQDTTDPIIQIGKILNAHMNSLQWIESQSTNISKKLEDIGKIQDSQKRDIFRAPF
//
ID  P37198;
PN  Nuclear pore glycoprotein p62;
GN  NUP62;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:1915414}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:24107630}. Nucleus envelope {ECO:0000269|PubMed:24107630}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:24107630}. Note=Central region of the nuclear pore, within the transporter (PubMed:1915414). During mitotic cell division, it associates with the poles of the mitotic spindle (PubMed:24107630). {ECO:0000269|PubMed:1915414, ECO:0000269|PubMed:24107630}.
DR  UNIPROT: P37198;
DR  UNIPROT: B3KWU5;
DR  UNIPROT: Q503A4;
DR  UNIPROT: Q6GTM2;
DR  UNIPROT: Q96C43;
DR  UNIPROT: Q9NSL1;
DR  PDB: 5IJN;
DR  PDB: 5IJO;
DR  PDB: 7PER;
DR  Pfam: PF05064;
DR  OMIM: 271930;
DR  OMIM: 605815;
DR  DisGeNET: 23636;
DE  Function: Essential component of the nuclear pore complex (PubMed:1915414). The N-terminal is probably involved in nucleocytoplasmic transport (PubMed:1915414). The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex (PubMed:1915414, PubMed:24107630). Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation (PubMed:24107630). It might be involved in protein recruitment to the centrosome after nuclear breakdown (PubMed:24107630). {ECO:0000269|PubMed:1915414, ECO:0000269|PubMed:24107630}.
DE  Disease: Infantile striatonigral degeneration (SNDI) [MIM:271930]: Neurological disorder characterized by symmetrical degeneration of the caudate nucleus, putamen, and occasionally the globus pallidus, with little involvement of the rest of the brain. The clinical features include developmental regression, choreoathetosis, dystonia, spasticity, dysphagia, failure to thrive, nystagmus, optic atrophy, and intellectual disability. {ECO:0000269|PubMed:16786527}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O00299; IntAct: EBI-3916132; Score: 0.37
DE  Interaction: O35387; IntAct: EBI-11010276; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: Q9UBU9; IntAct: EBI-7193172; Score: 0.88
DE  Interaction: P40425; IntAct: EBI-348670; Score: 0.00
DE  Interaction: Q13123; IntAct: EBI-735265; Score: 0.00
DE  Interaction: Q7Z3B4; IntAct: EBI-752836; Score: 0.90
DE  Interaction: O60941; IntAct: EBI-753073; Score: 0.74
DE  Interaction: Q96QU8; IntAct: EBI-754264; Score: 0.67
DE  Interaction: Q9Y3C0; IntAct: EBI-757057; Score: 0.83
DE  Interaction: Q9NVV9; IntAct: EBI-758710; Score: 0.89
DE  Interaction: Q9H8Y8; IntAct: EBI-759475; Score: 0.55
DE  Interaction: Q14653; IntAct: EBI-7476751; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-2514381; Score: 0.40
DE  Interaction: Q13283; IntAct: EBI-2514311; Score: 0.56
DE  Interaction: P24386; IntAct: EBI-2515120; Score: 0.40
DE  Interaction: Q8ZJB3; IntAct: EBI-2846229; Score: 0.00
DE  Interaction: O15265; IntAct: EBI-3866576; Score: 0.51
DE  Interaction: O15294; IntAct: EBI-8634423; Score: 0.37
DE  Interaction: Q9BVL2; IntAct: EBI-8635195; Score: 0.80
DE  Interaction: Q7Z3B3; IntAct: EBI-8648857; Score: 0.67
DE  Interaction: Q9Y547; IntAct: EBI-8649703; Score: 0.37
DE  Interaction: P05413; IntAct: EBI-8649834; Score: 0.78
DE  Interaction: Q6ZUS5; IntAct: EBI-8657403; Score: 0.67
DE  Interaction: Q9HD26; IntAct: EBI-3923919; Score: 0.37
DE  Interaction: Q53FT3; IntAct: EBI-6140503; Score: 0.44
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q93034; IntAct: EBI-21331078; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6515052; Score: 0.35
DE  Interaction: P10238; IntAct: EBI-6883966; Score: 0.52
DE  Interaction: Q2HR75; IntAct: EBI-6884745; Score: 0.40
DE  Interaction: Q9WMX2; IntAct: EBI-9081122; Score: 0.37
DE  Interaction: Q8WYP5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: P0C206; IntAct: EBI-9675633; Score: 0.49
DE  Interaction: Q85601; IntAct: EBI-9676198; Score: 0.49
DE  Interaction: P03410; IntAct: EBI-9676269; Score: 0.49
DE  Interaction: A1L4H1; IntAct: EBI-10172894; Score: 0.72
DE  Interaction: O43482; IntAct: EBI-10184009; Score: 0.72
DE  Interaction: O75971; IntAct: EBI-10190055; Score: 0.56
DE  Interaction: P25791; IntAct: EBI-10202758; Score: 0.56
DE  Interaction: P35900; IntAct: EBI-10206952; Score: 0.74
DE  Interaction: P40222; IntAct: EBI-10207843; Score: 0.72
DE  Interaction: P61970; IntAct: EBI-10219209; Score: 0.78
DE  Interaction: Q03933; IntAct: EBI-10223376; Score: 0.67
DE  Interaction: Q12934; IntAct: EBI-10227492; Score: 0.56
DE  Interaction: Q13444; IntAct: EBI-10229334; Score: 0.56
DE  Interaction: Q13526; IntAct: EBI-10229587; Score: 0.72
DE  Interaction: Q494R4; IntAct: EBI-10241471; Score: 0.56
DE  Interaction: Q5THT1; IntAct: EBI-10247205; Score: 0.56
DE  Interaction: P52292; IntAct: EBI-10251274; Score: 0.56
DE  Interaction: Q70UQ0; IntAct: EBI-10255735; Score: 0.56
DE  Interaction: Q71F23; IntAct: EBI-10255817; Score: 0.56
DE  Interaction: Q8IY31; IntAct: EBI-10262678; Score: 0.56
DE  Interaction: Q8IYE0; IntAct: EBI-10263081; Score: 0.56
DE  Interaction: Q8IYX8; IntAct: EBI-10263946; Score: 0.56
DE  Interaction: Q8NCX0; IntAct: EBI-10269350; Score: 0.56
DE  Interaction: Q8TAB5; IntAct: EBI-10271360; Score: 0.72
DE  Interaction: Q8TD06; IntAct: EBI-10274366; Score: 0.72
DE  Interaction: Q8TD31; IntAct: EBI-10274576; Score: 0.72
DE  Interaction: Q969G3; IntAct: EBI-10280555; Score: 0.56
DE  Interaction: Q96BD5; IntAct: EBI-10282314; Score: 0.78
DE  Interaction: Q96CS2; IntAct: EBI-10283634; Score: 0.56
DE  Interaction: Q9BVG8; IntAct: EBI-10299442; Score: 0.56
DE  Interaction: Q9H1K1; IntAct: EBI-10305100; Score: 0.72
DE  Interaction: Q9H614; IntAct: EBI-10307329; Score: 0.56
DE  Interaction: Q9NYB9; IntAct: EBI-10316691; Score: 0.74
DE  Interaction: Q9UGL9; IntAct: EBI-10320650; Score: 0.72
DE  Interaction: Q9UL45; IntAct: EBI-10323574; Score: 0.72
DE  Interaction: Q14129; IntAct: EBI-21248894; Score: 0.37
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q9D620; IntAct: EBI-11042984; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-11151540; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P31384; IntAct: EBI-11525237; Score: 0.56
DE  Interaction: P40014; IntAct: EBI-11530287; Score: 0.56
DE  Interaction: P40368; IntAct: EBI-11530824; Score: 0.56
DE  Interaction: P48232; IntAct: EBI-11532600; Score: 0.56
DE  Interaction: P48837; IntAct: EBI-11532748; Score: 0.56
DE  Interaction: P53829; IntAct: EBI-11533635; Score: 0.56
DE  Interaction: Q02831; IntAct: EBI-11534617; Score: 0.56
DE  Interaction: Q06707; IntAct: EBI-11535911; Score: 0.56
DE  Interaction: A0A0S2Z4Q4; IntAct: EBI-16437929; Score: 0.56
DE  Interaction: P55735; IntAct: EBI-11889192; Score: 0.49
DE  Interaction: P04259; IntAct: EBI-24284514; Score: 0.56
DE  Interaction: Q7L8S5; IntAct: EBI-24298857; Score: 0.56
DE  Interaction: P51687; IntAct: EBI-24262605; Score: 0.72
DE  Interaction: Q8N6Y0; IntAct: EBI-24316772; Score: 0.56
DE  Interaction: Q969G5; IntAct: EBI-24343552; Score: 0.56
DE  Interaction: Q9NWQ9; IntAct: EBI-24347714; Score: 0.56
DE  Interaction: Q8N7C3; IntAct: EBI-25244705; Score: 0.56
DE  Interaction: Q9HAT8; IntAct: EBI-25252947; Score: 0.56
DE  Interaction: P53365; IntAct: EBI-25253608; Score: 0.56
DE  Interaction: Q9BW11; IntAct: EBI-25255668; Score: 0.56
DE  Interaction: Q9ULV5; IntAct: EBI-24492690; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-24509399; Score: 0.56
DE  Interaction: Q99567; IntAct: EBI-24419613; Score: 0.67
DE  Interaction: P02538; IntAct: EBI-24402104; Score: 0.56
DE  Interaction: O14964; IntAct: EBI-24412058; Score: 0.56
DE  Interaction: Q6W0C5; IntAct: EBI-25262195; Score: 0.56
DE  Interaction: P12035; IntAct: EBI-24419369; Score: 0.56
DE  Interaction: Q04727; IntAct: EBI-24265280; Score: 0.56
DE  Interaction: P10599; IntAct: EBI-24436520; Score: 0.56
DE  Interaction: A0A024R8L2; IntAct: EBI-24260266; Score: 0.56
DE  Interaction: O95678; IntAct: EBI-24458252; Score: 0.63
DE  Interaction: P04264; IntAct: EBI-24260450; Score: 0.74
DE  Interaction: E5LBS6; IntAct: EBI-14062727; Score: 0.50
DE  Interaction: P62826; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: Q9NUU7; IntAct: EBI-21587900; Score: 0.35
DE  Interaction: Q96FN4; IntAct: EBI-21659658; Score: 0.35
DE  Interaction: P19338; IntAct: EBI-15687558; Score: 0.35
DE  Interaction: Q9Y6D6; IntAct: EBI-15687558; Score: 0.35
DE  Interaction: P70168; IntAct: EBI-16128776; Score: 0.44
DE  Interaction: Q86VP6; IntAct: EBI-16128814; Score: 0.44
DE  Interaction: Q9BPX3; IntAct: EBI-16128870; Score: 0.44
DE  Interaction: P30153; IntAct: EBI-16128852; Score: 0.44
DE  Interaction: P30154; IntAct: EBI-16128908; Score: 0.44
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P03427; IntAct: EBI-25769759; Score: 0.37
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P51531; IntAct: EBI-26515309; Score: 0.37
DE  Interaction: Q96LU5; IntAct: EBI-27050332; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: O75874; IntAct: EBI-27039737; Score: 0.37
DE  Interaction: Q9UQM7; IntAct: EBI-28947140; Score: 0.35
DE  Interaction: O75381; IntAct: EBI-30835357; Score: 0.44
DE  Interaction: Q05397; IntAct: EBI-30836789; Score: 0.44
DE  Interaction: P41212; IntAct: EBI-29015445; Score: 0.27
DE  Interaction: P40763; IntAct: EBI-29762103; Score: 0.27
DE  Interaction: Q14765; IntAct: EBI-29763222; Score: 0.27
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0090543;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:1990904;
GO  GO:0000922;
GO  GO:0003682;
GO  GO:0030544;
GO  GO:0051879;
GO  GO:0005543;
GO  GO:0051425;
GO  GO:0042169;
GO  GO:0030159;
GO  GO:0017056;
GO  GO:0043130;
GO  GO:0008219;
GO  GO:0007166;
GO  GO:0090398;
GO  GO:0098534;
GO  GO:0007098;
GO  GO:0007100;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0042059;
GO  GO:0043407;
GO  GO:0043069;
GO  GO:0046580;
GO  GO:0006913;
GO  GO:0046601;
GO  GO:0045893;
GO  GO:0045742;
GO  GO:0043123;
GO  GO:1903438;
GO  GO:0045840;
GO  GO:1904781;
GO  GO:0006606;
GO  GO:0060236;
GO  GO:0046578;
GO  GO:0009966;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGFNFGGTGAPTGGFTFGTAKTATTTPATGFSFSTSGTGGFNFGAPFQPATSTPSTGLFSLATQTPATQTTGFTFGTAT
SQ  LASGGTGFSLGIGASKLNLSNTAATPAMANPSGFGLGSSNLTNAISSTVTSSQGTAPTGFVFGPSTTSVAPATTSGGFSF
SQ  TGGSTAQPSGFNIGSAGNSAQPTAPATLPFTPATPAATTAGATQPAAPTPTATITSTGPSLFASIATAPTSSATTGLSLC
SQ  TPVTTAGAPTAGTQGFSLKAPGAASGTSTTTSTAATATATTTSSSSTTGFALNLKPLAPAGIPSNTAAAVTAPPGPGAAA
SQ  GAAASSAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQ
SQ  KELEDLLSPLEELVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNTSGAPADTSDPLQQICKILNA
SQ  HMDSLQWIDQNSALLQRKVEEVTKVCEGRRKEQERSFRITFD
//
ID  Q63850;
PN  Nuclear pore glycoprotein p62;
GN  Nup62;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P37198}. Nucleus envelope {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P37198}. Note=Central region of the nuclear pore, within the transporter. During mitotic cell division, it associates with the poles of the mitotic spindle. {ECO:0000250|UniProtKB:P37198}.
DR  UNIPROT: Q63850;
DR  UNIPROT: Q99JN7;
DR  Pfam: PF05064;
DE  Function: Essential component of the nuclear pore complex. The N- terminal is probably involved in nucleocytoplasmic transport. The C- terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex. Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation. It might be involved in protein recruitment to the centrosome after nuclear breakdown. {ECO:0000250|UniProtKB:P37198}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0005642;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0090543;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0032991;
GO  GO:1990904;
GO  GO:0000922;
GO  GO:0030544;
GO  GO:0051879;
GO  GO:0019894;
GO  GO:0046966;
GO  GO:0005543;
GO  GO:0044877;
GO  GO:0051425;
GO  GO:0042169;
GO  GO:0030159;
GO  GO:0017056;
GO  GO:0043130;
GO  GO:0008219;
GO  GO:0016477;
GO  GO:0007166;
GO  GO:0090398;
GO  GO:0098534;
GO  GO:0007098;
GO  GO:0000278;
GO  GO:0007100;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0042059;
GO  GO:0043407;
GO  GO:0043069;
GO  GO:0046580;
GO  GO:0006913;
GO  GO:0046601;
GO  GO:0045893;
GO  GO:0043123;
GO  GO:1903438;
GO  GO:0045840;
GO  GO:1904781;
GO  GO:0006606;
GO  GO:0060236;
GO  GO:0042306;
GO  GO:0006405;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGFNFGGTGAPAGGFTFGTAKTATTTPATGFSFSASGTGTGGFNFGTPSQPAATTPSTSLFSLTTQTPTTQTPGFNFGT
SQ  TPASGGTGFSLGISTPKLSLSNAAATPATANTGSFGLGSSTLTNAISSGSTSNQGTAPTGFVFGSSTTSAPSTGSTGFSF
SQ  TSGSASQPGASGFSLGSVGSSAQPTALSGSPFTPATLVTTTAGATQPAAAAPTAATTSAGSTLFASIAAAPASSSATGLS
SQ  LPAPVTTAATPSAGTLGFSLKAPGAAPGASTTSTTTTTTTTTTTAAAAAASTTTTGFALSLKPLVSAGPSSVAATALPAS
SQ  STAAGTATGPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFI
SQ  LSQQKELEDLLSPLEESVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDPLQQICK
SQ  ILNAHMDSLQWVDQSSALLQRRVEEASRVCEGRRKEQERSLRIAFD
//
ID  P17955;
PN  Nuclear pore glycoprotein p62;
GN  Nup62;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:8707840}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P37198}. Nucleus envelope {ECO:0000269|PubMed:2190987}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P37198}. Note=Central region of the nuclear pore, within the transporter. During mitotic cell division, it associates with the poles of the mitotic spindle. {ECO:0000250|UniProtKB:P37198}.
DR  UNIPROT: P17955;
DR  UNIPROT: A2VCW0;
DR  PDB: 3T97;
DR  PDB: 5H1X;
DR  Pfam: PF05064;
DE  Function: Essential component of the nuclear pore complex (PubMed:2190987, PubMed:8707840). The N-terminal is probably involved in nucleocytoplasmic transport (By similarity). The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex (By similarity). Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation (By similarity). It might be involved in protein recruitment to the centrosome after nuclear breakdown (By similarity). {ECO:0000250|UniProtKB:P37198, ECO:0000269|PubMed:2190987, ECO:0000269|PubMed:8707840}.
DE  Reference Proteome: Yes;
DE  Interaction: P70168; IntAct: EBI-15732706; Score: 0.36
GO  GO:0005642;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0090543;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0032991;
GO  GO:1990904;
GO  GO:0000922;
GO  GO:0030544;
GO  GO:0051879;
GO  GO:0019894;
GO  GO:0046966;
GO  GO:0005543;
GO  GO:0044877;
GO  GO:0051425;
GO  GO:0042169;
GO  GO:0030159;
GO  GO:0017056;
GO  GO:0043130;
GO  GO:0008219;
GO  GO:0007166;
GO  GO:0090398;
GO  GO:0098534;
GO  GO:0007098;
GO  GO:0000278;
GO  GO:0007100;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0043066;
GO  GO:0008285;
GO  GO:0042059;
GO  GO:0043407;
GO  GO:0043069;
GO  GO:0046580;
GO  GO:0046601;
GO  GO:0045893;
GO  GO:0043123;
GO  GO:1903438;
GO  GO:0045840;
GO  GO:1904781;
GO  GO:0006606;
GO  GO:0060236;
GO  GO:0042306;
GO  GO:0006405;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGFNFGGTGAPAGGFTFGTAKTATTTPATGFSFSASGTGTGGFNFGTPSQPAATTPSTSLFSLATQTSTTQTPGFNFGT
SQ  TPASGGTGFSLGISTPKLSLSSTAATPATANTGSFGLGSSTLTNAISGASTSSQGTAPTGFVFGSSTTSAPSTGTTGFSF
SQ  TSGSASQPGASGFNIGSVGSLAQPTALSGSPFTPATLATTTAGATQPAAATPTAATTSAGSTLFASIAAAPASSSTTVLS
SQ  LSAPATTAATPTAGTLGFSLKAPGAAPGASTTSTTTTTTTTTTTASTSSSTTTTGFALSLKPLVPAGPSSVAATALPASS
SQ  TAVGTTTGPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFIL
SQ  SQQKELEDLLSPLEESVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDPLQQICKI
SQ  LNAHMDSLQWVDQSSALLQRRVEEASRVCESRRKEQERSLRIAFD
//
ID  A1YK02;
PN  Nuclear pore complex protein Nup75;
GN  Nup75;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}.
DR  UNIPROT: A1YK02;
DR  UNIPROT: Q8SZH5;
DR  Pfam: PF07575;
DE  Function: Component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (By similarity). Required for nuclear import of phosphorylated Mad via importin msk (PubMed:20547758). Has no role in classical nuclear localization signal (cNLS)-dependent nuclear import via importin-beta (PubMed:20547758). Facilitates the interaction between Nup93 and sec13 with msk (PubMed:20547758). {ECO:0000250|UniProtKB:Q9BW27, ECO:0000269|PubMed:20547758}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8T0S6; IntAct: EBI-211888; Score: 0.00
DE  Interaction: Q9VX05; IntAct: EBI-226125; Score: 0.00
DE  Interaction: Q9VXS4; IntAct: EBI-244905; Score: 0.00
DE  Interaction: Q9VDI5; IntAct: EBI-249597; Score: 0.00
DE  Interaction: P39769; IntAct: EBI-254420; Score: 0.00
DE  Interaction: Q9W087; IntAct: EBI-256716; Score: 0.00
DE  Interaction: Q9VR15; IntAct: EBI-269063; Score: 0.00
DE  Interaction: Q7K0E3; IntAct: EBI-269271; Score: 0.00
DE  Interaction: Q03017; IntAct: EBI-279084; Score: 0.00
DE  Interaction: Q7JYZ0; IntAct: EBI-279088; Score: 0.00
DE  Interaction: Q9VLT9; IntAct: EBI-279092; Score: 0.00
DE  Interaction: Q9VLP3; IntAct: EBI-279096; Score: 0.00
DE  Interaction: Q9VZU6; IntAct: EBI-505546; Score: 0.00
DE  Interaction: P18431; IntAct: EBI-9950635; Score: 0.35
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:2000331;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDSGVFAFELGDDLATRCGNTLTGVFVPGSRIALSAYRHVTHSSRDEPTENAGQVPVLIYMAQESTLFDEPVLRSVLAE
SQ  ANATFATLQQLGSRATRAEYVNISRAYRSIVRSCLEKLEQAKKSPEVQTDEARLQRLCDAIVVFYAAECLWHLFEILYIQ
SQ  SNQLVVPQLLDWARFHSPHAEDRATDLLLMGEEASESDDYWSIVKSLIMLGEIDVTRAVLSQNRKAGQTSFKAAEQILKS
SQ  MPVYQEGYALQKFHSQWEFWHVDTERKIQSGLFATEPELEQLIRLVAGDSEQWDAGIKESQDFYEYLPGYLLFTKPTCKP
SQ  FELKIAAAKWLNRWCLLRPEREQCSMNRMVSQLMDHDLRLFIYDAQKLNDTHWFSTHLIDLIHHCGQLKSYFDQNNIDLP
SQ  ALRHSMIYEYGSYLMTSHNMWQLGIDYLDCCKQEGQAAIELLLPRITLRSERQATKLINLARQRGLISVEREICKVLSKR
SQ  SYDNERYGNALEWAIRSKDVLLVTAVADFILKHYSKTGCMLCPDTIANVGGRMFASPRLVFLSKYFEFYEFYRTRDFLSA
SQ  SELLVNLLESKITPDYFWPSLLIDSMPLLESKDPKIFAKETVAILHHIETDLVPIIERDVSKYGKHHTETVFKDYRVENV
SQ  DEIMNLLRLACARNLARALIIENTLPVV
//
ID  G0S4F3;
PN  Nucleoporin NUP82;
GN  NUP82;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P40368}. Nucleus membrane {ECO:0000250|UniProtKB:P40368}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40368}; Cytoplasmic side {ECO:0000250|UniProtKB:P40368}.
DR  UNIPROT: G0S4F3;
DR  UNIPROT: G0ZGT7;
DR  PDB: 5CWW;
DR  PROSITE: PS00678;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000250|UniProtKB:P40368}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S156; IntAct: EBI-16176459; Score: 0.46
DE  Interaction: G0SBQ3; IntAct: EBI-16176539; Score: 0.58
DE  Interaction: G0SAK3; IntAct: EBI-16176900; Score: 0.44
DE  Interaction: G0SBS8; IntAct: EBI-16176971; Score: 0.35
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P40368};
SQ  MPKIKSFAPAWLNEPAPGHKLFAPAADDGTATVPLAYGKKIKPGPRRTIARRGTEIFVACGKQIRWGDLAQLKESWESRP
SQ  SRSSVGPTSTKKDSSDFDDGAATAGYRIIKTPVADDIRQLVMSPNQDFLAVLTSHTVHICILPDSSHLHIQDTTPFKPKF
SQ  WTLGPTTHVTSRSAVVSAVWHPLGVNGHALVTVTEDAIVRVWELSTADRWTFDAPTLAIDLKKLADATYLDQDFGVSTSA
SQ  TNKGFSPDAFDMEVAAACFPTRDSGGWAPMTLWLAMTSGDVYALCPLLPQRWTPPPTLIPSLSASIVAKVAAAEDNPEST
SQ  PEERLVAQQQLEWMSEIDNQEPKLVEEATGEATIEVYTRPSRPGLVPKLQGPFDFDLNPEDEQDDEVELKDIYVIGEKPR
SQ  VADLMRGEEEELEMMKEDQHNGLSLNIICLLSTSGQVKICLDIDGVEAQWLPPRSKNKRLFAPPPEPPSLLTFQTFDTLK
SQ  PAEVTPDGWPMFSEDATSPYSFYVTHPAGITYISLTPWVFRLESELQSDSEAGTEFRIDLLAKGQGSERDRIFTQTRTQS
SQ  PLAAATSIDDPDLGYFILSATQTDPIALFFETPERPVVPKETSVVIPEHVEERPPSPYWEPRPLFHPAEALDKPSAVPAW
SQ  IDNLRTGRRRPLLTQELRLSMATLEVFHDGHKVVSTEVSDINDAVAELFRKCEALQGELRDQIKKVNEVKNRIHTITGDD
SQ  LSDDPPVSEDQLIKQRIRVARERQEELANRMERLRKKFGRTTTRELSDKEKAWIEEVQNMATSILGPEAGQGALATTPNL
SQ  AKQPWKRLEEIKTLRNALMAEAEQLQKVGDDTEESTPASQMPSLKIPSEIRKAKMAQVMSLLERESALVDAVKARIERLS
SQ  IG
//
ID  Q9P382;
PN  Nucleoporin nup82;
GN  nup82;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000305|PubMed:16823372}; Peripheral membrane protein {ECO:0000305|PubMed:16823372}; Cytoplasmic side {ECO:0000305|PubMed:16823372}.
DR  UNIPROT: Q9P382;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). {ECO:0000250|UniProtKB:P40368}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0044612;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:16823372};
SQ  MASTIMSQEVSWTDILEKHPALRWIKPIPEDWEIFPKHLCAFESFLYVAVGQEVRSLDCRLLKHKNEASHKNFYKKLFNP
SQ  ELDFMIEQICLSKNGRFLAVVGKSKIVILGLRSKLSEQNPLAESVSNFGESVNNFSNSEHQENGTNSLKLSEVTICSVAV
SQ  INPSSQIVSVRFHPLGKSGRSLVVLTETSLLLYEAGNGVLMPDYEIPLKLTHQASNSFDADVDLHIPTAFCFSNVSQGWG
SQ  VFTIYILTRGGDVFSVCPVMPANAMIPQDVLKQIRLILTKKEDDADAENHRRNVHWITKLLGEAALANDLSTSFVISEGS
SQ  SELFDSSDYVSVRRPDDFSFIPSMQGPFLLQPAVADDELIEDYCDIYSFGMNPIDVLAIGGSEGRLDLLLLVSEVSGRWS
SQ  KLNDHGLASMKLIVSQVHSLYLSNNNPYMVLQPDIQSPYSLIAYHANGLHVVDIESWARDLNLNFENSEFLNNEEENDED
SQ  ELSNVLVSIPSRTSVLERLDTNPLNESTDAVVGCAQLYYPSLGKILISLTRNWQTTVFDDSDLATMGVNKESLSNEMDYS
SQ  KSLGTSSLEQVDDLDEKLTYTPLYVSLLEKTPFTDPSIPSLVERTIVPAELQNEITVSSASLRFLGKVVARYRETLNLLD
SQ  HGCSELHHRLKLQREEYERQQNHIYKLSDRISNFREKAWSTEHLEHLTSDMSMCEKRIDQVLQRVMDLRVPDLSDKEKQF
SQ  IKEIGNYKEKVTGERGIEKRVETLKTLLQRTKPRDAQTTLVASSSDMRLAAIEQLQKLLAQQSLSIKELKTKTVSFQRLL
SQ  QTS
//
ID  P40368;
PN  Nucleoporin NUP82;
GN  NUP82;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10801828}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
DR  UNIPROT: P40368;
DR  UNIPROT: D6VWC1;
DR  PDB: 3PBP;
DR  PDB: 3TKN;
DR  PDB: 7N9F;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain. {ECO:0000269|PubMed:10801828, ECO:0000269|PubMed:10891509, ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:11739405, ECO:0000269|PubMed:7559750, ECO:0000269|PubMed:9843582}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-790236; Score: 0.87
DE  Interaction: P35729; IntAct: EBI-6325174; Score: 0.00
DE  Interaction: P36161; IntAct: EBI-8466646; Score: 0.40
DE  Interaction: P37198; IntAct: EBI-11530824; Score: 0.56
DE  Interaction: P40066; IntAct: EBI-797307; Score: 0.44
DE  Interaction: P53267; IntAct: EBI-517239; Score: 0.37
DE  Interaction: P40368; IntAct: EBI-7124268; Score: 0.57
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P11484; IntAct: EBI-790236; Score: 0.53
DE  Interaction: P10591; IntAct: EBI-790236; Score: 0.35
DE  Interaction: P40477; IntAct: EBI-790236; Score: 0.81
DE  Interaction: P40150; IntAct: EBI-794951; Score: 0.35
DE  Interaction: Q02630; IntAct: EBI-795280; Score: 0.67
DE  Interaction: P46673; IntAct: EBI-11889278; Score: 0.55
DE  Interaction: Q02629; IntAct: EBI-11889216; Score: 0.55
DE  Interaction: Q06410; IntAct: EBI-2342927; Score: 0.37
DE  Interaction: P29295; IntAct: EBI-2612057; Score: 0.35
DE  Interaction: P23291; IntAct: EBI-2614250; Score: 0.35
DE  Interaction: P24869; IntAct: EBI-2617071; Score: 0.35
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q04477; IntAct: EBI-2887856; Score: 0.00
DE  Interaction: P48363; IntAct: EBI-3817422; Score: 0.35
DE  Interaction: Q9Y3C0; IntAct: EBI-11530851; Score: 0.56
DE  Interaction: Q9HCM9; IntAct: EBI-11530842; Score: 0.56
DE  Interaction: Q9BQD3; IntAct: EBI-11530833; Score: 0.56
DE  Interaction: Q02199; IntAct: EBI-11889308; Score: 0.37
DE  Interaction: Q03790; IntAct: EBI-11889264; Score: 0.37
DE  Interaction: P49687; IntAct: EBI-11889248; Score: 0.37
DE  Interaction: Q12443; IntAct: EBI-16713207; Score: 0.37
DE  Interaction: P40003; IntAct: EBI-16298592; Score: 0.00
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0044612;
GO  GO:0005634;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0006913;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSQSSRLSALPIFQASLSASQSPRYIFSSQNGTRIVFIQDNIIRWYNVLTDSLYHSLNFSRHLVLDDTFHVISSTSGDLL
SQ  CLFNDNEIFVMEVPWGYSNVEDVSIQDAFQIFHYSIDEEEVGPKSSIKKVLFHPKSYRDSCIVVLKEDDTITMFDILNSQ
SQ  EKPIVLNKPNNSFGLDARVNDITDLEFSKDGLTLYCLNTTEGGDIFAFYPFLPSVLLLNEKDLNLILNKSLVMYESLDST
SQ  TDVIVKRNVIKQLQFVSKLHENWNSRFGKVDIQKEYRLAKVQGPFTINPFPGELYDYTATNIATILIDNGQNEIVCVSFD
SQ  DGSLILLFKDLEMSMSWDVDNYVYNNSLVLIERVKLQREIKSLITLPEQLGKLYVISDNIIQQVNFMSWASTLSKCINES
SQ  DLNPLAGLKFESKLEDIATIERIPNLAYINWNDQSNLALMSNKTLTFQNISSDMKPQSTAAETSISTEKSDTVGDGFKMS
SQ  FTQPINEILILNDNFQKACISPCERIIPSADRQIPLKNEASENQLEIFTDISKEFLQRIVKAQTLGVSIHNRIHEQQFEL
SQ  TRQLQSTCKIISKDDDLRRKFEAQNKKWDAQLSRQSELMERFSKLSKKLSQIAESNKFKEKKISHGEMKWFKEIRNQILQ
SQ  FNSFVHSQKSLQQDLSYLKSELTRIEAETIKVDKKSQNEWDELRKMLEIDSKIIKECNEELLQVSQEFTTKTQ
//
ID  G0SER9;
PN  Nucleoporin NUP84;
GN  NUP84;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P52891}. Nucleus membrane {ECO:0000250|UniProtKB:P52891}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52891}; Cytoplasmic side {ECO:0000250|UniProtKB:P52891}. Nucleus membrane {ECO:0000250|UniProtKB:P52891}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52891}; Nucleoplasmic side {ECO:0000250|UniProtKB:P52891}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P52891}.
DR  UNIPROT: G0SER9;
DR  UNIPROT: G0ZGU7;
DR  Pfam: PF04121;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP84 is involved in nuclear poly(A)+ RNA export, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000250|UniProtKB:P52891}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S0E7; IntAct: EBI-16069336; Score: 0.49
DE  Interaction: G0S2G1; IntAct: EBI-16069540; Score: 0.49
DE  Interaction: G0S9A7; IntAct: EBI-16069694; Score: 0.44
DE  Interaction: G0SAK3; IntAct: EBI-16069356; Score: 0.44
DE  Interaction: G0SDQ4; IntAct: EBI-16069651; Score: 0.35
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P52891};
SQ  MSPAFNIPDSIESSRGSSQSPHHGLNPEEMADIEATSQDNAVRVGEEIDYFAAQLDRYDADQTGSPPERRSRAFQLVDSY
SQ  YTFTRKRLDRLRERQARQRSAQRGSWQRAGSIEMDLDDADEENDDILDEELQQLEDEVQIWDLLRRILPLRYHDATQNQK
SQ  KEHDGSTKSRRQWWNEFMVSDSVARERKVVLEWLQNSASYGPPIDEVVSDLQHNAERGDILAHGWLHTRHKIKLQKSVNA
SQ  YQGVLDPRDAAAAQSHLSSNSLITQLDPDAVTRQARKLEPQDESFERAIWLGCFEMLRRGCSMSEIREWLAVRTELWRAF
SQ  SIAPLPLSNPDDEEQPDFDPVSLILWRRMCYAIATDGGTSDYDRAVYGLLAGDIPSVEKVCKTWDDVLFAHYNALLRTQF
SQ  DLFLIKHGGDAAAKAAQQFPSFNAVAYHGDPATATKRLIDSLETGMKTSAEAFRPAKALQAAIVADDLDKFLFHQGLLLS
SQ  IRANKKEKSKLIPEYPFPHESFSDKKYYDLGDHQGLRILAHVLIIILTLDRLSGVAKDKGPLQARHQAAENSIAAYISYL
SQ  RLVRLEEMIPLYCSKLHGPRVYSTLSRNLIHIVDIDARLHQLTIMRNLGIDVSEFVKSQPLIYLDDVQDELVSCDAKDQF
SQ  KILEDGPATLKYGRLVKPDFFGDDADYVDPEDDALIRSMEWLLLVPGLFVETCAYAVRIYKYFLKRTRLRAARAFSRRVR
SQ  GHEIIRTKFPNLLKDVDENDPAAWFEEFAAAQLPSDLLESCPASQEKLITITRHLWELESLVRALDSIETLTSLAALTRE
SQ  ESVPMTREMWQEVSQTVRIAKACMRPVLKEWLLTTYDGRSVEQDFLDIRQAYIPETILAYISCLHFAGTSLSRDNLLECM
SQ  DLAAIIAEKDSDVAKEFMRCGRMKELVEAFASASKALAIWSGEKKGSQTNSKKLRELGWSRELWSIKS
//
ID  P52891;
PN  Nucleoporin NUP84;
GN  NUP84;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P52891;
DR  UNIPROT: D6VRN4;
DR  PDB: 3IKO;
DR  PDB: 3JRO;
DR  PDB: 4XMM;
DR  PDB: 4XMN;
DR  PDB: 6X02;
DR  PDB: 6X03;
DR  PDB: 7N84;
DR  PDB: 7N9F;
DR  Pfam: PF04121;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP84 is involved in nuclear poly(A)+ RNA export, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:8565072}.
DE  Reference Proteome: Yes;
DE  Interaction: P35729; IntAct: EBI-800196; Score: 0.91
DE  Interaction: P36161; IntAct: EBI-7700705; Score: 0.55
DE  Interaction: P46673; IntAct: EBI-800196; Score: 0.73
DE  Interaction: P48837; IntAct: EBI-1269989; Score: 0.00
DE  Interaction: P49686; IntAct: EBI-1269571; Score: 0.00
DE  Interaction: P49687; IntAct: EBI-797641; Score: 0.95
DE  Interaction: P53550; IntAct: EBI-7349783; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P16140; IntAct: EBI-800196; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-800196; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-800196; Score: 0.35
DE  Interaction: P53011; IntAct: EBI-800196; Score: 0.64
DE  Interaction: Q04491; IntAct: EBI-800196; Score: 0.53
DE  Interaction: P34232; IntAct: EBI-800196; Score: 0.53
DE  Interaction: Q99257; IntAct: EBI-800196; Score: 0.61
DE  Interaction: P32582; IntAct: EBI-815440; Score: 0.27
DE  Interaction: Q02630; IntAct: EBI-1269725; Score: 0.00
DE  Interaction: Q02629; IntAct: EBI-11889422; Score: 0.59
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: P10591; IntAct: EBI-3673794; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3745803; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3781781; Score: 0.35
DE  Interaction: Q05166; IntAct: EBI-4325387; Score: 0.37
DE  Interaction: Q8WUM0; IntAct: EBI-11890201; Score: 0.40
DE  Interaction: P52891; IntAct: EBI-15805447; Score: 0.62
DE  Interaction: P25573; IntAct: EBI-16255136; Score: 0.00
DE  Interaction: P25579; IntAct: EBI-16255156; Score: 0.00
DE  Interaction: P25594; IntAct: EBI-16255176; Score: 0.00
DE  Interaction: P0CY08; IntAct: EBI-16255196; Score: 0.00
DE  Interaction: P10849; IntAct: EBI-16255216; Score: 0.00
DE  Interaction: P40316; IntAct: EBI-16255236; Score: 0.00
DE  Interaction: P43637; IntAct: EBI-16255276; Score: 0.00
DE  Interaction: P53053; IntAct: EBI-16255296; Score: 0.00
DE  Interaction: P32902; IntAct: EBI-16255316; Score: 0.00
DE  Interaction: P38690; IntAct: EBI-16255336; Score: 0.00
DE  Interaction: P47027; IntAct: EBI-16255356; Score: 0.00
DE  Interaction: Q08110; IntAct: EBI-16255376; Score: 0.00
DE  Interaction: Q08558; IntAct: EBI-16255396; Score: 0.00
DE  Interaction: Q08746; IntAct: EBI-16255416; Score: 0.00
DE  Interaction: P41921; IntAct: EBI-16255436; Score: 0.00
DE  Interaction: P33419; IntAct: EBI-16255456; Score: 0.00
DE  Interaction: P04173; IntAct: EBI-16274957; Score: 0.35
DE  Interaction: P46956; IntAct: EBI-16274957; Score: 0.35
DE  Interaction: P39692; IntAct: EBI-16274957; Score: 0.35
DE  Interaction: P25694; IntAct: EBI-16274957; Score: 0.35
GO  GO:0000781;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0042802;
GO  GO:0017056;
GO  GO:0006302;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0051664;
GO  GO:0006913;
GO  GO:0045893;
GO  GO:0045944;
GO  GO:0000973;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0030466;
GO  GO:0031509;
GO  GO:0034398;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MELSPTYQTERFTKFSDTLKEFKIEQNNEQNPIDPFNIIREFRSAAGQLALDLANSGDESNVISSKDWELEARFWHLVEL
SQ  LLVFRNADLDLDEMELHPYNSRGLFEKKLMQDNKQLYQIWIVMVWLKENTYVMERPKNVPTSKWLNSITSGGLKSCDLDF
SQ  PLRENTNVLDVKDKEEDHIFFKYIYELILAGAIDEALEEAKLSDNISICMILCGIQEYLNPVIDTQIANEFNTQQGIKKH
SQ  SLWRRTVYSLSQQAGLDPYERAIYSYLSGAIPNQEVLQYSDWESDLHIHLNQILQTEIENYLLENNQVGTDELILPLPSH
SQ  ALTVQEVLNRVASRHPSESEHPIRVLMASVILDSLPSVIHSSVEMLLDVVKGTEASNDIIDKPYLLRIVTHLAICLDIIN
SQ  PGSVEEVDKSKLITTYISLLKLQGLYENIPIYATFLNESDCLEACSFILSSLEDPQVRKKQIETINFLRLPASNILRRTT
SQ  QRVFDETEQEYSPSNEISISFDVNNIDMHLIYGVEWLIEGKLYVDAVHSIIALSRRFLLNGRVKALEQFMERNNIGEICK
SQ  NYELEKIADNISKDENEDQFLEEITQYEHLIKGIREYEEWQKSVSLLSSESNIPTLIEKLQGFSKDTFELIKTFLVDLTS
SQ  SNFADSADYEILYEIRALYTPFLLMELHKKLVEAAKLLKIPKFISEALAFTSLVANENDKIYLLFQSSGKLKEYLDLVAR
SQ  TATLSN
//
ID  Q8RXH2;
PN  Nuclear pore complex protein NUP85;
GN  NUP85;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q8RXH2;
DR  UNIPROT: O82634;
DR  UNIPROT: Q9ASW9;
DR  Pfam: PF07575;
DE  Function: Functions as component of the nuclear pore complex (NPC). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:0009737;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPGMSSESGGGELVLFSTKEKTPVLYPLSYGLKSPVHRLSISWGCGNNLRVTVLRNPELRDDDDGEVGGKVVNVRLSGED
SQ  GEISDPQWRRIAYGSVSPFALLQSRRNSISSLSKMDMSSSLYQTAWWEYVMEYSRDIKSLLSNTISLPAPLIEDPRSVIK
SQ  NAEEPTSLKAAWELMELFYADKTCLSWLPERLVDWLSEYDILLSSSHPTIYSKLQDFQKELVGLQAIEDDPRYWEVMASA
SQ  LSVGWLEIVVKLLHLHGSYQLDQLGHRETENGLVEAVAVLISKMPRMRPQLEDGKFGECSAAKPDFMKTRERWQSQITKL
SQ  ECSAFWVQCAHHQTREGLRNMLKIMIGNADCLRAATCNWMELFVSHLLYLRPFTKGLDGMHSLAQKCVQSKPVNTSHKLL
SQ  RLLIGILGENTEVVLAECSKEFGSWMVAHAMELLTAGSEEGEVLVHEEQRKLGGINMEELHRLVYAQVLSSHALTWQIAP
SQ  IYLASCEKQGLGLLELLFYRQPVQENQMLIKSLEICRLYELSNVSAKLMKISGVHHWKHGRKGSGIFWLQQARDENCLSV
SQ  IAQQLFDSVGKSLSDESLKQWEGLVELLGSESQISGGLDFLHKYRDFKRSLKVVHDGKTIDAAHEAVERLVSLMKSPSTP
SQ  QRFWLPLLHDSLKLLNWPERSLLNVTQTNLMLNKLQELSIARLRPGFIESELSAQAVGSVRLALATNLGRAFLEEC
//
ID  Q3ZC98;
PN  Nuclear pore complex protein Nup85;
GN  NUP85;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. Note=During mitosis, localizes to the kinetochores and spindle poles. Upon CCl2 stimulation translocates from the cytoplasm to the membrane and colocalizes with CCR2 at the front of migrating cells. {ECO:0000250|UniProtKB:Q9BW27}.
DR  UNIPROT: Q3ZC98;
DR  UNIPROT: A7E3X3;
DR  Pfam: PF07575;
DE  Function: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade. Involved in nephrogenesis. {ECO:0000250|UniProtKB:Q9BW27}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005819;
GO  GO:0017056;
GO  GO:0030032;
GO  GO:0048246;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0045893;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEFDGEPTVTWIPGVNSQKKQMCFDWGPGEMLVCETSFNKKEKSEMVAGCPFIHIIRKDIDVYSKILRKLFNESHGIFV
SQ  GLQRIEEELTGKSRKAQLVRVSKNYRSVIRACMEEMHQFAVADKDSAIGRQFSSQVSILSAVELIWNLCEILFIEVAPAG
SQ  PLLLYLLDWVRLHVCEVDSLSADVLGSENPSKHESFWNLVTTLVLQGRLDEARQMLSKEADSNPTSAGMCRVLGDLMRTM
SQ  PILSPGNTQTLTELELRWQHWHEECERHLQDGTFASNPHLESLCKVLLGDDAALLEHKELLSNWYHFLVTRLLYSQPTVK
SQ  PMDLHLYAQSSLDLFLGGESSPEPLDNILMAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCKLLQSHNLYFGSNMRE
SQ  FLLLEYASGLFAHHSLWQLGVDYCDHCPELGRVSLELHIERIPLTTEQKALKVLRVCEQRQMTEQVRSICKVLAMKAVRN
SQ  NRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGPAMMLSDRLTFLGKYREFHRLYGEKCFVDAASLL
SQ  LSLMTSQIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELLRCLEDLTSGRPLCGEPDAQQLQDDDIETTKVEILRLALA
SQ  RNLARSIIKEGSLEGS
//
ID  G0SDQ4;
PN  Nucleoporin NUP85;
GN  NUP85;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P46673}. Nucleus membrane {ECO:0000250|UniProtKB:P46673}; Peripheral membrane protein {ECO:0000250|UniProtKB:P46673}; Cytoplasmic side {ECO:0000250|UniProtKB:P46673}. Nucleus membrane {ECO:0000250|UniProtKB:P46673}; Peripheral membrane protein {ECO:0000250|UniProtKB:P46673}; Nucleoplasmic side {ECO:0000250|UniProtKB:P46673}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P46673}.
DR  UNIPROT: G0SDQ4;
DR  UNIPROT: G0ZGU8;
DR  Pfam: PF07575;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP85 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000250|UniProtKB:P46673}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S0E7; IntAct: EBI-16069336; Score: 0.62
DE  Interaction: G0S2G1; IntAct: EBI-16069488; Score: 0.62
DE  Interaction: G0S2X1; IntAct: EBI-16069488; Score: 0.35
DE  Interaction: G0S9A7; IntAct: EBI-16069651; Score: 0.35
DE  Interaction: G0SA60; IntAct: EBI-16069846; Score: 0.35
DE  Interaction: G0SAK3; IntAct: EBI-16069488; Score: 0.52
DE  Interaction: G0SER9; IntAct: EBI-16069651; Score: 0.35
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P46673};
SQ  MFRVPDDSILSSSPAPSTPDKSRRAGSSNLFRDSTASSAASTTPAGTPPVKFLGSSIMRPSDKNASSSVDDDQPAVGLFT
SQ  GIGGGVGVGMGAGTGATAAAKAAKKNLFAAVSGERRRNVPLGRSGRGHDSRQPSRLRKSIGVDDLEDEEEEEEKKKKPQL
SQ  LKPKGKVQEKKKDEPVRGLFTGTSLAPPPLSKAAAAATTTTTTGPTKSFGLTYEEFGESEEEDSGLTGGQDAEGELDDSM
SQ  WLERSPERPAIGDESDLLLMATPAATERVRREAEDIFRATAMGAGATTRRHEYRYASLAKDVYTQLGTAPLVEPPQLILS
SQ  TEALLEQLYDEGVGTHDDDARLDETLAAVAVQLINLWQDHVDAIAQPEEDGHVADIGPGPRASPFEKAYWLATLALQLHH
SQ  TRALDGGVEPLPATLFQWLNDRHDMYAGQVEEILRYRPSPACHSLFWQAVFMSLLRGRVKDATQLLRRAGWEHVRRGGQQ
SQ  RGEYAYSDRALENVLRVVDETVSVLESCPGYDGNWEIWSSEWTLFRVRAQGALEHLRRFAEGKDTSFGDSLFGSSTGSNR
SQ  GYTGYRDHTLAGLARRAESQVPWDVYESLNVVFDIVLGQQASILEAAQDWLEATIGLFGWWDERNNNNNNNNNNNNNNNG
SQ  YQKPGRTQALVLHSSPAHHINNDSESYLDRLARAFHAAVASDFHFNSQNPVEIGMACIFEDNIKGVIGLLRSWSLPIAAA
SQ  VAQVASLGRWLPPHRPKGMYALEDLDMDDLEVLGVDPGAPDEVDGVKDSTLVQYAQALVEYEGLETVRDRAGVYREGWEL
SQ  AISVLGRMDSPERSEEMVRDIVEHLVQGLTVDSTETVDRLWTMLNELSMITYAEEMTETFGDILARESHRYGEAMWYYAL
SQ  AHRPNKVREVMNLLISYSLIQSTAFPPAADLDDYLHRLLSDRKHTLEQYAKQDMEAAELLGKMLSGYAALRQFYDIRDNV
SQ  DATSISPVSRRQQAAAALISVIASSDDNIRGGLVDQTRDGIVSEDFLLALLGEALVFVSNPDNTFVHHGHAAVPILSQDQ
SQ  IDVLLKAVEDLTAVSERVYNVCDEFLQLVLASAPGGALKGSKPADLLKKGQDGQQMVLAGSSLIASQLQKSLLGGSGSAL
SQ  GKVPVKRGWDWREGMPAKMKGEDVIRRLRLGLAKDLARLWLAEADALVW
//
ID  Q6DBY0;
PN  Nuclear pore complex protein Nup85;
GN  nup85;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}.
DR  UNIPROT: Q6DBY0;
DR  Pfam: PF07575;
DE  Function: Component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (By similarity). Involved in nephrogenesis (By similarity). {ECO:0000250|UniProtKB:Q6DK84, ECO:0000250|UniProtKB:Q9BW27}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0045893;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELDVEPSTTLVPAAGVLQKHLGFEWGPGDLLVYETNYKLRGSSSAGSPLVHVVRKDEDICSPILRKLFNESHLIFMGL
SQ  QKIKEDAPSKNKKTQFVSISRNYRSVIRACMEELQQNAVTAQDGSLASQYGDQVSILLAIELIWNLCEVLFIEAAPAGSL
SQ  LLHLLNWVRLHKSDVDTRAREVLQSENPTQHPAYWDVVTSLVLQGRMDEARQILSKQASLRMESSSVFKRMDTLLQTMPI
SQ  FNPAGAQTLTEFDVKWRHWHEECDRCLQDHTFASSAELETLCKILLGDEDVILEQKDLMSTWYHFLVSRLLFTHPTIKPP
SQ  DLHYYAQSSMNMFLGPRATPEPLDIILLSAFEFDLHQVIKDCSIALNNWWFVAHLTDLLDHCKLLQSHNLHFGSNLREFL
SQ  VLEYASGLFTHHSLWQLAVDYLDHCPEFGRVYLELQIERVPLDTERKANKVLRICEDRQMSEQVRSICKIMAKRALRNNR
SQ  LGSALSWSIRAKDAALATLISERFLQDYSNKGSFTDLDVLDNLGPAMLLSDRLTFLGKYREFHRLYGENRFSDAAKLLLS
SQ  LMMAKIAPRSLWMTLLTDALPLLEQEEVIFTVDQTYELMSCLEELNSGTKDSNQMEQEEDLESTKTELLRVALARNLATA
SQ  IVKEGTIET
//
ID  Q54NA0;
PN  Nuclear pore complex protein nup85;
GN  nup85;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P46673}. Nucleus membrane {ECO:0000250}.
DR  UNIPROT: Q54NA0;
DR  Pfam: PF07575;
DE  Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250|UniProtKB:P46673}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0045893;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFSLNPQSNGNSNNLFGNVTLGNFSNNSNNLFGGSSTTSTNTNNSNNLFGGSSTTNSNNLFGSGGSSTTNNNNFNSNFNN
SQ  NNIKNENKIKNGKKFYNFRWSPTGEILLYNTLNNFDNHNFDQKNGGSDTIRYEMNTTLSTIKKFYNDLYTNFETMQRIAG
SQ  LSNQVIPDDRVREISHHSRTYLSVILAAINQMSKSQKTGSYIDDEDSCMNCDPLDNDLIKIQTPRVLEYFKQYPNKTLIF
SQ  FCGSIDSIYPYLCSKLSMETKSKCILIARESNVPNSKRLDLIRTISNQGELKILNKDEYSNRYQIANENYGELDDVLTLE
SQ  IDDTYLAYEREIDNLICMSTMWRVANLFYFSVSSSSNSVSPTQLLDCIELERKELLNSIEQQGTQDPMDSEYYNQIARLL
SQ  VCGCIDQVIQQLNILSRAPRSASQIKSTSRKSPINLLIDILSSIPLKKKSINGGGGAPLYPNEHLIQWNKWHQETQKILS
SQ  QYIESGSSSTNQVDENLLPIVKILLGDQQTIMSTCNSFLQLVVSNILFVEYTTSTTQLRQLFTQCYQTIQAPTTVDKIFL
SQ  SFATKDLDITLKKIFKHSPAWLAVHLSDLLYHHPYVMRKLPNSESQLTNIREYLLSDFGQSLASDSSLLSIGCNYLKYVK
SQ  NGGLEMIDQFISRQPIHFEKNAIKMLDKWATSVETKNSIYKMLSLQDFKRKRYAASLNWLMLANDNSHITLLSNYLLENQ
SQ  LNSEFLNDLQSLLEKNDEIDCNINNNNNNNNNNNSNNRISGNNNNNMIIDENKFEITNNSELIFLIRYRELISLWKERSF
SQ  KEYSSSLCLMFKDRVIPKRFWLRLLIDCVPLLESLKNLYFTYQDTLLLQSCLEEIIQSHLFDQYSFNISNQDIQILRSAL
SQ  ARNLAKSIIS
//
ID  Q9BW27;
PN  Nuclear pore complex protein Nup85;
GN  NUP85;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12196509, ECO:0000269|PubMed:12718872}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12718872, ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:16807356}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16807356}. Cytoplasm {ECO:0000269|PubMed:15995708}. Nucleus membrane {ECO:0000269|PubMed:12196509}. Note=During mitosis, localizes to the kinetochores and spindle poles (PubMed:12718872, PubMed:16807356). Upon CCl2 stimulation translocates from the cytoplasm to the membrane and colocalizes with CCR2 at the front of migrating cells (PubMed:15995708). {ECO:0000269|PubMed:12718872, ECO:0000269|PubMed:15995708, ECO:0000269|PubMed:16807356}.
DR  UNIPROT: Q9BW27;
DR  UNIPROT: B4DMQ3;
DR  UNIPROT: B4DPW1;
DR  UNIPROT: Q8NDI4;
DR  UNIPROT: Q9H9U1;
DR  PDB: 5A9Q;
DR  PDB: 7PEQ;
DR  Pfam: PF07575;
DR  OMIM: 170285;
DR  OMIM: 618176;
DR  DisGeNET: 79902;
DE  Function: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (PubMed:12718872). As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus (PubMed:12718872). The Nup107-160 complex seems to be required for spindle assembly during mitosis (PubMed:16807356). NUP85 is required for membrane clustering of CCL2-activated CCR2 (PubMed:15995708). Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3- kinase-Rac-lammellipodium protrusion cascade (PubMed:15995708). Involved in nephrogenesis (PubMed:30179222). {ECO:0000269|PubMed:12718872, ECO:0000269|PubMed:15995708, ECO:0000269|PubMed:16807356, ECO:0000269|PubMed:30179222}.
DE  Disease: Nephrotic syndrome 17 (NPHS17) [MIM:618176]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form that progresses to end-stage renal failure. NPHS17 is an autosomal recessive, steroid-resistant progressive form with onset in the first decade of life. {ECO:0000269|PubMed:30179222}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-9032422; Score: 0.40
DE  Interaction: P55735; IntAct: EBI-9032422; Score: 0.56
DE  Interaction: P57740; IntAct: EBI-9032422; Score: 0.56
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q12769; IntAct: EBI-9032422; Score: 0.59
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q8NFH3; IntAct: EBI-9032422; Score: 0.76
DE  Interaction: Q8NFH4; IntAct: EBI-9032422; Score: 0.56
DE  Interaction: Q8WUM0; IntAct: EBI-9032422; Score: 0.57
DE  Interaction: Q8WYP5; IntAct: EBI-9050503; Score: 0.57
DE  Interaction: Q96EE3; IntAct: EBI-9032422; Score: 0.70
DE  Interaction: P26641; IntAct: EBI-732758; Score: 0.00
DE  Interaction: Q9P275; IntAct: EBI-2512446; Score: 0.40
DE  Interaction: Q70CQ1; IntAct: EBI-2512828; Score: 0.40
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: P41597; IntAct: EBI-9822344; Score: 0.56
DE  Interaction: Q9C009; IntAct: EBI-11319301; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: Q7L5D6; IntAct: EBI-24515714; Score: 0.56
DE  Interaction: P32970; IntAct: EBI-21512742; Score: 0.35
DE  Interaction: Q8N490; IntAct: EBI-21596986; Score: 0.35
DE  Interaction: A8K8V0; IntAct: EBI-21612043; Score: 0.35
DE  Interaction: Q8NBZ7; IntAct: EBI-21638319; Score: 0.35
DE  Interaction: Q6EMK4; IntAct: EBI-21651359; Score: 0.35
DE  Interaction: Q6UWR7; IntAct: EBI-21723303; Score: 0.35
DE  Interaction: Q9UBP0; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q5T5S1; IntAct: EBI-21816407; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: Q15628; IntAct: EBI-20737473; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
DE  Interaction: Q9Y275; IntAct: EBI-21266480; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC5; IntAct: EBI-26495256; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005819;
GO  GO:0017056;
GO  GO:0030032;
GO  GO:0048246;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0006913;
GO  GO:0045893;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELDGEPTVTLIPGVNSKKNQMYFDWGPGEMLVCETSFNKKEKSEMVPSCPFIYIIRKDVDVYSQILRKLFNESHGIFL
SQ  GLQRIDEELTGKSRKSQLVRVSKNYRSVIRACMEEMHQVAIAAKDPANGRQFSSQVSILSAMELIWNLCEILFIEVAPAG
SQ  PLLLHLLDWVRLHVCEVDSLSADVLGSENPSKHDSFWNLVTILVLQGRLDEARQMLSKEADASPASAGICRIMGDLMRTM
SQ  PILSPGNTQTLTELELKWQHWHEECERYLQDSTFATSPHLESLLKIMLGDEAALLEQKELLSNWYHFLVTRLLYSNPTVK
SQ  PIDLHYYAQSSLDLFLGGESSPEPLDNILLAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCKLLQSHNLYFGSNMRE
SQ  FLLLEYASGLFAHPSLWQLGVDYFDYCPELGRVSLELHIERIPLNTEQKALKVLRICEQRQMTEQVRSICKILAMKAVRN
SQ  NRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGPAMMLSDRLTFLGKYREFHRMYGEKRFADAASLL
SQ  LSLMTSRIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELMRCLEDLTSRRPVHGESDTEQLQDDDIETTKVEMLRLSLA
SQ  RNLARAIIREGSLEGS
//
ID  Q8R480;
PN  Nuclear pore complex protein Nup85;
GN  Nup85;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. Note=During mitosis, localizes to the kinetochores and spindle poles. Upon CCl2 stimulation translocates from the cytoplasm to the membrane and colocalizes with CCR2 at the front of migrating cells. {ECO:0000250|UniProtKB:Q9BW27}.
DR  UNIPROT: Q8R480;
DR  UNIPROT: A2A9W9;
DR  UNIPROT: A2A9X0;
DR  UNIPROT: Q9CYI9;
DR  Pfam: PF07575;
DE  Function: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade. Involved in nephrogenesis. {ECO:0000250|UniProtKB:Q9BW27}.
DE  Reference Proteome: Yes;
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0031727;
GO  GO:0017056;
GO  GO:0006935;
GO  GO:0019221;
GO  GO:0030032;
GO  GO:0048246;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0006913;
GO  GO:0045893;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELDCEPAVTWIPGVNSKKKQMCFDWGPGEMLLCETSFNQTGKSEKVPSCPFIYIIRKDVDVYSQILRKLFNESHGIFV
SQ  GLQKIEEELSGKSRKAQLVRVSKNYRSVIRACMEEMHQVAIAAKDPASGRQFSSQVSILSAMELIWNLCEILFIEVAPAG
SQ  PLLLHLLDWVRLHVCEVDSLSADVLGGDNPSKHENFWDLVTVLVLQGRLDEARQMLAKEADANPSCAGMCRVLGDLMRTM
SQ  PILSPGNTQTLTELELKWQHWREECERHLQDNTFAANPRLESLCKIMLGDEAALLEQKELLSNWYHFLVTRLLYSNPTVK
SQ  PIDLHFYAQSSLDMFLGGESSPEPLDNILMAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCRLLQSHNLYFGSNMRE
SQ  FLLLEYASGLFAHHSLWQLGVDYFDYCPELGRVSLELHIERIPLNTEQKALKVLRICEQRQMTEQVKSICKILAMKAVRN
SQ  NRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGSAMMLSDRLTFLGKYREFHRLYGEKRFGDAASLL
SQ  LSLMTSQIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELMRCLEDLASGRPECGEPDAQRLQDDDIETTKVEMLRLALA
SQ  RNLARAIIREGSLEGS
//
ID  Q4QQS8;
PN  Nuclear pore complex protein Nup85;
GN  Nup85;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW27}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}. Note=During mitosis, localizes to the kinetochores and spindle poles. Upon CCl2 stimulation translocates from the cytoplasm to the membrane and colocalizes with CCR2 at the front of migrating cells. {ECO:0000250|UniProtKB:Q9BW27}.
DR  UNIPROT: Q4QQS8;
DR  Pfam: PF07575;
DE  Function: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade. Involved in nephrogenesis. {ECO:0000250|UniProtKB:Q9BW27}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:0017056;
GO  GO:0006935;
GO  GO:0030032;
GO  GO:0048246;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0045893;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELDCEPAVTWIPGVNSKKKQMCFDWGPGEMLLCETSFNKTDKSEKVPSCPFIYIIRKDVDVYSQILRKLFNESHGIFV
SQ  GLQRLEEELSGKSRKAQLVRVSKNYRSVIRACMEEMHQVAIAAKDPASGRQFSSQVSILSAMELIWNLCEILFIEVAPAG
SQ  PLLLHLLDWVRLHVCEVDSLSADVLGSDHPSKHESFWNLVTVLVLQGRLDEARQMLSKEADASPSSAGMCRVLGDLMRTM
SQ  PILSPGNTQTLTELELKWQHWREECERHLQDNTFAANPHLESLCKIMLGDEATLLEQKELMSNWYHFLVTRLLYSNPTVK
SQ  PTDLHLYAQSSLDMFLGGESSPEPLDNILMAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCRLLQSHNLYFGSNMRE
SQ  FLLLEYASGLFAHHSLWQLGVDYFDYCPELGRVSLELHIERIPLNTEQKALKVLRICEQRQMTEQVGSICKILAMKAVRN
SQ  NRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGPAMMLSDRLTFLGKYREFHRLYGEKRFGDAASLL
SQ  LSLMTSQIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELMRCLEDLASRRPECGEPDAQRLQDDDIETTKVEMLRLALA
SQ  RNLARAIIREGSLEGS
//
ID  Q9UUE5;
PN  Nucleoporin nup85;
GN  nup85;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:15226438}. Note=Localizes to the nuclear envelope and spindle pole body. {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9UUE5;
DR  Pfam: PF07575;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
DE  Interaction: Q10099; IntAct: EBI-1563788; Score: 0.35
DE  Interaction: Q9UTK4; IntAct: EBI-1563817; Score: 0.40
DE  Interaction: O43044; IntAct: EBI-1563722; Score: 0.40
GO  GO:0005829;
GO  GO:0000791;
GO  GO:0000792;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0140602;
GO  GO:0005634;
GO  GO:0005816;
GO  GO:1990188;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:0006407;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESSDEVDLPVYHLQNAPIENGKLNDWRSKGRTVAFKLHPFLRKGLAYINNKEFDENTLKSDKFEEVESLVYEFSTPSTL
SQ  IEPNYLLTAWHELWEELQDTYMTPILDSEANLLLLTQFYGKISSLFRSKIIQVLEELQSRINEGEKDCQPVLDSLWEVES
SQ  AWRCAEAIYFPPSSPYTLSTGILDWVNAYDPQPIADDGLEIMAYRIPYQHPEFWPYVNKTAIRGLFEQTISCLEMSGLTK
SQ  EWPVLKETVDELIDILRYSPCTHQKRIRSVSDFERRWKLWRSRLANLRHVVKKHRDIDSEVLDDFVVLLDILNGNKEVIM
SQ  LSCAHWQEYFSALAFLYGPLDCKNPEDISLLYQLATGEDSKFYVNGTIEYEQICVNLCSNEPLNAIKHAYLLDLGLAVHL
SQ  ADLLSKSGHLRDYITEEYPITLREHLILEYGQCVLESRNLWQTSFAYWKCVADSGYQRIKACIPYVPLSDVDAKETALQL
SQ  CKQLKLRDEAQLVLTHWADELIARNHYGEALIALDNAANYSALNRVTWELFDICIAEKKSFSPDKDELLYELFSSPKACT
SQ  PTLASIISPAATIHQYFFYLQHKKELNASELLVGLLTMVDFPSSRFPKLLELLHEFLNNPLQSNSTDFKLSLVNVYDCIA
SQ  VLQDQQSTVKDQQLLLSIHERLSSAISWYFLHLKK
//
ID  Q68FJ0;
PN  Nuclear pore complex protein Nup85;
GN  nup85;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}.
DR  UNIPROT: Q68FJ0;
DR  PDB: 6LK8;
DR  PDB: 7VCI;
DR  PDB: 7VOP;
DR  PDB: 7WB4;
DR  Pfam: PF07575;
DE  Function: Component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (By similarity). Involved in nephrogenesis (By similarity). {ECO:0000250|UniProtKB:Q6DK84, ECO:0000250|UniProtKB:Q9BW27}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0051028;
GO  GO:0072006;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELDVDPAETPIPGLGQQNRHIGFSWGPGDLLLYETLYQKQGNSETAARCPFMYLVRSDEDIYSPVLRKLFNESHSIFV
SQ  GLQKSAEEASGKSRKAQLVQVSRNYRSVLRACMEEMHTLSESTRETAQKYISQISILSAMELSWNLCEILFIESAPAGPL
SQ  LILLLEWVRLHVCEVDNIVQDVLRSEKPTEHEKFWDGVTGYVLQGRMNEARQLLAKEASTSASARSMCRVLDDLLKKMPM
SQ  LHTGGTQTLTEFELKWQHWREECERHLQNGTFSSNVHMEAVCRVLLGDEEVLLEKRDLMTTWYHFLVSRLLFKHPTVKPT
SQ  ELHFYAQSSLDMFLAGDSCPEPLDNILLAAFEFDIHQVIKEFSIVSSNWWFVAHLTDLLDHCQLFQAHNLYFGANMREFL
SQ  LLDYASGLFSHHSLWQLGVDYFDYCPNLGREYLKLHMERIPLSTEKKALKALRICEQRQMTEQVRSICKTMAMQSLCNRR
SQ  LGSALSWSIRAKDAAFATLISDRFLKEYCERGNFTDLDLIDNLGSAMLLSDRLTFLGKYREFHRMYSQEQFSEAASLLLS
SQ  LMTARIAPCSFWLTLLLDALPLLEQKQVIFSAEQTYELMRCLEDRMAAKLESTSPDEIQKQDSSIDNTKVEMLRLALARN
SQ  LARAIVTEGALQE
//
ID  Q6DK84;
PN  Nuclear pore complex protein Nup85;
GN  nup85;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}.
DR  UNIPROT: Q6DK84;
DR  Pfam: PF07575;
DE  Function: Component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (By similarity). Involved in nephrogenesis (PubMed:30179222). {ECO:0000250|UniProtKB:Q9BW27, ECO:0000269|PubMed:30179222}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0072006;
GO  GO:0045893;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEELDVDPAETPIPGLGQQNRHIGFSWGPGDLLLYETLYQKQGSETAARCPFMYLVRSDEDIYSPVLRKLFNESHSIFVG
SQ  LQKSAEENAGKSRKAQLVQVSRNYRSVLRACMEEMHALSESTREPSQNTKYISQISILSAMELSWNLCEILFIESAPAGP
SQ  LLILLLDWVRLHVCEVDNIVQDVLRSERPTEHEKFWDGVTGYVLQGRMNEARQLLAKEASSSVSARSMCRVLDDLLKKMP
SQ  MLNTAGTQTLTEFELKWQHWREECERHLQNGTFSSNPHMEVVCRVLVGDEEVILEKRDLMTTWYHFLVSRLLFKHPTVKP
SQ  TELHFYAQSSLDMFLAGNSSPEPLDNILLAAFEFDIHQVIKEFSIVSSNWWFVAHLTDLLDHCQLFQAHNLYFGANMREF
SQ  LLLDYASGLFSHHSLWQLGVDYFDYCPNLGHVYLELHMERVPLNTEKKALKALRICEKRQMTEQVRSICKTMAMQSLCNG
SQ  RLGSALSWSIRAKDAAFATLISDRFLKEYSERGNFTDLDLIDNLGSAMLLSDRLTFLGKYREFHRMYSQEQFSEAASLLL
SQ  SLMTARIAPCSFWLTLLLDALPLLEQKQVIFSAEQTYELMRCLEDRMAAKLDSTSPDEIQKQDSVDSTKIEMLRLALARN
SQ  LARAIVTEGALQE
//
ID  P46673;
PN  Nucleoporin NUP85;
GN  NUP85;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
DR  UNIPROT: P46673;
DR  UNIPROT: D6VWL3;
DR  PDB: 3EWE;
DR  PDB: 3F3F;
DR  PDB: 3F3G;
DR  PDB: 3F3P;
DR  PDB: 4XMM;
DR  PDB: 4XMN;
DR  PDB: 6X08;
DR  PDB: 7N84;
DR  PDB: 7N9F;
DR  Pfam: PF07575;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP85 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:8816998, ECO:0000269|PubMed:9774696}.
DE  Reference Proteome: Yes;
DE  Interaction: P32499; IntAct: EBI-1270055; Score: 0.00
DE  Interaction: P35729; IntAct: EBI-4325415; Score: 0.95
DE  Interaction: P36161; IntAct: EBI-295762; Score: 0.55
DE  Interaction: P40368; IntAct: EBI-11889278; Score: 0.55
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P51862; IntAct: EBI-788341; Score: 0.35
DE  Interaction: P49687; IntAct: EBI-797641; Score: 0.92
DE  Interaction: P52891; IntAct: EBI-800196; Score: 0.73
DE  Interaction: Q04491; IntAct: EBI-812133; Score: 0.53
DE  Interaction: P32582; IntAct: EBI-815440; Score: 0.27
DE  Interaction: Q07622; IntAct: EBI-817474; Score: 0.27
DE  Interaction: Q99257; IntAct: EBI-8435423; Score: 0.44
DE  Interaction: Q02630; IntAct: EBI-11889546; Score: 0.59
DE  Interaction: Q02629; IntAct: EBI-11889530; Score: 0.59
DE  Interaction: P53011; IntAct: EBI-1580856; Score: 0.92
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q03790; IntAct: EBI-4325410; Score: 0.37
DE  Interaction: Q05166; IntAct: EBI-4325425; Score: 0.37
DE  Interaction: Q8WUM0; IntAct: EBI-11890201; Score: 0.51
DE  Interaction: Q03648; IntAct: EBI-16274990; Score: 0.35
DE  Interaction: Q08224; IntAct: EBI-16274990; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-16274990; Score: 0.35
DE  Interaction: P16622; IntAct: EBI-16274990; Score: 0.35
DE  Interaction: P21560; IntAct: EBI-16274990; Score: 0.35
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0017056;
GO  GO:0006406;
GO  GO:0051664;
GO  GO:0006913;
GO  GO:0045893;
GO  GO:0006606;
GO  GO:0000055;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MTIDDSNRLLMDVDQFDFLDDGTAQLSNNKTDEEEQLYKRDPVSGAILVPMTVNDQPIEKNGDKMPLKFKLGPLSYQNMA
SQ  FITAKDKYKLYPVRIPRLDTSKEFSAYVSGLFEIYRDLGDDRVFNVPTIGVVNSNFAKEHNATVNLAMEAILNELEVFIG
SQ  RVKDQDGRVNRFYELEESLTVLNCLRTMYFILDGQDVEENRSEFIESLLNWINRSDGEPDEEYIEQVFSVKDSTAGKKVF
SQ  ETQYFWKLLNQLVLRGLLSQAIGCIERSDLLPYLSDTCAVSFDAVSDSIELLKQYPKDSSSTFREWKNLVLKLSQAFGSS
SQ  ATDISGELRDYIEDFLLVIGGNQRKILQYSRTWYESFCGFLLYYIPSLELSAEYLQMSLEANVVDITNDWEQPCVDIISG
SQ  KIHSILPVMESLDSCTAAFTAMICEAKGLIENIFEGEKNSDDYSNEDNEMLEDLFSYRNGMASYMLNSFAFELCSLGDKE
SQ  LWPVAIGLIALSATGTRSAKKMVIAELLPHYPFVTNDDIEWMLSICVEWRLPEIAKEIYTTLGNQMLSAHNIIESIANFS
SQ  RAGKYELVKSYSWLLFEASCMEGQKLDDPVLNAIVSKNSPAEDDVIIPQDILDCVVTNSMRQTLAPYAVLSQFYELRDRE
SQ  DWGQALRLLLLLIEFPYLPKHYLVLLVAKFLYPIFLLDDKKLMDEDSVATVIEVIETKWDDADEKSSNLYETIIEADKSL
SQ  PSSMATLLKNLRKKLNFKLCQAFM
//
ID  Q9FFK6;
PN  Nuclear pore complex protein NUP88;
GN  NUP88;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:19700630, ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:19700630, ECO:0000305|PubMed:21189294}.
DR  UNIPROT: Q9FFK6;
DR  UNIPROT: Q0WPM6;
DR  Pfam: PF10168;
DE  Function: Involved in the regulation of exportin-mediated nuclear protein export. Required for resistance mediated by multiple R proteins and for the appropriate nuclear accumulation of SNC1 and of the downstream defense signaling components EDS1 and NPR1. Not involved in salt tolerance, ethylene and auxin responses, but required for systemic acquired resistance. {ECO:0000269|PubMed:19700630, ECO:0000269|PubMed:21327081}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0045087;
GO  GO:0006406;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0009627;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKFNFNETEDAPDSRRSPTPKEPVRWVPLQSHPVFASLPSSQDEPAVSQLFPRNFMAWDGDSRVYYWDSRRYLLHRLSLR
SQ  LGEPEPSSVLAAVPSKVMQPDLQVTFSVSKISINKSGSAVLLAGSDGICVMYLFGRASVIEDNVICRVVSIGSEIYTSSD
SQ  SAITLLQASWHPDSDTHLGILSSDAVFRLFDLSSDTELPEQEYYLQPGEPGRSRTASSIYPADFSFGGDHLWDRFTVFIL
SQ  FTDGSIYILCPVVPFGSVYKWESVMEIYNDANMYGVKSSNSLAVSNSSLAIEWLEATFPDLTEQGTRGENILVVKAQPYA
SQ  LLDASLALQGPLYKASSGDGDEDFAVREAECKGRAVSLLYNLVSKDSILVTAWSAGQLQVDALVDEIQPVWISGNSSRLR
SQ  MNSHNKIQGVAMICESNISELPVATSNLPLDHTVWLGHPPPLLRLAMVDLALPKMREGGSLVTLFADSLLPERIYSLHDG
SQ  GIDSTVLHSLPFTSQASGKDEALKTPSVHTVLSTCQEESAVSPLLGFVPLSDSFGYSWIVAVLSSGECIVAEMKTWDLLL
SQ  PIHVSTDKTVSSSAIEKKEQENSCIISKELLAGPKIRIAPHALPNQRSTPANSVEGRSILLDYVKLFHENYIEYAHKVHF
SQ  ELQHHAPNLKRIIDDQHQRLAEANEKISKVEKNQSFLEKRIDKAIERHDSLEQCLQRLRSLPGTHKKPLTRAELDFKSEL
SQ  DQYAGVEVDALQSSIETLRARVKKSTQKSHKGTVVAASQKKQYSKKNLIQDTQMSQLQSTLAKLSLMNSDNSKKVKIVES
SQ  ALKSQESSFM
//
ID  A2CEI4;
PN  Nucleoporin 88;
GN  nup88;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q99567}.
DR  UNIPROT: A2CEI4;
DR  UNIPROT: A0A2R8QUY6;
DR  UNIPROT: Q501Y6;
DR  Pfam: PF10168;
DE  Function: Component of the nuclear pore complex. {ECO:0000250|UniProtKB:Q99567}.
DE  Reference Proteome: Yes;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASLAGDRWREALKNHDIFNNLQERLHLEPQGTSKRIAKNLTFCLNGDLFIWDSVESVFYTTNLRQLNSDGEPDTSRYQT
SQ  LLCINPPLFEVCQVLVSPSQYHVALIGQRGATVLELPQRWGKKSEFEGGRIQINCKTIPVAERFFTSSASVTLRQAVWYP
SQ  SETEEPHLVLLTSDNTIRFYNLKEPQSPARVLSVSQMDDDSSVHTRSRSYAASLGETAVAFDFGPLADSPHLSSLRMKAE
SQ  LVVYPLYILYGNGETFLNYISLSHSVGSLGKPMGPLPMYPAAEDNYGYDACAVLCLPCVPNILVIATESGMLYHCVVLEA
SQ  EEEEDGGAVERWSRGSETAPSLYVFECVELELTLKLPAGEEEEITESDFTCPIRLHRDPLCQHRYHCTHEAGVHSVGLTW
SQ  FKKLHKFLESDEEDKDSLQELAAEQRCIVEHILCTRPLANSLPAPVRGFWIVSDLSLGATMICITSTYECLLLPLLSSIR
SQ  PASPPLLCSHPGAGSDSSPLRGLAEDSFEQHIRNILARSSTNPLMLRSGDKDSSPPPSECLQLLSRATQVFREEYILKLG
SQ  LAHEEMQRRVKLLSGQKNKQLEDLALCREDRKSLTEAAERLADKYEDAKYRQEAIMNRVKRVLGSLRSQLPVLSDSEKDM
SQ  RKELQTINDQLRHLDNGIKQVNMKKDYQKKQMNAGASPAHSSLTLNAHQRKCLQGVLKEQGEHIAGMMKQIKDIKNHFSF
//
ID  Q9GYU8;
PN  Nuclear pore complex protein Nup88;
GN  mbo;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10921908}. Nucleus membrane {ECO:0000269|PubMed:10921908, ECO:0000269|PubMed:17032737}; Peripheral membrane protein {ECO:0000269|PubMed:10921908}; Cytoplasmic side {ECO:0000269|PubMed:10921908}. Chromosome {ECO:0000269|PubMed:20144761}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20144761}. Note=Is recruited to non-active chromatin sites (PubMed:20144761). Localization to the nuclear rim is promoted by Nup214 (PubMed:17032737). {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:20144761}.
DR  UNIPROT: Q9GYU8;
DR  UNIPROT: Q9VG41;
DR  Pfam: PF10168;
DE  Function: Essential component of nuclear pore complex (PubMed:10921908, PubMed:14638854, PubMed:17032737). Required for the anchoring of Nup214 and emb on the nuclear envelope and thereby attenuates nuclear export signal (NES)-mediated nuclear export (PubMed:14638854). Together with Nup214, required for the nuclear import of the Rel family transcription factors dorsal (dl) and Dorsal-related immunity factor (Dif) and the activation of an immune response (PubMed:10921908, PubMed:17032737). {ECO:0000269|PubMed:10921908, ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7JXF5; IntAct: EBI-280213; Score: 0.00
DE  Interaction: A1Z6E8; IntAct: EBI-202832; Score: 0.00
DE  Interaction: Q7K0A0; IntAct: EBI-225767; Score: 0.00
DE  Interaction: Q9VUG5; IntAct: EBI-230580; Score: 0.00
DE  Interaction: Q9VZ87; IntAct: EBI-232035; Score: 0.00
DE  Interaction: Q9VK23; IntAct: EBI-243781; Score: 0.00
DE  Interaction: Q9W4L6; IntAct: EBI-244337; Score: 0.00
DE  Interaction: Q9VWQ6; IntAct: EBI-253899; Score: 0.00
DE  Interaction: Q9VND7; IntAct: EBI-259900; Score: 0.00
DE  Interaction: Q9VNE1; IntAct: EBI-260005; Score: 0.00
DE  Interaction: Q86B91; IntAct: EBI-263437; Score: 0.00
DE  Interaction: Q9VF13; IntAct: EBI-263482; Score: 0.00
DE  Interaction: Q9VVK7; IntAct: EBI-265915; Score: 0.00
DE  Interaction: Q9VSB2; IntAct: EBI-266411; Score: 0.00
DE  Interaction: Q9VFF6; IntAct: EBI-269996; Score: 0.00
DE  Interaction: Q9XYW6; IntAct: EBI-277061; Score: 0.00
DE  Interaction: Q8INY6; IntAct: EBI-278797; Score: 0.00
DE  Interaction: Q9Y091; IntAct: EBI-280296; Score: 0.00
DE  Interaction: A1ZAW3; IntAct: EBI-280793; Score: 0.00
DE  Interaction: Q9VC66; IntAct: EBI-281109; Score: 0.00
DE  Interaction: Q9VT69; IntAct: EBI-281332; Score: 0.00
DE  Interaction: Q9VVT5; IntAct: EBI-281639; Score: 0.00
DE  Interaction: Q9VTP5; IntAct: EBI-281643; Score: 0.00
DE  Interaction: Q9VS62; IntAct: EBI-281647; Score: 0.00
DE  Interaction: Q9VS38; IntAct: EBI-281651; Score: 0.00
DE  Interaction: Q9VVB4; IntAct: EBI-281655; Score: 0.00
DE  Interaction: Q9W1A4; IntAct: EBI-464017; Score: 0.40
DE  Interaction: P98149; IntAct: EBI-872370; Score: 0.27
DE  Interaction: P15330; IntAct: EBI-872434; Score: 0.27
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
GO  GO:0000785;
GO  GO:0005635;
GO  GO:0031981;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0003682;
GO  GO:0017056;
GO  GO:0019730;
GO  GO:0006406;
GO  GO:0046826;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10921908};
SQ  MSLTDVLELNKTELFAKIRNGLPVVQRTQNLLDCKDDLLFAWHAKDSCLLVRNWRSSLAAKVNIQFQTLIPSSLVSLEVD
SQ  RVLASNEGSLVALSGPRGVVIMELPRRWGPDGYYKDGKPVITCRTFGLDTQLFLKNPHLEVRQVRWHPHSVSDSTLLVLL
SQ  NNNTIRVYNHSKLRHVWQVGPPVLRSGANNSLCDFGELAVDFDIAPAAKPRVTEPETAGNNETTLDKSNKTLVAAKSLPK
SQ  QERIEWPMVVLRENGNIYILMTGVDSENTRLQGPVTITPQAHDNYGLESCALMIIPSLPPTIVIAESNGKLHHALLMEAE
SQ  ATEHSFNEVDDSVLIEPAEYVVHVLETVELELGISAPATGKEGGNCPIYLKRDLINELRYFAYHNAGLHAVTVSFIAELQ
SQ  RYLESESDEDRLELAVSASAEYILCTKFDSSETVNAVFGLALLQIPAGIVLLLGSGQVISLKLVIDAQLLVTPNENKPVD
SQ  SEVSQQESGPPFVDTIKSLLQRSVNQPILADKLSSPSAQESFELLNQAIEVLREQYLKRHDLVRAAFTRHINQIQLKKEQ
SQ  QLQEIQDLEQERELISERAHKLAERFEEISYNQELLVRKCNALMQRANASLPNSVIAEREFSQEVIRLNKVTQSLAAGLE
SQ  TAKKTFNKQRYHIAQSQEDLKKNAYELPEKQHRTITEILTQLTGEIDRQITDVKRINKIVGI
//
ID  Q99567;
PN  Nuclear pore complex protein Nup88;
GN  NUP88;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:30543681}.
DR  UNIPROT: Q99567;
DR  UNIPROT: D3DTM2;
DR  UNIPROT: Q9BWE5;
DR  Pfam: PF10168;
DR  OMIM: 602552;
DR  OMIM: 618393;
DR  DisGeNET: 4927;
DE  Function: Component of nuclear pore complex. {ECO:0000269|PubMed:30543681}.
DE  Disease: Fetal akinesia deformation sequence 4 (FADS4) [MIM:618393]: A clinically and genetically heterogeneous group of disorders with congenital malformations related to impaired fetal movement. Clinical features include fetal akinesia, intrauterine growth retardation, polyhydramnios, arthrogryposis, pulmonary hypoplasia, craniofacial abnormalities, and cryptorchidism. FADS4 inheritance is autosomal recessive. {ECO:0000269|PubMed:30543681}. Note=The disease is caused by variants affecting the gene represented in this entry. Disease mechanism likely includes impaired formation of the neuromuscular junction. NUP88 silencing in vitro results in reduced levels of rapsyn, a key player in clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction. Decreased rapsyn levels have also been observed in a patient muscle biopsy. {ECO:0000269|PubMed:30543681}.
DE  Reference Proteome: Yes;
DE  Interaction: P0DTD1; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: P35658; IntAct: EBI-20936668; Score: 0.40
DE  Interaction: P37198; IntAct: EBI-24419613; Score: 0.67
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-21639337; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q6ZQH8; IntAct: EBI-2563113; Score: 0.56
DE  Interaction: Q80U93; IntAct: EBI-2555228; Score: 0.56
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8CEC0; IntAct: EBI-2562665; Score: 0.40
DE  Interaction: Q8WYP5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P27701; IntAct: EBI-737252; Score: 0.00
DE  Interaction: P24386; IntAct: EBI-2515120; Score: 0.40
DE  Interaction: Q8K2X3; IntAct: EBI-2562811; Score: 0.40
DE  Interaction: Q9GZQ8; IntAct: EBI-3045543; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-3050465; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-6262548; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P33993; IntAct: EBI-6875195; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q8N137; IntAct: EBI-11392655; Score: 0.27
DE  Interaction: Q9UBB9; IntAct: EBI-24429402; Score: 0.56
DE  Interaction: O43314; IntAct: EBI-11901203; Score: 0.00
DE  Interaction: O95487; IntAct: EBI-11904001; Score: 0.00
DE  Interaction: Q15149; IntAct: EBI-11914286; Score: 0.00
DE  Interaction: Q2M2I8; IntAct: EBI-11915197; Score: 0.00
DE  Interaction: Q3V6T2; IntAct: EBI-11929271; Score: 0.00
DE  Interaction: E5LBS6; IntAct: EBI-14062727; Score: 0.35
DE  Interaction: Q9NUU7; IntAct: EBI-21587900; Score: 0.35
DE  Interaction: Q9Y2V7; IntAct: EBI-21639337; Score: 0.35
DE  Interaction: Q9BVG3; IntAct: EBI-21639337; Score: 0.35
DE  Interaction: Q9H1M0; IntAct: EBI-21639337; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-21866171; Score: 0.35
DE  Interaction: Q9Y2H1; IntAct: EBI-20624096; Score: 0.42
DE  Interaction: P30556; IntAct: EBI-20802739; Score: 0.37
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: A0A0H3LN59; IntAct: EBI-25401114; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-25478856; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-26397353; Score: 0.35
DE  Interaction: Q96LU5; IntAct: EBI-27050332; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: Q9UQM7; IntAct: EBI-28947140; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-30817604; Score: 0.44
DE  Interaction: Q9Y490; IntAct: EBI-30823972; Score: 0.44
DE  Interaction: P41212; IntAct: EBI-29015445; Score: 0.27
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0017056;
GO  GO:0000278;
GO  GO:0006406;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAEGPVGDGELWQTWLPNHVVFLRLREGLKNQSPTEAEKPASSSLPSSPPPQLLTRNVVFGLGGELFLWDGEDSSFLV
SQ  VRLRGPSGGGEEPALSQYQRLLCINPPLFEIYQVLLSPTQHHVALIGIKGLMVLELPKRWGKNSEFEGGKSTVNCSTTPV
SQ  AERFFTSSTSLTLKHAAWYPSEILDPHVVLLTSDNVIRIYSLREPQTPTNVIILSEAEEESLVLNKGRAYTASLGETAVA
SQ  FDFGPLAAVPKTLFGQNGKDEVVAYPLYILYENGETFLTYISLLHSPGNIGKLLGPLPMHPAAEDNYGYDACAVLCLPCV
SQ  PNILVIATESGMLYHCVVLEGEEEDDHTSEKSWDSRIDLIPSLYVFECVELELALKLASGEDDPFDSDFSCPVKLHRDPK
SQ  CPSRYHCTHEAGVHSVGLTWIHKLHKFLGSDEEDKDSLQELSTEQKCFVEHILCTKPLPCRQPAPIRGFWIVPDILGPTM
SQ  ICITSTYECLIWPLLSTVHPASPPLLCTREDVEVAESPLRVLAETPDSFEKHIRSILQRSVANPAFLKASEKDIAPPPEE
SQ  CLQLLSRATQVFREQYILKQDLAKEEIQRRVKLLCDQKKKQLEDLSYCREERKSLREMAERLADKYEEAKEKQEDIMNRM
SQ  KKLLHSFHSELPVLSDSERDMKKELQLIPDQLRHLGNAIKQVTMKKDYQQQKMEKVLSLPKPTIILSAYQRKCIQSILKE
SQ  EGEHIREMVKQINDIRNHVNF
//
ID  Q8CEC0;
PN  Nuclear pore complex protein Nup88;
GN  Nup88;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q99567}.
DR  UNIPROT: Q8CEC0;
DR  UNIPROT: Q80Z13;
DR  UNIPROT: Q8K090;
DR  Pfam: PF10168;
DE  Function: Component of nuclear pore complex. {ECO:0000250|UniProtKB:Q99567}.
DE  Reference Proteome: Yes;
DE  Interaction: P62826; IntAct: EBI-2562665; Score: 0.40
DE  Interaction: Q8WYU3; IntAct: EBI-2562665; Score: 0.40
DE  Interaction: Q99567; IntAct: EBI-2562665; Score: 0.40
DE  Interaction: B4DYZ6; IntAct: EBI-2562665; Score: 0.40
DE  Interaction: O14980; IntAct: EBI-2562665; Score: 0.40
DE  Interaction: Q9EPK7; IntAct: EBI-17172030; Score: 0.35
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0017056;
GO  GO:0000278;
GO  GO:0006406;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAVGPLGDGELWQSWLPNHVVFLRLREGVRNQSPAEAEKPAASTSPSCPSLPPHLPTRNLVFGLGGELFLWDAEGSAF
SQ  LVVRLRGPSGGGVEPPLSQYQRLLCINPPLFEIHQVLLSPTQHHVALIGSKGLMALELPQRWGKDSEFEGGKATVNCSTI
SQ  PIAERFFTSSTSLTLKHAAWYPSEMLDPHIVLLTSDNVIRIYSLREPQTPTKVIVLSEAEEESLILNKGRAYTASLGETA
SQ  VAFDFGPLVTVSKNIFEQKDRDVVAYPLYILYENGETFLTYVSLLHSPGNIGKLLGPLPMHPAAEDNYGYDACAILCLPC
SQ  VPNILVIATESGMLYHCVVLEGEEEDDQTLEKSWDPRADFIPSLYVFECVELELALKLASGEDDPFASDFSCPIKLHRDP
SQ  KCPSRYHCSHEAGVHSVGLTWIHKLHKFLGSDEEDKDSLQELTAEQKCFVEHILCTKPLPCRQPAPIRGFWIVPDILGPT
SQ  MICITSTYECLIRPLLSTVHPASPPLLCTQEDAEVAESPLRILAETPDSFEKHIKRILQRSAANPAFLKNCSARSSEKDL
SQ  APPPEECLQLISRATQVFREQYILKQDLAKEEIQRRVKLLCDQKRKQLEDLNYCREERVSHLFRKSLREMAERLADKYEE
SQ  AKEKQEDIMNRMKKVLHSFHAQLPVLSDSERDMKKELQLIPDQLRHLGNAIKQVTMKKDYQQRKMEKVLSPQKPTITLSA
SQ  YQRKCIQSILKEEGEHIREMVKQINDIRNHVTF
//
ID  O08658;
PN  Nuclear pore complex protein Nup88;
GN  Nup88;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q99567}.
DR  UNIPROT: O08658;
DR  Pfam: PF10168;
DE  Function: Component of nuclear pore complex. {ECO:0000250|UniProtKB:Q99567}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0017056;
GO  GO:0000278;
GO  GO:0006406;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAAGPVGDGELWQSWLPNHVVFLRLREGLKNQSPAEADKPATSTSPSCPPLPPHLPTRNLVFGLGGELFLWDAEGSAF
SQ  LVVRLRGPSGGSVEPPLSQYQRLLCINPPLFEIHQVLLSPTQHHVALIGTKGLMALELPQRWGKDSEFEGGKATVNCSTI
SQ  PIAERFFTSSTSLTLKHAAWYPSEMLDPHIVLLTSDNVIRIYSLREPQTPTKVIVLSEAEEESLILNKGRAYTASLGETA
SQ  VAFDFGPLVTVSKNMFEQKDREAVAYPLYILYENGETFLTYVSLLHSPGNIGKLLGPLPMHPAAEDNYGYDACAILCLPC
SQ  VPNILVIATESGMLYHCVVLEGEEDDDQTLEKSWDPRADLIPSLYVFECVELELALKLASAEDDPFASDFSCPIKLHRDP
SQ  KCPSRYHCSHEAGVHSVGLTWIHKLHKFLGSDEEDKDSLQELTAEQKCFVEHILCTKPLPCRQPAPIRGFWIVPDILGPT
SQ  MICITSTYECLIRPLLSTVHPASPPLLCTREDAGVAESPLRILAEAPDSFEKHIKRILQRSAANPALLKSSEKDLAPPPE
SQ  ECLQLISRATQVFREQYILKQDLAKEEIQRRVKLLCDQKRKQLEDLNYCREERKSLREMAERLADKYEEAKEKQEDIMNR
SQ  MKKVLHSFHTQLPVLSDSERDMKKELQLIPDQLRHLGNAIKQVTMKKDYQQRKMEKVLSPQKPTITLSAYQRKCIQSILK
SQ  EEGEHIREMVKQINDIRNHVNF
//
ID  A5PJZ5;
PN  Nuclear pore complex protein Nup93;
GN  NUP93;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q66HC5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66HC5}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8N1F7}. Nucleus envelope {ECO:0000250|UniProtKB:Q8N1F7}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000250}.
DR  UNIPROT: A5PJZ5;
DR  Pfam: PF04097;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling. {ECO:0000250|UniProtKB:Q8N1F7}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0006998;
GO  GO:0051292;
GO  GO:0016973;
GO  GO:0060391;
GO  GO:0006606;
GO  GO:0060395;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q66HC5};
SQ  MDTEGFGELLQQAEQLAAETEGISELPHVERNLQEIQQAGERLRSRTLTRTSQETADVKASVLLGSRGLDISHISQRLES
SQ  LSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFGMAEEYHRESMLVEWEQVKQRILHTLLASGEDALDFTQ
SQ  ESEPSYISDAGPPGRSSLDSIEMAYARQIYIYNEKIVNGHLQPNLLDLCASVTELDDKNISDMWAMVKQMTDVLLVPATD
SQ  ALKSRNSVEVRMEFVRQALGYLEQSYKNYTLVTVFGNLHQAQLGGVPGTYQLVRSFLNIKLPAPLPGLQDGEVEGHPVWA
SQ  LIYYCMRCGDLLAASQVVNRAQHQLGEFKTWFQEYMNSKDRRLSPATENKLRLHYRRALRNNTDPYKRAVYCIIGRCDVT
SQ  DNQSEVADKTEDYLWLKLNQVCFDDDGTSSPQDRLTLSQFQKQLLEDYGESHFTVNQQPFLYFQVLFLTAQFEAAIAFLF
SQ  RMERLRCHAVHVALVLFELKLLLKSSGQSAQLLSHEPGDPPCMRRLNFVRLLMLYTRKFESTDPREALQYFYFLRDEKDS
SQ  QGENMFLRCVSELVIESREFDMILGKLENDGSRKPGVIDKFTSDTKPIINKVASVAENKGLFEEAAKLYDLAKNADKVLE
SQ  LMNKLLSPIVPQISAPQSNKERLKNMALSIAERYRAQGISANKFVDSTFYLLLDLITFFDEYHSGHIDRAFDIIDRLKLV
SQ  PLNQESVEERVAAFRNFSDEIRHNLSEVLLATMNILFTQFKRLKGTSPSSATRPQRVIEDRDSQLRSQARALITFAGMIP
SQ  YRTSGDTNARLVQMEVLMN
//
ID  Q7ZU29;
PN  Nuclear pore complex protein Nup93;
GN  dye;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000250}.
DR  UNIPROT: Q7ZU29;
DR  UNIPROT: P79740;
DR  UNIPROT: Q9DGQ8;
DR  Pfam: PF04097;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051292;
GO  GO:0016973;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDTEGFGELLQQAEQLAAETEAVSELPHVERNLQEIQQAGERLRSRTLTRTSQDTADVKASILLGSRGLDIFHISQRLES
SQ  LSAATTFEPLEPVKDTDIQGFLKNERDNALLSAIEESRRRTFLLAEEYHRDSMLVQWEQVKQRVLHTLLGAGEDALDFSQ
SQ  EVEPSFVSEVGVPGRSALDSVEVAYSRQIYVFNEKIVNGHLQPNLGDLCASVAESLDDKNVSEMWLMVKQMTDVLLVPAK
SQ  DTLKSRVSVDMQMAFVRQALQFLENSYKNYTLVTVFGNLHQAQLGGVPGTYQLVCSFLNIKLPTPLPGRQDGEVEGHPVW
SQ  ALIYFCLRCGDLSAAMQVVNKAQHQLGDFKIWFQEYMNSPDRRLSPATENKLRLHYRRVLRNSADPYKRAVYCLIGKCDI
SQ  GDNHGEVADKTEDYLWLKLNQVCFDEDGSSSPQDRMTLAQLQKQLLEDYGESHFSASHQPFLYFQVLFLTAQFEAAIAFL
SQ  FRVERLRSHAVHVALVLYELKLLLKSSGQSAQLLSQEAGDPPMVRRLNFIRLLMLYTRKFESTDPREALQYFYFLRNEKD
SQ  SQGENMFMRCVSELVIESREFDMLLGRLEKDGSRKPGVIDKFAGDTRAIITKVASEAENKGLFEEAVKLYELAKNADKVL
SQ  ELMNKLLSPVIAQVSEPQSNKERLKNMAVAIAERYRANGVAGEKSVDNTFYLLLDLMTFFDEYHAGHIDRAYDVIERLKL
SQ  VPLSQDSVEERVAAFRNFSDEVRHNLSEVLLATMNILFTQYKRLKGAAAGTPGRPQRTLEDRDMLLRIQARALITFAGMI
SQ  PYRMAGDTNARLVQMEVLMN
//
ID  Q8N1F7;
PN  Nuclear pore complex protein Nup93;
GN  NUP93;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q66HC5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66HC5}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:9348540}. Nucleus envelope {ECO:0000269|PubMed:26878725, ECO:0000269|PubMed:9348540}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000269|PubMed:9348540}.
DR  UNIPROT: Q8N1F7;
DR  UNIPROT: B3KPQ8;
DR  UNIPROT: Q14705;
DR  PDB: 5IJN;
DR  PDB: 5IJO;
DR  PDB: 7PER;
DR  Pfam: PF04097;
DR  OMIM: 614351;
DR  OMIM: 616892;
DR  DisGeNET: 9688;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:9348540). May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling (PubMed:26878725). {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:15703211, ECO:0000269|PubMed:26878725, ECO:0000269|PubMed:9348540}.
DE  Disease: Nephrotic syndrome 12 (NPHS12) [MIM:616892]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. NPHS12 inheritance is autosomal recessive. {ECO:0000269|PubMed:26878725}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P0DTC7; IntAct: EBI-25687011; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q6ZMQ8; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q6ZQH8; IntAct: EBI-2563113; Score: 0.56
DE  Interaction: Q80U93; IntAct: EBI-2555228; Score: 0.56
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: O75365; IntAct: EBI-1059612; Score: 0.00
DE  Interaction: Q9Y5J5; IntAct: EBI-1064828; Score: 0.00
DE  Interaction: P49662; IntAct: EBI-1066732; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-3893169; Score: 0.56
DE  Interaction: Q9HC98; IntAct: EBI-1069660; Score: 0.00
DE  Interaction: Q13418; IntAct: EBI-1070407; Score: 0.00
DE  Interaction: P62330; IntAct: EBI-1071623; Score: 0.00
DE  Interaction: Q9HAW0; IntAct: EBI-1072446; Score: 0.00
DE  Interaction: O14908; IntAct: EBI-1073459; Score: 0.00
DE  Interaction: Q9Y478; IntAct: EBI-1076145; Score: 0.00
DE  Interaction: Q9BUV8; IntAct: EBI-1076761; Score: 0.00
DE  Interaction: Q15714; IntAct: EBI-1078435; Score: 0.00
DE  Interaction: Q99623; IntAct: EBI-1078910; Score: 0.00
DE  Interaction: O00422; IntAct: EBI-1079733; Score: 0.00
DE  Interaction: Q96T60; IntAct: EBI-1079805; Score: 0.00
DE  Interaction: Q9Y2Q3; IntAct: EBI-1080109; Score: 0.00
DE  Interaction: O76071; IntAct: EBI-1083915; Score: 0.00
DE  Interaction: Q8AZK7; IntAct: EBI-9632715; Score: 0.35
DE  Interaction: Q8IY92; IntAct: EBI-2371551; Score: 0.35
DE  Interaction: Q504Q3; IntAct: EBI-2513052; Score: 0.40
DE  Interaction: P24386; IntAct: EBI-2515120; Score: 0.40
DE  Interaction: Q9Z0E3; IntAct: EBI-2549710; Score: 0.35
DE  Interaction: O43918; IntAct: EBI-2550555; Score: 0.40
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q13286; IntAct: EBI-3248480; Score: 0.35
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6268389; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q9UKV0; IntAct: EBI-6598230; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: Q96FW1; IntAct: EBI-10770028; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q07797; IntAct: EBI-11108624; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-11889606; Score: 0.37
DE  Interaction: O60733; IntAct: EBI-24312432; Score: 0.56
DE  Interaction: Q15777; IntAct: EBI-24327809; Score: 0.56
DE  Interaction: Q14982; IntAct: EBI-24419380; Score: 0.56
DE  Interaction: O43299; IntAct: EBI-24468599; Score: 0.56
DE  Interaction: Q9NV29; IntAct: EBI-24472902; Score: 0.56
DE  Interaction: P06465; IntAct: EBI-26504492; Score: 0.37
DE  Interaction: P56180; IntAct: EBI-14025693; Score: 0.35
DE  Interaction: Q921C5; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-16786806; Score: 0.27
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: O14880; IntAct: EBI-16796348; Score: 0.27
DE  Interaction: P62491; IntAct: EBI-16797971; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: O75880; IntAct: EBI-16799233; Score: 0.27
DE  Interaction: Q71U36; IntAct: EBI-16799705; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: Q8N4T4; IntAct: EBI-25408280; Score: 0.35
DE  Interaction: Q14CB8; IntAct: EBI-25409097; Score: 0.35
DE  Interaction: Q8WUY9; IntAct: EBI-25411615; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-26397631; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574619; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q05D32; IntAct: EBI-27113232; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
DE  Interaction: Q8TDD2; IntAct: EBI-29000537; Score: 0.35
DE  Interaction: P08047; IntAct: EBI-29385496; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
DE  Interaction: P35968; IntAct: EBI-32723270; Score: 0.27
DE  Interaction: Q8IWU2; IntAct: EBI-32723604; Score: 0.27
DE  Interaction: Q96Q04; IntAct: EBI-32723651; Score: 0.27
DE  Interaction: Q12866; IntAct: EBI-32723870; Score: 0.27
DE  Interaction: Q01973; IntAct: EBI-32725295; Score: 0.27
DE  Interaction: P08922; IntAct: EBI-32731758; Score: 0.27
DE  Interaction: Q02763; IntAct: EBI-32732012; Score: 0.35
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0006998;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0060391;
GO  GO:0006606;
GO  GO:0060395;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q66HC5};
SQ  MDTEGFGELLQQAEQLAAETEGISELPHVERNLQEIQQAGERLRSRTLTRTSQETADVKASVLLGSRGLDISHISQRLES
SQ  LSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFGMAEEYHRESMLVEWEQVKQRILHTLLASGEDALDFTQ
SQ  ESEPSYISDVGPPGRSSLDNIEMAYARQIYIYNEKIVNGHLQPNLVDLCASVAELDDKSISDMWTMVKQMTDVLLTPATD
SQ  ALKNRSSVEVRMEFVRQALAYLEQSYKNYTLVTVFGNLHQAQLGGVPGTYQLVRSFLNIKLPAPLPGLQDGEVEGHPVWA
SQ  LIYYCMRCGDLLAASQVVNRAQHQLGEFKTWFQEYMNSKDRRLSPATENKLRLHYRRALRNNTDPYKRAVYCIIGRCDVT
SQ  DNQSEVADKTEDYLWLKLNQVCFDDDGTSSPQDRLTLSQFQKQLLEDYGESHFTVNQQPFLYFQVLFLTAQFEAAVAFLF
SQ  RMERLRCHAVHVALVLFELKLLLKSSGQSAQLLSHEPGDPPCLRRLNFVRLLMLYTRKFESTDPREALQYFYFLRDEKDS
SQ  QGENMFLRCVSELVIESREFDMILGKLENDGSRKPGVIDKFTSDTKPIINKVASVAENKGLFEEAAKLYDLAKNADKVLE
SQ  LMNKLLSPVVPQISAPQSNKERLKNMALSIAERYRAQGISANKFVDSTFYLLLDLITFFDEYHSGHIDRAFDIIERLKLV
SQ  PLNQESVEERVAAFRNFSDEIRHNLSEVLLATMNILFTQFKRLKGTSPSSSSRPQRVIEDRDSQLRSQARTLITFAGMIP
SQ  YRTSGDTNARLVQMEVLMN
//
ID  Q8BJ71;
PN  Nuclear pore complex protein Nup93;
GN  Nup93;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q66HC5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66HC5}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8N1F7}. Nucleus envelope {ECO:0000269|PubMed:26878725}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000250}.
DR  UNIPROT: Q8BJ71;
DR  UNIPROT: Q3TED9;
DR  UNIPROT: Q8BIK7;
DR  UNIPROT: Q8K1R4;
DR  UNIPROT: Q8R592;
DR  Pfam: PF04097;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC (By similarity). During renal development, regulates podocyte migration and proliferation through SMAD4 signaling (By similarity) (PubMed:26878725). {ECO:0000250|UniProtKB:Q8N1F7, ECO:0000269|PubMed:26878725}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Z0E3; IntAct: EBI-2549816; Score: 0.35
DE  Interaction: P59240; IntAct: EBI-4287460; Score: 0.35
DE  Interaction: Q6P1J9; IntAct: EBI-20729673; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
GO  GO:0005813;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0006998;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0060391;
GO  GO:0006606;
GO  GO:0060395;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q66HC5};
SQ  MDTEGFGELLQQAEQLAAETEGISELPHVERNLQEIQQAGERLRSRTLTRTSQETADVKASVLLGSRGLDISHISQRLES
SQ  LSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFGMAEEYHRESMLVEWEQVKQRILHTLLASGEDALDFTQ
SQ  ESEPSYIGDVNPPGRSSLDSIEMAYARQIYIYNEKIVSGHLQPNLVDLCASVAELDDKSISDMWAMVKQMTDVVLTPATD
SQ  ALKSRSSVEVRMDFVKQALGYLEQSYKNYTLVTVFGNLHQAQLGGVPGTYQLVRSFLNIKLPAPSPGLQDGEVEGHPVWA
SQ  LIYYCMRCGDLLAASQVVSRAQHQLGEFKTWFQEYMNSKDRRLSPATENKLRLHYRRALRNNTDPYKRAVYCIIGRCDIT
SQ  DNQSEVADKTEDYLWLKLNQVCFDDDGTSSPQDRLTLSQFQKQLLEDYGESHFTVNQQPFLYFQVLFLTAQFEAAIAFLF
SQ  RMERLRCHAVHVALVLFELKLLLKSSGQSAQLLSHEPGDPPCMRRLNFVRLLMLYTRKFESTDPREALQYFYFLRDEKDS
SQ  QGENMFLRCVSELVIESREFDMILGKLENDGSRKPGVIDKFTSDTKPIINKVASVAENKGLFEEAAKLYDLAKNADKVLE
SQ  LMNKLLSPVVPQISAPQSNKERLKNMALSIAERYRAQGISANKFVDSTFYLLLDLITFFDEYHSGHIDRAFDIIDRLKLV
SQ  PLNQESVEERVAAFRNFSDEIRHNLSEVLLATMNILFTQFKRLKGTSPSSATRPQRVIEDRDSQLRSQARALITFAGMIP
SQ  YRTSGDTNARLVQMEVLMN
//
ID  Q5R822;
PN  Nuclear pore complex protein Nup93;
GN  NUP93;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q66HC5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66HC5}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8N1F7}. Nucleus envelope {ECO:0000250|UniProtKB:Q8N1F7}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000250}.
DR  UNIPROT: Q5R822;
DR  UNIPROT: Q5R8Y2;
DR  Pfam: PF04097;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling. {ECO:0000250|UniProtKB:Q8N1F7}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006998;
GO  GO:0051292;
GO  GO:0060391;
GO  GO:0015031;
GO  GO:0060395;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q66HC5};
SQ  MDTEGFGELLQQAEQLAAETEGISELPHVERNLQEIQQAGERLCSRTLTRTSQETADVKASVLLGSRGLDISHISQRLES
SQ  LSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFGMAEEYHRESMLVEWEQVKQRILHTLLASGEDALDFTQ
SQ  ESEPSYISDVGPPGRSSLDNIEMAYARQIYIYNEKIVNGHLQPNLVDLCASVAELDDKSISDMWTMVKQMTDVLLTPATD
SQ  ALKNRSSVEVRMEFVRQALAYLEQSYKNYTLVTVFGNLHQAQLGGVPGTYQLVRSFLNIKLPAPLPGLQDGEVEGHPVWA
SQ  LIYYCMRCGDLLAASQVVNRAQHQLGEFKTWFQEYMNSKDRRLSPATENKLRLHYRRALRNNTDPYKRAVYCIIGRCDVT
SQ  DNQSEVADKTEDYLWLKLNQVCFDDDGTSSPQDRLTLSQFQKQLLEDYGESHFTVNQQPFLYFQVLFLTAQFEAAIAFLF
SQ  RMERLRCHAVHVALVLFELKLLLKSSGQSAQLLSHEPGDPPCMRRLNFVRLLMLYTRKFESTDPREALQYFYFLRDEKDS
SQ  QGENMFLRCVSELVIESREFDMILGKLENDGSRKPGVIDKFTSDTKPIINKVASVAENKGLFEEAAKLYDLAKNADKVLE
SQ  LMNKLLSPVVPQISAPQSNKERLKNMALSIAERYRAQGISANKFVDSTFYLLLDLITFFDEYHSGHIDRAFDIIERLKLV
SQ  PLNQESVEERVAAFRNFSDEIRHNLSEVLLATMNILFTQFKRLKGTSPSSSSRPQRVIEDRDSQLRSQACTLITFAGMIP
SQ  YRTSGDTNARLVQMEVLMN
//
ID  Q66HC5;
PN  Nuclear pore complex protein Nup93;
GN  Nup93;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15703211}; Peripheral membrane protein {ECO:0000269|PubMed:15703211}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8N1F7}. Nucleus envelope {ECO:0000250|UniProtKB:Q8N1F7}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000250}.
DR  UNIPROT: Q66HC5;
DR  Pfam: PF04097;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling. {ECO:0000250|UniProtKB:Q8N1F7}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0006998;
GO  GO:0051292;
GO  GO:0016973;
GO  GO:0060391;
GO  GO:0006606;
GO  GO:0060395;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:15703211};
SQ  MDTEGFGELLQQAEQLAAETEGISELPHVERNLQEIQQAGERLRSRTLTRTSQETADVKASVLLGSRGLDISHISQRLES
SQ  LSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFGMAEEYHRESMLVEWEQVKQRILHTLLASGEDALDFTQ
SQ  ESEPSYVSDVSPPGRSSLDSIEMAYARQIYIYNEKIVSGHLQPNLVDLCASVAELDDKSISDMWAMVKQMTDVVLTPATD
SQ  ALKSRSSVEVRMDFVKQALGYLEQSYKNYTLVTVFGNLHQAQLGGVPGTYQLVRSFLNIKLPAPSPGLQDGEVEGHPVWA
SQ  LIYYCMRCGDLLAASQVVSRAQHQLGEFKTWFQEYMNSKDRRLSPATENKLRLHYRRALRNNTDPYKRAVYCIIGRCDIT
SQ  DNQSEVADKTEDYLWLKLNQVCFDDDGTSSPQDRLTLSQFQKQLLEDYGESHFTVNQQPFLYFQVLFLTAQFEAAIAFLF
SQ  RMERLRCHAVHVALVLFELKLLLKSSGQSAQLLSHEPGDPPCMRRLNFVRLLMLYTRKFESTDPREALQYFYFLRDEKDS
SQ  QGENMFLRCVSELVIESREFDMILGKLENDGSRKPGVIDKFTSDTKPIINKVASVAENKGLFEEAAKLYDLAKNADKVLE
SQ  LMNKLLSPVVPQISAPQSNKERLKNMALSIAERYRAQGISANKFVDSTFYLLLDLITFFDEYHSGHIDRAFDIIDRLKLV
SQ  PLNQESMEERVAAFRNFSDEIRHNLSEVLLATMNILFTQFKRLKGTSPSSATRPQRVIEDRDSQLRSQARALITFAGMIP
SQ  YRTSGDTNARLVQMEVLMN
//
ID  Q7ZX96;
PN  Nuclear pore complex protein Nup93;
GN  nup93;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000250}.
DR  UNIPROT: Q7ZX96;
DR  UNIPROT: P70035;
DR  PDB: 7VCI;
DR  PDB: 7VOP;
DR  PDB: 7WB4;
DR  PDB: 7WKK;
DR  Pfam: PF04097;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5EWX9; IntAct: EBI-8070373; Score: 0.35
DE  Interaction: Q6PAY1; IntAct: EBI-6285093; Score: 0.35
DE  Interaction: Q91349; IntAct: EBI-6285081; Score: 0.53
DE  Interaction: Q5EAX5; IntAct: EBI-16171164; Score: 0.35
DE  Interaction: K9ZTJ6; IntAct: EBI-16171164; Score: 0.35
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDGEGFGELLQQAEQLAAETEGVTELPHVERNLQEIQQAGERLRSKTMTRTSQESANVKASVLLGSRGLDISHISQRLES
SQ  LSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFVMAEEYHRESMLVEWEQVKQRVLHTLLASGEDALDFTQ
SQ  ESETSYISESGAPGRSSLDNVEMAYARQMYMYNEKVVSGHLQPSLVDLCTEAAERLDDKNVSDLWVMVKQMTDVPLIPAS
SQ  DTLKSRCSGQMQMAFVRQALNYLEQSYKNYTLISVFANLQQAQLGGVPGTYNLVRSFLNIRLPTPIPGLQDGEIEGYPVW
SQ  ALIYYCMRCGDLMAAQQVVNRAQHQLGDFKNCFQEYIHNKDRRLSPTTENKLRLHYRRAVRASTDPYKRAVYCIIGRCDV
SQ  SDNHSEVADKTEDYLWLKLSQVCFEDEANSSPQDRLTLPQFQKQLFEDYGESHFAVNQQPYLYFQVLFLTAQFEAAIAFL
SQ  FRLERTRCHAVHVALALFELKLLLKSTGQSAQLLSQEPGEPQGVRRLNFIRLLMLYTRKFEPTDPREALQYFYFLRNEKD
SQ  NQGESMFLRCVSELVIESREFDMLLGKLEKDGSRKPGAIDKFTRDTKTIINKVASVAENKGLFEEAAKLYDLAKNPDKVL
SQ  ELTNKLLSPVVSQISAPQSNRERLKNMALAIAERYKSQGVSAEKSINSTFYLLLDLITFFDEYHAGHIDLSFDVIERLKL
SQ  VPLSQDSVEERVAAFRNFSDEIRHNLSEILLATMNILFTQYKRLKGSGPTTLGRPQRVQEDKDSVLRSQARALITFAGMI
SQ  PYRMSGDTNARLVQMEVLMN
//
ID  Q6NX12;
PN  Nuclear pore complex protein Nup93;
GN  nup93;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000250}.
DR  UNIPROT: Q6NX12;
DR  Pfam: PF04097;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051292;
GO  GO:0016973;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MDGEGFGELLQQAEQLAAETEGVTELPHVERNLQEIQQAGERLRSKTMTRTSQESANVKASVLLGSRGLDISHISQRLES
SQ  LSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFVMAEEYHRESMLVEWEQVKQRVLHTLLASGEDALDFTQ
SQ  ESETSYISESGAPGRSSLDNVEMAYARQIYMYNEKVVSGHLQPSLVELCTEAAERLDDKNVSDLWVMVKQMTDVPLIPAS
SQ  DSLKSRCSVQMQMAFLRQALHFLEQSYKNYTLMSVFANLQQAQLGGVPGTYNLVRSFLNIRLPAPIPGLQDGEVEGYPVW
SQ  ALIYYCMRCGDLMAAQQVVNRAQHQLGDFKNCFQEYVHSKDRRLSPTTENKLRLHYRRAVRASTDPYKRVVYCIIGRCDV
SQ  TDNHSEVADKTEDYLWLKLSQVCFEDEANSSPQDRLTLPQFQKQLFEDYGESHFAVNQQPYLYFQVLFLTAQFEAAIAFL
SQ  FRLERTRCHAVHVALALFELKLLLKSTGQSAQLLSLEPGDPQGVRHLNFIRLLMLYTRKFEPTDPREALQYFYFLRNEKD
SQ  SQGESMFLRCVSELVIESREFDMLLGKLEKDGSRKPGAIDKFTRDTKTIINKVASVAENKGLFEEAAKLYDLAKNPDKVL
SQ  ELTNKLLSPVVSQISAPQSNRERLKNMALAIAERYKSQGVSAEKSINSTFYLLLDLITFFDEYHAGHVDLAFDVIERLKL
SQ  VPLSQDSVEERVAAFRNFSDEIRHNLSEILLATMNILFTQYKRLKGSGPNTLGRPQRAQEDKDSVLRSQARALITFAGMI
SQ  PYRMSGDTNARLVQMEVLMN
//
ID  Q8LLD0;
PN  Nuclear pore complex protein NUP96;
GN  NUP96;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:16751346}; Peripheral membrane protein {ECO:0000269|PubMed:16751346}; Nucleoplasmic side {ECO:0000269|PubMed:16751346}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:15772285, ECO:0000269|PubMed:21203492}.
DR  UNIPROT: Q8LLD0;
DR  UNIPROT: Q38941;
DR  UNIPROT: Q8LLD1;
DR  Pfam: PF04096;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Contributes to the transfer of mature mRNA from the nucleus to the cytosol. Required for both R gene-mediated and basal disease resistance. RNA export seems to play a critical role in stress responses and regulation of plant growth and development. {ECO:0000269|PubMed:15772285, ECO:0000269|PubMed:16751346, ECO:0000269|PubMed:21203492, ECO:0000269|PubMed:22288649}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0015288;
GO  GO:0017056;
GO  GO:0006952;
GO  GO:0002758;
GO  GO:0048574;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0009733;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16751346};
SQ  MTSLSIQPFPEISRMARDLDSRKKRRISLDGIAALCEHSKEIIDSLPMLNSPDYFLKPCINELVEREIESPDYCSRVPDF
SQ  TIGRIGYGYIRFLGNTDVRRLDLDHIVKFHRHEVIVYDDESSKPVVGEGLNKAAEVTLVVNIPDLTWGKQQVNHIAYKLK
SQ  QSTERQGATFISFDPDNGLWKFFVPHFSRFGLSDDEAEDIAMDDAPGLGDPVGLDGKKVADIDEEDQMETSELELSHSLP
SQ  AHLGLDPEKMKEMRMLMFPNEDEDESEDFREQTSHLMTSLTKRNVRPSQKIAQRNSHQDPPPVVRKTPLALLEYNPGNDK
SQ  SSPGSILMVQQNKNLAVRKSKTGGFELDISHVTPLTDNYSRNVVDAALFMGRSFRAGWGPNGVLFHTGKPICSSSSQMVL
SQ  SSVINKEKIAIDKVVWDRKGKVQKELIDSAFEAPLSLHKELNHVEEEVRFGSFSLKLQNVVTDRVVLSDICRSYIGIIEK
SQ  QLEVAGLSTSAKLFLMHQVMVWELIKVLFSERQSTERLMYAASDNEEDVMQDVKEDSAKIDTEALPLIRRAEFSCWLQES
SQ  VSHRVQEDVSDLNGSSYLEHLFFLLTGRELDSAVELAISKGDVRLACLLSQAGGSTVNRNDILQQLHLWRRNGLDFNFIE
SQ  KERIKLYELLAGNIHDALQDFTIDWKRFLGLLMWHHLPPDSSLPIIFRSYQLLLNQAKAPWPVPIYIDEGPADGFVSDNK
SQ  HSDILYYLMLLHSKEEEEFGFLQTMFSAFSSTDDPLDYHMIWHHRGILEAVGAFTSDDLHTLDMGFVAQLLSQGLCHWAI
SQ  YVVLHIPFREDHPYLHVTVIREILFQYCETWSSMESQRQFIKDLGIPSEWMHEALAVYYNYHGDFVKALDQFIECANWQR
SQ  AHSIFMTSVAHSLFLSANHSEIWRIATSMDDRKSEIENWDLGAGIYMSFYLLKSSLQEDADTMVELEPLDSTNESCRNFV
SQ  GRLNESLAVWGDRLPVEARVAYSKMAEEICDLLLSDLSKNPSRETQLTCFETAFDAPLPEDVRSTHLQDAVSLFSLYLSE
SQ  TGQISA
//
ID  G5EEH9;
PN  Nuclear pore complex protein Nup96;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: [Nuclear pore complex protein Nup98]: Cytoplasmic granule {ECO:0000269|PubMed:20335358}. Nucleus membrane {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:28122936}; Peripheral membrane protein {ECO:0000269|PubMed:20335358}; Nucleoplasmic side {ECO:0000269|PubMed:20335358}. Note=P granule localization dependent on nucleoporins npp-7, npp-8 and npp-9 which are involved in P granule integrity. {ECO:0000269|PubMed:20335358}. [Nuclear pore complex protein Nup96]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:20335358}. Nucleus envelope {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:22238360}. Chromosome {ECO:0000269|PubMed:16950114}. Note=Requires mel-28 for chromatin association during early steps of nuclear pore complex assembly. {ECO:0000269|PubMed:16950114}.
DR  UNIPROT: G5EEH9;
DR  UNIPROT: D1MN48;
DR  UNIPROT: H2L014;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC) (PubMed:20335358, PubMed:28122936). Required for the nuclear import of hcp-4 during mitotic prophase, this step is essential for centrosome assembly and resolution (PubMed:28122936). Regulates nucleoporin npp-5 localization to the nuclear membrane during interphase and to kinetochores during metaphase (PubMed:22238360). Has a role in P granule integrity; may promote the 'liquid phase' of P granules by increasing the number of interacting RNA-protein complexes (PubMed:20335358). Binds nos-2 mRNA, probably indirectly, and promotes its accumulation in P granules (PubMed:20335358). {ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:22238360, ECO:0000269|PubMed:28122936}.
DE  Reference Proteome: Yes;
DE  Interaction: O02333; IntAct: EBI-6455546; Score: 0.37
DE  Interaction: G5ECG0; IntAct: EBI-6455567; Score: 0.37
DE  Interaction: Q21443; IntAct: EBI-6455606; Score: 0.37
DE  Interaction: P91457; IntAct: EBI-6455580; Score: 0.37
DE  Interaction: Q8TA83; IntAct: EBI-6455645; Score: 0.37
DE  Interaction: P91400; IntAct: EBI-6455658; Score: 0.37
DE  Interaction: P34402; IntAct: EBI-6455619; Score: 0.37
DE  Interaction: P90900; IntAct: EBI-6455684; Score: 0.37
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0043186;
GO  GO:0003723;
GO  GO:0008236;
GO  GO:0017056;
GO  GO:0051301;
GO  GO:0009792;
GO  GO:1990893;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0006997;
GO  GO:0030719;
GO  GO:0006606;
GO  GO:0034501;
GO  GO:0090435;
GO  GO:0015031;
GO  GO:0006508;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:20335358};
SQ  MFGQNKSFGSSSFGGGSSGSGLFGQNNQNNQNKGLFGQPANNSGTTGLFGAAQNKPAGSIFGAASNTSSIFGSPQQPQNN
SQ  QSSLFGGGQNNANRSIFGSTSSAAPASSSLFGNNANNTGTSSIFGSNNNAPSGGGLFGASTVSGTTVKFEPPISSDTMMR
SQ  NGTTQTISTKHMCISAMSKYDGKSIEELRVEDYIANRKAPGTGTTSTGGGLFGASNTTNQAGSSGLFGSSNAQQKTSLFG
SQ  GASTSSPFGGNTSTANTGSSLFGNNNANTSAASGSLFGAKPAGSSLFGSTATTGASTFGQTTGSSLFGNQQPQTNTGGSL
SQ  FGNTQNQNQSGSLFGNTGTTGTGLFGQAQQQPQQQSSGFSFGGAPAATNAFGQPAAANTGGSLFGNTSTANTGSSLFGAK
SQ  PATSTGFTFGATQPTTTNAFGSTNTGGGLFGNNAAKPGGLFGNTTNTGTGGGLFGSQPQASSGGLFGSNTQATQPLNTGF
SQ  GNLAQPQIVMQQQVAPVPVIGVTADVLQMQANMKSLKSQLTNAPYGDSPLLKYNANPEIDGKSSPASTQRQLRFLAAKKG
SQ  ALSSSSDAQDSSFIIPPISKVMSDLSPAVTRSADVTKDLNYTSKEAPPSLARGLRNSTFNPNMSLTNRSVHESSALDKTI
SQ  DSALDASMNGTSNRLGVRGSVRRSNLKQLDMSLLADSSRVGRESRVADPDALPRISESERRQDVVTSTPAVDPVQAVIQR
SQ  HNDRNRDPPSLNLDTTCDEHTGLEPVSAATSSAASVVSTPSEETVNVNSAAGVKLTKPDYFSLPTINEMKNMIKNGRVVL
SQ  EDGLTVGRSSYGSVYWPGRVELKDVALDEIVVFRHREVTVYPNEEEKAPEGQELNRPAEVTLERVWYTDKKTKKEVRDVV
SQ  KLSEIGWREHLERQTIRMGAAFKDFRAETGSWVFRVDHFSKYGLADDDEPMDGSPPQQALQASSPLQVIDMNTSARDVNN
SQ  QVQRKKVHKATDAHHQEIILERVPAPAALGDVVPIIRRVNRKGLGGGTLDDSREESCIGNMTTEFNESGHDSIIEEGQQP
SQ  EKKPKLELLADLEYESSRFIRNLQELKVMPKANDPAHRFHGGGHSAKMIGYGKSKLIDIGIVKGRSSHVGWSETGCLVWS
SQ  AQPRHNQVLFGTIDRTSDVNENTLISMLDVNVHVSETSRKGPSSQSNSVKSSLTSNFVTYSDSYSSMFAKYIDVAQAGGY
SQ  DGHVSVWKLISALFPYERREGWSFERGEEIGEWLRTEAVKSVPDDRSADTSSNGVWNQLCLGDIDKAFQIAIDNNQPQLA
SQ  TMLQTSAVCPEATVHCFKAQLDNWKKCETLHLIPKETLKCYVLMSGLSHYEWDQDGKNHSINCLDGLNWIQALGLHVWYL
SQ  RAWTGLEESYDAYQKDVNAGRAASNRGDLPGELIKLACESQHSVEVVLDCAAGENPNDYFLQWHVWSLLYSVGYRTMSKT
SQ  SETRLHRNYSSQLEASSLSKYALFVLQHIDDDEERSTAVRSLLDRIARFTDNDMFDSISEQFDIPSEWIADAQFSIAKSV
SQ  DDSTQLFELAVAAKNYLEICRLFVDDIAPTAVVAGDHDALKAACAMVRPFENQIPEWGATGMVYTDYCRLINLIENDAEE
SQ  ELLQDVLESLETRLHAPTISKNSLQKLSLQTIGRVLFEYRADKNTLPEWTKLLGHRQMFKIFRDRSSWGIERFTIEFD
//
ID  Q54EQ8;
PN  Nuclear pore complex protein Nup96;
GN  nup98;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Note=Nup96 is localized to the nucleoplasmic side of the nuclear pore complex, at or near the nucleoplasmic basket. {ECO:0000250}.
DR  UNIPROT: Q54EQ8;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC). The repeat domain in Nup98 has a direct role in the transport (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFGGQFGSFGAKPAATASPFGAPSAAPTTSLFGSTAPSSGFGGFGSTAQTTQPTTGGFGGFGGFGGATTTQQPAASPFGG
SQ  GGTGGSGLFGSSAQTTTQQPGASPFGGGFGTTTTTTTQQPGASPFGGTGGGLFGSSAQTTTQQQGASPFGGFGGATTTQP
SQ  SLLSGATGGFGGFGGSTTSGTQLGGGGGATSGAFGGSSSPFGGSGGATTSSPFGGGGGSFGATTQKQYGTPIPYQQTTIE
SQ  GNTFVSISAMPQYNDRSFEELRFEDITHRKDIVYKTGGGSGGGNSLFGSTPTTQPSSPFGAQTTTQTTGGLFGGQTTTSP
SQ  FGGQTSATPGSSLFGSTQPTQQQTSGGLFGSVQPTQQQAGGGLFGSMPSTGGSSLFGSTQPTQQQTGGAQPTQSLFGGQT
SQ  QTTTSPFGSQTSTPFGQPQQTNTGSGLFGAQQTQQTNTGGGLFGAQPTQQTSGGGLFGTQPTSGTGLFGTSPTAGGTGLF
SQ  GTTQPTSQGTGLFGTTQPTTQGTGLFGTSPTSGTGLFGSTPTSGTGLFGSTPTSGTGLFGSAQPPQNQQSQTSLFGNTGT
SQ  GATNTGTGLFGSAQPSSNPGGGLFGSAQPSTTTGGLFGSNQPTAQPTTSLFGNTTGSVGGLGATPNITSGLFGSNPAQTG
SQ  GLFGSTQPTTQTSLFGNTGSTGGLGAQNGGGLFGNLSQPTATAGQGLSGGLFGNLSQPTATAGQGLSSGGLFGNTLLGQP
SQ  STQGLSSALPTLGLGLMGGQPQQTQQLPQGSLMLQQTQQPLQQQPLQQQQQPLQQSTIQLNNQINSASPYFPISSPAPFA
SQ  TFVKDLTSTSKVVSPPSYTQRSLSHHGYIPKSTTKLVPRRGPNNVDLGFSVIQNQNGLFPIDKFITKHSKSLNINTTNET
SQ  EDTLRSLNTKSSSLFNNNNNNNNNNNNRNVNTNVNDYQNNGLPSSSLYNSNINQLSNNNNNNNNIYNNNNNNNINNNNNN
SQ  NNISTQFNLRNNQSSSDNLNNDKSLSSSSSNKSQQQQQKEQKEEQPPKPIKEKEFINPNAPKLTRDGYQCVPSIKELSKK
SQ  TDKELSSVQGFTISRDGCGSIYFPGSTNLVALDLDDIVDIEPREVSVYKDEETKPEIGYGLNRDAVVTLENCWPKNKNGE
SQ  VVKEDGTILDKYENALKKVSAKSDCGFVSYSRSNGTWVFTVKHFSKYSAPDFDEDDQQMQQQTQQKQQQTQPSKVTFQQP
SQ  STKLTKPKFTANLDNFDSDSETSSGDENQDEMVPQKKTPFIKRVSNRESGLFDTPSVVPMSEKIETTPSKIARVSEPTSQ
SQ  SSRMSNNALKFSTFNPQQQQLQSSRFKSTGLSILSNPVKNLIQSDVNNEQSMFSNTTTTSTTRIQPLPSQQHLVQPIPTT
SQ  ISLNKNYFSKVRIDPQVYDRIVPKEESITNQYRMKNERLNHSTQDVSLFMRRSFRVGWAPGGKLISITKSSFKNLLIKKL
SQ  PTDTKEDKKESIIKFLKNHHSHSSLVPENLKSIGWFSISNVQEQIESQLTLNVPSSQSVYYNRIWSLISNLWGNVLKGNG
SQ  SKYINTNYSEDTIRKLNLNQWLKDVIAPLLRDEMDSLRKKTNSNYLEQIFSYLSAKQIKEASDLANENKDFRLATMMSQI
SQ  WSSSESGKELILKQLTTYHSNGSDEFINEKRLEILHLIAGSVNKIYKNLNDWIRCFAVSFWFKYSLEYSIEDSVENFERS
SQ  FNAHRSVYPLPPYLIKSTSTNSKQIEEQQHYYDICFLLLKLFAVNRGSSHFDKFKNIFYPENIGQDLLDYHLSWNLYTVL
SQ  KSIPSLNKQPDLVNASNLHSSFALQLERLGLWQWSIYVLLHTPDQSNHVREEAVKSLIARAAPVITSEDRVFLTTKLHIP
SQ  EIWIDEAKAWYSGYDCNNDIYDQIDALFKSYQYTKIHDIIFSNIGPNYIIQKRYHSLKDLLIRLEPHSSFISTWRYGGSI
SQ  FLEFADICIQYKEILSQLSNTAEEIQRTKYYVNLKDITTRIVNILSDISKITQSSEIKNTSASYKQSLSFMSEALITKAS
SQ  LLRDLPESIVKLVSTNNLVSTLNSLPLTQDYRSKNLESLTDQIQDTLLNSIYQ
//
ID  Q9VCH5;
PN  Nuclear pore complex protein Nup96;
GN  Nup98;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome {ECO:0000269|PubMed:20144761}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20144760}. Nucleus membrane {ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:25197089}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52948}; Nucleoplasmic side {ECO:0000250|UniProtKB:P52948}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:25310983}. Nucleus {ECO:0000269|PubMed:28366641}. Note=Associates with transcriptionally active chromatin. {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:28366641}. [Nuclear pore complex protein Nup98]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:25310983}. [Nuclear pore complex protein Nup96]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:25310983}.
DR  UNIPROT: Q9VCH5;
DR  UNIPROT: B8A421;
DR  UNIPROT: Q6NP55;
DR  Pfam: PF04096;
DR  Pfam: PF13634;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Part of the nuclear pore complex (NPC) (PubMed:25197089). Required for MAD import as part of the Nup107-160 complex and required for nuclear export of Moe probably via its association with Rae1 (PubMed:20547758, PubMed:28554770). Plays a role in nuclear mRNA export (PubMed:28554770). Promotes cell antiviral response by up-regulating FoxK-dependent antiviral gene transcription (PubMed:25197089, PubMed:25852164). In germline stem cells, involved in their maintenance and division together with the TGF-Beta and EGFR signaling pathways (PubMed:21949861). In larval lymph glands, has a role in the maintenance of hematopoiesis by regulating Pvr expression (PubMed:25201876). {ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:21949861, ECO:0000269|PubMed:25197089, ECO:0000269|PubMed:25201876, ECO:0000269|PubMed:25852164, ECO:0000269|PubMed:28554770}. [Nuclear pore complex protein Nup98]: Part of the nuclear pore complex (NPC) (PubMed:25310983). In the nucleoplasm, binds to transcriptionally active chromatin with a preference for regulatory regions; co-localizes with RNA polymerase II in a RNA-independent manner and before transition into transcription elongation (PubMed:20144760, PubMed:20144761, PubMed:28366641). Plays a role in the transcriptional memory process by stabilizing enhancer-promoter loops and by mediating anchoring of chromatin to the nuclear pore complex region (PubMed:28366641). During larval development, interacts with trx and MBD-R2 and regulates transcription of developmental genes including ecdysone-responsive genes such as Eip74 and E23 (PubMed:20144761, PubMed:25310983, PubMed:28366641). {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:25310983, ECO:0000269|PubMed:28366641}. [Nuclear pore complex protein Nup96]: Part of the nuclear pore complex (NPC). {ECO:0000269|PubMed:25310983}.
DE  Reference Proteome: Yes;
DE  Interaction: Q24568; IntAct: EBI-9919289; Score: 0.35
DE  Interaction: Q9VRM7; IntAct: EBI-199532; Score: 0.00
DE  Interaction: Q9VYG2; IntAct: EBI-199536; Score: 0.00
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: P18431; IntAct: EBI-9925534; Score: 0.35
DE  Interaction: Q9V3G9; IntAct: EBI-26831975; Score: 0.49
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005700;
GO  GO:0005704;
GO  GO:0005703;
GO  GO:0031490;
GO  GO:0140585;
GO  GO:1990841;
GO  GO:0017171;
GO  GO:0008236;
GO  GO:0017056;
GO  GO:0071390;
GO  GO:0034605;
GO  GO:0030718;
GO  GO:0035080;
GO  GO:0035167;
GO  GO:0036098;
GO  GO:0051028;
GO  GO:0043922;
GO  GO:0030838;
GO  GO:0002230;
GO  GO:0010628;
GO  GO:0045944;
GO  GO:0060261;
GO  GO:0006606;
GO  GO:0006508;
GO  GO:0046822;
GO  GO:0035075;
GO  GO:0006405;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P52948};
SQ  MFGGAKPSFGATPAATSFGGFSGTTTTTPFGQSAFGKPAAPAFGNTSTFAAQPAQQSLFGAAATPAQPAGGLFGANTSTG
SQ  FGSTATAQPTAFGAFSQPQQTSNIFGSTQTAASTSLFGQSTLPAFGAAKPTMTAFGQTAAAQPTGSLFGQPAAATSTTGF
SQ  GGFGTSAPTTTNVFGSGTASAFAQPQATAVGASGVNTGTAVAKYQPTIGTDTLMKSGQANSVNTKQHCITAMKEFEGKSL
SQ  EELRLEDYMCGRKGPQAGNAPGAFGFGAQVTQPAQPASGGLFGSTAQPSTGLFGQTVTENKSMFGTTAFGQQPATNNAFG
SQ  AATQQNNFLQKPFGATTTTPFAAPAADASNPFGAKPAFGQGGSLFGQAPATSAAPAFGQTNTGFGGFGTTAGATQQSTLF
SQ  GATPAADPNKSAFGLGTAASAATTGFGFGAPATSTAGGGLFGNKPATSFAAPTFGATSTASTPFSNFGLNTSTAATGGGL
SQ  FNSGLNKPATSGFGGFGATSAAPLNFNAGNTGGSLFGNTAKPGGGLFGGGTTTLGGTGAAPTGGLFGGGTTSFGGVGGSL
SQ  GGGGFGMGTNNSLTGGIMGAQPTLGIMTPSHQPIHQQILARVTSPYGDSPIFKDLKLSSEADATRATNPAAQQAVLDLTS
SQ  NQYKISTSNNPAPMKVKALGSTLNRKSLFDGLEEFDASVEGFNLKPSAKRLVIKPKVKSVEGGNPSSSIGSAPNTPQSRP
SQ  KGATPNKERESFSGAIPSEPLPPAGNSPGATNGRESQDNGRRESWLHPNNLEKVRQHNIQTGMDQGSPHNSTLNELVPRK
SQ  PLDTYRPSSTVRLSVSTIPENPFEDQSSTIARRETFTSQQANESVLSNRSNEAEDSAANQSRLAIEAAAAEAADDESHPT
SQ  GIVLRRVGYYTIPSLDDLRSYLAEDGSCVVPNFTVGREGYGNVFFGKEMDVAGLNLDEIVHFRNKEIIIYPDDENKPPIG
SQ  QGLNRDAQVTLDQVWPLDKTKHEAIKDPQRLLEMDWEGKLRRVCDKNDTRFIEYRPETGSWVFRVKHFSKYGLGDSDEED
SQ  ELPTDPKKAKIATLEAQQRANAEKMTLNSLRQAQKISEDAARNLDPKALVAGVASGFRPMDDTAEFLLMDKTQFFQAGGN
SQ  SDFSMFDPPRQRPTITSPTAVLAQEMVGNEAHKMQLMKSSFFVEDNAPEDEPMETTGRLLRHRKFFNVEPLVWKDGASES
SQ  SSQYDFEHPSPALPISSSVSEASLMCDAHYEETSSMATGSIVAAVKETKFEMPVTKAFKFVCKPKVAPIKLRATTVPLPR
SQ  SIAYEMRDNWIADLGFYKGRSFKLSFGPQNSLVLPSTYNNMQNLKEFTGPSLPVSMVFAPRSATDLSPSVMQLVEFNMVK
SQ  GNEGFRESIIPHLEVQLNDCLSVNVEGSECPCIHPDSGTKLVSKHFSESLKQRNAGLKEDYSVSVWSLLFALWGDHDELV
SQ  DLEKNSHYMVMCRRNLLSEWLENTLLGKDLLSKKVSTHSYLEHMLDLLSCHRVNEACELAFSYDDANLALVLSQLSSGAV
SQ  FRLLMEEQLFAWQQSKSDKYIDLERLKMYMLAAGAPMMQSSHGAINLLENKNWLTALALQLWYFTAPTSSITDALNAYND
SQ  AFQAEECYAEPPKPSYRDAPTDTKKPVYDLRYHLLQLHSKRMHSLEETLNPITHTADAMDFRLSWLLLQTLRALGYRHCS
SQ  PLTEARLSVDFASQLENEGLWQWGIFVLLHIKQQTQRERAVQQMLQRNVSVSAKVALYAEERFIVEELGIPMSWVDYAKA
SQ  VKAGASGKHHLQAKYLLKAKHFATAHDVIFQHIAPDAIINGKMKYLHSLLIQFEDTEGSSIRVPNWANQGQIFLDFIDIS
SQ  AKFKQIRSVTNIADINARWENLKPQLSELCSRISLLPCPTSKHRLCQSEISQSLSCLVHGMCIVCPEMESSTVLKVALER
SQ  LPLPQEFASKELRIWLEELLDKIQNEPPFSERQQPTMMEI
//
ID  P52948;
PN  Nuclear pore complex protein Nup96;
GN  NUP98;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:11106761, ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:20407419, ECO:0000269|PubMed:28221134, ECO:0000269|PubMed:33360543}; Peripheral membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:11839768}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:33097660}. Nucleus, nucleoplasm {ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:28221134}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket (PubMed:11839768). Dissociates from the dissasembled NPC structure early during prophase of mitosis (PubMed:12802065). Colocalized with NUP153 and TPR to the nuclear basket of NPC (PubMed:11839768). Colocalized with DHX9 in diffuse and discrete intranuclear foci (GLFG-body) (PubMed:11839768, PubMed:28221134). {ECO:0000269|PubMed:11106761, ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:28221134}. Nucleus membrane {ECO:0000269|PubMed:11106761}. Note=(Microbial infection) Remains localized to the nuclear membrane after poliovirus (PV) infection. {ECO:0000269|PubMed:11106761}.
DR  UNIPROT: P52948;
DR  UNIPROT: Q8IUT2;
DR  UNIPROT: Q8WYB0;
DR  UNIPROT: Q96E54;
DR  UNIPROT: Q9H3Q4;
DR  UNIPROT: Q9NT02;
DR  UNIPROT: Q9UF57;
DR  UNIPROT: Q9UHX0;
DR  UNIPROT: Q9Y6J4;
DR  UNIPROT: Q9Y6J5;
DR  PDB: 1KO6;
DR  PDB: 2Q5X;
DR  PDB: 2Q5Y;
DR  PDB: 3MMY;
DR  PDB: 4OWR;
DR  PDB: 5A9Q;
DR  PDB: 6BZM;
DR  PDB: 7PEQ;
DR  PDB: 7VPG;
DR  PDB: 7VPH;
DR  Pfam: PF04096;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DR  OMIM: 601021;
DR  DisGeNET: 4928;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC (PubMed:33097660). May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed:28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed:28221134). {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:33097660}. (Microbial infection) Interacts with HIV-1 capsid protein P24 and nucleocapsid protein P7 and may thereby promote the integration of the virus in the host nucleus (in vitro) (PubMed:23523133). Binding affinity to HIV-1 CA-NC complexes bearing the capsid change Asn-74-Asp is reduced (in vitro) (PubMed:23523133). {ECO:0000269|PubMed:23523133}.
DE  Disease: Note=Chromosomal aberrations involving NUP98 have been found in acute myeloid leukemia. Translocation t(7;11)(p15;p15) with HOXA9 (PubMed:8563753). The chimera includes NUP98 intrinsic disordered regions which contribute to aberrant liquid-liquid phase separation puncta of the chimera in the nucleus. This phase-separation enhances the chimera genomic targeting and induces organization of aberrant three-dimensional chromatin structures leading to tumorous transformation (PubMed:34163069). Translocation t(11;17)(p15;p13) with PHF23 (PubMed:17287853). {ECO:0000269|PubMed:17287853, ECO:0000269|PubMed:34163069, ECO:0000269|PubMed:8563753}. Note=A chromosomal aberration involving NUP98 has been found in M0 type acute myeloid leukemia. Translocation t(4;11)(q23;p15) with RAP1GDS1. {ECO:0000269|PubMed:16419055}. Note=A chromosomal aberration involving NUP98 has been found in T-cell acute lymphocytic leukemia. Translocation t(4;11)(q23;p15) with RAP1GDS1. {ECO:0000269|PubMed:10477737, ECO:0000269|PubMed:10929031}. Note=A chromosomal aberration involving NUP98 has been found in M5 type acute myeloid leukemia. Translocation t(11;12)(p15;p13) with KDM5A. {ECO:0000269|PubMed:23531517}. Note=Chromosomal aberrations involving NUP98 have been found in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) with NSD1. Translocation t(8;11)(p11.2;p15) with WHSC1L1. {ECO:0000269|PubMed:16028218}. Note=Chromosomal aberrations involving NUP98 have been found in M7 type childhood acute myeloid leukemia. Translocation t(11;12)(p15;p13) with KDM5A. {ECO:0000269|PubMed:16419055, ECO:0000269|PubMed:23531517}. Note=A chromosomal aberration involving NUP98 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with TOP1. {ECO:0000269|PubMed:16028218}. Note=A chromosomal aberration involving NUP98 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(3;11)(q12.2;p15.4) with LNP1. {ECO:0000269|PubMed:16028218}. Note=A chromosomal aberration involving NUP98 is associated with pediatric acute myeloid leukemia (AML) with intermediate characteristics between M2-M3 French-American-British (FAB) subtypes. Translocation t(9;11)(p22;p15) with PSIP1/LEDGF. The chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1/LEDGF exon 4. {ECO:0000269|PubMed:16028218}. Note=A chromosomal aberration involving NUP98 has been identified in acute leukemias. Translocation t(6;11)(q24.1;p15.5) with CCDC28A. The chimeric transcript is an in-frame fusion of NUP98 exon 13 to CCDC28A exon 2. Ectopic expression of NUP98-CCDC28A in mouse promotes the proliferative capacity and self-renewal potential of hematopoietic progenitors and rapidly induced fatal myeloproliferative neoplasms and defects in the differentiation of the erythro- megakaryocytic lineage. {ECO:0000269|PubMed:16028218}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P03519; IntAct: EBI-7228174; Score: 0.53
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-7193058; Score: 0.61
DE  Interaction: P57740; IntAct: EBI-295747; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-295755; Score: 0.35
DE  Interaction: Q9H0J4; IntAct: EBI-1065782; Score: 0.00
DE  Interaction: Q9H8S9; IntAct: EBI-1070106; Score: 0.00
DE  Interaction: Q9BUJ2; IntAct: EBI-7228393; Score: 0.40
DE  Interaction: Q93009; IntAct: EBI-2513133; Score: 0.61
DE  Interaction: P24386; IntAct: EBI-2515120; Score: 0.40
DE  Interaction: Q80U93; IntAct: EBI-2555228; Score: 0.40
DE  Interaction: Q8BH74; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q6ZQH8; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: Q6PFD9; IntAct: EBI-2563676; Score: 0.40
DE  Interaction: Q8ZIC6; IntAct: EBI-2862339; Score: 0.00
DE  Interaction: P25054; IntAct: EBI-3437342; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-3962281; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-5322129; Score: 0.44
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: P21698; IntAct: EBI-6155965; Score: 0.35
DE  Interaction: Q9BY41; IntAct: EBI-6598094; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: Q9BW27; IntAct: EBI-9032422; Score: 0.40
DE  Interaction: Q16543; IntAct: EBI-9393294; Score: 0.35
DE  Interaction: P03367; IntAct: EBI-9872763; Score: 0.40
DE  Interaction: P45983; IntAct: EBI-10103723; Score: 0.35
DE  Interaction: Q6ZQN5; IntAct: EBI-11318220; Score: 0.35
DE  Interaction: Q12952; IntAct: EBI-11318689; Score: 0.35
DE  Interaction: Q9C009; IntAct: EBI-11319301; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11024237; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q9JJ94; IntAct: EBI-11072967; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6ZYL4; IntAct: EBI-11129915; Score: 0.35
DE  Interaction: Q9P1W9; IntAct: EBI-11134827; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-11148324; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-11152254; Score: 0.35
DE  Interaction: O43809; IntAct: EBI-11152364; Score: 0.35
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: E5LBS6; IntAct: EBI-14062727; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-21512742; Score: 0.35
DE  Interaction: Q96C01; IntAct: EBI-21554623; Score: 0.35
DE  Interaction: Q8N490; IntAct: EBI-21596986; Score: 0.35
DE  Interaction: Q8NBZ7; IntAct: EBI-21638319; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-21639337; Score: 0.35
DE  Interaction: Q6EMK4; IntAct: EBI-21651359; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: Q9UBP0; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: P78406; IntAct: EBI-15616283; Score: 0.90
DE  Interaction: Q8NFH3; IntAct: EBI-21865034; Score: 0.35
DE  Interaction: Q82506; IntAct: EBI-15620563; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: Q93079; IntAct: EBI-20923674; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-20923666; Score: 0.40
DE  Interaction: Q92623; IntAct: EBI-20934396; Score: 0.40
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-21256730; Score: 0.37
DE  Interaction: Q9UKE5; IntAct: EBI-21381008; Score: 0.00
DE  Interaction: B2RTY4; IntAct: EBI-25409153; Score: 0.35
DE  Interaction: Q8IW93; IntAct: EBI-25410221; Score: 0.35
DE  Interaction: Q8NFH4; IntAct: EBI-25482031; Score: 0.35
DE  Interaction: P0DTC6; IntAct: EBI-25491317; Score: 0.91
DE  Interaction: P52948; IntAct: EBI-25794584; Score: 0.40
DE  Interaction: Q13627; IntAct: EBI-26367331; Score: 0.35
DE  Interaction: P59634; IntAct: EBI-26377272; Score: 0.84
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.35
DE  Interaction: A0A3Q8B233; IntAct: EBI-26955178; Score: 0.35
DE  Interaction: E0XIZ7; IntAct: EBI-26955195; Score: 0.35
DE  Interaction: P53667; IntAct: EBI-28938421; Score: 0.35
DE  Interaction: Q9Y6S9; IntAct: EBI-28948011; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q9UII6; IntAct: EBI-27115954; Score: 0.27
DE  Interaction: P41212; IntAct: EBI-29015445; Score: 0.27
GO  GO:0005829;
GO  GO:0016604;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:1990904;
GO  GO:0003729;
GO  GO:0008139;
GO  GO:1990841;
GO  GO:0008236;
GO  GO:0017056;
GO  GO:0003713;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0048026;
GO  GO:0006606;
GO  GO:0006508;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFG
SQ  FGTSTGTANTLFGTASTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGSTSGSLFGPSSFTAAPTGT
SQ  TIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGL
SQ  FSSSTTNSGFAYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTQNTGFSFGNTSTIGQPSTNTMGLFG
SQ  VTQASQPGGLFGTATNTSTGTAFGTGTGLFGQTNTGFGAVGSTLFGNNKLTTFGSSTTSAPSFGTTSGGLFGNKPTLTLG
SQ  TNTNTSNFGFGTNTSGNSIFGSKPAPGTLGTGLGAGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTTTATLGFG
SQ  APQAPVALTDPNASAAQQAVLQQHINSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRV
SQ  RPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNRDSENLASPSEYPENGERFSFLSKP
SQ  VDENHQQDGDEDSLVSHFYTNPIAKPIPQTPESAGNKHSNSNSVDDTIVALNMRAALRNGLEGSSEETSFHDESLQDDRE
SQ  EIENNSYHMHPAGIILTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVV
SQ  VYLDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHF
SQ  SKYGLQDSDEEEEEHPSKTSTKKLKTAPLPPASQTTPLQMALNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVLD
SQ  TMLEESMPEDQEPVSASTHIASSLGINPHVLQIMKASLLTDEEDVDMALDQRFSRLPSKADTSQEICSPRLPISASHSSK
SQ  TRSLVGGLLQSKFTSGAFLSPSVSVQECRTPRAASLMNIPSTSSWSVPPPLTSVFTMPSPAPEVPLKTVGTRRQLGLVPR
SQ  EKSVTYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLNGSHELENHQIADSMEFGFLPNPVAVKPLTESPFKVHLEK
SQ  LSLRQRKPDEDMKLYQTPLELKLKHSTVHVDELCPLIVPNLGVAVIHDYADWVKEASGDLPEAQIVKHWSLTWTLCEALW
SQ  GHLKELDSQLNEPREYIQILERRRAFSRWLSCTATPQIEEEVSLTQKNSPVEAVFSYLTGKRISEACSLAQQSGDHRLAL
SQ  LLSQFVGSQSVRELLTMQLVDWHQLQADSFIQDERLRIFALLAGKPVWQLSEKKQINVCSQLDWKRSLAIHLWYLLPPTA
SQ  SISRALSMYEEAFQNTSDSDRYACSPLPSYLEGSGCVIAEEQNSQTPLRDVCFHLLKLYSDRHYDLNQLLEPRSITADPL
SQ  DYRLSWHLWEVLRALNYTHLSAQCEGVLQASYAGQLESEGLWEWAIFVLLHIDNSGIREKAVRELLTRHCQLLETPESWA
SQ  KETFLTQKLRVPAKWIHEAKAVRAHMESDKHLEALCLFKAEHWNRCHKLIIRHLASDAIINENYDYLKGFLEDLAPPERS
SQ  SLIQDWETSGLVYLDYIRVIEMLRHIQQVDCSGNDLEQLHIKVTSLCSRIEQIQCYSAKDRLAQSDMAKRVANLLRVVLS
SQ  LHHPPDRTSDSTPDPQRVPLRLLAPHIGRLPMPEDYAMDELRSLTQSYLRELAVGSL
//
ID  Q6PFD9;
PN  Nuclear pore complex protein Nup96;
GN  Nup98;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P52948}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52948}; Nucleoplasmic side {ECO:0000250|UniProtKB:P52948}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P52948}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P52948}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket. Dissociates from the dissasembled NPC structure early during prophase of mitosis. Colocalized with NUP153 and TPR to the nuclear basket of NPC. Colocalized with DHX9 in diffuse and discrete intranuclear foci (GLFG-body). Remains localized to the nuclear membrane after poliovirus (PV) infection. {ECO:0000250|UniProtKB:P52948}.
DR  UNIPROT: Q6PFD9;
DR  UNIPROT: Q68G59;
DR  PDB: 3TKN;
DR  PDB: 7BYF;
DR  Pfam: PF04096;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes. Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body). {ECO:0000250|UniProtKB:P52948}.
DE  Reference Proteome: Yes;
DE  Interaction: A8CG34; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: O15504; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P12270; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P35658; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P46060; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-2563676; Score: 0.40
DE  Interaction: P55735; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: P57740; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: P62826; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P63165; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P78406; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q12769; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q14974; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q53GS7; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P39429; IntAct: EBI-655473; Score: 0.37
DE  Interaction: Q8NFH4; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q9BW27; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q8WYP5; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q8WUM0; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q8NFH3; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: Q96EE3; IntAct: EBI-2563676; Score: 0.40
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: P18754; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P32322; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q7Z3B4; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q9NXE4; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: O14715; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: E9PF10; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q15942; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q15165; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q99666; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: O95084; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q9BTX1; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q9UQN3; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q02878; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q12789; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q9UKK6; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q6NUQ4; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P61956; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q96SK2; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q9HC62; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q69YH5; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P51798; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q5JRG1; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P11172; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q9UKX7; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8TEM1; IntAct: EBI-10994876; Score: 0.35
GO  GO:0000776;
GO  GO:0016604;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:1990904;
GO  GO:0003729;
GO  GO:0008139;
GO  GO:0042277;
GO  GO:1990841;
GO  GO:0008236;
GO  GO:0017056;
GO  GO:0003713;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0006913;
GO  GO:0048026;
GO  GO:0006606;
GO  GO:0006508;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P52948};
SQ  MFNKSFGTPFGGSTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFG
SQ  FGTSTGTSNSLFGTASTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGSTSGSLFGPSSFTAAPTGT
SQ  TIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGGGTTAGLFGSSPATSSATGL
SQ  FSSSTTNSAFSYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTPNTGFSFGNTSTLGQPSTNTMGLFG
SQ  VTQASQPGGLFGTATNTSTGTAFGTGTGLFGQPNTGFGAVGSTLFGNNKLTTFGTSTTSAPSFGTTSGGLFGNKPTLTLG
SQ  TNTNTSNFGFGTNNSGSSIFGSKPAAGTLGTGLGTGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTSTAILGFG
SQ  APQAPVALTDPNASAAQQAVLQQHLNSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRV
SQ  RPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNHDSEDLASPSEYPENGERFSFLSKP
SQ  VDENNQQDGEDDSLVSRFYTNPIAKPIPQTPESVGNKNNSSSNVEDTIVALNMRAALRNGLEGSSEETSFHDESLQDDRE
SQ  EIENNAYHIHPAGIVLTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVI
SQ  VYVDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHF
SQ  SKYGLQDSDEEEEEHPPKTTSKKLKTAPLPPAGQATTFQMTLNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVPD
SQ  SVLEESVPEDQEPVSASTHIASSLGINPHVLQIMKASLLVDEEDVDAMDQRFGHIPSKGETVQEICSPRLPISASHSSKS
SQ  RSIVGGLLQSKFASGTFLSPSASVQECRTPRTSSRMNIPSTSPWSVPLPLATVFTVPSPAPEVQLKTVGIRRQPGLVPLE
SQ  KSITYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLHGSHELENHQVADSMEYGFLPNPVAVKSLSESPFKVHLEKL
SQ  GLRQRKLDEDLQLYQTPLELKLKHSTVHVDELCPLIVPNPGVSVIHDYADWVKDSPGDFLELPIVKHWSLTWTLCEALWG
SQ  HLKELDGQLDEPSEYIQTLERRRAFSRWLSHTAAPQIEEEVSLTRRDSPVEAVFSYLTGSRISGACCLAQQSGDHRLALL
SQ  LSQLVGSQSVRELLTMQLADWHQLQADSFIHDERLRIFALLAGKPVWQLSEQKQINVCSQLDWKRTLAIHLWYLLPPTAS
SQ  ISRALSMYEEAFQNTPEGDKYACSPLPSYLEGCGCMVEEEKDSRRPLQDVCFHLLKLYSDRHYELNQLLEPRSITADPLD
SQ  YRLSWHLWEVLRALNYTHLSEQCEGVLQASYAGQLESEGLWEWAIFVFLHIDNSGMREKAVRELLTRHCQLSETPESWAK
SQ  EAFLTQKLCVPAEWIHEAKAVRAHMESNKHLEALYLFKAGHWNRCHKLVIRHLASDAIINENYDYLKGFLEDLAPPERSS
SQ  LIQDWETSGLVYLDYIRVIEMLHRIQQVDCSGYELEHLHTKVTSLCNRIEQIPCYNAKDRLAQSDMAKRVANLLRVVLSL
SQ  QHAPDATSNSTPDPQRVPLRLLAPHIGRLPMPEDYALEELRGLTQSYLRELTVGSQ
//
ID  P49793;
PN  Nuclear pore complex protein Nup96;
GN  Nup98;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:11839768}; Peripheral membrane protein {ECO:0000269|PubMed:10087256}; Nucleoplasmic side {ECO:0000269|PubMed:10087256}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10087256}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10087256}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket (PubMed:10087256). Dissociates from the dissasembled NPC structure early during prophase of mitosis (By similarity). Colocalizes with NUP153 to the nuclear basket of NPC (By similarity). Colocalizes with TPR to the nuclear basket of NPC (PubMed:10087256, PubMed:11839768). Colocalized with DHX9 in diffuse and discrete intranuclear foci (GLFG- body) (By similarity). Remains localized to the nuclear membrane after poliovirus (PV) infection (By similarity). {ECO:0000250|UniProtKB:P52948, ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:11839768}.
DR  UNIPROT: P49793;
DR  UNIPROT: D3ZMW4;
DR  Pfam: PF04096;
DR  Pfam: PF12110;
DR  PROSITE: PS51434;
DE  Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. {ECO:0000250|UniProtKB:P52948}. Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes. Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body). {ECO:0000250|UniProtKB:P52948}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0016604;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:1990904;
GO  GO:0003729;
GO  GO:0008139;
GO  GO:0042277;
GO  GO:1990841;
GO  GO:0008236;
GO  GO:0017056;
GO  GO:0003713;
GO  GO:0051028;
GO  GO:0051292;
GO  GO:0048026;
GO  GO:0006606;
GO  GO:0006508;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10087256};
SQ  MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFG
SQ  FGTSTGTSNSLFGTANTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGNTSGSLFGPSSFTAAPTGT
SQ  TIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGL
SQ  FSSSTTNSAFSYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTPNTGFSFGNTSTLGQPSTNTMGLFG
SQ  VTQASQPGGLFGTATNTSTGTAFGTGTGLFGQPNTGFGAVGSTLFGNNKLTTFGTSTTSAPSFGTTSGGLFGNKPTLTLG
SQ  TNTNTSNFGFGTNNSGSSIFGSKPAAGTLGTGLGTGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTSTAILGFG
SQ  APQAPVALTDPNASAAQQAVLQQHLNSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRV
SQ  RPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNHDSEDLASPSEYPENGERFSFLSKP
SQ  VDENHQQDGDDDSLVSRFYTNPIAKPIPQTPESAGNKNNSSSNVEDTFIALNMRAALRNGLEGSSEETSFHDESLQDDRD
SQ  EIENSAFQIHPAGIVLTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVI
SQ  VYVDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHF
SQ  SKYGLQDSDEEEEEHPPKTTSKKLKTAPLPPAGQATTFQMTLNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVPD
SQ  SVLEESVPEDQEPVSASTQIASSLGINPHVLQIMKASLLVDEEDVDAMEQRFGHFPSRGDTAQEICSPRLPISASHSSKS
SQ  RSIVGGLLQSKFASGTFLSPSASVQECRTPRTSSLMNVPSTSPWSVPLPLATVFTVPSPAPEVPLKTVGIRRQPGLVPLE
SQ  KSITYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLHGSHELENHQVAESMEYGFLPNPVAVKSLSESPFKVHLEKL
SQ  GLRQRKLDEDLQLYQTPLELKLKHSTVHVDELCPLIVPNPGVSVIHGYADWVKKSPRDLLELPIVKHWSLTWTLCEALWG
SQ  HLKELDSQLDEPSEYIQTLERRRAFSRWLSHTAAPQIEEEVSLTRRDSPIEAVFSYLTGSRISEACCLAQQSGDHRLALL
SQ  LSQLVGSQSVRELLTMQLADWHQLQADSFIHDERLRIFALLAGKPVWQLSEQKQINVCSQLDWKRTLAIHLWYLLPPTAS
SQ  ISRALSMYEEAFQNTCEGDKYACPPLPSYLEGSGCVVEEEKDPQRPLQDVCFHLLKLYSDRHYGLNQLLEPRSITADPLD
SQ  YRLSWHLWEVLRALNYTHLSEQCEGVLQASYAGQLESEGLWEWAIFVFLHIDNSGMREKAVRELLTRHCQLSETPESWAK
SQ  ETFLTQKLCVPAEWIHEAKAVRAHMESNKHLEALYLFKAGHWNRCHKLVVRHLASDAIINENYDYLKGFLEDLAPPERSS
SQ  LIQDWETSGLVYLDYIRVIEMLHRIQQVDCSGYELEHLHTKVTSLCNRIEQIPCYNAKDRLAQSDMAKRVANLLRVVLSL
SQ  QHTPDATSNSTPDPQRVPLRLLAPHIGRLPMPEDYALEELRGLTQSYLRELTVGSQ
//
ID  O60356;
PN  Nuclear protein 1;
GN  NUPR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10092851, ECO:0000269|PubMed:16300740}. Cytoplasm {ECO:0000269|PubMed:16300740}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16300740}.
DR  UNIPROT: O60356;
DR  UNIPROT: B2R5C4;
DR  UNIPROT: O60357;
DR  UNIPROT: Q6FGG3;
DR  Pfam: PF10195;
DR  OMIM: 614812;
DR  DisGeNET: 26471;
DE  Function: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses (PubMed:16478804, PubMed:19650074, PubMed:16300740, PubMed:19723804, PubMed:11056169, PubMed:22858377, PubMed:11940591, PubMed:18690848, PubMed:22565310, PubMed:20181828, PubMed:30451898). Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (PubMed:18690848). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (PubMed:22565310). Negatively regulates apoptosis through interaction with PTMA (PubMed:16478804). Inhibits autophagy- induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter (PubMed:20181828). Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity). Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (By similarity). Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (PubMed:19650074). Coactivator of PAX2 transcription factor activity, both by recruiting EP300 to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (PubMed:11940591). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (PubMed:16300740). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (PubMed:19723804). Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (By similarity). Also required for LHB expression and ovarian maturation (By similarity). Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity). {ECO:0000250|UniProtKB:O54842, ECO:0000250|UniProtKB:Q9WTK0, ECO:0000269|PubMed:11056169, ECO:0000269|PubMed:11940591, ECO:0000269|PubMed:16300740, ECO:0000269|PubMed:16478804, ECO:0000269|PubMed:18690848, ECO:0000269|PubMed:19650074, ECO:0000269|PubMed:19723804, ECO:0000269|PubMed:20181828, ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:22858377, ECO:0000269|PubMed:30451898}.
DE  Reference Proteome: Yes;
DE  Interaction: P00352; IntAct: EBI-3908806; Score: 0.37
DE  Interaction: Q15761; IntAct: EBI-3918086; Score: 0.37
DE  Interaction: Q01105; IntAct: EBI-3918102; Score: 0.37
DE  Interaction: Q9H221; IntAct: EBI-3924120; Score: 0.37
DE  Interaction: Q02383; IntAct: EBI-21829397; Score: 0.35
DE  Interaction: P04279; IntAct: EBI-21829397; Score: 0.35
DE  Interaction: P35637; IntAct: EBI-15569761; Score: 0.37
DE  Interaction: P55036; IntAct: EBI-15569710; Score: 0.37
DE  Interaction: P06454; IntAct: EBI-15569727; Score: 0.67
DE  Interaction: Q68DK7; IntAct: EBI-15569812; Score: 0.37
DE  Interaction: Q15233; IntAct: EBI-15569848; Score: 0.37
DE  Interaction: P67812; IntAct: EBI-15569865; Score: 0.37
DE  Interaction: P62826; IntAct: EBI-15569882; Score: 0.37
DE  Interaction: Q15691; IntAct: EBI-15569899; Score: 0.37
DE  Interaction: Q9P2W9; IntAct: EBI-15569916; Score: 0.37
DE  Interaction: Q9Y448; IntAct: EBI-15569933; Score: 0.37
DE  Interaction: P43487; IntAct: EBI-15569950; Score: 0.37
DE  Interaction: O60506; IntAct: EBI-15569986; Score: 0.37
DE  Interaction: Q13765; IntAct: EBI-15570037; Score: 0.37
DE  Interaction: Q99547; IntAct: EBI-15570020; Score: 0.37
DE  Interaction: P62945; IntAct: EBI-15570054; Score: 0.37
DE  Interaction: Q494V2; IntAct: EBI-25918043; Score: 0.56
DE  Interaction: O15534; IntAct: EBI-25918035; Score: 0.56
DE  Interaction: P17655; IntAct: EBI-25918027; Score: 0.56
GO  GO:0005737;
GO  GO:0045171;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032993;
GO  GO:0010698;
GO  GO:0003682;
GO  GO:0003677;
GO  GO:0060090;
GO  GO:0003713;
GO  GO:0002526;
GO  GO:0044346;
GO  GO:0048144;
GO  GO:0042771;
GO  GO:0008584;
GO  GO:0043066;
GO  GO:1902902;
GO  GO:0010507;
GO  GO:0010667;
GO  GO:0045786;
GO  GO:0008285;
GO  GO:0043433;
GO  GO:1904036;
GO  GO:0050680;
GO  GO:0048147;
GO  GO:0045820;
GO  GO:0062099;
GO  GO:1904691;
GO  GO:0045787;
GO  GO:2000271;
GO  GO:2001244;
GO  GO:0150078;
GO  GO:0043525;
GO  GO:1903862;
GO  GO:1901800;
GO  GO:0031401;
GO  GO:0006473;
GO  GO:0065003;
GO  GO:0010506;
GO  GO:2000194;
GO  GO:1905897;
GO  GO:0009636;
GO  GO:0035914;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATFPPATSAPQQPPGPEDEDSSLDESDLYSLAHSYLGGGGRKGRTKREAAANTNRPSPGGHERKLVTKLQNSERKKRGA
SQ  RR
//
ID  Q9WTK0;
PN  Nuclear protein 1;
GN  Nupr1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O60356}. Cytoplasm {ECO:0000250|UniProtKB:O60356}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O60356}.
DR  UNIPROT: Q9WTK0;
DR  UNIPROT: Q9D756;
DR  Pfam: PF10195;
DE  Function: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses (PubMed:11896600, PubMed:19723804, PubMed:23900510, PubMed:27451286, PubMed:22565310, PubMed:20181828). Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (By similarity). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (PubMed:22565310). Negatively regulates apoptosis through interaction with PTMA (By similarity). Inhibits autophagy- induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter (PubMed:20181828). Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (PubMed:11896600). Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (By similarity). Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (By similarity). Coactivator of PAX2 transcription factor activity, both by recruiting the EP300 cofactor to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (By similarity). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (By similarity). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (PubMed:19723804). Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (PubMed:23900510). Also required for LHB expression and ovarian maturation (PubMed:18495683). Exacerbates CNS inflammation and demyelination upon cuprizone treatment (PubMed:16374777). {ECO:0000250|UniProtKB:O54842, ECO:0000250|UniProtKB:O60356, ECO:0000269|PubMed:11896600, ECO:0000269|PubMed:16374777, ECO:0000269|PubMed:18495683, ECO:0000269|PubMed:19723804, ECO:0000269|PubMed:20181828, ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:23900510, ECO:0000269|PubMed:27451286}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0045171;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032993;
GO  GO:0010698;
GO  GO:0003682;
GO  GO:0003677;
GO  GO:0003713;
GO  GO:0002526;
GO  GO:0044346;
GO  GO:0048144;
GO  GO:0042771;
GO  GO:0008584;
GO  GO:0043066;
GO  GO:1902902;
GO  GO:0010507;
GO  GO:0010667;
GO  GO:0045786;
GO  GO:0008285;
GO  GO:0043433;
GO  GO:1904036;
GO  GO:0050680;
GO  GO:0048147;
GO  GO:0045820;
GO  GO:0062099;
GO  GO:1904691;
GO  GO:0045787;
GO  GO:2000271;
GO  GO:2001244;
GO  GO:0150078;
GO  GO:0043525;
GO  GO:1903862;
GO  GO:1901800;
GO  GO:0031401;
GO  GO:0006473;
GO  GO:0065003;
GO  GO:0010506;
GO  GO:2000194;
GO  GO:1905897;
GO  GO:0009636;
GO  GO:0035914;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATLPPTANPSQQPLNLEDEDGILDEYDQYSLAHPCVVGGGRKGRTKREAAANTNRPSPGGHERKLLTKFQNSERKKAWR
//
ID  O54842;
PN  Nuclear protein 1;
GN  Nupr1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O60356}. Cytoplasm {ECO:0000250|UniProtKB:O60356}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O60356}.
DR  UNIPROT: O54842;
DR  Pfam: PF10195;
DE  Function: Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses (PubMed:27031958, PubMed:28694771, PubMed:20181828). Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (By similarity). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (By similarity). Negatively regulates apoptosis through interaction with PTMA (By similarity). Inhibits autophagy- induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter (PubMed:20181828). Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity). Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (PubMed:28694771, PubMed:27031958). Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (By similarity). Coactivator of PAX2 transcription factor activity, both by recruiting the EP300 cofactor to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (By similarity). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (By similarity). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (By similarity). Negatively regulates beta cell proliferation via inhibition of cell- cycle regulatory genes expression through the suppression of their promoter activities (By similarity). Also required for LHB expression and ovarian maturation (By similarity). Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity). {ECO:0000250|UniProtKB:O60356, ECO:0000250|UniProtKB:Q9WTK0, ECO:0000269|PubMed:20181828, ECO:0000269|PubMed:27031958, ECO:0000269|PubMed:28694771}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032993;
GO  GO:0010698;
GO  GO:0003682;
GO  GO:0003677;
GO  GO:0003713;
GO  GO:0002526;
GO  GO:0044346;
GO  GO:0048144;
GO  GO:0042771;
GO  GO:0008584;
GO  GO:0043066;
GO  GO:1902902;
GO  GO:0010507;
GO  GO:0010667;
GO  GO:0045786;
GO  GO:0008285;
GO  GO:0043433;
GO  GO:1904036;
GO  GO:0050680;
GO  GO:0048147;
GO  GO:0045820;
GO  GO:0062099;
GO  GO:1904691;
GO  GO:0043065;
GO  GO:0045787;
GO  GO:2000271;
GO  GO:2001244;
GO  GO:0150078;
GO  GO:0043525;
GO  GO:1903862;
GO  GO:1901800;
GO  GO:0031401;
GO  GO:0006473;
GO  GO:0065003;
GO  GO:0010506;
GO  GO:2000194;
GO  GO:1905897;
GO  GO:0009636;
GO  GO:0035914;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATLPPTAHTSQQPVNIEDEDGILDEYDQYSLAQSYVVGGGRKGRTKREAAANTNRPSPGGHERKLLTKFQNSERKKAWR
//
ID  Q759K4;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q759K4;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0043007;
GO  GO:0007096;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPKHHTFATKLEDLVLTSMSFRMSKHQAHPIEPEDVIREESEDFYSDEEEYKETWSRWALQLLSSSPYDLYLIVNENFES
SQ  INWDLKAKTLARPLGGTMTFLFFTVRLLQDNVIKPNYHKINRTTDGFDFSRSATLREYDYFSKYQHGASWSSANWRVNSL
SQ  SILDTLLKCLYILLLVSNSVLTYKFLFGYFLKYSLFHSAQPPASNNLTKKSLHDLAYRSATDVSRGSLWTLIRYTFFQRG
SQ  RVQEEKPTDEFYYEIKKWCPSSFLTALFASFPPISVWFMAFSDITFVSLLPVILTQYLFWYVIFDCYEDRIKDELAIFKG
SQ  MAAEYNNKVMKPKLSAQTQDAMVDATMYGQEFVQFYPSYSTARSGVFITHSLCGDVIKEKYNQRTKAFEDIPTGSHSQNI
SQ  IRYSRNERLYHSVFPQNPLKKINGAAMSVNPMSFNRSPTYGGRYGTPPSRSHGSGQTYSSTSAPTSPMLKNRRAIPTDHS
SQ  TGGNISGGNYVEYTSNDVHGEPPRRHSTSPLKRDITSSAGREDNHLAFGVNSPNIRSRTVDVKKNLHTHTTVVCPKSDLD
SQ  TSQLSSKQSSISPFKLSRRGSIESRPPFR
//
ID  Q6FL09;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6FL09;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFSWLIPDIPELFLTISVWFRLQGWEDNTKLGFIIGNTLTTIFYILRLAQDTLLAGVSRKLIRDYELFDLSKSETLLSDP
SQ  AFSSYHDVLFNKHHSTANASSYNKRVRKVTSTVYWSTYFLLLLSCYTCYRLFNTYKVYRIYYLKDLNLDKHPSLKKIEPD
SQ  YEVDEKLLKTSLKSKLLSRFIRLLQLQDEVETELPKVTEHYTLNKWDPSKLIISLSTSFSPTIIICLMYTNVTFLTVIPI
SQ  IIHQGIFYFMIWNRYEERFKDDALLMRENYLQYDTKYVKPLKQIMYQDVMTDTATISDGGFTKFFPVSKSTLFKHHEMSG
SQ  DVIIERYNKKSREFENVTDIIKPHHHINNTVKILPPTIRKDHKTNRYDHRQQSILKDRKFNIDSNEPQIINALTTAIPSR
SQ  SFFNNNPSGSNDDNCSGIKVRSSPTRETFFPATPLRKK
//
ID  Q6CKY2;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6CKY2;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAFWRNRHESPAISQERSPSPDRFQNSEDIREDNNNYNEDEKLGWFASFMGMFSLPYDWYLSINEDIAVIDWDSKSNSVA
SQ  WPLGNVLTFLFFSVRLLQDNVIAPNINKLTHSDDAFDFSKSKNLQKYDYFQQYGGSASSSENLYYKMLRQLHRLFYLLTV
SQ  LLLITNISVTYRYLFAHFQTYSIFYWKTVPKSKNVTKKSLHDLNHTYVEDAKRDSLWGMIKYLLFNGSHDDETNRAHYYE
SQ  LRKWTPSRFLTSFFVSFSPIAFCFLWMTDVTFKTLIPIIIHQYVLWFIVIDRYEQKLKDEQILSMSSVAELNSKVIQPKM
SQ  NVLKQDAMVDATPYNDGIVYFYPAYTTTRSHVFATHTLSGKLSKEKYNPRTDSFEDANSQRTENYVRFSYHHPKSINGAY
SQ  VRESYPSRQHSPRLSPSRYSHLQSGNTPSAPSTPLLIPSQQPHFDHSMLANASRNHNISERRNSHSPIKQHFANRLLNYP
SQ  DETNDSIPDVSDDRFRMDDRFRRGRQGYFNRSPDINSGTLHYDDGDDDDNRISKSPFRNSSSSPFR
//
ID  C5E3S7;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  559295;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: C5E3S7;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTFRLSRFESPLIEDDGESRASLLGYSPENELYTDVDENRESRFRRFMSFISSSPYDMFLAINEHVESIDWDSKASTIAG
SQ  PLGNFFTCSLYTARLLQDSLIRPNQQKLDKKRDSFDLSRSEILRKFEYLSQVPKSGVVVTHLNWYWKFLTFLNVALQITV
SQ  GFLILINLFVAYKFLIGHFQVYSLFYTKTSPRSKNVTKRSLSDLSFKSLEEVTNSSLWTMIRYMFVRKRLIIKDAPKGKY
SQ  YYQLRKWTPGKFYTALFSAFSPISVIFLLVTEVSFKTALAVIGHQYILFLVLFKRYESRLDDEACLAKAHFEEINEKVIK
SQ  PKTTIKTQDAMVDATTYGGGAAFFPSFTTTRSHIFQTHAVTGDIITERYNPETRNFEDVENTGRAKNYISQIQGVSHGQQ
SQ  VVSRSKAMNGATARPQFFSRQPSPSKIGTPSIILNYRTSPFSAPTTPTLKPVNGVQNGQSIFRNSPDPSKANSLNCDTSH
SQ  LSRNNTLSRLRRNSVSPTKSGNYCSASGMRAIHKSNFGADSSVSYSMEAPSNELPFEEVARRGRHPFEITASRDLPAGRS
SQ  SAVSSRHSSISPFKGNTSFAGRESLDSRPPFR
//
ID  A7TH24;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  436907;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A7TH24;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNGLDDENQIDERDHYTDDGDYEIDIDSMNMFKSLYYEMMAYFSDLQMHLGEHLMAIDWDMKCKSIAEPVGNCLTALFYI
SQ  IRLLQDTLLSNYKDVYVSTEAFDLSKSTTLQEFPFLIRFVEVSKTKNLQNAKYIKKKTFMFYFDKLLLFLMILILSTNAY
SQ  ISWTFIWRNFKTYSLLYVVDRPNSKNVTKCSRTDLDQSYMENVSYGSYWTMLSYYIRNFRKKDDLEDEITTVKQKTPNVN
SQ  EKDYYYQLKKWSPSKFLTSLFCSFSPTCLVFLILSDVSFTTSIAVILHQFIFKYVVFEGYESRINDESIIHSAMISEINQ
SQ  KFVEPRLSKKVQDAKIDATPEGKVYRTEFFPSLTNCKSNLFNRHDLKGRSITESYNDRIKEFEIVTNTNNETHNVIKVVK
SQ  K
//
ID  B3LGY4;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  285006;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: B3LGY4;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGSNDLINEAYDDSEVVGEERESKSAWMKRWYQLLTSPLDLQLVINEKLEMINWDAYAKSLAKPLGNFLTILFFIIRLLQ
SQ  DNLIKPNYYKLNVKSGAFDLSKSNKLKEFDYLWEISSSFQNSNQFYAFQSWYFVTLRFLNNLFRFTIFILLSLNLYVSCK
SQ  FMFGYFKTYNLFHLKKEFNSPNLTKHNLKDLSKEYYEDIYKQSLWSMLKHFFRGSRDDGPHVNQNEDEIFFQLRKWIPTN
SQ  FMINLFVSFSPTAIVFLSFSDVSFTSAIAIVFHQYILDYIITKRFQRSVDDDLILSSAALQEYEDKHIMARINQCSNIDT
SQ  LSSAMGTRSKTPRIFTTHSLCGEEIREVYNYEKREFEALPKMTESVPGSRETRIKDYGGISQVSDNQSHPIGFHYSPRMS
SQ  PYYRDKVLDNNLAQSSSNENLEKGGAFLPNQDQNRPSKSLSPLRKTPLSARQKRFEGSEFNVLNKNDINSILRSPKKKKN
SQ  YHKR
//
ID  C7GJM5;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  574961;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: C7GJM5;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGSNDLINEAYDDSEVVGEERESKSAWMKRWYQLLTSPLDLQLVINEKLEMINWDAYAKSLAKPLGNFLTILFFIIRLLQ
SQ  DNLIKPNYYKLNVKSGAFDLSKSNKLKEFDYLWEISSSFQNSNQFYAFQSWYFVTLRFLNNLFRFTIFILLSLNLYVSCK
SQ  FMFGYFKTYNLFHLKKEFNSPNLTKHNLKDLSKEYYEDIYKQSLWSMLKHFFRGSRDDGPHVNQNEVEIFFQLRKWIPTN
SQ  FIINLFVSFSPTAIVFLSFSDVSFTSAIAIVFHQYILDYIITKRFQRSVDDDLILSSAALQEYEDKHIMARINQCSNIDT
SQ  LSSAMGTRSKTPRIFTTHSLCGEEIREVYNYEKREFEALPKMTESVPGSRETRIKDYGGISQVSDNQSHPIGFHYSPRMS
SQ  PYYRDKVLDNNLAQSSSNENLEKGGAFLPNQDQNRPSKSLSPLRKTPLSARQKRFEGSEFNVLNKNDINSILRSPKKKKN
SQ  YHKR
//
ID  A6ZXN8;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A6ZXN8;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGSNDLINEAYDDSEVVGEERESKSAWMKRWYQLLTSPLDLQLVINEKLEMINWDAYAKSLAKPLGNFLTILFFIIRLLQ
SQ  DNLIKPNYYKLNVKSGAFDLSKSNKLKEFDYLWEISSSFQNSNQFYAFQSWYFVTLRFLNNLFRFTIFILLSLNLYVSCK
SQ  FMFGYFKTYNLFHLKKEFNSPNLTKHNLKDLSKEYYEDIYKQSLWSMLKHFFRGSRDDGPHVNQNEVEIFFQLRKWIPTN
SQ  FMINLFVSFSPTAIVFLSFSDVSFTSAIAIVFHQYILDYIITKRFQRSVDDDLILSSAALQEYEDKHIMARINQCSNIDT
SQ  LSSAMGTRSKTPRIFTTHSLCGEEIREVYNYEKREFEALPKMTESVPGSRETRIKDYGGISQVSDNQSHPIGFHYSPRMS
SQ  PYYRDKVLDNNLAQSSSNENLEKGGAFLPNQDQNRPSKSLSPLRKTPLSARQKRFEGSEFNVLNKNDINSILRSPKKKKN
SQ  YHKR
//
ID  C8Z6L4;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  643680;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: C8Z6L4;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGSNDLINEAYDDSEVVGEERESKSAWMKRWYQLLTSPLDLQLVINEKLEMINWDAYAKSLAKPLGNFLTILFFIIRLLQ
SQ  DNLIKPNYYKLNVKSGAFDLSKSNKLKEFDYLWEISSSFQNSNQFYAFQSWYFVTLRFLNNLFRFTIFILLSLNLYVSCK
SQ  FMFGYFKTYNLFHLKKEFNSPNLTKHNLKDLSKEYYEDIYKQSLWSMLKHFFRGSRDDGPHVNQNEVEIFFQLRKWIPTN
SQ  FMINLFVSFSPTAIVFLSFSDVSFTSAIAIVFHQYILDYIITKRFQRSVDDDLILSSAALQEYEDKHIMVRINQCSNIDT
SQ  LSSAMGTRSKTPRIFTTHSLCGEEIREVYNYEKREFEALPKMTESVPGSRETRIKDYGGISQVSDNQSHPIGFHYSPRMS
SQ  PYYRDKVLDNNLAQSSSNENLEKGGAFLPNQDQNRPSKSLSPLRKTPLSARQKRFEGSEFNVLNKNDINSILRSPKKKKN
SQ  YHKR
//
ID  Q12066;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: Q12066;
DR  UNIPROT: D6VRQ9;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability. {ECO:0000269|PubMed:18997772}.
DE  Reference Proteome: Yes;
DE  Interaction: Q03707; IntAct: EBI-795996; Score: 0.35
DE  Interaction: Q12066; IntAct: EBI-391962; Score: 0.55
DE  Interaction: Q06169; IntAct: EBI-391965; Score: 0.55
DE  Interaction: P40857; IntAct: EBI-856651; Score: 0.00
DE  Interaction: P25651; IntAct: EBI-977936; Score: 0.55
DE  Interaction: Q04087; IntAct: EBI-2212766; Score: 0.40
DE  Interaction: P11484; IntAct: EBI-3698627; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3717538; Score: 0.35
DE  Interaction: Q04947; IntAct: EBI-16254776; Score: 0.00
DE  Interaction: P40582; IntAct: EBI-16254796; Score: 0.00
DE  Interaction: P25087; IntAct: EBI-16254836; Score: 0.00
DE  Interaction: Q12402; IntAct: EBI-16254856; Score: 0.00
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0043007;
GO  GO:0007096;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGSNDLINEAYDDSEVVGEERESKSAWMKRWYQLLTSPLDLQLVINEKLEMINWDAYAKSLAKPLGNFLTILFFIIRLLQ
SQ  DNLIKPNYYKLNVKSGAFDLSKSNKLKEFDYLWEISSSFQNNNQFYAFQSWYFVTLRFLNNLFRFTIFILLSLNLYVSCK
SQ  FMFGYFKTYNLFHLKKEFNSPNLTKHNLKDLSKEYYEDIYKQSLWSMLKHFFRGSRDDGPHVNQNEDEIFFQLRKWIPTN
SQ  FMINLFVSFSPTAIVFLSFSDVSFTSAIAIVFHQYILDYIITKRFQRSVDDDLILSSAALQEYEDKHIMARINQCSNIDT
SQ  LSSAMGTRSKTPRIFTTHSLCGEEIREVYNYEKREFEALPKMTESVPGSRETRIKDYGGISQVSDHQSHPIGFHYSPRMS
SQ  PYYRDKVLDNNLAQSSSNENLEKGGAYLPNQDQNRPSKSLSPLRKTPLSARQKRFEGSEFNVLNKNDINSILRSPKKKKN
SQ  YHKR
//
ID  C5DQ18;
PN  Nuclear rim protein 1;
GN  NUR1;
OS  559307;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: C5DQ18;
DR  Pfam: PF10332;
DE  Function: Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLRISKDVSVSVNTADLLPEDDGFDRVDGDNRGWFSVFLGLFNTHPSDWNIALNEAIETIDWDSKSITLAQPLGNFFTF
SQ  AFYVVRLLQLSLIKPNLSRINEKTDHFDLSKSEMLKKYEYLYHFTNDKNQSVGNVYYRFLGRLGKFFDICIVLLTFTNGF
SQ  ITYKFFWGNFKMYCLFYLKKGPHLRNVTKASLQKLGQDDDDGSLWSSLRYFWNGTKDKEGSTDDRDDDDGDIHYKLFKWT
SQ  PSQFITMLFVSFAPTAVVFLLFTEVSFLTLIAVIVHQWVLHRLVIDCYGNRLVHESVIASANLAEVEAKFVKPRMSKKVQ
SQ  DVAIDCTPHGDGMVKFYPALTTNRSHIFQTHSLTGELITETFNPSTKEFEDLQTEGTTHNVIRTAPYAAGDLLHRDPYWY
SQ  QRNMIMRDVAHRPYFHSREVSPTRYHPSRISPRPGQYSPLVSSTSGMSTPLMRPDRSPFLNTRPSLGEREELFHRGNSRS
SQ  PLRQPIENFKSLDRSSDSQSPIRRHNGDSDA
//
ID  A6ZTA1;
PN  Nucleus-vacuole junction protein 1;
GN  NVJ1;
OS  307796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: A6ZTA1;
DE  Function: Involved in the formation of nucleus-vacuole (NV) junctions during piecemeal microautophagy of the nucleus (PMN). NV junctions are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process. Acts also as an outer-nuclear membrane receptor for OSH1 and TSC13 (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0005640;
GO  GO:0006914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTRPPLVRGIFSLGLSVAVLKGVEKTVRKHLERQGWIEPQKVDYELIFTIDRLKNLVDNKREALTAEQPDAGELSWRKVF
SQ  NFISRQSSELDARIYVLILLLSFLLPIAWTVLDGDRETTLEDKDNDCNVDLIENERRLKHYNDGERAVLQFGKNRSEPII
SQ  LSYKDMNVLEGEHEFTSKEEHSNSHLTSKSENALSQVGSEDLLGCHLEKQLEEDKNEPNGEADGEDDNNREKDCSSSSEV
SQ  ESQSKCRKESTAEPDSLSRDTRTTSSLKSSTSFPISFKGSIDLKSLNQPSSLLHIQVSPTKSSNLDAQVNTEQAYSQPFR
SQ  Y
//
ID  P38881;
PN  Nucleus-vacuole junction protein 1;
GN  NVJ1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:10888680, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:16912077}; Single-pass membrane protein {ECO:0000269|PubMed:10888680, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:16912077}.
DR  UNIPROT: P38881;
DR  UNIPROT: D3DLE3;
DR  PDB: 5H2C;
DR  PDB: 5XJG;
DE  Function: Involved in the formation of nucleus-vacuole (NV) junctions during piecemeal microautophagy of the nucleus (PMN). NV junctions are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process. Acts also as an outer-nuclear membrane receptor for OSH1 and TSC13. {ECO:0000269|PubMed:10888680, ECO:0000269|PubMed:12529432, ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:15958487, ECO:0000269|PubMed:16912077}.
DE  Reference Proteome: Yes;
DE  Interaction: P35845; IntAct: EBI-811418; Score: 0.35
DE  Interaction: Q06266; IntAct: EBI-811418; Score: 0.35
DE  Interaction: P39968; IntAct: EBI-2118506; Score: 0.77
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0034399;
GO  GO:0071561;
GO  GO:0006629;
GO  GO:0071562;
GO  GO:0034727;
GO  GO:0008104;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTRPPLVRGIFSLGLSVAVLKGVEKTVRKHLERQGWIEPQKVDYELIFTIDRLKNLVDNKREALTAEQPDAGELSWRKVF
SQ  NFISRQSSELDTRIYVLILLLSFLLPIAWTVLDGDRETTLEDKDNDCNVDLIENERRLKHYNDGERAVLQFGKNRSEPII
SQ  LSYKDMNVLEGEHEFTSKEEHSNSHLTSKSENALNQVGSEDLLGCHLEKQLEEDKNEPNGEADGEDDNNREKDCSSSSEV
SQ  ESQSKCRKESTAEPDSLSRDTRTTSSLKSSTSFPISFKGSIDLKSLNQPSSLLHIQVSPTKSSNLDAQVNTEQAYSQPFR
SQ  Y
//
ID  O94464;
PN  Nucleus-vacuole junction protein 2;
GN  nvj2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Single- pass type II membrane protein {ECO:0000305}. Note=Enriched at the nucleus-vacuole junction (By similarity). During endoplasmic reticulum (ER) stress, localizes to ER-Golgi contacts (By similarity). {ECO:0000250|UniProtKB:Q06833}.
DR  UNIPROT: O94464;
DR  PROSITE: PS51847;
DE  Function: During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, induces contacts between the ER and medial- Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. {ECO:0000250|UniProtKB:Q06833}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0071561;
GO  GO:0008289;
GO  GO:0006869;
GO  GO:1990854;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFFAFLITYLLGGVTFLPFILFIYLLTRPTHKSEELRIIEPNNDCLTKLDKDIRIQGWIRVTTKFLQGKSGSVKVQEIPQ
SQ  DQLPKSSSDNAVTDRKTISPSGINNQYVIRNPKDVYYATVQAGKLHLFDPVKTSELLHVINLHEYLVVFYPGTVTENELF
SQ  SNRNAIFLKYPAVSHKKESSTKSLLNKDLYVYGRTPSNKEDWYYALLSYSKISPAIKPLEAPIDFDYASVHHNLTALSSP
SQ  DTDWLNAFIGRIFLGIHKTEGFKSLVVEKLTKKLSRIKTPGIMTDVKVIDVDVGEAIPTVNGLKFESLSNGGELIVSADI
SQ  WYEGDCSFKAETTANIKFGSHFPSKTVPLALVIRLTHVSGKVRLLIKPPPSNRVWYAFYEKPRLHLIVEPMVARKQLTNN
SQ  YLINFITQKLVELVHETIVMPNMNDLAFFIDNEAPIKGGLWDIELFRAPTIQKPAEKDAKAERKKSGLSSSTSEESLNRH
SQ  ISKRSSNSNDTAPSSHIIADKNLEPTSNIQLKKNPDGNLVETSELSDSDENSVLSNKSSTLSKKVVENTSPLKYTHSASK
SQ  SFIGEVQDSLQALKTKAHKPRSIGGDSSQTTLSETTKKYGSVAKKSFFQGVSDAKSFVKKIKSTYIDDSSSNSPSDIESN
SQ  YSADDNEISKSKAQNAIDFNVTNTHSPSRSISSEKSYKAAERGQQDKHNDVLVDLNPNVEAEKSNPHSNSQKTSKNDMSR
SQ  NQRNKYAKEIMTGQPTLHPQGQLPIQNVEQRATHKPLPRPPVQVETREPVRPVPPIPKL
//
ID  Q06833;
PN  Nucleus-vacuole junction protein 2;
GN  NVJ2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Single-pass type II membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:22250200}; Single- pass type II membrane protein {ECO:0000305}. Note=Enriched at the nucleus-vacuole junction where it becomes increasingly concentrated as cells enter into the late-logarithmic growth phase (PubMed:22250200). During endoplasmic reticulum (ER) stress, localizes to ER-Golgi contacts (PubMed:28011845). {ECO:0000269|PubMed:22250200, ECO:0000269|PubMed:28011845}.
DR  UNIPROT: Q06833;
DR  UNIPROT: D6W491;
DR  Pfam: PF10296;
DR  Pfam: PF00169;
DR  PROSITE: PS51847;
DE  Function: During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, induces contacts between the ER and medial- Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. {ECO:0000269|PubMed:28011845}.
DE  Reference Proteome: Yes;
DE  Interaction: P39743; IntAct: EBI-7295400; Score: 0.65
DE  Interaction: P43603; IntAct: EBI-489033; Score: 0.00
DE  Interaction: Q02159; IntAct: EBI-860443; Score: 0.00
DE  Interaction: P47068; IntAct: EBI-7295421; Score: 0.44
DE  Interaction: P0CF34; IntAct: EBI-7295458; Score: 0.44
DE  Interaction: P80667; IntAct: EBI-7296890; Score: 0.44
DE  Interaction: P32790; IntAct: EBI-7310006; Score: 0.31
DE  Interaction: P10591; IntAct: EBI-3682273; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3719222; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3786837; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3803850; Score: 0.35
GO  GO:0071944;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0071561;
GO  GO:0008289;
GO  GO:0035621;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASLKVFLAVYLLGGITFLPLVLFTLYKIHLLYSNLKSASKKELDHDTADEIDEKTRLLARDIDPEFKARKLEEQLGVKV
SQ  FNKGWITVTKQYYYHSSEVAVILKNSNNNKDSDTALQEQILQRTDLKKKQRFFAVLRHGNLFLYKDDSQNANLVHAISLQ
SQ  NRFITIWPRFDELGKEELPDASLFTKRTCIAIFKNDLVSIDSKNHNVILPHFDPLTSAESNNGDISTNDTTHEYQSQFHS
SQ  SNQFFLYFDNNMDKEDWYYQLINASKNSNSLSTGLLDPNVSANAAHLKTKDMLQLIQDINSTENQLTTKWLNALLGRLFL
SQ  SLQQTDTLNKFIHEKICKKLNKIKTPGFLDDLVVEKVDVGDSAPLFTSPELLELSPEGSTKIAIDVQYRGNLTIIIATKA
SQ  SINLGSRFKQREVSLQLSIKIKEFSGPLLFLIKPPPSNRIWYAFRTEPIMDFEIEPIVSSSKLSYNVVTNAIKSKFAEAV
SQ  KESLVVPFMDDIVFYPTPNEVYRGGIWEEQDPEAAARARTAAAASDMNNTSAKEHLEALQEGGMKTQSRIKKALRPERKK
SQ  ENLKDLVDASGVATKTTTQTTVTTATNDDVSSSENSTKSRKYFKNSIKKIGRWYKDNVGNSSDTEDMDEIDVQDKKNDDS
SQ  ADERESDNPILTSNPKMISNRRPVPRRPSQPLNTLSPKLEGRKEKDTENFPVPPSASNMNASKMFANKENRKFSVSSNDS
SQ  QNSLKNGDPHVKASKLESSQAFVKKTSQNRFNDGFFKQDLEFEEQREPKL
//
ID  Q9U1H9;
PN  Nuclear RNA export factor 1;
GN  sbr;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:14729961}. Cytoplasm {ECO:0000269|PubMed:14729961}. Nucleus envelope {ECO:0000269|PubMed:14729961}. Note=Localized in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:14729961}.
DR  UNIPROT: Q9U1H9;
DR  UNIPROT: Q9NFQ2;
DR  UNIPROT: Q9NFQ3;
DR  UNIPROT: Q9VZ65;
DR  UNIPROT: Q9VZ68;
DR  PDB: 6IHJ;
DR  Pfam: PF02136;
DR  Pfam: PF09162;
DR  Pfam: PF03943;
DR  PROSITE: PS51450;
DR  PROSITE: PS50177;
DR  PROSITE: PS51281;
DE  Function: Mediates the export of the majority of mRNAs from the nucleus to the cytoplasm (PubMed:11779805, PubMed:11780633, PubMed:11780634, PubMed:27016737). In ovarian follicle cells, plays a role in transposable element silencing regulation by enabling the nuclear export of flamenco (flam) transcripts and subsequent piRNA biogenesis (PubMed:33856346). {ECO:0000269|PubMed:11779805, ECO:0000269|PubMed:11780633, ECO:0000269|PubMed:11780634, ECO:0000269|PubMed:27016737, ECO:0000269|PubMed:33856346}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VFS4; IntAct: EBI-236273; Score: 0.00
DE  Interaction: Q9UKK6; IntAct: EBI-302158; Score: 0.35
DE  Interaction: Q9V3H8; IntAct: EBI-873824; Score: 0.27
DE  Interaction: Q9V813; IntAct: EBI-1631868; Score: 0.00
DE  Interaction: Q24114; IntAct: EBI-9931823; Score: 0.35
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0047485;
GO  GO:0043021;
GO  GO:0003723;
GO  GO:0006406;
GO  GO:0051168;
GO  GO:0016973;
GO  GO:0046833;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPKRGGGSSQRYNNNVGNGGGRYNAPEDFDDFDVEDRQRRKDRNKRRVSFKPSQCLHNKKDIKLRPEDLRRWDEDDDMSD
SQ  MTTAVKDRPTSRRRGSPIPRGKFGKLMPNSFGWYQVTLQNAQIYEKETLLSALLAAMSPHVFIPQYWRVERNCVIFFTDD
SQ  YEAAERIQHLGKNGHLPDGYRLMPRVRSGIPLVAIDDAFKEKMKVTMAKRYNIQTKALDLSRFHADPDLKQVFCPLFRQN
SQ  VMGAAIDIMCDNIPDLEALNLNDNSISSMEAFKGVEKRLPNLKILYLGDNKIPSLAHLVVLRNLSILELVLKNNPCRSRY
SQ  KDSQQFISEVRRKFPKLVKLDGETLEPQITFDLSEQGRLLETKASYLCDVAGAEVVRQFLDQYFRIFDSGNRQALLDAYH
SQ  EKAMLSISMPSASQAGRLNSFWKFNRNLRRLLNGEENRTRNLKYGRLACVSTLDEWPKTQHDRRTFTVDLTIYNTSMMVF
SQ  TVTGLFKELNDETNNPASMELYDVRHFARTYVVVPQNNGFCIRNETIFITNATHEQVREFKRSQHQPAPGAMPSTSSAVT
SQ  SPQAGAAAGLQGRLNALGVATGPVAILSGDPLAATAPVNSGSAAISTTAVAPGAQDESTKMQMIEAMSAQSQMNVIWSRK
SQ  CLEETNWDFNHAAFVFEKLFKENKIPPEAFMK
//
ID  Q9UBU9;
PN  Nuclear RNA export factor 1;
GN  NXF1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:25662211}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332}. Nucleus speckle {ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Nucleus envelope {ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:23591820}. Cytoplasm {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:19864460}. Cytoplasm, Stress granule {ECO:0000269|PubMed:18596238}. Note=Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles (PubMed:23826332). Nucleus; nuclear rim (PubMed:25662211). {ECO:0000269|PubMed:23826332, ECO:0000269|PubMed:25662211}.
DR  UNIPROT: Q9UBU9;
DR  UNIPROT: B4E269;
DR  UNIPROT: Q99799;
DR  UNIPROT: Q9UQL2;
DR  PDB: 1FO1;
DR  PDB: 1FT8;
DR  PDB: 1GO5;
DR  PDB: 1JKG;
DR  PDB: 1JN5;
DR  PDB: 1KOH;
DR  PDB: 1KOO;
DR  PDB: 1OAI;
DR  PDB: 2Z5K;
DR  PDB: 2Z5M;
DR  PDB: 3RW6;
DR  PDB: 3RW7;
DR  PDB: 4WYK;
DR  PDB: 6E5U;
DR  Pfam: PF02136;
DR  Pfam: PF09162;
DR  Pfam: PF03943;
DR  PROSITE: PS51450;
DR  PROSITE: PS50177;
DR  PROSITE: PS51281;
DR  OMIM: 602647;
DR  DisGeNET: 10482;
DE  Function: Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway) (PubMed:10924507). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex (PubMed:18364396, PubMed:19165146, PubMed:9660949). ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export (PubMed:18364396, PubMed:19165146, PubMed:9660949). Also involved in nuclear export of m6A-containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:28984244, ECO:0000269|PubMed:9660949}.
DE  Reference Proteome: Yes;
DE  Interaction: O15234; IntAct: EBI-21728803; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: P35658; IntAct: EBI-7193202; Score: 0.69
DE  Interaction: P37198; IntAct: EBI-7193172; Score: 0.88
DE  Interaction: P46060; IntAct: EBI-6262548; Score: 0.53
DE  Interaction: P49790; IntAct: EBI-7193245; Score: 0.76
DE  Interaction: P49792; IntAct: EBI-6262548; Score: 0.53
DE  Interaction: P52948; IntAct: EBI-7193058; Score: 0.61
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: P78406; IntAct: EBI-7193130; Score: 0.54
DE  Interaction: Q06609; IntAct: EBI-3914918; Score: 0.37
DE  Interaction: Q13625; IntAct: EBI-10319914; Score: 0.56
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q53GS7; IntAct: EBI-21728803; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-6262548; Score: 0.35
DE  Interaction: Q92900; IntAct: EBI-3867844; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-6262548; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: Q9NRR5; IntAct: EBI-955046; Score: 0.00
DE  Interaction: Q08211; IntAct: EBI-866311; Score: 0.76
DE  Interaction: Q92973; IntAct: EBI-7193088; Score: 0.54
DE  Interaction: Q9BUJ2; IntAct: EBI-7193279; Score: 0.54
DE  Interaction: Q9UKK6; IntAct: EBI-1032165; Score: 0.84
DE  Interaction: Q16629; IntAct: EBI-398917; Score: 0.67
DE  Interaction: Q07955; IntAct: EBI-398948; Score: 0.76
DE  Interaction: P38919; IntAct: EBI-619182; Score: 0.35
DE  Interaction: P22575; IntAct: EBI-866704; Score: 0.62
DE  Interaction: P84103; IntAct: EBI-7034677; Score: 0.54
DE  Interaction: P06730; IntAct: EBI-8582156; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-8582181; Score: 0.35
DE  Interaction: Q81WW5; IntAct: EBI-2828496; Score: 0.00
DE  Interaction: Q81WF3; IntAct: EBI-2828485; Score: 0.00
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-3050465; Score: 0.35
DE  Interaction: Q9H1J1; IntAct: EBI-3866025; Score: 0.53
DE  Interaction: Q9BZI7; IntAct: EBI-3866041; Score: 0.53
DE  Interaction: Q9Y5S9; IntAct: EBI-3867848; Score: 0.40
DE  Interaction: Q15287; IntAct: EBI-3867852; Score: 0.40
DE  Interaction: Q8IYB3; IntAct: EBI-3867860; Score: 0.40
DE  Interaction: Q86V81; IntAct: EBI-3869257; Score: 0.66
DE  Interaction: Q9NXV2; IntAct: EBI-3922211; Score: 0.49
DE  Interaction: P11474; IntAct: EBI-3935683; Score: 0.37
DE  Interaction: O43765; IntAct: EBI-3935713; Score: 0.37
DE  Interaction: P62995; IntAct: EBI-3935703; Score: 0.37
DE  Interaction: Q13595; IntAct: EBI-3941843; Score: 0.37
DE  Interaction: Q9BTP6; IntAct: EBI-3941863; Score: 0.37
DE  Interaction: P68400; IntAct: EBI-5295255; Score: 0.44
DE  Interaction: P36578; IntAct: EBI-6262560; Score: 0.35
DE  Interaction: Q14444; IntAct: EBI-6262560; Score: 0.35
DE  Interaction: Q9Y2W1; IntAct: EBI-6262560; Score: 0.62
DE  Interaction: P39023; IntAct: EBI-6262560; Score: 0.35
DE  Interaction: O00571; IntAct: EBI-6262560; Score: 0.60
DE  Interaction: P62424; IntAct: EBI-6262560; Score: 0.35
DE  Interaction: Q02878; IntAct: EBI-6262560; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-6262560; Score: 0.35
DE  Interaction: P23396; IntAct: EBI-6262560; Score: 0.35
DE  Interaction: P62917; IntAct: EBI-6262560; Score: 0.35
DE  Interaction: P19338; IntAct: EBI-6262560; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-6262560; Score: 0.35
DE  Interaction: P11940; IntAct: EBI-6262659; Score: 0.40
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P10238; IntAct: EBI-8845500; Score: 0.62
DE  Interaction: Q9Y3Y2; IntAct: EBI-9077975; Score: 0.65
DE  Interaction: Q96QD9; IntAct: EBI-9085098; Score: 0.35
DE  Interaction: Q96FV9; IntAct: EBI-9085185; Score: 0.35
DE  Interaction: Q13769; IntAct: EBI-9085185; Score: 0.35
DE  Interaction: Q8NI27; IntAct: EBI-9085185; Score: 0.35
DE  Interaction: B4DYC6; IntAct: EBI-9484856; Score: 0.40
DE  Interaction: Q96RS6; IntAct: EBI-9484872; Score: 0.40
DE  Interaction: O95751; IntAct: EBI-10319882; Score: 0.67
DE  Interaction: P14136; IntAct: EBI-10319892; Score: 0.78
DE  Interaction: Q6A162; IntAct: EBI-10319926; Score: 0.56
DE  Interaction: Q92997; IntAct: EBI-10319936; Score: 0.56
DE  Interaction: Q96CG3; IntAct: EBI-10319946; Score: 0.72
DE  Interaction: Q9UJV3; IntAct: EBI-10319956; Score: 0.56
DE  Interaction: P17844; IntAct: EBI-10096841; Score: 0.40
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q68CZ1; IntAct: EBI-11368346; Score: 0.27
DE  Interaction: P41219; IntAct: EBI-24298299; Score: 0.56
DE  Interaction: O75031; IntAct: EBI-24498836; Score: 0.56
DE  Interaction: P49639; IntAct: EBI-24510395; Score: 0.56
DE  Interaction: Q9H079; IntAct: EBI-24515747; Score: 0.56
DE  Interaction: P49761; IntAct: EBI-24515603; Score: 0.56
DE  Interaction: Q13867; IntAct: EBI-24523474; Score: 0.56
DE  Interaction: P49760; IntAct: EBI-24524233; Score: 0.56
DE  Interaction: Q86WS4; IntAct: EBI-25264291; Score: 0.56
DE  Interaction: Q9BX10; IntAct: EBI-24622152; Score: 0.56
DE  Interaction: Q9BQ95; IntAct: EBI-24628881; Score: 0.56
DE  Interaction: P79522; IntAct: EBI-24660575; Score: 0.56
DE  Interaction: P15622; IntAct: EBI-24661566; Score: 0.56
DE  Interaction: Q9UK41; IntAct: EBI-24666279; Score: 0.56
DE  Interaction: Q6ZUT1; IntAct: EBI-24668590; Score: 0.56
DE  Interaction: B2RXH4; IntAct: EBI-24673822; Score: 0.56
DE  Interaction: Q6NTE8; IntAct: EBI-24678138; Score: 0.56
DE  Interaction: Q8N6V9; IntAct: EBI-24680526; Score: 0.56
DE  Interaction: A0A1B0GWI1; IntAct: EBI-23711325; Score: 0.56
DE  Interaction: Q5T5B0; IntAct: EBI-24686853; Score: 0.56
DE  Interaction: Q9ULR0; IntAct: EBI-24705892; Score: 0.56
DE  Interaction: Q13573; IntAct: EBI-24724810; Score: 0.56
DE  Interaction: O00746; IntAct: EBI-23790873; Score: 0.56
DE  Interaction: Q9BZL4; IntAct: EBI-24733395; Score: 0.56
DE  Interaction: Q8IZU3; IntAct: EBI-24735253; Score: 0.56
DE  Interaction: Q14457; IntAct: EBI-24738527; Score: 0.56
DE  Interaction: Q96M83; IntAct: EBI-24743255; Score: 0.56
DE  Interaction: Q9NQY0; IntAct: EBI-24754052; Score: 0.56
DE  Interaction: Q9H7T9; IntAct: EBI-24755679; Score: 0.56
DE  Interaction: Q96DF8; IntAct: EBI-24767131; Score: 0.56
DE  Interaction: Q9NR46; IntAct: EBI-24770768; Score: 0.56
DE  Interaction: Q7Z4V0; IntAct: EBI-24778309; Score: 0.56
DE  Interaction: Q5SWW7; IntAct: EBI-24779073; Score: 0.56
DE  Interaction: Q96P16; IntAct: EBI-24779655; Score: 0.56
DE  Interaction: Q8TDR4; IntAct: EBI-24797571; Score: 0.56
DE  Interaction: Q6P1L6; IntAct: EBI-25280752; Score: 0.56
DE  Interaction: Q13555; IntAct: EBI-24372650; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-24375283; Score: 0.56
DE  Interaction: Q5JR59; IntAct: EBI-24388879; Score: 0.56
DE  Interaction: Q9BYV9; IntAct: EBI-24392545; Score: 0.56
DE  Interaction: Q9UMX0; IntAct: EBI-24446611; Score: 0.56
DE  Interaction: Q13490; IntAct: EBI-24538264; Score: 0.56
DE  Interaction: Q8IZU1; IntAct: EBI-24539795; Score: 0.56
DE  Interaction: Q8WWB5; IntAct: EBI-24551261; Score: 0.56
DE  Interaction: Q8N8U2; IntAct: EBI-24581617; Score: 0.56
DE  Interaction: Q86WP2; IntAct: EBI-24598279; Score: 0.56
DE  Interaction: P31321; IntAct: EBI-24598989; Score: 0.56
DE  Interaction: Q9H0A9; IntAct: EBI-24646318; Score: 0.56
DE  Interaction: Q96HB5; IntAct: EBI-24647419; Score: 0.56
DE  Interaction: Q8NCU1; IntAct: EBI-24656214; Score: 0.56
DE  Interaction: Q8WWY6; IntAct: EBI-24657169; Score: 0.56
DE  Interaction: Q13829; IntAct: EBI-24777447; Score: 0.56
DE  Interaction: Q8ND83; IntAct: EBI-25203964; Score: 0.56
DE  Interaction: Q96MP8; IntAct: EBI-24809398; Score: 0.56
DE  Interaction: Q9C0B1; IntAct: EBI-25266832; Score: 0.56
DE  Interaction: Q9P2M4; IntAct: EBI-25269837; Score: 0.56
DE  Interaction: Q8IVT5; IntAct: EBI-14035831; Score: 0.35
DE  Interaction: Q9Y2Z4; IntAct: EBI-21728803; Score: 0.35
DE  Interaction: Q9H000; IntAct: EBI-21728803; Score: 0.35
DE  Interaction: Q99666; IntAct: EBI-21728803; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-21728803; Score: 0.35
DE  Interaction: O15354; IntAct: EBI-21812535; Score: 0.35
DE  Interaction: Q9NPJ8; IntAct: EBI-21875490; Score: 0.35
DE  Interaction: Q82506; IntAct: EBI-15620563; Score: 0.35
DE  Interaction: Q9BTM9; IntAct: EBI-15902832; Score: 0.35
DE  Interaction: P03430; IntAct: EBI-25769373; Score: 0.37
DE  Interaction: P15659; IntAct: EBI-25769186; Score: 0.37
DE  Interaction: P03427; IntAct: EBI-25769439; Score: 0.37
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: O76021; IntAct: EBI-20924306; Score: 0.40
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q2HR75; IntAct: EBI-22084769; Score: 0.35
DE  Interaction: P10644; IntAct: EBI-25387530; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.35
DE  Interaction: Q96KG9; IntAct: EBI-28944481; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
DE  Interaction: Q93009; IntAct: EBI-30844801; Score: 0.44
DE  Interaction: A6NLX3; IntAct: EBI-28997234; Score: 0.27
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0042405;
GO  GO:0005643;
GO  GO:0042272;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADEGKSYSEHDDERVNFPQRKKKGRGPFRWKYGEGNRRSGRGGSGIRSSRLEEDDGDVAMSDAQDGPRVRYNPYTTRPN
SQ  RRGDTWHDRDRIHVTVRRDRAPPERGGAGTSQDGTSKNWFKITIPYGRKYDKAWLLSMIQSKCSVPFTPIEFHYENTRAQ
SQ  FFVEDASTASALKAVNYKILDRENRRISIIINSSAPPHTILNELKPEQVEQLKLIMSKRYDGSQQALDLKGLRSDPDLVA
SQ  QNIDVVLNRRSCMAATLRIIEENIPELLSLNLSNNRLYRLDDMSSIVQKAPNLKILNLSGNELKSERELDKIKGLKLEEL
SQ  WLDGNSLCDTFRDQSTYISAIRERFPKLLRLDGHELPPPIAFDVEAPTTLPPCKGSYFGTENLKSLVLHFLQQYYAIYDS
SQ  GDRQGLLDAYHDGACCSLSIPFIPQNPARSSLAEYFKDSRNVKKLKDPTLRFRLLKHTRLNVVAFLNELPKTQHDVNSFV
SQ  VDISAQTSTLLCFSVNGVFKEVDGKSRDSLRAFTRTFIAVPASNSGLCIVNDELFVRNASSEEIQRAFAMPAPTPSSSPV
SQ  PTLSPEQQEMLQAFSTQSGMNLEWSQKCLQDNNWDYTRSAQAFTHLKAKGEIPEVAFMK
//
ID  Q99JX7;
PN  Nuclear RNA export factor 1;
GN  Nxf1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus speckle {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9UBU9}. Note=Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles. Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q9UBU9}.
DR  UNIPROT: Q99JX7;
DR  UNIPROT: O88985;
DR  UNIPROT: Q3TJA5;
DR  Pfam: PF02136;
DR  Pfam: PF09162;
DR  Pfam: PF03943;
DR  PROSITE: PS51450;
DR  PROSITE: PS50177;
DR  PROSITE: PS51281;
DE  Function: Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1- NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex. ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export. Also involved in nuclear export of m6A- containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A- containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export. {ECO:0000250|UniProtKB:Q9UBU9}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0042405;
GO  GO:0005643;
GO  GO:0042272;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000346;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADEGKSYNEHDDRVSFPQRRKKGRGPFRWKCGEGNRRSGRGGSGVQSSRFEEDDGDVAMNDPQDGPRVRYNPYTNRPNR
SQ  RGDGWHDRDRIHITVRRDRAPAERGGAGTSQDGTTKNWFKITIPYGRKYDKTWLLSMIQSKCSVPFNPIEFHYENTRAHF
SQ  FVEDATTASALKGVNHKIQDRENRRISIIINASAPPYTVQNELKPEQIEQLKLIMSKRYDGNQQALDLKGLRSDPDLVAQ
SQ  NIDVVLNRRSCMAATLRIIEENIPELLSLNLSSNRLYKLDDMSSIVQKAPNLKTLNLSGNELKTERELDKIKGLKLEELW
SQ  LDRNPMCDNFGDQSSYISAIRERFPKLLRLDGHELPPPISFDVEAPTMLPPCKGSYFGTENLKSLVLRFLQQYYVIYDSG
SQ  DRQGLLYAYHDGACCSLSIPYNPQNPVRKNLAEYVKDSRNVKKLKEPTQRFRLLKHTRLNVVAFLNELPKTQHDVNAFVV
SQ  DISAQTSTLLCFSVNGVFKEVDGKSRDSLRAFTRTFIAVPASNSGLCIVNDELFVRNASPEEIQRAFAMSAPTPSSSPVP
SQ  TLSPEQQEMLQAFSTQSGMNLEWSQKCLQDNNWDYTRSAQAFTLLKAKGEIPEVAFMK
//
ID  O88984;
PN  Nuclear RNA export factor 1;
GN  Nxf1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus speckle {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9UBU9}. Note=Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles. Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q9UBU9}.
DR  UNIPROT: O88984;
DR  Pfam: PF02136;
DR  Pfam: PF09162;
DR  Pfam: PF03943;
DR  PROSITE: PS51450;
DR  PROSITE: PS50177;
DR  PROSITE: PS51281;
DE  Function: Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1- NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex. ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export. Also involved in nuclear export of m6A- containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A- containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export. {ECO:0000250|UniProtKB:Q9UBU9}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0042405;
GO  GO:0005643;
GO  GO:0042272;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0015031;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADEGKSYNEHDDRVSFPQRRKKGRGPFRWKCGVGNRRSGRGGSGIRSSRFEEDDGDVAMNDPQDGPRVRFNPYTTRPNR
SQ  RRDTWHDRDRIHVTVRRDRAPQERGGAGTSQDGTTKNWFKITIPYGKKYDKMWLLSMIQSKCSVPFNPIEFHYENTRAHF
SQ  FVENATTASALKAVNYKIQDRENGRISIIINSSAPPYIVQNELKPEQVEQLKLIMSKRYDGSQQALDLKGLRSDPDLVAQ
SQ  NIDVVLNRRGCMAAALRIIEENIPELLSLNLSNNRLYKLDDMSSIVQKAPNLKILNLSGNELKSEWELDKIKGLKLEELW
SQ  LDRNPMCDTFLDQSTYISTIRERFPKLLRLDGHELPPPIAFDVEAPTMLPPCKGSYFGTENLKSLVLHFLQQYYAIYDSG
SQ  DRQGLLDAYHDGACCSLSTPSNPQNPVRHNLAKYFNDSRNVKKIKDTTTRFRLLKHTRLNVVAFLNELPKTHHDVNSFVV
SQ  DISAQTSTLLCFSVNGVFKEVDGKSRDSLRAFTRTFIAVPASNSGLCIVNDELFVRNASPEEIQRAFAMPAPTPSSSPVP
SQ  TLSQEQQDMLQAFSTQSGMNLEWSQKCLQDNNWDYTRSAQAFTHLKAKGEIPEVAFMK
//
ID  Q9V3H8;
PN  NTF2-related export protein;
GN  Nxt1;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:31384064}. Nucleus envelope {ECO:0000269|PubMed:31384064}. Note=Associates with the nuclear pore complex. {ECO:0000269|PubMed:31384064}.
DR  UNIPROT: Q9V3H8;
DR  PDB: 6IHJ;
DR  PDB: 6MRK;
DR  Pfam: PF02136;
DR  PROSITE: PS50177;
DE  Function: Stimulator of protein export for NES-containing proteins (By similarity). Plays a role in the nuclear export of mRNA (PubMed:14729961). Also plays a role in the nuclear export of U1 snRNA, tRNA, and mRNA (By similarity). In ovaries, plays a role in transposable element silencing regulation (PubMed:31219034, PubMed:31368590, PubMed:31384064, PubMed:31570835, PubMed:33856346). Forms a complex with nxf2, Panx and piwi which acts as effector of cotranscriptional transposon silencing (PubMed:31219034, PubMed:31368590, PubMed:31384064, PubMed:31570835). In ovarian follicle cells, enables the nuclear export of flamenco (flam) transcripts and subsequent piRNA biogenesis (PubMed:33856346). {ECO:0000250|UniProtKB:Q9UKK6, ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31384064, ECO:0000269|PubMed:31570835, ECO:0000269|PubMed:33856346}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9U1H9; IntAct: EBI-873824; Score: 0.27
DE  Interaction: Q8IQK4; IntAct: EBI-15170706; Score: 0.49
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0044613;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0017053;
GO  GO:0050829;
GO  GO:0045824;
GO  GO:0006913;
GO  GO:0016973;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDSDLKAKVESCARTADTFTRLYYASVDNRRQQIGRLYLDNATLSWNGNGAIGRQMIESYFQELPSSNHQLNTLDAQPIV
SQ  DQAVSNQLAYLIMASGSVKFADQQLRKFQQTFIVTAENDKWKVVSDCYRMQEV
//
ID  F1N3B8;
PN  2'-5'-oligoadenylate synthase 2;
GN  OAS2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}.
DR  UNIPROT: F1N3B8;
DR  UNIPROT: Q53AV7;
DR  Pfam: PF01909;
DR  Pfam: PF10421;
DR  PROSITE: PS00833;
DR  PROSITE: PS50152;
DE  Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation. Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (By similarity). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity). {ECO:0000250|UniProtKB:E9Q9A9, ECO:0000250|UniProtKB:P29728}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0001730;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0042742;
GO  GO:0051607;
GO  GO:0070106;
GO  GO:0045071;
GO  GO:0032728;
GO  GO:0032760;
GO  GO:1903487;
GO  GO:0060700;
GO  GO:0009615;
GO  GO:0060337;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P29728};
SQ  MGSRESHLYEKPSEKLEEFIQNHLRPSEDCQKDIDQSVDTICEVLQEPCPSLTVTGVAKGGSYGRRTVLRGNSDGILVVF
SQ  FGDLEQFQDQEKRQYELLSKIWAQMKHCESTWKLAAKMELQNTNRSSRVTIQLSTKQQSITFNVLPAFNALGLSEKSSLW
SQ  SYRELKRSLDMVKARPGEFSVCFTELQEKFFSNYPSKLKDLILLVKHWFQKCQEKLINSSLLPPYALELLTVYAWEQGCG
SQ  AEDFDMAEGVRTVLRLIEKQEQLCVYWTVNYNFGDEIVRNILLSQLQAPRPVILDPTDPTNNVSMDNTCWLQLKHEAQNW
SQ  LRSLRQNESPGPSWNVLPASLYITPGHLLDKFVKDFLQPNQTFQDQIKKALKIICSFLEENCFRHSTTKIQVIQGGSTVK
SQ  GTALKTGSDASLVVFANSLKSYTSPKNERYNIIKEIHEQLEACRQEKDFEVKFEISKWKPPWVLSFTLKSKVLNESVDFD
SQ  VLPAFNALGELKSGSTPSPRTYTELIHLYKPSDVFLEGEFSACFTKLQRNFVRSLPLKLKDLIRLLKHWYCGCEKKLKQK
SQ  GSLPPKYALELLSIYAWEKGSGAQDFDMAEGFRTVLELVIQYQHLCVFWTVNYSFDDEILRNFLLGQIRRTRPVILDPAD
SQ  PTGDVGGGHRWCWHLLAKEATEWLSSLCFKDKSGCPIQPWNVPKKRVQTPGSCGAGIYSMVNEMHLLRSHRFLD
//
ID  P29728;
PN  2'-5'-oligoadenylate synthase 2;
GN  OAS2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:19923450}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19923450}.
DR  UNIPROT: P29728;
DR  UNIPROT: A8K9T1;
DR  UNIPROT: Q6PJ33;
DR  UNIPROT: Q86XX8;
DR  Pfam: PF01909;
DR  Pfam: PF10421;
DR  PROSITE: PS00832;
DR  PROSITE: PS00833;
DR  PROSITE: PS50152;
DR  OMIM: 603350;
DR  DisGeNET: 4939;
DE  Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:10464285, PubMed:9880569). Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'- oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:10464285, PubMed:9880569, PubMed:11682059). Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:10464285, PubMed:9880569). Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity). {ECO:0000250|UniProtKB:E9Q9A9, ECO:0000269|PubMed:10464285, ECO:0000269|PubMed:11682059, ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:9880569, ECO:0000303|PubMed:21142819}.
DE  Reference Proteome: Yes;
DE  Interaction: P49761; IntAct: EBI-10211450; Score: 0.67
DE  Interaction: Q96EF6; IntAct: EBI-25275989; Score: 0.56
DE  Interaction: Q8ND71; IntAct: EBI-21862528; Score: 0.35
DE  Interaction: Q13976; IntAct: EBI-21883113; Score: 0.35
DE  Interaction: Q13085; IntAct: EBI-21883113; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0001730;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0042742;
GO  GO:0051607;
GO  GO:0070106;
GO  GO:0045071;
GO  GO:0006139;
GO  GO:0032728;
GO  GO:0032760;
GO  GO:1903487;
GO  GO:0060700;
GO  GO:0009615;
GO  GO:0006401;
GO  GO:0060337;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:2211721};
SQ  MGNGESQLSSVPAQKLGWFIQEYLKPYEECQTLIDEMVNTICDVLQEPEQFPLVQGVAIGGSYGRKTVLRGNSDGTLVLF
SQ  FSDLKQFQDQKRSQRDILDKTGDKLKFCLFTKWLKNNFEIQKSLDGFTIQVFTKNQRISFEVLAAFNALSLNDNPSPWIY
SQ  RELKRSLDKTNASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAWEQGCRKD
SQ  NFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKICWQWLKKEAQTWLT
SQ  SPNLDNELPAPSWNVLPAPLFTTPGHLLDKFIKEFLQPNKCFLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKG
SQ  TALKTGSDADLVVFHNSLKSYTSQKNERHKIVKEIHEQLKAFWREKEEELEVSFEPPKWKAPRVLSFSLKSKVLNESVSF
SQ  DVLPAFNALGQLSSGSTPSPEVYAGLIDLYKSSDLPGGEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKPK
SQ  GSLPPKYALELLTIYAWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAE
SQ  PTGDVGGGDRWCWHLLAKEAKEWLSSPCFKDGTGNPIPPWKVPTMQTPGSCGARIHPIVNEMFSSRSHRILNNNSKRNF
//
ID  E9Q9A9;
PN  2'-5'-oligoadenylate synthase 2;
GN  Oas2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}.
DR  UNIPROT: E9Q9A9;
DR  UNIPROT: Q8K4E5;
DR  UNIPROT: Q8VI92;
DR  Pfam: PF01909;
DR  Pfam: PF10421;
DR  PROSITE: PS00832;
DR  PROSITE: PS00833;
DR  PROSITE: PS50152;
DE  Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:12396720, PubMed:29117179). Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'- oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:29117179). Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:21142819). Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (PubMed:29117179). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (PubMed:29117179). {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:15865429, ECO:0000269|PubMed:29117179, ECO:0000303|PubMed:21142819}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0001730;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0042742;
GO  GO:0051607;
GO  GO:0070106;
GO  GO:0045071;
GO  GO:0032728;
GO  GO:0032760;
GO  GO:1903487;
GO  GO:0060700;
GO  GO:0009617;
GO  GO:0009615;
GO  GO:0006401;
GO  GO:0060337;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P29728};
SQ  MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESL
SQ  KQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVK
SQ  HEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILL
SQ  VKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILL
SQ  HQLRSQRPVILDPTDPTNNVGKDDGFWELLTEEAMAWLYSPSLNTESPAPYWDVLPMPLFVTPSHLLNKFIKDFLQPNKL
SQ  FLKQIKEAVDIICSFLKNVCFLNSDTKVLKTVKGGSTAKGTALKRGSDADIVVFLSSLESYDSLKTNRSQFVQEIQKQLE
SQ  EFVQAQEWEVTFEISKWKAPRVLSFTLKSKTLNESVEFDVLPAYDALGQLRSDFTLRPEAYKDLIELCASQDIKEGEFSI
SQ  CFTELQRNFIQTRPTKLKSLLRLIKHWYKQYERKMKPKASLPPKYALELLTVYAWEQGSGTDDFDIAEGFRTVLDLVIKY
SQ  RQLCIFWTVNYNFEEEYMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAEEAKEWLSSPCFQVEQKGLVQPWKV
SQ  PVMQTPGSCGGQIYPTVGGVTK
//
ID  Q5MYU0;
PN  2'-5'-oligoadenylate synthase 2;
GN  Oas2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}.
DR  UNIPROT: Q5MYU0;
DR  Pfam: PF01909;
DR  Pfam: PF10421;
DR  PROSITE: PS00832;
DR  PROSITE: PS00833;
DR  PROSITE: PS50152;
DE  Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation. Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (By similarity). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity). {ECO:0000250|UniProtKB:E9Q9A9, ECO:0000250|UniProtKB:P29728}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0001730;
GO  GO:0005524;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0042742;
GO  GO:0051607;
GO  GO:0070106;
GO  GO:0045071;
GO  GO:0032728;
GO  GO:0032760;
GO  GO:1903487;
GO  GO:0060700;
GO  GO:0009617;
GO  GO:0009615;
GO  GO:0006401;
GO  GO:0060337;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P29728};
SQ  MGNWMPGWSSSGSLGVPPMPVQKLEKSVQVNLEPDEKCLSQTEVSSVPSQKLEEYIQANLKPDEESLKQIDQAVDAISDL
SQ  LCSEVMIDVLKVVKGGSYGRKTVLRDCSDGTLVLFTGLFKQFQDQKKYQDKLLDLIEQRLKSHEKYKKSVKRKLSLLEVQ
SQ  VSIPGQSILLQLLPTFNPLCISENPSAQVYQNLKRSMDQVKASPGEFSDCFTTLQQRFFEKYPGRLKDLILLVKHWYKQL
SQ  QDKWIIPSPPPLLYALELLTVYAWEQGCQTKDFDITQGIRTVLQLISQPTNLCVYWLDNYNFEDETVRNNLLHQLNSPRP
SQ  VILDPTDPTNNVGKDDRFWQLLAEEAQEWLNSLRLNKPHKPCWDVLPMPFFITPSHCLDKFIKDFLQPDKVFLNQIKRAV
SQ  DIICSFLKETCFQNSDIKVLKIIKGGSTAKGTALQQRSDADIIVFLSSLDSYDSLETERSQYVQEIRKQLEACQKAFNLG
SQ  VKFDISKWMAPRVLSFTLESKSLKQSVEFDVLPAYDALGQLRSDYTSRLKAYKKLIELYASQDSLKGGEFSVCFTELQRD
SQ  FIETRPTKLKGLIRLIKHWYKQCERKMKPKASLPPKYALELLTVYAWEHGSGTDGFDTAEGFRTVLDLVIRYRQLCVFWT
SQ  VNYNFEEDHMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAKEAKEWLSSSCFQVEPKSPVQPWKVPVVQTPGS
SQ  CGAQIYPVVGGVY
//
ID  O75147;
PN  Obscurin-like protein 1;
GN  OBSL1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:24793695}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24793695}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24793695}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons (PubMed:21572988).
DR  UNIPROT: O75147;
DR  UNIPROT: A0A024R468;
DR  UNIPROT: A4KVA4;
DR  UNIPROT: A4KVA5;
DR  UNIPROT: Q96IW3;
DR  UNIPROT: S4R3M6;
DR  PDB: 2CPC;
DR  PDB: 2E6P;
DR  PDB: 2E6Q;
DR  PDB: 2LU7;
DR  PDB: 2LVC;
DR  PDB: 2WP3;
DR  PDB: 2WWK;
DR  PDB: 2WWM;
DR  PDB: 3KNB;
DR  PDB: 5FM5;
DR  Pfam: PF07679;
DR  PROSITE: PS50853;
DR  PROSITE: PS50835;
DR  OMIM: 610991;
DR  OMIM: 612921;
DR  DisGeNET: 23363;
DE  Function: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695, PubMed:24793696). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons. {ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.
DE  Disease: 3M syndrome 2 (3M2) [MIM:612921]: An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies. {ECO:0000269|PubMed:19481195, ECO:0000269|PubMed:23018678}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P02768; IntAct: EBI-1224020; Score: 0.35
DE  Interaction: Q8WZ42; IntAct: EBI-7984019; Score: 0.78
DE  Interaction: Q8IYT8; IntAct: EBI-3622897; Score: 0.35
DE  Interaction: Q8WVZ9; IntAct: EBI-3232144; Score: 0.35
DE  Interaction: Q96RR4; IntAct: EBI-3251427; Score: 0.53
DE  Interaction: A7MCY6; IntAct: EBI-6116450; Score: 0.35
DE  Interaction: Q16539; IntAct: EBI-6256566; Score: 0.64
DE  Interaction: Q15759; IntAct: EBI-6381006; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-7903232; Score: 0.53
DE  Interaction: O35182; IntAct: EBI-8456591; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-6871150; Score: 0.37
DE  Interaction: Q8IYM1; IntAct: EBI-10819473; Score: 0.37
DE  Interaction: Q8NEP3; IntAct: EBI-12449710; Score: 0.51
DE  Interaction: C5E524; IntAct: EBI-12584280; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12588729; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-14035664; Score: 0.35
DE  Interaction: P43353; IntAct: EBI-21500028; Score: 0.35
DE  Interaction: Q96H86; IntAct: EBI-21521634; Score: 0.35
DE  Interaction: Q86WR7; IntAct: EBI-21530662; Score: 0.35
DE  Interaction: Q9H6X2; IntAct: EBI-21542347; Score: 0.35
DE  Interaction: Q9UF02; IntAct: EBI-21554221; Score: 0.35
DE  Interaction: Q8IYS4; IntAct: EBI-21565697; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21580477; Score: 0.35
DE  Interaction: Q8NFN8; IntAct: EBI-21600104; Score: 0.35
DE  Interaction: Q8NA56; IntAct: EBI-21620988; Score: 0.35
DE  Interaction: O14958; IntAct: EBI-21622768; Score: 0.35
DE  Interaction: Q9P286; IntAct: EBI-21659874; Score: 0.35
DE  Interaction: Q92832; IntAct: EBI-21661122; Score: 0.35
DE  Interaction: D6R9G5; IntAct: EBI-21662389; Score: 0.35
DE  Interaction: Q92997; IntAct: EBI-21693668; Score: 0.35
DE  Interaction: Q9BT43; IntAct: EBI-21704895; Score: 0.35
DE  Interaction: Q9BQE6; IntAct: EBI-21711641; Score: 0.35
DE  Interaction: O75386; IntAct: EBI-21712804; Score: 0.35
DE  Interaction: Q9BUG6; IntAct: EBI-21733185; Score: 0.35
DE  Interaction: Q6NZI2; IntAct: EBI-21738912; Score: 0.35
DE  Interaction: Q8IVT2; IntAct: EBI-21751011; Score: 0.35
DE  Interaction: Q8IW50; IntAct: EBI-21781744; Score: 0.35
DE  Interaction: Q9HBJ0; IntAct: EBI-21786331; Score: 0.35
DE  Interaction: A5YM69; IntAct: EBI-21785987; Score: 0.35
DE  Interaction: O95400; IntAct: EBI-21786026; Score: 0.35
DE  Interaction: O95644; IntAct: EBI-21786135; Score: 0.35
DE  Interaction: P30047; IntAct: EBI-21786208; Score: 0.35
DE  Interaction: P54922; IntAct: EBI-21786269; Score: 0.35
DE  Interaction: Q32MK0; IntAct: EBI-21786294; Score: 0.35
DE  Interaction: Q9NYB9; IntAct: EBI-21786440; Score: 0.35
DE  Interaction: Q9UKA8; IntAct: EBI-21786597; Score: 0.35
DE  Interaction: Q8N3Y1; IntAct: EBI-15927108; Score: 0.35
DE  Interaction: Q14999; IntAct: EBI-15927148; Score: 0.54
DE  Interaction: Q9NPC1; IntAct: EBI-20809680; Score: 0.37
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: O84388; IntAct: EBI-22302856; Score: 0.35
DE  Interaction: Q9H9E1; IntAct: EBI-26656693; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-27127583; Score: 0.35
DE  Interaction: O75381; IntAct: EBI-30835247; Score: 0.44
GO  GO:1990393;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0014704;
GO  GO:0031430;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0030018;
GO  GO:0008093;
GO  GO:0055003;
GO  GO:0007010;
GO  GO:0007030;
GO  GO:0007156;
GO  GO:0000226;
GO  GO:0050775;
GO  GO:0034067;
GO  GO:0007088;
GO  GO:0010842;
GO  GO:0007416;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKASSGDQGSPPCFLRFPRPVRVVSGAEAELKCVVLGEPPPVVVWEKGGQQLAASERLSFPADGAEHGLLLTAALPTDAG
SQ  VYVCRARNAAGEAYAAAAVTVLEPPASDPELQPAERPLPSPGSGEGAPVFLTGPRSQWVLRGAEVVLTCRAGGLPEPTLY
SQ  WEKDGMALDEVWDSSHFALQPGRAEDGPGASLALRILAARLPDSGVYVCHARNAHGHAQAGALLQVHQPPESPPADPDEA
SQ  PAPVVEPLKCAPKTFWVNEGKHAKFRCYVMGKPEPEIEWHWEGRPLLPDRRRLMYRDRDGGFVLKVLYCQAKDRGLYVCA
SQ  ARNSAGQTLSAVQLHVKEPRLRFTRPLQDVEGREHGIAVLECKVPNSRIPTAWFREDQRLLPCRKYEQIEEGTVRRLIIH
SQ  RLKADDDGIYLCEMRGRVRTVANVTVKGPILKRLPRKLDVLEGENAVLLVETLEAGVEGRWSRDGEELPVICQSSSGHMH
SQ  ALVLPGVTREDAGEVTFSLGNSRTTTLLRVKCVKHSPPGPPILAEMFKGHKNTVLLTWKPPEPAPETPFIYRLERQEVGS
SQ  EDWIQCFSIEKAGAVEVPGDCVPSEGDYRFRICTVSGHGRSPHVVFHGSAHLVPTARLVAGLEDVQVYDGEDAVFSLDLS
SQ  TIIQGTWFLNGEELKSNEPEGQVEPGALRYRIEQKGLQHRLILHAVKHQDSGALVGFSCPGVQDSAALTIQESPVHILSP
SQ  QDRVSLTFTTSERVVLTCELSRVDFPATWYKDGQKVEESELLVVKMDGRKHRLILPEAKVQDSGEFECRTEGVSAFFGVT
SQ  VQDPPVHIVDPREHVFVHAITSECVMLACEVDREDAPVRWYKDGQEVEESDFVVLENEGPHRRLVLPATQPSDGGEFQCV
SQ  AGDECAYFTVTITDVSSWIVYPSGKVYVAAVRLERVVLTCELCRPWAEVRWTKDGEEVVESPALLLQKEDTVRRLVLPAV
SQ  QLEDSGEYLCEIDDESASFTVTVTEPPVRIIYPRDEVTLIAVTLECVVLMCELSREDAPVRWYKDGLEVEESEALVLERD
SQ  GPRCRLVLPAAQPEDGGEFVCDAGDDSAFFTVTVTAPPERIVHPAARSLDLHFGAPGRVELRCEVAPAGSQVRWYKDGLE
SQ  VEASDALQLGAEGPTRTLTLPHAQPEDAGEYVCETRHEAITFNVILAEPPVQFLALETTPSPLCVAPGEPVVLSCELSRA
SQ  GAPVVWSHNGRPVQEGEGLELHAEGPRRVLCIQAAGPAHAGLYTCQSGAAPGAPSLSFTVQVAEPPVRVVAPEAAQTRVR
SQ  STPGGDLELVVHLSGPGGPVRWYKDGERLASQGRVQLEQAGARQVLRVQGARSGDAGEYLCDAPQDSRIFLVSVEEPLLV
SQ  KLVSELTPLTVHEGDDATFRCEVSPPDADVTWLRNGAVVTPGPQVEMAQNGSSRILTLRGCQLGDAGTVTLRAGSTATSA
SQ  RLHVRETELLFLRRLQDVRAEEGQDVCLEVETGRVGAAGAVRWVRGGQPLPHDSRLSMAQDGHIHRLFIHGVILADQGTY
SQ  GCESHHDRTLARLSVRPRQLRVLRPLEDVTISEGGSATFQLELSQEGVTGEWARGGVQLYPGPKCHIHSDGHRHRLVLNG
SQ  LGLADSGCVSFTADSLRCAARLIVREVPVTIVRGPHDLEVTEGDTATFECELSQALADVTWEKDGNALTPSPRLRLQALG
SQ  TRRLLQLRRCGPSDAGTYSCAVGTARAGPVRLTVRERTVAVLSELRSVSAREGDGATFECTVSEVETTGRWELGGRPLRP
SQ  GARVRIRQEGKKHILVLSELRAEDAGEVRFQAGPAQSLALLEVEALPLQMCRHPPREKTVLVGRRAVLEVTVSRSGGHVC
SQ  WLREGAELCPGDKYEMRSHGPTHSLVIHDVRPEDQGTYCCQAGQDSTHTRLLVEGN
//
ID  D3YYU8;
PN  Obscurin-like protein 1;
GN  Obsl1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O75147}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75147}. Golgi apparatus {ECO:0000250|UniProtKB:O75147}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:O75147}.
DR  UNIPROT: D3YYU8;
DR  UNIPROT: F7AD47;
DR  UNIPROT: Q80WA6;
DR  Pfam: PF07679;
DR  PROSITE: PS50853;
DR  PROSITE: PS50835;
DE  Function: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Acts as a regulator of the Cul7- RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:1990393;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0007030;
GO  GO:0007156;
GO  GO:0000226;
GO  GO:0050775;
GO  GO:0034067;
GO  GO:0007088;
GO  GO:0010842;
GO  GO:0007416;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKAGSGDQGSPPCFLRFPRPVRVVSGAEAELKCVVLGEPPPTVVWEKGGQQLVASERLSFPEDGAEHGLLLSGALPTDAG
SQ  VYVCRARNAAGEAYAAAAVTVLEPPAPEPEPESSECPLPTPGTGEGAPKFLTGPQSQWVLRGEEVVLTCQVGGLPEPKLY
SQ  WEKDGMALDEVWDSSHFKLEPGRGASDEGASLTLRILAARLPDSGVYVCHARNAHGHAQAGALLQVHQPRESPPQDPDEN
SQ  PKPVLEPLKGAPKTFWVNEGKHAKFRCYVMGKPEPEIEWHLEGRPLLPDRRRLMYRDRDGGFVLKVLYCQAKDRGLYVCA
SQ  ARNSAGQTLSAVQLHVKEPRLRFTRPLQDVEGREHGIVVLECKVPNSRIPTAWFREDQRLLPCRKYEQIEEGAVRRLVIH
SQ  KLKADDDGVYLCEMRGRVRTVANVTVKGPILKRLPRKLDVLEGENAVLLVETQEAGVQGCWSRDGEDLPDTCQSSCGHMH
SQ  ALVLPGVTREDAGEITFSLGNSRTTTLLRVKCVKHSPPGPPVMVEMFKGQKNKVLLTWKPPEPPPETSFIYRLERQEVGS
SQ  DDWIQCFSIEKAGAVEVPGDCVPTEGDYHFRICTVSEHGRSPHVVFNGSAHLVPTARLVSGLEDVQVYDGEDAVFSLDLS
SQ  AIIQGSWFLNGEQLQSNEPEGQVEPGALRYRIEQKGLQHRLILQAVKHRDSGALVGFSCPGVQDSAALTIQESSVHILSP
SQ  QDKVSLTFTTSERVVLTCELSRVDFPATWYKDGQKVEESESLIVKTEGRKHRLILPEAQVRDSGEFECRTEGVSAFFGVT
SQ  VQDPPVHIVNPQEHVFVHAITSECVRLTCEVDREDTTVHWYKDGQEVEESDIIVLENKGPHHRLVLPAARPSDGGEFQCV
SQ  AGDERAYFTVTITDVFSWIVYPSSEVHVAAVRLERVVLTCELCRPWAEVRWTKDGEEVVESPALLLEKEDTIRRLVLPSV
SQ  QLEDSGEYLCEIHDESASFTITVTEPPVRIIYPQDEVTLHAVSLECVVLTCELSREDAPVRWYKDGLEVEESEALVLQSD
SQ  GPRRRLVLPAAQPEDGGEFVCDAGDDSAFFTVTVTAPPERIVHPAARSLDLQFGAPGHVELRCEVAPAGSQVRWYKDGLE
SQ  VEVSDALQLGAEGPARTLTLPHAQPEDAGEYVCETRDEAVTFNVSLAELPVQFLAPEAAPNPLCVVPGEPVVLSCELSRA
SQ  SAQVFWSHNGSPVQQGEGLELRAEGPRRILCIQAADLAHTGVYTCQSGASPGAPSLSFNVQVAELPPVKLVSELTPLTVH
SQ  EGDDATFQCEVSPPDAEVTWLRNGAVITAGPQLEMVQNGSSRTLIIRGCQLKDAGTVTARAGAADTSARLHVRETELLFL
SQ  RRLQDVRAEEGQDVHLEVETGRVGAAGTVRWIRGGEPLPLDSRLTTAQDGHVHRLSIHGVLLTDQGTYGCESRHDRTLAR
SQ  LSVRPRQLRELRPLEDVTVHEGGSATFQLELSQEGVTGEWAQGGVRLHPGPKCHIQSEGRTHRLVLSGLGLADSGCVSFT
SQ  ADTLRCAARLTVREVPVTIVQGPQDLEVTEGDTATFECELSQTLADVIWEKDGQALSLSPRLRLQALGTRRLLLLRRCCS
SQ  SDAGTYSCVVGTARSEPARLTVREREVSVLRELRSVSAREGDGATFECTVSETEITGRWELGGRALRPGGRVRIRQEGKK
SQ  HILVLSELRTEDTGEVCFQAGPAQSLARLEVEALPLQMCRRPPREKTVLVNRRAVLEVTVSRPGGHVCWMREGVELCPGN
SQ  KYETRRHGTTHSLVIHDVRPEDQGTYSCQAGQDSADTQLLVDGD
//
ID  D3ZZ80;
PN  Obscurin-like protein 1;
GN  Obsl1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O75147}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75147}. Golgi apparatus {ECO:0000250|UniProtKB:O75147}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:O75147}.
DR  UNIPROT: D3ZZ80;
DR  Pfam: PF07679;
DR  PROSITE: PS50853;
DR  PROSITE: PS50835;
DE  Function: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (By similarity). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons. {ECO:0000250, ECO:0000269|PubMed:21572988}.
DE  Reference Proteome: Yes;
GO  GO:1990393;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0007030;
GO  GO:0007156;
GO  GO:0000226;
GO  GO:0050775;
GO  GO:0034067;
GO  GO:0007088;
GO  GO:0010842;
GO  GO:0007416;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKASSGDQGSPPCFLRFPRPVRVVSGAEAELKCVVLGEPPPTVLWEKGGQQLVASERLSFPEDGAEHGLLLSGALPTDAG
SQ  VYVCRARNAAGEAYAAAAVTVLEPPAPEPEPQSSECPPPPPGTGEGAPVFLTGPQSQWVLRGAEVVLTCQVGGLPEPKLY
SQ  WEKDGMALDEVWDSSHYTLEPDRGASDGGASLTLRILAARLPDSGVYVCHARNAHGHAQAGALLQVHQPHENPPQDPDEP
SQ  PVRVIEPLKCAPKTFWVNEGKHAKFRCYVMGKPEPEIEWHLEGRPLLPDRRRLMYRDRDGGFVLKVLYCQAKDRGLYVCA
SQ  ARNSAGQTLSAVQLHVKEPRLRFTRPLQDVEGREHGIVVLECKVPNSRIPTAWFREDQRLLPCRKYEQIEEGTVRRLVIH
SQ  RLKADDDGVYLCEMRGRVRTVANVTVKGPILKRLPRKLDVLEGENAVLLVETQEAGVQGCWSRDGEELPATCQSSCGHMH
SQ  ALVLPGVTREDAGEVTFSLGNSRTTTLLRVKCVKHSPPGPPVLVEMFKGQKNTVLLTWKPPEPPPETSFIYRLERQEVGS
SQ  EDWIQCFSIEKAGAVEVPGDCVPTEGDYRFRICTVSEHGRSPHVVFNGSAHLVPTARLVSGLEDVQVYDGEDAVFSLDLS
SQ  TIIQGSWFLNGELLKNDEAEGQVEPGALRYRIEQKGLQHRLILQTVKHQDNGALVGFICPGVQDSAALSIQESPVHILSP
SQ  QDKVLLTFTTSERVVLTCELSRVDFPATWYKDGQKVEESESLVVKMDGRKHRLILPEAQVRDSGEFECRTEGISAFFSVT
SQ  VQDPPVHIVDPQEHVFVHAITSESVMLTCEVDREDAAVHWYKDGQEVEESAVIVLEKEGPRHRLVLPAAQPSDGGEFQCV
SQ  VGDERAYFTVTITDVSSWIVYPNGKVYVAAVRLERVVLTCELCRPWAEVRWTKDGEEVLESPALLLEKEDTIRRLVLPSV
SQ  QLEDSGEYLCEIHDESASFTITVTEPPVRIIYPQDEVTLHAVSLECVVLTCELSRVDAPVRWYKDGLEVEETEALVLQSD
SQ  GPRRRLVLPAAQPEDGGEFVCDAGDDSAFFTVTVTAPPERIVHPVARSLDLQFGAPGHVELRCEVAPAGSQVRWYKDGLE
SQ  VEVSDALQLGAEGPARTLTLPHAQPEDAGEYVCETRDEAVTFNVSLAELPVQFLAPEAVPNPLCVVPGEPVMLSCELSRA
SQ  SAHVSWSHNGNPVKQGEGLELRAEGPRRILCIQAADLAHTGVYTCQSGTAPGAPSLSFNVQVAEPPPVKLVSELTPLTVH
SQ  EGDDATFQCEVSPPDAEVTWLRNGAIVTPGPQLEMVHSGSSRTLIIRGCQLKDAGTVTARAGATDTSARLHVRETELLFL
SQ  RRLQDVRAEEGQDVYLEVETGRVGAPGAVRWLRGGEPLPLDSRLTTAQDGHVHRLSIHGVLLTDQGTYGCESHHDRTLAR
SQ  LSVRPRQLRELRPLEDVTVHEGGSATFQLELSQEGVTGEWAQGGVRLHPGPKCHIHSEGRTHCLVLSGLGLADSGCISFT
SQ  ADTLRCAARLTVREVPVTIVQGPQDLEVTEGDTATFECELSQTLADVIWEKDGQALSLSPRLRLQSLGTRRLLLLRRCSS
SQ  SDAGTYCCAVGTARSGPARLTVREREVSVLGELRSLSAREGDSATFECTVSESETTGRWELGGRALRPGGRVRIRQEGKK
SQ  HILVLSELRTEDTGEVCFQAGPAQSLARLEVEALPLQMCRRPPREKTVLVDRRAVLEVTVSRPGGHVCWMREGVELCPGS
SQ  KYEMRSHGTTHSLVIHDVRPEDQGTYSCQAGQDSADTQLLVEGDD
//
ID  P41933;
PN  Nuclear hormone receptor family member odr-7;
GN  odr;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm, perinuclear region.
DR  UNIPROT: P41933;
DR  UNIPROT: C3U4U8;
DR  UNIPROT: C3U4U9;
DR  UNIPROT: C3U4V2;
DR  Pfam: PF00105;
DR  PROSITE: PS00031;
DR  PROSITE: PS51030;
DE  Function: Required for the function of one pair of chemosensory neurons called AWA neurons that are involved in chemotaxis to volatile odorants. Acts in a pathway that specifies olfactory neuronal fate. Regulates the transcription of olfactory signaling molecules such as odr-10 that specify AWA neuron identity and function. Represses the expression in AWA neurons of factors such as str-2 which specify AWC neuron identity. {ECO:0000269|PubMed:10421632, ECO:0000269|PubMed:11018015, ECO:0000269|PubMed:11546744, ECO:0000269|PubMed:14704165, ECO:0000269|PubMed:8601313}.
DE  Reference Proteome: Yes;
DE  Interaction: G5EFI7; IntAct: EBI-6731847; Score: 0.00
DE  Interaction: O45291; IntAct: EBI-6736675; Score: 0.00
DE  Interaction: Q19418; IntAct: EBI-6740943; Score: 0.00
DE  Interaction: Q22289; IntAct: EBI-6740956; Score: 0.00
DE  Interaction: Q9NAE4; IntAct: EBI-6740969; Score: 0.00
DE  Interaction: Q9TXN8; IntAct: EBI-6740982; Score: 0.00
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001228;
GO  GO:0003700;
GO  GO:0043565;
GO  GO:0008270;
GO  GO:0022401;
GO  GO:0050918;
GO  GO:0045944;
GO  GO:0006357;
GO  GO:0007608;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MIVPDTEGLLIYSYGLMYGSYCMACQMLIPHFQCIPGIFPNFRISTELIKTMTDKLEQPNNNVPQQPWGPFPPAFGGRPS
SQ  GEQTDGNPGEFDNDAAHQQTAPFMTHFFPRIGLQFPDFTEYQRFNGFQRNAFFPNPFGSQFTGQAFAQSFPLHNSMTTMD
SQ  GFNLTHAPHPFSTNTNSTKPKDIENTVQSTIKHSSENIQDKPPVLSVEYPVKYDSELKFDANVDFTAVPKQESSDDSTLK
SQ  NLKKSDQQLQQPQQFTFPPPLLAEKSFEQPRMREDVLPFHPQFYPAPLDMGTNFKQEMRTPPIDGHIDYRKFDASGKRME
SQ  FQPPGALHDCQVCLSTHANGLHFGARTCAACAAFFRRTISDDKRYVCKRNQRCNNASRDGTGYRKICRSCRMKRCLEIGM
SQ  LPENVQHKRNRRDSGSPPRKTPFDTFFNGFYPSFQPSGSAAQPITVSSSESPRHTTN
//
ID  Q9QXY4;
PN  Opioid growth factor receptor;
GN  Ogfr;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11890982}. Nucleus {ECO:0000269|PubMed:11890982}. Note=The OGF/OGFR complex is probably translocated to the nucleus. Colocalized with OGF in the perinuclear region.
DR  UNIPROT: Q9QXY4;
DR  Pfam: PF04664;
DE  Function: Receptor for opioid growth factor (OGF), also known as Met- enkephalin. Seems to be involved in growth regulation.
DE  Reference Proteome: Yes;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0140625;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDPDCDSTWEEESEEDGEDGQADDTTDEDTGDDDGDAEEARPSLFQSRMTGYRNWRAMQDMQRYRHNYPDLTDQDCNGD
SQ  MCNLSFYKNEICFQPNGALIEDILQNWKDNYDLLEENHSYIQWLFPLREPGVNWHAKPLTLKEVEAFKSSKEVRERLVRA
SQ  YELMLGFYGFHLEDRGTGAVCRAQNFQPRFHNLNSHSHNNLRITRILKSLGELGLEHYQAPLVRFFLEETLVQHKLPSVR
SQ  QSALDYFLFAVRCRHQRRELVYFAWEHFKPRREFVWGPRDKLRRFKPQTIPQPLTGPGQADKDEGSRDPSQEAGTQGRTC
SQ  GSGRDLSGDSGTAEDPSLLNTKPSDGGTLDGNQRDEAKSLSPKESKKRKLEGNRQEQVPGEADPQGVSEVEKIALNLEEC
SQ  ALSPISQEPREAEPPCPVARVANEVRKRRKVEEGAEGDGVVSNTQMQASALPPTPSECPEAQKDGNGPEDSNSQVGAEDS
SQ  KSQVGPEDPNSQVGLEDPNSQVGPEDPNSQVGPEDPNSQVGPEDPNSQVGPEDPNSQVVGPEQAASKSPVEDPDSDTMGT
SQ  SVDESEELARIEASAEPPKP
//
ID  O18158;
PN  UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase;
GN  ogt;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:9083068}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9083068}.
DR  UNIPROT: O18158;
DR  UNIPROT: Q21232;
DR  Pfam: PF13844;
DR  Pfam: PF00515;
DR  Pfam: PF13181;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. {ECO:0000250|UniProtKB:O15294}.
DE  Reference Proteome: Yes;
DE  Interaction: Q17446; IntAct: EBI-332876; Score: 0.00
DE  Interaction: P83351; IntAct: EBI-16128561; Score: 0.40
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016262;
GO  GO:0097363;
GO  GO:0004722;
GO  GO:0040024;
GO  GO:0006112;
GO  GO:0005977;
GO  GO:0009100;
GO  GO:0019915;
GO  GO:0006470;
GO  GO:0006493;
GO  GO:0000003;
GO  GO:0009266;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKPNYFQSYNKVIGATGEQLAPGAVPPHPVLAPSIAPGGVAGVSAANMANIMQTPGFANLVQQAIRTQLENQAAQQLAV
SQ  NQQFQLNGATAVQQQLLLTPQQSLAQPIALAPQPTVVLNGVSETLKKVTELAHRQFQSGNYVEAEKYCNLVFQSDPNNLP
SQ  TLLLLSAINFQTKNLEKSMQYSMLAIKVNNQCAEAYSNLGNYYKEKGQLQDALENYKLAVKLKPEFIDAYINLAAALVSG
SQ  GDLEQAVTAYFNALQINPDLYCVRSDLGNLLKAMGRLEEAKVCYLKAIETQPQFAVAWSNLGCVFNSQGEIWLAIHHFEK
SQ  AVTLDPNFLDAYINLGNVLKEARIFDRAVSAYLRALNLSGNHAVVHGNLACVYYEQGLIDLAIDTYKKAIDLQPHFPDAY
SQ  CNLANALKEKGSVVEAEQMYMKALELCPTHADSQNNLANIKREQGKIEDATRLYLKALEIYPEFAAAHSNLASILQQQGK
SQ  LNDAILHYKEAIRIAPTFADAYSNMGNTLKEMGDSSAAIACYNRAIQINPAFADAHSNLASIHKDAGNMAEAIQSYSTAL
SQ  KLKPDFPDAYCNLAHCHQIICDWNDYDKRVRKLVQIVEDQLCKKRLPSVHPHHSMLYPLSHAARIAIAAKHASLCFDKVH
SQ  VQMLGKTPLIHADRFSVQNGQRLRIGYVSSDFGNHPTSHLMQSIPGMHDRSRVEVFCYALSVNDGTNFRSKLMNESEHFV
SQ  DLSQIPCNGKAAEKIAQDGIHILINMNGYTKGARNEIFALRPAPIQVMWLGYPSTSGATFMDYIITDAVTSPLRLANAFT
SQ  EKLAYMPHTFFIGDHAQMLRHLTDKVVVKDKETTERDSCLIMNTANMDPILAKSEIKEQVLDTEVVSGPNKELVRAEMVL
SQ  PVLEVPTEPIKQMIMTGQMTMNVMEDMNVQNGLGQSQMHHKAATGEEIPNSVLLTSRAQYQLPDDAIVFCNFNQLYKIDP
SQ  STLDMWIKILENVPKSILWLLRFPYQGEEHIRKYCVERGLDPSRIVFSNVAAKEEHVRRGQLADVCLDTPLCNGHTTGMD
SQ  ILWTGTPMVTMPLESLASRVATSQLYALGVPELVAKTRQEYVSIAVRLGTDADHLANMRAKVWMARTSSTLFDVKQYCHD
SQ  MEDLLGQMWKRYESGMPIDHITNNTETPHGL
//
ID  Q29RU2;
PN  Oncoprotein-induced transcript 3 protein;
GN  OIT3;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}. Note=Can be secreted into blood. {ECO:0000250}.
DR  UNIPROT: Q29RU2;
DR  Pfam: PF00100;
DR  PROSITE: PS00010;
DR  PROSITE: PS01187;
DR  PROSITE: PS51034;
DE  Function: May be involved in hepatocellular function and development. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005509;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPQLLLLACLLIIVTRVAPRALDPCSAYISLNEPWRNTEHQFDESRGSPLCDNSVDGEWYRFTGMAGDAMPTFCIPENHC
SQ  GTHAPVWLNGSHPLEGDGIVQRQACASFNGNCCLWNTTVEVKSCPGGYYVYRLTKPSVCFHVYCGHFYDICDDDCHGSCL
SQ  GTSECTCAPGTVLGPDRQTCFDENECEQNNGGCSEICVNLKNSYRCECGIGRVLRSDGKTCEDIEGCHNNNGGCSHSCLT
SQ  SETGYQCECPRGLVLSEDNHTCQVPVFCKSNTIEVSIPRDLVGGLELFLTNTSCRGVSNGTHVNILFSLKTCGTVVDVVN
SQ  DKIVASNLVTGLPKQTPGSSGDIIIRTSKLLIPVTCEFPRLYTISEGYVPNLRNTPLEIMSRSHGIFPFTLEIFKDHEFE
SQ  EPYREALPTLKLRDSLYFGIEPLVHVNGLESLVESCFATPTSKIDEIMKYYIIQDGCVSDDSVKQYTSRDHLAKHFQVPV
SQ  FKFVGKDHKEVFLHCRVLVCGMLDERSRCAQGCHRRVRREASTEGEDASGPRSQMLTGGPISIDWED
//
ID  Q8WWZ8;
PN  Oncoprotein-induced transcript 3 protein;
GN  OIT3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:12939600}. Note=Can be secreted into blood.
DR  UNIPROT: Q8WWZ8;
DR  UNIPROT: A0AVP3;
DR  UNIPROT: Q8N1M8;
DR  Pfam: PF00100;
DR  PROSITE: PS00010;
DR  PROSITE: PS01187;
DR  PROSITE: PS51034;
DR  OMIM: 609330;
DR  DisGeNET: 170392;
DE  Function: May be involved in hepatocellular function and development. {ECO:0000269|PubMed:12939600}.
DE  Reference Proteome: Yes;
DE  Interaction: P50222; IntAct: EBI-10277774; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24315346; Score: 0.56
DE  Interaction: Q08AM6; IntAct: EBI-25244773; Score: 0.56
DE  Interaction: P32242; IntAct: EBI-22731180; Score: 0.56
DE  Interaction: Q8IUC1; IntAct: EBI-24605215; Score: 0.56
DE  Interaction: Q5T754; IntAct: EBI-24631199; Score: 0.56
DE  Interaction: P49639; IntAct: EBI-24571845; Score: 0.56
DE  Interaction: Q9UGL9; IntAct: EBI-24579040; Score: 0.56
DE  Interaction: Q5T751; IntAct: EBI-24579925; Score: 0.56
DE  Interaction: Q5TA76; IntAct: EBI-24808784; Score: 0.56
DE  Interaction: Q9NWN3; IntAct: EBI-25228050; Score: 0.56
DE  Interaction: Q92844; IntAct: EBI-20737844; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
GO  GO:0009986;
GO  GO:0005615;
GO  GO:0005635;
GO  GO:0005509;
GO  GO:0005201;
GO  GO:1903118;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPPFLLLTCLFITGTSVSPVALDPCSAYISLNEPWRNTDHQLDESQGPPLCDNHVNGEWYHFTGMAGDAMPTFCIPENHC
SQ  GTHAPVWLNGSHPLEGDGIVQRQACASFNGNCCLWNTTVEVKACPGGYYVYRLTKPSVCFHVYCGHFYDICDEDCHGSCS
SQ  DTSECTCAPGTVLGPDRQTCFDENECEQNNGGCSEICVNLKNSYRCECGVGRVLRSDGKTCEDVEGCHNNNGGCSHSCLG
SQ  SEKGYQCECPRGLVLSEDNHTCQVPVLCKSNAIEVNIPRELVGGLELFLTNTSCRGVSNGTHVNILFSLKTCGTVVDVVN
SQ  DKIVASNLVTGLPKQTPGSSGDFIIRTSKLLIPVTCEFPRLYTISEGYVPNLRNSPLEIMSRNHGIFPFTLEIFKDNEFE
SQ  EPYREALPTLKLRDSLYFGIEPVVHVSGLESLVESCFATPTSKIDEVLKYYLIRDGCVSDDSVKQYTSRDHLAKHFQVPV
SQ  FKFVGKDHKEVFLHCRVLVCGVLDERSRCAQGCHRRMRRGAGGEDSAGLQGQTLTGGPIRIDWED
//
ID  Q8R4V5;
PN  Oncoprotein-induced transcript 3 protein;
GN  Oit3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:15346761}. Note=Secreted into blood in a truncated form.
DR  UNIPROT: Q8R4V5;
DR  UNIPROT: P97806;
DR  UNIPROT: Q811T0;
DR  UNIPROT: Q8C9U1;
DR  Pfam: PF00100;
DR  PROSITE: PS51034;
DE  Function: May be involved in hepatocellular function and development. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0005615;
GO  GO:0005635;
GO  GO:0005509;
GO  GO:0005201;
GO  GO:1903118;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPLSLLLTCLSTTVTLVSPAVLDPCSAYISLNEPWRNTDHQFDESQNQPLCDNHMNGEWYRFTGMAGDAMPTFCIPENHC
SQ  GTHAPVWLNGSHPLEEDGIVQRQACASFKGNCCLWNATVEVKACPRGYYVYRLARPSVCFHVYCGHFYDICDEDCHGNCL
SQ  DTTECACSPGTSLGPDGQTCFDENECEHNNGGCSEICVNLKNSHRCACGVGRVLRSDGKTCEDIEGCHNNNGGCSHSCLG
SQ  SEEGYQCECPRGLVLSEDNHTCQVPVLCKSSAIEVSVPRELVGGLELFLTNTSCRGVSNGTHVNIVFSLKTCGTVVDVVN
SQ  DKIVASNIVTGLPKETPGSSGDIIIRTSKLLIPVTCEFPRLYTISEGYVPNLRNAPLEIRSRNHGIFPFTLEIFKDHEFE
SQ  EPYRETLPTLKLRDSLYFGIEPLVHVNGLESLVESCFATPTAKMDEILKYYLIQDGCVSDDSVKQYSSRDHLAKHFQAPV
SQ  FKFVGKDHKEVFLHCRVLVCGVLDERSRCAQGCHRRVRREVGEDEDSAGLQSQTLTGGPIAIDWED
//
ID  Q6V0K7;
PN  Oncoprotein-induced transcript 3 protein;
GN  Oit3;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}. Note=Can be secreted into blood. {ECO:0000250}.
DR  UNIPROT: Q6V0K7;
DR  Pfam: PF00100;
DR  PROSITE: PS51034;
DE  Function: May be involved in hepatocellular function and development. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0005615;
GO  GO:0005635;
GO  GO:0005509;
GO  GO:0005201;
GO  GO:1903118;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPLSLLLACLFTTVTLQSPVVLDPCSAYISLNEPWRNTDHQFDESQSQPLCDNHMDGEWYRFTGMAGDAMPTFCIPENHC
SQ  GTHAPVWLNGSHPLEGDGIVQRQACASFKGNCCLWNTTVEVKACPGGYYVYRLAKPSVCFHIYCGHFYDICDEDCHGSCL
SQ  DTTECACSPGTSLGPDGQTCFDENECEHNNGGCSEICVNLKNSHRCACGVGRVLRSDGKTCEDIEGCHSNNGGCSHSCLG
SQ  SEKGYQCECPRGLVLSEDNHTCQVPVLCKSSAIEVSVPRELVGGLELFLTNTSCRGVSNGTHVNIIFSLKTCGTVVDVVN
SQ  DKIVASNLVTGLPKQTPGSSGDIIIRTSKLLIPVTCEFPRLYTISEGYVPNLRNAPLEIRSRNHGIFPFTLEIFKDHEFE
SQ  EPYRETLPTLKLRDSLYFGIEPLVHVSGLESLVESCFATPTAKVDEILKYYLIRDGCVSDDSVKQYSSRDHLAKHFQVPV
SQ  FKFVGKDHKEVFLHCRVLVCGVLDERSRCAQGCHRRVRREAGEDEDSAGLQSQTLTGGPISIDWEE
//
ID  O60175;
PN  Protein OPI10 homolog;
GN  SPBC21H7;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O60175;
DR  Pfam: PF05603;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: O59855; IntAct: EBI-9392528; Score: 0.40
DE  Interaction: Q10265; IntAct: EBI-9392545; Score: 0.40
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGAICAGRLVQTNLQQVADNQFVFQLDSAESLNHIVVFLLPNSPFPVGMGAKVYFQWPGKPFQFLGYLTNEKPSAIFRL
SQ  KNTIQTLSENENCVGITAMLGISVEPLTNFTETPAVSTSASNVIAKPLPPVTSVAQKILTNLYNFLASFATSQLPPNSIG
SQ  LGDLRPNDTFIPLRVFQDWHAKFLNKLSNNPNFLDSEDQI
//
ID  P51490;
PN  Short-wave-sensitive opsin 1;
GN  OPN1SW;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P03999}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P03999}.
DR  UNIPROT: P51490;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  PROSITE: PS00238;
DE  Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (By similarity). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (By similarity). Involved in ensuring correct abundance and localization of retinal membrane proteins (By similarity). May increase spectral sensitivity in dim light (By similarity). {ECO:0000250|UniProtKB:P03999, ECO:0000250|UniProtKB:P51491}.
DE  Reference Proteome: Yes;
GO  GO:0120199;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0005886;
GO  GO:0008020;
GO  GO:0071482;
GO  GO:0071492;
GO  GO:0007186;
GO  GO:0007602;
GO  GO:0007601;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKMSEEEEFLLFKNISLVGPWDGPQYHLAPVWAFHLQAVFMGFVFFVGTPLNATVLVATLRYRKLRQPLNYILVNVSLG
SQ  GFIYCIFSVFIVFITSCYGYFVFGRHVCALEAFLGCTAGLVTGWSLAFLAFERYIIICKPFGNFRFSSKHALMVVVATWT
SQ  IGIGVSIPPFFGWSRFVPEGLQCSCGPDWYTVGTKYYSEYYTWFLFIFCYIVPLSLICFSYSQLLGALRAVAAQQQESAS
SQ  TQKAEREVSHMVVVMVGSFCLCYTPYAALAMYIVNNRNHGVDLRLVTIPAFFSKSACVYNPIIYCFMNKQFRACIMEMVC
SQ  GKPMTDESELSSSQKTEVSTVSSSQVGPN
//
ID  P03999;
PN  Short-wave-sensitive opsin 1;
GN  OPN1SW;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:2937147, ECO:0000269|PubMed:31380578, ECO:0000269|PubMed:31730232}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:30168605}.
DR  UNIPROT: P03999;
DR  UNIPROT: Q13877;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  PROSITE: PS00238;
DR  OMIM: 190900;
DR  OMIM: 613522;
DR  DisGeNET: 611;
DE  Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (Probable). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (By similarity). Involved in ensuring correct abundance and localization of retinal membrane proteins (By similarity). May increase spectral sensitivity in dim light (By similarity). {ECO:0000250|UniProtKB:P51491, ECO:0000305|PubMed:2937147}.
DE  Disease: Tritan color blindness (CBT) [MIM:190900]: A disorder of vision characterized by a selective deficiency of blue spectral sensitivity. {ECO:0000269|PubMed:1386496, ECO:0000269|PubMed:1531728, ECO:0000269|PubMed:23022137}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9GZY8; IntAct: EBI-24523945; Score: 0.56
GO  GO:0120199;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0097381;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0005886;
GO  GO:0008020;
GO  GO:0038023;
GO  GO:0071482;
GO  GO:0071492;
GO  GO:0007186;
GO  GO:0007602;
GO  GO:0007165;
GO  GO:0007601;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRKMSEEEFYLFKNISSVGPWDGPQYHIAPVWAFYLQAAFMGTVFLIGFPLNAMVLVATLRYKKLRQPLNYILVNVSFGG
SQ  FLLCIFSVFPVFVASCNGYFVFGRHVCALEGFLGTVAGLVTGWSLAFLAFERYIVICKPFGNFRFSSKHALTVVLATWTI
SQ  GIGVSIPPFFGWSRFIPEGLQCSCGPDWYTVGTKYRSESYTWFLFIFCFIVPLSLICFSYTQLLRALKAVAAQQQESATT
SQ  QKAEREVSRMVVVMVGSFCVCYVPYAAFAMYMVNNRNHGLDLRLVTIPSFFSKSACIYNPIIYCFMNKQFQACIMKMVCG
SQ  KAMTDESDTCSSQKTEVSTVSSTQVGPN
//
ID  P51491;
PN  Short-wave-sensitive opsin 1;
GN  Opn1sw;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P03999}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000269|PubMed:21219924}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:21219924}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P03999}.
DR  UNIPROT: P51491;
DR  UNIPROT: Q548Z8;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  PROSITE: PS00238;
DE  Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (By similarity). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (PubMed:21219924, PubMed:25416279). Involved in ensuring correct abundance and localization of retinal membrane proteins (PubMed:25416279). May increase spectral sensitivity in dim light (PubMed:11055434). {ECO:0000250|UniProtKB:P03999, ECO:0000269|PubMed:11055434, ECO:0000269|PubMed:21219924, ECO:0000269|PubMed:25416279}.
DE  Reference Proteome: Yes;
GO  GO:0044297;
GO  GO:0120199;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0005886;
GO  GO:0043195;
GO  GO:0008020;
GO  GO:0071482;
GO  GO:0071492;
GO  GO:0007186;
GO  GO:0007602;
GO  GO:0007601;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGEDDFYLFQNISSVGPWDGPQYHLAPVWAFRLQAAFMGFVFFVGTPLNAIVLVATLHYKKLRQPLNYILVNVSLGGFL
SQ  FCIFSVFTVFIASCHGYFLFGRHVCALEAFLGSVAGLVTGWSLAFLAFERYVVICKPFGSIRFNSKHALMVVLATWIIGI
SQ  GVSIPPFFGWSRFIPEGLQCSCGPDWYTVGTKYRSEYYTWFLFIFCFIIPLSLICFSYSQLLRTLRAVAAQQQESATTQK
SQ  AEREVSHMVVVMVGSFCLCYVPYAALAMYMVNNRNHGLDLRLVTIPAFFSKSSCVYNPIIYCFMNKQFRACILEMVCRKP
SQ  MADESDVSGSQKTEVSTVSSSKVGPH
//
ID  P60573;
PN  Short-wave-sensitive opsin 1;
GN  OPN1SW;
OS  9597;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P03999}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P03999}.
DR  UNIPROT: P60573;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  PROSITE: PS00238;
DE  Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (By similarity). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (By similarity). Involved in ensuring correct abundance and localization of retinal membrane proteins (By similarity). May increase spectral sensitivity in dim light (By similarity). {ECO:0000250|UniProtKB:P03999, ECO:0000250|UniProtKB:P51491}.
DE  Reference Proteome: Yes;
GO  GO:0120199;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0097381;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0004930;
GO  GO:0009881;
GO  GO:0071492;
GO  GO:0007602;
GO  GO:0007601;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRKMSEEEFYLFKNISSVGPWDGPQYHIAPVWAFYLQAAFMGTVFLIGFPLNAMVLVATLRYKKLRQPLNYILVNVSFGG
SQ  FLLCIFSVFPVFVASCNGYFVFGRHVCALEGFLGTVAGLVTGWSLAFLAFERYIVICKPFGNFRFSSKHALTVVLATWTI
SQ  GIGVSIPPFFGWSRFIPEGLQCSCGPDWYTVGTKYRSESYTWFLFIFCFIVPLSLICFSYTQLLRALKAVAAQQQESATT
SQ  QKAEREVSRMVVVMVGSFCVCYVPYAAFAMYMVNNRNHGLDLRLVTIPSFFSKSACIYNPIIYCFMNKQFQACIMKMVCG
SQ  KAMTDESDTCSSQKTEVSTVSSTQVGPN
//
ID  P60015;
PN  Short-wave-sensitive opsin 1;
GN  OPN1SW;
OS  9598;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P03999}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P03999}.
DR  UNIPROT: P60015;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  PROSITE: PS00238;
DE  Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (By similarity). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (By similarity). Involved in ensuring correct abundance and localization of retinal membrane proteins (By similarity). May increase spectral sensitivity in dim light (By similarity). {ECO:0000250|UniProtKB:P03999, ECO:0000250|UniProtKB:P51491}.
DE  Reference Proteome: Yes;
GO  GO:0120199;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0097381;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0005886;
GO  GO:0008020;
GO  GO:0071482;
GO  GO:0071492;
GO  GO:0007186;
GO  GO:0007602;
GO  GO:0007601;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRKMSEEEFYLFKNISSVGPWDGPQYHIAPVWAFYLQAAFMGTVFLIGFPLNAMVLVATLRYKKLRQPLNYILVNVSFGG
SQ  FLLCIFSVFPVFVASCNGYFVFGRHVCALEGFLGTVAGLVTGWSLAFLAFERYIVICKPFGNFRFSSKHALTVVLATWTI
SQ  GIGVSIPPFFGWSRFIPEGLQCSCGPDWYTVGTKYRSESYTWFLFIFCFIVPLSLICFSYTQLLRALKAVAAQQQESATT
SQ  QKAEREVSRMVVVMVGSFCVCYVPYAAFAMYMVNNRNHGLDLRLVTIPSFFSKSACIYNPIIYCFMNKQFQACIMKMVCG
SQ  KAMTDESDTCSSQKTEVSTVSSTQVGPN
//
ID  Q63652;
PN  Short-wave-sensitive opsin 1;
GN  Opn1sw;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P03999}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P03999}.
DR  UNIPROT: Q63652;
DR  UNIPROT: O70363;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  PROSITE: PS00238;
DE  Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (By similarity). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (By similarity). Involved in ensuring correct abundance and localization of retinal membrane proteins (By similarity). May increase spectral sensitivity in dim light (By similarity). {ECO:0000250|UniProtKB:P03999, ECO:0000250|UniProtKB:P51491}.
DE  Reference Proteome: Yes;
GO  GO:0044297;
GO  GO:0120199;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0005886;
GO  GO:0043195;
GO  GO:0008020;
GO  GO:0071482;
GO  GO:0071492;
GO  GO:0007186;
GO  GO:0007602;
GO  GO:0007601;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGEDEFYLFQNISSVGPWDGPQYHIAPVWAFHLQAAFMGFVFFAGTPLNATVLVATLHYKKLRQPLNYILVNVSLGGFL
SQ  FCIFSVFTVFIASCHGYFLFGRHVCALEAFLGSVAGLVTGWSLAFLAFERYLVICKPFGNIRFNSKHALTVVLITWTIGI
SQ  GVSIPPFFGWSRFIPEGLQCSCGPDWYTVGTKYRSEHYTWFLFIFCFIIPLSLICFSYFQLLRTLRAVAAQQQESATTQK
SQ  AEREVSHMVVVMVGSFCLCYVPYAALAMYMVNNRNHGLYLRLVTIPAFFSKSSCVYNPIIYCFMNKQFRACILEMVCRKP
SQ  MTDESDMSGSQKTEVSTVSSSKVGPH
//
ID  O13092;
PN  Short-wave-sensitive opsin 1;
GN  OPN1SW;
OS  39432;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P03999}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P03999}.
DR  UNIPROT: O13092;
DR  Pfam: PF00001;
DR  PROSITE: PS00237;
DR  PROSITE: PS50262;
DR  PROSITE: PS00238;
DE  Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (By similarity). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (By similarity). Involved in ensuring correct abundance and localization of retinal membrane proteins (By similarity). May increase spectral sensitivity in dim light (By similarity). {ECO:0000250|UniProtKB:P03999, ECO:0000250|UniProtKB:P51491}.
DE  Reference Proteome: Yes;
GO  GO:0120199;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0097381;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0004930;
GO  GO:0009881;
GO  GO:0071492;
GO  GO:0007602;
GO  GO:0007601;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKMPEEEEFYLFKNISSVGPWDGPQYHIAPVWAFQLQAAFMGIVFLAGLPLNSMVLVATVRYKKLRHPLNYVLVNVSVG
SQ  GFLLCIFSVLPVFVNSCNGYFVFGRHVCALEGFLGTVAGLVTGWSLAFLAFERYIVICKPFGNFRFSSKHALMVVLTTWT
SQ  IGIGVSIPPFFGWSRYIAEGLQCSCGPDWYTVGTKYRSEYYTWFLFIFCFIVPLSLICFSYAQLLRALKAVAAQQQESAT
SQ  TQKAEREVSRMVVVMVGSFCVCYVPYAALAMYMVNNRNHGLDLRLVSIPAFFSKSSCIYNPIIYCFMNKQFRACIMEMVC
SQ  GKAMTDESDISSSQKTEVSTVSSSQVGPN
//
ID  Q90Z16;
PN  Optineurin;
GN  OPTN;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11777338, ECO:0000269|PubMed:12169269}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:12169269}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}.
DR  UNIPROT: Q90Z16;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis. May act as autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. {ECO:0000269|PubMed:11777338, ECO:0000269|PubMed:12169269}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0006914;
GO  GO:0090161;
GO  GO:0034067;
GO  GO:0043122;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSKPQIRPAENGEHCRSKMENGMDSMAPPTLSTYTPEEMVQQMKELITENNELKEAMKLHNQAMKDRYEELSIWREKQK
SQ  EEREFYETKFKEAKQCLLAKCVENEQLQQQLQSLKEREEGAEMEGCATPEKEARQLKSKVQRLQAEKADLLAIISELQVK
SQ  LNIASAEDSFVEIGMNEEVNRTARENQDNSSEMASNIAVYIRSKSADESKNLESEELTVSQLLCCLRNETQRREKLEKEL
SQ  QDHKERLSKMENETSNCLESGTQTNQEEESSEAIGSEVESLKKQICALFKELQEAHEKLKEAELIQKKLQEKCQTLEKVN
SQ  SAAATELEEKQQLIYTIKKLELQVESVQAEVKLEQAKTQDEKTRYSSLQDAYNKLLAELTEAMKTISEMKVKEHDRVDKV
SQ  VVEELNAKVLLAEQALAAKQLQMDEMKQLIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLAVQLAYLLK
SQ  EQQNLEDLGRSSLAEMQNRHGARAPDREHSPRLVQRGTGSQEWPEQRNISIYSCPKCEEILPDLDTLQIHVMDCIN
//
ID  Q5RI56;
PN  Optineurin;
GN  optn;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}.
DR  UNIPROT: Q5RI56;
DR  UNIPROT: Q6P3H5;
DR  UNIPROT: Q7SXF4;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0006914;
GO  GO:0007409;
GO  GO:0042742;
GO  GO:0090161;
GO  GO:0034067;
GO  GO:0043122;
GO  GO:0051648;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNGDISHPRGSGPGNLGSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLN
SQ  TMDVENEALKNQVKELEKSGAECLHTELEALRGQILRIQAEKNDLVAMNSELQLKMGQGSPSNSFIEIRIADDDLKVTKD
SQ  LSSVPEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAETNASTEV
SQ  KNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQKKT
SQ  QDEKNNLNQLKDAYTKLFEDYSELQEEKKKRESCVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETISV
SQ  FQAQAEIYSSDFYAERAAREKIHEEKERLATQLEYVKKQNSQLQEEMESLGRHSMSEMQRRHVPRGANPQGPTAPNNLPG
SQ  GRGEWQQQNIPDHACPKCGEVLPDLDSLQIHIMDCII
//
ID  Q96CV9;
PN  Optineurin;
GN  OPTN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Golgi apparatus {ECO:0000269|PubMed:27534431, ECO:0000269|PubMed:27538435}. Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle, autophagosome. Cytoplasmic vesicle. Recycling endosome. Note=Found in the perinuclear region and associates with the Golgi apparatus (PubMed:27534431). Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy. {ECO:0000269|PubMed:27534431}.
DR  UNIPROT: Q96CV9;
DR  UNIPROT: B3KP00;
DR  UNIPROT: D3DRS4;
DR  UNIPROT: D3DRS8;
DR  UNIPROT: Q5T672;
DR  UNIPROT: Q5T673;
DR  UNIPROT: Q5T674;
DR  UNIPROT: Q5T675;
DR  UNIPROT: Q7LDL9;
DR  UNIPROT: Q8N562;
DR  UNIPROT: Q9UET9;
DR  UNIPROT: Q9UEV4;
DR  UNIPROT: Q9Y218;
DR  PDB: 2LO4;
DR  PDB: 2LUE;
DR  PDB: 3VTV;
DR  PDB: 3VTW;
DR  PDB: 5AAZ;
DR  PDB: 5B83;
DR  PDB: 5EOA;
DR  PDB: 5EOF;
DR  PDB: 7CZM;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DR  OMIM: 137760;
DR  OMIM: 602432;
DR  OMIM: 606657;
DR  OMIM: 613435;
DR  DisGeNET: 10133;
DE  Function: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8 (PubMed:27534431). Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation (PubMed:27534431). Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation (PubMed:27538435). In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8- mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000269|PubMed:11834836, ECO:0000269|PubMed:15837803, ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:21617041, ECO:0000269|PubMed:22854040, ECO:0000269|PubMed:27534431, ECO:0000269|PubMed:27538435}. (Microbial infection) May constitute a cellular target for adenovirus E3 14.7 and Bluetongue virus protein NS3 to inhibit innate immune response. {ECO:0000269|PubMed:27538435, ECO:0000269|PubMed:9488477}.
DE  Disease: Glaucoma 1, open angle, E (GLC1E) [MIM:137760]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. {ECO:0000269|PubMed:11834836, ECO:0000269|PubMed:12939304, ECO:0000269|PubMed:14597044, ECO:0000269|PubMed:15226658, ECO:0000269|PubMed:15326130, ECO:0000269|PubMed:15557444, ECO:0000269|PubMed:17389490, ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:22854040, ECO:0000269|PubMed:23669351, ECO:0000269|PubMed:24752605}. Note=The disease is caused by variants affecting the gene represented in this entry. Glaucoma, normal pressure (NPG) [MIM:606657]: A primary glaucoma characterized by intraocular pression consistently within the statistically normal population range. {ECO:0000269|PubMed:15370540}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Amyotrophic lateral sclerosis 12 with or without frontotemporal dementia (ALS12) [MIM:613435]: A form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. ALS12 inheritance can be autosomal dominant or autosomal recessive. There is also sporadic occurrence. ALS12 patients may develop frontotemporal dementia. {ECO:0000269|PubMed:20428114, ECO:0000269|PubMed:27534431}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O14656; IntAct: EBI-25847280; Score: 0.56
DE  Interaction: O60711; IntAct: EBI-25910777; Score: 0.56
DE  Interaction: O75604; IntAct: EBI-24491151; Score: 0.56
DE  Interaction: P14335; IntAct: EBI-11423434; Score: 0.37
DE  Interaction: P61026; IntAct: EBI-10218281; Score: 0.56
DE  Interaction: Q03001; IntAct: EBI-5357450; Score: 0.45
DE  Interaction: Q13023; IntAct: EBI-5357521; Score: 0.45
DE  Interaction: Q29122; IntAct: EBI-15804564; Score: 0.60
DE  Interaction: Q8IZQ1; IntAct: EBI-25910907; Score: 0.56
DE  Interaction: Q8N205; IntAct: EBI-25911446; Score: 0.56
DE  Interaction: Q8N3K9; IntAct: EBI-5662034; Score: 0.00
DE  Interaction: P42858; IntAct: EBI-7473268; Score: 0.82
DE  Interaction: P61007; IntAct: EBI-7473283; Score: 0.53
DE  Interaction: Q9Y3C5; IntAct: EBI-7220058; Score: 0.37
DE  Interaction: Q9Y3C0; IntAct: EBI-756949; Score: 0.95
DE  Interaction: Q9HA65; IntAct: EBI-759844; Score: 0.74
DE  Interaction: Q9UHD2; IntAct: EBI-7821337; Score: 0.90
DE  Interaction: Q8TBZ3; IntAct: EBI-2515515; Score: 0.40
DE  Interaction: P0CK53; IntAct: EBI-2622646; Score: 0.37
DE  Interaction: Q9UPN3; IntAct: EBI-2682283; Score: 0.00
DE  Interaction: Q96NC0; IntAct: EBI-25911422; Score: 0.68
DE  Interaction: P38646; IntAct: EBI-2682326; Score: 0.00
DE  Interaction: P78344; IntAct: EBI-2682339; Score: 0.00
DE  Interaction: P07199; IntAct: EBI-2682313; Score: 0.00
DE  Interaction: Q8N183; IntAct: EBI-2682370; Score: 0.00
DE  Interaction: O95197; IntAct: EBI-2682352; Score: 0.00
DE  Interaction: Q96PV0; IntAct: EBI-2682383; Score: 0.00
DE  Interaction: Q99848; IntAct: EBI-2682431; Score: 0.00
DE  Interaction: Q15018; IntAct: EBI-2682444; Score: 0.00
DE  Interaction: P37231; IntAct: EBI-2684672; Score: 0.00
DE  Interaction: O14949; IntAct: EBI-2690962; Score: 0.00
DE  Interaction: Q8IX21; IntAct: EBI-2690975; Score: 0.00
DE  Interaction: P61513; IntAct: EBI-2690988; Score: 0.00
DE  Interaction: P84996; IntAct: EBI-2691001; Score: 0.00
DE  Interaction: Q15884; IntAct: EBI-8636651; Score: 0.37
DE  Interaction: Q8N448; IntAct: EBI-8638727; Score: 0.67
DE  Interaction: Q9UJX2; IntAct: EBI-8638780; Score: 0.79
DE  Interaction: Q15025; IntAct: EBI-8638815; Score: 0.96
DE  Interaction: Q8N2W9; IntAct: EBI-3941509; Score: 0.37
DE  Interaction: P20929; IntAct: EBI-5357463; Score: 0.27
DE  Interaction: Q14BN4; IntAct: EBI-5357483; Score: 0.45
DE  Interaction: P04275; IntAct: EBI-5357436; Score: 0.45
DE  Interaction: Q9UNH7; IntAct: EBI-5357503; Score: 0.45
DE  Interaction: O75923; IntAct: EBI-5357074; Score: 0.50
DE  Interaction: Q8WZ42; IntAct: EBI-5357536; Score: 0.45
DE  Interaction: A0AUZ9; IntAct: EBI-5661999; Score: 0.00
DE  Interaction: Q00610; IntAct: EBI-5662016; Score: 0.00
DE  Interaction: Q86YF9; IntAct: EBI-5662068; Score: 0.00
DE  Interaction: P02794; IntAct: EBI-5662086; Score: 0.00
DE  Interaction: P11055; IntAct: EBI-5662103; Score: 0.00
DE  Interaction: Q96CV9; IntAct: EBI-10486995; Score: 0.93
DE  Interaction: P0CG47; IntAct: EBI-5662277; Score: 0.00
DE  Interaction: P0CG48; IntAct: EBI-5662311; Score: 0.00
DE  Interaction: P55072; IntAct: EBI-5662328; Score: 0.00
DE  Interaction: Q2M3W8; IntAct: EBI-5662362; Score: 0.00
DE  Interaction: Q9NR11; IntAct: EBI-25911097; Score: 0.56
DE  Interaction: Q9BUY5; IntAct: EBI-24531605; Score: 0.67
DE  Interaction: Q9Y462; IntAct: EBI-5662416; Score: 0.00
DE  Interaction: P63104; IntAct: EBI-6115969; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-6115969; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-6115969; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-6115969; Score: 0.35
DE  Interaction: Q8TF68; IntAct: EBI-6115969; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-6115969; Score: 0.35
DE  Interaction: Q9GZV4; IntAct: EBI-6115969; Score: 0.35
DE  Interaction: Q9NZW5; IntAct: EBI-6115969; Score: 0.35
DE  Interaction: Q00013; IntAct: EBI-6115969; Score: 0.50
DE  Interaction: Q8N5Z5; IntAct: EBI-6115969; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-6873662; Score: 0.37
DE  Interaction: Q99IB8; IntAct: EBI-6929183; Score: 0.49
DE  Interaction: Q8IUH5; IntAct: EBI-9091427; Score: 0.51
DE  Interaction: P61006; IntAct: EBI-9636359; Score: 0.63
DE  Interaction: Q8IYU2; IntAct: EBI-9692526; Score: 0.69
DE  Interaction: Q9GZQ8; IntAct: EBI-9686007; Score: 0.40
DE  Interaction: Q13501; IntAct: EBI-9683643; Score: 0.56
DE  Interaction: P62991; IntAct: EBI-9683699; Score: 0.35
DE  Interaction: P54845; IntAct: EBI-9819121; Score: 0.59
DE  Interaction: Q15038; IntAct: EBI-10235566; Score: 0.72
DE  Interaction: Q86UD4; IntAct: EBI-10258929; Score: 0.56
DE  Interaction: Q8TC07; IntAct: EBI-10273957; Score: 0.81
DE  Interaction: Q8TD17; IntAct: EBI-10284210; Score: 0.56
DE  Interaction: Q9BS34; IntAct: EBI-10297343; Score: 0.72
DE  Interaction: P29882; IntAct: EBI-11736184; Score: 0.37
DE  Interaction: Q8QXP6; IntAct: EBI-11423426; Score: 0.37
DE  Interaction: P01123; IntAct: EBI-11522853; Score: 0.56
DE  Interaction: P40302; IntAct: EBI-11530596; Score: 0.56
DE  Interaction: P40325; IntAct: EBI-11530772; Score: 0.56
DE  Interaction: P40454; IntAct: EBI-11531041; Score: 0.56
DE  Interaction: Q9NTZ6; IntAct: EBI-24303106; Score: 0.72
DE  Interaction: P78424; IntAct: EBI-25257980; Score: 0.56
DE  Interaction: Q12904; IntAct: EBI-24374520; Score: 0.56
DE  Interaction: Q96B67; IntAct: EBI-24377191; Score: 0.56
DE  Interaction: P17021; IntAct: EBI-24397642; Score: 0.56
DE  Interaction: Q9NWF9; IntAct: EBI-24401865; Score: 0.56
DE  Interaction: O00560; IntAct: EBI-24450679; Score: 0.56
DE  Interaction: O75031; IntAct: EBI-24454388; Score: 0.56
DE  Interaction: Q9NRD5; IntAct: EBI-24457528; Score: 0.56
DE  Interaction: Q8IYE1; IntAct: EBI-24553668; Score: 0.56
DE  Interaction: Q99732; IntAct: EBI-12703418; Score: 0.56
DE  Interaction: Q86Y82; IntAct: EBI-21524609; Score: 0.35
DE  Interaction: Q8TBN0; IntAct: EBI-21785841; Score: 0.35
DE  Interaction: O95789; IntAct: EBI-21819321; Score: 0.40
DE  Interaction: O95361; IntAct: EBI-21888746; Score: 0.35
DE  Interaction: Q13490; IntAct: EBI-20736936; Score: 0.35
DE  Interaction: P21580; IntAct: EBI-20737918; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25607852; Score: 0.35
DE  Interaction: Q92870; IntAct: EBI-25831379; Score: 0.56
DE  Interaction: P50570; IntAct: EBI-25844868; Score: 0.56
DE  Interaction: P49821; IntAct: EBI-25876451; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25897979; Score: 0.56
DE  Interaction: Q96GM5; IntAct: EBI-25910593; Score: 0.56
DE  Interaction: Q92185; IntAct: EBI-25910585; Score: 0.56
DE  Interaction: P23297; IntAct: EBI-25910577; Score: 0.56
DE  Interaction: Q99942; IntAct: EBI-25910569; Score: 0.56
DE  Interaction: P10276; IntAct: EBI-25910561; Score: 0.56
DE  Interaction: Q13702; IntAct: EBI-25910553; Score: 0.56
DE  Interaction: P52306; IntAct: EBI-25910545; Score: 0.56
DE  Interaction: P35998; IntAct: EBI-25910532; Score: 0.56
DE  Interaction: P07225; IntAct: EBI-25910524; Score: 0.56
DE  Interaction: P55058; IntAct: EBI-25910516; Score: 0.56
DE  Interaction: Q08499; IntAct: EBI-25910508; Score: 0.56
DE  Interaction: P51582; IntAct: EBI-25910500; Score: 0.56
DE  Interaction: P51608; IntAct: EBI-25910492; Score: 0.56
DE  Interaction: Q15797; IntAct: EBI-25910484; Score: 0.56
DE  Interaction: Q14847; IntAct: EBI-25910466; Score: 0.56
DE  Interaction: Q13123; IntAct: EBI-25910458; Score: 0.56
DE  Interaction: Q02556; IntAct: EBI-25910450; Score: 0.56
DE  Interaction: P28566; IntAct: EBI-25910442; Score: 0.56
DE  Interaction: A0A1C3PI11; IntAct: EBI-25910434; Score: 0.56
DE  Interaction: P04440; IntAct: EBI-25910410; Score: 0.56
DE  Interaction: P10074; IntAct: EBI-25910402; Score: 0.56
DE  Interaction: Q8N1C3; IntAct: EBI-25910394; Score: 0.56
DE  Interaction: Q14894; IntAct: EBI-25910386; Score: 0.56
DE  Interaction: P15169; IntAct: EBI-25910378; Score: 0.56
DE  Interaction: P23528; IntAct: EBI-25910360; Score: 0.56
DE  Interaction: P49450; IntAct: EBI-25910352; Score: 0.56
DE  Interaction: Q9Y5L3; IntAct: EBI-25910344; Score: 0.56
DE  Interaction: P07384; IntAct: EBI-25910336; Score: 0.56
DE  Interaction: O15392; IntAct: EBI-25910328; Score: 0.56
DE  Interaction: P08758; IntAct: EBI-25910320; Score: 0.56
DE  Interaction: P24666; IntAct: EBI-25910312; Score: 0.56
DE  Interaction: P26639; IntAct: EBI-25910610; Score: 0.56
DE  Interaction: Q96PU8; IntAct: EBI-25910793; Score: 0.56
DE  Interaction: Q5VZL5; IntAct: EBI-25910767; Score: 0.56
DE  Interaction: O95340; IntAct: EBI-25910759; Score: 0.56
DE  Interaction: Q9P2R7; IntAct: EBI-25910751; Score: 0.56
DE  Interaction: O95671; IntAct: EBI-25910743; Score: 0.56
DE  Interaction: A2RRN7; IntAct: EBI-25910735; Score: 0.56
DE  Interaction: Q9BUB5; IntAct: EBI-25910717; Score: 0.56
DE  Interaction: O00203; IntAct: EBI-25910709; Score: 0.56
DE  Interaction: Q9Y6Q9; IntAct: EBI-25910701; Score: 0.56
DE  Interaction: O95872; IntAct: EBI-25910693; Score: 0.56
DE  Interaction: Q9ULX5; IntAct: EBI-25910685; Score: 0.56
DE  Interaction: P17029; IntAct: EBI-25910677; Score: 0.56
DE  Interaction: O43829; IntAct: EBI-25910669; Score: 0.56
DE  Interaction: P18206; IntAct: EBI-25910661; Score: 0.56
DE  Interaction: P49459; IntAct: EBI-25910653; Score: 0.56
DE  Interaction: P52888; IntAct: EBI-25910644; Score: 0.56
DE  Interaction: P54274; IntAct: EBI-25910636; Score: 0.56
DE  Interaction: P28347; IntAct: EBI-25910628; Score: 0.56
DE  Interaction: O60927; IntAct: EBI-25910620; Score: 0.56
DE  Interaction: Q13586; IntAct: EBI-25910602; Score: 0.56
DE  Interaction: Q9NSI6; IntAct: EBI-25911013; Score: 0.56
DE  Interaction: Q9Y574; IntAct: EBI-25911005; Score: 0.56
DE  Interaction: Q9Y221; IntAct: EBI-25910992; Score: 0.56
DE  Interaction: Q8WXF7; IntAct: EBI-25910984; Score: 0.56
DE  Interaction: O15195; IntAct: EBI-25910974; Score: 0.56
DE  Interaction: Q9NY26; IntAct: EBI-25910965; Score: 0.56
DE  Interaction: Q9UBT3; IntAct: EBI-25910957; Score: 0.56
DE  Interaction: Q96G97; IntAct: EBI-25910949; Score: 0.56
DE  Interaction: Q96EZ4; IntAct: EBI-25910941; Score: 0.56
DE  Interaction: Q53HV7; IntAct: EBI-25910933; Score: 0.56
DE  Interaction: Q9UDX5; IntAct: EBI-25910925; Score: 0.56
DE  Interaction: Q9Y2X9; IntAct: EBI-25910917; Score: 0.56
DE  Interaction: Q13573; IntAct: EBI-25910899; Score: 0.56
DE  Interaction: Q9UQ53; IntAct: EBI-25910889; Score: 0.56
DE  Interaction: Q9BV73; IntAct: EBI-25910879; Score: 0.56
DE  Interaction: P78410; IntAct: EBI-25910869; Score: 0.56
DE  Interaction: Q8IVL6; IntAct: EBI-25910861; Score: 0.56
DE  Interaction: Q13113; IntAct: EBI-25910843; Score: 0.56
DE  Interaction: P50749; IntAct: EBI-25910835; Score: 0.56
DE  Interaction: P51116; IntAct: EBI-25910819; Score: 0.56
DE  Interaction: P61296; IntAct: EBI-25910811; Score: 0.56
DE  Interaction: Q9Y5Y5; IntAct: EBI-25910785; Score: 0.56
DE  Interaction: Q96HQ0; IntAct: EBI-25911233; Score: 0.56
DE  Interaction: Q6ZNA4; IntAct: EBI-25911031; Score: 0.56
DE  Interaction: Q9C0D3; IntAct: EBI-25911215; Score: 0.56
DE  Interaction: Q5VYS8; IntAct: EBI-25911207; Score: 0.56
DE  Interaction: Q9H6R3; IntAct: EBI-25911199; Score: 0.56
DE  Interaction: Q6YHU6; IntAct: EBI-25911181; Score: 0.56
DE  Interaction: Q6PCB6; IntAct: EBI-25911173; Score: 0.56
DE  Interaction: Q6ZS81; IntAct: EBI-25911165; Score: 0.56
DE  Interaction: Q9BUH8; IntAct: EBI-25911150; Score: 0.56
DE  Interaction: A4FUJ8; IntAct: EBI-25911142; Score: 0.56
DE  Interaction: Q9HBL8; IntAct: EBI-25911134; Score: 0.56
DE  Interaction: Q96G46; IntAct: EBI-25911126; Score: 0.56
DE  Interaction: Q9NRA0; IntAct: EBI-25911118; Score: 0.56
DE  Interaction: Q9UIR0; IntAct: EBI-25911110; Score: 0.56
DE  Interaction: Q9P209; IntAct: EBI-25911089; Score: 0.56
DE  Interaction: Q9NWS9; IntAct: EBI-25911081; Score: 0.56
DE  Interaction: Q8N0Y2; IntAct: EBI-25911073; Score: 0.56
DE  Interaction: Q9BWG1; IntAct: EBI-25911065; Score: 0.56
DE  Interaction: Q8N302; IntAct: EBI-25911057; Score: 0.56
DE  Interaction: Q9BUL9; IntAct: EBI-25911049; Score: 0.56
DE  Interaction: Q6NXG1; IntAct: EBI-25911041; Score: 0.56
DE  Interaction: I6L9D0; IntAct: EBI-25911225; Score: 0.56
DE  Interaction: Q6XD76; IntAct: EBI-25911341; Score: 0.56
DE  Interaction: Q71DI3; IntAct: EBI-25911349; Score: 0.56
DE  Interaction: Q96QE2; IntAct: EBI-25911323; Score: 0.56
DE  Interaction: Q9BYZ2; IntAct: EBI-25911315; Score: 0.56
DE  Interaction: Q86TI2; IntAct: EBI-25911305; Score: 0.56
DE  Interaction: Q96EF9; IntAct: EBI-25911297; Score: 0.56
DE  Interaction: Q8TDB4; IntAct: EBI-25911289; Score: 0.56
DE  Interaction: Q49A26; IntAct: EBI-25911281; Score: 0.56
DE  Interaction: Q8N5A5; IntAct: EBI-25911273; Score: 0.56
DE  Interaction: Q3KNW7; IntAct: EBI-25911265; Score: 0.56
DE  Interaction: Q969S8; IntAct: EBI-25911257; Score: 0.56
DE  Interaction: Q9BYQ4; IntAct: EBI-25911249; Score: 0.56
DE  Interaction: Q6IE81; IntAct: EBI-25911241; Score: 0.56
DE  Interaction: Q496A3; IntAct: EBI-25911454; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-25911438; Score: 0.56
DE  Interaction: Q96LL4; IntAct: EBI-25911430; Score: 0.56
DE  Interaction: Q8TBB0; IntAct: EBI-25911414; Score: 0.56
DE  Interaction: Q8TBE1; IntAct: EBI-25911406; Score: 0.56
DE  Interaction: Q96LX8; IntAct: EBI-25911388; Score: 0.56
DE  Interaction: Q32M92; IntAct: EBI-25911380; Score: 0.56
DE  Interaction: Q8WVJ2; IntAct: EBI-25911367; Score: 0.56
DE  Interaction: Q2NKQ1; IntAct: EBI-25911357; Score: 0.56
DE  Interaction: Q96MN9; IntAct: EBI-25911333; Score: 0.56
DE  Interaction: Q96RQ9; IntAct: EBI-25911462; Score: 0.56
DE  Interaction: Q8IXS6; IntAct: EBI-25911588; Score: 0.56
DE  Interaction: A2RU56; IntAct: EBI-25911580; Score: 0.56
DE  Interaction: Q8N1Y9; IntAct: EBI-25911570; Score: 0.56
DE  Interaction: A1A4Y4; IntAct: EBI-25911546; Score: 0.56
DE  Interaction: Q5TZF3; IntAct: EBI-25911536; Score: 0.56
DE  Interaction: Q0P5N6; IntAct: EBI-25911528; Score: 0.56
DE  Interaction: Q0P5P2; IntAct: EBI-25911520; Score: 0.56
DE  Interaction: Q96EY8; IntAct: EBI-25911512; Score: 0.56
DE  Interaction: Q9BUH6; IntAct: EBI-25911504; Score: 0.56
DE  Interaction: Q8IV33; IntAct: EBI-25911496; Score: 0.56
DE  Interaction: Q3SX64; IntAct: EBI-25911478; Score: 0.56
DE  Interaction: Q8IZS5; IntAct: EBI-25911470; Score: 0.56
DE  Interaction: Q8TB36; IntAct: EBI-25923368; Score: 0.56
DE  Interaction: Q9HAD4; IntAct: EBI-26619290; Score: 0.40
GO  GO:0005776;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0055038;
GO  GO:0005802;
GO  GO:0042802;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0031593;
GO  GO:0008022;
GO  GO:0030674;
GO  GO:0031267;
GO  GO:0006914;
GO  GO:0008219;
GO  GO:0034620;
GO  GO:0050829;
GO  GO:0007030;
GO  GO:0090161;
GO  GO:0043001;
GO  GO:0045087;
GO  GO:0043124;
GO  GO:0001920;
GO  GO:0061734;
GO  GO:0010508;
GO  GO:1904417;
GO  GO:0034067;
GO  GO:0043122;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSHQPLSCLTEKEDSPSESTGNGPPHLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQK
SQ  EERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRTQVVRLQAEKADLLGI
SQ  VSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTGTALSKYRSRSADGAKNYFEHEELTVSQLLLCL
SQ  REGNQKVERLEVALKEAKERVSDFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKL
SQ  SEAELMKKRLQEKCQALERKNSAIPSELNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTHNKLLQEH
SQ  NNALKTIEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERA
SQ  AREKIHEEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDSDQQAYLVQRGAEDRDWRQQRNIPIHSCPKCGE
SQ  VLPDIDTLQIHVMDCII
//
ID  Q95KA2;
PN  Optineurin;
GN  OPTN;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans- Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DR  UNIPROT: Q95KA2;
DR  UNIPROT: Q9BGR3;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8- mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy) and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0006914;
GO  GO:0034620;
GO  GO:0090161;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSHQPLSCLTEKGDSPSESTGNGPPHLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQK
SQ  EERQFFETQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTGDSRLPRAEAEQEKDQLRTQVTRLQAEKADLLGI
SQ  VSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSIGTSRSAEGAKNYLEHEELTVSQLLLCLREGNQK
SQ  VERLEIALKEAKERVSDFEKKASNRSEIETQTEGSTEKENEEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSEAELM
SQ  KKRLQEKCQALERKNSATPSELNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLAMLQLTHNKLLQEHNHALKT
SQ  IEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTVLRAQMEVYCSDFHAERAAREKIH
SQ  EEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDPDQQAYLVQRGTEDRDWQQQRNIPIHSCPKCGEVLPDID
SQ  TLQIHVMDCII
//
ID  Q861Q8;
PN  Optineurin;
GN  OPTN;
OS  9544;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans- Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DR  UNIPROT: Q861Q8;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8- mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy) and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0006914;
GO  GO:0034620;
GO  GO:0090161;
GO  GO:0034067;
GO  GO:0043122;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSHQPLSCLTEKGDSPSESTGNGPPHLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQK
SQ  EERQFFETQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRTQVTRLQAEKADLLGI
SQ  VSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSIGTSRSAEGAKNYLEHEELTVSQLLLCLREGNQK
SQ  VERLEIALKEAKERVSDFEKKASNRSEIETQTEGSTEKENEEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSEAELM
SQ  KKRLQEKCQALERKNSATPSELNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLAMLQLTHNKLLQEHNHALKT
SQ  IEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTVLRAQMEVYCSDFHAERAAREKIH
SQ  EEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDPDQQAYLVQRGTEDRDWQQQRNIPIHSCPKCGEVLPDID
SQ  TLQIHVMDCII
//
ID  Q8K3K8;
PN  Optineurin;
GN  Optn;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15607428}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3- positive cytoplasmic vesicles upon induction of autophagy (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DR  UNIPROT: Q8K3K8;
DR  UNIPROT: A2ASP3;
DR  PDB: 5WQ4;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation. In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000250|UniProtKB:Q96CV9, ECO:0000269|PubMed:26677802}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3U0D9; IntAct: EBI-9683581; Score: 0.35
DE  Interaction: Q64337; IntAct: EBI-9683581; Score: 0.35
DE  Interaction: Q9WUN2; IntAct: EBI-12521947; Score: 0.40
GO  GO:0005776;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0042802;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0031593;
GO  GO:0008022;
GO  GO:0030674;
GO  GO:0031267;
GO  GO:0001155;
GO  GO:0043130;
GO  GO:0006914;
GO  GO:0034620;
GO  GO:0050829;
GO  GO:0007030;
GO  GO:0090161;
GO  GO:0043001;
GO  GO:0045087;
GO  GO:0008285;
GO  GO:0043124;
GO  GO:0043524;
GO  GO:0001920;
GO  GO:0061734;
GO  GO:0010508;
GO  GO:0008284;
GO  GO:0001819;
GO  GO:0010628;
GO  GO:2000179;
GO  GO:0043525;
GO  GO:1904417;
GO  GO:0008104;
GO  GO:0034067;
GO  GO:0043122;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSHQPLSCLTEKGDSPCETPGNGPSNMVHPSLDTFTPEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQK
SQ  EERLLFEMQSKEVKERLKALTHENERLKEELGKFKEKSEKPLEDLTGGYRYPRALEEEVEKLKTQVEQEVEHLKIQVMRL
SQ  RAEKADLLGIVSELQLKLNSGGSSEDSFVEIRMTEGETEGAMKEMKNCPTPTRTDPISLSNCTEDARSCAEFEELTVSQL
SQ  LLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAH
SQ  TKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLL
SQ  QEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHA
SQ  ERAAREKIHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQCRHGARTSDSDQQTYLFQRGAEDRSWQHGQQPRSIPIH
SQ  SCPKCGEVLPDIDTLQIHVMDCII
//
ID  Q7YS99;
PN  Optineurin;
GN  OPTN;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans- Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DR  UNIPROT: Q7YS99;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8- mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy) and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0042802;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0008022;
GO  GO:0030674;
GO  GO:0031267;
GO  GO:0006914;
GO  GO:0034620;
GO  GO:0050829;
GO  GO:0090161;
GO  GO:0043001;
GO  GO:0043124;
GO  GO:0001920;
GO  GO:0061734;
GO  GO:1904417;
GO  GO:0034067;
GO  GO:0043122;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSHQPLSCLTEKGDSPTETTGNGPPTLAHPNLDTFTPHELLQQMRELLIENHQLKEAMKLNNQAMKGRFEELSAWTEKQK
SQ  EERLFFETQSKEAKERLTALSLENEKLKQELGKLKGKTERSFEDLTGDPRVPKAEAEQEVEQLKTQVARLQAEKADLLGI
SQ  VSELQLKLNSGGPSEDSFVEIRMAEGEADAAMKEIKTSPGPIRTDSIDTSKSAEGTRNYLEFEELTVSQLLLCLREGNQK
SQ  VERLEIALKEAKERILDFEKKAKDRSETETQTEEHKEQEKEEEKSPETVGSEVEMLNLQVTTLFKELQEAHTKLSEAELM
SQ  KKRLQEKCQALERKNSATPSELNEKQELLYNNKKLELQVESMRSEIKMEQAKTEEEKSKLTTLQLTHNRLLQEYNNALKT
SQ  IEELKRRESEKVDKVVLQELNGKLEMAEKALASKQLQMDEMKQTIAKQEKDLETMAVLRAQMEVYCSDFHAERAAREKIH
SQ  EEKEQLALQLAVLLKDDNAFEEGASRQSLMEMQSRHGARASDADQQAFLVQRGAEDRNWLQQQQQNIPIHSCPKCGEVLP
SQ  DIDTLLIHVTDCII
//
ID  Q5R923;
PN  Optineurin;
GN  OPTN;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans- Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DR  UNIPROT: Q5R923;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8- mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy) and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0006914;
GO  GO:0034620;
GO  GO:0090161;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSHQPLSCLTEKEDSPTESTGNGPPYLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQK
SQ  EERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRTQVVRLQAEKADLLGI
SQ  VSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTSRALSKYRSRSAEGAKNYLEHEELTVSQLLLCL
SQ  REGNQKVERLEIALKEAKERVSDFEKKASNRSEIETQTEGSTEKENDEEKGLETVGSEVEALNLQVTSLFKELQEAHTKL
SQ  SEAELMKKRLQEKSKLTVLQMTHNKLLREHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEQALASKQLQMDEMKQT
SQ  IAKQEEDLETMTVLRAQMEVYCSDFHAERAAREKIHEQKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSGADQ
SQ  QAYLVQRGAEDRDWRQQRNIPIHSCPKCGEVLPDIDTLQIHVMDCII
//
ID  Q8R5M4;
PN  Optineurin;
GN  Optn;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans- Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DR  UNIPROT: Q8R5M4;
DR  UNIPROT: Q5PQX8;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8- mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy) and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005794;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0042802;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0031593;
GO  GO:0008022;
GO  GO:0030674;
GO  GO:0031267;
GO  GO:0001155;
GO  GO:0043130;
GO  GO:0006914;
GO  GO:0070301;
GO  GO:1905232;
GO  GO:1990090;
GO  GO:0071356;
GO  GO:0034620;
GO  GO:0050829;
GO  GO:0007030;
GO  GO:0090161;
GO  GO:0043001;
GO  GO:0008285;
GO  GO:0043124;
GO  GO:0043524;
GO  GO:0001920;
GO  GO:0003407;
GO  GO:0061734;
GO  GO:0010508;
GO  GO:0008284;
GO  GO:0001819;
GO  GO:0010628;
GO  GO:2000179;
GO  GO:0043525;
GO  GO:1904417;
GO  GO:0008104;
GO  GO:0034067;
GO  GO:0043122;
GO  GO:0042060;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSHQPLSCLTEKGDSSCETPGNGPSNMVHPNLDTFTPEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQK
SQ  EERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERPFEDITGRCGFPRTDLEQEVEQLKRQVEQEVEHLKIQVRR
SQ  LQAEKADLLGIVSELQLKLNSGGSSEDSFVEIRMTEGEAEGAMKEMRNSAGPTRTDSISMGKCTEDARTCVEFEELTVSQ
SQ  LLLCLREGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEA
SQ  HTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKL
SQ  LQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFH
SQ  AERAAREKIHEEKEQLALQLAILLKENNDFEDGGSRQSLMEMQCRHGARTSDSDQQAYLFQRGAEDMSWQHGQQPRSIPI
SQ  HSCPKCGEVLPDIDTLQIHVMDCII
//
ID  Q5M7B7;
PN  Optineurin;
GN  optn;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}.
DR  UNIPROT: Q5M7B7;
DR  Pfam: PF16516;
DR  Pfam: PF11577;
DR  PROSITE: PS51801;
DE  Function: Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0055037;
GO  GO:0070530;
GO  GO:0046872;
GO  GO:0006914;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENELLNHPHNNNMVNGHQDAPYDALSMKNDAEMLEQIKQLLMENNNLKETMKQMNQEMKERLEELLKRHNQHLLDLNSA
SQ  NEVLRKELQSLKEKIATSNQGSAVCSTSEEASENKQLKNQLTRLQAEKADLLGLISELQLKLGSFSEDSFVEIGFSERES
SQ  GEIVNEEKANKILSDHNISYRTNSIKEEGGGTEPEEVAISRLLRSLREETQKVERLEKELFSANKRLAELEKQTSEFCDK
SQ  GVQTEQESEQSQSEVIISSEVDILKEKVKSLNKELQETNDKLNEAKQFKNSLQEKCILLDKRLQENQVDLEEKQSLRYSI
SQ  KKLELQVESQESEIKLEQNKTEAEKNQLGILQVSYDKLNSEYQELRIREIEKVSKVEFNELLEKLDVCEKALAKKQFEID
SQ  EMREMDTKHEEDKETIELLRAQVDVYCADFHAERSARENIHQEKEQLATRLAYMIQEYEKLKEEMMGKQSIEQLQRRHGA
SQ  TSLLDASEGPYLVARGAANMEQPSITVYTCPKCNLTVPDMDTLQIHVMDCIT
//
ID  Q9VSR3;
PN  Translational regulator orb2;
GN  orb2;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Perikaryon {ECO:0000269|PubMed:21900268}. Cell projection, axon {ECO:0000269|PubMed:21900268}. Cell projection, dendrite {ECO:0000269|PubMed:21900268}. Synapse {ECO:0000269|PubMed:22284910, ECO:0000269|PubMed:23083740, ECO:0000269|PubMed:24523662}. Cytoplasm {ECO:0000269|PubMed:21900268, ECO:0000269|PubMed:23209437}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23209437}. Note=In embryonic and larval nervous system, concentrated in the perikaryon (PubMed:21900268). In the adult central nervous system, localizes to synaptic terminals (PubMed:21900268). In the ovary, localizes to the cytoplasm of nurse cells (PubMed:21900268). Localizes to neuromuscular junctions (PubMed:29105522). In spermatocytes, localizes throughout the cytoplasm with higher levels concentrated in a ring around the nucleus (PubMed:23209437). The oligomeric form is enriched in the synaptic region (PubMed:22284910). {ECO:0000269|PubMed:21900268, ECO:0000269|PubMed:22284910, ECO:0000269|PubMed:29105522}. [Isoform A]: Synapse {ECO:0000269|PubMed:26095367}. [Isoform B]: Perikaryon {ECO:0000269|PubMed:26095367}. Cell projection, axon {ECO:0000269|PubMed:26095367}. Synapse {ECO:0000269|PubMed:26095367}.
DR  UNIPROT: Q9VSR3;
DR  UNIPROT: Q95T31;
DR  UNIPROT: Q9VSR2;
DR  PDB: 6VPS;
DR  Pfam: PF16366;
DR  Pfam: PF16367;
DR  PROSITE: PS50102;
DE  Function: RNA-binding protein involved in translational regulation and required for long-term memory (PubMed:28525754, PubMed:29105522). Required in mushroom body gamma neurons for long-term memory in male courtship (PubMed:17965711, PubMed:23083740). Binds to mRNA 3'-UTRs (PubMed:20547833, PubMed:26638074, PubMed:24830287, PubMed:26095367, PubMed:32165583). In its monomeric form, acts as a translational repressor of genes involved in neuronal growth, synapse formation and protein turnover (PubMed:20547833, PubMed:26638074, PubMed:32165583). In its amyloid-like oligomeric form, acts as a translational activator (PubMed:26638074, PubMed:32165583). The monomeric form reduces poly(A) tail length and destabilizes mRNA while the oligomeric form protects and elongates the poly(A) tail and stabilizes mRNA (PubMed:26638074). Involved in asymmetric cell division in the central nervous system (PubMed:21900268). Plays a role in synapse formation and morphology at neuromuscular junctions by modulating the translation of the tumor suppressor brat (PubMed:29105522). Required for the progression of spermatogenesis through meiosis and for sperm differentiation (PubMed:23209437). During sperm differentiation, required to asymmetrically localize and activate the translation of protein kinase aPKC mRNAs which is necessary for spermatid cyst polarization (PubMed:24830287). Also required during spermatid cyst polarization for localization and translation of its own mRNA (PubMed:24830287). {ECO:0000269|PubMed:17965711, ECO:0000269|PubMed:20547833, ECO:0000269|PubMed:21900268, ECO:0000269|PubMed:23083740, ECO:0000269|PubMed:23209437, ECO:0000269|PubMed:24830287, ECO:0000269|PubMed:26095367, ECO:0000269|PubMed:26638074, ECO:0000269|PubMed:28525754, ECO:0000269|PubMed:29105522, ECO:0000269|PubMed:32165583}. [Isoform A]: Required for initial memory acquisition (PubMed:26095367, PubMed:28525754). Following subsequent late dopaminergic pathway activation, recruits isoform B into a complex to activate translation of CaMKII which is required for long-term memory consolidation (PubMed:26095367). {ECO:0000269|PubMed:26095367, ECO:0000269|PubMed:28525754}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8T498; IntAct: EBI-266854; Score: 0.00
DE  Interaction: Q9VXJ9; IntAct: EBI-279104; Score: 0.00
DE  Interaction: Q7KNM2; IntAct: EBI-469685; Score: 0.00
DE  Interaction: Q9VJK3; IntAct: EBI-469712; Score: 0.00
DE  Interaction: P13238; IntAct: EBI-469751; Score: 0.00
DE  Interaction: O76136; IntAct: EBI-469970; Score: 0.00
DE  Interaction: Q27297; IntAct: EBI-470372; Score: 0.00
DE  Interaction: Q961D1; IntAct: EBI-470579; Score: 0.00
DE  Interaction: Q9VYF9; IntAct: EBI-470732; Score: 0.00
DE  Interaction: B6VQA1; IntAct: EBI-470876; Score: 0.00
DE  Interaction: Q27889; IntAct: EBI-471017; Score: 0.00
DE  Interaction: P07548; IntAct: EBI-471068; Score: 0.00
DE  Interaction: Q0E8J0; IntAct: EBI-471797; Score: 0.00
DE  Interaction: Q9VSR3; IntAct: EBI-16193652; Score: 0.60
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0044297;
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0044292;
GO  GO:1990124;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0098793;
GO  GO:0032991;
GO  GO:0045202;
GO  GO:0097060;
GO  GO:0042802;
GO  GO:0003730;
GO  GO:0000900;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0008494;
GO  GO:0008135;
GO  GO:0008356;
GO  GO:0007616;
GO  GO:0008049;
GO  GO:0007141;
GO  GO:2000766;
GO  GO:0017148;
GO  GO:0045727;
GO  GO:0050821;
GO  GO:0007288;
GO  GO:0007291;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDSLKLPKANSATSSASGSNSNLSGSTSASASAATSPTSSGTAVGGILSGAPKSPPGLGSSTPISVRFNANEESLDDILQ
SQ  SFHHSKHSPSGGASGGGDASPTSNLLGMKNNGLGLVVGNCDSLSSSPSQPQMHAGSASLFGNDEVSLRNNFMQAGGFFNR
SQ  KSCGGLPNLNLNKPPQLHQQQHQQQHQQHQQHQQQQQLHQHQQQLSPNLSALHHHHQQQQQLRESGGSHSPSSPGGGGGG
SQ  SPYNGSQAGCSSGGISPIPPQMGVSPKYRRSISFPIKGNSPTAIYGNMHMDGMGSGHMNIPTLSIGNGGGGGSTGMVSAG
SQ  ATGGGDAPYLGNSYGNMMTSNGQMHHGGGLDNSLCDYMRNMSLGGNGGGDGSNSMSLMQDRMRVMGGPKHLSEADAMAIA
SQ  ASGNDPSVYLNALKMGSPSRLSPHSPHSPIQGGNGGNVGDGTARFSRKVFVGGLPPDIDEDEITTSFRRFGPLVVDWPHK
SQ  AESKSYFPPKGYAFLLFQDESSVQQLIDSCITDEDKLYLCVSSPTIKDKAVQIRPWRLADADYVLDATMSLDPRKTVFVG
SQ  GVPRPLKAFELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGDIDKRVEVKPYVLDDQ
SQ  MCDECEGQRCGGKFAPFFCANVTCLQYYCEHCWAVIHSRPGREYHKPLVKEGADRPRAVPFRWC
//
ID  Q9H4L5;
PN  Oxysterol-binding protein-related protein 3;
GN  OSBPL3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16143324}; Peripheral membrane protein {ECO:0000269|PubMed:16143324}. Cytoplasm, cytosol {ECO:0000269|PubMed:16143324}. Cell membrane {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:25447204}; Peripheral membrane protein {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:25447204}. Cell projection, filopodium tip {ECO:0000269|PubMed:18270267}. Nucleus membrane {ECO:0000269|PubMed:16143324}; Peripheral membrane protein {ECO:0000305}. Note=Co-localizes with OSBPL6 at contact sites between the plasma membrane and the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9DBS9}.
DR  UNIPROT: Q9H4L5;
DR  UNIPROT: A4D167;
DR  UNIPROT: A4D168;
DR  UNIPROT: A4D169;
DR  UNIPROT: A4D170;
DR  UNIPROT: A4D171;
DR  UNIPROT: A4D172;
DR  UNIPROT: B8ZZ79;
DR  UNIPROT: B8ZZP0;
DR  UNIPROT: O14591;
DR  UNIPROT: O43357;
DR  UNIPROT: O43358;
DR  UNIPROT: Q8N702;
DR  UNIPROT: Q8N703;
DR  UNIPROT: Q8N704;
DR  UNIPROT: Q8NFH0;
DR  UNIPROT: Q8NFH1;
DR  UNIPROT: Q8NI12;
DR  UNIPROT: Q8NI13;
DR  UNIPROT: Q9BZF4;
DR  UNIPROT: Q9UED6;
DR  PDB: 7CYZ;
DR  PDB: 7DEI;
DR  PDB: 7DEJ;
DR  Pfam: PF01237;
DR  Pfam: PF15409;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DR  OMIM: 606732;
DR  DisGeNET: 26031;
DE  Function: Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER morphology (PubMed:16143324). Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:25447204}.
DE  Reference Proteome: Yes;
DE  Interaction: P61981; IntAct: EBI-7303529; Score: 0.69
DE  Interaction: P31946; IntAct: EBI-7305790; Score: 0.59
DE  Interaction: P31947; IntAct: EBI-7544306; Score: 0.40
DE  Interaction: Q04917; IntAct: EBI-1644092; Score: 0.53
DE  Interaction: P03366; IntAct: EBI-6174791; Score: 0.46
DE  Interaction: Q9Q2G4; IntAct: EBI-6174875; Score: 0.56
DE  Interaction: O95292; IntAct: EBI-8801774; Score: 0.35
DE  Interaction: Q9H6Z9; IntAct: EBI-12503146; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: Q14683; IntAct: EBI-11040305; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104527; Score: 0.35
DE  Interaction: Q9R0Q3; IntAct: EBI-11111571; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P09450; IntAct: EBI-11127973; Score: 0.35
DE  Interaction: Q8N4V1; IntAct: EBI-11130635; Score: 0.35
DE  Interaction: Q15560; IntAct: EBI-24293360; Score: 0.56
DE  Interaction: Q8N8B7; IntAct: EBI-24300464; Score: 0.56
DE  Interaction: Q9Y2P0; IntAct: EBI-24306429; Score: 0.56
DE  Interaction: Q5T619; IntAct: EBI-24314910; Score: 0.56
DE  Interaction: O00444; IntAct: EBI-24327550; Score: 0.56
DE  Interaction: Q3B820; IntAct: EBI-24328349; Score: 0.56
DE  Interaction: Q96EZ8; IntAct: EBI-24331233; Score: 0.56
DE  Interaction: P60520; IntAct: EBI-24342952; Score: 0.56
DE  Interaction: P19544; IntAct: EBI-24350451; Score: 0.56
DE  Interaction: O43395; IntAct: EBI-24351483; Score: 0.56
DE  Interaction: Q08AH1; IntAct: EBI-24352702; Score: 0.56
DE  Interaction: Q9H0R8; IntAct: EBI-24363322; Score: 0.56
DE  Interaction: Q86X27; IntAct: EBI-25244819; Score: 0.56
DE  Interaction: P62913; IntAct: EBI-25248804; Score: 0.56
DE  Interaction: Q8TDR2; IntAct: EBI-24364594; Score: 0.56
DE  Interaction: Q9Y228; IntAct: EBI-24506787; Score: 0.56
DE  Interaction: Q05516; IntAct: EBI-24369800; Score: 0.56
DE  Interaction: Q6ZNH5; IntAct: EBI-24370723; Score: 0.56
DE  Interaction: Q99633; IntAct: EBI-24372266; Score: 0.56
DE  Interaction: Q96MX3; IntAct: EBI-24395759; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-24425275; Score: 0.56
DE  Interaction: Q96C24; IntAct: EBI-24450153; Score: 0.56
DE  Interaction: Q13895; IntAct: EBI-24452794; Score: 0.56
DE  Interaction: Q9Y3M2; IntAct: EBI-11941222; Score: 0.00
DE  Interaction: Q9Y597; IntAct: EBI-11942327; Score: 0.00
DE  Interaction: Q76RG8; IntAct: EBI-14063537; Score: 0.35
DE  Interaction: Q96JJ6; IntAct: EBI-21570881; Score: 0.35
DE  Interaction: Q9NWT6; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: O14965; IntAct: EBI-21639587; Score: 0.35
DE  Interaction: Q96FN4; IntAct: EBI-21659658; Score: 0.35
DE  Interaction: Q9P1U1; IntAct: EBI-21724091; Score: 0.35
DE  Interaction: Q9NZM5; IntAct: EBI-21744295; Score: 0.35
DE  Interaction: O43900; IntAct: EBI-21747441; Score: 0.35
DE  Interaction: O95159; IntAct: EBI-21768155; Score: 0.35
DE  Interaction: Q8N5I2; IntAct: EBI-21770417; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-21787335; Score: 0.35
DE  Interaction: Q13077; IntAct: EBI-21795913; Score: 0.35
DE  Interaction: Q9H0U9; IntAct: EBI-21872538; Score: 0.35
DE  Interaction: A1L0T0; IntAct: EBI-21879063; Score: 0.35
DE  Interaction: Q6NXR4; IntAct: EBI-21899961; Score: 0.40
DE  Interaction: P27348; IntAct: EBI-21902679; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-21909838; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-20200875; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-30830128; Score: 0.44
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0032433;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0097038;
GO  GO:0005886;
GO  GO:0015485;
GO  GO:0032934;
GO  GO:0015248;
GO  GO:0006699;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MMSDEKNLGVSQKLVSPSRSTSSCSSKQGSRQDSWEVVEGLRGEMNYTQEPPVQKGFLLKKRKWPLKGWHKRFFYLDKGI
SQ  LKYAKSQTDIEREKLHGCIDVGLSVMSVKKSSKCIDLDTEEHIYHLKVKSEEVFDEWVSKLRHHRMYRQNEIAMFPHEVN
SQ  HFFSGSTITDSSSGVFDSISSRKRSSISKQNLFQTGSNVSFSCGGETRVPLWLQSSEDMEKCSKDLAHCHAYLVEMSQLL
SQ  QSMDVLHRTYSAPAINAIQGGSFESPKKEKRSHRRWRSRAIGKDAKGTLQVPKPFSGPVRLHSSNPNLSTLDFGEEKNYS
SQ  DGSETSSEFSKMQEDLCHIAHKVYFTLRSAFNIMSAEREKLKQLMEQDASSSPSAQVIGLKNALSSALAQNTDLKERLRR
SQ  IHAESLLLDSPAVAKSGDNLAEENSRDENRALVHQLSNESRLSITDSLSEFFDAQEVLLSPSSSENEISDDDSYVSDISD
SQ  NLSLDNLSNDLDNERQTLGPVLDSGREAKSRRRTCLPAPCPSSSNISLWNILRNNIGKDLSKVAMPVELNEPLNTLQRLC
SQ  EELEYSELLDKAAQIPSPLERMVYVAAFAISAYASSYYRAGSKPFNPVLGETYECIREDKGFQFFSEQVSHHPPISACHA
SQ  ESRNFVFWQDVRWKNKFWGKSMEIVPIGTTHVTLPVFGDHFEWNKVTSCIHNILSGQRWIEHYGEIVIKNLHDDSCYCKV
SQ  NFIKAKYWSTNAHEIEGTVFDRSGKAVHRLFGKWHESIYCGGGSSSACVWRANPMPKGYEQYYSFTQFALELNEMDPSSK
SQ  SLLPPTDTRFRPDQRFLEEGNLEEAEIQKQRIEQLQRERRRVLEENHVEHQPRFFRKSDDDSWVSNGTYLELRKDLGFSK
SQ  LDHPVLW
//
ID  Q9DBS9;
PN  Oxysterol-binding protein-related protein 3;
GN  Osbpl3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30028970}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:30028970}. Cell membrane {ECO:0000269|PubMed:30028970}; Peripheral membrane protein {ECO:0000305}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:Q9H4L5}. Nucleus membrane {ECO:0000250|UniProtKB:Q9H4L5}; Peripheral membrane protein {ECO:0000305}. Note=Co-localizes with OSBPL6 at contact sites between the plasma membrane and the endoplasmic reticulum. {ECO:0000269|PubMed:30028970}.
DR  UNIPROT: Q9DBS9;
DR  UNIPROT: E9QNI5;
DR  Pfam: PF01237;
DR  Pfam: PF15409;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DE  Function: Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes. Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With VAPA, may regulate ER morphology. Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion. Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3. Also binds 25-hydroxycholesterol and cholesterol. {ECO:0000250|UniProtKB:Q9H4L5}.
DE  Reference Proteome: Yes;
DE  Interaction: Q80YT7; IntAct: EBI-16732484; Score: 0.35
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0032433;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0097038;
GO  GO:0005886;
GO  GO:0015485;
GO  GO:0032934;
GO  GO:0015248;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSDEKNLGVSQKLVSPSRSTSSCSSKQGSRQDSWEVVEGLRGEMTYTQEPPVQKGFLLKKRKWPLKGWHKRFFCLEKGIL
SQ  KYAKSQADIEREKLHGCIDVGLSVMSVKKSSKCIDLDTEEHIYHLKVKSEELFDEWVSKLRHHRMYRQNEIAMFPRDVNH
SQ  FFSGSSVTDSAPGVFESVSSRKRSSLSKQNSFPPGSNLSFSCGGDTRVPFWLQSSEDMEKCSKDMAHCHAYLLEMSQLLE
SQ  SMDVLHRTYSAPAINAIQVPKPFSGPVRLHSSNPNLSTLDFGEEKSYSDGSEASSEFSKMQEDLCHVAHKVYFALRSAFN
SQ  SISVEREKLKQLMELDTSPSPSAQVVGLKHALSSALAQNTDLKERLRRIHAESLLLDPPAVPKPGDNLAEENSRDEGRAL
SQ  VHQLSNESRLSITDSLSEFFDAQEVLLSPSSSENEISDDDSYVSDISDNLSLDNLSNDLDNERQTLGPVLESSGEARSKR
SQ  RTSLPAPGPNTSSVSLWSILRNNIGKDLSKVAMPVELNEPLNTLQRLCEELEYSELLDKASRIPSPLERMVYVAAFAISA
SQ  YASSYFRAGSKPFNPVLGETYECIRQDKGFQFFAEQVSHHPPISACHAESGNFVFWQDVRWKNKFWGKSMEIVPIGTTHV
SQ  TLPAFGDHFEWNKVTSCIHNILSGQRWIEHYGEIDIKNLNDDSCHCKVNFIKAKYWSTNAHEIEGTVFDRSGKAVHRLFG
SQ  KWHESIYCGGASSSTCVWRANPMPKGYEQYYGFTQFALELNEMDPLSRSLLPPTDTRFRPDQRLLEEGNIEEAEVQKQRI
SQ  EKLQRERRRVLEENGVEHQPRFFRKSSDDAWVSNGTYLELRKDLGFSKLDHPVLW
//
ID  Q9BZF3;
PN  Oxysterol-binding protein-related protein 6;
GN  OSBPL6;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:30028970}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:26941018, ECO:0000269|PubMed:30028970}; Peripheral membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:14593528}. Cell membrane {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:30028970}; Peripheral membrane protein {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:26941018}; Peripheral membrane protein {ECO:0000305}. Note=Co-localizes with OSBPL3 at contact sites between the plasma membrane and the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q8BXR9}.
DR  UNIPROT: Q9BZF3;
DR  UNIPROT: B4DTW1;
DR  UNIPROT: C4AMC0;
DR  UNIPROT: C4AME4;
DR  UNIPROT: D3DPF6;
DR  UNIPROT: D3DPF7;
DR  UNIPROT: Q4ZG68;
DR  UNIPROT: Q53T68;
DR  UNIPROT: Q59H61;
DR  UNIPROT: Q7Z4Q1;
DR  UNIPROT: Q86V84;
DR  UNIPROT: Q8N9T0;
DR  UNIPROT: Q96SR1;
DR  Pfam: PF01237;
DR  Pfam: PF15409;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DR  OMIM: 606734;
DR  DisGeNET: 114880;
DE  Function: Regulates cellular transport and efflux of cholesterol (PubMed:26941018). Plays a role in phosphatidylinositol-4-phophate (PI4P) turnover at the neuronal membrane (By similarity). Binds via its PH domain PI4P, phosphatidylinositol-4,5-diphosphate, phosphatidylinositol-3,4,5-triphosphate, and phosphatidic acid (By similarity). Weakly binds 25-hydroxycholesterol (PubMed:17428193). {ECO:0000250|UniProtKB:Q8BXR9, ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:26941018}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9BVL2; IntAct: EBI-21639380; Score: 0.35
DE  Interaction: P53350; IntAct: EBI-2372594; Score: 0.53
DE  Interaction: Q9Q2G4; IntAct: EBI-6174875; Score: 0.56
DE  Interaction: O95292; IntAct: EBI-8801774; Score: 0.35
DE  Interaction: Q96IW2; IntAct: EBI-10698427; Score: 0.37
DE  Interaction: Q9H6Z9; IntAct: EBI-12503146; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O43166; IntAct: EBI-11900942; Score: 0.00
DE  Interaction: O60307; IntAct: EBI-11902057; Score: 0.00
DE  Interaction: O75044; IntAct: EBI-11902776; Score: 0.00
DE  Interaction: O75420; IntAct: EBI-11903362; Score: 0.00
DE  Interaction: P21359; IntAct: EBI-11906164; Score: 0.00
DE  Interaction: P30307; IntAct: EBI-11907486; Score: 0.00
DE  Interaction: P56524; IntAct: EBI-11909660; Score: 0.00
DE  Interaction: Q08AD1; IntAct: EBI-11911957; Score: 0.00
DE  Interaction: Q6Y7W6; IntAct: EBI-11919103; Score: 0.00
DE  Interaction: Q86X27; IntAct: EBI-11920973; Score: 0.00
DE  Interaction: Q9BQK8; IntAct: EBI-11929945; Score: 0.00
DE  Interaction: Q9ULR3; IntAct: EBI-11930929; Score: 0.00
DE  Interaction: Q9BST9; IntAct: EBI-11930920; Score: 0.00
DE  Interaction: Q8TEH3; IntAct: EBI-11930911; Score: 0.00
DE  Interaction: Q8IVT5; IntAct: EBI-11930902; Score: 0.00
DE  Interaction: Q5VZ89; IntAct: EBI-11930893; Score: 0.00
DE  Interaction: Q5TCZ1; IntAct: EBI-11930884; Score: 0.00
DE  Interaction: O60573; IntAct: EBI-11930875; Score: 0.00
DE  Interaction: Q9NQT8; IntAct: EBI-11933394; Score: 0.00
DE  Interaction: Q9NRR6; IntAct: EBI-11933906; Score: 0.00
DE  Interaction: Q9P244; IntAct: EBI-11935434; Score: 0.00
DE  Interaction: Q9P2M7; IntAct: EBI-11936126; Score: 0.00
DE  Interaction: Q9UHB6; IntAct: EBI-11936854; Score: 0.00
DE  Interaction: Q9ULJ3; IntAct: EBI-11938866; Score: 0.00
DE  Interaction: Q9Y3M2; IntAct: EBI-11941204; Score: 0.00
DE  Interaction: Q9Y597; IntAct: EBI-11942318; Score: 0.00
DE  Interaction: Q76RG8; IntAct: EBI-14063537; Score: 0.35
DE  Interaction: P22732; IntAct: EBI-21554490; Score: 0.35
DE  Interaction: Q96JJ6; IntAct: EBI-21570881; Score: 0.35
DE  Interaction: Q96IQ9; IntAct: EBI-21636586; Score: 0.35
DE  Interaction: O14965; IntAct: EBI-21639587; Score: 0.35
DE  Interaction: Q9NYP9; IntAct: EBI-21663541; Score: 0.35
DE  Interaction: Q9NZM5; IntAct: EBI-21744295; Score: 0.35
DE  Interaction: O95159; IntAct: EBI-21768155; Score: 0.35
DE  Interaction: Q8N5I2; IntAct: EBI-21770417; Score: 0.35
DE  Interaction: Q15363; IntAct: EBI-21784458; Score: 0.35
DE  Interaction: Q13077; IntAct: EBI-21795913; Score: 0.35
DE  Interaction: P53004; IntAct: EBI-21805374; Score: 0.35
DE  Interaction: P20160; IntAct: EBI-21867396; Score: 0.35
DE  Interaction: A1L0T0; IntAct: EBI-21879063; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-21902679; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-21903886; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21907689; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-21909838; Score: 0.35
DE  Interaction: Q16778; IntAct: EBI-20913574; Score: 0.40
DE  Interaction: P0DOF2; IntAct: EBI-25607852; Score: 0.35
DE  Interaction: O14901; IntAct: EBI-25906103; Score: 0.56
DE  Interaction: Q9GZQ8; IntAct: EBI-30831552; Score: 0.44
GO  GO:0005829;
GO  GO:0031901;
GO  GO:0005789;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0097038;
GO  GO:0005886;
GO  GO:0015485;
GO  GO:0032934;
GO  GO:0015248;
GO  GO:0006699;
GO  GO:0032374;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSSDEKGISPAHKTSTPTHRSASSSTSSQRDSRQSIHILERTASSSTEPSVSRQLLEPEPVPLSKEADSWEIIEGLKIGQ
SQ  TNVQKPDKHEGFMLKKRKWPLKGWHKRFFVLDNGMLKYSKAPLDIQKGKVHGSIDVGLSVMSIKKKARRIDLDTEEHIYH
SQ  LKVKSQDWFDAWVSKLRHHRLYRQNEIVRSPRDASFHIFPSTSTAESSPAANVSVMDGKMQPNSFPWQSPLPCSNSLPAT
SQ  CTTGQSKVAAWLQDSEEMDRCAEDLAHCQSNLVELSKLLQNLEILQRTQSAPNFTDMQANCVDISKKDKRVTRRWRTKSV
SQ  SKDTKIQLQVPFSATMSPVRLHSSNPNLCADIEFQTPPSHLTDPLESSTDYTKLQEEFCLIAQKVHSLLKSAFNSIAIEK
SQ  EKLKQMVSEQDHSKGHSTQMARLRQSLSQALNQNAELRSRLNRIHSESIICDQVVSVNIIPSPDEAGEQIHVSLPLSQQV
SQ  ANESRLSMSESVSEFFDAQEVLLSASSSENEASDDESYISDVSDNISEDNTSVADNISRQILNGELTGGAFRNGRRACLP
SQ  APCPDTSNINLWNILRNNIGKDLSKVSMPVELNEPLNTLQHLCEEMEYSELLDKASETDDPYERMVLVAAFAVSGYCSTY
SQ  FRAGSKPFNPVLGETYECIREDKGFRFFSEQVSHHPPISACHCESKNFVFWQDIRWKNKFWGKSMEILPVGTLNVMLPKY
SQ  GDYYVWNKVTTCIHNILSGRRWIEHYGEVTIRNTKSSVCICKLTFVKVNYWNSNMNEVQGVVIDQEGKAVYRLFGKWHEG
SQ  LYCGVAPSAKCIWRPGSMPTNYELYYGFTRFAIELNELDPVLKDLLPPTDARFRPDQRFLEEGNLEAAASEKQRVEELQR
SQ  SRRRYMEENNLEHIPKFFKKVIDANQREAWVSNDTYWELRKDPGFSKVDSPVLW
//
ID  Q8BXR9;
PN  Oxysterol-binding protein-related protein 6;
GN  Osbpl6;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:14593528}. Cytoplasm, cytosol {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:30028970}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:30028970}; Peripheral membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:14593528}; Peripheral membrane protein {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:30028970}; Peripheral membrane protein {ECO:0000305}. Note=Co-localizes with OSBPL3 at contact sites between the plasma membrane and the endoplasmic reticulum. {ECO:0000269|PubMed:30028970}.
DR  UNIPROT: Q8BXR9;
DR  UNIPROT: Q8BYW2;
DR  Pfam: PF01237;
DR  Pfam: PF15409;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DE  Function: Regulates cellular transport and efflux of cholesterol (By similarity). Plays a role in phosphatidylinositol-4-phophate (PI4P) turnover at the neuronal membrane (PubMed:30028970). Binds via its PH domain PI4P, phosphatidylinositol-4,5-diphosphate, phosphatidylinositol-3,4,5-triphosphate, and phosphatidic acid (PubMed:30028970). Weakly binds 25-hydroxycholesterol (By similarity). {ECO:0000250|UniProtKB:Q9BZF3, ECO:0000269|PubMed:30028970}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9EPK7; IntAct: EBI-17171503; Score: 0.35
GO  GO:0005829;
GO  GO:0031901;
GO  GO:0005789;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0097038;
GO  GO:0005886;
GO  GO:0015485;
GO  GO:0032934;
GO  GO:0015248;
GO  GO:0032374;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSSDEKGISPAHKTSTPTHRSASSSTSSQRESRQSIHVLERTASSSTEPSVSRQLLEPEPIPLSKEADSWEIIEGLKIGQ
SQ  TNVQKPDRHEGFMLKKRKWPLKGWHKRFFVLDNGMLKYSKAPLDIQKGKVHGSIDVGLSVMSIKKKARRIDLDTEEHIYH
SQ  LKVKSQDWFDAWVSKLRHHRLYRQNEIVRSPRDASFHIFPATSTAESSPAANVSVVDGKMQPNSFPWQSPLPCSNSLPAT
SQ  CTTGQSKVAAWLQDSEEMDRCAEDLAHCQSNLVELSKLLQNLEILQRTQSAPNFTDMQANCVDISKKDKRVTRRWRTKSV
SQ  SKDTKIQLQEGPPAKGQFNTTRRRQRLAAAVATTVPFSATMSPVRLHSSNPNLCADIEFQTPPSHLTDPLESSTDYTKLQ
SQ  EEFCLIAQKVHSLLKSAFNSIAIEKEKLKQVVSEQDHNKGHSTQMARLRQSLSQALNQNAELRSRLNRIHSESTICDHVV
SQ  SVNIIPSPDEPGEQIHVSLPLSQQVANESRLSMSESVSEFFDAQEVLLSASSSENEASDDESYISDVSDNISEDNTSVAD
SQ  NISRQILNGELTGGAFRNGRRTCLPAPCPDTSNINLWNILRNNIGKDLSKVSMPVELNEPLNTLQHLCEEMEYSELLDKA
SQ  SETDDPYERMVLVAAFAVSGYCSTYFRAGSKPFNPVLGETYECIREDKGFRFFSEQVSHHPPISACHCESKNFVFWQDIR
SQ  WKNKFWGKSMEILPVGTLNVTLPKYGDYYVWNKVTTCIHNILSGRRWIEHYGEVTLRNTKSSVCICKLTFVKVNYWNSNV
SQ  NEVQGVVIDQEGKVVHRLFGKWHEGLYCGVAPSAKCIWRPGSLPTNYELYYGFTRFAVELNELDPVLKDLLPPTDARFRP
SQ  DQRFLEEGNLEAAAAEKQRVEELQRSRRRYMEENNLEHIPKFFKKVIDANQREAWVSNDTYWELRKDPGFSKVDSPVLW
//
ID  Q9BZF1;
PN  Oxysterol-binding protein-related protein 8;
GN  OSBPL8;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17991739, ECO:0000269|PubMed:26206935}; Single-pass membrane protein {ECO:0000269|PubMed:17991739}. Nucleus membrane {ECO:0000269|PubMed:21698267}. Note=The presence of the N-terminus extension contains an overall negative charge that may explain the weak localization to the cortical endoplasmic reticulum (Probable). {ECO:0000305|PubMed:26206935}. [Isoform 3]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26206935}; Single-pass membrane protein. Note=Localizes to the cortical endoplasmic reticulum at the endoplasmic reticulum-plasma membrane contact sites. {ECO:0000269|PubMed:26206935}.
DR  UNIPROT: Q9BZF1;
DR  UNIPROT: A8K1T2;
DR  UNIPROT: E9PE66;
DR  UNIPROT: E9PE68;
DR  UNIPROT: Q52LQ3;
DR  UNIPROT: Q68D75;
DR  UNIPROT: Q8WXP8;
DR  UNIPROT: Q9P277;
DR  PDB: 1V88;
DR  PDB: 5U77;
DR  PDB: 5U78;
DR  Pfam: PF01237;
DR  Pfam: PF00169;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DR  OMIM: 606736;
DR  DisGeNET: 114882;
DE  Function: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206935). Binds oxysterol, 25- hydroxycholesterol and cholesterol (PubMed:17428193, PubMed:17991739, PubMed:21698267). {ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:17991739, ECO:0000269|PubMed:21698267, ECO:0000269|PubMed:26206935}.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q12800; IntAct: EBI-2684046; Score: 0.00
DE  Interaction: A0A2U2H272; IntAct: EBI-2846189; Score: 0.00
DE  Interaction: Q7ARD3; IntAct: EBI-2862180; Score: 0.00
DE  Interaction: Q13501; IntAct: EBI-3197899; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: O36551; IntAct: EBI-14062552; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q8IZF4; IntAct: EBI-21536448; Score: 0.35
DE  Interaction: P16070; IntAct: EBI-21554944; Score: 0.35
DE  Interaction: P47900; IntAct: EBI-21566266; Score: 0.35
DE  Interaction: Q8WWF5; IntAct: EBI-21589535; Score: 0.35
DE  Interaction: Q96FT7; IntAct: EBI-21589962; Score: 0.35
DE  Interaction: P43115; IntAct: EBI-21607127; Score: 0.35
DE  Interaction: P34741; IntAct: EBI-21628438; Score: 0.35
DE  Interaction: Q92838; IntAct: EBI-21651770; Score: 0.35
DE  Interaction: Q86W33; IntAct: EBI-21657892; Score: 0.35
DE  Interaction: Q9H1C3; IntAct: EBI-21662351; Score: 0.35
DE  Interaction: Q9UBU6; IntAct: EBI-21677026; Score: 0.35
DE  Interaction: P32249; IntAct: EBI-21703149; Score: 0.35
DE  Interaction: Q8TCT7; IntAct: EBI-21710636; Score: 0.35
DE  Interaction: P43119; IntAct: EBI-21748886; Score: 0.35
DE  Interaction: Q9GZQ4; IntAct: EBI-21806349; Score: 0.35
DE  Interaction: Q9H0X9; IntAct: EBI-16165776; Score: 0.40
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16795318; Score: 0.27
DE  Interaction: Q16778; IntAct: EBI-20899844; Score: 0.40
DE  Interaction: O14776; IntAct: EBI-20932072; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: O15524; IntAct: EBI-25373793; Score: 0.35
DE  Interaction: Q8N5H7; IntAct: EBI-25374973; Score: 0.35
DE  Interaction: O15530; IntAct: EBI-25375702; Score: 0.53
DE  Interaction: Q92934; IntAct: EBI-25378368; Score: 0.35
DE  Interaction: P05771; IntAct: EBI-25379671; Score: 0.35
DE  Interaction: Q96R06; IntAct: EBI-25466806; Score: 0.60
DE  Interaction: Q9UKV5; IntAct: EBI-25770556; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: P19784; IntAct: EBI-28934542; Score: 0.35
DE  Interaction: P43405; IntAct: EBI-28935283; Score: 0.35
DE  Interaction: Q15746; IntAct: EBI-28941345; Score: 0.35
DE  Interaction: Q8NCB2; IntAct: EBI-28943408; Score: 0.35
DE  Interaction: Q9Y2K2; IntAct: EBI-28947183; Score: 0.35
DE  Interaction: P08922; IntAct: EBI-32719572; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: Q16832; IntAct: EBI-32720227; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
GO  GO:0032541;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0015485;
GO  GO:0070273;
GO  GO:0001786;
GO  GO:0140343;
GO  GO:0005548;
GO  GO:0032934;
GO  GO:0015248;
GO  GO:0032148;
GO  GO:0045444;
GO  GO:0030336;
GO  GO:0010891;
GO  GO:0036150;
GO  GO:0015914;
GO  GO:0046326;
GO  GO:0046628;
GO  GO:0051897;
GO  GO:0090204;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGGLADGEPDRTSLLGDSKDVLGPSTVVANSDESQLLTPGKMSQRQGKEAYPTPTKDLHQPSLSPASPHSQGFERGKED
SQ  ISQNKDESSLSMSKSKSESKLYNGSEKDSSTSSKLTKKESLKVQKKNYREEKKRATKELLSTITDPSVIVMADWLKIRGT
SQ  LKSWTKLWCVLKPGVLLIYKTQKNGQWVGTVLLNACEIIERPSKKDGFCFKLFHPLEQSIWAVKGPKGEAVGSITQPLPS
SQ  SYLIIRATSESDGRCWMDALELALKCSSLLKRTMIREGKEHDLSVSSDSTHVTFYGLLRANNLHSGDNFQLNDSEIERQH
SQ  FKDQDMYSDKSDKENDQEHDESDNEVMGKSEESDTDTSERQDDSYIEPEPVEPLKETTYTEQSHEELGEAGEASQTETVS
SQ  EENKSLIWTLLKQVRPGMDLSKVVLPTFILEPRSFLDKLSDYYYHADFLSEAALEENPYFRLKKVVKWYLSGFYKKPKGL
SQ  KKPYNPILGETFRCLWIHPRTNSKTFYIAEQVSHHPPISAFYVSNRKDGFCLSGSILAKSKFYGNSLSAILEGEARLTFL
SQ  NRGEDYVMTMPYAHCKGILYGTMTLELGGTVNITCQKTGYSAILEFKLKPFLGSSDCVNQISGKLKLGKEVLATLEGHWD
SQ  SEVFITDKKTDNSEVFWNPTPDIKQWRLIRHTVKFEEQGDFESEKLWQRVTRAINAKDQTEATQEKYVLEEAQRQAARDR
SQ  KTKNEEWSCKLFELDPLTGEWHYKFADTRPWDPLNDMIQFEKDGVIQTKVKHRTPMVSVPKMKHKPTRQQKKVAKGYSSP
SQ  EPDIQDSSGSEAQSVKPSTRRKKGIELGDIQSSIESIKQTQEEIKRNIMALRNHLVSSTPATDYFLQQKDYFIIFLLILL
SQ  QVIINFMFK
//
ID  B9EJ86;
PN  Oxysterol-binding protein-related protein 8;
GN  Osbpl8;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BZF1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9BZF1}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BZF1}. Note=The presence of the N-terminus extension contains an overall negative charge that may explain the weak localization to the cortical endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9BZF1}.
DR  UNIPROT: B9EJ86;
DR  UNIPROT: G3X9N6;
DR  UNIPROT: Q69ZJ4;
DR  Pfam: PF01237;
DR  Pfam: PF00169;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DE  Function: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner. Binds oxysterol, 25-hydroxycholesterol and cholesterol. {ECO:0000250|UniProtKB:Q9BZF1}.
DE  Reference Proteome: Yes;
GO  GO:0032541;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0015485;
GO  GO:0070273;
GO  GO:0001786;
GO  GO:0140343;
GO  GO:0032934;
GO  GO:0015248;
GO  GO:0032148;
GO  GO:0045444;
GO  GO:0030336;
GO  GO:0010891;
GO  GO:0015914;
GO  GO:0046326;
GO  GO:0046628;
GO  GO:0051897;
GO  GO:0090204;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEAALADGEPDRSSLLGDSKDVLGPSTVVANSDEPQHLTPGKMSQRQGRDANPTPTRDLPQPSLSPASLHSQGFERGKED
SQ  ISQNKDDSSLSMSKSKSESKLYNGSEKDSSTSSKLTKKESLKVQKKNYREEKKRATKELLSTITDPSVIVMADWLKIRGT
SQ  LKSWTKLWCVLKPGVLLIYKTQKNGQWVGTVLLNACEIIERPSKKDGFCFKLFHPLEQSIWAVKGPKGEAVGSITQPLPS
SQ  SYLIIRATSESDGRCWMDALELALKCSSLLKRTMVREGKEHDLSISSDSTHVTLYGLLRANNLHSGDNFQLNDSEIERQH
SQ  FKDQDLYSDKSDKENDPEHDESDNEVLGKSEESDTDTSERQDDSYIDPEPVEPLKETTYMEQSHEELGEAGEASQTETVS
SQ  EENKSLIWTLLKQVRPGMDLSRVVLPTFILEPRSFLDKLSDYYYHADFLSEAALEENPYFRLKKVVKWYLSGFYKKPKGL
SQ  KKPYNPILGETFRCLWIHPRTNSKTFYIAEQVSHHPPISAFYVSNRKDGFCLSGSILAKSKFYGNSLSAILEGEARLTFL
SQ  NRGEDYVMTMPYAHCKGILYGTMTLELGGTVNITCQKTGYSAILEFKLKPFLGSSDYVNQISGKLKLGKEVLATLEGHWD
SQ  SEVFINDKKTDNSEIFWNPTPDIKQWRLIRHTVKFEEQDDFESEKLWQRVTKAINAKDQTEATQEKYVLEEAQRQAARDR
SQ  KTKTQEWVCKLFELDPLTGEWHYKFSDTRPWDPLNDMIQFEKDGVIQTKVKHRTPMVSVPKMKHKPTRQQKKVVKGYSSP
SQ  EPDIQDSSGSEAQSVKPSTRRKKGIDLGDIQSSIESIKQTQEEIKRNIMALRNHLLSSTPATDYFLQQKDYFVIFLLILL
SQ  QVIINFIFK
//
ID  P22059;
PN  Oxysterol-binding protein 1;
GN  OSBP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:24209621, ECO:0000269|PubMed:29514919}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24209621}. Golgi apparatus membrane; Peripheral membrane protein {ECO:0000269|PubMed:24209621}. Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000269|PubMed:24209621}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:29514919}. Note=Predominantly cytosolic. {ECO:0000269|PubMed:24209621}.
DR  UNIPROT: P22059;
DR  UNIPROT: Q6P524;
DR  PDB: 2RR3;
DR  Pfam: PF01237;
DR  Pfam: PF00169;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DR  OMIM: 167040;
DR  DisGeNET: 5007;
DE  Function: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (PubMed:24209621). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25- hydroxycholesterol causes its disassembly (PubMed:15746430). Regulates cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749). {ECO:0000269|PubMed:15746430, ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:18450749, ECO:0000269|PubMed:24209621}.
DE  Reference Proteome: Yes;
DE  Interaction: P08047; IntAct: EBI-2681899; Score: 0.00
DE  Interaction: P68400; IntAct: EBI-5321687; Score: 0.44
DE  Interaction: O75344; IntAct: EBI-9364555; Score: 0.62
DE  Interaction: A0A0H3NDL6; IntAct: EBI-10690222; Score: 0.52
DE  Interaction: Q8ZNG2; IntAct: EBI-10710869; Score: 0.52
DE  Interaction: Q9P0L0; IntAct: EBI-11120309; Score: 0.74
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q86UE6; IntAct: EBI-21507777; Score: 0.35
DE  Interaction: Q6UX41; IntAct: EBI-21529766; Score: 0.35
DE  Interaction: Q7KYR7; IntAct: EBI-21541130; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-21550215; Score: 0.35
DE  Interaction: Q8WWF5; IntAct: EBI-21589535; Score: 0.35
DE  Interaction: Q9NRJ7; IntAct: EBI-21590428; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-21650356; Score: 0.35
DE  Interaction: Q9Y5G8; IntAct: EBI-21697051; Score: 0.35
DE  Interaction: P05120; IntAct: EBI-21713063; Score: 0.35
DE  Interaction: Q96FV0; IntAct: EBI-21840089; Score: 0.35
DE  Interaction: P61769; IntAct: EBI-20911136; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q92685; IntAct: EBI-25468424; Score: 0.51
DE  Interaction: Q8NHP6; IntAct: EBI-25617363; Score: 0.40
DE  Interaction: A0A0F6B423; IntAct: EBI-27033608; Score: 0.46
DE  Interaction: A0A0F6B1Q8; IntAct: EBI-27036840; Score: 0.46
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0097038;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005802;
GO  GO:0008142;
GO  GO:0070273;
GO  GO:0019904;
GO  GO:0032934;
GO  GO:0120015;
GO  GO:0015248;
GO  GO:0006699;
GO  GO:0035627;
GO  GO:0032367;
GO  GO:0015914;
GO  GO:0035774;
GO  GO:1904411;
GO  GO:0042531;
GO  GO:0006686;
GO  GO:0015918;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:24209621};
SQ  MAATELRGVVGPGPAAIAALGGGGAGPPVVGGGGGRGDAGPGSGAASGTVVAAAAGGPGPGAGGVAAAGPAPAPPTGGSG
SQ  GSGAGGSGSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQTYH
SQ  LKASSEVERQRWVTALELAKAKAVKMLAESDESGDEESVSQTDKTELQNTLRTLSSKVEDLSTCNDLIAKHGTALQRSLS
SQ  ELESLKLPAESNEKIKQVNERATLFRITSNAMINACRDFLMLAQTHSKKWQKSLQYERDQRIRLEETLEQLAKQHNHLER
SQ  AFRGATVLPANTPGNVGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLGHKRTGSNISGASSDISLDEQYKHQLEE
SQ  TKKEKRTRIPYKPNYSLNLWSIMKNCIGKELSKIPMPVNFNEPLSMLQRLTEDLEYHELLDRAAKCENSLEQLCYVAAFT
SQ  VSSYSTTVFRTSKPFNPLLGETFELDRLEENGYRSLCEQVSHHPPAAAHHAESKNGWTLRQEIKITSKFRGKYLSIMPLG
SQ  TIHCIFHATGHHYTWKKVTTTVHNIIVGKLWIDQSGEIDIVNHKTGDKCNLKFVPYSYFSRDVARKVTGEVTDPSGKVHF
SQ  ALLGTWDEKMECFKVQPVIGENGGDARQRGHEAEESRVMLWKRNPLPKNAENMYYFSELALTLNAWESGTAPTDSRLRPD
SQ  QRLMENGRWDEANAEKQRLEEKQRLSRKKREAEAMKATEDGTPYDPYKALWFERKKDPVTKELTHIYRGEYWECKEKQDW
SQ  SSCPDIF
//
ID  Q3B7Z2;
PN  Oxysterol-binding protein 1;
GN  Osbp;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P22059}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Note=Predominantly cytosolic. {ECO:0000250|UniProtKB:P22059}.
DR  UNIPROT: Q3B7Z2;
DR  UNIPROT: E9QPD4;
DR  UNIPROT: Q3V163;
DR  UNIPROT: Q52KH7;
DR  UNIPROT: Q570Y8;
DR  Pfam: PF01237;
DR  Pfam: PF00169;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DE  Function: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds cholesterol and a range of oxysterols including 25- hydroxycholesterol. Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly. Regulates cholesterol efflux by decreasing ABCA1 stability. {ECO:0000250|UniProtKB:P22059}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A0F6B423; IntAct: EBI-27035120; Score: 0.46
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0097038;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005802;
GO  GO:0070273;
GO  GO:0019904;
GO  GO:0032934;
GO  GO:0120015;
GO  GO:0015248;
GO  GO:0035627;
GO  GO:0032367;
GO  GO:0015914;
GO  GO:0035774;
GO  GO:1904411;
GO  GO:0042531;
GO  GO:0006686;
GO  GO:0015918;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P22059};
SQ  MAATELRGVVGPGPAAIAAPGGGGAGPPAVGGGGGRGDAGPGPGVAAATAATAGGPGPGAGGVAAGGPGSAPPAAGSGGS
SQ  GAGGSGSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQTYHLK
SQ  ASSEVERQRWVTALELAKAKAVKMLAESDDSGDEESVSQTDKTELQSTLRTLSSKVEDLSTCNDLIAKHGTALQRSLSEL
SQ  ESLKLPAESNEKIKQVNERATLFRITSNAMINACRDFLMLAQTHSKKWQKSLQYERDQRIRLEETLEQLAKQHNHLERAF
SQ  RGATVLPANPPGSAGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLGHKRTGSNISGASSDVSLDEQYKHQLEETK
SQ  KEKRTRIPYKPNYSLNLWSIMKNCIGKELSKIPMPVNFNEPLSMLQRLTEDLEYHELLDRAAKCENSLEQLCYVAAFTVS
SQ  SYSTTVFRTSKPFNPLLGETFELDRLEENGYRSICEQVSHHPPAAAHHAESKNGWTLRQEIKITSKFRGKYLSIMPLGTI
SQ  HCIFHSTGHHYTWKKVTTTVHNIIVGKLWIDQSGEIDIVNHKTGDKCNLKFVPYSYFSRDVARKVTGEVTDPSGKVHFAL
SQ  LGTWDEKMDCFKVQAASGENGGDARQRGHEAEDSRVMLWKRNPLPKNAENMYYFSELALTLNAWEGGTAPTDSRLRPDQR
SQ  LMENGRWDEANAEKQRLEEKQRLSRKKREAEAAKATEDGTPHDPYKALWFERKKDPVTRELTHIYSGEYWECKEKQDWGS
SQ  CPDIF
//
ID  P16258;
PN  Oxysterol-binding protein 1;
GN  OSBP;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P22059}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Note=Predominantly cytosolic. {ECO:0000250|UniProtKB:P22059}.
DR  UNIPROT: P16258;
DR  Pfam: PF01237;
DR  Pfam: PF00169;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DE  Function: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (By similarity). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:18165705). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (By similarity). Regulates cholesterol efflux by decreasing ABCA1 stability (By similarity). {ECO:0000250|UniProtKB:P22059, ECO:0000269|PubMed:18165705}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0048471;
GO  GO:0005802;
GO  GO:0015485;
GO  GO:0070273;
GO  GO:0120015;
GO  GO:0032367;
GO  GO:0015918;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P22059};
SQ  MAATELRGVVGPGPAAIAAPGGGGAGPPVVGGGGGGRGDAGPGSGAASGTVAAAAAGGQGPGAGGVAAAAGPAPTPPAGG
SQ  SGSSGTGGSGSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQT
SQ  YHLKASSEVERQRWVTALELAKAKAVKMLAESDESGDEESVSQTDKTELQNTLRTLSSKVEDLSTCNDLIAKHGTALQRS
SQ  LSELESLKLPAESNEKIKQVNERATLFRITSNAMINACRDFLVLAQTHSKKWQKSLQYERDQRIRLEETLEQLAKQHNHL
SQ  ERAFRGATVLPAHTSGSAGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLGHKRTGSNISGASSDISLDEQYKHQL
SQ  EETKKEKRTRIPYKPNYSLNLWSIMKNCIGKELSKIPMPVNFNEPLSMLQRLTEDLEYHELLDRAAKCENSLEQLCYVAA
SQ  FTVSSYSTTVFRTSKPFNPLLGETFELDRLEENGYRSLCEQVSHHPPAAAHHAESKNGWTLRQEIKITSKFRGKYLSIMP
SQ  LGTIHCIFHATGHHYTWKKVTTTVHNIIVGKLWIDQSGEIDIVNHKTGDKCNLKFVPYSYFSRDVARKVTGEVTDPSGKV
SQ  HFALLGTWDEKMDCFKVQPVSGENGGDARQRGHEAEESRVMLWKRNPLPKNAENMYYFSELALTLNAWEGGTAPTDSRLR
SQ  PDQRLMENGRWDEANAEKQRLEEKQRLSRKKREAEAMKATEDGTPYDPYKALWFERKKDPVTKELTHIYRGEYWECKEKQ
SQ  DWNSCPDIF
//
ID  P35845;
PN  Oxysterol-binding protein homolog 1;
GN  SWH1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Golgi apparatus membrane {ECO:0000269|PubMed:11408574}. Nucleus outer membrane {ECO:0000269|PubMed:11408574, ECO:0000269|PubMed:12727870, ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:25420878}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12727870}. Vacuole membrane {ECO:0000269|PubMed:11408574, ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:25420878}. Note=Soluble protein that accumulates on the surface of late Golgi membranes and at nucleus-vacuole (NV) junctions, interorganelle interfaces between the nuclear envelope and the vacuole membrane formed during piecemeal microautophagy of the nucleus (PMN). Targeted exclusively to NV junctions in stationary phase. {ECO:0000269|PubMed:11408574, ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:25420878}.
DR  UNIPROT: P35845;
DR  UNIPROT: D6VPN6;
DR  UNIPROT: P39555;
DR  UNIPROT: P80234;
DR  UNIPROT: Q86ZC4;
DR  UNIPROT: Q86ZS1;
DR  PDB: 5H28;
DR  PDB: 5H2C;
DR  Pfam: PF13637;
DR  Pfam: PF01237;
DR  Pfam: PF00169;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS01013;
DR  PROSITE: PS50003;
DE  Function: Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide- coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transfering it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis (PubMed:8017104, PubMed:11238399, PubMed:15173322). Involved in non-vesicular transport of ergosterol and PI(4)P at the NVJ. Binds sterol and PI4P in a mutually exclusive manner (PubMed:28319008). May be involved in formation of PMN vesicles by altering the membrane lipid composition (PubMed:15173322). {ECO:0000269|PubMed:11238399, ECO:0000269|PubMed:15173322, ECO:0000269|PubMed:28319008, ECO:0000269|PubMed:8017104}.
DE  Reference Proteome: Yes;
DE  Interaction: P80667; IntAct: EBI-600773; Score: 0.37
DE  Interaction: P40510; IntAct: EBI-784727; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-784727; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-784727; Score: 0.56
DE  Interaction: P12385; IntAct: EBI-784727; Score: 0.44
DE  Interaction: P10592; IntAct: EBI-784727; Score: 0.53
DE  Interaction: P26786; IntAct: EBI-784727; Score: 0.35
DE  Interaction: P05753; IntAct: EBI-784727; Score: 0.35
DE  Interaction: P23248; IntAct: EBI-784727; Score: 0.35
DE  Interaction: P41805; IntAct: EBI-784727; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-784727; Score: 0.35
DE  Interaction: P32317; IntAct: EBI-784727; Score: 0.35
DE  Interaction: P29056; IntAct: EBI-793115; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-794579; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-794579; Score: 0.53
DE  Interaction: P11484; IntAct: EBI-794579; Score: 0.53
DE  Interaction: P32324; IntAct: EBI-794579; Score: 0.35
DE  Interaction: P32794; IntAct: EBI-794579; Score: 0.35
DE  Interaction: P40075; IntAct: EBI-803541; Score: 0.55
DE  Interaction: P38881; IntAct: EBI-811418; Score: 0.35
DE  Interaction: P38829; IntAct: EBI-855610; Score: 0.00
DE  Interaction: P53919; IntAct: EBI-858505; Score: 0.00
DE  Interaction: P38249; IntAct: EBI-7208690; Score: 0.40
DE  Interaction: Q04636; IntAct: EBI-7445082; Score: 0.40
DE  Interaction: P12945; IntAct: EBI-7445120; Score: 0.40
DE  Interaction: Q12451; IntAct: EBI-7445135; Score: 0.44
DE  Interaction: P06103; IntAct: EBI-7445165; Score: 0.40
DE  Interaction: Q99176; IntAct: EBI-7762329; Score: 0.40
DE  Interaction: P35845; IntAct: EBI-8224563; Score: 0.62
DE  Interaction: P39968; IntAct: EBI-6325802; Score: 0.00
DE  Interaction: Q03860; IntAct: EBI-6342190; Score: 0.00
DE  Interaction: P43613; IntAct: EBI-3655372; Score: 0.35
DE  Interaction: P40564; IntAct: EBI-3657076; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3678244; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3703395; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3730378; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3747563; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-4383599; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-4385804; Score: 0.35
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0000138;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0071561;
GO  GO:0097038;
GO  GO:0005886;
GO  GO:0005774;
GO  GO:0008289;
GO  GO:0032934;
GO  GO:0120015;
GO  GO:0015248;
GO  GO:0006897;
GO  GO:0006887;
GO  GO:0030011;
GO  GO:0034727;
GO  GO:0015918;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEQPDLSSVAISKPLLKLKLLDALRQGSFPNLQDLLKKQFQPLDDPNVQQVLHLMLHYAVQVAPMAVIKEIVHHWVSTTN
SQ  TTFLNIHLDLNERDSNGNTPLHIAAYQSRGDIVAFLLDQPTINDCVLNNSHLQAIEMCKNLNIAQMMQVKRSTYVAETAQ
SQ  EFRTAFNNRDFGHLESILSSPRNAELLDINGMDPETGDTVLHEFVKKRDVIMCRWLLEHGADPFKRDRKGKLPIELVRKV
SQ  NENDTATNTKIAIDIELKKLLERATREQSVIDVTNNNLHEAPTYKGYLKKWTNFAQGYKLRWFILSSDGKLSYYIDQADT
SQ  KNACRGSLNMSSCSLHLDSSEKLKFEIIGGNNGVIRWHLKGNHPIETNRWVWAIQGAIRYAKDREILLHNGPYSPSLALS
SQ  HGLSSKVSNKENLHATSKRLTKSPHLSKSTLTQNDHDNDDDSTNNNNNKSNNDYDDNNNNNNNDDDDYDDDDESRPLIEP
SQ  LPLISSRSQSLSEITPGPHSRKSTVSSTRAADIPSDDEGYSEDDSDDDGNSSYTMENGGENDGDEDLNAIYGPYIQKLHM
SQ  LQRSISIELASLNELLQDKQQHDEYWNTVNTSIETVSEFFDKLNRLTSQREKRMIAQMTKQRDVNNVWIQSVKDLEMELV
SQ  DKDEKLVALDKERKNLKKMLQKKLNNQPQVETEANEESDDANSMIKGSQESTNTLEEIVKFIEATKESDEDSDADEFFDA
SQ  EEAASDKKANDSEDLTTNKETPANAKPQEEAPEDESLIVISSPQVEKKNQLLKEGSFVGYEDPVRTKLALDEDNRPKIGL
SQ  WSVLKSMVGQDLTKLTLPVSFNEPTSLLQRVSEDIEYSHILDQAATFEDSSLRMLYVAAFTASMYASTTNRVSKPFNPLL
SQ  GETFEYARTDGQYRFFTEQVSHHPPISATWTESPKWDFYGECNVDSSFNGRTFAVQHLGLWYITIRPDHNISVPEETYSW
SQ  KKPNNTVIGILMGKPQVDNSGDVKVTNHTTGDYCMLHYKAHGWTSAGAYEVRGEVFNKDDKKLWVLGGHWNDSIYGKKVT
SQ  ARGGELTLDRIKTANSATGGPKLDGSKFLIWKANERPSVPFNLTSFALTLNALPPHLIPYLAPTDSRLRPDQRAMENGEY
SQ  DKAAAEKHRVEVKQRAAKKEREQKGEEYRPKWFVQEEHPVTKSLYWKFNGEYWNKRKNHDFKDCADIF
//
ID  P20240;
PN  Otefin;
GN  Ote;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18410727, ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:27174470, ECO:0000269|PubMed:8999964, ECO:0000269|PubMed:9199347, ECO:0000269|PubMed:9632815}; Peripheral membrane protein {ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:8999964, ECO:0000269|PubMed:9199347}; Nucleoplasmic side {ECO:0000269|PubMed:2517292}. Nucleus, nucleoplasm {ECO:0000269|PubMed:8999964}. Cytoplasm {ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:9199347}. Chromosome {ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:2517292}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:2186029, ECO:0000269|PubMed:22751930}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:22751930}. Note=Component of the spindle envelope during early mitotic cycles (PubMed:2186029, PubMed:2517292). Following nuclear envelope breakdown, becomes dispersed in the cytoplasm and concentrated at the spindle poles (PubMed:22751930, PubMed:2517292). At anaphase (when the nuclear envelope begins to reassemble), locates to the chromosomes accumulating first in areas adjacent to centrosomes and at the peripheral sites of the chromosomes (PubMed:22751930, PubMed:2517292). At telophase, expressed as a continuous rim around the chromatin and increased expression in the midspindle area (PubMed:22751930). During cytokinesis, locates to the nuclear periphery with some remaining in the cytoplasm and at the mid-body (PubMed:22751930). At stage 4 of egg development, expression in the oocyte nuclear envelope is higher than in the nurse nuclear envelope (PubMed:9199347). Expression in oocyte cytoplasm increases after stages 6 to 7 of egg development (PubMed:9199347). {ECO:0000269|PubMed:2186029, ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:9199347}.
DR  UNIPROT: P20240;
DR  UNIPROT: Q9V8E5;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Inner nuclear membrane protein (PubMed:2186029, PubMed:9199347, PubMed:18410727, PubMed:22751930). Involved in the attachment of membrane vesicles to chromatin during nuclear assembly, and is probably required for centrosome maturation and cell cycle progression during mitosis (PubMed:9199347, PubMed:22751930). Essential for differentiation of certain tissues and the maintenance of progenitor cell populations (PubMed:18410727, PubMed:24700158, PubMed:23806619, PubMed:27174470). Required for the differentiation and maintenance of male and female germline stem cells (GSCs), as well as the maintenance of somatic cells in the GSC niche (PubMed:18410727, PubMed:23806619, PubMed:27174470). This role is likely to be independent of the BMP (Dpp) pathway that negatively regulates bam transcription during GSC differentiation (PubMed:18410727, PubMed:23806619). During development, plays essential and redundant functions with the other LEM domain proteins; bocks and MAN1 (PubMed:24700158). Also has a redundant but important role with bocks during larval development (PubMed:24700158). {ECO:0000269|PubMed:18410727, ECO:0000269|PubMed:2186029, ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:23806619, ECO:0000269|PubMed:24700158, ECO:0000269|PubMed:27174470, ECO:0000269|PubMed:9199347}.
DE  Reference Proteome: Yes;
DE  Interaction: P08928; IntAct: EBI-873490; Score: 0.50
DE  Interaction: Q94524; IntAct: EBI-221780; Score: 0.00
DE  Interaction: P23572; IntAct: EBI-871822; Score: 0.27
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: Q24568; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VHX7; IntAct: EBI-26718525; Score: 0.49
DE  Interaction: A2VEE1; IntAct: EBI-26718505; Score: 0.49
DE  Interaction: Q9I7U2; IntAct: EBI-26718495; Score: 0.49
DE  Interaction: Q8SXS4; IntAct: EBI-26718485; Score: 0.49
DE  Interaction: Q9VPB8; IntAct: EBI-26718475; Score: 0.49
DE  Interaction: Q9VV87; IntAct: EBI-26718465; Score: 0.49
DE  Interaction: Q9V3Q9; IntAct: EBI-26718455; Score: 0.49
DE  Interaction: Q4V4P2; IntAct: EBI-26718515; Score: 0.49
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0012505;
GO  GO:0005815;
GO  GO:0005641;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005654;
GO  GO:0000922;
GO  GO:0003714;
GO  GO:0008134;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0030718;
GO  GO:0060250;
GO  GO:0045892;
GO  GO:0031468;
GO  GO:0048477;
GO  GO:0030513;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MADVDDFDSLSNAELRAKMLAQGLPNIPVTDSSRKVLVKRLRASIGGQASPAASPKKTNRRETLAPAPGAPSAPAAASTP
SQ  VDKLDGNKVAPATKARRTITAAEAKEPVRRLPEEAIRRRPDEADRLRSEEPVAARKPTTAPAAQPVQTRRTSTSSGSERK
SQ  VVEPLRKPETIVEQPASSKRADREENYLKVNSLIVLESDEEEDEQLVQAADLVEQEHAARQKTTKLASSGTTTYEYKSKV
SQ  VEPPRRQVYEATAAPVLPPSVPSARAQTTSSTRSYDYASNPAPGRYSSFVRTAAQGYVTAEAPPVASYSSSYKRTYANEL
SQ  SDDTDSKEDQYESTFARNLARLRAERIGDRISPYSRRTLASGNAGSGSLGYEPRARRSLRPNDNSVSEAFNRWLNSLEQK
SQ  YHIKSKLFIVLLVLLLIGVYYIFY
//
ID  Q9NUU6;
PN  Inactive ubiquitin thioesterase OTULINL;
GN  OTULINL;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:31056421}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:31056421}; Peripheral membrane protein {ECO:0000269|PubMed:31056421}. Nucleus envelope {ECO:0000269|PubMed:31056421}.
DR  UNIPROT: Q9NUU6;
DR  UNIPROT: Q53H50;
DR  UNIPROT: Q9H037;
DR  PDB: 6DRM;
DR  Pfam: PF16218;
DR  DisGeNET: 54491;
DE  Function: Lacks deubiquitinase activity. {ECO:0000269|PubMed:31056421}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8N661; IntAct: EBI-24707345; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-23781782; Score: 0.56
DE  Interaction: Q8N5M9; IntAct: EBI-24740431; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-24742825; Score: 0.56
DE  Interaction: Q8IWU4; IntAct: EBI-24756288; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-25288281; Score: 0.56
DE  Interaction: Q8NBQ5; IntAct: EBI-24654642; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24792326; Score: 0.56
DE  Interaction: Q6ZVE7; IntAct: EBI-25274316; Score: 0.56
DE  Interaction: Q02223; IntAct: EBI-21757502; Score: 0.35
DE  Interaction: O14901; IntAct: EBI-25905530; Score: 0.56
DE  Interaction: O43464; IntAct: EBI-25920284; Score: 0.56
GO  GO:0005737;
GO  GO:0042406;
GO  GO:0005635;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:31056421};
SQ  MAATRSPTRARERERSGAPAAGSDQVHSWMLATSQALDTVWRMAKGFVMLAVSFLVAAICYFRRLHLYSGHKLKWWIGYL
SQ  QRKFKRNLSVEAEVDLLSYCAREWKGETPRNKLMRKAYEELFWRHHIKCVRQVRRDNYDALRSVLFQIFSQGISFPSWMK
SQ  EKDIVKLPEKLLFSQGCNWIQQYSFGPEKYTGSNVFGKLRKYVELLKTQWTEFNGIRDYHKRGSMCNTLFSDAILEYKLY
SQ  EALKFIMLYQVTEVYEQMKTKKVIPSLFRLLFSRETSSDPLSFMMNHLNSVGDTCGLEQIDMFILGYSLEVKIKVFRLFK
SQ  FNSRDFEVCYPEEPLRDWPEISLLTENDRHYHIPVF
//
ID  Q3TVP5;
PN  Inactive ubiquitin thioesterase OTULINL;
GN  Otulinl;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9NUU6}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NUU6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NUU6}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NUU6}.
DR  UNIPROT: Q3TVP5;
DR  UNIPROT: Q3U8Q4;
DR  UNIPROT: Q80WP7;
DR  Pfam: PF16218;
DE  Function: Lacks deubiquitinase activity. {ECO:0000250|UniProtKB:Q9NUU6}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0042406;
GO  GO:0005635;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9NUU6};
SQ  MEAPRSAPRERERARTTSGSDQVHSWILVTSQVLSAAWRIARAFVMTTLSPLSATFSYFRSLYLYLGHQLKWWIGYLQRK
SQ  FKRNLSVEAEVDLLSYCAREWKGEAPRARLMRKAYEELFWRHHIKCVRAVKRDNYDALRSVLFQIFSQGLSFPSWMKEKD
SQ  IVKLPEKLLFSQGCNWIQQYSFGPEKYTGSNVFGKLRKCVELLKLQWTEFSGMRDHHKRGSMCNSLFSDAILECKLYEAL
SQ  KFLMLYQVTEAYEQMKTNKVIPSLFRLLFSRESSPDPLSFMMNHLNSIGDTCGLDQIDMFILGYSLQVKIKVFRLFKFNS
SQ  RDFAVCYPEEPLREWPEISLLTENGHHYHIPVF
//
ID  Q3B7D8;
PN  Inactive ubiquitin thioesterase OTULINL;
GN  Otulinl;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9NUU6}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NUU6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NUU6}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NUU6}.
DR  UNIPROT: Q3B7D8;
DR  Pfam: PF16218;
DE  Function: Lacks deubiquitinase activity. {ECO:0000250|UniProtKB:Q9NUU6}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0042406;
GO  GO:0005635;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9NUU6};
SQ  MKATRSAPRERERSRTTSGSDQVHSWILVPSQVLHAVWRIARASVMTALSLLSATLSYFRSLYLYLGHQLKWWIGYLQRK
SQ  FKRNLSVEAEVDLLSYCAREWKGETPRARLMRKAYEELFWRYHVKCVRPVKRDNYDALRSVLFQIFSQGLSFPSWMKEKD
SQ  IVKLPEKLLFSQGCNWIQQYSFGPEKYTGSNVFGKLRKCVELLKLQWTEFSGMRDYHKRGSMCNSLFSDAILECKLYEAL
SQ  KFLMLYQVTEVYEQMKTNKIVPSLFRLLFSRESSPDPLSFMMNHLNSIGDTCGLDQIDMFILGYSLQVKIKVFRLFKFNS
SQ  RDFAVYYPEEPLREWPEISLLTENDHQYHIPVF
//
ID  Q96HA1;
PN  Nuclear envelope pore membrane protein POM 121;
GN  POM121;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17900573}. Nucleus membrane {ECO:0000269|PubMed:17900573}; Single-pass membrane protein {ECO:0000269|PubMed:17900573}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase. {ECO:0000250}.
DR  UNIPROT: Q96HA1;
DR  UNIPROT: A6NFS9;
DR  UNIPROT: A8CDT4;
DR  UNIPROT: A8K933;
DR  UNIPROT: A8MXF9;
DR  UNIPROT: O75115;
DR  UNIPROT: Q96DI0;
DR  UNIPROT: Q9H9X1;
DR  UNIPROT: Q9Y2N3;
DR  UNIPROT: Q9Y4S7;
DR  PDB: 5T6W;
DR  OMIM: 615753;
DR  DisGeNET: 9883;
DE  Function: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269|PubMed:17900573}.
DE  Reference Proteome: Yes;
DE  Interaction: A1KXE4; IntAct: EBI-24715141; Score: 0.56
DE  Interaction: O60711; IntAct: EBI-24358856; Score: 0.56
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-11889618; Score: 0.37
DE  Interaction: Q14974; IntAct: EBI-30827588; Score: 0.44
DE  Interaction: Q7Z3B4; IntAct: EBI-11889100; Score: 0.37
DE  Interaction: Q8WYP5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: Q9Y5P4; IntAct: EBI-752566; Score: 0.37
DE  Interaction: O95994; IntAct: EBI-752794; Score: 0.67
DE  Interaction: Q15654; IntAct: EBI-24332278; Score: 0.56
DE  Interaction: P46976; IntAct: EBI-754300; Score: 0.37
DE  Interaction: P36406; IntAct: EBI-24306440; Score: 0.56
DE  Interaction: Q53EZ4; IntAct: EBI-756040; Score: 0.37
DE  Interaction: P63010; IntAct: EBI-24498237; Score: 0.56
DE  Interaction: P14136; IntAct: EBI-757885; Score: 0.37
DE  Interaction: Q8IYF3; IntAct: EBI-758542; Score: 0.67
DE  Interaction: P25963; IntAct: EBI-24355218; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-25252899; Score: 0.56
DE  Interaction: Q93062; IntAct: EBI-759391; Score: 0.67
DE  Interaction: P54253; IntAct: EBI-25981994; Score: 0.56
DE  Interaction: P69961; IntAct: EBI-2861010; Score: 0.00
DE  Interaction: Q8D014; IntAct: EBI-2861003; Score: 0.00
DE  Interaction: Q92731; IntAct: EBI-2880211; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-3437412; Score: 0.00
DE  Interaction: P51116; IntAct: EBI-8637014; Score: 0.67
DE  Interaction: Q05322; IntAct: EBI-6159823; Score: 0.35
DE  Interaction: Q9NSC5; IntAct: EBI-10287122; Score: 0.56
DE  Interaction: Q6ZW49; IntAct: EBI-10287154; Score: 0.56
DE  Interaction: Q8TAP6; IntAct: EBI-10287176; Score: 0.56
DE  Interaction: P42262; IntAct: EBI-11041024; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: Q8CI51; IntAct: EBI-11124806; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-11519933; Score: 0.37
DE  Interaction: Q2PJP0; IntAct: EBI-11520513; Score: 0.37
DE  Interaction: P03508; IntAct: EBI-11520975; Score: 0.37
DE  Interaction: Q20MH4; IntAct: EBI-11521180; Score: 0.37
DE  Interaction: Q0A2H1; IntAct: EBI-11521369; Score: 0.37
DE  Interaction: Q2PJP1; IntAct: EBI-11521569; Score: 0.37
DE  Interaction: Q6DP94; IntAct: EBI-11521763; Score: 0.37
DE  Interaction: Q9Y5V3; IntAct: EBI-24285600; Score: 0.56
DE  Interaction: P14373; IntAct: EBI-24287635; Score: 0.56
DE  Interaction: Q9UHD9; IntAct: EBI-24294799; Score: 0.56
DE  Interaction: Q96R06; IntAct: EBI-24364662; Score: 0.56
DE  Interaction: Q9UBB9; IntAct: EBI-24486689; Score: 0.56
DE  Interaction: Q8N9W6; IntAct: EBI-24500998; Score: 0.56
DE  Interaction: Q9H0C1; IntAct: EBI-24506831; Score: 0.56
DE  Interaction: Q9Y2V7; IntAct: EBI-24507828; Score: 0.56
DE  Interaction: P40199; IntAct: EBI-24532782; Score: 0.56
DE  Interaction: P40763; IntAct: EBI-24614960; Score: 0.56
DE  Interaction: Q5VZ52; IntAct: EBI-24772111; Score: 0.56
DE  Interaction: P0CI25; IntAct: EBI-24374702; Score: 0.56
DE  Interaction: Q13114; IntAct: EBI-24413959; Score: 0.56
DE  Interaction: Q7L8S5; IntAct: EBI-24426023; Score: 0.56
DE  Interaction: O60684; IntAct: EBI-24426816; Score: 0.56
DE  Interaction: Q2TAC2; IntAct: EBI-24449313; Score: 0.56
DE  Interaction: Q10567; IntAct: EBI-24463567; Score: 0.56
DE  Interaction: Q12933; IntAct: EBI-24474317; Score: 0.56
DE  Interaction: P0C870; IntAct: EBI-24592839; Score: 0.56
DE  Interaction: Q9Y4F3; IntAct: EBI-11926683; Score: 0.00
DE  Interaction: Q504Q3; IntAct: EBI-11926674; Score: 0.00
DE  Interaction: Q2M3V2; IntAct: EBI-11926665; Score: 0.00
DE  Interaction: P42694; IntAct: EBI-11926656; Score: 0.00
DE  Interaction: D0UZL9; IntAct: EBI-14061866; Score: 0.40
DE  Interaction: A4D1S0; IntAct: EBI-21511461; Score: 0.35
DE  Interaction: P20036; IntAct: EBI-21511890; Score: 0.35
DE  Interaction: Q9UGM1; IntAct: EBI-21517134; Score: 0.35
DE  Interaction: O15482; IntAct: EBI-21523851; Score: 0.35
DE  Interaction: P55345; IntAct: EBI-21544312; Score: 0.35
DE  Interaction: Q96JJ6; IntAct: EBI-21570881; Score: 0.35
DE  Interaction: Q504Y0; IntAct: EBI-21572157; Score: 0.35
DE  Interaction: P36941; IntAct: EBI-21581171; Score: 0.35
DE  Interaction: O43291; IntAct: EBI-21587968; Score: 0.35
DE  Interaction: Q8WWF5; IntAct: EBI-21589535; Score: 0.35
DE  Interaction: Q9NRJ7; IntAct: EBI-21590428; Score: 0.35
DE  Interaction: O14595; IntAct: EBI-21619731; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-21650356; Score: 0.35
DE  Interaction: Q8IV45; IntAct: EBI-21699883; Score: 0.35
DE  Interaction: Q6UXL0; IntAct: EBI-21748090; Score: 0.35
DE  Interaction: Q96G97; IntAct: EBI-21755399; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-21866171; Score: 0.35
DE  Interaction: Q9UI95; IntAct: EBI-20219138; Score: 0.35
DE  Interaction: Q13627; IntAct: EBI-26367331; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: P46934; IntAct: EBI-30833846; Score: 0.44
DE  Interaction: Q93009; IntAct: EBI-30844051; Score: 0.44
DE  Interaction: P46937; IntAct: EBI-30848026; Score: 0.44
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSPAAAAAGAGERRRPIASVRDGRGRGCGGPARAVLLGLSLVGLLLYLVPAAAALAWLTVGATAAWWGLSREPRGSRPLS
SQ  SFVRKARHRRPLSSFVRKARHRRTLFASPLAKSTANGNLLEPRTLLEGPDPAELLLMGSYLGKPGPPQPAAAPEGQDLRD
SQ  RPGRRPPARPAPRSPPPRSPPPRSPPPSPPTHRAHHVYPSLPTPLLRPSRRPSPRDCGTLPNRFVITPRRRYPIHQAQYS
SQ  CLGVLPTVCWNGYHKKAVLSPRNSRMVCSPVTVRIAPPDRRFSRSAIPEQIISSTLSSPSSNAPDPCAKETVLSALKEKE
SQ  KKRTVEEEDQIFLDGQENKRRRHDSSGSGHSAFEPLVANGVPASFVPKPGSLKRGLNSQSSDDHLNKRSRSSSMSSLTGA
SQ  YASGIPSSSRNAITSSYSSTRGISQLWKRNGPSSSPFSSPASSRSQTPERPAKKIREEELCHHSSSSTPLAADRESQGEK
SQ  AADTTPRKKQNSNSQSTPGSSGQRKRKVQLLPSRRGEQLTLPPPPQLGYSITAEDLDLEKKASLQWFNQALEDKSDAASN
SQ  SVTETPPITQPSFTFTLPAAAPASPPTSLLAPSTNPLLESLKKMQTPPSLPPCPESAGAATTEALSPPKTPSLLPPLGLS
SQ  QSGPPGLLPSPSFDSKPPTTLLGLIPAPSMVPATDTKAPPTLQAETATKPQATSAPSPAPKQSFLFGTQNTSPSSPAAPA
SQ  ASSAPPMFKPIFTAPPKSEKEGPTPPGPSVTATAPSSSSLPTTTSTTAPTFQPVFSSMGPPASVPLPAPFFKQTTTPATA
SQ  PTTTAPLFTGLASATSAVAPITSASPSTDSASKPAFGFGINSVSSSSVSTTTSTATAASQPFLFGAPQASAASFTPAMGS
SQ  IFQFGKPPALPTTTTVTTFSQSLHTAVPTATSSSAADFSGFGSTLATSAPATSSQPTLTFSNTSTPTFNIPFGSSAKSPL
SQ  PSYPGANPQPAFGAAEGQPPGAAKPALAPSFGSSFTFGNSAAPAAAPTPAPPSMIKVVPAYVPTPIHPIFGGATHSAFGL
SQ  KATASAFGAPASSQPAFGGSTAVFFGAATSSGFGATTQTASSGSSSSVFGSTTPSPFTFGGSAAPAGSGSFGINVATPGS
SQ  STTTGAFSFGAGQSGSTATSTPFAGGLGQNALGTTGQSTPFAFNVSSTTESKPVFGGTATPTFGLNTPAPGVGTSGSSLS
SQ  FGASSAPAQGFVGVAPFGSAALSFSIGAGSKTPGARQRLQARRQHTRKK
//
ID  A6NF01;
PN  Putative nuclear envelope pore membrane protein POM 121B;
GN  POM121B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: A6NF01;
DE  Function: Putative component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q14974; IntAct: EBI-30827108; Score: 0.44
DE  Interaction: P46934; IntAct: EBI-30831794; Score: 0.44
DE  Interaction: Q93009; IntAct: EBI-30840675; Score: 0.44
DE  Interaction: P46937; IntAct: EBI-30845750; Score: 0.44
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRRVRTSELWKRNGPSSSPFSSPASSRSQTPERPAKKIREEEMCHHSSSSTPLAADKESQGEKAADTTPRKKQNSNSQS
SQ  TPGSSGQRKRKVQLLPSRRGEQLTLPPPPQLGYSITAEDLDLEKKASLQWFNQALEDKSDAASNSVTETPPITQPSFTFT
SQ  LPAAAPASPPTSLLAPSTNPLLESLKKMQTPPSLPPCPESAGAATTEALSPPKTPNLLPPLGLSQSGPPGLLPSPSFDSN
SQ  PPTTLLGLIPAPSMVPATDTKAPPTLQAETTTKPQATSAPSPAPKQSFLFGTQNTSPSSPAAPAASSASPMFKPIFTAPP
SQ  KSEKEGPTPPGPSVSATAPSSSSLPTTTSTTAPTFQPVFSSMGPPASVPLPAPFFKQTTTPATAPTTTAPLFTGLASATS
SQ  AVAPITSASPSTDSASKPAFGFGINSVSSSSVSTTTSTATAASQPFLFGAPQASAASFTPAMGSIFQFGKPPALPTTTTV
SQ  TTFSQSLPTAVPTATSSSAADFSGFGSTLATSAPATSSQPTLTFSNTSTPTFNIPFGSSAKSPLPSYPGANPQPAFGAAE
SQ  GQPPGAAKPALTPSFGSSFTFGNSAAPAAAPTPAPPSMIKIVPAHVPTPIQPTFGGATHSAFGLKATASAFGAPASSQPA
SQ  FGGSTAVFSFGAATSSGFGATTQTASSGSSSSVFGSTTPSPFTFGGSAAPAGSGSFGINVATPGSSATTGAFSFGAGQSG
SQ  STATSTPFAGGLGQNALGTTGQSTPFAFNVGSTTESKPVFGGTATPTFGLNTPAPGVGTSGSSLSFGASSAPAQGFVGVA
SQ  PFGSAAPSFSIGAGSKTLGARQRLQARRQHTRKK
//
ID  A8CG34;
PN  Nuclear envelope pore membrane protein POM 121C;
GN  POM121C;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17900573}. Nucleus membrane {ECO:0000269|PubMed:17900573}; Single-pass membrane protein {ECO:0000269|PubMed:17900573}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase. {ECO:0000250}.
DR  UNIPROT: A8CG34;
DR  UNIPROT: A0A075B7F8;
DR  UNIPROT: A0A087WY75;
DR  UNIPROT: O75115;
DR  UNIPROT: Q9Y2N3;
DR  UNIPROT: Q9Y4S7;
DR  OMIM: 615754;
DE  Function: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269|PubMed:17900573}.
DE  Reference Proteome: Yes;
DE  Interaction: Q92731; IntAct: EBI-2880211; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-3437854; Score: 0.00
DE  Interaction: P42229; IntAct: EBI-3943935; Score: 0.37
DE  Interaction: Q05322; IntAct: EBI-6159823; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-11109663; Score: 0.55
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.59
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q9NRA8; IntAct: EBI-11898977; Score: 0.00
DE  Interaction: Q504Q3; IntAct: EBI-11898968; Score: 0.00
DE  Interaction: Q2M3V2; IntAct: EBI-11898959; Score: 0.00
DE  Interaction: P42694; IntAct: EBI-11898950; Score: 0.00
DE  Interaction: Q9Y2I1; IntAct: EBI-11940179; Score: 0.00
DE  Interaction: Q9Y4F3; IntAct: EBI-11941734; Score: 0.00
DE  Interaction: Q504Y0; IntAct: EBI-21572157; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P20309; IntAct: EBI-20809896; Score: 0.37
DE  Interaction: Q9Y463; IntAct: EBI-28947247; Score: 0.35
DE  Interaction: P46934; IntAct: EBI-30831805; Score: 0.44
DE  Interaction: Q93009; IntAct: EBI-30840708; Score: 0.44
DE  Interaction: P46937; IntAct: EBI-30845790; Score: 0.44
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSPAAAAAGAGERRRPIASVRDGRGRGCGGPAGAALLGLSLVGLLLYLVPAAAALAWLAVGTTAAWWGLSREPRGSRPLS
SQ  SFVQKARHRRTLFASPPAKSTANGNLLEPRTLLEGPDPAELLLMGSYLGKPGPPQPAPAPEGQDLRNRPGRRPPARPAPR
SQ  STPPSQPTHRVHHFYPSLPTPLLRPSGRPSPRDRGTLPDRFVITPRRRYPIHQTQYSCPGVLPTVCWNGYHKKAVLSPRN
SQ  SRMVCSPVTVRIAPPDRRFSRSAIPEQIISSTLSSPSSNAPDPCAKETVLSALKEKKKKRTVEEEDQIFLDGQENKRRRH
SQ  DSSGSGHSAFEPLVASGVPASFVPKPGSLKRGLNSQSSDDHLNKRSRSSSMSSLTGAYTSGIPSSSRNAITSSYSSTRGI
SQ  SQLWKRNGPSSSPFSSPASSRSQTPERPAKKIREEELCHHSSSSTPLAADKESQGEKAADTTPRKKQNSNSQSTPGSSGQ
SQ  RKRKVQLLPSRRGEQLTLPPPPQLGYSITAEDLDLEKKASLQWFNQALEDKSDAASNSVTETPPTTQPSFTFTLPAAATA
SQ  SPPTSLLAPSTNPLLESLKKMQTPPSLPPCPESAGAATTEALSPPKTPSLLPPLGLSQSGPPGLLPSPSFDSKPPTTLLG
SQ  LIPAPSMVPATDTKAPPTLQAETATKPQATSAPSPAPKQSFLFGTQNTSPSSPAAPAASSASPMFKPIFTAPPKSEKEGL
SQ  TPPGPSVSATAPSSSSLPTTTSTTAPTFQPVFSSMGPPASVPLPAPFFKQTTTPATAPTTTAPLFTGLASATSAVAPITS
SQ  ASPSTDSASKPAFGFGINSVSSSSVSTTTSTATAASQPFLFGAPQASAASFTPAMGSIFQFGKPPALPTTTTVTTFSQSL
SQ  PTAVPTATSSSAADFSGFGSTLATSAPATSSQPTLTFSNTSTPTFNIPFGSSAKSPLPSYPGANPQPAFGAAEGQPPGAA
SQ  KPALTPSFGSSFTFGNSAAPAPATAPTPAPASTIKIVPAHVPTPIQPTFGGATHSAFGLKATASAFGAPASSQPAFGGST
SQ  AVFSFGAATSSGFGATTQTASSGSSSSVFGSTTPSPFTFGGSAAPAGSGSFGINVATPGSSATTGAFSFGAGQSGSTATS
SQ  TPFTGGLGQNALGTTGQSTPFAFNVGSTTESKPVFGGTATPTFGQNTPAPGVGTSGSSLSFGASSAPAQGFVGVGPFGSA
SQ  APSFSIGAGSKTPGARQRLQARRQHTRKK
//
ID  Q9SXA1;
PN  Phosphatidylinositol 4-kinase alpha 1;
GN  PI4KA1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000269|PubMed:12805633}; Peripheral membrane protein {ECO:0000269|PubMed:12805633}; Cytoplasmic side {ECO:0000269|PubMed:12805633}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12805633}.
DR  UNIPROT: Q9SXA1;
DR  UNIPROT: O81129;
DR  Pfam: PF00454;
DR  Pfam: PF00613;
DR  Pfam: PF19274;
DR  PROSITE: PS00915;
DR  PROSITE: PS50290;
DR  PROSITE: PS51545;
DE  Function: Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,- trisphosphate (Probable). Can bind to phosphatidylinositol 4- monophosphate (PI-4-P or PtdIns4P), phosphatidylinositol 4,5- bisphosphate (PI-4,5-P2 or PtdIns4,5P2), and phosphatidic acid (PtdOH), but not to 3-phosphoinositides (PubMed:9712908). May function upstream of the cold response phosphoinositide-dependent phospholipase C (PI- PLC) pathway (PubMed:22318862). {ECO:0000269|PubMed:22318862, ECO:0000269|PubMed:9712908, ECO:0000305|PubMed:9712908}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031234;
GO  GO:0016020;
GO  GO:0098857;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098797;
GO  GO:0009506;
GO  GO:0004430;
GO  GO:0051015;
GO  GO:0001727;
GO  GO:0070300;
GO  GO:0052742;
GO  GO:0005546;
GO  GO:0070273;
GO  GO:0046854;
GO  GO:0048015;
GO  GO:0009555;
GO  GO:0006468;
GO  GO:0048831;
GO  GO:0048364;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:12805633};
SQ  MEALTELCDIIAKNPKQFSEKLAWICGRCPQTEWLLAESPRVSRSHLNAVLAVARIISKNPESIDNRAKSVVNEFLSAIP
SQ  ASFRRSFWPHSFPSQLISSFYCDFLSYLSCAADLSPEFGTEVARFTGEVVIAAIAPSSGDSDGDPAISKAFLVALSQHFP
SQ  SILQSDGDKLITMLLDQFVLNRAPASPKEQRQQNSANSETDTSSSQGSPISTNRYPSGKTEMASPGDEVASHGSNLSSKS
SQ  SSSVVMNGGSIVWKSGVDQLSFGFSEGSGGANPVFRQQVASFEDESIESLEKQEIAFRLITHILDKVKIDSKLQDQVRFI
SQ  AKRQLQSMSAFLKSRKRDWNEQGQVLKTRVNAKLSVYQAAAKMKIKSLVSLETDGKTSKRLVLETLALLLDAADACLTSV
SQ  WRKMKACEELFDSLLSGIAKIAVARGGQPLRVLLIRLKPLVLAVCALPDQGAMLESIFKTSCVIIESAWAKDRAPVDNFI
SQ  MGLASSIRERNDYEEQVDREKQVPAVQLNVIRLLADLNVAVKKPEVADMILPLFIESLEEGDASTPSFLRLQLLDAVSRI
SQ  ATLGFDKSYRETVVLMTRSYLSKLSSVGSVESKTSAPEATTERVETLPAGFLTIASGLMDTKLRSDYRHRLLSLCSDVGL
SQ  AAESKSGGSGVDFLGPLLPAVAEICSDFDPTMDVEPSLLKLFRNLWFYIALFGLAPPIVKTPTPPLKSTSNSVNSVGSMS
SQ  ATALQAVGGPYMWDNQWALAVQRIAQGTPPLVVSSVKWLEDELELNALHNPGSRRGNGNEKVASTQRLALSTALGGRVDV
SQ  AAMNTISGVKATYLLAVAFLEIIRFISNGGILNGESSVSASRSAFSCVFEYLKTPNLTPAVSQCLTAIVHRAFETAVSWL
SQ  EDRISLTGKDARNRELTTYAHACFLIKSMSQRDEHVRDISVNLLTQLRDKFPQVLWHSSCLDSLLFSVHDNTPSTVVNDP
SQ  AWTAAVRSLYQKVVREWIIISLSYAPCTSQGLLQDKLCKANTWQRAQTTTDVVSLLSEIKIGTGKNELWSGIRTANIPAV
SQ  MAAAAAASGANLKVSEAFNLEVLGTGVVSATVKCNHAGEIAGMRRLYNSIGGFQSGSTPSGFGGGLQRLISGAFSQAPQP
SQ  EDDSFNEMLIARFVRLLQQFVNTAEKGGEVEKSQFRETCSQATALLLSNLGGESKTNVEGFSQLLRLLCWCPAYISTPDA
SQ  METGIFIWTWLVSAAPQLVSLVLAELVDAWIWTIDTKRGLFASDVRYSGPAAKLRPHLSPGEPEDPPESDPVDQIVAHRL
SQ  WLGFLIDRFEVVRHNSAEQLLLLGRMLQRSTDLEWCFTRHPAAAGTFFSLMLLGLKFCSCQTQGNMQKFRSGLQLLEDRI
SQ  YRTSLGWFAHQPEWYDVNIPNFCHSEALSVSVFVHFLSNELSESSQSDSKGKPRESGNLIDVTDQYHPVWGEMDNYTLGK
SQ  EKRKQLLLMLCQHEADRLDVWAQPISSKDSPYSRLKISSEKWTEYAKTAFSVDPRIALSVASRFPANASVKSEVTQLVQT
SQ  NIVDLRTIPEALPYFVTPKNVEENSVLLQQLPHWAACSITQALEFLTPAYKGHPRVMAYVLRVLESYPPERVTFFMPQLV
SQ  QSLRYDDGRLVEGYLLRATQRSDIFAHILIWHLQGEDVQETPKDGSIDKNAAFQEILPQVRQHIIDGFSPNALDMFTREF
SQ  DFFDKVTSISGVLFPLPKEERRAGIRRELEKIEMQGDDLYLPTAPNKLVRGIRVDSGIPLQSAAKVPIMITFNVIDRDGD
SQ  HSDVKPQACIFKVGDDCRQDVLALQVISLLRDIFQAAGLNLYLFPYGVLPTGAERGIIEVVPNTRSRSQMGETTDGGLYE
SQ  IFQQDYGPVGSTTFETARENFLISSAGYAVASLLLQPKDRHNGNLLFDDVGRLVHIDFGFILETSPGGNMRFESAHFKLS
SQ  HEMTQLLDPSGVMKSKTWHQFVSLCVKGYLAARRQMDGIISTVQMMLESGLPCFSRGDPIGNLRKRFHPEMSEREAAHFM
SQ  IHVCTDAYNKWTTAGYDLIQYLQQGIEK
//
ID  A4IFJ5;
PN  Lysophospholipase;
GN  PLA2G4A;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
DR  UNIPROT: A4IFJ5;
DR  UNIPROT: Q1XD55;
DR  Pfam: PF00168;
DR  Pfam: PF01735;
DR  PROSITE: PS50004;
DR  PROSITE: PS51210;
DE  Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium- independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity). {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005509;
GO  GO:0047498;
GO  GO:0005544;
GO  GO:0047499;
GO  GO:1902387;
GO  GO:0004622;
GO  GO:0008374;
GO  GO:0102545;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0004623;
GO  GO:0019369;
GO  GO:0006071;
GO  GO:0046475;
GO  GO:0019370;
GO  GO:0006640;
GO  GO:0036151;
GO  GO:0034638;
GO  GO:0034478;
GO  GO:0010572;
GO  GO:0001516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFIDPYQHIIVEHHYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISSTPDSRKRTRHFNNDINPVWNETFEFILD
SQ  PNQENILEITLMDANYVMDETLGTTTFPISSMKVGEKKQVPFIFNQVTEMILEMSLEVCSSPDLRFSMALCDQEKAFRQQ
SQ  RKENIKENMKKLLGPKNSEGLHSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYSH
SQ  PDFPEKGPEEINKELMKNVSHNPLLLLTPQKIKRYVESLWRKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVN
SQ  TGQCPLPLFTCLHVKPDVSELMFADWVEFSPFEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSIL
SQ  FNRVLGVSGSQSKGSTMEEELENITAKHIVSNDSSDSDDESQGPKGTEHEEAEREYQNDNQASWVQRMLMALVSDSALFN
SQ  TREGRAGKVHNFMLGLNLNTSYPMSPLRDFTMQESLDEDELDAAVADPDEFEQIYEPLDVKSKKIHVVDSGLTFNLPYPL
SQ  ILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHF
SQ  VLANINFRKYKAPGVPRETNEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKNAIVESIEYRR
SQ  QNPSRCSVSLSSVEARRFFNKEFLSKPTA
//
ID  O77793;
PN  Lysophospholipase;
GN  PLA2G4A;
OS  9796;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
DR  UNIPROT: O77793;
DR  Pfam: PF00168;
DR  Pfam: PF01735;
DR  PROSITE: PS50004;
DR  PROSITE: PS51210;
DE  Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium- independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity). {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000139;
GO  GO:0005635;
GO  GO:0005509;
GO  GO:0047498;
GO  GO:0005544;
GO  GO:1902387;
GO  GO:0004622;
GO  GO:0008374;
GO  GO:0102545;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0004623;
GO  GO:0019369;
GO  GO:0006071;
GO  GO:0019370;
GO  GO:0006640;
GO  GO:0034638;
GO  GO:0034478;
GO  GO:0001516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISSTPDSRKRTRHFNNNINPVWNETFEFILD
SQ  PNQENVLEITLMDANYVMDETLGTATFTLSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRQQ
SQ  RKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYLAGLSGSSWYMSTLYSH
SQ  PDFPEKGPEEINKELMKNVSYDPLLLLTPQKIKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVN
SQ  TAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSIL
SQ  FNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDESQEPKGTENEDAERDYQNDNQASWVHRMLMALVSDSALFN
SQ  TREGRAGKVHNFMLGLNLNTSYPLSPLRNFTTQESLDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPL
SQ  ILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHF
SQ  VLANINFRKYKAPGVPRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKNAMVESIEYRR
SQ  QNPSRCSVSLSNVEARRFFNKEFLNKPTA
//
ID  P47712;
PN  Lysophospholipase;
GN  PLA2G4A;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11375391}. Golgi apparatus membrane {ECO:0000269|PubMed:11375391}. Nucleus envelope. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000269|PubMed:11375391}.
DR  UNIPROT: P47712;
DR  UNIPROT: B1AKG4;
DR  UNIPROT: Q29R80;
DR  PDB: 1BCI;
DR  PDB: 1CJY;
DR  PDB: 1RLW;
DR  Pfam: PF00168;
DR  Pfam: PF01735;
DR  PROSITE: PS50004;
DR  PROSITE: PS51210;
DR  OMIM: 600522;
DR  OMIM: 618372;
DR  DisGeNET: 5321;
DE  Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (PubMed:7794891, PubMed:8619991, PubMed:8702602, PubMed:9425121, PubMed:10358058, PubMed:14709560, PubMed:16617059, PubMed:17472963, PubMed:27642067, PubMed:18451993). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:7794891, PubMed:8619991, PubMed:9425121, PubMed:10358058, PubMed:17472963, PubMed:18451993). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway (PubMed:18451993, PubMed:7794891, PubMed:9425121, PubMed:10358058, PubMed:17472963). In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids (PubMed:27642067). Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific (PubMed:7794891). Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides (PubMed:12672805). Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (PubMed:7794891). {ECO:0000250|UniProtKB:P47713, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:14709560, ECO:0000269|PubMed:16617059, ECO:0000269|PubMed:17472963, ECO:0000269|PubMed:18451993, ECO:0000269|PubMed:27642067, ECO:0000269|PubMed:7794891, ECO:0000269|PubMed:8619991, ECO:0000269|PubMed:8702602, ECO:0000269|PubMed:9425121}.
DE  Disease: Gastrointestinal ulceration, recurrent, with dysfunctional platelets (GURDP) [MIM:618372]: An autosomal recessive disorder characterized by recurrent gastrointestinal mucosal ulcers, gastrointestinal bleeding, chronic anemia, iron deficiency, and abdominal pain. Disease features also include platelet dysfunction, and globally decreased eicosanoid synthesis. {ECO:0000269|PubMed:18451993, ECO:0000269|PubMed:23268370, ECO:0000269|PubMed:25102815}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P78545; IntAct: EBI-1071980; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-3962281; Score: 0.35
DE  Interaction: P40763; IntAct: EBI-11322256; Score: 0.35
DE  Interaction: D6RFU6; IntAct: EBI-11044384; Score: 0.35
DE  Interaction: P60229; IntAct: EBI-11148789; Score: 0.35
DE  Interaction: H9XIJ5; IntAct: EBI-11514356; Score: 0.37
DE  Interaction: Q04206; IntAct: EBI-15690169; Score: 0.37
DE  Interaction: Q01518; IntAct: EBI-15690508; Score: 0.37
DE  Interaction: Q04323; IntAct: EBI-15690588; Score: 0.37
DE  Interaction: Q96GS4; IntAct: EBI-15690716; Score: 0.37
DE  Interaction: Q92499; IntAct: EBI-20913834; Score: 0.40
DE  Interaction: Q68FS2; IntAct: EBI-22259026; Score: 0.35
DE  Interaction: Q06884; IntAct: EBI-22259026; Score: 0.35
DE  Interaction: G3V9U7; IntAct: EBI-22259026; Score: 0.35
DE  Interaction: D3ZYG0; IntAct: EBI-22259026; Score: 0.35
DE  Interaction: P00176; IntAct: EBI-22259026; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0005743;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005509;
GO  GO:0047498;
GO  GO:0005544;
GO  GO:0047499;
GO  GO:1902387;
GO  GO:0004622;
GO  GO:0008374;
GO  GO:0102545;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0004623;
GO  GO:0019369;
GO  GO:0050482;
GO  GO:0071236;
GO  GO:0051649;
GO  GO:0006071;
GO  GO:0046475;
GO  GO:0006690;
GO  GO:0019370;
GO  GO:0006640;
GO  GO:0036151;
GO  GO:0034638;
GO  GO:0034478;
GO  GO:0006663;
GO  GO:0043032;
GO  GO:0010572;
GO  GO:0032308;
GO  GO:0002827;
GO  GO:0001516;
GO  GO:0042127;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILD
SQ  PNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEVPFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQ
SQ  RKEHIRESMKKLLGPKNSEGLHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
SQ  PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVN
SQ  TAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSIL
SQ  FNRVLGVSGSQSRGSTMEEELENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
SQ  TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPL
SQ  ILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHF
SQ  VLANINFRKYRAPGVPRETEEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
SQ  QNPSRCSVSLSNVEARRFFNKEFLSKPKA
//
ID  P47713;
PN  Lysophospholipase;
GN  Pla2g4a;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
DR  UNIPROT: P47713;
DR  Pfam: PF00168;
DR  Pfam: PF01735;
DR  PROSITE: PS50004;
DR  PROSITE: PS51210;
DE  Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (PubMed:1904318, PubMed:9403692, PubMed:9403693). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (PubMed:9403692, PubMed:9403693). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity). {ECO:0000250|UniProtKB:P47712, ECO:0000269|PubMed:1904318, ECO:0000269|PubMed:9403692, ECO:0000269|PubMed:9403693}.
DE  Reference Proteome: Yes;
DE  Interaction: P35438; IntAct: EBI-396959; Score: 0.46
DE  Interaction: P51807; IntAct: EBI-657945; Score: 0.37
DE  Interaction: O08709; IntAct: EBI-657956; Score: 0.37
DE  Interaction: P37040; IntAct: EBI-657998; Score: 0.37
DE  Interaction: P70670; IntAct: EBI-658008; Score: 0.37
DE  Interaction: Q91Y86; IntAct: EBI-658048; Score: 0.37
DE  Interaction: Q99K43; IntAct: EBI-658119; Score: 0.37
DE  Interaction: Q9D8F3; IntAct: EBI-658210; Score: 0.37
DE  Interaction: Q99P91; IntAct: EBI-658221; Score: 0.37
DE  Interaction: Q9EQS3; IntAct: EBI-658881; Score: 0.37
DE  Interaction: O89032; IntAct: EBI-658577; Score: 0.37
DE  Interaction: Q6P542; IntAct: EBI-6909752; Score: 0.35
DE  Interaction: A0A0F6B5H5; IntAct: EBI-27035347; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042588;
GO  GO:0005509;
GO  GO:0047498;
GO  GO:0005544;
GO  GO:0047499;
GO  GO:1902387;
GO  GO:0035035;
GO  GO:0004622;
GO  GO:0008374;
GO  GO:0102545;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0004623;
GO  GO:0019369;
GO  GO:0050482;
GO  GO:0071236;
GO  GO:0046697;
GO  GO:0051649;
GO  GO:0006071;
GO  GO:0046475;
GO  GO:0046456;
GO  GO:0019370;
GO  GO:0006640;
GO  GO:0001542;
GO  GO:0036151;
GO  GO:0034638;
GO  GO:0034478;
GO  GO:0006663;
GO  GO:0043065;
GO  GO:0008284;
GO  GO:0050729;
GO  GO:0043032;
GO  GO:0010572;
GO  GO:0031394;
GO  GO:0032308;
GO  GO:0002827;
GO  GO:0031340;
GO  GO:0001516;
GO  GO:0042127;
GO  GO:0051592;
GO  GO:0010033;
GO  GO:0043129;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILD
SQ  PNQENVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRQQ
SQ  RKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYSH
SQ  PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIQNRMSMTLSSLKEKVN
SQ  AARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSIL
SQ  FNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDEAQGPKGTENEEAEKEYQSDNQASWVHRMLMALVSDSALFN
SQ  TREGRAGKVHNFMLGLNLNTSYPLSPLRDFSSQDSFDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLI
SQ  LRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFV
SQ  LANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKDAIVESIEYRRQ
SQ  NPSRCSVSLSNVEARKFFNKEFLSKPTV
//
ID  Q5R8A5;
PN  Lysophospholipase;
GN  PLA2G4A;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
DR  UNIPROT: Q5R8A5;
DR  Pfam: PF00168;
DR  Pfam: PF01735;
DR  PROSITE: PS50004;
DR  PROSITE: PS51210;
DE  Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium- independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity). {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000139;
GO  GO:0005635;
GO  GO:0005509;
GO  GO:0047498;
GO  GO:0005544;
GO  GO:0047499;
GO  GO:1902387;
GO  GO:0004622;
GO  GO:0008374;
GO  GO:0102545;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0019369;
GO  GO:0006071;
GO  GO:0019370;
GO  GO:0006640;
GO  GO:0034638;
GO  GO:0034478;
GO  GO:0001516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFIDPYQHIIVEHQYSHKFTVVVLCATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILD
SQ  PNQENVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRQQ
SQ  RKEHIRESMKKLLGPKNSEGLHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
SQ  PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVN
SQ  TAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSIL
SQ  FNRVLGVSGSQSRGSTMEEELENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
SQ  TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPL
SQ  ILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHF
SQ  VLANINFRKYKAPGVPRETEEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
SQ  QNPSRCSVSLSNVEARRFFNKEFLSKPKA
//
ID  Q9TT38;
PN  Lysophospholipase;
GN  PLA2G4A;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
DR  UNIPROT: Q9TT38;
DR  Pfam: PF00168;
DR  Pfam: PF01735;
DR  PROSITE: PS50004;
DR  PROSITE: PS51210;
DE  Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium- independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity). {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000139;
GO  GO:0005635;
GO  GO:0005509;
GO  GO:0047498;
GO  GO:0005544;
GO  GO:0047499;
GO  GO:1902387;
GO  GO:0004622;
GO  GO:0008374;
GO  GO:0102545;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0019369;
GO  GO:0006071;
GO  GO:0019370;
GO  GO:0006640;
GO  GO:0034638;
GO  GO:0034478;
GO  GO:0001516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFIATTPDSRKRTRHFNNDINPVWNEAFEFILD
SQ  PNQGNVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSSPDLRFSMALCDQEKAFRQQ
SQ  RKENIKENMRKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYSH
SQ  PDFPEKGPQEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMHTTLSSLKEKVS
SQ  SAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSIL
SQ  FNRVLGVSGSHNKGSTMEEELENITAKHIVSNDSSDSDDESQEPKGTEGEDAEREYQNDHQASWVHRMLMALVSDSALFN
SQ  TREGRAGKVHNFMLGLNLNTSYPLSPLRDFTQESFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLI
SQ  LRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPIIIHFV
SQ  LANINFRKYKSPGVPRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKDAMVESIEYRRQ
SQ  NPSRCSVSLSNVEARRFFNKEFLSKPTA
//
ID  P50393;
PN  Lysophospholipase;
GN  Pla2g4a;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
DR  UNIPROT: P50393;
DR  Pfam: PF00168;
DR  Pfam: PF01735;
DR  PROSITE: PS50004;
DR  PROSITE: PS51210;
DE  Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium- independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity). {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042588;
GO  GO:0005509;
GO  GO:0047498;
GO  GO:0005544;
GO  GO:0047499;
GO  GO:1902387;
GO  GO:0035035;
GO  GO:0004622;
GO  GO:0008374;
GO  GO:0102545;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0004623;
GO  GO:0007568;
GO  GO:0019369;
GO  GO:0050482;
GO  GO:0071236;
GO  GO:0046697;
GO  GO:0051649;
GO  GO:0006071;
GO  GO:0046475;
GO  GO:0046456;
GO  GO:0019370;
GO  GO:0001554;
GO  GO:0006640;
GO  GO:0001542;
GO  GO:0036151;
GO  GO:0034638;
GO  GO:0034478;
GO  GO:0006663;
GO  GO:0043065;
GO  GO:0030501;
GO  GO:0008284;
GO  GO:0031622;
GO  GO:0050729;
GO  GO:0043032;
GO  GO:0010572;
GO  GO:0031394;
GO  GO:0032308;
GO  GO:0002827;
GO  GO:0031340;
GO  GO:0001516;
GO  GO:0042127;
GO  GO:0051592;
GO  GO:0051384;
GO  GO:0009408;
GO  GO:0009725;
GO  GO:0042542;
GO  GO:0032496;
GO  GO:0010226;
GO  GO:0051597;
GO  GO:0010033;
GO  GO:0010243;
GO  GO:0033280;
GO  GO:0043129;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILD
SQ  PNQENVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRRQ
SQ  RKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
SQ  PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIQNRMSTTLSSLKEKVS
SQ  AARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMTPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSIL
SQ  FNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDEAQGPKGTENEDAEREYQNDNQASWVHRMLMALVSDSALFN
SQ  TREGRAGKEHNFMLGLNLNTSYPLSPLRDFSPQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPL
SQ  ILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHF
SQ  VLANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKDAIVESIEYRR
SQ  QNPSRCSVSLSNVEARKFFNKEFLSKPTAESI
//
ID  Q64GA5;
PN  Cytosolic phospholipase A2 gamma;
GN  Pla2g4c;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:15950603}. Nucleus envelope {ECO:0000269|PubMed:15950603}. Cytoplasm, cell cortex {ECO:0000269|PubMed:15950603}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15950603}. Note=In germinal vesicle stage oocytes and early embryos, shows mainly uniform nuclear and cortical expression. During germinal vesicle breakdown, found in intensely stained foci which accumulate near the dissolving nuclear envelope. Also localizes to spindle poles at metaphase II. {ECO:0000269|PubMed:15950603}.
DR  UNIPROT: Q64GA5;
DR  UNIPROT: Q08EC7;
DR  UNIPROT: Q3UWS1;
DR  UNIPROT: Q7TN01;
DR  Pfam: PF01735;
DR  PROSITE: PS51210;
DE  Function: Calcium-independent phospholipase, lysophospholipase and O- acyltransferase involved in phospholipid remodeling. Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids with choline and ethanolamine head groups, producing lysophospholipids that are used in deacylation-reacylation cycles. Transfers the sn-1 fatty acyl from one lysophospholipid molecule to the sn-2 position of another lysophospholipid to form diacyl, alkylacyl and alkenylacyl glycerophospholipids. Cleaves ester bonds but not alkyl or alkenyl ether bonds at the sn-1 position of lysophospholipids. Catalyzes sn-2 fatty acyl transfer from phospholipids to the sn-2 position of 1-O-alkyl or 1-O-alkenyl lysophospholipids with lower efficiency. {ECO:0000250|UniProtKB:Q9UP65}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005811;
GO  GO:0031966;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005819;
GO  GO:0005509;
GO  GO:0047498;
GO  GO:0005544;
GO  GO:0047499;
GO  GO:0004622;
GO  GO:0008374;
GO  GO:0102545;
GO  GO:0004623;
GO  GO:0046475;
GO  GO:0140042;
GO  GO:0036151;
GO  GO:0036152;
GO  GO:0006663;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MELSSGVCPATRLQEAEKAAVHKRSPKVLEALRKLNIQADQAPVIAVLGSGGGLRAHIACLGVLSELKELGLLDAVTYLA
SQ  GVSGSTWALSSLYTKNGNMEGIEEELKHRYEKNEWDFHESLEKAIQASKRENYSLTDFWAYLIVSRQIRELQDSNLSSLK
SQ  KQVEEGVLPYPIFAAIDEDLLADWRERKTQNSWFEFTPHHAGYPALGAYVPITEFGSRFENGKLVKSEPERDLTFLRGLW
SQ  GSAFADIKEIKNYILNYFRNPFGKLKFIEGPVTYSEAPRMNVDAMLLDLVMAYFTDMNDPSIKDKLCALQQALGTETDEF
SQ  GIEMAEIIQNWNETSAEKKEQFLDHLLDRFKKTQEDTTTYSLMNWNTGLVWDRCVFVNETRKCVSKWQWGTVYNFLYKHG
SQ  KIADETMCSRELLHLVDAGFAINTPYPLVLPPVRETHLILSFDFSAGDPLETIRATADYCQRHEIPFPEVSEDQLKEWAK
SQ  APASCYVLRGETGPVVMHFTLFNKDNCGDDIETWRKKYGTVKLSDSYTPDLVRDLLRVSKENVKKNKINILSEMRKVAGN
SQ  PGNIPRVNKEACLGDRVKDPQGSQTVEFKKSHNISKD
//
ID  Q5E9B2;
PN  PCNA-associated factor;
GN  PCLAF;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q15004}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15004}. Note=Following DNA damage, localizes to DNA damage sites. Colocalizes with centrosomes in perinuclear region. {ECO:0000250|UniProtKB:Q15004}.
DR  UNIPROT: Q5E9B2;
DR  Pfam: PF15715;
DE  Function: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork- blocking lesions. Also acts as a regulator of centrosome number (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003682;
GO  GO:0060090;
GO  GO:0006974;
GO  GO:0007098;
GO  GO:0006260;
GO  GO:0051726;
GO  GO:0009411;
GO  GO:0019985;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRTKANSVPGSYRKVVASRAPRKVLGSSTSAANSTPLSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFSLSPKDSEKEN
SQ  RIPEEAGSSGLGKAKRKACPLPPDHTDDEKE
//
ID  Q15004;
PN  PCNA-associated factor;
GN  PCLAF;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:11313979, ECO:0000269|PubMed:16288740, ECO:0000269|PubMed:21673012, ECO:0000269|PubMed:23000965}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21673012}. Note=Following DNA damage, localizes to DNA damage sites (PubMed:21628590). Colocalizes with centrosomes in perinuclear region (PubMed:21673012).
DR  UNIPROT: Q15004;
DR  UNIPROT: A6NNU5;
DR  UNIPROT: A8K3Y3;
DR  UNIPROT: G9G694;
DR  UNIPROT: G9G696;
DR  PDB: 4D2G;
DR  PDB: 6EHT;
DR  PDB: 6GWS;
DR  PDB: 6IIW;
DR  Pfam: PF15715;
DR  OMIM: 610696;
DR  DisGeNET: 9768;
DE  Function: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork- blocking lesions. Also acts as a regulator of centrosome number. {ECO:0000269|PubMed:21673012, ECO:0000269|PubMed:23000965}.
DE  Reference Proteome: Yes;
DE  Interaction: P17918; IntAct: EBI-10999136; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-11109663; Score: 0.74
DE  Interaction: P54274; IntAct: EBI-24714227; Score: 0.56
DE  Interaction: Q8IYD8; IntAct: EBI-21821472; Score: 0.35
DE  Interaction: P38936; IntAct: EBI-21259335; Score: 0.35
GO  GO:0005813;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003682;
GO  GO:0060090;
GO  GO:0006974;
GO  GO:0007098;
GO  GO:0006260;
GO  GO:0051726;
GO  GO:0009411;
GO  GO:0019985;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRTKADSVPGTYRKVVAARAPRKVLGSSTSATNSTSVSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSEKEN
SQ  QIPEEAGSSGLGKAKRKACPLQPDHTNDEKE
//
ID  Q9CQX4;
PN  PCNA-associated factor;
GN  Pclaf;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q15004}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15004}. Note=Following DNA damage, localizes to DNA damage sites. Colocalizes with centrosomes in perinuclear region. {ECO:0000250|UniProtKB:Q15004}.
DR  UNIPROT: Q9CQX4;
DR  UNIPROT: Q4VAG2;
DR  UNIPROT: Q9CZ17;
DR  UNIPROT: Q9D0A5;
DR  Pfam: PF15715;
DE  Function: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork- blocking lesions. Also acts as a regulator of centrosome number (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
GO  GO:0005813;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003682;
GO  GO:0060090;
GO  GO:0006974;
GO  GO:0007098;
GO  GO:0006260;
GO  GO:0051726;
GO  GO:0009411;
GO  GO:0019985;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRTKANYVPGAYRKAVASQAPRKVLGSSTFVTNSSSSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKESKKENQ
SQ  APEEAGTSGLGKAKRKACPLQPDHRDDENE
//
ID  Q6RIA2;
PN  PCNA-associated factor;
GN  Pclaf;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q15004}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15004}. Note=Following DNA damage, localizes to DNA damage sites. Colocalizes with centrosomes in perinuclear region. {ECO:0000250|UniProtKB:Q15004}.
DR  UNIPROT: Q6RIA2;
DR  Pfam: PF15715;
DE  Function: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with PCNA is disrupted, facilitating the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, facilitating the bypass of replication-fork- blocking lesions. Also acts as a regulator of centrosome number (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003682;
GO  GO:0006974;
GO  GO:0007098;
GO  GO:0006260;
GO  GO:0051726;
GO  GO:0009411;
GO  GO:0019985;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRTKANYVPGAYRKVVASQAPRKVLGSSTFVTNSSGSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSKKENQ
SQ  IPEEAGSSGLGKAKRKACPLQPDHRDDENE
//
ID  Q5HZL4;
PN  PCNA-associated factor;
GN  pclaf;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q15004}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15004}. Note=Following DNA damage, localizes to DNA damage sites. Colocalizes with centrosomes in perinuclear region. {ECO:0000250|UniProtKB:Q15004}.
DR  UNIPROT: Q5HZL4;
DR  Pfam: PF15715;
DE  Function: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with pcna is disrupted, facilitating the interaction between monoubiquitinated pcna and the translesion DNA synthesis DNA polymerase eta (polh) at stalled replisomes, facilitating the bypass of replication-fork- blocking lesions. Also acts as a regulator of centrosome number (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003682;
GO  GO:0006974;
GO  GO:0007098;
GO  GO:0006260;
GO  GO:0051726;
GO  GO:0009411;
GO  GO:0019985;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRTKADCAGSSSGSYRKAVAARAPRKTFGSSSSGSNHDTSPTGKKSECKYAGGNPVCVRPIPTWQKGIGDFFGSPSTSQ
SQ  PEKENRIPSDDEEAGGSGAGKKPRKSRPLPPDPSEEAADSGDE
//
ID  Q6AZL2;
PN  PCNA-associated factor;
GN  pclaf;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q15004}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15004}. Note=Following DNA damage, localizes to DNA damage sites. Colocalizes with centrosomes in perinuclear region. {ECO:0000250|UniProtKB:Q15004}.
DR  UNIPROT: Q6AZL2;
DR  Pfam: PF15715;
DE  Function: PCNA-binding protein that acts as a regulator of DNA repair during DNA replication. Following DNA damage, the interaction with pcna is disrupted, facilitating the interaction between monoubiquitinated pcna and the translesion DNA synthesis DNA polymerase eta (polh) at stalled replisomes, facilitating the bypass of replication-fork- blocking lesions. Also acts as a regulator of centrosome number (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003682;
GO  GO:0006974;
GO  GO:0007098;
GO  GO:0006260;
GO  GO:0051726;
GO  GO:0009411;
GO  GO:0019985;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRTKADSAGSSASSGSYRKAVAARAPRKTFGSSSSGSNHVTSPTGKKSESKYAGGNPVCVRPTPTWQKGIGEFFGSPST
SQ  SQPEKENRIPSDDEEAGGSGAGKAPRKSRPLPPDPSEEAADSDDE
//
ID  P32567;
PN  Phosphatidic acid phosphohydrolase 1;
GN  PAH1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
DR  UNIPROT: P32567;
DR  UNIPROT: D6VZY7;
DR  Pfam: PF04571;
DR  Pfam: PF08235;
DE  Function: Mg(2+)-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol (PubMed:16467296, PubMed:16968695, PubMed:17910939, PubMed:17971454, PubMed:20876142, PubMed:21081492, PubMed:29765047). Required for de novo lipid synthesis and formation of lipid droplets (PubMed:21422231). Controls transcription of phospholipid biosynthetic genes and nuclear structure by regulating the amount of membrane present at the nuclear envelope (PubMed:15889145). Involved in plasmid maintenance, in respiration and in cell proliferation (PubMed:8437575). {ECO:0000269|PubMed:15889145, ECO:0000269|PubMed:16467296, ECO:0000269|PubMed:16968695, ECO:0000269|PubMed:17910939, ECO:0000269|PubMed:17971454, ECO:0000269|PubMed:20876142, ECO:0000269|PubMed:21081492, ECO:0000269|PubMed:21422231, ECO:0000269|PubMed:29765047, ECO:0000269|PubMed:8437575}.
DE  Reference Proteome: Yes;
DE  Interaction: P30822; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P35719; IntAct: EBI-390744; Score: 0.37
DE  Interaction: P16140; IntAct: EBI-809535; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-809535; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-809535; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-809535; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-809535; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-809535; Score: 0.53
DE  Interaction: P00549; IntAct: EBI-809535; Score: 0.35
DE  Interaction: P40038; IntAct: EBI-2612835; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3721470; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3752559; Score: 0.35
DE  Interaction: Q06677; IntAct: EBI-3758717; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0019898;
GO  GO:0005811;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005773;
GO  GO:0008195;
GO  GO:0000976;
GO  GO:0009060;
GO  GO:0044255;
GO  GO:0009062;
GO  GO:0034389;
GO  GO:0008654;
GO  GO:0006276;
GO  GO:0019432;
GO  GO:0042144;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MQYVGRALGSVSKTWSSINPATLSGAIDVIVVEHPDGRLSCSPFHVRFGKFQILKPSQKKVQVFINEKLSNMPMKLSDSG
SQ  EAYFVFEMGDQVTDVPDELLVSPVMSATSSPPQSPETSILEGGTEGEGEGENENKKKEKKVLEEPDFLDINDTGDSGSKN
SQ  SETTGSLSPTESSTTTPPDSVEERKLVEQRTKNFQQKLNKKLTEIHIPSKLDNNGDLLLDTEGYKPNKNMMHDTDIQLKQ
SQ  LLKDEFGNDSDISSFIKEDKNGNIKIVNPYEHLTDLSPPGTPPTMATSGSVLGLDAMESGSTLNSLSSSPSGSDTEDETS
SQ  FSKEQSSKSEKTSKKGTAGSGETEKRYIRTIRLTNDQLKCLNLTYGENDLKFSVDHGKAIVTSKLFVWRWDVPIVISDID
SQ  GTITKSDALGHVLAMIGKDWTHLGVAKLFSEISRNGYNILYLTARSAGQADSTRSYLRSIEQNGSKLPNGPVILSPDRTM
SQ  AALRREVILKKPEVFKIACLNDIRSLYFEDSDNEVDTEEKSTPFFAGFGNRITDALSYRTVGIPSSRIFTINTEGEVHME
SQ  LLELAGYRSSYIHINELVDHFFPPVSLDSVDLRTNTSMVPGSPPNRTLDNFDSEITSGRKTLFRGNQEEKFTDVNFWRDP
SQ  LVDIDNLSDISNDDSDNIDEDTDVSQQSNISRNRANSVKTAKVTKAPQRNVSGSTNNNEVLAASSDVENASDLVSSHSSS
SQ  GSTPNKSTMSKGDIGKQIYLELGSPLASPKLRYLDDMDDEDSNYNRTKSRRASSAAATSIDKEFKKLSVSKAGAPTRIVS
SQ  KINVSNDVHSLGNSDTESRREQSVNETGRNQLPHNSMDDKDLDSRVSDEFDDDEFDEDEFED
//
ID  Q8NC51;
PN  Plasminogen activator inhibitor 1 RNA-binding protein;
GN  SERBP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:28695742}. Nucleus {ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:28695742}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12505151}.
DR  UNIPROT: Q8NC51;
DR  UNIPROT: Q5VU19;
DR  UNIPROT: Q5VU20;
DR  UNIPROT: Q5VU22;
DR  UNIPROT: Q8WUH0;
DR  UNIPROT: Q96SE2;
DR  UNIPROT: Q9BTY3;
DR  UNIPROT: Q9BUM4;
DR  UNIPROT: Q9Y367;
DR  UNIPROT: Q9Y4S3;
DR  PDB: 4V6X;
DR  PDB: 6Z6M;
DR  PDB: 6Z6N;
DR  Pfam: PF04774;
DR  Pfam: PF16174;
DR  OMIM: 607378;
DR  DisGeNET: 26135;
DE  Function: May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation (PubMed:28695742). {ECO:0000269|PubMed:11001948, ECO:0000269|PubMed:28695742}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25509548; Score: 0.35
DE  Interaction: Q06787; IntAct: EBI-8844408; Score: 0.35
DE  Interaction: Q12873; IntAct: EBI-523588; Score: 0.58
DE  Interaction: Q53HC9; IntAct: EBI-1064285; Score: 0.00
DE  Interaction: P62330; IntAct: EBI-1068138; Score: 0.00
DE  Interaction: Q15654; IntAct: EBI-1069923; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1076169; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1079918; Score: 0.00
DE  Interaction: O75815; IntAct: EBI-1080874; Score: 0.00
DE  Interaction: O94817; IntAct: EBI-1085290; Score: 0.00
DE  Interaction: P32121; IntAct: EBI-1642567; Score: 0.35
DE  Interaction: Q00005; IntAct: EBI-2211497; Score: 0.35
DE  Interaction: Q8AZK7; IntAct: EBI-9632715; Score: 0.35
DE  Interaction: O15264; IntAct: EBI-2255044; Score: 0.35
DE  Interaction: P52735; IntAct: EBI-2654400; Score: 0.00
DE  Interaction: P01100; IntAct: EBI-2679744; Score: 0.00
DE  Interaction: P14921; IntAct: EBI-2680135; Score: 0.00
DE  Interaction: A0A6L8PVV9; IntAct: EBI-2828099; Score: 0.00
DE  Interaction: A0A5P8YLY5; IntAct: EBI-2861962; Score: 0.00
DE  Interaction: Q92731; IntAct: EBI-2880601; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-3045543; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-3050465; Score: 0.35
DE  Interaction: Q8TB96; IntAct: EBI-7383128; Score: 0.37
DE  Interaction: P68400; IntAct: EBI-5322101; Score: 0.44
DE  Interaction: Q0HD54; IntAct: EBI-6155110; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q15843; IntAct: EBI-21328206; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q9NR22; IntAct: EBI-8481541; Score: 0.37
DE  Interaction: O35182; IntAct: EBI-8456591; Score: 0.35
DE  Interaction: Q4VGL6; IntAct: EBI-8759371; Score: 0.35
DE  Interaction: P0C090; IntAct: EBI-8759987; Score: 0.35
DE  Interaction: Q99873; IntAct: EBI-8844279; Score: 0.35
DE  Interaction: P09651; IntAct: EBI-8844279; Score: 0.43
DE  Interaction: Q01844; IntAct: EBI-8844325; Score: 0.35
DE  Interaction: P51116; IntAct: EBI-8844325; Score: 0.35
DE  Interaction: P19338; IntAct: EBI-8845229; Score: 0.27
DE  Interaction: P31483; IntAct: EBI-8844366; Score: 0.27
DE  Interaction: P67809; IntAct: EBI-8853354; Score: 0.50
DE  Interaction: Q8NC51; IntAct: EBI-10486506; Score: 0.37
DE  Interaction: Q16666; IntAct: EBI-9995438; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: P23116; IntAct: EBI-11020127; Score: 0.35
DE  Interaction: Q9D287; IntAct: EBI-11022935; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-11088773; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-11145880; Score: 0.35
DE  Interaction: P19712; IntAct: EBI-10901232; Score: 0.35
DE  Interaction: Q9NRD5; IntAct: EBI-24463602; Score: 0.56
DE  Interaction: Q9NZI8; IntAct: EBI-13949271; Score: 0.35
DE  Interaction: Q15813; IntAct: EBI-21887754; Score: 0.40
DE  Interaction: Q9BTM9; IntAct: EBI-15902832; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: O00429; IntAct: EBI-20305770; Score: 0.35
DE  Interaction: Q99497; IntAct: EBI-20306366; Score: 0.35
DE  Interaction: Q99714; IntAct: EBI-20306067; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-20306992; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-20307233; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-20623424; Score: 0.35
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-20821761; Score: 0.35
DE  Interaction: Q969X2; IntAct: EBI-20903424; Score: 0.40
DE  Interaction: P30622; IntAct: EBI-20908792; Score: 0.40
DE  Interaction: P15918; IntAct: EBI-20921596; Score: 0.40
DE  Interaction: P46783; IntAct: EBI-20931200; Score: 0.40
DE  Interaction: Q5VT25; IntAct: EBI-20938284; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: O96013; IntAct: EBI-26962273; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-26966879; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: F5H7Q8; IntAct: EBI-21261537; Score: 0.35
DE  Interaction: O95183; IntAct: EBI-21267749; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: Q16828; IntAct: EBI-25377680; Score: 0.35
DE  Interaction: P06241; IntAct: EBI-25385167; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P41229; IntAct: EBI-25480257; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: Q8NHP6; IntAct: EBI-25617558; Score: 0.35
DE  Interaction: P50454; IntAct: EBI-25836558; Score: 0.56
DE  Interaction: P16284; IntAct: EBI-25881385; Score: 0.56
DE  Interaction: P37173; IntAct: EBI-25892860; Score: 0.56
DE  Interaction: Q09161; IntAct: EBI-26396507; Score: 0.35
DE  Interaction: P14240; IntAct: EBI-26968430; Score: 0.35
DE  Interaction: Q99608; IntAct: EBI-26955247; Score: 0.27
DE  Interaction: P0DTC9; IntAct: EBI-26994159; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045296;
GO  GO:0003730;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0032183;
GO  GO:0030578;
GO  GO:0043488;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKN
SQ  PLPPSVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGEGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDR
SQ  PIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQK
SQ  QISYNYSDLDQSNVTEETPEGEEHHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWK
SQ  KGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDD
SQ  PEAFPALA
//
ID  Q9CY58;
PN  Plasminogen activator inhibitor 1 RNA-binding protein;
GN  Serbp1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8NC51}. Nucleus {ECO:0000250|UniProtKB:Q8NC51}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8NC51}.
DR  UNIPROT: Q9CY58;
DR  UNIPROT: Q8BHS2;
DR  UNIPROT: Q8BHU0;
DR  UNIPROT: Q91WP3;
DR  UNIPROT: Q9CSN0;
DR  UNIPROT: Q9DBY6;
DR  PDB: 7LS1;
DR  PDB: 7LS2;
DR  Pfam: PF04774;
DR  Pfam: PF16174;
DE  Function: May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation. {ECO:0000250|UniProtKB:Q8NC51}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9CQT7; IntAct: EBI-7770477; Score: 0.37
DE  Interaction: Q9JIF0; IntAct: EBI-6393214; Score: 0.35
DE  Interaction: P14094; IntAct: EBI-20566937; Score: 0.35
DE  Interaction: Q6UWE0; IntAct: EBI-22050272; Score: 0.35
DE  Interaction: D0ZIB5; IntAct: EBI-27035217; Score: 0.46
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003730;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0032183;
GO  GO:0030578;
GO  GO:0042981;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKN
SQ  PLPPSVGVADKKEETQPPVALKKEGIRRVGRRPDQQLQGDGKLIDRRAERRPPRERRFEKPLEEKGEGGEFSVDRPIIER
SQ  PIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQK
SQ  QISYNCSDLDQSNVTEETPEGEEHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKK
SQ  GFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDP
SQ  EAFPALA
//
ID  Q6AXS5;
PN  Plasminogen activator inhibitor 1 RNA-binding protein;
GN  Serbp1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q8NC51}. Nucleus {ECO:0000250|UniProtKB:Q8NC51}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8NC51}.
DR  UNIPROT: Q6AXS5;
DR  UNIPROT: Q8VHU3;
DR  Pfam: PF04774;
DR  Pfam: PF16174;
DE  Function: May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation. {ECO:0000250|UniProtKB:Q8NC51}.
DE  Reference Proteome: Yes;
DE  Interaction: P61980; IntAct: EBI-931202; Score: 0.35
DE  Interaction: Q62976; IntAct: EBI-1638145; Score: 0.35
DE  Interaction: P35968; IntAct: EBI-22252438; Score: 0.35
DE  Interaction: P43403; IntAct: EBI-22252989; Score: 0.35
DE  Interaction: P11274; IntAct: EBI-22253187; Score: 0.35
DE  Interaction: P08575; IntAct: EBI-22253598; Score: 0.35
DE  Interaction: P51692; IntAct: EBI-22257101; Score: 0.35
DE  Interaction: Q96RT1; IntAct: EBI-22258042; Score: 0.35
DE  Interaction: O75096; IntAct: EBI-22258804; Score: 0.35
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003730;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0032183;
GO  GO:0030578;
GO  GO:0042981;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKN
SQ  PLPPSVGVADKKEETQPPVALKKEGIRRVGRRPDQQLQGDGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIER
SQ  PIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQK
SQ  QISYNCSDLEQSNVTEETPEGEEHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKK
SQ  GFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDP
SQ  EAFPALA
//
ID  Q13177;
PN  PAK-2p34;
GN  PAK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Serine/threonine-protein kinase PAK 2]: Cytoplasm {ECO:0000269|PubMed:19923322, ECO:0000269|PubMed:21555521}. Nucleus {ECO:0000269|PubMed:12853446, ECO:0000269|PubMed:21555521}. Note=MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane. {ECO:0000269|PubMed:19923322}. [PAK-2p34]: Nucleus {ECO:0000269|PubMed:12853446}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15471851}. Membrane {ECO:0000269|PubMed:16617111}; Lipid-anchor {ECO:0000269|PubMed:16617111}. Note=Interaction with ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear region (PubMed:15471851). Myristoylation changes PAK-2p34 location to the membrane (PubMed:16617111). {ECO:0000269|PubMed:15471851, ECO:0000269|PubMed:16617111}.
DR  UNIPROT: Q13177;
DR  UNIPROT: Q13154;
DR  UNIPROT: Q6ISC3;
DR  PDB: 3PCS;
DR  Pfam: PF00786;
DR  Pfam: PF00069;
DR  PROSITE: PS50108;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 605022;
DR  DisGeNET: 5062;
DE  Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation (PubMed:7744004, PubMed:19273597, PubMed:19923322, PubMed:9171063, PubMed:12853446, PubMed:16617111). Acts as downstream effector of the small GTPases CDC42 and RAC1 (PubMed:7744004). Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues (PubMed:7744004). Full-length PAK2 stimulates cell survival and cell growth (PubMed:7744004). Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration (PubMed:21317288). Phosphorylates JUN and plays an important role in EGF-induced cell proliferation (PubMed:21177766). Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP (PubMed:21724829). Phosphorylates CASP7, thereby preventing its activity (PubMed:21555521, PubMed:27889207). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (PubMed:19273597, PubMed:19923322). On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway (PubMed:9171063, PubMed:12853446, PubMed:16617111). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (PubMed:15234964). {ECO:0000269|PubMed:12853446, ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:16617111, ECO:0000269|PubMed:19273597, ECO:0000269|PubMed:19923322, ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:21317288, ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:21724829, ECO:0000269|PubMed:27889207, ECO:0000269|PubMed:7744004, ECO:0000269|PubMed:9171063}.
DE  Reference Proteome: Yes;
DE  Interaction: O60711; IntAct: EBI-21816074; Score: 0.35
DE  Interaction: O94875; IntAct: EBI-7976043; Score: 0.52
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P07948; IntAct: EBI-7975774; Score: 0.40
DE  Interaction: P12931; IntAct: EBI-7975714; Score: 0.52
DE  Interaction: Q03001; IntAct: EBI-3446930; Score: 0.00
DE  Interaction: Q07912; IntAct: EBI-8143865; Score: 0.44
DE  Interaction: P08631; IntAct: EBI-7975744; Score: 0.52
DE  Interaction: P07947; IntAct: EBI-7975821; Score: 0.40
DE  Interaction: P06241; IntAct: EBI-7975850; Score: 0.40
DE  Interaction: Q5TCZ1; IntAct: EBI-7975880; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-7975909; Score: 0.52
DE  Interaction: Q14155; IntAct: EBI-7975939; Score: 0.69
DE  Interaction: Q15052; IntAct: EBI-7975985; Score: 0.71
DE  Interaction: P16333; IntAct: EBI-7976014; Score: 0.71
DE  Interaction: O60504; IntAct: EBI-7976072; Score: 0.77
DE  Interaction: Q9BX66; IntAct: EBI-7976162; Score: 0.52
DE  Interaction: Q8TEJ3; IntAct: EBI-7976191; Score: 0.52
DE  Interaction: Q7Z6J0; IntAct: EBI-7976274; Score: 0.40
DE  Interaction: P21266; IntAct: EBI-1062011; Score: 0.00
DE  Interaction: Q13404; IntAct: EBI-1062077; Score: 0.00
DE  Interaction: Q15019; IntAct: EBI-1062392; Score: 0.00
DE  Interaction: O00264; IntAct: EBI-1062413; Score: 0.00
DE  Interaction: P04179; IntAct: EBI-1062777; Score: 0.00
DE  Interaction: P25786; IntAct: EBI-1062798; Score: 0.00
DE  Interaction: O75534; IntAct: EBI-1063779; Score: 0.00
DE  Interaction: P30086; IntAct: EBI-1064612; Score: 0.00
DE  Interaction: Q13526; IntAct: EBI-1065182; Score: 0.00
DE  Interaction: P27797; IntAct: EBI-1065704; Score: 0.00
DE  Interaction: Q00005; IntAct: EBI-1066757; Score: 0.00
DE  Interaction: P20290; IntAct: EBI-1067029; Score: 0.00
DE  Interaction: P50395; IntAct: EBI-1067128; Score: 0.00
DE  Interaction: Q99436; IntAct: EBI-1067229; Score: 0.00
DE  Interaction: P83731; IntAct: EBI-1067438; Score: 0.00
DE  Interaction: P27695; IntAct: EBI-1067694; Score: 0.00
DE  Interaction: P07355; IntAct: EBI-1067788; Score: 0.00
DE  Interaction: P06730; IntAct: EBI-1068542; Score: 0.00
DE  Interaction: Q9Y2X7; IntAct: EBI-8553586; Score: 0.74
DE  Interaction: Q13263; IntAct: EBI-1069311; Score: 0.00
DE  Interaction: Q16630; IntAct: EBI-1069571; Score: 0.00
DE  Interaction: Q04637; IntAct: EBI-1069690; Score: 0.00
DE  Interaction: P22061; IntAct: EBI-1069927; Score: 0.00
DE  Interaction: P60953; IntAct: EBI-10228458; Score: 0.87
DE  Interaction: P07237; IntAct: EBI-1070610; Score: 0.00
DE  Interaction: P25205; IntAct: EBI-1070728; Score: 0.00
DE  Interaction: P23526; IntAct: EBI-1071072; Score: 0.00
DE  Interaction: P35580; IntAct: EBI-1071084; Score: 0.00
DE  Interaction: P30084; IntAct: EBI-1071541; Score: 0.00
DE  Interaction: P54819; IntAct: EBI-1071554; Score: 0.00
DE  Interaction: Q9Y266; IntAct: EBI-1072180; Score: 0.00
DE  Interaction: P24666; IntAct: EBI-1072337; Score: 0.00
DE  Interaction: Q14697; IntAct: EBI-1072589; Score: 0.00
DE  Interaction: Q9UNM6; IntAct: EBI-1072597; Score: 0.00
DE  Interaction: Q13347; IntAct: EBI-1072860; Score: 0.00
DE  Interaction: Q14161; IntAct: EBI-11070372; Score: 0.56
DE  Interaction: P25787; IntAct: EBI-1073377; Score: 0.00
DE  Interaction: P62910; IntAct: EBI-1073488; Score: 0.00
DE  Interaction: P00505; IntAct: EBI-1073588; Score: 0.00
DE  Interaction: P62750; IntAct: EBI-1073686; Score: 0.00
DE  Interaction: P61224; IntAct: EBI-1074059; Score: 0.00
DE  Interaction: P53667; IntAct: EBI-1182678; Score: 0.56
DE  Interaction: P04049; IntAct: EBI-1182700; Score: 0.56
DE  Interaction: Q13177; IntAct: EBI-1182717; Score: 0.60
DE  Interaction: Q14247; IntAct: EBI-7852779; Score: 0.44
DE  Interaction: O55043; IntAct: EBI-8169547; Score: 0.65
DE  Interaction: P63000; IntAct: EBI-8583033; Score: 0.83
DE  Interaction: P15056; IntAct: EBI-3438072; Score: 0.00
DE  Interaction: Q09472; IntAct: EBI-3446937; Score: 0.00
DE  Interaction: O14730; IntAct: EBI-3932905; Score: 0.37
DE  Interaction: P55210; IntAct: EBI-5326935; Score: 0.62
DE  Interaction: P42858; IntAct: EBI-5327199; Score: 0.40
DE  Interaction: Q13153; IntAct: EBI-6256371; Score: 0.64
DE  Interaction: Q9BUB5; IntAct: EBI-6590754; Score: 0.27
DE  Interaction: P42574; IntAct: EBI-6590924; Score: 0.27
DE  Interaction: P14618; IntAct: EBI-9353313; Score: 0.44
DE  Interaction: Q9H4E5; IntAct: EBI-10228468; Score: 0.72
DE  Interaction: P04020; IntAct: EBI-11736846; Score: 0.37
DE  Interaction: P06429; IntAct: EBI-11737257; Score: 0.37
DE  Interaction: Q9WVM1; IntAct: EBI-11008211; Score: 0.35
DE  Interaction: Q3THE2; IntAct: EBI-11063194; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-11070372; Score: 0.35
DE  Interaction: Q9NVF7; IntAct: EBI-11070372; Score: 0.53
DE  Interaction: B7Z6G2; IntAct: EBI-11070372; Score: 0.35
DE  Interaction: Q9NXV6; IntAct: EBI-11125351; Score: 0.35
DE  Interaction: Q96NL6; IntAct: EBI-11376636; Score: 0.27
DE  Interaction: Q9NYB9; IntAct: EBI-24349863; Score: 0.56
DE  Interaction: O43639; IntAct: EBI-24478338; Score: 0.67
DE  Interaction: Q8WVK2; IntAct: EBI-21500567; Score: 0.35
DE  Interaction: P05362; IntAct: EBI-21568860; Score: 0.35
DE  Interaction: P02675; IntAct: EBI-21646531; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-21647926; Score: 0.35
DE  Interaction: Q9BTV5; IntAct: EBI-21692187; Score: 0.35
DE  Interaction: Q92845; IntAct: EBI-21702814; Score: 0.35
DE  Interaction: Q9NYY3; IntAct: EBI-21720972; Score: 0.35
DE  Interaction: Q96K76; IntAct: EBI-21756437; Score: 0.35
DE  Interaction: Q01968; IntAct: EBI-21818611; Score: 0.35
DE  Interaction: O60404; IntAct: EBI-21879957; Score: 0.35
DE  Interaction: Q2HZL0; IntAct: EBI-15571943; Score: 0.40
DE  Interaction: Q5PP90; IntAct: EBI-15780462; Score: 0.56
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21381204; Score: 0.00
DE  Interaction: P49023; IntAct: EBI-25376663; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: Q7L0Q8; IntAct: EBI-28939307; Score: 0.35
DE  Interaction: Q16891; IntAct: EBI-28939307; Score: 0.35
DE  Interaction: Q16610; IntAct: EBI-28939307; Score: 0.35
DE  Interaction: P55265; IntAct: EBI-28939307; Score: 0.35
DE  Interaction: P54756; IntAct: EBI-28939307; Score: 0.35
DE  Interaction: O75390; IntAct: EBI-28939307; Score: 0.35
DE  Interaction: Q14145; IntAct: EBI-30821841; Score: 0.44
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098978;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0030141;
GO  GO:0005524;
GO  GO:0045296;
GO  GO:0042802;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0030296;
GO  GO:0031267;
GO  GO:0034333;
GO  GO:0006915;
GO  GO:0070830;
GO  GO:0003300;
GO  GO:0071407;
GO  GO:0071560;
GO  GO:0060996;
GO  GO:0035556;
GO  GO:0051179;
GO  GO:0043066;
GO  GO:2001271;
GO  GO:0006469;
GO  GO:0051497;
GO  GO:0018105;
GO  GO:0016310;
GO  GO:2001238;
GO  GO:0050731;
GO  GO:0046777;
GO  GO:0150105;
GO  GO:0006468;
GO  GO:0050770;
GO  GO:0051493;
GO  GO:0043408;
GO  GO:0007165;
GO  GO:0002223;
GO  GO:0048010;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16617111};
SQ  MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGTEKGSKKKEKERPEISPPSDF
SQ  EHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAK
SQ  GTEAPAVVTEEEDDDEETAPPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIV
SQ  SIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELF
SQ  VVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKR
SQ  STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRC
SQ  LEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR
//
ID  Q8CIN4;
PN  PAK-2p34;
GN  Pak2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: [Serine/threonine-protein kinase PAK 2]: Cytoplasm {ECO:0000250|UniProtKB:Q13177}. Nucleus {ECO:0000250|UniProtKB:Q13177}. Note=MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane. {ECO:0000250|UniProtKB:Q13177}. [PAK-2p34]: Nucleus {ECO:0000250|UniProtKB:Q13177}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13177}. Membrane {ECO:0000250|UniProtKB:Q13177}; Lipid-anchor {ECO:0000250|UniProtKB:Q13177}. Note=Interaction with ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear region. Myristoylation changes PAK-2p34 location to the membrane. {ECO:0000250|UniProtKB:Q13177}.
DR  UNIPROT: Q8CIN4;
DR  Pfam: PF00786;
DR  Pfam: PF00069;
DR  PROSITE: PS50108;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation (PubMed:11278362). Acts as downstream effector of the small GTPases CDC42 and RAC1 (By similarity). Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues (By similarity). Full-length PAK2 stimulates cell survival and cell growth (By similarity). Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration (By similarity). Phosphorylates JUN and plays an important role in EGF-induced cell proliferation (By similarity). Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP (PubMed:11278362). Phosphorylates CASP7, thereby preventing its activity (By similarity). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (By similarity). On the other hand, apoptotic stimuli such as DNA damage lead to caspase- mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway (By similarity). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (By similarity). {ECO:0000250|UniProtKB:Q13177, ECO:0000269|PubMed:11278362}.
DE  Reference Proteome: Yes;
DE  Interaction: P28867; IntAct: EBI-16006728; Score: 0.35
DE  Interaction: Q96B97; IntAct: EBI-6953756; Score: 0.40
DE  Interaction: Q01112; IntAct: EBI-1559309; Score: 0.40
DE  Interaction: P42858; IntAct: EBI-5327215; Score: 0.40
DE  Interaction: P42859; IntAct: EBI-5327412; Score: 0.40
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: P60953; IntAct: EBI-16881295; Score: 0.37
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0030141;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0030296;
GO  GO:0031267;
GO  GO:0034333;
GO  GO:0006915;
GO  GO:0070830;
GO  GO:0003300;
GO  GO:0071407;
GO  GO:0071560;
GO  GO:0060996;
GO  GO:0035556;
GO  GO:0043066;
GO  GO:2001271;
GO  GO:0051497;
GO  GO:0018105;
GO  GO:0016310;
GO  GO:2001238;
GO  GO:0050731;
GO  GO:0046777;
GO  GO:0150105;
GO  GO:0006468;
GO  GO:0050770;
GO  GO:0051493;
GO  GO:0043408;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q13177};
SQ  MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRNKIISIFSGTEKGSKKKEKERPEISPPSDF
SQ  EHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNTK
SQ  GSETSAVVTEEDDDDEDAAPPVIAPRPDHTKSIYTRSVIDPIPAPVGDSNVDSGAKSSDKQKKKAKMTDEEIMEKLRTIV
SQ  SIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELF
SQ  VVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKR
SQ  STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRC
SQ  LEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLILAAKEAMKSNR
//
ID  Q29502;
PN  PAK-2p34;
GN  PAK2;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: [Serine/threonine-protein kinase PAK 2]: Cytoplasm {ECO:0000250|UniProtKB:Q13177}. Nucleus {ECO:0000250|UniProtKB:Q13177}. Note=MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane. {ECO:0000250|UniProtKB:Q13177}. [PAK-2p34]: Nucleus {ECO:0000250|UniProtKB:Q13177}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13177}. Membrane {ECO:0000250|UniProtKB:Q13177}; Lipid-anchor {ECO:0000250|UniProtKB:Q13177}. Note=Interaction with ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear region. Myristoylation changes PAK-2p34 location to the membrane. {ECO:0000250|UniProtKB:Q13177}.
DR  UNIPROT: Q29502;
DR  Pfam: PF00786;
DR  Pfam: PF00069;
DR  PROSITE: PS50108;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Phosphorylates CASP7, thereby preventing its activity. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (By similarity). {ECO:0000250|UniProtKB:Q13177}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6Y5D8; IntAct: EBI-4396533; Score: 0.53
GO  GO:0005911;
GO  GO:0005829;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0030296;
GO  GO:0031267;
GO  GO:0034333;
GO  GO:0070830;
GO  GO:0071407;
GO  GO:0060996;
GO  GO:0097194;
GO  GO:2001271;
GO  GO:0051497;
GO  GO:0018105;
GO  GO:0043065;
GO  GO:2001238;
GO  GO:0046777;
GO  GO:0150105;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q13177};
SQ  MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRNKIISIFSGTEKGSKKKEKERPEISPPSDF
SQ  EHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGAPALNTK
SQ  VSETSAVVTEEDDDDEEAAPPVIAPRPDHTKSIYTRSVIDPIPAPVGDSHVDSGAKSSDKQKKKTKMTDEEIMEKLRTIV
SQ  SIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELF
SQ  VVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKR
SQ  STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRC
SQ  LEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR
//
ID  Q64303;
PN  PAK-2p34;
GN  Pak2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: [Serine/threonine-protein kinase PAK 2]: Cytoplasm {ECO:0000250|UniProtKB:Q13177}. Nucleus {ECO:0000250|UniProtKB:Q13177}. Note=MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane. {ECO:0000250|UniProtKB:Q13177}. [PAK-2p34]: Nucleus {ECO:0000250|UniProtKB:Q13177}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q13177}. Membrane {ECO:0000250|UniProtKB:Q13177}; Lipid-anchor {ECO:0000250|UniProtKB:Q13177}. Note=Interaction with ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear region. Myristoylation changes PAK-2p34 location to the membrane. {ECO:0000250|UniProtKB:Q13177}.
DR  UNIPROT: Q64303;
DR  UNIPROT: Q9QYU0;
DR  PDB: 2DF6;
DR  Pfam: PF00786;
DR  Pfam: PF00069;
DR  PROSITE: PS50108;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Phosphorylates CASP7, thereby preventing its activity. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (By similarity). {ECO:0000250|UniProtKB:Q13177}.
DE  Reference Proteome: Yes;
DE  Interaction: O75096; IntAct: EBI-22258804; Score: 0.35
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0030141;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0030296;
GO  GO:0031267;
GO  GO:0034333;
GO  GO:0070830;
GO  GO:0003300;
GO  GO:0071407;
GO  GO:0071560;
GO  GO:0060996;
GO  GO:0035556;
GO  GO:0043066;
GO  GO:2001271;
GO  GO:0051497;
GO  GO:0018105;
GO  GO:0016310;
GO  GO:2001238;
GO  GO:0050731;
GO  GO:0046777;
GO  GO:0150105;
GO  GO:0006468;
GO  GO:0050770;
GO  GO:0051493;
GO  GO:0043408;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q13177};
SQ  MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRNKIISIFSSTEKGSKKKEKERPEISPPSDF
SQ  EHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNTK
SQ  GSETSAVVTEEDDDDEDAAPPVIAPRPDHTKSIYTRSVIDPIPAPVGDSNVDSGAKSSDKQKKKAKMTDEEIMEKLRTIV
SQ  SIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELF
SQ  VVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKR
SQ  STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRC
SQ  LEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLILAAKEAMKSNR
//
ID  Q9NR21;
PN  Protein mono-ADP-ribosyltransferase PARP11;
GN  PARP11;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:25673562}. Note=Colocalizes with NUP153 at nuclear pores. {ECO:0000269|PubMed:25673562}.
DR  UNIPROT: Q9NR21;
DR  UNIPROT: B4DRQ0;
DR  UNIPROT: F8WBZ7;
DR  UNIPROT: Q68DS1;
DR  UNIPROT: Q8N5Y9;
DR  PDB: 2DK6;
DR  Pfam: PF00644;
DR  Pfam: PF02825;
DR  PROSITE: PS51059;
DR  PROSITE: PS50918;
DR  OMIM: 616706;
DR  DisGeNET: 57097;
DE  Function: Mono-ADP-ribosyltransferase that mediates mono-ADP- ribosylation of target proteins (PubMed:25043379, PubMed:25673562). Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:Q8CFF0, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:25673562}.
DE  Reference Proteome: Yes;
DE  Interaction: Q969Y2; IntAct: EBI-24262695; Score: 0.56
DE  Interaction: Q15645; IntAct: EBI-2350330; Score: 0.49
DE  Interaction: Q8TEB1; IntAct: EBI-2510918; Score: 0.40
DE  Interaction: Q9Y508; IntAct: EBI-2510918; Score: 0.40
DE  Interaction: P61626; IntAct: EBI-2510918; Score: 0.40
DE  Interaction: Q99750; IntAct: EBI-10177824; Score: 0.49
DE  Interaction: Q9UBR4; IntAct: EBI-24526909; Score: 0.56
DE  Interaction: Q96ED9; IntAct: EBI-24447418; Score: 0.56
DE  Interaction: Q8N9I9; IntAct: EBI-24546487; Score: 0.56
DE  Interaction: Q969G2; IntAct: EBI-24559454; Score: 0.56
DE  Interaction: Q96A37; IntAct: EBI-21646475; Score: 0.35
DE  Interaction: P53778; IntAct: EBI-21646475; Score: 0.35
DE  Interaction: P07550; IntAct: EBI-25830529; Score: 0.56
DE  Interaction: P28329; IntAct: EBI-25838070; Score: 0.56
DE  Interaction: G5E9A7; IntAct: EBI-25843022; Score: 0.56
DE  Interaction: P22607; IntAct: EBI-25854609; Score: 0.56
DE  Interaction: P28799; IntAct: EBI-25861404; Score: 0.56
DE  Interaction: Q14957; IntAct: EBI-25862867; Score: 0.56
DE  Interaction: P06396; IntAct: EBI-25864317; Score: 0.56
DE  Interaction: O60260; IntAct: EBI-25880612; Score: 0.56
DE  Interaction: Q86WV8; IntAct: EBI-25893727; Score: 0.56
DE  Interaction: Q9Y649; IntAct: EBI-25901282; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25915986; Score: 0.56
DE  Interaction: Q9Y3C5; IntAct: EBI-25919257; Score: 0.56
DE  Interaction: Q8WXH2; IntAct: EBI-25928163; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25932431; Score: 0.56
DE  Interaction: P37840; IntAct: EBI-25942243; Score: 0.56
DE  Interaction: Q13148; IntAct: EBI-25985743; Score: 0.56
GO  GO:0005829;
GO  GO:0016604;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003950;
GO  GO:0140803;
GO  GO:0140804;
GO  GO:1990404;
GO  GO:0030154;
GO  GO:0051028;
GO  GO:0006998;
GO  GO:0070213;
GO  GO:0140289;
GO  GO:0015031;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MWEANPEMFHKAEELFSKTTNNEVDDMDTSDTQWGWFYLAECGKWHMFQPDTNSQCSVSSEDIEKSFKTNPCGSISFTTS
SQ  KFSYKIDFAEMKQMNLTTGKQRLIKRAPFSISAFSYICENEAIPMPPHWENVNTQVPYQLIPLHNQTHEYNEVANLFGKT
SQ  MDRNRIKRIQRIQNLDLWEFFCRKKAQLKKKRGVPQINEQMLFHGTSSEFVEAICIHNFDWRINGIHGAVFGKGTYFARD
SQ  AAYSSRFCKDDIKHGNTFQIHGVSLQQRHLFRTYKSMFLARVLIGDYINGDSKYMRPPSKDGSYVNLYDSCVDDTWNPKI
SQ  FVVFDANQIYPEYLIDFH
//
ID  Q8CFF0;
PN  Protein mono-ADP-ribosyltransferase PARP11;
GN  Parp11;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9NR21}. Note=Colocalizes with NUP153 at nuclear pores. {ECO:0000250|UniProtKB:Q9NR21}.
DR  UNIPROT: Q8CFF0;
DR  UNIPROT: Q3UAF2;
DR  UNIPROT: Q3UZR7;
DR  Pfam: PF00644;
DR  Pfam: PF02825;
DR  PROSITE: PS51059;
DR  PROSITE: PS50918;
DE  Function: Mono-ADP-ribosyltransferase that mediates mono-ADP- ribosylation of target proteins (By similarity). Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (PubMed:25673562). {ECO:0000250|UniProtKB:Q9NR21, ECO:0000269|PubMed:25673562}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016604;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003950;
GO  GO:0140803;
GO  GO:0140804;
GO  GO:1990404;
GO  GO:0030154;
GO  GO:0051028;
GO  GO:0006998;
GO  GO:0070213;
GO  GO:0140289;
GO  GO:0015031;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFHKTEEFFPKKTDSDVDDMDTSDTQWGWFYLAECGKWHMFQPDTNIQCSVSSEDIEKSFKTNPCGSISFTTSKFSYKID
SQ  FAEMKQMNLVTGKQRLIKRAPFSISAFSYICENEAIPMPTHWENVNPDVPYQLVSLQNQTHEYNEVASLFGKTMDRNRIK
SQ  RIQRIQNLDLWEFFCRKKAQLKKKRGVPQINEQMLFHGTSSEFVEAICIHNFDWRINGVHGAVFGKGTYFARDAAYSSRF
SQ  CKDDIKHGNTFQIHGVSLQQRHLFRTYKSMFLARVLIGDYINGDSKYMRPPSKDGSYVNLYDSCVDDTWNPKIFVVFDAN
SQ  QIYPEYLIDFH
//
ID  Q2TBN6;
PN  PCI domain-containing protein 2;
GN  PCID2;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q5JVF3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q5JVF3}.
DR  UNIPROT: Q2TBN6;
DR  Pfam: PF01399;
DR  PROSITE: PS50250;
DE  Function: Required for B-cell survival through the regulation of the expression of cell-cycle checkpoint MAD2L1 protein during B cell differentiation (By similarity). As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (By similarity). Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and transcription- associated genomic instability (By similarity). Blocks the activity of the SRCAP chromatin remodeling complex by interacting with SRCAP complex member ZNHIT1 and inhibiting its interaction with the complex (By similarity). This prevents the deposition of histone variant H2AZ1/H2A.Z at the nucleosomes of key lymphoid fate regulator genes which suppresses their expression and restricts lymphoid lineage commitment (By similarity). {ECO:0000250|UniProtKB:Q5JVF3, ECO:0000250|UniProtKB:Q8BFV2}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0003690;
GO  GO:0003723;
GO  GO:0043066;
GO  GO:2000117;
GO  GO:1905457;
GO  GO:0016973;
GO  GO:0045893;
GO  GO:0090267;
GO  GO:0000973;
GO  GO:1900049;
GO  GO:0043488;
GO  GO:0048536;
GO  GO:0006368;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHITINQYLQQVCEAIDTRDGASLAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMFAAHLRCTYAVGNHDFIEA
SQ  YKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRIFANNADQQLVKKGKSKVGDMLEKAAELLMGCFRVCASDTRAGI
SQ  EDSKKRGMLFLVNQLFKIYFKINKLHLCKPLIRAIDSSNLKDDYSTAQRVTYRYYVGRKAMFDSDFKQAEEYLSFAFEHC
SQ  HRSSQKNKRMVLIYLLPVKMLLGHMPTIELLRKYHLMQFAEVTRAVSEGNLLLLNEALAAHETFFIRCGIFLILEKLKII
SQ  TYRNLFKKVNSLSSASSRYLLLKTHQLSLDAFLVALKFMQVEDVDIAEVQCILANLIYMGHIKGYISHQHQKLVVSKQNP
SQ  FPPLSTVC
//
ID  Q9VTL1;
PN  PCI domain-containing protein 2 homolog;
GN  PCID2;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:18086857, ECO:0000269|PubMed:27016737}. Cytoplasm {ECO:0000269|PubMed:18086857, ECO:0000269|PubMed:33602059}. Nucleus membrane {ECO:0000269|PubMed:33602059}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33602059}. Note=Shuttles in and out of the nucleus by a emb/Crm1-dependent mechanism (PubMed:18086857). The ubiquitinated forms are localized to the cytoplasm, the nonubiquitinated forms are localized to the nucleus, and both forms are associated with the nuclear membrane (PubMed:33602059). Associated with cytoplasmic microtubules (PubMed:33602059). Associates with mRNA in the nucleus and cytoplasm (PubMed:33602059). {ECO:0000269|PubMed:18086857, ECO:0000269|PubMed:33602059}.
DR  UNIPROT: Q9VTL1;
DR  Pfam: PF01399;
DR  PROSITE: PS50250;
DE  Function: Required for the export of nuclear mRNAs and involved in mRNA trafficking in the cytoplasm (PubMed:27016737, PubMed:28554770, PubMed:33602059). Component of the nuclear pore complex (NPC)- associated TREX-2/AMEX complex (anchoring and mRNA export complex) which functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), thereby enabling the export of mRNAs to the cytoplasm through the nuclear pores (PubMed:27016737, PubMed:28554770, PubMed:33602059). Within the complex, specifically promotes the association of factors involved in regulating nuclear mRNA export, such as Moe, sbr/NXF1 and the ORC complex, to the mRNPs particles (PubMed:27016737, PubMed:28554770, PubMed:33602059). In the cytoplasm, functions independently of its role in the TREX-2/AMEX complex, to promote cytoplasmic mRNA trafficking together with nudC (PubMed:33602059). Associates with translationally active polysomes (PubMed:18086857). {ECO:0000269|PubMed:18086857, ECO:0000269|PubMed:27016737, ECO:0000269|PubMed:28554770, ECO:0000269|PubMed:33602059}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VM46; IntAct: EBI-15146793; Score: 0.62
DE  Interaction: O18388; IntAct: EBI-258749; Score: 0.00
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0070390;
GO  GO:0003690;
GO  GO:0019904;
GO  GO:0003723;
GO  GO:0006406;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0015031;
GO  GO:0006417;
GO  GO:0006368;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGTVNNYLSGVLHAAQDLDGESLATYLSLRDVHVQNHNLYIAQPEKLVDRFLKPPLDEVVSAHLKVLYHLAQEPPGYME
SQ  AYTQQSAACGAVVRLLQQLKDENWCLPLMYRVCLDLRYLAQACEKHCQGFTPGHVLEKAADCIMACFRVCAADGRASEED
SQ  TKRLGMMNLVNQLFKIYFRINKLHLCKPLIRAIDNCIFKDSFPLPEQITYKYFVGRRAMFDSNYQAAVQYLSYAFSNCPD
SQ  RFASNKRLILIYLVPVKMLLGYLPSKSLLQRYDLLLFLDLAMAMKAGNVNRFDEIVRDQELVLIRSGIYLLVEKLKFLVY
SQ  RNLFKKVFVIRKSHQLDMGDFLSALHFVGLTDVSLDETHCIVANLIYDGKIKGYISHAHNKLVVSKQNPFPSVSL
//
ID  Q5JVF3;
PN  PCI domain-containing protein 2;
GN  PCID2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}.
DR  UNIPROT: Q5JVF3;
DR  UNIPROT: A6NK09;
DR  UNIPROT: Q3ZCX1;
DR  UNIPROT: Q5TC57;
DR  UNIPROT: Q5TC58;
DR  UNIPROT: Q9H7K1;
DR  UNIPROT: Q9HBZ7;
DR  UNIPROT: Q9NUK6;
DR  UNIPROT: Q9NVY1;
DR  UNIPROT: Q9NW44;
DR  UNIPROT: Q9NWH3;
DR  PDB: 3T5X;
DR  Pfam: PF01399;
DR  PROSITE: PS50250;
DR  OMIM: 613713;
DR  DisGeNET: 55795;
DE  Function: Required for B-cell survival through the regulation of the expression of cell-cycle checkpoint MAD2L1 protein during B cell differentiation (By similarity). As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (PubMed:22307388). Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and transcription-associated genomic instability (PubMed:24896180). Blocks the activity of the SRCAP chromatin remodeling complex by interacting with SRCAP complex member ZNHIT1 and inhibiting its interaction with the complex (By similarity). This prevents the deposition of histone variant H2AZ1/H2A.Z at the nucleosomes of key lymphoid fate regulator genes which suppresses their expression and restricts lymphoid lineage commitment (By similarity). {ECO:0000250|UniProtKB:Q8BFV2, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:24896180, ECO:0000305|PubMed:23591820}.
DE  Reference Proteome: Yes;
DE  Interaction: O60318; IntAct: EBI-15970583; Score: 0.35
DE  Interaction: Q9HAW0; IntAct: EBI-1064032; Score: 0.00
DE  Interaction: Q13418; IntAct: EBI-1066382; Score: 0.00
DE  Interaction: Q9HC98; IntAct: EBI-1068849; Score: 0.00
DE  Interaction: Q15796; IntAct: EBI-2695978; Score: 0.40
DE  Interaction: P03496; IntAct: EBI-6154589; Score: 0.35
DE  Interaction: Q9WPI5; IntAct: EBI-6156643; Score: 0.35
DE  Interaction: Q99AU3; IntAct: EBI-6157083; Score: 0.35
DE  Interaction: C3W5S7; IntAct: EBI-6158924; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q9UKT9; IntAct: EBI-10244567; Score: 0.56
DE  Interaction: Q8XA11; IntAct: EBI-10039010; Score: 0.37
DE  Interaction: P52732; IntAct: EBI-11007621; Score: 0.35
DE  Interaction: Q8BFY9; IntAct: EBI-11018381; Score: 0.35
DE  Interaction: O60293; IntAct: EBI-11060132; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-11155257; Score: 0.35
DE  Interaction: P60896; IntAct: EBI-15970426; Score: 0.61
DE  Interaction: Q96PV6; IntAct: EBI-24759679; Score: 0.56
DE  Interaction: C5E524; IntAct: EBI-12584088; Score: 0.35
DE  Interaction: Q194T2; IntAct: EBI-12587357; Score: 0.35
DE  Interaction: Q12798; IntAct: EBI-21576600; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-16786806; Score: 0.27
DE  Interaction: P49336; IntAct: EBI-16790360; Score: 0.27
DE  Interaction: P62753; IntAct: EBI-16798663; Score: 0.27
DE  Interaction: Q53F19; IntAct: EBI-20623276; Score: 0.53
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055586; Score: 0.35
DE  Interaction: Q8WV16; IntAct: EBI-30863977; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
GO  GO:0005737;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0003690;
GO  GO:0003723;
GO  GO:0043066;
GO  GO:2000117;
GO  GO:1905457;
GO  GO:0016973;
GO  GO:0045579;
GO  GO:0045893;
GO  GO:0090267;
GO  GO:0000973;
GO  GO:0015031;
GO  GO:1900049;
GO  GO:0043488;
GO  GO:0048536;
GO  GO:0006368;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHITINQYLQQVYEAIDSRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMFAAHLRCTYAVGNHDFIEA
SQ  YKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRVFANNADQQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGI
SQ  EDSKKWGMLFLVNQLFKIYFKINKLHLCKPLIRAIDSSNLKDDYSTAQRVTYKYYVGRKAMFDSDFKQAEEYLSFAFEHC
SQ  HRSSQKNKRMILIYLLPVKMLLGHMPTVELLKKYHLMQFAEVTRAVSEGNLLLLHEALAKHEAFFIRCGIFLILEKLKII
SQ  TYRNLFKKVYLLLKTHQLSLDAFLVALKFMQVEDVDIDEVQCILANLIYMGHVKGYISHQHQKLVVSKQNPFPPLSTVC
//
ID  Q8BFV2;
PN  PCI domain-containing protein 2;
GN  Pcid2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q5JVF3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q5JVF3}.
DR  UNIPROT: Q8BFV2;
DR  UNIPROT: Q147Z6;
DR  UNIPROT: Q8C951;
DR  Pfam: PF01399;
DR  PROSITE: PS50250;
DE  Function: Required for B-cell survival through the regulation of the expression of cell-cycle checkpoint MAD2L1 protein during B cell differentiation (PubMed:20870947). As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores (By similarity). Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and transcription-associated genomic instability (By similarity). Blocks the activity of the SRCAP chromatin remodeling complex by interacting with SRCAP complex member ZNHIT1 and inhibiting its interaction with the complex (PubMed:29138493). This prevents the deposition of histone variant H2AZ1/H2A.Z at the nucleosomes of key lymphoid fate regulator genes which suppresses their expression and restricts lymphoid lineage commitment (PubMed:29138493). {ECO:0000250|UniProtKB:Q5JVF3, ECO:0000269|PubMed:20870947, ECO:0000269|PubMed:29138493}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9EPK7; IntAct: EBI-17171503; Score: 0.35
GO  GO:0005737;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0003690;
GO  GO:0003723;
GO  GO:0043066;
GO  GO:2000117;
GO  GO:1905457;
GO  GO:0016973;
GO  GO:0045579;
GO  GO:0045893;
GO  GO:0090267;
GO  GO:0000973;
GO  GO:1900049;
GO  GO:0043488;
GO  GO:0048536;
GO  GO:0006368;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHITINQYLQQVYEAIDTRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMFAAHLRCTYAVGNHDFIEA
SQ  YKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRIFANNADQQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGI
SQ  EDSKKWGMLFLVNQLFKIYFKINKLHLCKPLIRAIDSSNLKDDYSTAQRITYKYYVGRKAMFDSDFKQAEEYLSFAFEHC
SQ  HRSSQKNKRMILIYLLPVKMLLGHMPTIELLRKYHLMQFSEVTKAVSEGNLLLLNEALAKHETFFIRCGIFLILEKLKII
SQ  TYRNLFKKVYLLLKTHQLSLDAFLVALKFMHVEDVDIDEVQCILANLIYMGHIKGYISHQHQKLVVSKQNPFPPLSTVC
//
ID  P40345;
PN  Phospholipid:diacylglycerol acyltransferase;
GN  LRO1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22446555, ECO:0000269|PubMed:22454508, ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}; Single-pass type II membrane protein {ECO:0000269|PubMed:22446555}. Nucleus inner membrane {ECO:0000269|PubMed:31422915}; Single-pass type II membrane protein {ECO:0000255}. Note=Localizes to sites of lipid droplet biogenesis in the endoplasmic reticulum (PubMed:22454508, PubMed:32349126). Relocates from the endoplasmic reticulum to a subdomain of the inner nuclear membrane that associates with the nucleolus upon nutrient starvation (PubMed:31422915). {ECO:0000269|PubMed:22454508, ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}.
DR  UNIPROT: P40345;
DR  UNIPROT: D6W1I3;
DR  Pfam: PF02450;
DE  Function: Catalyzes triacylglycerol (TAG) formation by an acyl-CoA independent pathway. The enzyme specifically transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol (DAG), thus forming an sn-1-lysophospholipid (PubMed:10747858, PubMed:10829075, PubMed:32349126). The preferred acyl donors are phosphatidylethanolamine (PE) and phosphatidylcholine (PC). Also capable of using broad acyl donors such as phosphatidic acid (PA), phosphatidylserine (PS), phosphatidylglycerol (PG) and phosphatidylinositol (PI), as well as monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), and acyl-CoA, and it is more likely to use unsaturated acyl donors. As acyl acceptors, it prefers 1,2- over 1,3-diacylglycerol (DAG). Additionally, has esterification activity that can utilize methanol as acyl acceptor to generate fatty acid methyl esters (FAME) (PubMed:30706417). Can also utilize ceramide instead of DAG, acylating the ceramides by attaching a fatty acid to the hydroxy group on the first carbon atom of the long-chain base to produce 1-O-acylceramides (PubMed:22738231). Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains (PubMed:32349126). Relocates from the endoplasmic reticulum to a subdomain of the inner nuclear membrane upon nutrient starvation, where it provides a site of TAG synthesis, which is coupled with nuclear membrane remodeling (PubMed:31422915). {ECO:0000269|PubMed:10747858, ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:22738231, ECO:0000269|PubMed:30706417, ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}.
DE  Reference Proteome: Yes;
DE  Interaction: P53919; IntAct: EBI-858436; Score: 0.00
DE  Interaction: P25294; IntAct: EBI-3661091; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3672140; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3690189; Score: 0.35
DE  Interaction: Q04675; IntAct: EBI-16281991; Score: 0.35
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005637;
GO  GO:0097038;
GO  GO:0003824;
GO  GO:0008374;
GO  GO:0046027;
GO  GO:0006672;
GO  GO:0006629;
GO  GO:0019915;
GO  GO:0055091;
GO  GO:0019432;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGTLFRRNVQNQKSDSDENNKGGSVHNKRESRNHIHHQQGLGHKRRRGISGSAKRNERGKDFDRKRDGNGRKRWRDSRRL
SQ  IFILGAFLGVLLPFSFGAYHVHNSDSDLFDNFVNFDSLKVYLDDWKDVLPQGISSFIDDIQAGNYSTSSLDDLSENFAVG
SQ  KQLLRDYNIEAKHPVVMVPGVISTGIESWGVIGDDECDSSAHFRKRLWGSFYMLRTMVMDKVCWLKHVMLDPETGLDPPN
SQ  FTLRAAQGFESTDYFIAGYWIWNKVFQNLGVIGYEPNKMTSAAYDWRLAYLDLERRDRYFTKLKEQIELFHQLSGEKVCL
SQ  IGHSMGSQIIFYFMKWVEAEGPLYGNGGRGWVNEHIDSFINAAGTLLGAPKAVPALISGEMKDTIQLNTLAMYGLEKFFS
SQ  RIERVKMLQTWGGIPSMLPKGEEVIWGDMKSSSEDALNNNTDTYGNFIRFERNTSDAFNKNLTMKDAINMTLSISPEWLQ
SQ  RRVHEQYSFGYSKNEEELRKNELHHKHWSNPMEVPLPEAPHMKIYCIYGVNNPTERAYVYKEEDDSSALNLTIDYESKQP
SQ  VFLTEGDGTVPLVAHSMCHKWAQGASPYNPAGINVTIVEMKHQPDRFDIRGGAKSAEHVDILGSAELNDYILKIASGNGD
SQ  LVEPRQLSNLSQWVSQMPFPM
//
ID  Q0VCW8;
PN  Phosducin-like protein 3;
GN  PDCL3;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9H2J4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
DR  UNIPROT: Q0VCW8;
DR  Pfam: PF02114;
DE  Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (By similarity). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity). {ECO:0000250|UniProtKB:Q4KLJ8, ECO:0000250|UniProtKB:Q9H2J4}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0001525;
GO  GO:0006915;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQDPNADTEWNDILRKKGILPSKEDLKDLEKEAEEEEQRILQQSIVKTYEDMTLEELEDNEDEFNEEDERAIEMYRQQRL
SQ  AEWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKFIKAISTTCIPSYP
SQ  DRNLPTVFVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLSESGAIKTSLEENPKKPVEDVLLSAVRCSVPAKRDSDSEDD
//
ID  Q6P268;
PN  Phosducin-like protein 3;
GN  pdcl3;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9H2J4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
DR  UNIPROT: Q6P268;
DR  UNIPROT: Q800E3;
DR  Pfam: PF02114;
DE  Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (PubMed:26059764). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity). {ECO:0000250|UniProtKB:Q4KLJ8, ECO:0000250|UniProtKB:Q9H2J4, ECO:0000269|PubMed:26059764}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0044183;
GO  GO:0043184;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0010628;
GO  GO:0006457;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQDPNADTEWNDILRKKGILPPKETPVEEEEDEQLHLQSQSVVKTYEDMTLEELEENEDEFSEEDEHAMEMYRLKRLAEW
SQ  KANQMKNVFGELKEISGQDYVQEVNKAGEGIWVVLHLYKQGIPLCSLINQHLAQLARKFPQSKFLKSISSTCIPNYPDRN
SQ  LPTLFVYRDGEMKAQFIGPLVFGGMNLTCDELEWRLSESGAVKTDLEENPRKQIQDQLMTSIRCSANTHRDGEEDSDED
//
ID  Q9H2J4;
PN  Phosducin-like protein 3;
GN  PDCL3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15371430, ECO:0000269|PubMed:26059764}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26059764}. Endoplasmic reticulum {ECO:0000269|PubMed:26059764}.
DR  UNIPROT: Q9H2J4;
DR  UNIPROT: B2RA00;
DR  UNIPROT: Q53S68;
DR  PDB: 7NVM;
DR  Pfam: PF02114;
DR  OMIM: 611678;
DR  DisGeNET: 79031;
DE  Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (PubMed:23792958, PubMed:26059764). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (PubMed:17429077). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (PubMed:15371430). {ECO:0000250|UniProtKB:Q4KLJ8, ECO:0000269|PubMed:15371430, ECO:0000269|PubMed:17429077, ECO:0000269|PubMed:23792958, ECO:0000269|PubMed:26059764}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6ZMQ8; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: P80318; IntAct: EBI-2555132; Score: 0.56
DE  Interaction: P80313; IntAct: EBI-2560725; Score: 0.56
DE  Interaction: P80314; IntAct: EBI-2561730; Score: 0.56
DE  Interaction: P80315; IntAct: EBI-11016531; Score: 0.35
DE  Interaction: P42932; IntAct: EBI-11029792; Score: 0.35
DE  Interaction: Q8R5C5; IntAct: EBI-11073047; Score: 0.35
DE  Interaction: P23258; IntAct: EBI-11085623; Score: 0.48
DE  Interaction: P61160; IntAct: EBI-11156891; Score: 0.35
DE  Interaction: Q9NXB0; IntAct: EBI-11377799; Score: 0.27
DE  Interaction: Q9UPM9; IntAct: EBI-11379035; Score: 0.27
DE  Interaction: Q8NBT0; IntAct: EBI-11394140; Score: 0.27
DE  Interaction: Q562R1; IntAct: EBI-21540493; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-21594461; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-21594293; Score: 0.35
DE  Interaction: P57775; IntAct: EBI-21688280; Score: 0.35
DE  Interaction: P42025; IntAct: EBI-21800784; Score: 0.35
DE  Interaction: O00628; IntAct: EBI-21853334; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-16799955; Score: 0.27
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: Q13547; IntAct: EBI-25383649; Score: 0.35
DE  Interaction: Q96LU5; IntAct: EBI-27049466; Score: 0.27
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0097356;
GO  GO:0032991;
GO  GO:0044183;
GO  GO:0043184;
GO  GO:0030036;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0061077;
GO  GO:1903645;
GO  GO:2000059;
GO  GO:0045766;
GO  GO:0001938;
GO  GO:0010628;
GO  GO:0006457;
GO  GO:0050821;
GO  GO:0050730;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQDPNADTEWNDILRKKGILPPKESLKELEEEAEEEQRILQQSVVKTYEDMTLEELEDHEDEFNEEDERAIEMYRRRRLA
SQ  EWKATKLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSGLARKFPDVKFIKAISTTCIPNYPD
SQ  RNLPTIFVYLEGDIKAQFIGPLVFGGMNLTRDELEWKLSESGAIMTDLEENPKKPIEDVLLSSVRRSVLMKRDSDSEGD
//
ID  Q8BVF2;
PN  Phosducin-like protein 3;
GN  Pdcl3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:27496612}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
DR  UNIPROT: Q8BVF2;
DR  UNIPROT: Q3TH06;
DR  UNIPROT: Q99JX2;
DR  UNIPROT: Q9D0W3;
DR  Pfam: PF02114;
DE  Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (PubMed:26059764). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity). {ECO:0000250|UniProtKB:Q4KLJ8, ECO:0000250|UniProtKB:Q9H2J4, ECO:0000269|PubMed:26059764}.
DE  Reference Proteome: Yes;
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: P35279; IntAct: EBI-11566531; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0097356;
GO  GO:0032991;
GO  GO:0044183;
GO  GO:0043184;
GO  GO:0030036;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0034605;
GO  GO:0061077;
GO  GO:1903645;
GO  GO:2000059;
GO  GO:0045766;
GO  GO:0001938;
GO  GO:0010628;
GO  GO:0006457;
GO  GO:0050821;
GO  GO:0050730;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQDPNADTEWNDILRKKGILPPKESLKELEEEEAEKEEQLLQQSVVKTYEDMTLEELEENEDEFSEEDERAIEMYRQQRL
SQ  AEWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCSLINHHLSGLARKFPDVKFIKAISTTCIPNYP
SQ  DRNLPTVFVYREGDIKAQFIGPLVFGGMNLTIDELEWKLSESGAIKTALEENPKKPIQDLLLSSVRGPVPMRRDSDSEDD
//
ID  Q5RB77;
PN  Phosducin-like protein 3;
GN  PDCL3;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9H2J4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
DR  UNIPROT: Q5RB77;
DR  Pfam: PF02114;
DE  Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (By similarity). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity). {ECO:0000250|UniProtKB:Q4KLJ8, ECO:0000250|UniProtKB:Q9H2J4}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0001525;
GO  GO:0006915;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQDPNADTEWNDILRKKGILPPKESLKELEEEAEEEQRILQQSVVKTYEDMTLEELDDHEDEFNEEDERAIEMYRRQRLA
SQ  EWKVTKLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSGLARKFPDVKFIKAISTTCIPNYPD
SQ  RNLPTIFVYLEGDIKAQFIGPLVFGGMNLTRDELEWKLSESGAIMTDLEENPKKPIEDVLLSSVRRSALMKRDSDSEGD
//
ID  Q4KLJ8;
PN  Phosducin-like protein 3;
GN  Pdcl3;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9H2J4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
DR  UNIPROT: Q4KLJ8;
DR  Pfam: PF02114;
DE  Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (By similarity). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (PubMed:27496612). Modulates the activation of caspases during apoptosis (By similarity). {ECO:0000250|UniProtKB:Q9H2J4, ECO:0000269|PubMed:27496612}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0097356;
GO  GO:0032991;
GO  GO:0044183;
GO  GO:0043184;
GO  GO:0030036;
GO  GO:0001525;
GO  GO:0006915;
GO  GO:0034605;
GO  GO:0061077;
GO  GO:1903645;
GO  GO:2000059;
GO  GO:0045766;
GO  GO:0001938;
GO  GO:0010628;
GO  GO:0006457;
GO  GO:0050821;
GO  GO:0050730;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQDPNADTEWNDILRKKGILPPKESLKELEEEEEGKEEQRLQQSVVKTYEDMTLEELQENEDEFSEEDERAIEMYRQQRL
SQ  AEWKATQLRNKFGEVLEISGKDYVQEVTKAGEGLWVVLHLYKQGIPLCSLINHHLSGLARKFPDVKFIKAISTTCIPNYP
SQ  DRNLPTVFVYREGDIKAQFIGPLVFGGMNLTIDELEWKLSESGAIKTELEENPKKAIKDVLLSSVRDPVPMRRDSDSEDD
//
ID  P27815;
PN  cAMP-specific 3',5'-cyclic phosphodiesterase 4A;
GN  PDE4A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15738310}. [Isoform 2]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15738310}. Cell projection, ruffle membrane {ECO:0000269|PubMed:15738310}. [Isoform 3]: Cytoplasm, cytosol {ECO:0000269|PubMed:7888306}. [Isoform 4]: Membrane; Peripheral membrane protein {ECO:0000269|PubMed:9677330}. Note=Isoform 4 has propensity for association with membranes. {ECO:0000269|PubMed:9677330}. [Isoform 6]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11306681, ECO:0000269|PubMed:15738310}. [Isoform 7]: Cytoplasm, cytosol. Membrane; Peripheral membrane protein {ECO:0000269|PubMed:18095939}. Note=Predominantly cytosolic. {ECO:0000269|PubMed:18095939}.
DR  UNIPROT: P27815;
DR  UNIPROT: O75522;
DR  UNIPROT: O76092;
DR  UNIPROT: Q16255;
DR  UNIPROT: Q16691;
DR  UNIPROT: Q5DM53;
DR  UNIPROT: Q6PMT2;
DR  UNIPROT: Q8IVA7;
DR  UNIPROT: Q8WUQ3;
DR  UNIPROT: Q9H3H2;
DR  PDB: 2QYK;
DR  PDB: 3I8V;
DR  PDB: 3TVX;
DR  Pfam: PF18100;
DR  Pfam: PF00233;
DR  PROSITE: PS00126;
DR  PROSITE: PS51845;
DR  OMIM: 600126;
DR  DisGeNET: 5141;
DE  Function: Hydrolyzes the second messenger 3',5'-cyclic AMP (cAMP), which is a key regulator of many important physiological processes. {ECO:0000269|PubMed:11566027, ECO:0000269|PubMed:2160582}. [Isoform 1]: Efficiently hydrolyzes cAMP. {ECO:0000269|PubMed:11306681, ECO:0000269|PubMed:15738310}. [Isoform 2]: Efficiently hydrolyzes cAMP. {ECO:0000269|PubMed:15738310}. [Isoform 3]: Efficiently hydrolyzes cAMP. The phosphodiesterase activity is not affected by calcium, calmodulin or cyclic GMP (cGMP) levels. Does not hydrolyze cGMP. {ECO:0000269|PubMed:7888306}. [Isoform 4]: Efficiently hydrolyzes cAMP. {ECO:0000269|PubMed:9677330}. [Isoform 6]: Efficiently hydrolyzes cAMP. {ECO:0000269|PubMed:11306681, ECO:0000269|PubMed:15738310, ECO:0000269|PubMed:17727341}. [Isoform 7]: Efficiently hydrolyzes cAMP. {ECO:0000269|PubMed:18095939}.
DE  Reference Proteome: Yes;
DE  Interaction: P31016; IntAct: EBI-7970649; Score: 0.44
DE  Interaction: P27987; IntAct: EBI-11069427; Score: 0.35
DE  Interaction: Q9UJX0; IntAct: EBI-24327666; Score: 0.56
DE  Interaction: O14569; IntAct: EBI-24684076; Score: 0.56
DE  Interaction: P16118; IntAct: EBI-24601320; Score: 0.56
DE  Interaction: O75344; IntAct: EBI-21665235; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-20929192; Score: 0.40
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P55212; IntAct: EBI-25834679; Score: 0.56
DE  Interaction: P13473; IntAct: EBI-25872955; Score: 0.56
DE  Interaction: Q9Y371; IntAct: EBI-25921942; Score: 0.56
DE  Interaction: O75400; IntAct: EBI-25923927; Score: 0.56
DE  Interaction: Q13554; IntAct: EBI-28939469; Score: 0.35
DE  Interaction: Q13555; IntAct: EBI-28939534; Score: 0.35
DE  Interaction: Q13557; IntAct: EBI-28939579; Score: 0.35
DE  Interaction: Q9UQM7; IntAct: EBI-28947140; Score: 0.35
GO  GO:0005829;
GO  GO:0019898;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0004115;
GO  GO:0004114;
GO  GO:0030552;
GO  GO:0046872;
GO  GO:0006198;
GO  GO:0071466;
GO  GO:0007186;
GO  GO:0106070;
GO  GO:0010738;
GO  GO:0007608;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:18095939};
SQ  MEPPTVPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERAERERQPHRPIERADAMDTSDRPGLR
SQ  TTRMSWPSSFHGTGTGSGGAGGGSSRRFEAENGPTPSPGRSPLDSQASPGLVLHAGAATSQRRESFLYRSDSDYDMSPKT
SQ  MSRNSSVTSEAHAEDLIVTPFAQVLASLRSVRSNFSLLTNVPVPSNKRSPLGGPTPVCKATLSEETCQQLARETLEELDW
SQ  CLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISTTFLDKQNEVEIPSPTMKEREKQQAPRPRPSQ
SQ  PPPPPVPHLQPMSQITGLKKLMHSNSLNNSNIPRFGVKTDQEELLAQELENLNKWGLNIFCVSDYAGGRSLTCIMYMIFQ
SQ  ERDLLKKFRIPVDTMVTYMLTLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGV
SQ  SNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLSKRQRQSLRKMVIDMVLATDMSKHMTLLADLKTMV
SQ  ETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLELYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEK
SQ  SQVGFIDYIVHPLWETWADLVHPDAQEILDTLEDNRDWYYSAIRQSPSPPPEEESRGPGHPPLPDKFQFELTLEEEEEEE
SQ  ISMAQIPCTAQEALTAQGLSGVEEALDATIAWEASPAQESLEVMAQEASLEAELEAVYLTQQAQSTGSAPVAPDEFSSRE
SQ  EFVVAVSHSSPSALALQSPLLPAWRTLSVSEHAPGLPGLPSTAAEVEAQREHQAAKRACSACAGTFGEDTSALPAPGGGG
SQ  SGGDPT
//
ID  O76083;
PN  High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A;
GN  PDE9A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform PDE9A1]: Cell projection, ruffle membrane {ECO:0000269|PubMed:17090334}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17090334}. Golgi apparatus {ECO:0000269|PubMed:17090334}. Endoplasmic reticulum {ECO:0000269|PubMed:17090334}. Cell membrane, sarcolemma {ECO:0000269|PubMed:25799991}. [Isoform PDE9A2]: Cell projection, ruffle membrane {ECO:0000269|PubMed:17090334}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17090334}. [Isoform PDE9A3]: Cytoplasm {ECO:0000269|PubMed:17090334}. Endoplasmic reticulum {ECO:0000269|PubMed:17090334}. [Isoform PDE9A17]: Cytoplasm {ECO:0000269|PubMed:17090334}. Endoplasmic reticulum {ECO:0000269|PubMed:17090334}.
DR  UNIPROT: O76083;
DR  UNIPROT: B2RBI5;
DR  UNIPROT: B4DFI5;
DR  UNIPROT: D3DSJ8;
DR  UNIPROT: D3DSJ9;
DR  UNIPROT: O75490;
DR  UNIPROT: O75491;
DR  UNIPROT: O95225;
DR  UNIPROT: Q53Y40;
DR  UNIPROT: Q5QD39;
DR  UNIPROT: Q86SF7;
DR  UNIPROT: Q86SI6;
DR  UNIPROT: Q86SJ3;
DR  UNIPROT: Q86WN3;
DR  UNIPROT: Q86WN4;
DR  UNIPROT: Q86WN5;
DR  UNIPROT: Q86WN6;
DR  UNIPROT: Q86WN7;
DR  UNIPROT: Q86WN8;
DR  UNIPROT: Q86WN9;
DR  UNIPROT: Q86WP0;
DR  PDB: 2HD1;
DR  PDB: 2YY2;
DR  PDB: 3DY8;
DR  PDB: 3DYL;
DR  PDB: 3DYN;
DR  PDB: 3DYQ;
DR  PDB: 3DYS;
DR  PDB: 3JSI;
DR  PDB: 3JSW;
DR  PDB: 3K3E;
DR  PDB: 3K3H;
DR  PDB: 3N3Z;
DR  PDB: 3QI3;
DR  PDB: 3QI4;
DR  PDB: 4E90;
DR  PDB: 4G2J;
DR  PDB: 4G2L;
DR  PDB: 4GH6;
DR  PDB: 4Y86;
DR  PDB: 4Y87;
DR  PDB: 4Y8C;
DR  PDB: 6A3N;
DR  PDB: 6LZZ;
DR  PDB: 7F0I;
DR  Pfam: PF00233;
DR  PROSITE: PS00126;
DR  PROSITE: PS51845;
DR  OMIM: 602973;
DR  DisGeNET: 5152;
DE  Function: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP (PubMed:9624146, PubMed:18757755, PubMed:21483814). Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart (PubMed:25799991). Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory (By similarity). {ECO:0000250|UniProtKB:Q8QZV1, ECO:0000269|PubMed:18757755, ECO:0000269|PubMed:21483814, ECO:0000269|PubMed:25799991, ECO:0000269|PubMed:9624146, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13049; IntAct: EBI-753319; Score: 0.88
DE  Interaction: Q96FC7; IntAct: EBI-10285664; Score: 0.56
DE  Interaction: O76083; IntAct: EBI-16433405; Score: 0.56
DE  Interaction: Q8NAJ2; IntAct: EBI-10173127; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-10190681; Score: 0.56
DE  Interaction: Q7Z3S9; IntAct: EBI-10190711; Score: 0.67
DE  Interaction: Q9BYQ4; IntAct: EBI-10190721; Score: 0.56
DE  Interaction: Q9BYR5; IntAct: EBI-10190731; Score: 0.56
DE  Interaction: O95817; IntAct: EBI-10192173; Score: 0.56
DE  Interaction: P25791; IntAct: EBI-10202658; Score: 0.56
DE  Interaction: P49759; IntAct: EBI-10211130; Score: 0.56
DE  Interaction: P49888; IntAct: EBI-10211543; Score: 0.56
DE  Interaction: Q14657; IntAct: EBI-10233665; Score: 0.56
DE  Interaction: Q49AN0; IntAct: EBI-10241753; Score: 0.56
DE  Interaction: Q9BRA0; IntAct: EBI-10296698; Score: 0.56
DE  Interaction: Q9BRU9; IntAct: EBI-10297143; Score: 0.56
DE  Interaction: Q9H8Y8; IntAct: EBI-10309418; Score: 0.67
DE  Interaction: Q9Y260; IntAct: EBI-10325620; Score: 0.56
DE  Interaction: P25377; IntAct: EBI-11524546; Score: 0.56
DE  Interaction: P32502; IntAct: EBI-11525726; Score: 0.56
DE  Interaction: P38744; IntAct: EBI-11529381; Score: 0.56
DE  Interaction: P39518; IntAct: EBI-11529837; Score: 0.56
DE  Interaction: P40454; IntAct: EBI-11530904; Score: 0.56
DE  Interaction: Q00618; IntAct: EBI-11534143; Score: 0.56
DE  Interaction: Q12259; IntAct: EBI-11536954; Score: 0.56
DE  Interaction: O00560; IntAct: EBI-24276653; Score: 0.56
DE  Interaction: P61964; IntAct: EBI-24286856; Score: 0.56
DE  Interaction: O15205; IntAct: EBI-24291537; Score: 0.56
DE  Interaction: P26371; IntAct: EBI-24298959; Score: 0.56
DE  Interaction: Q99633; IntAct: EBI-24316761; Score: 0.56
DE  Interaction: Q16649; IntAct: EBI-24491918; Score: 0.56
DE  Interaction: Q15051; IntAct: EBI-24524430; Score: 0.56
DE  Interaction: P59991; IntAct: EBI-24372163; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-24378365; Score: 0.56
DE  Interaction: P60411; IntAct: EBI-24407802; Score: 0.56
DE  Interaction: Q63ZY3; IntAct: EBI-24409161; Score: 0.56
DE  Interaction: P60328; IntAct: EBI-25262737; Score: 0.56
DE  Interaction: Q07627; IntAct: EBI-24418030; Score: 0.56
DE  Interaction: Q8IUG1; IntAct: EBI-24436343; Score: 0.56
DE  Interaction: O76011; IntAct: EBI-24437958; Score: 0.56
DE  Interaction: Q16543; IntAct: EBI-24460241; Score: 0.56
DE  Interaction: P60409; IntAct: EBI-24468187; Score: 0.56
DE  Interaction: Q96DX4; IntAct: EBI-11903808; Score: 0.00
DE  Interaction: Q8TAD7; IntAct: EBI-11903800; Score: 0.00
DE  Interaction: Q7Z494; IntAct: EBI-11903789; Score: 0.00
DE  Interaction: Q13237; IntAct: EBI-11903780; Score: 0.00
DE  Interaction: Q13432; IntAct: EBI-21558921; Score: 0.35
DE  Interaction: P51114; IntAct: EBI-26510978; Score: 0.37
DE  Interaction: P51116; IntAct: EBI-26512056; Score: 0.37
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005654;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0047555;
GO  GO:0004114;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0046069;
GO  GO:0046068;
GO  GO:0019934;
GO  GO:0010613;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRP
SQ  VAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQV
SQ  AEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDV
SQ  PTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCV
SQ  AQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNI
SQ  FSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCL
SQ  LEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAM
SQ  KELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
//
ID  O70628;
PN  High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A;
GN  Pde9a;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O76083}. Golgi apparatus {ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O76083}.
DR  UNIPROT: O70628;
DR  Pfam: PF00233;
DR  PROSITE: PS00126;
DR  PROSITE: PS51845;
DE  Function: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes (PubMed:9624145). Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide- dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide- dependent cGMP in heart (PubMed:25799991). Additional experiments are required to confirm whether its ability to hydrolyze natriuretic- peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory (PubMed:22328573, PubMed:24746365). {ECO:0000269|PubMed:22328573, ECO:0000269|PubMed:24746365, ECO:0000269|PubMed:25799991, ECO:0000269|PubMed:9624145, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005654;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0047555;
GO  GO:0004114;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0046069;
GO  GO:0046068;
GO  GO:0019934;
GO  GO:0010613;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGAGSSSYRPKAIYLDIDGRIQKVVFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRP
SQ  VAVKQVSEREELIQGVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARNSRTN
SQ  CPCKYSFLDNKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPITLRRWLLC
SQ  VHDNYRNNPFHNFRHCFCVTQMMYSMVWLCGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPL
SQ  ENHHCAIAFQILARPECNIFASVPPEGFRQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHLTLLKMILIKCC
SQ  DISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPVVEETMLR
SQ  PLWESREHYEELKQLDDAMKELQKKTESLTSGAPENTTEKNRDAKDSEGHSPPN
//
ID  H2QL32;
PN  High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A;
GN  PDE9A;
OS  9598;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O76083}. Golgi apparatus {ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O76083}.
DR  UNIPROT: H2QL32;
DR  UNIPROT: K7AGW3;
DR  PDB: 4QGE;
DR  Pfam: PF00233;
DR  PROSITE: PS00126;
DR  PROSITE: PS51845;
DE  Function: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein. In brain, involved in cognitive function, such as learning and long-term memory. {ECO:0000250|UniProtKB:O76083, ECO:0000250|UniProtKB:Q8QZV1}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0047555;
GO  GO:0004114;
GO  GO:0046872;
GO  GO:0046069;
GO  GO:0046068;
GO  GO:0019934;
GO  GO:0010613;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRP
SQ  VAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCCQEGQRIPPEREELIQSVLAQV
SQ  AEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDV
SQ  PTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCV
SQ  AQMMYSMVWLCSLQENFSQMDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNI
SQ  FSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCL
SQ  LEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAM
SQ  KELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
//
ID  Q8QZV1;
PN  High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A;
GN  Pde9a;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O76083}. Golgi apparatus {ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O76083}.
DR  UNIPROT: Q8QZV1;
DR  UNIPROT: F1LRG6;
DR  Pfam: PF00233;
DR  PROSITE: PS00126;
DR  PROSITE: PS51845;
DE  Function: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (By similarity). In brain, involved in cognitive function, such as learning and long-term memory (PubMed:18674549, PubMed:22070409, PubMed:22328573). {ECO:0000250|UniProtKB:O76083, ECO:0000269|PubMed:18674549, ECO:0000269|PubMed:22070409, ECO:0000269|PubMed:22328573}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005654;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0032587;
GO  GO:0042383;
GO  GO:0047555;
GO  GO:0004114;
GO  GO:0046872;
GO  GO:0046069;
GO  GO:0046068;
GO  GO:0019934;
GO  GO:0010613;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGAGSSSYRPKAIYLDIDGRIQKVVFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRP
SQ  VAVKQVSEREELVQGVLAQVAEQFSRAFKINELKAEVANHLAMLEKRVELEGLKVVEIEKCKSDIKKMREELAARNNRTN
SQ  CPCKYSFLDNKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPITLRRWLLC
SQ  VHDNYRSNPFHNFRHCFCVTQMMYSMVWLCGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPL
SQ  ENHHCAIAFQILARPECNIFASVPPEGFRQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHLTLLKMILIKCC
SQ  DISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPIVEETMLR
SQ  PLWESREHYEELKQLDDAMKELQKKTENLTSGATENAPEKTRDAKDNEDRSPPN
//
ID  Q3T005;
PN  PDZ and LIM domain protein 4;
GN  PDLIM4;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P36202}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P36202}. Early endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Recycling endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Nucleus {ECO:0000250|UniProtKB:P50479}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50479}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P50479}. Synapse, synaptosome {ECO:0000250|UniProtKB:P36202}. Note=Localizes to actin stress fibers in nonmuscle cells. Colocalizes with GRIA1 in early endosomes. Enriched in numerous but not all spine-like structures along dendritic branches. Colocalizes with actin and enriched at sites containing larger amounts of actin and alpha-actinin. Targeted efficiently to spines via its PDZ domain-mediated interaction with the alpha-actinin/actin cytoskeletal complex. Localizes to synaptosomes in brain (By similarity). Colocalizes with F-actin. Colocalizes with TRIP6 at cell-cell contacts and lamellipodia. In the cytoplasm, displays a fibrillar pattern with characteristic thick fibers and occasional clusters. Colocalizes with the actin stress fibers. Oxidative stress induces redistribution from cytoskeleton to cytosol. Colocalizes with SRC at the perinuclear region, but not at focal adhesions (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
DR  UNIPROT: Q3T005;
DR  Pfam: PF15936;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DE  Function: Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle. Involved in reorganization of the actin cytoskeleton (By similarity). In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers. Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1- containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
DE  Reference Proteome: Yes;
GO  GO:0005912;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0043197;
GO  GO:0031905;
GO  GO:0031901;
GO  GO:0031941;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045211;
GO  GO:0034777;
GO  GO:0055038;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0051393;
GO  GO:0046872;
GO  GO:0051371;
GO  GO:0042803;
GO  GO:0019903;
GO  GO:0030036;
GO  GO:0031532;
GO  GO:0098976;
GO  GO:0007507;
GO  GO:0061061;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P36202};
SQ  MPHSVTLRGPSPWGFRLVGGRDFSVPLTISRVHAGSKAALAALCPGDLIQAINGESTELMTHLEAQNRIKGCRDHLTLSV
SQ  SRPEGRSWPSTPEDNKAQAHRIHIDSEAQDGSPLTSRRPSATGLGPEDGRPGLGSPYGQSPRLPVPHNGSNSEATLLAQM
SQ  GALHVSPPHSTDPARGLPRSRDCGVDLGSEVYRMLREPAEPAAAEPKQSGSFRYLQGMLEAGEGGERPGPGGPRNLKPTA
SQ  SKLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCESHAKARVKPPEGYDVV
SQ  AVYPNAKVELV
//
ID  Q9PW72;
PN  PDZ and LIM domain protein 4;
GN  PDLIM4;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P36202}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P36202}. Early endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Recycling endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Nucleus {ECO:0000250|UniProtKB:P50479}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50479}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P50479}. Synapse, synaptosome {ECO:0000250|UniProtKB:P36202}. Note=Localizes to actin stress fibers in nonmuscle cells. Colocalizes with GRIA1 in early endosomes. Enriched in numerous but not all spine-like structures along dendritic branches. Colocalizes with actin and enriched at sites containing larger amounts of actin and alpha-actinin. Targeted efficiently to spines via its PDZ domain-mediated interaction with the alpha-actinin/actin cytoskeletal complex. Localizes to synaptosomes in brain (By similarity). Colocalizes with F-actin. Colocalizes with TRIP6 at cell-cell contacts and lamellipodia. In the cytoplasm, displays a fibrillar pattern with characteristic thick fibers and occasional clusters. Colocalizes with the actin stress fibers. Oxidative stress induces redistribution from cytoskeleton to cytosol. Colocalizes with SRC at the perinuclear region, but not at focal adhesions (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
DR  UNIPROT: Q9PW72;
DR  Pfam: PF15936;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DE  Function: Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle. Involved in reorganization of the actin cytoskeleton (By similarity). In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers. Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1- containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
DE  Reference Proteome: Yes;
GO  GO:0005912;
GO  GO:0005737;
GO  GO:0043197;
GO  GO:0031905;
GO  GO:0031901;
GO  GO:0031941;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045211;
GO  GO:0034777;
GO  GO:0055038;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0046872;
GO  GO:0051371;
GO  GO:0030036;
GO  GO:0098976;
GO  GO:0007507;
GO  GO:0060173;
GO  GO:0061061;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P36202};
SQ  MPHSVALRGPSPWGFRLVGGKDFSTPLTISRINPGSKAALANLCPGDIILAINGESTEAMTHLEAQNKIKACVEQLLLSV
SQ  SRAEERSWSPPILEDGKAQAYRINIEPEPQDNGPAVGKRPMPHAAGGSPVDSRPALSLQHPQPSRPHASSSADAALPLQL
SQ  SGLHISPSQSTDPLKSLPRNRNGIDVESDVYKMLQDYERPASEPKQSGSFRYLQGMLEAGENGEKLDRLSNPRSIKPAGP
SQ  KLGAAMSGLQMLPECTRCGNGIVGTIVKARDKLYHPECFMCDDCGLNLKQRGYFFIEEQLYCETHAKERVKPPEGYDVVA
SQ  VYPNAKVELV
//
ID  P50479;
PN  PDZ and LIM domain protein 4;
GN  PDLIM4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21636573}. Nucleus {ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:21636573}. Cytoplasm {ECO:0000269|PubMed:21636573}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19307596}. Cell projection, lamellipodium {ECO:0000269|PubMed:10826496}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P36202}. Early endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Recycling endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Synapse, synaptosome {ECO:0000250|UniProtKB:P36202}. Note=Localizes to actin stress fibers in nonmuscle cells. Colocalizes with GRIA1 in early endosomes. Enriched in numerous but not all spine-like structures along dendritic branches. Colocalizes with actin and enriched at sites containing larger amounts of actin and alpha-actinin. Targeted efficiently to spines via its PDZ domain-mediated interaction with the alpha-actinin/actin cytoskeletal complex. Localizes to synaptosomes in brain (By similarity). Colocalizes with F-actin (PubMed:10826496). Colocalizes with TRIP6 at cell-cell contacts and lamellipodia (PubMed:10826496). In the cytoplasm, displays a fibrillar pattern with characteristic thick fibers and occasional clusters. Colocalizes with the actin stress fibers. Oxidative stress induces redistribution from cytoskeleton to cytosol (PubMed:21636573). Colocalizes with SRC at the perinuclear region, but not at focal adhesions (PubMed:19307596). {ECO:0000250|UniProtKB:P36202, ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:21636573}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:21636573}. Note=Stains more diffusely in the cytoplasm with thin fibers forming a dense mesh-like pattern. {ECO:0000269|PubMed:21636573}.
DR  UNIPROT: P50479;
DR  UNIPROT: B2R8U1;
DR  UNIPROT: Q53Y39;
DR  UNIPROT: Q96AT8;
DR  UNIPROT: Q9BTW8;
DR  UNIPROT: Q9Y292;
DR  PDB: 2EEG;
DR  PDB: 2V1W;
DR  PDB: 4Q2O;
DR  Pfam: PF15936;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DR  OMIM: 603422;
DR  DisGeNET: 8572;
DE  Function: [Isoform 1]: Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle (PubMed:19307596). Involved in reorganization of the actin cytoskeleton (PubMed:21636573). In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers. Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1- containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:21636573}. [Isoform 2]: Involved in reorganization of the actin cytoskeleton and in regulation of cell migration. In response to oxidative stress, binds to NQO1, which stabilizes it and protects it from ubiquitin-independent degradation by the core 20S proteasome. Stabilized protein is able to heterodimerize with isoform 1 changing the subcellular location of it from cytoskeleton and nuclei to cytosol, leading to loss of isoforms 1 ability to induce formation of actin stress fibers. Counteracts the effects produced by isoform 1 on organization of actin cytoskeleton and cell motility to fine-tune actin cytoskeleton rearrangement and to attenuate cell migration. {ECO:0000269|PubMed:21636573}.
DE  Reference Proteome: Yes;
DE  Interaction: P03246; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9H9D4; IntAct: EBI-374211; Score: 0.00
DE  Interaction: Q93062; IntAct: EBI-753946; Score: 0.37
DE  Interaction: P01106; IntAct: EBI-3962281; Score: 0.35
DE  Interaction: Q12923; IntAct: EBI-7288509; Score: 0.35
DE  Interaction: Q15654; IntAct: EBI-7288509; Score: 0.35
DE  Interaction: Q9Z1Y4; IntAct: EBI-7288509; Score: 0.35
DE  Interaction: Q64512; IntAct: EBI-8166794; Score: 0.44
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: P0CK58; IntAct: EBI-11732874; Score: 0.35
DE  Interaction: P30119; IntAct: EBI-11733103; Score: 0.35
DE  Interaction: Q2MG95; IntAct: EBI-11733653; Score: 0.35
DE  Interaction: Q69117; IntAct: EBI-11733954; Score: 0.35
DE  Interaction: P12814; IntAct: EBI-22746497; Score: 0.56
DE  Interaction: P48728; IntAct: EBI-24547082; Score: 0.56
DE  Interaction: O00560; IntAct: EBI-24538434; Score: 0.56
DE  Interaction: Q8WU58; IntAct: EBI-24759935; Score: 0.56
DE  Interaction: P06932; IntAct: EBI-26504756; Score: 0.37
DE  Interaction: P06465; IntAct: EBI-26504437; Score: 0.37
DE  Interaction: P36817; IntAct: EBI-26505368; Score: 0.37
DE  Interaction: P06430; IntAct: EBI-26505254; Score: 0.37
DE  Interaction: P06788; IntAct: EBI-26505830; Score: 0.49
DE  Interaction: P03129; IntAct: EBI-26505753; Score: 0.49
DE  Interaction: P36827; IntAct: EBI-26506230; Score: 0.37
DE  Interaction: P24837; IntAct: EBI-26506651; Score: 0.37
DE  Interaction: P06429; IntAct: EBI-26506472; Score: 0.37
DE  Interaction: P43630; IntAct: EBI-21561965; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-27084109; Score: 0.35
GO  GO:0005912;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0043197;
GO  GO:0031905;
GO  GO:0031901;
GO  GO:0031941;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045211;
GO  GO:0034777;
GO  GO:0055038;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0051393;
GO  GO:0046872;
GO  GO:0051371;
GO  GO:0042803;
GO  GO:0019903;
GO  GO:0030036;
GO  GO:0031532;
GO  GO:0098976;
GO  GO:0007507;
GO  GO:0061061;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P36202};
SQ  MPHSVTLRGPSPWGFRLVGGRDFSAPLTISRVHAGSKAALAALCPGDLIQAINGESTELMTHLEAQNRIKGCHDHLTLSV
SQ  SRPEGRSWPSAPDDSKAQAHRIHIDPEIQDGSPTTSRRPSGTGTGPEDGRPSLGSPYGQPPRFPVPHNGSSEATLPAQMS
SQ  TLHVSPPPSADPARGLPRSRDCRVDLGSEVYRMLREPAEPVAAEPKQSGSFRYLQGMLEAGEGGDWPGPGGPRNLKPTAS
SQ  KLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCESHAKARVKPPEGYDVVA
SQ  VYPNAKVELV
//
ID  P70271;
PN  PDZ and LIM domain protein 4;
GN  Pdlim4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P36202}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P36202}. Early endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Recycling endosome membrane {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Nucleus {ECO:0000250|UniProtKB:P50479}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50479}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P50479}. Synapse, synaptosome {ECO:0000250|UniProtKB:P36202}. Note=Localizes to actin stress fibers in nonmuscle cells. Colocalizes with GRIA1 in early endosomes. Enriched in numerous but not all spine-like structures along dendritic branches. Colocalizes with actin and enriched at sites containing larger amounts of actin and alpha-actinin. Targeted efficiently to spines via its PDZ domain-mediated interaction with the alpha-actinin/actin cytoskeletal complex. Localizes to synaptosomes in brain (By similarity). Colocalizes with F-actin. Colocalizes with TRIP6 at cell-cell contacts and lamellipodia. In the cytoplasm, displays a fibrillar pattern with characteristic thick fibers and occasional clusters. Colocalizes with the actin stress fibers. Oxidative stress induces redistribution from cytoskeleton to cytosol. Colocalizes with SRC at the perinuclear region, but not at focal adhesions (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
DR  UNIPROT: P70271;
DR  UNIPROT: Q5SWV2;
DR  UNIPROT: Q8K0W4;
DR  Pfam: PF15936;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DE  Function: Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle. Involved in reorganization of the actin cytoskeleton (By similarity). In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers. Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1- containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (By similarity). {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
DE  Reference Proteome: Yes;
DE  Interaction: Q15654; IntAct: EBI-7288337; Score: 0.37
DE  Interaction: Q9Z1Y4; IntAct: EBI-7288409; Score: 0.50
DE  Interaction: P15806; IntAct: EBI-26677548; Score: 0.37
DE  Interaction: Q07279; IntAct: EBI-26677540; Score: 0.37
DE  Interaction: Q8CDC7; IntAct: EBI-26678400; Score: 0.37
DE  Interaction: Q9D032; IntAct: EBI-26682455; Score: 0.37
GO  GO:0015629;
GO  GO:0005912;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0043197;
GO  GO:0031905;
GO  GO:0031901;
GO  GO:0031941;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045211;
GO  GO:0034777;
GO  GO:0055038;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0042805;
GO  GO:0051393;
GO  GO:0046872;
GO  GO:0051371;
GO  GO:0042803;
GO  GO:0019903;
GO  GO:0030036;
GO  GO:0031532;
GO  GO:0098976;
GO  GO:0007507;
GO  GO:0061061;
GO  GO:0051496;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P36202};
SQ  MTHSVTLRGPSPWGFRLVGGRDFSAPLTISRVHAGSKAALAALCPGDLIQAINGESTELMTHLEAQNRIKGCHDHLTLSV
SQ  SRPENKNWPSAPDDKAQAHRIHIDPESQDCSPATSRRSSVSGISLEDNRSGLGSPYGQPPRLPVPHNGSSNEATLPAQMS
SQ  ALHVSPPTSADTARVLPRNRDCRVDLGSEVYRMLREPAEPTASEPKQSGSFRYLQGMLEAGEGGDRPGSGGPRNLKPAAS
SQ  KLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCENHAKARVKPPEGYDVVA
SQ  VYPNAKVELV
//
ID  P36202;
PN  PDZ and LIM domain protein 4;
GN  Pdlim4;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14729062, ECO:0000269|PubMed:15456832, ECO:0000269|PubMed:22659164}. Cell projection, dendritic spine {ECO:0000269|PubMed:15456832}. Early endosome membrane {ECO:0000269|PubMed:15456832}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Recycling endosome membrane {ECO:0000269|PubMed:15456832}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:P50479}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50479}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P50479}. Synapse, synaptosome {ECO:0000269|PubMed:15456832}. Note=Localizes to actin stress fibers in nonmuscle cells (PubMed:14729062, PubMed:22659164). Colocalizes with GRIA1 in early endosomes. Enriched in numerous but not all spine-like structures along dendritic branches. Colocalizes with actin and enriched at sites containing larger amounts of actin and alpha-actinin. Targeted efficiently to spines via its PDZ domain-mediated interaction with the alpha-actinin/actin cytoskeletal complex. Localizes to synaptosomes in brain (PubMed:15456832). Colocalizes with F-actin. Colocalizes with TRIP6 at cell-cell contacts and lamellipodia. In the cytoplasm, displays a fibrillar pattern with characteristic thick fibers and occasional clusters. Colocalizes with the actin stress fibers. Oxidative stress induces redistribution from cytoskeleton to cytosol. Colocalizes with SRC at the perinuclear region, but not at focal adhesions (By similarity). {ECO:0000250|UniProtKB:P50479, ECO:0000269|PubMed:14729062, ECO:0000269|PubMed:15456832, ECO:0000269|PubMed:22659164}.
DR  UNIPROT: P36202;
DR  Pfam: PF15936;
DR  Pfam: PF00412;
DR  Pfam: PF00595;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS50106;
DE  Function: Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle (By similarity). Involved in reorganization of the actin cytoskeleton. In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers (PubMed:14729062, PubMed:22659164). Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1-containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (PubMed:15456832). {ECO:0000250|UniProtKB:P50479, ECO:0000269|PubMed:14729062, ECO:0000269|PubMed:15456832, ECO:0000269|PubMed:22659164}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q969Q1; IntAct: EBI-21997483; Score: 0.35
GO  GO:0015629;
GO  GO:0005912;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0043197;
GO  GO:0031905;
GO  GO:0031901;
GO  GO:0031941;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045211;
GO  GO:0034777;
GO  GO:0055038;
GO  GO:0001725;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0042805;
GO  GO:0051393;
GO  GO:0046872;
GO  GO:0051371;
GO  GO:0042803;
GO  GO:0019903;
GO  GO:0030036;
GO  GO:0031532;
GO  GO:0098976;
GO  GO:0007507;
GO  GO:0061061;
GO  GO:0051496;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MTHAVTLRGPSPWGFRLVGGRDFSAPLTISRVHAGSKAALAALCPGDSIQAINGESTELMTHLEAQNRIKGCHDHLTLSV
SQ  SRPENKNWPSSPNDKAQAHRIHIDPEAQDGSPATSRRSSISGISLEDNRSGLGSPYGQPPRLPVPHNGSSNEVTLPSQMS
SQ  ALHVSPPPSADTPRILPRNRDCRVDLGSEVYRMLREPAEPAASEPKQSGSFRYLQGMLEAGEGGDRPGSGGSRNLKPAAS
SQ  KLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCENHAKARVKPPEGYDVVA
SQ  VYPNAKVELV
//
ID  O15055;
PN  Period circadian protein homolog 2;
GN  PER2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform 1]: Nucleus {ECO:0000269|PubMed:22274616}. Cytoplasm {ECO:0000250|UniProtKB:O54943}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54943}. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. PML regulates its nuclear localization. {ECO:0000250|UniProtKB:O54943}. [Isoform 2]: Nucleus, nucleolus {ECO:0000269|PubMed:24202686}.
DR  UNIPROT: O15055;
DR  UNIPROT: A2I2P7;
DR  UNIPROT: Q4ZG49;
DR  UNIPROT: Q6DT41;
DR  UNIPROT: Q9UQ45;
DR  PDB: 6OF7;
DR  Pfam: PF08447;
DR  Pfam: PF12114;
DR  PROSITE: PS50112;
DR  OMIM: 603426;
DR  OMIM: 604348;
DR  DisGeNET: 8864;
DE  Function: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock- controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK- ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK- ARTNL/BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like ARNTL or G6PC1. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby inhibiting transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000250|UniProtKB:O54943}.
DE  Disease: Advanced sleep phase syndrome, familial, 1 (FASPS1) [MIM:604348]: A disorder characterized by very early sleep onset and offset. Individuals are 'morning larks' with a 4 hours advance of the sleep, temperature and melatonin rhythms. {ECO:0000269|PubMed:11232563}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q92956; IntAct: EBI-1084363; Score: 0.00
DE  Interaction: P49674; IntAct: EBI-1187581; Score: 0.81
DE  Interaction: Q9JMK2; IntAct: EBI-2558429; Score: 0.40
DE  Interaction: P11441; IntAct: EBI-24310618; Score: 0.56
DE  Interaction: P61968; IntAct: EBI-24316651; Score: 0.56
DE  Interaction: Q14241; IntAct: EBI-25247254; Score: 0.56
DE  Interaction: P40692; IntAct: EBI-24486259; Score: 0.56
DE  Interaction: Q96PV6; IntAct: EBI-24508105; Score: 0.56
DE  Interaction: J3QSH9; IntAct: EBI-24381697; Score: 0.56
DE  Interaction: P48730; IntAct: EBI-24428236; Score: 0.68
DE  Interaction: P29590; IntAct: EBI-21986094; Score: 0.46
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000976;
GO  GO:0003713;
GO  GO:0001222;
GO  GO:0032922;
GO  GO:0097167;
GO  GO:0007623;
GO  GO:0043153;
GO  GO:0006631;
GO  GO:0006094;
GO  GO:0005978;
GO  GO:0070932;
GO  GO:0019249;
GO  GO:0042754;
GO  GO:0045892;
GO  GO:0070345;
GO  GO:0031397;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0120162;
GO  GO:0051726;
GO  GO:0042752;
GO  GO:0051946;
GO  GO:0050796;
GO  GO:0050767;
GO  GO:0019229;
GO  GO:0002931;
GO  GO:0050872;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNGYAEFPPSPSNPTKEPVEPQPSQVPLQEDVDMSSGSSGHETNENCSTGRDSQGSDCDDSGKELGMLVEPPDARQSPDT
SQ  FSLMMAKSEHNPSTSGCSSDQSSKVDTHKELIKTLKELKVHLPADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMS
SQ  SEGHPCGADVPSYTVEEMESVTSEHIVKNADMFAVAVSLVSGKILYISDQVASIFHCKRDAFSDAKFVEFLAPHDVGVFH
SQ  SFTSPYKLPLWSMCSGADSFTQECMEEKSFFCRVSVRKSHENEIRYHPFRMTPYLVKVRDQQGAESQLCCLLLAERVHSG
SQ  YEAPRIPPEKRIFTTTHTPNCLFQDVDERAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQSGGQPFDYSPIRF
SQ  RARNGEYITLDTSWSSFINPWSRKISFIIGRHKVRVGPLNEDVFAAHPCTEEKALHPSIQELTEQIHRLLLQPVPHSGSS
SQ  GYGSLGSNGSHEHLMSQTSSSDSNGHEDSRRRRAEICKNGNKTKNRSHYSHESGEQKKKSVTEMQTNPPAEKKAVPAMEK
SQ  DSLGVSFPEELACKNQPTCSYQQISCLDSVIRYLESCNEAATLKRKCEFPANVPALRSSDKRKATVSPGPHAGEAEPPSR
SQ  VNSRTGVGTHLTSLALPGKAESVASLTSQCSYSSTIVHVGDKKPQPELEMVEDAASGPESLDCLAGPALACGLSQEKEPF
SQ  KKLGLTKEVLAAHTQKEEQSFLQKFKEIRKLSIFQSHCHYYLQERSKGQPSERTAPGLRNTSGIDSPWKKTGKNRKLKSK
SQ  RVKPRDSSESTGSGGPVSARPPLVGLNATAWSPSDTSQSSCPAVPFPAPVPAAYSLPVFPAPGTVAAPPAPPHASFTVPA
SQ  VPVDLQHQFAVQPPPFPAPLAPVMAFMLPSYSFPSGTPNLPQAFFPSQPQFPSHPTLTSEMASASQPEFPSRTSIPRQPC
SQ  ACPATRATPPSAMGRASPPLFQSRSSSPLQLNLLQLEEAPEGGTGAMGTTGATETAAVGADCKPGTSRDQQPKAPLTRDE
SQ  PSDTQNSDALSTSSGLLNLLLNEDLCSASGSAASESLGSGSLGCDASPSGAGSSDTSHTSKYFGSIDSSENNHKAKMNTG
SQ  MEESEHFIKCVLQDPIWLLMADADSSVMMTYQLPSRNLEAVLKEDREKLKLLQKLQPRFTESQKQELREVHQWMQTGGLP
SQ  AAIDVAECVYCENKEKGNICIPYEEDIPSLGLSEVSDTKEDENGSPLNHRIEEQT
//
ID  O54943;
PN  Period circadian protein homolog 2;
GN  Per2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:11889036, ECO:0000269|PubMed:22208286}. Cytoplasm {ECO:0000269|PubMed:11889036, ECO:0000269|PubMed:22208286}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22274616}. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. PML regulates its nuclear localization (PubMed:22274616). {ECO:0000269|PubMed:22274616}.
DR  UNIPROT: O54943;
DR  UNIPROT: O54954;
DR  PDB: 3GDI;
DR  PDB: 4CT0;
DR  PDB: 4U8H;
DR  Pfam: PF08447;
DR  Pfam: PF12114;
DR  PROSITE: PS50112;
DE  Function: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock- controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK- ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK- ARTNL/BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like ARNTL or G6PC1. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11395012, ECO:0000269|PubMed:16595674, ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:17404161, ECO:0000269|PubMed:19605937, ECO:0000269|PubMed:19917250, ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:21768648, ECO:0000269|PubMed:21930935, ECO:0000269|PubMed:22504074, ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:23977055, ECO:0000269|PubMed:24413057}.
DE  Reference Proteome: Yes;
DE  Interaction: O54864; IntAct: EBI-16089648; Score: 0.35
DE  Interaction: Q3ULA2; IntAct: EBI-1266793; Score: 0.35
DE  Interaction: Q9WTL8; IntAct: EBI-1795028; Score: 0.73
DE  Interaction: O08785; IntAct: EBI-1794648; Score: 0.78
DE  Interaction: Q923E4; IntAct: EBI-1802814; Score: 0.35
DE  Interaction: Q96EB6; IntAct: EBI-1802956; Score: 0.44
DE  Interaction: Q9R194; IntAct: EBI-4408807; Score: 0.88
DE  Interaction: P97784; IntAct: EBI-8094277; Score: 0.97
DE  Interaction: Q9JMK2; IntAct: EBI-8094277; Score: 0.75
DE  Interaction: P67870; IntAct: EBI-6145564; Score: 0.00
DE  Interaction: O14503; IntAct: EBI-6145699; Score: 0.00
DE  Interaction: Q06486; IntAct: EBI-6145987; Score: 0.00
DE  Interaction: P51449; IntAct: EBI-6146041; Score: 0.00
DE  Interaction: Q99PV5; IntAct: EBI-6146248; Score: 0.00
DE  Interaction: Q91VJ2; IntAct: EBI-8094277; Score: 0.54
DE  Interaction: O54724; IntAct: EBI-8094277; Score: 0.35
DE  Interaction: O35973; IntAct: EBI-8094277; Score: 0.67
DE  Interaction: Q9DC28; IntAct: EBI-15900328; Score: 0.40
DE  Interaction: Q8C4V4; IntAct: EBI-6899301; Score: 0.59
DE  Interaction: Q8BFZ4; IntAct: EBI-6899655; Score: 0.40
DE  Interaction: O54943; IntAct: EBI-15772091; Score: 0.79
DE  Interaction: Q8BK63; IntAct: EBI-15900219; Score: 0.40
DE  Interaction: P63085; IntAct: EBI-15900242; Score: 0.40
DE  Interaction: Q3UV55; IntAct: EBI-15959294; Score: 0.40
DE  Interaction: O09106; IntAct: EBI-16089666; Score: 0.35
DE  Interaction: Q62318; IntAct: EBI-16089666; Score: 0.35
DE  Interaction: Q9EQQ0; IntAct: EBI-16089666; Score: 0.35
DE  Interaction: P23198; IntAct: EBI-16089666; Score: 0.35
DE  Interaction: Q3TQ03; IntAct: EBI-16101596; Score: 0.40
DE  Interaction: Q8N365; IntAct: EBI-16101942; Score: 0.57
DE  Interaction: P20393; IntAct: EBI-16102088; Score: 0.50
DE  Interaction: O15516; IntAct: EBI-16102160; Score: 0.37
DE  Interaction: O70361; IntAct: EBI-16102653; Score: 0.37
DE  Interaction: Q16526; IntAct: EBI-21985224; Score: 0.53
DE  Interaction: Q60953; IntAct: EBI-21986176; Score: 0.46
DE  Interaction: P29590; IntAct: EBI-21986403; Score: 0.27
DE  Interaction: P58462; IntAct: EBI-26666852; Score: 0.37
DE  Interaction: G3UW74; IntAct: EBI-26673555; Score: 0.37
DE  Interaction: Q99PM3; IntAct: EBI-26684532; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0140297;
GO  GO:0042826;
GO  GO:1990226;
GO  GO:0042802;
GO  GO:0019900;
GO  GO:0016922;
GO  GO:0036002;
GO  GO:0070063;
GO  GO:0000978;
GO  GO:0000976;
GO  GO:0003713;
GO  GO:0001222;
GO  GO:0032922;
GO  GO:0097167;
GO  GO:0007623;
GO  GO:0043153;
GO  GO:0006631;
GO  GO:0006094;
GO  GO:0005978;
GO  GO:0070932;
GO  GO:0019249;
GO  GO:0042754;
GO  GO:0045892;
GO  GO:0070345;
GO  GO:0031397;
GO  GO:0060567;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0120162;
GO  GO:0051726;
GO  GO:0042752;
GO  GO:0051946;
GO  GO:0050796;
GO  GO:0050767;
GO  GO:0019229;
GO  GO:0002931;
GO  GO:0050872;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNGYVDFSPSPTSPTKEPGAPQPTQAVLQEDVDMSSGSSGNENCSTGRDSQGSDCDDNGKELRMLVESSNTHPSPDDAFR
SQ  LMMTEAEHNPSTSGCSSEQSAKADAHKELIRTLKELKVHLPADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMSSE
SQ  SQPCSVDVPSYSMEQVEGITSEYIVKNADMFAVAVSLVSGKILYISNQVASIFHCKKDAFSDAKFVEFLAPHDVSVFHSY
SQ  TTPYKLPPWSVCSGLDSFTQECMEEKSFFCRVSVGKHHENEIRYQPFRMTPYLVKVQEQQGAESQLCCLLLAERVHSGYE
SQ  APRIPPEKRIFTTTHTPNCLFQAVDERAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQAGGQPFDYSPIRFRT
SQ  RNGEYITLDTSWSSFINPWSRKISFIIGRHKVRVGPLNEDVFAAPPCPEEKTPHPSVQELTEQIHRLLMQPVPHSGSSGY
SQ  GSLGSNGSHEHLMSQTSSSDSNGQEESHRRRSGIFKTSGKIQTKSHVSHESGGQKEASVAEMQSSPPAQVKAVTTIERDS
SQ  SGASLPKASFPEELAYKNQPPCSYQQISCLDSVIRYLESCSEAATLKRKCEFPANIPSRKATVSPGLHSGEAARPSKVTS
SQ  HTEVSAHLSSLTLPGKAESVVSLTSQCSYSSTIVHVGDKKPQPELETVEDMASGPESLDGAAGGLSQEKGPLQKLGLTKE
SQ  VLAAHTQKEEQGFLQRFREVSRLSALQAHCQNYLQERSRAQASDRGLRNTSGLESSWKKTGKNRKLKSKRVKTRDSSEST
SQ  GSGGPVSHRPPLMGLNATAWSPSDTSQSSCPSAPFPTAVPAYPLPVFQAPGIVSTPGTVVAPPAATHTGFTMPVVPMGTQ
SQ  PEFAVQPLPFAAPLAPVMAFMLPSYPFPPATPNLPQAFLPSQPHFPAHPTLASEITPASQAEFPSRTSTLRQPCACPVTP
SQ  PAGTVALGRASPPLFQSRGSSPLQLNLLQLEEAPEGSTGAAGTLGTTGTAASGLDCTSGTSRDRQPKAPPTCNEPSDTQN
SQ  SDAISTSSDLLNLLLGEDLCSATGSALSRSGASATSDSLGSSSLGFGTSQSGAGSSDTSHTSKYFGSIDSSENNHKAKMI
SQ  PDTEESEQFIKYVLQDPIWLLMANTDDSIMMTYQLPSRDLQAVLKEDQEKLKLLQRSQPRFTEGQRRELREVHPWVHTGG
SQ  LPTAIDVTGCVYCESEEKGNICLPYEEDSPSPGLCDTSEAKEEEGEQLTGPRIEAQT
//
ID  Q9Z301;
PN  Period circadian protein homolog 2;
GN  Per2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:11533252}. Cytoplasm {ECO:0000269|PubMed:11533252}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54943}. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. PML regulates its nuclear localization (By similarity). {ECO:0000250|UniProtKB:O54943}.
DR  UNIPROT: Q9Z301;
DR  Pfam: PF08447;
DR  Pfam: PF12114;
DR  PROSITE: PS50112;
DE  Function: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock- controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK- ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK- ARTNL/BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like ARNTL or G6PC1. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000269|PubMed:14672706}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0140297;
GO  GO:0042826;
GO  GO:1990226;
GO  GO:0042802;
GO  GO:0019900;
GO  GO:0016922;
GO  GO:0036002;
GO  GO:0070063;
GO  GO:0000978;
GO  GO:0000976;
GO  GO:0003713;
GO  GO:0001222;
GO  GO:0032922;
GO  GO:0097167;
GO  GO:0007623;
GO  GO:0043153;
GO  GO:0006631;
GO  GO:0006094;
GO  GO:0005978;
GO  GO:0070932;
GO  GO:0019249;
GO  GO:0042754;
GO  GO:0045892;
GO  GO:0070345;
GO  GO:0031397;
GO  GO:0060567;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0120162;
GO  GO:0051726;
GO  GO:0042752;
GO  GO:0051946;
GO  GO:0050796;
GO  GO:0050767;
GO  GO:0019229;
GO  GO:0002931;
GO  GO:0050872;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNGYVDFSPSPTSPTQEPGEPQPTQAVLQEDVDMSSGSSGNENCSTGRDSQGSDCDDSGKELRMLVESSNTHPSPDDTFR
SQ  LMMTEAEHNPSTSGCSSEQSAKADAHKELIRTLRELKVHLPADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMSSE
SQ  SQPCSVDVPSYTMEQVEGITSEYIVKNSDMFAVAVSLVSGKILYISNQVAPIFHCKKDAFSDAKFVEFLAPHDVSVFHSY
SQ  TTPYKLPPWSVSSGLDSFTQECMEEKSFFCRVSVGKHHENEIRYQPFRMTPYLVKVQEQKGAASQLCCLLLAERVHSGYE
SQ  APRIPPEKRIFTTTHTPNCLFQDVDERAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQASGQPFDYSPIRFRT
SQ  RNGEYITLDTSWSSFINPWSRKISFIIGRHKVRVGPLNEDVFAASPCPEEKTPHPSVQELTEQIHRLLMQPVPHSGSSGY
SQ  GSLGSNGSHEHLMSQTSSSDSNGQEESHWRRSGIFKTSGKSQSKSHFSPESGGQKEASVAEMQSSPPAQVRSVTTMERDS
SQ  SGASLPKASFPEELTYKSQPPCSYQQISCLDSVIRYLESCNEAATLKRKCEFPANIPSRKATVSPGLHSGEAARSSKVTS
SQ  HTEVSAHLSSLALPGKAESVVSLTSQCSYSSTIVHVGDKKPQPELETVEDVASGPESQDDAAGGLSQEKGSLQKLGLTKE
SQ  VLAAHTQREEQGFLQRFREVSRLGALQAHCQNYLQERSRAPASDRGLRNASGIESSWKKTGKNRKLKSKRVKTRDSSEST
SQ  GSGGPVSHRPPLVGLNATAWSPSDTSQSSCPSAPFPAPVPAYPLPVFPAPGIVSTPGTVVAPPAAAHTGFTMPVVPMGTQ
SQ  PEFAVQPLPFAAPLAPVMAFMLPSYPFPPATPNLPQAFFPSQPHFPAHPTLASEITPASQAEFPSRTSMLRQPCACPVTP
SQ  PAGTVALGRASPPLFQSRGSSPLQLNLLQLEEAPESSTGAAGTLGTTGTAASGLDCTSGASRDRQPKAPPTCSEPSDTQN
SQ  SDAISTSSDLLNLLLGEDLCSATGSALSRSGASATSDSLGSSSLGCDTSRSGAGSSDTSHTSKYFGSIDSSENNHKAKMI
SQ  TDTEESEQFIKYVLQDPIWLLMANTDDNIMMTYQLPSRDLQAVLKEDQEKLKLLQRSQPHFTEGQRRELREVHPWVHTGG
SQ  LPTAIDVTGCVYCESEEKGNLCLPYEEDSPSLGLCDTSEAKEEESGQLANPRKEAQT
//
ID  Q8K3T2;
PN  Period circadian protein homolog 2;
GN  PER2;
OS  134510;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O54943}. Cytoplasm {ECO:0000250|UniProtKB:O54943}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54943}. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. PML regulates its nuclear localization (By similarity). {ECO:0000250|UniProtKB:O54943}.
DR  UNIPROT: Q8K3T2;
DR  Pfam: PF08447;
DR  Pfam: PF12114;
DR  PROSITE: PS50112;
DE  Function: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock- controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK- ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK- ARTNL/BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like ARNTL or G6PC1. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1. {ECO:0000250|UniProtKB:O54943}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000976;
GO  GO:0003713;
GO  GO:0032922;
GO  GO:0097167;
GO  GO:0006631;
GO  GO:0006094;
GO  GO:0005978;
GO  GO:0070932;
GO  GO:0019249;
GO  GO:0042754;
GO  GO:0045892;
GO  GO:0070345;
GO  GO:0031397;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0051726;
GO  GO:0042752;
GO  GO:0051946;
GO  GO:0050796;
GO  GO:0050767;
GO  GO:0019229;
GO  GO:0002931;
GO  GO:0050872;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNGYVEFSPSPTKESVEPQPSQAVLQEDVDMSSGSSGHENCSMGRDSQGSDCDDNGKELRMLVEPSDTHSSPDAFRLMMT
SQ  EPQHNPSTSGCSSEQSAKANAHKELIRTLRELKVHLPADKKAKGKASTLAILKYALRSVKQVKANEEYYQLLMSSESQPC
SQ  SMDVPSYTVEQVEGITSEYIVKNADMFAVAVSLVSGKILYISNQVASIFHCKKDAFSDAKFVEFLAPHDVSVFHSYTTPY
SQ  KLPPWSMCCGVDSFTQECMEEKSFFCRVSVGKHHESEIRYQPFRMTPYLVKVQEQQGAESQLCCLLLAERIHSGYEAPRI
SQ  PPEKRIFTTTHIPNCLFQDVDERAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQAGGQPFDYSPIRFRARNGE
SQ  YITLDTSWSSFINPWSRKISFIIGRHKVRVGPLNEDVFAASPCPEGKTPHPSIQELTEQIHRLLMQPVPHSGSSGYGSLG
SQ  SNGSHEHLMSQTSSSDSNGHEESRWRKSGISKNGSKTQTRSHFSHESGEQKEIAVTEMQSSTPAQAKAAPTVERDSSGSS
SQ  LPKASFPEELAYKNQPACSYQQISCLDSVIRYLESCNEAATLKRKCEFPANIPSRKATVSPGLHAEEAAPPPSKVSSHAE
SQ  VRARLSSLTLPDKAESVVSLTSQCSYSSTIVHVGDKKPQPELETVEDAVSGPESLDGAPGGLSQEKGPLQKLGLTKEVLA
SQ  AHTQREEQGFLQRFREVSRLGALQAHRQNYRAQASERAAPGLRNASGMDSSWKKTGKNRKLKSKRVKTRDSSESTGSGGP
SQ  VSHRPPLVGLNATAWSPSDTSQSSCPSAPFPAPVPAYPLPVFEAPGITSTPAPPEAAHSSFTVPVVPMGAQPDFAVQPLP
SQ  LAAPLAPVLAFMLPSYPFPPANPNLSHAFFPGQPHFPAQPTFASEMTPASQADFPSQTPLLRQQCTCPVTPPAATVTSGR
SQ  ASPPLFQSRGSSPLQLNLLQLEEAPEGSTGAAGTSGTTGTAAAGLDCTPGTSRDRQPKAPSTCKEPSDTQNSDALSTSSD
SQ  LLNLLLAEDLCSATGSALSGSGASATSDSLGSGSLGCDASRSGAGSSDTSHTSKYFGSIDSSENNHKAKVSTDTEESEQF
SQ  IKYVLQDPIWLLVANTDDSVMMTYQLPSRDLESVLREGRERLKLLQRAQPRFTEGQRRELREVHPWVQTGGLPAAIDVAE
SQ  CVYCKSERKGDICLPYEEDSPSPGLCDTSEAKEEEGEQLTGPRIEAQT
//
ID  Q12144;
PN  Pore and endoplasmic reticulum protein of 33 kDa;
GN  PER33;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus, nuclear pore complex.
DR  UNIPROT: Q12144;
DR  UNIPROT: D6VY65;
DR  Pfam: PF03661;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P38822; IntAct: EBI-600045; Score: 0.37
DE  Interaction: P32790; IntAct: EBI-600273; Score: 0.55
DE  Interaction: P32793; IntAct: EBI-600550; Score: 0.37
DE  Interaction: Q03880; IntAct: EBI-8492693; Score: 0.44
DE  Interaction: P25294; IntAct: EBI-3662851; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3681238; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3699984; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3718402; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0071786;
GO  GO:0061024;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTVPRNRPMAPFGTIIKSRIKQPQFYWFIGHFLTIFNFIQFHLSITSKQNQLSCYRRSLFYISVTYAIVLYQFFKSDQLK
SQ  FNFTLLRQEMKKLDNLQYFAMLFILFLLSQFNIIISGSLYSPVIFSIFHFLNYFKENLLPFLPLIPLNLKNLLNSKITVF
SQ  IQNYNGFFLQMAQVFEIICGLRVGLFLVPFNFFLLLVRRANVSFEVVGTMLAGLTYVWFFKLRYLQSESMRQIFKQYVLR
SQ  LDAYVSRTLPPYCSRLWNGYKNFVMTVFWKIPV
//
ID  Q17285;
PN  Period circadian protein;
GN  per;
OS  34689;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q17285;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SKSSTGTPPSYNQLNYNENLMRFFKSKPVTVGKEESMAVEQSYNDVELQRDPSPDQCCDYSGESGSAGNLSSGSNVQMEI
SQ  ITNGSNTGTGTSSGSFQPPLLTEALLN
//
ID  Q03293;
PN  Period circadian protein;
GN  per;
OS  7217;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q03293;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  EGSGGSGSSGNFTTGSNVHMSSVTNTSNAGTGGTGTNTGTNTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGKGA
SQ  GAGTGTATNETAGPGTTTTTTTRSTTTAATAASPPVTLTESLLNK
//
ID  P91607;
PN  Period circadian protein;
GN  per;
OS  46840;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P91607;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVEPSYVSSAREDAHRTLSPVQGFEGSGGTGSSGNFTTGSNLHM
SQ  SSVTNTSNAGTGTSGTGNSGGGGGGGGGGGPGNGAVTPVTLTESLLNKHNDEMEKFMLKKHRESRGRSGEKNKKSANDTL
SQ  KMVEYSGPGPGPGHGHGIKRGGSHSWEGEANKPKQLLTLNTGGMPPLLDIHTSSASLSKCQASGAGGGGSGSVGGTGNIG
SQ  SGGSNAQPSTNQYAQSGLSCTQNINLWPPFSVGITTPTSVLSTHTAVAQSSFSTQHNLFPTFYYIPASIAASSPSGTSPN
SQ  PRPHKHTLVHKSAEQPSTSQAAAATMPLQYMTGLMYPHPSLFYTHPAAAAATAMV
//
ID  P92203;
PN  Period circadian protein;
GN  per;
OS  46790;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P92203;
DR  UNIPROT: P92207;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVESSYVSSARGEDARSTLSPVQGFEGSGGSGSSGNFTTGSNLH
SQ  MSSVTNTSNAGTGTSGTGNSGDGGGGGGADGTGSGAAPPVTLTESLLNKHNDEMEKFMLKKHRESRGRSGEKNKKSANEA
SQ  MKMLEYSGPGPGHGHGIKRGGSHSWEGEANKPKQQLTLNTSGGGGGGGGGGGMPLFLDMTHASSSSQNKGLAGVGVGGAG
SQ  GVVGGGSGTGLGGNGNVGSGNGNNNQPSTNQYTQSRLPCTQNINLWPPFSVGITTPTSVLSSHTAVPPSSFSPQHSLFPT
SQ  FYYIPASIAASSPSGTNTNPNRPHKHAHVHNSSEKPSTSQAAAATMPLQYMTGVMYPHPSLFYTHPAAAAATAMV
//
ID  Q26288;
PN  Period circadian protein;
GN  per;
OS  7220;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q26288;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  GGSGGSGSSGNFTTASNIHMSSVTNTSIAGTGGTGGTGTGTGTGTGTGTGTGTGTDTGTGTGTRNGTNSGTNSGTRTGTA
SQ  SSYRGGGGGAGGGGGVTIQHLTLTESLLNK
//
ID  Q03294;
PN  Period circadian protein;
GN  per;
OS  7250;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q03294;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  EGSGGSGSSGNFTTGSNVRMSSVTNTSNAGTGTSGGGNSAAASGASVNAPPVTVTLTESLLNK
//
ID  P91613;
PN  Period circadian protein;
GN  per;
OS  46792;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P91613;
DR  UNIPROT: P91612;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVESSYVSSARGEDARSTLSPVQGFEGSGGSGSSGNFTTGSNLH
SQ  MSSVTNTSNAGTGTSGTGNSGDGGGGGGADGPGSGAAPPVTLTESLLNKHNDEMEKFMLKKHRESRGRSGEKNKKSANDA
SQ  MKMLEYSGPGPGHGHGIKRGGSHSWEGEANKPKQQLTLNTGGGGGGMPPFLDIQHTSSSTQNKGLAGVGVGGAGGGVVGV
SQ  GSSAGGNGSGTGNNNGNGNNNQPTTNQFTQSGLSCTQNINLWPPFSVGITTPTSVLSSHTAVAQSSFSPQHSLFPTFYYI
SQ  PASIAASSPSGTSPNPNRPHKHAHVHSSSEKPSTSQAAAATMPLQYMTGVMYPHPSLFYTHPAAAAATAMV
//
ID  Q03353;
PN  Period circadian protein;
GN  per;
OS  7226;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q03353;
DR  UNIPROT: Q26283;
DR  Pfam: PF00989;
DR  PROSITE: PS50112;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048856;
GO  GO:0006357;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  KVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMIIKRNKDKSRKKKKNKGAGQGAGQAQTLIS
SQ  ASTSLEGRDEEKPRPSGTGCVEQQICRELQDQQHGEDHSEPQATEQLQQEEEDQSGSESEADRVEGVAKSEAAQSFPIPS
SQ  PLSVTIVPPSMGGCGGVGHAAGLDSGLAKFDKTWEAGPGKLESMTGVGAAAAGTGQRGERVKEDSFCCVISMHDGIVLYT
SQ  TPSITDVLGYPRDMWLGRSFIDFVHLKDRATFASQITTGIPIAESRGSVPKDAKSTFCVMLRRYRGLKSGGFGVIGRPVS
SQ  YEPFRLGLTFREAPEEARPDNYMVSNGTNMLLVICATPIKSSYKVPDEILSQKSPKFAIRHTATGIISHVDSAAVSALGY
SQ  LPQDLIGRSIMDFYHHEDLSVMKETYETVMKKGQTAGASFCSKPYRFLIQNGCYVLLETEWTSFVNPWSRKLEFVVGHHR
SQ  VFQGPKQCNVFEAAPTCKLKISEEAQSRNTRIKEDIVKRLAETVSRPSDTVKQEVSRRCQALASFMETLMDEVSRADLKE
SQ  GSGGSGSSGNFTTASNIHMSSVTNTSIAGTGGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTG
SQ  TGNGTNSCTGTGTTSSSRGGSAAIPPVTLTESLLNK
//
ID  P07663;
PN  Period circadian protein;
GN  per;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm, perinuclear region. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization.
DR  UNIPROT: P07663;
DR  UNIPROT: O17483;
DR  UNIPROT: O76882;
DR  UNIPROT: O76883;
DR  UNIPROT: O76884;
DR  UNIPROT: O76885;
DR  UNIPROT: Q24446;
DR  UNIPROT: Q24447;
DR  UNIPROT: Q24448;
DR  UNIPROT: Q24449;
DR  UNIPROT: Q6PVA3;
DR  UNIPROT: Q8MLY0;
DR  UNIPROT: Q9GN20;
DR  UNIPROT: Q9GN51;
DR  UNIPROT: Q9GQH9;
DR  UNIPROT: Q9GV48;
DR  UNIPROT: Q9GV53;
DR  UNIPROT: Q9GV54;
DR  UNIPROT: Q9GV55;
DR  UNIPROT: Q9W4X0;
DR  PDB: 1WA9;
DR  PDB: 3GEC;
DR  PDB: 3RTY;
DR  Pfam: PF00989;
DR  PROSITE: PS50112;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition. Required for binding of cwo to the E box regions in the promoters of target genes of the transcriptional activator Clock, probably by binding to Clock-cycle heterodimers, reducing their affinity for E box binding and allowing cwo to bind instead (PubMed:27814361). {ECO:0000269|PubMed:27814361}.
DE  Reference Proteome: Yes;
DE  Interaction: O77059; IntAct: EBI-872150; Score: 0.27
DE  Interaction: Q7JWQ7; IntAct: EBI-496457; Score: 0.37
DE  Interaction: Q26416; IntAct: EBI-496464; Score: 0.00
DE  Interaction: P49021; IntAct: EBI-15772062; Score: 0.59
DE  Interaction: P33438; IntAct: EBI-496485; Score: 0.37
DE  Interaction: Q9VB55; IntAct: EBI-496492; Score: 0.00
DE  Interaction: Q9VXJ0; IntAct: EBI-496499; Score: 0.37
DE  Interaction: P11996; IntAct: EBI-496506; Score: 0.00
DE  Interaction: Q9VTW8; IntAct: EBI-496513; Score: 0.37
DE  Interaction: Q9VLX9; IntAct: EBI-496520; Score: 0.00
DE  Interaction: O61735; IntAct: EBI-872062; Score: 0.27
DE  Interaction: Q24533; IntAct: EBI-872282; Score: 0.27
DE  Interaction: O76324; IntAct: EBI-15718462; Score: 0.44
DE  Interaction: P07663; IntAct: EBI-15772031; Score: 0.68
DE  Interaction: P08181; IntAct: EBI-16073655; Score: 0.35
DE  Interaction: P08182; IntAct: EBI-16073713; Score: 0.35
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0000976;
GO  GO:0003712;
GO  GO:0003714;
GO  GO:0001222;
GO  GO:0008134;
GO  GO:0048148;
GO  GO:0048512;
GO  GO:0032922;
GO  GO:0007623;
GO  GO:0042745;
GO  GO:0060086;
GO  GO:0007620;
GO  GO:0007619;
GO  GO:0008340;
GO  GO:0008062;
GO  GO:0009649;
GO  GO:0043153;
GO  GO:0045475;
GO  GO:0007616;
GO  GO:0045433;
GO  GO:0007617;
GO  GO:0045892;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0042752;
GO  GO:0045187;
GO  GO:1904059;
GO  GO:0001932;
GO  GO:0009416;
GO  GO:0006979;
GO  GO:0009266;
GO  GO:0007622;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGGESTESTHNTKVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMIIKRNKDKSRKKKKNKG
SQ  AGQGAGQAQTLISASTSLEGRDEEKPRPSGTGCVEQQICRELQDQQHGEDHSEPQAIEQLQQEEEEDQSGSESEADRVEG
SQ  VAKSEAAQSFPIPSPLSVTIVPPSMGGCGGVGHAAGLDSGLAKFDKTWEAGPGKLESMTGVGAAAAGTGQRGERVKEDSF
SQ  CCVISMHDGIVLYTTPSITDVLGYPRDMWLGRSFIDFVHLKDRATFASQITTGIPIAESRGSVPKDAKSTFCVMLRRYRG
SQ  LKSGGFGVIGRPVSYEPFRLGLTFREAPEEARPDNYMVSNGTNMLLVICATPIKSSYKVPDEILSQKSPKFAIRHTATGI
SQ  ISHVDSAAVSALGYLPQDLIGRSIMDFYHHEDLSVMKETYETVMKKGQTAGASFCSKPYRFLIQNGCYVLLETEWTSFVN
SQ  PWSRKLEFVVGHHRVFQGPKQCNVFEAAPTCKLKISEEAQSRNTRIKEDIVKRLAETVSRPSDTVKQEVSRRCQALASFM
SQ  ETLMDEVSRADLKLELPHENELTVSERDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNENLLRFFNSKPVTAPAELDP
SQ  PKTEPPEPRGTCVSGASGPMSPVHEGSGGSGSSGNFTTASNIHMSSVTNTSIAGTGGTGTGTGTGTGTGTGTGTGTGTGT
SQ  GTGTGTGTGTGTGTGTGTGTGTGNGTNSGTGTGTASSSKGGTAAIPPVTLTESLLNKHNDEMEKFMLKKHRESRGRTGEK
SQ  SKKSANDTLKMLEYSGPGHGIKRGGSHSWEGEANKPKQQLTLGTDAIKGAAGSAGGAVGTGGVGSGGAGVAGGGGSGTGV
SQ  AGTPEGRATTTSGTGTPGGAGGGGGAGAAAAAGASSSVGSSTPGPSSYPTCTQNINLWPPFSVGITPPVHSTHTAMAQSS
SQ  FSSAGLFPTFYYIPASLTPTSPTRSPRMHKHPHKGGTDMPTTSQQAAAAAAQAMPLQYMAGVMYPHPSLFYTHPAAAAAT
SQ  AMMYQPMPFPGMANALQIPERPLGSQSAYNKSVYTTTPASMTKKVPGAFHSVTTPAQVQRPSSQSASVKTEPGSSAAVSD
SQ  PCKKEVPDSSPIPSVMGDYNSDPPCSSSNPANNKKYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDTEKDPKHRKL
SQ  KSMSTSESKIMEHPEEDQTQHGDG
//
ID  Q03295;
PN  Period circadian protein;
GN  per;
OS  7230;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q03295;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  EGSGGSGSSGNFTTGSNVRMSSVTNTSNAGTGTSAGDNSAGGNGSGNSNSAPAVTVTLTESLLNK
//
ID  Q04535;
PN  Period circadian protein;
GN  per;
OS  7269;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q04535;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  EGSGGSGSSGNFTTGSNVRMSSVTNTSNTGTGTSGGGNSAAASGARHNAPPVSVTLTESLLNK
//
ID  P91686;
PN  Period circadian protein;
GN  per;
OS  7271;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P91686;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SSTETPPSYNQLNYNENLLRFFNSKPVTAPVPVELDPPKVESSYVSSAREDARSTLSPVQGFEGSGGSGSSGNFTTGSNL
SQ  HMSSVTNTSNAGTGTSGTGNSGDGGGGGAGDGPGSGAVPPVTLTESLLNKHNDEMEKFMLKNDRESRGWSGEKNKKSAND
SQ  TLKMVEYSGPGPGHGHGIKRGGSHSWEGEANKPKQQLTLNAGGMPPLVDIHASSSSLSKCQTSVAGGGGGGGAGSASGTC
SQ  GTGNNGAGGGGGSNAQSSTNQYTQSGLSCTQNINLWPPFSVGITTPTSVLSTHMAVAQSSFSPQHSLFPTFYYIPASIAA
SQ  SSPASGTSPNPRPHKHTHVHPSSEQPSTSQGAAATMPLQYMTGVMYPHPSLFYTHPAAAAATAMV
//
ID  Q26289;
PN  Period circadian protein;
GN  per;
OS  7233;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q26289;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  GGSGGSGSSGNFTTASNIHMSSVTNTSIAGTGGTGGTGTGTGTGTGTGTGTGTGTGTGTDTGTGTGTGTETGTGTGTGTR
SQ  NGTNSGTKTGTASSYRGGGVAIQPVTLTESLLNK
//
ID  Q25206;
PN  Period circadian protein;
GN  per;
OS  7235;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q25206;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SKSSTETPLSYNQLNYKENLQRFFNSKPVTAPTQLDPVNRDSSYASTSREDACSAISPDHGGECSGGSGSSGNCTTNSNI
SQ  RMSSFTNTSITGTGTSGCGNSGGKLSESGPVEVGGAAADAGPSLAADNSIPPISVTLTESLLN
//
ID  P12348;
PN  Period circadian protein;
GN  per;
OS  46245;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P12348;
DR  UNIPROT: Q29I05;
DR  Pfam: PF00989;
DR  PROSITE: PS50112;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048856;
GO  GO:0006357;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGESTESTQNTKVSDSAYSNSCSNSQSQRSGSSKSMLSGSHSSGSSGYGGKPSIQTSSSDMAIKRNKEKSRKKKKAKCT
SQ  QAQATISSSLEGAEEQPHSSGTTCDQKILHVLATTQQLGDQPSSLDHKLGEQLEARHNCGVGKAEQPQSFSLPCPLSVST
SQ  LMPGIGVCHGGNAPGGKWEKTFESCKLDTGPAKTERVKEDSFCCVISMHDGIVLYTTPSITDVLGFPRDMWLGRSFIDFV
SQ  HTKDRATFASQITTGIPIAESRCSMPKDARSTFCVMLRQYRGLQTSGYGVIGRSVNYEPFRLGMSFREAPEEERSDNYMV
SQ  ANSSNMLLVICATPIKSSYRVPEEIHSQRSPKFAIRHTAAGIISHVDSAAVSALGYLPQDLMGRSIMDLYHHDDLPVIKE
SQ  IYESVMKKGQTAGASFCSKPYRFLIQNGCYILLETEWSSFVNPWSRKLEFVVGHHRVFQGPKICNVFETPPNSEPKIAEE
SQ  LQNKNTRIKEEIVNLLAEKVSRPSDTVKQEVSRRCQALASFMETLMDEVSRADLKLELPHENELTVSERDSVMLGEISPH
SQ  HDYYDSKSSIETPPSYNQLNYNENLLRFFNSKPVTAPVEVDPPKVGSSDVSSTREDARSTLSPLNGFEGSGASGSSGHLT
SQ  SGSNIHMSSATNTSNAGTGTGTVTGTGTIIATSGTGTVTCASGNMDANTSAAFNIAANTSAADNFGADTSAADTSGADTS
SQ  AADNYAVDNYGPGNFGAENSCADNSGAENSCADNSGVDNSRPGNSGADNSAADNFGADNSGPDNSGADNSGPDNTGPDNS
SQ  GAENSRAENSRADNSRPDHPRPDISGASNSRPDKTGPDKSGAENSASGSGSGTSGNEGPSSGGQDTRTTAGTPDSPPVSL
SQ  TESLLNKHNDEMEKFMLKKHRESRGDRRTVEKNKNKTTNTIDSLKILEYSSTGPGHGTKRGGSYSWEGEGNKPKQQPTLN
SQ  SVGVGTGAPEAPIPPVHPTHTTHTAIAQSSFSAQQSLFPTFYYIPATPLAASTPAPGALSPTPRNQKHHHHAHQHAPKVP
SQ  DQASTSQQAAGPAAIPLQYVTGVMYPHPSLFYTHPAAAAATAMMYQPMPFPGIANAMQLPEQPSTSQSNYSKTVFSVIVA
SQ  PPTITTTTATTTPKTQGAFHSITPAQLQRPSSQDTSVKTEPASNATPSHSSNKKKANSSIASGIGDYNSNQACSRNRANV
SQ  KKYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDNDKEAKHRKLKNITRLSSKIMEHPEEDQTQHGDG
//
ID  P91697;
PN  Period circadian protein;
GN  per;
OS  46793;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P91697;
DR  UNIPROT: P91692;
DR  UNIPROT: P91693;
DR  UNIPROT: P91694;
DR  UNIPROT: P91695;
DR  UNIPROT: P91696;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVESSYVSSARGEDARSTLSPVQGFEGSGGSGSSGNFTTGSNLH
SQ  MSSVTNTSNAGTGTSGTGNSGDGGGGGGANGTGSGAAPPVTLTESLLNKHNDEMEKFMLKKHRESRGRSGEKNKKSANEA
SQ  MKMLEYSGPGPGHGHGIKRGGSHSWEGEANKPKQQLTLNTIGGGGGGGVGGGMPLFLDITHASSSSQNKGLAGVGVGGAG
SQ  GVVGGGGSGTGLGGNGNVGSGNGNNNQPSTNQYTQSRLPCTQNINLWPPFSVGITTPTSVLSSHTAVPPSSFSPQHSLFP
SQ  TFYYIPASIAASSPSSTNTNPNRPHKHAHVHNSSEKPSTSQAAAATMPLQYMTGVMYPHPSLFYTHPAAAAATAMV
//
ID  P91698;
PN  Period circadian protein;
GN  per;
OS  46795;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P91698;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVESSYVSSARGEDARSTLSPVQGFEGSGGSGSSGNFTTGSNLH
SQ  MSSVTNTSNAGTGTSGTGNSGDGGGGGGANGTGSGAAPPVTLTESLLNKHNDEMEKFMLKKHRESRGRSGEKNKKSANEA
SQ  MKMLEYSGPGPGHGHGIKRGGSHSWEGEANKPKQQLTLNTSGGGGGVGVGGGMPLFLDITHASSSSQNKGLAGVGVGGAG
SQ  GVVGGGGSGTGLGGNGNVGSGNGNNNQPSTNQYTQSRLPCTQNINLWPPFSVGITTPTSVLSSHTAVPPSSFSPQHSLFP
SQ  TFYYIPASIAASSPSSTNTNPNRPHKHAHVHNSSEKPSTSQAAAATMPLQYMTGVMYPHPSLFYTHPAAAAATAMV
//
ID  Q03296;
PN  Period circadian protein;
GN  per;
OS  7257;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q03296;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  EGSGGSGSSGNFTTGSNIRMSSVTNTSNAGTGTGTGTGTGTATGTGTATGTGTSAGGTSAGGNASGNSGNPPPAFAITLT
SQ  ETLLNK
//
ID  Q04536;
PN  Period circadian protein;
GN  per;
OS  7273;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q04536;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  EGSGGSGSSGNFTTGSNIHMSSVTNTSNAGTGTSGTGNSGGGSGGGTGPGSGAIPPVTLTESLLNK
//
ID  P91705;
PN  Period circadian protein;
GN  per;
OS  46791;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P91705;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVEPSYVSSAREDARSTLSPVQGFEGSGGTGSSGNFTTGSNLHM
SQ  SSVTNTSNAGTGTSGTGNSGGGGGGGGGAGPGNGAVPPVTLTESLLNKHNDEMEKFMLKKHRESRGRSGEKNKKSANDTL
SQ  KMVEYSGPGPGPGHGHGIKRGGSHSWEGEANKPKQLLTLNTGGMPPLLDIHTSSASLSKCQASGAGGGGSGSVGGTGNIG
SQ  SGGSNAQPSTNQYTQSGLSCTQNINLWPPFSVGITTPTSVLSTHTAVAQSSFSTQHNLFPTFYYIPASIAASSPSGTSPN
SQ  PRPHKHTLVHKSAEQPSTSQAAAATMPLQYMTGLMYPHPSLFYTHPAAAAATAMV
//
ID  Q03354;
PN  Period circadian protein;
GN  per;
OS  7238;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q03354;
DR  UNIPROT: Q26285;
DR  Pfam: PF00989;
DR  PROSITE: PS50112;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044297;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0032922;
GO  GO:0060086;
GO  GO:0007620;
GO  GO:0008340;
GO  GO:0008062;
GO  GO:0043153;
GO  GO:0045475;
GO  GO:0007616;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0045187;
GO  GO:1904059;
GO  GO:0001932;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  KVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMIIKRNKDKSRKKKKNKGAGQGAGQAQTLIS
SQ  ASTSLEGRDEEKPRPSGTGCVEQQICRELQDQQHGEDHSEPQAAEQLQQEEDQSGSESEADRVEGVAKSEAVQSFPIPSP
SQ  LSVTIVPPSMGGCGGVGHAAGLDSGLAKFDKTWEAGPGKLESMTGVGAAAAGTGQRGERVKEDSFCCVISMHDGIVLYTT
SQ  PSITDVLGYPRDMWLGRSFIDFVHLKDRATFASQITTGIPIAESRGSVPKDAKSTFCVMLRRYRGLKSGGFGVIGRPVSY
SQ  EPFRLGLTFREAPEEARPDNYMVSNGTNMLLVICATPIKSSYKVPDEILSQKSPKFAIRHTATGIISHVDSAAVSALGYL
SQ  PQDLIGRSIMDFYHHEDLSVMKETYETVMKKGQTAGASFCSKPYRFLIQNGCYVLLETEWTSFVNPWSRKLEFVVGHHRV
SQ  FQGPKQCNVFEAAPTCKLKISEEAQSRNTRIKEDIVKRLAETVSRPSDTVKQEVSRRCQALASFMETLMDEVSRADLKEG
SQ  SGGSGSSGNFTTASNIHMSSVTNTSIAGTGGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGNGTNSGTTS
SQ  SSRGGSAAAPPVTLTESLLNK
//
ID  Q03355;
PN  Period circadian protein;
GN  per;
OS  7240;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q03355;
DR  UNIPROT: Q24626;
DR  UNIPROT: Q24627;
DR  UNIPROT: Q24628;
DR  UNIPROT: Q26282;
DR  UNIPROT: Q26284;
DR  Pfam: PF00989;
DR  PROSITE: PS50112;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044297;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0032922;
GO  GO:0060086;
GO  GO:0007620;
GO  GO:0008340;
GO  GO:0008062;
GO  GO:0043153;
GO  GO:0045475;
GO  GO:0007616;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0045187;
GO  GO:1904059;
GO  GO:0001932;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  KVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMIIKRNKDKSRKKKKNKGTGQGAGQAQTLIS
SQ  ASTSLEGRDEEKPRPSGTGCVEQQICRELQDQQHGEDHSEPQATEQLQQEEEDQSGSESEADRVEGVAKSEAAQSFPIPS
SQ  PLSVTIVPPSMGGCGGVGHAAGLDSGLAKFDKTWEAGPGKLESMTGVGAAAAGTGQRGERVKEDSFCCVISMHDGIVLYT
SQ  TPSITDVLGYPRDMWLGRSFIDFVHLKDRATFASQITTGIPIAESRGSVPKDAKSTFCVMLRRYRGLKSGGFGVIGRPVS
SQ  YEPFRLGLTFREAPEEARPDNYMVSNGTNMLLVICATPIKSSYKVPDEILSQKSPKFAIRHTATGIISHVDSAAVSALGY
SQ  LPQDLIGRSIMDFYHHEDLSVMKETYETVMKKGQTAGASFCSKPYRFLIQNGCYVLLETEWTSFVNPWSRKLEFVVGHHR
SQ  VFQGPKQCNVFEAAPTCKLKISEEAQSRNTRIKEDIVKRLAETVSRPSDTVKQEVSRRCQALASFMETLMDEVSRADLKS
SQ  GSSGNFTTASNIHMSSVTNTSIAGTGGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGNGTNSGT
SQ  GTGTTSSSRGGSTAIP
//
ID  Q04537;
PN  Period circadian protein;
GN  per;
OS  7274;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q04537;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  EGSGGSGSSGHFTTGSNVHMSSVTNTSNGGTGGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTGTASGTATGTASGT
SQ  ATGTANGTGTGKGTDTHTAGSGSGSGTGTGTGTGTTTTTTTGNNSSSSTPPVTLTESLLNK
//
ID  Q26287;
PN  Period circadian protein;
GN  per;
OS  7243;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q26287;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  EGSGGSGSSGNFTTASNIHMSSVTNTSIAGTGGTGTGTGTGTGTGTGTGTGTGTGTGTGTGNGSASSNYRGGGVAIQPVT
SQ  LTESLLNK
//
ID  P91716;
PN  Period circadian protein;
GN  per;
OS  46794;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P91716;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVESSYVSSARGEDARSTLSPVQGFEGSGGSGSSGNFTTGSNLH
SQ  MSSVTNTSNAGTGTSGTGNSGDGGGGGGADGTGSGAAPPVTLTESLLNKHNDEMEKFMLKKHRESRGRSGEKNKKSANEA
SQ  MKMLEYSGPGPGHGHGIKRGGSHSWEGEANKPKQQLTLNPSGGGGGMPLLLDITHTSSSTQNKGLAGVGVGGAGGGVGGG
SQ  GSGTGLGGNGNVGSGNGNNNQASTNQYTQSGLPCTQNINLWPPFSVGITTPTSVLSSHTAVAQSSFSPQHSLFPTFYYIP
SQ  ASIAASSPSGTNPSPNRPHKHAHVHSSSEKPSTSQAAAATMPLQYMTGVMYPHPSLFYTHPAAAAATAMV
//
ID  P12349;
PN  Period circadian protein;
GN  per;
OS  7244;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: P12349;
DR  Pfam: PF00989;
DR  PROSITE: PS50112;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048856;
GO  GO:0006357;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGESTESTHNTKVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMAVKRNKDKSRKKKKAKSP
SQ  AQATAATTTTIKSLEQTEEPLLVKPNNGSCEQQLELQDAQQLGAPTPSDAHDAHGDKPQLDVDEQQDDPQAEQIQQLETA
SQ  TAATISPDTMSASVTVTIDGCTSMEKTCEWTDRPGRLEAHAACIGKQHVQQQQHDRVKEDSFCCVISMHDGVVLFTTANL
SQ  NEMLGYPREMWLGRSFIDFVHIKDRATFASQITTGIPIAESRCSQSKDARTTFCVMLRRYRGLASGGFGIIGRPVSYAPF
SQ  RLGLTFREAPEEVQPDGCTLSNATSMLLVISATPIKSCYKEPDEFLSPKGPKFAIQHTAAGIISHVDTAAVSALGYLPQD
SQ  LIGRSILDFYHHEDLSDIKDIYEKVVKKGQTVGATFCSKPFRFLIQNGCYILLETEWTSFVNPWSRKLEFVVGHHRVFQG
SQ  PKQCDVFEMSPNVTPNIPEDEQNRNACIKEDILKMMTETVTRPSDTVKQEVSRRCQALASFMETLMDEVARGDLKLDLPH
SQ  ETELTVSERDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNENLLRFFNSKPVTAPVDTDPPKMDSSYVSSAREDALSP
SQ  VHGFEGSGGSGSSGNLTTASNVRMSSVTNTSNTGTGTSGGENSASGSSNPLPVNMTLTEILLNKHNDEMEKCMLKKHRES
SQ  RGRTGDKTKKSVIEKMPEYSGPGHGQTMKRGGSHSWEGDANKPKQQLTLSAVVVAPTVSVSPAEDSQTTAKWQAPMTGSH
SQ  LFQSSYNFPQSINLWPPFSLGLTTPTVHTTHTSMAQKSFSPQHNLFPAFYYIPAPLATATAGSAAAQTSVSSASAAQHSP
SQ  KSSENPSTSQPEATAATAMPMPYMAGVMYPHPSLFYAYQPMPFPSVSGAVQMSVQSSGSQSNNNNKSIYTMAPASTTTQK
SQ  PGAFHSITPAELNKPDAPDTLLHTETSPKISVQEAPKKELSDLPSTSARRGSSSDQRNNSNNPKKYTDSNGNSDDMDGSS
SQ  FSSFYSSFIKTTDGSESPPDNEKETKVHKLKPIVEHPEEDQTQHGDG
//
ID  Q03297;
PN  Period circadian protein;
GN  per;
OS  7260;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q03297;
DR  UNIPROT: O18421;
DR  UNIPROT: O18422;
DR  UNIPROT: P91721;
DR  UNIPROT: P91722;
DR  Pfam: PF00989;
DR  PROSITE: PS50112;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044297;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0032922;
GO  GO:0060086;
GO  GO:0007620;
GO  GO:0008340;
GO  GO:0008062;
GO  GO:0043153;
GO  GO:0045475;
GO  GO:0007616;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0045187;
GO  GO:1904059;
GO  GO:0001932;
GO  GO:0006979;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  NKDKSRKKKKPKCIALATATAVSLEGTRESPLPASGSCEKVLQELQDTQQLGEPLVVTETQLSEQLLETEQNEDQNKSEQ
SQ  LAQFPLPTPIVTTLSPGIGPGHDCVGGASGGAVAGGCLVVGAGTDKTSELIPGKLESAGTKPSQERPKEESFCCVISMHD
SQ  GIVLYTTPSISDVLGFPRDMWLGRSFVDFVHHKDRATFASQITTGIPIAESRGCMPKDARSTFCVMLRRYRGLNSGGFGV
SQ  IGRAVNYEPFRLGLTFREAPEEARPDNYMVSNGTNMLLVICATPIKSSYKVPDEILSQKSPKFAIRHTATGIISHVDSAA
SQ  VSALGYLPQDLIGRSIMDFYHHEDLSVMKDTYETVMKKGQTAGASFCSKPYRFLIQNGCFVLLETEWTSFVNPWSRKLEF
SQ  VVGHHRVFQGPKLCNVFETSVSAKPKISEEAQNRNARIKEDIVKLLAETVSRPSDTVKQEVSRRCQALANFMETLMDEIT
SQ  RADLKLDLPHENELTVSERDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKVESSYV
SQ  SSARGEDARSTLSPVQGFEGSGGSGSSGNFTTGSNLHMSSVTNTSNAGTGTSGTGNSGDGGGGGGADGTGSGAAPPVTLT
SQ  ESLLNKHNDEMEKFMLKKHRESRGRSGDKNKKSANEAMKMLEYSGPGPGHGHGIKRGGSHSWEGEANKPKQQLTLNTGGG
SQ  GGGGGGGGGGGGGGLPLFLDVTHTSSSSQNKGPTGVAAGGAGGGVGGGGGSCSGLGGNGNVGSGNGNNSQPSTNQYTQSG
SQ  LPCTQNINLWPPFSVGITTPTSVLSSHTAVPPSSFSPQHSLFPTFYYIPASIAASSPSSTNTNPNRPHKHAHVHSSSEKP
SQ  STSQAAAATMPLQYMTGVMYPHPSLFYTHPAAAAATAMVYQPVPFAGVANPMQLPEQASKNVYTTQPVMVAPPTATNKTQ
SQ  GAFHSITPAPPQRPSSQATSVKAETGSNVAPSDTSKKEVPDSPITPTMGDFTLDQPCNNNATTLKKYTDSNGNSDDMDGS
SQ  SFSSFYSSFIKTTDGSESPPENDKDAKHRKLKSLDQSDNKIVEHPEEDQTQHG
//
ID  Q24767;
PN  Period circadian protein;
GN  per;
OS  7245;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q24767;
DR  UNIPROT: Q26286;
DR  Pfam: PF00989;
DR  PROSITE: PS50112;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0048471;
GO  GO:0090575;
GO  GO:0001228;
GO  GO:0017022;
GO  GO:0046982;
GO  GO:0043565;
GO  GO:0007420;
GO  GO:0071456;
GO  GO:0008347;
GO  GO:0016348;
GO  GO:0008286;
GO  GO:0000122;
GO  GO:0048477;
GO  GO:0045676;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGGESAESTHNTKVSDSAYSNSCSNSQSQRSGSSKSRLSGSHSSGSSGYGGKPSTQASSSDMIIKRNKDKSRKKKKNKG
SQ  AGQGAGQAGQSLISASTSLEGGAEEKPRPSGSGCGVEQQSCRELLQDQQHGEDHSEPKATEQLQQEEGDRSGSESEAERV
SQ  ENAAKSEAAQSFPIPSPLSVTIVPPSMGGCAGVGHAASLDSGLAKLDKTWEAGGPGKVEPVPGVPGTAAAGTGQRGERLK
SQ  EESFCCVISMHDGIVLYTTPSITDVLGYPRDMWLGRSFIDFVHLKDRATFASQITTGIPIAESRGSVPKDTKSTFCVMLR
SQ  RYRGLKSGGFGVIGRPVSYEPFRLGLTFREAPEEARPDNYMVSNGTNMLLVICATPIKSSYKIPDEILSQKSPKFAIRHT
SQ  ATGIISHVDSAAVSALGYLPQDLIGRSIMDFYHQEDLSVMKETYEMVMKKGQTAGASFCSKPYRFLIQNGCYVLLETEWT
SQ  SFVNPWSRKLEFVVGHHRVFQGPKSCNVFEAAPTCKLKMSEEAQSRNTRIKEDIVKRLAETVSRPSDTVKQEVSRRCQAL
SQ  ASFMETLMDEVSRADLKLELPHENELTVSERDSVMLGEISPHHDYYDSKSSTETPPSYNQLNYNENLLRFFNSKPVTAPA
SQ  ELDPPKTEPPEPRGTCVSGASGPMSPVHEGSGGSGSSGNFTTASNIHMSSVTNTSIAGTGGTGTGTGTGTGTGTGTGTGT
SQ  GTGTGTGTGTGNGTNSGTGTGSASSNYRGGSVAIQPVTLTEALLNKHNDEMEKFMLKKHRESRGRSGEKSKKSATDTLKM
SQ  LEYSGPGHGIKRGGSHSWEGEANKPKQQLTLGTDAIKGVVGGSGGVVGTGGGAGVAGGGGTGTGLAGTSDGRLTMSSGAG
SQ  GVVGGPGGAAAAAGVISSVGSSMPGPSSYPTCTQNINLWPPFSVGITPPVHSTHTAMAQSSFSSAGLFPTFYYIPASLTP
SQ  TSPTRSPRMHKHPHKGGPEMPTTSQQAAAAAAQAAQAMPLQYMAGVMYPHPSLFYTHPAAAAATAMMYQPMPFTGMTNAL
SQ  QIPERPLGSQSAYNKSMYTTTPPSMAKKVPGAFHSVTTPSQVQRSSSQSASVNAEPGCSASVSDPCKKEAPGSSPIPSVM
SQ  GDYNSELPCSSSNPANNKKYTDSNGNSDDMDGSSFSSFYSSFIKTTDGSESPPDIEKDPKHRKLKSMSPSDSKIMEHPEE
SQ  DQTQHGDG
//
ID  Q25109;
PN  Period circadian protein;
GN  per;
OS  7255;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q25109;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SKSSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKGESSYVSSAREDARSTLSPVHGFEGSGGSGSSGNFTTGSNV
SQ  RMSSVTNTSNAGTGTSSAGGNGNGGSGASHAPPVTVTLTESLLN
//
ID  Q25221;
PN  Period circadian protein;
GN  per;
OS  34685;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q25221;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SKSSTETPPSYNQLNYNENLQRFFNSKPITAPVDVDPHEVEQSYDASTDARSFRSPLRHFEGSGGSGSSGNFNSGSNLHI
SQ  GSITNTSNTGTGTSSGSVQLITLTESLLN
//
ID  Q25435;
PN  Period circadian protein;
GN  per;
OS  7370;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q25435;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SKSSIETPPSYNQLNYNENLQRFFNSKPVTAPVETDPIKMEQSYSTPANTGSNLSPMQCFEDSGGSGSSRNCTSGSNLNM
SQ  GSVTNTSNTGTGTSSGSAPLVTLTESLLK
//
ID  Q26231;
PN  Period circadian protein;
GN  per;
OS  34679;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q26231;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SKSSTETPPSYNQLNYNENLQRFFNSKPVTAPVEVDPMKNEQSYSISADARNTLSPVQCFEGSGGSGSSGNFTSGSQIHM
SQ  SSITNTSNAGTGTSSGSAQLVSLTESLLN
//
ID  Q26612;
PN  Period circadian protein;
GN  per;
OS  34682;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q26612;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SKSSTETPPSYNQLNYNENLQRFFNSKPATAPVEFDPIKMDQSYNEPAEAECTVSPVQCFEGSGGSGSSGNFTSGSNLNM
SQ  RSVTNTSNTGTGTSSESVPLVTLTEALIS
//
ID  Q27135;
PN  Period circadian protein;
GN  per;
OS  7297;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with Tim is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: Q27135;
DE  Function: Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  SKSSTETPPSYNQLNYNENLLRFFNSKPVTAPVELDPPKLESSYVSSAREDARSTLSPVHGFEGSGGSGSSGNFTTGSNV
SQ  RMSSVTNTSNAGTGTSGGGNSAGGASGGVGAVGVAANAPLVTVTLTESLLN
//
ID  Q9P6S6;
PN  PGA2-homolog C27.01c;
GN  SPBC27;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Single- pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9P6S6;
DR  UNIPROT: P78948;
DR  Pfam: PF07543;
DE  Function: Involved processing and trafficking glycosylated proteins. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q10169; IntAct: EBI-21244123; Score: 0.37
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006886;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGFDVAGYLQSYSLKDWIRIIVYVGGYMLIRPYLMKLGAKIQEREHRKSLLEGEVDGTLDPEMTHGTKPKEHGEFDTDDE
SQ  EEEENPDAEFRWGYSARRRIRKQREEYFKNQDKSPLDAYADDDEDIEEHLED
//
ID  P53903;
PN  Processing of GAS1 and ALP protein 2;
GN  PGA2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14690591}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:14690591}; Single- pass membrane protein {ECO:0000255}.
DR  UNIPROT: P53903;
DR  UNIPROT: D6W133;
DR  Pfam: PF07543;
DE  Function: Involved in the processing and trafficking of GAS1 and PHO8 glycosylated proteins. {ECO:0000269|PubMed:16943325}.
DE  Reference Proteome: Yes;
DE  Interaction: P15790; IntAct: EBI-7963857; Score: 0.40
DE  Interaction: P36076; IntAct: EBI-8224868; Score: 0.22
DE  Interaction: Q12154; IntAct: EBI-2345001; Score: 0.37
DE  Interaction: Q08234; IntAct: EBI-20814547; Score: 0.37
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSEVAETWVDTWMAKLVNYDYKHFIRLVIIVGGYLLLRNIASRELAKKQLAAQVEKDKRDKEEKRSKDLIDKPDDAATAE
SQ  TTSFGWGKKTRRRVKRQQELFENALEEAKRRNQGLDPDSDADIEELLEE
//
ID  Q9H7Z7;
PN  Prostaglandin E synthase 2 truncated form;
GN  PTGES2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000269|PubMed:12835322}; Single-pass membrane protein {ECO:0000255}. [Prostaglandin E synthase 2 truncated form]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12835322}. Note=Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. The truncated form is cytoplasmic and is enriched in the perinuclear region. {ECO:0000269|PubMed:12835322}.
DR  UNIPROT: Q9H7Z7;
DR  UNIPROT: Q53EW9;
DR  UNIPROT: Q5SYV6;
DR  UNIPROT: Q96GI0;
DR  UNIPROT: Q96GL2;
DR  Pfam: PF13417;
DR  PROSITE: PS00195;
DR  PROSITE: PS51354;
DR  PROSITE: PS50405;
DR  OMIM: 608152;
DR  DisGeNET: 80142;
DE  Function: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (in vitro) (PubMed:12804604, PubMed:18198127, PubMed:17585783). The biological function and the GSH- dependent property of PTGES2 is still under debate (PubMed:18198127, PubMed:17585783). In vivo, PTGES2 could form a complex with GSH and heme and would not participate in PGE2 synthesis but would catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy- 5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) (PubMed:17585783) (By similarity). {ECO:0000250|UniProtKB:Q9N0A4, ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:17585783, ECO:0000269|PubMed:18198127}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: P0C6X7; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q01780; IntAct: EBI-373752; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.35
DE  Interaction: P16104; IntAct: EBI-2564373; Score: 0.35
DE  Interaction: Q5NFN4; IntAct: EBI-2803788; Score: 0.00
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-6452059; Score: 0.40
DE  Interaction: Q5VU69; IntAct: EBI-10308949; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q13296; IntAct: EBI-21513670; Score: 0.35
DE  Interaction: P61421; IntAct: EBI-21518921; Score: 0.35
DE  Interaction: P80370; IntAct: EBI-21555448; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-21684279; Score: 0.35
DE  Interaction: O14949; IntAct: EBI-21689809; Score: 0.35
DE  Interaction: O60518; IntAct: EBI-21713634; Score: 0.35
DE  Interaction: Q9UG63; IntAct: EBI-21764870; Score: 0.35
DE  Interaction: Q8N140; IntAct: EBI-21773860; Score: 0.35
DE  Interaction: E9PK12; IntAct: EBI-21841096; Score: 0.35
DE  Interaction: Q0VDI3; IntAct: EBI-21891210; Score: 0.35
DE  Interaction: Q6UWI4; IntAct: EBI-21898440; Score: 0.35
DE  Interaction: O75208; IntAct: EBI-21930142; Score: 0.35
DE  Interaction: O00483; IntAct: EBI-21930681; Score: 0.35
DE  Interaction: Q9C002; IntAct: EBI-21935327; Score: 0.35
DE  Interaction: P07550; IntAct: EBI-20801899; Score: 0.37
DE  Interaction: A0A0H3LG06; IntAct: EBI-25401076; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
GO  GO:0035578;
GO  GO:0005829;
GO  GO:0005576;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0036134;
GO  GO:0003677;
GO  GO:0043295;
GO  GO:0020037;
GO  GO:0016829;
GO  GO:0050220;
GO  GO:0019371;
GO  GO:0006629;
GO  GO:0045893;
GO  GO:0046903;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLGAAALALGGALGLYHTARWHL
SQ  RAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRAFLDFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQ
SQ  QLNDSSVIISALKTYLVSGQPLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADD
SQ  WLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNVREDLYEAADKWVAAVGK
SQ  DRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAITEASPAH
//
ID  Q9N0A4;
PN  Prostaglandin E synthase 2 truncated form;
GN  PTGES2;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H7Z7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9H7Z7}. [Prostaglandin E synthase 2 truncated form]: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H7Z7}. Note=Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. The truncated form is cytoplasmic and is enriched in the perinuclear region. {ECO:0000250|UniProtKB:Q9H7Z7}.
DR  UNIPROT: Q9N0A4;
DR  UNIPROT: Q5DI73;
DR  PDB: 1Z9H;
DR  PDB: 2PBJ;
DR  Pfam: PF13417;
DR  PROSITE: PS00195;
DR  PROSITE: PS51354;
DR  PROSITE: PS50405;
DE  Function: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (in vitro) (PubMed:11866447, PubMed:23426368). The biological function and the GSH-dependent property of PTGES2 is still under debate (PubMed:23426368). In vivo, PTGES2 could form a complex with GSH and heme and would not participate in PGE2 synthesis but would catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) (PubMed:23426368). {ECO:0000269|PubMed:11866447, ECO:0000269|PubMed:23426368}.
DE  Reference Proteome: Yes;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0036134;
GO  GO:0043295;
GO  GO:0020037;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0050220;
GO  GO:0001516;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPATRVVRALWTGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGQGPVAAARKGSPRLLGAAALALGGALGLYHTARWHL
SQ  HAQDLHAERSAVQLSLSSRLQLTLYQYKTCPFCSKVRAFLDFHALPYQVVEVNPVLRAEIKFSSYRKVPILVAQEGESSQ
SQ  QLNDSSVIISALKTYLVSGQPLEEIITYYPAMKAVNDQGKEVTEFGNKYWLMLNEKEAQQVYSGKEARTEEMKWRQWADD
SQ  WLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNVREDLYEAADKWVAAVGK
SQ  DRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAITEASPAH
//
ID  O62698;
PN  Prostaglandin G/H synthase 2;
GN  PTGS2;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
DR  UNIPROT: O62698;
DR  UNIPROT: O46517;
DR  UNIPROT: O62665;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S- RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11- diHETE) (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R- lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:P35354, ECO:0000250|UniProtKB:Q05769}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0043005;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0016702;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0071347;
GO  GO:0019371;
GO  GO:0006954;
GO  GO:0000212;
GO  GO:0001550;
GO  GO:0040019;
GO  GO:1904146;
GO  GO:1900195;
GO  GO:0001934;
GO  GO:0001516;
GO  GO:0008217;
GO  GO:0150077;
GO  GO:0006979;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35354};
SQ  MLARALLLCAAVALSGAANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTH
SQ  FKGVWNIVNKISFLRNMIMRYVLTSRSHLIESPPTYNVHYSYKSWEAFSNLSYYTRALPPVPDDCPTPMGVKGRKELPDS
SQ  KEVVKKVLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTDFERGPAFTKGKNHGVDLSHIYGESLERQHKLRLFKDGKMKY
SQ  QMINGEMYPPTVKDTQVEMIYPPHVPEHLKFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRL
SQ  ILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDVFQIDGQEYNYQQFIYNNSVL
SQ  LEHGLTQFVESFTRQRAGRVAGGRNLPVAVEKVSKASIDQSREMKYQSFNEYRKRFLVKPYESFEELTGEKEMAAELEAL
SQ  YGDIDAMEFYPALLVEKPRPDAIFGETMVEAGAPFSLKGLMGNPICSPEYWKPSTFGGEVGFKIINTASIQSLICSNVKG
SQ  CPFTSFSVQDTHLTKTVTINASSSHSGLDDINPTVLLKERSTEL
//
ID  P70682;
PN  Prostaglandin G/H synthase 2;
GN  PTGS2;
OS  10141;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
DR  UNIPROT: P70682;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S- RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11- diHETE). {ECO:0000250|UniProtKB:P35354}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0051213;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0019371;
GO  GO:0006954;
GO  GO:0001516;
GO  GO:0008217;
GO  GO:0150077;
GO  GO:0006979;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35354};
SQ  MLARALLLCAALALGQAANPCCSNPCQNRGECLSVGFDRYKCDCTRTGYYGENCTTPEFLTRIKLLLKPTPNTVHYILTH
SQ  FKGVWNIVNNIPFLRNAIMIYVLTSRSHLIDSPPTYNAHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDS
SQ  NEVLEKVLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKSDQKRGPAFTTGLAHGVDLSHIYGETLDRQHKLRLFKDGKMKY
SQ  QIIDGEMYPPTVKETQVEMMYPPYIPEHARFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDERLFQTSRL
SQ  ILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLLPDTFQIDDQVYNFQQFLYNNSIL
SQ  VEHGLTQFVESFTKQIAGRVAGGRNVPLAVQRVAKASIEHSRKMKYQSLNEYRKRFLMKPYTSFEELTGEKEMAAGLEAL
SQ  YGDIDAMELYPALLVEKPRPDAIFGETMVEMGAPFSLKGLMGNPICSPHYWKPSTFGGEVGFQIVNTASIQSLICNNVKG
SQ  CPVTAFNLPDPQLAKTVTINASASHSRLEDLSPTVLLKGRSTEL
//
ID  O19183;
PN  Prostaglandin G/H synthase 2;
GN  PTGS2;
OS  9796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
DR  UNIPROT: O19183;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S- RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11- diHETE). {ECO:0000250|UniProtKB:P35354}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0043005;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0016702;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0019371;
GO  GO:0006954;
GO  GO:0001516;
GO  GO:0008217;
GO  GO:0150077;
GO  GO:0006979;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35354};
SQ  MLARALLLCVALALGHAANPCCSNPCQNRGVCMSVGFDQYQCDCTRTGFYGENCSTPEFLTRIKLFLKPTPNTVHYILTH
SQ  FKGVWNIVNSFPFLRNAVMKYVLVSRSHLIESPPTYNAQYGYKSWESFSNLSYYTRALPPVADGCPTPMGVKGKKELPDS
SQ  KEIVEKFLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDPKRGPAFTKGLGHGVDLSHIYGETLDRQHKLRLFKDGKMKY
SQ  QIINGEVYPPTVKDTQVEMIYPPHIPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDERLFQTSRL
SQ  ILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDTFQIDDQEYNFQQFLYNNSIL
SQ  LEHGLTQFVESFSRQIAGRVAGGRNVPAAAQKIAKASIDQSREMKYQSLNEYRKRFRLTPYKSFEELTGEKEMAAELEAL
SQ  YGDIDAMELYPALLVEKPRPDAIFGETMVELGAPFSLKGLLGNPICSPDYWKPSTFGGEVGFKIINTASIQSLICNNVKG
SQ  CPFTAFSVQDPQLSKAVTINASASHSGLDDVNPTVLLKERSTEL
//
ID  P35354;
PN  Prostaglandin G/H synthase 2;
GN  PTGS2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Nucleus inner membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Nucleus outer membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000269|PubMed:9545330}.
DR  UNIPROT: P35354;
DR  UNIPROT: A8K802;
DR  UNIPROT: Q16876;
DR  PDB: 5F19;
DR  PDB: 5F1A;
DR  PDB: 5IKQ;
DR  PDB: 5IKR;
DR  PDB: 5IKT;
DR  PDB: 5IKV;
DR  PDB: 5KIR;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DR  OMIM: 600262;
DR  DisGeNET: 5743;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response (PubMed:7947975, PubMed:7592599, PubMed:9261177, PubMed:16373578, PubMed:22942274, PubMed:26859324, PubMed:27226593, PubMed:11939906, PubMed:19540099). The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes (PubMed:7947975, PubMed:7592599, PubMed:9261177, PubMed:16373578, PubMed:22942274, PubMed:26859324, PubMed:27226593). This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons (PubMed:7947975, PubMed:7592599, PubMed:9261177, PubMed:16373578, PubMed:22942274, PubMed:26859324, PubMed:27226593). Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3- series prostaglandins (PubMed:11939906, PubMed:19540099). In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids (PubMed:27642067). Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response (PubMed:22942274). Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols (PubMed:11034610, PubMed:11192938, PubMed:9048568, PubMed:9261177). Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation (PubMed:12391014). Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D- series resolvins (RvDs) (PubMed:12391014). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S- RvE2 (PubMed:21206090). In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13- series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection (PubMed:26236990). In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE) (PubMed:22068350, PubMed:26282205). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:Q05769, ECO:0000269|PubMed:11034610, ECO:0000269|PubMed:11192938, ECO:0000269|PubMed:11939906, ECO:0000269|PubMed:12391014, ECO:0000269|PubMed:16373578, ECO:0000269|PubMed:21206090, ECO:0000269|PubMed:22068350, ECO:0000269|PubMed:22942274, ECO:0000269|PubMed:26236990, ECO:0000269|PubMed:26282205, ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27642067, ECO:0000269|PubMed:7592599, ECO:0000269|PubMed:7947975, ECO:0000269|PubMed:9048568, ECO:0000269|PubMed:9261177, ECO:0000303|PubMed:19540099}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9WMX2; IntAct: EBI-9083640; Score: 0.37
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.35
DE  Interaction: O14936; IntAct: EBI-21252062; Score: 0.37
DE  Interaction: Q9H0V9; IntAct: EBI-21845712; Score: 0.35
DE  Interaction: P35354; IntAct: EBI-15578876; Score: 0.40
DE  Interaction: P04439; IntAct: EBI-20910216; Score: 0.40
DE  Interaction: Q86V38; IntAct: EBI-25846357; Score: 0.56
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0043231;
GO  GO:0043005;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0032991;
GO  GO:0019899;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0016702;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0042803;
GO  GO:0007568;
GO  GO:0001525;
GO  GO:0030282;
GO  GO:0050873;
GO  GO:0071318;
GO  GO:0071498;
GO  GO:0034605;
GO  GO:0071456;
GO  GO:0071284;
GO  GO:0071260;
GO  GO:0071471;
GO  GO:0034644;
GO  GO:0019371;
GO  GO:0046697;
GO  GO:0007566;
GO  GO:0042633;
GO  GO:0006954;
GO  GO:0007612;
GO  GO:0035633;
GO  GO:0007613;
GO  GO:0051926;
GO  GO:0045786;
GO  GO:0008285;
GO  GO:0043154;
GO  GO:1902219;
GO  GO:0045986;
GO  GO:0032227;
GO  GO:0030728;
GO  GO:0043065;
GO  GO:0090336;
GO  GO:0090050;
GO  GO:0031622;
GO  GO:0090271;
GO  GO:0045429;
GO  GO:0033138;
GO  GO:0090362;
GO  GO:0031394;
GO  GO:0042307;
GO  GO:0048661;
GO  GO:0045987;
GO  GO:0031915;
GO  GO:0051968;
GO  GO:0071636;
GO  GO:0010575;
GO  GO:0045907;
GO  GO:0001516;
GO  GO:0032310;
GO  GO:0008217;
GO  GO:0050727;
GO  GO:0150077;
GO  GO:1990776;
GO  GO:0032355;
GO  GO:0070542;
GO  GO:0009750;
GO  GO:0051384;
GO  GO:0032496;
GO  GO:0010226;
GO  GO:0010042;
GO  GO:0009624;
GO  GO:0006979;
GO  GO:0034612;
GO  GO:0033280;
GO  GO:0009410;
GO  GO:0019233;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MLARALLLCAVLALSHTANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFLTRIKLFLKPTPNTVHYILTH
SQ  FKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNADYGYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDS
SQ  NEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKY
SQ  QIIDGEMYPPTVKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRL
SQ  ILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQNRIAAEFNTLYHWHPLLPDTFQIHDQKYNYQQFIYNNSIL
SQ  LEHGITQFVESFTRQIAGRVAGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEAL
SQ  YGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEVGFQIINTASIQSLICNNVKG
SQ  CPFTSFSVPDPELIKTVTINASSSRSGLDDINPTVLLKERSTEL
//
ID  Q05769;
PN  Prostaglandin G/H synthase 2;
GN  Ptgs2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:9545330}; Peripheral membrane protein. Nucleus inner membrane {ECO:0000305|PubMed:9545330}; Peripheral membrane protein. Nucleus outer membrane {ECO:0000305|PubMed:9545330}; Peripheral membrane protein. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
DR  UNIPROT: Q05769;
DR  UNIPROT: Q543K3;
DR  PDB: 1CVU;
DR  PDB: 1CX2;
DR  PDB: 1DDX;
DR  PDB: 1PXX;
DR  PDB: 3HS5;
DR  PDB: 3HS6;
DR  PDB: 3HS7;
DR  PDB: 3KRK;
DR  PDB: 3LN0;
DR  PDB: 3LN1;
DR  PDB: 3MDL;
DR  PDB: 3MQE;
DR  PDB: 3NT1;
DR  PDB: 3NTB;
DR  PDB: 3NTG;
DR  PDB: 3OLT;
DR  PDB: 3OLU;
DR  PDB: 3PGH;
DR  PDB: 3Q7D;
DR  PDB: 3QH0;
DR  PDB: 3QMO;
DR  PDB: 3RR3;
DR  PDB: 3TZI;
DR  PDB: 4COX;
DR  PDB: 4E1G;
DR  PDB: 4FM5;
DR  PDB: 4M10;
DR  PDB: 4M11;
DR  PDB: 4OTJ;
DR  PDB: 4OTY;
DR  PDB: 4PH9;
DR  PDB: 4RRW;
DR  PDB: 4RRX;
DR  PDB: 4RRY;
DR  PDB: 4RRZ;
DR  PDB: 4RS0;
DR  PDB: 4RUT;
DR  PDB: 4Z0L;
DR  PDB: 5COX;
DR  PDB: 5FDQ;
DR  PDB: 5JVY;
DR  PDB: 5JVZ;
DR  PDB: 5JW1;
DR  PDB: 5W58;
DR  PDB: 6BL3;
DR  PDB: 6BL4;
DR  PDB: 6COX;
DR  PDB: 6OFY;
DR  PDB: 6V3R;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response (PubMed:22942274, PubMed:12925531, PubMed:20463020, PubMed:20810665, PubMed:21489986). The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons (PubMed:22942274, PubMed:12925531, PubMed:20463020, PubMed:20810665, PubMed:21489986). Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3- series prostaglandins (By similarity). In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids (By similarity). Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response (By similarity). Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols (By similarity). Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection (By similarity). In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE) (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (PubMed:29662056). {ECO:0000250|UniProtKB:P35354, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:22942274, ECO:0000269|PubMed:29662056}.
DE  Reference Proteome: Yes;
DE  Interaction: P16054; IntAct: EBI-298523; Score: 0.35
DE  Interaction: Q05769; IntAct: EBI-5324876; Score: 0.44
DE  Interaction: Q9Z0J4; IntAct: EBI-15717353; Score: 0.40
DE  Interaction: A0A0F6B5H5; IntAct: EBI-27034767; Score: 0.46
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0043231;
GO  GO:0043005;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0032991;
GO  GO:0019899;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0016702;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0042803;
GO  GO:0007568;
GO  GO:0001525;
GO  GO:0030282;
GO  GO:0050873;
GO  GO:0071318;
GO  GO:0071498;
GO  GO:0034605;
GO  GO:0071456;
GO  GO:0071284;
GO  GO:0071260;
GO  GO:0071471;
GO  GO:0034644;
GO  GO:0019371;
GO  GO:0046697;
GO  GO:0007566;
GO  GO:0042633;
GO  GO:0006954;
GO  GO:0030216;
GO  GO:0007612;
GO  GO:0035633;
GO  GO:0007613;
GO  GO:0043066;
GO  GO:0051926;
GO  GO:0045786;
GO  GO:0008285;
GO  GO:0043154;
GO  GO:1902219;
GO  GO:0045986;
GO  GO:0032227;
GO  GO:0030728;
GO  GO:0043065;
GO  GO:0090336;
GO  GO:0010942;
GO  GO:0090050;
GO  GO:0008284;
GO  GO:0031622;
GO  GO:0090271;
GO  GO:0045429;
GO  GO:0033138;
GO  GO:0090362;
GO  GO:0031394;
GO  GO:0042307;
GO  GO:0048661;
GO  GO:0045987;
GO  GO:0031915;
GO  GO:0051968;
GO  GO:0071636;
GO  GO:0010575;
GO  GO:0045907;
GO  GO:0001516;
GO  GO:0032310;
GO  GO:0008217;
GO  GO:0042127;
GO  GO:0150077;
GO  GO:1990776;
GO  GO:0034097;
GO  GO:0032355;
GO  GO:0070542;
GO  GO:0009750;
GO  GO:0051384;
GO  GO:0032496;
GO  GO:0010226;
GO  GO:0010042;
GO  GO:0009624;
GO  GO:0006979;
GO  GO:0034612;
GO  GO:0033280;
GO  GO:0009410;
GO  GO:0019233;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MLFRAVLLCAALGLSQAANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTH
SQ  FKGVWNIVNNIPFLRSLIMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDS
SQ  KEVLEKVLLRREFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLNHIYGETLDRQHKLRLFKDGKLKY
SQ  QVIGGEVYPPTVKDTQVEMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWGDEQLFQTSRL
SQ  ILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLLPDTFNIEDQEYSFKQFLYNNSIL
SQ  LEHGLTQFVESFTRQIAGRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEELTGEKEMAAELKAL
SQ  YSDIDVMELYPALLVEKPRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFGGEVGFKIINTASIQSLICNNVKG
SQ  CPFTSFNVQDPQPTKTATINASASHSRLDDINPTVLIKRRSTEL
//
ID  O62725;
PN  Prostaglandin G/H synthase 2;
GN  PTGS2;
OS  452646;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
DR  UNIPROT: O62725;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S- RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11- diHETE). {ECO:0000250|UniProtKB:P35354}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0051213;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0019371;
GO  GO:0006954;
GO  GO:0001516;
GO  GO:0008217;
GO  GO:0150077;
GO  GO:0006979;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35354};
SQ  MLARAGLLCASLSPPHAANPCCSNPCQNQGVCMSIGFDQYMCDCSRTGFYGENCSTPEFLTRVKLLLKPTPNTVHYILTH
SQ  FKGVWNIVNKIPFLADVIMKYVRTSRSHCIEPPPTYNVHYAYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDS
SQ  KEIVEKFLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDHKRGPGFTKGLGHGVDLSHVYGETLDRQHKLRLFKDGKMKY
SQ  QVIDGEVYPPTVKDTQVEMIYPPHVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEQGEWDDERLFRRSRL
SQ  ILIGETIKIVIEDYVRHLSGYHFSLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDTLQIDDQEYNFQQFVYNNSIL
SQ  LEHGLTQFGESFSRQIAGRVAGGRNVPAAVQQEQRASIDQSRQMKYQSLNEYRKRFSVKPYASFEELTGEKEMAGELKAL
SQ  YQDIDAMELYPALLVEKPRPDAIFGETMVEIGAPFSLKGLMGNPICSPDYWKPSHFGGEVGFKIINTASIQSLICNNVKG
SQ  CPFTAFSVQDPQLTKTVTINGSSSHSGLDDINPTVLLKERSTEL
//
ID  O02768;
PN  Prostaglandin G/H synthase 2;
GN  PTGS2;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
DR  UNIPROT: O02768;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S- RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11- diHETE) (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R- lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:P35354, ECO:0000250|UniProtKB:Q05769}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0043005;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0051213;
GO  GO:0019899;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0042803;
GO  GO:0050873;
GO  GO:0071498;
GO  GO:0071456;
GO  GO:0071471;
GO  GO:0019371;
GO  GO:0046697;
GO  GO:0007566;
GO  GO:0006954;
GO  GO:0043154;
GO  GO:1902219;
GO  GO:0090336;
GO  GO:0031622;
GO  GO:0033138;
GO  GO:0031394;
GO  GO:0001516;
GO  GO:0032310;
GO  GO:0008217;
GO  GO:0042127;
GO  GO:0150077;
GO  GO:0009624;
GO  GO:0006979;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35354};
SQ  MLARALLLCAAVALSHAANPCCSNPCQNRGVCMTMGFDQYKCDCTRTGFYGENCSTPEFLTRIKLLLKPTPDTVHYILTH
SQ  FKGVWNIVNSIPFLRNSIMKYVLTSRSHMIDSPPTYNVHYNYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDS
SQ  KDVVEKLLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDLKRGPAFTKGLGHGVDLNHIYGETLDRQHKLRLFKDGKMKY
SQ  QVIDGEVYPPTVKDTQVEMIYPPHIPAHLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDEQLFQTSRL
SQ  ILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDTFQIDDQQYNYQQFLYNNSIL
SQ  LEHGLTQFVESFTRQIAGRVAGGRNVPPAVQKVAKASIDQSRQMKYQSLNEYRKRFLLKPYESFEELTGEKEMAAELEAL
SQ  YGDIDAVELYPALLVERPRPDAIFGESMVEMGAPFSLKGLMGNPICSPNYWKPSTFGGEVGFKIVNTASIQSLICNNVKG
SQ  CPFTSFNVPDPQLTKTVTINASASHSRLEDINPTVLLKGRSTEL
//
ID  P35355;
PN  Prostaglandin G/H synthase 2;
GN  Ptgs2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
DR  UNIPROT: P35355;
DR  UNIPROT: Q64379;
DR  UNIPROT: Q925V4;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S- RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11- diHETE) (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R- lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:P35354, ECO:0000250|UniProtKB:Q05769}.
DE  Reference Proteome: Yes;
DE  Interaction: P49286; IntAct: EBI-11578730; Score: 0.00
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0043005;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0032991;
GO  GO:0019899;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0016702;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0042803;
GO  GO:0007568;
GO  GO:0001525;
GO  GO:0030282;
GO  GO:0050873;
GO  GO:0071318;
GO  GO:0071498;
GO  GO:0034605;
GO  GO:0071456;
GO  GO:0071284;
GO  GO:0071260;
GO  GO:0071471;
GO  GO:0034644;
GO  GO:0019371;
GO  GO:0046697;
GO  GO:0007566;
GO  GO:0042633;
GO  GO:0006954;
GO  GO:0007612;
GO  GO:0035633;
GO  GO:0007613;
GO  GO:0043066;
GO  GO:0051926;
GO  GO:0045786;
GO  GO:0008285;
GO  GO:0043154;
GO  GO:1902219;
GO  GO:0045986;
GO  GO:0032227;
GO  GO:0030728;
GO  GO:0043065;
GO  GO:0090336;
GO  GO:0010942;
GO  GO:0090050;
GO  GO:0008284;
GO  GO:0031622;
GO  GO:0090271;
GO  GO:0045429;
GO  GO:0033138;
GO  GO:0090362;
GO  GO:0031394;
GO  GO:0042307;
GO  GO:0048661;
GO  GO:0045987;
GO  GO:0031915;
GO  GO:0051968;
GO  GO:0071636;
GO  GO:0010575;
GO  GO:0045907;
GO  GO:0001516;
GO  GO:0032310;
GO  GO:0008217;
GO  GO:0042127;
GO  GO:0150077;
GO  GO:1990776;
GO  GO:0034097;
GO  GO:0032355;
GO  GO:0070542;
GO  GO:0009750;
GO  GO:0051384;
GO  GO:0032496;
GO  GO:0010226;
GO  GO:0010042;
GO  GO:0009624;
GO  GO:0014070;
GO  GO:0010033;
GO  GO:0010243;
GO  GO:0006979;
GO  GO:0009314;
GO  GO:0034612;
GO  GO:0033280;
GO  GO:0009410;
GO  GO:0019233;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35354};
SQ  MLFRAVLLCAALALSHAANPCCSNPCQNRGECMSIGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTH
SQ  FKGVWNIVNNIPFLRNSIMRYVLTSRSHLIDSPPTYNVHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDS
SQ  KEVLEKVLLRREFIPDPQGTNMMFAFFAQHFTHQFFKTDQKRGPGFTRGLGHGVDLNHVYGETLDRQHKLRLFQDGKLKY
SQ  QVIGGEVYPPTVKDTQVDMIYPPHVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWDDERLFQTSRL
SQ  ILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLLPDTFNIEDQEYTFKQFLYNNSIL
SQ  LEHGLAHFVESFTRQIAGRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEELTGEKEMAAELKAL
SQ  YHDIDAMELYPALLVEKPRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFGGEVGFRIINTASIQSLICNNVKG
SQ  CPFASFNVQDPQPTKTATINASASHSRLDDINPTVLIKRRSTEL
//
ID  P79208;
PN  Prostaglandin G/H synthase 2;
GN  PTGS2;
OS  9940;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
DR  UNIPROT: P79208;
DR  Pfam: PF03098;
DR  Pfam: PF00008;
DR  PROSITE: PS50026;
DR  PROSITE: PS50292;
DE  Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response (PubMed:10438452). The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes (PubMed:10438452). This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S- stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons (By similarity). Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins (By similarity). In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids (By similarity). Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n- 3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols (By similarity). Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs) (By similarity). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2 (By similarity). In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection (By similarity). In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE) (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:P35354, ECO:0000250|UniProtKB:Q05769, ECO:0000269|PubMed:10438452}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0051213;
GO  GO:0020037;
GO  GO:0046872;
GO  GO:0004601;
GO  GO:0004666;
GO  GO:0019371;
GO  GO:0006954;
GO  GO:0001516;
GO  GO:0008217;
GO  GO:0150077;
GO  GO:0006979;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P35354};
SQ  MLARALLLCAAVVCGAANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPDTVHYILTHF
SQ  KGVWNIVNKISFLRNMIMRYVLTSRSHLIESPPTYNVHYSYKSWEAFSNLSYYTRALPPVPDDCPTPMGVKGRKELPDSK
SQ  EVVKKVLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTDIERGPAFTKGKNHGVDLSHVYGESLERQHNRRLFKDGKMKYQ
SQ  MINGEMYPPTVKDTQVEMIYPPHIPEHLKFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLI
SQ  LIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDVFQIDGQEYNYQQFIYNNSVLL
SQ  EHGVTQFVESFTRQIAGRVAGRRNLPAAVEKVSKASLDQSREMKYQSFNEYRKRFLLKPYESFEELTGEKEMAAELEALY
SQ  GDIDAMELYPALLVEKPAPDAIFGETMVEAGAPFSLKGLMGNPICSPEYWKPSTFGGEVGFKIINTASIQSLICSNVKGC
SQ  PFTSFSVQDAHLTKTVTINASSSHSGLDDINPTVLLKERSTEL
//
ID  O15173;
PN  Membrane-associated progesterone receptor component 2;
GN  PGRMC2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Membrane {ECO:0000305|PubMed:23793472}; Single- pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:27754849, ECO:0000269|PubMed:28111073}. Endoplasmic reticulum {ECO:0000269|PubMed:27754849}.
DR  UNIPROT: O15173;
DR  UNIPROT: Q569H1;
DR  Pfam: PF00173;
DR  OMIM: 607735;
DR  DisGeNET: 10424;
DE  Function: Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (By similarity). May serve as a universal non-classical progesterone receptor in the uterus (Probable). Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus (By similarity). Plays a role in adipocyte function and systemic glucose homeostasis (PubMed:28111073). In brown fat, which has a high demand for heme, delivery of labile heme in the nucleus regulates the activity of heme-responsive transcriptional repressors such as NR1D1 and BACH1 (By similarity). {ECO:0000250|UniProtKB:Q80UU9, ECO:0000269|PubMed:28111073, ECO:0000305|PubMed:28396637}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O14681; IntAct: EBI-24712104; Score: 0.56
DE  Interaction: Q14164; IntAct: EBI-1083472; Score: 0.00
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P03246; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06461; IntAct: EBI-11723785; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P06927; IntAct: EBI-11724813; Score: 0.35
DE  Interaction: P0CK49; IntAct: EBI-11725356; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: P0CK58; IntAct: EBI-11732874; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: Q2MG95; IntAct: EBI-11733653; Score: 0.35
DE  Interaction: Q5HYA8; IntAct: EBI-11367583; Score: 0.27
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11372136; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q9WMX2; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: Q9NWU2; IntAct: EBI-12450239; Score: 0.51
DE  Interaction: Q96G75; IntAct: EBI-12452053; Score: 0.51
DE  Interaction: O95429; IntAct: EBI-24341628; Score: 0.56
DE  Interaction: Q6UX40; IntAct: EBI-24668603; Score: 0.56
DE  Interaction: Q01453; IntAct: EBI-24674117; Score: 0.56
DE  Interaction: Q8N5I4; IntAct: EBI-24674227; Score: 0.56
DE  Interaction: O60906; IntAct: EBI-24683333; Score: 0.56
DE  Interaction: Q14656; IntAct: EBI-24687401; Score: 0.56
DE  Interaction: Q9P0L0; IntAct: EBI-24691023; Score: 0.56
DE  Interaction: P01031; IntAct: EBI-24694240; Score: 0.56
DE  Interaction: Q13021; IntAct: EBI-24695750; Score: 0.56
DE  Interaction: Q8IVQ6; IntAct: EBI-24706532; Score: 0.56
DE  Interaction: P59542; IntAct: EBI-24708148; Score: 0.56
DE  Interaction: Q7RTY0; IntAct: EBI-24708883; Score: 0.56
DE  Interaction: Q9NZ01; IntAct: EBI-24711415; Score: 0.56
DE  Interaction: O43681; IntAct: EBI-24715630; Score: 0.56
DE  Interaction: Q86UD5; IntAct: EBI-24720671; Score: 0.56
DE  Interaction: Q8IWU4; IntAct: EBI-24722592; Score: 0.56
DE  Interaction: Q8IWB1; IntAct: EBI-23781080; Score: 0.56
DE  Interaction: O14569; IntAct: EBI-24726780; Score: 0.56
DE  Interaction: Q5RI15; IntAct: EBI-24727330; Score: 0.56
DE  Interaction: O00264; IntAct: EBI-24738362; Score: 0.56
DE  Interaction: O76064; IntAct: EBI-23831845; Score: 0.56
DE  Interaction: Q9Y5Y5; IntAct: EBI-23837903; Score: 0.56
DE  Interaction: Q9H2H9; IntAct: EBI-24767413; Score: 0.56
DE  Interaction: Q9H2L4; IntAct: EBI-24768625; Score: 0.56
DE  Interaction: O95159; IntAct: EBI-24772852; Score: 0.56
DE  Interaction: O60636; IntAct: EBI-24779563; Score: 0.56
DE  Interaction: P11215; IntAct: EBI-24786003; Score: 0.56
DE  Interaction: Q9UBY5; IntAct: EBI-24793347; Score: 0.56
DE  Interaction: Q9BWQ6; IntAct: EBI-24796209; Score: 0.56
DE  Interaction: P02787; IntAct: EBI-24797200; Score: 0.56
DE  Interaction: Q9H3K2; IntAct: EBI-24797448; Score: 0.56
DE  Interaction: P78329; IntAct: EBI-24798035; Score: 0.56
DE  Interaction: Q96H72; IntAct: EBI-25284904; Score: 0.56
DE  Interaction: Q96JF0; IntAct: EBI-25286104; Score: 0.56
DE  Interaction: Q96PS8; IntAct: EBI-24548121; Score: 0.56
DE  Interaction: Q7L5A8; IntAct: EBI-25146219; Score: 0.56
DE  Interaction: Q9H9B4; IntAct: EBI-24642361; Score: 0.56
DE  Interaction: Q13277; IntAct: EBI-25147430; Score: 0.56
DE  Interaction: Q96GQ5; IntAct: EBI-24650336; Score: 0.56
DE  Interaction: Q8N2M4; IntAct: EBI-24655777; Score: 0.56
DE  Interaction: I3L0A0; IntAct: EBI-24658689; Score: 0.56
DE  Interaction: Q9H0Q3; IntAct: EBI-24746517; Score: 0.56
DE  Interaction: Q96HH6; IntAct: EBI-25185187; Score: 0.56
DE  Interaction: Q96IV6; IntAct: EBI-24774155; Score: 0.56
DE  Interaction: O00124; IntAct: EBI-25192578; Score: 0.56
DE  Interaction: A0A024RCD1; IntAct: EBI-24790520; Score: 0.56
DE  Interaction: Q9Y342; IntAct: EBI-24803718; Score: 0.56
DE  Interaction: Q9BTX3; IntAct: EBI-24803996; Score: 0.56
DE  Interaction: Q9P0S3; IntAct: EBI-24804382; Score: 0.56
DE  Interaction: Q6ZPD8; IntAct: EBI-24804564; Score: 0.56
DE  Interaction: Q8N661; IntAct: EBI-25218050; Score: 0.56
DE  Interaction: Q6N075; IntAct: EBI-24807339; Score: 0.56
DE  Interaction: Q8TDV0; IntAct: EBI-25267216; Score: 0.56
DE  Interaction: P22315; IntAct: EBI-12523269; Score: 0.50
DE  Interaction: Q78IK4; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q8CI59; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q62351; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q9CR62; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q60930; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: P51881; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: P48962; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q61102; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q9JI39; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q9Z2I9; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: P08680; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: P58281; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q8CAQ8; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q80UU9; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: O55022; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.42
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q9Y4C4; IntAct: EBI-20589710; Score: 0.44
DE  Interaction: Q83DF6; IntAct: EBI-21285326; Score: 0.37
DE  Interaction: Q9BVC6; IntAct: EBI-20900351; Score: 0.40
DE  Interaction: P05154; IntAct: EBI-20911464; Score: 0.40
DE  Interaction: P04233; IntAct: EBI-21258980; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: Q96GC9; IntAct: EBI-21267986; Score: 0.35
DE  Interaction: M0R671; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: F1LML3; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: F1LM93; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: A0A0G2K261; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: Q5U2U8; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: Q5RKH1; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: D4A1H9; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: D4A7J8; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: P42346; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: A0A0G2K781; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: P00176; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: O08662; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: Q5PQL2; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: D3ZYG0; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: Q925D4; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: D3ZGM1; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: Q8K4V4; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: Q5RKH0; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: D4A104; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: Q9BY14; IntAct: EBI-25505061; Score: 0.35
DE  Interaction: Q9BUN8; IntAct: EBI-25770511; Score: 0.35
DE  Interaction: Q9IH62; IntAct: EBI-25750665; Score: 0.35
DE  Interaction: P34972; IntAct: EBI-26880846; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NG92; IntAct: EBI-27055968; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: Q8NI60; IntAct: EBI-28943519; Score: 0.35
DE  Interaction: Q9H5K3; IntAct: EBI-28948637; Score: 0.35
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: Q9ULR3; IntAct: EBI-27116214; Score: 0.27
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
DE  Interaction: Q01974; IntAct: EBI-32725367; Score: 0.27
DE  Interaction: Q6J9G0; IntAct: EBI-32731895; Score: 0.27
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0020037;
GO  GO:0015232;
GO  GO:0003707;
GO  GO:0005496;
GO  GO:0060612;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAGDGDVKLGTLGSGSESSNDGGSESPGDAGAAAEGGGWAAAALALLTGGGEMLLNVALVALVLLGAYRLWVRWGRRGL
SQ  GAGAGAGEESPATSLPRMKKRDFSLEQLRQYDGSRNPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCL
SQ  DKDALRDEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHNKQD
//
ID  Q80UU9;
PN  Membrane-associated progesterone receptor component 2;
GN  Pgrmc2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:O15173}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O15173}.
DR  UNIPROT: Q80UU9;
DR  Pfam: PF00173;
DE  Function: Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (PubMed:28005395). May serve as a universal non-classical progesterone receptor in the uterus (Probable). Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus. Plays a role in adipocyte function and systemic glucose homeostasis. In brown fat, which has a high demand for heme, delivery of labile heme in the nucleus regulates the activity of heme-responsive transcriptional repressors such as NR1D1 and BACH1 (PubMed:31748741). {ECO:0000269|PubMed:28005395, ECO:0000269|PubMed:31748741, ECO:0000305|PubMed:28005395}.
DE  Reference Proteome: Yes;
DE  Interaction: O15173; IntAct: EBI-12523269; Score: 0.35
DE  Interaction: Q08460; IntAct: EBI-2024267; Score: 0.35
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: Q8BP00; IntAct: EBI-4283417; Score: 0.35
DE  Interaction: P22830; IntAct: EBI-12523198; Score: 0.35
DE  Interaction: O00264; IntAct: EBI-12523216; Score: 0.35
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0020037;
GO  GO:0015232;
GO  GO:0005496;
GO  GO:0060612;
GO  GO:0015886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAGDGDVKLSTLGSGGESGGDGSPGGAGATAARSSWVAALLATGGEMLLNVALVALVLLGAYRLWVRWGRRGLCSGPGA
SQ  GEESPAATLPRMKKRDFSLEQLRQYDGARTPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCLDKDALR
SQ  DEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHSKQD
//
ID  Q5XIU9;
PN  Membrane-associated progesterone receptor component 2;
GN  Pgrmc2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q80UU9}; Single- pass membrane protein {ECO:0000250|UniProtKB:Q80UU9}. Nucleus envelope {ECO:0000250|UniProtKB:O15173}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O15173}.
DR  UNIPROT: Q5XIU9;
DR  Pfam: PF00173;
DE  Function: Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan. May serve as a universal non- classical progesterone receptor in the uterus. Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus. Plays a role in adipocyte function and systemic glucose homeostasis. In brown fat, which has a high demand for heme, delivery of labile heme in the nucleus regulates the activity of heme-responsive transcriptional repressors such as NR1D1 and BACH1. {ECO:0000250|UniProtKB:Q80UU9}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0020037;
GO  GO:0015232;
GO  GO:0005496;
GO  GO:0060612;
GO  GO:0015886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAGDGDVKLSTLGSGGERGGDGSPGGAGATAARSSWVAALLATGGEMLLNVALVALVLLGAYRLWVRWGRRGLCSGPGA
SQ  GEESPAATLPRMKKRDFSLEQLRQYDGARTPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCLDKDALR
SQ  DEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHSKQD
//
ID  Q9WTR8;
PN  PH domain leucine-rich repeat protein phosphatase 1;
GN  Phlpp1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12594205}. Membrane {ECO:0000269|PubMed:12594205}; Peripheral membrane protein {ECO:0000269|PubMed:12594205}. [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:20819118}. Cell membrane {ECO:0000269|PubMed:20819118}. [Isoform 2]: Nucleus, nucleoplasm {ECO:0000269|PubMed:20819118}. Nucleus membrane {ECO:0000269|PubMed:20819118}. Cytoplasm {ECO:0000269|PubMed:20819118}. Cell membrane {ECO:0000269|PubMed:20819118}.
DR  UNIPROT: Q9WTR8;
DR  Pfam: PF13516;
DR  Pfam: PF13855;
DR  Pfam: PF00169;
DR  Pfam: PF00481;
DR  PROSITE: PS51450;
DR  PROSITE: PS50003;
DR  PROSITE: PS51746;
DE  Function: Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT2 and AKT3, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA (PubMed:20819118). Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons while isoform 1 may promote Akt and PKC activation and inhibit ERK signaling (PubMed:20819118). Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis (By similarity). Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation (By similarity). Inhibits cancer cell proliferation and may act as a tumor suppressor (By similarity). Dephosphorylates RAF1 inhibiting its kinase activity (By similarity). May act as a negative regulator of K-Ras signaling in membrane rafts (PubMed:12594205). Involved in the hippocampus-dependent long-term memory formation (By similarity). Involved in circadian control by regulating the consolidation of circadian periodicity after resetting (By similarity). Involved in development and function of regulatory T-cells (By similarity). {ECO:0000250|UniProtKB:O60346, ECO:0000250|UniProtKB:Q8CHE4, ECO:0000269|PubMed:12594205, ECO:0000269|PubMed:20819118}.
DE  Reference Proteome: Yes;
DE  Interaction: O14745; IntAct: EBI-11165272; Score: 0.40
GO  GO:0005737;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005886;
GO  GO:0046872;
GO  GO:0017018;
GO  GO:0004722;
GO  GO:0006915;
GO  GO:0007623;
GO  GO:0009649;
GO  GO:0021766;
GO  GO:0070373;
GO  GO:0051898;
GO  GO:0090038;
GO  GO:0051897;
GO  GO:0090037;
GO  GO:0006470;
GO  GO:0042981;
GO  GO:0046328;
GO  GO:0043408;
GO  GO:1900744;
GO  GO:0001932;
GO  GO:0002667;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:12594205};
SQ  MEPAAAAPAQRLADPTGEDRAPAAAAAAEGGRSPDSVLSAAAPSGGNGGAAREEAPCEAPPGPLPGRAGGTGRRRRRGVP
SQ  QPAAGGAAPVTAAGGGANSLLLRRGRLKRNLSAAASSSSSPSSASSAAGGLPASCSASASLCTRSLDRKTLLQKHRQLLQ
SQ  LQPSDRDWVRHQLQRGCVHVFDRHMASSYLRPVLCTLDTTAAEVAARLLQLGHKGGGVVKVLGHGPPPAAAPAASDQTPA
SQ  TELGRDVEPPPSSSTVGAVRGPARAPPADLPLPGGAWTRCAPRVNPAPSDSSPGELFAGGPCSPSRAPRPASDTESFSLS
SQ  PSAESVSDRLDPYSSGGGSSSSSEELEADPATVLTGPSGPPHHPVRSSQPRPPSPKTSALLQPKAPTGVDGTGLVVGEGP
SQ  GDDKAVAAAAPGVPLWTPGRIRETVQKTSSPPSLYVQLHGETTRRLEADEKPLQIQNDYLFQLGFGELWRVQEEGMDSEI
SQ  GCLIRFYAGKPHSTGSSERIQLSGMYNVRKGKMQLPVNRWTRRQVILCGTCLIVSSVKDSSSGKMHVLPLIGGKVEEVKK
SQ  HQHCLAFSSSGPQSQTYYICFDTFTEYLRWLRQVSKVASQRISSVDLSCCSLEHLPANLFYSQDLTHLNLKQNFLRQNPS
SQ  LPAARGLGELQRFTKLKSLNLSNNHLGAFPSAVCSIPTLAELNVSCNALQEVPAAVGAMQNLQTFLLDGNFLQSLPAELE
SQ  NMHQLSYLGLSFNEFTDIPEVLEKLTAVDKLCMAGNCMETLRLQALRRMPHIKHVDLRLNILRKLITDEVDFLQHVTQLD
SQ  LRDNKLGDLDAMIFNNIEVLHCERNQLVTLNICGYFLKALYASSNELVQLDVYPVPNYLSYMDVSRNCLESVPEWVCESR
SQ  KLEVLDIGHNQICELPARLFCNSSLRKLLAGHNRLARLPERLERTSVEVLDVQHNQIIELPPNLLMKADSLRFLNASANK
SQ  LETLPPATLSEETSSILQELYLTNNSLTDKCVPLLTGHPRLKILHMAYNRLQSFPASKMAKLEELEEIDISGNKLKAIPT
SQ  TIMNCRRMHTVIAHSNCIEVFPEVMQLPEVKCVDLSCNELSEITLPENLPPKLQELDLTGNPRLALDHKSLELLNNIRCF
SQ  KIDQPSAGDASGAPAVWSHGYTEASGVKNKLCVAALSVNNFRDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTK
SQ  NEEEYMVNTFIVMQRKLGTAGQKLGGAAVLCHIRHDPVDLGGSFTLTSANVGKCQTVLCRNGKPLSLSRSYTMSCEEERK
SQ  RIKQHKAIITEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSIEEAVEAVRNVPDALA
SQ  AAKKLCTLAQSYGCHDSISAVVVQLSVTEDSFCCCELSVGGSMPPPSPGIFPPSVSMVIKDRPSDGLGVPSSSSGMASEI
SQ  SSELSTSEMSSEVGSTASDEPPSGALSESSPAYPSEQRCMLHPVCLSNSFQRQLSSATFSSAFSDNGLDSDDEEPIEGVF
SQ  SNGSRVEVEVDIHCSRAKEKERQQHLLQVPAEASDEGIVISANEDESGLSKKTDISAVGTIGRRRANGSVPPQERSHNVI
SQ  EVATDAPLRKPGGYFAAPAQPDPDDQFIIPPELEEEVKEIMKHHQEQQQQQQQQQQQQQQQPPPPPQPPQAQAQAQAQAQ
SQ  RPFQMDHLPDCYDTPL
//
ID  P34349;
PN  MOB-like protein phocein;
GN  mob;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y3A3}. Membrane {ECO:0000250|UniProtKB:Q9Y3A3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y3A3}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9Y3A3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y3A3}.
DR  UNIPROT: P34349;
DR  Pfam: PF03637;
DE  Function: May play a role in membrane trafficking, specifically in membrane budding reactions. {ECO:0000250|UniProtKB:Q9QYW3}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0032580;
GO  GO:0048471;
GO  GO:0046872;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9Y3A3};
SQ  MTAATENRTVRRNGPGTKRADWNNWSPLAFEEMDSALNIQQYIQQTIKANPADVATILTPPLDQDEGVWKYEHLRQFCIE
SQ  LNGLALLLQRECIPETCQQMTATEQWIFLCAAHKNPNECPAIDYTRHTLDGAATLLNSNKYFPSRVNIKEISISKLGSVA
SQ  RRVYRIFSHAFFHHRKLFDEFENETHLCKRFTTYVSKYNLMQQEHLIVPILPNQQQQQQTTVQ
//
ID  Q9Y3A3;
PN  MOB-like protein phocein;
GN  MOB4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11319234}. Membrane {ECO:0000269|PubMed:11319234}; Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11319234}; Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Note=In a perinuclear punctate pattern. Associated with membranes and the Golgi stacks.
DR  UNIPROT: Q9Y3A3;
DR  UNIPROT: B4DML0;
DR  UNIPROT: Q53SE0;
DR  UNIPROT: Q7Z4Y6;
DR  UNIPROT: Q9H2P3;
DR  UNIPROT: Q9H5J1;
DR  UNIPROT: Q9Y4T8;
DR  PDB: 5YF4;
DR  PDB: 7K36;
DR  Pfam: PF03637;
DR  OMIM: 609361;
DR  DisGeNET: 25843;
DE  Function: May play a role in membrane trafficking, specifically in membrane budding reactions. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-4397868; Score: 0.55
DE  Interaction: Q13459; IntAct: EBI-737438; Score: 0.00
DE  Interaction: Q6P5Z2; IntAct: EBI-11918474; Score: 0.00
DE  Interaction: P49736; IntAct: EBI-730585; Score: 0.00
DE  Interaction: P22234; IntAct: EBI-730588; Score: 0.00
DE  Interaction: Q13332; IntAct: EBI-730591; Score: 0.00
DE  Interaction: Q5UIP0; IntAct: EBI-730594; Score: 0.00
DE  Interaction: Q9Y3C7; IntAct: EBI-732941; Score: 0.00
DE  Interaction: O60383; IntAct: EBI-732944; Score: 0.00
DE  Interaction: Q9ULH0; IntAct: EBI-732947; Score: 0.00
DE  Interaction: P60660; IntAct: EBI-732950; Score: 0.00
DE  Interaction: Q96GD3; IntAct: EBI-732953; Score: 0.00
DE  Interaction: Q15047; IntAct: EBI-732956; Score: 0.00
DE  Interaction: Q15819; IntAct: EBI-732959; Score: 0.00
DE  Interaction: Q14194; IntAct: EBI-735462; Score: 0.00
DE  Interaction: Q13158; IntAct: EBI-735465; Score: 0.00
DE  Interaction: Q9BTT4; IntAct: EBI-735468; Score: 0.00
DE  Interaction: Q9Y4G2; IntAct: EBI-735471; Score: 0.00
DE  Interaction: Q96KS0; IntAct: EBI-737429; Score: 0.00
DE  Interaction: P19419; IntAct: EBI-737432; Score: 0.00
DE  Interaction: P23142; IntAct: EBI-737435; Score: 0.00
DE  Interaction: Q15831; IntAct: EBI-737441; Score: 0.00
DE  Interaction: Q8WY91; IntAct: EBI-737444; Score: 0.00
DE  Interaction: O94989; IntAct: EBI-752704; Score: 0.37
DE  Interaction: Q15834; IntAct: EBI-759730; Score: 0.37
DE  Interaction: Q9Y6E0; IntAct: EBI-2480091; Score: 0.74
DE  Interaction: Q8TDY2; IntAct: EBI-1061436; Score: 0.00
DE  Interaction: Q9NZ47; IntAct: EBI-1061519; Score: 0.00
DE  Interaction: Q9Y376; IntAct: EBI-1062295; Score: 0.00
DE  Interaction: P40337; IntAct: EBI-1062909; Score: 0.00
DE  Interaction: Q9Y5L4; IntAct: EBI-1063567; Score: 0.00
DE  Interaction: Q9P031; IntAct: EBI-1070283; Score: 0.00
DE  Interaction: P23508; IntAct: EBI-1077095; Score: 0.00
DE  Interaction: P67775; IntAct: EBI-1773521; Score: 0.77
DE  Interaction: P62714; IntAct: EBI-1773687; Score: 0.64
DE  Interaction: P30153; IntAct: EBI-2479208; Score: 0.71
DE  Interaction: Q59GV6; IntAct: EBI-1774238; Score: 0.35
DE  Interaction: Q9P289; IntAct: EBI-1774238; Score: 0.76
DE  Interaction: O43815; IntAct: EBI-2476554; Score: 0.74
DE  Interaction: P63167; IntAct: EBI-1774238; Score: 0.53
DE  Interaction: Q9ULQ0; IntAct: EBI-2479515; Score: 0.46
DE  Interaction: Q13033; IntAct: EBI-2476710; Score: 0.77
DE  Interaction: Q9NVK5; IntAct: EBI-2480091; Score: 0.53
DE  Interaction: Q5VSL9; IntAct: EBI-1774238; Score: 0.53
DE  Interaction: A8K3H8; IntAct: EBI-1774238; Score: 0.35
DE  Interaction: Q14BN4; IntAct: EBI-2479515; Score: 0.67
DE  Interaction: Q8WZ74; IntAct: EBI-1774238; Score: 0.60
DE  Interaction: Q9P2B4; IntAct: EBI-1774238; Score: 0.73
DE  Interaction: Q9BRV8; IntAct: EBI-2479515; Score: 0.60
DE  Interaction: Q9Y228; IntAct: EBI-2476666; Score: 0.50
DE  Interaction: Q9NRL3; IntAct: EBI-2479446; Score: 0.46
DE  Interaction: P30154; IntAct: EBI-2479515; Score: 0.46
DE  Interaction: O55106; IntAct: EBI-2479967; Score: 0.54
DE  Interaction: P40227; IntAct: EBI-2480091; Score: 0.35
DE  Interaction: Q9BUL8; IntAct: EBI-2480091; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-2480091; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-2480091; Score: 0.35
DE  Interaction: O00506; IntAct: EBI-2480091; Score: 0.64
DE  Interaction: P17987; IntAct: EBI-2480091; Score: 0.35
DE  Interaction: Q92526; IntAct: EBI-2480091; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-2480091; Score: 0.35
DE  Interaction: P78371; IntAct: EBI-2480091; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-2480091; Score: 0.35
DE  Interaction: Q99JT2; IntAct: EBI-2480319; Score: 0.35
DE  Interaction: Q9UGI0; IntAct: EBI-2511131; Score: 0.40
DE  Interaction: P63168; IntAct: EBI-2556165; Score: 0.40
DE  Interaction: Q9Y4G8; IntAct: EBI-3450242; Score: 0.00
DE  Interaction: Q86WH2; IntAct: EBI-6912050; Score: 0.35
DE  Interaction: Q13188; IntAct: EBI-8799700; Score: 0.48
DE  Interaction: Q13043; IntAct: EBI-8799766; Score: 0.27
DE  Interaction: Q76MZ3; IntAct: EBI-10991736; Score: 0.35
DE  Interaction: P63330; IntAct: EBI-11049240; Score: 0.35
DE  Interaction: Q91YI4; IntAct: EBI-11102575; Score: 0.35
DE  Interaction: Q8C079; IntAct: EBI-11110036; Score: 0.35
DE  Interaction: Q9ERG2; IntAct: EBI-11110170; Score: 0.35
DE  Interaction: O15259; IntAct: EBI-11365282; Score: 0.27
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: O95684; IntAct: EBI-11381827; Score: 0.27
DE  Interaction: Q15154; IntAct: EBI-11382763; Score: 0.27
DE  Interaction: Q68CZ1; IntAct: EBI-11386978; Score: 0.27
DE  Interaction: Q6ZU80; IntAct: EBI-11388429; Score: 0.27
DE  Interaction: Q86SG6; IntAct: EBI-11389773; Score: 0.27
DE  Interaction: Q96ST8; IntAct: EBI-11396670; Score: 0.27
DE  Interaction: Q9C0F1; IntAct: EBI-11397104; Score: 0.27
DE  Interaction: Q9HC77; IntAct: EBI-11397411; Score: 0.27
DE  Interaction: P40454; IntAct: EBI-11531126; Score: 0.56
DE  Interaction: P62195; IntAct: EBI-21656272; Score: 0.35
DE  Interaction: P19438; IntAct: EBI-21717945; Score: 0.35
DE  Interaction: Q9GZV8; IntAct: EBI-21754819; Score: 0.35
DE  Interaction: P20155; IntAct: EBI-21762493; Score: 0.35
DE  Interaction: Q9Y343; IntAct: EBI-21763225; Score: 0.35
DE  Interaction: P20933; IntAct: EBI-21878313; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-16792938; Score: 0.27
DE  Interaction: P13569; IntAct: EBI-25417249; Score: 0.35
DE  Interaction: P17813; IntAct: EBI-22197897; Score: 0.35
DE  Interaction: Q5NHT8; IntAct: EBI-22298716; Score: 0.37
DE  Interaction: A0A0H3LAM7; IntAct: EBI-25401616; Score: 0.35
DE  Interaction: Q13555; IntAct: EBI-28939534; Score: 0.35
DE  Interaction: Q8N4C8; IntAct: EBI-28943316; Score: 0.35
DE  Interaction: Q9UKE5; IntAct: EBI-28946906; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0005794;
GO  GO:0032580;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0019900;
GO  GO:0046872;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11319234};
SQ  MVMAEGTAVLRRNRPGTKAQDFYNWPDESFDEMDSTLAVQQYIQQNIRADCSNIDKILEPPEGQDEGVWKYEHLRQFCLE
SQ  LNGLAVKLQSECHPDTCTQMTATEQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVAKLGSVC
SQ  RRIYRIFSHAYFHHRQIFDEYENETFLCHRFTKFVMKYNLMSKDNLIVPILEEEVQNSVSGESEA
//
ID  Q6PEB6;
PN  MOB-like protein phocein;
GN  Mob4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11319234}. Membrane {ECO:0000269|PubMed:11319234}; Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11319234}; Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Note=In a perinuclear punctate pattern. Associated with membranes and the Golgi stacks.
DR  UNIPROT: Q6PEB6;
DR  UNIPROT: Q3TS21;
DR  UNIPROT: Q8BSA3;
DR  UNIPROT: Q9CX28;
DR  Pfam: PF03637;
DE  Function: May play a role in membrane trafficking, specifically in membrane budding reactions.
DE  Reference Proteome: Yes;
DE  Interaction: P62158; IntAct: EBI-911456; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043197;
GO  GO:0005794;
GO  GO:0032580;
GO  GO:0016020;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0019900;
GO  GO:0046872;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11319234};
SQ  MVMAEGTAVLRRNRPGTKAQDFYNWPDESFDEMDSTLAVQQYIQQNIRADCSNIDKILEPPEGQDEGVWKYEHLRQFCLE
SQ  LNGLAVKLQSECHPDTCTQMTATEQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVAKLGSVC
SQ  RRIYRIFSHAYFHHRQIFDEYENETFLCHRFTKFVMKYNLMSKDNLIVPILEEEVQNSVSGESEA
//
ID  Q5RDB1;
PN  MOB-like protein phocein;
GN  MOB4;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Membrane; Peripheral membrane protein. Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
DR  UNIPROT: Q5RDB1;
DR  UNIPROT: Q5R8K8;
DR  Pfam: PF03637;
DE  Function: May play a role in membrane trafficking, specifically in membrane budding reactions. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0032580;
GO  GO:0048471;
GO  GO:0019900;
GO  GO:0046872;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVMAEGTAVLRRNRPGTKAQDFYNWPDESFDEMDSTLAVQQYIQQNIRADCSNIDKILEPPEGQDEGVWKYEHLRQFCLE
SQ  LNGLAVKLQSECHPDTCTQMTATEQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVAKLGSVC
SQ  RRIYRIFSHAYFHHRQIFDEYENETFLCHRFTKFVMKYNLMSKDNLIVPILEEEVQNSVSGESEA
//
ID  Q9UBF8;
PN  Phosphatidylinositol 4-kinase beta;
GN  PI4KB;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system. Mitochondrion outer membrane; Peripheral membrane protein. Rough endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus {ECO:0000269|PubMed:22124328}. Golgi apparatus membrane {ECO:0000269|PubMed:24672044, ECO:0000269|PubMed:27009356, ECO:0000269|PubMed:28289207}. Cytoplasm, perinuclear region. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5- bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi apparatus membrane by ACBD3 (PubMed:24672044, PubMed:27009356, PubMed:28289207). GGA2 is also involved in the recruitment (PubMed:28289207). {ECO:0000269|PubMed:24672044, ECO:0000269|PubMed:27009356, ECO:0000269|PubMed:28289207}.
DR  UNIPROT: Q9UBF8;
DR  UNIPROT: B4DGI2;
DR  UNIPROT: O15096;
DR  UNIPROT: P78405;
DR  UNIPROT: Q5VWB9;
DR  UNIPROT: Q5VWC0;
DR  UNIPROT: Q5VWC1;
DR  UNIPROT: Q9BWR6;
DR  PDB: 2N73;
DR  PDB: 4D0L;
DR  PDB: 4D0M;
DR  PDB: 4WAE;
DR  PDB: 4WAG;
DR  PDB: 5C46;
DR  PDB: 5C4G;
DR  PDB: 5EUQ;
DR  PDB: 5FBL;
DR  PDB: 5FBQ;
DR  PDB: 5FBR;
DR  PDB: 5FBV;
DR  PDB: 5FBW;
DR  PDB: 5LX2;
DR  PDB: 5NAS;
DR  PDB: 6GL3;
DR  Pfam: PF00454;
DR  PROSITE: PS00915;
DR  PROSITE: PS00916;
DR  PROSITE: PS50290;
DR  PROSITE: PS51545;
DR  OMIM: 602758;
DR  DisGeNET: 5298;
DE  Function: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol- 1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By similarity). {ECO:0000250|UniProtKB:O08561, ECO:0000269|PubMed:10559940, ECO:0000269|PubMed:11277933, ECO:0000269|PubMed:12749687, ECO:0000269|PubMed:9405935}. (Microbial infection) Plays an essential role in Aichi virus RNA replication (PubMed:22124328, PubMed:27989622, PubMed:22258260). Recruited by ACBD3 at the viral replication sites (PubMed:22124328, PubMed:27989622). {ECO:0000269|PubMed:22124328, ECO:0000269|PubMed:22258260, ECO:0000269|PubMed:27989622}. (Microbial infection) Required for cellular spike-mediated entry of human coronavirus SARS-CoV. {ECO:0000269|PubMed:22253445}.
DE  Reference Proteome: Yes;
DE  Interaction: P50613; IntAct: EBI-21835901; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-7300211; Score: 0.69
DE  Interaction: P61981; IntAct: EBI-7300335; Score: 0.69
DE  Interaction: P27348; IntAct: EBI-7300557; Score: 0.76
DE  Interaction: P31947; IntAct: EBI-7544334; Score: 0.40
DE  Interaction: Q8WVZ9; IntAct: EBI-3232144; Score: 0.35
DE  Interaction: Q9H3P7; IntAct: EBI-7587837; Score: 0.54
DE  Interaction: P17047; IntAct: EBI-9103729; Score: 0.27
DE  Interaction: P11438; IntAct: EBI-9103723; Score: 0.27
DE  Interaction: P03495; IntAct: EBI-9116831; Score: 0.51
DE  Interaction: P46939; IntAct: EBI-11070450; Score: 0.40
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9Y3M2; IntAct: EBI-11936324; Score: 0.00
DE  Interaction: Q96QF0; IntAct: EBI-11936315; Score: 0.00
DE  Interaction: P06930; IntAct: EBI-26506878; Score: 0.37
DE  Interaction: Q8IXB1; IntAct: EBI-21546557; Score: 0.35
DE  Interaction: P29466; IntAct: EBI-21873638; Score: 0.35
DE  Interaction: Q8NG50; IntAct: EBI-21900783; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21907689; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-21909838; Score: 0.35
DE  Interaction: P62491; IntAct: EBI-16107859; Score: 0.68
DE  Interaction: O75154; IntAct: EBI-16107877; Score: 0.58
DE  Interaction: Q6PJG9; IntAct: EBI-21228157; Score: 0.35
DE  Interaction: O94776; IntAct: EBI-21228157; Score: 0.35
DE  Interaction: P63151; IntAct: EBI-21228157; Score: 0.35
DE  Interaction: P04062; IntAct: EBI-21228157; Score: 0.35
DE  Interaction: Q5T2E6; IntAct: EBI-21228157; Score: 0.35
DE  Interaction: P03300; IntAct: EBI-21253323; Score: 0.50
DE  Interaction: O75592; IntAct: EBI-26513164; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016020;
GO  GO:0005741;
GO  GO:0048471;
GO  GO:0030867;
GO  GO:0004430;
GO  GO:0071889;
GO  GO:0005524;
GO  GO:0052742;
GO  GO:0007040;
GO  GO:0006661;
GO  GO:0046854;
GO  GO:0048015;
GO  GO:0016310;
GO  GO:0006898;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MGDTVVEPAPLKPTSEPTSGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAVSSRGTPLELVNG
SQ  DGVDSEIRCLDDPPAQIREEEDEMGAAVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYI
SQ  GNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLI
SQ  LSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPV
SQ  RLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIY
SQ  VEVLECENFDTTSVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCD
SQ  NISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLS
SQ  VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGS
SQ  YTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGG
SQ  LDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSI
SQ  TTKLYDGFQYLTNGIM
//
ID  Q2T9M1;
PN  PRKCA-binding protein;
GN  PICK1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present at excitatory synapses. {ECO:0000250}.
DR  UNIPROT: Q2T9M1;
DR  Pfam: PF06456;
DR  Pfam: PF00595;
DR  PROSITE: PS50870;
DR  PROSITE: PS50106;
DE  Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005856;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0051015;
GO  GO:0071933;
GO  GO:0046872;
GO  GO:0019904;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0097062;
GO  GO:0097061;
GO  GO:0021782;
GO  GO:0060292;
GO  GO:0034316;
GO  GO:0002092;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFADLGYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKG
SQ  KTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTA
SQ  ELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLN
SQ  KAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKME
SQ  LLDQEHVQDIVLQLQRFVSTMSKYYNDCYSVLRDADVFPIEVDLAHTTLAYGLSQDEFTDGEDEEDEDEEDTAAGEPPRD
SQ  SRGAAGPLDKGGSWCNS
//
ID  Q9NRD5;
PN  PRKCA-binding protein;
GN  PICK1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present at excitatory synapses. {ECO:0000250}.
DR  UNIPROT: Q9NRD5;
DR  UNIPROT: B3KS52;
DR  UNIPROT: O95906;
DR  PDB: 2GZV;
DR  PDB: 6AR4;
DR  PDB: 6BJN;
DR  PDB: 6BJO;
DR  Pfam: PF06456;
DR  Pfam: PF00595;
DR  PROSITE: PS50870;
DR  PROSITE: PS50106;
DR  OMIM: 605926;
DR  DisGeNET: 9463;
DE  Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function. {ECO:0000269|PubMed:20403402}.
DE  Reference Proteome: Yes;
DE  Interaction: O75604; IntAct: EBI-24275762; Score: 0.56
DE  Interaction: P05129; IntAct: EBI-953356; Score: 0.00
DE  Interaction: Q06787; IntAct: EBI-26509641; Score: 0.55
DE  Interaction: Q13330; IntAct: EBI-24459255; Score: 0.56
DE  Interaction: Q15056; IntAct: EBI-24336001; Score: 0.56
DE  Interaction: Q6ZRP7; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q8NC51; IntAct: EBI-24463602; Score: 0.56
DE  Interaction: Q92993; IntAct: EBI-24509305; Score: 0.56
DE  Interaction: Q96CV9; IntAct: EBI-24457528; Score: 0.56
DE  Interaction: Q9BUZ4; IntAct: EBI-24332833; Score: 0.56
DE  Interaction: Q9BVI4; IntAct: EBI-24505850; Score: 0.56
DE  Interaction: Q16515; IntAct: EBI-79148; Score: 0.51
DE  Interaction: P78348; IntAct: EBI-79188; Score: 0.54
DE  Interaction: Q01959; IntAct: EBI-7839657; Score: 0.54
DE  Interaction: P23975; IntAct: EBI-7839909; Score: 0.51
DE  Interaction: P31645; IntAct: EBI-7840397; Score: 0.37
DE  Interaction: P49683; IntAct: EBI-8009407; Score: 0.46
DE  Interaction: Q9NRR5; IntAct: EBI-950320; Score: 0.00
DE  Interaction: Q7Z2E3; IntAct: EBI-950686; Score: 0.00
DE  Interaction: P54252; IntAct: EBI-952456; Score: 0.00
DE  Interaction: O15265; IntAct: EBI-952462; Score: 0.00
DE  Interaction: Q14CW9; IntAct: EBI-952498; Score: 0.00
DE  Interaction: Q96RK0; IntAct: EBI-952534; Score: 0.00
DE  Interaction: P38432; IntAct: EBI-952630; Score: 0.00
DE  Interaction: Q16595; IntAct: EBI-952768; Score: 0.00
DE  Interaction: Q99684; IntAct: EBI-952774; Score: 0.00
DE  Interaction: Q5VTD9; IntAct: EBI-953050; Score: 0.00
DE  Interaction: Q9NZJ4; IntAct: EBI-953494; Score: 0.00
DE  Interaction: Q93009; IntAct: EBI-953614; Score: 0.00
DE  Interaction: Q3KSR8; IntAct: EBI-2622155; Score: 0.37
DE  Interaction: Q3KSS4; IntAct: EBI-2623394; Score: 0.37
DE  Interaction: Q9NZN4; IntAct: EBI-3918707; Score: 0.37
DE  Interaction: Q9WMX2; IntAct: EBI-9081130; Score: 0.37
DE  Interaction: P31749; IntAct: EBI-9063779; Score: 0.37
DE  Interaction: Q15223; IntAct: EBI-11668410; Score: 0.37
DE  Interaction: Q15911; IntAct: EBI-24274297; Score: 0.56
DE  Interaction: Q8TAP4; IntAct: EBI-24274829; Score: 0.56
DE  Interaction: Q96KN3; IntAct: EBI-24275930; Score: 0.56
DE  Interaction: Q96ST8; IntAct: EBI-24276888; Score: 0.56
DE  Interaction: Q9UJX0; IntAct: EBI-24278192; Score: 0.56
DE  Interaction: Q99633; IntAct: EBI-24278416; Score: 0.56
DE  Interaction: Q9BT17; IntAct: EBI-24278563; Score: 0.56
DE  Interaction: P49247; IntAct: EBI-24280459; Score: 0.56
DE  Interaction: Q9P2J8; IntAct: EBI-24280504; Score: 0.56
DE  Interaction: P07947; IntAct: EBI-24281210; Score: 0.56
DE  Interaction: Q12774; IntAct: EBI-24281059; Score: 0.56
DE  Interaction: Q86VK4; IntAct: EBI-24281311; Score: 0.56
DE  Interaction: P55273; IntAct: EBI-24281941; Score: 0.56
DE  Interaction: O75771; IntAct: EBI-24282267; Score: 0.56
DE  Interaction: Q7Z6G3; IntAct: EBI-24282418; Score: 0.56
DE  Interaction: P09661; IntAct: EBI-24284868; Score: 0.56
DE  Interaction: Q6PF18; IntAct: EBI-24285776; Score: 0.56
DE  Interaction: Q9BY14; IntAct: EBI-24286791; Score: 0.56
DE  Interaction: P13682; IntAct: EBI-24287175; Score: 0.56
DE  Interaction: Q56NI9; IntAct: EBI-24290604; Score: 0.56
DE  Interaction: O75031; IntAct: EBI-24291316; Score: 0.56
DE  Interaction: Q9H0A9; IntAct: EBI-24292384; Score: 0.56
DE  Interaction: Q7L273; IntAct: EBI-24293130; Score: 0.56
DE  Interaction: Q8N554; IntAct: EBI-24294832; Score: 0.56
DE  Interaction: Q13043; IntAct: EBI-24295848; Score: 0.56
DE  Interaction: P61457; IntAct: EBI-24296668; Score: 0.56
DE  Interaction: Q8IYH5; IntAct: EBI-24298036; Score: 0.56
DE  Interaction: Q6ZNH5; IntAct: EBI-24297929; Score: 0.56
DE  Interaction: P49910; IntAct: EBI-24298635; Score: 0.56
DE  Interaction: Q8IW40; IntAct: EBI-24299060; Score: 0.56
DE  Interaction: Q9BYV2; IntAct: EBI-24300061; Score: 0.56
DE  Interaction: Q6NX45; IntAct: EBI-24301397; Score: 0.56
DE  Interaction: O95983; IntAct: EBI-24302986; Score: 0.56
DE  Interaction: Q9BPX1; IntAct: EBI-24303900; Score: 0.56
DE  Interaction: Q9ULW3; IntAct: EBI-24305866; Score: 0.56
DE  Interaction: Q5W5X9; IntAct: EBI-24305955; Score: 0.56
DE  Interaction: P43358; IntAct: EBI-24307997; Score: 0.56
DE  Interaction: P42772; IntAct: EBI-24308278; Score: 0.56
DE  Interaction: Q8WWY3; IntAct: EBI-24308705; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-24309537; Score: 0.56
DE  Interaction: Q7Z4V0; IntAct: EBI-24309655; Score: 0.56
DE  Interaction: Q9BSW7; IntAct: EBI-24310347; Score: 0.56
DE  Interaction: Q13895; IntAct: EBI-24310949; Score: 0.56
DE  Interaction: Q9HC52; IntAct: EBI-24311604; Score: 0.56
DE  Interaction: Q15772; IntAct: EBI-24312386; Score: 0.56
DE  Interaction: Q9C086; IntAct: EBI-24314142; Score: 0.56
DE  Interaction: Q8N6Y0; IntAct: EBI-24314498; Score: 0.56
DE  Interaction: Q9Y250; IntAct: EBI-24315716; Score: 0.56
DE  Interaction: Q96G04; IntAct: EBI-24317376; Score: 0.56
DE  Interaction: Q8N9N8; IntAct: EBI-24317590; Score: 0.56
DE  Interaction: Q96H86; IntAct: EBI-24318883; Score: 0.56
DE  Interaction: P23025; IntAct: EBI-24319146; Score: 0.56
DE  Interaction: Q12824; IntAct: EBI-24323353; Score: 0.56
DE  Interaction: P61966; IntAct: EBI-24324433; Score: 0.56
DE  Interaction: Q9NX01; IntAct: EBI-24326050; Score: 0.56
DE  Interaction: Q9H1K1; IntAct: EBI-24326107; Score: 0.56
DE  Interaction: P32321; IntAct: EBI-24327302; Score: 0.56
DE  Interaction: Q7L5A3; IntAct: EBI-24329389; Score: 0.56
DE  Interaction: Q9UGP5; IntAct: EBI-24329540; Score: 0.56
DE  Interaction: Q5JST6; IntAct: EBI-24329690; Score: 0.56
DE  Interaction: Q9Y5B8; IntAct: EBI-24330141; Score: 0.56
DE  Interaction: Q96MY7; IntAct: EBI-24331110; Score: 0.56
DE  Interaction: Q9NQZ8; IntAct: EBI-24332534; Score: 0.56
DE  Interaction: Q6ZN57; IntAct: EBI-24332969; Score: 0.56
DE  Interaction: Q68J44; IntAct: EBI-24333287; Score: 0.56
DE  Interaction: Q504U0; IntAct: EBI-24333616; Score: 0.56
DE  Interaction: Q9HBT8; IntAct: EBI-24334718; Score: 0.56
DE  Interaction: Q6P1J9; IntAct: EBI-24334924; Score: 0.56
DE  Interaction: Q8N680; IntAct: EBI-24336367; Score: 0.56
DE  Interaction: Q8TCE9; IntAct: EBI-24336562; Score: 0.56
DE  Interaction: Q8WYJ6; IntAct: EBI-24341060; Score: 0.56
DE  Interaction: A0A024R4Z4; IntAct: EBI-24342526; Score: 0.56
DE  Interaction: Q9HAN9; IntAct: EBI-24343045; Score: 0.56
DE  Interaction: Q4VC12; IntAct: EBI-24344148; Score: 0.56
DE  Interaction: Q7LBR1; IntAct: EBI-24347130; Score: 0.56
DE  Interaction: Q86T90; IntAct: EBI-24351146; Score: 0.56
DE  Interaction: Q5T6S3; IntAct: EBI-24353562; Score: 0.56
DE  Interaction: Q92917; IntAct: EBI-24353414; Score: 0.56
DE  Interaction: Q5QJE6; IntAct: EBI-24353678; Score: 0.56
DE  Interaction: Q9H147; IntAct: EBI-24359365; Score: 0.56
DE  Interaction: P40938; IntAct: EBI-24360427; Score: 0.56
DE  Interaction: Q17RB8; IntAct: EBI-24360679; Score: 0.56
DE  Interaction: Q9BQP7; IntAct: EBI-24360919; Score: 0.56
DE  Interaction: Q96T60; IntAct: EBI-24360963; Score: 0.56
DE  Interaction: Q9UJW9; IntAct: EBI-24361138; Score: 0.56
DE  Interaction: Q96QA6; IntAct: EBI-24361956; Score: 0.56
DE  Interaction: P61086; IntAct: EBI-24362532; Score: 0.56
DE  Interaction: Q969R5; IntAct: EBI-24363925; Score: 0.56
DE  Interaction: P31751; IntAct: EBI-25246907; Score: 0.56
DE  Interaction: Q16512; IntAct: EBI-25246962; Score: 0.56
DE  Interaction: P47897; IntAct: EBI-25248117; Score: 0.56
DE  Interaction: Q3SY00; IntAct: EBI-25249747; Score: 0.56
DE  Interaction: Q96MU7; IntAct: EBI-25249902; Score: 0.56
DE  Interaction: Q9NSI2; IntAct: EBI-25249983; Score: 0.56
DE  Interaction: Q14119; IntAct: EBI-25251633; Score: 0.56
DE  Interaction: Q9BV90; IntAct: EBI-25252778; Score: 0.56
DE  Interaction: Q9NQT4; IntAct: EBI-25253504; Score: 0.56
DE  Interaction: Q14451; IntAct: EBI-25254111; Score: 0.56
DE  Interaction: Q8NEH6; IntAct: EBI-25254288; Score: 0.56
DE  Interaction: Q9BXS5; IntAct: EBI-25254630; Score: 0.56
DE  Interaction: Q96MN5; IntAct: EBI-25254880; Score: 0.56
DE  Interaction: Q96HH0; IntAct: EBI-25255196; Score: 0.56
DE  Interaction: Q08AG9; IntAct: EBI-25256463; Score: 0.56
DE  Interaction: P08311; IntAct: EBI-25256928; Score: 0.56
DE  Interaction: Q8IVS8; IntAct: EBI-25256884; Score: 0.56
DE  Interaction: Q969R2; IntAct: EBI-25257560; Score: 0.56
DE  Interaction: Q9BZR8; IntAct: EBI-25257945; Score: 0.56
DE  Interaction: Q96C55; IntAct: EBI-24364583; Score: 0.56
DE  Interaction: Q9BX10; IntAct: EBI-24365161; Score: 0.56
DE  Interaction: Q8NC69; IntAct: EBI-24366062; Score: 0.56
DE  Interaction: P57086; IntAct: EBI-24366391; Score: 0.56
DE  Interaction: Q08426; IntAct: EBI-24366679; Score: 0.56
DE  Interaction: P52564; IntAct: EBI-24366773; Score: 0.56
DE  Interaction: O75400; IntAct: EBI-24368824; Score: 0.56
DE  Interaction: P15622; IntAct: EBI-24368717; Score: 0.56
DE  Interaction: Q9BU76; IntAct: EBI-24369460; Score: 0.56
DE  Interaction: Q9BUI4; IntAct: EBI-24478617; Score: 0.56
DE  Interaction: O75487; IntAct: EBI-24478788; Score: 0.56
DE  Interaction: Q86YS7; IntAct: EBI-24479316; Score: 0.56
DE  Interaction: Q9HC98; IntAct: EBI-24481182; Score: 0.56
DE  Interaction: Q15014; IntAct: EBI-24482268; Score: 0.56
DE  Interaction: Q8TAU3; IntAct: EBI-24483381; Score: 0.56
DE  Interaction: P00540; IntAct: EBI-24484736; Score: 0.56
DE  Interaction: P61289; IntAct: EBI-24485685; Score: 0.56
DE  Interaction: O43296; IntAct: EBI-24486434; Score: 0.56
DE  Interaction: Q9H9D4; IntAct: EBI-24487140; Score: 0.56
DE  Interaction: O60437; IntAct: EBI-24486864; Score: 0.56
DE  Interaction: P08579; IntAct: EBI-24487243; Score: 0.56
DE  Interaction: P25786; IntAct: EBI-24489535; Score: 0.56
DE  Interaction: Q8NHY3; IntAct: EBI-24489781; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24490101; Score: 0.56
DE  Interaction: Q7L590; IntAct: EBI-24491037; Score: 0.56
DE  Interaction: O75564; IntAct: EBI-24492868; Score: 0.56
DE  Interaction: Q96MH2; IntAct: EBI-24493184; Score: 0.56
DE  Interaction: Q6ZN18; IntAct: EBI-24493171; Score: 0.56
DE  Interaction: Q96GE4; IntAct: EBI-24496817; Score: 0.56
DE  Interaction: P26196; IntAct: EBI-24497555; Score: 0.56
DE  Interaction: Q96DX7; IntAct: EBI-24499846; Score: 0.56
DE  Interaction: Q29RF7; IntAct: EBI-24499780; Score: 0.56
DE  Interaction: Q9UJD0; IntAct: EBI-24502869; Score: 0.56
DE  Interaction: Q12905; IntAct: EBI-24504771; Score: 0.56
DE  Interaction: Q969T4; IntAct: EBI-24505369; Score: 0.56
DE  Interaction: Q9BTE7; IntAct: EBI-24505977; Score: 0.56
DE  Interaction: Q02363; IntAct: EBI-24512109; Score: 0.56
DE  Interaction: Q9BYU1; IntAct: EBI-24516770; Score: 0.56
DE  Interaction: Q9NQ48; IntAct: EBI-24395147; Score: 0.56
DE  Interaction: Q9UII2; IntAct: EBI-24530813; Score: 0.56
DE  Interaction: Q8IZU1; IntAct: EBI-24607193; Score: 0.56
DE  Interaction: Q13322; IntAct: EBI-24618876; Score: 0.56
DE  Interaction: O14613; IntAct: EBI-24622916; Score: 0.56
DE  Interaction: P17021; IntAct: EBI-24369822; Score: 0.56
DE  Interaction: P25800; IntAct: EBI-24371855; Score: 0.56
DE  Interaction: Q9NUL5; IntAct: EBI-24372255; Score: 0.56
DE  Interaction: Q15041; IntAct: EBI-24372801; Score: 0.56
DE  Interaction: Q5VV52; IntAct: EBI-24373417; Score: 0.56
DE  Interaction: Q8IVW4; IntAct: EBI-24373579; Score: 0.56
DE  Interaction: P29084; IntAct: EBI-24374306; Score: 0.56
DE  Interaction: Q9UKT7; IntAct: EBI-24376141; Score: 0.56
DE  Interaction: P67936; IntAct: EBI-24377202; Score: 0.56
DE  Interaction: P30086; IntAct: EBI-24377450; Score: 0.56
DE  Interaction: Q9P291; IntAct: EBI-24377941; Score: 0.56
DE  Interaction: Q9UJV3; IntAct: EBI-24378214; Score: 0.56
DE  Interaction: O15371; IntAct: EBI-24378913; Score: 0.56
DE  Interaction: Q9NR46; IntAct: EBI-24379419; Score: 0.56
DE  Interaction: Q86YV0; IntAct: EBI-24379784; Score: 0.56
DE  Interaction: P08397; IntAct: EBI-24380711; Score: 0.56
DE  Interaction: Q6IPR3; IntAct: EBI-24380890; Score: 0.56
DE  Interaction: Q719H9; IntAct: EBI-24381244; Score: 0.56
DE  Interaction: Q96LK0; IntAct: EBI-24382692; Score: 0.56
DE  Interaction: Q9NU19; IntAct: EBI-24384246; Score: 0.56
DE  Interaction: O76064; IntAct: EBI-24384325; Score: 0.56
DE  Interaction: Q86XF7; IntAct: EBI-24384959; Score: 0.56
DE  Interaction: Q92785; IntAct: EBI-24386803; Score: 0.56
DE  Interaction: P51946; IntAct: EBI-24387020; Score: 0.56
DE  Interaction: Q8IVT4; IntAct: EBI-24388553; Score: 0.56
DE  Interaction: Q9BV20; IntAct: EBI-24389069; Score: 0.56
DE  Interaction: Q8IYX8; IntAct: EBI-24389157; Score: 0.56
DE  Interaction: Q6NT76; IntAct: EBI-24389102; Score: 0.56
DE  Interaction: Q8TBE0; IntAct: EBI-24389462; Score: 0.56
DE  Interaction: P63241; IntAct: EBI-24390128; Score: 0.56
DE  Interaction: Q15102; IntAct: EBI-24390311; Score: 0.56
DE  Interaction: Q5MJ10; IntAct: EBI-24391549; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-24392096; Score: 0.56
DE  Interaction: Q9GZM8; IntAct: EBI-24393020; Score: 0.56
DE  Interaction: Q5T7W7; IntAct: EBI-24394814; Score: 0.56
DE  Interaction: Q9BPY8; IntAct: EBI-24394561; Score: 0.56
DE  Interaction: O43167; IntAct: EBI-24395737; Score: 0.56
DE  Interaction: Q9H7E9; IntAct: EBI-24396085; Score: 0.56
DE  Interaction: Q6ZSB9; IntAct: EBI-24396546; Score: 0.56
DE  Interaction: O15078; IntAct: EBI-24396419; Score: 0.56
DE  Interaction: Q96GM5; IntAct: EBI-24397745; Score: 0.56
DE  Interaction: Q9NTM9; IntAct: EBI-24398287; Score: 0.56
DE  Interaction: O43159; IntAct: EBI-24399822; Score: 0.56
DE  Interaction: Q9NW75; IntAct: EBI-24400845; Score: 0.67
DE  Interaction: Q6IQ23; IntAct: EBI-24401489; Score: 0.56
DE  Interaction: Q49AN0; IntAct: EBI-24401410; Score: 0.56
DE  Interaction: Q9UPY8; IntAct: EBI-24401669; Score: 0.56
DE  Interaction: P45984; IntAct: EBI-24403198; Score: 0.56
DE  Interaction: Q13214; IntAct: EBI-24403974; Score: 0.56
DE  Interaction: Q70IA8; IntAct: EBI-24404275; Score: 0.56
DE  Interaction: Q86YD7; IntAct: EBI-24404691; Score: 0.56
DE  Interaction: O60941; IntAct: EBI-24405462; Score: 0.56
DE  Interaction: Q15631; IntAct: EBI-24406696; Score: 0.56
DE  Interaction: Q8TBB0; IntAct: EBI-24407185; Score: 0.56
DE  Interaction: Q92551; IntAct: EBI-24408028; Score: 0.56
DE  Interaction: Q14005; IntAct: EBI-24408787; Score: 0.56
DE  Interaction: Q9H257; IntAct: EBI-24409408; Score: 0.56
DE  Interaction: Q96IQ9; IntAct: EBI-24411745; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-24413327; Score: 0.56
DE  Interaction: Q96CD0; IntAct: EBI-24413904; Score: 0.56
DE  Interaction: Q68D86; IntAct: EBI-24413834; Score: 0.56
DE  Interaction: Q96GN5; IntAct: EBI-24414466; Score: 0.56
DE  Interaction: P28702; IntAct: EBI-24414850; Score: 0.56
DE  Interaction: P56524; IntAct: EBI-24415246; Score: 0.56
DE  Interaction: Q9H788; IntAct: EBI-24415751; Score: 0.56
DE  Interaction: P19784; IntAct: EBI-24416093; Score: 0.56
DE  Interaction: O95696; IntAct: EBI-25260284; Score: 0.56
DE  Interaction: P26367; IntAct: EBI-25260785; Score: 0.56
DE  Interaction: P59910; IntAct: EBI-25260844; Score: 0.56
DE  Interaction: O96006; IntAct: EBI-25261606; Score: 0.56
DE  Interaction: Q96FN4; IntAct: EBI-25261540; Score: 0.56
DE  Interaction: O14530; IntAct: EBI-25262634; Score: 0.56
DE  Interaction: Q3MJ62; IntAct: EBI-25263054; Score: 0.56
DE  Interaction: Q8N8B7; IntAct: EBI-25263780; Score: 0.56
DE  Interaction: Q13541; IntAct: EBI-24416710; Score: 0.56
DE  Interaction: Q3B820; IntAct: EBI-24416662; Score: 0.56
DE  Interaction: O43320; IntAct: EBI-24417591; Score: 0.56
DE  Interaction: Q8N6N6; IntAct: EBI-24418647; Score: 0.56
DE  Interaction: Q9UBB9; IntAct: EBI-24420579; Score: 0.56
DE  Interaction: Q9BWG6; IntAct: EBI-24422624; Score: 0.56
DE  Interaction: Q9UHV2; IntAct: EBI-24422762; Score: 0.56
DE  Interaction: Q9GZT3; IntAct: EBI-24423161; Score: 0.56
DE  Interaction: Q9NR81; IntAct: EBI-24423597; Score: 0.56
DE  Interaction: Q96NC0; IntAct: EBI-24425015; Score: 0.56
DE  Interaction: Q9HBH7; IntAct: EBI-24425308; Score: 0.56
DE  Interaction: Q53S33; IntAct: EBI-24425720; Score: 0.56
DE  Interaction: O75344; IntAct: EBI-24425856; Score: 0.56
DE  Interaction: Q8TAE8; IntAct: EBI-24426925; Score: 0.56
DE  Interaction: O15481; IntAct: EBI-24428439; Score: 0.56
DE  Interaction: Q9H609; IntAct: EBI-24428748; Score: 0.56
DE  Interaction: O00463; IntAct: EBI-24430288; Score: 0.56
DE  Interaction: P11532; IntAct: EBI-24430507; Score: 0.56
DE  Interaction: O00488; IntAct: EBI-24430913; Score: 0.56
DE  Interaction: Q9NQZ2; IntAct: EBI-24431310; Score: 0.56
DE  Interaction: A8MXD5; IntAct: EBI-24431411; Score: 0.56
DE  Interaction: P41223; IntAct: EBI-24432260; Score: 0.56
DE  Interaction: Q9UFW8; IntAct: EBI-24432238; Score: 0.56
DE  Interaction: Q8N954; IntAct: EBI-24432937; Score: 0.56
DE  Interaction: Q4G0R1; IntAct: EBI-24434657; Score: 0.56
DE  Interaction: P19544; IntAct: EBI-24435564; Score: 0.56
DE  Interaction: P38919; IntAct: EBI-24435989; Score: 0.56
DE  Interaction: P51451; IntAct: EBI-24437371; Score: 0.56
DE  Interaction: Q9NRX1; IntAct: EBI-24437947; Score: 0.56
DE  Interaction: Q8NBZ0; IntAct: EBI-24438358; Score: 0.56
DE  Interaction: Q8NHQ9; IntAct: EBI-24438211; Score: 0.56
DE  Interaction: Q96JC9; IntAct: EBI-24439310; Score: 0.56
DE  Interaction: Q5XKK7; IntAct: EBI-24439630; Score: 0.56
DE  Interaction: P56270; IntAct: EBI-24440260; Score: 0.56
DE  Interaction: Q9NRD5; IntAct: EBI-24440238; Score: 0.56
DE  Interaction: Q9HAT0; IntAct: EBI-24441340; Score: 0.56
DE  Interaction: O43805; IntAct: EBI-24442839; Score: 0.56
DE  Interaction: Q9NP66; IntAct: EBI-24443445; Score: 0.56
DE  Interaction: Q13573; IntAct: EBI-24446534; Score: 0.56
DE  Interaction: Q9BRG1; IntAct: EBI-24447109; Score: 0.56
DE  Interaction: B7ZLI8; IntAct: EBI-24447554; Score: 0.56
DE  Interaction: Q13671; IntAct: EBI-24447914; Score: 0.56
DE  Interaction: Q96HR9; IntAct: EBI-24448669; Score: 0.56
DE  Interaction: Q14919; IntAct: EBI-24449156; Score: 0.56
DE  Interaction: Q9BUL9; IntAct: EBI-24450780; Score: 0.56
DE  Interaction: Q9P0N9; IntAct: EBI-24450912; Score: 0.56
DE  Interaction: Q9H0I2; IntAct: EBI-24451265; Score: 0.56
DE  Interaction: Q9Y530; IntAct: EBI-24452827; Score: 0.56
DE  Interaction: Q15560; IntAct: EBI-24454204; Score: 0.56
DE  Interaction: Q03933; IntAct: EBI-24456616; Score: 0.56
DE  Interaction: Q7L775; IntAct: EBI-24460252; Score: 0.56
DE  Interaction: Q5SQQ9; IntAct: EBI-24460787; Score: 0.56
DE  Interaction: Q9Y3S2; IntAct: EBI-24462021; Score: 0.56
DE  Interaction: Q6UWP7; IntAct: EBI-24461920; Score: 0.56
DE  Interaction: P48775; IntAct: EBI-24463913; Score: 0.56
DE  Interaction: Q14565; IntAct: EBI-24463865; Score: 0.56
DE  Interaction: P20719; IntAct: EBI-24464716; Score: 0.56
DE  Interaction: Q9BT49; IntAct: EBI-24465323; Score: 0.56
DE  Interaction: Q86UD4; IntAct: EBI-24465290; Score: 0.56
DE  Interaction: Q8IXL7; IntAct: EBI-24466095; Score: 0.56
DE  Interaction: O14737; IntAct: EBI-24467314; Score: 0.56
DE  Interaction: Q5JTD7; IntAct: EBI-24468020; Score: 0.56
DE  Interaction: O95201; IntAct: EBI-24469813; Score: 0.56
DE  Interaction: Q9Y5A6; IntAct: EBI-24470493; Score: 0.56
DE  Interaction: Q4VC44; IntAct: EBI-24470388; Score: 0.56
DE  Interaction: Q15735; IntAct: EBI-24470900; Score: 0.56
DE  Interaction: Q9UBU8; IntAct: EBI-24471970; Score: 0.56
DE  Interaction: Q8IZ69; IntAct: EBI-24473683; Score: 0.56
DE  Interaction: Q15287; IntAct: EBI-24473661; Score: 0.56
DE  Interaction: Q8IYA8; IntAct: EBI-24475631; Score: 0.56
DE  Interaction: Q9H1K6; IntAct: EBI-24476134; Score: 0.56
DE  Interaction: Q9UBL6; IntAct: EBI-24477247; Score: 0.56
DE  Interaction: Q86Y79; IntAct: EBI-24477236; Score: 0.56
DE  Interaction: P80188; IntAct: EBI-24533066; Score: 0.56
DE  Interaction: Q6QNY1; IntAct: EBI-24535192; Score: 0.56
DE  Interaction: P48443; IntAct: EBI-24539056; Score: 0.56
DE  Interaction: O14519; IntAct: EBI-24546970; Score: 0.56
DE  Interaction: Q9H0C1; IntAct: EBI-24564635; Score: 0.56
DE  Interaction: Q5T686; IntAct: EBI-24574195; Score: 0.56
DE  Interaction: Q8N7C3; IntAct: EBI-24578447; Score: 0.56
DE  Interaction: Q6PF05; IntAct: EBI-24582383; Score: 0.56
DE  Interaction: Q96BT7; IntAct: EBI-24593875; Score: 0.56
DE  Interaction: Q6NTE8; IntAct: EBI-24637325; Score: 0.56
DE  Interaction: P16444; IntAct: EBI-21514808; Score: 0.35
DE  Interaction: Q92692; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q13563; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: P52799; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q9Y697; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q9Y624; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q9Y613; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q9UL01; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q9UGV2; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q9NVR0; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q9NQY0; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q9C073; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q9BZF9; IntAct: EBI-21519718; Score: 0.55
DE  Interaction: Q8NDH6; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q86WK6; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q86U70; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q7RTV5; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q3T906; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q15904; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q15375; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q05084; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: P98196; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: P98172; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: P53367; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: P23229; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: P17028; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: A1L0T0; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: Q02833; IntAct: EBI-21525884; Score: 0.35
DE  Interaction: Q8TDR4; IntAct: EBI-21617027; Score: 0.35
DE  Interaction: P43355; IntAct: EBI-21634905; Score: 0.35
DE  Interaction: O75787; IntAct: EBI-21856696; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: Q99996; IntAct: EBI-21369499; Score: 0.00
DE  Interaction: Q9Y6R4; IntAct: EBI-21380388; Score: 0.00
DE  Interaction: P07196; IntAct: EBI-21380808; Score: 0.00
DE  Interaction: P08621; IntAct: EBI-21387006; Score: 0.00
DE  Interaction: Q01082; IntAct: EBI-21387372; Score: 0.00
DE  Interaction: P82094; IntAct: EBI-21387842; Score: 0.00
DE  Interaction: B5ME19; IntAct: EBI-21388090; Score: 0.00
DE  Interaction: Q8TDR0; IntAct: EBI-21392320; Score: 0.00
DE  Interaction: P42858; IntAct: EBI-25962458; Score: 0.56
DE  Interaction: Q96QS3; IntAct: EBI-26508337; Score: 0.51
DE  Interaction: P26358; IntAct: EBI-26508381; Score: 0.51
DE  Interaction: Q13936; IntAct: EBI-26508359; Score: 0.51
DE  Interaction: P60484; IntAct: EBI-26508587; Score: 0.51
DE  Interaction: Q9BYB0; IntAct: EBI-26508663; Score: 0.51
DE  Interaction: P49815; IntAct: EBI-26508755; Score: 0.51
DE  Interaction: Q92574; IntAct: EBI-26508735; Score: 0.51
DE  Interaction: P51531; IntAct: EBI-26508695; Score: 0.51
DE  Interaction: P78352; IntAct: EBI-26509348; Score: 0.37
DE  Interaction: P51116; IntAct: EBI-26512077; Score: 0.37
DE  Interaction: Q9NZ94; IntAct: EBI-26513344; Score: 0.37
DE  Interaction: Q7TLC7; IntAct: EBI-26377368; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0030666;
GO  GO:0005794;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098842;
GO  GO:0042734;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0032588;
GO  GO:0051015;
GO  GO:0071933;
GO  GO:0019899;
GO  GO:0001664;
GO  GO:0042802;
GO  GO:0140090;
GO  GO:0046872;
GO  GO:0005543;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0005080;
GO  GO:0005102;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0097062;
GO  GO:0097061;
GO  GO:0043045;
GO  GO:0043046;
GO  GO:0021782;
GO  GO:0006886;
GO  GO:0060292;
GO  GO:0015844;
GO  GO:0034316;
GO  GO:0045161;
GO  GO:0002092;
GO  GO:0007205;
GO  GO:0006468;
GO  GO:0043113;
GO  GO:0034315;
GO  GO:0050796;
GO  GO:0006890;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKG
SQ  KTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTA
SQ  ELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLN
SQ  KAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKME
SQ  LLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGLNQEEFTDGEEEEEEEDTAAGEPSRDTR
SQ  GAAGPLDKGGSWCDS
//
ID  Q4R7Q5;
PN  PRKCA-binding protein;
GN  PICK1;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present at excitatory synapses. {ECO:0000250}.
DR  UNIPROT: Q4R7Q5;
DR  Pfam: PF06456;
DR  Pfam: PF00595;
DR  PROSITE: PS50870;
DR  PROSITE: PS50106;
DE  Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005856;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0051015;
GO  GO:0071933;
GO  GO:0046872;
GO  GO:0019904;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0097062;
GO  GO:0097061;
GO  GO:0021782;
GO  GO:0060292;
GO  GO:0034316;
GO  GO:0002092;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKG
SQ  KTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTA
SQ  ELYKGMTEHTKNLLRVFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLN
SQ  KAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKME
SQ  LLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGLNQEEFTDGEEEEEEEDTAAGEPSRDTR
SQ  GAAGPLDKGGSWCDS
//
ID  Q62083;
PN  PRKCA-binding protein;
GN  Pick1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:24068808}; Lipid-anchor {ECO:0000269|PubMed:24068808}. Postsynaptic density {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present at excitatory synapses. {ECO:0000250}.
DR  UNIPROT: Q62083;
DR  UNIPROT: E9PY04;
DR  Pfam: PF06456;
DR  Pfam: PF00595;
DR  PROSITE: PS50870;
DR  PROSITE: PS50106;
DE  Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function. {ECO:0000269|PubMed:14976185, ECO:0000269|PubMed:20445062}.
DE  Reference Proteome: Yes;
DE  Interaction: P23819; IntAct: EBI-77578; Score: 0.40
DE  Interaction: P54763; IntAct: EBI-537741; Score: 0.37
DE  Interaction: P54759; IntAct: EBI-537826; Score: 0.37
DE  Interaction: P98172; IntAct: EBI-538301; Score: 0.37
DE  Interaction: P04409; IntAct: EBI-8668941; Score: 0.58
DE  Interaction: Q62083; IntAct: EBI-8669033; Score: 0.37
DE  Interaction: Q925H0; IntAct: EBI-8056172; Score: 0.51
DE  Interaction: P55926; IntAct: EBI-8056336; Score: 0.37
DE  Interaction: Q16515; IntAct: EBI-8056415; Score: 0.40
DE  Interaction: Q15223; IntAct: EBI-7580732; Score: 0.46
DE  Interaction: Q9D8B7; IntAct: EBI-7580779; Score: 0.51
DE  Interaction: O88792; IntAct: EBI-7580866; Score: 0.51
DE  Interaction: Q9NQS3; IntAct: EBI-7580958; Score: 0.37
DE  Interaction: Q92692; IntAct: EBI-7581041; Score: 0.37
DE  Interaction: Q96NY8; IntAct: EBI-7581181; Score: 0.37
DE  Interaction: P57087; IntAct: EBI-7581497; Score: 0.37
DE  Interaction: Q61327; IntAct: EBI-7839749; Score: 0.60
DE  Interaction: Q01959; IntAct: EBI-7840170; Score: 0.27
DE  Interaction: O55192; IntAct: EBI-7840516; Score: 0.27
DE  Interaction: Q60857; IntAct: EBI-15633479; Score: 0.35
DE  Interaction: P97411; IntAct: EBI-16056227; Score: 0.40
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0005739;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098842;
GO  GO:0098843;
GO  GO:0042734;
GO  GO:0032991;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0032588;
GO  GO:0051015;
GO  GO:0071933;
GO  GO:0008092;
GO  GO:0019899;
GO  GO:0001664;
GO  GO:0042802;
GO  GO:0035255;
GO  GO:0140090;
GO  GO:0046872;
GO  GO:0005543;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0005080;
GO  GO:0005102;
GO  GO:0005484;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0097062;
GO  GO:0097061;
GO  GO:0021782;
GO  GO:0006886;
GO  GO:0035556;
GO  GO:0060292;
GO  GO:0015844;
GO  GO:0034316;
GO  GO:0060548;
GO  GO:0010629;
GO  GO:0002092;
GO  GO:0007205;
GO  GO:0006468;
GO  GO:0006605;
GO  GO:0043113;
GO  GO:0034315;
GO  GO:0050796;
GO  GO:0099149;
GO  GO:0050803;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:24068808};
SQ  MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGKSIKG
SQ  KTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTA
SQ  ELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLN
SQ  KAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIGPRRALYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKME
SQ  LLDQKHVQDIVFQLQRFVSTMSKYYNDCYAVLQDADVFPIEVDLAHTTLAYGPNQGSFTDGEEEDEEEEDGAAREVSKDA
SQ  CGATGPTDKGGSWCDS
//
ID  Q5REH1;
PN  PRKCA-binding protein;
GN  PICK1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present at excitatory synapses. {ECO:0000250}.
DR  UNIPROT: Q5REH1;
DR  Pfam: PF06456;
DR  Pfam: PF00595;
DR  PROSITE: PS50870;
DR  PROSITE: PS50106;
DE  Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005856;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0014069;
GO  GO:0051015;
GO  GO:0071933;
GO  GO:0046872;
GO  GO:0019904;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0097062;
GO  GO:0097061;
GO  GO:0021782;
GO  GO:0060292;
GO  GO:0034316;
GO  GO:0002092;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKG
SQ  KTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTA
SQ  ELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLN
SQ  KAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKME
SQ  LLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGLNQEEFTDGEEEEEEEDTAAGEPARDTR
SQ  GAAGPLDKGGSWCDS
//
ID  Q9EP80;
PN  PRKCA-binding protein;
GN  Pick1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:23889934}. Membrane {ECO:0000269|PubMed:23889934}; Peripheral membrane protein {ECO:0000269|PubMed:23889934}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Postsynaptic density {ECO:0000269|PubMed:23889934}. Synapse, synaptosome {ECO:0000269|PubMed:23889934}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23889934}. Note=Also membrane-associated, present at excitatory synapses.
DR  UNIPROT: Q9EP80;
DR  UNIPROT: Q546X4;
DR  UNIPROT: Q925D1;
DR  PDB: 2LUI;
DR  PDB: 2PKU;
DR  PDB: 3HPK;
DR  PDB: 3HPM;
DR  Pfam: PF06456;
DR  Pfam: PF00595;
DR  PROSITE: PS50870;
DR  PROSITE: PS50106;
DE  Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function. {ECO:0000269|PubMed:16138078, ECO:0000269|PubMed:18297063, ECO:0000269|PubMed:21252856, ECO:0000269|PubMed:23843614}.
DE  Reference Proteome: Yes;
DE  Interaction: P19491; IntAct: EBI-77537; Score: 0.92
DE  Interaction: P19492; IntAct: EBI-77774; Score: 0.75
DE  Interaction: P27049; IntAct: EBI-79266; Score: 0.58
DE  Interaction: Q62962; IntAct: EBI-8056539; Score: 0.44
DE  Interaction: Q9EP80; IntAct: EBI-7717521; Score: 0.82
DE  Interaction: P97879; IntAct: EBI-7717670; Score: 0.61
DE  Interaction: Q9WTW1; IntAct: EBI-7717820; Score: 0.46
DE  Interaction: P35400; IntAct: EBI-7405112; Score: 0.74
DE  Interaction: P31421; IntAct: EBI-7405163; Score: 0.40
DE  Interaction: P05696; IntAct: EBI-7405337; Score: 0.40
DE  Interaction: P19493; IntAct: EBI-8170512; Score: 0.37
DE  Interaction: Q63337; IntAct: EBI-8170558; Score: 0.51
DE  Interaction: P31422; IntAct: EBI-8170780; Score: 0.40
DE  Interaction: P23819; IntAct: EBI-8170847; Score: 0.40
DE  Interaction: P85970; IntAct: EBI-8567525; Score: 0.40
DE  Interaction: Q9QZ81; IntAct: EBI-9981505; Score: 0.46
DE  Interaction: P42262; IntAct: EBI-15823188; Score: 0.56
DE  Interaction: Q01959; IntAct: EBI-15823213; Score: 0.56
DE  Interaction: Q68ED2; IntAct: EBI-15823307; Score: 0.40
DE  Interaction: Q63054; IntAct: EBI-16056296; Score: 0.40
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0030425;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0005739;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098842;
GO  GO:0098843;
GO  GO:0042734;
GO  GO:0032991;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0032588;
GO  GO:0051015;
GO  GO:0071933;
GO  GO:0008092;
GO  GO:0019899;
GO  GO:0046875;
GO  GO:0035256;
GO  GO:0001664;
GO  GO:0051020;
GO  GO:0042802;
GO  GO:0035255;
GO  GO:0140090;
GO  GO:0046872;
GO  GO:0005543;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0005080;
GO  GO:0030971;
GO  GO:0005102;
GO  GO:0005484;
GO  GO:0036294;
GO  GO:0042149;
GO  GO:0097062;
GO  GO:0097061;
GO  GO:0015872;
GO  GO:0021782;
GO  GO:0006886;
GO  GO:0060292;
GO  GO:0015844;
GO  GO:0034316;
GO  GO:0060548;
GO  GO:0010629;
GO  GO:0002092;
GO  GO:0007205;
GO  GO:0006468;
GO  GO:0006605;
GO  GO:0043113;
GO  GO:0034315;
GO  GO:0050796;
GO  GO:0099149;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKG
SQ  KTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTA
SQ  ELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLN
SQ  KAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKME
SQ  LLDQKHVQDIVFQLQRFVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGPNQGGFTDGEDEEEEEEDGAAREVSKDA
SQ  RGATGPTDKGGSWCDS
//
ID  Q19541;
PN  Protein pid-1;
GN  pid;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:24696453, ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Nucleus {ECO:0000269|PubMed:24696453}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Note=Expressed predominantly in the cytoplasm (PubMed:24696453). A small fraction is nuclear or located near the nucleus (PubMed:24696453). Dispersedly distributes throughout the cytoplasm in early embryos (PubMed:31147388). Localizes to puncta in the perinuclear region in the germline syncytium (PubMed:31216475, PubMed:31147388). {ECO:0000269|PubMed:24696453, ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
DR  UNIPROT: Q19541;
DE  Function: Component of the pid-1 variant of the PETISCO complex which is required for the biogenesis of a class of 21 nucleotide PIWI- interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) (PubMed:31147388, PubMed:31216475). Within the complex acts as an adapter which binds to the complex via erh-2 (PubMed:31147388). Involved in the biogenesis of 21U-RNAs which guide the piwi protein prg-1 to its DNA targets for silencing (PubMed:24696453, PubMed:33231880). Plays a role in small RNA-directed transgenerational epigenetic inheritance (PubMed:33231880). {ECO:0000269|PubMed:24696453, ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:33231880, ECO:0000305|PubMed:31216475}.
DE  Reference Proteome: Yes;
DE  Interaction: O61955; IntAct: EBI-21448974; Score: 0.46
DE  Interaction: O76616; IntAct: EBI-21448974; Score: 0.56
DE  Interaction: Q09293; IntAct: EBI-21448974; Score: 0.46
DE  Interaction: Q22640; IntAct: EBI-21448974; Score: 0.35
DE  Interaction: Q18244; IntAct: EBI-21448974; Score: 0.35
DE  Interaction: Q9U2X0; IntAct: EBI-21448974; Score: 0.46
DE  Interaction: O62102; IntAct: EBI-21448974; Score: 0.35
DE  Interaction: Q27488; IntAct: EBI-21448974; Score: 0.46
DE  Interaction: Q20057; IntAct: EBI-21448974; Score: 0.55
DE  Interaction: Q21962; IntAct: EBI-21449552; Score: 0.35
DE  Interaction: P91477; IntAct: EBI-21449552; Score: 0.35
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0034518;
GO  GO:0034585;
GO  GO:0031047;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAKREFSHITLASTPFKKRIDQNSLKTDSDIEKDTNIAHKCAERFNYNTNLHRKVTLSDRFELAALGYEMKAKPRTIIE
SQ  KHNDCDEFHFIYRKEKKNDYGTGSPLSAGLSLSNPLPAGRGFLSPAIQNTSNQFTFSGSPRITPQKHTPVSANHKPARSI
SQ  FDDIPSNIA
//
ID  Q9N3P1;
PN  Protein pid-2;
GN  pid;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:33231880, ECO:0000269|PubMed:33438773}. Cytoplasmic granule {ECO:0000269|PubMed:33438773}. Note=Localizes to perinuclear granules, adjacent to P granules in adult germ cells (PubMed:33438773, PubMed:33231880). These perinuclear granules segregate with germline blastomeres during embryonic development (PubMed:33438773). Localizes to the outer periphery of Z granules, which are liquid-like condensates in the cytoplasm (PubMed:33438773). {ECO:0000269|PubMed:33231880, ECO:0000269|PubMed:33438773}.
DR  UNIPROT: Q9N3P1;
DE  Function: Involved in gene silencing mediated by a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and that guide the Piwi protein prg-1 to its DNA targets for silencing (PubMed:33438773, PubMed:33231880). Not required for the biogenesis of 21U-RNAs (PubMed:33231880). May also be involved in gene silencing mediated by 22G-siRNAs (a class of 22 nucleotide endogenous small interfering RNAs (siRNAs) that possess a triphosphorylated guanine residue at the 5'- end) and 26G-siRNAs (a class of 26 nucleotide siRNAs that possess a guanine residue at the 5'-end) (PubMed:33231880). Required for the biogenesis of secondary and tertiary 22G-siRNAs from many loci (PubMed:33231880). Specifically, promotes the production of 22G-siRNAs from the 5' end of target mRNAs (PubMed:33231880). May play a role in the production of 26G-siRNAs (PubMed:33231880). Plays a role in small RNA-directed transgenerational epigenetic inheritance (also called RNAe) over several generations and germline immortality (PubMed:33438773, PubMed:33231880). Together with the argonaut protein hrde-1, promotes the silencing of the DNA transposable element Tc1 (PubMed:33231880). Required for the formation of liquid-like condensates in the cytoplasm called Z granules, playing a role in maintaining their assembly, viscosity and morphology in adult germ cells, and localization in early embryos (PubMed:33438773, PubMed:33231880). {ECO:0000269|PubMed:33231880, ECO:0000269|PubMed:33438773}.
DE  Reference Proteome: Yes;
DE  Interaction: Q21994; IntAct: EBI-344489; Score: 0.00
DE  Interaction: Q20420; IntAct: EBI-344483; Score: 0.00
DE  Interaction: Q21018; IntAct: EBI-344486; Score: 0.00
DE  Interaction: Q965X6; IntAct: EBI-344492; Score: 0.00
GO  GO:0048471;
GO  GO:0031047;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVIIASHWGPQSKQMLPPEPPRIILREVPVQNNQKEHPPVQEIKTVSSKSKEHRVSSSRKIPDHFDVGPRFYMNVPADG
SQ  SEVFEDDEKDVENECWAVIERIGSEDDKFEASELVEYRDHDWYIALAINKEKTPDKANYQHLLYSYRGGIQRIILTPQQT
SQ  DSIDKTPLVKYKIIGDGLYEVLPIHSSLPQTGLISPKYRYNKGVELRIFGIVNWIDFVLDDDHQTHRTMVWTDAVGPIYL
SQ  SAADRANIRRKLLLTEMQIFAPLRMCHITVKAEFNFSIPDGSPIQWTISSFQPLIEESEKDPNIGRNLWPARVLRFDDLV
SQ  VTKKTPNGYWLKSQRLEGHVNVFAGANQIGIIESAGEKYATKGSMMAFVVPCYQNSTFAYFEALIAGPPRVVMIITEGRF
SQ  LNYCPKTWPPSVRKMRDQYQKEHVLKSEVRSSPICMKQPDYCLKSLRGFSECPF
//
ID  O76616;
PN  Protein pid-3;
GN  pid;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:31147388}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:31147388}. Nucleus {ECO:0000269|PubMed:31216475}. Note=Dispersedly distributes throughout the cytoplasm in early embryos (PubMed:31147388). During early embryogenesis, localizes to the nucleus at prophase of cell division, and remains in the cytosol at interphase in 2- and 4-cell embryos (PubMed:31216475). Localizes to puncta in the perinuclear region in the germline syncytium (PubMed:31147388). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
DR  UNIPROT: O76616;
DR  PDB: 7D1L;
DR  PDB: 7D2Y;
DR  PDB: 7EJS;
DR  PDB: 7O6N;
DR  PDB: 7OCX;
DR  PDB: 7OCZ;
DE  Function: Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Within the pid-1 variant of the PETISCO complex may stabilize 21U-RNA precursor molecules (PubMed:31147388). Promotes the biogenesis of 21U-RNAs (PubMed:31216475). Required for chromosome segregation and cell division in early embryos (PubMed:31216475). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475, ECO:0000305|PubMed:31216475}.
DE  Reference Proteome: Yes;
DE  Interaction: O61955; IntAct: EBI-21449031; Score: 0.35
DE  Interaction: Q09293; IntAct: EBI-2415585; Score: 0.68
DE  Interaction: Q19541; IntAct: EBI-21448974; Score: 0.56
DE  Interaction: A0A1D3PDA8; IntAct: EBI-21449031; Score: 0.35
DE  Interaction: Q18490; IntAct: EBI-21449031; Score: 0.35
DE  Interaction: Q20057; IntAct: EBI-21449031; Score: 0.48
DE  Interaction: Q18244; IntAct: EBI-21449880; Score: 0.35
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0034518;
GO  GO:0034585;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0009792;
GO  GO:0031047;
GO  GO:1990511;
GO  GO:0051781;
GO  GO:0051984;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVAHQKADFKSKWAMVVTVNNLNDKKRADLREFSEWFIETLRLEGAFIGHYFNYEAAPVTIVETLPGNFDSCTNAYQKIH
SQ  KEHPQVVLVVHILPQSQSNEYEWMKVLASRYGFVRQGLLYDNCANRFQNVETDQNSVFRNMCQWIYRSGTAIVRNEGNAC
SQ  GILHGKDPKPTFDKVLFNSEDIKDSVFKVLHAEEEPRGADQENMLKISGYPGMLNTFGIAQLLTPYRVNGITITGAQSAV
SQ  VALENKFQVYQAVQDFNGKKLDRNHKLQVSSLVVSSPAVPLEWPSLKKSKKLVEQVGKPIRLSKVSS
//
ID  O44749;
PN  Protein pid-4;
GN  pid;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:33231880}. Cytoplasm, P-body {ECO:0000269|PubMed:33231880}. Note=Co-localizes with pid-5 at P granules in germ cells. {ECO:0000269|PubMed:33231880}.
DR  UNIPROT: O44749;
DE  Function: Together with pid-5, it is involved in gene silencing mediated by a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and guide the Piwi protein prg-1 to its DNA targets for silencing (PubMed:33231880). Together with pid-5, it is required for the biogenesis of secondary and tertiary 22G-siRNAs (PubMed:33231880). Specifically, promotes the production of 22G-siRNAs from the 5' end of target mRNAs (PubMed:33231880). Together with pid-5, plays a role in small RNA-directed transgenerational epigenetic inheritance (also called RNAe) over several generations and germline immortality (PubMed:33231880). Together with pid-5, plays a role in the formation of liquid-like condensates in the cytoplasm called Z granules (PubMed:33231880). {ECO:0000269|PubMed:33231880}.
DE  Reference Proteome: Yes;
DE  Interaction: Q20655; IntAct: EBI-2418054; Score: 0.49
DE  Interaction: P41932; IntAct: EBI-2419419; Score: 0.49
DE  Interaction: Q17604; IntAct: EBI-16012007; Score: 0.35
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0031047;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNTHNARDSDDESPLESEEHLKRFFAGRNLYSQTKIDDARKKSHDAKYAKEVEWDAKDTAKGKPVFKKYRQEIADKTSRC
SQ  DAQFINNLHTYYGNGSELRELPETHYAVDFMGTTIATTEMTAELKKLKVLKKKTATSQFVREHRQLGFIPTPSRRSLSCT
SQ  GRFMNFETKCDERPDRTNPEFSVGNNNFLSATISNLDEDFKTPSNCEHVASIVPKEISNALTALIPHVNVFDYEKGEMEI
SQ  GKVLCSNKNLHAYVIPKQHDQEQMLKDFSARFLAWYNKLSHLQRDTFGTDKDPKRSGKQEDGKPMKPYFWRVNVILCLQE
SQ  FQEEGTMFRRARHVCGIRPHKSQPGLDLYIEIDTGSMRALKTNYLTVRKLPQEFANVPTPILEVRFEGAKTEEDVARRIA
SQ  HIRKTGRAYIKSFDTGKRKIYQNSFFNGQPKDWSNIETAVLLPPKESSMSKLFCEDRDCMGLCCTDQWLENAESSPGIST
SQ  IPASWIADKNKKPFVDRSPQKFKFPASGSYMKPAN
//
ID  Q9GUI6;
PN  Protein pid-5;
GN  pid;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:33231880}. Cytoplasm, P-body {ECO:0000269|PubMed:33231880}. Note=Co-localizes with pid-4 at P granules in germ cells. {ECO:0000269|PubMed:33231880}.
DR  UNIPROT: Q9GUI6;
DR  UNIPROT: A0A163VU95;
DR  UNIPROT: A0A168HAZ2;
DR  Pfam: PF01321;
DR  Pfam: PF00557;
DR  Pfam: PF16188;
DE  Function: Together with pid-4, it is involved in gene silencing mediated by a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and guide the Piwi protein prg-1 to its DNA targets for silencing (PubMed:33231880). Together with pid-4, it is required for the biogenesis of secondary and tertiary 22G-siRNAs (PubMed:33231880). Specifically, promotes the production of 22G-siRNAs from the 5' end of target mRNAs (PubMed:33231880). Together with pid-4, plays a role in small RNA-directed transgenerational epigenetic inheritance (also called RNAe) over several generations and germline immortality (PubMed:33231880). Together with pid-4, plays a role in the formation of liquid-like condensates in the cytoplasm called Z granules (PubMed:33231880). {ECO:0000269|PubMed:33231880}.
DE  Reference Proteome: Yes;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0070006;
GO  GO:0031047;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTSADDSLPLEDSEECDAYIAKFLRPRTHLFSTVKQEKQRRESHDNKYETAVRSKAIMPSQASKVYRKEMFYSTSKCDS
SQ  RFINNLHTFNTFDGGSGYSEASPHYAMDFVKNKGFADDEMAGHLKSLEVSRKMTENVKWLNDNRNDLKTALRRSNSCPEF
SQ  PIDRDREKITTLRRNEKRNENAKISNFDASFVPELCCSDDYPSILCSIATAFKTVVSRVNAQSIGSGELKIAKVLCSTED
SQ  LFAYVIPKRFNTRDALFAFSNQFRAWLEYKPNVQLYTHYRFINVILYLEEFKHERTEFRRARHVCNLKSRRNHGLFLELD
SQ  TGMLRVVEITPEKVRFLANSWAHNPSAIVEVRFDGVKNEKDISEEIQAIRNTGRATMISFDREHREHMNGKWPNPRTWSS
SQ  LGTVVLRRECTHHKDHSKPPLTRLFCEDRDCIGLCSTGDYFKVPIPEEPNPSHDKLVELRARFASERTLGYTDRTPIAAY
SQ  ILPNTDAHQNELIPDFFSRVQFLNGYSGPSGLAIITLNEAMFWVDNGLLKSAESQVDDRSWTVKEYQSVEEVINWLAKIL
SQ  PPKSKVGFDPTLVSYTWHQQALQSMTSDRFELVAIPGNIVDEIWRMRPFQRGDVVKMLDKNTPEIPVHVKIDRLRKSLKP
SQ  NKCLAAVITSLEDIMWLLNIRGNDLPYNPVTYSYLFITMSDVRLFIDAKRLNDVSKAYFARQSIDVDDYKAASPYIYDWI
SQ  SATKSSFADKKILISPETNYLIGRLIGEDHSMIDPSIMERIKKIKNTDQLKGMRASNLRDSIAIVEFLCKFEKERRDGYT
SQ  FTEYELAADIEEVKTRNREYIGLKQPTIFSAGEHSSVHAHRPDAQKIVFHYQQFMFQTGSHYTDGATNCARTIWDSYPTE
SQ  EFMNQYTLVLKGHIRLASASFPKTLTYGSRLDIFARIALWDAGLDYDHETGHSVGHFLNIRDTQIVIGREPYSSNSIIEA
SQ  GQVMTIEPGYYSEGMYGIRIGNCYETVDVTLSQNDQYFLRFEPLTLIPIQTSIVNKDLLTSEEINWLNKYHFKVFSKIGY
SQ  ILRKENRMEEYDWLFNACQPI
//
ID  Q9TXI7;
PN  Phosphatidylinositol 3-kinase catalytic subunit type 3;
GN  vps;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:11927551}; Peripheral membrane protein {ECO:0000269|PubMed:11927551}. Cytoplasm {ECO:0000269|PubMed:11927551}. Cytoplasmic granule {ECO:0000269|PubMed:11927551}. Cell projection, phagocytic cup {ECO:0000269|PubMed:18425118}. Note=Colocalizes with rab-5 and dyn-1 at the phagocytic cup. {ECO:0000269|PubMed:18425118}.
DR  UNIPROT: Q9TXI7;
DR  UNIPROT: Q5TYK9;
DR  UNIPROT: Q9TXI6;
DR  UNIPROT: Q9XZR0;
DR  Pfam: PF00454;
DR  Pfam: PF00792;
DR  Pfam: PF00613;
DR  PROSITE: PS51547;
DR  PROSITE: PS00915;
DR  PROSITE: PS00916;
DR  PROSITE: PS50290;
DR  PROSITE: PS51545;
DE  Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate (PubMed:11927551). Together with bec-1, mediates the production of phosphatidylinositol 3-phosphate on intracellular vesicles and thereby regulates membrane trafficking (PubMed:11927551, PubMed:16111945). Plays a role in endosome-to-Golgi retrograde transport of mig-14 (PubMed:21183797). Involved in clearance of apoptotic cell corpses by phagosomes (PubMed:22272187). Phagosome maturation requires two sequential and non-overlapping pulses of phosphatidylinositol-3-phosphate (PI3P) on the vesicle surface which mediates recruitment of sortins snx-1 and lst-4 and small GTPases rab- 5, rab-2 and rab-7, downstream of dynamin dyn-1 (PubMed:22272187, PubMed:18425118). The first pulse is initiated by piki-1, then maintained by vps-34 which also produces the second pulse (PubMed:22272187). Required for embryonic development (PubMed:22272187). Together with bec-1, involved in L3/L4 larval molting stage probably by regulating cuticle shedding (PubMed:11927551). Regulates the expansion of the nucleus outer membrane (PubMed:11927551). Involved in the secretion and localization of lrp-1 at the apical surface of hyp7 syncytium (PubMed:16111945). May regulate endocytosis in hypodermal cells (PubMed:11927551). May play a role in the formation of gut granules (a lysosome-related organelle) (PubMed:15843430). Plays a role in germ stem cell proliferation during larval development (PubMed:28285998). {ECO:0000269|PubMed:11927551, ECO:0000269|PubMed:15843430, ECO:0000269|PubMed:16111945, ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:21183797, ECO:0000269|PubMed:22272187, ECO:0000269|PubMed:28285998}.
DE  Reference Proteome: Yes;
DE  Interaction: Q22592; IntAct: EBI-25295921; Score: 0.52
GO  GO:0042995;
GO  GO:0005737;
GO  GO:0005768;
GO  GO:0016020;
GO  GO:0005640;
GO  GO:0005730;
GO  GO:0005777;
GO  GO:0001891;
GO  GO:0000407;
GO  GO:0034271;
GO  GO:0034272;
GO  GO:0016303;
GO  GO:0005524;
GO  GO:0052742;
GO  GO:0000045;
GO  GO:0030242;
GO  GO:0008340;
GO  GO:0042395;
GO  GO:0006897;
GO  GO:0002119;
GO  GO:0006998;
GO  GO:0090386;
GO  GO:0046854;
GO  GO:0036092;
GO  GO:0048015;
GO  GO:0016310;
GO  GO:1901076;
GO  GO:0061365;
GO  GO:0030100;
GO  GO:0051036;
GO  GO:0050708;
GO  GO:0000003;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11927551};
SQ  MIPGMRATPTESFSFVYSCDLQTNVQVKVAEFEGIFRDVLNPVRRLNQLFAEITVYCNNQQIGYPVCTSFHTPPDSSQLA
SQ  RQKLIQKWNEWLTLPIRYSDLSRDAFLHITIWEHEDDEIVNNSTFSRRLVAQSKLSMFSKRGILKSGVIDVQMNVSTTPD
SQ  PFVKQPETWKYSDAWGDEIDLLFKQVTRQSRGLVEDVPWLDPFASRRIEMIRAKYKYSSPDRHVFLVLEMAAIRLGPTFY
SQ  KVVYYEDETKNMRVSTSVNGGVGIVSACTRYCVADPELLLESLAEVKHSAMTRRIRDVEDERHRQVKPNKQAKDRLETIV
SQ  NLPSSQVLTREQRDLVWKFRHYLRQFPKALNKYLRSVNWVHPQEVKTALALMNDWELIEAEDALELLSSAFTHPAVRAYS
SQ  VSRLLEAASPEQVLLYLPQLVQALKYEQGQQLPEEGNPVPVVSEEEGKIPSVATTPTEELEGRDMTVVTKKEARKAASGD
SQ  LATFLIDYALASPKVSNYLYWHLKTEIESTKESKEEHSKMYQNIQDRLMEALVKRPDTRAQVDSLHQQQIFVEDLIILMN
SQ  EAKARGGRLNESKSAEFRTMLSRAKHMLDLKGVHLPLDPSFRLSSVIPDTASFFKSEMMPAKISFKVLQPNGKADRNIPE
SQ  EYTVIFKTGDDLRQDQLIQQMVRLIDIILKKGQLDLKLTPYLVLSTGVGQGFVQCIKSKPLRAIQEQYKAHKMDCIREAM
SQ  KELRPGDGPFGIEPNVIDNYVRSLAGYSVIMYILGLGDRHLDNLLLCENGKLFHVDFGFILGRDPKPMPPPMKLTSEMVQ
SQ  VMGGVKSKQFLEFVQHVDSAYRILRRHSNVLLNLFSLMLDAGIPDIAAEPDKAIFKIEQRLRLDLSDEAATKHIFTQIES
SQ  SLNAKMAMISDIIHAYKQNLM
//
ID  Q96S99;
PN  Pleckstrin homology domain-containing family F member 1;
GN  PLEKHF1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:16188880}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16188880}. Lysosome {ECO:0000269|PubMed:16188880}. Note=Translocates to lysosome during apoptosis.
DR  UNIPROT: Q96S99;
DR  UNIPROT: Q96K11;
DR  UNIPROT: Q9BUB9;
DR  Pfam: PF01363;
DR  Pfam: PF00169;
DR  PROSITE: PS50003;
DR  PROSITE: PS50178;
DR  OMIM: 615200;
DR  DisGeNET: 79156;
DE  Function: May induce apoptosis through the lysosomal-mitochondrial pathway. Translocates to the lysosome initiating the permeabilization of lysosomal membrane (LMP) and resulting in the release of CTSD and CTSL to the cytoplasm. Triggers the caspase-independent apoptosis by altering mitochondrial membrane permeabilization (MMP) resulting in the release of PDCD8. {ECO:0000269|PubMed:16188880}.
DE  Reference Proteome: Yes;
DE  Interaction: P13805; IntAct: EBI-754699; Score: 0.37
DE  Interaction: Q96EK5; IntAct: EBI-757246; Score: 0.37
DE  Interaction: Q96JM7; IntAct: EBI-10293337; Score: 0.56
DE  Interaction: O95810; IntAct: EBI-24333775; Score: 0.56
DE  Interaction: Q9UKJ5; IntAct: EBI-24626977; Score: 0.56
DE  Interaction: Q86SE8; IntAct: EBI-24411098; Score: 0.56
DE  Interaction: O95379; IntAct: EBI-24584209; Score: 0.56
GO  GO:0005769;
GO  GO:0010008;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0035091;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0006915;
GO  GO:0007032;
GO  GO:0008333;
GO  GO:0010508;
GO  GO:2001244;
GO  GO:0072659;
GO  GO:0016050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDHLANTEINSQRIAAVESCFGASGQPLALPGRVLLGEGVLTKECRKKAKPRIFFLFNDILVYGSIVLNKRKYRSQHII
SQ  PLEEVTLELLPETLQAKNRWMIKTAKKSFVVSAASATERQEWISHIEECVRRQLRATGRPPSTEHAAPWIPDKATDICMR
SQ  CTQTRFSALTRRHHCRKCGFVVCAECSRQRFLLPRLSPKPVRVCSLCYRELAAQQRQEEAEEQGAGSPGQPAHLARPICG
SQ  ASSGDDDDSDEDKEGSRDGDWPSSVEFYASGVAWSAFHS
//
ID  Q3TB82;
PN  Pleckstrin homology domain-containing family F member 1;
GN  Plekhf1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:16188880}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16188880}. Lysosome {ECO:0000269|PubMed:16188880}. Note=Translocates to lysosome during apoptosis.
DR  UNIPROT: Q3TB82;
DR  UNIPROT: Q99M16;
DR  Pfam: PF01363;
DR  Pfam: PF00169;
DR  PROSITE: PS50003;
DR  PROSITE: PS50178;
DE  Function: May induce apoptosis through the lysosomal-mitochondrial pathway. Translocates to the lysosome initiating the permeabilization of lysosomal membrane (LMP) and resulting in the release of CTSD and CTSL to the cytoplasm. Triggers the caspase-independent apoptosis by altering mitochondrial membrane permeabilization (MMP) resulting in the release of PDCD8 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005769;
GO  GO:0005768;
GO  GO:0005764;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0035091;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0006915;
GO  GO:0007032;
GO  GO:0008333;
GO  GO:0010508;
GO  GO:2001244;
GO  GO:0072659;
GO  GO:0046902;
GO  GO:0016050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDHLANTEINSQRIAAVESCFGASGQPLALPGRVLLGEGVLTKECRKKAKPRIFFLFNDILVYGSIVLSKRKYRSQHII
SQ  PLEEVTLEPLPETLQAKNRWMIKTAKKSFVVSAASTTERQEWISHIEECVRRQLLATGRQPTTEHAAPWIPDKATDICMR
SQ  CTQTRFSALTRRHHCRKCGFVVCAECSRERFLLPRLSPKPLRVCSLCYRELAAQKLREEAREGIGGSPPQLSHLGGTVCG
SQ  ASSGDDDDSDEDREGNGDGDWPTQVEFYASGVSWSAFHS
//
ID  Q68FU1;
PN  Pleckstrin homology domain-containing family F member 1;
GN  Plekhf1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Lysosome {ECO:0000250}. Note=Translocates to lysosome during apoptosis. {ECO:0000250}.
DR  UNIPROT: Q68FU1;
DR  Pfam: PF01363;
DR  Pfam: PF00169;
DR  PROSITE: PS50003;
DR  PROSITE: PS50178;
DE  Function: May induce apoptosis through the lysosomal-mitochondrial pathway. Translocates to the lysosome initiating the permeabilization of lysosomal membrane (LMP) and resulting in the release of CTSD and CTSL to the cytoplasm. Triggers the caspase-independent apoptosis by altering mitochondrial membrane permeabilization (MMP) resulting in the release of PDCD8 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005769;
GO  GO:0005764;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0035091;
GO  GO:0032266;
GO  GO:0070273;
GO  GO:0010314;
GO  GO:0006915;
GO  GO:0007032;
GO  GO:0008333;
GO  GO:0010508;
GO  GO:2001244;
GO  GO:0072659;
GO  GO:0016050;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDHLANTEINSQRIAAVENCFGASGQPLALPGRVLLGEGVLTKECRKKAKPRIFFLFNDILVYGSIVLSKRKYRSQHII
SQ  PLEEVTLEPLPETLQAKNRWMIKTAKKSFVVSAASTTERQEWISHIEECVRRQLLATGRQPTTEHAAPWIPDKATDICMR
SQ  CTQTRFSALTRRHHCRKCGFVVCAECSRERFLLPRLSPKPLRVCSLCYRELAAQKRREEAKERFRGSPGQLTHLGSTMCG
SQ  ASSGDDDDSDEDREGSGDGDWPTQVEFYASGVSWSAFHS
//
ID  O94827;
PN  Pleckstrin homology domain-containing family G member 5;
GN  PLEKHG5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q66T02}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q66T02}. Cell membrane {ECO:0000250|UniProtKB:Q66T02}. Cell junction {ECO:0000250|UniProtKB:Q66T02}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q66T02}. Note=Predominantly cytoplasmic, however when endothelial cells are stimulated with lysophosphatidic acid, PLEKHG5 is found in perinuclear regions and at the cell membrane. Localizes at cell-cell junctions in quiescent endothelial cells, and relocalizes to cytoplasmic vesicle and the leading edge of lamellipodia in migrating endothelial cells. {ECO:0000250|UniProtKB:Q66T02}.
DR  UNIPROT: O94827;
DR  UNIPROT: B3KU07;
DR  UNIPROT: B7Z2M3;
DR  UNIPROT: B7Z5X2;
DR  UNIPROT: F5GZ21;
DR  UNIPROT: F5H1I0;
DR  UNIPROT: Q5SY17;
DR  UNIPROT: Q5T8W5;
DR  UNIPROT: Q5T8W9;
DR  UNIPROT: Q6ZNM0;
DR  UNIPROT: Q7Z436;
DR  UNIPROT: Q86YD8;
DR  UNIPROT: Q96BS1;
DR  Pfam: PF00621;
DR  PROSITE: PS50010;
DR  PROSITE: PS50003;
DR  OMIM: 611067;
DR  OMIM: 611101;
DR  OMIM: 615376;
DR  DisGeNET: 57449;
DE  Function: Functions as a guanine exchange factor (GEF) for RAB26 and thus regulates autophagy of synaptic vesicles in axon terminal of motoneurons (By similarity). Involved in the control of neuronal cell differentiation (PubMed:11704860). Plays a role in angiogenesis through regulation of endothelial cells chemotaxis. Affects also the migration, adhesion, and matrix/bone degradation in macrophages and osteoclasts (PubMed:23777631). {ECO:0000250|UniProtKB:Q66T02, ECO:0000269|PubMed:11704860, ECO:0000269|PubMed:23777631}.
DE  Disease: Distal spinal muscular atrophy, autosomal recessive, 4 (DSMA4) [MIM:611067]: A neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. DSMA4 is characterized by childhood onset, generalized muscle weakness and atrophy with denervation and normal sensation. Bulbar symptoms and pyramidal signs are absent. {ECO:0000269|PubMed:17564964}. Note=The disease is caused by variants affecting the gene represented in this entry. Charcot-Marie-Tooth disease, recessive, intermediate type, C (CMTRIC) [MIM:615376]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Recessive intermediate forms of Charcot-Marie-Tooth disease are characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. {ECO:0000269|PubMed:23777631, ECO:0000269|PubMed:23844677}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A0A6L7HHZ0; IntAct: EBI-2827572; Score: 0.00
DE  Interaction: A0A5P8YKG0; IntAct: EBI-2846040; Score: 0.00
DE  Interaction: O43865; IntAct: EBI-25250609; Score: 0.56
DE  Interaction: P61587; IntAct: EBI-22760144; Score: 0.56
DE  Interaction: Q15669; IntAct: EBI-22760016; Score: 0.56
DE  Interaction: Q9Y297; IntAct: EBI-21860334; Score: 0.35
DE  Interaction: Q9UKB1; IntAct: EBI-21860334; Score: 0.35
DE  Interaction: Q9P0J1; IntAct: EBI-21860334; Score: 0.35
DE  Interaction: Q9HAV0; IntAct: EBI-21860334; Score: 0.35
DE  Interaction: Q93009; IntAct: EBI-21860334; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21860334; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-21860334; Score: 0.35
DE  Interaction: P62258; IntAct: EBI-21860334; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21860334; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-21860334; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-21903886; Score: 0.35
DE  Interaction: Q8N3R9; IntAct: EBI-21911733; Score: 0.35
DE  Interaction: Q8NI35; IntAct: EBI-21910914; Score: 0.35
GO  GO:0030424;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030139;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005085;
GO  GO:0035767;
GO  GO:0043542;
GO  GO:0043123;
GO  GO:0051056;
GO  GO:0007266;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MHYDGHVRFDLPPQGSVLARNVSTRSCPPRTSPAVDLEEEEEESSVDGKGDRKSTGLKLSKKKARRRHTDDPSKECFTLK
SQ  FDLNVDIETEIVPAMKKKSLGEVLLPVFERKGIALGKVDIYLDQSNTPLSLTFEAYRFGGHYLRVKAPAKPGDEGKVEQG
SQ  MKDSKSLSLPILRPAGTGPPALERVDAQSRRESLDILAPGRRRKNMSEFLGEASIPGQEPPTPSSCSLPSGSSGSTNTGD
SQ  SWKNRAASRFSGFFSSGPSTSAFGREVDKMEQLEGKLHTYSLFGLPRLPRGLRFDHDSWEEEYDEDEDEDNACLRLEDSW
SQ  RELIDGHEKLTRRQCHQQEAVWELLHTEASYIRKLRVIINLFLCCLLNLQESGLLCEVEAERLFSNIPEIAQLHRRLWAS
SQ  VMAPVLEKARRTRALLQPGDFLKGFKMFGSLFKPYIRYCMEEEGCMEYMRGLLRDNDLFRAYITWAEKHPQCQRLKLSDM
SQ  LAKPHQRLTKYPLLLKSVLRKTEEPRAKEAVVAMIGSVERFIHHVNACMRQRQERQRLAAVVSRIDAYEVVESSSDEVDK
SQ  LLKEFLHLDLTAPIPGASPEETRQLLLEGSLRMKEGKDSKMDVYCFLFTDLLLVTKAVKKAERTRVIRPPLLVDKIVCRE
SQ  LRDPGSFLLIYLNEFHSAVGAYTFQASGQALCRGWVDTIYNAQNQLQQLRAQEPPGSQQPLQSLEEEEDEQEEEEEEEEE
SQ  EEEGEDSGTSAASSPTIMRKSSGSPDSQHCASDGSTETLAMVVVEPGDTLSSPEFDSGPFSSQSDETSLSTTASSATPTS
SQ  ELLPLGPVDGRSCSMDSAYGTLSPTSLQDFVAPGPMAELVPRAPESPRVPSPPPSPRLRRRTPVQLLSCPPHLLKSKSEA
SQ  SLLQLLAGAGTHGTPSAPSRSLSELCLAVPAPGIRTQGSPQEAGPSWDCRGAPSPGSGPGLVGCLAGEPAGSHRKRCGDL
SQ  PSGASPRVQPEPPPGVSAQHRKLTLAQLYRIRTTLLLNSTLTASEV
//
ID  Q66T02;
PN  Pleckstrin homology domain-containing family G member 5;
GN  Plekhg5;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16467373}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16467373}. Cell membrane {ECO:0000269|PubMed:16467373}. Cell junction {ECO:0000269|PubMed:21543326}. Cell projection, lamellipodium {ECO:0000269|PubMed:21543326}. Note=Predominantly cytoplasmic, however when endothelial cells are stimulated with lysophosphatidic acid, PLEKHG5 is found in perinuclear regions and at the cell membrane (PubMed:16467373). Localizes at cell-cell junctions in quiescent endothelial cells, and relocalizes to cytoplasmic vesicle and the leading edge of lamellipodia in migrating endothelial cells (PubMed:21543326). {ECO:0000269|PubMed:16467373, ECO:0000269|PubMed:21543326}.
DR  UNIPROT: Q66T02;
DR  UNIPROT: A2A8B6;
DR  UNIPROT: A2A8B7;
DR  UNIPROT: Q66T00;
DR  UNIPROT: Q6P3B1;
DR  UNIPROT: Q6ZQ62;
DR  UNIPROT: Q8R571;
DR  Pfam: PF00621;
DR  PROSITE: PS50010;
DR  PROSITE: PS50003;
DE  Function: Functions as a guanine exchange factor (GEF) for RAB26 and thus regulates autophagy of synaptic vesicles in axon terminal of motoneurons (PubMed:29084947). Involved in the control of neuronal cell differentiation. Plays a role in angiogenesis through regulation of endothelial cells chemotaxis (PubMed:21543326). Affects also the migration, adhesion, and matrix/bone degradation in macrophages and osteoclasts (By similarity). {ECO:0000250|UniProtKB:O94827, ECO:0000269|PubMed:21543326, ECO:0000269|PubMed:29084947}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Z254; IntAct: EBI-9079994; Score: 0.40
DE  Interaction: P02563; IntAct: EBI-9080038; Score: 0.40
DE  Interaction: P35294; IntAct: EBI-11567325; Score: 0.35
DE  Interaction: Q6PK04; IntAct: EBI-25409900; Score: 0.35
DE  Interaction: O75947; IntAct: EBI-25409900; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-25409900; Score: 0.35
DE  Interaction: O75970; IntAct: EBI-25409900; Score: 0.35
DE  Interaction: Q9NUP9; IntAct: EBI-25409900; Score: 0.35
DE  Interaction: Q8NI35; IntAct: EBI-25409900; Score: 0.35
DE  Interaction: O14908; IntAct: EBI-25409900; Score: 0.35
GO  GO:0030424;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0030139;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0005085;
GO  GO:0035767;
GO  GO:0043542;
GO  GO:0099575;
GO  GO:0007266;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGTGPGVSGRRAAARPSSELPSPDSQLLWVGGHAHSSDSQVCHHADCQQLHHRGPLNLCETCDSKFHSTLHYDGHVRFDL
SQ  PPQGSVLARNVSTRSCPPRTSPAADLEEEEEGCTDGKGDRKSAGLKISKKKARRRHTDDPSKECFTLKFDLNVDIETEIV
SQ  PAMKKKSLGEVLLPVFERKGIALGKVDIYLDQSNTPLSLTFEAYRFGGHYLRVKAKPGDEGKVEQGVKDSKSLSLPALRP
SQ  SGAGPPVSERVDPQSRRESSLDILAPGRRRKNMSEFLGEAGIPGHEPPAPSSCSLPVGSSGGTSSGINESWKNRAASRFS
SQ  GFFSSSPSTSAFSREVDKMEQLESKLHAYSLFGLPRMPRRLRFDHDSWEEEEEDDEEDEESSGLRLEDSWRELTDGHEKL
SQ  TRRQCHQQEAVWELLHTEVSYIRKLRVITNLFLCCLLNLQESGLLCEVEAERLFSNIPEIAKLHRGLWGSVMVPVLEKAR
SQ  RTRALLQPSDFLKGFKMFGSLFKPYIRYCMEEEGCMEYMRGLLRDNDLFRAYVTWAEKHQQCQRLKLSDMLAKPHQRLTK
SQ  YPLLLKSVLRKTDDPRTKEAIVTMISSVERFIHHVNTCMRQRQERQRLAGVVSRIDAYEVVEGSNDEVDKLLKEFLHLDL
SQ  TAPMPGTSPEETRQLLLEGSLRMKEGKDSKMDVYCFLFTDLLLVTKAVKKAERTKVIRPPLLVDKIVCRELRDPGSFLLI
SQ  YLNEFHSAVGAYTFQASSQALCRSWVDTIYNAQNQLQQLRAQLSAQEHPGSQHLQSLEEEEDEQEEEGEESGTSAASSPT
SQ  ILRKSSNSLDSEHCTSDGSTETLAMVVVEPGATLSSPEFEGGPVSSQSDESSLSNTASSVTPTSELLPLGPVDGRSCSMD
SQ  SAYGTLSPTSLQDFVAPHPVVEPAPVPQTPSPQPSPRLRRRTPVQLLPRPPRLLKSKSEASLLQLLSGTPAARGVPPAPS
SQ  RSLSELCLISVAPGVRTQRPLQEGGPGWNGPGMCDPCHGPQLSESENRPSHMTGGPADSARRRCREMPSGTMSRVQSEPP
SQ  SGVSAQHRKLTLAQLYRIRTTLLLNSTLTASEV
//
ID  Q6RFZ7;
PN  Pleckstrin homology domain-containing family G member 5;
GN  Plekhg5;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16467373}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16467373}. Cell membrane {ECO:0000269|PubMed:16467373}. Cell junction {ECO:0000250|UniProtKB:Q66T02}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q66T02}. Note=Predominantly cytoplasmic, however when endothelial cells are stimulated with lysophosphatidic acid, PLEKHG5 is found in perinuclear regions and at the cell membrane (PubMed:16467373). Localizes at cell-cell junctions in quiescent endothelial cells, and relocalizes to cytoplasmic vesicle and the leading edge of lamellipodia in migrating endothelial cells (By similarity). {ECO:0000250|UniProtKB:Q66T02, ECO:0000269|PubMed:16467373}.
DR  UNIPROT: Q6RFZ7;
DR  Pfam: PF00621;
DR  PROSITE: PS50010;
DR  PROSITE: PS50003;
DE  Function: Functions as a guanine exchange factor (GEF) for RAB26 and thus regulates autophagy of synaptic vesicles in axon terminal of motoneurons (By similarity). Involved in the control of neuronal cell differentiation. Plays a role in angiogenesis through regulation of endothelial cells chemotaxis. Affects also the migration, adhesion, and matrix/bone degradation in macrophages and osteoclasts (By similarity). {ECO:0000250|UniProtKB:O94827, ECO:0000250|UniProtKB:Q66T02}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Z254; IntAct: EBI-9079906; Score: 0.46
GO  GO:0030424;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0030139;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0005085;
GO  GO:0035767;
GO  GO:0043542;
GO  GO:0099575;
GO  GO:0007266;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDKGRAAKVCHHADCQQLHHRGPLNLCEICDSKFHNTTHYDGHVRFDLPPQGSVLARNVSTRSCPPRTSPAGDLEEEDEG
SQ  YTNGKGDRKSAGLKISKKKARRRHTDDPSKECFTLKFDLNVDIETEIVPAMKKKSLGEVLLPVFERKGIALGKVDIYLDQ
SQ  SNTPLSLTFEAYRFGGHYLRVKAKPGDEGKVEQGVKDSKSLSLPALRPSGAGTPVLERVDPQSRRESSLDILAPGRRRKN
SQ  MSEFLGDTSIPGQESPAPSSCSLPVGSSVGSSGSSESWKNRAASRFSGFFSSSPSTGAFGREVDKMEQLESKLHAYSLFG
SQ  LPRMPRRLRFDHDSWEEEEDDEEEEDNSGLRLEDSWRELIDGHEKLTRRQCHQQEAVWELLHTEVSYIRKLRVITNLFLC
SQ  CLLNLQESGLLCEVEAERLFSNIPELARLHRGLWSSVMVPVLEKARRTRALLQPSDFLKGFKMFGSLFKPYIRYCMEEEG
SQ  CMEYMRSLLRDNDLFRAYVTWAEKHQQCQRLKLSDMLAKPHQRLTKYPLLLKSVLRKTDEPRAKEAIITMISSVERFIHH
SQ  VNTCMRQRQERQRLAGVVSRIDAYEVVEGSNDEVDKFLKEFLHLDLTAPMPGTSPEETRQLLLEGSLRMKEGKDSKMDVY
SQ  CFLFTDLLLVTKAVKKAERTKVIRPPLLVDKIVCRELRDPGSFLLIHLNEFHSAVGAYTFQASSQALCRSWVDTLYNAQN
SQ  QLQQLRAQLLCAQEHPGTQHLQSLEEEEDEQEEEGEESGTSAASSPTILRKSSNSLDSEHCASDGSTETLAMVVVEPGET
SQ  LSSPEFDRGPFSSQSDEASLSNTTSSITPTSELLPLGPVDGRSCSMDSAYGTLSPTSLQDFAAPHPVVEPVPVPQTLSPQ
SQ  PSPRLRRRTPVQLLPRLPHLLKSKSEASLLQLLSGTTTSVSPPAPSRSLSELCLITMAPGVRTQSSLQEGGPGWNCPGAC
SQ  GPCQGPPLSESENRPSHKAGGPADSARRKCREMPCGTVPRVQPEPSPGISAQHRKLTLAQLYRIRTTLLLNSTLTASEV
//
ID  Q6P5Z2;
PN  Serine/threonine-protein kinase N3;
GN  PKN3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10441506}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10441506}. Note=Nuclear and perinuclear Golgi region.
DR  UNIPROT: Q6P5Z2;
DR  UNIPROT: Q9UM03;
DR  Pfam: PF02185;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS51860;
DR  OMIM: 610714;
DR  DisGeNET: 29941;
DE  Function: Contributes to invasiveness in malignant prostate cancer. {ECO:0000269|PubMed:15282551}.
DE  Reference Proteome: Yes;
DE  Interaction: A1A4S6; IntAct: EBI-1390955; Score: 0.68
DE  Interaction: O00165; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: O15027; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: O96018; IntAct: EBI-21604776; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q13393; IntAct: EBI-7796971; Score: 0.54
DE  Interaction: Q15569; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q22038; IntAct: EBI-8669452; Score: 0.54
DE  Interaction: Q9UNA1; IntAct: EBI-1390909; Score: 0.68
DE  Interaction: Q8IVD9; IntAct: EBI-9395191; Score: 0.35
DE  Interaction: P17918; IntAct: EBI-10999136; Score: 0.35
DE  Interaction: Q96BD8; IntAct: EBI-11000226; Score: 0.35
DE  Interaction: Q9UKF6; IntAct: EBI-11006031; Score: 0.35
DE  Interaction: O95235; IntAct: EBI-11007956; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-11009211; Score: 0.35
DE  Interaction: Q62376; IntAct: EBI-11015551; Score: 0.35
DE  Interaction: Q8BQ46; IntAct: EBI-11018041; Score: 0.35
DE  Interaction: Q96L14; IntAct: EBI-11022408; Score: 0.35
DE  Interaction: P19788; IntAct: EBI-11032999; Score: 0.35
DE  Interaction: Q9EQU5; IntAct: EBI-11047846; Score: 0.35
DE  Interaction: Q9D8B3; IntAct: EBI-11052854; Score: 0.35
DE  Interaction: P62714; IntAct: EBI-11056306; Score: 0.35
DE  Interaction: P67775; IntAct: EBI-11058007; Score: 0.35
DE  Interaction: P58771; IntAct: EBI-11063826; Score: 0.35
DE  Interaction: Q9Z2X1; IntAct: EBI-11066678; Score: 0.35
DE  Interaction: D3Z482; IntAct: EBI-11073201; Score: 0.35
DE  Interaction: Q13033; IntAct: EBI-11077798; Score: 0.35
DE  Interaction: P23258; IntAct: EBI-11085623; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-11088773; Score: 0.35
DE  Interaction: Q91YI4; IntAct: EBI-11102575; Score: 0.35
DE  Interaction: Q9UBN7; IntAct: EBI-11116627; Score: 0.35
DE  Interaction: P55795; IntAct: EBI-11129092; Score: 0.35
DE  Interaction: Q9P2B7; IntAct: EBI-11131339; Score: 0.35
DE  Interaction: Q14134; IntAct: EBI-11137164; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-11139064; Score: 0.35
DE  Interaction: P62937; IntAct: EBI-11141455; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-11152836; Score: 0.35
DE  Interaction: Q13352; IntAct: EBI-11156428; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-11897791; Score: 0.35
DE  Interaction: Q5JR59; IntAct: EBI-24358565; Score: 0.56
DE  Interaction: Q9UBB9; IntAct: EBI-25244295; Score: 0.56
DE  Interaction: Q8N1B4; IntAct: EBI-25245406; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-25247991; Score: 0.56
DE  Interaction: Q15323; IntAct: EBI-24477843; Score: 0.56
DE  Interaction: Q8ND90; IntAct: EBI-24507203; Score: 0.56
DE  Interaction: O95619; IntAct: EBI-11918232; Score: 0.00
DE  Interaction: Q6NZI2; IntAct: EBI-11917959; Score: 0.00
DE  Interaction: O43482; IntAct: EBI-11918214; Score: 0.00
DE  Interaction: O15516; IntAct: EBI-11918205; Score: 0.00
DE  Interaction: O00327; IntAct: EBI-11918196; Score: 0.00
DE  Interaction: O00233; IntAct: EBI-11918187; Score: 0.00
DE  Interaction: Q5R372; IntAct: EBI-11918178; Score: 0.00
DE  Interaction: O43815; IntAct: EBI-11918223; Score: 0.00
DE  Interaction: Q8TBA6; IntAct: EBI-11918349; Score: 0.00
DE  Interaction: Q8TD31; IntAct: EBI-11918358; Score: 0.00
DE  Interaction: Q7Z4H7; IntAct: EBI-11918331; Score: 0.00
DE  Interaction: Q6NSJ2; IntAct: EBI-11918322; Score: 0.00
DE  Interaction: Q5VIR6; IntAct: EBI-11918313; Score: 0.00
DE  Interaction: Q5T0U0; IntAct: EBI-11918304; Score: 0.00
DE  Interaction: Q567U6; IntAct: EBI-11918295; Score: 0.00
DE  Interaction: Q53HC9; IntAct: EBI-11918286; Score: 0.00
DE  Interaction: Q4V328; IntAct: EBI-11918277; Score: 0.00
DE  Interaction: Q15276; IntAct: EBI-11918268; Score: 0.00
DE  Interaction: Q14161; IntAct: EBI-11918259; Score: 0.00
DE  Interaction: P61244; IntAct: EBI-11918250; Score: 0.00
DE  Interaction: P0C1Z6; IntAct: EBI-11918241; Score: 0.00
DE  Interaction: Q9BZD4; IntAct: EBI-11918402; Score: 0.00
DE  Interaction: Q96P16; IntAct: EBI-11918393; Score: 0.00
DE  Interaction: Q96JG6; IntAct: EBI-11918385; Score: 0.00
DE  Interaction: Q96EK4; IntAct: EBI-11918376; Score: 0.00
DE  Interaction: Q96BD5; IntAct: EBI-11918367; Score: 0.00
DE  Interaction: Q86Y13; IntAct: EBI-11918340; Score: 0.00
DE  Interaction: Q9Y3A3; IntAct: EBI-11918474; Score: 0.00
DE  Interaction: Q9Y2X7; IntAct: EBI-11918465; Score: 0.00
DE  Interaction: Q9UKL0; IntAct: EBI-11918456; Score: 0.00
DE  Interaction: Q9UJ41; IntAct: EBI-11918447; Score: 0.00
DE  Interaction: Q9UID3; IntAct: EBI-11918438; Score: 0.00
DE  Interaction: Q9NP66; IntAct: EBI-11918429; Score: 0.00
DE  Interaction: Q9NNX1; IntAct: EBI-11918420; Score: 0.00
DE  Interaction: Q9HCH0; IntAct: EBI-11918411; Score: 0.00
DE  Interaction: Q9H8J5; IntAct: EBI-21537025; Score: 0.35
DE  Interaction: Q15768; IntAct: EBI-21537920; Score: 0.35
DE  Interaction: P04201; IntAct: EBI-21538834; Score: 0.35
DE  Interaction: O60232; IntAct: EBI-21543889; Score: 0.35
DE  Interaction: Q8TDQ0; IntAct: EBI-21556046; Score: 0.35
DE  Interaction: Q9Y279; IntAct: EBI-21556596; Score: 0.35
DE  Interaction: O15460; IntAct: EBI-21563604; Score: 0.35
DE  Interaction: Q96F46; IntAct: EBI-21578337; Score: 0.35
DE  Interaction: P52799; IntAct: EBI-21582984; Score: 0.35
DE  Interaction: Q9Y5G3; IntAct: EBI-21584582; Score: 0.35
DE  Interaction: Q86WV1; IntAct: EBI-21601309; Score: 0.35
DE  Interaction: P43115; IntAct: EBI-21607127; Score: 0.35
DE  Interaction: A8K8V0; IntAct: EBI-21612043; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-21650356; Score: 0.35
DE  Interaction: P37173; IntAct: EBI-21668347; Score: 0.35
DE  Interaction: Q8N831; IntAct: EBI-21684562; Score: 0.35
DE  Interaction: Q6ZN54; IntAct: EBI-21689078; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-21721324; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20749487; Score: 0.35
DE  Interaction: Q8NB46; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q9Y4W2; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q9Y4I1; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q9UNE7; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q9ULX6; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q9UJP4; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q9NWS0; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q9NNW5; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q9HD67; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q9H6T3; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q9H4I3; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q99733; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q96TA2; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q96K37; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q96IX5; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q96EY1; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q93008; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q8NF37; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q8NEJ9; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q86VI3; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q69YQ0; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q5XKP0; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q5T9A4; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q14318; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q13557; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q13555; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q13554; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q13451; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q01813; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q00587; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: P43307; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: P42356; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: P30876; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: P30154; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: P27708; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: P09543; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: P00367; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: O94763; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: O43819; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: O43251; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: O14773; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: O14654; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: O00459; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: O00170; IntAct: EBI-28941754; Score: 0.35
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0031267;
GO  GO:0010631;
GO  GO:0035556;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEEGAPRQPGPSQWPPEDEKEVIRRAIQKELKIKEGVENLRRVATDRRHLGHVQQLLRSSNRRLEQLHGELRELHARILL
SQ  PGPGPGPAEPVASGPRPWAEQLRARHLEALRRQLHVELKVKQGAENMTHTCASGTPKERKLLAAAQQMLRDSQLKVALLR
SQ  MKISSLEASGSPEPGPELLAEELQHRLHVEAAVAEGAKNVVKLLSSRRTQDRKALAEAQAQLQESSQKLDLLRLALEQLL
SQ  EQLPPAHPLRSRVTRELRAAVPGYPQPSGTPVKPTALTGTLQVRLLGCEQLLTAVPGRSPAAALASSPSEGWLRTKAKHQ
SQ  RGRGELASEVLAVLKVDNRVVGQTGWGQVAEQSWDQTFVIPLERARELEIGVHWRDWRQLCGVAFLRLEDFLDNACHQLS
SQ  LSLVPQGLLFAQVTFCDPVIERRPRLQRQERIFSKRRGQDFLRASQMNLGMAAWGRLVMNLLPPCSSPSTISPPKGCPRT
SQ  PTTLREASDPATPSNFLPKKTPLGEEMTPPPKPPRLYLPQEPTSEETPRTKRPHMEPRTRRGPSPPASPTRKPPRLQDFR
SQ  CLAVLGRGHFGKVLLVQFKGTGKYYAIKALKKQEVLSRDEIESLYCEKRILEAVGCTGHPFLLSLLACFQTSSHACFVTE
SQ  FVPGGDLMMQIHEDVFPEPQARFYVACVVLGLQFLHEKKIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFC
SQ  GTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEEEVFDCIVNMDAPYPGFLSVQGLEFIQKLLQKCPEK
SQ  RLGAGEQDAEEIKVQPFFRTTNWQALLARTIQPPFVPTLCGPADLRYFEGEFTGLPPALTPPAPHSLLTARQQAAFRDFD
SQ  FVSERFLEP
//
ID  Q8K045;
PN  Serine/threonine-protein kinase N3;
GN  Pkn3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear and perinuclear Golgi region. {ECO:0000250}.
DR  UNIPROT: Q8K045;
DR  Pfam: PF02185;
DR  Pfam: PF00069;
DR  Pfam: PF00433;
DR  PROSITE: PS51285;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  PROSITE: PS51860;
DE  Function: Contributes to invasiveness in malignant prostate cancer. {ECO:0000269|PubMed:15282551}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0004698;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0031267;
GO  GO:0010631;
GO  GO:0035556;
GO  GO:0018105;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEHRKPGTGQRAPKDEKEMVRRAIQKELKIKEGMENMRRVATDRRHLGHVQQLLRASNRRLEQLHGELRELHAQVLLPAS
SQ  AEPVTSEPQPRAEQSRARLSEALHRQLQVELKVKQGAENMIHTCASGTPKERKLLAAAQQMLKDSQLKVALLRMKISSLE
SQ  SSGSPEPGPDLLAEELQHRLRVEAAVAAGAKNVVKLLGGQRMQDRKALAEAQAQLQESSQKLDLLRLALELLLERLPPTH
SQ  SLRSRVTQELWMAMLGNPQPLGTLVKPIALTGTLQVRLLGCKDLLVAVPGRSPMAVLAGSPSESWLRTRSRQQRGGGELA
SQ  SEVLAVLKVDNRVVGQTGWGLVAEKSWDQSFIISLDRARELEIGVHWRDWRQLCGVAFLKLEDFLDNACHQLSLSLVPQG
SQ  RLFAQVTFCEPVIERRPRLQRQRCIFSKRRGRDFMRASQMNLSMAAWGRLVMSLLPPCSSPNTASPPKGRPSTAVCGTPS
SQ  AASPSNFLPMKTLSKEDTKPPPKPPRLYLQEPAPGTPCTKRPHMDPRPAVVPALAALSTRKPPRLQDFRCLAVLGRGHFG
SQ  KVLLVQYKGTGKYYAIKALKKQEVLGRDEIDSLYCEKRILETVGRTGHPFLLSLLACLQTSSHACFVTEFLPGGDLMAQI
SQ  HEDVFPEPQACFYLACVVLGLQFLHEKRIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVL
SQ  TQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEEEVFECIVSADVPCPHFLSVQGLELIQKLLQKSPEKRLGAGERDAEE
SQ  IKVQPFFRTTNWQALLARTVQPPFVPTLCGPADLRYFEGEFTSLPPTLTPPVSQSSLTARQQAAFRDFDFVSEQFLES
//
ID  P53816;
PN  Phospholipase A and acyltransferase 3;
GN  PLAAT3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P53817}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:17374643}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8R3U1}. Peroxisome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q8R3U1}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum, nuclear envelope and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain. {ECO:0000250|UniProtKB:Q8R3U1}.
DR  UNIPROT: P53816;
DR  UNIPROT: B2R7Q4;
DR  UNIPROT: B7XAK5;
DR  UNIPROT: Q3SYI3;
DR  UNIPROT: Q9HDD1;
DR  PDB: 2KYT;
DR  PDB: 4DOT;
DR  PDB: 4FA0;
DR  PDB: 4Q95;
DR  PDB: 7C3Z;
DR  PDB: 7C41;
DR  Pfam: PF04970;
DR  PROSITE: PS51934;
DR  OMIM: 613867;
DR  DisGeNET: 11145;
DE  Function: Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:22923616). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N- acylphosphatidylethanolamine (NAPE), which serves as precursor for N- acylethanolamines (NAEs) (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity). {ECO:0000250|UniProtKB:Q8R3U1, ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:22923616, ECO:0000303|PubMed:26503625}. (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878). The lipid- modifying enzyme activity is required for this process (PubMed:28077878). {ECO:0000269|PubMed:28077878}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UMX0; IntAct: EBI-755041; Score: 0.78
DE  Interaction: Q9NRR5; IntAct: EBI-954950; Score: 0.00
DE  Interaction: P30153; IntAct: EBI-1224594; Score: 0.64
DE  Interaction: Q9UHD9; IntAct: EBI-24275391; Score: 0.56
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0031966;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005778;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:0052740;
GO  GO:0016746;
GO  GO:0008289;
GO  GO:0016410;
GO  GO:0052739;
GO  GO:0008970;
GO  GO:0004623;
GO  GO:0046485;
GO  GO:0070306;
GO  GO:0016042;
GO  GO:0051179;
GO  GO:0030397;
GO  GO:0070292;
GO  GO:1903008;
GO  GO:0007031;
GO  GO:0036152;
GO  GO:0008654;
GO  GO:0006644;
GO  GO:1904177;
GO  GO:0009617;
GO  GO:0006641;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKH
SQ  DDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASVAGMGLAAMSLIGVMFSRNKRQ
SQ  KQ
//
ID  Q8R3U1;
PN  Phospholipase A and acyltransferase 3;
GN  Plaat3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P53817}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:33854238}. Cytoplasm, cytosol {ECO:0000269|PubMed:33854238}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18614531}. Peroxisome membrane {ECO:0000269|PubMed:22134920}; Single-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:33854238}. Lysosome membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:33854238}; Single-pass membrane protein {ECO:0000305}. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum, nuclear envelope and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain. {ECO:0000269|PubMed:33854238}.
DR  UNIPROT: Q8R3U1;
DR  UNIPROT: B7X6T3;
DR  UNIPROT: Q3V3C3;
DR  UNIPROT: Q8BWF7;
DR  Pfam: PF04970;
DR  PROSITE: PS51934;
DE  Function: Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19047760). Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:18614531, PubMed:19047760, PubMed:19136964, PubMed:22134920). For most substrates, PLA1 activity is much higher than PLA2 activity (By similarity). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity,catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19047760). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light (PubMed:33854238). Organelle membrane degradation is probably catalyzed by the phospholipase activity (PubMed:33854238). {ECO:0000250|UniProtKB:P53816, ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19136964, ECO:0000269|PubMed:22134920, ECO:0000269|PubMed:33854238}. (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). {ECO:0000269|PubMed:28077878}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0016020;
GO  GO:0031966;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005778;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:0052740;
GO  GO:0016410;
GO  GO:0052739;
GO  GO:0008970;
GO  GO:0004623;
GO  GO:0004620;
GO  GO:0046485;
GO  GO:0070306;
GO  GO:0016042;
GO  GO:0030397;
GO  GO:0070292;
GO  GO:0045786;
GO  GO:1903008;
GO  GO:0007031;
GO  GO:0008654;
GO  GO:0006644;
GO  GO:1904177;
GO  GO:0009617;
GO  GO:0006641;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLAPIPEPKPGDLIEIFRPMYRHWAIYVGDGYVIHLAPPSEIAGAGAASIMSALTDKAIVKKELLCHVAGKDKYQVNNKH
SQ  DEEYTPLPLSKIIQRAERLVGQEVLYRLTSENCEHFVNELRYGVPRSDQVRDAVKAVGIAGVGLAALGLVGVMLSRNKKQ
SQ  KQ
//
ID  Q5R611;
PN  Phospholipase A and acyltransferase 3;
GN  PLAAT3;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P53817}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P53816}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8R3U1}. Peroxisome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q8R3U1}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum, nuclear envelope and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain. {ECO:0000250|UniProtKB:Q8R3U1}.
DR  UNIPROT: Q5R611;
DR  Pfam: PF04970;
DR  PROSITE: PS51934;
DE  Function: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (By similarity). For most substrates, PLA1 activity is much higher than PLA2 activity (By similarity). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (By similarity). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity). {ECO:0000250|UniProtKB:P53816, ECO:0000250|UniProtKB:Q8R3U1}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0031966;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005778;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:0052740;
GO  GO:0016410;
GO  GO:0052739;
GO  GO:0008970;
GO  GO:0004623;
GO  GO:0004620;
GO  GO:0046485;
GO  GO:0070306;
GO  GO:0016042;
GO  GO:0030397;
GO  GO:0070292;
GO  GO:1903008;
GO  GO:0007031;
GO  GO:1904177;
GO  GO:0006641;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKH
SQ  DDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASAAGMGLAAMSLIGVMFSRNKRQ
SQ  KQ
//
ID  P53817;
PN  Phospholipase A and acyltransferase 3;
GN  Plaat3;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:8290259}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:8290259}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8290259}. Peroxisome membrane {ECO:0000250|UniProtKB:Q8R3U1}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q8R3U1}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein {ECO:0000305}. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum, nuclear envelope and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain. {ECO:0000250|UniProtKB:Q8R3U1}.
DR  UNIPROT: P53817;
DR  UNIPROT: B7X6T2;
DR  Pfam: PF04970;
DR  PROSITE: PS51934;
DE  Function: Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19047760). Shows phospholipase A1 (PLA1) and A2 (PLA2), ccatalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19047760). For most substrates, PLA1 activity is much higher than PLA2 activity (By similarity). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:17158102, PubMed:19047760). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity). {ECO:0000250|UniProtKB:P53816, ECO:0000250|UniProtKB:Q8R3U1, ECO:0000269|PubMed:17158102, ECO:0000269|PubMed:19047760}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0016020;
GO  GO:0031966;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005778;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:0052740;
GO  GO:0016410;
GO  GO:0052739;
GO  GO:0008970;
GO  GO:0004623;
GO  GO:0004620;
GO  GO:0046485;
GO  GO:0070306;
GO  GO:0016042;
GO  GO:0030397;
GO  GO:0070292;
GO  GO:0045786;
GO  GO:1903008;
GO  GO:0007031;
GO  GO:0008654;
GO  GO:0006644;
GO  GO:1904177;
GO  GO:0009617;
GO  GO:0006641;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPIPEPKPGDLIEIFRPMYSHWAIYVGDGYVIHLAPPSEIPGAGAASIMSALTDKAIVKKELLRDVAGKDKYQVNNKHDK
SQ  EYTPLPLNKIIQRAEELVGQEVLYRLTSENCEHFVNELRYGVPRSDQVRDAVKVATVTGVGLAALGLIGVMLSRNKKQKQ
//
ID  P10894;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;
GN  PLCB1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}. Cytoplasm {ECO:0000250|UniProtKB:P10687}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}.
DR  UNIPROT: P10894;
DR  Pfam: PF06631;
DR  Pfam: PF09279;
DR  Pfam: PF17787;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  Pfam: PF08703;
DR  PROSITE: PS50004;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5- bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein- coupled receptors. Regulates the function of the endothelial barrier. {ECO:0000250|UniProtKB:Q9Z1B3}.
DE  Reference Proteome: Yes;
DE  Interaction: P70441; IntAct: EBI-7385831; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005509;
GO  GO:0005516;
GO  GO:0019899;
GO  GO:0005096;
GO  GO:0004435;
GO  GO:0005546;
GO  GO:0007420;
GO  GO:0070498;
GO  GO:0035722;
GO  GO:0035723;
GO  GO:0016042;
GO  GO:0007613;
GO  GO:0046488;
GO  GO:0048015;
GO  GO:0046330;
GO  GO:0051726;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9Z1B3};
SQ  MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWEDDSTVVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKA
SQ  PKDPKLRELLDVGNIGRLEHRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLK
SQ  LQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
SQ  TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLAKKGQISVDGFMRYLSGEENGVVSPEKLDLNEDMSQ
SQ  PLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAF
SQ  KTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLDKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
SQ  KLSEQASNTYSDSSSVFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKK
SQ  RNRSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLAMQINMGMY
SQ  EYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
SQ  NAVNPIWEEEPIVFKKVVLPSLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLMLPALFVYIEVKDYVP
SQ  DTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETPSEAPSEARPTPAENGVNHTTSLTPKPPSQALH
SQ  SQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYL
SQ  RRRAALEKTAKKDNKKKSEPSSPDHVSSTIEQDLAALDAEMTQKLVDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQ
SQ  KLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKR
SQ  QEKLVEKHKEIRQQILDEKPKLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHSSAPPLMTSDSGKLNQKPPSS
SQ  EELEGENPGKEFDTPL
//
ID  Q9NQ66;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;
GN  PLCB1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}. Cytoplasm {ECO:0000250|UniProtKB:P10687}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}.
DR  UNIPROT: Q9NQ66;
DR  UNIPROT: D3DW12;
DR  UNIPROT: D3DW13;
DR  UNIPROT: O60325;
DR  UNIPROT: Q17RQ6;
DR  UNIPROT: Q5TFF7;
DR  UNIPROT: Q5TGC9;
DR  UNIPROT: Q8IV93;
DR  UNIPROT: Q9BQW2;
DR  UNIPROT: Q9H4H2;
DR  UNIPROT: Q9H8H5;
DR  UNIPROT: Q9NQ65;
DR  UNIPROT: Q9NQH9;
DR  UNIPROT: Q9NTH4;
DR  UNIPROT: Q9UJP6;
DR  UNIPROT: Q9UM26;
DR  Pfam: PF06631;
DR  Pfam: PF09279;
DR  Pfam: PF17787;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  Pfam: PF08703;
DR  PROSITE: PS50004;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DR  OMIM: 607120;
DR  OMIM: 613722;
DR  DisGeNET: 23236;
DE  Function: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5- bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein- coupled receptors (PubMed:9188725). Regulates the function of the endothelial barrier. {ECO:0000250|UniProtKB:Q9Z1B3, ECO:0000269|PubMed:9188725}.
DE  Disease: Developmental and epileptic encephalopathy 12 (DEE12) [MIM:613722]: A form of epilepsy characterized by frequent tonic seizures or spasms beginning in infancy with a specific EEG finding of suppression-burst patterns, characterized by high-voltage bursts alternating with almost flat suppression phases. Patients may progress to West syndrome, which is characterized by tonic spasms with clustering, arrest of psychomotor development, and hypsarrhythmia on EEG. {ECO:0000269|PubMed:20833646}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q01082; IntAct: EBI-3447119; Score: 0.00
DE  Interaction: P56545; IntAct: EBI-10311798; Score: 0.56
DE  Interaction: Q12800; IntAct: EBI-10311808; Score: 0.56
DE  Interaction: Q13363; IntAct: EBI-10311818; Score: 0.56
DE  Interaction: Q8TAP6; IntAct: EBI-10311838; Score: 0.56
DE  Interaction: Q7KYR7; IntAct: EBI-21541130; Score: 0.35
DE  Interaction: P43115; IntAct: EBI-21607127; Score: 0.35
DE  Interaction: Q6ZN54; IntAct: EBI-21689078; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: P05067; IntAct: EBI-20821761; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-20901888; Score: 0.40
DE  Interaction: Q02539; IntAct: EBI-20928184; Score: 0.40
DE  Interaction: P04156; IntAct: EBI-21014654; Score: 0.35
DE  Interaction: Q969F8; IntAct: EBI-21282024; Score: 0.40
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0098982;
GO  GO:0098978;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0098794;
GO  GO:0032991;
GO  GO:0005509;
GO  GO:0005516;
GO  GO:0019899;
GO  GO:0005096;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0004435;
GO  GO:0005546;
GO  GO:0004629;
GO  GO:0060466;
GO  GO:1902618;
GO  GO:1905631;
GO  GO:1904637;
GO  GO:1904117;
GO  GO:0021987;
GO  GO:0045444;
GO  GO:0007213;
GO  GO:0007186;
GO  GO:0000086;
GO  GO:0007215;
GO  GO:0032957;
GO  GO:0048009;
GO  GO:0070498;
GO  GO:0035722;
GO  GO:0035723;
GO  GO:0007612;
GO  GO:0007613;
GO  GO:0045892;
GO  GO:2000438;
GO  GO:0031161;
GO  GO:0046488;
GO  GO:0048015;
GO  GO:2000344;
GO  GO:2000560;
GO  GO:0048639;
GO  GO:0045893;
GO  GO:0040019;
GO  GO:1900087;
GO  GO:0032735;
GO  GO:0046330;
GO  GO:0045663;
GO  GO:0099170;
GO  GO:1903140;
GO  GO:0080154;
GO  GO:0008277;
GO  GO:0099178;
GO  GO:0007165;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9Z1B3};
SQ  MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGRHAKA
SQ  PKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLK
SQ  LQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
SQ  TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLSGEENGVVSPEKLDLNEDMSQ
SQ  PLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAF
SQ  KTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
SQ  KLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKK
SQ  RNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMY
SQ  EYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
SQ  NAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVP
SQ  DTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALH
SQ  SQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYL
SQ  RRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQ
SQ  KLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKR
SQ  QEKLVEKHKEIRQQILDEKPKLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSS
SQ  EELGGDIPGKEFDTPL
//
ID  Q9Z1B3;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;
GN  Plcb1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:18802028}. Cytoplasm {ECO:0000250|UniProtKB:P10687}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000269|PubMed:18802028}.
DR  UNIPROT: Q9Z1B3;
DR  UNIPROT: Q62075;
DR  UNIPROT: Q6PDH1;
DR  UNIPROT: Q8K5A5;
DR  UNIPROT: Q8K5A6;
DR  UNIPROT: Q9Z0E5;
DR  UNIPROT: Q9Z2T5;
DR  Pfam: PF06631;
DR  Pfam: PF09279;
DR  Pfam: PF17787;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  Pfam: PF08703;
DR  PROSITE: PS50004;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5- bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein- coupled receptors (PubMed:27653213). Regulates the function of the endothelial barrier (PubMed:27653213). {ECO:0000269|PubMed:27653213, ECO:0000303|PubMed:27653213}.
DE  Reference Proteome: Yes;
DE  Interaction: P35438; IntAct: EBI-398049; Score: 0.35
DE  Interaction: P63101; IntAct: EBI-2255635; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16726570; Score: 0.53
DE  Interaction: Q6NZM9; IntAct: EBI-26472137; Score: 0.35
DE  Interaction: P16056; IntAct: EBI-27118288; Score: 0.35
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098982;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0043209;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0032991;
GO  GO:0005509;
GO  GO:0005516;
GO  GO:0019899;
GO  GO:0005096;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0004435;
GO  GO:0005546;
GO  GO:0060466;
GO  GO:0007420;
GO  GO:0007155;
GO  GO:1902618;
GO  GO:1905631;
GO  GO:1904637;
GO  GO:1904117;
GO  GO:0021987;
GO  GO:0030218;
GO  GO:0045444;
GO  GO:0007213;
GO  GO:0000086;
GO  GO:0007215;
GO  GO:0032957;
GO  GO:0008286;
GO  GO:0048009;
GO  GO:0070498;
GO  GO:0035722;
GO  GO:0035723;
GO  GO:0007612;
GO  GO:0030225;
GO  GO:0007613;
GO  GO:0006397;
GO  GO:0045892;
GO  GO:2000438;
GO  GO:0001556;
GO  GO:0031161;
GO  GO:0046488;
GO  GO:0048015;
GO  GO:2000344;
GO  GO:2000560;
GO  GO:0048639;
GO  GO:0045893;
GO  GO:0040019;
GO  GO:1900087;
GO  GO:0032735;
GO  GO:0046330;
GO  GO:0045663;
GO  GO:0032417;
GO  GO:0099170;
GO  GO:1903140;
GO  GO:0080154;
GO  GO:0008277;
GO  GO:0099178;
GO  GO:0034284;
GO  GO:0043434;
GO  GO:0007165;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:27653213};
SQ  MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKA
SQ  PKDPKLRELLDVGNIGHLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLK
SQ  LQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPDVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
SQ  TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNSSLAKKGQMSVDGFMRYLSGEENGVVSPEKLDLNEDMSQ
SQ  PLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAF
SQ  KTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
SQ  KLSEQASNTYSDSSSVFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKK
SQ  RNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLAMQINMGMY
SQ  EYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
SQ  NAVNPVWEEEPIVFKKVVLPSLACLRIAAYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVP
SQ  DTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETSSEAPSETRTTPAENGVNHTASLAPKPPSQAPH
SQ  SQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTELIKEHTTKYNEIQNDYL
SQ  RRRAALEKSAKKDSKKKSEPSSPDHGSSAIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQ
SQ  KLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKR
SQ  QEKLVEKHNEIRQQILDEKPKLQTELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPPSLASDAAKVNLKSPSS
SQ  EEIERENPGREFDTPL
//
ID  P10687;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;
GN  Plcb1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}. Cytoplasm {ECO:0000269|PubMed:8454637}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}.
DR  UNIPROT: P10687;
DR  Pfam: PF06631;
DR  Pfam: PF09279;
DR  Pfam: PF17787;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  Pfam: PF08703;
DR  PROSITE: PS50004;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5- bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein- coupled receptors. Regulates the function of the endothelial barrier. {ECO:0000250|UniProtKB:Q9Z1B3}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8TEW0; IntAct: EBI-7551325; Score: 0.52
DE  Interaction: Q9NPB6; IntAct: EBI-7551375; Score: 0.52
DE  Interaction: Q96T51; IntAct: EBI-22240696; Score: 0.35
DE  Interaction: P54578; IntAct: EBI-22241262; Score: 0.35
DE  Interaction: P17948; IntAct: EBI-22251830; Score: 0.35
DE  Interaction: P51692; IntAct: EBI-22257101; Score: 0.35
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098982;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0098794;
GO  GO:0032991;
GO  GO:0005509;
GO  GO:0005516;
GO  GO:0019899;
GO  GO:0005096;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0004435;
GO  GO:0005546;
GO  GO:0060466;
GO  GO:0007420;
GO  GO:1902618;
GO  GO:1905631;
GO  GO:1904637;
GO  GO:1904117;
GO  GO:0021987;
GO  GO:0045444;
GO  GO:0007213;
GO  GO:0000086;
GO  GO:0007215;
GO  GO:0032957;
GO  GO:0048009;
GO  GO:0070498;
GO  GO:0035722;
GO  GO:0035723;
GO  GO:0007612;
GO  GO:0007613;
GO  GO:0045892;
GO  GO:2000438;
GO  GO:0031161;
GO  GO:0046488;
GO  GO:0048015;
GO  GO:2000344;
GO  GO:2000560;
GO  GO:0048639;
GO  GO:0045893;
GO  GO:0040019;
GO  GO:1900087;
GO  GO:0032735;
GO  GO:0046330;
GO  GO:0045663;
GO  GO:0099170;
GO  GO:1903140;
GO  GO:0080154;
GO  GO:0008277;
GO  GO:0099178;
GO  GO:0034284;
GO  GO:0010243;
GO  GO:0043434;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9Z1B3};
SQ  MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKA
SQ  PKDPKLRELLDVGNIGHLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLK
SQ  LQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPDVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
SQ  TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNSSLAKKGQMSVDGFMRYLSGEENGVVSPEKLDLNEDMSQ
SQ  PLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAF
SQ  KTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
SQ  KLSEQASNTYSDSSSVFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFETSKK
SQ  RNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLAMQINMGMY
SQ  EYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
SQ  NAVNPVWEEEPIVFKKVVLPSLACLRIAAYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLMLPAVFVYIEVKDYVP
SQ  DTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETSSEAPSETRTTPAENGVNHTATLAPKPPSQAPH
SQ  SQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTELIKEHTTKYNEIQNDYL
SQ  RRRAALEKSAKKDSKKKSEPSSPDHGSSAIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQ
SQ  KLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKR
SQ  QEKLVEKHKEIRQQILDEKPKLQMELEQEYQDKFKRLPLEILEFVQEAMKGKVSEDSNHGSAPPSLASDPAKVNLKSPSS
SQ  EEVQGENAGREFDTPL
//
ID  Q9NRZ7;
PN  1-acyl-sn-glycerol-3-phosphate acyltransferase gamma;
GN  AGPAT3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20537980, ECO:0000269|PubMed:21173190}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:21173190}.
DR  UNIPROT: Q9NRZ7;
DR  UNIPROT: D3DSL2;
DR  UNIPROT: Q3ZCU2;
DR  UNIPROT: Q6UWP6;
DR  UNIPROT: Q6ZUC6;
DR  UNIPROT: Q8N3Q7;
DR  UNIPROT: Q9NRZ6;
DR  Pfam: PF16076;
DR  Pfam: PF01553;
DR  OMIM: 614794;
DR  DisGeNET: 56894;
DE  Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (PubMed:21173190). Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor (PubMed:21173190). Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA (PubMed:21173190). Has a preference for arachidonoyl-CoA as a donor (By similarity). Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity). {ECO:0000250|UniProtKB:Q9D517, ECO:0000269|PubMed:21173190}.
DE  Reference Proteome: Yes;
DE  Interaction: A0PK00; IntAct: EBI-11898699; Score: 0.00
DE  Interaction: Q12982; IntAct: EBI-24609790; Score: 0.56
DE  Interaction: Q9BXJ8; IntAct: EBI-11930596; Score: 0.00
DE  Interaction: Q5NHZ4; IntAct: EBI-2803610; Score: 0.00
DE  Interaction: O43889; IntAct: EBI-8646574; Score: 0.37
DE  Interaction: Q6ZUT1; IntAct: EBI-24518926; Score: 0.56
DE  Interaction: Q00013; IntAct: EBI-24605803; Score: 0.56
DE  Interaction: Q96BA8; IntAct: EBI-24610867; Score: 0.56
DE  Interaction: Q14973; IntAct: EBI-24660485; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24661822; Score: 0.56
DE  Interaction: Q9NRX6; IntAct: EBI-24671223; Score: 0.56
DE  Interaction: Q6ZVE7; IntAct: EBI-24734954; Score: 0.56
DE  Interaction: Q9NQQ7; IntAct: EBI-25280941; Score: 0.56
DE  Interaction: O95870; IntAct: EBI-25286406; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-25288560; Score: 0.56
DE  Interaction: Q8N9Q2; IntAct: EBI-24578171; Score: 0.56
DE  Interaction: Q8N9E0; IntAct: EBI-24636212; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-24646805; Score: 0.56
DE  Interaction: Q8NBQ5; IntAct: EBI-24791121; Score: 0.56
DE  Interaction: Q7Z5P4; IntAct: EBI-25204894; Score: 0.56
DE  Interaction: Q5SR56; IntAct: EBI-25266380; Score: 0.56
DE  Interaction: Q15155; IntAct: EBI-11914340; Score: 0.00
DE  Interaction: Q969V3; IntAct: EBI-11925952; Score: 0.00
DE  Interaction: Q9H1A3; IntAct: EBI-11931217; Score: 0.00
DE  Interaction: Q9NXU5; IntAct: EBI-11933987; Score: 0.00
DE  Interaction: Q9NRX5; IntAct: EBI-11933969; Score: 0.00
DE  Interaction: P30825; IntAct: EBI-21505748; Score: 0.35
DE  Interaction: Q9GZM5; IntAct: EBI-21509346; Score: 0.35
DE  Interaction: Q96FV3; IntAct: EBI-21591007; Score: 0.35
DE  Interaction: Q96KG9; IntAct: EBI-21614942; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-21614942; Score: 0.35
DE  Interaction: O75674; IntAct: EBI-21614942; Score: 0.35
DE  Interaction: B7ZAQ6; IntAct: EBI-21614942; Score: 0.35
DE  Interaction: Q9H2J7; IntAct: EBI-21614809; Score: 0.35
DE  Interaction: P62079; IntAct: EBI-21619035; Score: 0.35
DE  Interaction: Q15884; IntAct: EBI-21620222; Score: 0.35
DE  Interaction: Q9Y2T5; IntAct: EBI-21760939; Score: 0.35
DE  Interaction: O43731; IntAct: EBI-21830599; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0003841;
GO  GO:0016746;
GO  GO:0016024;
GO  GO:0006654;
GO  GO:0008654;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQLVMLLEWWSCTECTLFTDQA
SQ  TVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKVLAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLR
SQ  RLSDYPEYMWFLLYCEGTRFTETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSL
SQ  LGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFKPARRPWTLLNFLSWATILLS
SQ  PLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTEIEKGSSYGNQEFKKKE
//
ID  Q9D517;
PN  1-acyl-sn-glycerol-3-phosphate acyltransferase gamma;
GN  Agpat3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19114731}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NRZ7}.
DR  UNIPROT: Q9D517;
DR  UNIPROT: C4B4E7;
DR  UNIPROT: Q7TT39;
DR  UNIPROT: Q8BST2;
DR  Pfam: PF16076;
DR  Pfam: PF01553;
DE  Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (PubMed:15367102). Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor (By similarity). Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA (By similarity). Has a preference for arachidonoyl-CoA as a donor (PubMed:19114731). Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (PubMed:19114731). {ECO:0000250|UniProtKB:Q9NRZ7, ECO:0000269|PubMed:15367102, ECO:0000269|PubMed:19114731}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0003841;
GO  GO:0016746;
GO  GO:0042171;
GO  GO:0016024;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLLAYLKTQFVVHLLIGFVFVVSGLIINFTQLCTLALWPISKHLYRRINCRLAYSLWSQLVMLLEWWSCTECTLFTDQA
SQ  TVDHFGKEHVVVILNHNFEIDFLCGWTMCERFGVLGSSKVLAKRELLCVPLIGWTWYFLEIVFCKRKWEEDRDTVIEGLR
SQ  RLADYPEYMWFLLYCEGTRFTETKHRISMEVAASKGLPPLKYHLLPRTKGFTTAVQCLRGTVAAIYDVTLNFRGNKNPSL
SQ  LGILYGKKYEADMCVRRFPLEDIPADETSAAQWLHKLYQEKDALQEMYKQKGVFPGEQFKPARRPWTLLNFLCWATILLS
SQ  PLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTEIEKGSSYGNQELKKKE
//
ID  Q5RA57;
PN  1-acyl-sn-glycerol-3-phosphate acyltransferase gamma;
GN  AGPAT3;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NRZ7}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NRZ7}.
DR  UNIPROT: Q5RA57;
DR  Pfam: PF16076;
DR  Pfam: PF01553;
DE  Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor (By similarity). Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA. Has a preference for arachidonoyl-CoA as a donor (By similarity). Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity). {ECO:0000250|UniProtKB:Q9D517, ECO:0000250|UniProtKB:Q9NRZ7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0003841;
GO  GO:0016024;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLLAFLKTQFVLHPLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQLVMLLEWWSCTECTLFTDQA
SQ  TVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKVLAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLR
SQ  RLSDYPEYMWFLLYCEGTRFTETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSL
SQ  LGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFKPARRPWTLLNFLSWATILLS
SQ  PLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTEIEKGSSYGNQEFKKKE
//
ID  Q9NUQ2;
PN  1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon;
GN  AGPAT5;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21173190}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:21173190}. Mitochondrion {ECO:0000269|PubMed:21173190}.
DR  UNIPROT: Q9NUQ2;
DR  UNIPROT: Q8IZ47;
DR  UNIPROT: Q9BQG4;
DR  Pfam: PF16076;
DR  Pfam: PF01553;
DR  OMIM: 614796;
DR  DisGeNET: 55326;
DE  Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (PubMed:21173190). Acts on LPA containing saturated or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor (PubMed:21173190). Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl- CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA (PubMed:21173190). Activity toward lysophosphatidylglycerol not detectable (PubMed:21173190). {ECO:0000269|PubMed:21173190}.
DE  Reference Proteome: Yes;
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: Q9UMX0; IntAct: EBI-10314214; Score: 0.72
DE  Interaction: Q96BA8; IntAct: EBI-24523147; Score: 0.56
DE  Interaction: Q8NBI2; IntAct: EBI-24754929; Score: 0.56
DE  Interaction: Q9NY72; IntAct: EBI-23905509; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-25241264; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-21512742; Score: 0.35
DE  Interaction: Q6UWJ1; IntAct: EBI-21540820; Score: 0.35
DE  Interaction: P35414; IntAct: EBI-21559824; Score: 0.35
DE  Interaction: P13473; IntAct: EBI-21591420; Score: 0.35
DE  Interaction: P55290; IntAct: EBI-21736384; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-25394264; Score: 0.35
GO  GO:0012505;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0003841;
GO  GO:0016746;
GO  GO:0006639;
GO  GO:0016024;
GO  GO:0002244;
GO  GO:0006654;
GO  GO:0008654;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLSLVLHTYSMRYLLPSVVLLGTAPTYVLAWGVWRLLSAFLPARFYQALDDRLYCVYQSMVLFFFENYTGVQILLYGDL
SQ  PKNKENIIYLANHQSTVDWIVADILAIRQNALGHVRYVLKEGLKWLPLYGCYFAQHGGIYVKRSAKFNEKEMRNKLQSYV
SQ  DAGTPMYLVIFPEGTRYNPEQTKVLSASQAFAAQRGLAVLKHVLTPRIKATHVAFDCMKNYLDAIYDVTVVYEGKDDGGQ
SQ  RRESPTMTEFLCKECPKIHIHIDRIDKKDVPEEQEHMRRWLHERFEIKDKMLIEFYESPDPERRKRFPGKSVNSKLSIKK
SQ  TLPSMLILSGLTAGMLMTDAGRKLYVNTWIYGTLLGCLWVTIKA
//
ID  Q9D1E8;
PN  1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon;
GN  Agpat5;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NUQ2}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NUQ2}. Mitochondrion {ECO:0000250|UniProtKB:Q9NUQ2}.
DR  UNIPROT: Q9D1E8;
DR  UNIPROT: Q3U702;
DR  UNIPROT: Q8BG61;
DR  UNIPROT: Q8CGN6;
DR  Pfam: PF16076;
DR  Pfam: PF01553;
DE  Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (PubMed:15367102). Acts on LPA containing saturated or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor (By similarity). Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl- CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA (By similarity). Activity toward lysophosphatidylglycerol not detectable (By similarity). {ECO:0000250|UniProtKB:Q9NUQ2, ECO:0000269|PubMed:15367102}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
GO  GO:0012505;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0003841;
GO  GO:0016746;
GO  GO:0006639;
GO  GO:0016024;
GO  GO:0002244;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLSLVLHTYSMRYLLPSVLLLGSAPTYLLAWTLWRVLSALMPARLYQRVDDRLYCVYQNMVLFFFENYTGVQILLYGDL
SQ  PKNKENVIYLANHQSTVDWIVADMLAARQDALGHVRYVLKDKLKWLPLYGFYFAQHGGIYVKRSAKFNDKEMRSKLQSYV
SQ  NAGTPMYLVIFPEGTRYNATYTKLLSASQAFAAQRGLAVLKHVLTPRIKATHVAFDSMKSHLDAIYDVTVVYEGNEKGSG
SQ  KYSNPPSMTEFLCKQCPKLHIHFDRIDRNEVPEEQEHMKKWLHERFEIKDRLLIEFYDSPDPERRNKFPGKSVHSRLSVK
SQ  KTLPSVLILGSLTAVMLMTESGRKLYMGTWLYGTLLGCLWFVIKA
//
ID  Q1RML2;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1;
GN  PLCZ1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronucleus at interphase following meiosis and mitosis (By similarity). {ECO:0000250|UniProtKB:Q8K4D7}.
DR  UNIPROT: Q1RML2;
DR  UNIPROT: Q5IT24;
DR  Pfam: PF00168;
DR  Pfam: PF09279;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  PROSITE: PS50004;
DR  PROSITE: PS50222;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q86YW0, ECO:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:15744020, ECO:0000269|PubMed:18284699, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045120;
GO  GO:0061827;
GO  GO:0005509;
GO  GO:0004435;
GO  GO:0032266;
GO  GO:0005546;
GO  GO:0010314;
GO  GO:0006816;
GO  GO:0007343;
GO  GO:0016042;
GO  GO:0048015;
GO  GO:0060470;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENKWFLLMVRDDFKGGKITLEKALKLLEKLDIQCNTIHVKYIFKDNDRLKQGRITIEEFRTIYRIITYREEIIEIFNTY
SQ  SENRKILLEKNLVEFLMREQYTLDFNKSIASEIIQKYEPIEEVKQAHQMSFEGFRRYMDSSECLLFDNKCDHVYQDMTHP
SQ  LTDYFISSSHNTYLISDQLWGPSDLWGYISALVKGCRCLEIDCWDGSQNEPVVYHGYTFTSKLLFKTVIQAINKYAFLAS
SQ  EYPVVLSLENHCSPSQQEVMADSLLATFGDALLSYTLDNFSDRLPSPEALKFKILVRNKKIGTLHETLERKGSDMHGKVE
SQ  EFEEEEEIEQEEDGSGAKEPEPVGDFQDDLAKEEQLKRVVGIPLFRKKKIKISMALSDLVIYTKVEKFKSFHHSHLYQQF
SQ  NESNSIGESQARKLTKLAAREFILHTRRFITRVYPKALRADSSNFNPQEFWNVGCQMVALNFQTPGVPMDLQNGKFLDNG
SQ  CSGYVLKPRFLRDKKTKFNPHKVQIDSNPLTLTIRLISGIQLPPSYQNKADTLVIVEIFGVPNDQMKQQSRVIKKNAFNP
SQ  RWNETFTFVIQVPELALIRFVAENQGLIAGNEFLGQYTLPVLCMNRGYRRVPLFSKMGESLEPASLFIYVWYIR
//
ID  Q2VRL0;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1;
GN  PLCZ1;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronucleus at interphase following meiosis and mitosis (By similarity). {ECO:0000250|UniProtKB:Q8K4D7}.
DR  UNIPROT: Q2VRL0;
DR  Pfam: PF00168;
DR  Pfam: PF09279;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  PROSITE: PS50004;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q86YW0, ECO:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:16049153, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045120;
GO  GO:0061827;
GO  GO:0004435;
GO  GO:0032266;
GO  GO:0005546;
GO  GO:0010314;
GO  GO:0006816;
GO  GO:0016042;
GO  GO:0048015;
GO  GO:0060470;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEENRWFLNIIQDGFMNGKIDFDSTVKLLEKLHMPFNLAHVKHVFKKTVDKRKIHTINIEDFRAIYRAIVHRNEFHEIFC
SQ  AYSENRKNLADTELTAFLKKEQFKTEGAETTALEVILKYEPIDEVRKRRQLSFEGFIRYMSSEDCTIFKKEHRTVYQDMN
SQ  HPLCDYFISSSHNTYLVSDQLIGPSDLNGYISALLKGCRCLEIDCWDGSNNDPVVYHGHTLTSKITFCSVIHVVDKYAFA
SQ  ASDYPVVLSLENHCSTKQQERIAQYLLNILGDKLLTSPIGDIEVTQLPSPEALKFKILVKNKKCGTIEETMLRKGRDSHG
SQ  ETGEVSEEEITSSDEETDEKTPLYPKSGSSKRKSEGRSSPPPRKKAKVKKMKIAMGLSDLVIYTKSEKFVSFEHSLAHQK
SQ  CYENNSIGELKAQKFVKHAANQFVSHTSRFITRIYPKGTRAGSSNYNPQEFWNVGCQMVALNFQTSGTPMELQNGKFLDN
SQ  GGCGYILKPEFLRNRNSTFNPHNVGRYSNPLSLSIRLISGHQLPPSNLSKSNKADPLVQLEIYGVPEDQAKRKSSVIKSN
SQ  ALSPRWDETFSFTVQVPELALIRFCVQDEISLVANDFLGQYTLPLLSLSKGYCTVPLFSKSGGKLEPASLFVYVWYY
//
ID  Q86YW0;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1;
GN  PLCZ1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronucleus at interphase following meiosis and mitosis (By similarity). {ECO:0000250|UniProtKB:Q8K4D7}.
DR  UNIPROT: Q86YW0;
DR  UNIPROT: Q08AQ7;
DR  UNIPROT: Q96J70;
DR  Pfam: PF00168;
DR  Pfam: PF09279;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  PROSITE: PS50004;
DR  PROSITE: PS50222;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DR  OMIM: 608075;
DR  OMIM: 617214;
DR  DisGeNET: 89869;
DE  Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:12416999, ECO:0000269|PubMed:14697805, ECO:0000269|PubMed:15579586, ECO:0000269|PubMed:26721930, ECO:0000305}.
DE  Disease: Spermatogenic failure 17 (SPGF17) [MIM:617214]: An autosomal recessive infertility disorder due to failure of oocyte activation and fertilization by sperm that otherwise exhibits normal morphology. {ECO:0000269|PubMed:26721930}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q15828; IntAct: EBI-21829478; Score: 0.35
DE  Interaction: Q8IW75; IntAct: EBI-21829478; Score: 0.35
DE  Interaction: Q16610; IntAct: EBI-21829478; Score: 0.35
DE  Interaction: P49862; IntAct: EBI-21829478; Score: 0.35
DE  Interaction: P42357; IntAct: EBI-21829478; Score: 0.35
DE  Interaction: P04279; IntAct: EBI-21829478; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-20903472; Score: 0.40
DE  Interaction: P68032; IntAct: EBI-20905688; Score: 0.40
DE  Interaction: P14314; IntAct: EBI-20907800; Score: 0.40
GO  GO:0005829;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045120;
GO  GO:0061827;
GO  GO:0005509;
GO  GO:0004435;
GO  GO:0032266;
GO  GO:0005546;
GO  GO:0010314;
GO  GO:0006816;
GO  GO:0007343;
GO  GO:0016042;
GO  GO:0048015;
GO  GO:0007204;
GO  GO:0060470;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEMRWFLSKIQDDFRGGKINLEKTQRLLEKLDIRCSYIHVKQIFKDNDRLKQGRITIEEFRAIYRIITHREEIIEIFNTY
SQ  SENRKILLASNLAQFLTQEQYAAEMSKAIAFEIIQKYEPIEEVRKAHQMSLEGFTRYMDSRECLLFKNECRKVYQDMTHP
SQ  LNDYFISSSHNTYLVSDQLLGPSDLWGYVSALVKGCRCLEIDCWDGAQNEPVVYHGYTLTSKLLFKTVIQAIHKYAFMTS
SQ  DYPVVLSLENHCSTAQQEVMADNLQATFGESLLSDMLDDFPDTLPSPEALKFKILVKNKKIGTLKETHERKGSDKRGDNQ
SQ  DKETGVKKLPGVMLFKKKKTRKLKIALALSDLVIYTKAEKFKSFQHSRLYQQFNENNSIGETQARKLSKLRVHEFIFHTR
SQ  KFITRIYPKATRADSSNFNPQEFWNIGCQMVALNFQTPGLPMDLQNGKFLDNGGSGYILKPHFLRESKSYFNPSNIKEGM
SQ  PITLTIRLISGIQLPLTHSSSNKGDSLVIIEVFGVPNDQMKQQTRVIKKNAFSPRWNETFTFIIHVPELALIRFVVEGQG
SQ  LIAGNEFLGQYTLPLLCMNKGYRRIPLFSRMGESLEPASLFVYVWYVR
//
ID  Q95JS1;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1;
GN  PLCZ1;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronucleus at interphase following meiosis and mitosis (By similarity). {ECO:0000250|UniProtKB:Q8K4D7}.
DR  UNIPROT: Q95JS1;
DR  UNIPROT: Q95JS0;
DR  Pfam: PF00168;
DR  Pfam: PF09279;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  PROSITE: PS50004;
DR  PROSITE: PS50222;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q86YW0, ECO:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:12416999, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0004435;
GO  GO:0006816;
GO  GO:0007343;
GO  GO:0035556;
GO  GO:0016042;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEMKWFLSKIQDDFRGGKINLEKTQRLLEKLDIRCSYIHVKRIFKDNDRLKQGRITIEEFRAIYRILTHREEIVEIFNAY
SQ  SENRKILLENNLVQFLTQEQYTTEMSKTIAFEIIQKYEPIEEVRKARQMSLEGFTRYMDSRECQLFKNECRKVYQDMTHP
SQ  LNDYFISSSHNTYLVSDQLVGPSDLWGYVSALVKGCRCLEIDCWDGAQNEPVVYHGYTLTSKLLFKTVIQAIHKYAFMTS
SQ  DYPVVLSLENHCSPAQQEIMADNLQTTFGESLLSDMLADFPDTLPSPEALKFKVLVKNKKIGTLKETHERKGSDKRGKVE
SQ  EWEEEVADLEEEEEEEEKFKESEIFESVLGENQDKETGVKKLSGVTLFKKKKTRKLKIALALSDLVIYTKAEKFKSFQHS
SQ  RLYQQFNENNSIGETQARKLSKLRAHEFIFHTRKFITRIYPKATRADSSNFNPQEFWNIGCQMVALNFQTPGLPMDLQNG
SQ  KFLDNGGSGYILKPHFLRESESYFNPSDIKDSMPITLTIRLISGIQLPLTHSSSNKGDTLVIIEVFGVPNDQMKQQTRVI
SQ  KKNAFSPRWNETFTFIIHVPELALIRFVVESQGLIAGNEFLGQYTLPLLCMNKGYRRVPLFSRMGESLEPASLFVYVWYV
SQ  R
//
ID  Q8K4D7;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1;
GN  Plcz1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronuclei at interphase following meiosis and mitosis. {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}.
DR  UNIPROT: Q8K4D7;
DR  UNIPROT: Q3KPE5;
DR  Pfam: PF00168;
DR  Pfam: PF09279;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  PROSITE: PS50004;
DR  PROSITE: PS50222;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q86YW0, ECO:0000269|PubMed:12117804, ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15790568, ECO:0000269|PubMed:16000311, ECO:0000269|PubMed:16854985, ECO:0000269|PubMed:17933795, ECO:0000269|PubMed:18028898, ECO:0000269|PubMed:18322275}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045120;
GO  GO:0061827;
GO  GO:0005509;
GO  GO:0004435;
GO  GO:0032266;
GO  GO:0005546;
GO  GO:0010314;
GO  GO:0004629;
GO  GO:0006816;
GO  GO:0007343;
GO  GO:0016042;
GO  GO:0048015;
GO  GO:0007204;
GO  GO:0060470;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESQLHELAEARWFLSKVQDDFRGGKINVEITHKLLEKLDFPCHFAHVKHIFKENDRQNQGRITIEEFRAIYRCIVHREE
SQ  ITEIFNTYTENRKILSENSLIEFLTQEQYEMEIDHSDSVEIINKYEPIEEVKGERQMSIEGFARYMFSSECLLFKENCKT
SQ  VYQDMNHPLSDYFISSSHNTYLISDQILGPSDIWGYVSALVKGCRCLEIDCWDGSQNEPIVYHGYTFTSKLLFKTVVQAI
SQ  NKYAFVTSDYPVVLSLENHCSPGQQEVMASILQSTFGDFLLSDMLEEFPDTLPSPEALKFKILVKNRKVGTLSETHERIG
SQ  TDKSGQVLEWKEVIYEDGDEDSGMDPETWDVFLSRIKEEREADPSTLSGIAGVKKRKRKMKIAMALSDLVIYTKAEKFRN
SQ  FQYSRVYQQFNETNSIGESRARKLSKLRVHEFIFHTAAFITRVYPKMMRADSSNFNPQEFWNVGCQMVALNFQTPGLPMD
SQ  LQNGKFLDNGGSGYILKPDILRDTTLGFNPNEPEYDDHPVTLTIRIISGIQLPVSSSSNTPDIVVIIEVYGVPNDHVKQQ
SQ  TRVVKNNAFSPKWNETFTFLIQVPELALIRFVVETQQGLLSGNELLGQYTLPVLCMNKGYRRVPLFSKSGANLEPSSLFI
SQ  YVWYFRE
//
ID  Q7YRU3;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1;
GN  PLCZ;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronucleus at interphase following meiosis and mitosis (By similarity). {ECO:0000250|UniProtKB:Q8K4D7}.
DR  UNIPROT: Q7YRU3;
DR  Pfam: PF00168;
DR  Pfam: PF09279;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  PROSITE: PS50004;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q86YW0, ECO:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:16098961, ECO:0000269|PubMed:16940280, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004435;
GO  GO:0006816;
GO  GO:0007343;
GO  GO:0016042;
GO  GO:0048015;
GO  GO:0060470;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENKWFLSMVRDDFKGGKINLEKAQKLLEKLDIQCNTIHVKCIFKDNDRLKQGRITIEEFRTIYRIIAHREEIIEIFNAY
SQ  PENRKILFERNLIDFLTQEQYSLDINRSIVYEIIQKYEPIEEVKQAHQMSFEGFTRDMGSSECLLFNNECGSVYQDMTHP
SQ  LSDYFISSSHNTYLISDQIMGPSNLWGYVSALVKGCRCLEIDCWDGSQNEPVVYHGYTLTSKLLFKTVIQAIHKYAFITS
SQ  DYPVVLSLENHCSLSQQEVMADNLQSVFGDALLSDVLDDCPDRLPSPEALKFKILVRNKKIGTLKETHERKGFDKHGQVQ
SQ  ECEEEEEAEQEEEENEVRDSEILDILQDDLEKEELKRGVGIKFFKKKKVKIATALSDLVIYTKVEKFRSFHYSRLYQQFN
SQ  ETNSIGETQARKLSKLRASEFILHTRKFITRIYPKATRADSSNFNPQEFWNIGCQMVALNFQTPGLPMDLQNGKFLENGN
SQ  SGYILKPHFLRDGKSIFNPNKAPINSNPITLTIRLISGIQLPPSYHSSSNKADTLVIIEIFGVPNDQMKQQTRVIKKNAF
SQ  SPRWNETFTFIIQVPELALIRFVVENQGLITGNEFLGQYTLPVLCMNKGYRRVPLFSKMGESLEPASLFIYVWYIR
//
ID  Q5FX52;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1;
GN  Plcz1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q8K4D7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K4D7}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronucleus at interphase following meiosis and mitosis (By similarity). {ECO:0000250|UniProtKB:Q8K4D7}.
DR  UNIPROT: Q5FX52;
DR  Pfam: PF00168;
DR  Pfam: PF09279;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  PROSITE: PS50004;
DR  PROSITE: PS50222;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. {ECO:0000250|UniProtKB:Q86YW0, ECO:0000250|UniProtKB:Q8K4D7, ECO:0000269|PubMed:18322275, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0045120;
GO  GO:0061827;
GO  GO:0005509;
GO  GO:0004435;
GO  GO:0032266;
GO  GO:0005546;
GO  GO:0010314;
GO  GO:0004629;
GO  GO:0006816;
GO  GO:0007343;
GO  GO:0016042;
GO  GO:0048015;
GO  GO:0007204;
GO  GO:0060470;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESHYELAEARWFMSKIQDYFRGGKISAGITHKLLEKLDFPCHFAHVKRIFKENDRHNQGRITTEDFRTIYRCIVHREEI
SQ  VEIFNTYTENRKILPEDSLIEFLTQEQYEMEMDESSSVEIIQKYEPIAEVKNERQMSIEGFARYMFSSECLLFKETCNTV
SQ  YQDMNKPLNDYYISSSHNTYLISDQILGPSDIWGYISALVKGCRCLEIDCWDGAQNEPIVYHGYTLTSKLLFKTVIQAIN
SQ  KYAFVTSDYPVVLSLENHCSPGQQEVMTDILQSTFGDFLLSDILDEFPDSLPSPEALKFKILVKNKKVGTLSETRERLGT
SQ  DKRGIALDLEEEIYENEDEDSGKEPETWDDFLSRVKEEQEADPSTLSGIADAKKKIRKLRVALALSDLVIYTKAEKFRNF
SQ  QYSRVYQQFNETTSMGESRARKLSKLRAHEFIFHTAAFITRVYPKFTRADSSNFNPQEFWNVGCQMVALNFQTPGLPMDL
SQ  QNGKFLDNGGSGYVLKPDFLRDTTLGFNPNEPEGDGHPVTLTIRLISGIQLPVNVPSNTSDIIVIIEVYGVPNDHMKQQS
SQ  RAVKNNAFSPRWNETFTFLIQVPELALIRFVVETQGFLSGNELLGQYTLPVLCMNKGYRRVPLFSKSGANLEPSSLFIYV
SQ  WYYRE
//
ID  O08684;
PN  Phospholipase D1;
GN  PLD1;
OS  10029;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Late endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
DR  UNIPROT: O08684;
DR  Pfam: PF00169;
DR  Pfam: PF00614;
DR  Pfam: PF13091;
DR  Pfam: PF00787;
DR  PROSITE: PS50035;
DR  PROSITE: PS50195;
DE  Function: Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0031902;
GO  GO:0048471;
GO  GO:0070290;
GO  GO:0035091;
GO  GO:0004630;
GO  GO:0048017;
GO  GO:0016042;
GO  GO:0006654;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSLKSEHRVNTSALQKIAADMSNLIDNLDTRELHFEGEEVEFDTSPGDPKAQEKYIPFSSIYNTQGFKEPNIQTYLSGCP
SQ  IKAQVLEVERFTSTTRVPSINLYTIELTHGEFTWQVKRKFKHFQEFHRELLKYKAFIRIPIPTKRHTFRRQNVKEEPREM
SQ  PSLPRSSENTIQEEQFFGRRKQLEDYLTKILKMPMYRNYHATTEFLDVSQLSFIHDLGPKGLEGMIMKRSGGHRIPGLNC
SQ  CGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRIKVGRKETETKYGLRIDNLSRTLILKCNSYRHARWWG
SQ  GAIEEFIQKHGSDFLKDHRFGSYAAVHENMLAKWYVNAKGYFEDIANAMEEAAEEIFITDWWLSPEIFLKRPVVEGNRWR
SQ  LDCILKRKAQQGVRIFIMLYKEVELALGINSEYSKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKLVIIDQSVAFVGGI
SQ  DLAYGRWDDNEHRLTDVGSVKRVTSGLSMGSLAAATMESMESLSLKDNHRSHKNEPILKSVDDVDPKLKGVGKPRKFSKF
SQ  SLYRQLHRRHLHNSDSVSSIDSASNTGSIRSVQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRIPW
SQ  HDIGSVLHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLLPKSQSTAHELRYQVPGAVPAKVQLLRSAADWSAGIKHH
SQ  EESIHSAYINVIENSKHYIYIENQFFISCADDKVVFNKVGDAIAQRILKAHREGQRYRVYIVIPRLPGFEGDISTGGGNA
SQ  LQAIMHFNYRTMCRGENSILGQLKPELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRS
SQ  MLGKRDSEMAVIVQDTETVPSIMDGKEYQAGCFAQGLRLQCFRLVLGYLSDPSEDLQDPVSDKFFKEIWVSTAARNATIY
SQ  DKVFRCLPNDEVHNLMQLRDFISKPILAKDDPIRAEEELRKIRGFLVQFPFYFLSEENLLPSVGTKEAIVPMEVWT
//
ID  Q13393;
PN  Phospholipase D1;
GN  PLD1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Z280}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}.
DR  UNIPROT: Q13393;
DR  PDB: 6U8Z;
DR  Pfam: PF00169;
DR  Pfam: PF00614;
DR  Pfam: PF13091;
DR  Pfam: PF00787;
DR  PROSITE: PS50035;
DR  PROSITE: PS50195;
DR  OMIM: 212093;
DR  OMIM: 602382;
DR  DisGeNET: 5337;
DE  Function: Function as phospholipase selective for phosphatidylcholine (PubMed:8530346, PubMed:9582313). Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity). {ECO:0000250|UniProtKB:Q9Z280, ECO:0000269|PubMed:8530346, ECO:0000269|PubMed:9582313}.
DE  Disease: Cardiac valvular defect, developmental (CVDD) [MIM:212093]: An autosomal recessive form of congenital heart defects, characterized by valvular malformations involving the pulmonic, tricuspid and mitral valves. {ECO:0000269|PubMed:27799408}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q08AE8; IntAct: EBI-25882505; Score: 0.56
DE  Interaction: Q6P5Z2; IntAct: EBI-7796971; Score: 0.54
DE  Interaction: P23528; IntAct: EBI-7602859; Score: 0.57
DE  Interaction: P61764; IntAct: EBI-6941067; Score: 0.36
DE  Interaction: P19174; IntAct: EBI-6941115; Score: 0.36
DE  Interaction: Q81WH6; IntAct: EBI-2827553; Score: 0.00
DE  Interaction: O75787; IntAct: EBI-11037152; Score: 0.35
DE  Interaction: Q66GS9; IntAct: EBI-11052108; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: Q9NXR8; IntAct: EBI-11069098; Score: 0.35
DE  Interaction: Q61699; IntAct: EBI-11091301; Score: 0.35
DE  Interaction: Q91YS4; IntAct: EBI-11094920; Score: 0.35
DE  Interaction: Q9R0Q3; IntAct: EBI-11111571; Score: 0.35
DE  Interaction: Q9Y253; IntAct: EBI-11141689; Score: 0.35
DE  Interaction: C5E527; IntAct: EBI-12585653; Score: 0.35
DE  Interaction: Q9P296; IntAct: EBI-21519943; Score: 0.35
DE  Interaction: Q9UF02; IntAct: EBI-21554221; Score: 0.35
DE  Interaction: Q8N5Z5; IntAct: EBI-21592259; Score: 0.35
DE  Interaction: Q8NFN8; IntAct: EBI-21600104; Score: 0.35
DE  Interaction: Q8N344; IntAct: EBI-21628820; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-21650356; Score: 0.35
DE  Interaction: Q9HBV2; IntAct: EBI-21670400; Score: 0.35
DE  Interaction: Q9NS68; IntAct: EBI-21682735; Score: 0.35
DE  Interaction: Q9Y6I9; IntAct: EBI-21737815; Score: 0.35
DE  Interaction: Q6ZWK4; IntAct: EBI-21782601; Score: 0.35
DE  Interaction: Q99767; IntAct: EBI-21817505; Score: 0.35
DE  Interaction: O95218; IntAct: EBI-21822006; Score: 0.35
DE  Interaction: Q9H0X9; IntAct: EBI-21874768; Score: 0.35
DE  Interaction: Q9C0C9; IntAct: EBI-21880940; Score: 0.35
DE  Interaction: P49769; IntAct: EBI-15566405; Score: 0.40
DE  Interaction: Q15382; IntAct: EBI-15709078; Score: 0.40
DE  Interaction: P51812; IntAct: EBI-15709130; Score: 0.40
DE  Interaction: D3Z8E0; IntAct: EBI-15709151; Score: 0.40
DE  Interaction: P60903; IntAct: EBI-20903520; Score: 0.40
DE  Interaction: Q8WWI1; IntAct: EBI-20930688; Score: 0.40
DE  Interaction: P60033; IntAct: EBI-25645944; Score: 0.35
DE  Interaction: Q6NXG1; IntAct: EBI-25882497; Score: 0.56
DE  Interaction: Q12888; IntAct: EBI-25882489; Score: 0.56
DE  Interaction: P15923; IntAct: EBI-25882481; Score: 0.56
DE  Interaction: O15287; IntAct: EBI-25882473; Score: 0.56
DE  Interaction: Q6ZQX7; IntAct: EBI-25882541; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-25882533; Score: 0.56
DE  Interaction: Q6XD76; IntAct: EBI-25882525; Score: 0.56
DE  Interaction: Q9H7C4; IntAct: EBI-25882515; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25938382; Score: 0.56
DE  Interaction: A0A0F6B1Q8; IntAct: EBI-27036840; Score: 0.35
DE  Interaction: P63252; IntAct: EBI-28956128; Score: 0.27
DE  Interaction: Q16832; IntAct: EBI-32717626; Score: 0.35
GO  GO:0016324;
GO  GO:0098981;
GO  GO:0030139;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0035579;
GO  GO:0070821;
GO  GO:0070290;
GO  GO:0035091;
GO  GO:0004630;
GO  GO:0006935;
GO  GO:0048017;
GO  GO:0006654;
GO  GO:0009395;
GO  GO:0045727;
GO  GO:0007265;
GO  GO:0032534;
GO  GO:0098693;
GO  GO:0060627;
GO  GO:0007264;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCP
SQ  IKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREM
SQ  PSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNC
SQ  CGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWG
SQ  GAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWR
SQ  LDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGI
SQ  DLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKF
SQ  SLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGLKPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGE
SQ  TRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLL
SQ  PKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFNKIGDA
SQ  IAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRT
SQ  HAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCF
SQ  RVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEEELKKI
SQ  RGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
//
ID  Q9Z280;
PN  Phospholipase D1;
GN  Pld1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9395408}. Endoplasmic reticulum membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
DR  UNIPROT: Q9Z280;
DR  UNIPROT: O35911;
DR  Pfam: PF00169;
DR  Pfam: PF00614;
DR  Pfam: PF13091;
DR  Pfam: PF00787;
DR  PROSITE: PS50003;
DR  PROSITE: PS50035;
DR  PROSITE: PS50195;
DE  Function: Function as phospholipase selectivefor phosphatidylcholine (PubMed:9395408). Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (PubMed:9395408). {ECO:0000269|PubMed:9395408}.
DE  Disease: Note=Defects in Pld1 may result in coa which is associated with coat color dilution and white spotting. It is also associated with platelet-storage pool deficiency characterized by decreased levels in serotonin and dense granules.
DE  Reference Proteome: Yes;
DE  Interaction: P49769; IntAct: EBI-15566353; Score: 0.40
GO  GO:0016324;
GO  GO:0098981;
GO  GO:0030139;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0031985;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0030027;
GO  GO:0031902;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0031982;
GO  GO:0070290;
GO  GO:0035091;
GO  GO:0004630;
GO  GO:0050830;
GO  GO:0048017;
GO  GO:0006654;
GO  GO:0008654;
GO  GO:0009395;
GO  GO:0030335;
GO  GO:0045727;
GO  GO:0032534;
GO  GO:0098693;
GO  GO:0060627;
GO  GO:0043434;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSLKSETRVNTSTLQKIAADMSNLIENLDTRELHFEGEEVEYDASPGDPKAQEGCIPFSSIYNTQGFKEPNIQTYLSGCP
SQ  IKAQVLEVERFTSTSRVPSINLYTIELTHGEFTWQVKRKFKHFQEFHRELLKYKAFIRIPIPTKRHTFRRQNVKEEPREM
SQ  PSLPRSSENAIQEEQFFGRRKQLEDYLTKILKMPMYRNYHATTEFLDVSQLSFIHDLGPKGLEGMIMKRSGGHRIPGVNC
SQ  CGHGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRVKVGRKETETKYGLRIDNLSRTLILKCNSYRHARWWG
SQ  GAIEEFIRKHGADFLKDHRFGSYAALHENTLAKWYVNAKGYFEDIANAMEEASEEIFITDWWLSPEIFLKRPVVEGNRWR
SQ  LDCILKRKAQQGVRIFIMLYKEVELALGINSEYSKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKLVIIDQSVAFVGGI
SQ  DLAYGRWDDNEHRLTDVGSVKRVTSGLSLGSLTAASVESMESLSLKDKHEFHKKEPISKIVDETDMKLKGIGKSRKFSKF
SQ  SLYRQLHRHHLHNADSISSIDSTSSYFSHCRSHQNLIHGLKPHLKLFHPSSESEQGLTRHSTDTGSIRSVQTGVGELHGE
SQ  TRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIGSVVHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLL
SQ  PKSQATAHELRYQVPGAVPAKVQLLRSAADWSAGIKHHEESIHAAYIHVIENSKHYIYIENQFFISCADDKVVFNKVGDR
SQ  IAQRILKAHREGQRYRVYIVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGESSILEQLKPELGNKWINYISFCGLRT
SQ  HAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARDLRLECF
SQ  RLVLGYLSDPSEDLQDPVSDKFFKEIWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPILAKEDALRAEEELRKI
SQ  RGFLVQFPLYFLSEENLLPSVGTKEAIVPMEVWT
//
ID  P70496;
PN  Phospholipase D1;
GN  Pld1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Z280}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}.
DR  UNIPROT: P70496;
DR  UNIPROT: O08959;
DR  UNIPROT: O35856;
DR  UNIPROT: O54765;
DR  UNIPROT: P70497;
DR  UNIPROT: Q9QWJ6;
DR  Pfam: PF00169;
DR  Pfam: PF00614;
DR  Pfam: PF13091;
DR  Pfam: PF00787;
DR  PROSITE: PS50003;
DR  PROSITE: PS50035;
DR  PROSITE: PS50195;
DE  Function: Function as phospholipase selective for phosphatidylcholine (By similarity). Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity). {ECO:0000250|UniProtKB:Q13393, ECO:0000250|UniProtKB:Q9Z280}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Z2F5; IntAct: EBI-8605013; Score: 0.40
GO  GO:0016324;
GO  GO:0098981;
GO  GO:0030139;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0031985;
GO  GO:0000139;
GO  GO:0043231;
GO  GO:0030027;
GO  GO:0031902;
GO  GO:0048471;
GO  GO:0045202;
GO  GO:0031982;
GO  GO:0070290;
GO  GO:0035091;
GO  GO:0004630;
GO  GO:0050830;
GO  GO:0048017;
GO  GO:0006654;
GO  GO:0008654;
GO  GO:0009395;
GO  GO:0030335;
GO  GO:0045727;
GO  GO:0032534;
GO  GO:0098693;
GO  GO:0060627;
GO  GO:0043434;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:11121416};
SQ  MSLRSEARVNTSTLQKIAADMSNLIENLDTRELHFEGEEVEYDASPGDPTAQEACIPFSSIYNTQGFKEPNIQIYLSGCP
SQ  VKAQVLEVERFTSTSRMPSVNLYTIELTHGEFTWQVKRKFKHFQEFHRELLKYKAFIRIPIPTKRHTFRRQNVKEEPREM
SQ  PSLPRSSENAIQEEQFFGRRKQLEDYLTKILKMPMYRNYHATTEFLDVSQLSFIHDLGPKGLEGMIMKRSGGHRIPGVNC
SQ  CGHGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRIKVGKKETETKYGLRIDNLSRTLILKCNSYRHARWWG
SQ  GAIEEFIQKHGTDFLKDHRFGSYAAVHENILAKWYVNAKGYFEDIANAMEGATEEIFITDWWLSPEIFLKRPVVEGNRWR
SQ  LDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKLVIIDQSVAFVGGI
SQ  DLAYGRWDDNEHRLTDVGSVKRVTSGQSLGSLTAASVESMESLSLKDKHQSHKNEPVLKSVNDTDMKLKGIGKSRKFSKF
SQ  SLYRQLHRRNLHNSDSISSVDSASSYFNHYRSHQNLIHGIKPHLKLFRPSSESEQGLTRHSADTGSIRSVQTGVGELHGE
SQ  TRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIGSVVHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLL
SQ  PKSQATAHELRYQVPGAVHAKAQLLRSAADWSAGIKHHEESIHAAYTHVIENSKHYIYIENQFFISCADDKVVFNKVGNA
SQ  IAQRILKAHREGQRYRVYIVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGESSILEQLKPELGNKWINYISFCGLRT
SQ  HAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFAQGLRLECF
SQ  RLVLGYLSDPSEDIQDPVSDKFFKEIWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPILAKEDRLRAEEELRKI
SQ  RGFLVQFPFYFLSEENLLPSVGTKEAIVPMEVWT
//
ID  E1BE10;
PN  Mitochondrial cardiolipin hydrolase;
GN  PLD6;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q5SWZ9}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5SWZ9}. Nucleus membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Cell membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Golgi apparatus {ECO:0000250|UniProtKB:Q5SWZ9}. Note=Localization in the mitochondrial outer membrane is found in different cell types where phospholipase was the predominant activity, however, in pachytene spermatocytes and spermatids of mouse testes where nuclease activity is predominant, localization is restricted to the Golgi, suggesting this enzyme is localized in different subcellular compartments depending on the role (phospholipase or nuclease) it needs to play in each cell type and developmental stage. {ECO:0000250|UniProtKB:Q5SWZ9}.
DR  UNIPROT: E1BE10;
DR  Pfam: PF13091;
DR  PROSITE: PS50035;
DE  Function: Presents phospholipase and nuclease activities, depending on the different physiological conditions. Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity. Plays a key role in mitochondrial fusion and fission via its phospholipase activity. In its phospholipase role, it uses the mitochondrial lipid cardiolipin as substrate to generate phosphatidate (PA or 1,2-diacyl-sn-glycero-3- phosphate), a second messenger signaling lipid. Production of PA facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by the Lipin family of phosphatases produces diacylgycerol (DAG) which promotes mitochondrial fission. Both Lipin and DAG regulate mitochondrial dynamics and membrane fusion/fission, important processes for adapting mitochondrial metabolism to changes in cell physiology. Mitochondrial fusion enables cells to cope with the increased nucleotide demand during DNA synthesis (By similarity). Mitochondrial function and dynamics are closely associated with biological processes such as cell growth, proliferation, and differentiation. Mediator of MYC activity, promotes mitochondrial fusion and activates AMPK which in turn inhibits YAP/TAZ, thereby inducing cell growth and proliferation. The endonuclease activity plays a critical role in PIWI-interacting RNA (piRNA) biogenesis during spermatogenesis. Implicated in spermatogenesis and sperm fertility in testicular germ cells, its single strand-specific nuclease activity is critical for the biogenesis/maturation of PIWI-interacting RNA (piRNA). MOV10L1 selectively binds to piRNA precursors and funnels them to the endonuclease that catalyzes the first cleavage step of piRNA processing to generate piRNA intermediate fragments that are subsequently loaded to Piwi proteins. Cleaves either DNA or RNA substrates with similar affinity, producing a 5' phosphate end, in this way it participates in the processing of primary piRNA transcripts. piRNAs provide essential protection against the activity of mobile genetic elements. piRNA- mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation. PA may act as signaling molecule in the recognition/transport of the precursor RNAs of primary piRNAs. Interacts with tesmin in testes, suggesting a role in spermatogenesis via association with its interacting partner (By similarity). {ECO:0000250|UniProtKB:Q5SWZ9, ECO:0000250|UniProtKB:Q8N2A8}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0035755;
GO  GO:0016891;
GO  GO:0046872;
GO  GO:0042803;
GO  GO:0043046;
GO  GO:0016042;
GO  GO:0051321;
GO  GO:0008053;
GO  GO:0030719;
GO  GO:0034587;
GO  GO:0010636;
GO  GO:0007286;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRPLRWQVAVVAAAGLALALETLPAVLRWLWVRRRRPRREVLFFPSQVTCTEALLRSPGATPSGCPCSLPHGESSLSRLL
SQ  SALLAARVSLELCLFAFSSPQLGRAVQLLHQRGVRVRVVTDCDYMALNGSQIGLLRKAGIQVRHDQDLGYMHHKFAIVDR
SQ  KVLITGSLNWTTQAIQNNRENVLIVEDEEYVRLFLEEFERIWEEFNPTRFSFFPQKERAR
//
ID  E2RD63;
PN  Mitochondrial cardiolipin hydrolase;
GN  PLD6;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q5SWZ9}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5SWZ9}. Nucleus membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Cell membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Golgi apparatus {ECO:0000250|UniProtKB:Q5SWZ9}. Note=Localization in the mitochondrial outer membrane is found in different cell types where phospholipase was the predominant activity, however, in pachytene spermatocytes and spermatids of mouse testes where nuclease activity is predominant, localization is restricted to the Golgi, suggesting this enzyme is localized in different subcellular compartments depending on the role (phospholipase or nuclease) it needs to play in each cell type and developmental stage. {ECO:0000250|UniProtKB:Q5SWZ9}.
DR  UNIPROT: E2RD63;
DR  Pfam: PF13091;
DR  PROSITE: PS50035;
DE  Function: Presents phospholipase and nuclease activities, depending on the different physiological conditions. Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity. Plays a key role in mitochondrial fusion and fission via its phospholipase activity. In its phospholipase role, it uses the mitochondrial lipid cardiolipin as substrate to generate phosphatidate (PA or 1,2-diacyl-sn-glycero-3- phosphate), a second messenger signaling lipid. Production of PA facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by the Lipin family of phosphatases produces diacylgycerol (DAG) which promotes mitochondrial fission. Both Lipin and DAG regulate mitochondrial dynamics and membrane fusion/fission, important processes for adapting mitochondrial metabolism to changes in cell physiology. Mitochondrial fusion enables cells to cope with the increased nucleotide demand during DNA synthesis (By similarity). Mitochondrial function and dynamics are closely associated with biological processes such as cell growth, proliferation, and differentiation. Mediator of MYC activity, promotes mitochondrial fusion and activates AMPK which in turn inhibits YAP/TAZ, thereby inducing cell growth and proliferation. The endonuclease activity plays a critical role in PIWI-interacting RNA (piRNA) biogenesis during spermatogenesis. Implicated in spermatogenesis and sperm fertility in testicular germ cells, its single strand-specific nuclease activity is critical for the biogenesis/maturation of PIWI-interacting RNA (piRNA). MOV10L1 selectively binds to piRNA precursors and funnels them to the endonuclease that catalyzes the first cleavage step of piRNA processing to generate piRNA intermediate fragments that are subsequently loaded to Piwi proteins. Cleaves either DNA or RNA substrates with similar affinity, producing a 5' phosphate end, in this way it participates in the processing of primary piRNA transcripts. piRNAs provide essential protection against the activity of mobile genetic elements. piRNA- mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation. PA may act as signaling molecule in the recognition/transport of the precursor RNAs of primary piRNAs. Interacts with tesmin in testes, suggesting a role in spermatogenesis via association with its interacting partner (By similarity). {ECO:0000250|UniProtKB:Q5SWZ9, ECO:0000250|UniProtKB:Q8N2A8}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0035755;
GO  GO:0016891;
GO  GO:0046872;
GO  GO:0042803;
GO  GO:0043046;
GO  GO:0016042;
GO  GO:0051321;
GO  GO:0008053;
GO  GO:0030719;
GO  GO:0034587;
GO  GO:0007286;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MERFRWQVAAVAAVGLALALEALPSVLCWLRAGRRQQQRPPRRQVLFFPSQVTCTEALLQAPGEAPSGPPAGCRCSLPHG
SQ  ESSLSRLLRALLAARASLELCLFAFSSPQLGRAVQLLHQRGVRVRVITDCDYMALNGSQIGLLRKAGIQVRHDQDLGYMH
SQ  HKFAIVDKKVLITGSLNWTTQAIQNNRENVLIMEDEEYVRLFLEEFERIWEEFNPTKYTFFPQKKTGTSLPPQVSCFGQL
SQ  VSCHSKCSHHLSQV
//
ID  Q5SWZ9;
PN  Mitochondrial cardiolipin hydrolase;
GN  Pld6;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Mitochondrion outer membrane {ECO:0000269|PubMed:21397847}; Single-pass membrane protein {ECO:0000269|PubMed:21397847}. Nucleus membrane {ECO:0000269|PubMed:21397847}. Cell membrane {ECO:0000269|PubMed:21397847}. Golgi apparatus {ECO:0000269|PubMed:33783608}. Note=Localization in the mitochondrial outer membrane is found in different cell types where phospholipase was the predominant activity, however, in pachytene spermatocytes and spermatids of mouse testes where nuclease activity is predominant, localization is restricted to the Golgi, suggesting this enzyme is localized in different subcellular compartments depending on the role (phospholipase or nuclease) it needs to play in each cell type and developmental stage. {ECO:0000305}.
DR  UNIPROT: Q5SWZ9;
DR  UNIPROT: B7ZN71;
DR  UNIPROT: Q3UTA3;
DR  UNIPROT: Q8BVM0;
DR  PDB: 4GGJ;
DR  PDB: 4GGK;
DR  Pfam: PF13091;
DR  PROSITE: PS50035;
DE  Function: Presents phospholipase and nuclease activities, depending on the different physiological conditions. Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity. Plays a key role in mitochondrial fusion and fission via its phospholipase activity. In its phospholipase role, it uses the mitochondrial lipid cardiolipin as substrate to generate phosphatidate (PA or 1,2-diacyl-sn-glycero-3- phosphate), a second messenger signaling lipid. Production of PA facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by the Lipin family of phosphatases produces diacylgycerol (DAG) which promotes mitochondrial fission. Both Lipin and DAG regulate mitochondrial dynamics and membrane fusion/fission, important processes for adapting mitochondrial metabolism to changes in cell physiology. Mitochondrial fusion enables cells to cope with the increased nucleotide demand during DNA synthesis (By similarity). Mitochondrial function and dynamics are closely associated with biological processes such as cell growth, proliferation, and differentiation (PubMed:21397848). Mediator of MYC activity, promotes mitochondrial fusion and activates AMPK which in turn inhibits YAP/TAZ, thereby inducing cell growth and proliferation (PubMed:26678338). The endonuclease activity plays a critical role in PIWI-interacting RNA (piRNA) biogenesis during spermatogenesis (PubMed:21397847, PubMed:21397848). Implicated in spermatogenesis and sperm fertility in testicular germ cells, its single strand-specific nuclease activity is critical for the biogenesis/maturation of PIWI-interacting RNA (piRNA) (PubMed:21397847, PubMed:23064230, PubMed:23064227). MOV10L1 selectively binds to piRNA precursors and funnels them to the endonuclease that catalyzes the first cleavage step of piRNA processing to generate piRNA intermediate fragments that are subsequently loaded to Piwi proteins (PubMed:25762440). Cleaves either DNA or RNA substrates with similar affinity, producing a 5' phosphate end, in this way it participates in the processing of primary piRNA transcripts. piRNAs provide essential protection against the activity of mobile genetic elements. piRNA-mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation (PubMed:23064230, PubMed:23064227). PA may act as signaling molecule in the recognition/transport of the precursor RNAs of primary piRNAs (PubMed:21397847). Interacts with tesmin in testes, suggesting a role in spermatogenesis via association with its interacting partner (PubMed:33783608). {ECO:0000250|UniProtKB:Q8N2A8, ECO:0000269|PubMed:21397847, ECO:0000269|PubMed:21397848, ECO:0000269|PubMed:23064227, ECO:0000269|PubMed:23064230, ECO:0000269|PubMed:25762440, ECO:0000269|PubMed:26678338, ECO:0000269|PubMed:33783608}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5SWZ9; IntAct: EBI-16017319; Score: 0.62
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0035755;
GO  GO:0016891;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0004630;
GO  GO:0042803;
GO  GO:0043046;
GO  GO:0016042;
GO  GO:0051321;
GO  GO:0008053;
GO  GO:0030719;
GO  GO:0034587;
GO  GO:0010636;
GO  GO:0007286;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGRSSWRLVFAAGAGLALALEALPWLMRWLLAGRRPRREVLFFPSQVTCTEALLQAPGLPPGPSGCPCSLPHSESSLSRL
SQ  LRALLAARSSLELCLFAFSSPQLGRAVQLLHQRGVRVRVITDCDYMALNGSQIGLLRKAGIQVRHDQDLGYMHHKFAIVD
SQ  KKVLITGSLNWTTQAIQNNRENVLIMEDTEYVRLFLEEFERIWEEFDPTKYSFFPQKHRGH
//
ID  Q58DI5;
PN  Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6;
GN  PLPP6;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IY26}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IY26}. Nucleus envelope {ECO:0000250|UniProtKB:Q8IY26}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8IY26}.
DR  UNIPROT: Q58DI5;
DR  UNIPROT: A6QLK7;
DR  Pfam: PF01569;
DE  Function: Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates. Functions in the innate immune response through the dephosphorylation of presqualene diphosphate which acts as a potent inhibitor of the signaling pathways contributing to polymorphonuclear neutrophils activation. May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway. May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins. Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols. May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine- 1-phosphate. {ECO:0000250|UniProtKB:Q8IY26}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0052642;
GO  GO:0042392;
GO  GO:0045339;
GO  GO:0033383;
GO  GO:1902247;
GO  GO:0045087;
GO  GO:0006720;
GO  GO:0046839;
GO  GO:1902565;
GO  GO:0018342;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQSPRRNAEGRPLGTCDPSSSGSPAHGGGSRFEFQSLLSSRMPGADPTSARLRASESPVHRRGSFPLAGAGSSQALPPQL
SQ  PEEDRIDLNPSFLGIALRSLLAIDLWLSKKLGVCAGESSSWGSMRPLMKLLEISGHGIPWLLGTLYCLSRSDSWAGREVL
SQ  MNLLFALLLDLLLVSLIKGLVRRRRPAHNQMDMFFTISVDKYSFPSGHTTRAALVSRFILNHLVLAIPLRVLVVLWAFIL
SQ  GLSRVMLGRHNVTDVAFGFFLGYMQYSIVDYCWLSPRTAPVLFVLWNQP
//
ID  Q5TZ07;
PN  Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6;
GN  plpp6;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IY26}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IY26}. Nucleus envelope {ECO:0000250|UniProtKB:Q8IY26}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8IY26}.
DR  UNIPROT: Q5TZ07;
DR  UNIPROT: Q502I4;
DR  UNIPROT: Q5TZD1;
DR  Pfam: PF01569;
DE  Function: Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates. May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway. May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins. Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols. May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine- 1-phosphate. {ECO:0000250|UniProtKB:Q8IY26}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0042392;
GO  GO:0045339;
GO  GO:0033383;
GO  GO:1902247;
GO  GO:0046839;
GO  GO:0018342;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSPKARSGSGRSGSVPCPGGNGRYEFISLNRTPPSPVPPQLLQRQGSDPTTARLRASESPVRRRGSGSSNSSTGGGGQQ
SQ  LPEEDCMRLNPSFFGIALSSLLAIDLWLSKRLGVCACEDSSWGSVRPLMKLIEVSGHGIPWLAGAAYCLYKSDSPAGQEV
SQ  MLNLLMALVLDVVLVGVLKAVVRRRRPAHNRMDMFATFSVDSYSFPSGHATRAAMCARFLLNHLVLAAPLRVLVLLWATI
SQ  VGFSRVLLGRHNVTDVAFGFFMGYWQYNLVEMLWLSPVMLQSAIGQLH
//
ID  Q8IY26;
PN  Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6;
GN  PLPP6;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16464866, ECO:0000269|PubMed:18930839, ECO:0000269|PubMed:20110354}; Multi-pass membrane protein {ECO:0000305|PubMed:20110354}. Nucleus envelope {ECO:0000269|PubMed:18930839}. Nucleus inner membrane {ECO:0000305|PubMed:20110354}.
DR  UNIPROT: Q8IY26;
DR  UNIPROT: B3KY05;
DR  UNIPROT: Q5JVJ6;
DR  UNIPROT: Q8NCK9;
DR  Pfam: PF01569;
DR  OMIM: 611666;
DR  DisGeNET: 403313;
DE  Function: Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates (PubMed:16464866, PubMed:19220020, PubMed:20110354). Functions in the innate immune response through the dephosphorylation of presqualene diphosphate which acts as a potent inhibitor of the signaling pathways contributing to polymorphonuclear neutrophils activation (PubMed:16464866, PubMed:23568778). May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway (PubMed:20110354). May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins (PubMed:20110354). Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols (PubMed:18930839). May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine- 1-phosphate (PubMed:18930839, PubMed:20110354). {ECO:0000269|PubMed:16464866, ECO:0000269|PubMed:18930839, ECO:0000269|PubMed:19220020, ECO:0000269|PubMed:20110354, ECO:0000269|PubMed:23568778}.
DE  Reference Proteome: Yes;
DE  Interaction: Q15125; IntAct: EBI-24647840; Score: 0.56
DE  Interaction: Q5JX71; IntAct: EBI-24705960; Score: 0.56
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06461; IntAct: EBI-11723785; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: Q16623; IntAct: EBI-24308796; Score: 0.56
DE  Interaction: Q96BA8; IntAct: EBI-24358086; Score: 0.56
DE  Interaction: Q99942; IntAct: EBI-25250644; Score: 0.56
DE  Interaction: Q8N205; IntAct: EBI-24502926; Score: 0.56
DE  Interaction: Q9BVX2; IntAct: EBI-24526872; Score: 0.56
DE  Interaction: Q9NS71; IntAct: EBI-24620536; Score: 0.56
DE  Interaction: Q68D85; IntAct: EBI-24663138; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24665438; Score: 0.56
DE  Interaction: Q96KR7; IntAct: EBI-24675213; Score: 0.56
DE  Interaction: P11912; IntAct: EBI-24675949; Score: 0.56
DE  Interaction: Q96K19; IntAct: EBI-24679699; Score: 0.56
DE  Interaction: Q9BY50; IntAct: EBI-24684166; Score: 0.56
DE  Interaction: Q14627; IntAct: EBI-24690777; Score: 0.56
DE  Interaction: Q3SXP7; IntAct: EBI-23741658; Score: 0.56
DE  Interaction: Q8TBB6; IntAct: EBI-24709774; Score: 0.56
DE  Interaction: Q8TBE3; IntAct: EBI-24715286; Score: 0.56
DE  Interaction: Q86WK6; IntAct: EBI-23772817; Score: 0.56
DE  Interaction: Q8WWF3; IntAct: EBI-24726073; Score: 0.56
DE  Interaction: O94778; IntAct: EBI-24726609; Score: 0.56
DE  Interaction: P16471; IntAct: EBI-23796159; Score: 0.56
DE  Interaction: Q9UBN6; IntAct: EBI-24733686; Score: 0.56
DE  Interaction: Q13113; IntAct: EBI-24744120; Score: 0.56
DE  Interaction: Q8TBG9; IntAct: EBI-24748614; Score: 0.56
DE  Interaction: Q96PQ1; IntAct: EBI-23825067; Score: 0.56
DE  Interaction: O95484; IntAct: EBI-24754063; Score: 0.56
DE  Interaction: P15151; IntAct: EBI-24755178; Score: 0.56
DE  Interaction: Q9H5X1; IntAct: EBI-23854556; Score: 0.56
DE  Interaction: Q9Y680; IntAct: EBI-24767186; Score: 0.56
DE  Interaction: Q13651; IntAct: EBI-24768822; Score: 0.56
DE  Interaction: Q7KYR7; IntAct: EBI-24769740; Score: 0.56
DE  Interaction: Q8N4V1; IntAct: EBI-24782120; Score: 0.56
DE  Interaction: Q9H2X3; IntAct: EBI-24784754; Score: 0.56
DE  Interaction: Q6UX15; IntAct: EBI-24786495; Score: 0.56
DE  Interaction: O95377; IntAct: EBI-24786749; Score: 0.56
DE  Interaction: Q5T7V8; IntAct: EBI-24787652; Score: 0.56
DE  Interaction: Q8TBP5; IntAct: EBI-24793718; Score: 0.56
DE  Interaction: Q96LL3; IntAct: EBI-25275685; Score: 0.56
DE  Interaction: P15941; IntAct: EBI-25280137; Score: 0.56
DE  Interaction: Q8N6L0; IntAct: EBI-24446133; Score: 0.56
DE  Interaction: Q5T700; IntAct: EBI-24457346; Score: 0.56
DE  Interaction: Q96FX9; IntAct: EBI-24535956; Score: 0.56
DE  Interaction: A0A024R644; IntAct: EBI-24558177; Score: 0.56
DE  Interaction: P21964; IntAct: EBI-24574096; Score: 0.56
DE  Interaction: Q96HJ5; IntAct: EBI-24595440; Score: 0.56
DE  Interaction: P16234; IntAct: EBI-24599449; Score: 0.56
DE  Interaction: Q6UXG8; IntAct: EBI-25151294; Score: 0.56
DE  Interaction: Q8TED1; IntAct: EBI-24760742; Score: 0.56
DE  Interaction: Q9H7M9; IntAct: EBI-25188861; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-25196945; Score: 0.56
DE  Interaction: Q14802; IntAct: EBI-24802281; Score: 0.56
DE  Interaction: Q96KR6; IntAct: EBI-24808861; Score: 0.56
DE  Interaction: Q0VAQ4; IntAct: EBI-25226356; Score: 0.56
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: H9EJ66; IntAct: EBI-25685143; Score: 0.35
GO  GO:0030176;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0016787;
GO  GO:0106405;
GO  GO:0042577;
GO  GO:0016829;
GO  GO:0052642;
GO  GO:0008195;
GO  GO:0042392;
GO  GO:0006695;
GO  GO:0045339;
GO  GO:0033383;
GO  GO:1902247;
GO  GO:0045087;
GO  GO:0006720;
GO  GO:0046839;
GO  GO:1902565;
GO  GO:0018342;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSPRRSMEGRPLGVSASSSSSSPGSPAHGGGGGGSRFEFQSLLSSRATAVDPTCARLRASESPVHRRGSFPLAAAGPSQ
SQ  SPAPPLPEEDRMDLNPSFLGIALRSLLAIDLWLSKKLGVCAGESSSWGSVRPLMKLLEISGHGIPWLLGTLYCLCRSDSW
SQ  AGREVLMNLLFALLLDLLLVALIKGLVRRRRPAHNQMDMFVTLSVDKYSFPSGHATRAALMSRFILNHLVLAIPLRVLVV
SQ  LWAFVLGLSRVMLGRHNVTDVAFGFFLGYMQYSIVDYCWLSPHNAPVLFLLWSQR
//
ID  Q9D4F2;
PN  Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6;
GN  Plpp6;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IY26}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IY26}. Nucleus envelope {ECO:0000250|UniProtKB:Q8IY26}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8IY26}.
DR  UNIPROT: Q9D4F2;
DR  Pfam: PF01569;
DE  Function: Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates. Functions in the innate immune response through the dephosphorylation of presqualene diphosphate which acts as a potent inhibitor of the signaling pathways contributing to polymorphonuclear neutrophils activation. May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway. May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins. Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols. May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine- 1-phosphate. {ECO:0000250|UniProtKB:Q8IY26}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0106405;
GO  GO:0042577;
GO  GO:0052642;
GO  GO:0008195;
GO  GO:0042392;
GO  GO:0045339;
GO  GO:0033383;
GO  GO:1902247;
GO  GO:0045087;
GO  GO:0006720;
GO  GO:0046839;
GO  GO:1902565;
GO  GO:0018342;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSPRRTIEGRPLGSSGGSSVPGSPAHGGGSGGGRFEFQSLLNCRAGADPACARLRASDSPVHRRGSFPLAASGPAQAAP
SQ  APPPEDARMNLNPSFLGIALRSLLAIDLWLSKKLGVCAGESSAWGSVRPLMKLLEISGHGIPWLLGTLYCLLRSDSWAGR
SQ  EVLMNLLFALLLDLLLVAVIKGLVRRRRPAHNQKDMFFTLSVDRYSFPSGHATRAALVSRFILNHLVLAIPLRVLVVLWA
SQ  FVLGLSRVMLGRHNVTDVAFGFFLGYMQYSIVDYCWLSPHNVPVLFVLWNQQ
//
ID  Q66H88;
PN  Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6;
GN  Plpp6;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IY26}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IY26}. Nucleus envelope {ECO:0000250|UniProtKB:Q8IY26}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8IY26}.
DR  UNIPROT: Q66H88;
DR  Pfam: PF01569;
DE  Function: Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates. Functions in the innate immune response through the dephosphorylation of presqualene diphosphate which acts as a potent inhibitor of the signaling pathways contributing to polymorphonuclear neutrophils activation. May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway. May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins. Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols. May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine- 1-phosphate. {ECO:0000250|UniProtKB:Q8IY26}.
DE  Reference Proteome: Yes;
GO  GO:0030176;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0106405;
GO  GO:0042577;
GO  GO:0052642;
GO  GO:0008195;
GO  GO:0042392;
GO  GO:0045339;
GO  GO:0033383;
GO  GO:1902247;
GO  GO:0045087;
GO  GO:0006720;
GO  GO:0046839;
GO  GO:1902565;
GO  GO:0018342;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSPRRTIEGRPLGSSGGSSVPGSPAHGGGGGGSGRFEFQSLLSCRSGADPACARLRASDSPVHRRGSFPLAAACPAQVA
SQ  PAPPPEDAGMNLNPSFLGIALRSLLAIDLWLSKKLGVCAGESSAWGSVRPLMKLLEISGHGIPWLLGTLYCLLRSDSWAG
SQ  REVLMNLLFALLLDLLLVAVIKGLVRRRRPAHNQMDMFFTLSVDKYSFPSGHATRAALVSRFILNHLVLAIPLRVLVVLW
SQ  AFVLGLSRVMLGRHNVTDVAFGFFLGYMQYSIVDYCWLSPLNVPVLFVLWNQQ
//
ID  Q6P0E8;
PN  Inactive phospholipid phosphatase 7;
GN  plpp7;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope. Endoplasmic reticulum membrane. Membrane; Multi-pass membrane protein. Note=Both the N- and C-terminal are exposed to the cytoplasm/nucleoplasm. {ECO:0000250}.
DR  UNIPROT: Q6P0E8;
DR  Pfam: PF01569;
DE  Function: Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0042392;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPANQTRSRARERNNVLNRPEFMSLNQPIKSGGGGGGGESRGTARRPSQRQQQNQQQQGDNPQPENNKDKKELPEEDCMQ
SQ  LNPSFKGIAMNSLLAIDICMSKRLGVCAHPSSSWGSVRSMVKLLALTGHGIPWVFGTIVCLMRSNTLAGQEVLVNLLLAL
SQ  LLDVMTVSGMQKLVKRKGPWEMPPGFFDYLAMDIYSFPAAHASRAVMVSKFLLAHLVLAVPLRILLVLWAILVGISRVLL
SQ  GRHHLTDVGCGFALGFLHYSLVEMVWLSSNTCQTLISIGTFNWSPLY
//
ID  Q8NBV4;
PN  Inactive phospholipid phosphatase 7;
GN  PLPP7;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope. Endoplasmic reticulum membrane. Membrane; Multi-pass membrane protein. Note=Both the N- and C-terminal are exposed to the cytoplasm/nucleoplasm. {ECO:0000250}.
DR  UNIPROT: Q8NBV4;
DR  UNIPROT: Q5T6P0;
DR  UNIPROT: Q96SS7;
DR  UNIPROT: Q9BRC3;
DR  Pfam: PF01569;
DR  OMIM: 618743;
DR  DisGeNET: 84814;
DE  Function: Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q99835; IntAct: EBI-20811975; Score: 0.37
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0042392;
GO  GO:0010832;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPASQSRARARDRNNVLNRAEFLSLNQPPKGGPEPRSSGRKASGPSAQPPPAGDGARERRQSQQLPEEDCMQLNPSFKGI
SQ  AFNSLLAIDICMSKRLGVCAGRAASWASARSMVKLIGITGHGIPWIGGTILCLVKSSTLAGQEVLMNLLLALLLDIMTVA
SQ  GVQKLIKRRGPYETSPSLLDYLTMDIYAFPAGHASRAAMVSKFFLSHLVLAVPLRVLLVLWALCVGLSRVMIGRHHVTDV
SQ  LSGFVIGYLQFRLVELVWMPSSTCQMLISAW
//
ID  Q91WB2;
PN  Inactive phospholipid phosphatase 7;
GN  Plpp7;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope. Endoplasmic reticulum membrane. Membrane; Multi-pass membrane protein. Note=Both the N- and C-terminal are exposed to the cytoplasm/nucleoplasm.
DR  UNIPROT: Q91WB2;
DR  Pfam: PF01569;
DE  Function: Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity. Knockdown in myoblasts strongly promotes differentiation, whereas overexpression represses myogenesis. {ECO:0000269|PubMed:19704009}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0042392;
GO  GO:0010832;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPASQSRARARDRNNVLNRAEFLSLNQPPKGTQEPRSSGRKASGPSTQPPPSSDGARERRQSQQLPEEDCMQLNPSFKGI
SQ  AFNSLLAIDICMSKRLGVCAGRAASWASARSMVKLIGITGHGIPWIGGTILCLVRSSTLAGQEVLMNLLLALLLDIMTVA
SQ  GVQKLIKRRGPYETSPGLLDYLTMDIYAFPAGHASRAAMVSKFFLSHLVLAVPLRVLLVLWAFCVGLSRVMIGRHHITDV
SQ  ISGFIIGYFQFRLVELVWMSSNTCQMLISAW
//
ID  Q5FVJ3;
PN  Inactive phospholipid phosphatase 7;
GN  Plpp7;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope. Endoplasmic reticulum membrane. Membrane; Multi-pass membrane protein. Note=Both the N- and C-terminal are exposed to the cytoplasm/nucleoplasm. {ECO:0000250}.
DR  UNIPROT: Q5FVJ3;
DR  Pfam: PF01569;
DE  Function: Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0042392;
GO  GO:0010832;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPVSQSRARARDRNNVLNRAEFLSLNQPPKGTQEPRSSGRKASGPSTQPPPSSDGARERRQSQQLPEEDCMQLNPSFKGI
SQ  AFNSLLAIDICMSKRLGVCAGRAASWASARSMVKLIGITSHGIPWIGGTILCLVRSSTLAGQEVLMNLLLALLLDIMTVA
SQ  GVQKLIKRRGPYETSPGLLDYLTMDIYAFPAGHASRAAMVSKFFLSHLVLAVPLRVLLVLWAFCVGLSRVMIGRHHITDV
SQ  ISGFIIGYFQFRLVELVWMSSNTCQMLISAW
//
ID  O15162;
PN  Phospholipid scramblase 1;
GN  PLSCR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:26745724}; Single-pass type II membrane protein {ECO:0000269|PubMed:26745724}. Cell membrane {ECO:0000269|PubMed:12564925}; Lipid-anchor {ECO:0000305|PubMed:12564925}; Cytoplasmic side. Nucleus {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:16091359, ECO:0000269|PubMed:24648509}. Cytoplasm {ECO:0000269|PubMed:22052202}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:26745724}. Note=Localizes to the perinuclear region in the presence of RELT (PubMed:22052202). Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus (PubMed:12564925). {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:22052202}.
DR  UNIPROT: O15162;
DR  UNIPROT: B2R8H8;
DR  UNIPROT: B4DTE8;
DR  PDB: 1Y2A;
DR  Pfam: PF03803;
DR  OMIM: 604170;
DR  DisGeNET: 5359;
DE  Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface (PubMed:9218461, PubMed:8663431, PubMed:10770950, PubMed:9572851, PubMed:9485382, PubMed:18629440, PubMed:23590222, PubMed:24648509, PubMed:24343571, PubMed:32110987, PubMed:23659204, PubMed:29748552). Mediates calcium- dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (By similarity). Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A (PubMed:27206388, PubMed:17567603). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages (PubMed:26745724). May contribute to cytokine-regulated cell proliferation and differentiation (By similarity). May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes (PubMed:15308695). Acts as an attachment receptor for HCV (PubMed:21806988). {ECO:0000250|UniProtKB:Q9JJ00, ECO:0000269|PubMed:10770950, ECO:0000269|PubMed:15308695, ECO:0000269|PubMed:17567603, ECO:0000269|PubMed:18629440, ECO:0000269|PubMed:21806988, ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:23659204, ECO:0000269|PubMed:24343571, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:26745724, ECO:0000269|PubMed:27206388, ECO:0000269|PubMed:29748552, ECO:0000269|PubMed:32110987, ECO:0000269|PubMed:8663431, ECO:0000269|PubMed:9218461, ECO:0000269|PubMed:9485382, ECO:0000269|PubMed:9572851}.
DE  Reference Proteome: Yes;
DE  Interaction: Q92734; IntAct: EBI-760686; Score: 0.51
DE  Interaction: Q16630; IntAct: EBI-760770; Score: 0.51
DE  Interaction: Q8WWR8; IntAct: EBI-760826; Score: 0.51
DE  Interaction: P50995; IntAct: EBI-752707; Score: 0.55
DE  Interaction: Q9Y272; IntAct: EBI-752746; Score: 0.37
DE  Interaction: Q16526; IntAct: EBI-752884; Score: 0.55
DE  Interaction: P12236; IntAct: EBI-752902; Score: 0.37
DE  Interaction: Q86UW9; IntAct: EBI-752956; Score: 0.37
DE  Interaction: P49639; IntAct: EBI-753064; Score: 0.37
DE  Interaction: Q6UY11; IntAct: EBI-753187; Score: 0.37
DE  Interaction: Q9UQ90; IntAct: EBI-753205; Score: 0.37
DE  Interaction: Q14847; IntAct: EBI-753385; Score: 0.37
DE  Interaction: Q9HB63; IntAct: EBI-753493; Score: 0.37
DE  Interaction: Q9GZM5; IntAct: EBI-753622; Score: 0.37
DE  Interaction: Q8WV24; IntAct: EBI-753994; Score: 0.37
DE  Interaction: Q15637; IntAct: EBI-754123; Score: 0.37
DE  Interaction: Q8N5R6; IntAct: EBI-754207; Score: 0.37
DE  Interaction: Q9H7M9; IntAct: EBI-754333; Score: 0.37
DE  Interaction: O95967; IntAct: EBI-754366; Score: 0.37
DE  Interaction: Q9BVI4; IntAct: EBI-754600; Score: 0.37
DE  Interaction: P04899; IntAct: EBI-754627; Score: 0.37
DE  Interaction: Q9H0B3; IntAct: EBI-754753; Score: 0.37
DE  Interaction: Q9H0I2; IntAct: EBI-754936; Score: 0.37
DE  Interaction: O94817; IntAct: EBI-755323; Score: 0.37
DE  Interaction: P17509; IntAct: EBI-755602; Score: 0.37
DE  Interaction: Q02218; IntAct: EBI-755686; Score: 0.37
DE  Interaction: Q96RN5; IntAct: EBI-755719; Score: 0.37
DE  Interaction: Q9UHH9; IntAct: EBI-755854; Score: 0.37
DE  Interaction: Q96D16; IntAct: EBI-756055; Score: 0.37
DE  Interaction: Q9NVZ3; IntAct: EBI-756250; Score: 0.37
DE  Interaction: Q9NTK1; IntAct: EBI-756334; Score: 0.37
DE  Interaction: Q9BTL3; IntAct: EBI-756349; Score: 0.37
DE  Interaction: Q9NRQ2; IntAct: EBI-756400; Score: 0.55
DE  Interaction: Q5TA45; IntAct: EBI-756403; Score: 0.37
DE  Interaction: P46108; IntAct: EBI-756454; Score: 0.37
DE  Interaction: Q9H1Q7; IntAct: EBI-756592; Score: 0.37
DE  Interaction: Q9BQ66; IntAct: EBI-756703; Score: 0.37
DE  Interaction: O60269; IntAct: EBI-756826; Score: 0.37
DE  Interaction: O43597; IntAct: EBI-757330; Score: 0.37
DE  Interaction: P50552; IntAct: EBI-757717; Score: 0.37
DE  Interaction: Q00587; IntAct: EBI-757975; Score: 0.37
DE  Interaction: Q9P0T4; IntAct: EBI-758233; Score: 0.37
DE  Interaction: P31269; IntAct: EBI-758332; Score: 0.37
DE  Interaction: Q9UBP5; IntAct: EBI-758455; Score: 0.37
DE  Interaction: Q9NRY6; IntAct: EBI-758575; Score: 0.37
DE  Interaction: Q6UY14; IntAct: EBI-758659; Score: 0.37
DE  Interaction: Q9NXX0; IntAct: EBI-758836; Score: 0.67
DE  Interaction: Q9NQX5; IntAct: EBI-758863; Score: 0.37
DE  Interaction: Q8TC90; IntAct: EBI-759061; Score: 0.55
DE  Interaction: Q96H86; IntAct: EBI-759202; Score: 0.37
DE  Interaction: Q01844; IntAct: EBI-759382; Score: 0.67
DE  Interaction: Q8N9H8; IntAct: EBI-759559; Score: 0.37
DE  Interaction: P26992; IntAct: EBI-759679; Score: 0.37
DE  Interaction: P49901; IntAct: EBI-759850; Score: 0.37
DE  Interaction: O76003; IntAct: EBI-759904; Score: 0.67
DE  Interaction: Q96LJ7; IntAct: EBI-759907; Score: 0.37
DE  Interaction: Q15038; IntAct: EBI-759946; Score: 0.67
DE  Interaction: Q14966; IntAct: EBI-759949; Score: 0.37
DE  Interaction: P78381; IntAct: EBI-759955; Score: 0.55
DE  Interaction: Q05516; IntAct: EBI-759961; Score: 0.37
DE  Interaction: Q96CW7; IntAct: EBI-760078; Score: 0.37
DE  Interaction: Q5T681; IntAct: EBI-760102; Score: 0.37
DE  Interaction: P54259; IntAct: EBI-956422; Score: 0.00
DE  Interaction: Q9P2R6; IntAct: EBI-956766; Score: 0.00
DE  Interaction: P0CK47; IntAct: EBI-2622485; Score: 0.37
DE  Interaction: P0C722; IntAct: EBI-2623040; Score: 0.37
DE  Interaction: P46109; IntAct: EBI-2652697; Score: 0.00
DE  Interaction: Q5NI93; IntAct: EBI-2797189; Score: 0.00
DE  Interaction: Q5NGT6; IntAct: EBI-2797199; Score: 0.00
DE  Interaction: Q5NHR7; IntAct: EBI-2798447; Score: 0.00
DE  Interaction: Q5NGM7; IntAct: EBI-2798462; Score: 0.00
DE  Interaction: Q5NEB5; IntAct: EBI-2803594; Score: 0.00
DE  Interaction: Q5NFA1; IntAct: EBI-2803587; Score: 0.00
DE  Interaction: A0A6L8PQR4; IntAct: EBI-2811640; Score: 0.00
DE  Interaction: Q6KMS8; IntAct: EBI-2812684; Score: 0.00
DE  Interaction: A0A6L7HFG1; IntAct: EBI-2815730; Score: 0.00
DE  Interaction: Q81WR4; IntAct: EBI-2827454; Score: 0.00
DE  Interaction: A0A6L7H5N1; IntAct: EBI-2827487; Score: 0.00
DE  Interaction: A0A6L7HFV2; IntAct: EBI-2827473; Score: 0.00
DE  Interaction: A0A6L7HHZ0; IntAct: EBI-2827494; Score: 0.00
DE  Interaction: A0A6H3AF39; IntAct: EBI-2827480; Score: 0.00
DE  Interaction: A0A6L8PQV1; IntAct: EBI-2827466; Score: 0.00
DE  Interaction: A0A2P0HLN8; IntAct: EBI-2827520; Score: 0.00
DE  Interaction: A0A348A6M1; IntAct: EBI-2827501; Score: 0.00
DE  Interaction: A0A6L8PXB2; IntAct: EBI-2827513; Score: 0.00
DE  Interaction: Q8D162; IntAct: EBI-2846005; Score: 0.00
DE  Interaction: Q8D1M8; IntAct: EBI-2845998; Score: 0.00
DE  Interaction: Q8CZX8; IntAct: EBI-2846017; Score: 0.00
DE  Interaction: Q7ARD3; IntAct: EBI-2861159; Score: 0.00
DE  Interaction: Q7CGI0; IntAct: EBI-2861152; Score: 0.00
DE  Interaction: Q8CZQ9; IntAct: EBI-2861145; Score: 0.00
DE  Interaction: P51828; IntAct: EBI-3926300; Score: 0.37
DE  Interaction: Q09472; IntAct: EBI-3929145; Score: 0.37
DE  Interaction: P23142; IntAct: EBI-3929501; Score: 0.37
DE  Interaction: P04196; IntAct: EBI-3930936; Score: 0.44
DE  Interaction: P29590; IntAct: EBI-3932985; Score: 0.44
DE  Interaction: Q15466; IntAct: EBI-3933005; Score: 0.44
DE  Interaction: P28749; IntAct: EBI-3932995; Score: 0.37
DE  Interaction: Q14764; IntAct: EBI-3933015; Score: 0.44
DE  Interaction: Q92837; IntAct: EBI-3934906; Score: 0.37
DE  Interaction: P09022; IntAct: EBI-3957769; Score: 0.57
DE  Interaction: Q9WMX2; IntAct: EBI-7048894; Score: 0.58
DE  Interaction: Q16625; IntAct: EBI-7049161; Score: 0.40
DE  Interaction: Q16659; IntAct: EBI-7214663; Score: 0.37
DE  Interaction: P04578; IntAct: EBI-6174459; Score: 0.35
DE  Interaction: A5D8V6; IntAct: EBI-10173568; Score: 0.56
DE  Interaction: A8KA13; IntAct: EBI-10174837; Score: 0.56
DE  Interaction: O43559; IntAct: EBI-10184229; Score: 0.56
DE  Interaction: O75716; IntAct: EBI-10189073; Score: 0.56
DE  Interaction: P49796; IntAct: EBI-10211533; Score: 0.56
DE  Interaction: P60411; IntAct: EBI-10217269; Score: 0.56
DE  Interaction: P60412; IntAct: EBI-10217496; Score: 0.56
DE  Interaction: Q13563; IntAct: EBI-10230119; Score: 0.56
DE  Interaction: Q15077; IntAct: EBI-10235792; Score: 0.56
DE  Interaction: Q5T5A8; IntAct: EBI-10245304; Score: 0.49
DE  Interaction: Q5TA78; IntAct: EBI-10246371; Score: 0.56
DE  Interaction: Q5TA82; IntAct: EBI-10246765; Score: 0.56
DE  Interaction: Q6DKI2; IntAct: EBI-10249446; Score: 0.56
DE  Interaction: Q6L8G9; IntAct: EBI-10250607; Score: 0.56
DE  Interaction: Q6RVD6; IntAct: EBI-10254257; Score: 0.56
DE  Interaction: Q8IWZ5; IntAct: EBI-10262279; Score: 0.56
DE  Interaction: Q8NEC5; IntAct: EBI-10270454; Score: 0.56
DE  Interaction: Q8TAU3; IntAct: EBI-10272105; Score: 0.56
DE  Interaction: Q92608; IntAct: EBI-10278739; Score: 0.56
DE  Interaction: Q92731; IntAct: EBI-10279178; Score: 0.67
DE  Interaction: Q92922; IntAct: EBI-10279735; Score: 0.56
DE  Interaction: Q96SQ5; IntAct: EBI-10293486; Score: 0.56
DE  Interaction: Q9BWG6; IntAct: EBI-10300516; Score: 0.67
DE  Interaction: Q9BYQ4; IntAct: EBI-10302096; Score: 0.56
DE  Interaction: Q9BYQ6; IntAct: EBI-10302425; Score: 0.56
DE  Interaction: Q9BYR5; IntAct: EBI-10302754; Score: 0.56
DE  Interaction: Q9H2X0; IntAct: EBI-10306163; Score: 0.56
DE  Interaction: Q9H4E7; IntAct: EBI-10306705; Score: 0.56
DE  Interaction: Q9HBR3; IntAct: EBI-10310204; Score: 0.56
DE  Interaction: Q9NQL9; IntAct: EBI-10312022; Score: 0.56
DE  Interaction: Q9NZ81; IntAct: EBI-10316901; Score: 0.56
DE  Interaction: Q9UBR2; IntAct: EBI-10319318; Score: 0.56
DE  Interaction: Q9HBZ2; IntAct: EBI-21247269; Score: 0.37
DE  Interaction: X5DP31; IntAct: EBI-21247635; Score: 0.37
DE  Interaction: Q12756; IntAct: EBI-21249906; Score: 0.37
DE  Interaction: X5D7R7; IntAct: EBI-21250449; Score: 0.37
DE  Interaction: P78337; IntAct: EBI-21251600; Score: 0.37
DE  Interaction: P15625; IntAct: EBI-11523414; Score: 0.56
DE  Interaction: Q12329; IntAct: EBI-11537219; Score: 0.56
DE  Interaction: A0A0S2Z5X4; IntAct: EBI-16429025; Score: 0.56
DE  Interaction: Q16799; IntAct: EBI-21515832; Score: 0.35
DE  Interaction: Q9UBU6; IntAct: EBI-21677026; Score: 0.35
DE  Interaction: Q00765; IntAct: EBI-21723128; Score: 0.35
DE  Interaction: Q96S66; IntAct: EBI-21724762; Score: 0.35
DE  Interaction: Q86VR2; IntAct: EBI-21724593; Score: 0.35
DE  Interaction: B7Z3K1; IntAct: EBI-21724478; Score: 0.35
DE  Interaction: Q9H902; IntAct: EBI-21724908; Score: 0.35
DE  Interaction: Q9Y3E2; IntAct: EBI-21724951; Score: 0.35
DE  Interaction: Q9H741; IntAct: EBI-21724817; Score: 0.35
DE  Interaction: P61417; IntAct: EBI-20592260; Score: 0.51
DE  Interaction: Q56973; IntAct: EBI-20592286; Score: 0.51
DE  Interaction: P69974; IntAct: EBI-20592294; Score: 0.51
DE  Interaction: Q8ZG77; IntAct: EBI-20592328; Score: 0.51
DE  Interaction: Q7ARI8; IntAct: EBI-20817460; Score: 0.37
DE  Interaction: A0A0H2VZS6; IntAct: EBI-20817960; Score: 0.37
DE  Interaction: O84569; IntAct: EBI-22303917; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-25936136; Score: 0.56
DE  Interaction: Q7Z417; IntAct: EBI-26508567; Score: 0.51
DE  Interaction: P34972; IntAct: EBI-26880846; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P46934; IntAct: EBI-30831962; Score: 0.44
DE  Interaction: P46937; IntAct: EBI-30845911; Score: 0.44
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0005887;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005509;
GO  GO:0042609;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0019899;
GO  GO:0005154;
GO  GO:0032791;
GO  GO:0000287;
GO  GO:0045340;
GO  GO:0004518;
GO  GO:0017128;
GO  GO:0017124;
GO  GO:0001618;
GO  GO:0008270;
GO  GO:0006953;
GO  GO:0006915;
GO  GO:0051607;
GO  GO:0050765;
GO  GO:0045071;
GO  GO:0006659;
GO  GO:0070782;
GO  GO:0017121;
GO  GO:0030168;
GO  GO:1905820;
GO  GO:2000373;
GO  GO:0010628;
GO  GO:0045089;
GO  GO:0045944;
GO  GO:0060368;
GO  GO:0033003;
GO  GO:0035456;
GO  GO:0010288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:23590222};
SQ  MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGA
SQ  AGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPF
SQ  TLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCC
SQ  GDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW
//
ID  Q9JJ00;
PN  Phospholipid scramblase 1;
GN  Plscr1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:O15162}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O15162}. Cell membrane {ECO:0000250|UniProtKB:O15162}; Lipid-anchor {ECO:0000250|UniProtKB:O15162}; Cytoplasmic side. Nucleus {ECO:0000250|UniProtKB:O15162}. Cytoplasm {ECO:0000250|UniProtKB:O15162}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O15162}. Note=Localizes to the perinuclear region in the presence of RELT. Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus. {ECO:0000250|UniProtKB:O15162}.
DR  UNIPROT: Q9JJ00;
DR  UNIPROT: O54730;
DR  UNIPROT: O54731;
DR  UNIPROT: Q9D1F8;
DR  Pfam: PF03803;
DE  Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific distribution of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface (PubMed:32110987). Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (PubMed:32110987). Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A (By similarity). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages (PubMed:26745724). May contribute to cytokine-regulated cell proliferation and differentiation (PubMed:12010804). {ECO:0000250|UniProtKB:O15162, ECO:0000269|PubMed:12010804, ECO:0000269|PubMed:26745724, ECO:0000269|PubMed:32110987}.
DE  Disease: Note=Participates in a chromosomal translocation that produces MMTRA1A which is leukemogenic to syngenic SL mice and athymic nude mice.
DE  Reference Proteome: Yes;
DE  Interaction: O35626; IntAct: EBI-4325299; Score: 0.37
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005887;
GO  GO:0045121;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005509;
GO  GO:0042609;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0019899;
GO  GO:0005154;
GO  GO:0032791;
GO  GO:0000287;
GO  GO:0045340;
GO  GO:0004518;
GO  GO:0017128;
GO  GO:0017124;
GO  GO:0001618;
GO  GO:0008270;
GO  GO:0006953;
GO  GO:0071345;
GO  GO:0071222;
GO  GO:0051607;
GO  GO:0006955;
GO  GO:0097193;
GO  GO:0030099;
GO  GO:0050765;
GO  GO:0032091;
GO  GO:0045071;
GO  GO:0006659;
GO  GO:0070782;
GO  GO:0017121;
GO  GO:0043065;
GO  GO:1905820;
GO  GO:2000373;
GO  GO:0045089;
GO  GO:1902231;
GO  GO:0045944;
GO  GO:0060368;
GO  GO:0033003;
GO  GO:0035455;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MENHSKQTEAPHPGTYMPAGYPPPYPPAAFQGPSDHAAYPIPQAGYQGPPGPYPGPQPGYPVPPGGYAGGGPSGFPVQNQ
SQ  PAYNHPGGPGGTPWMPAPPPPLNCPPGLEYLAQIDQLLVHQQIELLEVLTGFETNNKYEIKNSLGQRVYFAVEDTDCCTR
SQ  NCCGASRPFTLRILDNLGREVMTLERPLRCSSCCFPCCLQEIEIQAPPGVPVGYVTQTWHPCLPKFTLQNEKKQDVLKVV
SQ  GPCVVCSCCSDIDFELKSLDEESVVGKISKQWSGFVREAFTDADNFGIQFPLDLDVKMKAVMLGACFLIDFMFFERTGNE
SQ  EQRSGAWQ
//
ID  P58195;
PN  Phospholipid scramblase 1;
GN  Plscr1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:O15162}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O15162}. Cell membrane {ECO:0000250|UniProtKB:O15162}; Lipid-anchor {ECO:0000250|UniProtKB:O15162}; Cytoplasmic side. Nucleus {ECO:0000250|UniProtKB:O15162}. Cytoplasm {ECO:0000250|UniProtKB:O15162}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O15162}. Note=Localizes to the perinuclear region in the presence of RELT. Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus. {ECO:0000250|UniProtKB:O15162}.
DR  UNIPROT: P58195;
DR  Pfam: PF03803;
DE  Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific distribution of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface (By similarity). Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (By similarity). Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A (By similarity). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages (By similarity). May contribute to cytokine-regulated cell proliferation and differentiation (By similarity). {ECO:0000250|UniProtKB:O15162, ECO:0000250|UniProtKB:Q9JJ00}.
DE  Reference Proteome: Yes;
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005887;
GO  GO:0045121;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005509;
GO  GO:0042609;
GO  GO:0003677;
GO  GO:0001228;
GO  GO:0019899;
GO  GO:0005154;
GO  GO:0032791;
GO  GO:0000287;
GO  GO:0045340;
GO  GO:0004518;
GO  GO:0017128;
GO  GO:0017124;
GO  GO:0001618;
GO  GO:0008270;
GO  GO:0006953;
GO  GO:0006915;
GO  GO:0071345;
GO  GO:0071222;
GO  GO:0051607;
GO  GO:0006955;
GO  GO:0097193;
GO  GO:0030099;
GO  GO:0050765;
GO  GO:0032091;
GO  GO:0045071;
GO  GO:0006659;
GO  GO:0070782;
GO  GO:0015914;
GO  GO:0017121;
GO  GO:0043065;
GO  GO:1905820;
GO  GO:2000373;
GO  GO:0010628;
GO  GO:0045089;
GO  GO:1902231;
GO  GO:0045944;
GO  GO:0060368;
GO  GO:0033003;
GO  GO:0035455;
GO  GO:0035456;
GO  GO:0010288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEKHGPPEHAAYPIPQADYQGSQGPYPGPQGPYPGPQGPYAGPQGPYPGPQGPYAGPQGPYPGPQPGYPVPPGSYAGGDP
SQ  SGFPVQHQPAYNHPGGPGGTPWMQAPPPPLDCPPGLEYLTQIDQILVHQQIELLEVLTGFETNNKYEIKNSLGQRVYFAV
SQ  EDTDCCTRNCCGASRPFTLRILDNMGREVMTLERPLRCSSCCFPCCLQEIEIQAPPGVPVGYVIQTWHPCLPKFTLQNEK
SQ  RQDVLKVVGPCVVCSCCSDIDFELKSLDEESVVGKISKQWSGFVREAFTDADNFGIQFPLDLDVKMKAVMLGACFLIDFM
SQ  FFERTGNEEQRSGVW
//
ID  Q9BX97;
PN  Plasmalemma vesicle-associated protein;
GN  PLVAP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9WV78}. Note=Membrane-associated protein of caveolae. Found in fenestral and stomatal diaphragms in fenestrated endothelia and transendothelial channels. Also colocalized with CAV1 in perinuclear region. {ECO:0000250|UniProtKB:Q9WV78}.
DR  UNIPROT: Q9BX97;
DR  UNIPROT: Q86VP0;
DR  UNIPROT: Q8N8Y0;
DR  UNIPROT: Q8ND68;
DR  UNIPROT: Q8TER8;
DR  UNIPROT: Q9BZD5;
DR  Pfam: PF06637;
DR  OMIM: 607647;
DR  OMIM: 618183;
DR  DisGeNET: 83483;
DE  Function: Endothelial cell-specific membrane protein involved in the formation of the diaphragms that bridge endothelial fenestrae. It is also required for the formation of stomata of caveolae and transendothelial channels. Functions in microvascular permeability, endothelial fenestrae contributing to the passage of water and solutes and regulating transcellular versus paracellular flow in different organs. Plays a specific role in embryonic development. {ECO:0000250|UniProtKB:Q91VC4}.
DE  Disease: Diarrhea 10, protein-losing enteropathy type (DIAR10) [MIM:618183]: An autosomal recessive, congenital diarrheal disorder characterized by intractable secretory diarrhea with massive protein loss due to leaky fenestrated capillaries, severe hypoalbuminemia, hypogammaglobulinemia, hypertriglyceridemia, and electrolyte abnormalities. Disease severity is variable and death in infancy may occur in severe cases. Some patients show facial dysmorphic features, and cardiac and renal abnormalities. {ECO:0000269|PubMed:26207260, ECO:0000269|PubMed:29661969, ECO:0000269|PubMed:29875123}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q5NHQ9; IntAct: EBI-2803580; Score: 0.00
DE  Interaction: Q5NGF1; IntAct: EBI-2803569; Score: 0.00
DE  Interaction: Q8ZED8; IntAct: EBI-2840183; Score: 0.00
DE  Interaction: A0A3N4B652; IntAct: EBI-2841453; Score: 0.00
DE  Interaction: A0A380PFZ4; IntAct: EBI-2845991; Score: 0.00
DE  Interaction: Q56974; IntAct: EBI-2861066; Score: 0.00
DE  Interaction: A0A6M0NNK5; IntAct: EBI-2861059; Score: 0.00
DE  Interaction: Q8ZDG9; IntAct: EBI-2861077; Score: 0.00
DE  Interaction: A0A1U9X8X8; IntAct: EBI-24315482; Score: 0.56
DE  Interaction: Q9H6R6; IntAct: EBI-21781012; Score: 0.35
DE  Interaction: Q9H0V9; IntAct: EBI-21781012; Score: 0.35
DE  Interaction: Q9BYC5; IntAct: EBI-21781012; Score: 0.35
DE  Interaction: Q9BXB4; IntAct: EBI-21781012; Score: 0.35
DE  Interaction: O60906; IntAct: EBI-21781012; Score: 0.35
DE  Interaction: P07306; IntAct: EBI-21852777; Score: 0.35
GO  GO:0005901;
GO  GO:0009986;
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0032502;
GO  GO:0000165;
GO  GO:0002693;
GO  GO:0043114;
GO  GO:0033209;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLAMEHGGSYARAGGSSRGCWYYLRYFFLFVSLIQFLIILGLVLFMVYGNVHVSTESNLQATERRAEGLYSQLLGLTAS
SQ  QSNLTKELNFTTRAKDAIMQMWLNARRDLDRINASFRQCQGDRVIYTNNQRYMAAIILSEKQCRDQFKDMNKSCDALLFM
SQ  LNQKVKTLEVEIAKEKTICTKDKESVLLNKRVAEEQLVECVKTRELQHQERQLAKEQLQKVQALCLPLDKDKFEMDLRNL
SQ  WRDSIIPRSLDNLGYNLYHPLGSELASIRRACDHMPSLMSSKVEELARSLRADIERVARENSDLQRQKLEAQQGLRASQE
SQ  AKQKVEKEAQAREAKLQAECSRQTQLALEEKAVLRKERDNLAKELEEKKREAEQLRMELAIRNSALDTCIKTKSQPMMPV
SQ  SRPMGPVPNPQPIDPASLEEFKRKILESQRPPAGIPVAPSSG
//
ID  Q91VC4;
PN  Plasmalemma vesicle-associated protein;
GN  Plvap;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9WV78}. Note=Membrane-associated protein of caveolae. Found in fenestral and stomatal diaphragms in fenestrated endothelia and transendothelial channels. Also colocalized with CAV1 in perinuclear region. {ECO:0000250|UniProtKB:Q9WV78}.
DR  UNIPROT: Q91VC4;
DR  UNIPROT: Q99JB1;
DR  Pfam: PF06637;
DE  Function: Endothelial cell-specific membrane protein involved in the formation of the diaphragms that bridge endothelial fenestrae. It is also required for the formation of stomata of caveolae and transendothelial channels. Functions in microvascular permeability, endothelial fenestrae contributing to the passage of water and solutes and regulating transcellular versus paracellular flow in different organs. Plays a specific role in embryonic development. {ECO:0000269|PubMed:22782339}.
DE  Reference Proteome: Yes;
GO  GO:0005901;
GO  GO:0009986;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0032502;
GO  GO:0000165;
GO  GO:0002693;
GO  GO:0043114;
GO  GO:0033209;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLSMDRSPYARTGDQQRGCWYYLRYFFLFVSLIQFLIILGLVLFMIYGNVHATTESSLRATEIRADSLYSQVVGLSASQ
SQ  ANLSKQLNISLLVKETVMQQLLTTRREMERINASFRQCQGDLITYINYNRFIAAIILSEKQCQEQLKEVNKTCEALLFKL
SQ  GEKVKTLEMEVAKEKAVCSKDKESLLAGKRQTEEQLEACGKARERQQQEQQVTEENLRKVQSLCIPLDQEKFQADVLSAW
SQ  RDSLIYRTLETLPYHYQLMPEYASLRRTCESLPGIMTTKIEELARGLRAGIERVTRENAELRRQKLELERAAQAAQEARA
SQ  RAGTEAQARETQLRAECARQTQLALEEKAALRAQRDNLERELEARKRELEQLRTEVDVRISALDTCVKAKSLPAVPPRVS
SQ  GPPPNPPPIDPASLEEFKKRILESQRLPVVNPAAQPSG
//
ID  Q9WV78;
PN  Plasmalemma vesicle-associated protein;
GN  Plvap;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:10366592, ECO:0000269|PubMed:10557298}; Single-pass type II membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000269|PubMed:10366592, ECO:0000269|PubMed:10557298}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15640522}. Note=Membrane-associated protein of caveolae (PubMed:10366592). Found in fenestral and stomatal diaphragms in fenestrated endothelia and transendothelial channels (PubMed:10557298). Also colocalized with CAV1 in perinuclear region (PubMed:15640522). {ECO:0000269|PubMed:10366592, ECO:0000269|PubMed:10557298, ECO:0000269|PubMed:15640522}.
DR  UNIPROT: Q9WV78;
DR  Pfam: PF06637;
DE  Function: Endothelial cell-specific membrane protein involved in the formation of the diaphragms that bridge endothelial fenestrae. It is also required for the formation of stomata of caveolae and transendothelial channels. Functions in microvascular permeability, endothelial fenestrae contributing to the passage of water and solutes and regulating transcellular versus paracellular flow in different organs. Plays a specific role in embryonic development. {ECO:0000250|UniProtKB:Q91VC4}.
DE  Reference Proteome: Yes;
DE  Interaction: P15127; IntAct: EBI-10768744; Score: 0.35
GO  GO:0005901;
GO  GO:0009986;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0042802;
GO  GO:0032502;
GO  GO:0000165;
GO  GO:0002693;
GO  GO:0043114;
GO  GO:0033209;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLSMDRSPYSRTGDRDRGCWYYLRYFFLFVSLIQFLIILGLVLFMIYGNVHATTESSLRATEIRADNLYSQVVGLSAAQ
SQ  ANLSKQLNISTLVKDTVMQQLLTTRREVERINASFRQCQGDLITYINYNRFIAAIILSEKQCQEQLKEGNKTCEALLFKL
SQ  GEKVKTLEMEVVKEKAVCSKDKDSLLAGKRQAEMQQEACGKAREQQKQDQQVTEEQLRKVQSLCLPLDQEKFQADVLNVW
SQ  RDSLVYRSLDNIGYHYSLMPEFSSLRRTCESLPGIMTTKVEELARGLRAGIERVTRENGELRRQKLELERAIQGEREART
SQ  RAGTEAQARETQLRTECARQTQLALEEKAALRTQRDDLERQLEARKRELEQLRTEVDVRISALDTCVKAKSLPAIQPRLP
SQ  GPPPNPPPIDPASLEEFKKRILESQRPPLVNPAVPPSG
//
ID  Q03760;
PN  Pre-mRNA leakage protein 39;
GN  PML39;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16162818}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16162818}; Lumenal side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16162818}. Note=Associated with a subset of nuclear pores opposite to the nucleolus.
DR  UNIPROT: Q03760;
DR  UNIPROT: D6W0H7;
DR  Pfam: PF07967;
DE  Function: Involved in the nuclear retention of improperly spliced pre- mRNAs. {ECO:0000269|PubMed:16162818}.
DE  Reference Proteome: Yes;
DE  Interaction: P30822; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04636; IntAct: EBI-7457619; Score: 0.40
DE  Interaction: Q04212; IntAct: EBI-8224497; Score: 0.22
DE  Interaction: P40150; IntAct: EBI-3800253; Score: 0.35
GO  GO:0031965;
GO  GO:0008270;
GO  GO:0051237;
GO  GO:0051028;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MEKDALEVRLKSIRHSLDKNTKLLPGKYRNTLGERLITKWRYKKKSHNGSSMLPEKCKSHVQLYDDLVQESSKHFVGFRL
SQ  HDLRALLKRICSIQNYTRHVLIEWDVRWVNPLTLASKGWEPYQSASQSQVPFKCCCCHAIMTIPLLKNGDDVADYTMKLN
SQ  EKIWNSNIIGNHLQKCPWRENQVDLNKEYYLSSQNLIREIERIHTEIDRIVSGSNEFSLKRNSSRIFHYLSEKEIQKLAF
SQ  FFDCKDYSLVGLLLLGYTKFQKDDLVQCTACFHRASLKKLEYTEFNGHALWCRYYNKELLPTMLLELIGKEDKLITKLGV
SQ  GERLNKLEAVLQTL
//
ID  O13898;
PN  Dolichyl-phosphate-mannose--protein mannosyltransferase 1;
GN  ogm1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein {ECO:0000269|PubMed:15809069}. Nucleus membrane {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein {ECO:0000269|PubMed:15809069}.
DR  UNIPROT: O13898;
DR  Pfam: PF02815;
DR  Pfam: PF02366;
DR  Pfam: PF16192;
DR  PROSITE: PS50919;
DE  Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Required for normal cell growth and septum formation. Shown to actively O-mannosylate wsc1. {ECO:0000269|PubMed:15809069, ECO:0000269|PubMed:15948957}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0004169;
GO  GO:0000032;
GO  GO:0044845;
GO  GO:0035269;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDKQSTFQDPKEKHRIQRDVKLSRPRKRFSFLDYVVVIFLTVVAFCVRAQRLMNPAKVVFEELRYYNYAVDYVNNKLLMD
SQ  VYPPLGKLLFSLVAALTGNKYELNTLDEPGQQYPFTDVAYSMRLFTCLLGSLLVPLMYGTVYFPTKSKTAASLAALFVIF
SQ  DNGLITMSRYIMIEIPALYFMSLTAFYWSVYEAQQKRPFSLRWHTSLLSTGVALGLALSTKLSAMFTFGWLLILAAFHLW
SQ  NLLGDLSVPMYRIVKHLFSYIFYLIGVPITVYLAVFAVHSHIAYKASVADAFLPPEHRHALAGNRFDDQFADVAYGSLVT
SQ  IRNAIPEHGYLHSSELLYPEGTEQQIISLVDEPNQNALWIIEHEHSQDNNRSNIELLKDGSVVRLRHVMTGRALHSHEHK
SQ  PIVSNNDWQLEASAYGGFGFEGDANDLFRIQILEKKSKHATSNGTVETLNTKFRLIHVFANCELMSSHRRFPDWGDYQRE
SQ  VTCCRNCVERSTTWFIESNYHDGLPSDSRKITYRKPGFLESFVEHNKLMWLKDRKMGDGHVYESSALTWPLLLGPLRFFY
SQ  EQHLQVFFMGNPFVWYSVISLVAFFVIVQIFCLARWNLGYNDFGPSAFHYNYNIGKFVVAWLLHWAPYILETDRVFLYHY
SQ  LPALYFGIAALGVSWSFLGNAVFGNRTAYKALSVIIMALMFLVYRLYSPFTYMTTLTKSSCRALELKGSWNFHCNTYLDN
SQ  LSDYKFSSDAGETYFEKAAPHPFVYSEDTAKKSEGDTPLNKNLNDYYPSWDQRVEAGYKLAAQQKAEQEAREAAEKAASE
SQ  AAERSSSEAAASSSSESVAAASVEAERLAMEADEFNGASETVDGASVEAERSAMEAAALNNAAESTEVVGSSPESVASEQ
SQ  EENVAESAQARVE
//
ID  Q9C100;
PN  Dolichyl-phosphate-mannose--protein mannosyltransferase 2;
GN  ogm2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein {ECO:0000269|PubMed:15809069}. Nucleus membrane {ECO:0000269|PubMed:15809069}; Multi-pass membrane protein {ECO:0000269|PubMed:15809069}.
DR  UNIPROT: Q9C100;
DR  Pfam: PF02815;
DR  Pfam: PF02366;
DR  Pfam: PF16192;
DR  PROSITE: PS50919;
DE  Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. {ECO:0000269|PubMed:15809069}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0004169;
GO  GO:0035269;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSYEQLHAQSGQLRQRFPSKHSEIEDEVANEKEELKDATKSALGEVKTNKKYYILGYFLVPLLLTVIAGFVRVWKIADSN
SQ  VVIWDEAHFGKFASYYLKHEFYFDVHPPLGKMLNAVAGKLVGYDGSFDFSSGATYPEDLNYKFMRLWNAAFGTLCIPLVY
SQ  FTALNFNYSFLAATLCTLMVALDNHLATISRFILLDSMLLFFIISTFFCLSRYHVYHKAPFTFYWFKWLFLTGVCIGCVC
SQ  SVKLVGLFITAVVGLYTVDELWCLLNDKRVTWKAYAGHWIARVCLLIFLPILIYAFTFWIQFAVLYRSGPGDAQMPSLFQ
SQ  ARLEGSPLTKNPIDLMYGSKFTLKSRNPTGALLHSHVQTYPEGSEQQQVTGYHHKDGNNEWMFVPTHGVAYNYEENDPMN
SQ  PILNGSVVRLIHPFTNRNLHTHKIPAPLNKRMYEVSGYGLGDVGDEKDYWIVNILYDTAHRDAYNVRSLSTVFQLYNPVV
SQ  GCYLSSSSSSLPSWGFGQIEMYCDPDPDPSNTDTQWNVEEHINPRLPEGSINDYPSSFWSDFLHLNRAMLRANNGLIPDE
SQ  DKLDALRSEAYQWPFLLATLRMCGWGDNQIKYLLVGNPVAYWFATSSLIVFALFVVGAVLAWRRRVLRWSQEACDTFHYA
SQ  GIYPFLGWFFNYLPYYIMGRVLYVHHYEPSYALSTFTAAFVVDWFTKKMPKIVRVVVFISLYAIIAGVFIYFKDVTFGMH
SQ  GPASDFHRLRWLNSWNVHD
//
ID  Q8K3Z9;
PN  Nuclear envelope pore membrane protein POM 121;
GN  Pom121;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single- pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase. {ECO:0000250}.
DR  UNIPROT: Q8K3Z9;
DR  UNIPROT: Q7TSH5;
DE  Function: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSPAAAAADGGERRRPPLGGREGRSRARGYGGPAGAAALGLALLGLALYLVPAAAALAWLAVGASAAWWGLSREPRGPRA
SQ  LSSFVRDARRHPRPALTASPPPAKSPVNGSLCEPRSPLGGPDPAELLLMGSYLGKPGPPEPALRQDPRERPGRRPPARSP
SQ  PPASAVQRVHHVYPALPTPLLRPSRRPPHRDCGPLSSRFVITPRRRYPIQQAQYSLLGALPTVCWNGGHKKAVLSPRNSR
SQ  MVCSPVTVRIAPPDSKLFRSSMSEQILDTTLSSPSSNAPDPCAKETVLNALKEKKKRTVAEEDQLHLDGQENKRRRHDSG
SQ  GSGHSAFEPLVANGVPAAFVPKPGSLKRSLASQSSDDHLNKRSRTSSVSSLASACTGGIPSSSRNAITSSYSSTRGISQL
SQ  WKRSGPTSSPFSSPASSRSQTPERPAKKTREEEPCQQSSSSPPLVTDKESPGEKVTDTTTGKQQSSWTSPPTPGSSGQRK
SQ  RKIQLLPSRRGDQLTLPPPPELGYSITAEDLDMERKASLQWFNKVLEDKPDDASASATDGPPSTSPPFTFTLPAVGPAAS
SQ  PASLPAPSSNPLLESLKKMQESPAPSSSEPAEAATVAAPSPPKTPSLLAPLVSPLAGPLASTSSDSKPAATFLGLASASS
SQ  ITPLTDSKSSGVSQAEQSVSTPASTASSPTPKPSMLFGMLSPPASSSSLATPAPACASPMFKPIFPATPKSESDSPLPSS
SQ  SSAATTASSSTAPPTAASTTPTFKPIFDKMEPFTAMPLSTPFSLKQTTATATTTATSAPLFTGLGTATSTVASGTAASAS
SQ  KPVFGFGVTTAASTASSTMTSTSQSVLFGGAPPVTTSSSAPALASIFQFGKPLAPAASAAGTSFSQPLASSTQTAASNSG
SQ  FSGFGSTLTTSTSAPATTSQPTLTFSNTVTPTFNIPFSSSAKPALPTYPGANSQPTFGATDGATKPALAPSFGSSFTFGN
SQ  SVASAPSAAPAPATFGSAAQPAFGGLKAAASTFGAPASTQPAFGSTTSVFSFGSATTSGFGAAATAATTTQTTNSGSSSS
SQ  LFGSSAPSPFTFGGSAAPAGSGGFGLSATPGTSSTSGTFSFGSGQSGTPGTTTSFGSLSQNTLGAPSQGSPFAFSVGSTP
SQ  ESKPVFGGTSTPTFGQSAPAPGVGTTGSSLSFGASSTPAQGFVGVGPFGSAAPSFSIGAGSKTPGARQRLQARRQHTRKK
//
ID  P52591;
PN  Nuclear envelope pore membrane protein POM 121;
GN  Pom121;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11448991}. Nucleus membrane {ECO:0000269|PubMed:11448991}; Single-pass membrane protein {ECO:0000269|PubMed:11448991}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11448991}; Single-pass membrane protein {ECO:0000269|PubMed:11448991}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase.
DR  UNIPROT: P52591;
DR  PDB: 4YI0;
DE  Function: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL).
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0008139;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006606;
GO  GO:0006405;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSPAAAAADGGERRRPPLGVREGRGRTRGCGGPAGAAALGLALLGLALYLVPAAAALAWLAVGASAAWWGLSREPRGPRG
SQ  LSSFVRESRRHPRPALTASPLPAKSPVNGSLCEPRSPLGGPDPAELLLMGSYLGKPGPPEPALPQDPRDRPGRRPPSRSP
SQ  PSSSTAQRVHHVYPALPTPLLRPSRRPPHRDCGPLSSRFVITPRRRYPIQQAQYSLLGALPTVCWNGGHKKAVLSARNSR
SQ  MVCSPVTVRIAPPDSKLFRSPMPEQILSTTLSSPSSNAPDPCAKETVLNALKEKKKRTVAEEDQLHLDGQENKRRRHDSS
SQ  GSGHSAFEPLVANGVPAAFVPKPGSLKRSLASQSSDDHLNKRSRTSSVSSLTSTCTGGIPSSSRNAITSSYSSTRGVSQL
SQ  WKRSGPTSSPFSSPASSRSQTPERPAKKTREEEPCHQSSSSAPLVTDKESPGEKVTDPATGKQQSLWTSPPTPGSSGQRK
SQ  RKIQLLPSRRGDQLTLPPPPELGYSITAEDLDMERRASLQWFNKVLEDKTDDASTPATDTSPATSPPFTLTLPTVGPAAS
SQ  PASLPAPSSNPLLESLKKMQESPAPSSSEPPEAATVAAPSPPKTPSLLAPLVSPLTGPLASTSSDSKPTTTFLGLASASS
SQ  ATPLTDTKAPGVSQAQLCVSTPAATAPSPTPASTLFGMLSPPASSSSLATPGPACASPMFKPIFPATPKSESDNPLPTSS
SQ  SAATTTPASTALPTTATATAHTFKPIFESVEPFAAMPLSPPFSLKQTTAPATTAATSAPLLTGLGTATSTVATGTTASAS
SQ  KPVFGFGVTTAASTASTIASTSQSILFGGAPPVTASSSAPALASIFQFGKPLAPAASVAGTSFSQSLASSAQTAASNSSG
SQ  GFSGFGGTLTTSTSAPATTSQPTLTFSNTVTPTFNIPFSASAKPALPTYPGANSQPTFGATDGATKPALAPSFGSSFTFG
SQ  NSVASAPSAAPAPAAFGGAAQPAFGGLKASASTFGTPASTQPAFGSTTSVFSFGSATTSGFGAAAATTQTTHSGSSSSLF
SQ  GSSTPSPFTFGGSAAPAGGGGFGLSATPGTGSTSGTFSFGSGQSGTTGTTTSFGGSLSQNTLGAPSQSSPFAFSVGSTPE
SQ  SKPVFGGTSTPTFGQSAPAPGVGTTGSSLSFGAPSTPAQGFVGVGPFGSGAPSFSIGAGSKTPGARQRLQARRQHTRKK
//
ID  G0SB44;
PN  Nucleoporin POM152;
GN  POM152;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P39685}. Nucleus membrane {ECO:0000250|UniProtKB:P39685}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P39685}. Note=Central core structure of the nuclear pore complex. {ECO:0000250|UniProtKB:P39685}.
DR  UNIPROT: G0SB44;
DR  UNIPROT: G0ZGV5;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. POM152 is important for the de novo assembly of NPCs. {ECO:0000250|UniProtKB:P39685}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSDAPAVGAFPQTPVAARRGPARPSDSTTSTTIKRTSPLPLAPQAGRQATNISPVIPLHILDAPTQRFYAFAFYLALTAW
SQ  KLYDWTQVLEEDTESFLLFLKWIAIDCVFLFGLPELRIPWLELSQPFVMVAFAIHAMFDWILMFNIGFPWQSWVIGLLKV
SQ  FYDREIAISEHNVKLSSILQNSSLIMGRQIINILPEGSAILNPELQPFCLGGDRKTANIPIFFNSTIPVEVELIRTDFET
SQ  GQQESIKLSKSQLRDIERRAKRESQDGDTVQSIVQFDFPVKKTGAYRLGRVLDEYKLEVQRRNPLTFVVSCPKAWVGPAL
SQ  SAHRCVGDLSDLSMMVEGTPPLKIKYSRMINGKDHSFHFQSLQPEGFVSPLSGLRSNNWGYDEDDISWARAQKVPVGLNE
SQ  SMHSSGDWQYSIDEVQDGFGNIIKYDSLADDPDGKPKPKHLTQSFVVKKRPVIRLEGCDLRHPLKVAKGKSKNLPVSYGL
SQ  SGGSREDSTYQIAWQFSPIDTLTESGDHGDVVTIGTYTAKNNRDRPTISAPGLYTLKSVSASQCEGEIQEPSSCLLLNPL
SQ  EPRLSLRHEEIPDTCAGNSIGLRVDLDLIGTPPFIVRYDVISNGERRSERVSIPGLRYQLDLVPRIAGHHKYIFTHVGDS
SQ  IYDGQKLSGPEYVLEQDVKPAAAALIQHSTGKMSSCLGDQVTVDILLLGDPPFTLEWELIHDGKRKQFKVPNIQENSYQI
SQ  KTAPLTTGGEYTLGLTSVQDKRGCRNFLQEELKISVRRQSPRAAFGQVDGKRKILAVEGSSVKLPLRLTGEGPWKVYYAN
SQ  LHDGSPDKPKVQEKIIKSDNGFLEVRGRGAFAITDVWDSQCHGVVDPKASRFDVDWFPRPELSVALTHGVSKTETGFQLQ
SQ  DVCEGDVSGFEVALKGTPPFTVEYEVRHHPLQGSSSLSKKKIEGVVGKEAIQADTSKAGTYTYKFTALEDDLYSSNRGFQ
SQ  PIIVKQNVNRKPTASFVKPGQTFKYCKSEQDNEDGIPITLTGVPPFFLEVEIKHQSAAVPEIYRTPAIDSHSYELKIPRH
SQ  HLRLGTQHIRIRDIRDGSGCHSTSGILSGPSVQVQLFEAPTIYPLETRTDYCVGERISYTLSGQAPFEVWYTFNGVELKA
SQ  KSPNTNFRRIAESPGEFTITSVSDKASECRAPVSITKTIHPLPAVRISKGKSVRVDIHEGGEVDILFEFFGTPPFEFTYT
SQ  RSTNARKGQKSQVLETRHDISHEHSKVIKASQEGTYEVVAIKDKYCSFSTQAVVGLEGGKKDKTKKLKVY
//
ID  O94385;
PN  Nucleoporin pom152;
GN  pom152;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein. Note=Central core structure of the nuclear pore complex. {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94385;
DR  UNIPROT: Q9USB0;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). {ECO:0000250|UniProtKB:P39685}.
DE  Reference Proteome: Yes;
DE  Interaction: O13961; IntAct: EBI-7633650; Score: 0.27
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVTRVASSERPRPLVPESIVDAPTQRLYAIGVFVALQAYKIYDLLKLETSSISDVPKSGFLVKWIIIDAIYLRLLPKFRI
SQ  PWLSFQPAATLLQIAIFAAINLLLSSLSSLKWISIGSILLPYFKKKELSISEHKINPNNVIHNSSRILGQYTLQVLPEGT
SQ  AKINPLHENYCLNSLRKDQYVDLAIQFNSTIPKYIQYSHVDLETKEETLVEVSGRSLRKLLSSSSKNPKEPRLQTIYLKT
SQ  NKRGLYTLKHVVDKSKLDVRIFRSEAVVVSCPTATFASRQSGGRLRERCVGDTDNAELKVTGVAPLQVTYRNWDGKHFNT
SQ  HIIDSTIPDDFHPPAVVLSSNPKDIVFYKGIDIQWARSSEIFVPINTLLKAPGQWIYAVTQVTDALGNSQQFPSNDQFLL
SQ  RFAHGYTEADGESHSLPENVYSVFVHQRPDIQFRGCSIESPANLFPNKETSLSLYSSFSEYNSLEVGVDRYELGLDPQNI
SQ  TVPPLSHKTYQISPRSSANINVKKPGIYVLSSVSSQYCSGEVLEPNTCLVVTPPEAKVSVSFEEISDQCAGSIGARADLE
SQ  LEGTPPFTIAYRMTKDNEASRIQYVTTDRTRYQLNFTPKKAGKYRYIILGIQDANYGYRELSGSSFYKDQTVFPLADASF
SQ  EERRNGDLSTVVKTSCIGDTMSLPVLLTGSAPWTLEYEIFRNNKREESHVVESKDPRYILEVPMLVHGSQYTITLVSVKD
SQ  SNGCKRSLNTADTVIKVRRQRPTATFYSSDNTYTLKSVEGALMKIPLRLAGEKPWYVEYSHTSGLNKVSHHKEVLNDPNS
SQ  YLTVRKSGTYTLLSVSDSSCPGTIQNVEQKYQVEWLPRPFLSIPSLESSVKGKTRYYEQNAVCAGDSSAFEVQLSGSGPF
SQ  LLKHDKILVDEKSKTYPKQKSELSTVQNTVLVKADTAVPGVYHYEFTKLSDSLYSDSDAVTIVNNQSYQAVVLQRVNSLP
SQ  KASFMNVEKLYTFCINTDVTQSNAQLIAIQLQGASPFSLVIGIKNELTGSVSKYTLNDIHESVYKFAFPQEQLTLGKHVV
SQ  RLLQVRDANGCAASITKTQPAAKVSVVEMASLAPLGSRQYYCVGDRLSFALQGLPPFDVEYEFNGVTQHATSDSHILTRL
SQ  IELPGVVAMKSISDHGSHCKSYINPPIEQIVHDIPTVRISNGKDVIENIHEGDQAEISFHFTGTPPFSFSYARRALGKKR
SQ  PGKVLETHTVTGINEYEYKVLSSVEGVYTVLSVQDKYCRYPQDSTSSSNI
//
ID  P39685;
PN  Nucleoporin POM152;
GN  POM152;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Multi-pass membrane protein. Note=Central core structure of the nuclear pore complex.
DR  UNIPROT: P39685;
DR  UNIPROT: D6VZV2;
DR  PDB: 5TVZ;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. POM152 is important for the de novo assembly of NPCs. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11352933, ECO:0000269|PubMed:8682855, ECO:0000269|PubMed:9988776}.
DE  Reference Proteome: Yes;
DE  Interaction: P47042; IntAct: EBI-390972; Score: 0.37
DE  Interaction: Q03790; IntAct: EBI-390975; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: P02994; IntAct: EBI-804163; Score: 0.40
DE  Interaction: Q12158; IntAct: EBI-821936; Score: 0.35
DE  Interaction: P40358; IntAct: EBI-3657572; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3674542; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3692806; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-3734723; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3756439; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3757151; Score: 0.35
DE  Interaction: P39102; IntAct: EBI-3761596; Score: 0.35
DE  Interaction: P39078; IntAct: EBI-3822546; Score: 0.35
GO  GO:0071944;
GO  GO:0016021;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005641;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0043495;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEHRYNVFNDTPRGNHWMGSSVSGSPRPSYSSRPNVNTTRRFQYSDDEPAEKIRPLRSRSFKSTESNISDEKSRISERDS
SQ  KDRYINGDKKVDIYSLPLISTDVLEISKQRTFAVILFLIIQCYKIYDLVILKSGLPLSGLLFKNYRFNFISKYFIIDSFF
SQ  LYVLPSFNIPRLTFKPWVVYLQILAMLLLNIFISSDHEFVLISLIMTTWRKLYTKELSVTGSAINHHRIFDSSAHFKGAL
SQ  TIKILPENTAMFNPLHESYCLPMDTNLFKINSIDVPIRINSTEEIEYIELEYRDLYTNSVELRSLSKKDFKIIDNPKSFL
SQ  KKDQSVLKSHSNDFEEGSTIRYLAVTLQDIGFYQIKKIVDSKKLNLKIHQSHLVVPYCPIASITGTGSNDRCIGDSDNVS
SQ  FEIQGVPPMKLAYSKIVNGQTFSYVDSSLQPEYFESPLQSSKSKQSFTQGELNDLKWGRNQPVNINLDSSITQDGKFAYK
SQ  IDKITDGLGNVVDFTSLPEELKKRYDLSYNFNVHEVPRAALEERFDPKSPTKRSIAIVFEEIKNWISDIPYVISLSYTDA
SQ  QDKSKKIMNVTTDSLTKVLQADLPGSYNLEYIESKFCPGEIVGKSNVLVTMPVAPTMEVKSFPILDQCVGQVGLNFELSF
SQ  TGAPPYYYNTKIYKLENGERKLYDAKRYTSEGTRNRFSYSPPKEGNYEIVFDTVSNKLFTEPIKLEPVKEYTFKTSMRVK
SQ  PSASLKLHHDLKLCLGDHSSVPVALKGQGPFTLTYDIIETFSSKRKTFEIKEIKTNEYVIKTPVFTTGGDYILSLVSIKD
SQ  STGCVVGLSQPDAKIQVRRDIPSAAFNFFEPIKEAKIKHGSVTEIPLKLSGEGPFTVKFKHMDYDGNIVKEFENKFQNSY
SQ  KPALKVSKEGLYQLVDIRDSSCQGNVIYRNSLYKVSFLEKPKFAIQDNHHITKVTENLFSKEEVCQGMEGTVDLALFGSP
SQ  PFILEYDLMAPNGHISTKKIQVATKYASLKLPNQIPGEYITTIKAIFDGNYGESDIHFREHQSELIIKQTVHPIPDVAFA
SQ  DGGKTLRACAANVDQISFLEPINLKFLQGESPFSITFSVYHESTSRTDQYTIDNIDSENFSFEKLYEGMKLGNHAITIDS
SQ  VVDANGCVNSLISGPRNQILVSITDAPKIHILDPSTEYCVGDYVAYQLNGVAPFMIKYEFNGIPLKSKERSSQFVRLASE
SQ  PGIISITSLQDSSSQCIVDFTNPKLKSEFDDLSLNIHPIPSVTVSQGNYVTEDIREGDQAEVIFSFEGTPPFSLTYVRTE
SQ  ETDGKHGKRRSQVVETHKVTDIYSHEYKVITSLQGTYEAIEITDAYCFAKNDLFFNN
//
ID  A1Z6H7;
PN  Nuclear pore membrane glycoprotein 210;
GN  Gp210;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:3919018}; Single-pass type I membrane protein {ECO:0000255}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. Cytoplasm {ECO:0000269|PubMed:2517292}. Note=During mitosis diffusively localized throughout the cytoplasm. {ECO:0000269|PubMed:2517292}.
DR  UNIPROT: A1Z6H7;
DR  UNIPROT: Q6NP18;
DR  UNIPROT: Q9GPI0;
DE  Function: Component of the nuclear pore complex. {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VQA2; IntAct: EBI-273039; Score: 0.00
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: P34082; IntAct: EBI-9928090; Score: 0.35
DE  Interaction: Q9VLS7; IntAct: EBI-9929131; Score: 0.35
DE  Interaction: Q9W0U0; IntAct: EBI-26783748; Score: 0.49
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044611;
GO  GO:0044615;
GO  GO:0070762;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006606;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDSILCMILLILVRNHASEAARLNHPRVLLPIFEDKAINFTLEVDEPNCYKWSSSRQDLISVMPIYKGFSECAYQAVVTV
SQ  RTHDRRRNTAIVFAEEVQTGETLRSDVIVDVIASLNVRTATRQLYLEEAPAMFELHAFDEQGNEFFTLEGIEFDWEILEP
SQ  GSKRPTAMRYLTFTDSPYHTVPPTIEKFEADGKKGHMILLEGINTGTAKVTIAMPQAEYKHVRPVEVYISVLANIIIEPS
SQ  EVTIMAGDSVSFRILQLKMDRLHVIDNNQYYLEVEDSSIAYLRGNSATGAALGRTQVFLRDRNMADSDEVQKGPSALLTV
SQ  AYPNRLSISLLPHLNWVTVQGEHHAIALDLFAADGQKITMGTKYSINSEVDESFFAIVDRTRNGSRLFGQAKKEGITQVY
SQ  GSYKDLSVQAELQIFEELQLAPTKVVLPYDPNSLKPLKLQFHASGGDNNYAWFSGNPQVIQIDTQGQATTEIRDVKSAYV
SQ  NQEVLKDGGKLTAHTTVKVALSKNQKISRVAHIYFLPPERLQITRSNFETALKDFVHVHVGVYARINNSEVPYTSCDNLH
SQ  FQLDFSQPILQLEGNEGAEAAHEACHVLRLRATAVGTTSLRVSYMYMDKVLYDIIDLYVFEPLVVLNPIENEVVLPVGSS
SQ  RNIIYANGPQRSFTVAAEIIQSTAFDEKILKVSKLEFDTQNLITAFTVLCRELGETQFTYRVHNSLPTSSFALYQSEVTT
SQ  KVHCVRPRFLKLYARHNLRDSCPLEKRTSLLFLKDPENKIEIEIEVHDSNNRRLMNISSLGLDWEFSAGEERYQKNIIPH
SQ  RQISELEFNHGVTLPSRDLLVLTLSEVATNFRIKGTVSQYNDKLLAQHGIHAERPPFGIKNPQTGLIYTPLIENEIRLHA
SQ  VNSTLLPKDYMSIFLASGYSERIPIAQGSGYLQLELSEAGIVQVEYNENTRILVLTPLRLGHVRLELTDRCLMNEPSHLS
SQ  ISVVGIGAIEVVSMDRLERTTRIEAIVRLFDTNDNLLLVDQSKLSAYDLSEVVADQSILSVRLGEQENVGPGEIRYTITG
SQ  NQVGETKILFQSGKGIYKVASDPLNIQVFAPIRLFPRDSTLVVGSSIQVYFHGGPHPNTNMIISVEKEQVATISSTVVTA
SQ  HKLGTTKIVGKCLLKNPVTGKDEVVSQDSVEVHVVALKGVQIRTPLVRIHSGAVMPATLWGLSDLSPMILGTLQNTKISW
SQ  KVSQPQVVEIFNVFTTAGIEYQSGDLISVRVRALNPGKATITASVTLADGTILPPATVDLQVFKTLELVTPNAIKMDSIL
SQ  AAPRSILQLKSNMDNVVYKLDDRSNGIVSVTPDGLVHTKDSLGRDLIIATTADQSLPIGIEVKNVQYILVTLMPILKLRE
SQ  LEHKIPRGMNFVFKVSLHDNLGNELSHNIEDFNGLRYELGNKDDVDVQIDNNLTFALNLMRETNNVIGISLKDSTGVKHS
SQ  MDFIKLSVVESDNLFPTKTIFSVGDIICFDSPLTLSSTWRSSNEQIVYINKHTGIAQVLSHRLKPGEKIEITNGDETKRG
SQ  GFLKYDLEVRESDTILFVKSVDTFSGPEYRGQLVIRNHLQSEKYSNLIAQNVSKCARELGSVPVNFFTCRLAAKDALGRN
SQ  LLKMYKVDALFEPSIGQYSCRLQLLTGFIELLSIVKTHDVYLELEAVVAKGVSDKMSLKLVPGIKVFPESVRVTDLKPHE
SQ  IHISGLDKALLKVQVKPSDSKYFAVDFIEHGHGLSKYRLELFDDLPLDENFYILVVSPDTKQSIEVPIIGNTMLAPKCTD
SQ  RRYGGPLVYRILENLGFVLTTTVIVIISIWVYMSCFQTQGVTQVNFEAFKKGKSRTELMQQSGRSSQDDTFGDSFNVRNF
SQ  SPDRRRPPSNALSESYIYGHPRLNSSNRSENSTSFS
//
ID  Q8TEM1;
PN  Nuclear pore membrane glycoprotein 210;
GN  NUP210;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:2195063}. Nucleus membrane {ECO:0000269|PubMed:2195063}; Single-pass type I membrane protein {ECO:0000269|PubMed:2195063}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:2195063}; Single-pass type I membrane protein {ECO:0000269|PubMed:2195063}.
DR  UNIPROT: Q8TEM1;
DR  UNIPROT: A6NN56;
DR  UNIPROT: O94980;
DR  UNIPROT: Q6NXG6;
DR  UNIPROT: Q8NBJ1;
DR  UNIPROT: Q9H6C8;
DR  UNIPROT: Q9UFP3;
DR  Pfam: PF02368;
DR  OMIM: 607703;
DR  DisGeNET: 23225;
DE  Function: Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity. {ECO:0000269|PubMed:14517331}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-32717697; Score: 0.35
DE  Interaction: P0C6X7; IntAct: EBI-26377113; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25490940; Score: 0.53
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9NQT4; IntAct: EBI-373692; Score: 0.00
DE  Interaction: Q81S14; IntAct: EBI-2827359; Score: 0.00
DE  Interaction: Q81X77; IntAct: EBI-2827366; Score: 0.00
DE  Interaction: P02866; IntAct: EBI-2906001; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-3045543; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-3050465; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6191076; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q5TB80; IntAct: EBI-11362825; Score: 0.35
DE  Interaction: Q2MV58; IntAct: EBI-11366929; Score: 0.27
DE  Interaction: O94955; IntAct: EBI-21879222; Score: 0.35
DE  Interaction: Q9UK39; IntAct: EBI-21901186; Score: 0.40
DE  Interaction: P11279; IntAct: EBI-16795231; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: Q9NR11; IntAct: EBI-20904296; Score: 0.40
DE  Interaction: Q9NRD1; IntAct: EBI-21259874; Score: 0.35
DE  Interaction: Q96JQ5; IntAct: EBI-21261679; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: J3KSN0; IntAct: EBI-21264801; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: Q8IYR2; IntAct: EBI-25485167; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: P60033; IntAct: EBI-25645944; Score: 0.35
DE  Interaction: Q6PB30; IntAct: EBI-26354359; Score: 0.35
DE  Interaction: K9N7A1; IntAct: EBI-26374565; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.50
DE  Interaction: O00311; IntAct: EBI-28930020; Score: 0.35
DE  Interaction: P36888; IntAct: EBI-28935096; Score: 0.35
DE  Interaction: P42685; IntAct: EBI-28935169; Score: 0.35
DE  Interaction: Q14012; IntAct: EBI-28939656; Score: 0.35
DE  Interaction: Q86UX6; IntAct: EBI-28942129; Score: 0.35
DE  Interaction: Q8NI60; IntAct: EBI-28943519; Score: 0.35
DE  Interaction: Q9BUB5; IntAct: EBI-28944975; Score: 0.35
DE  Interaction: Q9NSY0; IntAct: EBI-28946547; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-28946805; Score: 0.35
DE  Interaction: Q9Y6S9; IntAct: EBI-28948011; Score: 0.35
DE  Interaction: Q9H5K3; IntAct: EBI-28948637; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q96IA0; IntAct: EBI-27116623; Score: 0.27
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
DE  Interaction: Q9UN86; IntAct: EBI-28955513; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-30863806; Score: 0.35
DE  Interaction: P21860; IntAct: EBI-32718413; Score: 0.35
DE  Interaction: P08069; IntAct: EBI-32718669; Score: 0.35
DE  Interaction: P06213; IntAct: EBI-32718777; Score: 0.42
DE  Interaction: Q16288; IntAct: EBI-32719212; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-32719373; Score: 0.35
DE  Interaction: Q5JZY3; IntAct: EBI-32720634; Score: 0.27
DE  Interaction: P08581; IntAct: EBI-32723963; Score: 0.27
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAARGRGLLLLTLSVLLAAGPSAAAAKLNIPKVLLPFTRATRVNFTLEASEGCYRWLSTRPEVASIEPLGLDEQQCSQKA
SQ  VVQARLTQPARLTSIIFAEDITTGQVLRCDAIVDLIHDIQIVSTTRELYLEDSPLELKIQALDSEGNTFSTLAGLVFEWT
SQ  IVKDSEADRFSDSHNALRILTFLESTYIPPSYISEMEKAAKQGDTILVSGMKTGSSKLKARIQEAVYKNVRPAEVRLLIL
SQ  ENILLNPAYDVYLMVGTSIHYKVQKIRQGKITELSMPSDQYELQLQNSIPGPEGDPARPVAVLAQDTSMVTALQLGQSSL
SQ  VLGHRSIRMQGASRLPNSTIYVVEPGYLGFTVHPGDRWVLETGRLYEITIEVFDKFSNKVYVSDNIRIETVLPAEFFEVL
SQ  SSSQNGSYHRIRALKRGQTAIDAALTSVVDQDGGVHILQVPVWNQQEVEIHIPITLYPSILTFPWQPKTGAYQYTIRAHG
SQ  GSGNFSWSSSSHLVATVTVKGVMTTGSDIGFSVIQAHDVQNPLHFGEMKVYVIEPHSMEFAPCQVEARVGQALELPLRIS
SQ  GLMPGGASEVVTLSDCSHFDLAVEVENQGVFQPLPGRLPPGSEHCSGIRVKAEAQGSTTLLVSYRHGHVHLSAKITIAAY
SQ  LPLKAVDPSSVALVTLGSSKEMLFEGGPRPWILEPSKFFQNVTAEDTDSIGLALFAPHSSRNYQQHWILVTCQALGEQVI
SQ  ALSVGNKPSLTNPFPAVEPAVVKFVCAPPSRLTLAPVYTSPQLDMSCPLLQQNKQVVPVSSHRNPRLDLAAYDQEGRRFD
SQ  NFSSLSIQWESTRPVLASIEPELPMQLVSQDDESGQKKLHGLQAILVHEASGTTAITATATGYQESHLSSARTKQPHDPL
SQ  VPLSASIELILVEDVRVSPEEVTIYNHPGIQAELRIREGSGYFFLNTSTADVVKVAYQEARGVAMVHPLLPGSSTIMIHD
SQ  LCLVFPAPAKAVVYVSDIQELYIRVVDKVEIGKTVKAYVRVLDLHKKPFLAKYFPFMDLKLRAASPIITLVALDEALDNY
SQ  TITFLIRGVAIGQTSLTASVTNKAGQRINSAPQQIEVFPPFRLMPRKVTLLIGATMQVTSEGGPQPQSNILFSISNESVA
SQ  LVSAAGLVQGLAIGNGTVSGLVQAVDAETGKVVIISQDLVQVEVLLLRAVRIRAPIMRMRTGTQMPIYVTGITNHQNPFS
SQ  FGNAVPGLTFHWSVTKRDVLDLRGRHHEASIRLPSQYNFAMNVLGRVKGRTGLRVVVKAVDPTSGQLYGLARELSDEIQV
SQ  QVFEKLQLLNPEIEAEQILMSPNSYIKLQTNRDGAASLSYRVLDGPEKVPVVHVDEKGFLASGSMIGTSTIEVIAQEPFG
SQ  ANQTIIVAVKVSPVSYLRVSMSPVLHTQNKEALVAVPLGMTVTFTVHFHDNSGDVFHAHSSVLNFATNRDDFVQIGKGPT
SQ  NNTCVVRTVSVGLTLLRVWDAEHPGLSDFMPLPVLQAISPELSGAMVVGDVLCLATVLTSLEGLSGTWSSSANSILHIDP
SQ  KTGVAVARAVGSVTVYYEVAGHLRTYKEVVVSVPQRIMARHLHPIQTSFQEATASKVIVAVGDRSSNLRGECTPTQREVI
SQ  QALHPETLISCQSQFKPAVFDFPSQDVFTVEPQFDTALGQYFCSITMHRLTDKQRKHLSMKKTALVVSASLSSSHFSTEQ
SQ  VGAEVPFSPGLFADQAEILLSNHYTSSEIRVFGAPEVLENLEVKSGSPAVLAFAKEKSFGWPSFITYTVGVLDPAAGSQG
SQ  PLSTTLTFSSPVTNQAIAIPVTVAFVVDRRGPGPYGASLFQHFLDSYQVMFFTLFALLAGTAVMIIAYHTVCTPRDLAVP
SQ  AALTPRASPGHSPHYFAASSPTSPNALPPARKASPPSGLWSPAYASH
//
ID  Q9QY81;
PN  Nuclear pore membrane glycoprotein 210;
GN  Nup210;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single- pass type I membrane protein {ECO:0000250}.
DR  UNIPROT: Q9QY81;
DR  UNIPROT: Q3U031;
DR  UNIPROT: Q69ZW2;
DR  UNIPROT: Q7TQM1;
DR  Pfam: PF02368;
DE  Function: Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity.
DE  Reference Proteome: Yes;
DE  Interaction: Q15654; IntAct: EBI-5796496; Score: 0.37
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0065003;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARASLVQPALWALLLLQVVGPAAAAKLNIPKVLLPFTRATRVNFTLEASEGCYRWSSTRPEVASIEPLGSSEQQCSQKA
SQ  VVQARLTQPARLTSIIFAEDITTGQVLRCDAIVDLIHGIQIVSTTRELYLEDSPLELKIQALDSEGNTFSTLAGLVFDWT
SQ  IVKDTEANGFSDSHNALRILTFLESTYIPPSYISEMEKAAKQGDTILVSGMKTGSSKLKARIQEAVYKNVRPAEVRLLIL
SQ  ENILLNPAYDVYLLVGTSIHYKVQKIRQGKITELSMPSDQYELQLQNSIPDPQGDPARPVAILTQDTSRVTAMQMGQSNL
SQ  VLGHRSIRMQGASRLPNSTIYVVEAGYLGFTVYPGDRWVLETGHLYAITIEVFDRSSNKVYPSDNIRIEAVLPAEFFEVL
SQ  SSSQNGSYHHIRAIQSGQTAISATLTSVVDQDGGVHVLQVPVWNQQEVDIHIPITLYPSILTFPWQPKTGAYQYTIKAHG
SQ  GSGNFSWSSSSSMVATVTVKGVMTTSGDTGLSVIRAHDVQNPLHFGEMKVYVIEPSSMEFAPCQVEARVGHTLELPLTIS
SQ  GFMPGGGSEVVTLSDCSHFDLVVEVENQGVFQPLPGRLPPGPEHCSGVKVKADAQGSTTLLVSYTHGHVHLDAKITLAAY
SQ  LPLKAVDPSSVAVVTLGSSKEMLFEGGPRPWVLEPSKFFRNVTSEDTGSISLSLLGPPASRNYQQHRVLMTCQALGEQVI
SQ  ALSVGNRPSLSNPFPAVEPTVVKSICAPPSRLTLMPVYALPQLDLSCPLLQQNKQVVPVSSHRNPLLDLGAYDQQGRRFD
SQ  NFSSLSIQWESSRPLLASIELDQPMQLVSQDDGNGQKKLHGLQTVSVHEASGTTAISATATGYQQSHLSEARVKQPHDPL
SQ  VPVSASIELILVEDVRVSPEEMTIYNHPGVQVELYITEGSGYFFLNTSTQDIIKVAYQDTRGVALVHPLLPGSSTVMVHD
SQ  LCLAFPAPAKAIIHVSDIQELYVRVVDKVEIGKAVKAYVRVLDFYKKPFLAKYFTFMDLKLQAASQIITLVTLDEALDNY
SQ  TATFLVHGVAIGQTSLSASVTDKSGQRVSSTPQQIEVFPPFRLIPRKVTLIIGAMMQITSEGGPQPQSNILFSINNESVA
SQ  AVSSSGLVRGLMVGNGSVLGVVQAVDAETGKVIIVSQDLVEVEVLQLQAVRIRAPITRMRTGTQMPVFVTGITSNQSPFS
SQ  FGNAVPGLTFHWSVTKRDVLDLRGRHHEVSIRLPPQYNFAMNVYGRVKGRTGLRVVVKALDPTAGQLHGLGKELSDEIQI
SQ  QVFEKLRLLNPEIEAEQILMSPNSFIKLQTNRDGAAILSYRVLDGPEKAPIVHTDEKGFLVSGSGIGVSTLEVIAQEPFG
SQ  TNQTILVAVKVSPVSYLRISMSPVLHTQHKEALTALPLGMTVTFIVHFHDSSGDIFHAHNSVLNFATNRDDFVQIGKGAT
SQ  NNTCIIRTVSVGLTLLHVWDVEHLGLSDFVPLPVLQAITPELSGAVVVGDILCLASVLTSLGGVSGTWSSSASHVLYVDP
SQ  KTGVAIARDAGSVTVYYEIAGQLKTFKEIVVGTPQKIVARRLHSAQTSIQEATASKVTVSVGDRSSNLLGECSPAQREAI
SQ  EALHPESLISCQLQFKQDVFDFPACDVFTVEPGFDAALGQYLCSVTMRRLTDKQLKHLNMKKTSLAVTASIPSSYTSVEK
SQ  VGAEVPFSPGLYANQAEILLSNHYTSSEVKVFGAVESLENLEVKSGSPAVLAFVKEKSFGLPSFITYTVGVLDPTAGSQG
SQ  PLSTALTFSSPATNQAITIPVTVAFVLDRRGPGPYGASLLSHFLDSYQVMFFTFFALLAGTAVTIIAYHTVCAPRELASP
SQ  LALTPRASPQHSPHYLASSPAAFNTLPSGRKASPPSGLWSPAYASH
//
ID  P11654;
PN  Nuclear pore membrane glycoprotein 210;
GN  Nup210;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex. Nucleus membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein.
DR  UNIPROT: P11654;
DR  Pfam: PF02368;
DE  Function: Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0065003;
TP  Membrane Topology: Transmembrane; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MARASLIQPGLWALLLLQAVGPAVAAKLNIPKVLLPFTRATRVNFTLEASEGCYRWSSTRPEVASIEPLGSSEQQCSQKA
SQ  VVQARLTQPARLTSIIFAEDITTGQVLRCDAIVDLIHGIQIVSTTRELYLEDSPLELKIQALDSEGNTFSTLAGLVFDWT
SQ  IVKDTEANGFSDSHNALRILTFLESTYIPPSYISEMEKAAKQGDTILVSGMKTGSSKLKARIQEAVYKNVRPAEVRLLIL
SQ  ENILLNPAYDVYLLVGTSIHYKVQKIRQGKITELSMPSDQYELQLQNSIPDPQGDPARPVAVLTQDTSRVTAMQMGQSNL
SQ  VLGHRSIRMQGASRLPNSTIYVVEAGYLGFTVHPGDRWVLETGHLYAVTIEVFDRSSNKVYPSDNIRIEAVFPAEFFEVL
SQ  SSSQNGSYHHVRAIQSGQTTISASLTSVVDQDGGVHVLQVPVWNQQEVDIHIPITLYPSILTFPWQPKTGAYQYTIKAHG
SQ  GSGNFTWSSSSYMVATVTVKGVMTTGGDTGLSVIRAHDVQNPLHFGEMKVYVIEPSSMEFAPCQVEARVGHTLELPLTIS
SQ  GLMPGGSSEVVTLSDCSHFDLVVEVENQGVFQPLPGRLPPGPEHCSGVKVRADAQGSTTLLVSYTHGHVHLGAKITLAAY
SQ  LPLKAVDPSSVAVVTLGSSKEMLFEGGPRPWVLEPSKFFRNVTSEDTGSISLSLLGPPASRNYQQHRVLVTCQALGEQVI
SQ  ALSVGNRPSLSNPFPAVEPTVVKSVCAPPSRLTLMPVYALPQLDLSCPLLQQNKQVVPVSSHRNPLLDLGAYDQQGRRFD
SQ  NFSSLSIQWESFRPLLASIEVDQPMQLVSQDDGNGQKKLHGLQTVSVHEASGTTAISATATGYQQSHLSAAGVKQLRDPL
SQ  VPVSASIELILVEDVRVSPEEVTIYNHPGVQVELHITEGSGYFFLNTSTQDIINVAYQDTRGVAMVHPLFPGSSTVMVHD
SQ  LCLTFPAPAKATIHVSDIQELYVRVVDKVEIGKAVKAYVRVLDFYKKPFLAKYFTFMDLKLRAASQIITLVTLDEALDNY
SQ  TATFLVHGVAIGQTSLSASVTDKSGQRVSSTAQQIEVFPPFRLIPRKVTLIIGAMIQITSEGGPQPQSNILFSINNESVA
SQ  AVSSAGLVRGLMVGNGSVLGVVQAVDAETGKVIIVSQDHVEVEVLQLQAVRIRAPITRMRTGTQMPVYVTGITSNQSPFS
SQ  FGNAVPGLTFHWSVTKRDVLDLRGRHHEVSIRLSPQYNFAMNVHGRVKGRTGLRVVVKALDPTAGQLHGLGKELSDEIQI
SQ  QVFEKLRLLNPEVEAEQILMSPNSFIKLQTNRDGAAILSYRVLDGPEKAPIVHIDEKGFLVSGSGIGVSTLEVIAQEPFG
SQ  TNQTVLVAVKVSPISYLRISMSPVLHTQHKEVLTALPLGMTVTFTVHFHDSSGDIFHAHNSDLNFATNRDDFVQIGKGAT
SQ  NNTCIIRTVSVGLTLLHVWDVEHLGLSDFVPLPVLQAITPELSGAVVVGDILCLASVLISLGGVSGTWSSSAGNVLYVDP
SQ  KTGVAIARDAGPVTVYYEIAGHLKTFKEIVVVTPQKIVARRLHATQTSIQEATASKVTVSVGDRSSNLLGECSSAQREAI
SQ  EALHPESLISCQLQFKQDVFDFPARDIFSVEPGFDTALGQYLCSVTMHRLTDKQLKHLNMKKTSLAVTASMPSSRTSVEK
SQ  VGAEVPFSPGLYANQAEILLSNHYPSSEVKIFGAVEILENLEVRSGSPAVLASVKEKSFGLPSFITYTVGVLDPTAGSQG
SQ  PLSTALTFSSPATNQAITIPVTVAFVLDRRGPGPYGASLLSHFLDSYQVMFFTFFALLAGTAVTIIAYHTVCAPRELASP
SQ  LALTPHASPQHSPHYLASSPTAFNTLPSDRKASPPSGLWSPAYASH
//
ID  Q9WNW0;
PN  RNA-directed RNA polymerase;
GN  POL1;
OS  76875;
SL  Nucleus Position: SL-0382;
SL  Comments: [Putative helicase]: Host membrane {ECO:0000250|UniProtKB:P03600}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03600}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}.
DR  UNIPROT: Q9WNW0;
DR  Pfam: PF00548;
DR  Pfam: PF00680;
DR  Pfam: PF00910;
DR  PROSITE: PS51874;
DR  PROSITE: PS50507;
DR  PROSITE: PS51218;
DE  Function: [Picornain 3C-like protease]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000250|UniProtKB:P03600}. [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral single-stranded RNA1 and RNA2 molecules. {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins. The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [Putative helicase]: The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000250|UniProtKB:P03600}.
DE  Reference Proteome: No;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0018144;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDFSTMQVVVGFLKTSMGLQSIRDIVQKAKVDEKDKTLLHIHLCFFHANEMARDLNEGMDVSQIHSSAAIKYRAAIVTRH
SQ  VKMNVETGGYDRKRMVEYNNETCVNWFSCEFKEEKEESQELPVDEDCVEEIVENFLENCGISDQNDQISTTSNANYAFGQ
SQ  GLYEYATRVSDAIVAVISGSIKKGIDEFLDKVYAAMSQIFAAWMPKIRAAFQWFENIKEVVKNWARTMHEKINCILVGME
SQ  DCLYMGAGLVAATCIVTLLEKFMVVTKILPAPCGAATLFLTTAMATISAAYVCTKAVEKSVMLTNVLHFVTTNCQIVLNA
SQ  LFNHDATKKELGANQNEGEAPTGVGQFGISTMLQDVANLMSTWSTNSVTEIGRTFGAISQIKNGILALRDMVYFVFEKLS
SQ  DLAHKVLGFESQVLADLTILLGENVADWLSECDCMVSYMLEFNSRNREIFDRLSQLIEKGRLIRTGVLRTGHRGSSQVMA
SQ  LVTKALEKLIELHNSVVMSGSNTTRKAPFMVFFTGASGTGKTSVVQRVAINWLQEEQLGTNEIYSRNGQDPFWSGYKRHA
SQ  VVTYDDFGAVPGTTSNEAEIINVISRNPYATVMAGLAEKGMYFDSRLVLASRNFLAANPESGVHDSEAYERRRHAVIRVS
SQ  LKPGVPYNADDPCANQTYTLLDSKTPFREIQTFETYAELWSYLYTSFKEHEVQEELYLKSLPILDSDKKEALEGLVGLTV
SQ  IATSFAPKAVMQYGMEKFPGHHFLVSDGEKCYFWHGDGSVESASVEQMQLSKQDVAQLKQQGLSTAMMYKDLAKAFPTLN
SQ  SLAVLYAKNIVVKRWVGPDLEPTKTCEDVYMREQIGNLPKWQRAYLYVLSKYLTTQSPRGWFMECLEETKKNLRATYLWE
SQ  YKQWPLPLKLALGSLIAIMAGGAIWYSLQSLWCMSGDASFVAGAATVFSVSSFAGQSDIPNRDNSERSFRNRKVRARTWQ
SQ  GQSSCFGDSALWIAETCMATLTFSNVRTQVCLAPGRGFFGVNHCLAAIPAGVMVKMDSSIGVTYFVWGKEKLLQFDGNEI
SQ  ALYMTSTLPKTVDSLLGRIHFDVETLPKTFSAVFFSYKYDPMIQQMVPELGSVTCKVHNKAYTLAHGEYRREIPQSLSYE
SQ  ASTVAGDCGSLILAEIEGKFKLVGMHVAFNGREGSASFMPYHASLDQKVGQGDFMLKYQEWAEPKILGPGCRAMGLIDPE
SQ  HALAASGKTTFVETPEEWHLDYPCDKLPSVLARGDPRLAGTVHADYDPFASGMSKYAKEAGPFDAASLKQVCSGIVEIWE
SQ  DASADFPMDEVDLDTAINGLENVEFFDALVLGTSEGFPYRLDRGPGDKGKSRYVSGESGSLKITDEGVLSDIAWFEEVSK
SQ  TQVPDLYCIECVKDERLPIRKVLHEPKSRLFTVLPMSYNIVIRKKFLNFVRFFMKRRDVLTAQVGINPYSREWTRMANKL
SQ  LSKGNNILCCDYSRFDGFLPKCIMNEIGNMIARLMKTDEVSRTQIKNLMLACTSRYAMCNRVLYRVENGIPSGFPLTVIV
SQ  NSILNEILVKYAYWHCFEDNPSVQSNFDAHVSMVVYGDDNLISVSDAISSRFDGNFLVSFMEGLGIKVTDGIDKTKVGIE
SQ  FRRLENCDFLKRSFKMSPDGTWRSPMSKESLWPQLHFVKAKKLEMAEAYINNCNNILRELWLHDVKEAEEFRNKVLRNLR
SQ  WIGHEQLLNMQQLAVFHSEQMNGVSDFLSTCVTVDSIPLMDPLVPGMLPVKTSEIIPRVFVAAEKHFEGNFNDFFTISIT
SQ  TSRKFEEDKGFVLLFPYGAGRGGLPTTQFMRENVIRKGCSIQKKFRQAYEKGNNILFISQSSVVPSYVFAVMLLHSIGAI
SQ  SRLSSNKALTQAMQTCKRLEYLPKEYEEFF
//
ID  Q76L40;
PN  RNA-directed RNA polymerase;
GN  RNA1;
OS  649895;
SL  Nucleus Position: SL-0382;
SL  Comments: [Putative helicase]: Host membrane {ECO:0000250|UniProtKB:P03600}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03600}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}.
DR  UNIPROT: Q76L40;
DR  Pfam: PF00548;
DR  Pfam: PF00680;
DR  Pfam: PF00910;
DR  PROSITE: PS51874;
DR  PROSITE: PS50507;
DR  PROSITE: PS51218;
DE  Function: [Picornain 3C-like protease]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000250|UniProtKB:P03600}. [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral single-stranded RNA1 and RNA2 molecules. {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins. The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [Putative helicase]: The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000250|UniProtKB:P03600}.
DE  Reference Proteome: Yes;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0018144;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDSETIDMCVKFLKISFGLQSLKNLVKELFGGSELEKLAYVHAAFFHANEMAIHWNADLPWEEVMSSKRIKERFGYVKSH
SQ  FLRNVVYNADASGQMIRYNTTTCEQWFCCNFNLASYSASYNSLVPEEGGSMPINEEAEIKIGQSLLTCAQSVTKAIYAKL
SQ  STLTTRSIQGFLECLRDAICGAFSSWLPCIRGAFAWFGNIIEVLKHWAGAAHEKLHNFLEGIEECLYMGLGLVASTCIVA
SQ  LIEKFLVTMSVISGPCGRPTLFLTSAMAIISSTYLLSKAVEKSSAFTMLLGFVTQSCQTVLGSLFGKSAKGSEEAQGQFG
SQ  PSAMLESLATLVSSWSSSSVTEIGRTFGAISQIKNGIIALKDMALFVFSKLCEMASKVLGFESQILADLSIILGENVADW
SQ  LDECDCMLAYLLEFNSNARDIFDRLSQLIEKGKAIRMGILRTTHRGPSQVLSLVTKALDKLTELHNSVIMSGANSTRKTP
SQ  FMLFFTGKSGVGKTSVVQRMAANWLQQEQLGSNEVYSRNGLDPFWSGYKRQAVVTYDDFGAVPGSVSNEAEIINVVSSNP
SQ  HSVMMADLKEKGMYFDSRLIIASSNFLAANPESGVHDSEAYERRRHVVVQVSLKEDMAYDPGNPCANQRYTLLESKAPFA
SQ  EKAVFESYEELWSHVYNAFKAHEEKEKLFLSSLPIPERSEKEALQALIGICVMTTSYAPKAVIQYGIDHLVGYHYLISSA
SQ  EHVYFWHEKGEVEIVPMHLMKLDKMDKATMASTSLKSALMCQDMAKNFPTLNPLAVLYAKNIVIRGWVDANLQASKKCED
SQ  SYMREQIESLPKWQRAYLHVLSGHIASNETRGWFLNCLEVTKSNSRSSYIWEYKSWPMPLKLALGSFLAILAGSAIFCSL
SQ  QSLWSISGNASFVAGAASIFTIGSATAQSAPPNKDGSEYTYRNKKIKIRNWEGQGPCFGDSALWIAENCMATLVVMKDRV
SQ  QVCMAPGRSFLGVNHFLRMIPNGVMVKLETGMTETYFVWEKSKLKLFENSEIALYTSSNLPKAPDSLVDRFHFDLETLPK
SQ  TFPAQFFTYKFDKDMQQYVPELGELLCKKAERALCVVSGEYRRVISHHLTYRNPTVAGDCGGLVLAIIEGKCKLVGLHVA
SQ  SDGEEGAASPVPWDPDFKVAQGQSDFLLSYDEWAVPKVLGPGCKAVGIISPEHTVGSGGKTSFLETPIEWQLNRPCGKIP
SQ  SILVKGDVRLAGTENADYDPFAVGMTKYAKEAGPFEPNGLDRVCESIAETWHDASDGFEFGPVDLEAALNGIENMEYFDA
SQ  LVLSTSEGYPYRLDRKPGEKGKARYVEGEPGNLEITDERILADIHWFEEISKTQVPDLYCIECVKDERLPVRKVIKEPKS
SQ  RLFTVLPMSYNLAIRKKFLNFVRFIMKRRDVLPCQVGINPYSRQWGKVADRLLEKGNSILCCDYSRFDGFLPKCIMVKIA
SQ  EMFSNIVGETGAEREQTKNLMLACCSRYAICGRVLYRVENGIPSGFPLTVIVNSILNEILIKYAYWKCFETESLIRDHFD
SQ  TYVAMVVYGDDNLISVSEAISSKFNGNFLVNFMCNLGIKVTDGVDKTKVGIEFRTIEDCDFLKRKFKENADGTWSGVMAE
SQ  EHLWPQLHFVKAKKVEMSEAYISNCNNILRELWLGSPEKAAAFRREVISKLKWVEPQRLLTISQVALFHNEQMNGEHPFV
SQ  EACHQLENLELMAPLEPGMLPIKTQEIMPGLFVASEKNFTGNFDDYFTISITTNRKFEDGKGFQIIFPYGAGRGGLPSKA
SQ  FMEQNVIRKGCAIQKAFKQGLEKGNKMLFISQSSVIPAYVFAIMLYRSVDRLPRALSNKALTSALGICKKLSYLPKDFPD
SQ  LF
//
ID  Q9YJU5;
PN  RNA-directed RNA polymerase;
GN  POL1;
OS  31715;
SL  Nucleus Position: SL-0382;
SL  Comments: [Putative helicase]: Host membrane {ECO:0000250|UniProtKB:P03600}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03600}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}.
DR  UNIPROT: Q9YJU5;
DR  Pfam: PF00680;
DR  Pfam: PF00910;
DR  PROSITE: PS51874;
DR  PROSITE: PS50507;
DR  PROSITE: PS51218;
DE  Function: [Picornain 3C-like protease]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000250|UniProtKB:P03600}. [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral single-stranded RNA1 and RNA2 molecules. {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins. The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [Putative helicase]: The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000250|UniProtKB:P03600}.
DE  Reference Proteome: No;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0018144;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKFYPGQNISEIVYHFQSNETANRLDAYFACGCEEDTEVLARLKQCNPRLLHLSYAAFCLEMGSHSIEEMEYDDGELIFS
SQ  YFQNFLLSIVSNSSKTTKLRAYIRSAFAYHFQHFVEFDQYTNDSLNTVDTSVSAQGIADLALSMVRWIPTQIKKVVNFGV
SQ  GSVIESFSEHFNKLLMQYCPIVFQAFSWVNNIWTMVKEWIEEAAKEISWFLQGCKELHAWGMCILASSCALGLVEKCLIS
SQ  LGMISESFDLVGLFVRSAIVGAFCVSIKTGKFVTNSELITCATIAVSTIATVMSQAFKPSEEIKGQFQALSVLEGLATQL
SQ  TSFCDTSLVAMGKTCTAFNQICTAGKNVKVIAGRLLEVVSNFVRKLLGLDSAFLRDAALIFSQDVDGWLRNISWCQEQFL
SQ  LKAYMSQDDLIVLRSLVVKGERMREQMLEGEVKVSPSVCNLIVKGCEEANKLMRESRLHCSKTIRKIPFVIFAHGESRVG
SQ  KSLLVDRLITDFCDHLEIGEDAVYSRNPSDPFWSGYRRQPIVTIDDFAAVVSEPSAEAQLIPLVSSAPYPINMAGLEEKG
SQ  MHFDSQIMMCSSNFLEPSPEAKIRDDMAFRNRRHVLITVELKPGVEYDESDFTKNQRYLLKTWFHYHYVVDQTFESYADL
SQ  LAHCFTKWERHVKEQESNLSQIKGKKSESGHFYNFQQLMDLAVSWNLNADIMKNRIKAERNDMVYVFSAGRKDKILHCFL
SQ  NKEGECTVRPDSIDDPEAQALLKASETMLMKAYAFLKYNNATNLIVRTHLAELVNEDFYDEKFNFIGTIGTPAFHRQIAA
SQ  HLEKMPLWQKAILCGMGHCLSRKSKETWYTGMKEKFVQMMKSIYETEVTDWPVPLKIISGTILATILGTTFWKLFSFLRD
SQ  AGNGGVFVGNVASAFTTSSVLEAQSRKPNRYEVSQYRYRNVPIKRRAWVEGQMSFDQSVVAIMSKCKASMRMGNTDAQIL
SQ  MVPGRRFIAHGHFFKNLTQKVRVQIVTSEKSYWHVYDPDKFQMFDNSEIGLYTNPTLEDIPHSAWDLFCWDSEKTLPNNF
SQ  SAELLSCKLDTVTGQYYPRMAPINCRVHRQPIHITEGNYVRKQDVSIEYDACTIPNDCGSLVVAKVGNHKQIVGFHVAGS
SQ  KGRLGYASLIPYVEPVVQAQSAEVYFDFFPVEVDSQEGVAHIGELKSGVYVPLPTKTNLVETPKEWQLDLPCDKIPSVLT
SQ  TTDERLVGTEHEDMTHSWWYSKYATPMMPLDEEILSKVAQDMVEEWFDCVDEEDTFEEVSLSAALNGVEGLDYMERIPLA
SQ  TSEGFPHVLSRKNGEKGKRRFVTGDGEEMSLIPGTSVEEAYNKLTVELEKCVPTLVGIECPKDEKLPRRKIFDKPKTRCF
SQ  TILPMEFNLVVRQKFLNFVRFIMKKRDKLSCQVGINPYSMEWTGLANRLLSKGNDILCCDYASFSGLITKQVMSKMAEMI
SQ  NSLCGGDEKLMRERTHLLLACCSRMAICKKDIWRVECGIPSGFPLTVICNSIFNEMLIRYSYEKLLRQAKAPSMFLQSFR
SQ  NFISLCVYGDDNLISVHEYVKPYFSGSKLKSFLASHNITITDGIDKTSATLQFRKLSECDFLKRNFKQMSNVLWVAPEDK
SQ  ASLWSQLHYVSCNNLEMQEAYLVNLVNVLRELYLHSPEEARRLRRKALSCIEWLQKADVPTIAQIEEFHSMQRIMNAPDS
SQ  NDNIDLLLSIDLLGLQGAARPSQIRLWFDDKLVLANTQEFFDGNFPADSWLPIFVNCLYPVSQLPAEAVIVNVVCGSGRG
SQ  GLPTTAWISSAVNNRSSDINKKIRTALGKGKKIVFLTRVDPFPVALLAVLFGVKNEILSSNATNPMLTRLLENCKSLKYL
SQ  VDECPFAFVN
//
ID  P03600;
PN  RNA-directed RNA polymerase;
GN  POL1;
OS  928299;
SL  Nucleus Position: SL-0382;
SL  Comments: [Putative helicase]: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12021362}. [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000269|PubMed:10864669}. [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12021362}.
DR  UNIPROT: P03600;
DR  Pfam: PF00548;
DR  Pfam: PF00680;
DR  Pfam: PF00910;
DR  PROSITE: PS51874;
DR  PROSITE: PS50507;
DR  PROSITE: PS51218;
DE  Function: [Picornain 3C-like protease]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000269|PubMed:16453750, ECO:0000269|PubMed:16789216, ECO:0000269|PubMed:8811039}. [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral single-stranded RNA1 and RNA2 molecules. {ECO:0000269|PubMed:11883002, ECO:0000269|PubMed:16453534}. [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins (PubMed:1413528). The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis (PubMed:12021362). {ECO:0000269|PubMed:12021362, ECO:0000269|PubMed:1413528}. [Putative helicase]: The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000269|PubMed:12021362}. [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000305|PubMed:1431806}.
DE  Reference Proteome: Yes;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0008234;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0039690;
GO  GO:0006508;
GO  GO:0070613;
GO  GO:0018144;
GO  GO:0018259;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLPEYEADSEALLSQLTIEFTPGMTVSSLLAQVTTNDFHSAIEFFAAEKAVDIEGVHYNAYMQQIRKNPSLLRISVVAY
SQ  AFHVSDMVAETMSYDVYEFLYKHYALFISNLVTRTLRFKELLLFCKQQFLEKMQASIVWAPELEQYLQVEGDAVAQGVSQ
SQ  LLYKMVTWVPTFVRGAVDWSVDAILVSFRKHFEKMVQEYVPMAHRVCSWLSQLWDKIVQWISQASETMGWFLDGCRDLMT
SQ  WGIATLATCSALSLVEKLLVAMGFLVEPFGLSGIFLRTGVVAAACYNYGTNSKGFAEMMALLSLAANCVSTVIVGGFFPG
SQ  EKDNAQSSPVILLEGLAGQMQNFCETTLVSVGKTCTAVNAISTCCGNLKALAGRILGMLRDFIWKTLGFETRFLADASLL
SQ  FGEDVDGWLKAISDLRDQFIAKSYCSQDEMMQILVLLEKGRQMRKSGLSKGGISPAIINLILKGINDLEQLNRSCSVQGV
SQ  RGVRKMPFTIFFQGKSRTGKSLLMSQVTKDFQDHYGLGGETVYSRNPCDQYWSGYRRQPFVLMDDFAAVVTEPSAEAQMI
SQ  NLISSAPYPLNMAGLEEKGICFDSQFVFVSTNFLEVSPEAKVRDDEAFKNRRHVIVQVSNDPAKAYDAANFASNQIYTIL
SQ  AWKDGRYNTVCVIEDYDELVAYLLTRSQQHAEEQEKNLANMMKSATFESHFKSLVEVLELGSMISAGFDIIRPEKLPSEA
SQ  KEKRVLYSIPYNGEYCNALIDDNYNVTCWFGECVGNPEQLSKYSEKMLLGAYEFLLCSESLNVVIQAHLKEMVCPHHYDK
SQ  ELNFIGKIGETYYHNQMVSNIGSMQKWHRAILFGIGVLLGKEKEKTWYQVQVANVKQALYDMYTKEIRDWPMPIKVTCGI
SQ  VLAAIGGSAFWKVFQQLVGSGNGPVLMGVAAGAFSAEPQSRKPNRFDMQQYRYNNVPLKRRVWADAQMSLDQSSVAIMSK
SQ  CRANLVFGGTNLQIVMVPGRRFLACKHFFTHIKTKLRVEIVMDGRRYYHQFDPANIYDIPDSELVLYSHPSLEDVSHSCW
SQ  DLFCWDPDKELPSVFGADFLSCKYNKFGGFYEAQYADIKVRTKKECLTIQSGNYVNKVSRYLEYEAPTIPEDCGSLVIAH
SQ  IGGKHKIVGVHVAGIQGKIGCASLLPPLEPIAQAQGAEEYFDFLPAEENVSSGVAMVAGLKQGVYIPLPTKTALVETPSE
SQ  WHLDTPCDKVPSILVPTDPRIPAQHEGYDPAKSGVSKYSQPMSALDPELLGEVANDVLELWHDCAVDWDDFGEVSLEEAL
SQ  NGCEGVEYMERIPLATSEGFPHILSRNGKEKGKRRFVQGDDCVVSLIPGTTVAKAYEELEASAHRFVPALVGIECPKDEK
SQ  LPMRKVFDKPKTRCFTILPMEYNLVVRRKFLNFVRFIMANRHRLSCQVGINPYSMEWSRLAARMKEKGNDVLCCDYSSFD
SQ  GLLSKQVMDVIASMINELCGGEDQLKNARRNLLMACCSRLAICKNTVWRVECGIPSGFPMTVIVNSIFNEILIRYHYKKL
SQ  MREQQAPELMVQSFDKLIGLVTYGDDNLISVNAVVTPYFDGKKLKQSLAQGGVTITDGKDKTSLELPFRRLEECDFLKRT
SQ  FVQRSSTIWDAPEDKASLWSQLHYVNCNNCEKEVAYLTNVVNVLRELYMHSPREATEFRRKVLKKVSWITSGDLPTLAQL
SQ  QEFYEYQRQQGGADNNDTCDLLTSVDLLGPPLSFEKEAMHGCKVSEEIVTKNLAYYDFKRKGEDEVVFLFNTLYPQSSLP
SQ  DGCHSVTWSQGSGRGGLPTQSWMSYNISRKDSNINKIIRTAVSSKKRVIFCARDNMVPVNIVALLCAVRNKLMPTAVSNA
SQ  TLVKVMENAKAFKFLPEEFNFAFSDV
//
ID  P36312;
PN  RNA-directed RNA polymerase;
GN  POL1;
OS  31716;
SL  Nucleus Position: SL-0382;
SL  Comments: [Putative helicase]: Host membrane {ECO:0000250|UniProtKB:P03600}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03600}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}.
DR  UNIPROT: P36312;
DR  Pfam: PF00548;
DR  Pfam: PF00680;
DR  Pfam: PF00910;
DR  PROSITE: PS51874;
DR  PROSITE: PS50507;
DR  PROSITE: PS51218;
DE  Function: [Picornain 3C-like protease]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000250|UniProtKB:P03600}. [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral single-stranded RNA1 and RNA2 molecules. {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins. The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [Putative helicase]: The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000250|UniProtKB:P03600}.
DE  Reference Proteome: No;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0018144;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MKFFAGQTVMDVLQHVSSPTTNLRLLSYCNLKKEEDGKMMLAIKEQRHRRLLTLSYGAMCFQFSNSVGDEGIEVDDDELM
SQ  FEIFDALLRTKISNSKGMTHLYSWMRGVYLSTFKVEVQCDDYNSNLLEKDLAGEAQGLSQFVSGLADWIPSRVKTLAGYA
SQ  AEGIIEAFKKHFDKLLVEYCPMAVAACSWITTVWTTIKEWVQSAMDAMSWIMAGCTELISWGMCVIAGSCALSLLEKALV
SQ  AMGLISSSFDLAGIFVRSAVVGAFCLTVVNKRSRNCAELLQLVSLAVGAVSSATSSCFQSPVGQATDVSAESQSGGVEML
SQ  ESLAKNLTNFCDGTLVSIGKTCNAVNSINTAAGTIKNLVGRLLSMLSNFAYKLLGLESTFLRDASVVFSENVDGWLKQIS
SQ  WCQDQFLAKAYINQDELMVLRSLITRGEVMQREMIMGGMKVSPTVCGLINKGCTDLAKLMAGAVMHGTSGTRKIPFVVYA
SQ  HGASRVGKTMVINRLIEDFRKELELGEDCVYPRNVVDDYWSGYKRQPIVVIDDFGAVSSDPSAEAQLIPLISSAPYPLNM
SQ  ADLSEKGMHFDSAIVMCSSNFIECSPESKVRDEMAFRNRRHVLFTVSLDPNIPYDGDDITKNQIYEIKTWFHDSYHVEAT
SQ  FTSYGDLLAYCKNKWVEHNTEQEANLKQLGVKKESVAFQQFRSILDLAVFVNQDAENFKQRLETPDGRCHFVSCYDKSGI
SQ  LRHYTIDATGDVQEMEKVDSSLDDILLEKTNKMVLAAYKMIKYHKDTNLVIKTQLADLVDPTKYTADFQFDGVIGSPLFS
SQ  SQVMPSVKALPLWQRMVLYTVGQNLGRTHSSWYEGIKDKCMLALSKAYSTEIKDWPVALKIVVGVILATVAGKAFWRFYA
SQ  SMADAGNGGHFVGAVASAFAGSQAVVAQSRKPNRFDVAQYRYRNIPLRKRNWAEGQMSLDQSTMLIMEKCKANFVFSNIS
SQ  CQIVMLPGRQFLCYKHVFASLNSPMYVDIYTANKKYKLYYKPQNRVYFETDSEIMLYKDASLEDIPASCWDLFCFDAEKS
SQ  LPRGSFPAEILSCKLDRTTNQHIPEWADISARTVNQKLDVEFGEYQTIFYSYLQYDVSTKAEDCGSLIIATIDGRKKIIG
SQ  IHTAGRANRSGFASYMPQVEIPVQAQAAEKFFDFLEKEQHVTEGIGKVGNLKKGVWVPLPTKTNLVETPKEWHLGTEKTK
SQ  EPSILSSTDLRLGDKQYDPFVGGIQKYAEPMGILDDEVLRHVATDIVEEWFDCVDPQEDTFEEVDLQVAINGLEGMEYME
SQ  RVPMATSEGFPHILTRKSGEKGKGRFVYGDGEIFDLIPGTSVHEAYLTLEETCADTVPALVGIECPKDEKLPLRKIYEKP
SQ  KTRCFTVLPMEYNLVVRRKFLKFVVFIMKNRHRLSCQVGINPYGMEWSRLAMSLLEKGNNILCCDYSSFDGLLTKQVMHL
SQ  MSEMINELCGGSSRLKQQRTNLLMACCSRYALCKGEVWRVECGIPSGFPLTVICNSIFNELLVRYSYIKICQQARVPATI
SQ  TYGFSTFVKMVTYGDDNLLSVQSAITHVFDGTKLKEFLKLNGITITDGKDKTSPVLNFRNLEDCDFLKRGFKKESDVVWV
SQ  GPEEKESLWAQLHYVTTNNLEKHEAYLVNVVNVIRELYLHDPREAAELRRKAIQNVDFLKENPKDLPTMAAIKEFYNMQR
SQ  QQQFVDSNDNLDSLLNPDFLFVAPHRKMHEAEMELVPKWYLRDLGKAPINVLTGEADRICVLVNASIPDHLLPEKVVNIS
SQ  WPYGPGRGGLPTHGWAQANLYNPNSAVVKKLRTLVNQNPDDRVDICFRHDAVPVAIATIIFLVHLGKVKGRSANEYLTKI
SQ  IDSAKSLKFLPKECDIIF
//
ID  P35930;
PN  RNA-directed RNA polymerase;
GN  POL1;
OS  12262;
SL  Nucleus Position: SL-0382;
SL  Comments: [Putative helicase]: Host membrane {ECO:0000250|UniProtKB:P03600}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03600}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}.
DR  UNIPROT: P35930;
DR  UNIPROT: Q66182;
DR  Pfam: PF00548;
DR  Pfam: PF00680;
DR  Pfam: PF00910;
DR  PROSITE: PS51874;
DR  PROSITE: PS50507;
DR  PROSITE: PS51218;
DE  Function: [Picornain 3C-like protease]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000250|UniProtKB:P03600}. [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral single-stranded RNA1 and RNA2 molecules. {ECO:0000250|UniProtKB:P03600}. [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins. The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [Putative helicase]: The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}. [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000250|UniProtKB:P03600}.
DE  Reference Proteome: No;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0004197;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0018144;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MYMLTFEPGLCVAGIIRQVRSNPFMHVVQAYARTTETYREDIEMTKSMLKLKADEPLLVMSIVAAAMDFQTMVMAPIEME
SQ  ASEFLYGFYAERMSYIVTNRGMSELHEYIQLQCQRHLLVKVEIDGQYLVQEHEYEAQGFNIKRVKELITDVATWVPKKVK
SQ  GMIGWSVDAVLDSFQEYFYKVITERIPMAMKVCSWVATVWDQIKTWIEDAMTAMSSFLQGCNELLTWGLATLAACCALNV
SQ  LERILIFMEFLDESIDIAGIFLRTGVVAAACYHFSSTAKGFTEMMSVLSVATTAVAAVVCANYFGGSKTKKVNAQGNPVD
SQ  LLERIAAGLSSISQDSLVSLGKSCSAINSIATSYGHLRNFAGRVLTMLRDFAWKILGLETRFLADAALVFGEDVDGWLQR
SQ  ISALREAYVSKAYSSQDEVFEMNVLLERGYKMRHLMATGSRVSPAIGNMLMQGLADLERLHRNAAVQGVKGVRKIPFTVF
SQ  AHGNSRCGKSLLIGKLISDFQEHKGLGEDTVYSRNTTETHWSGYRRQPIVVIDDFAAVESDISAEAQLINLVSSTPYSVV
SQ  MAAIEEKGMTFDSQFIFASTNFLEVSPNGKIRCDDAFRNRRHVLIDVKLKPEVEYQSDDFTANQSYNILEHSHGRYNVVA
SQ  TFDNYEELLAYCLTKHEQHEAEQEANLAKLRRTNKFESHFKKFEQVLQLSTYFSSSIERIKREALATTDGADDYHLLYVV
SQ  PRNGSYLHVAANKDFQIQQWYGPVEEVAEEDILRASERMLLGAYEFLLLSTELNVVVKNHLPELICTDNYDHNLEFCGVV
SQ  GDPVYHQQLLKNIRALKPWHRAVLFGIGTLMGAKNPTPWYKRMWEGIKDVLYKAYSTEISQWPVPLKITCGIVLVGIVGA
SQ  GFWKTVSVLTNAGNGAGLVGAAVNSFSVVSTAEAQSRKPNRFEVQQYRYKNVPLTRRSWGNAQMSLDQSTVSILNKCHAK
SQ  FIIASQHAQIVLVPGRRFIGYSHFFCNLKHPLMVQIETADRTYFHRYQPENMEYIEDSELCVYHSSCLEDISHSCWDLFC
SQ  WDPDKELPKKFSADFVSCKYNTWTKSVEPTWANVDAEVIKEDFTICDGEYRNTVSTSIRYEAPTVMSDCGSMIITNVGGK
SQ  TKIVGIHVAGRDNKIGMASLLPPLLPCAQAQGAEKYFNFYPIEYDAAEGIARVGELKPKLYIPLPKKTSLVKTPEEWHLG
SQ  TPCDKVPSILVKGDPRLADTVHADYDPCLSGLTKYSTPMSPLDSVLLGETCQEILDEWFDCLPEGFELGEVTINEALNGV
SQ  DGVDYMDRIPLATSEGFPHVMSREQGEKGKQRFVQGDGHIVSLIPGTSVHEAYETLSRTIATEVPTLVGIECPKDEKLPF
SQ  RKVFTKPKTRNFTILPMEYNILVRQYFLNFVRFIMKKRDVLPCQVGINPYSMEWSIVASRLKSQGNDILCCDYSSFDGLL
SQ  SKQIMEMMADMINRFCGGGTLICAKRKNLLMACCSRLAISRDSVWRIECGIPSGFPLTVICNSIFNEILVRYHYKLLLQE
SQ  HNAPNMYVQSFKNLISMVTYGDDNLISVNAVVKPYFDGTKLKQAMARNGIIITDGKDKTSATLEFRRLEDCDFLKRGFLK
SQ  RSSVLWDAPEEKASLWAQLHYVNVNNCEMQVAYMTNLVNVLRELYMHDPTEMVEFRRLALKSIPWLNTTDLPTLYQVKEF
SQ  YAEQRLRNIPDHNDSLDMLTSVDLLGPAILGEGVPQEALVLSELLEVRDLRYHTVPDNDNGKEVWILFNTMYPQKLLPSN
SQ  CHSFTWNCGQGRGGLPTQHWLATNVTRTDSKLNKLIRTAVAANKKIVLATKDNILPINVIAVLLAARNKVMPSLATNALL
SQ  TYVIGAAKKLNFLTSECQFAFFNV
//
ID  Q91B85;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  172148;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q91B85;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
DE  Interaction: Q8N5G2; IntAct: EBI-11423711; Score: 0.37
DE  Interaction: Q7Z5R6; IntAct: EBI-11422597; Score: 0.37
DE  Interaction: O00327; IntAct: EBI-11422682; Score: 0.37
DE  Interaction: Q68CP9; IntAct: EBI-11422659; Score: 0.37
DE  Interaction: Q8IVT2; IntAct: EBI-11422779; Score: 0.37
DE  Interaction: Q9NWQ4; IntAct: EBI-11422771; Score: 0.37
DE  Interaction: O94983; IntAct: EBI-11422816; Score: 0.37
DE  Interaction: Q96EA4; IntAct: EBI-11422856; Score: 0.37
DE  Interaction: Q9BV73; IntAct: EBI-11422888; Score: 0.37
DE  Interaction: P55287; IntAct: EBI-11422872; Score: 0.37
DE  Interaction: Q5QJE6; IntAct: EBI-11422958; Score: 0.37
DE  Interaction: P06733; IntAct: EBI-11423030; Score: 0.37
DE  Interaction: Q14192; IntAct: EBI-11423090; Score: 0.37
DE  Interaction: P28799; IntAct: EBI-11423122; Score: 0.37
DE  Interaction: P31942; IntAct: EBI-11423154; Score: 0.37
DE  Interaction: P78504; IntAct: EBI-11423186; Score: 0.37
DE  Interaction: P55268; IntAct: EBI-11423228; Score: 0.37
DE  Interaction: Q99750; IntAct: EBI-11423276; Score: 0.37
DE  Interaction: Q96CN5; IntAct: EBI-11423252; Score: 0.37
DE  Interaction: Q9NS15; IntAct: EBI-11423260; Score: 0.37
DE  Interaction: Q9BV36; IntAct: EBI-11423300; Score: 0.37
DE  Interaction: P35579; IntAct: EBI-11423324; Score: 0.37
DE  Interaction: Q9BPW8; IntAct: EBI-11423372; Score: 0.37
DE  Interaction: Q8IXK0; IntAct: EBI-11423474; Score: 0.37
DE  Interaction: Q5VU43; IntAct: EBI-11423458; Score: 0.37
DE  Interaction: Q9Y6X2; IntAct: EBI-11423506; Score: 0.37
DE  Interaction: Q9H7J1; IntAct: EBI-11423530; Score: 0.37
DE  Interaction: Q02833; IntAct: EBI-11423570; Score: 0.37
DE  Interaction: Q9H814; IntAct: EBI-11423602; Score: 0.37
DE  Interaction: Q14160; IntAct: EBI-11423642; Score: 0.37
DE  Interaction: Q92804; IntAct: EBI-11423674; Score: 0.37
DE  Interaction: P19474; IntAct: EBI-11423783; Score: 0.37
DE  Interaction: O14530; IntAct: EBI-11423807; Score: 0.37
DE  Interaction: P08670; IntAct: EBI-11423823; Score: 0.37
DE  Interaction: Q13105; IntAct: EBI-11423863; Score: 0.37
DE  Interaction: Q9H270; IntAct: EBI-11423839; Score: 0.37
DE  Interaction: P52742; IntAct: EBI-11423887; Score: 0.37
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0046718;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKGAVLKGKGGGPPRRVPKETAKKTRQGPGRLPNGLVLMRMMGVLWHMIAGTARSPILKRFWATVPVRQAIAALRKIRK
SQ  TVGLLLDSLNRRRGKRRSTTGLLTSILLACLATLVISATIRRERTGDMVIRAEGKDAATQVEVVNGTCIILATDMGSWCD
SQ  DSIMYECVTIDSGEEPVDVDCFCRGVERVSLEYGRCGKPVGGRSRRSVSIPVHAHSDLTGRGHKWLRGDSVKTHLTRVEG
SQ  WVWKNKLLTMAFCAVVWMVTDSLPTRFIVITVALCLAPTYATRCTHLQNRDFVSGIQGTTRVSLVLELGGCVTLTAEGKP
SQ  SVDVWLDDIHQENPAKTREYCLHAKLASSKVVARCPAMGPATLPEEHQASTVCRRDQSDRGWGNHCGLFGKGSIVACAKF
SQ  ACEAKKKATGYVYDVNKITYVVKVEPHTGDYLAANESHSNRKTASFTTQSEKTILTLGDYGDISLTCRVTSGVDPAQTVV
SQ  LELDKTAEHLPKAWQVHRDWFEDLSLPWRHEGAHEWNHADRLVEFGEPHAVKMDIFNLGDQTGILLKSLAGVPVANIEGS
SQ  KYHLQSGHVTCDVGLEKLKMKGMTYTVCEGSKFAWKRPPTDSGHDTVVMEVTYTGSKPCRIPVRAVAHGEPNVNVASLIT
SQ  PNPSMETTGGGFVELQLPPGDNIIYVGELSHQWFQKGSTIGRVLEKTRRGIERLTVVGEHAWDFGSVGGVLSSVGKALHT
SQ  AFGAAFNTIFGGVGFLPRILLGVALAWLGLNSRNPTLSVGFLITGGLVLTMTLGVGADMGCAIDANRMELRCGEGLVVWR
SQ  EVTDWYDGYAFHPESPPVLAASLKEAYEEGVCGIVPQNRLEMAMWRRVEAVLNLALAESDANLTVVVDRRDPSDYRGGKV
SQ  GILKRSGKEMKTSWKGWSQSFVWSVPESPRRFMVGIEGTGECPLDKRRTGVFTVAEFGMGMRTKIFLDLRETSSSDCDTG
SQ  VMGAAVKSGHAVHTDQSLWMKSHRNATGVFISELIVTDLRNCTWPASHTLDNAGVVDSKLFLPVSLAGPRSHYNHIPGYA
SQ  EQVRGPWNQTPLRVVREPCPGTTVKIDQNCDKRGSSLRSTTESGKAIPEWCCRTCELPPVTFRSGTDCWYAMEIRPVHQQ
SQ  GGLVRSMVLADNGAMLSEGGVPGIVAVFVVLELVIRRRPTTGTSVVWCGVVVLGLVVTGLVTIEGLCRYVVAVGILMSME
SQ  LGPEIVALVLLQAVFDMRTGLLVAFAVKRAYTTREAVVTYFLLLVLELGFPEASLSNIWKWADSLAMGTLILQACSQEGR
SQ  ARVGYLLAAMMTQKDMAIIHTGLTIFLSAATAMAVWSMIKGQRDQKGLSWATPLVGLFGGEGVGLRLLAFRRLAERRNRR
SQ  SFSEPLTVVGVMLTVASGMVRHTSQEALCALVAGAFLLLMMVLGTRKMQLIAEWCGEVEWNPDLVNEGGEVNLKVRQDAM
SQ  GNLHLTEVEKEERAMALWLLAGLVASAFHWAGILIVLAIWTFFEMLSSGRRSELVFSGQGTRTERNRPFEIKDGAYRIYS
SQ  PGLLWGHRQIGVGYGAKGVLHTMWHVTRGAALVVEEAISGPYWADVREDVVCYGGAWSLESRWRGETVQVHAFPPGRPQE
SQ  THQCQPGELILENGRKLGAVPIDLSKGTSGSPIINAQGEVVGLYGNGLKTNEAYVSSIAQGEAEKSRPELPLSVQGTGWM
SQ  SKGQITVLDMHPGSGKTHRVLPELVRQCANRGMRTLVLAPTRVVLKEMEKALAGKKVRFHSPAVEGQSTAGAVVDVMCHA
SQ  TYVHRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSLAKENRCALVLMTATPPGRGDPFPESNGAIMSEERAIPDGE
SQ  WREGFDWITEYEGRTAWFVPSISKGGAIARTLRQRGKSVICLNSKTFEKDYLRVREEKPDFVVTTDISEMGANLDVSRVI
SQ  DGRTNIKPEEVDGKVEMTGTRKITTASAAQRRGRVGRTSGRTDEYIYSGQCDDDDTSLVQWKEAQILLDNITTLRGPVAT
SQ  FYGPEQMKMPEVAGHYRLNEEKRKHFRHLMTQCDFTPWLAWHVATNTSNVLDRSWTWQGPEGNAIDGADGDLVRFKTPGG
SQ  SERVLQPVWKDCRMFREGRDVKDFILYASGRRSVGDVLGGLAGVPGLLRHRCASALDVVYTLLNENPGSRAMRMAERDAP
SQ  EAFLTIVEVAVLGVATLGILWCFVARTSVSRMFLGTVVLFAALLLLWIGGVDYGYMAGIALIFYIFLTVLQPEPGKQRSS
SQ  DDNRLAYFLLGLLSLAGLVTANEMGMLDKTKADLAGLMWHGEQRHPAWEEWTNVDIQPARSWGTYVLIVSLFTPYMLHQL
SQ  QTKIQQLVNSSVASGAQAMRDLGGGTPFFGVAGHVIALGVTSLVGATPLSLGLGVALAAFHLAIVASGLEAELTQRAHRV
SQ  FFSAMVKNPMVDGDVINPFPDGEPKPVLYERRMSLILAIALCMVSVVLNRTAASMTEAGAVGLAALGQLVHPETETLWTM
SQ  PMACGMAGLVRGSFWGLLPMGHRLWLKTTGTRRGGADGETLGDIWKRRLNGCSREEFFQYRRSGVMETERDRARELLKRG
SQ  ETNMGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMGVKAYTIGGKGHEVPRLITSLGWNLIKFR
SQ  TGMDVYSLEAHRADTILCDIGESNPDPLVEGERSRRVILLMEKWKLRNPDASCVFKVLAPYRPEVLEALHRFQLQWGGGL
SQ  VRVPFSRNSTHEMYFSTAVSGNIVNSVNIQSRKLLARFGDQRGPAKVPEVDLGTGTRCVVLAEDKVREADVAERITALKT
SQ  QYGDSWHVDKEHPYRTWQYWGSYKTEATGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKEKVDTKAQEP
SQ  QVGTKIIMRAVNDWILERLAGKKTPRLCTREEFIAKVRSNAALGAWSDEQNRWSNAREAVEDPEFWRLVDEERERHLRGR
SQ  CAQCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRYLEFEALGFLNEDHWASRDLSGAGVEGISLNYLGWHLKRLSELE
SQ  GGLFYADDTAGWDTRITNADLEDEEQILRYLRGEHRTLAKTILEKAYHAKVVKVARPSSSGGCVMDIITRRDQRGSGQVV
SQ  TYALNTLTNIKVQLIRMMEGEGVIGPSDSQDPRLLRVEAWLKEYGEERLTRMLVSGDDCVVRPIDDRFGKALYFLNDMAK
SQ  VRKDIGEWEPSEGYSSWEEVPFCSHHFHELTMKDGRVIIVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSY
SQ  FHRRDLRTLGLAICSAVPIDWVPQGRTTWSIHASGAWMTTEDMLEVWNRVWILDNPFMSDKGKVKEWRDIPYLPKSQDGL
SQ  CSSLVGRRERAEWAKNIWGSVEKVRRMIGPERYADYLSCMDRHELHWDLKLESNII
//
ID  C8XPA8;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  38837;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: C8XPA8;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0046718;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVNPKGVNVMAARVKRAAQKTKKKAVQVSRGLRGFVLFVLTQLFMGRKLTPNVRRLWKSSDKNSLIHVLTKIKKIVGNLL
SQ  MGVSRRKKRRSATTSGTVFMAMLGLTLAASVARHAHHTLINITKDDAHKLLTLRNGNCTVVATDIGNWCPDNVEYDCVTL
SQ  QDNEDPDDVDCWCYRVNNVRVTYGRCKDGNTPRRSKRAVVITAHLDQGLTTKKETWLGSSHFETQVQKVEKWIIRNPTYA
SQ  IAAILMSWYIGNSLKQRVVLLLLTLALGPAYATHCVGIPKRDFVQGVQGTTWVNLVLEQGGCVTIMAEGKPSVDVWMDNI
SQ  KFTSPTLVRRISHTATISDTKIATACPSNGEAKLDEEHIKEYACKRLYSDRGWGNGCGLFGKGSLVACAKYESTGHMDVY
SQ  EMDMTKVEYTVKTQVHSGAKSGDLSGVKTVSFAPTSGSQPVEFSGYGNMGLQCMIQSNVDFSTHYLVVMGNDAWLVHKAW
SQ  VEDITLPWKHGEGGTWKDKQYMVEFGEPHATTVKVLALGPQEGALRNALAGAMIVTYESSGKTFKLHGGHVTCKATVSGL
SQ  ALKGTTYTNCRGGLSFVKTPTDTGHGTVVMQVKVAKSAPCRLTAIAADDASGHVNRGTLVTSNPIAASNNDEVMIEINPP
SQ  YGTSYLIVGVGDDKLVYQWKKSGSTIGSLFSETVKGAQRMAIVGSSSWDFSSTSGFFSSVGKAIHTVFGTAFHGIFGGLS
SQ  WMTRILIGVLLVWLGLNSRNGTATTLMMLTGFIILFLSLGVGAEVGCSVNWGQKELKCGDGIFVYNDVDDWMHKYKYHPE
SQ  DPKVMAGLIAKAWEKGACGLTSVSELEHVMWVKIASEINAILEENEIDLTVVVHENKSVYRRGSRRFPRVETELTYGWES
SQ  WGKNFITDGKVSNNTFHVDGKEDQCASKNRVWNSLEIEEFGFGVFHTNVFLRQKADKTNSCDTTLMGAAVKGNVAAHADP
SQ  GFWMESQENNGTWEIQSIEFTAYRECEWPVSHTVHGTQVMESDMFMPKGIGGPVSHLNRMQGYKVQTNGAWAYGKTVVQR
SQ  ELCPDTSVVVDSSCSDRGKSIRSTTTEGKVIKEWCCRSCTLPPVSYWTSEGCWYAMEVRPMKTPEKHLVRSWVTAGDSYP
SQ  AWSIGLVAMFLFVDIMARSRPTRKMMIGGTMLLLAIMIMGELSYLDLLRYIIVVGEHFIERENGGDVAYMAIMAASHLRP
SQ  GLMAMVFAKSMWSPKQRVLLALGCAILQPFLTAQASALVWEWADSIGLVLLIVQGMVRNKEKNWALVLLALCSPVSMPVI
SQ  RKASMIIGTGGLLLSLWKGGGSSMRKGLPLFAASAARVLGLTKAHLSVLFILLITKNGKRTWPISECLAAVGIFGAAFGT
SQ  MFSEDETLLGPLALVGVVLIVYTMFTQSDGLELVKAADISWSDEAVVSGEARRFDVALNDSGEFKLLDEPPVSWLNVSFL
SQ  VVAIVASSLHPIALVVTLVAWTYWRTEKRSGVLWDVPLAPKVEACEHLEDGVFRIIQKGLFGSSQVGIGVAKDGVFHTMW
SQ  HVTRGAFLMHSGKQLTPTWGSVRKDLVCYGGTWKLDGAWNGVDEVQLIAVPPGKPATNVQTKPGTFVLPTGDEAGAVLLD
SQ  FPSGTSGSPIIDRHGNILGLYGNGIVLENGAYASAISQAQPGSVAEVETPGLDKMLRKGEFTMLDYHPGAGKTRKHLPNI
SQ  LKECERKRLRTLVLAPTRVVLSEMKEALTSVQAKFHTQAFNSTTTGREIIDVMCHATFVHRMLEGLRSGNWEVIIMDEAH
SQ  FLDPTSIAARGWAHHKSKTKESAVIFMTATPPGTSNEFPESNAEIEDVKKEIPSEPWSKGHEWILEDRRPTVWFLPSIKA
SQ  ANVMAACLRKAERSVVVLNRSTFENVYPTIKTKKPDFILATDIAEMGANLPVERVIDCRTAYKPVLVDERVALKGPLRIA
SQ  AAAAAQRRGRVGRNPDRDGDTYVYSEDTCEQNDHLVCWTEGSMLLDNMQVKGGFVAPLYEEEASKTTMTPGECRLRDDQR
SQ  KVFRTLIRKHDMPVWLSWQVAKSGLAADDRKWCFDGEDDNAILGDNGEVIKARSPGGQRKELKPRWSDARIASDNTSLMN
SQ  FIAFAEGRRSLPLSILWSVPNQLSEKLVQSIDTLTILLRSEEGSRAHKLALQQAPEAVSTLLLLGMMAICTLGLVILLMK
SQ  PKATDKMSMAMVTMAITGYLLKLGGMTHAQVGGILLVFFIMMVVIIPESGTQRSINDNKLAYVIILVGLVIGGVACNELG
SQ  WLEKTKADLFGNNMTHAQTVVLPTINWNWLDFRPGAAWSLYVGMATFLTPVFVHWIKNEYGNASLTGITPTAGILGALNQ
SQ  GVPFVKLNTSVGVLLLSVWNNFTTSSMLAAMVMLACHCLFVLPGVRAQCLREAQIRVFHGVAKNPMVDGNPTVDLEKEND
SQ  MPDLYEKKLALVALGMAAVLNAAMVRTALTTAEMVVLGSAAVGPLLEGNTSAFWNGPLAVAVAGVMRGNHYALIGIVYNL
SQ  WLLKTARRGGSSALTYGEVWKRQLNLLGKQEFMNYKVSDILEVDRSHAREVLNSGNDAVGVAVSRGSSKLNWLIERGYLR
SQ  PTGRVVDLGCGRGGWSYTCAAERQVTSVKAYTLGKEGHEKPRLIQSLGWNIIKFKDKSDITRMTPHASDTLLCDIGESSS
SQ  NPEVEKERTLRVIEAVEKWMSPTTVSFCFKVLAPYKPDVIEALERFQLKHGGGIIRNPYSRNSTHEMYYVSGVRNNILHM
SQ  VNSTSRMLMRRMSRPSGRSTVVPDLIYPTGTRSVASEAGPLDLEKVKARINRLKEEQESTWFVDSDHPYRTWHYHGSYVA
SQ  KQSGTAASMINGVVKLLSGPWDRIEEVTNMAMTDTTPFGQQRVFKEKVDTRAPEPPQGTREIMKVVNQWLFDYLGRTKQP
SQ  RICTKEEFINKVRSHAALGGILTEQEGWSSAAEAVADPRFWSLVDKERQAHLEGRCETCIYNMMGKREKKPSEFGRAKGS
SQ  RAIWYMWLGARFLEFEALGFLNEDHWLGRENSKAGVEGIGLQYLGYVVEEVARKGNGLVYADDTAGWDTRITEADLEDEQ
SQ  YIMKRMSAEHRQLAWAVMELTYRNKVVKVPRPGPGGKILMDVISRRDQRGSGQVVTYPLNTATNMKVQLIRMAEAENVIT
SQ  RNDVEKVSLITLKELQLWLEVNGVNRLERMAVSGDDCIVAPVDESFAGALHHLNAMSKTRKDISEWENSRGWTDWESVPF
SQ  CSHHFHTLYLKDGRTIIAPCRCQDELIGRARISPGNGWMIKETAGLSKAYTQMWTLMYFHRRDLRLMANAICSAVPIDWV
SQ  PTGRTTWSIHATGEWMSSDDMLEVWNKVWIQDNPHVKDKTPIFAWRDVPYIQKGQDRACGSLVGTSLRASWAESIMTSVH
SQ  RVRMLIGNERYVNYMESMDRYATQRCSAYGELL
//
ID  Q32ZE0;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  64304;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q32ZE0;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARKPGRPGGNRVVNMLKRTAANAASPLGLAKRLLGDAFAGRGPLRVILAVVAFFRFTAIKMSPALLKKWGTVEKGAAIA
SQ  IMKSFKKEIGSMLDVVARRKTKNKGKRSVESSALLVLLTACLALGFKVVTGPEGPIMDVTKKDVGKALEIPFQNFNNTCW
SQ  VMAMDVGHPCEDTIEYECPSLDIGAEPNDIDCWCDTMPMRVRYGRCTKGSIPKRSRRNAVFPQHTENVLATRQETWMNTD
SQ  VIMKHLIKVETWALRNPGFALVAITLGWMLGSNRSQKIIFTILLLLVAPAYNMRCIGVENRDFVEGLSGGTWVDVVLEHG
SQ  GCVTVRVEGKPTLDFELVQTKATGLAAVRAYCYQAKVSDIQISAACPAVQLTENSKATDSNYLCRRGVTNRGWNNGCGLF
SQ  GKGDIHTCVKFKCEKKAAGFSIGKENLEYEVRASVHNSIGADKFSNELADGEPHTQKMKFSPLSPSAEKSFGDYGTLGMD
SQ  CEPQSGLDFGQLYLMTIESKSWLVNRDWYHDLHLPYTVGSGSQWNNREALVEFQEPHATKQEVLALGSQEGALHSALAGA
SQ  IMANRETSSPHALLLTAGHLKCRIKMDKMVIKGITYGQCSGTFKMEKHPADTGHGTVVLDVSYQGDDAPCKIPIVITSNL
SQ  AEVEPVGRLVSAHPVITAKNVRTMLEVEPPYGDSYIVIGVGDGRLKQHWFKKGSVIGGAFSTTMKGAKRLAVLGDAAWDF
SQ  GSVGGVFNSLGKAVHQLFGGIFRTLFGGMSWLSRLMIGALCLWIGINARDHSIAVTMLSVGGILIFLSINVSADTGCVVD
SQ  IERKELKCGSGIFIMNDIEAWRDEYAFHPSGPKALAASVVEAFSQGVCGVRSVNRLEHKMWESIADELNAILEENEREIT
SQ  IVVKDMENPAQKGKMRLRPVEKELKYGWKKWGASFFKRASRKNATFLVDGPSGEECPNSNRAWNSFFIEDFGFGVFKTSV
SQ  WLGLNEQMTEVCDTKMIGTGVKNDRAVHSDLGYWIESRKNLTWEISRARLIETKACIWPRSHTLWSDGIEETQLIIPKSL
SQ  GGPRSRHNMRSGYKTQINGPWDQIPLDIKFEECPGTSVTVTPNCGGRGPSARSTTASGKVIADWCCRDCILPPLTFRSGE
SQ  TCWYAMEIRPVSEREETLIRSKVSAGDGNEIDTFSLGLLVAMLVTQEGLRKRWATRHIMVASLTMLAAMVTGHITYRDLL
SQ  RYVVLLGATFAQINDGGDVMHLALVAVFKVQPGFLLGFLLRRRWTPRESMLLAISACFLHLVFSELSTDITTLAHNFSLA
SQ  LLILRAIIQTDVSSVTLPVLSMMAPSFQLSVLGTFRMAVAVYVIVNLMMSKRNDAVKKAAPSVVAAALGQFGMVNATAAL
SQ  GTLYVLEKHGKRSWPPSEIFSAVGVLCALVGALGNVQSTPLAGPMAACGLLIAAYVVTGKSTDIEIERAGLISWSEDAEV
SQ  SGSSPRVDVALDENGDFSLIDGQGPSLESVILKTALVAFSGLFPVSIPFCAAAWYLHGKSGRRAGALWDIPAPREVKKGS
SQ  TENGVYRILANRLFGKTQVGVGVMHEGVFHTMWHVTRGAALKSGEGRLDPYWGDVKKDLISYGGPWKLEGRWDGVSEVQL
SQ  IAVPPKEKAKNVQTTPGVFKTPHGEIGAIVLDFPAGSSGSPIINKLGEVIGLYGNGLMMGDAYASSIAQAEVEDEPDTPN
SQ  CLPPDVTHKKKLTVLDLHPGAGKTRKVLPKLLQEALEKRLRTVVLAPTRVVAAEMAEALKGMPIRYQTAAVTSSHSGNEI
SQ  IDLMCHATFTSRLMQPHRVPNYNLYIMDEAHFTDPASIAARGFIATKVSLGEAAAVFMTATPPGSDNPFPASNAPITDTE
SQ  AQIPDKAWSTGFDWITEYGGKTVWFVPSVRMGNEIAACLTKAKKKVIQLSRRTFNTEYPKCKQGDWDFVVTTDISEMGAN
SQ  FKATRVIDSRRAIKPSIMQDQEERVVLSGPTPISPASAAQRRGRVGRNPNQLGDEYVFSGLTQANDEGNACWTEARMLLD
SQ  NIHMQNGLIAQLYGPEQDKCFATDGEFKLREKERATFLEFLKADLPVWLSFKAASSGVQYHDRKWCFDGPDNNLVLEDNV
SQ  PVEIWTKSGERKKLKPRWSDARTYCDHGALTAFKEFAGGRRSVTTGLLEGVGRLPEHLGQRLKESIDTLYLAFTAEVGSR
SQ  PHREAMQEMPAALETVLVFFLLMIMTGCTFFLLMRHKGINKMGYGMVVMSAVGGLLWYGNVPAPKIAGILLLTFLLMVVL
SQ  IPNPEKQRSIQDNQLALVVLGCLMFLGGIAANEMGMLERTKQDLAGVFHKTERKSTEFTLLTPPDLRPATAWSIYAIGTT
SQ  LITPLIHHMITTHYANFSLMAMANQAGSLFGMQTGAPFSKMDWAVPAIVVGCWQQLTPATLMTALVLLAVHYIYMIPGWQ
SQ  AGAARAAQRRTAAGIMKNPVVDGLVVTDIPTLEEVDPLVEKKLGQYILLAVAIAAAVLRQDLQSWSECATLSAAAAATLW
SQ  EGSPGKIWNASTACSLVNIFRGHTLAAVPFMFTILRNTGNTGKRGGVEGETLGEKWKHLLNAMDKYEFSRYKVNGIFEVD
SQ  REPARMALANGLVTSGHAVSRGSAKLRWMVERAAVRPTGRVIDLGCGRGGWSYYCATLKQVQEVRGYTKGGPGHEEPRMV
SQ  QSYGWNIVTLKSGVDVFHRPAEVGDTILCDIGESSATPEVEEARTLKVLEMVEPWLKNKPEFCIKVLCPYRPKVIERLSA
SQ  LQRTYGGGLVRVPLSRNSTHEMYWTSGTAGNIINAVNLTSKVLLHRMEKKWIGPRYEKDVNLGSGTRAVIVKRKAPDMDK
SQ  IGNRVKRLKEEHIATWCYDDMNPYRTWNYHGSYEVKPTGSASSMINHVVKMLSKPWDTLNSVTSISMTDTTPFGQQRVFK
SQ  EKVDTKAPEPPTGVAEVMDIISDWTWRLLSRQKKPRLCTRDEFKAKVNNHAAMGSIFEEEHQWQTAKEAVEDPGFWALVD
SQ  REREAHLAGRCETCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWLSRENSYAGVEGLGLQRLG
SQ  YVLRDISRRPGGKMYADDTAGWDTRITEKDLDNEAKIIDQMEGEHKQLAKAIMELTYRHKVVKVMRPGPGGKTYMDIISR
SQ  EDQRGSGQVVTYALNTFTNMIVQLTRCAEAEGVLIPSMRERKLTPAEHRALLLWLDTEGVKRLKKMAISGDDCVVKGEDE
SQ  RFATALYFLNAMAKVRKDIQEWKPSSGWADWQEVPFCSHHFKELQLKDGRTIVVPCRHQDELVGRARVSPGAAWTVRESA
SQ  GLAKAYAQMWKLMYFHRRDLRLMANAICSAVPKDWVPTGRTTWSIHGKGEWMTNEDMLEVWNRVWIRENPHVEDKTEVAD
SQ  WKDVPYLGKREDQWCGSLIGSRTRATWAENIWVAVNQVRAKIGKEEYSDHLSSQQRFENWGEVRFSGVL
//
ID  P27912;
PN  Non-structural protein 1;
GN  POLG;
OS  11057;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
DR  UNIPROT: P27912;
DR  Pfam: PF01003;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF01570;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0046983;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKTGNPSFNMLKRARNRVSTGSQLAKRFSKGLLSGQGPMKLVMAFVAFLRFLAIPPTAGILKRWGSFKKNGAINV
SQ  LRGFRKEISNMLNIMNRRRRSVTMILMLLPTALAFHLTTRGGEPTLIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCE
SQ  DTMTYKCPRMTEAEPDDVDCWCNATDTWVTYGTCSQTGEHRRDKRSVALDPHVGLGLETRTETWMSSEGAWKQIQKVETW
SQ  ALRHPGFTVIGLFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKNKPT
SQ  LDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDTNFVCRRTFVDRGWGNGCGLFGKGSLITCAKFK
SQ  CVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTIATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNRVVLLT
SQ  MKKKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFA
SQ  GHLKCRLKMDKLTLKGVSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSSQDEKGVTQNGRLITANPIVID
SQ  KEKPVNIEAEPPFGESYIVVGAGEKALKLSWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLIHQIF
SQ  GTAYGVLFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGKELKCGS
//
ID  P27913;
PN  Non-structural protein 1;
GN  POLG;
OS  11058;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
DR  UNIPROT: P27913;
DR  Pfam: PF01003;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF01570;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0046983;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKTGRPSFNMLKRARNRVSTGSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWSSFKKNGAIKV
SQ  LRGFKKEISSMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPTLIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCE
SQ  DTMTYKCPRITERQPDDVDCWCNATDTWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETW
SQ  ALRHPGFTVIGLFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKNKPT
SQ  LDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDANFVCRRTFVDRGWGNGCGLFGKGSFLTCAKFK
SQ  CVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTIATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNRVVLLT
SQ  MKKKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFA
SQ  GHLKCRLKMDKLTLKGMSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSSQDEKGVTQNGRLITANPIVID
SQ  KEKPVNIEAEPPFGESYIVVGSGEKALKLSWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLIHQIF
SQ  GTAYGILFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGKELKCG
//
ID  P33478;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  33741;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P33478;
DR  PDB: 3L6P;
DR  PDB: 3LKW;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA c. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKTARPSFNMLKRARNRVSTGSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWGSFKKNGAIKV
SQ  LRGFKKEISNMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPHMIVSKQEREKSLLFKTSVGVNMCTLIAMDLGELCE
SQ  DTMTYKCPRITEAEPDDVDCWCNATDTWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQRVETW
SQ  ALRHPGFTVIALFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGSRDFVEGLSGATWVDVVLEHGSCVTTMAKDKPT
SQ  LDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDANFVCRRTFVDRGWGNGCGLFGKGSLLTCAKFK
SQ  CVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTIATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNEMVLLT
SQ  MKEKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFA
SQ  GHLKCRLKMDKLTLKGMSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSTQDEKGVTQNRLITANPIVTDK
SQ  EKPVNIETEPPFGESYIVVGAGEKALKQCWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLVHQVFG
SQ  TAYGVLFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGRELKCGSGIFVTNEVH
SQ  TWTEQYKFQADSPKRLSAAIGKAWEEGVCGIRSATRLENIMWKQISNELNHILLENDMKFTVVVGDVVGILAQGKKMIRP
SQ  QPMEHKYSWKSWGKAKIIGADIQNTTFIIDGPDTPECPDDQRAWNIWEVEDYGFGIFTTNIWLKLRDSYTQMCDHRLMSA
SQ  AIKDSKAVHADMGYWIESEKNETWKLARASFIEVKTCVWPKSHTLWSNGVLESEMIIPKIYGGPISQHNYRPGYFTQTAG
SQ  PWHLGKLELDFDLCEGTTVVVDEHCGNRGPSLRTTTVTGKIIHEWCCRSCTLPPLRFKGEDGCWYGMEIRPVKEKEENLV
SQ  KSMVSAGSGEVDSFSLGLLCISIMIEEVMRSRWSRKMLMTGTLAVFLLLIMGQLTWNDLIRLCIMVGANASDRMGMGTTY
SQ  LALMATFKMRPMFAVGLLFRRLTSREVLLLTIGLSLVASVELPNSLEELGDGLAMGIMILKLLTDFQSHQLWATLLSLTF
SQ  VKTTFSLHYAWKTMAMVLSIVSLFPLCLSTTSQKTTWLPVLLGSLGCKPLTMFLIAENKIWGRKSWPLNEGIMAVGIVSI
SQ  LLSSLLKNDVPLAGPLIAGGMLIACYVISGSSADLSLEKAAEVSWEEEAEHSGASHNILVEVQDDGTMKIKDEERDDTLT
SQ  ILLKATLLAVSGVYPLSIPATLFVWYFWQKKKQRSGVLWDTPSPPEVERAVLDDGIYRIMQRGLLGRSQVGVGVFQDGVF
SQ  HTMWHVTRGAVLMYQGKRLEPSWASVKKDLISYGGGWRFQGSWNTGEEVQVIAVEPGKNPKNVQTAPGTFKTPEGEVGAI
SQ  ALDFKPGTSGSPIVNREGKIVGLYGNGVVTTSGTYVSAIAQAKASQEGPLPEIEDEVFRKRNLTIMDLHPGSGKTRRYLP
SQ  AIVREAIRRNVRTLILAPTRVVASEMAEALKGMPIRYQTTAVKSEHTGKEIVDLMCHATFTMRLLSPVRVPNYNMIIMDE
SQ  AHFTDPASIARRGYISTRVGMGEAAAIFMTATPPGSVEAFPQSNAVIQDEERDIPERSWNSGYEWITDFPGKTVWFVPSI
SQ  KSGNDIANCLRKNGKRVIQLSRKTFDTEYQKTKNNDWDYVVTTDISEMGANFRADRVIDPRRCLKPVILKDGPERVILAG
SQ  PMPVTVASAAQRRGRIGRNQNKEGDQYVYMGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRL
SQ  RGEARKTFVELMRRGDLPVWLSYKVASEGFQYSDRRWCFDGERNNQVLEENMDVEMWTKEGERKKLRPRWLDARTYSDPL
SQ  ALREFKEFAAGRRSVSGDLILEIGKLPQHLTQRAQNALDNLVMLHNSEQGGRAYRHAMEELPDTIETLMLLALIAVLTGG
SQ  VTLFFLSGKGLGKTSIGLLCVMASSVLLWMASVEPHWIAASIILEFFLMVLLIPEPDRQRTPQDNQLAYVVIGLLFMILT
SQ  VAANEMGLLETTKKDLGIGHVAAENHHHATMLDVDLRPASAWTLYAVATTVITPMMRHTIENTTANISLTAIANQAAILM
SQ  GLDKGWPISKMDIGVPLLALGCYSQVNPLTLTAAVLMLVAHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIVAIDLD
SQ  PVVYDAKFEKQLGQIMLLILCTSQILLMRTTWALCESITLATGPLTTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLA
SQ  FSLMKSLGGGRRGTGAKGKHWERNGKDRLNQLSKSEFNTYKRSGIMEVDRSEAKEGLKRGETTKHAVSRGTAKLRWFVER
SQ  NLVKPEGKVIDLGCGRGGWSYYCAGLKKVTEVKGYTKGGPGHEEPIPMATYGWNLVKLYSGKDVFFTPPEKCDTLLCDIG
SQ  ESSPNPTIEEGRTLRVLKMVEPWLRGNQFCIKILNPYMPSVVETLEQMQRKHGGMLVRNPLSRNSTHEMYWVSCGTGNIV
SQ  SAVNMTSRMLLNRFTMAHRKPTYERDVDLGAGTRHVAVEPEVANLDIIGQRIENIKHEHKSTWHYDEDNPYKTWAYHGSY
SQ  EVKPSGSASSMVNGVVKLLTKPWDAIPMVTQIAMTDTTPFGQQRVFKEKVDTRTPKAKRGTAQIMEVTARWLWGFLSRNK
SQ  KPRICTREEFTRKVRSNAAIGAVFVDENQWNSAKEAVEDERFWDLVHRERELHKQGKCATCVYNMMGKREKKLGEFGKAK
SQ  GSRAIWYMWLGARFLEFEALGFMNEDHWFSRENSLSGVEGEGLHKLGYILRDISKIPGGNMYADDTAGWDTRITEDDLQN
SQ  EAKITDIMEPEHALLATSIFKLTYQNKVVRVQRPAKNGTVMDVISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMESEGIF
SQ  SPSELETPNLAERVLDWLEKYGVERLKRMAISGDDCVVKPIDDRFATALTALNDMGKVRKDIPQWEPSKGWNDWQQVPFC
SQ  SHHFHQLIMKDGREIVVPCRNQDELVGRARVSQGAGWSLRETACLGKSYAQMWQLMYFHRRDLRLAANAICSAVPVDWVP
SQ  TSRTTWSIHAHHQWMTTEDMLSVWNRVWIEENPWMEDKTHVSSWEDVPYLGKREDQWCGSLIGLTARATWATNIQVAINQ
SQ  VRRLIGNENYLDYMTSMKRFKNESDPEGALW
//
ID  P17763;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11059;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion. Host nucleus {ECO:0000269|PubMed:18420804}. Host cytoplasm {ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:19889084}. [Peptide pr]: Secreted {ECO:0000269|PubMed:19759134}. [Small envelope protein M]: Virion membrane {ECO:0000269|PubMed:9971841}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:9971841}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000269|PubMed:20181718}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:20181718}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000269|PubMed:10364366, ECO:0000269|PubMed:26655246}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000305}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:23408612}; Multi-pass membrane protein {ECO:0000269|PubMed:23408612}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000269|PubMed:26072288}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:17276984}; Multi-pass membrane protein {ECO:0000269|PubMed:17276984}. Host mitochondrion {ECO:0000269|PubMed:27252539}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000269|PubMed:17276984, ECO:0000269|PubMed:27252539}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:16436383}; Multi-pass membrane protein {ECO:0000269|PubMed:16436383}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:16699025}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000303|PubMed:28441781}.
DR  UNIPROT: P17763;
DR  UNIPROT: P27910;
DR  UNIPROT: P89313;
DR  UNIPROT: P89314;
DR  PDB: 3J8D;
DR  PDB: 3L6P;
DR  PDB: 3LKW;
DR  PDB: 4AL8;
DR  PDB: 4GSX;
DR  PDB: 4GT0;
DR  PDB: 4LCY;
DR  PDB: 4OIG;
DR  PDB: 5VIC;
DR  PDB: 5WJL;
DR  PDB: 5WKF;
DR  PDB: 7DWT;
DR  PDB: 7DWU;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle (PubMed:11893341). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions (PubMed:18420804, PubMed:21909430). Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed:23522008). {ECO:0000269|PubMed:11893341, ECO:0000269|PubMed:18420804, ECO:0000269|PubMed:21909430, ECO:0000269|PubMed:23522008}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000269|PubMed:18369148, ECO:0000269|PubMed:19759134}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release (PubMed:9971841). prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion (PubMed:21388812). {ECO:0000269|PubMed:18369148, ECO:0000269|PubMed:25326389, ECO:0000269|PubMed:9971841, ECO:0000303|PubMed:21388812}. [Small envelope protein M]: May play a role in virus budding (PubMed:25326389). Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M extodomain (PubMed:13679613). May display a viroporin activity (PubMed:16007501). {ECO:0000269|PubMed:13679613, ECO:0000269|PubMed:16007501, ECO:0000269|PubMed:25326389}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers (PubMed:18369148). prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion (PubMed:11893341). {ECO:0000269|PubMed:11893341, ECO:0000269|PubMed:18369148}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000269|PubMed:27416066}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000269|PubMed:25392211}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (PubMed:26728778). {ECO:0000255|PROSITE- ProRule:PRU00859, ECO:0000269|PubMed:26728778}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27252539}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000269|PubMed:17276984}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of a cellular antiviral state by blocking the IFN- alpha/beta pathway (PubMed:15956546). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15956546}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000269|PubMed:17267492, ECO:0000269|PubMed:19279106, ECO:0000269|PubMed:19850911}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9BRP8; IntAct: EBI-11687894; Score: 0.40
GO  GO:0039714;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0046762;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MNNQRKKTGRPSFNMLKRARNRVSTVSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWGSFKKNGAIKV
SQ  LRGFKKEISNMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPHMIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCE
SQ  DTMTYKCPRITETEPDDVDCWCNATETWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETW
SQ  ALRHPGFTVIALFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKDKPT
SQ  LDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDTNFVCRRTFVDRGWGNGCGLFGKGSLITCAKFK
SQ  CVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTTATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNEMVLLT
SQ  MEKKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFA
SQ  GHLKCRLKMDKLTLKGMSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSSQDEKGVTQNGRLITANPIVTD
SQ  KEKPVNIEAEPPFGESYIVVGAGEKALKLSWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLIHQIF
SQ  GTAYGVLFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGRELKCGSGIFVTNEV
SQ  HTWTEQYKFQADSPKRLSAAIGKAWEEGVCGIRSATRLENIMWKQISNELNHILLENDMKFTVVVGDVSGILAQGKKMIR
SQ  PQPMEHKYSWKSWGKAKIIGADVQNTTFIIDGPNTPECPDNQRAWNIWEVEDYGFGIFTTNIWLKLRDSYTQVCDHRLMS
SQ  AAIKDSKAVHADMGYWIESEKNETWKLARASFIEVKTCIWPKSHTLWSNGVLESEMIIPKIYGGPISQHNYRPGYFTQTA
SQ  GPWHLGKLELDFDLCEGTTVVVDEHCGNRGPSLRTTTVTGKTIHEWCCRSCTLPPLRFKGEDGCWYGMEIRPVKEKEENL
SQ  VKSMVSAGSGEVDSFSLGLLCISIMIEEVMRSRWSRKMLMTGTLAVFLLLTMGQLTWNDLIRLCIMVGANASDKMGMGTT
SQ  YLALMATFRMRPMFAVGLLFRRLTSREVLLLTVGLSLVASVELPNSLEELGDGLAMGIMMLKLLTDFQSHQLWATLLSLT
SQ  FVKTTFSLHYAWKTMAMILSIVSLFPLCLSTTSQKTTWLPVLLGSLGCKPLTMFLITENKIWGRKSWPLNEGIMAVGIVS
SQ  ILLSSLLKNDVPLAGPLIAGGMLIACYVISGSSADLSLEKAAEVSWEEEAEHSGASHNILVEVQDDGTMKIKDEERDDTL
SQ  TILLKATLLAISGVYPMSIPATLFVWYFWQKKKQRSGVLWDTPSPPEVERAVLDDGIYRILQRGLLGRSQVGVGVFQEGV
SQ  FHTMWHVTRGAVLMYQGKRLEPSWASVKKDLISYGGGWRFQGSWNAGEEVQVIAVEPGKNPKNVQTAPGTFKTPEGEVGA
SQ  IALDFKPGTSGSPIVNREGKIVGLYGNGVVTTSGTYVSAIAQAKASQEGPLPEIEDEVFRKRNLTIMDLHPGSGKTRRYL
SQ  PAIVREAIRRNVRTLVLAPTRVVASEMAEALKGMPIRYQTTAVKSEHTGKEIVDLMCHATFTMRLLSPVRVPNYNMIIMD
SQ  EAHFTDPASIAARGYISTRVGMGEAAAIFMTATPPGSVEAFPQSNAVIQDEERDIPERSWNSGYDWITDFPGKTVWFVPS
SQ  IKSGNDIANCLRKNGKRVVQLSRKTFDTEYQKTKNNDWDYVVTTDISEMGANFRADRVIDPRRCLKPVILKDGPERVILA
SQ  GPMPVTVASAAQRRGRIGRNQNKEGDQYIYMGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYR
SQ  LRGEARKTFVELMRRGDLPVWLSYKVASEGFQYSDRRWCFDGERNNQVLEENMDVEIWTKEGERKKLRPRWLDARTYSDP
SQ  LALREFKEFAAGRRSVSGDLILEIGKLPQHLTQRAQNALDNLVMLHNSEQGGKAYRHAMEELPDTIETLMLLALIAVLTG
SQ  GVTLFFLSGRGLGKTSIGLLCVIASSALLWMASVEPHWIAASIILEFFLMVLLIPEPDRQRTPQDNQLAYVVIGLLFMIL
SQ  TAAANEMGLLETTKKDLGIGHAAAENHHHAAMLDVDLHPASAWTLYAVATTIITPMMRHTIENTTANISLTAIANQAAIL
SQ  MGLDKGWPISKMDIGVPLLALGCYSQVNPLTLTAAVFMLVAHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIVAIDL
SQ  DPVVYDAKFEKQLGQIMLLILCTSQILLMRTTWALCESITLATGPLTTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGL
SQ  AFSLMKSLGGGRRGTGAQGETLGEKWKRQLNQLSKSEFNTYKRSGIIEVDRSEAKEGLKRGEPTKHAVSRGTAKLRWFVE
SQ  RNLVKPEGKVIDLGCGRGGWSYYCAGLKKVTEVKGYTKGGPGHEEPIPMATYGWNLVKLYSGKDVFFTPPEKCDTLLCDI
SQ  GESSPNPTIEEGRTLRVLKMVEPWLRGNQFCIKILNPYMPSVVETLEQMQRKHGGMLVRNPLSRNSTHEMYWVSCGTGNI
SQ  VSAVNMTSRMLLNRFTMAHRKPTYERDVDLGAGTRHVAVEPEVANLDIIGQRIENIKNGHKSTWHYDEDNPYKTWAYHGS
SQ  YEVKPSGSASSMVNGVVRLLTKPWDVIPMVTQIAMTDTTPFGQQRVFKEKVDTRTPKAKRGTAQIMEVTARWLWGFLSRN
SQ  KKPRICTREEFTRKVRSNAAIGAVFVDENQWNSAKEAVEDERFWDLVHRERELHKQGKCATCVYNMMGKREKKLGEFGKA
SQ  KGSRAIWYMWLGARFLEFEALGFMNEDHWFSRENSLSGVEGEGLHKLGYILRDISKIPGGNMYADDTAGWDTRITEDDLQ
SQ  NEAKITDIMEPEHALLATSIFKLTYQNKVVRVQRPAKNGTVMDVISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMESEGI
SQ  FSPSELETPNLAERVLDWLKKHGTERLKRMAISGDDCVVKPIDDRFATALTALNDMGKVRKDIPQWEPSKGWNDWQQVPF
SQ  CSHHFHQLIMKDGREIVVPCRNQDELVGRARVSQGAGWSLRETACLGKSYAQMWQLMYFHRRDLRLAANAICSAVPVDWV
SQ  PTSRTTWSIHAHHQWMTTEDMLSVWNRVWIEENPWMEDKTHVSSWEDVPYLGKREDRWCGSLIGLTARATWATNIQVAIN
SQ  QVRRLIGNENYLDFMTSMKRFKNESDPEGALW
//
ID  P29990;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  31634;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:19889084}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Host nucleus {ECO:0000269|PubMed:16699025}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:30550790}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17763}; Cytoplasmic side {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000269|PubMed:16699025, ECO:0000269|PubMed:30550790}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P29990;
DR  PDB: 2R69;
DR  PDB: 4O6B;
DR  PDB: 6WER;
DR  PDB: 6ZQU;
DR  PDB: 7K93;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed:23522008). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:23522008}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes (PubMed:19272179). Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM (By similarity). They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E (By similarity). The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers (By similarity). prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease (By similarity). Mediates complement activation, which may contribute to the pathogenesis of the vascular leakage that occurs in severe dengue disease (PubMed:16544248). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:16544248}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000269|PubMed:15956546}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway (PubMed:15956546). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15956546}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed:19850911). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:15944325). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:19754307). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (PubMed:30550790). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:15944325, ECO:0000269|PubMed:19754307, ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:30550790}.
DE  Reference Proteome: No;
DE  Interaction: P00974; IntAct: EBI-9520307; Score: 0.70
DE  Interaction: P29990; IntAct: EBI-9542338; Score: 0.44
DE  Interaction: Q99653; IntAct: EBI-20639119; Score: 0.35
DE  Interaction: P35613; IntAct: EBI-20639119; Score: 0.35
DE  Interaction: O43251; IntAct: EBI-20639119; Score: 0.35
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0140272;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039653;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNDQRKKAKNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLYMALVAFLRFLTIPPTAGILKRWGTIKKSKAINV
SQ  LRGFRKEIGRMLNILNRRRRSAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCE
SQ  DTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCTTMGEHRRQKRSVALVPHVGMGLETRTETWMSSEGAWKHVQRIETW
SQ  ILRHPGFTMMAAILAYTIGTTHFQRALIFILLTAVTPSMTMRCIGMSNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT
SQ  LDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFR
SQ  CKKNMEGKVVQPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSTTEAELTGYGTVTMECSPRTGLDFNEMVLLQ
SQ  MENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFT
SQ  GHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTE
SQ  KDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVF
SQ  GAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVTLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFITDNV
SQ  HTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITPELNHILSENEVKLTIMTGDIKGIMQAGKRSLR
SQ  PQPTELKYSWKTWGKAKMLSTESHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLKEKQDVFCDSKLMS
SQ  AAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKNCHWPKSHTLWSNGVLESEMIIPKNLAGPVSQHNYRPGYHTQIT
SQ  GPWHLGKLEMDFDFCDGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENL
SQ  VNSLVTAGHGQVDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLIIGNMSFRDLGRVMVMVGATMTDDIGMGVT
SQ  YLALLAAFKVRPTFAAGLLLRKLTSKALMMTTIGIVLSSQSTTPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAIL
SQ  CVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKTDWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVS
SQ  ILASSLLKNDIPMTGPLVAGGPLTVCYVLTGRSADLELERAADVKWEDQAEISGSSPILSITISEDGSMSIKNEEEEQTL
SQ  TILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPMGKAELEDGAYRIKQKGILGYSQIGAGVYKEGT
SQ  FHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFKTNAGTIGA
SQ  VSLDFSPGTSGSPIIDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLP
SQ  AIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDE
SQ  AHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIIDEEREIPERSWNSGHEWVTDFKGKTVWFVPSI
SQ  KAGNDIAACLSKNGKKVIQLSRKTFDSEYAKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAG
SQ  PMPVTHSSAAQRRGRIGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRL
SQ  RGEARTTFVDLMRRGDLPVWLAYRVAAEGINYADRRWCFDGVKNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPL
SQ  ALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGG
SQ  ILLFLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAA
SQ  TMANEMGFLEKTKKDLGLGSIATQQPESNILDIDLRPASAWTLYAVATTFVTPMLRHSIENSSVNVSLTAIANQATVLMG
SQ  LGKGWPLSKMDIGVPLLAIGCYSQVNPTTLTAALFLLVAHYAIIGPALQAKASREAQKRAAAGIMKNPTVDGITVIDLDP
SQ  IPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEVLTLATGPISTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLF
SQ  SIMKNTTNARRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERN
SQ  MVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFIPPEKCDTLLCDIGE
SQ  SSPNPTVEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMEALQRKYGGALVRNPLSRNSTHEMYWVSNASGNIV
SQ  SSVNMISRMLINRFTMRYKKATYEPDVDLGSGTRNIGIESEIPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSY
SQ  ETKQTGSASSMVNGVFRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKK
SQ  TPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNIMGKREKKLGEFGKAK
SQ  GSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKN
SQ  EAMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVF
SQ  KSIQHLTITEEIAVQNWLARVGRERLSRMAISGDDCVVKPLDDRLPSALTALNDTGKIRKDIQQWEPSRGWNDWTQVPFC
SQ  SHHFHELIMKDGRVLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYDQMWSLMYFHRRDLRLAANAICSAVPSHWVP
SQ  TSRTTWSIHAKHEWMTTEDMLTVWNRVWIQENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQAAINQ
SQ  VRSLIGNEEYTDYMPSMKRFRREEEEAGVLW
//
ID  P29991;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  31635;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P29991;
DR  PDB: 2R29;
DR  PDB: 3EVG;
DR  PDB: 6FLA;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (PubMed:29902443). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:29902443}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.
DE  Reference Proteome: No;
DE  Interaction: P12036; IntAct: EBI-6158234; Score: 0.35
DE  Interaction: P52630; IntAct: EBI-8828360; Score: 0.37
DE  Interaction: P34931; IntAct: EBI-6158234; Score: 0.35
DE  Interaction: P17844; IntAct: EBI-8826490; Score: 0.49
DE  Interaction: Q969X0; IntAct: EBI-8826506; Score: 0.49
DE  Interaction: Q9ULJ7; IntAct: EBI-8826522; Score: 0.49
DE  Interaction: Q8IUD2; IntAct: EBI-8826538; Score: 0.49
DE  Interaction: P27797; IntAct: EBI-8826570; Score: 0.49
DE  Interaction: P61201; IntAct: EBI-8826586; Score: 0.49
DE  Interaction: Q99996; IntAct: EBI-8826554; Score: 0.49
DE  Interaction: Q92564; IntAct: EBI-8826634; Score: 0.49
DE  Interaction: P04114; IntAct: EBI-8826602; Score: 0.49
DE  Interaction: Q9Y6B2; IntAct: EBI-8826618; Score: 0.49
DE  Interaction: P49327; IntAct: EBI-8829477; Score: 0.37
DE  Interaction: Q8IWT0; IntAct: EBI-8829493; Score: 0.49
DE  Interaction: O75592; IntAct: EBI-8829509; Score: 0.49
DE  Interaction: P0C0L4; IntAct: EBI-8826672; Score: 0.37
DE  Interaction: Q8IX03; IntAct: EBI-8826686; Score: 0.37
DE  Interaction: O14972; IntAct: EBI-8826658; Score: 0.37
DE  Interaction: Q14999; IntAct: EBI-8826732; Score: 0.37
DE  Interaction: P02671; IntAct: EBI-8826718; Score: 0.37
DE  Interaction: Q13561; IntAct: EBI-8826794; Score: 0.37
DE  Interaction: P14543; IntAct: EBI-8826809; Score: 0.37
DE  Interaction: P78344; IntAct: EBI-8826854; Score: 0.37
DE  Interaction: Q96NL6; IntAct: EBI-8826914; Score: 0.37
DE  Interaction: P0C7X2; IntAct: EBI-8826929; Score: 0.37
DE  Interaction: Q6FHW4; IntAct: EBI-8826944; Score: 0.37
DE  Interaction: P01042; IntAct: EBI-8826993; Score: 0.37
DE  Interaction: Q9NX95; IntAct: EBI-8827023; Score: 0.37
DE  Interaction: O00584; IntAct: EBI-8827008; Score: 0.37
DE  Interaction: P02751; IntAct: EBI-8827038; Score: 0.37
DE  Interaction: A5YKK6; IntAct: EBI-8827053; Score: 0.37
DE  Interaction: P07942; IntAct: EBI-8827115; Score: 0.37
DE  Interaction: Q9H074; IntAct: EBI-8827100; Score: 0.37
DE  Interaction: P02774; IntAct: EBI-8827160; Score: 0.37
DE  Interaction: O60333; IntAct: EBI-8827145; Score: 0.37
DE  Interaction: Q9UQ90; IntAct: EBI-8827175; Score: 0.37
DE  Interaction: P02647; IntAct: EBI-8827190; Score: 0.37
DE  Interaction: O95154; IntAct: EBI-8827205; Score: 0.37
DE  Interaction: Q14692; IntAct: EBI-8827280; Score: 0.37
DE  Interaction: Q9H6D7; IntAct: EBI-8827340; Score: 0.37
DE  Interaction: O15020; IntAct: EBI-8827355; Score: 0.37
DE  Interaction: O00505; IntAct: EBI-8827370; Score: 0.37
DE  Interaction: O15117; IntAct: EBI-8827385; Score: 0.37
DE  Interaction: Q14980; IntAct: EBI-8827475; Score: 0.37
DE  Interaction: A6NCC3; IntAct: EBI-8827496; Score: 0.37
DE  Interaction: Q92667; IntAct: EBI-8827590; Score: 0.37
DE  Interaction: Q9BWH2; IntAct: EBI-8827575; Score: 0.37
DE  Interaction: Q86VP1; IntAct: EBI-8827620; Score: 0.37
DE  Interaction: Q8NEF9; IntAct: EBI-8827650; Score: 0.37
DE  Interaction: Q15154; IntAct: EBI-8827665; Score: 0.37
DE  Interaction: Q9BVG3; IntAct: EBI-8827695; Score: 0.37
DE  Interaction: O14763; IntAct: EBI-8827710; Score: 0.37
DE  Interaction: Q15643; IntAct: EBI-8827740; Score: 0.37
DE  Interaction: P05546; IntAct: EBI-8827785; Score: 0.37
DE  Interaction: Q8IVP5; IntAct: EBI-8827770; Score: 0.37
DE  Interaction: Q99715; IntAct: EBI-8827830; Score: 0.37
DE  Interaction: O95232; IntAct: EBI-8827860; Score: 0.37
DE  Interaction: O94979; IntAct: EBI-8827875; Score: 0.37
DE  Interaction: Q0VF96; IntAct: EBI-8827890; Score: 0.37
DE  Interaction: Q99614; IntAct: EBI-8827920; Score: 0.37
DE  Interaction: O75521; IntAct: EBI-8827905; Score: 0.37
DE  Interaction: O75925; IntAct: EBI-8827935; Score: 0.37
DE  Interaction: A6NI86; IntAct: EBI-8828025; Score: 0.37
DE  Interaction: Q9P219; IntAct: EBI-8828073; Score: 0.37
DE  Interaction: Q08379; IntAct: EBI-8828118; Score: 0.37
DE  Interaction: P68543; IntAct: EBI-8828180; Score: 0.37
DE  Interaction: P05787; IntAct: EBI-8828165; Score: 0.37
DE  Interaction: P63279; IntAct: EBI-8828210; Score: 0.37
DE  Interaction: Q05519; IntAct: EBI-8828255; Score: 0.37
DE  Interaction: Q9ULX6; IntAct: EBI-8828285; Score: 0.37
DE  Interaction: Q9UKX7; IntAct: EBI-8828330; Score: 0.37
DE  Interaction: Q7Z406; IntAct: EBI-8828375; Score: 0.37
DE  Interaction: Q13625; IntAct: EBI-8828390; Score: 0.37
DE  Interaction: P30041; IntAct: EBI-8828405; Score: 0.37
DE  Interaction: Q03001; IntAct: EBI-8828450; Score: 0.37
DE  Interaction: Q8WXH0; IntAct: EBI-8828465; Score: 0.37
DE  Interaction: O95613; IntAct: EBI-8828480; Score: 0.37
DE  Interaction: P04040; IntAct: EBI-8828495; Score: 0.37
DE  Interaction: Q14789; IntAct: EBI-8828510; Score: 0.37
DE  Interaction: P02675; IntAct: EBI-8828525; Score: 0.37
DE  Interaction: A2RUB6; IntAct: EBI-8828555; Score: 0.37
DE  Interaction: P00558; IntAct: EBI-8828570; Score: 0.37
DE  Interaction: A8MPP1; IntAct: EBI-8828585; Score: 0.37
DE  Interaction: Q53SF7; IntAct: EBI-8828630; Score: 0.37
DE  Interaction: Q8WUM4; IntAct: EBI-8828645; Score: 0.37
DE  Interaction: Q9NYJ8; IntAct: EBI-8828705; Score: 0.37
DE  Interaction: P43243; IntAct: EBI-8828780; Score: 0.37
DE  Interaction: Q9Y6C2; IntAct: EBI-8828795; Score: 0.37
DE  Interaction: Q9UJC3; IntAct: EBI-8828825; Score: 0.37
DE  Interaction: Q5JTC6; IntAct: EBI-8828840; Score: 0.37
DE  Interaction: Q13813; IntAct: EBI-8828915; Score: 0.37
DE  Interaction: Q9BZF9; IntAct: EBI-8828930; Score: 0.37
DE  Interaction: P26599; IntAct: EBI-8828960; Score: 0.37
DE  Interaction: P35222; IntAct: EBI-8829095; Score: 0.37
DE  Interaction: Q14203; IntAct: EBI-8829140; Score: 0.37
DE  Interaction: Q9P0K7; IntAct: EBI-8829155; Score: 0.37
DE  Interaction: Q8NEZ2; IntAct: EBI-8829200; Score: 0.37
DE  Interaction: Q66GS9; IntAct: EBI-8829215; Score: 0.37
DE  Interaction: Q13137; IntAct: EBI-8829245; Score: 0.37
DE  Interaction: Q86SQ7; IntAct: EBI-8829327; Score: 0.37
DE  Interaction: Q8NF91; IntAct: EBI-8829342; Score: 0.37
DE  Interaction: Q8N302; IntAct: EBI-8829372; Score: 0.37
DE  Interaction: O00571; IntAct: EBI-8829387; Score: 0.37
DE  Interaction: Q86UP2; IntAct: EBI-8829417; Score: 0.37
DE  Interaction: P51648; IntAct: EBI-8829447; Score: 0.37
DE  Interaction: Q99460; IntAct: EBI-8829432; Score: 0.37
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNDQRKEAKNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLYMALVAFLRFLTIPPTAGILKRWGTIKKSKAINV
SQ  LRGFRKEIGRMLNILNRRRRSAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEVGVNMCTLMAMDLGELCE
SQ  DTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCTTMGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHVQRIETW
SQ  ILRHPGFTMMAAILAYTIGTTHFQRALILILLTAVTPSMTMRCIGMSNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT
SQ  LDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFR
SQ  CKKNMEGKVVQPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSITEAELTGYGTITMECSPRTGLDFNEIVLLQ
SQ  MENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFT
SQ  GHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTE
SQ  KDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVF
SQ  GAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVTLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFITDNV
SQ  HTWTEQYKFQPESPSKLASAIQKAHEEDICGIRSVTRLENLMWKQITPELNHILSENEVKLTIMTGDIKGIMQAGKRSLR
SQ  PQPTELKYSWKTWGKAKMLSTESHNQTFFIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLKEKQDVFCDSKLMS
SQ  AAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKNCHWPKSHTLWSNGVLESEMIIPKNLAGPVSKHNYRPGYHTQIT
SQ  GPWHLGKLEMDFDFCDGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENL
SQ  VNSLVTAGHGQVDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLIIGNRSFRDLGRVMVMVGATMTDDIGMGVT
SQ  YLALLAAFKVRPTFAAGLLLRKLTSKELMMTTIGIVLSSQSTIPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAIL
SQ  CVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKTDWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVS
SQ  ILASSLLKNDIPMTGPLVAGGLLTVCYVLTGRSADLELERAADVKWEDQAEISGSSPILSITISEDGSMSIKNEEEEQTL
SQ  TILIRRGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPMGKAELEDGAYRIKQKGILGYSQIGAGVYKEGT
SQ  FHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALDPGKNPRAVQTKPGLFKTNAGTIGA
SQ  VSLDFSPGTSGSPIIDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLP
SQ  AIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDE
SQ  AHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIIDEEREIPERSWNSGHEWVTDFKGKTVWFVPSI
SQ  KAGNDIAACLRKNGKKVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAG
SQ  PMPVTHSSAAQRRGRIGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRL
SQ  RGEARTTFVDLMRRGDLPVWLAYRVAAEGINYADRRWCFDGVKNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPL
SQ  ALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARNALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGG
SQ  IFLFLMSARGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAA
SQ  TMANEMGFLEKTKKDLGLGSIATQQPESNILDIDLRPASAWTLYAVATTFVTPMLRHSIENSSVNVSLTAIANQATVLMG
SQ  LGKGWPLSKMDIGVPLLAIGCYSQVNPTTLTAALFLLVAHYAIIGPALQAKASREAQKRAAAGIMKNPTVDGITVIDLDP
SQ  IPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEALTLATGPISTLSEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLF
SQ  SIMKNTTNTRRVTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERN
SQ  MVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFIPPEKCDTLLCDIGE
SQ  SSPNPTVEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMEALQRKYGGALVRNPLSRNSTHEMYWVSNASGNIV
SQ  SSVNMISRMLINRFTMRYKKATYEPDVDLGSGTRNIGIESEIPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSY
SQ  ETKQTGSASSMVNGVFRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKK
SQ  TPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNIMGKREKKLGEFGKAK
SQ  GSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKN
SQ  EEMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVF
SQ  KSIQHLTITEEIAVQNWLARVGRERLSRMAISGDDCVVKPLDDRLPSALTALNDMGKIRKDIQQWEPSRGWNDWTQVPFC
SQ  SHHFHELIMKDGRVLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQMWSLMYFHRRDLRLAANAICSAVPSHWVP
SQ  TSRTTWSIHAKHEWMTTEDMLTVWNRVWIQENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQAAINQ
SQ  VRSLIGNEEYTDYMPSMKRFRREEEEAGVLW
//
ID  P14337;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  413041;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P14337;
DR  UNIPROT: Q20II6;
DR  PDB: 1P58;
DR  PDB: 2M9P;
DR  PDB: 2M9Q;
DR  PDB: 3C6D;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKAKNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINV
SQ  LRGFRKEIGRMLNILNRRRRSAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCE
SQ  DTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETW
SQ  ILRHPGFTIMAAILAYTIGTTHFQRALIFILLTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT
SQ  LDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFT
SQ  CKKNMEGKIVQPENLEYTIVVTPHSGEEHAVGNDTGKHGKEIKVTPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQ
SQ  MENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFT
SQ  GHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTE
SQ  KDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVF
SQ  GAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFITDNV
SQ  HTWTEQYKFQPESPSKLASAIQKAQEEGICGIRSVTRLENLMWKQITPELNHILAENEVKLTIMTGDIKGIMQAGKRSLR
SQ  PQPTELKYSWKTWGKAKMLSTESHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLKEKQDAFCDSKLMS
SQ  AAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKNCHWPKSHTLWSNGVLESEMIIPKNLAGPVSQHNYRPGYHTQIA
SQ  GPWHLGKLEMDFDFCDGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENL
SQ  VNSLVTAGHGQVDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFKDLGRVVVMVGATMTDDIGMGVT
SQ  YLALLAAFKVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSTIPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAIL
SQ  CVPNAVILQNAWKVSCTILAVVSVSPLLLTSSQQKTDWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVS
SQ  ILASSLLKNDIPMTGPLVAGGLLTVCYVLTGRSADLELERAADVKWEDQAEISGSSPILSITISEDGSMSIKNEEEEQTL
SQ  TILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPMGKAELEDGAYRIKQKGILGYSQIGAGVYKEGT
SQ  FHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFKTNAGTIGA
SQ  VSLDFSPGTSGSPIIDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLP
SQ  AIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDE
SQ  AHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIIDEEREIPERSWNSGHEWVTDFKGKTVWFVPSI
SQ  KAGNDIAACLRKNGKKVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAG
SQ  PMPVTHSSAAQRRGRIGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRL
SQ  RGEARKTFVDLMRRGDLPVWLAYKVAAEGINYADRRWCFDGIKNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPL
SQ  ALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKTRDALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGG
SQ  IFLFLMSGRGIGKMTLGMCCIITASVLLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAA
SQ  TMANEMGFLEKTKKDLGLGSIATQQPESNILDIDLRPASAWTLYAVATTFVTPMLRHSIENSSVNVSLTAIANQATVLMG
SQ  LGKGWPLSKMDIGVPLLAIGCYSQVNPITLTAALLLLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDP
SQ  IPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEALTLATGPISTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLF
SQ  SIMKNTTNTRRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERN
SQ  MVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFIPPEKCDTLLCDIGE
SQ  SSPSPTVEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMETLQRKYGGALVRNPLSRNSTHEMYWVSNASGNIV
SQ  SSVNMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESEIPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSY
SQ  ETKQTGSASSMVNGVVRLLTKPWDVLPTVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKK
SQ  TPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNMMGKREKKLGEFGKAK
SQ  GSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKN
SQ  EEMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVF
SQ  KNIQHLTVTEEIAVQNWLARVGRERLSRMAISGDDCVVKPLDDRFASALTALNDMGKIRKDIQQWEPSRGWNDWTQVPFC
SQ  SHHFHELIMKDGRVLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQMWSLMYFHRRDLRLAANAICSAVPSHWVP
SQ  TSRTTWSIHAKHEWMTTEDMLTVWNRVWIQENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQAAINQ
SQ  VRSLIGNEEYTDYMPSMKRFRREEEEAGVLW
//
ID  P30026;
PN  Non-structural protein 1;
GN  POLG;
OS  31636;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
DR  UNIPROT: P30026;
DR  UNIPROT: Q66450;
DR  Pfam: PF01003;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01570;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0046983;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKARSTPFNMLRRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVALPRFLTIPPTAGILKRWGTIKKSKAIND
SQ  VRGCRKEIGRMLNILNRRRRTAGVIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAIDFGELCE
SQ  DTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTRTTTGEHGREKRSVALVPHVGMGLETGTETWMSSDGAWKRACRMETW
SQ  ILRHPGFTIMAAILAYTIGTTHFQRGLILILQTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT
SQ  LDFELIKTEATQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFT
SQ  CKKNMEGNIVQPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSITEAELTGYGTVTMECSPRTGLDFNEIVLLQ
SQ  MEDKAWLVHRQWFLDLPLPWLPGADTQGSNRIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFT
SQ  GHLKCRLRMDKLQLKGMSYSMCTGKFQIVKEIAETQHGTIVIRVQYEGDGSPCKIPLEIMDLEKRHVLGRLITVNPIVTE
SQ  KDSPVNIEAEPPFGDSYIIIGVEPGQLKLHWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVF
SQ  GAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGVITLYLGAMVQADSGCVVSWKNKELKCGSGIFITDNV
SQ  HTWTEQYNFQPESPSKLASAMRKAHEEGICGIRSVTRLENLMWKQITPELKHILSEIEVKLTIMTGDIKGIMQAGTRSLR
SQ  PQPTELKFSWETWRKAKMVPTEPHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLREKEDLCCDSKVMS
SQ  AASKDNRAVHDDMGYWIESALNDTWKMEKASFIEVKSCHWPKSHTLWINGGLESEMIIPKSFAGPVSQHNYRPGYYTQTA
SQ  GPRHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSSTIPPLRIKGEDGCWYGMEIRPLKEKEENL
SQ  VTSLVTA
//
ID  P07564;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11064;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P07564;
DR  UNIPROT: P07565;
DR  UNIPROT: Q88642;
DR  UNIPROT: Q88643;
DR  UNIPROT: Q88644;
DR  UNIPROT: Q88645;
DR  PDB: 3UZV;
DR  PDB: 6VG5;
DR  PDB: 6VSO;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKARSTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINV
SQ  LRGFRKEIGRMLNILNRRRRTAGVIIMLIPTAMAFHLTTRNGEPHMIVGRQEKGKSLLFKTEDGVNMCTLMAIDLGELCE
SQ  DTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCATTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHVQRIETW
SQ  ILRHPGFTIMAAILAYTIGTTHFQRALIFILLTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT
SQ  LDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFLCKHSMVDRGWGNGCGLFGKGGIVTCAMFT
SQ  CKKNMEGKVVLPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQ
SQ  MEDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFT
SQ  GHLKCRLRMDKLQLKGMSYSMCTGKFKIVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTE
SQ  KDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVF
SQ  GAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGVVTLYLGAMVQADSGCVVSWKNKELKCGSGIFITDNV
SQ  HTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITPELNHILSENEVKLTIMTGDIKGIMQAGKRSLR
SQ  PQPTELKYSWKTWGKAKMLSTESHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLREKQDVFCDSKLMS
SQ  AAIKDNRAVHADMGYWIESALNDTWKMEKASFIEVKSCHWPKSHTLWSNGVLESEMIIPKNFAGPVSQHNYRPGYHTQTA
SQ  GPWHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENL
SQ  VNSLVTAGHGQIDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDLGRVMVMVGATMTDDIGMGVT
SQ  YLALLAAFKVRPTFAAGLLLRKLTSKELMMATIGIALLSQSTIPETILELTDALALGMMVLKIVRNMEKYQLAVTIMAIL
SQ  CVPNAVILQNAWKVSCTILAAVSVSPLLLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVS
SQ  ILASSLLKNDIPMTGPLVAGGLLTVCYVLTGRSADLELERAADVKWEDQAEISGSSPILSITISEDGSMSIKNEEEEQTL
SQ  TILIRTGLLVISGVFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPVGKAELEDGAYRIKQRGILGYSQIGAGVYKEGT
SQ  FHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFKTNTGTIGA
SQ  VSLDFSPGTSGSPIVDRKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKKRLTIMDLHPGAGKTKRYLP
SQ  AIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDE
SQ  AHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDEEREIPERSWNSGHEWVTDFKGKTVWFVPSI
SQ  KAGNDIAACLRKNGKKVIQLSRKTFDSEYVKTRANDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAG
SQ  PMPVTHSSAAQRRGRIGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRL
SQ  RGEARKTFVDLMRRGDLPVWLAYRVAAEGINYADRRWCFDGIKNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPL
SQ  ALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGG
SQ  IFLFLMSGKGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAA
SQ  TMANEMGFLEKTKKDLGLGSITTQESESNILDIDLRPASAWTLYAVATTFVTPMLRHSIENSSVNVSLTAIANQATVLMG
SQ  LGKGWPLSKIHIGVPLLAIGCYSQVNPITLTAALLLLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDP
SQ  IPYDPKFEKQLGQVMLLILCVTQVLMMRTTWALCEALTLATGPISTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLF
SQ  SIMKNTTNTRRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERN
SQ  MVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFTPPEKCDTLLCDIGE
SQ  SSPNPTIEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMETLQRKYGGALVRNPLSRNSTHEMYWVSNASGNIV
SQ  SSVNMISRMLINRFTMKHKKATYETDVDLGSGTRNIGIESEIPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSY
SQ  ETKQTGSASSMVNGVVRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKK
SQ  TPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDRERNLHLEGKCETCVYNMMGKREKKLGEFGKAK
SQ  GSRAIWYMWLGARFLEFEALGFLNEDHWFSRGNSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKN
SQ  EEMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGIF
SQ  KSIQHLTVTEEIAVQNWLARVGRERLSRMAISGDDCVVKPLDDRFASALTALNDMGKVRKDIQQWEPSRGWNDWTQVPFC
SQ  SHHFHELVMKDGRVLVVPCRNQDELIGRARISQGAGWSLKETACLGKSYAQMWTLMYFHRRDLRLAANAICSAVPSHWVP
SQ  TSRTTWSIHAKHEWMTTEDMLAVWNRVWIQENPWMEDKTPVESWEEVPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQ
SQ  VRSLIGNEEYTDYMPSMKRFRREEEEAGVLW
//
ID  P14340;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11065;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:23408612}; Multi-pass membrane protein {ECO:0000269|PubMed:23408612}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:17276984}; Multi-pass membrane protein {ECO:0000269|PubMed:17276984}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:16436383}; Multi-pass membrane protein {ECO:0000269|PubMed:16436383}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P14340;
DR  UNIPROT: Q66347;
DR  UNIPROT: Q66348;
DR  UNIPROT: Q66349;
DR  UNIPROT: Q66350;
DR  UNIPROT: Q66351;
DR  UNIPROT: Q66352;
DR  UNIPROT: Q66353;
DR  UNIPROT: Q66354;
DR  UNIPROT: Q66355;
DR  UNIPROT: Q66356;
DR  UNIPROT: Q89579;
DR  PDB: 3IYA;
DR  PDB: 3J27;
DR  PDB: 3J2P;
DR  PDB: 4CBF;
DR  PDB: 4UIH;
DR  PDB: 6FLA;
DR  PDB: 6FLB;
DR  PDB: 6FLC;
DR  PDB: 6IZX;
DR  PDB: 6IZY;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000269|PubMed:17276984}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.
DE  Reference Proteome: No;
DE  Interaction: Q9UHY1; IntAct: EBI-465775; Score: 0.54
DE  Interaction: O88351; IntAct: EBI-9825940; Score: 0.37
DE  Interaction: P25963; IntAct: EBI-9826056; Score: 0.52
DE  Interaction: Q15653; IntAct: EBI-9826073; Score: 0.52
DE  Interaction: P08670; IntAct: EBI-9844714; Score: 0.64
DE  Interaction: P06733; IntAct: EBI-9844507; Score: 0.35
DE  Interaction: P14618; IntAct: EBI-9844507; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-9844507; Score: 0.35
DE  Interaction: P11413; IntAct: EBI-9844507; Score: 0.35
DE  Interaction: P50395; IntAct: EBI-9844507; Score: 0.35
DE  Interaction: P60709; IntAct: EBI-9844507; Score: 0.35
DE  Interaction: P68104; IntAct: EBI-9844507; Score: 0.35
DE  Interaction: P55265; IntAct: EBI-11512952; Score: 0.51
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKARNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINV
SQ  LRGFRKEIGRMLNILNRRRRTAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCE
SQ  DTITYKCPFLKQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETW
SQ  ILRHPGFTIMAAILAYTIGTTHFQRALIFILLTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT
SQ  LDFELIETEAKQPATLRKYCIEAKLTNTTTDSRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFT
SQ  CKKNMKGKVVQPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQ
SQ  MENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFT
SQ  GHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTE
SQ  KDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSSIGQMIETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVF
SQ  GAIYGAAFSGVSWIMKILIGVIITWIGMNSRSTSLSVSLVLVGVVTLYLGVMVQADSGCVVSWKNKELKCGSGIFITDNV
SQ  HTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITPELNHILSENEVKLTIMTGDIKGIMQAGKRSLQ
SQ  PQPTELKYSWKTWGKAKMLSTESHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLREKQDVFCDSKLMS
SQ  AAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKSCHWPKSHTLWSNGVLESEMIIPKNFAGPVSQHNYRPGYHTQTA
SQ  GPWHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENL
SQ  VNSLVTAGHGQIDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDLGRVMVMVGATMTDDIGMGVT
SQ  YLALLAAFKVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSTIPETILELTDALALGMMVLKMVRKMEKYQLAVTIMAIL
SQ  CVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTNKKRSWPLNEAIMAVGMVS
SQ  ILASSLLKNDIPMTGPLVAGGLLTVCYVLTGRSADLELERAADVKWEDQAEISGSSPILSITISEDGSMSIKNEEEEQTL
SQ  TILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPVGKAELEDGAYRIKQKGILGYSQIGAGVYKEGT
SQ  FHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFKTNAGTIGA
SQ  VSLDFSPGTSGSPIIDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRKLTIMDLHPGAGKTKRYLP
SQ  AIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDE
SQ  AHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDEEREIPERSWSSGHEWVTDFKGKTVWFVPSI
SQ  KAGNDIAACLRKNGKKVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAG
SQ  PMPVTHSSAAQRRGRIGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRL
SQ  RGEARKTFVDLMRRGDLPVWLAYRVAAEGINYADRRWCFDGIKNNQILEENVEVEIWTKEGERKKLKPRWLDAKIYSDPL
SQ  ALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGG
SQ  IFLFLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAA
SQ  TMANEMGFLEKTKKDLGLGSITTQQPESNILDIDLRPASAWTLYAVATTFVTPMLRHSIENSSVNVSLTAIANQATVLMG
SQ  LGKGWPLSKMDIGVPLLAIGCYSQVNPITLTAALFLLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDP
SQ  IPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEALTLATGPISTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLF
SQ  SIMKNTTNTRRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERN
SQ  MVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFTPPEKCDTLLCDIGE
SQ  SSPNPTVEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMEALQRKYGGALVRNPLSRNSTHEMYWLSNASGNIV
SQ  SSVNMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESEIPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSY
SQ  ETKQTGSASSMGNGVVRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKK
SQ  TPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNMMGKREKKLGEFGKAK
SQ  GSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKN
SQ  EEMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVF
SQ  KSIQHLTVTEEIAVQNWLARVGRERLSRMAISGDDCVVKPLDDRFASALTALNDMGKVRKDIQQWEPSRGWNDWTQVPFC
SQ  SHHFHELIMKDGRVLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQMWSLMYFHRRDLRLAANAICSAVPSHWVP
SQ  TSRTTWSIHAKHEWMTTEDMLTVWNRVWIQENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQ
SQ  VRSLIGNEEYTDYMPSMKRFRKEEEEAGVLW
//
ID  P12823;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11066;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P12823;
DR  UNIPROT: Q88646;
DR  UNIPROT: Q88647;
DR  UNIPROT: Q88648;
DR  UNIPROT: Q88649;
DR  UNIPROT: Q88650;
DR  UNIPROT: Q88651;
DR  UNIPROT: Q88652;
DR  UNIPROT: Q88653;
DR  UNIPROT: Q88654;
DR  UNIPROT: Q88655;
DR  PDB: 1L9K;
DR  PDB: 1OAN;
DR  PDB: 1OK8;
DR  PDB: 1OKE;
DR  PDB: 1P58;
DR  PDB: 1R6A;
DR  PDB: 1R6R;
DR  PDB: 1THD;
DR  PDB: 2P1D;
DR  PDB: 2P3L;
DR  PDB: 2P3O;
DR  PDB: 2P3Q;
DR  PDB: 2P40;
DR  PDB: 2P41;
DR  PDB: 3J8D;
DR  PDB: 3ZKO;
DR  PDB: 4M9F;
DR  PDB: 4M9I;
DR  PDB: 4M9K;
DR  PDB: 4M9M;
DR  PDB: 4M9T;
DR  PDB: 5HHG;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNDQRKKARNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINV
SQ  LRGFRKEIGRMLNILNRRRRTAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTKDGTNMCTLMAMDLGELCE
SQ  DTITYKCPFLKQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETW
SQ  ILRHPGFTIMAAILAYTIGTTHFQRVLIFILLTAIAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT
SQ  LDFELIKTEAKQPATLRKYCIEAKLTNTTTDSRCPTQGEPTLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFT
SQ  CKKNMEGKIVQPENLEYTVVITPHSGEEHAVGNDTGKHGKEVKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQ
SQ  MKDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFT
SQ  GHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKTPFEIMDLEKRHVLGRLTTVNPIVTE
SQ  KDSPVNIEAEPPFGDSYIIIGVEPGQLKLDWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVF
SQ  GAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFVTDNV
SQ  HTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITSELNHILSENEVKLTIMTGDIKGIMQVGKRSLR
SQ  PQPTELRYSWKTWGKAKMLSTELHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLRLREKQDAFCDSKLMS
SQ  AAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKSCHWPKSHTLWSNGVLESEMVIPKNFAGPVSQHNNRPGYHTQTA
SQ  GPWHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENL
SQ  VSSLVTAGHGQIDNFSLGILGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDLGRVMVMVGATMTDDIGMGVT
SQ  YLALLAAFKVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSSIPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAIL
SQ  CVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVS
SQ  ILASSLLKNDTPMTGPLVAGGLLTVCYVLTGRSADLELERATDVKWDDQAEISGSSPILSITISEDGSMSIKNEEEEQTL
SQ  TILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPVGKAELEDGAYRIKQKGILGYSQIGAGVYKEGT
SQ  FHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFRTNTGTIGA
SQ  VSLDFSPGTSGSPIVDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLP
SQ  AIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPIRVPNYNLIIMDE
SQ  AHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDEEREIPERSWNSGHEWVTDFKGKTVWFVPSI
SQ  KTGNDIAACLRKNGKRVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAG
SQ  PMPVTHSSAAQRRGRIGRNPRNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRL
SQ  RGEARKTFVDLMRRGDLPVWLAYKVAAEGINYADRRWCFDGTRNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPL
SQ  ALKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGKAYNHALSELPETLETLLLLTLLATVTGGIFL
SQ  FLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVIIAILTVVAATMA
SQ  NEMGFLEKTKKDLGLGNIATQQPESNILDIDLRPASAWTLYAVATTFITPMLRHSIENSSVNVSLTAIANQATVLMGLGK
SQ  GWPLSKMDIGVPLLAIGCYSQVNPITLTAALLLLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDPIPY
SQ  DPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEALTLATGPVSTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLFSIM
SQ  KNTTSTRRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNLVT
SQ  PEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFVPPEKCDTLLCDIGESSP
SQ  NPTVEAGRTLRVLNLVENWLNNNTQFCVKVLNPYMPSVIERMETLQRKYGGALVRNPLSRNSTHEMYWVSNASGNIVSSV
SQ  NMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESETPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSYETK
SQ  QTGSASSMVNGVVRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPR
SQ  MCTREEFTKKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNMMGKREKKLGEFGKAKGSR
SQ  AIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILREVSKKEGGAMYADDTAGWDTRITIEDLKNEEM
SQ  ITNHMAGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGIFKSI
SQ  QHLTASEEIAVQDWLARVGRERLSRMAISGDDCVVKPLDDRFARALTALNDMGKVRKDIQQWEPSRGWNDWTQVPFCSHH
SQ  FHELIMKDGRTLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQMWSLMYFHRRDLRLAANAICSAVPSHWVPTSR
SQ  TTWSIHASHEWMTTEDMLTVWNKVWILENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQVRS
SQ  LIGNEEYTDYMPSMKRFRREEEEAGVLW
//
ID  Q9WDA6;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  408694;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q9WDA6;
DR  PDB: 3IXY;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKARNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINV
SQ  LRGFRKEIGRMLNILNRRRRTAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTKDGTNMCTLMAMDLGELCE
SQ  DTITYKCPFLKQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETW
SQ  ILRHPGFTIMAAILAYTIGTTHFQRVLIFILLTAIAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT
SQ  LDFELIKTEAKQPATLRKYCIEAKLTNTTTDSRCPTQGEPTLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFT
SQ  CKKNMEGKIVQPENLEYTVVITPHSGEEHAVGNDTGKHGKEVKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQ
SQ  MEDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFT
SQ  GHLKCRLRMDKLQLKGMSYSMCTGKFKIVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTE
SQ  KDSPVNIEAEPPFGDSYIIIGAEPGQLKLDWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVF
SQ  GAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFVTDNV
SQ  HTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITSELNHILSENEVKLTIMTGDIKGIMQVGKRSLR
SQ  PQPTELRYSWKTWGKAKMLSTELHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLRLREKQDAFCDSKLMS
SQ  AAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKSCHWPKSHTLWSNGVLESEMVIPKNIAGPVSQHNNRPGYHTQTA
SQ  GPWHLGKLEMDFDFCEGTTVVVTEECGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENL
SQ  VSSLVTAGHGQIDNFSLGILGMALFLEEMLRTRVGTKHAILLVAVSFLTLITGNMSFRDLGRVMVMVGATMTDDIGMGVT
SQ  YLALLAAFKVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSSIPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAIL
SQ  CVPNAVILQNAWKVSCTTLAVVSVSPLLLTSSQQKADWIPLALTIKGLNPTAIFLTTLTRTSKKRSWPLNEAIMAVGMVS
SQ  ILASSLLKNDIPMTGPLVAGGLLTVCYVLTGRSADLELERATDVKWDDQAEISGSSPILSITISEDGSMSIKNEEEEQTL
SQ  TILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPVGRAELEDGAYRIKQKGILGYSQIGAGVYKEGT
SQ  FHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFRTNTGTIGA
SQ  VSLDFSPGTSGSPIVDKKGKVVGLYGNGVVTRGGAYVSAIAQTEKGIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLP
SQ  AIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPIRVPNYNLIIMDE
SQ  AHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDEEREIPERSWNSGHEWVTDFKGKTVWFVPSI
SQ  KTGNDIAACLRKNGKRVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAG
SQ  PMPVTHSSAAQRRGRIGRNPRNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRL
SQ  RGEARKTFVDLMRRGDLPVWLAYKVAAEGINYADRRWCFDGTRNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPL
SQ  ALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGKAYNHALSELPETLETLLLLTLLATVTGG
SQ  IFLFLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVIIAILTVVAA
SQ  TMANEMGFLEKTKKDLGLGHIATQQPESNILDIDLRPASAWTLYAVATTFITPMLRHSIENSSVNVSLTAIANQATVLMG
SQ  LGKGWPLSKMDIGVPLLAIGCYSQVNPITLTAALLMLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDP
SQ  IPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEALTLATGPVSTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLF
SQ  SIMKNTTSTRRGTGNMGETLGEKWKNRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERN
SQ  LVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFVPPEKCDTLLCDIGE
SQ  SSPNPTVEAGRTLRVLNLVENWLNNNTQFCVKVLNPYMPSVIERMETLQRKYGGALVRNPLSRNSTHEMYWVSNASGNIV
SQ  SSVNMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESETPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSY
SQ  ETKQTGSASSMVNGVVRLLTKPWDVIPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKK
SQ  TPRMCTREEFTKKVRSNAALGAIFTDENKWKSAREAVEDNRFWELVDKERNLHLEGKCETCVYNMMGKREKKLGEFGKAK
SQ  GSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILREVSKKEGGAMYADDTAGWDTRITIEDLKN
SQ  EEMITNHMAGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVVTYGLNTFTNMEAQLIRQMEGEGVF
SQ  KSIQHLTASEEIAVQDWLVRVGRERLSRMAISGDDCVVKPLDDRFAKALTALNDMGKVRKDIQQWEPSRGWNDWTQVPFC
SQ  SHHFHELIMKDGRTLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQMWSLMYFHRRDLRLAANAICSAVPSHWVP
SQ  TSRTTWSIHASHEWMTTEDMLTVWNRVWILENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQ
SQ  VRSLIGNEEYTDYMPSMKRFRREEEEVGVLW
//
ID  Q99D35;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  408690;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q99D35;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKTGKPSINMLKRVRNRVSTGSQLAKRFSRGLLNGQGPMKLVMAFIAFLRFLAIPPTAGVLARWGTFKKSGAIKV
SQ  LKGFKKEISNMLSIINKRKKTSLCLMMMLPATLAFHLTSRDGEPRMIVGKNERGKSLLFKTASGINMCTLIAMDLGEMCD
SQ  DTVTYKCPHITEVEPEDIDCWCNLTSTWVTYGTCNQAGEHRRDKRSVALAPHVGMGLDTRTQTWMSAEGAWRQVEKVETW
SQ  ALRHPGFTILALFLAHYIGTSLTQKVVIFILLMLVTPSMTMRCVGVGNRDFVEGLSGATWVDVVLEHGGCVTTMAKNKPT
SQ  LDIELQKTEATQLATLRKLCIEGKITNITTDSRCPTQGEAILPEEQDQNYVCKHTYVDRGWGNGCGLFGKGSLVTCAKFQ
SQ  CLESIEGKVVQHENLKYTVIITVHTGDQHQVGNETQGVTAEITSQASTAEAILPEYGTLGLECSPRTGLDFNEMILLTMK
SQ  NKAWMVHRQWFFDLPLPWTSGATTKTPTWNRKELLVTFKNAHAKKQEVVVLGSQEGAMHTALTGATEIQTLGGTSIFAGH
SQ  LKCRLKMDKLELKGMSYAMCLNTFVLKKEVSETQHGTILIKVEYKGEDAPCKIPFSTEDGQGKAHNGRLITANPVVTKKE
SQ  EPVNIEAEPPFGESNIVIGIGDKALKINWYRKGSSIGKMFEATARGARRMAILGDTAWDFGSVGGVLNSLGKMVHQIFGS
SQ  AYTALFSGVSWIMKIGIGVLLTWIGLNSKNTSMSFSCIAIGIITLYLGVVVQADMGCVINWKGKELKCGSGIFVTNEVHT
SQ  WTEQYKFQADSPKRLATAIAGAWENGVCGIRSTTRMENLLWKQIANELNYILWENNIKLTVVVGDITGVLEQGKRTLTPQ
SQ  PMELKYSWKTWGKAKIVTAETQNSSFIIDGPSTPECPSASRAWNVWEVEDYGFGVFTTNIWLKLREVYTQLCDHRLMSAA
SQ  VKDERAVHADMGYWIESQKNGSWKLEKASLIEVKTCTWPKSHTLWSNGVLESDMIIPKSLAGPISQHNHRPGYHTQTAGP
SQ  WHLGKLELDFNYCEGTTVVISENCGTRGPSLRTTTVSGKLIHEWCCRSCTLPPLRYMGEDGCWYGMEIRPINEKEENMVK
SQ  SLASAGSGKVDNFTMGVLCLAILFEEVMRGKFGKKHMIAGVLFTFVLLLSGQITWRDMAHTLIMIGSNASDRMGMGVTYL
SQ  ALIATFKIQPFLALGFFLRKLTSRENLLLGVGLAMAATLRLPEDIEQMANGIALGLMALKLITQFETYQLWTALVSLTCS
SQ  NTIFTLTVAWRTATLILAGISLLPVCQSSSMRKTDWLPMTVAAMGVPPLPLFIFSLKDTLKRRSWPLNEGVMAVGLVSIL
SQ  ASSLLRNDVPMAGPLVAGGLLIACYVITGTSADLTVEKAADVTWEEEAEQTGVSHNLMITVDDDGTMRIKDDETENILTV
SQ  LLKTALLIVSGIFPCSIPATLLVWHTWQKQTQRSGVLWDVPSPPETQKAELEEGVYRIKQQGIFGKTQVGVGVQKEGVFH
SQ  TMWHVTRGAVLTHNGKRLEPNWASVKKDLISYGGGWRLSAQWQKGEEVQVIAVEPGKNPKNFQTMPGIFQTTTGEIGAIA
SQ  LDFKPGTSGSPIINREGKVVGLYGNGVVTKNGGYVSGIAQTNAEPDGPTPELEEEMFKKRNLTIMDLHPGSGKTRKYLPA
SQ  IVREAIKRRLRTLILAPTRVVAAEMEEALKGLPIRYQTTATKSEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEA
SQ  HFTDPASIAARGYISTRVGMGEAAAIFMTATPPGTADAFPQSNAPIQDEERDIPERSWNSGNEWITDFVGKTVWFVPSIK
SQ  AGNDIANCLRKNGKKVIQLSRKTFDTEYQKTKLNDWDFVVTTDISEMGANFKADRVIDPRRCLKPVILTDGPERVILAGP
SQ  MPVTVASAAQRRGRVGRNPQKENDQYIFMGQPLNKDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLK
SQ  GESRKTFVELMRRGDLPVWLAHKVASEGIKYTDRKWCFDGERNNQILEENMDVEIWTKEGEKKKLRPRWLDARTYSDPLA
SQ  LKEFKDFAAGRKSIALDLVTEIGRVPSHLAHRTRNALDNLVMLHTSEHGGRAYRHAVEELPETMETLLLLGLMILLTGGA
SQ  MLFLISGKGIGKTSIGLICVIASSGMLWMADVPLQWIASAIVLEFFMMVLLIPEPEKQRTPQDNQLAYVVIGILTLAAIV
SQ  AANEMGLLETTKRDLGMSKEPGVVSPTSYLDVDLHPASAWTLYAVATTVITPMLRHTIENSTANVSLAAIANQAVVLMGL
SQ  DKGWPISKMDLGVPLLALGCYSQVNPLTLIAAVLLLVTHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIMTIDLDPV
SQ  IYDSKFEKQLGQVMLLVLCAVQLLLMRTSWALCEVLTLATGPITTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLAFS
SQ  IMKSVGTGKRGTGSQGETLGEKWKKKLNQLSRKEFDLYKKSGITEVDRTEAKEGLKRGEITHHAVSRGSAKLQWFVERNM
SQ  VIPEGRVIDLGCGRGGWSYYCAGLKKVTEVRGYTKGGPGHEEPVPMSTYGWNIVKLMSGKDVFYLPPEKCDTLLCDIGES
SQ  SPSPTVEESRTIRVLKMVEPWLKNNQFCIKVLNPYMPTVIEHLERLQRKHGGMLVRNPLSRNSTHEMYWISNGTGNIVSS
SQ  VNMVSRLLLNRFTMTHRRPTIEKDVDLGAGTRHVNAEPETPNMDVIGERIKRIKEEHSSTWHYDDENPYKTWAYHGSYEV
SQ  KATGSASSMINGVVKLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTPRPMPGTRKVMEITAEWLWRTLGRNKRP
SQ  RLCTREEFTKKVRTNAAMGAVFTEENQWDSARAAVEDEEFWKLVDRERELHKLGKCGSCVYNMMGKREKKLGEFGKAKGS
SQ  RAIWYMWLGARYLEFEALGFLNEDHWFSRENSYSGVEGEGLHKLGYILRDISKIPGGAMYADDTAGWDTRITEDDLHNEE
SQ  KITQQMDPEHRQLANAIFKLTYQNKVVKVQRPTPKGTVMDIISRKDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVLSK
SQ  ADLENPHPLEKKITQWLETKGVERLKRMAISGDDCVVKPIDDRFANALLALNDMGKVRKDIPQWQPSKGWHDWQQVPFCS
SQ  HHFHELIMKDGRKLVVPCRPQDELIGRARISQGAGWSLRETACLGKAYAQMWTLMYFHRRDLRLASNAICSAVPVHWVPT
SQ  SRTTWSIHAHHQWMTTEDMLTVWNRVWIEDNPWMEDKTPITTWEDVPYLGKREDQWCGSLIGLTSRATWAQNILTAIQQV
SQ  RSLIGNEEFLDYMPSMKRFRKEEESEGAIW
//
ID  Q5UB51;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  408693;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q5UB51;
DR  PDB: 3U1I;
DR  PDB: 3U1J;
DR  PDB: 4CTJ;
DR  PDB: 4CTK;
DR  PDB: 4V0Q;
DR  PDB: 4V0R;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKTGKPSINMLKRVRNRVSTGSQLAKRFSRGLLNGQGPMKLVMAFIAFLRFLAIPPTAGVLARWGTFKKSGAIKV
SQ  LKGFKKEISNMLSIINKRKKTSLCLMMILPATLAFHLTSRDGEPRMIVGKNERGKSLLFKTASGINMCTLIAMDLGEMCD
SQ  DTVTYKCPLIAEVEPEDIDCWCNLTSTWVTYGTCNQAGEHRRDKRSVALAPHVGMGLDTRTQTWMSAEGAWRQVEKVETW
SQ  ALRHPGFTILALFLAHYIGTSLTQKVVIFILLMLVTPSMTMRCVGVGNRDFVEGLSGATWVDVVLEHGGCVTTMAKNKPT
SQ  LDIELQKTEATQLATLRKLCIEGKITNITTDSRCPTQGEAILPEEQDQNYVCKHTYVDRGWGNGCGLFGKGSLVTCAKFQ
SQ  CLEPIEGKVVQHENLKYTVIITVHTGDQHQVGNDTQGVTVEITPQASTVEAILPEYGTLGLECSPRTGLDFNEMILLTMK
SQ  NKAWMVHRQWFFDLPLPWTSGATTEAPTWNRKELLVTFKNAHAKKQEVVVLGSQEGAMHTALTGATEIQNSGGTSIFAGH
SQ  LKCRLKMDKLELKGMSYAMCLNTFVLKKEVSETQHGTILIKVEYKGEDAPCKIPFSTEDGQGKAHNGRLITANPVVTKKE
SQ  EPVNIEAEPPFGESNIVIGIGDKALKINWYKKGSSIGKMFEATARGARRMAILGDTAWDFGSVGGVLNSLGKMVHQIFGS
SQ  AYTALFSGVSWIMKIGIGVLLTWIGLNSKNTSMSFSCIAIGIITLYLGAVVQADMGCVINWKGKELKCGSGIFVTNEVHT
SQ  WTEQYKFQADSPKRLATAIAGAWENGVCGIRSTTRMENLLWKQIANELNYILWENNIKLTVVVGDIIGVLEQGKRTLTPQ
SQ  PMELKYSWKTWGKAKIVTAETQNSSFIIDGPNTPECPSASRAWNVWEVEDYGFGVFTTNIWLKLREVYTQSCDHRLMSAA
SQ  IKDERAVHADMGYWIESQKNGSWKLEKASFIEVKTCTWPKSHTLWSNGVLESDMIIPKSLAGPISQHNHRPGYHTQTAGP
SQ  WHLGKLELDFNYCEGTTVVITENCGTRGPSLRATTVSGKLIHEWCCRSCTLPPLRYMGEDGCWYGMEIRPVNEKEENMVK
SQ  SLVSAGSGKVDNFTMGVLCLAILFEEVMRGKFGKKHMIAGVLFTFVLLLSGQITWRDMAHTLIMIGSNASDRMGMGVTCL
SQ  ALIATFKIQPFLALGFFLRKLTSRENLLLGVGLAMATTLQLPEDIEQMANGIALGLMTLKLITQFETYQLWTALVSLTCS
SQ  NTIFTLTVAWRTATLILAGVSLLPVCQSSSMRKTDWLPMTVAAMGVPPLPLFIFSLKDALKRRSWPLNEGVMAVGLVSIL
SQ  ASSLLRNDVPMAGPLVAGGLLIACYVITGTSADLTVEKAADVTWEEEAEQTGVSHNLMITVDDDGTMRIKDDETENILTV
SQ  LLKTALLIVSGIFPYSIPATLLVWHTWQKQTQRSGVLWDVPSPPETQKAELEEGVYRIKQQGIFGKTQVGVGVQKEGVFH
SQ  TMWHVTRGAVLTHNGKRLEPNWASVKKDLISYGGGWRLSAQWQKGEEVQVIAVEPGKNPKNFQTMPGIFQTTTGEIGAIA
SQ  LDFKPGTSGSPIINREGKVVGLYGNGVVTKNGGYVSGIAQTNAEPDGPTPELEEEMFKKRNLTIMDLHPGSGKTRKYLPA
SQ  IVREAIKRRLRTLILAPTRVVAAEMEEALKGLPIRYQTTATKSEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEA
SQ  HFTDPASIAARGYISTRVGMGEAAAIFMTATPPGTAEAFPQSNAPIQDEERDIPERSWNSGNEWITDFVGKTVWFVPSIK
SQ  AGNDIANCLRKNGKKVIQLSRKTFDTEYQKTKLNDWDFVVTTDISEMGANFKADRVIDPRRCLKPVILTDGPERVILAGP
SQ  MPVTAASAAQRRGRVGRNPQKENDQYIFTGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLK
SQ  GESRKTFVELMRRGDLPVWLAHKVASEGIKYTDRKWCFDGERNNQILEENMDVEIWTKEGERKKLRPRWLDARTYSDPLA
SQ  LKEFKDFAAGRKSIALDLVTEIGRVPSHLAHRTRNALDNLVMLHTSEHGGRAYRHAVEELPETMETLLLLGLMILLTGGA
SQ  MLFLISGKGIGKTSIGLICVIASSGMLWMADVPLQWIASAIVLEFFMMVLLIPEPEKQRTPQDNQLAYVVIGILTLAAIV
SQ  AANEMGLLETTKRNLGMSKEPGVVSPTSYLDVDLHPASAWTLYAVATTVITPMLRHTIENSTANVSLAAIANQAVVLMGL
SQ  DKGWPISKMDLGVPLLALGCYSQVNPLTLTAAVLLLVTHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIMTIDLDPV
SQ  IYDSKFEKQLGQVMLLVLCAVQLLLMKTSWALCEVLTLATGPITTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLAFS
SQ  IMKSVGTGKRGTGSQGETLGEKWKKKLNQLSRKEFDLYKKSGITEVDRTEAKEGLKRGEITHHAVSRGSAKLQWFVERNM
SQ  VIPEGRVIDLGCGRGGWSYYCAGLKKVTEVRGYTKGGPGHEEPVPMSTYGWNIVKLMSGKDVFYLPPEKCDTLLCDIGES
SQ  SPSPTVEESRTIRVLKMVEPWLKNNQFCIKVLNPYMPTVIEHLERLQRKHGGMLVRNPLSRNSTHEMYWISNGTGNIVSS
SQ  VNMVSRLLLNRFTMTHRRPTIEKDVDLGAGTRHVNAEPETPNMDVIGERIKRIKEEHSSTWHYDDENPYKTWAYHGSYEV
SQ  KATGSASSMINGVVKLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTPRPMPGTRKVMEITAEWLWRTLGRNKRP
SQ  RLCTREEFTKKVRTNAAMGAVFTEENQWDSARAAVEDEEFWKLVDRERELHKLGKCGSCVYNMMGKREKKLGEFGKAKGS
SQ  RAIWYMWLGARYLEFEALGFLNEDHWFSRENSYSGVEGEGLHKLGYILRDISKIPGGAMYADDTAGWDTRITEDDLHNEE
SQ  KITQQMDPEHRQLANAIFKLTYQNKVVKVQRPTPKGTVMDIISRKDQRGSGQVGTYGLNTFTNMEAQLVRQMEGEGVLSK
SQ  ADLENPHPLEKKITQWLETKGVERLKRMAISGDDCVVKPIDDRFANALLALNDMGKVRKDIPQWQPSKGWHDWQQVPFCS
SQ  HHFHELIMKDGRKLVVPCRPQDELIGRARISQGAGWSLKETACLGKAYAQMWSLMYFHRRDLRLASNAICSAVPVHWVPT
SQ  SRTTWSIHAHHQWMTTEDMLTVWNRVWIEDNPWMEDKTPVTTWEDVPYLGKREDQWCGSLIGLTSRATWAQNILIAIQQV
SQ  RSLIGDEEFLDYMPSMKRFRKEEESEGAIW
//
ID  Q6YMS3;
PN  RNA-directed RNA polymerase NS5;
GN  pol;
OS  408691;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q6YMS3;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKTGKPSINMLKRVRNRVSTGSQLAKRFSKGLLNGQGPMKLVMAFIAFLRFLAIPPTAGVLARWGTFKKSGAIKV
SQ  LKGFKKEISNMLSIINKRKKTSLCLMMIMPAALAFHLTSRDGEPRMIVGKNERGKSLLFKTASGINMCTLIAMDLGEMCD
SQ  DTVTYKCPHITEVEPEDIDCWCNLTSTWVTYGTCNQAGERRRDKRSVALAPHVGMGLDTRTQTWMSAEGAWRQVEKVETW
SQ  ALRHPGFTILALFLAHYIGTSLTQKVVIFILLMLVTPSMTMRCVGVGNRDFVEGLSGATWVDVVLEHGGCVTTMAKNKPT
SQ  LDIELQKTEATQLATLRKLCIEGKITNITTDSRCPTQGEAVLPEEQDQNYVCKHTYVDRGWGNGCGLFGKGSLVTCAKFQ
SQ  CLEPIEGKVVQYENLKYTVIITVHTGDQHQVGNETQGVTAEITPQASTTEAILPEYGTLGLECSPRTGLDFNEMILLTMK
SQ  NKAWMVHRQWFFDLPLPWTSGATTETPTWNRKELLVTFKNAHAKKQEVVVLGSQEGAMHTALTGATEIQNSGGTSIFAGH
SQ  LKCRLKMDKLELKGMSYAMCTNTFVLKKEVSETQHGTILIKVEYKGEDAPCKIPFSTEDGQGKAHNGRLITANPVVTKKE
SQ  EPVNIEAEPPFGESNIVIGIGDNALKINWYKKGSSIGKMFEATARGARRMAILGDTAWDFGSVGGVLNSLGKMVHQIFGS
SQ  AYTALFSGVSWVMKIGIGVLLTWIGLNSKNTSMSFSCIAIGIITLYLGAVVQADMGCVINWKGKELKCGSGIFVTNEVHT
SQ  WTEQYKFQADSPKRLATAIAGAWENGVCGIRSTTRMENLLWKQIANELNYILWENNIKLTVVVGDIIGVLEQGKRTLTPQ
SQ  PMELKYSWKTWGKAKIVTAETQNSSFIIDGPNTPECPSASRAWNVWEVEDYGFGVFTTNIWLKLREVYTQLCDHRLMSAA
SQ  VKDERAVHADMGYWIESQKNGSWKLEKASLIEVKTCTWPKSHTLWSNGVLESDMIIPKSLAGPISQHNHRPGYHTQTAGP
SQ  WHLGKLELDFNYCEGTTVVITENCGTRGPSLRTTTVSGKLIHEWCCRSCTLPPLRYMGEDGCWYGMEIRPISEKEENMVK
SQ  SLVSAGSGKVDNFTMGVLCLAILFEEVMRGKFGKKHMIAGVFFTFVLLLSGQITWRDMAHTLIMIGSNASDRMGMGVTYL
SQ  ALIATFKIQPFLALGFFLRKLTSRENLLLGVGLAMATTLQLPEDIEQMANGIALGLMALKLITQFETYQLWTALISLTCS
SQ  NTMFTLTVAWRTATLILAGVSLLPVCQSSSMRKTDWLPMAVAAMGVPPLPLFIFSLKDTLKRRSWPLNEGVMAVGLVSIL
SQ  ASSLLRNDVPMAGPLVAGGLLIACYVITGTSADLTVEKAADITWEEEAEQTGVSHNLMITVDDDGTMRIKDDETENILTV
SQ  LLKTALLIVSGVFPYSIPATLLVWHTWQKQTQRSGVLWDVPSPPETQKAELEEGVYRIKQQGIFGKTQVGVGVQKEGVFH
SQ  TMWHVTRGAVLTYNGKRLEPNWASVKKDLISYGGGWRLSAQWQKGEEVQVIAVEPGKNPKNFQTMPGTFQTTTGEIGAIA
SQ  LDFKPGTSGSPIINREGKVVGLYGNGVVTKNGGYVSGIAQTNAEPDGPTPELEEEMFKKRNLTIMDLHPGSGKTRKYLPA
SQ  IVREAIKRRLRTLILAPTRVVAAEMEEALKGLPIRYQTTATKSEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEA
SQ  HFTDPASIAARGYISTRVGMGEAAAIFMTATPPGTADAFPQSNAPIQDEERDIPERSWNSGNEWITDFAGKTVWFVPSIK
SQ  AGNDIANCLRKNGKKVIQLSRKTFDTEYQKTKLNDWDFVVTTDISEMGANFKADRVIDPRRCLKPVILTDGPERVILAGP
SQ  MPVTAASAAQRRGRVGRNPQKENDQYIFTGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLK
SQ  GESRKTFVELMRRGDLPVWLAHKVASEGIKYTDRKWCFDGQRNNQILEENMDVEIWTKEGEKKKLRPRWLDARTYSDPLA
SQ  LKEFKDFAAGRKSIALDLVTEIGRVPSHLAHRTRNALDNLVMLHTSEHGGRAYRHAVEELPETMETLLLLGLMILLTGGA
SQ  MLFLISGKGIGKTSIGLICVIASSGMLWMAEIPLQWIASAIVLEFFMMVLLIPEPEKQRTPQDNQLAYVVIGILTLAAII
SQ  AANEMGLLETTKRDLGMSKEPGVVSPTSYLDVDLHPASAWTLYAVATTVITPMLRHTIENSTANVSLAAIANQAVVLMGL
SQ  DKGWPISKMDLGVPLLALGCYSQVNPLTLTAAVLLLITHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIMTIDLDPV
SQ  IYDSKFEKQLGQVMLLVLCAVQLLLMRTSWALCEALTLATGPITTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLAFS
SQ  IMKSVGTGKRGTGSQGETLGEKWKKKLNQLSRKEFDLYKKSGITEVDRTEAKEGLKRGEITHHAVSRGSAKLQWFVERNM
SQ  VIPEGRVIDLGCGRGGWSYYCAGLKKVTEVRGYTKGGPGHEEPVPMSTYGWNIVKLMSGKDVFYLPPEKCDTLLCDIGES
SQ  SPSPTVEESRTIRVLKMVEPWLKNNQFCIKVLNPYMPTVIEHLERLQRKHGGMLVRNPLSRNSTHEMYWISNGTGNIVAS
SQ  VNMVSRLLLNRFTMTHRRPTIEKDVDLGAGTRHVNAEPETPNMDVIGERIKRIKEEHNSTWHYDDENPYKTWAYHGSYEV
SQ  KATGSASSMINGVVKLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTPRSMPGTRRVMGITAEWLWRTLGRNKKP
SQ  RLCTREEFTKKVRTNAAMGAVFTEENQWDSAKAAVEDEDFWKLVDRERELHKLGKCGSCVYNMMGKREKKLGEFGKAKGS
SQ  RAIWYMWLGARYLEFEALGFLNEDHWFSRENSYSGVEGEGLHKLGYILRDISKIPGGAMYADDTAGWDTRITEDDLHNEE
SQ  KITQQMDPEHRQLANAIFKLTYQNKVVKVQRPTPTGTVMDIISRKDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVLSK
SQ  ADLENPHLPEKKITQWLETKGVERLKRMAISGDDCVVKPIDDRFANALLALNDMGKVRKDIPQWQPSKGWHDWQQVPFCS
SQ  HHFHELIMKDGRKLVVPCRPQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASNAICSAVPVHWVPT
SQ  SRTTWSIHAHHQWMTTEDMLTVWNRVWIEDNPWMEDKTPVTTWENVPYLGKREDQWCGSLIGLTSRATWAQNIPTAIQQV
SQ  RSLIGNEEFLDYMPSMKRFRKEEESEGAIW
//
ID  P27915;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  408870;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P27915;
DR  PDB: 1UZG;
DR  PDB: 2J7U;
DR  PDB: 2J7W;
DR  PDB: 3P8Z;
DR  PDB: 3P97;
DR  PDB: 3UZE;
DR  PDB: 3VTT;
DR  PDB: 5CCV;
DR  PDB: 5E9Q;
DR  PDB: 5EC8;
DR  PDB: 5EHG;
DR  PDB: 5EHI;
DR  PDB: 5EIF;
DR  PDB: 5EIW;
DR  PDB: 5EKX;
DR  PDB: 7A3S;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKTGKPSINMLKRVRNRVSTGSQLAKRFSRGLLNGQGPMKLVMAFIAFLRFLAIPPTAGVLARWGTFKKSGAIKV
SQ  LKGFKKEISNMLSIINKRKKTSLCLMMMLPATLAFHLTSRDGEPRMIVGKNERGKSLLFKTASGINMCTLIAMDLGEMCD
SQ  DTVTYKCPHITEVEPEDIDCWCNLTSTWVTYGTCNQAGEHRRDKRSVALAPHVGMGLDTRTQTWMSAEGAWRQVEKVETW
SQ  ALRHPGFTILALFLAHYIGTSLTQKVVIFILLMLVTPSMTMRCVGVGNRDFVEGLSGATWVDVVLEHGGCVTTMAKNKPT
SQ  LDIELQKTEATQLATLRKLCIEGKITNITTDSRCPTQGEAILPEEQDQNYVCKHTYVDRGWGNGCGLFGKGSLVTCAKFQ
SQ  CLESIEGKVVQHENLKYTVIITVHTGDQHQVGNETQGVTAEITSQASTAEAILPEYGTLGLECSPRTGLDFNEMILLTMK
SQ  NKAWMVHRQWFFDLPLPWTSGATTKTPTWNRKELLVTFKNAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGGTSIFAGH
SQ  LKCRLKMDKLKLKGMSYAMCLNTFVLKKEVSETQHGTILIKVEYKGEDAPCKIPFSTEDGQGKAHNGRLITANPVVTKKE
SQ  EPVNIEAEPPFGESNIVIGIGDKALKINWYRKGSSIGKMFEATARGARRMAILGDTAWDFGSVGGVLNSLGKMVHQIFGS
SQ  AYTALFSGVSWIMKIGIGVLLTWIGLNSKNTSMSFSCIAIGIITLYLGVVVQADMGCVINWKGKELKCGSGIFVTNEVHT
SQ  WTEQYKFQADSPKRVATAIAGAWENGVCGIRSTTRMENLLWKQIANELNYILWENDIKLTVVVGDITGVLEQGKRTLTPQ
SQ  PMELKYSWKTWGLAKIVTAETQNSSFIIDGPSTPECPSASRAWNVWEVEDYGFGVFTTNIWLKLREVYTQLCDHRLMSAA
SQ  VKDERAVHADMGYWIESQKNGSWKLEKASLIEVKTCTWPKSHTLWSNGVLESDMIIPKSLAGPISQHNHRPGYHTQTAGP
SQ  WHLGKLELDFNYCEGTTVVISENCGTRGPSLRTTTVSGKLIHEWCCRSCTLPPLRYMGEDGCWYGMEIRPINEKEENMVK
SQ  SLASAGSGKVDNFTMGVLCLAILFEEVMRGKFGKKHMIAGVLFTFVLLLSGQITWRGMAHTLIMIGSNASDRMGMGVTYL
SQ  ALIATFKIQPFLALGFFLRKLTSRENLLLGVGLAMAATLRLPEDIEQMANGIALGLMALKLITQFETYQLWTALVSLTCS
SQ  NTIFTLTVAWRTATLILAGISLLPVCQSSSMRKTDWLPMTVAAMGVPPLPLFIFSLKDTLKRRSWPLNEGVMAVGLVSIL
SQ  ASSLLRNDVPMAGPLVAGGLLIACYVITGTSADLTVEKAADVTWEEEAEQTGVSHNLMITVDDDGTMRIKDDETENILTV
SQ  LLKTALLIVSGIFPYSIPATMLVWHTWQKQTQRSGVLWDVPSPPETQKAELEEGVYRIKQQGIFGKTQVGVGVQKEGVFH
SQ  TMWHVTRGAVLTHNGKRLEPNWASVKKDLISYGGGWRLSAQWQKGEEVQVIAVEPGKNPKNFQTMPGIFQTTTGEIGAIA
SQ  LDFKPGTSGSPIINREGKVVGLYGNGVVTKNGGYVSGIAQTNAEPDGPTPELEEEMFKKRNLTIMDLHPGSGKTRKYLPA
SQ  IVREAIKRRLRTLILAPTRVVAAEMEEAMKGLPIRYQTTATKSEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEA
SQ  HFTDPASIAARGYISTRVGMGEAAAIFMTATPPGTADAFPQSNAPIQDEERDIPERSWNSGNEWITDFVGKTVWFVPSIK
SQ  AGNVIANCLRKNGKKVIQLSRKTFDTEYQKTKLNDWDFVVTTDISEMGANFIADRVIDPRRCLKPVILTDGPERVILAGP
SQ  MPVTVASAAQRRGRVGRNPQKENDQYIFMGQPLNKDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLK
SQ  GESRKTFVELMRRGDLPVWLAHKVASEGIKYTDRKWCFDGERNNQILEENMDVEIWTKEGEKKKLRPRWLDARTYSDPLA
SQ  LKEFKDFAAGRKSIALDLVTEIGRVPSHLAHRTRNALDNLVMLHTSEHGGRAYRHAVEELPETMETLLLLGLMILLTGGA
SQ  MLFLISGKGIGKTSIGLICVIASSGMLWMADVPLQWIASAIVLEFFMMVLLIPEPEKQRTPQDNQLAYVVIGILTLAAIV
SQ  AANEMGLLETTKRDLGMSKEPGVVSPTSYLDVDLHPASAWTLYAVATTVITPMLRHTIENSTANVSLAAIANQAVVLMGL
SQ  DKGWPISKMDLGVPLLALGCYSQVNPLTLIAAVLLLVTHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIMTIDLDPV
SQ  IYDSKFEKQLGQVMLLVLCAVQLLLMRTSWALCEVLTLATGPITTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLALS
SQ  IMKSVGTGKRGTGSQGETLGEKWKKKLNQLSRKEFDLYKKSGITEVDRTEAKEGLKRGEITHHAVSRGSAKLQWFVERNM
SQ  VIPEGRVIDLGCGRGGWSYYCAGLKKVTEVRGYTKGGPGHEEPVPMSTYGWNIVKLMSGKDVFYLPPEKCDTLLCDIGES
SQ  SPSPTVEESRTIRVLKMVEPWLKNNQFCIKVLNPYMPTVIEHLERLQRKHGGMLVRNPLSRNSTHEMYWISNGTGNIVSS
SQ  VNMVSRLLLNRFTMTHRRPTIEKDVDLGAGTRHVNAEPETPNMDVIGERIKRIKEEHSSTWHYDDENPYKTWAYHGSYEV
SQ  KATGSASSMINGVVKLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTPRPMPGTRKVMEITAEWLWRTLGRNKRP
SQ  RLCTREEFTKKVRTNAAMGAVFTEENQWDSARAAVEDEEFWKLVDRERELHKLGKCGSCVYNMMGKREKKLGEFGKAKGS
SQ  RAIWYMWLGARYLEFEALGFLNEDHWFSRENSYSGVEGEGLHKLGYILRDISKIPGGAMYADDTAGWDTRITEDDLHNEE
SQ  KITQQMDPEHRQLANAIFKLTYQNKVVKVQRPTPKGTVMDIISRKDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVLSK
SQ  ADLENPHPLEKKITQWLETKGVERLKRMAISGDDCVVKPIDDRFANALLALNDMGKVRKDIPQWQPSKGWHDWQQVPFCS
SQ  HHFHELIMKDGRKLVVPCRPQDELIGRARISQGAGWSLRETACLGKAYAQMWTLMYFHRRDLRLASNAICSAVPVHWVPT
SQ  SRTTWSIHAHHQWMTTEDMLTVWNRVWIEDNPWMEDKTPVTTWEDVPYLGKREDQWCGSLIGLTSRATWAQNILTAIQQV
SQ  RSLIGNEEFLDYMPSMKRFRKEEESEGAIW
//
ID  Q6YMS4;
PN  RNA-directed RNA polymerase NS5;
GN  pol;
OS  408692;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q6YMS4;
DR  UNIPROT: Q6DLV0;
DR  PDB: 2J7U;
DR  PDB: 2J7W;
DR  PDB: 3VWS;
DR  PDB: 4C11;
DR  PDB: 4HHJ;
DR  PDB: 5DTO;
DR  PDB: 5EIW;
DR  PDB: 5F3T;
DR  PDB: 5F3Z;
DR  PDB: 5F41;
DR  PDB: 5HMW;
DR  PDB: 5HMX;
DR  PDB: 5HMY;
DR  PDB: 5HMZ;
DR  PDB: 5HN0;
DR  PDB: 5I3P;
DR  PDB: 5I3Q;
DR  PDB: 5IQ6;
DR  PDB: 5JJR;
DR  PDB: 5JJS;
DR  PDB: 5WJN;
DR  PDB: 5WKH;
DR  PDB: 6H80;
DR  PDB: 6H9R;
DR  PDB: 6XD0;
DR  PDB: 6XD1;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNNQRKKTGKPSINMLKRVRNRVSTGSQLAKRFSKGLLNGQGPMKLVMAFIAFLRFLAIPPTAGVLARWGTFKKSGAIKV
SQ  LKGFKKEISNMLSIINQRKKTSLCLMMILPAALAFHLTSRDGEPRMIVGKNERGKSLLFKTASGINMCTLIAMDLGEMCD
SQ  DTVTYKCPHITEVEPEDIDCWCNLTSTWVTYGTCNQAGEHRRDKRSVALAPHVGMGLDTRTQTWMSAEGAWRQVEKVETW
SQ  ALRHPGFTILALFLAHYIGTSLTQKVVIFILLMLVTPSMTMRCVGVGNRDFVEGLSGATWVDVVLEHGGCVTTMAKNKPT
SQ  LDIELQKTEATQLATLRKLCIEGKITNITTDSRCPTQGEAVLPEEQDQNYVCKHTYVDRGWGNGCGLFGKGSLVTCAKFQ
SQ  CLEPIEGKVVQYENLKYTVIITVHTGDQHQVGNETQGVTAEITPQASTTEAILPEYGTLGLECSPRTGLDFNEMILLTMK
SQ  NKAWMVHRQWFFDLPLPWASGATTETPTWNRKELLVTFKNAHAKKQEVVVLGSQEGAMHTALTGATEIQNSGGTSIFAGH
SQ  LKCRLKMDKLELKGMSYAMCTNTFVLKKEVSETQHGTILIKVEYKGEDAPCKIPFSTEDGQGKAHNGRLITANPVVTKKE
SQ  EPVNIEAEPPFGESNIVIGIGDNALKINWYKKGSSIGKMFEATERGARRMAILGDTAWDFGSVGGVLNSLGKMVHQIFGS
SQ  AYTALFSGVSWVMKIGIGVLLTWIGLNSKNTSMSFSCIAIGIITLYLGAVVQADMGCVINWKGKELKCGSGIFVTNEVHT
SQ  WTEQYKFQADSPKRLATAIAGAWENGVCGIRSTTRMENLLWKQIANELNYILWENNIKLTVVVGDTLGVLEQGKRTLTPQ
SQ  PMELKYSWKTWGKAKIVTAETQNSSFIIDGPNTPECPSASRAWNVWEVEDYGFGVFTTNIWLKLREVYTQLCDHRLMSAA
SQ  VKDERAVHADMGYWIESQKNGSWKLEKASLIEVKTCTWPKSHTLWTNGVLESDMIIPKSLAGPISQHNYRPGYHTQTAGP
SQ  WHLGKLELDFNYCEGTTVVITESCGTRGPSLRTTTVSGKLIHEWCCRSCTLPPLRYMGEDGCWYGMEIRPISEKEENMVK
SQ  SLVSAGSGKVDNFTMGVLCLAILFEEVLRGKFGKKHMIAGVFFTFVLLLSGQITWRDMAHTLIMIGSNASDRMGMGVTYL
SQ  ALIATFKIQPFLALGFFLRKLTSRENLLLGVGLAMATTLQLPEDIEQMANGVALGLMALKLITQFETYQLWTALVSLTCS
SQ  NTIFTLTVAWRTATLILAGVSLLPVCQSSSMRKTDWLPMTVAAMGVPPLPLFIFSLKDTLKRRSWPLNEGVMAVGLVSIL
SQ  ASSLLRNDVPMAGPLVAGGLLIACYVITGTSADLTVEKAPDVTWEEEAEQTGVSHNLMITVDDDGTMRIKDDETENILTV
SQ  LLKTALLIVSGIFPYSIPATLLVWHTWQKQTQRSGVLWDVPSPPETQKAELEEGVYRIKQQGIFGKTQVGVGVQKEGVFH
SQ  TMWHVTRGAVLTHNGKRLEPNWASVKKDLISYGGGWRLSAQWQKGEEVQVIAVEPGKNPKNFQTTPGTFQTTTGEIGAIA
SQ  LDFKPGTSGSPIINREGKVVGLYGNGVVTKNGGYVSGIAQTNAEPDGPTPELEEEMFKKRNLTIMDLHPGSGKTRKYLPA
SQ  IVREAIKRRLRTLILAPTRVVAAEMEEALKGLPIRYQTTATKSEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEA
SQ  HFTDPASIAARGYISTRVGMGEAAAIFMTATPPGTADAFPQSNAPIQDEERDIPERSWNSGNEWITDFAGKTVWFVPSIK
SQ  AGNDIANCLRKNGKKVIQLSRKTFDTEYQKTKLNDWDFVVTTDISEMGANFKADRVIDPRRCLKPVILTDGPERVILAGP
SQ  MPVTAASAAQRRGRVGRNPQKENDQYIFTGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLK
SQ  GESRKTFVELMRRGDLPVWLAHKVASEGIKYTDRKWCFDGQRNNQILEENMDVEIWTKEGEKKKLRPRWLDARTYSDPLA
SQ  LKEFKDFAAGRKSIALDLVTEIGRVPSHLAHRTRNALDNLVMLHTSEDGGRAYRHAVEELPETMETLLLLGLMILLTGGA
SQ  MLFLISGKGIGKTSIGLICVIASSGMLWMAEVPLQWIASAIVLEFFMMVLLIPEPEKQRTPQDNQLAYVVIGILTLAATI
SQ  AANEMGLLETTKRDLGMSKEPGVVSPTSYLDVDLHPASAWTLYAVATTVITPMLRHTIENSTANVSLAAIANQAVVLMGL
SQ  DKGWPISKMDLGVPLLALGCYSQVNPLTLTAAVLLLITHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIMTIDLDSV
SQ  IFDSKFEKQLGQVMLLVLCAVQLLLMRTSWALCEALTLATGPITTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLAFS
SQ  IMKSVGTGKRGTGSQGETLGEKWKKKLNQLSRKEFDLYKKSGITEVDRTEAKEGLKRGETTHHAVSRGSAKLQWFVERNM
SQ  VVPEGRVIDLGCGRGGWSYYCAGLKKVTEVRGYTKGGPGHEEPVPMSTYGWNIVKLMSGKDVFYLPPEKCDTLLCDIGES
SQ  SPSPTVEESRTIRVLKMVEPWLKNNQFCIKVLNPYMPTVIEHLERLQRKHGGMLVRNPLSRNSTHEMYWISNGTGNIVSS
SQ  VNMVSRLLLNRFTMTHRRPTIEKDVDLGAGTRHVNAEPETPNMDVIGERIKRIKEEHNSTWHYDDENPYKTWAYHGSYEV
SQ  KATGSASSMINGVVKLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTPRPMPGTRKAMEITAEWLWRTLGRNKRP
SQ  RLCTREEFTKKVRTNAAMGAVFTEENQWDSAKAAVEDEEFWKLVDRERELHKLGKCGSCVYNMMGKREKKLGEFGKAKGS
SQ  RAIWYMWLGARYLEFEALGFLNEDHWFSRENSYSGVEGEGLHKLGYILRDISKIPGGAMYADDTAGWDTRITEDDLHNEE
SQ  KIIQQMDPEHRQLANAIFKLTYQNKVVKVQRPTPTGTVMDIISRKDQRGSGQLGTYGLNTFTNMEAQLVRQMEGEGVLTK
SQ  ADLENPHLLEKKITQWLETKGVERLKRMAISGDDCVVKPIDDRFANALLALNDMGKVRKDIPQWQPSKGWHDWQQVPFCS
SQ  HHFHELIMKDGRKLVVPCRPQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASNAICSAVPVHWVPT
SQ  SRTTWSIHAHHQWMTTEDMLTVWNRVWIEENPWMEDKTPVTTWENVPYLGKREDQWCGSLIGLTSRATWAQNIPTAIQQV
SQ  RSLIGNEEFLDYMPSMKRFRKEEESEGAIW
//
ID  P09866;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  408871;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17763}; Cytoplasmic side {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000269|PubMed:30550790}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P09866;
DR  UNIPROT: Q88661;
DR  UNIPROT: Q88662;
DR  UNIPROT: Q88663;
DR  UNIPROT: Q88664;
DR  UNIPROT: Q88665;
DR  UNIPROT: Q88666;
DR  UNIPROT: Q88667;
DR  UNIPROT: Q88668;
DR  UNIPROT: Q88669;
DR  UNIPROT: Q88670;
DR  UNIPROT: Q88671;
DR  UNIPROT: Q99BK4;
DR  UNIPROT: Q9DKQ5;
DR  UNIPROT: Q9DKQ6;
DR  UNIPROT: Q9DKQ7;
DR  PDB: 2H0P;
DR  PDB: 3UAJ;
DR  PDB: 3UC0;
DR  PDB: 3WE1;
DR  PDB: 4X42;
DR  PDB: 5B1C;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (PubMed:30550790). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:30550790}.
DE  Reference Proteome: No;
DE  Interaction: P09866; IntAct: EBI-7591638; Score: 0.44
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0140272;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039653;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNQRKKVVRPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKIL
SQ  IGFRKEIGRMLNILNGRKRSTITLLCLIPTVMAFSLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCED
SQ  TVTYKCPLLVNTEPEDIDCWCNLTSTWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWI
SQ  LRNPGFALLAGFMAYMIGQTGIQRTVFFVLMMLVAPSYGMRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTL
SQ  DFELTKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDVVDRGWGNGCGLFGKGGVVTCAKFSC
SQ  SGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDTSNHGVTAMITPRSPSVEVKLPDYGELTLDCEPRSGIDFNEMILMKM
SQ  KKKTWLVHKQWFLDLPLPWTAGADTSEVHWNYKERMVTFKVPHAKRQDVTVLGSQEGAMHSALAGATEVDSGDGNHMFAG
SQ  HLKCKVRMEKLRIKGMSYTMCSGKFSIDKEMAETQHGTTVVKVKYEGAGAPCKVPIEIRDVNKEKVVGRIISSTPLAENT
SQ  NSVTNIELEPPFGDSYIVIGVGNSALTLHWFRKGSSIGKMFESTYRGAKRMAILGETAWDFGSVGGLFTSLGKAVHQVFG
SQ  SVYTTMFGGVSWMIRILIGFLVLWIGTNSRNTSMAMTCIAVGGITLFLGFTVQADMGCVASWSGKELKCGSGIFVVDNVH
SQ  TWTEQYKFQPESPARLASAILNAHKDGVCGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLTKGKRALTP
SQ  PVSDLKYSWKTWGKAKIFTPEARNSTFLIDGPDTSECPNERRAWNSLEVEDYGFGMFTTNIWMKFREGSSEVCDHRLMSA
SQ  AIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKSYAGPFSQHNYRQGYATQTVG
SQ  PWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLSEKEENMV
SQ  KSQVTAGQGTSETFSMGLLCLTLFVEECLRRRVTRKHMILVVVITLCAIILGGLTWMDLLRALIMLGDTMSGRIGGQIHL
SQ  AIMAVFKMSPGYVLGVFLRKLTSRETALMVIGMAMTTVLSIPHDLMELIDGISLGLILLKIVTQFDNTQVGTLALSLTFI
SQ  RSTMPLVMAWRTIMAVLFVVTLIPLCRTSCLQKQSHWVEITALILGAQALPVYLMTLMKGASRRSWPLNEGIMAVGLVSL
SQ  LGSALLKNDVPLAGPMVAGGLLLAAYVMSGSSADLSLEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEETNMIT
SQ  LLVKLALITVSGLYPLAIPVTMTLWYMWQVKTQRSGALWDVPSPAATKKAALSEGVYRIMQRGLFGKTQVGVGIHMEGVF
SQ  HTMWHVTRGSVICHETGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAV
SQ  TLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPS
SQ  IVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEA
SQ  HFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGATDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIK
SQ  AGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILPDGPERVILAGP
SQ  IPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLKNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKTQAIDGEFRLR
SQ  GEQRKTFVELMRRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPRWLDARVYADPMA
SQ  LKDFKEFASGRKSITLDILTEIASLPTYLSSRAKLALDNIVMLHTTERGGRAYQHALNELPESLETLMLVALLGAMTAGI
SQ  FLFFMQGKGIGKLSMGLITIAVASGLLWVAEIQPQWIAASIILEFFLMVLLIPEPEKQRTPQDNQLIYVILTILTIIGLI
SQ  AANEMGLIEKTKTDFGFYQVKTETTILDVDLRPASAWTLYAVATTILTPMLRHTIENTSANLSLAAIANQAAVLMGLGKG
SQ  WPLHRMDLGVPLLAMGCYSQVNPTTLTASLVMLLVHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYD
SQ  PKFEKQLGQVMLLVLCAGQLLLMRTTWAFCEVLTLATGPILTLWEGNPGRFWNTTIAVSTANIFRGSYLAGAGLAFSLIK
SQ  NAQTPRRGTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKHAVSRGSSKIRWIVERGMVKP
SQ  KGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSN
SQ  PTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGNLVRCPLSRNSTHEMYWVSGASGNIVSSVN
SQ  TTSKMLLNRFTTRHRKPTYEKDVDLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDQENPYRTWAYHGSYEAPS
SQ  TGSASSMVNGVVKLLTKPWDVIPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKPGTRMVMTTTANWLWALLGKKKNPRL
SQ  CTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGKCESCVYNMMGKREKKLGEFGRAKGSRA
SQ  IWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEEIDKKDGDLMYADDTAGWDTRITEDDLQNEELI
SQ  TEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPRGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITQDD
SQ  MQNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFGTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHH
SQ  FHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSR
SQ  TTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMTDKTPVHSWEDIPYLGKREDLWCGSLIGLSSRATWAKNIHTAITQVRN
SQ  LIGKEEYVDYMPVMKRYSAPSESEGVL
//
ID  Q2YHF2;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  408689;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P09866, ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q2YHF2;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:P09866, ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNQRKKVVRPPFNMLKRERNRVSTPQGLVKRFSIGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKTKAIKIL
SQ  TGFRKEIGRMLNILNGRKRSTVTLLCLIPTVMAFHLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCED
SQ  TVTYKCPLLVNTEPEDIDCWCNLTSTWVMYGTCTQNGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWI
SQ  LRNPGFALLAGFMAYMIGQTGIQRTVFFVLMMLVAPSYGMRCIGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTL
SQ  DFELIKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDVVDRGWGNGCGLFGKGGVVTCAKFSC
SQ  SGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDTSNHGVTATITPRSPSVEVELPDYGELSLDCEPRSGIDFNEMILMKM
SQ  EKKTWLVHKQWFLDLPLPWTAGADTSEVHWNHKERMVTFKVPHAKRQDVTVLGSQEGAMHSALTGATEVDSGDGNHMFAG
SQ  HLKCKVRMEKLRIKGMSYTMCSGKFSIDREMAETQHGTTVVKVKYEGTGAPCKVPIEIRDVNKEKVVGRIISSTPFAENT
SQ  NSVTNIELEPPFGDSYIVIGVGDSALTLHWFRKGSSIGKMFESTYRGAKRMAILGETAWDFGSVGGLFTSLGKAVHQVFG
SQ  SVYTTMFGGVSWMVRILIGLLVLWIGTNSRNTPMAMTCIAVGGITLFLGFTVQADMGCVVSWTGKELKCGSGIFVTDNVH
SQ  TWTEQYQFQPESPARLASAILNAHKDGVCGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLVKGKRALTP
SQ  PVNDLKYSWKTWGKAKIFTPEAKNSTFLIDGPDTSECPNERRAWNFLEVEDYGFGMFTTSIWMKFREGSSEVCDHRLMSA
SQ  AIKDQKAVHADMGYWLESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKAYAGPFSQHNYRQGYATQTMG
SQ  PWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLSEREENMV
SQ  KSQVSAGQGSSETFSMGLLCLTLFIEECLRRKVTRKHMILVVVTTFCAIILGGLTWMDLLRAIIMLGDTMLSRVGGQTHL
SQ  AIMIVFKMSPGYVLGVFLRKLTSRETALMVIGMAMTTVFSIPHDLMELIDGISLGLILLKMVTHFDNTQVGTLALSLTFI
SQ  RSTMPLTMAWRTIMAVLFAVTLIPLCRTSCLQKQSHWVEITAIILGAQALPVYLMTLMKGASKRSWPLNEGIMAVGLVSL
SQ  LGSALLKNDVPLAGPMVAGGLLLAAYVMSGSSADLSLERAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEETNMIT
SQ  LLVKLALITVSGLYPLAIPITMTLWYMWQVRTQRSGALWDVPSPATAQKATLTEGVYRIMQRGLLGRTQVGVGIHMEGVF
SQ  HTMWHVTRGSVICHETGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAV
SQ  TLDFKPGTSGSPIINKKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPS
SQ  IVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEA
SQ  HFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGATDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIK
SQ  AGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILTDGPERVILAGP
SQ  IPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLKNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKTQAIDGEFRLR
SQ  GEQRKTFVELMKRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPKWLDARVYADPMA
SQ  LKDFKEFASGRKSITLDILTEIASLPTYLSSRAKLALDNIVMLHTTERGGRAYQHALNELPESLETLMLVALLGAMTAGI
SQ  FLFFMQGKGIGKLSVGLIAIAVASGLLWVAEIQPQWIAASIILEFFLMVLLIPEPEKQRTPQDNQLIYVILAILTIIGLV
SQ  AANEMGLIEKTKADFGFYQVKTETTILDVDLRPASAWTLYAVATTILTPMLRHTIENTSANLSLAAIANQAAVLMGLGKG
SQ  WPLHRMDLGVPLLAMGCYSQVNPTTLTASLVMLLVHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYD
SQ  PKFEKQLGQVMLLVLCAGQLLLMRTTWAFCEVLTLATGPVLTLWEGNPGRFWNTTIAVSTANIFRGSYLAGAGLAFSLIK
SQ  NAQTPRRGTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKHAVSRGSSKIRWIVERGMVKP
SQ  KGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSN
SQ  PTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGSLIRCPLSRNSTHEMYWVSGASGNIVSSVN
SQ  TTSKMLLNRFTTRHRKPTYEKDVDLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDQENPYRTWAYHGSYEAPS
SQ  TGSASSMVNGVVKLLTKPWDVIPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKLGTRVVMTTTANWLWALLGRKKNPRL
SQ  CTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGKCESCVYNMMGKREKKLGEFGRAKGSRA
SQ  IWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEDIDRKDGDLMYADDTAGWDTRITEDDLLNEELI
SQ  TEQMAPHHRILAKAIFKLTYQNKVVKVLRPTPKGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITQDD
SQ  MQNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFSTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHH
SQ  FHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLKETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSR
SQ  TTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMTDKTPVHSWEDIPYLGKREDLWCGSLIGLSSRATWAKNIHTAITQVRN
SQ  LIGKEEYVDYMPVMRRYSALSESEGVL
//
ID  Q58HT7;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  408686;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P09866, ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q58HT7;
DR  PDB: 4AM0;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:P09866, ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNQRKKVVRPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKIL
SQ  TGFRKEIGRMLNILNGRKRSTMTLLCLIPTAMAFHLSTRDGEPLMIVARHERGRPLLFKTTEGINKCTLIAMDLGEMCED
SQ  TVTYECPLLVNTEPEDIDCWCNLTSAWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWI
SQ  LRNPGFALLAGFMAYMIGQTGIQRTVFFVLMMLVAPSYGMRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTL
SQ  DFELIKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDVVDRGWGNGCGLFGKGGVVTCAKFSC
SQ  SGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDIPNHGVTATITPRSPSVEVKLPDYGELTLDCEPRSGIDFNEMILMKM
SQ  KKKTWLVHKQWFLDLPLPWAAGADTSEVHWNYKERMVTFKVPHAKRQDVTVLGSQEGAMHSALTGATEVDSGDGNHMFAG
SQ  HLKCKVRMEKLRIKGMSYTMCSGKFSIDKEMAETQHGTTVVKVKYEGAGAPCKVPIEIRDVNKEKVVGRIISSTPFAEYT
SQ  NSVTNIELEPPFGDSYIVIGVGDSALTLHWFRKGSSIGKMLESTYRGAKRMAILGETAWDFGSVGGLLTSLGKAVHQVFG
SQ  SVYTTMFGGVSWMVRILIGFLVLWIGTNSRNTSMAMTCIAVGGITLFLGFTVHADTGCAVSWSGKELKCGSGIFVIDNVH
SQ  TWTEQYKFQPESPARLASAILNAHEDGVCGIRSTTRLENIMWKQITNELNYVLWEGGHDLTVVAGDVKGVLSKGKRALAP
SQ  PVNDLKYSWKTWGKAKIFTPEAKNSTFLIDGPDTSECPNERRAWNFLEVEDYGFGMFTTNIWMKFREGSSEVCDHRLMSA
SQ  AIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKAYAGPFSQHNYRQGYATQTVG
SQ  PWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLSEKEENMV
SQ  KSQVSAGQGTSETFSMGLLCLTLFVEECLRRRVTRKHMILVVVTTLCAIILGGLTWMDLLRALIMLGDTMSGRMGGQIHL
SQ  AIMAVFKMSPGYVLGIFLRKLTSRETALMVIGMAMTTVLSIPHDLMEFIDGISLGLILLKMVTHFDNTQVGTLALSLTFI
SQ  RSTMPLVMAWRTIMAVLFVVTLIPLCRTSCLQKQSHWVEITALILGAQALPVYLMTLMKGASKRSWPLNEGIMAVGLVSL
SQ  LGSALLKNDVPLAGPMVAGGLLLAAYVMSGSSADLSLEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDIEETNMIT
SQ  LLVKLALITVSGLYPLAIPVTMTLWYMWQVKTQRSGALWDVPSPAAAQKATLTEGVYRIMQRGLFGKTQVGVGIHMEGVF
SQ  HTMWHVTRGSVICHETGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAV
SQ  TLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERTGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPS
SQ  IVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEA
SQ  HFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGATDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIK
SQ  AGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVISTDGPERVILAGP
SQ  IPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLKNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKNQAIDGEFRLR
SQ  GEQRKTFVELMRRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPKWLDARVYADPMA
SQ  LKDFKEFASGRKSITLDILTEIASLPTYLSSRAKLALDNIVMLHTTERGGKAYQHALNELPESLETLMLVALLGAMTAGI
SQ  FLFFMQGKGIGKLSMGLIAIAVASGLLWVAEIQPQWIAASIILEFFLMVLLIPEPEKQRTPQDNQLIYVILTILTIIGLI
SQ  AANEMGLIEKTKTDFGFYQVKTETTILDVDLRPASAWTLYAVATTILTPMLRHTIENTSANLSLAAIANQAAVLMGLGKG
SQ  WPLHRMDLGVPLLAMGCYSQVNPTTLIASLVMLLVHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYD
SQ  PKFEKQLGQVMLLVLCAGQLLLMRTTWAFCEVLTLATGPVLTLWEGNPGRFWNTTIAVSTANIFRGSYLAGAGLAFSLIK
SQ  NAQTPRRGTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKHAVSRGSSKIRWIVERGMVKP
SQ  KGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSN
SQ  PTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGSLVRCPLSRNSTHEMYWVSGVSGNIVSSVN
SQ  TTSKMLLNRFTTRHRKPTYEKDVDLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDQENPYRTWAYHGSYEAPS
SQ  TGSASSMVNGVVKLLTKPWDVIPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKPGTRMVMTTTANWLWALLGKKKNPRL
SQ  CTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGKCESCVYNMMGKREKKLGEFGRAKGSRA
SQ  IWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEDIDKKDGDLIYADDTAGWDTRITEDDLLNEELI
SQ  TEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPKGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITQDD
SQ  MHNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFSTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHH
SQ  FHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSR
SQ  TTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMTDKTPVHSWEDIPYLGKREDLWCGSLIGLSSRATWAKNIHTAITQVRN
SQ  LIGKEEYVDYMPVMKRYSAPFESEGVL
//
ID  Q5UCB8;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  408687;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P09866, ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q5UCB8;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:P09866, ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNQRKKVVRPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKIL
SQ  IGFRKEIGRMLNILNGRKRSTMTLLCLIPTVMAFHLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCED
SQ  TVTYKCPLLVNTEPEDIDCWCNLTSTWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWI
SQ  LRNPGFALLAGFMAYMIGQTGIQRTVFFVLMMLVAPSYGMRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTL
SQ  DFELTKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDVVDRGWGNGCGLFGKGGVVTCAKFSC
SQ  SGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDTSNHGVTATITPRSPSVEVKLPDYGELTLDCEPRSGIDFNEMILMEM
SQ  KKKTWLVHKQWFLDLPLPWTAGADTSEVHWNYKERMVTFKVPHAKRQDVTVLGSQEGAMHSALAGATEVDSGDGNHMFAG
SQ  HLKCKVRMEKLRIKGMSYTMCSGKFSIDKEMAETQHGTTVVKVKYEGAGAPCKVPIEIRDVNKEKVVGRVISSTPLAENT
SQ  NSVTNIELEPPFGDSYIVIGVGNSALTLHWFRKGSSIGKMFESTYRGAKRMAILGETAWDFGSVGGLFTSLGKAVHQVFG
SQ  SVYTTMFGGVSWMVRILIGFLVLWIGTNSRNTSMAMTCIAVGGITLFLGFTVQADMGCVVSWSGKELKCGSGIFVADNVH
SQ  TWTEQYKFQPESPARLASAILNAHKDGVCGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLTKGKRALTP
SQ  PVNDLKYSWKTWGKAKIFTPEARNSTFLIDGPDTSECPNERRAWNFLEVEDYGFGMFTTNIWMKFREGSSEVCDHRLMSA
SQ  AIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKSYAGPFSQHNYRQGYATQTVG
SQ  PWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLSEKEENMV
SQ  KSQVTAGQGTSETFSMGLLCLTLFMEECLRRRVTRKHMILVVVITLCAIILGGLTWMDLLRALIMLGDTMSGRIGGQVHL
SQ  AIMAVFKMSPGYVLGVFLRKLTSRETALMVIGMAMTTVLSIPHDLMELIDGISLGLILLKIVTQFDNTQVGTLALSLTFI
SQ  RSTMPLVMAWRTIMAVLFVVTLIPLCRTSCLQKQSHWVEITALILGAQALPVYLMTLMKGASRRSWPLNEGIMAVGLVSL
SQ  LGSALLKNDVPLAGPMVAGGLLLAAYVMSGSSADLSLEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEETNMIT
SQ  LLVKLALITVSGLYPLAIPVTMTLWYMWQVKTQRSGALWDVPSPAATQKAALSEGVYRIMQRGLFGKTQVGVGIHIEGVF
SQ  HTMWHVTRGSVICHETGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAV
SQ  TLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPS
SQ  IVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEA
SQ  HFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGTTDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIK
SQ  AGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILPDGPERVILAGP
SQ  IPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLKNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKTQAIDGEFRLR
SQ  GEQRKTFVELMRRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPKWLDARVYADPMA
SQ  LKDFKEFASGRKSITLDILTEIASLPTYLSSRAKLALDNIVMLHTTEKGGRAYQHALNELPESLETLMLVALLGAMTAGT
SQ  FLFFMQGKGIGKLSMGLITIAVASGLLWVAELQPQWIAASIILEFFLMVLLIPEPEKQRTPQDNQLIYVILTILTIIGLI
SQ  AANEMGLIEKTKTDFGFYQVKTETTILDVDLRPASAWTLYAVATTILTPMLRHTIENTSANLSLAAIANQAAVLMGLGKG
SQ  WPLHRVDLGVPLLAMGCYSQVNPTTLTASLVMLLVHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYD
SQ  PKFEKQLGQVMLLVLCAGQLLLMRTTWAFCEVLTLATGPILTLWEGNPGRFWNTTIAVSTANIFRGSYLAGAGLAFSLIK
SQ  NAQTPRRGTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGIIEVDRTEAKSALKDGSKIKHAVSRGSSKIRWIVERGMVKP
SQ  KGKVVDLGCGRGGWSYYMATLKNVTEVRGFTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSN
SQ  PTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGNLVRCPLSRNSTHEMYWVSGASGNIVSSVN
SQ  TTSKMLLNRFTTRHRKPTYEKDVDLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDQENPYRTWAYHGSYEAPS
SQ  TGSASSMVNGVVKLLTKPWDVIPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKPGTRMVMTTTANWLWTLLGKKKNPRL
SQ  CTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGRCESCVYNMMGKREKKLGEFGRAKGSRA
SQ  IWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEDIDKKDGDLMYADDTAGWDTRITEDDLQNEELI
SQ  TEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPRGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITQDD
SQ  MQNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFSTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHH
SQ  FHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSR
SQ  TTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMTDKTPVHSWEDVPYLGKREDLWCGSLIGLSSRATWAKNIHTAITQVRN
SQ  LIGKEEYVDYMPVMKRYSAPSESEGVL
//
ID  Q2YHF0;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  408688;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. Interacts with host MAVS in the mitochondrion-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P09866, ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4 serotypes. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q2YHF0;
DR  PDB: 2JLQ;
DR  PDB: 2JLR;
DR  PDB: 2JLS;
DR  PDB: 2JLU;
DR  PDB: 2JLV;
DR  PDB: 2JLW;
DR  PDB: 2JLX;
DR  PDB: 2JLY;
DR  PDB: 2JLZ;
DR  PDB: 2WHX;
DR  PDB: 2WZQ;
DR  PDB: 3UYP;
DR  PDB: 5YVV;
DR  PDB: 5YVW;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway (By similarity). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:P09866, ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005216;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNQRKKVARPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKIL
SQ  TGFRKEIGRMLNILNGRKRSTITLLCLIPTVMAFHLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCED
SQ  TVTYKCPLLVNTEPEDIDCWCNLTSAWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWI
SQ  LRNPGFALLAGFMAYMIGQTGIQRTVFFILMMLVAPSYGMRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTL
SQ  DFELIKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDMVDRGWGNGCGLFGKGGVVTCAKFSC
SQ  SGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDTSNHGVTATITPRSPSVEVKLPDYGELTLDCEPRSGIDFNEMILMKM
SQ  KTKTWLVHKQWFLDLPLPWTAGADTLEVHWNHKERMVTFKVPHAKRQDVTVLGSQEGAMHSALAGATEVDSGDGNHMFAG
SQ  HLKCKVRMEKLRIKGMSYTMCSGKFSIDKEMAETQHGTTVVKVKYEGTGAPCKVPIEIRDVNKEKVVGRIISSTPFAENT
SQ  NSVTNIELEPPFGDSYIVIGVGDSALTLHWFRKGSSIGKMFESTYRGAKRMAILGETAWDFGSVGGLLTSLGKAVHQVFG
SQ  SVYTTMFGGVSWMVRILIGLLVLWIGTNSRNTSMAMSCIAVGGITLFLGFTVHADMGCAVSWSGKELKCGSGIFVIDNVH
SQ  TWTEQYKFQPESPARLASAILNAHKDGVCGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLSKGKRALAP
SQ  PVNDLKYSWKTWGKAKIFTPETRNSTFLVDGPDTSECPNERRAWNFLEVEDYGFGMFTTNIWMKFREGSSEVCDHRLMSA
SQ  AIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKAYAGPISQHNYRQGYATQTVG
SQ  PWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLNEKEENMV
SQ  KSQVSAGQGTSETFSMGLLCLTLFVEECLRRRVTRKHMILVVVTTLCAIILGGLTWMDLLRALIMLGDTMSGRMGGQIHL
SQ  AIMAVFKMSPGYVLGIFLRKLTSRETALMVIGMAMTTVLSIPHDLMEFIDGISLGLILLKMVTHFDNTQVGTLALSLTFI
SQ  KSTMPLVMAWRTIMAVLFVVTLIPLCRTSCLQKQSHWVEITALILGAQALPVYLMTLMKGASKRSWPLNEGIMAVGLVSL
SQ  LGSALLKNDVPLAGPMVAGGLLLAAYVMSGSSADLSLEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEETNMIT
SQ  LLVKLALITVSGLYPLAIPVTMTLWYMWQVKTQRSGALWDVPSPAAAQKATLTEGVYRIMQRGLFGKTQVGVGIHMEGVF
SQ  HTMWHVTRGSVICHESGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAV
SQ  TLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPS
SQ  IVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEA
SQ  HFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGTTDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIK
SQ  AGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILTDGPERVILAGP
SQ  IPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLRNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKTQAIDGEFRLR
SQ  GEQRKTFVELMRRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPKWLDARVYADPMA
SQ  LKDFKEFASGRKSITLDILTEIASLPTYLSSRAKLALDNIVMLHTTERGGKAYQHALNELPESLETLMLVALLGAMTAGI
SQ  FLFFMQGKGIGKLSMGLIAIAVASGLLWVAEIQPQWIAASIILEFFLMVLLVPEPEKQRTPQDNQLIYVILTILTIIALV
SQ  AANEMGLIEKTKTDFGFYQAKTETTILDVDLRPASAWTLYAVATTILTPMLRHTIENTSANLSLAAIANQAAVLMGLGKG
SQ  WPLHRMDLGVPLLAMGCYSQVNPTTLTASLVMLLVHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYD
SQ  PKFEKQLGQVMLLVLCAGQLLLMRTTWAFCEVLTLATGPILTLWEGNPGRFWNTTIAVSTANIFRGSYLAGAGLAFSLIK
SQ  NAQTPRRGTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKYAVSRGTSKIRWIVERGMVKP
SQ  KGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSN
SQ  PTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGSLVRCPLSRNSTHEMYWVSGVSGNIVSSVN
SQ  TTSKMLLNRFTTRHRKPTYEKDADLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDHENPYRTWAYHGSYEAPS
SQ  TGSASSMVNGVVKLLTKPWDVVPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKPGTRVVMTTTANWLWALLGRKKNPRL
SQ  CTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGKCESCVYNMMGKREKKLGEFGRAKGSRA
SQ  IWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEDIDKKDGDLIYADDTAGWDTRITEDDLLNEELI
SQ  TEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPKGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITRDD
SQ  MHNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFSTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHH
SQ  FHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSR
SQ  TTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMIDKTPVHSWEDIPYLGKREDLWCGSLIGLSSRATWAKNIQTAITQVRN
SQ  LIGKEEYVDYMPVMKRYSAHFESEGVL
//
ID  C8XPB2;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  64296;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: C8XPB2;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0046718;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPVRPRNKPKGVNVMAAGKVAQKIKNKLKSKAKAIGNISKGLRGFILFILAQIFWARKLTPRVRTMWKKVDKAKATRVLK
SQ  GIRNIATQLITGLAGRKKRRSMTHGIILSLGVTMVIGASLHHHGGRYLLNVTHADLGKTFTIGSGNCTANIVEAGSWCSD
SQ  SMEYECVTLAEAEEPDDIDCWCRGVERVRVTYGRCKNGLDSRRSRRAAVITAHIDKGLTTRQEKWLSTSMGERQIQRIER
SQ  WMMRNPFYAAISLLLAWWVGSDIKQKVLIAFLVLAIGPAYSTHCVGIPKRDFVQGVQGNTWVNLVLDQGSCVTLSSDNKP
SQ  SVDIWLDSIFISSPVLVRRVSHTATISDTKVQTACPTNGEAKLEEEASAEYECKKTYSDRGWGNGCGLFGKGSIVACAKY
SQ  TSTGHMDVYEIDSTKIEYVTKAQVHAGMKHDDTTMVKEVKFEPTTGSMDVEFTGYGTLGLECHVQTMVDMANYYLVVMGQ
SQ  EAWLVHKQWVEDITLPWKIGEGGFWRDKHYMVEFTEPHATTMTVMVLGAQEGALRTALAGAMVVTYTDSSGTKKFSLKGG
SQ  HVSCKARMNGLVLKGSTYTMCKGGFSFVKTPTDTGHGTAVMQVKVSKGTPCRIPVQAVDSSNGGTNRATLITANPIAATT
SQ  EDEVMIELSPPYGESYIMIGTGDDKLTYHWHKSGSTIGSLFTETYKGAQRMAIIGDDAWDFSSSSNFFNSIGKALHTVFG
SQ  NVFHSIFGGLSWITKIILGGMFLWLGVNSRNQTMCMVLMAVGGILLFMTLGVSGEVGCSLDIKRRELKCGDGLFLFNDVN
SQ  DWTHKYKFHPEDPKLLASLIKKSHQEGRCGLSSVNEVEHRMWNSIKTEINAMFEENGVDLSVVVKDSKLHYKMGSHAFPK
SQ  VEEGLSLGWKNWGKSLVFEPKQSNVSFIIDGTSEDCPFTNRIWNAFVVEEFGIGMFTTNVFLTHKVDFTKQCDASLLGAG
SQ  VKGDVAVHGDPTLWMESRKENGTWQLHTIQMNGLRECFWPQTHTIHGSSVMESAMFLPKQYGGPVSHHNHYTGYAVQTAG
SQ  PWNVQPLIVKRETCPGTQVRVDEQCRDRGNSVRSTTSEGKIIPEWCCRSCTLPPVSFWGPDSCWYAMEIRPQNVHEEHLV
SQ  RSWASAGTGMAESSLGLVALFLFTDIFARKRMTRKFMVIGCLGVLSVMIVGGFTALDLIRYIIVVGQHFASMNHGGDVAY
SQ  LAIIAVGKLRPGLLMMYSFKAAWSPKERVMVALGLLVFQAVLGDFVHTGLWEWADAAGMCILIIQGMATRKEKTYIMPIL
SQ  ALLTPLSMEIIRKTGIFACVGLLGLSLWRGGDTTMRKGMPLLAGAATAASGLTRASLSVVFILCATAASRRSWPIGEIMA
SQ  IVGIVGTGFGMAVNDQASLAGPMLVFGLIMIVYATLGRADGLTLKRVGDITWEEEAVHSGSSTRYDVTLNEAGEFKLVHE
SQ  EPVVWSHVVFLVVALIAASVHPIALVVVTIIWTYGKKHLRGGVLWDIPIAPPVEEAEPLEDGVYAILQSGLMGKAQAGVG
SQ  VAQEGVFHTMWHVTRGGFLMVGGKRLTPHWASVKRDLICYGGNWKLDGKWDGVEEVQLIAVAPGKAPTNVQTKPGVFRMA
SQ  DGTEIGAVALDYPSGTSGSPIVNEKGQVIGLYGNGIVIGGSGYVSSIAQIAGGEGVTEEPLLDTATMLRKGKLTVLDYHP
SQ  GAGKTRIFLPYILKECVRRKLRTLVLAPTRVVLSEMREALRDVAVKYHTQAFQAAGTGRELVDAMCHATLSHRMLESSRS
SQ  VNWEVIIMDEAHYMDPTSIAARGWAAHKANNHESAVIFMTATPPGSANEFPESNGEIEDLRRDIPTEPWNKGHEWILEDR
SQ  RPTVWFLPSIRAANNIAACLRRSERSVVVLNRQTFETVYPTIKTKKPDFILATDIAEMGANLGVERVIDCRTSYKPVLTT
SQ  DGRVVIKGPLRIPASAAAQRRGRVGRCKDRDTDSYVYSEETSEDNGHYVCWTEASMLLDNMEVKGGMVAPLYDVEAQKTE
SQ  MVPGEARLRDDQRKVFRTLIKRYDLPVWVSWQVAKSGLMLEDRKWCFDGDDENTILNDNGEKILARSPGGQRKFLCPRWN
SQ  DSRLYYDNASLMSFLAFAEGRRSYLGVWHAVQMAPLKLGEKLTESLDTMVMLMRSEEGTRAYKLASTNAPEAVTILLMTG
SQ  IVVACTLGVGLAFMWPKGVDKMSMGMITMSIAGYLMLQGGLTPVQVASVLLIFFIFMVVLIPEAGTQRSINDNKTLYVLL
SQ  GVALLIGAITANEMGYLEKTKRDLLGERVQNEWKLELPMFDLRPGAAWSIYVGLATLVMPVLDHWIRTEYGSLSLTGIAQ
SQ  QASILQAMDKGVPFFKLNMSVIVLLVSVWNNFSMLSVLCGVGLLGVHCAFVLPGLRAQAAKQAQRRVYHGVAKNPVVDGQ
SQ  TTAEIETAPEMPPLYEKKLALVLLGVVAIANGVMVRSAFSMAETVVLLSAAVGPLLEGNTSAIWNGPMAVAMAGIMRGNY
SQ  YAGIGLAYNLWILQSPKRGRSTTMTLGELWKRQLNLMGKREFELYKITDIHEVDRSQAQAVMKAGIDNVGISVSRGTSKL
SQ  KWMVDRNYVEPLGRVVDLGCGRGGWSYLCAASKRVSSVKAYTLGITGHEKPVNVQSLGWNIIKFKDKTDVFKMEPHACET
SQ  LLCDIGESSSNPLVEMERTLKVIDNVERWMSPTTESYCFKVLAPYRPEVIERLERFQLKYGGGIVRVPFSRNSTHEMYYV
SQ  SGVKNNLTHMVSCVSRLLLRRMTHPDGRCKVEADVVFPTGTRNVASDLGPMDLSKVKDRVNRLRSEQGTWFQDDSHPYRT
SQ  WHYLGSYVAKQSGSAATMVNGVVKMLSMPWDRIENVTQLAMTDTTPYGQQRVFKEKVDTRAPPPPPGTRAIMEVVNKWMF
SQ  DFLAREKAPRICTKEEFINKVRSNAALGNMLEEQDGWKDAATAVQDPRFWALVDRERQVHLEGRCETCIYNMMGKREKKP
SQ  AEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFGRENSLAGVEGVGLQYLGYVVKNVWEKSNGIMYADDTAGWDTRV
SQ  TEADLDDEQYLLSKMEGYHKKLASAVMNMTYKYKVVKVPRPGPGGKVFMDVIARQDQRGSGQVVTYPLNTGTNMKVQLIR
SQ  MAEGEGVISRHDIERVTIKTLNALRVWLAENGAERLSRMAVSGDDCVVAPLDERFGLALHHLNAMSKIRKDIDDWTESIP
SQ  WRSWESVPFCSHHFHQLFLKDGRSIVVPCRDQDELVGRARVSPGNGWKLKETACLSKAYAQMWLLMYFHKRDLRLMGNAI
SQ  CSSVPAHWVPTGRTTWSIHAHNEWISSERMLDVWNKVWIVDNPHMPDKTCIDDWRDVPYLPKSQDRLCGSLIGITARASW
SQ  AENIRAVVNKIRGMIGNEVYSDHLSVMGRYTYSVQEVGTVL
//
ID  Q69422;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  2847087;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [p13]: Host endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q69422;
DR  UNIPROT: Q6QLR5;
DR  UNIPROT: Q6QLR6;
DR  UNIPROT: Q6QLR7;
DR  UNIPROT: Q6QLR8;
DR  UNIPROT: Q6QLR9;
DR  UNIPROT: Q6QLS0;
DR  UNIPROT: Q8JKE4;
DR  UNIPROT: Q999T0;
DR  UNIPROT: Q9QEW5;
DR  PDB: 2LZP;
DR  PDB: 2LZQ;
DR  PDB: 2MKB;
DR  Pfam: PF07652;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Probably affects various cell signaling pathways, host immunity and lipid metabolism (Probable). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). {ECO:0000250|UniProtKB:P27958}. [p13]: May function as a multimeric ion channel protein (viroporin). {ECO:0000269|PubMed:16492760}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (PubMed:10497107). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (PubMed:17093192). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:10497107, ECO:0000269|PubMed:17093192}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly. {ECO:0000250|UniProtKB:Q99IB8}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0032993;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0003677;
GO  GO:1990814;
GO  GO:0005216;
GO  GO:0140691;
GO  GO:0003724;
GO  GO:0033592;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0043489;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0046718;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPVISTQTSPVPAPRTRKNKQTQASYPVSIKTSVERGQRAKRKVQRDARPRNYKIAGIHDGLQTLAQAALPAHGWGRQDP
SQ  RHKSRNLGILLDYPLGWIGDVTTHTPLVGPLVAGAVVRPVCQIVRLLEDGVNWATGWFGVHLFVVCLLSLACPCSGARVT
SQ  DPDTNTTILTNCCQRNQVIYCSPSTCLHEPGCVICADECWVPANPYISHPSNWTGTDSFLADHIDFVMGALVTCDALDIG
SQ  ELCGACVLVGDWLVRHWLIHIDLNETGTCYLEVPTGIDPGFLGFIGWMAGKVEAVIFLTKLASQVPYAIATMFSSVHYLA
SQ  VGALIYYASRGKWYQLLLALMLYIEATSGNPIRVPTGCSIAEFCSPLMIPCPCHSYLSENVSEVICYSPKWTRPVTLEYN
SQ  NSISWYPYTIPGARGCMVKFKNNTWGCCRIRNVPSYCTMGTDAVWNDTRNTYEACGVTPWLTTAWHNGSALKLAILQYPG
SQ  SKEMFKPHNWMSGHLYFEGSDTPIVYFYDPVNSTLLPPERWARLPGTPPVVRGSWLQVPQGFYSDVKDLATGLITKDKAW
SQ  KNYQVLYSATGALSLTGVTTKAVVLILLGLCGSKYLILAYLCYLSLCFGRASGYPLRPVLPSQSYLQAGWDVLSKAQVAP
SQ  FALIFFICCYLRCRLRYAALLGFVPMAAGLPLTFFVAAAAAQPDYDWWVRLLVAGLVLWAGRDRGPRIALLVGPWPLVAL
SQ  LTLLHLATPASAFDTEIIGGLTIPPVVALVVMSRFGFFAHLLPRCALVNSYLWQRWENWFWNVTLRPERFLLVLVCFPGA
SQ  TYDTLVTFCVCHVALLCLTSSAASFFGTDSRVRAHRMLVRLGKCHAWYSHYVLKFFLLVFGENGVFFYKHLHGDVLPNDF
SQ  ASKLPLQEPFFPFEGKARVYRNEGRRLACGDTVDGLPVVARLGDLVFAGLAMPPDGWAITAPFTLQCLSERGTLSAMAVV
SQ  MTGIDPRTWTGTIFRLGSLATSYMGFVCDNVLYTAHHGSKGRRLAHPTGSIHPITVDAANDQDIYQPPCGAGSLTRCSCG
SQ  ETKGYLVTRLGSLVEVNKSDDPYWCVCGALPMAVAKGSSGAPILCSSGHVIGMFTAARNSGGSVSQIRVRPLVCAGYHPQ
SQ  YTAHATLDTKPTVPNEYSVQILIAPTGSGKSTKLPLSYMQEKYEVLVLNPSVATTASMPKYMHATYGVNPNCYFNGKCTN
SQ  TGASLTYSTYGMYLTGACSRNYDVIICDECHATDATTVLGIGKVLTEAPSKNVRLVVLATATPPGVIPTPHANITEIQLT
SQ  DEGTIPFHGKKIKEENLKKGRHLIFEATKKHCDELANELARKGITAVSYYRGCDISKIPEGDCVVVATDALCTGYTGDFD
SQ  SVYDCSLMVEGTCHVDLDPTFTMGVRVCGVSAIVKGQRRGRTGRGRAGIYYYVDGSCTPSGMVPECNIVEAFDAAKAWYG
SQ  LSSTEAQTILDTYRTQPGLPAIGANLDEWADLFSMVNPEPSFVNTAKRTADNYVLLTAAQLQLCHQYGYAAPNDAPRWQG
SQ  ARLGKKPCGVLWRLDGADACPGPEPSEVTRYQMCFTEVNTSGTAALAVGVGVAMAYLAIDTFGATCVRRCWSITSVPTGA
SQ  TVAPVVDEEEIVEECASFIPLEAMVAAIDKLKSTITTTSPFTLETALEKLNTFLGPHAATILAIIEYCCGLVTLPDNPFA
SQ  SCVFAFIAGITTPLPHKIKMFLSLFGGAIASKLTDARGALAFMMAGAAGTALGTWTSVGFVFDMLGGYAAASSTACLTFK
SQ  CLMGEWPTMDQLAGLVYSAFNPAAGVVGVLSACAMFALTTAGPDHWPNRLLTMLARSNTVCNEYFIATRDIRRKILGILE
SQ  ASTPWSVISACIRWLHTPTEDDCGLIAWGLEIWQYVCNFFVICFNVLKAGVQSMVNIPGCPFYSCQKGYKGPWIGSGMLQ
SQ  ARCPCGAELIFSVENGFAKLYKGPRTCSNYWRGAVPVNARLCGSARPDPTDWTSLVVNYGVRDYCKYEKLGDHIFVTAVS
SQ  SPNVCFTQVPPTLRAAVAVDGVQVQCYLGEPKTPWTTSACCYGPDGKGKTVKLPFRVDGHTPGVRMQLNLRDALETNDCN
SQ  SINNTPSDEAAVSALVFKQELRRTNQLLEAISAGVDTTKLPAPSIEEVVVRKRQFRARTGSLTLPPPPRSVPGVSCPESL
SQ  QRSDPLEGPSNLPSSPPVLQLAMPMPLLGAGECNPFTAIGCAMTETGGGPDDLPSYPPKKEVSEWSDGSWSTTTTASSYV
SQ  TGPPYPKIRGKDSTQSAPAKRPTKKKLGKSEFSCSMSYTWTDVISFKTASKVLSATRAITSGFLKQRSLVYVTEPRDAEL
SQ  RKQKVTINRQPLFPPSYHKQVRLAKEKASKVVGVMWDYDEVAAHTPSKSAKSHITGLRGTDVRSGAARKAVLDLQKCVEA
SQ  GEIPSHYRQTVIVPKEEVFVKTPQKPTKKPPRLISYPHLEMRCVEKMYYGQVAPDVVKAVMGDAYGFVDPRTRVKRLLSM
SQ  WSPDAVGATCDTVCFDSTITPEDIMVETDIYSAAKLSDQHRAGIHTIARQLYAGGPMIAYDGREIGYRRCRSSGVYTTSS
SQ  SNSLTCWLKVNAAAEQAGMKNPRFLICGDDCTVIWKSAGADADKQAMRVFASWMKVMGAPQDCVPQPKYSLEELTSCSSN
SQ  VTSGITKSGKPYYFLTRDPRIPLGRCSAEGLGYNPSAAWIGYLIHHYPCLWVSRVLAVHFMEQMLFEDKLPETVTFDWYG
SQ  KNYTVPVEDLPSIIAGVHGIEAFSVVRYTNAEILRVSQSLTDMTMPPLRAWRKKARAVLASAKRRGGAHAKLARFLLWHA
SQ  TSRPLPDLDKTSVARYTTFNYCDVYSPEGDVFVTPQRRLQKFLVKYLAVIVFALGLIAVGLAIS
//
ID  P26664;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  11104;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:7491770}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000269|PubMed:15254168}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99IB8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q99IB8}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:Q99IB8}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:12082096}; Multi-pass membrane protein {ECO:0000269|PubMed:12082096}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000305}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26662}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P26662}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:P26662}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: P26664;
DR  UNIPROT: Q9IFE5;
DR  PDB: 1RTL;
DR  PDB: 2A4G;
DR  PDB: 2GVF;
DR  PDB: 3EYD;
DR  PDB: 3HKW;
DR  PDB: 3KN2;
DR  PDB: 3QGH;
DR  PDB: 3QGI;
DR  PDB: 3RC4;
DR  PDB: 3RC5;
DR  PDB: 3SU4;
DR  PDB: 6MVO;
DR  PDB: 6N4N;
DR  PDB: 6VDO;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (PubMed:8533458). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (PubMed:9110985). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (PubMed:9524287). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (PubMed:9811706). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:8533458, ECO:0000269|PubMed:9110985, ECO:0000269|PubMed:9524287, ECO:0000269|PubMed:9811706, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (PubMed:10390359, PubMed:11152499). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:10390359, ECO:0000269|PubMed:11152499}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (PubMed:15784895). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (PubMed:9143277). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:15784895, ECO:0000269|PubMed:9143277}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: P42224; IntAct: EBI-6941441; Score: 0.52
DE  Interaction: P07900; IntAct: EBI-7017290; Score: 0.40
DE  Interaction: Q91XE4; IntAct: EBI-8066992; Score: 0.56
DE  Interaction: O00571; IntAct: EBI-9209770; Score: 0.54
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQKKNKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRTWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSTGLYHVTNDCPNSSIVYEAADAILHTPGCVPCVREGNASRCWV
SQ  AMTPTVATRDGKLPATQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRRHWTTQGCNCSIYPGHITGHRMAW
SQ  DMMMNWSPTTALVMAQLLRIPQAILDMIAGAHWGVLAGIAYFSMVGNWAKVLVVLLLFAGVDAETHVTGGSAGHTVSGFV
SQ  SLLAPGAKQNVQLINTNGSWHLNSTALNCNDSLNTGWLAGLFYHHKFNSSGCPERLASCRPLTDFDQGWGPISYANGSGP
SQ  DQRPYCWHYPPKPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGENDTDVFVLNNTRPPLGNWFGCTWMNSTGF
SQ  TKVCGAPPCVIGGAGNNTLHCPTDCFRKHPDATYSRCGSGPWITPRCLVDYPYRLWHYPCTINYTIFKIRMYVGGVEHRL
SQ  EAACNWTRGERCDLEDRDRSELSPLLLTTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVV
SQ  LLFLLLADARVCSCLWMMLLISQAEAALENLVILNAASLAGTHGLVSFLVFFCFAWYLKGKWVPGAVYTFYGMWPLLLLL
SQ  LALPQRAYALDTEVAASCGGVVLVGLMALTLSPYYKRYISWCLWWLQYFLTRVEAQLHVWIPPLNVRGGRDAVILLMCAV
SQ  HPTLVFDITKLLLAVFGPLWILQASLLKVPYFVRVQGLLRFCALARKMIGGHYVQMVIIKLGALTGTYVYNHLTPLRDWA
SQ  HNGLRDLAVAVEPVVFSQMETKLITWGADTAACGDIINGLPVSARRGREILLGPADGMVSKGWRLLAPITAYAQQTRGLL
SQ  GCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSL
SQ  TPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVEN
SQ  LETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRT
SQ  GVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHP
SQ  NIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDAL
SQ  MTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCEC
SQ  YDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAP
SQ  PPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCV
SQ  VIVGRVVLSGKPAIIPDREVLYREFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTASRQAEVIAPAVQTNWQKLETF
SQ  WAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTSQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAAIG
SQ  SVGLGKVLIDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPCSGSWLRDIWDWICEVLSDFKTWLKAKLM
SQ  PQLPGIPFVSCQRGYKGVWRVDGIMHTRCHCGAEITGHVKNGTMRIVGPRTCRNMWSGTFPINAYTTGPCTPLPAPNYTF
SQ  ALWRVSAEEYVEIRQVGDFHYVTGMTTDNLKCPCQVPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSVASSSASQLSAPSLKATCTANHDSPDAELIEANLLWRQEMGGN
SQ  ITRVESENKVVILDSFDPLVAEEDEREISVPAEILRKSRRFAQALPVWARPDYNPPLVETWKKPDYEPPVVHGCPLPPPK
SQ  SPPVPPPRKKRTVVLTESTLSTALAELATRSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDAESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSSEANAEDVVCCSMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRQKKVTFDRLQVL
SQ  DSHYQDVLKEVKAAASKVKANLLSVEEACSLTPPHSAKSKFGYGAKDVRCHARKAVTHINSVWKDLLEDNVTPIDTTIMA
SQ  KNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVTKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGFSYD
SQ  TRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCRASGVLTTSCGNTLTCYIKAR
SQ  AACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKR
SQ  VYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALDCEIYGACYSIEPLDLP
SQ  PIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRARSVRARLLARGGRAAICGKYLFNWAVRTKLKLTPIA
SQ  AAGQLDLSGWFTAGYSGGDIYHSVSHARPRWIWFCLLLLAAGVGIYLLPNR
//
ID  Q5I2N3;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356391;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q5I2N3;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTLPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQPQGRHWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPHWGPNDPRRRSRNLGKVIDTLTCGFADLMGYIPVVGAPLGGVAAALAHGVRAIED
SQ  GINYATGNLPGCSFSIFLLALLSCLTTPASALTYGNSSGLYHLTNDCPNSSIVLEADAMILHLPGCLPCVKVGNQSTCWH
SQ  AVSPTLAIPNASTPATGFRRHVDLLAGAAVVCSSLYIGDLCGSLFLAGQLFTFQPRRHWTVQECNCSIYTGHVTGHRMAW
SQ  DMMMSWSPTTTLVLSSILRVPEICASVIFGGHWGILLAVAYFGMAGNWLKVLAVLFLFAGVEATTTVGHGVARTTAGITG
SQ  LFSPGASQNLQLIKNGSSWHINRTALNCNDSLQTGFLASLFYVRKFNSSGCPERMAVCKSLADFRQGWGQITYKVNISGP
SQ  SDDRPYCWHYAPRPCDVVPASTVCGPVYCFTPSPVVIGTTDRRGNPTYTWGENETDVFMLESLRPPTGGWFGCTWMNSTG
SQ  FTKTCGAPPCQIIPGDYNSSANELLCPTDCFRKHPEATYQRCGSGPWVTPRCLVDYPYRLWHYPCTVNFTVHKVRMFVGG
SQ  IEHRFDAACNWTRGERCELHDRDRIEMSPLLFSTTQLAILPCSFSTMPALSTGLIHLHQNIVDVQYLYGVSSSVTSWVVK
SQ  WEYIVLMFLVLADARICTCLWLMLLISNVEAAVERLVVLNAASAAGTAGWWWAVLFLCCVWYVKGRLVPACTYMALGMWP
SQ  LLLTILALPHRAYAMDNEQAASLGAVGLLAITIFTITPTYKKLLTCFIWWNQYFLARAEAMVHEWVPDLRVRGGRDSIIL
SQ  LTCLLHPQLGFEVTKILLAILAPLYILQYSLLKVPYFVRAHILLRACLLVRRLAGGRYVQACLLRLGAWTGTFIYDHLAP
SQ  LSDWASDGLRDLAVAVEPVIFSPMEKKIITWGADTAACGDILSGLPVSARLGNLVLLGPADDMQRGGWKLLAPITAYAQQ
SQ  TRGLVGTIVTSLTGRDKNEVEGEVQVVSTATQSFLATSINGVMWTVYHGAGSKTLAGPKGPVCQMYTNVDKDLVGWPSPP
SQ  GARSLTPCTCGSSDLYLVTREADVIPARRRGDNRAALLSPRPISTLKGSSGGPVMCPSGHVVGLFRAAVCTRGVAKSLDF
SQ  IPVENMETTMRSPSFTDNSTPPAVPQTYQVGYLHAPTGSGKSTRVPAAYASQGYKVLVLNPSVAATLSFGSYMRQAYGVE
SQ  PNVRTGVRTVTTGGAITYSTYGKFLADGGCSGGAYDIIICDECHSTDPTTVLGIGTVLDQAETAGARLTVLATATPPGSI
SQ  TVPHPNITETALPTTGEIPFYGKAIPLEYIKGGRHLIFCHSKKKCDELAGKLKSLGLNAVAFYRGVDVSVIPTSGDVVIC
SQ  ATDALMTGYTGDFDSVIDCNVAVTQVVDFSLDPTFSIETTTVPQDAVSRSQRRGRTGRGKPGVYRFVSQGERPSGMFDTV
SQ  VLCEAYDTGCAWYELTPSETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQGGENFAYLVAYQATVCA
SQ  RAKAPPPSWDTMWKCLIRLKPTLTGPTPLLYRLGAVQNEIITTHPITKYIMTCMSADLEVITSTWVLVGGVLAALAAYCL
SQ  SVGCVVICGRITLTGKPAVVPDREILYQQFDEMEECSRHIPYLAEGQQIAEQFRQKVLGLLQASAKQAEELKPAVHSAWP
SQ  RMEEFWRKHMWNFVSGIQYLAGLSTLPGNPAVASLMSFTASLTSPLRTSQTLLLNILGGWIAAQVAPPPASTAFVVSGLA
SQ  GAAVGSIRLGRVLVDVLAGYGAGVSGALVAFKIMSGDCPTTEDMVNLLPALLSPGALVVGVVCAAILRRHVGPAEGANQW
SQ  MNRLIAFASRGNHVSPTHYVPETDASKNVTQILTSLTITSLLRRLHQWVNEDTATPCATSWLRDVWDWVCTVLSDFKVWL
SQ  QAKLFPRLPGIPFLSCQTGYRGVWAGDGVCHTTCTCGAVIAGHVKNGTMKITGPKTCSNTWHGTFPINATTTGPSTPRPA
SQ  PNYQRALWRVSAEDYVEVRRLGDCHYVVGVTAEGLKCPCQVPAPEFFTEVDGVRIHRYAPPCKPLLRDEVTFSVGLSNYA
SQ  IGSQLPCEPEPDVTVVTSMLTDPTHITAETASRRLKRGSPPSLASSSASQLSAPSLKATCTTSKDHPDMELIEANLLWRQ
SQ  EMGGNITRVESENKVVVLDSFEPLTAEYDEREISVSAECHRPPRHKFPPALPIWARPDYNPPLLQAWQMPGYEPPVVSGC
SQ  AVAPPKPAPIPPPRRKRLVHLDESTVSRALAQLADKVFVEGSSDPGPSSDSGLSITSPDPPAPTTPDDACSEAESYSSMP
SQ  PLEGEPGDPDLSSGSWSTVSDQDDVVCCSMSYSWTGALITPCAAEEEKLPINPLSNSLIRHHNMVYSTTSRSASLRQKKV
SQ  TFDRLQVFDQHYQDVLKEIKLRASTVQARLLSIEEACDLTPSHSARSKYGYGAQDVRSHASKAINHIRSVWEDLLEDSDT
SQ  PIPTTIMAKNEVFCVDPSKGGRKPARLIVYPDLGVRVCEKMALYDVTRKLPQAVMGSAYGFQYSPNQRVEYLLKMWRSKK
SQ  VPMGFSYDTRCFDSTVTERDIRTENDIYQSCQLDPVARRAVSSLTERLYVGGPMVNSKGQSCGYRRCRASGVLPTSMGNT
SQ  LTCYLKAQAACRAANIKDCDMLVCGDDLVVICESAGVQEDTASLRAFTDAMTRYSAPPGDVPQPTYDLELITSCSSNVSV
SQ  AHDGNGKRYYYLTRDCTTPLARAAWETARHTPVNSWLGNIIMFAPTIWVRMVLMTHFFSILQSQEQLEKALDFDIYGVTY
SQ  SVSPLDLPAIIQRLHGMAAFSLHGYSPTELNRVGACLRKLGVPPLRAWRHRARAVRAKLIAQGGKAAICGKYLFNWAVKT
SQ  KLKLTPLVSASKLDLSGWFVAGYDGGDIYHSVSQARPRLLLLGLLLLTVGVGIFLVPAR
//
ID  P27958;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  63746;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000269|PubMed:9037030}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000269|PubMed:11706032, ECO:0000269|PubMed:9037030}. Note=Only a minor proportion of core protein is present in the nucleus (PubMed:9037030). Probably present on the surface of lipid droplets (PubMed:9037030). {ECO:0000269|PubMed:9037030}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:10729138}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (PubMed:10729138). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (PubMed:10729138). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (PubMed:12065403). These events explain the final topology of the protein (PubMed:12065403). {ECO:0000269|PubMed:10729138, ECO:0000269|PubMed:12065403}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:10729138}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (PubMed:10729138). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (PubMed:10729138). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (PubMed:12065403). These events explain the final topology of the protein (PubMed:12065403). {ECO:0000269|PubMed:10729138, ECO:0000269|PubMed:12065403}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:11907211}; Multi-pass membrane protein {ECO:0000269|PubMed:11907211}. Host mitochondrion {ECO:0000269|PubMed:29039530}. Host cell membrane {ECO:0000269|PubMed:11907211, ECO:0000269|PubMed:27320856}. Note=The C- terminus of p7 membrane domain acts as a signal sequence (PubMed:11907211). After cleavage by host signal peptidase, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (PubMed:11907211). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (PubMed:11907211). {ECO:0000269|PubMed:11907211}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26664}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000305}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:12692244, ECO:0000269|PubMed:17030859}; Multi-pass membrane protein {ECO:0000269|PubMed:12692244}. Note=A reorientation of the N-terminus into the ER lumen occurs post-translationally (PubMed:17030859). Localized in the vicinity of host lipid droplet (PubMed:26185986). {ECO:0000269|PubMed:17030859, ECO:0000269|PubMed:26185986}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:11744739, ECO:0000269|PubMed:15247283}; Peripheral membrane protein {ECO:0000269|PubMed:15247283, ECO:0000269|PubMed:17192310}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:15247283}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000269|PubMed:8982089}. Host nucleus {ECO:0000269|PubMed:10702287}. Host lipid droplet {ECO:0000250|UniProtKB:P26662}. Note=Host membrane insertion occurs after processing by the NS3 protease (PubMed:11744739). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000269|PubMed:11744739}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000269|PubMed:17229681}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000269|PubMed:11557752}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000269|PubMed:11557752}.
DR  UNIPROT: P27958;
DR  UNIPROT: O36579;
DR  UNIPROT: O36608;
DR  UNIPROT: O36609;
DR  UNIPROT: O36610;
DR  PDB: 1A1R;
DR  PDB: 1A1V;
DR  PDB: 1CWX;
DR  PDB: 1HEI;
DR  PDB: 1JR6;
DR  PDB: 1N1L;
DR  PDB: 1ONB;
DR  PDB: 1R7C;
DR  PDB: 1R7D;
DR  PDB: 1R7E;
DR  PDB: 1R7F;
DR  PDB: 1R7G;
DR  PDB: 1RGQ;
DR  PDB: 2A4R;
DR  PDB: 2F9V;
DR  PDB: 2HD0;
DR  PDB: 2JXF;
DR  PDB: 2KDR;
DR  PDB: 2N1P;
DR  PDB: 2O8M;
DR  PDB: 2OBO;
DR  PDB: 2OBQ;
DR  PDB: 2OC0;
DR  PDB: 2OC1;
DR  PDB: 2OC7;
DR  PDB: 2OC8;
DR  PDB: 2OIN;
DR  PDB: 2P59;
DR  PDB: 2QV1;
DR  PDB: 2XI2;
DR  PDB: 2XI3;
DR  PDB: 2XNI;
DR  PDB: 3RC4;
DR  PDB: 3RC5;
DR  PDB: 4CL1;
DR  PDB: 4JZN;
DR  PDB: 4JZO;
DR  PDB: 4MWF;
DR  PDB: 4N0Y;
DR  PDB: 4Q0X;
DR  PDB: 4XVJ;
DR  PDB: 4Z0X;
DR  PDB: 5EOC;
DR  PDB: 5ERW;
DR  PDB: 5FGB;
DR  PDB: 5FGC;
DR  PDB: 5JZI;
DR  PDB: 5YXN;
DR  PDB: 5YXU;
DR  PDB: 6BQJ;
DR  PDB: 6BQK;
DR  PDB: 6BZU;
DR  PDB: 6BZV;
DR  PDB: 6BZW;
DR  PDB: 6BZY;
DR  PDB: 6UYD;
DR  PDB: 6WO5;
DR  PDB: 6WOQ;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (PubMed:18033802). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (PubMed:23799612) (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (PubMed:11086025, PubMed:17881511). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (PubMed:14602201). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (PubMed:14602201). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:11086025, ECO:0000269|PubMed:14602201, ECO:0000269|PubMed:17881511, ECO:0000269|PubMed:18033802, ECO:0000269|PubMed:23799612, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (PubMed:14990718, PubMed:16894197). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (PubMed:16533059, PubMed:29505618, PubMed:24698129). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro- particle (LVP) (PubMed:25122793, PubMed:29695434, PubMed:24838241). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (PubMed:12970454, PubMed:12356718, PubMed:12913001, PubMed:28404852, PubMed:22767607). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (PubMed:22767607, PubMed:12913001). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (PubMed:22855500). Diffusion of the complex E1/E2-EGFR-SCARB1- CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (PubMed:12970454, PubMed:24038151, PubMed:12913001, PubMed:20375010, PubMed:19182773) (By similarity). {ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:12356718, ECO:0000269|PubMed:12913001, ECO:0000269|PubMed:12970454, ECO:0000269|PubMed:14990718, ECO:0000269|PubMed:16533059, ECO:0000269|PubMed:16894197, ECO:0000269|PubMed:19182773, ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:22767607, ECO:0000269|PubMed:22855500, ECO:0000269|PubMed:24038151, ECO:0000269|PubMed:24698129, ECO:0000269|PubMed:24838241, ECO:0000269|PubMed:25122793, ECO:0000269|PubMed:28404852, ECO:0000269|PubMed:29505618, ECO:0000269|PubMed:29695434}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (PubMed:14990718, PubMed:16894197). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (PubMed:16533059, PubMed:29505618, PubMed:24698129). The interaction between E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (PubMed:25122793, PubMed:29695434). This interaction is probably promoted via the up-regulation of cellular autophagy by the virus (PubMed:29695434). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro- particle (LVP) (PubMed:25122793, PubMed:29695434, PubMed:24838241). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (PubMed:12970454, PubMed:12356718, PubMed:12913001, PubMed:28404852, PubMed:22767607). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (PubMed:22767607, PubMed:12913001). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (PubMed:20375010, PubMed:12970454, PubMed:24038151, PubMed:12913001, PubMed:19182773, PubMed:22855500) (By similarity). Diffusion of the complex E1/E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (PubMed:20375010, PubMed:12970454, PubMed:24038151, PubMed:12913001, PubMed:19182773) (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on DCs, and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (PubMed:15371595). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (PubMed:15371595). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (PubMed:30341327). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:12356718, ECO:0000269|PubMed:12913001, ECO:0000269|PubMed:12970454, ECO:0000269|PubMed:14990718, ECO:0000269|PubMed:15371595, ECO:0000269|PubMed:16533059, ECO:0000269|PubMed:16894197, ECO:0000269|PubMed:19182773, ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:22767607, ECO:0000269|PubMed:22855500, ECO:0000269|PubMed:24038151, ECO:0000269|PubMed:24698129, ECO:0000269|PubMed:24838241, ECO:0000269|PubMed:25122793, ECO:0000269|PubMed:28404852, ECO:0000269|PubMed:29505618, ECO:0000269|PubMed:29695434, ECO:0000269|PubMed:30341327}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (PubMed:12719519, PubMed:20824094, PubMed:27320856). Participates in virus envelopment by coordinating the encounter between NS5A and NS2-based assembly sites loaded with E1/E2 heterodimer, which subsequently leads to nucleocapsid envelopment (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (Probable) (PubMed:20824094). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). The release of Ca(2+) may also activate the inflamasome leading to chronic inflammation (Probable) (PubMed:31801866). Targets also host mitochondria and induces mitochondrial depolarization (PubMed:29039530). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (PubMed:27320856). {ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:12719519, ECO:0000269|PubMed:20824094, ECO:0000269|PubMed:27320856, ECO:0000269|PubMed:29039530, ECO:0000303|PubMed:31801866, ECO:0000305, ECO:0000305|PubMed:14741348, ECO:0000305|PubMed:24006444}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (PubMed:8248148). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (PubMed:21147927). {ECO:0000250|UniProtKB:P26663, ECO:0000269|PubMed:21147927, ECO:0000269|PubMed:8248148}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (PubMed:25551442). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (PubMed:8189513, PubMed:8035505, PubMed:8386278). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (PubMed:30341327). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (Probable). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (PubMed:21940894). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (PubMed:16301520, PubMed:16177806). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (PubMed:15710891). {ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:15710891, ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:16301520, ECO:0000269|PubMed:21940894, ECO:0000269|PubMed:25551442, ECO:0000269|PubMed:30341327, ECO:0000269|PubMed:8035505, ECO:0000269|PubMed:8189513, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:15269774}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (PubMed:8189513, PubMed:21507982). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (PubMed:30341327). {ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:21507982, ECO:0000269|PubMed:30341327, ECO:0000269|PubMed:8189513}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (PubMed:12021330). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (PubMed:12021330). NS4B self-interaction contributes to its function in membranous web formation (PubMed:16731940). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (PubMed:29782532). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (PubMed:23542348). {ECO:0000269|PubMed:12021330, ECO:0000269|PubMed:16731940, ECO:0000269|PubMed:23542348, ECO:0000269|PubMed:29782532}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (Probable). Zinc is essential for RNA-binding (PubMed:20926572). Participates in the viral particle production as a result of its interaction with the viral mature core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (PubMed:16951545). Prevents BIN1-induced apoptosis (PubMed:16530520). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (PubMed:31801866). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (PubMed:28743875). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:16530520, ECO:0000269|PubMed:16951545, ECO:0000269|PubMed:20926572, ECO:0000269|PubMed:28743875, ECO:0000269|PubMed:31801866, ECO:0000305|PubMed:20926572}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000269|PubMed:20729191}.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P05783; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: P07948; IntAct: EBI-710656; Score: 0.70
DE  Interaction: P19525; IntAct: EBI-8765629; Score: 0.70
DE  Interaction: P20591; IntAct: EBI-8788892; Score: 0.27
DE  Interaction: P26660; IntAct: EBI-6875553; Score: 0.65
DE  Interaction: P06240; IntAct: EBI-710566; Score: 0.66
DE  Interaction: P06241; IntAct: EBI-710580; Score: 0.70
DE  Interaction: P62993; IntAct: EBI-710623; Score: 0.66
DE  Interaction: P08631; IntAct: EBI-710691; Score: 0.73
DE  Interaction: P06239; IntAct: EBI-762326; Score: 0.40
DE  Interaction: Q7Z434; IntAct: EBI-3648904; Score: 0.46
DE  Interaction: Q9UHD2; IntAct: EBI-3649547; Score: 0.57
DE  Interaction: Q14164; IntAct: EBI-8788614; Score: 0.52
DE  Interaction: O00499; IntAct: EBI-8847572; Score: 0.74
DE  Interaction: P61604; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P61956; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P10599; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P80723; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: Q15717; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P12236; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P60174; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P06733; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-8849933; Score: 0.40
DE  Interaction: Q04941; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P29966; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: Q06830; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P62937; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P16949; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P05455; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P55209; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: O94966; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: Q14318; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: Q9H8S9; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-8849923; Score: 0.78
DE  Interaction: Q7L9L4; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P14174; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: Q562R1; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P68371; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: O14654; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: Q9H7B4; IntAct: EBI-6159185; Score: 0.35
DE  Interaction: Q07021; IntAct: EBI-6377391; Score: 0.51
DE  Interaction: P28062; IntAct: EBI-6671778; Score: 0.58
DE  Interaction: P25789; IntAct: EBI-6671824; Score: 0.40
DE  Interaction: P27958; IntAct: EBI-6901603; Score: 0.94
DE  Interaction: Q9Z2B5; IntAct: EBI-6902945; Score: 0.66
DE  Interaction: P60033; IntAct: EBI-6914053; Score: 0.84
DE  Interaction: O60603; IntAct: EBI-6914676; Score: 0.27
DE  Interaction: Q99IB8; IntAct: EBI-8763465; Score: 0.50
DE  Interaction: P02675; IntAct: EBI-6931833; Score: 0.54
DE  Interaction: Q9UHD4; IntAct: EBI-7212239; Score: 0.54
DE  Interaction: Q9Z2A7; IntAct: EBI-8763431; Score: 0.40
DE  Interaction: Q96CW1; IntAct: EBI-8767461; Score: 0.54
DE  Interaction: P29590; IntAct: EBI-8785421; Score: 0.46
DE  Interaction: P04637; IntAct: EBI-8785378; Score: 0.53
DE  Interaction: Q8NBT2; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P57682; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q6DCA0; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9Y6V0; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q96PT4; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P26583; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q96B01; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q16600; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: O14965; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P01100; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: O00559; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8N5Y2; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P54274; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q15651; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9UFF9; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q14919; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P37231; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q96PI1; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P62857; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P61964; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q14247; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q16644; IntAct: EBI-8785468; Score: 0.62
DE  Interaction: Q7Z6M1; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8IW41; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q99986; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9H8X2; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P19784; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8N5I9; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8N6L7; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9P270; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8NEG0; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9BU76; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9BUV0; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8NEG7; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8IXS8; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9BWK5; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9Y2S6; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9H9L4; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q96E40; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: O14598; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9H7E9; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9Y3C1; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8IWP9; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P60006; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: O95424; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8N3C7; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q12894; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9UMY1; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9H4G4; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8IV56; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q96EH5; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9NU19; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9Y5B9; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q16763; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q6B0I6; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P06746; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8IXJ9; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q96DX7; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P60002; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9Y5P8; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: O43852; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9UHV2; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q5MJ08; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8N6M0; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q68E01; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P11137; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8WWL7; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: O75937; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9Y3T9; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: O15205; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P61328; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P55036; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: O14576; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9Y3E1; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q13442; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9HCS5; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q96CN9; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P51959; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q08426; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q8NHQ9; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P62888; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P47914; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q13243; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q13242; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P35268; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P09132; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: O14602; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P62750; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q15020; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q6ZT98; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q9Y237; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P22736; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: Q86WV6; IntAct: EBI-8790013; Score: 0.54
DE  Interaction: O60488; IntAct: EBI-8789904; Score: 0.27
DE  Interaction: P07355; IntAct: EBI-8792407; Score: 0.46
DE  Interaction: P42356; IntAct: EBI-8803192; Score: 0.70
DE  Interaction: Q9NYQ3; IntAct: EBI-8803192; Score: 0.35
DE  Interaction: P17844; IntAct: EBI-8840942; Score: 0.73
DE  Interaction: P05155; IntAct: EBI-8853131; Score: 0.44
DE  Interaction: Q99941; IntAct: EBI-8853188; Score: 0.54
DE  Interaction: P18850; IntAct: EBI-9006382; Score: 0.37
DE  Interaction: Q9UJM8; IntAct: EBI-9031127; Score: 0.37
DE  Interaction: O95801; IntAct: EBI-9031120; Score: 0.37
DE  Interaction: P12814; IntAct: EBI-9031134; Score: 0.61
DE  Interaction: P28070; IntAct: EBI-8870944; Score: 0.37
DE  Interaction: Q9BW66; IntAct: EBI-9031113; Score: 0.37
DE  Interaction: O00571; IntAct: EBI-9079545; Score: 0.80
DE  Interaction: P12277; IntAct: EBI-9097029; Score: 0.37
DE  Interaction: Q9P035; IntAct: EBI-9083202; Score: 0.40
DE  Interaction: Q9H6S0; IntAct: EBI-9086804; Score: 0.46
DE  Interaction: O96017; IntAct: EBI-9086721; Score: 0.56
DE  Interaction: Q13315; IntAct: EBI-9086715; Score: 0.56
DE  Interaction: Q99836; IntAct: EBI-9086987; Score: 0.40
DE  Interaction: P02788; IntAct: EBI-9103830; Score: 0.75
DE  Interaction: P24627; IntAct: EBI-9098870; Score: 0.68
DE  Interaction: H6U5Q1; IntAct: EBI-9099577; Score: 0.40
DE  Interaction: P19338; IntAct: EBI-9099624; Score: 0.46
DE  Interaction: P08238; IntAct: EBI-9103887; Score: 0.40
DE  Interaction: P07900; IntAct: EBI-9103887; Score: 0.40
DE  Interaction: Q96P48; IntAct: EBI-9105883; Score: 0.51
DE  Interaction: Q9H6F5; IntAct: EBI-9105756; Score: 0.51
DE  Interaction: P29762; IntAct: EBI-9105871; Score: 0.51
DE  Interaction: Q86XR8; IntAct: EBI-9105655; Score: 0.37
DE  Interaction: Q92597; IntAct: EBI-9105595; Score: 0.37
DE  Interaction: Q9NX38; IntAct: EBI-9105720; Score: 0.37
DE  Interaction: P02794; IntAct: EBI-9105647; Score: 0.37
DE  Interaction: P06454; IntAct: EBI-9105704; Score: 0.37
DE  Interaction: P08493; IntAct: EBI-9105679; Score: 0.37
DE  Interaction: P09758; IntAct: EBI-9105671; Score: 0.37
DE  Interaction: Q6FHJ7; IntAct: EBI-9105586; Score: 0.37
DE  Interaction: Q09666; IntAct: EBI-9105580; Score: 0.37
DE  Interaction: Q8WTV0; IntAct: EBI-9163465; Score: 0.52
DE  Interaction: Q920L9; IntAct: EBI-9209522; Score: 0.50
DE  Interaction: P07823; IntAct: EBI-9209516; Score: 0.50
DE  Interaction: P02652; IntAct: EBI-9209687; Score: 0.37
DE  Interaction: Q14240; IntAct: EBI-9210579; Score: 0.66
DE  Interaction: O00410; IntAct: EBI-9210654; Score: 0.58
DE  Interaction: Q6ZRS2; IntAct: EBI-9211613; Score: 0.46
DE  Interaction: P42224; IntAct: EBI-9525439; Score: 0.46
DE  Interaction: P39429; IntAct: EBI-9249981; Score: 0.61
DE  Interaction: P38936; IntAct: EBI-9251021; Score: 0.50
DE  Interaction: P09651; IntAct: EBI-9253755; Score: 0.60
DE  Interaction: P18124; IntAct: EBI-9253755; Score: 0.35
DE  Interaction: Q02878; IntAct: EBI-9253755; Score: 0.35
DE  Interaction: Q14141; IntAct: EBI-9253869; Score: 0.57
DE  Interaction: Q96BZ9; IntAct: EBI-9254487; Score: 0.70
DE  Interaction: O77811; IntAct: EBI-9349150; Score: 0.44
DE  Interaction: P23528; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: P24666; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: O76003; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: Q9Y680; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: Q6P1N9; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: Q9Y694; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: Q6ZTP6; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: Q95HD8; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: P08727; IntAct: EBI-9350927; Score: 0.35
DE  Interaction: P08670; IntAct: EBI-9350927; Score: 0.58
DE  Interaction: P05787; IntAct: EBI-9350927; Score: 0.57
DE  Interaction: Q8IUD2; IntAct: EBI-9352530; Score: 0.65
DE  Interaction: Q8TEX9; IntAct: EBI-9352661; Score: 0.37
DE  Interaction: P08107; IntAct: EBI-9352669; Score: 0.37
DE  Interaction: Q96QK1; IntAct: EBI-9352665; Score: 0.37
DE  Interaction: A0A1U7Q6W2; IntAct: EBI-9537409; Score: 0.40
DE  Interaction: A0A1U7R619; IntAct: EBI-9537252; Score: 0.40
DE  Interaction: Q13625; IntAct: EBI-9389968; Score: 0.64
DE  Interaction: P04114; IntAct: EBI-9392112; Score: 0.40
DE  Interaction: Q9UPY3; IntAct: EBI-9392140; Score: 0.40
DE  Interaction: P62314; IntAct: EBI-9541482; Score: 0.60
DE  Interaction: O15350; IntAct: EBI-9525503; Score: 0.46
DE  Interaction: Q9NPY3; IntAct: EBI-9541020; Score: 0.40
DE  Interaction: P25118; IntAct: EBI-9636604; Score: 0.35
DE  Interaction: P02649; IntAct: EBI-10092067; Score: 0.54
DE  Interaction: P11226; IntAct: EBI-26572921; Score: 0.40
GO  GO:0039714;
GO  GO:0033116;
GO  GO:0030430;
GO  GO:0044164;
GO  GO:0044165;
GO  GO:0044167;
GO  GO:0044177;
GO  GO:0044186;
GO  GO:0033644;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0033647;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0060590;
GO  GO:0004197;
GO  GO:0017151;
GO  GO:0019899;
GO  GO:0031072;
GO  GO:0042802;
GO  GO:0005216;
GO  GO:1990254;
GO  GO:0019900;
GO  GO:0042288;
GO  GO:0140721;
GO  GO:0002039;
GO  GO:0008233;
GO  GO:0019903;
GO  GO:0030291;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0005124;
GO  GO:0004252;
GO  GO:0008236;
GO  GO:0017124;
GO  GO:0031267;
GO  GO:0097677;
GO  GO:0005198;
GO  GO:0035663;
GO  GO:0008134;
GO  GO:0031369;
GO  GO:0008270;
GO  GO:0098671;
GO  GO:0075512;
GO  GO:0098670;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0019054;
GO  GO:0039645;
GO  GO:0044833;
GO  GO:0019056;
GO  GO:0002674;
GO  GO:0032780;
GO  GO:0030889;
GO  GO:0060548;
GO  GO:0050689;
GO  GO:1900102;
GO  GO:1900118;
GO  GO:0032715;
GO  GO:0070104;
GO  GO:0033673;
GO  GO:0031953;
GO  GO:0050709;
GO  GO:0090201;
GO  GO:0034136;
GO  GO:0034144;
GO  GO:0034156;
GO  GO:0034164;
GO  GO:0000122;
GO  GO:0010804;
GO  GO:0042532;
GO  GO:0039707;
GO  GO:1990216;
GO  GO:0010694;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0032467;
GO  GO:0010628;
GO  GO:1903301;
GO  GO:1903721;
GO  GO:0045862;
GO  GO:0051047;
GO  GO:0045727;
GO  GO:1903265;
GO  GO:0048524;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:1900101;
GO  GO:0019050;
GO  GO:0046774;
GO  GO:0039560;
GO  GO:0039563;
GO  GO:0039644;
GO  GO:0039613;
GO  GO:0039547;
GO  GO:0039653;
GO  GO:0039611;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0140533;
GO  GO:0019087;
GO  GO:0044053;
GO  GO:0046762;
GO  GO:0019069;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11557752};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRTWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSSGLYHVTNDCPNSSVVYEAADAILHTPGCVPCVREGNASRCWV
SQ  AVTPTVATRDGKLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRHHWTTQDCNCSIYPGHITGHRMAW
SQ  NMMMNWSPTAALVVAQLLRIPQAIMDMIAGAHWGVLAGIKYFSMVGNWAKVLVVLLLFAGVDAETHVTGGNAGRTTAGLV
SQ  GLLTPGAKQNIQLINTNGSWHINSTALNCNESLNTGWLAGLFYQHKFNSSGCPERLASCRRLTDFAQGWGPISYANGSGL
SQ  DERPYCWHYPPRPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGANDTDVFVLNNTRPPLGNWFGCTWMNSTGF
SQ  TKVCGAPPCVIGGVGNNTLLCPTDCFRKYPEATYSRCGSGPRITPRCMVDYPYRLWHYPCTINYTIFKVRMYVGGVEHRL
SQ  EAACNWTRGERCDLEDRDRSELSPLLLSTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVV
SQ  LLFLLLADARVCSCLWMMLLISQAEAALENLVILNAASLAGTHGLVSFLVFFCFAWYLKGRWVPGAVYALYGMWPLLLLL
SQ  LALPQRAYALDTEVAASCGGVVLVGLMALTLSPYYKRYISWCMWWLQYFLTRVEAQLHVWVPPLNVRGGRDAVILLTCVV
SQ  HPALVFDITKLLLAIFGPLWILQASLLKVPYFVRVQGLLRICALARKIAGGHYVQMAIIKLGALTGTCVYNHLAPLRDWA
SQ  HNGLRDLAVAVEPVVFSRMETKLITWGADTAACGDIINGLPVSARRGQEILLGPADGMVSKGWRLLAPITAYAQQTRGLL
SQ  GCIITSLTGRDKNQVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQTYTNVDQDLVGWPAPQGSRSL
SQ  TPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTRGVAKAVDFIPVEN
SQ  LETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAKGYKVLVLNPSVAATLGFGAYMSKAHGVDPNIRT
SQ  GVRTITTGSPITYSTYGKFLADAGCSGGAYDIIICDECHSTDATSISGIGTVLDQAETAGARLVVLATATPPGSVTVSHP
SQ  NIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVSTDAL
SQ  MTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCEC
SQ  YDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLGFWEGVFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARAQAP
SQ  PPSWDQMRKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCV
SQ  VIVGRIVLSGKPAIIPDREVLYQEFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTASRHAEVITPAVQTNWQKLEVF
SQ  WAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTGQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAALD
SQ  SVGLGKVLVDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALAVGVVFASILRRRVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPCSGSWLRDIWDWICEVLSDFKTWLKAKLM
SQ  PQLPGIPFVSCQRGYRGVWRGDGIMHTRCHCGAEITGHVKNGTMRIVGPRTCKNMWSGTFFINAYTTGPCTPLPAPNYKF
SQ  ALWRVSAEEYVEIRRVGDFHYVSGMTTDNLKCPCQIPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSMASSSASQLSAPSLKATCTANHDSPDAELIEANLLWRQEMGGN
SQ  ITRVESENKVVILDSFDPLVAEEDEREVSVPAEILRKSRRFAPALPVWARPDYNPLLVETWKKPDYEPPVVHGCPLPPPR
SQ  SPPVPPPRKKRTVVLTESTLPTALAELATKSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDVESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSSGADTEDVVCCSMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRKKKVTFDRLQVL
SQ  DSHYQDVLKEVKAAASKVKANLLSVEEACSLAPPHSAKSKFGYGAKDVRCHARKAVAHINSVWKDLLEDSVTPIDTTIMA
SQ  KNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGLSYD
SQ  TRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCRASRVLTTSCGNTLTRYIKAR
SQ  AACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKR
SQ  VYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALNCEIYGACYSIEPLDLP
SQ  PIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRAWSVRARLLARGGKAAICGKYLFNWAVRTKLKLTPIT
SQ  AAGRLDLSGWFTAGYSGGDIYHSVSHARPRWFWFCLLLLAAGVGIYLLPNR
//
ID  Q68749;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356413;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q68749;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRAARKTSERSQPRGRRQPIPKDRRSTGKSWGRPG
SQ  YPWPLYRNEGLGWAGWLLSPRGSRPSWGPSDPRHKSRNLGKVIDTLTCGFADLMGYIPVVGAPVGGVARALAHGVRVLED
SQ  GINYATGNLPGCSFSIFLLALLSCISVPVSAVEVRNTSSSYMATNDCSNSSIVWQLEGAVLHTPGCVPCEKTGNKSRCWV
SQ  PVTPNIAINQPGALTKGLRAHIDVIVMSATLCSALYVGDVCGALMIAAQVVVVSPQHHHFVQECNCSIYPGKITGHRMAW
SQ  DMMMNWSPTTTMLLAYLVRIPEVVLDIITGGHWGVMFGLAYFSMQGAWAKVVVILLLTAGVEASTYTTGAVVGRSTHLFT
SQ  SMFSLGSQQRVQLIHTNGSWHINRTALNCNDSLETGFLAALFYTSSFNSSGCPERLAACRSIESFRIGWGSLEYEESVTN
SQ  DADMRPYCWHYPPRPCGIVPARTVCGPVYCFTPSPVVVGTTDRAGAPTYNWGENETDVFLLNSTRPPKGAWFGCTWMNGT
SQ  GFTKTCGAPPCRIRKDFNASEDLLCPTDCFRKHPGATYIKCGAGPWLTPRCLVDYPYRLWHYPCTVNYTIYKVRMFVGGI
SQ  EHRLQAACNFTRGDRCNLEDRDRSQLSPLLHSTTEWAILPCSYTDLPALSTGLLHLHQNIVDVQYLYGLSPAITKYVVKW
SQ  EWVVLLFLLLADARVCACLWMLLLLGQAEAALEKLVILHAASAASSNGLLYFILFFVAAWCIKGRAVPMVTYTLLGCWSF
SQ  VLLLMALPHQAYALDAAEQGQIGMALLIAITAFTITPAYKILLSRCLWWTCYMLVLAEALIQDWIPPLQARGGRDGVIWA
SQ  MTMFYPGVVFDITKWLLAILGPGYLFRAAVMRTPYFVRANALLRMCALVKQLAGGKYVQVALITLGKWTGTYIYDHLSPM
SQ  SDWAADGLRDLAVAVEPIVFSPMERKVIVWGAETTACGDIIHGLPVSARLGQEVLLGPADGYTSKGWRLLAPITAYAQQT
SQ  RGLLSAIVVSMTGRDKTDQAGEIQVLSTVTQSFLGTSISGVLWTVFHGAGNKTLAGSRGPVTQMYSSAEGDLVGWPSPPG
SQ  TRSLEPCTCGAVDLYLVTRNADVIPARRRGDRRGALLSPRPLSSLKGSSGGPVLCPRGHAVGIFRAAVCSRGVAKSIDFI
SQ  PVESLDVVTRSPNFTDNSTPPAVPQTYQVGYLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAYGINP
SQ  NIRTGVRTVTTGDAITYSTYGKFLADGGCSGGAYDVIICDECHSVDSTTILGIGTVLDQAETAGVRLTVLATATPPGSVT
SQ  TPHPNIEEVALGHEGEIPFYGKAIPLSAIKGGRHLIFCHSKKKCDELAVALRGMGLNAVAYYRGLDVSIIPTQGDVVVVA
SQ  TDALMTGYTGDFDSVIDCNVAVTQVVDFSLDPTFTITTQTVPQDSVSRSQRRGRTGRGRLGIYRYVSSGERASGMFDTVV
SQ  LCECYDAGAAWYELTPAETTVRLRAYFNTPGLPVCQDHLEFWEAVFTGLTHIDAHFLSQTKQAGEGFPYLVAYQATVCAR
SQ  AKAPPPSWDVMWKCLIRLKPTLVGPTPLLYRLGSVTNEVTLTHPVTKYIATCMQADLEIMTSTWVLAGGVLAAVAAYCLA
SQ  TGCVSIIGRIHVNQKTIIAPDKEVLYEAFDEMEECASRTALIEEGHRIAEMLKSKIQGLMQQASKQAQGVQPAVQATWPK
SQ  LEQFWAKHMWNFISGIQYLAGLSTLPGNPAVASMMSFSAALTSPLSTSTTILLNIMGGWLASQIAPPAGATGFVVSGLVG
SQ  AAVGSIGLGKILVDVLAGYGAGISGALVAFKIMSGEKPSVEDVVNLLPAILSPGALVVGVICAAILRRHVGQGEGAVQWM
SQ  NRLIAFASRGNHVAPTHYVAESDASQRVTQLLGSLTITSLLRRLHQWITEDCPVPCSGSWLRDVWDWVCSILIDFKNWLS
SQ  AKLFPRLPGIPFISCQKGYRGTWAGTGIMTTRCPCGANITGNVRLGTMRISGPKTCLNTWQGTFPINCYTEGSCVPKPAP
SQ  NFKTAIWRVAASEYAEVTQHDSHAYVTGLTADNLKVPCQLPCPEFFSWVDGVQIHRFAPTPKAFMRDEVSFSVGLNSYVV
SQ  GSQLPCEPEPDTEVLASMLTDPSHITAEAAARRLARGSPPSAASSSASQLSAPSLRATCTTHAKCPDIDMVDANLFCWCT
SQ  MGGNMTRIESESKVLMVDSFDPVVDKEDEREPSIPSEYLLPKSRFPPALPPWARPDYNPPLLETWKRPDYQPPVVAGCAL
SQ  PPPGTTPVPPPRRRRAVVLDQSNVGEALKELAIKSFGCPPPSGDPGHSTGGGTTGETSKSPPDEPDDSEAGSVSSMPPLE
SQ  GEPGDPDLEPEQVEHPAPPQEGGAAPGSDSGSWSTCSDVDDSVVCCSMSYSWTGALITPCSPEEEKLPINPLSNSLLRYH
SQ  NKVYCTTSRSASQRAKKVTFDRVQLLDSHYESVLKDVKQAATKVSAKLLSIEEACALTPPHSARSKYGFGAKEVRSLSRR
SQ  AVDHIKSVWEDLLEDHCSPIDTTIMAKNEVFCVDPTKGGKKPARLIVYPDLGVRVCEKMALYDITQKLPVAVMGQSYGFQ
SQ  YSPAQRVDFLLQAWKEKKTPMGFSYDTRCFDSTVTERDIRTEESIYLSCSLPEEARTAIHSLTERLYVGGPMTNSKGQSC
SQ  GYRRCRASGVLTTSMGNTLTCYVKAKAACNAAGIVAPTMLVCGDDLVVISESQGVEEDERNLRVFTEAMTRYSAPPGDPP
SQ  KAEYDLELITSCSSNVSVALDPRGRRRYYLTRDPTTPLARAAWETARHSPVNSWLGNIIQYAPTVWVRMVLMTHFFSVLM
SQ  AQDTLDQDLNFEMYGAVYSVSPLDLPAIIERLHGLEAFSLHSYSPHELTRVAAALRKLGAPPLRAWKSRARAVRASLISR
SQ  GGSAATCGRYLFNWAVRTKLKLTPLPAARLLDLSSWFTVSAGGGDIYHSVSRARPRLLLLGLLLLCVGVGIFLLPAR
//
ID  P26663;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  11105;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000269|PubMed:17188392}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (PubMed:17188392). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:17188392}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: P26663;
DR  PDB: 1A1Q;
DR  PDB: 1BT7;
DR  PDB: 1C2P;
DR  PDB: 1CSJ;
DR  PDB: 1CU1;
DR  PDB: 1GX5;
DR  PDB: 1GX6;
DR  PDB: 1JXP;
DR  PDB: 1NHU;
DR  PDB: 1NHV;
DR  PDB: 1NS3;
DR  PDB: 1OS5;
DR  PDB: 1QUV;
DR  PDB: 2AWZ;
DR  PDB: 2AX0;
DR  PDB: 2AX1;
DR  PDB: 2BRK;
DR  PDB: 2BRL;
DR  PDB: 2DXS;
DR  PDB: 2GIQ;
DR  PDB: 2GIR;
DR  PDB: 2HAI;
DR  PDB: 2HWH;
DR  PDB: 2HWI;
DR  PDB: 2I1R;
DR  PDB: 2JC0;
DR  PDB: 2JC1;
DR  PDB: 2O5D;
DR  PDB: 2WCX;
DR  PDB: 2WHO;
DR  PDB: 2WRM;
DR  PDB: 2XWY;
DR  PDB: 2ZKU;
DR  PDB: 3BR9;
DR  PDB: 3BSA;
DR  PDB: 3BSC;
DR  PDB: 3CDE;
DR  PDB: 3CIZ;
DR  PDB: 3CJ0;
DR  PDB: 3CJ2;
DR  PDB: 3CJ3;
DR  PDB: 3CJ4;
DR  PDB: 3CJ5;
DR  PDB: 3CO9;
DR  PDB: 3CVK;
DR  PDB: 3CWJ;
DR  PDB: 3D28;
DR  PDB: 3D5M;
DR  PDB: 3E51;
DR  PDB: 3FQK;
DR  PDB: 3FRZ;
DR  PDB: 3G86;
DR  PDB: 3GYN;
DR  PDB: 3H2L;
DR  PDB: 3H59;
DR  PDB: 3H5S;
DR  PDB: 3H5U;
DR  PDB: 3H98;
DR  PDB: 3IGV;
DR  PDB: 3MF5;
DR  PDB: 3RVB;
DR  PDB: 3UA7;
DR  PDB: 3UDL;
DR  PDB: 3VQS;
DR  PDB: 4A92;
DR  PDB: 4B6E;
DR  PDB: 4B6F;
DR  PDB: 4B71;
DR  PDB: 4B73;
DR  PDB: 4B74;
DR  PDB: 4B75;
DR  PDB: 4B76;
DR  PDB: 4DGV;
DR  PDB: 4DGY;
DR  PDB: 4EO6;
DR  PDB: 4EO8;
DR  PDB: 4IH5;
DR  PDB: 4IH6;
DR  PDB: 4IH7;
DR  PDB: 4K8B;
DR  PDB: 4KAI;
DR  PDB: 4KB7;
DR  PDB: 4KBI;
DR  PDB: 4KE5;
DR  PDB: 4MIA;
DR  PDB: 4MIB;
DR  PDB: 4MK7;
DR  PDB: 4MK8;
DR  PDB: 4MK9;
DR  PDB: 4MKA;
DR  PDB: 4MKB;
DR  PDB: 4TN2;
DR  PDB: 4WXP;
DR  PDB: 5FPS;
DR  PDB: 5FPT;
DR  PDB: 5FPY;
DR  PDB: 5KZP;
DR  PDB: 5W2E;
DR  PDB: 6MVP;
DR  PDB: 6W4G;
DR  PDB: 8OHM;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (Probable). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome- dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up- regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305, ECO:0000305|PubMed:8189501}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (Probable) (PubMed:11591719). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (PubMed:11591719). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:11591719, ECO:0000305|PubMed:9261354}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (PubMed:9614113). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:9614113}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the viral mature core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles. Down-regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: P52480; IntAct: EBI-7949443; Score: 0.53
DE  Interaction: P14618; IntAct: EBI-7949705; Score: 0.27
DE  Interaction: Q62245; IntAct: EBI-7535585; Score: 0.56
DE  Interaction: P26663; IntAct: EBI-6838569; Score: 0.78
DE  Interaction: Q9WMX2; IntAct: EBI-6874511; Score: 0.65
DE  Interaction: P04637; IntAct: EBI-6902998; Score: 0.66
DE  Interaction: Q8WTV0; IntAct: EBI-9163490; Score: 0.40
GO  GO:0030430;
GO  GO:0044164;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0042802;
GO  GO:0005216;
GO  GO:0002020;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0008236;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRAPRKTSERSQPRGRRQPIPKARRPEGRTWAQPG
SQ  YPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTTPASAYEVHNVSGIYHVTNDCSNASIVYEAADLIMHTPGCVPCVREGNSSRCWV
SQ  ALTPTLAARNVTIPTTTIRRHVDLLVGAAAFCSAMYVGDLCGSVFLVSQLFTFSPRRHVTLQDCNCSIYPGHVSGHRMAW
SQ  DMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMAGNWAKVLIVMLLFAGVDGDTHVTGGAQAKTTNRLV
SQ  SMFASGPSQKIQLINTNGSWHINRTALNCNDSLQTGFLAALFYTHSFNSSGCPERMAQCRTIDKFDQGWGPITYAESSRS
SQ  DQRPYCWHYPPPQCTIVPASEVCGPVYCFTPSPVVVGTTDRFGVPTYRWGENETDVLLLNNTRPPQGNWFGCTWMNSTGF
SQ  TKTCGGPPCNIGGVGNNTLTCPTDCFRKHPEATYTKCGSGPWLTPRCMVDYPYRLWHYPCTVNFTIFKVRMYVGGVEHRL
SQ  NAACNWTRGERCDLEDRDRPELSPLLLSTTEWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGIGSAVVSFAIKWEYVL
SQ  LLFLLLADARVCACLWMMLLIAQAEAALENLVVLNSASVAGAHGILSFLVFFCAAWYIKGRLVPGATYALYGVWPLLLLL
SQ  LALPPRAYAMDREMAASCGGAVFVGLVLLTLSPYYKVFLARLIWWLQYFTTRAEADLHVWIPPLNARGGRDAIILLMCAV
SQ  HPELIFDITKLLIAILGPLMVLQAGITRVPYFVRAQGLIHACMLVRKVAGGHYVQMAFMKLGALTGTYIYNHLTPLRDWP
SQ  RAGLRDLAVAVEPVVFSDMETKIITWGADTAACGDIILGLPVSARRGKEILLGPADSLEGRGLRLLAPITAYSQQTRGLL
SQ  GCIITSLTGRDKNQVEGEVQVVSTATQSFLATCVNGVCWTVYHGAGSKTLAAPKGPITQMYTNVDQDLVGWPKPPGARSL
SQ  TPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPFGHAVGIFRAAVCTRGVAKAVDFVPVES
SQ  METTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRT
SQ  GVRTITTGAPVTYSTYGKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHP
SQ  NIEEVALSNTGEIPFYGKAIPIEAIRGGRHLIFCHSKKKCDELAAKLSGLGINAVAYYRGLDVSVIPTIGDVVVVATDAL
SQ  MTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRRGIYRFVTPGERPSGMFDSSVLCEC
SQ  YDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAP
SQ  PPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSV
SQ  VIVGRIILSGRPAIVPDRELLYQEFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRALETF
SQ  WAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQSTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVG
SQ  SIGLGKVLVDILAGYGAGVAGALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLRDVWDWICTVLTDFKTWLQSKLL
SQ  PQLPGVPFFSCQRGYKGVWRGDGIMQTTCPCGAQITGHVKNGSMRIVGPKTCSNTWHGTFPINAYTTGPCTPSPAPNYSR
SQ  ALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFSEVDGVRLHRYAPACRPLLREEVTFQVGLNQYLVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHVSPDADLIEANLLWRQEMGGN
SQ  ITRVESENKVVVLDSFDPLRAEEDEREVSVPAEILRKSKKFPAAMPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPPIK
SQ  APPIPPPRRKRTVVLTESSVSSALAELATKTFGSSESSAVDSGTATALPDQASDDGDKGSDVESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSEEASEDVVCCSMSYTWTGALITPCAAEESKLPINALSNSLLRHHNMVYATTSRSAGLRQKKVTFDRLQVLD
SQ  DHYRDVLKEMKAKASTVKAKLLSVEEACKLTPPHSAKSKFGYGAKDVRNLSSKAVNHIHSVWKDLLEDTVTPIDTTIMAK
SQ  NEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQVVMGSSYGFQYSPGQRVEFLVNTWKSKKNPMGFSYDT
SQ  RCFDSTVTENDIRVEESIYQCCDLAPEARQAIKSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKASA
SQ  ACRAAKLQDCTMLVNGDDLVVICESAGTQEDAASLRVFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRV
SQ  YYLTRDPTTPLARAAWETARHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQ
SQ  IIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRARLLSQGGRAATCGKYLFNWAVKTKLKLTPIPA
SQ  ASRLDLSGWFVAGYSGGDIYHSLSRARPRWFMLCLLLLSVGVGIYLLPNR
//
ID  Q9WMX2;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  333284;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:P27958}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000269|PubMed:21187906}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000269|PubMed:21187906}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000269|PubMed:21187906}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q9WMX2;
DR  PDB: 1ZH1;
DR  PDB: 2JY0;
DR  PDB: 2KWT;
DR  PDB: 2KWZ;
DR  PDB: 3FQL;
DR  PDB: 3FQM;
DR  PDB: 3FQQ;
DR  PDB: 3KN2;
DR  PDB: 3KQH;
DR  PDB: 3KQK;
DR  PDB: 3KQL;
DR  PDB: 3KQN;
DR  PDB: 3KQU;
DR  PDB: 3Q0Z;
DR  PDB: 3QGD;
DR  PDB: 3QGE;
DR  PDB: 3QGF;
DR  PDB: 3QGG;
DR  PDB: 4NLD;
DR  PDB: 4U01;
DR  PDB: 5E4F;
DR  PDB: 5PZK;
DR  PDB: 5PZL;
DR  PDB: 5PZM;
DR  PDB: 5PZN;
DR  PDB: 5PZO;
DR  PDB: 5PZP;
DR  PDB: 5TRH;
DR  PDB: 5TRI;
DR  PDB: 5TRJ;
DR  PDB: 5TRK;
DR  PDB: 5TWN;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (PubMed:21187906). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:21187906}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity) (PubMed:27226535). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (PubMed:12702807). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (PubMed:27226535). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (PubMed:15841462). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:12702807, ECO:0000269|PubMed:15841462, ECO:0000269|PubMed:27226535}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (PubMed:12702807). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:12702807}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (PubMed:15542681). Involved in RNA- binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the viral mature core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles. Down-regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:15542681}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: O14681; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: O15162; IntAct: EBI-7048894; Score: 0.58
DE  Interaction: O15173; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: O60711; IntAct: EBI-9078253; Score: 0.37
DE  Interaction: O94875; IntAct: EBI-9082089; Score: 0.51
DE  Interaction: O95248; IntAct: EBI-9079822; Score: 0.37
DE  Interaction: P04406; IntAct: EBI-9078245; Score: 0.37
DE  Interaction: P07948; IntAct: EBI-710977; Score: 0.67
DE  Interaction: P20700; IntAct: EBI-9081801; Score: 0.37
DE  Interaction: P22309; IntAct: EBI-9083684; Score: 0.37
DE  Interaction: P26663; IntAct: EBI-6874511; Score: 0.65
DE  Interaction: P31689; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P32456; IntAct: EBI-9081889; Score: 0.51
DE  Interaction: P35354; IntAct: EBI-9083640; Score: 0.37
DE  Interaction: P37198; IntAct: EBI-9081122; Score: 0.37
DE  Interaction: P54851; IntAct: EBI-9083575; Score: 0.37
DE  Interaction: P57088; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: P62879; IntAct: EBI-9079674; Score: 0.37
DE  Interaction: Q13137; IntAct: EBI-9081202; Score: 0.57
DE  Interaction: Q13625; IntAct: EBI-9082105; Score: 0.37
DE  Interaction: Q14739; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q14764; IntAct: EBI-9079726; Score: 0.37
DE  Interaction: Q14974; IntAct: EBI-11513409; Score: 0.50
DE  Interaction: Q15125; IntAct: EBI-9083439; Score: 0.37
DE  Interaction: Q27J81; IntAct: EBI-9081849; Score: 0.37
DE  Interaction: Q6PIW4; IntAct: EBI-9079662; Score: 0.37
DE  Interaction: Q8NF91; IntAct: EBI-9081937; Score: 0.37
DE  Interaction: Q92832; IntAct: EBI-9081118; Score: 0.37
DE  Interaction: Q9BV73; IntAct: EBI-9082134; Score: 0.37
DE  Interaction: Q9BVC6; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q9GZN7; IntAct: EBI-9081929; Score: 0.37
DE  Interaction: Q9NRD5; IntAct: EBI-9081130; Score: 0.37
DE  Interaction: Q9NRR5; IntAct: EBI-9081813; Score: 0.37
DE  Interaction: Q9P0L0; IntAct: EBI-12738328; Score: 0.54
DE  Interaction: Q9UBB4; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P06241; IntAct: EBI-710957; Score: 0.59
DE  Interaction: P62993; IntAct: EBI-738184; Score: 0.40
DE  Interaction: P06239; IntAct: EBI-738205; Score: 0.40
DE  Interaction: P08631; IntAct: EBI-738237; Score: 0.40
DE  Interaction: P14618; IntAct: EBI-7949624; Score: 0.56
DE  Interaction: Q7L7L0; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P20671; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P55795; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P31942; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P0C0S8; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: Q9BTM1; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P04908; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: O00571; IntAct: EBI-9082166; Score: 0.63
DE  Interaction: P55209; IntAct: EBI-9081749; Score: 0.49
DE  Interaction: Q99878; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P62269; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P31943; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: Q16777; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P62805; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: Q93077; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: Q6FI13; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: Q99733; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: Q96KK5; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: Q32P51; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P09651; IntAct: EBI-6154835; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-6859077; Score: 0.40
DE  Interaction: P21333; IntAct: EBI-6859111; Score: 0.46
DE  Interaction: P08670; IntAct: EBI-9081300; Score: 0.37
DE  Interaction: P27824; IntAct: EBI-9005424; Score: 0.35
DE  Interaction: P60709; IntAct: EBI-6863840; Score: 0.51
DE  Interaction: O60664; IntAct: EBI-8841247; Score: 0.60
DE  Interaction: P42356; IntAct: EBI-8849076; Score: 0.40
DE  Interaction: P61020; IntAct: EBI-8853299; Score: 0.27
DE  Interaction: Q9WMX2; IntAct: EBI-8853267; Score: 0.43
DE  Interaction: Q86Y82; IntAct: EBI-9005424; Score: 0.35
DE  Interaction: P56945; IntAct: EBI-9078225; Score: 0.37
DE  Interaction: O75095; IntAct: EBI-9078271; Score: 0.37
DE  Interaction: Q86UE6; IntAct: EBI-9078263; Score: 0.37
DE  Interaction: Q9H8L6; IntAct: EBI-9078275; Score: 0.37
DE  Interaction: O96013; IntAct: EBI-9078279; Score: 0.37
DE  Interaction: Q96EP0; IntAct: EBI-9078288; Score: 0.37
DE  Interaction: Q53X94; IntAct: EBI-9078292; Score: 0.37
DE  Interaction: Q8N2S1; IntAct: EBI-9078314; Score: 0.37
DE  Interaction: P08572; IntAct: EBI-9078233; Score: 0.37
DE  Interaction: Q5XG79; IntAct: EBI-9078221; Score: 0.37
DE  Interaction: P34810; IntAct: EBI-9078229; Score: 0.37
DE  Interaction: P98095; IntAct: EBI-9078237; Score: 0.37
DE  Interaction: Q9UBX5; IntAct: EBI-9078241; Score: 0.37
DE  Interaction: P28799; IntAct: EBI-9078249; Score: 0.37
DE  Interaction: P13378; IntAct: EBI-9078253; Score: 0.37
DE  Interaction: P22736; IntAct: EBI-9078322; Score: 0.37
DE  Interaction: Q9BYW2; IntAct: EBI-9078318; Score: 0.37
DE  Interaction: P04275; IntAct: EBI-9078310; Score: 0.37
DE  Interaction: Q9Y5V3; IntAct: EBI-9078267; Score: 0.49
DE  Interaction: P60900; IntAct: EBI-9078412; Score: 0.37
DE  Interaction: Q5MIZ7; IntAct: EBI-9078420; Score: 0.37
DE  Interaction: P41225; IntAct: EBI-9078384; Score: 0.37
DE  Interaction: Q9P2D6; IntAct: EBI-9078380; Score: 0.37
DE  Interaction: P05556; IntAct: EBI-9078376; Score: 0.37
DE  Interaction: P62328; IntAct: EBI-9078349; Score: 0.37
DE  Interaction: P07737; IntAct: EBI-9078345; Score: 0.37
DE  Interaction: P05412; IntAct: EBI-9078341; Score: 0.37
DE  Interaction: P20265; IntAct: EBI-9078445; Score: 0.37
DE  Interaction: P10643; IntAct: EBI-9078433; Score: 0.37
DE  Interaction: Q8N2Y8; IntAct: EBI-9081284; Score: 0.49
DE  Interaction: Q99435; IntAct: EBI-9081280; Score: 0.37
DE  Interaction: Q9UKK3; IntAct: EBI-9081252; Score: 0.37
DE  Interaction: Q9BRK4; IntAct: EBI-9081248; Score: 0.37
DE  Interaction: P23142; IntAct: EBI-9081240; Score: 0.37
DE  Interaction: Q9H869; IntAct: EBI-9081232; Score: 0.37
DE  Interaction: P36406; IntAct: EBI-9081214; Score: 0.37
DE  Interaction: P16144; IntAct: EBI-9081222; Score: 0.37
DE  Interaction: O75398; IntAct: EBI-9081218; Score: 0.37
DE  Interaction: O75093; IntAct: EBI-9081226; Score: 0.37
DE  Interaction: Q9NY15; IntAct: EBI-9081194; Score: 0.37
DE  Interaction: Q07666; IntAct: EBI-9081174; Score: 0.37
DE  Interaction: Q13164; IntAct: EBI-9081186; Score: 0.37
DE  Interaction: Q9NSC5; IntAct: EBI-9081166; Score: 0.49
DE  Interaction: Q9Y2D8; IntAct: EBI-9081146; Score: 0.37
DE  Interaction: O95967; IntAct: EBI-9081011; Score: 0.37
DE  Interaction: P67870; IntAct: EBI-9081007; Score: 0.37
DE  Interaction: Q5VU43; IntAct: EBI-9081126; Score: 0.37
DE  Interaction: Q8N3Z6; IntAct: EBI-9080979; Score: 0.49
DE  Interaction: Q9HCS7; IntAct: EBI-9080975; Score: 0.37
DE  Interaction: Q6PKC3; IntAct: EBI-9082114; Score: 0.51
DE  Interaction: Q15276; IntAct: EBI-9080959; Score: 0.49
DE  Interaction: Q49A26; IntAct: EBI-9080955; Score: 0.49
DE  Interaction: P46531; IntAct: EBI-9080951; Score: 0.37
DE  Interaction: Q14112; IntAct: EBI-9080947; Score: 0.37
DE  Interaction: P14543; IntAct: EBI-9080943; Score: 0.37
DE  Interaction: P55196; IntAct: EBI-9080939; Score: 0.37
DE  Interaction: Q7Z7M0; IntAct: EBI-9080935; Score: 0.37
DE  Interaction: Q9P2E2; IntAct: EBI-9080927; Score: 0.37
DE  Interaction: O43559; IntAct: EBI-9080907; Score: 0.57
DE  Interaction: Q75N90; IntAct: EBI-9080903; Score: 0.37
DE  Interaction: Q9NRA8; IntAct: EBI-9080899; Score: 0.57
DE  Interaction: Q96GW7; IntAct: EBI-9080891; Score: 0.37
DE  Interaction: Q8IUX7; IntAct: EBI-9080887; Score: 0.37
DE  Interaction: Q8IYH5; IntAct: EBI-9080883; Score: 0.37
DE  Interaction: Q9Y2K1; IntAct: EBI-9080871; Score: 0.37
DE  Interaction: P13611; IntAct: EBI-9080863; Score: 0.37
DE  Interaction: O75962; IntAct: EBI-9080843; Score: 0.49
DE  Interaction: P14373; IntAct: EBI-9080839; Score: 0.37
DE  Interaction: Q9UPU7; IntAct: EBI-9080827; Score: 0.37
DE  Interaction: Q9BQ16; IntAct: EBI-9080811; Score: 0.37
DE  Interaction: O95219; IntAct: EBI-9080807; Score: 0.37
DE  Interaction: Q8IUQ4; IntAct: EBI-9080803; Score: 0.37
DE  Interaction: Q13435; IntAct: EBI-9080799; Score: 0.37
DE  Interaction: Q86SQ7; IntAct: EBI-9080787; Score: 0.37
DE  Interaction: Q86VW0; IntAct: EBI-9080795; Score: 0.37
DE  Interaction: Q96T21; IntAct: EBI-9080791; Score: 0.37
DE  Interaction: Q86UC2; IntAct: EBI-9079818; Score: 0.37
DE  Interaction: Q58EX7; IntAct: EBI-9079784; Score: 0.37
DE  Interaction: Q8TE76; IntAct: EBI-9079722; Score: 0.37
DE  Interaction: Q9C099; IntAct: EBI-9079710; Score: 0.37
DE  Interaction: Q86U70; IntAct: EBI-9079706; Score: 0.37
DE  Interaction: Q9Y6N6; IntAct: EBI-9079702; Score: 0.37
DE  Interaction: Q2M1P5; IntAct: EBI-9079690; Score: 0.37
DE  Interaction: Q3T8J9; IntAct: EBI-9079678; Score: 0.37
DE  Interaction: Q14CM0; IntAct: EBI-9079670; Score: 0.37
DE  Interaction: Q96EK7; IntAct: EBI-9079650; Score: 0.37
DE  Interaction: P35555; IntAct: EBI-9079654; Score: 0.37
DE  Interaction: Q6NUQ1; IntAct: EBI-9079810; Score: 0.37
DE  Interaction: Q8N1W1; IntAct: EBI-9079806; Score: 0.37
DE  Interaction: Q9BWF3; IntAct: EBI-9079802; Score: 0.37
DE  Interaction: Q9NP80; IntAct: EBI-9079794; Score: 0.37
DE  Interaction: Q99447; IntAct: EBI-9079772; Score: 0.37
DE  Interaction: Q9P0K7; IntAct: EBI-9079798; Score: 0.49
DE  Interaction: Q9HCM3; IntAct: EBI-9079686; Score: 0.37
DE  Interaction: Q9Y219; IntAct: EBI-9079682; Score: 0.37
DE  Interaction: Q8NFF5; IntAct: EBI-9079666; Score: 0.37
DE  Interaction: Q9UHL4; IntAct: EBI-9079646; Score: 0.37
DE  Interaction: Q92782; IntAct: EBI-9079642; Score: 0.37
DE  Interaction: P07332; IntAct: EBI-9079658; Score: 0.37
DE  Interaction: P14136; IntAct: EBI-9081304; Score: 0.37
DE  Interaction: P61289; IntAct: EBI-9081276; Score: 0.37
DE  Interaction: Q12805; IntAct: EBI-9082013; Score: 0.51
DE  Interaction: P35609; IntAct: EBI-9081264; Score: 0.49
DE  Interaction: Q9BR76; IntAct: EBI-9081236; Score: 0.37
DE  Interaction: P12814; IntAct: EBI-9081256; Score: 0.37
DE  Interaction: O94813; IntAct: EBI-9081210; Score: 0.37
DE  Interaction: Q9H4I2; IntAct: EBI-9081198; Score: 0.37
DE  Interaction: O75094; IntAct: EBI-9081190; Score: 0.37
DE  Interaction: Q96JM7; IntAct: EBI-9081178; Score: 0.49
DE  Interaction: P02751; IntAct: EBI-9081162; Score: 0.37
DE  Interaction: P27918; IntAct: EBI-9081158; Score: 0.37
DE  Interaction: Q4LDE5; IntAct: EBI-9081150; Score: 0.37
DE  Interaction: Q9UHV2; IntAct: EBI-9081142; Score: 0.37
DE  Interaction: Q9BXP5; IntAct: EBI-9081154; Score: 0.37
DE  Interaction: A7KAX9; IntAct: EBI-9081134; Score: 0.49
DE  Interaction: P31629; IntAct: EBI-9081015; Score: 0.49
DE  Interaction: P21675; IntAct: EBI-9080967; Score: 0.37
DE  Interaction: Q96D15; IntAct: EBI-9080963; Score: 0.37
DE  Interaction: Q5VWN6; IntAct: EBI-9080983; Score: 0.37
DE  Interaction: Q58WW2; IntAct: EBI-9080923; Score: 0.37
DE  Interaction: P10253; IntAct: EBI-9080919; Score: 0.37
DE  Interaction: Q9BTY2; IntAct: EBI-9080915; Score: 0.37
DE  Interaction: P02794; IntAct: EBI-9080911; Score: 0.37
DE  Interaction: Q9Y3M2; IntAct: EBI-9080895; Score: 0.37
DE  Interaction: Q86VK4; IntAct: EBI-9080879; Score: 0.37
DE  Interaction: Q9Y2X9; IntAct: EBI-9080875; Score: 0.37
DE  Interaction: Q9H0D6; IntAct: EBI-9080867; Score: 0.37
DE  Interaction: Q8N6Y0; IntAct: EBI-9080855; Score: 0.37
DE  Interaction: Q15643; IntAct: EBI-9080851; Score: 0.37
DE  Interaction: Q9UBK9; IntAct: EBI-9080859; Score: 0.37
DE  Interaction: Q9NVV9; IntAct: EBI-9080835; Score: 0.37
DE  Interaction: O43294; IntAct: EBI-9080831; Score: 0.37
DE  Interaction: P40763; IntAct: EBI-9080823; Score: 0.37
DE  Interaction: Q9HCB6; IntAct: EBI-9080815; Score: 0.37
DE  Interaction: O60687; IntAct: EBI-9080819; Score: 0.37
DE  Interaction: Q92932; IntAct: EBI-9079788; Score: 0.37
DE  Interaction: P55347; IntAct: EBI-9079780; Score: 0.37
DE  Interaction: Q5VST9; IntAct: EBI-9079768; Score: 0.37
DE  Interaction: P07197; IntAct: EBI-9079764; Score: 0.37
DE  Interaction: Q96HC4; IntAct: EBI-9079776; Score: 0.37
DE  Interaction: P07196; IntAct: EBI-9079734; Score: 0.37
DE  Interaction: O14594; IntAct: EBI-9079730; Score: 0.37
DE  Interaction: Q9HAP2; IntAct: EBI-9079718; Score: 0.37
DE  Interaction: P55268; IntAct: EBI-9079698; Score: 0.37
DE  Interaction: P17661; IntAct: EBI-9078577; Score: 0.37
DE  Interaction: Q9NP73; IntAct: EBI-9078573; Score: 0.37
DE  Interaction: P29279; IntAct: EBI-9078569; Score: 0.37
DE  Interaction: Q8IZ52; IntAct: EBI-9078565; Score: 0.37
DE  Interaction: Q8TEP8; IntAct: EBI-9078561; Score: 0.37
DE  Interaction: Q9HCU4; IntAct: EBI-9078553; Score: 0.37
DE  Interaction: O94986; IntAct: EBI-9078557; Score: 0.37
DE  Interaction: Q9UJX2; IntAct: EBI-9078549; Score: 0.37
DE  Interaction: O43866; IntAct: EBI-9078533; Score: 0.49
DE  Interaction: Q8TD31; IntAct: EBI-9078529; Score: 0.49
DE  Interaction: Q8NBZ0; IntAct: EBI-9078525; Score: 0.37
DE  Interaction: A2RUB6; IntAct: EBI-9078521; Score: 0.49
DE  Interaction: Q8N0Z3; IntAct: EBI-9078517; Score: 0.37
DE  Interaction: Q494V2; IntAct: EBI-9078513; Score: 0.37
DE  Interaction: Q96H12; IntAct: EBI-9078509; Score: 0.37
DE  Interaction: Q6P1W5; IntAct: EBI-9078505; Score: 0.37
DE  Interaction: Q7L4P6; IntAct: EBI-9078501; Score: 0.37
DE  Interaction: Q9H9L4; IntAct: EBI-9078497; Score: 0.37
DE  Interaction: Q8IX21; IntAct: EBI-9078493; Score: 0.37
DE  Interaction: O95153; IntAct: EBI-9078489; Score: 0.37
DE  Interaction: P41182; IntAct: EBI-9078485; Score: 0.37
DE  Interaction: Q8IXJ9; IntAct: EBI-9078481; Score: 0.37
DE  Interaction: P27540; IntAct: EBI-9078477; Score: 0.37
DE  Interaction: Q15052; IntAct: EBI-9078473; Score: 0.37
DE  Interaction: O15084; IntAct: EBI-9078465; Score: 0.37
DE  Interaction: Q6UB98; IntAct: EBI-9078461; Score: 0.37
DE  Interaction: Q9P0V9; IntAct: EBI-9078457; Score: 0.37
DE  Interaction: P53365; IntAct: EBI-9078469; Score: 0.37
DE  Interaction: O15230; IntAct: EBI-9079694; Score: 0.37
DE  Interaction: Q9UMX0; IntAct: EBI-9081809; Score: 0.37
DE  Interaction: O94966; IntAct: EBI-9081761; Score: 0.55
DE  Interaction: Q9H7B4; IntAct: EBI-9081757; Score: 0.55
DE  Interaction: O00499; IntAct: EBI-9081765; Score: 0.75
DE  Interaction: Q9BQ52; IntAct: EBI-9081733; Score: 0.37
DE  Interaction: P68371; IntAct: EBI-9081781; Score: 0.37
DE  Interaction: Q76N32; IntAct: EBI-9081773; Score: 0.37
DE  Interaction: Q9H0Q3; IntAct: EBI-9081797; Score: 0.37
DE  Interaction: Q86U42; IntAct: EBI-9081829; Score: 0.37
DE  Interaction: O15523; IntAct: EBI-9081817; Score: 0.37
DE  Interaction: Q9UHF1; IntAct: EBI-9081821; Score: 0.37
DE  Interaction: Q9UBW7; IntAct: EBI-9081957; Score: 0.37
DE  Interaction: Q5T3F8; IntAct: EBI-9081949; Score: 0.37
DE  Interaction: Q9HAU4; IntAct: EBI-9081933; Score: 0.51
DE  Interaction: Q96M27; IntAct: EBI-9081917; Score: 0.37
DE  Interaction: O14777; IntAct: EBI-9081913; Score: 0.37
DE  Interaction: Q9UBU8; IntAct: EBI-9081905; Score: 0.37
DE  Interaction: Q96NW7; IntAct: EBI-9081901; Score: 0.37
DE  Interaction: P52294; IntAct: EBI-9081897; Score: 0.51
DE  Interaction: P61978; IntAct: EBI-9081893; Score: 0.37
DE  Interaction: Q8TES7; IntAct: EBI-9081885; Score: 0.37
DE  Interaction: Q6ZS17; IntAct: EBI-9081881; Score: 0.37
DE  Interaction: P41567; IntAct: EBI-9081877; Score: 0.37
DE  Interaction: P68104; IntAct: EBI-9081873; Score: 0.37
DE  Interaction: Q96N67; IntAct: EBI-9081869; Score: 0.37
DE  Interaction: P10515; IntAct: EBI-9081865; Score: 0.37
DE  Interaction: P00414; IntAct: EBI-9081861; Score: 0.37
DE  Interaction: Q6P2H3; IntAct: EBI-9081857; Score: 0.51
DE  Interaction: Q9Y2B5; IntAct: EBI-9081853; Score: 0.37
DE  Interaction: Q16548; IntAct: EBI-9081845; Score: 0.37
DE  Interaction: O14874; IntAct: EBI-9081841; Score: 0.51
DE  Interaction: P61769; IntAct: EBI-9081837; Score: 0.37
DE  Interaction: Q9Y228; IntAct: EBI-9081965; Score: 0.37
DE  Interaction: O43889; IntAct: EBI-9081961; Score: 0.37
DE  Interaction: Q8TBC4; IntAct: EBI-9081953; Score: 0.37
DE  Interaction: P24557; IntAct: EBI-9081945; Score: 0.37
DE  Interaction: Q9UMS6; IntAct: EBI-9081941; Score: 0.37
DE  Interaction: Q9UJF2; IntAct: EBI-9081925; Score: 0.51
DE  Interaction: P28065; IntAct: EBI-9081921; Score: 0.51
DE  Interaction: Q13438; IntAct: EBI-9082142; Score: 0.37
DE  Interaction: Q9H8S9; IntAct: EBI-9082045; Score: 0.51
DE  Interaction: O15015; IntAct: EBI-9082130; Score: 0.37
DE  Interaction: Q9NXP7; IntAct: EBI-9082126; Score: 0.37
DE  Interaction: Q8N1B4; IntAct: EBI-9082122; Score: 0.51
DE  Interaction: P82094; IntAct: EBI-9082101; Score: 0.37
DE  Interaction: P07996; IntAct: EBI-9082097; Score: 0.37
DE  Interaction: Q9H0F6; IntAct: EBI-9082085; Score: 0.37
DE  Interaction: Q9P2E9; IntAct: EBI-9082081; Score: 0.37
DE  Interaction: Q02543; IntAct: EBI-9082077; Score: 0.37
DE  Interaction: Q8WUF5; IntAct: EBI-9082069; Score: 0.51
DE  Interaction: Q15126; IntAct: EBI-9082065; Score: 0.37
DE  Interaction: Q9HBI0; IntAct: EBI-9082061; Score: 0.37
DE  Interaction: Q02818; IntAct: EBI-9082057; Score: 0.37
DE  Interaction: Q16621; IntAct: EBI-9082053; Score: 0.37
DE  Interaction: Q9ULW6; IntAct: EBI-9082049; Score: 0.51
DE  Interaction: G3V185; IntAct: EBI-9082041; Score: 0.37
DE  Interaction: Q7Z4I7; IntAct: EBI-9082037; Score: 0.37
DE  Interaction: P20701; IntAct: EBI-9082033; Score: 0.51
DE  Interaction: P15814; IntAct: EBI-9082029; Score: 0.37
DE  Interaction: Q13227; IntAct: EBI-9082025; Score: 0.51
DE  Interaction: Q08379; IntAct: EBI-9082021; Score: 0.51
DE  Interaction: Q14192; IntAct: EBI-9082017; Score: 0.37
DE  Interaction: Q96EY1; IntAct: EBI-9082009; Score: 0.37
DE  Interaction: Q03188; IntAct: EBI-9081997; Score: 0.37
DE  Interaction: Q8N7W2; IntAct: EBI-9081981; Score: 0.37
DE  Interaction: O15169; IntAct: EBI-9081977; Score: 0.37
DE  Interaction: P57075; IntAct: EBI-9082118; Score: 0.37
DE  Interaction: Q9H2D6; IntAct: EBI-9082109; Score: 0.37
DE  Interaction: O60504; IntAct: EBI-9082093; Score: 0.37
DE  Interaction: Q8N960; IntAct: EBI-9081993; Score: 0.37
DE  Interaction: Q86UW7; IntAct: EBI-9081989; Score: 0.37
DE  Interaction: Q9ULU8; IntAct: EBI-9081985; Score: 0.37
DE  Interaction: Q96MT8; IntAct: EBI-9082005; Score: 0.37
DE  Interaction: P53367; IntAct: EBI-9081973; Score: 0.37
DE  Interaction: P53396; IntAct: EBI-9081969; Score: 0.37
DE  Interaction: P08962; IntAct: EBI-9083739; Score: 0.37
DE  Interaction: Q15485; IntAct: EBI-9083586; Score: 0.37
DE  Interaction: P02753; IntAct: EBI-9083711; Score: 0.37
DE  Interaction: P81172; IntAct: EBI-9083707; Score: 0.37
DE  Interaction: Q9NPA0; IntAct: EBI-9083703; Score: 0.37
DE  Interaction: Q04941; IntAct: EBI-9083666; Score: 0.37
DE  Interaction: Q9HC24; IntAct: EBI-9083657; Score: 0.37
DE  Interaction: Q9Y320; IntAct: EBI-9083652; Score: 0.37
DE  Interaction: P03905; IntAct: EBI-9083644; Score: 0.37
DE  Interaction: P14209; IntAct: EBI-9083636; Score: 0.37
DE  Interaction: P27701; IntAct: EBI-9083632; Score: 0.37
DE  Interaction: P02647; IntAct: EBI-9083624; Score: 0.37
DE  Interaction: Q06481; IntAct: EBI-9083620; Score: 0.37
DE  Interaction: P02679; IntAct: EBI-9083590; Score: 0.37
DE  Interaction: Q9NY26; IntAct: EBI-9083599; Score: 0.37
DE  Interaction: P23378; IntAct: EBI-9083603; Score: 0.37
DE  Interaction: Q56VL3; IntAct: EBI-9083467; Score: 0.37
DE  Interaction: Q6UX53; IntAct: EBI-9083544; Score: 0.37
DE  Interaction: P23284; IntAct: EBI-9980884; Score: 0.61
DE  Interaction: P01009; IntAct: EBI-9083366; Score: 0.37
DE  Interaction: P02750; IntAct: EBI-9083459; Score: 0.37
DE  Interaction: P06733; IntAct: EBI-9083322; Score: 0.37
DE  Interaction: O14818; IntAct: EBI-9083370; Score: 0.37
DE  Interaction: P26641; IntAct: EBI-9077454; Score: 0.37
DE  Interaction: Q6N075; IntAct: EBI-9083729; Score: 0.37
DE  Interaction: P04920; IntAct: EBI-9083721; Score: 0.37
DE  Interaction: Q99942; IntAct: EBI-9083717; Score: 0.37
DE  Interaction: Q00765; IntAct: EBI-9083725; Score: 0.37
DE  Interaction: P25311; IntAct: EBI-9083694; Score: 0.37
DE  Interaction: P22310; IntAct: EBI-9083680; Score: 0.37
DE  Interaction: Q06055; IntAct: EBI-9083661; Score: 0.37
DE  Interaction: P04114; IntAct: EBI-9083628; Score: 0.37
DE  Interaction: Q96EC8; IntAct: EBI-9083607; Score: 0.37
DE  Interaction: Q8N6L1; IntAct: EBI-9083548; Score: 0.37
DE  Interaction: Q9P0B6; IntAct: EBI-9083475; Score: 0.37
DE  Interaction: O96005; IntAct: EBI-9083463; Score: 0.37
DE  Interaction: Q15084; IntAct: EBI-9083435; Score: 0.37
DE  Interaction: P05182; IntAct: EBI-9083492; Score: 0.37
DE  Interaction: Q15388; IntAct: EBI-9083427; Score: 0.37
DE  Interaction: Q8TCT9; IntAct: EBI-9083382; Score: 0.37
DE  Interaction: P00167; IntAct: EBI-9083471; Score: 0.37
DE  Interaction: Q15166; IntAct: EBI-9083676; Score: 0.37
DE  Interaction: O75306; IntAct: EBI-9083354; Score: 0.37
DE  Interaction: P05141; IntAct: EBI-9083350; Score: 0.37
DE  Interaction: P02792; IntAct: EBI-9083338; Score: 0.37
DE  Interaction: P38117; IntAct: EBI-9083334; Score: 0.37
DE  Interaction: P47813; IntAct: EBI-9083318; Score: 0.37
DE  Interaction: Q08830; IntAct: EBI-9083595; Score: 0.37
DE  Interaction: P00734; IntAct: EBI-9083581; Score: 0.37
DE  Interaction: O95789; IntAct: EBI-9083733; Score: 0.37
DE  Interaction: Q9P035; IntAct: EBI-9083168; Score: 0.51
DE  Interaction: Q14318; IntAct: EBI-9084705; Score: 0.80
DE  Interaction: Q9UKC9; IntAct: EBI-9099770; Score: 0.40
DE  Interaction: P27105; IntAct: EBI-10092811; Score: 0.59
DE  Interaction: P54116; IntAct: EBI-10074676; Score: 0.27
DE  Interaction: Q70UQ0; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q9Y3I0; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q16880; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q92499; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: P60468; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q15629; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q9UGP8; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: O75127; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: P08574; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q03154; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: O14598; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: P53985; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q07021; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q9UNL2; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q53GQ0; IntAct: EBI-11513187; Score: 0.50
DE  Interaction: P28288; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q9Y605; IntAct: EBI-11513238; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-11513238; Score: 0.35
DE  Interaction: Q15758; IntAct: EBI-11513238; Score: 0.35
DE  Interaction: O00264; IntAct: EBI-11513238; Score: 0.35
DE  Interaction: F5GZS6; IntAct: EBI-11513238; Score: 0.35
DE  Interaction: O43504; IntAct: EBI-11513238; Score: 0.50
DE  Interaction: O14980; IntAct: EBI-11513409; Score: 0.50
DE  Interaction: P78527; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q92973; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q969Z0; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P49411; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q16637; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q99615; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q13885; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P43487; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: O43175; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: C9JDS9; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P0DME0; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q9HAV4; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q86Y56; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P53618; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q6NXR4; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q96PU8; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q9UPT5; IntAct: EBI-11513409; Score: 0.50
DE  Interaction: Q9Y277; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q13148; IntAct: EBI-11513409; Score: 0.50
DE  Interaction: P22102; IntAct: EBI-11513409; Score: 0.35
DE  Interaction: Q9NVI1; IntAct: EBI-11513452; Score: 0.35
DE  Interaction: O43852; IntAct: EBI-11513452; Score: 0.35
DE  Interaction: Q12905; IntAct: EBI-11515481; Score: 0.40
DE  Interaction: Q9H4A3; IntAct: EBI-11513452; Score: 0.35
DE  Interaction: Q7Z6Z7; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: Q3V6T2; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: P38646; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: Q9P219; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: Q9UHI6; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: P08754; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: Q9UNF1; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: Q7L9L4; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: Q9GZT9; IntAct: EBI-11513460; Score: 0.50
DE  Interaction: A8KA83; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-11513460; Score: 0.35
DE  Interaction: Q9BQG0; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: O95373; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: Q4VCS5; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: Q9GZU8; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: Q9NX58; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: Q9HB71; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: P12277; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: Q13451; IntAct: EBI-11513489; Score: 0.50
DE  Interaction: P07900; IntAct: EBI-11513489; Score: 0.35
DE  Interaction: P11586; IntAct: EBI-11513985; Score: 0.40
DE  Interaction: O75344; IntAct: EBI-11688279; Score: 0.60
DE  Interaction: Q8WXG1; IntAct: EBI-12738366; Score: 0.43
GO  GO:0030430;
GO  GO:0044165;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0033650;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0032991;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0003779;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0042802;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075520;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0075519;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0039690;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0019079;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQPEGRAWAQPG
SQ  YPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNVSGVYHVTNDCSNASIVYEAADMIMHTPGCVPCVRENNSSRCWV
SQ  ALTPTLAARNASVPTTTIRRHVDLLVGAAALCSAMYVGDLCGSVFLVAQLFTFSPRRHETVQDCNCSIYPGHVTGHRMAW
SQ  DMMMNWSPTAALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMVGNWAKVLIVMLLFAGVDGGTYVTGGTMAKNTLGIT
SQ  SLFSPGSSQKIQLVNTNGSWHINRTALNCNDSLNTGFLAALFYVHKFNSSGCPERMASCSPIDAFAQGWGPITYNESHSS
SQ  DQRPYCWHYAPRPCGIVPAAQVCGPVYCFTPSPVVVGTTDRFGVPTYSWGENETDVLLLNNTRPPQGNWFGCTWMNSTGF
SQ  TKTCGGPPCNIGGIGNKTLTCPTDCFRKHPEATYTKCGSGPWLTPRCLVHYPYRLWHYPCTVNFTIFKVRMYVGGVEHRL
SQ  EAACNWTRGERCNLEDRDRSELSPLLLSTTEWQVLPCSFTTLPALSTGLIHLHQNVVDVQYLYGIGSAVVSFAIKWEYVL
SQ  LLFLLLADARVCACLWMMLLIAQAEAALENLVVLNAASVAGAHGILSFLVFFCAAWYIKGRLVPGAAYALYGVWPLLLLL
SQ  LALPPRAYAMDREMAASCGGAVFVGLILLTLSPHYKLFLARLIWWLQYFITRAEAHLQVWIPPLNVRGGRDAVILLTCAI
SQ  HPELIFTITKILLAILGPLMVLQAGITKVPYFVRAHGLIRACMLVRKVAGGHYVQMALMKLAALTGTYVYDHLTPLRDWA
SQ  HAGLRDLAVAVEPVVFSDMETKVITWGADTAACGDIILGLPVSARRGREIHLGPADSLEGQGWRLLAPITAYSQQTRGLL
SQ  GCIITSLTGRDRNQVEGEVQVVSTATQSFLATCVNGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWQAPPGARSL
SQ  TPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHAVGIFRAAVCTRGVAKAVDFVPVES
SQ  METTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRT
SQ  GVRTITTGAPITYSTYGKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHP
SQ  NIEEVALSSTGEIPFYGKAIPIETIKGGRHLIFCHSKKKCDELAAKLSGLGLNAVAYYRGLDVSVIPTSGDVIVVATDAL
SQ  MTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRMGIYRFVTPGERPSGMFDSSVLCEC
SQ  YDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAP
SQ  PPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVTTTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSV
SQ  VIVGRIILSGKPAIIPDREVLYREFDEMEECASHLPYIEQGMQLAEQFKQKAIGLLQTATKQAEAAAPVVESKWRTLEAF
SQ  WAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQHTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVG
SQ  SIGLGKVLVDILAGYGAGVAGALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLRDVWDWICTVLTDFKTWLQSKLL
SQ  PRLPGVPFFSCQRGYKGVWRGDGIMQTTCPCGAQITGHVKNGSMRIVGPRTCSNTWHGTFPINAYTTGPCTPSPAPNYSR
SQ  ALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPACKPLLREEVTFLVGLNQYLVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTRHDSPDADLIEANLLWRQEMGGN
SQ  ITRVESENKVVILDSFEPLQAEEDEREVSVPAEILRRSRKFPRAMPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPPAK
SQ  APPIPPPRRKRTVVLSESTVSSALAELATKTFGSSESSAVDSGTATASPDQPSDDGDAGSDVESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSEEASEDVVCCSMSYTWTGALITPCAAEETKLPINALSNSLLRHHNLVYATTSRSASLRQKKVTFDRLQVLD
SQ  DHYRDVLKEMKAKASTVKAKLLSVEEACKLTPPHSARSKFGYGAKDVRNLSSKAVNHIRSVWKDLLEDTETPIDTTIMAK
SQ  NEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPGQRVEFLVNAWKAKKCPMGFAYDT
SQ  RCFDSTVTENDIRVEESIYQCCDLAPEARQAIRSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKAAA
SQ  ACRAAKLQDCTMLVCGDDLVVICESAGTQEDEASLRAFTEAMTRYSAPPGDPPKPEYDLELITSCSSNVSVAHDASGKRV
SQ  YYLTRDPTTPLARAAWETARHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQ
SQ  IIQRLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRARLLSQGGRAATCGKYLFNWAVRTKLKLTPIPA
SQ  ASQLDLSSWFVAGYSGGDIYHSLSRARPRWFMWCLLLLSVGVGIYLLPNR
//
ID  O39929;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356418;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: O39929;
DR  PDB: 6P6Z;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRSWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPSWGPNDPRGRSRNLGKVIDTLTCGFADLMGYIPLVGAPVGSVARALAHGVRALED
SQ  GINYATGNLPGCSFSIFLLALLSCLTVPASAVNYRNVSGIYHVTNDCPNSSIVYEADHHIMHLPGCVPCVREGNQSRCWV
SQ  ALTPTVAAPYIGAPLESLRSHVDLMVGAATVCSGLYIGDLCGGLFLVGQMFSFRPRRHWTTQDCNCSIYTGHITGHRMAW
SQ  DMMMNWSPTTTLVLAQVMRIPTTLVDLLSGGHWGVLVGVAYFSMQANWAKVILVLFLFAGVDAETHVSGAAVGRSTAGLA
SQ  NLFSSGSKQNLQLINSNGSWHINRTALNCNDSLNTGFLASLFYTHKFNSSGCSERLACCKSLDSYGQGWGPLGVANISGS
SQ  SDDRPYCWHYAPRPCGIVPASSVCGPVYCFTPSPVVVGTTDHVGVPTYTWGENETDVFLLNSTRPPHGAWFGCVWMNSTG
SQ  FTKTCGAPPCEVNTNNGTWHCPTDCFRKHPETTYAKCGSGPWITPRCLIDYPYRLWHFPCTANFSVFNIRTFVGGIEHRM
SQ  QAACNWTRGEVCGLEHRDRVELSPLLLTTTAWQILPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSAVVSWALKWEYVV
SQ  LAFLLLADARVSAYLWMMFMVSQVEAALSNLININAASAAGAQGFWYAILFICIVWHVKGRFPAAAAYAACGLWPCFLLL
SQ  LMLPERAYAYDQEVAGSLGGAIVVMLTILTLSPHYKLWLARGLWWIQYFIARTEAVLHVYIPSFNVRGPRDSVIVLAVLV
SQ  CPDLVFDITKYLLAILGPLHILQASLLRIPYFVRAQALVKICSLLRGVVYGKYFQMVVLKSRGLTGTYIYDHLTPMSDWP
SQ  PYGLRDLAVALEPVVFTPMEKKVIVWGADTAACGDIIRGLPVSARLGNEILLGPADTETSKGWRLLAPITAYAQQTRGLF
SQ  STIVTSLTGRDTNENCGEVQVLSTATQSFLGTAVNGVMWTVYHGAGAKTISGPKGPVNQMYTNVDQDLVGWPAPPGVRSL
SQ  APCTCGSADLYLVTRHADVIPVRRRGDTRGALLSPRPISILKGSSGGPLLCPMGHRAGIFRAAVCTRGVAKAVDFVPVES
SQ  LETTMRSPVFTDNSTPPAVPQTYQVAHLHAPTGSGKSTKVPAAHAAQGYKVLVLNPSVAATLGFGVYMSKAYGIDPNIRS
SQ  GVRTITTGAPITYSTYGKFLADGGCSGGAYDIIICDECYSTDSTTILGIGTVLDQAETAGVRLTVLATATPPGSVTTPHS
SQ  NIEEVALPTTGEIPFYGKAIPLELIKGGRHLIFCHSKKKCDELARQLTSLGLNAVAYYRGLDVSVIPTSGDVVVCATDAL
SQ  MTGFTGDFDSVIDCNTSVIQTVDFSLDPTFSIEITTVPQDAVSRSQRRGRTGRGRLGTYRYVTPGERPSGMFDTAELCEC
SQ  YDAGCAWYELTPAETTTRLKAYFDTPGLPVCQDHLEFWESVFTGLTHIDGHFLSQTKQSGENFPYLVAYQATVSAKVWLA
SQ  PPSWDTMWKCLIRLKPTLHGPTPLLYRLGSVQNEVVLTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLSVGSV
SQ  VIVGRVVLSGQPAVIPDREVLYQQFDEMEECSKHLPLVEHGLQLAEQFKQKALGLLNFAGKQAQEATPVIQSNFAKLEQF
SQ  WANDMWNFISGIQYLAGLSTLPGNPAIASLMSFTAAVTSPLTTQQTLLFNILGGWVASQIRDSDASTAFVVSGLAGAAVG
SQ  SVGLGKILVDILPGYGAGVRGAVVTFKIMSGEMPSTEDLVNLLPAILSPGALVVEVVCPAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAARRVTTILSSLTVTSLLRRLHKWINEDCSTPCAESWLWEVWDWVLHVLSDFKTCLKAKFV
SQ  PLMPGIPLLSWPRGYKGEWRGDGVMHTTCPCGADLAGHIKNGSMRITGPKTCSNTWHGTFPINAYTTGPGVPIPAPNYKF
SQ  ALWRVSAEDYVEVRRVGDFHYVTGVTQDNIKFPCQVPAPELFTEVDGIRIHRHAPKCKPLLRDEVSFSVGLNSFVVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAESARRRLARGSRPSLASSSASQLSPRLLQATCTAPHDSPGTDLLEANLLWGSTATRV
SQ  ETDEKVIILDSFESCVAEQNDDREVSVAAEILRPTKKFPPALPIWARPDYNPPLTETWKQQDYQAPTVHGCALPPAKQPP
SQ  VPSPRRKRTVQLTESVVSTALAELAAKTFGQSEPSSDRDTDLTTPTETTDSGPIVVDDASDDGSYSSMPPLEGEPGDPDL
SQ  TSDSWSTVSGSEDVVCCSMSYSWTGALVTPCAAEESKLPISPLSNSLLRHHNMVYATTTRSAVTRQKKVTFDRLQVVDST
SQ  YNEVLKEIKARASRVKPRLLTTEEACDLTPPHSARSKFGYGKKDVRSHSRKAINHISSVWKDLLDDNNTPIPTTIMAKNE
SQ  VFAVNPAKGGRKPARLIVYPDLGSRVCEKRALHDVIKKTALAVMGAAYGFQYSPAQRVEFLLTAWKSKNDPMGFSYDTRC
SQ  FDSTVTEKDIRVEEEVYQCCDLEPEARKVITALTDRLYVGGPMHNSKGDLCGYRRCRATGVYTTSFGNTLTCYLKATAAI
SQ  RAAALRDCTMLVCGDDLVVIAESDGVEEDNRALRAFTEAMTRYSAPPGDAPQPAYDLELITSCSSNVSVAHDVTGKKVYY
SQ  LTRDPETPLARAVWETVRHTPVNSWLGNIIVYAPTIWVRMILMTHFFSILQSQEALEKALDFDMYGVTYSITPLDLPAII
SQ  QRLHGLSAFTLHGYSPHELNRVAGALRKLGVPPLRAWRHRARAVRAKLIAQGGRAKICGIYLFNWAVKTKLKLTPLPAAA
SQ  KLDLSGWFTVGAGGGDIYHSMSHARPRYLLLCLLILTVGVGIFLLPAR
//
ID  O39927;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356420;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: O39927;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTLPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRKGPRLGVRATRKTSERSQPRGRRQPIPKARQPQGRHWAQPG
SQ  YPWPLYGSEGCGWAGWLLSPRGSRPHWGPNDPRRRSRNLGKVIDTLTCGFADLMWYIPVVGAPLGGVAAALAHGVRAIED
SQ  GINYATGNLPGCSFSIFLLALLSCLTTPASALTYGNSSGLYHLTNDCSNSSIVLEADAMILHLPGCLPCVRVGNQSTCWH
SQ  AVSPTLATPNASTPATGFRRHVDLLAGAAVVCSSLYIGDLCGSLFLAGQLFAFQPRRHWTVQDCNCSIYTGHVTGHKMAW
SQ  DMMMNWSPTTTLVLSSILRVPEICASVIFGGHWGILLAVAYFGMAGNWLKVLAVLFLFAGVEAQTMIAHGVSQTTSGFAS
SQ  LLTPGAKQNIQLINTNGSWHINRTALNCNDSLQTGFLASLFYTHKFNSSGCPERMAACKPLAEFRQGWGQITHKNVSGPS
SQ  DDRPYCWHYAPRPCEVVPARSVCGPVYCFTPSPVVVGTTDKRGNPTYTWGENETDVFMLESLRPPTGGWFGCTWMNSTGF
SQ  TKTCGAPPCQIVPGNYNSSANELLCPTDCFRKHPEATYQRCGSGPWVTPRCLVDYAYRLWHYPCTVNFTLHKVRMFVGGT
SQ  EHRFDVACNWTRGERCELHDRNRIEMSPLLFSTTQLSILPCSFSTMPALSTGLIHLHQNIVDVQYLYGVSTNVTSWVVKW
SQ  EYIVLMFLVLADARICTCLWLMLLISTVEAAVERLVVLNAASAAGTAGWWWAVLFLCCVWYVKGRLVPACTYMALGMWPL
SQ  LLTILALPPRAYAMDNEQAASLGAVGLLVITIFSITPMYKKLLNCFIWWNQYFLARAEAMVHEWVPDLRVRGGRDSIILL
SQ  TCLLHPQLGFEVTKILLAVLAPLYILQYSLLKVPYFVRAHILLRACLLVRRLAGGKYVQACLLRLGAWTGTFVYDHLAPL
SQ  SDWASDGLRDLAVAVEPVIFSPMEKKIITWGADTAACGDILSGLPVSARLGNLVLLGPADDMQRGGWKLLAPITAYAQQT
SQ  RGLVGTIVTSLTGRDKNEVEGEVQVVSTDTQSFVATSINGVMWTVYHGPGFKTLAGPKGPVCQMYTNVDLDLVGWPSPPG
SQ  ARSLTPCNCGSSDLYLVTREADVIPARRRGDSRAALLSPRPISTLKGSSGGPIMCPSGHVVGLFRAAVCTRGVAKSLDFI
SQ  PVENMETTMRSPSFTDNSTPPAVPQTYQVGYLHAPTGSGKSTRVPAAYASQGYKVLVLNPSVAATLSFGSYMRQAYGVEP
SQ  NIRTGVRTVTTGGAITYSTYGEFLADGGCSGGAYDIIICDECHSTDPTTVLGVGTVLDQAETAGVRLTVLPTATPPGSVT
SQ  VPHPNITETALPTTGEIPFYGKAIPLEYIKGGRHLIFCHSKKKCDELAGKLKSLGLNAVAFYRGVDVSVIPTSGDVVVCA
SQ  TDALMTGYTGDFDSVIDCNVAVTQVVDFSLDPTFSIETTTVPQDAVSRSQRRGRTGRGKPGVYRFVSQGERPSGMFDTVV
SQ  LCEAYDTGCAWYELTPSETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSHTKQAGENFAYLVAYQATVCAR
SQ  AKAPPPSWDMMWKCLIRLKPTLTGPTPLLYRLGAVQNGVITTHPITKYIMTCMSADLEVITSTWVLVGGVLAALAAYCLS
SQ  VGCVVICGRITLTGKPAVVPDREILYQQFDEMEECSRHIPYLAEGQQIAEQFRQKVLGLLQASAKQAEELKPAVHSAWPR
SQ  VEDFWRKHMWNFVSGIQYLAGLSTLPGNPAVASLMSFTASLTSPLRTSQTLLLNILGGWIAAQVAPPPASTAFVVSGLAG
SQ  AAVGSIRLGRVLVDVLAGYGAGVSGALVAFKIMSGECPSTEDMVNLLPALLSPGVALVGVVCAAILRRHVGPAEGANQWM
SQ  NRLIAFASRGNHVSPTHYVPETDASKNVTQILTSLTITSLLRRLHQWVNEDTATPCATSWLRDVWDWVCTVLSDFKVWLQ
SQ  AKLFPRLPGIPFLSCQAGYRGVWAGDGVCHTTCTCGAVIAGHVKNGTMKITGPKTCSNTWHGTFPINATTTGPSTPRPAP
SQ  NYQRALWRVSAEDYVEVRRLGDCHYVVGVTAEGLKCPCQVPAPEFFTEVDGVRIHRYAPPCKPLLRDEVTFSVGLSNYAV
SQ  GSQLPCEPEPDVTVVTSMLTDPTHITAETAARRLKKGSPPSLASSSANQLSAPSLRATCTTSQKHPEMELLQANLLWKHE
SQ  MGSHIPRVQSENKVVVLDSFELYPLEYEEREISVSVECHRQPRCKFPPVFPVWARPDNNPPFIQAWQMPGYEPPVVSGCA
SQ  VAPPKPAPVPPPRRKRLVHLDESTVSHALAQLADKVFVESSNDPGPSSDSGLSITSPVPPDPTTPEDAGSEAESYSSMPP
SQ  LEGEPGDPDLSSGSWSTVSDEDDVVCCSMSYSWTGALITPCAAEEEKLPINPLSNSLVRHHNMVYSTTSRSASLRQKKVT
SQ  FDRVQVFDQHYQDVLKEIKLRASTVQAKLLSIEEACDLTPSHSARSKYGYGAQDVRSRASKAVDHIPSVWEGLLEDSDTP
SQ  IPTTIMAKNEVFCVDPSKGGRKPARLIVYPDLGVRVCEKMALYDVTQKLPQAVMGPAYGFQYSPNQRVEYLLKMWRSKKV
SQ  PMGFSYDTRCFDSTVTERDIRTENDIYQSCQLDPVARRVVSSLTERLYVGGPMANSKGQSCGYRRCRASGVLPTSMGNTL
SQ  TCYLKAQAACRAANIKDCDMLVCGDDLVVICESAGVQEDTASLRAFTDAMTRYSAPPGDAPQPTYDLELITSCSSNVSVA
SQ  HEGNGKKYYYLTRDCTTPLARAAWETARHTPVNSWLGNIIMFAPTIWVRMVLMNHFFSILQSQEQLEKAFDFDIYGVTYS
SQ  VSPLDLPAIIQRLHGMAAFSLHGYSPVELNRVGACLRKLGVLPSRAWRHRARAVRAKLIAQGGKAAICGKYLFNWAVKTK
SQ  LKLTPLVSASKLDLSGWFVAGYDGGDIYHSVSQARPRFLLLGLLLLTVGVGIFLLPAR
//
ID  O39928;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356419;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: O39928;
DR  PDB: 2M6X;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPKLGVRATRKNSERSQPRGRRQPIPKARRPTGRSWGQPG
SQ  YPWPLYANEGLGWAGWLLSPRSSRPNWGPNDPRRKSPNLGRVIHTLTCGFPHLMGYIPLVGGPVGGVSRALAHGVKVLED
SQ  GINYATGNLPGCPFSIFVLALLWCLTVPASAVPYRNASGVYHVTNDCPNSSIVYEADNLILHAPGCVPCVLEDNVSRCWV
SQ  QITPTLSAPSFGAVTALLRRAVDYLAGGAAFCSALYVGDACGALSLVGQMFTYKPRQHTTVQDCNCSIYSGHITGHRMAW
SQ  DMMMKWSPTTALLMAQLLRIPQVVIDIIAGGHWGVLLAAAYFASTANWAKVILVLFLFAGVDGRTHTVGGTVGQGLKSLT
SQ  SFFNPGPQRQLQFVNTNGSWHINSTALNCNDSLQTGFIAGLMYAHKFNSSGCPERMSSCRPLAAFDQGWGTISYATISGP
SQ  SDDKPYCWHYPPRPCGVVPARDVCGPVYCFTPSPVVVGTTDRRGCPTYNWGSNETDILLLNNIRPPAGNWFGCTWMNSTG
SQ  FVKNCGAPPCNLGPTGNNSLKCPTDCFRKHPDATYTRCGSGPWLTPRCLVHYPYRLWHYPCTVNYTIFKVRMFIGGLEHR
SQ  LEAACNWTYGERCDLEDRDRAELSPLLHTTTQWAILPCSFTPTPALSTGLIHLHQNIVDTQYLYGLSSSIVSWAVKWEYI
SQ  MLVFLLLADARICTCLLILLLICQAEATCKNVIVLNAAAAAGNHGFFWGLLVVCLAWHVKGRLVPGATYLCLGVWPLLLV
SQ  RLLRPHRALALDSSDGGTVGCLVLIVLTIFTLTPGYKKKVVLVMWWLQYFIARVEAIIHVWVPPLQVKGGRDAVIMLTCL
SQ  FHPALGFEITKILFGILGPLYLLQHSLTKVPYFLRARALLRLCLLAKHLVYGKYVQAALLHLGRLTGTYIYDHLAPMKDW
SQ  AASGLRELTVATEPIVFSAMETKVITWGADTAACGNILAVLPVSARRGREIFLGPADDIKTSGWRLLAPITAYAQQTRGV
SQ  LGAIVLSLTGRDKNEAEGEVQFLSTATQTFLGICINGVMWTLFHGAGSKTLAGPKGPVVQMYTNVDKDLVGWPSPPGKGS
SQ  LTRCTCGSADLYLVTRHADVIPARRRGDTRASLLSPRPISYLKGSSGGPIMCPSGHVVGVFRAAVCTRGVAKALEFVPVE
SQ  NLETTMRSPVFTDNSTPPAVPHEFQVGHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATFGFGAYMSRAYGVDPNIR
SQ  TGVRTVTTGAGITYSTYGKFFADGGCSGGAYDVIICDECHSQDATTILGIGTVLDQAETAGARLVVLATAIPPGSVTTPH
SQ  PNIEEVALPSEGEIPFYGRAIPLVLIKGGRHLIFCHSKKKCDELAKQLTSLGVNAVAYYRGLDVAVIPATGDVVVCSTDA
SQ  LMTGFTGDFDSVIDCNSAVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRHGIYRYVSSGERPSGIFDSVVLCE
SQ  CYDAGCAWYDLTPAETTVRLRAYLNTPGLPVCQEHLEFWEGVFTGLTNIDAHMLSQAKQGGENFPYLVAYQATVCVRAKA
SQ  PPPSWDTMWKCMICLKPTLTGPTPLLYRLGAVQNEITLTHPITKYIMACMSADLEVITSTWVLVGGVVAALAAYCLTVGS
SQ  VAIVGRIILSGRPAITPDREVLYQQFDEMEECSASLPYVDEARAIAGQFKEKVLGLIGTAGQKAETLKPAATSMWSKAEQ
SQ  FWAKHMWNFVSGIQYLAGLSTLPGNPAVATLMSFTAAVTSPLTTHQTLLFNILGGWVASQIAPPTAATAFVVSGMAGAAV
SQ  GNIGLGRVLIDILAGYGTGVAGALVAFKIMCGERPTAEELVNLLPSILCPGALVVGVICAAVLRRHIGPGEGAVQWMNRL
SQ  IAFASRGNHGSPTHYVPETDASAKVTQLLSSLTVTSLLKRLHTWIGEDYSTPCDGTWLRAIWDWVCTALTDFKAWLQAKL
SQ  LPQLPGVPFFSCQKGYKGVWRGDGVNSTKCPCGATISGHVKNGTMRIVGPKLCSNTWQGTFPINATTTGPSVPAPAPNYK
SQ  FALWRVGAADYAEVRRVGDYHYITGVTQDNLKCPCQVPSPEFFTELDGVRIHRFAPPCNPLLREEVTFSVGLHSYVVGSQ
SQ  LPCEPEPDVTVLTSMLSDPAHITAETAKRRLNRGSPPSLANSSASQLSAPSLKATCTIQGHHPDADLIKANLLWRQCMGG
SQ  NITRVEAENKVEILDCFKPLKEEEDDREISVSADCFKKGPAFPPALPVWARPGYDPPLLETWKRPDYDPPQVWGCPIPPA
SQ  GPPPVPLPRRKRKPMELSDSTVSQVMADLADARFKVDTPSIEGQDSALGTSSQHDSGPEEKRDDNSDAASYSSMPPLEGE
SQ  PGDPDLSSGSWSTVSGEDNVVCCSMSYTWTGALITPCSAEEEKLPINPLSNTLLRHHNLVYSTSSRSAGLRQKKVTFDRL
SQ  QVLDDHYREVVDEMKRLASKVKARLLPLEEACGLTPPHSARSKYGYGAKEVRSLDKKALKHIEGVWQDLLDDSDTPLPTT
SQ  IMAKNEVFAVEPSKGGKKPARLIVYPDLGVRVCEKRALYDVAQKLPTALMGPSYGFQYSPAQRVDFLLKAWKSKKIPMAF
SQ  SYDTRCFDSTITEHDIMTEESIYQSCDLQPEARVAIRSLTQRLYCGGPMYNSKGQQCGYRRCRASGVFTTSMGNTMTCYI
SQ  KALASCRAAKLRDCTLLVCGDDLVAICESQGTHEDEASLRAFTEAMTRYSAPPGDPPVPAYDLELVTSCSSNVSVARDAS
SQ  GNRIYYLTRDPQVPLAKAAWETAKHSPVNSWLGNIIMYAPTLWARIVLMTHFFSVLQSQEQLEKTLAFEMYGSVYSVTPL
SQ  DLPAIIQRLHGLSAFSLHSYSPSEINRVASCLRKLGVPPLRAWRHRARAVRAKLIAQGGRAAICGIYLFNWAVKTKRKLT
SQ  PLADADRLDLSSWFTVGAGGGDIYHSMSRARPRNLLLCLLLLSVGVGIFLLPAR
//
ID  Q81754;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356410;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q81754;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRVGVRATRKTSERSQPRGRRQPIPKARRPEGRSWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPSWGPSDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTVPASAVGVRNSSGVYHVTNDCPNASVVYETENLIMHLPGCVPYVREGNASRCWV
SQ  SLSPTVAARDSRVPVSEVRRRVDSIVGAAAFCSAMYVGDLCGSIFLVGQIFTFSPRHHWTTQDCNCSIYPGHVTGHRMAW
SQ  DMMMNWSPTGALVVAQLLRIPQAIVDMIAGAHWGVLAGLAYYSMVGNWAKVVVVLLLFAGVDAETRVTGGAAGHTAFGFA
SQ  SFLAPGAKQKIQLINTNGSWHINRTALNCNESLDTGWLAGLLYYHKFNSSGCPERMASCQPLTAFDQGWGPITHEGNASD
SQ  DQRPYCWHYALRPCGIVPAKKVCGPVYCFTPSPVVVGTTDRAGVPTYRWGANETDVLLLNNSRPPMGNWFGCTWMNSSGF
SQ  TKTCGAPACNIGGSGNNTLLCPTDCFRKHPDATYSRCGSGPWLTPRCLVDYPYRLWHYPCTVNYTIFKIRMFVGGVEHRL
SQ  DAACNWTRGERCDLDDRDRAELSPLLLSTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGLSSAVTSWVIKWEYVV
SQ  LLFLLLADARICACLWMMLLISQVEAALENLIVLNAASLVGTHGIVPFFIFFCAAWYLKGKWAPGLAYSVYGMWPLLLLL
SQ  LALPQRAYALDQELAASCGATVFICLAVLTLSPYYKQYMARGIWWLQYMLTRAEALLQVWVPPLNARGGRDGVVLLTCVL
SQ  HPHLLFEITKIMLAILGPLWILQASLLKVPYFVRAHGLIRLCMLVRKTAGGQYVQMALLKLGAFAGTYIYNHLSPLQDWA
SQ  HSGLRDLAVATEPVIFSRMEIKTITWGADTAACGDIINGLPVSARRGREVLLGPADALTDKGWRLLAPITAYAQQTRGLL
SQ  GCIITSLTGRDKNQVEGEVQIVSTATQTFLATCVNGVCWTVYHGAGSRTIASASGPVIQMYTNVDQDLVGWPAPQGARSL
SQ  TPCTCGASDLYLVTRHADVIPVRRRGDNRGSLLSPRPISYLKGSSGGPLLCPMGHAVGIFRAAVCTRGVAKAVDFVPVES
SQ  LETTMRSPVFTDNSSPPTVPQSYQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNVRT
SQ  GVRTITTGSPITHSTYGKFLADGGCSGGAYDIIICDECHSVDATSILGIGTVLDQAETAGVRLTILATATPPGSVTVPHS
SQ  NIEEVALSTEGEIPFYGKAIPLNYIKGGRHLIFCHSKKKCDELAAKLVGLGVNAVAFYRGLDVSVIPTTGDVVVVATDAL
SQ  MTGYTGDFDSVIDCNTCVVQTVDFSLDPTFSIETSTVPQDAVSRSQRRGRTGRGKHGIYRYVSPGERPSGMFDSVVLCEC
SQ  YDAGCAWYELTPAETTVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARAKAP
SQ  PPSWDQMWKCLIRLKPTLTGATPLLYRLGGVQNEITLTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLSTGSV
SQ  VIVGRIILSGKPAVIPDREVLYREFDEMEECAAHIPYLEQGMHLAEQFKQKALGLLQTASKQAETITPAVHTNWQKLESF
SQ  WAKHMWNFVSGIQYLAGLSTLPGNPAIASLMSFTAAVTSPLTTQQTLLFNILGGWVAAQLAAPAAATAFVGAGITGAVIG
SQ  SVGLGKVLVDILAGYGAGVAGALVAFKIMSGEAPTAEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDASVRVTHILTSLTVTQLLKRLHVWISSDCTAPCAGSWLKDVWDWICEVLSDFKSWLKAKLM
SQ  PQLPGIPFVSCQRGYRGVWRGEGIMHARCPCGADITGHVKNGSMRIVGPKTCSNTWRGSFPINAHTTGPCTPSPAPNYTF
SQ  ALWRVSAEEYVEVRRLGDFHYITGVTTDKIKCPCQVPSPEFFTEVDGVRLHRYAPPCKPLLRDEVTFSIGLNEYLVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAETAARRLNRGSPPSLASSSASQLSAPSLKATCTTHHDSPDADLITANLLWRQEMGGN
SQ  ITRVESENKIVILDSFDPLVAEEDDREISVPAEILLKSKKFPPAMPIWARPDYNPPLVEPWKRPDYEPPLVHGCPLPPPK
SQ  PTPVPPPRRKRTVVLDESTVSSALAELATKTFGSSTTSGVTSGEAAESSPAPSCDGELDSEAESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSSDGGTEDVVCCSMSYSWTGALITPCAAEETKLPINALSNSLLRHHNLVYSTTSRSAGQRQKKVTFDRLQVL
SQ  DDHYRDVLKEAKAKASTVKAKLLSVEEACSLTPPHSARSKFGYGAKDVRSHSSKAIRHINSVWQDLLEDNTTPIDTTIMA
SQ  KNEVFCVKPEKGGRKPARLIVYPDLGVRVCEKRALYDVVKQLPIAVMGTSYGFQYSPAQRVDFLLNAWKSKKNPMGFSYD
SQ  TRCFDSTVTEADIRTEEDLYQSCDLVPEARAAIRSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTITCYLKAS
SQ  AACRAAKLRDCTMLVCGDDLVVICESAGVQEDAANLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKR
SQ  VYYLTRDPETPLARAAWETARHTPVNSWLGNIIMFAPTLWVRMVLMTHFFSILIAQEHLEKALDCEIYGAVHSVQPLDLP
SQ  EIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRARSVRATLLSQGGRAAICGKYLFNWAVKTKLKLTPLP
SQ  SASQLDLSNWFTGGYSGGDIYHSVSHVRPRWFFWCLLLLSVGVGIYLLPNR
//
ID  Q913D4;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356386;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q913D4;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQNVKFPGGGQIVGGVCLLPRRGPRVGVRATRKTSERSQPRGRRQPIPKARRPEGRSWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPSRGPSDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTVPASAVEVRNSSGIYHVTNDCPNASVVYETDSLIIHLPGCVPCVREGNASRCWV
SQ  SLSPTVAAKDPGVPVNEIRRHVDLIVGAAAFCSAMYVGDLCGSIFLVGQLFTLSPRRHWTTQDCNCSIYPGHVTGHRMAW
SQ  DMMMNWSPTGALVVAQLLRIPQAVLDMIAGAHWGVLAGPAYYSMVGNWAKVLVVLLLFAGVDATTQVTGGTAGRNAYRLA
SQ  SLFSTGPSQNIQLINSNGSWHINRTALNCNDSLHTGWVAALFYSHKFNSSGRPERMASCRPLTAFDQGWGPITYGGKASN
SQ  DQRPYCWHYAPRPCGIVPAKEVCGPVYCFTPSPVVVGTTDKYGVPTYTWGENETDVLLLNNSRPPIGNWFGCTWMNSTGF
SQ  TKTCGAPACNVGGSETNTLSCPTDCFRRHPDATYAKCGSGPWLNPRCMVDYPYRLWHYPCTVNYTIFKIRMFVGGIEHRL
SQ  TAACNWTRGERCDLDDRDRAELSPLLLSTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGLSSVVTSWAIRWEYVV
SQ  LLFLLLADARICACLWMMLLISQVEAALENLIVLNAASLAGTHGIVPFFIFFCAAWYLKGKWAPGLVYSVYGMWPLLLLL
SQ  LALPQRAYALDQELAASCGAVVFISLAVLTLSPYYKQYMARGIWWLQYMLTRAEALLHVWVPSLNARGGRDGAILLMCVL
SQ  HPHLLFDITKIMLAILGPLWILQASLLRVPYFVRAHGLIRLCMLVRKTAGGHYVQMALLKLGALTGTYIYNHLSPLQDWA
SQ  HGSLRDLAVATEPVIFSRMEIKTITWGADTAACGDIINGLPVSARRGREVLLGPADALTDKGWRLLAPITAYAQQTRGLL
SQ  GCIVTSLTGRDKNQVEGEIQIVSTATQTFLATCINGACWTVYHGAGSRTIASASGPVVRMYTNVDQDLVGWPAPQGARSL
SQ  TPCTCGASDLYLVTRHADVIPVRRRGDNRGSLLSPRPISYLKGSSGGPLLCPMGHVAGIFRAAVCTRGVAKAVDFVPVES
SQ  LETTMRSPVFTDNSSPPTVPQSYQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNVRT
SQ  GVRTITTGSPITYSTYGKFLADGGCPGGAYDIIICDECHSVDATSILGIGTVLDQAETAGVRLTVLATATPPGLVTVPHS
SQ  NIEEVALSADGEKPFYGKAIPLNYIKGGRHLIFCHSKKKCDELAAKLVGLGVNAVAFYRGLDVSVIPTTGDVVVVATDAL
SQ  MTGFTGDFDSVIDCNTCVVQTVDFSLDPIFSIETSTVPQDAVSRSQRRGRTGRGKHGIYRYVSPGERPSGMFDSVVLCEC
SQ  YDAGCAWYELTPAETTVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARARAP
SQ  PPSWDQMWKCLIRLKPTLTGATPLLYRLGSVQNEITLTHPITQYIMACMSADLEVVTSTWVLVGGVLAALAAYCLSTGSV
SQ  VIVGRIILGGKPAVIPDREVLYREFDEMEECAAHVPYLEQGMHLAGQFKQKALGLLQTASKQAETITPTVRTNWQKLESF
SQ  WAKHMWNFVSGIQYLAGLSTLPGNPAIASLMSFTAAVTSPLTTQQTLFFNILGGWVAAQLASPAAATAFVGAGITGAVVG
SQ  SVGLGKVLVDIIAGYGAGVAGALVAFKIMSGETPTTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDASARVTQILTSLTVTQLLKRLHVWISSDCIAPCASSWLKDVWDWICEVLSDFKNWLKAKLV
SQ  PQLPGIPFVSCQRGYRGVWRGEGIVHTRCPCGANITGHVKNGSMRIVGPKTCSNTWRGSFPINAYTTGPCTPSPAPNYTF
SQ  ALWRVSAEEYVEVRRLGDFHYVTGVTTDKLKCPCQVPSPEFFTEVDGVRLHRYAPPCKPLLREEVTFSIGLNEYLVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAETAARRLKRGSPPSLASSSASQLSAPSLKATCTTHHDSPDADLIEANLLWRQEMGGN
SQ  ITRVESENKIVVLDSFDPLVAEEDDREISIPAEILRKFKQFPPAMPIWARPDYNPPLVEPWKRPDYEPPLVHGCPLPPPK
SQ  PTPVPPPRRKRTVVLDESTVSSALAELATKTFGSSTTSGVTSGEATESSPAPSCGGELDSEAESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSSDGGTEDVVCCSMSYSWTGALITPCASEEAKLPINALSNSLLRHHNLVYSTTSRSAGQRQKKVTFDRVQVL
SQ  DDHYRDVLKEAKAKASTVKARLLSVEEACSLTPPHSARSKFGYGAKDVRSHSSKAIRHINSVWQDLLEDNTTPIDTTIMA
SQ  KNEVFCVKPEKGGRKPARLIVYPDLGVRVCEKRALYDVVKQLPIAVMGASYGFQYSPAQRVDFLLKAWKSKKVPMGFSYD
SQ  TRCFDSTVTEADIRTEEDLYQSCDLAPEARIAIRSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTITCFLKAS
SQ  AACRAAKLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVARDGAGKR
SQ  VYYLTRDPETPLARAAWETARHTPVNSWLGNIIMFAPTLWVRMVLMTHFFSILIAQEHLGKALDCEIYGAVHSVQPLDLP
SQ  EIIQRLHSLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRARSVRATLLSQGGKAAICGKYLFNWAVKTKLKLTPLP
SQ  SMSQLDLSNWFTGGYSGGDIYHSVSHARPRLFLWCLLLLSVGVGIYLLPNR
//
ID  Q03463;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  421877;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q03463;
DR  PDB: 2KNU;
DR  PDB: 3MRG;
DR  PDB: 3MRH;
DR  PDB: 3MRI;
DR  PDB: 3MRJ;
DR  PDB: 3MRL;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: P51571; IntAct: EBI-1266915; Score: 0.37
DE  Interaction: Q6UXK2; IntAct: EBI-1266937; Score: 0.37
DE  Interaction: Q96SI9; IntAct: EBI-1266952; Score: 0.37
DE  Interaction: Q9H2W1; IntAct: EBI-1266996; Score: 0.37
DE  Interaction: O95466; IntAct: EBI-1267014; Score: 0.37
DE  Interaction: Q9P0L0; IntAct: EBI-8803422; Score: 0.67
DE  Interaction: O95292; IntAct: EBI-8803434; Score: 0.54
DE  Interaction: P12277; IntAct: EBI-9081642; Score: 0.50
DE  Interaction: Q03463; IntAct: EBI-9159727; Score: 0.62
DE  Interaction: Q9P035; IntAct: EBI-9083218; Score: 0.52
DE  Interaction: Q99836; IntAct: EBI-9097331; Score: 0.40
DE  Interaction: P51617; IntAct: EBI-9086976; Score: 0.35
DE  Interaction: P19793; IntAct: EBI-9210728; Score: 0.52
DE  Interaction: P11498; IntAct: EBI-9246904; Score: 0.63
DE  Interaction: P07237; IntAct: EBI-9246854; Score: 0.35
DE  Interaction: Q9H2X3; IntAct: EBI-9257417; Score: 0.40
DE  Interaction: Q9NNX6; IntAct: EBI-9257328; Score: 0.54
GO  GO:0030430;
GO  GO:0044165;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0033648;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048306;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0046965;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0070373;
GO  GO:0032687;
GO  GO:0032715;
GO  GO:0034125;
GO  GO:0034136;
GO  GO:0034144;
GO  GO:0034156;
GO  GO:0034164;
GO  GO:0039707;
GO  GO:1990216;
GO  GO:0043388;
GO  GO:0032728;
GO  GO:0010867;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039580;
GO  GO:0039547;
GO  GO:0039653;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTIPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKVRRPEGRTWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSTGLYHVTNDCPNSSIVYEAHDAILHTPGCVPCVREGNVSRCWV
SQ  AMTPTVATRDGKLPATQLRRHIDLLVGSATLCSALYVGDLCGSVFLIGQLFTFSPRRHWTTQGCNCSIYPGHITGHRMAW
SQ  DMMMNWSPTAALVMAQLLRIPQAILDMIAGAHWGVLAGIAYFSMVGNWAKVLVVLLLFAGVDAETIVSGGQAARAMSGLV
SQ  SLFTPGAKQNIQLINTNGSWHINSTALNCNESLNTGWLAGLIYQHKFNSSGCPERLASCRRLTDFDQGWGPISHANGSGP
SQ  DQRPYCWHYPPKPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYNWGANDTDVFVLNNTRPPLGNWFGCTWMNSTGF
SQ  TKVCGAPPCVIGGGGNNTLHCPTDCFRKHPEATYSRCGSGPWITPRCLVDYPYRLWHYPCTINYTIFKVRMYVGGVEHRL
SQ  DAACNWTRGERCDLEDRDRSELSPLLLSTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVV
SQ  LLFLLLADARVCSCLWMMLLISQAEAALENLVILNAASLAGTRGLVSFLVFFCFAWYLKGRWVPGAAYALYGMWPLLLLL
SQ  LALPQRAYALDTEVAASCGGVVLVGLMALTLSPYYKRCISWCLWWLQYFLTRVEAQLHVWVPPLNVRGGRDAVILLMCVV
SQ  HPTLVFDITKLLLAVLGPLWILQASLLKVPYFVRVQGLLRICALARKMVGGHYVQMAIIKLGALTGTYVYNHLTPLRDWA
SQ  HNGLRDLAVAVEPVVFSQMETKLITWGADTAACGDIINGLPVSARKGREILLGPADGMVSKGWRLLAPITAYAQQTRGLL
SQ  GCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGARSL
SQ  TPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHVVGIFRAAVCTRGVAKAVDFIPVES
SQ  LETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRT
SQ  GVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSVLGIGTVLDQAETAGARLVVLATATPPGSITVPHA
SQ  NIEEVALSTTGEIPFYGKAIPLEAIKGGRHLIFCHSKKKCDELAAKLVALGVNAVAYYRGLDVSVIPTSGDVVVVATDAL
SQ  MTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSILCEC
SQ  YDTGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQGGENFPYLVAYQATVCARAQAP
SQ  PPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQGEVTLTHPVTKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCV
SQ  VIVGRIVLSGRPAIIPDREVLYREFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTASRQAEVIAPTVQTNWQKLEAF
SQ  WAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTSQTLLFNILGGWVAAQLAAPGAATAFVGSGLAGAAVG
SQ  SVGLGRVLVDILAGYGAGVAGALVAFKIMSGELPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWLSSESTTPCSGSWLRDIWDWICEVLSDFKTWLKTKLM
SQ  PHLPGIPFVSCQHGYKGVWRGDGIMHTRCHCGAEITGHVKNGTMRIVGPKTCRNMWSGTFPINAYTTGPCTPLPAPNYTF
SQ  ALWRVSAEEYVEIRRVGDFHYVTGMTTDNLKCPCQVPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHDYPVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAAAAGRRLARGSPPSEASSSASQLSAPSLKATCTINHDSPDAELIEANLLWRQEMGGN
SQ  ITRVESENKVVILDSFDPLVAEEDEREISVPAEILRKSRRFTQALPIWARPDYNPPLIETWKKPNYEPPVVHGCPLPPPQ
SQ  SPPVPPPRKKRTVVLTESTLSTALAELAAKSFGSSSTSGITGDNTTTSSEPAPSGCSPDSDAESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSSEAGTEDVVCCSMSYTWTGALITPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRQKKVTFDRLQVL
SQ  DSHYQDVLKEVKAAASKVKANLLSVEEACSLTPPHSAKSKFGYGAKDVRCHARKAVNHINSVWKDLLEDSVTPIQTTIMA
SQ  KNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSKLPPAVMGSSYGFQYSPGQRVEFLVQAWKSKRTPMGFSYD
SQ  TRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIRSLTERLYVGGPLTNSRGENCGYRRCRASGVLTTSCGNTLTCYIKAR
SQ  AACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGTGKR
SQ  VYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALDCEIYGACYSIEPLDLP
SQ  PIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRARSVRARLLSRGGRAAICGKYLFNWAVRTKLKLTPIA
SQ  AAGRLDLSGWFTAGYSGGDIYHSVSHARPRWFWFCLLLLAAGVGIYLLPNR
//
ID  O92972;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  420174;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: O92972;
DR  UNIPROT: O92969;
DR  UNIPROT: O92970;
DR  UNIPROT: O92971;
DR  UNIPROT: Q02828;
DR  PDB: 1NB4;
DR  PDB: 1NB6;
DR  PDB: 1NB7;
DR  PDB: 2F55;
DR  PDB: 2MTS;
DR  PDB: 2XHU;
DR  PDB: 2XHV;
DR  PDB: 2XHW;
DR  PDB: 2YOJ;
DR  PDB: 3CSO;
DR  PDB: 3GNV;
DR  PDB: 3GNW;
DR  PDB: 3GOL;
DR  PDB: 3HKY;
DR  PDB: 3LKH;
DR  PDB: 3MWV;
DR  PDB: 3MWW;
DR  PDB: 3SKA;
DR  PDB: 3SKE;
DR  PDB: 3SKH;
DR  PDB: 3TYQ;
DR  PDB: 3TYV;
DR  PDB: 3U4O;
DR  PDB: 3U4R;
DR  PDB: 3UPH;
DR  PDB: 3UPI;
DR  PDB: 4DRU;
DR  PDB: 4EAW;
DR  PDB: 4GMC;
DR  PDB: 4IZ0;
DR  PDB: 4J02;
DR  PDB: 4J04;
DR  PDB: 4J06;
DR  PDB: 4J08;
DR  PDB: 4J0A;
DR  PDB: 4JJS;
DR  PDB: 4JJU;
DR  PDB: 4JTW;
DR  PDB: 4JTY;
DR  PDB: 4JTZ;
DR  PDB: 4JU1;
DR  PDB: 4JU2;
DR  PDB: 4JU3;
DR  PDB: 4JU4;
DR  PDB: 4JU6;
DR  PDB: 4JU7;
DR  PDB: 4JVQ;
DR  PDB: 4JY0;
DR  PDB: 4JY1;
DR  PDB: 4MZ4;
DR  PDB: 4OOW;
DR  PDB: 4RY4;
DR  PDB: 4RY5;
DR  PDB: 4RY6;
DR  PDB: 4RY7;
DR  PDB: 5CZB;
DR  PDB: 5NPH;
DR  PDB: 5NPI;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent transmission to permissive cells (By similarity). Capture of circulating HCV particles by these SIGN+ cells may facilitate virus infection of proximal hepatocytes and lymphocyte subpopulations and may be essential for the establishment of persistent infection (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (Probable). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (Probable). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305, ECO:0000305|PubMed:12560074}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (PubMed:17239391). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (PubMed:17239391). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:17239391}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: P06241; IntAct: EBI-706402; Score: 0.59
DE  Interaction: P06240; IntAct: EBI-710538; Score: 0.59
DE  Interaction: P62993; IntAct: EBI-710611; Score: 0.59
DE  Interaction: P07948; IntAct: EBI-710647; Score: 0.59
DE  Interaction: P08631; IntAct: EBI-710681; Score: 0.59
DE  Interaction: P19525; IntAct: EBI-6918687; Score: 0.40
DE  Interaction: O92972; IntAct: EBI-8852124; Score: 0.44
DE  Interaction: P62258; IntAct: EBI-9213571; Score: 0.63
DE  Interaction: P35213; IntAct: EBI-9213618; Score: 0.40
DE  Interaction: P29311; IntAct: EBI-9213629; Score: 0.40
DE  Interaction: Q5VT25; IntAct: EBI-9258286; Score: 0.37
DE  Interaction: Q16513; IntAct: EBI-9998408; Score: 0.67
DE  Interaction: P84022; IntAct: EBI-10040401; Score: 0.40
GO  GO:0030430;
GO  GO:0044164;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0033644;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0071889;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0060090;
GO  GO:0030295;
GO  GO:0019901;
GO  GO:0005080;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0046332;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0032091;
GO  GO:0010991;
GO  GO:0030512;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKASERSQPRGRRQPIPKARRPEGRAWAQPG
SQ  YPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNVSGIYHVTNDCSNSSIVYEAADVIMHTPGCVPCVREGNSSRCWV
SQ  ALTPTLAARNASVPTTTIRRHVDLLVGTAAFCSAMYVGDLCGSIFLVSQLFTFSPRRHETVQDCNCSIYPGHVSGHRMAW
SQ  DMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMVGNWAKVLIVALLFAGVDGETHTTGRVAGHTTSGFT
SQ  SLFSSGASQKIQLVNTNGSWHINRTALNCNDSLQTGFFAALFYAHKFNSSGCPERMASCRPIDWFAQGWGPITYTKPNSS
SQ  DQRPYCWHYAPRPCGVVPASQVCGPVYCFTPSPVVVGTTDRSGVPTYSWGENETDVMLLNNTRPPQGNWFGCTWMNSTGF
SQ  TKTCGGPPCNIGGVGNRTLICPTDCFRKHPEATYTKCGSGPWLTPRCLVDYPYRLWHYPCTLNFSIFKVRMYVGGVEHRL
SQ  NAACNWTRGERCNLEDRDRSELSPLLLSTTEWQILPCAFTTLPALSTGLIHLHQNIVDVQYLYGVGSAFVSFAIKWEYIL
SQ  LLFLLLADARVCACLWMMLLIAQAEAALENLVVLNAASVAGAHGILSFLVFFCAAWYIKGRLAPGAAYAFYGVWPLLLLL
SQ  LALPPRAYALDREMAASCGGAVLVGLVFLTLSPYYKVFLTRLIWWLQYFITRAEAHMQVWVPPLNVRGGRDAIILLTCAV
SQ  HPELIFDITKLLLAILGPLMVLQAGITRVPYFVRAQGLIRACMLVRKVAGGHYVQMAFMKLGALTGTYVYNHLTPLRDWA
SQ  HAGLRDLAVAVEPVVFSAMETKVITWGADTAACGDIILGLPVSARRGKEIFLGPADSLEGQGWRLLAPITAYSQQTRGVL
SQ  GCIITSLTGRDKNQVEGEVQVVSTATQSFLATCINGVCWTVYHGAGSKTLAGPKGPITQMYTNVDLDLVGWQAPPGARSM
SQ  TPCSCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHVVGVFRAAVCTRGVAKAVDFIPVES
SQ  METTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRT
SQ  GVRTITTGGSITYSTYGKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHP
SQ  NIEEIGLSNNGEIPFYGKAIPIEAIKGGRHLIFCHSKKKCDELAAKLTGLGLNAVAYYRGLDVSVIPPIGDVVVVATDAL
SQ  MTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRSGIYRFVTPGERPSGMFDSSVLCEC
SQ  YDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAP
SQ  PPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVILTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSV
SQ  VIVGRIILSGKPAVVPDREVLYQEFDEMEECASQLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRALETF
SQ  WAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQNTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVG
SQ  SIGLGKVLVDILAGYGAGVAGALVAFKVMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLRDVWDWICTVLTDFKTWLQSKLL
SQ  PRLPGVPFLSCQRGYKGVWRGDGIMQTTCPCGAQIAGHVKNGSMRIVGPRTCSNTWHGTFPINAYTTGPCTPSPAPNYSR
SQ  ALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPACKPLLREDVTFQVGLNQYLVGSQL
SQ  PCEPEPDVTVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHDSPDADLIEANLLWRQEMGGN
SQ  ITRVESENKVVILDSFEPLHAEGDEREISVAAEILRKSRKFPSALPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPPTK
SQ  APPIPPPRRKRTVVLTESNVSSALAELATKTFGSSGSSAVDSGTATALPDLASDDGDKGSDVESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSEEASEDVVCCSMSYTWTGALITPCAAEESKLPINPLSNSLLRHHNMVYATTSRSASLRQKKVTFDRLQVLD
SQ  DHYRDVLKEMKAKASTVKAKLLSIEEACKLTPPHSAKSKFGYGAKDVRNLSSRAVNHIRSVWEDLLEDTETPIDTTIMAK
SQ  SEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPKQRVEFLVNTWKSKKCPMGFSYDT
SQ  RCFDSTVTESDIRVEESIYQCCDLAPEARQAIRSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKATA
SQ  ACRAAKLQDCTMLVNGDDLVVICESAGTQEDAAALRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRV
SQ  YYLTRDPTTPLARAAWETARHTPINSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQ
SQ  IIERLHGLSAFTLHSYSPGEINRVASCLRKLGVPPLRTWRHRARSVRAKLLSQGGRAATCGRYLFNWAVRTKLKLTPIPA
SQ  ASQLDLSGWFVAGYSGGDIYHSLSRARPRWFPLCLLLLSVGVGIYLLPNR
//
ID  P26660;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  11113;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: P26660;
DR  PDB: 1YUY;
DR  PDB: 1YV2;
DR  PDB: 1YVX;
DR  PDB: 1YVZ;
DR  PDB: 2XWH;
DR  PDB: 4ADP;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: P07948; IntAct: EBI-710635; Score: 0.40
DE  Interaction: P06241; IntAct: EBI-706320; Score: 0.40
DE  Interaction: P06240; IntAct: EBI-706353; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-710599; Score: 0.40
DE  Interaction: P08631; IntAct: EBI-710670; Score: 0.40
DE  Interaction: P26660; IntAct: EBI-6893867; Score: 0.44
DE  Interaction: P27958; IntAct: EBI-6875553; Score: 0.65
DE  Interaction: Q07820; IntAct: EBI-9637535; Score: 0.40
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0016032;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKDRRSTGKSWGKPG
SQ  YPWPLYGNEGLGWAGWLLSPRGSRPSWGPNDPRHRSRNVGKVIDTLTCGFADLMGYIPVVGAPLGGVARALAHGVRVLED
SQ  GVNFATGNLPGCSFSIFLLALLSCITTPVSAAEVKNISTGYMVTNDCTNDSITWQLQAAVLHVPGCVPCEKVGNTSRCWI
SQ  PVSPNVAVQQPGALTQGLRTHIDMVVMSATLCSALYVGDLCGGVMLAAQMFIVSPQHHWFVQDCNCSIYPGTITGHRMAW
SQ  DMMMNWSPTATMILAYAMRVPEVIIDIIGGAHWGVMFGLAYFSMQGAWAKVVVILLLAAGVDAQTHTVGGSTAHNARTLT
SQ  GMFSLGARQKIQLINTNGSWHINRTALNCNDSLHTGFLASLFYTHSFNSSGCPERMSACRSIEAFRVGWGALQYEDNVTN
SQ  PEDMRPYCWHYPPRQCGVVSASSVCGPVYCFTPSPVVVGTTDRLGAPTYTWGENETDVFLLNSTRPPQGSWFGCTWMNST
SQ  GYTKTCGAPPCRIRADFNASMDLLCPTDCFRKHPDTTYIKCGSGPWLTPRCLIDYPYRLWHYPCTVNYTIFKIRMYVGGV
SQ  EHRLTAACNFTRGDRCNLEDRDRSQLSPLLHSTTEWAILPCTYSDLPALSTGLLHLHQNIVDVQFMYGLSPALTKYIVRW
SQ  EWVVLLFLLLADARVCACLWMLILLGQAEAALEKLVVLHAASAASCNGFLYFVIFFVAAWYIKGRVVPLATYSLTGLWSF
SQ  GLLLLALPQQAYAYDASVHGQIGAALLVLITLFTLTPGYKTLLSRFLWWLCYLLTLAEAMVQEWAPPMQVRGGRDGIIWA
SQ  VAIFCPGVVFDITKWLLAVLGPAYLLKGALTRVPYFVRAHALLRMCTMVRHLAGGRYVQMVLLALGRWTGTYIYDHLTPM
SQ  SDWAANGLRDLAVAVEPIIFSPMEKKVIVWGAETAACGDILHGLPVSARLGREVLLGPADGYTSKGWSLLAPITAYAQQT
SQ  RGLLGTIVVSMTGRDKTEQAGEIQVLSTVTQSFLGTTISGVLWTVYHGAGNKTLAGSRGPVTQMYSSAEGDLVGWPSPPG
SQ  TKSLEPCTCGAVDLYLVTRNADVIPARRRGDKRGALLSPRPLSTLKGSSGGPVLCPRGHAVGVFRAAVCSRGVAKSIDFI
SQ  PVETLDIVTRSPTFSDNSTPPAVPQTYQVGYLHAPTGSGKSTKVPVAYAAQGYKVLVLNPSVAATLGFGAYLSKAHGINP
SQ  NIRTGVRTVTTGAPITYSTYGKFLADGGCAGGAYDIIICDECHAVDSTTILGIGTVLDQAETAGVRLTVLATATPPGSVT
SQ  TPHPNIEEVALGQEGEIPFYGRAIPLSYIKGGRHLIFCHSKKKCDELAAALRGMGLNAVAYYRGLDVSVIPTQGDVVVVA
SQ  TDALMTGFTGDFDSVIDCNVAVTQVVDFSLDPTFTITTQTVPQDAVSRSQRRGRTGRGRLGIYRYVSTGERASGMFDSVV
SQ  LCECYDAGAAWYELTPAETTVRLRAYFNTPGLPVCQDHLEFWEAVFTGLTHIDAHFLSQTKQSGENFAYLTAYQATVCAR
SQ  AKAPPPSWDVMWKCLTRLKPTLVGPTPLLYRLGSVTNEVTLTHPVTKYIATCMQADLEVMTSTWVLAGGVLAAVAAYCLA
SQ  TGCVCIIGRLHVNQRAVVAPDKEVLYEAFDEMEECASRAALIEEGQRIAEMLKSKIQGLLQQASKQAQDIQPAVQASWPK
SQ  VEQFWAKHMWNFISGIQYLAGLSTLPGNPAVASMMAFSAALTSPLSTSTTILLNILGGWLASQIAPPAGATGFVVSGLVG
SQ  AAVGSIGLGKVLVDILAGYGAGISGALVAFKIMSGEKPSMEDVVNLLPGILSPGALVVGVICAAILRRHVGPGEGAVQWM
SQ  NRLIAFASRGNHVAPTHYVTESDASQRVTQLLGSLTITSLLRRLHNWITEDCPIPCSGSWLRDVWDWVCTILTDFKNWLT
SQ  SKLFPKMPGLPFISCQKGYKGVWAGTGIMTTRCPCGANISGNVRLGSMRITGPKTCMNIWQGTFPINCYTEGQCVPKPAP
SQ  NFKIAIWRVAASEYAEVTQHGSYHYITGLTTDNLKVPCQLPSPEFFSWVDGVQIHRFAPIPKPFFRDEVSFCVGLNSFVV
SQ  GSQLPCDPEPDTDVLTSMLTDPSHITAETAARRLARGSPPSEASSSASQLSAPSLRATCTTHGKAYDVDMVDANLFMGGD
SQ  VTRIESESKVVVLDSLDPMVEERSDLEPSIPSEYMLPKKRFPPALPAWARPDYNPPLVESWKRPDYQPATVAGCALPPPK
SQ  KTPTPPPRRRRTVGLSESSIADALQQLAIKSFGQPPPSGDSGLSTGADAADSGSRTPPDELALSETGSISSMPPLEGEPG
SQ  DPDLEPEQVELQPPPQGGVVTPGSGSGSWSTCSEEDDSVVCCSMSYSWTGALITPCSPEEEKLPINPLSNSLLRYHNKVY
SQ  CTTSKSASLRAKKVTFDRMQALDAHYDSVLKDIKLAASKVTARLLTLEEACQLTPPHSARSKYGFGAKEVRSLSGRAVNH
SQ  IKSVWKDLLEDTQTPIPTTIMAKNEVFCVDPTKGGKKAARLIVYPDLGVRVCEKMALYDITQKLPQAVMGASYGFQYSPA
SQ  QRVEFLLKAWAEKKDPMGFSYDTRCFDSTVTERDIRTEESIYRACSLPEEAHTAIHSLTERLYVGGPMFNSKGQTCGYRR
SQ  CRASGVLTTSMGNTITCYVKALAACKAAGIIAPTMLVCGDDLVVISESQGTEEDERNLRAFTEAMTRYSAPPGDPPRPEY
SQ  DLELITSCSSNVSVALGPQGRRRYYLTRDPTTPIARAAWETVRHSPVNSWLGNIIQYAPTIWARMVLMTHFFSILMAQDT
SQ  LDQNLNFEMYGAVYSVSPLDLPAIIERLHGLDAFSLHTYTPHELTRVASALRKLGAPPLRAWKSRARAVRASLISRGGRA
SQ  AVCGRYLFNWAVKTKLKLTPLPEARLLDLSSWFTVGAGGGDIYHSVSRARPRLLLLGLLLLFVGVGLFLLPAR
//
ID  P26661;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  11115;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: P26661;
DR  PDB: 1XCQ;
DR  PDB: 1XCT;
DR  PDB: 1XF5;
DR  PDB: 3GSZ;
DR  PDB: 3HVO;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKDRRSTGKSWGKPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPTWGPTDPRHRSRNLGRVIDTITCGFADLMGYIPVVGAPVGGVARALAHGVRVLED
SQ  GINYATGNLPGCSFSIFLLALLSCVTVPVSAVEVRNISSSYYATNDCSNNSITWQLTDAVLHLPGCVPCENDNGTLHCWI
SQ  QVTPNVAVKHRGALTRSLRTHVDMIVMAATACSALYVGDVCGAVMILSQAFMVSPQRHNFTQECNCSIYQGHITGHRMAW
SQ  DMMLSWSPTLTMILAYAARVPELVLEIIFGGHWGVVFGLAYFSMQGAWAKVIAILLLVAGVDATTYSSGQEAGRTVAGFA
SQ  GLFTTGAKQNLYLINTNGSWHINRTALNCNDSLQTGFLASLFYTHKFNSSGCPERLSSCRGLDDFRIGWGTLEYETNVTN
SQ  DGDMRPYCWHYPPRPCGIVPARTVCGPVYCFTPSPVVVGTTDKQGVPTYTWGENETDVFLLNSTRPPRGAWFGCTWMNGT
SQ  GFTKTCGAPPCRIRKDYNSTIDLLCPTDCFRKHPDATYLKCGAGPWLTPRCLVDYPYRLWHYPCTVNFTIFKARMYVGGV
SQ  EHRFSAACNFTRGDRCRLEDRDRGQQSPLLHSTTEWAVLPCSFSDLPALSTGLLHLHQNIVDVQYLYGLSPALTRYIVKW
SQ  EWVILLFLLLADARICACLWMLIILGQAEAALEKLIILHSASAASANGPLWFFIFFTAAWYLKGRVVPVATYSVLGLWSF
SQ  LLLVLALPQQAYALDAAEQGELGLAILVIISIFTLTPAYKILLSRSVWWLSYMLVLAEAQIQQWVPPLEVRGGRDGIIWV
SQ  AVILHPRLVFEVTKWLLAILGPAYLLKASLLRIPYFVRAHALLRVCTLVKHLAGARYIQMLLITIGRWTGTYIYDHLSPL
SQ  STWAAQGLRDLAIAVEPVVFSPMEKKVIVWGAETVACGDILHGLPVSARLGREVLLGPADGYTSKGWKLLAPITAYTQQT
SQ  RGLLGAIVVSLTGRDKNEQAGQVQVLSSVTQTFLGTSISGVLWTVYHGAGNKTLAGPKGPVTQMYTSAEGDLVGWPSPPG
SQ  TKSLDPCTCGAVDLYLVTRNADVIPVRRKDDRRGALLSPRPLSTLKGSSGGPVLCSRGHAVGLFRAAVCARGVAKSIDFI
SQ  PVESLDVATRTPSFSDNSTPPAVPQSYQVGYLHAPTGSGKSTKVPAAYASQGYKVLVLNPSVAATLGFGAYMSKAHGINP
SQ  NIRTGVRTVTTGDSITYSTYGKFIADGGCAAGAYDIIICDECHSVDATTILGIGTVLDQAETAGVRLVVLATATPPGTVT
SQ  TPHSNIEEVALGHEGEIPFYGKAIPLAFIKGGRHLIFCHSKKKCDELAAALRGMGVNAVAYYRGLDVSVIPTQGDVVVVA
SQ  TDALMTGYTGDFDSVIDCNVAVSQIVDFSLDPTFTITTQTVPQDAVSRSQRRGRTGRGRLGVYRYVSSGERPSGMFDSVV
SQ  LCECYDAGAAWYELTPAETTVRLRAYFNTPGLPVCQDHLEFWEAVFTGLTHIDAHFLSQTKQGGENFAYLTAYQATVCAR
SQ  AKAPPPSWDVMWKCLTRLKPTLTGPTPLLYRLGAVTNEVTLTHPVTKYIATCMQADLEIMTSSWVLAGGVLAAVAAYCLA
SQ  TGCISIIGRLHLNDRVVVAPDKEILYEAFDEMEECASKAALIEEGQRMAEMLKSKIQGLLQQATRQAQDIQPAIQSSWPK
SQ  LEQFWAKHMWNFISGIQYLAGLSTLPGNPAVASMMAFSAALTSPLPTSTTILLNIMGGWLASQIAPPAGATGFVVSGLVG
SQ  AAVGSIGLGKILVDVLAGYGAGISGALVAFKIMSGEKPTVEDVVNLLPAILSPGALVVGVICAAILRRHVGQGEGAVQWM
SQ  NRLIAFASRGNHVAPTHYVVESDASQRVTQVLSSLTITSLLRRLHAWITEDCPVPCSGSWLQDIWDWVCSILTDFKNWLS
SQ  SKLLPKMPGIPFISCQKGYKGVWAGTGVMTTRCPCGANISGHVRMGTMKITGPKTCLNLWQGTFPINCYTEGPCVPKPPP
SQ  NYKTAIWRVAASEYVEVTQHGSFSYVTGLTSDNLKVPCQVPAPEFFSWVDGVQIHRFAPVPGPFFRDEVTFTVGLNSFVV
SQ  GSQLPCDPEPDTEVLASMLTDPSHITAEAAARRLARGSPPSQASSSASQLSAPSLKATCTTHKTAYDCDMVDANLFMGGD
SQ  VTRIESDSKVIVLDSLDSMTEVEDDREPSVPSEYLIKRRKFPPALPPWARPDYNPVLIETWKRPGYEPPTVLGCALPPTP
SQ  QTPVPPPRRRRAKVLTQDNVEGVLREMADKVLSPLQDNNDSGHSTGADTGGDIVQQPSDETAASEAGSLSSMPPLEGEPG
SQ  DPDLEFEPVGSAPPSEGECEVIDSDSKSWSTVSDQEDSVICCSMSYSWTGALITPCGPEEEKLPINPLSNSLMRFHNKVY
SQ  STTSRSASLRAKKVTFDRVQVLDAHYDSVLQDVKRAASKVSARLLTVEEACALTPPHSAKSRYGFGAKEVRSLSRRAVNH
SQ  IRSVWEDLLEDQHTPIDTTIMAKNEVFCIDPTKGGKKPARLIVYPDLGVRVCEKMALYDIAQKLPKAIMGPSYGFQYSPA
SQ  ERVDFLLKAWGSKKDPMGFSYDTRCFDSTVTERDIRTEESIYQACSLPQEARTVIHSLTERLYVGGPMTNSKGQSCGYRR
SQ  CRASGVFTTSMGNTMTCYIKALAACKAAGIVDPVMLVCGDDLVVISESQGNEEDERNLRAFTEAMTRYSAPPGDLPRPEY
SQ  DLELITSCSSNVSVALDSRGRRRYFLTRDPTTPITRAAWETVRHSPVNSWLGNIIQYAPTIWVRMVIMTHFFSILLAQDT
SQ  LNQNLNFEMYGAVYSVNPLDLPAIIERLHGLEAFSLHTYSPHELSRVAATLRKLGAPPLRAWKSRARAVRASLIAQGARA
SQ  AICGRYLFNWAVKTKLKLTPLPEASRLDLSGWFTVGAGGGDIYHSVSHARPRLLLLCLLLLSVGVGIFLLPAR
//
ID  P26662;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  11116;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:15163730, ECO:0000269|PubMed:15613354, ECO:0000305|PubMed:9621068}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000269|PubMed:15613354}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000269|PubMed:9621068}. Host nucleus {ECO:0000269|PubMed:15163730, ECO:0000269|PubMed:15613354, ECO:0000269|PubMed:9621068}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99IB8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q99IB8}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:Q99IB8}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26664}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000305}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:16227268, ECO:0000269|PubMed:16844119}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:7769656}. Host mitochondrion {ECO:0000269|PubMed:16844119}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000269|PubMed:23468497}. Host lipid droplet {ECO:0000269|PubMed:23935497}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (PubMed:23935497). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:23935497}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: P26662;
DR  UNIPROT: P89966;
DR  UNIPROT: Q81755;
DR  PDB: 1DXP;
DR  PDB: 1DY8;
DR  PDB: 1DY9;
DR  PDB: 1W3C;
DR  PDB: 2K8J;
DR  PDB: 3OYP;
DR  PDB: 3P8N;
DR  PDB: 3P8O;
DR  PDB: 4A1T;
DR  PDB: 4A1V;
DR  PDB: 4A1X;
DR  PDB: 4I31;
DR  PDB: 4I32;
DR  PDB: 4I33;
DR  PDB: 4JMY;
DR  PDB: 4KTC;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (PubMed:15760888). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon- alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin- mediated proteasome-dependent degradation of STAT1 (PubMed:16940534, PubMed:15825084). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c- myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (PubMed:14559998). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up- regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:14559998, ECO:0000269|PubMed:15760888, ECO:0000269|PubMed:15825084, ECO:0000269|PubMed:16940534, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (PubMed:20667830). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:20667830, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (PubMed:16126720). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (Probable). Down- regulates viral IRES translation initiation (PubMed:31585734). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (PubMed:23468497) (Probable). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:16126720, ECO:0000269|PubMed:23468497, ECO:0000269|PubMed:31585734, ECO:0000305|PubMed:16227268, ECO:0000305|PubMed:9343247}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: P97633; IntAct: EBI-8524401; Score: 0.44
DE  Interaction: P67870; IntAct: EBI-8524425; Score: 0.44
DE  Interaction: P37231; IntAct: EBI-7134322; Score: 0.46
DE  Interaction: P26662; IntAct: EBI-8872867; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-9099480; Score: 0.52
DE  Interaction: Q07812; IntAct: EBI-9355947; Score: 0.59
GO  GO:0030430;
GO  GO:0044164;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0032993;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0003677;
GO  GO:1990814;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0033592;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0043066;
GO  GO:1902807;
GO  GO:0039707;
GO  GO:0060139;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0043489;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRTWAQPG
SQ  YPWPLYGNEGMGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNVSGIYHVTNDCSNSSIVYEAADMIMHTPGCVPCVRESNFSRCWV
SQ  ALTPTLAARNSSIPTTTIRRHVDLLVGAAALCSAMYVGDLCGSVFLVSQLFTFSPRRYETVQDCNCSIYPGHVSGHRMAW
SQ  DMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMVGNWAKVLIVMLLFAGVDGHTHVTGGRVASSTQSLV
SQ  SWLSQGPSQKIQLVNTNGSWHINRTALNCNDSLQTGFIAALFYAHRFNASGCPERMASCRPIDEFAQGWGPITHDMPESS
SQ  DQRPYCWHYAPRPCGIVPASQVCGPVYCFTPSPVVVGTTDRFGAPTYSWGENETDVLLLSNTRPPQGNWFGCTWMNSTGF
SQ  TKTCGGPPCNIGGVGNNTLVCPTDCFRKHPEATYTKCGSGPWLTPRCMVDYPYRLWHYPCTVNFTVFKVRMYVGGVEHRL
SQ  NAACNWTRGERCDLEDRDRSELSPLLLSTTEWQILPCSFTTLPALSTGLIHLHRNIVDVQYLYGIGSAVVSFAIKWEYIL
SQ  LLFLLLADARVCACLWMMLLIAQAEATLENLVVLNAASVAGAHGLLSFLVFFCAAWYIKGRLVPGAAYALYGVWPLLLLL
SQ  LALPPRAYAMDREMAASCGGAVFVGLVLLTLSPYYKVFLARLIWWLQYFITRAEAHLQVWVPPLNVRGGRDAIILLTCAV
SQ  HPELIFDITKLLLAILGPLMVLQAGITRVPYFVRAQGLIRACMLVRKVAGGHYVQMAFMKLAALTGTYVYDHLTPLRDWA
SQ  HAGLRDLAVAVEPVVFSDMETKLITWGADTAACGDIISGLPVSARRGKEILLGPADSFGEQGWRLLAPITAYSQQTRGLL
SQ  GCIITSLTGRDKNQVDGEVQVLSTATQSFLATCVNGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWPAPPGARSM
SQ  TPCTCGSSDLYLVTRHADVVPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPSGHVVGIFRAAVCTRGVAKAVDFIPVES
SQ  METTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIEPNIRT
SQ  GVRTITTGGPITYSTYCKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSITVPHP
SQ  NIEEVALSNTGEIPFYGKAIPIEAIKGGRHLIFCHSKKKCDELAAKLTGLGLNAVAYYRGLDVSVIPTSGDVVVVATDAL
SQ  MTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRAQRRGRTGRGRSGIYRFVTPGERPSGMFDSSVLCEC
SQ  YDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNLPYLVAYQATVCARAQAP
SQ  PPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSV
SQ  VIVGRIILSGRPAVIPDREVLYQEFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRALEVF
SQ  WAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQNTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVG
SQ  SIGLGKVLVDILAGYGAGVAGALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLKDVWDWICTVLSDFKTWLQSKLL
SQ  PRLPGLPFLSCQRGYKGVWRGDGIMQTTCPCGAQITGHVKNGSMRIVGPKTCSNTWHGTFPINAYTTGPCTPSPAPNYSR
SQ  ALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPVCKPLLREEVVFQVGLNQYLVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHDSPDADLIEANLLWRQEMGGN
SQ  ITRVESENKVVILDSFDPIRAVEDEREISVPAEILRKPRKFPPALPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPSTK
SQ  APPIPPPRRKRTVVLTESTVSSALAELATKTFGSSGSSAVDSGTATGPPDQASDDGDKGSDVESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSGEAGEDVVCCSMSYTWTGALITPCAAEESKLPINPLSNSLLRHHSMVYSTTSRSASLRQKKVTFDRLQVLD
SQ  DHYRDVLKEMKAKASTVKARLLSIEEACKLTPPHSAKSKFGYGAKDVRSLSSRAVNHIRSVWEDLLEDTETPIDTTIMAK
SQ  NEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGPSYGFQYSPGQRVEFLVNTWKSKKCPMGFSYDT
SQ  RCFDSTVTENDIRTEESIYQCCDLAPEARQAIRSLTERLYVGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKATA
SQ  ACRAAKLQDCTMLVNGDDLVVICESAGTQEDAAALRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRV
SQ  YYLTRDPTTPLARAAWETVRHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQ
SQ  IIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRAKLLSQGGRAATCGKYLFNWAVKTKLKLTPIPA
SQ  ASQLDLSGWFVAGYNGGDIYHSLSRARPRWFMLCLLLLSVGVGIYLLPNR
//
ID  Q99IB8;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356411;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000269|PubMed:23543610}. Host cytoplasm {ECO:0000269|PubMed:23543610}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000269|PubMed:29352312}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:17170445}; Multi-pass membrane protein {ECO:0000269|PubMed:17170445}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000269|PubMed:17170445}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26664}. Host lipid droplet {ECO:0000269|PubMed:21347350}. Note=Probably present on the surface of lipid droplets. {ECO:0000305|PubMed:21347350}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000305}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cytoplasm {ECO:0000269|PubMed:31511391}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000269|PubMed:29352312}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q99IB8;
DR  PDB: 2KZQ;
DR  PDB: 2LIF;
DR  PDB: 2LVG;
DR  PDB: 2XXD;
DR  PDB: 2XYM;
DR  PDB: 3I5K;
DR  PDB: 4AEP;
DR  PDB: 4AEX;
DR  PDB: 4E76;
DR  PDB: 4E78;
DR  PDB: 4E7A;
DR  PDB: 4J1V;
DR  PDB: 4OBC;
DR  PDB: 4WT9;
DR  PDB: 4WTA;
DR  PDB: 4WTC;
DR  PDB: 4WTD;
DR  PDB: 4WTE;
DR  PDB: 4WTF;
DR  PDB: 4WTG;
DR  PDB: 4WTI;
DR  PDB: 4WTJ;
DR  PDB: 4WTK;
DR  PDB: 4WTL;
DR  PDB: 4WTM;
DR  PDB: 5NPJ;
DR  PDB: 5QJ0;
DR  PDB: 5QJ1;
DR  PDB: 5TWM;
DR  PDB: 5UJ2;
DR  PDB: 6HT4;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (PubMed:18524832). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000269|PubMed:18524832, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity) (PubMed:17325668). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:17325668}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity) (PubMed:17325668). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:17325668}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (PubMed:29253880). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (PubMed:29253880). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:29253880, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (PubMed:31121874, PubMed:21347350). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:21347350, ECO:0000269|PubMed:31121874}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (PubMed:29070684). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:29070684}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (PubMed:29167346). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (PubMed:29167346). NS4B self-interaction contributes to its function in membranous web formation (PubMed:29167346). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:29167346}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (PubMed:31511391). Both hypo- and hyperphosphorylated states are required for the viral life cycle (PubMed:31511391). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA- binding and especially in binding to the viral genome (PubMed:20592076). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the viral mature core protein (PubMed:18524832). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down-regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity) (PubMed:30281972). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:18524832, ECO:0000269|PubMed:20592076, ECO:0000269|PubMed:30281972, ECO:0000269|PubMed:31511391}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: P02760; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: P27958; IntAct: EBI-8763465; Score: 0.50
DE  Interaction: P42167; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: P57088; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P62834; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: P80303; IntAct: EBI-6927977; Score: 0.37
DE  Interaction: Q03001; IntAct: EBI-6928217; Score: 0.37
DE  Interaction: Q07065; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q13137; IntAct: EBI-6928172; Score: 0.37
DE  Interaction: Q14999; IntAct: EBI-6928202; Score: 0.37
DE  Interaction: Q86WV6; IntAct: EBI-8786474; Score: 0.46
DE  Interaction: Q8NEF9; IntAct: EBI-6928142; Score: 0.37
DE  Interaction: Q96AG4; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q96CV9; IntAct: EBI-6929183; Score: 0.49
DE  Interaction: O00571; IntAct: EBI-6929355; Score: 0.60
DE  Interaction: Q08211; IntAct: EBI-6674329; Score: 0.35
DE  Interaction: P67809; IntAct: EBI-6862000; Score: 0.58
DE  Interaction: Q99IB8; IntAct: EBI-6901435; Score: 0.84
DE  Interaction: P17844; IntAct: EBI-6927869; Score: 0.37
DE  Interaction: P78344; IntAct: EBI-6927888; Score: 0.37
DE  Interaction: Q13129; IntAct: EBI-6927924; Score: 0.51
DE  Interaction: P02749; IntAct: EBI-6927905; Score: 0.37
DE  Interaction: P35222; IntAct: EBI-6927962; Score: 0.37
DE  Interaction: Q99816; IntAct: EBI-6927945; Score: 0.37
DE  Interaction: O00584; IntAct: EBI-6928007; Score: 0.37
DE  Interaction: Q13099; IntAct: EBI-6928022; Score: 0.37
DE  Interaction: Q99550; IntAct: EBI-6928037; Score: 0.37
DE  Interaction: O94880; IntAct: EBI-6927992; Score: 0.37
DE  Interaction: P98175; IntAct: EBI-6928082; Score: 0.37
DE  Interaction: P27986; IntAct: EBI-6928067; Score: 0.37
DE  Interaction: Q15154; IntAct: EBI-6928052; Score: 0.37
DE  Interaction: Q9UQ90; IntAct: EBI-6928097; Score: 0.37
DE  Interaction: Q13813; IntAct: EBI-6928112; Score: 0.37
DE  Interaction: Q9H8Y8; IntAct: EBI-6928292; Score: 0.57
DE  Interaction: Q08379; IntAct: EBI-6928187; Score: 0.37
DE  Interaction: P02675; IntAct: EBI-6928247; Score: 0.37
DE  Interaction: P02751; IntAct: EBI-6928262; Score: 0.57
DE  Interaction: P11142; IntAct: EBI-6928330; Score: 0.57
DE  Interaction: Q9BXC0; IntAct: EBI-6928307; Score: 0.37
DE  Interaction: O75592; IntAct: EBI-6928360; Score: 0.57
DE  Interaction: Q86UP2; IntAct: EBI-6928345; Score: 0.37
DE  Interaction: P22307; IntAct: EBI-6928375; Score: 0.37
DE  Interaction: Q9ULJ7; IntAct: EBI-6928407; Score: 0.37
DE  Interaction: Q86SQ7; IntAct: EBI-6928422; Score: 0.37
DE  Interaction: Q14BN4; IntAct: EBI-6928465; Score: 0.49
DE  Interaction: P05546; IntAct: EBI-6928437; Score: 0.37
DE  Interaction: Q86VW0; IntAct: EBI-6928452; Score: 0.37
DE  Interaction: P02787; IntAct: EBI-6928495; Score: 0.37
DE  Interaction: Q9NQB0; IntAct: EBI-6928480; Score: 0.37
DE  Interaction: P67936; IntAct: EBI-6928525; Score: 0.49
DE  Interaction: O14628; IntAct: EBI-6928540; Score: 0.37
DE  Interaction: Q14966; IntAct: EBI-6928555; Score: 0.37
DE  Interaction: P04035; IntAct: EBI-6928587; Score: 0.37
DE  Interaction: P01024; IntAct: EBI-6928572; Score: 0.37
DE  Interaction: Q9Y5W7; IntAct: EBI-6928602; Score: 0.37
DE  Interaction: Q13464; IntAct: EBI-6928617; Score: 0.37
DE  Interaction: P02649; IntAct: EBI-6928632; Score: 0.37
DE  Interaction: P45973; IntAct: EBI-6928647; Score: 0.37
DE  Interaction: Q9UNS2; IntAct: EBI-6928677; Score: 0.37
DE  Interaction: Q96MT8; IntAct: EBI-6928662; Score: 0.37
DE  Interaction: Q15717; IntAct: EBI-6928707; Score: 0.55
DE  Interaction: Q96KQ7; IntAct: EBI-6928797; Score: 0.55
DE  Interaction: Q5JTC6; IntAct: EBI-6928722; Score: 0.37
DE  Interaction: Q9GZR7; IntAct: EBI-6928782; Score: 0.37
DE  Interaction: Q02818; IntAct: EBI-6928812; Score: 0.57
DE  Interaction: P50440; IntAct: EBI-6928827; Score: 0.37
DE  Interaction: Q13576; IntAct: EBI-6928844; Score: 0.37
DE  Interaction: Q9H074; IntAct: EBI-6928874; Score: 0.37
DE  Interaction: Q13670; IntAct: EBI-6928889; Score: 0.37
DE  Interaction: O14763; IntAct: EBI-6928938; Score: 0.37
DE  Interaction: Q9UNK0; IntAct: EBI-6928923; Score: 0.37
DE  Interaction: P55265; IntAct: EBI-6928953; Score: 0.49
DE  Interaction: Q8N302; IntAct: EBI-6928981; Score: 0.37
DE  Interaction: P61201; IntAct: EBI-6928996; Score: 0.37
DE  Interaction: Q9P219; IntAct: EBI-6929026; Score: 0.37
DE  Interaction: Q9UK99; IntAct: EBI-6929056; Score: 0.37
DE  Interaction: Q86YP4; IntAct: EBI-6929086; Score: 0.37
DE  Interaction: Q9NZM3; IntAct: EBI-6929114; Score: 0.37
DE  Interaction: P26927; IntAct: EBI-6929129; Score: 0.49
DE  Interaction: Q7Z406; IntAct: EBI-6929168; Score: 0.37
DE  Interaction: A2RUB6; IntAct: EBI-6929226; Score: 0.37
DE  Interaction: O95613; IntAct: EBI-6929211; Score: 0.37
DE  Interaction: Q96RK0; IntAct: EBI-6929248; Score: 0.37
DE  Interaction: Q14683; IntAct: EBI-6929278; Score: 0.57
DE  Interaction: P46939; IntAct: EBI-6929308; Score: 0.37
DE  Interaction: Q9Y2W2; IntAct: EBI-6929323; Score: 0.57
DE  Interaction: P04114; IntAct: EBI-6929340; Score: 0.37
DE  Interaction: Q9Y262; IntAct: EBI-6929370; Score: 0.37
DE  Interaction: Q86SX6; IntAct: EBI-6929385; Score: 0.37
DE  Interaction: P06748; IntAct: EBI-6929400; Score: 0.37
DE  Interaction: Q969X0; IntAct: EBI-6929419; Score: 0.37
DE  Interaction: Q15643; IntAct: EBI-6929434; Score: 0.37
DE  Interaction: O43716; IntAct: EBI-6929449; Score: 0.37
DE  Interaction: P08603; IntAct: EBI-6929471; Score: 0.37
DE  Interaction: Q15084; IntAct: EBI-6929486; Score: 0.37
DE  Interaction: Q4ZG55; IntAct: EBI-6929501; Score: 0.37
DE  Interaction: P04196; IntAct: EBI-6929529; Score: 0.37
DE  Interaction: P14543; IntAct: EBI-6929559; Score: 0.37
DE  Interaction: Q92802; IntAct: EBI-6929544; Score: 0.37
DE  Interaction: Q9BVG3; IntAct: EBI-6929626; Score: 0.37
DE  Interaction: P02647; IntAct: EBI-6929641; Score: 0.37
DE  Interaction: Q6Q788; IntAct: EBI-6929656; Score: 0.37
DE  Interaction: P0C0L4; IntAct: EBI-6929686; Score: 0.37
DE  Interaction: Q8WWM7; IntAct: EBI-6929701; Score: 0.37
DE  Interaction: O75907; IntAct: EBI-8764433; Score: 0.40
DE  Interaction: Q9Z2A7; IntAct: EBI-8753555; Score: 0.43
DE  Interaction: Q96CW1; IntAct: EBI-8767411; Score: 0.40
DE  Interaction: P23458; IntAct: EBI-8781875; Score: 0.40
DE  Interaction: Q15392; IntAct: EBI-8784130; Score: 0.35
DE  Interaction: Q9P035; IntAct: EBI-8784130; Score: 0.56
DE  Interaction: Q14318; IntAct: EBI-8784130; Score: 0.35
DE  Interaction: P62937; IntAct: EBI-8784130; Score: 0.59
DE  Interaction: Q9P0L0; IntAct: EBI-8784130; Score: 0.56
DE  Interaction: P48729; IntAct: EBI-8784130; Score: 0.35
DE  Interaction: P53621; IntAct: EBI-8784130; Score: 0.35
DE  Interaction: P42356; IntAct: EBI-8784130; Score: 0.73
DE  Interaction: Q9NP72; IntAct: EBI-8784130; Score: 0.57
DE  Interaction: P29590; IntAct: EBI-8785013; Score: 0.27
DE  Interaction: G3IDM9; IntAct: EBI-8786534; Score: 0.27
DE  Interaction: Q969R2; IntAct: EBI-8787282; Score: 0.46
DE  Interaction: Q16584; IntAct: EBI-8792269; Score: 0.61
DE  Interaction: P07355; IntAct: EBI-8792405; Score: 0.57
DE  Interaction: P51636; IntAct: EBI-8792484; Score: 0.37
DE  Interaction: P49327; IntAct: EBI-8840042; Score: 0.56
DE  Interaction: P53350; IntAct: EBI-8841159; Score: 0.46
DE  Interaction: O60664; IntAct: EBI-8841287; Score: 0.27
DE  Interaction: P05455; IntAct: EBI-8849129; Score: 0.56
DE  Interaction: P60033; IntAct: EBI-8850857; Score: 0.56
DE  Interaction: Q9Y6A9; IntAct: EBI-8852194; Score: 0.63
DE  Interaction: P26196; IntAct: EBI-11599139; Score: 0.35
DE  Interaction: Q6PKG0; IntAct: EBI-8863462; Score: 0.27
DE  Interaction: Q9Y6M1; IntAct: EBI-8863567; Score: 0.27
DE  Interaction: Q07021; IntAct: EBI-8863325; Score: 0.27
DE  Interaction: Q14457; IntAct: EBI-8874048; Score: 0.35
DE  Interaction: Q8NEB9; IntAct: EBI-8874048; Score: 0.35
DE  Interaction: P20339; IntAct: EBI-8874048; Score: 0.35
DE  Interaction: Q62625; IntAct: EBI-8874029; Score: 0.27
DE  Interaction: P36897; IntAct: EBI-9050541; Score: 0.65
DE  Interaction: P37173; IntAct: EBI-9050576; Score: 0.44
DE  Interaction: P12277; IntAct: EBI-9081652; Score: 0.40
DE  Interaction: Q99836; IntAct: EBI-9086997; Score: 0.40
DE  Interaction: O95793; IntAct: EBI-9098828; Score: 0.27
DE  Interaction: P11498; IntAct: EBI-9276691; Score: 0.40
DE  Interaction: O60260; IntAct: EBI-10060527; Score: 0.51
DE  Interaction: Q9HD23; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q9BRP8; IntAct: EBI-11422269; Score: 0.56
DE  Interaction: Q8NG48; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q96DV4; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q9P015; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q13405; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q15672; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q15020; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q9NWU5; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: P67870; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q9Y3D3; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q96DH6; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q9BZ29; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q9Y3D5; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: P55209; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q2KHT3; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q9C0C9; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q2TBE0; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q9Y6H1; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q13724; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: Q99733; IntAct: EBI-11422269; Score: 0.35
DE  Interaction: P46379; IntAct: EBI-11599079; Score: 0.35
DE  Interaction: Q8N163; IntAct: EBI-11599079; Score: 0.35
DE  Interaction: Q9UKV3; IntAct: EBI-11599079; Score: 0.35
DE  Interaction: Q96I24; IntAct: EBI-11599079; Score: 0.35
DE  Interaction: Q92879; IntAct: EBI-11599079; Score: 0.35
DE  Interaction: Q99856; IntAct: EBI-11599079; Score: 0.35
DE  Interaction: Q9UDY4; IntAct: EBI-11599079; Score: 0.35
DE  Interaction: O00422; IntAct: EBI-11599091; Score: 0.35
DE  Interaction: P29508; IntAct: EBI-11599091; Score: 0.35
DE  Interaction: P48594; IntAct: EBI-11599091; Score: 0.35
DE  Interaction: O14828; IntAct: EBI-11599103; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-11599103; Score: 0.35
DE  Interaction: Q9BTV4; IntAct: EBI-11599103; Score: 0.35
DE  Interaction: O95758; IntAct: EBI-11599118; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-11599118; Score: 0.53
DE  Interaction: Q04837; IntAct: EBI-11599650; Score: 0.46
DE  Interaction: Q7L5D6; IntAct: EBI-11599118; Score: 0.35
DE  Interaction: Q05519; IntAct: EBI-11599118; Score: 0.35
DE  Interaction: C9JLW8; IntAct: EBI-11599139; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-11599139; Score: 0.35
DE  Interaction: P49756; IntAct: EBI-11599139; Score: 0.35
DE  Interaction: Q9Y3L5; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: P57678; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: Q8N442; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: Q12904; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: P48556; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: Q9H4B7; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: P63151; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: O15084; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: Q96J01; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: Q9BZH6; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: Q16401; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: Q9NRN7; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: Q96JJ3; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: Q9BV38; IntAct: EBI-11599512; Score: 0.35
DE  Interaction: Q9NWW5; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q9GZP9; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-11599534; Score: 0.50
DE  Interaction: P05026; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q6YN16; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q96NT5; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q9P2W9; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q7LGA3; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q5GH72; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q9UL46; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q92544; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q9UBV8; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: O96005; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q9BRX8; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: P01111; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q9NVJ2; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: P38435; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: P13929; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: P60604; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q9BU23; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q96A83; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q9NTJ5; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: P98194; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q9UGP8; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: P00846; IntAct: EBI-11599610; Score: 0.35
DE  Interaction: O43169; IntAct: EBI-11599610; Score: 0.50
DE  Interaction: O95197; IntAct: EBI-11599610; Score: 0.35
DE  Interaction: P23434; IntAct: EBI-11599610; Score: 0.35
DE  Interaction: P50895; IntAct: EBI-11599610; Score: 0.35
DE  Interaction: Q8N456; IntAct: EBI-11599610; Score: 0.35
DE  Interaction: P12259; IntAct: EBI-11599650; Score: 0.35
DE  Interaction: O94966; IntAct: EBI-11599650; Score: 0.46
DE  Interaction: O00499; IntAct: EBI-11599650; Score: 0.46
DE  Interaction: Q8NBS9; IntAct: EBI-11599650; Score: 0.46
DE  Interaction: Q7RTV0; IntAct: EBI-11599650; Score: 0.46
DE  Interaction: P22455; IntAct: EBI-11599650; Score: 0.35
DE  Interaction: P51659; IntAct: EBI-11599650; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-11599695; Score: 0.35
DE  Interaction: Q32P51; IntAct: EBI-11599695; Score: 0.35
DE  Interaction: P56182; IntAct: EBI-11599695; Score: 0.35
DE  Interaction: P51575; IntAct: EBI-11599695; Score: 0.35
DE  Interaction: Q9NY93; IntAct: EBI-11599695; Score: 0.35
DE  Interaction: Q5T9A4; IntAct: EBI-11599695; Score: 0.35
DE  Interaction: O14617; IntAct: EBI-11599695; Score: 0.35
DE  Interaction: Q8NET6; IntAct: EBI-11599695; Score: 0.35
DE  Interaction: O43264; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q9Y3D8; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q6NXE6; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q9H840; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: O60220; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q58FF3; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q8WTW3; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q96P70; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q9NR31; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: O94813; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q14746; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q9UPT5; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q9NTJ3; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q9H0F6; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q96S52; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q96MW5; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q96JJ7; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q969Z0; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q8NF37; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q86TG7; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q6NUK1; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: P28066; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: Q96JB2; IntAct: EBI-11599782; Score: 0.35
DE  Interaction: P01031; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: O14735; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P46781; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P62269; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: O75477; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P49257; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P48047; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9H936; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9NUV7; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q13200; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P16435; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9BRT8; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-11614323; Score: 0.40
DE  Interaction: P17987; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P07225; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q53GQ0; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P51648; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q5T750; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: O60762; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P13667; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9Y265; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q15005; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q13438; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9Y277; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P53007; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q96IV0; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P40616; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P30101; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9Y5M8; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q02978; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P30040; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q96TA2; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P50454; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9UBM7; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P40939; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9UBB4; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P02771; IntAct: EBI-11613941; Score: 0.50
DE  Interaction: P67812; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9UM00; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P68363; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q16891; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: B4DP54; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P12235; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P05141; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9Y4W6; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P07237; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P08195; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P55157; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9UBS4; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q14697; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P27797; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9Y320; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q8TCT9; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P45880; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9NYU2; IntAct: EBI-11614317; Score: 0.40
DE  Interaction: P14625; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q96DZ1; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: O14983; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P04844; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: O15260; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P06576; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P39656; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P35232; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q92542; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P51570; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P47897; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: P28288; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q8WXG1; IntAct: EBI-12737242; Score: 0.38
GO  GO:0030430;
GO  GO:0044165;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0042802;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0005160;
GO  GO:0031625;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0052064;
GO  GO:0039520;
GO  GO:0039614;
GO  GO:0039645;
GO  GO:1902902;
GO  GO:0010507;
GO  GO:1903147;
GO  GO:0032715;
GO  GO:1903637;
GO  GO:1903215;
GO  GO:0031397;
GO  GO:0034136;
GO  GO:0034144;
GO  GO:0034156;
GO  GO:0034164;
GO  GO:0039707;
GO  GO:0032967;
GO  GO:0032914;
GO  GO:1901397;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039653;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPEDVKFPGGGQIVGGVYLLPRRGPRLGVRTTRKTSERSQPRGRRQPIPKDRRSTGKAWGKPG
SQ  RPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRHRSRNVGKVIDTLTCGFADLMGYIPVVGAPLSGAARAVAHGVRVLED
SQ  GVNYATGNLPGFPFSIFLLALLSCITVPVSAAQVKNTSSSYMVTNDCSNDSITWQLEAAVLHVPGCVPCERVGNTSRCWV
SQ  PVSPNMAVRQPGALTQGLRTHIDMVVMSATFCSALYVGDLCGGVMLAAQVFIVSPQYHWFVQECNCSIYPGTITGHRMAW
SQ  DMMMNWSPTATMILAYVMRVPEVIIDIVSGAHWGVMFGLAYFSMQGAWAKVIVILLLAAGVDAGTTTVGGAVARSTNVIA
SQ  GVFSHGPQQNIQLINTNGSWHINRTALNCNDSLNTGFLAALFYTNRFNSSGCPGRLSACRNIEAFRIGWGTLQYEDNVTN
SQ  PEDMRPYCWHYPPKPCGVVPARSVCGPVYCFTPSPVVVGTTDRRGVPTYTWGENETDVFLLNSTRPPQGSWFGCTWMNST
SQ  GFTKTCGAPPCRTRADFNASTDLLCPTDCFRKHPDATYIKCGSGPWLTPKCLVHYPYRLWHYPCTVNFTIFKIRMYVGGV
SQ  EHRLTAACNFTRGDRCDLEDRDRSQLSPLLHSTTEWAILPCTYSDLPALSTGLLHLHQNIVDVQYMYGLSPAITKYVVRW
SQ  EWVVLLFLLLADARVCACLWMLILLGQAEAALEKLVVLHAASAANCHGLLYFAIFFVAAWHIRGRVVPLTTYCLTGLWPF
SQ  CLLLMALPRQAYAYDAPVHGQIGVGLLILITLFTLTPGYKTLLGQCLWWLCYLLTLGEAMIQEWVPPMQVRGGRDGIAWA
SQ  VTIFCPGVVFDITKWLLALLGPAYLLRAALTHVPYFVRAHALIRVCALVKQLAGGRYVQVALLALGRWTGTYIYDHLTPM
SQ  SDWAASGLRDLAVAVEPIIFSPMEKKVIVWGAETAACGDILHGLPVSARLGQEILLGPADGYTSKGWKLLAPITAYAQQT
SQ  RGLLGAIVVSMTGRDRTEQAGEVQILSTVSQSFLGTTISGVLWTVYHGAGNKTLAGLRGPVTQMYSSAEGDLVGWPSPPG
SQ  TKSLEPCKCGAVDLYLVTRNADVIPARRRGDKRGALLSPRPISTLKGSSGGPVLCPRGHVVGLFRAAVCSRGVAKSIDFI
SQ  PVETLDVVTRSPTFSDNSTPPAVPQTYQVGYLHAPTGSGKSTKVPVAYAAQGYKVLVLNPSVAATLGFGAYLSKAHGINP
SQ  NIRTGVRTVMTGEAITYSTYGKFLADGGCASGAYDIIICDECHAVDATSILGIGTVLDQAETAGVRLTVLATATPPGSVT
SQ  TPHPDIEEVGLGREGEIPFYGRAIPLSCIKGGRHLIFCHSKKKCDELAAALRGMGLNAVAYYRGLDVSIIPAQGDVVVVA
SQ  TDALMTGYTGDFDSVIDCNVAVTQAVDFSLDPTFTITTQTVPQDAVSRSQRRGRTGRGRQGTYRYVSTGERASGMFDSVV
SQ  LCECYDAGAAWYDLTPAETTVRLRAYFNTPGLPVCQDHLEFWEAVFTGLTHIDAHFLSQTKQAGENFAYLVAYQATVCAR
SQ  AKAPPPSWDAMWKCLARLKPTLAGPTPLLYRLGPITNEVTLTHPGTKYIATCMQADLEVMTSTWVLAGGVLAAVAAYCLA
SQ  TGCVSIIGRLHVNQRVVVAPDKEVLYEAFDEMEECASRAALIEEGQRIAEMLKSKIQGLLQQASKQAQDIQPAMQASWPK
SQ  VEQFWARHMWNFISGIQYLAGLSTLPGNPAVASMMAFSAALTSPLSTSTTILLNIMGGWLASQIAPPAGATGFVVSGLVG
SQ  AAVGSIGLGKVLVDILAGYGAGISGALVAFKIMSGEKPSMEDVINLLPGILSPGALVVGVICAAILRRHVGPGEGAVQWM
SQ  NRLIAFASRGNHVAPTHYVTESDASQRVTQLLGSLTITSLLRRLHNWITEDCPIPCSGSWLRDVWDWVCTILTDFKNWLT
SQ  SKLFPKLPGLPFISCQKGYKGVWAGTGIMTTRCPCGANISGNVRLGSMRITGPKTCMNTWQGTFPINCYTEGQCAPKPPT
SQ  NYKTAIWRVAASEYAEVTQHGSYSYVTGLTTDNLKIPCQLPSPEFFSWVDGVQIHRFAPTPKPFFRDEVSFCVGLNSYAV
SQ  GSQLPCEPEPDADVLRSMLTDPPHITAETAARRLARGSPPSEASSSVSQLSAPSLRATCTTHSNTYDVDMVDANLLMEGG
SQ  VAQTEPESRVPVLDFLEPMAEEESDLEPSIPSECMLPRSGFPRALPAWARPDYNPPLVESWRRPDYQPPTVAGCALPPPK
SQ  KAPTPPPRRRRTVGLSESTISEALQQLAIKTFGQPPSSGDAGSSTGAGAAESGGPTSPGEPAPSETGSASSMPPLEGEPG
SQ  DPDLESDQVELQPPPQGGGVAPGSGSGSWSTCSEEDDTTVCCSMSYSWTGALITPCSPEEEKLPINPLSNSLLRYHNKVY
SQ  CTTSKSASQRAKKVTFDRTQVLDAHYDSVLKDIKLAASKVSARLLTLEEACQLTPPHSARSKYGFGAKEVRSLSGRAVNH
SQ  IKSVWKDLLEDPQTPIPTTIMAKNEVFCVDPAKGGKKPARLIVYPDLGVRVCEKMALYDITQKLPQAVMGASYGFQYSPA
SQ  QRVEYLLKAWAEKKDPMGFSYDTRCFDSTVTERDIRTEESIYQACSLPEEARTAIHSLTERLYVGGPMFNSKGQTCGYRR
SQ  CRASGVLTTSMGNTITCYVKALAACKAAGIVAPTMLVCGDDLVVISESQGTEEDERNLRAFTEAMTRYSAPPGDPPRPEY
SQ  DLELITSCSSNVSVALGPRGRRRYYLTRDPTTPLARAAWETVRHSPINSWLGNIIQYAPTIWVRMVLMTHFFSILMVQDT
SQ  LDQNLNFEMYGSVYSVNPLDLPAIIERLHGLDAFSMHTYSHHELTRVASALRKLGAPPLRVWKSRARAVRASLISRGGKA
SQ  AVCGRYLFNWAVKTKLKLTPLPEARLLDLSSWFTVGAGGGDIFHSVSRARPRSLLFGLLLLFVGVGLFLLPAR
//
ID  Q68801;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356417;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q68801;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTLPKPQRITKRNINRRPQDVKFPGGGQIVGGVYVLPRRGPKLGVRAVRKTSERSQPRSRRQPIPRARRTEGRSWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPSWGPNDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPVGGVARALAHGVRALED
SQ  GINFATGNLPGCSFSIFLLALLSCLLTPTAGLEYRNASGLYTVTNDCSNGSIVYEAGDVILHLPGCIPCVRLNNASKCWT
SQ  PVSPTVAVSRPGAATASLRTHVDMMVGAATLCSALYVGDLCGALFLVGQGFSWRHRQHWTVQDCNCSIYPGHLTGHRMAW
SQ  DMMMNWSPAMTLIVSQVLRLPQTMFDLVIGAHWGVMAGVAYYSMQGNWAKVFLVLCLFSGVDASTTITGGVAASGAFTIT
SQ  SLFSTGAKQPLHLVNTNGSWHINRTALNCNDSLNTGFIAGLLYYHKFNSSGCVERMSACSPLDRFAQGWGPLGPANISGP
SQ  SSEKPYCWHYAPRPCDTVPAQSVCGPVYCFTPSPVVVGATDKRGAPTYTWGENESDVFLLESARPPTEPWFGCTWMNGSG
SQ  YVKTCGAPPCHIYGGREGKSNNSLVCPTDCFRKHPDATYNRCGAGPWLTPRCLVDYPYRLWHYPCTVNYTIFKVRMFVGG
SQ  LEHRFNAACNWTRGERCNLEDRDRSEMYPLLHSTTEQAILPCSFVPIPALSTGLIHLHQNIVDVQYLYGISSGLVGWAIK
SQ  WEFVILIFLLLADARVCVVLWMMMLISQAEAALENLIVLNAISAAGTHGIWWSLVAFCVAWHVRGRIFPIAVYSIVGLWP
SQ  LLLLVLMLPYRAYAWTGTDTSTLGAGVLSLFALFTLSPWYKHWIARLIWWNQYTIARCEAALQIWVPPLLARGARDGIIL
SQ  LAGLFYPALVFDITKLLLAILGPLYILQASLVRVPYFVRAHAVVRLCILVRNITGGKYVQMVLLALARGFNTYLYDHLSP
SQ  MTDWAAEGLKDLAVAVEPVIFSPMEVKVITWGADTTACGDILCGLPVSARLGKEVLLGPADDYRSMGWRLLAPITAHAQQ
SQ  TRGLFGTIVTSLTGRDKNIVTGEIQVLSTSTQTFLGTSVGGVMWTVYHGAGSRTLAGNKRPALQMYTNVDQDLVGWPSPP
SQ  GAKSLVPCTCGSADLYLITRDADVLPARRRGDSTASLLSPRPLACLKGSSGGPIMCPSGHVAGIFRAAVCTRGVAKALQF
SQ  IPVESLSAQTRSPSFSDNSTPPAVPQTFQVGYLHAPTGSGESTKVPASYVAQGYTVLVLNPSVAATLGFGRFMSHAYGID
SQ  PNVRTGTRTITTGAKLTYSTYGKFLADGGCSGGAYDVIICDECHAQDATSILGIGTVLDQAETAGARLVVLATATPPGSI
SQ  TVPHSNIEEVALTGEGEIPFYGRAIPLGVIKGGRHLIFCHSKKKCDELAKQLTSLGVNAVAFYRGLDVSVIPTQGDVVVC
SQ  ATDALITGYTGDFDSVIDCNVAVEQYVDFSLDPTFSIETHTVPQDAVSRSQRRGRTGRGKSGTYRYVSPGERPSGMFDSV
SQ  VLCECYDAGCAWYELTPSETTVRLRAYLSTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQQGLNFPYLTAYQATVCA
SQ  RAAALPPSWDETWKCLIRLKPTLHGPTPLLYRLGAVQNEICTTHPVTKYIATCMAADLEVATSAWVLLGGVMAALTAYCL
SQ  SVGSVVIVGHLVLGGKPALVPDKEVLYQQYDEMEECSRAAPYIEQAQGIAQQFKEKVIGLLQQADQKAADIKPIATPYWQ
SQ  KLETFWSKHMWNFVSGIQYLAGLSTLPGNPAIASLMAFTASVTSPLTTNQTLLFNIMGGWVASNLAPPPASTAFVVSGLA
SQ  GAAVGSIGLGKVLLDILAGYGAGVAGALVAFKIMGGEMPSTEDMVNLLPAILSPGALVVGVICAAILRRHVGPGEGAVQW
SQ  MNRLIAFASRGNHVAPTHYVPESDAAAKVTALLSSLTVTQLLRRLHQWINEDYPTPCDGNWLYDIWNWVCTVLADFKLWL
SQ  GAKILPKMPGIPFLSCQKGYRGTWRGDGVVSTRCPCGALLSGHVKNGTMRLVGPRWCANTWHGTFPINGYTTGPSTPAPS
SQ  YAYSRALWRVASDSYVEVRKVGDFHYVTGTTDDGLKCPCQVPLPEFFTELDGVRLHRYAPVCRPLLRDDVTFTVGLNSYV
SQ  IGSQLPCEPEPDVAVVTSMLQDPSHITVETAKRRLDRGSPPSLASSSASQLSAPSRKATCTTHGRHPDAELITANLLWRQ
SQ  EMGSNITRVESESKVVILDSFEPLRACDDEDELSVAAECFKKPPKYPPALPIWARPDYNPPLVEPWKDPDYVPPTVHGCA
SQ  LPPQKLPPVPPPRRKRTIVLSESTVSKALASLAEKSFPQPTCSAEDESTSGVGTQSGSLTGPVQLDDDDSDNESHSSMPP
SQ  LEGEPGDPDLSSGSWSTVSGEEQSVVCCSMSYSWTGALITPCAAEEEKLPISPLSNSLLRHHNLVYSTSSRSAAQRQKKV
SQ  TFDRLQVLDDHYNTTLKEIKELASGVKAELLSVEEACRLVPSHSARSKFGYGAKEVRSLSSKAINHINSVWEDLLEDNTT
SQ  PIPTTIMAKNEVFAVAPHKGGRKPARLIVYPDLGVRICEKRALYDVIQKLPSAIMGSAYGFQYSPKQRVEYLLKMWNSKK
SQ  TPLGFSYDTRCFDSTVTEQDIRVEESIYQACDLKDEARRVITSLTERLYCGGPMFNSKGQHCGYRRCRASGVLPTSFGNT
SQ  VTCYLKAKAATKAAGIKDPSFLVCGDDLVVIAESAGIDEDKSALRAFTEAMTRYSAPPGDPPQPTYDLELITSCSSNVSV
SQ  AHDGAGKRYYYLTRDPETPLARAAWETARHTPVNSWLGNIIMYAPTIWVRMVIMTHFFSILQAQEQLEKALDFEMYGAVY
SQ  SVTPLDLPAIIERLHGLSAFSLHSYSPVELNRVAGALRKLGIPPLRAWRHRARAVRAKLISQGGKAKICGLYLFNWAVRT
SQ  KAKLTPLPQAGLLDLSRWFTVGAGGNDIYHSVSRARSRHLLLGLLLLTVGVGIFLLPAR
//
ID  Q68798;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356423;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q68798;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRQTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRQTGRAWGQPG
SQ  YAWPLYGNEGCGWAGWLLSPRGSRPTWGPNDPRRRSRNLGKVIDTLTCGLADLMGYIPVIGGPLGGVAAALAHGVRAVED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTVPASAVNYANKSGIYHLTNDCPNSSMVYEAEAIILHLPGCVPCIRTGNQSRCWT
SQ  PATPTLAIPNSTVPASGFRQHIDLMVGAAALCSAMYLGDLCGGVFLVGQLFTFRPRIHQTVQDCNCSIYTGHVTGHRMAW
SQ  DMMMNWSPTATFVVSSALRAPQVLFDIFAGGHWGIIGALLYYSTAANWAKVIIVLLLFAGVDASTYVASSVSQATSGLVS
SQ  LFSAGARQNLQLINTNGSWHINRTALNCNDSLQTGFIASLFYRNKFNATGCPERLSACKTLDSFDQGWGPITYANISGPA
SQ  VEKPYCWHYPPRPCEVVSALNVCGPVYCFTPSPVVLGTTDRRGNPTYTWGANETDVFMMSSLRPPAGGWYGCTWMNTSGF
SQ  VKTCGAPPCNIRPNPEENRTETLRCPTDCFRKHPGATYAKCGSGPWLTPRCLVDYPYRLWHYPCTVNYTLHKVRMYIAGS
SQ  EHRFTAACNWTRGERCDLADRDRIEMSPLLFSTTELAILPCSFTTMPALSTGLIHLHQNVVDVQYLYGLSTSIVNWAIKW
SQ  EYVVLLFLVLADSRICLALWLMLLIGQAEAALENLIVLNAASAAATRGWECFLLFMCWAWYVRGRVVPAVTYGLLNLWPL
SQ  LLLVLLLPHRAYAYDGVQAGSIGAAVIAALTIFSLTPAYKTLLAHFLWWTQYFIAHIEAKLHVWVPFLRVRGGRDAIILL
SQ  TCVFHPSLGFEVTKILLALIGPLYLLHASLLRVPYYVRAHALIRICALVQNVAGGKYVQAAILRAGSWTGTYIYDHLVPL
SQ  RTWASDGLRDLAVAVEPVVFSPMEKKVITWGADTAACGDILAGLPVSARRGNLILLGPADDVKDKGWSLLAPITAYAQQT
SQ  RGLLGTIVTSLTGRDKNEAAGEIQILSTATQTFLATCVNGVCWTVYHGAGSKTLAGPRGPVCQMYTNVDQDMVGWPAPAG
SQ  TRSYTPCTCGASDLYLITRQADVIPARRRGDNRAGLISPRPISTLKGSSGGPLLCPSGHVVGLFRAAVCTRGVAKALDFV
SQ  PCEAMDATTRSPTFTDNSTPPAVPQAYQVGYLHAPTGSGKSTKVPVAYASQGYKVLVLNPSVAATLSFGSYLSRAHGIDP
SQ  NIRTGVRTITTGAPITYSTYGKFLADGGCSGGAYDVIICDECHSTDPTTVLGIGTVLDQAETAGCRLTVLATATPPGSVT
SQ  VPHPNIQETALPLTGEVPFYGKAIPLEYIKGGRHLIFCHSKKKCDELAAQLRTLGLNAVAFYRGVDVSVIPTSGDVVVCA
SQ  TDALMTGYTGDFDSVIDCNVAVTQIVDFSLDPTFSIETTTVPQDAVARSQRRGRTGRGKPGVYRYVSQGERPSGMFDTVV
SQ  LCEAYDTGAAWYELTPAETTVRLRAYLNTPGLPVCQDHLEFWEAVFTGLTHIDAHFLSQTKQGGENFAYLVAYQATVCAR
SQ  AKAPPPSWDTMWKCLLRLKPTLTGPTPLLYRLGAVQNEVTPTHPVTKYIMACMSADLEVITSTWVVAGGILAAIAAYCLT
SQ  VGSVVICGRITTSSRPAVIPDREVMYQQYDEMEECSRHLPYLVEGQQLAEQFKQNVLGLIQVTTKQAEELKPAVHSAWPK
SQ  LEQFWYKHMWNFISGIQYLAGLSTLPGNPAVAALMSFSASLTSPLTTAQTLLLNVLGGWVASQLATPVPATAFVVSGLAG
SQ  AAIGSIGLGKVIVDILAGYGAGVSGALVAFKIMSGETPSVEDMVNLLPALLSPGALVVGVVRAAILRRHVGPSEGAAQWM
SQ  NRLIAFASRGNHVSPTHYVPETDASRAVTNILSSLTITSLLRKLHHWITEDYATPCGSTWLRDIWDWVCTVLSDFRVWLK
SQ  SKLMPSLPGVPFFSCQRGYRGTWRGDGICNTTCPCGASIAGHVKNGTMRIVGPRTCSNVWNGTFPINATTTGPSIPIPAP
SQ  NYKKALWRVSATEYVEVVRVGDSHYITGVTAENTKCPCQVPAPEFFTEVDGVRLHRYAPECKPILRDEVTFTVGLSTYVV
SQ  GSQLPCEPEPDVLVVTSMLRDPDHITAEEASRRLKRGSPPSLASSSASQLSAPSLKATCTTHADHPDAELVEANLLWRQE
SQ  MGGNITRVESENKIVILDSFEPLKAEFDDREISVAAECHRPPRFKYPPALPVWARPDYNPPLLETWKAPDYDPPVVSGCA
SQ  LPPQGLPPVPPPRRKKLVQLDDSVVGHVLAQLAEKSFPATPDQPQTNSDSGHGTNGAASLPSAEDDDASDADSYSSMPPL
SQ  EGEPGDPDLSDGGGSGSWSTVSSEETSVVCCSMSYSWTGALITPCAAEEEKLPISPLSNTLIRHHNMVYSTTSRSAALRQ
SQ  KKVTFDRQQVVDQHYYDTLKEMKARASTVSAKLLSVEEACDLTPAHSARSKFGYGAKDVRGRTSKALNHINSVWEDLLED
SQ  NVTPIPTTIMAKNEVFCVDVSKGGRKPARLIVYPDLSVRVCEKRALYDVTRKLPVAVMGAAYGFQYSPSQRVEYLLKIWR
SQ  SKKTPMGFSYDTRCFDSTVTERDIRTEESIYQCCELDPVARKAISSLTERLYVGGPMYNSQGQSCGYRRCRASGVLPTSM
SQ  GNTLTCYLKAMAACKAAGLKNFDMLVCGDDLVVISESLGVSEDASALRAFTDAMTRYSAPPGDEPHPEYDLEHITSCSSN
SQ  VSVAHDHTGQRYYYLTRDPTNVLARAAWETARHTPVNSWLGNIIMYAPTIWVRMVLMTHFFGILQPQEQLHKALDFDMYG
SQ  VTYNITPLDLPQIIQRLHGMAAFSLHGYSPGELNRVGACLRKLGAPPLRAWRHRARAVRAKLIAQGGKAAICGMYLFNWA
SQ  VKTKLKLTPLRDAHRLDLSGWFVAGYSGGDIFHSVSHARPRVLLLCLLLLTVGVGIFFLPPR
//
ID  Q9DHD6;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356412;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q9DHD6;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKDRRSTGKSWGKPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPTWGPSDPRHRSRNLGRVIDTITCGFADLMGYIPVVGAPVGGVARALAHGVRVLED
SQ  GINYATRNLPGCSFSIFLLALLSCVTVPVSSVEIRNISTSYYATNDCSNNSITWQLTNAVLHLPGCVPCENDNGTLRCWI
SQ  QVTPNVAVKHRGALTHNLRAHVDVIVMAATVCSALYVGDVCGAVMIVSQALIVSPERHNFTQECNCSIYQGHITGQRMAW
SQ  DMMLNWSPTLTMILAYAARVPELVLEIVFGGHWGVVFGLAYFSMQGAWAKVIAILLLVAGVDATTYSTGATVGRTVGSFA
SQ  GLFKLGAQQNVQLINTNGSWHINRTALNCNDSLHTGFMAALFYANKFNSSGCPERLSSCRGLDDFRIGWGTLEYETNVTN
SQ  VEDMRPYCWHYPPKPCGIVPAQSVCGPVYCFTPSPVVVGTTDRQGVPTYNWGDNETDVFLLNSTRPPRGAWFGCTWMNGT
SQ  GFTKTCGAPPCRIRKDFNSTLDLLCPTDCFRKHPDATYVKCGAGPWLTPRCLIDYPYRLWHYPCTVNFTIFKVRMYVGGV
SQ  EHRFSAACNFTRGDRCRLEDRDRGQQSPLLHSTTEWAVLPCSFSDLPALSTGLLHLHQNIVDVQYLYGLSPAVTKYIVKW
SQ  EWVVLLFLLLADARICACLWMLIILGQAEAALEKLIILHSASAASANGPLWFFIFFTAAWYLKGRVVPAATYSVLGLWSF
SQ  LLLVLALPQQAYALDAAEQGELGLVILMIISIFTLTPAYKILLSRSVWWLSYMLVLAEAQVQQWVPPLEARGGRDGIIWV
SQ  AVILHPHLVFEVTKWLLAILGSAYLLKASLLRVPYFVRAHALLRVCTLVRHLAGARYIQMLLITMGRWTGTYIYDHLSPL
SQ  STWAAQGLRDLAVAVEPVVFSPMEKKVIVWGAETVACGDILHGLPVSARLGREVLLGPADGYTSKGWKLLAPITAYTQQT
SQ  RGLLGAIVVSLTGRDKNEQAGQVQVLSSVTQSFLGTSISGVLWTVYHGAGNKTLASPRGPVTQMYTSAEGDLVGWPSPPG
SQ  TKSLDPCTCGAVDLYLVTRNADVIPVRRKDDRRGALLSPRPLSTLKGSSGGPVLCPRGHAVGLFRAAVCARGVAKSIDFI
SQ  PVESLDIARRTPSFSDNSTPPAVPQTYQVGYLHAPTGSGKSTKVPAAYTSQGYKVLVLNPSVAATLGFGAYMSKAHGINP
SQ  NIRTGVRTVTTGDSITYSTYGKFLADGGCSAGAYDIIICDECHSVDATTILGIGTVLDQAETAGVRLVVLATATPPGTVT
SQ  TPHANIEEVALGHEGEIPFYGKAIPLASIKGGRHLIFCHSKKKCDELAAALRGMGVNAVAYYRGLDVSVIPTQGDVVVVA
SQ  TDALMTGYTGDFDSVIDCNVAVTQIVDFSLDPTFTITTQTVPQDAVSRSQRRGRTGRGRLGTYRYVSSGERPSGMFDSVV
SQ  LCECYDAGAAWYELTPAETTVRLRAYFNTPGLPVCQDHLEFWEAVFTGLTHIDAHFLSQTKQGGDNFAYLTAYQATVCAR
SQ  AKAPPPSWDVMWKCLTRLKPTLTGPTPLLYRLGAVTNEITLTHPVTKYIATCMQADLEVMTSTWVLAGGVLAAVAAYCLA
SQ  TGCISIIGRIHLNDQVVVAPDKEILYEAFDEMEECASKAALIEEGQRMAEMLKSKILGLLQQATKQAQDIQPAMQSSWPK
SQ  IEQFWARHMWNFISGIQYLAGLSTLPGNPAVASMMAFSAALTSPLPTSTTILLNIMGGWLASQIAPPAGATGFVVSGLVG
SQ  AAVGSIGLGKILVDVLAGYGAGISGALVAFKIMSGEKPSVEDVVNLLPAILSPGALVVGVICAAILRRHVGQGEGAVQWM
SQ  NRLIAFASRGNHVAPTHYVAESDASLRVTQVLSSLTITSLLRRLHAWITEDCPVPCSGSWLRDIWEWVCSILTDFKNWLS
SQ  AKLLPKMPGLPFISCQKGYRGVWAGTGVMTTRCSCGANISGHVRLGTMKITGPKTCLNMWQGTFPINCYTEGPCVPKPPP
SQ  NYKTAIWRVAASEYVEVTQHGSFSYVTGLTSDNLKVPCQVPAPEFFSWVDGVQIHRFAPTPGPFFRDEVTFTVGLNSLVV
SQ  GSQLPCDPEPDTEVLASMLTDPSHITAETAARRLARGSPPSQASSSASQLSAPSLKATCTTHKTAYDCDMVDANLFMGGD
SQ  VTRIESDSKVIVLDSLDSMTEVEDDREPSVPSEYLTRRRKFPPALPPWARPDYNPPVIETWKRPDYEPPTVLGCALPPTP
SQ  QAPVPPPRRRRARVLTQDNVEGVLREMADKVLSPLQDTNDSGHSTGADTGGDSVQQPSGETAASDAGSLSSMPPLEGEPG
SQ  DPDLEFEPARSAPPSEGECEVIDSDSKSWSTVSDQEDSVICCSMSYSWTGALITPCGPEEEKLPISPLSNSLMRFHNKVY
SQ  STTSRSASLRAKKVTFDRVQVLDAHYDSVLQDVKRAASKVSARLLSVEEACALTPPHSAKSRYGFGAKEVRSLSRGAVNH
SQ  IRSVWEDLLEDQHTPIDTTAMAKNEVFCIDPAKGGKKPARLIVYPDLGVRVCEKMALYDIAQKLPKAIMGPSYGFQYSPA
SQ  ERVDFLLKAWGSKKDPMGFSYDTRCFDSTVTERDIRTEESIYQACSLPQEARTVIHSITERLYVGGPMTNSKGQSCGYRR
SQ  CRASGVFTTSMGNTMTCYIKALAACKAAGIVDPTMLVCGDDLVVISESQGNEEDERNLRAFTEAMTRYSAPPGDLPRPEY
SQ  DLELITSCSSNVSVALDSRGRRRYFLTRDPTTPITRAAWETVRHSPVNSWLGNIIQYAPTIWVRMVIMTHFFSILLAQDT
SQ  LNQNLNFEMYGAVYSVNPLDLPAIIERLHGLDAFSLHTYSPHELSRVAATLRKLGAPPLRAWKSRARAVRASLIIQGGRA
SQ  ATCGRYLFNWAVKTKLKLTPLPEASRLDLSGWFTVGAGGGDIFHSVSHARPRLLLLCLLLLSVGVGIFLLPAR
//
ID  Q00269;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  31642;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q00269;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTYRRPQDVKFPGGGQIVGGVYVLPRRGPTLGVRATRKTSERSQPRGRRQPIPKARRPEGRAWAQPG
SQ  YPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTIPASAYQVRNASGLYHVTNDCSNSSIVYEAAGMIMHTPGCVPCVRENNASRCWV
SQ  ALTPTLAARNTSIPTTTIRRHVDLLVGAAAFCSAMYVGDLCGSVFLVSQLFTFSPRRYETVQDCNCSIYPGHVSGHRMAW
SQ  DMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMVGNWAKVLIVMLLFAGVDGVTYTTGGSQARHTQSVT
SQ  SFFTQGPAQRIQLINTNGSWHINRTALNCNESLNTGFFAALFYAHKFNSSGCPERMASCSSIDKFAQGWGPITYTEPRDL
SQ  DQRPYCWHYAPRQCGIVPASQVCGPVYCFTPSPVVVGTTDRSGAPTYNWGANETDVLLLNNTRPPQGNWFGCTWMNSTGF
SQ  TKTCGGPPCNIGGVGNLTLTCPTDCFRKHPEATYTKCGSGPWLTPRCIVDYPYRLWHYPCTVNFTIFKVRMYVGGVEHRL
SQ  SAACNWTRGERCDLEDRDRSELSPLLLSTTEWQTLPCSFTTLPALSTGLIHLHQNIVDVQYLYGIGSAVVSFVIKWEYIV
SQ  LLFLLLADARVCACLWMMLLIAQAEAALENLVVLNAASLAGADGILSFLVFFCAAWYIKGRLVPGAAYALYGVWPLLLLL
SQ  LALPPRAYAMDREMAASCGGVVFVGLILLTLSPHYKVFLARLIWWLQYFITRAEAHLCVWVPPLNVRGGRDAIILLTCAA
SQ  HPELIFDITKLLLAILGPLMVLQAAITAMPYFVRAQGLIRACMLVRKVAGGHYVQMAFMKLAALTGTYVYDHLTPLQDWA
SQ  HAGLRDLAVAVEPVVFSDMETKIITWGADTAACGDIILGLPVSARRGREILLGPADSIEGQGWRLLAPITAYAQQTRGLL
SQ  GCIVTSLTGRDKNQVEGEVQVVSTATQSFLATCVNGVCWTVFHGAGSKTLAGPKGPITQMYTNVDQDLVGWHAPPGARSL
SQ  TPCTCGSSDLYLVTRHADVIPVRRRGDGRGSLLSPRPVSYLKGSSGGPLLCPSGHAVGIFRAAVCTRGVAKAVDFIPVES
SQ  METTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGTDPNIRT
SQ  GVRTITTGAPITYSTYGKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHP
SQ  NIEEVALSNTGEIPFYGKAIPLEAIKGGRHLIFCHSKKKCDELAAKLSGLGINAVAYYRGLDVSVIPTSGDVVIVATDAL
SQ  MTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRGGIYRFVTPGERPSGMFDSSVLCEC
SQ  YDAGCAWYELTPAETTVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAP
SQ  PPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPITKFIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSV
SQ  VIVGRIILSGRPAVVPDREVLYREFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESRWRALEAF
SQ  WAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQNTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAIG
SQ  SIGLGKVLVDILAGYGAGVAGALVAFKVMSGEAPSAEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLKDVWDWICTVLTDFKTWLQSKLL
SQ  PKLPGVPFFSCQRGYKGVWRGDGIMQTTCPCGAQITGHVKNGSMRIVGPKTCSNTWHGTFPINAYTTGPCTPSPAPNYSR
SQ  ALWRVAAEEYVEITRVGDFHYVTGMTTDNVKCPCQVPAPEFFTELDGVRLHRYAPACRPLLREDVTFQVGLNQYLVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHDSPDADLIEANLLWRQEMGGN
SQ  ITRVESENKVVILDSFDPLRAEEDEREVSVAAEILRKSKKFPPALPIWARPDYNPPLLESWKSPDYVPPAVHGCPLPPTT
SQ  GPPIPPPRKKRTVVLTESTVSSALAELATKTFGSSGSSAVDSGTATAPPDQTSDDGDKESDVESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSGEASDDIVCCSMSYTWTGALITPCAAEESKLPINALSNSLLRHHNMVYATTSRSASLRQKKVTFDRLQVLD
SQ  DHYRDVLKEMKAKASTVKAKLLSVEEACKLTPPHSAKSKFGYGAKDVRNLSSKAINHIRSVWKDLLEDTETPIDTTIMAK
SQ  SEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPGQRVEFLVNAWKSKKSPMGFSYDT
SQ  RCFDSTVTESDIRVEESIYQCCDLAPEARQAIKSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKATA
SQ  ACRAAKLQDCTMLVNGDDLVVICESAGTQEDAASLRVFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRV
SQ  YYLTRDPTTPLARAAWETARHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQ
SQ  IIQRLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRARLLSQGGRAATCGKYLFNWAVRTKLKLTPIPA
SQ  ASQLDLSSWFVAGYSGGDIYHSLSRARPRWFMWCLLLLSVGVGIYLLPNR
//
ID  Q81495;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356416;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q81495;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTLPKPQRKTKRNTIRRPQDVKFPGGGVIYVGVYVLPRRGPRLGVRATRKTSERSQPRGRRKPIPKARRSEGRSWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPNWAPNDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRALED
SQ  GINFATGNLPGCSFSIFLLALFSCLIHPAASLEWRNTSGLYVLTNDCSNSSIVYEADDVILHTPGCIPCVQDGNTSTCWT
SQ  PVTPTVAVRYVGATTASIRSHVDLLVGAGTMCSALYVGDMCGPVFLVGQAFTFRPRRHRTVQTCNCSLYPGHLSGQRMAW
SQ  DMMMNWSPAVGMVVAHILRLPQTLFDVVAGAHWGIIAGLAYYSMQGNWAKVAIIMVMFSGVDASTHVTAGQAARNAYGIT
SQ  SLFSVGAKQNLQLINTNGSWHINRTALNCNESINTGFIAGLFYYHKFNSTGCPQRLSSCKPITFFKQGWGPLTDANITGP
SQ  SDDKPYCWHYAPRPCGIVPALNVCGPVYCFTPSPVVVGTTDAKGAPTYTWGANKTDVFLLESLRPPSGRWFGCTWMNSTG
SQ  FVKTCGAPPCNIYGDGRDAQNESDLFCPTDCFRKHPEATYSRCGAGPWLTPRCLVDYPYRLWHYPCTVNFTLFKVRMFVG
SQ  GFEHRFTAACNWTRGERCDIEDRDRSEQHPLLHSTTELAILPCSFTPMPALSTGLIHLHQNIVDVQYLYGIGSGMVGWAL
SQ  KWEFVILIFLLLADARVCVALWLILTISQAEAALENLVTLNAVAAAGTHGIGWYLVAFCAAWYVRGKLVPLVTYSLTGLW
SQ  SLALLVLLLPQRAYAWSGEDSATLGAGILVLFGFFTLSPWYKHWIARLIWWNQYTICRCESALHVWVPPLLARGGRDGVI
SQ  LLTSLLYPSLIFDITKLLIAALGPLYLIQATITATPYFVRAHVLVRLCMLVRSVMGGKYFQMIILSLADGSNTYLYDHLA
SQ  PMQHWAAAGLKDLAVATEPVIFSPMEIKVITWGADTAACGDILCGLPVSARLGREVLLGPADDYREMGWRLLAPITAYAQ
SQ  QTRGLLGTIVTSLTGRDKNVVAGEVQVLSTATQTFLGTTVGGVMWTVYHGAGSRTLAGVKHPALQMYTNVDQDLVGWPAP
SQ  PGAKSLEPCTCGSADLYLVTRDADVIPARRRGDSTASLLSPRPLARLKGSSGGPVMCPSGHVAGIFRAAVCTRGVAKALQ
SQ  FIPVETLSTQARSPSFSDNSTPPAVPQSYQVGYLHAPTGSGKSTKVPAAYVAQGYNVLVLNPSVAATLGFGSFMSRAYGI
SQ  DPNIRTGNRTVTTGAKLTYSTYGKFLAGGGCSGGAYDVIICDDCHAQDATSILGIGTVLDQAETAGVRLTVLATATPPGS
SQ  ITVPHSNIEEVALGSEGEIPFYGKAIPIACIKGGRHLIFCHSKKKCDKMASKLRGMGLNAVAYYRGLDVSVIPTTGDVVV
SQ  CATDALMTGFTGDFDSVIDCNVAVEQYVDFSLDPTFSIETCTAPQDAVSRSQRRGRTGRGRLGTYRYVTPGERPSGMFDS
SQ  VVLCECYDAGCSWYDLQPAETTVRLRAYLSTPGLPVCQDHLDLWESVFTGLTHIDAHFLSQTKQAGLNFSYLTAYQATVC
SQ  ARAQAPPPSWDETWKCLVRLKPTLHGPTPLLYRLGPVQNEICLTHPITKYVMACMSADLEVTTSTWVLLGGVLAAVAAYC
SQ  LSVGCVVIVGHIELGGKPALVPDKEVLYQQYDEMEECSQARPYIEQAQVIAHQFKEKVLGLLQRATQQQAVIEPIVVSNW
SQ  QKLEVLWHKHMWNFVSGIQYLAGLSTLPGNPAVASLMAFTASVTSPLTTNQTMFFNILGGWVATHLAGPQASSAFVVSGL
SQ  AGAAIGGIGLGRVLLDILAGYGAGVSGALVAFKIMGGEPPTTEDMVNLLPAILSPGALVVGVICAAILRRHVGPGEGPVQ
SQ  WMNRLIAFASRGNHVSPAHYVPESDAAARVTALLSSLTVTSLLRRLHQWINEDYPSPCSGDWLRIIWDWVCSVVSDFKTW
SQ  LSAKIMPALPGLPFISCQKGYKGVWRGDGVMSTRCPCGASIAGHVKNGSMRLAGPRTCANMCHGTFPINEYTTGPSTPCP
SQ  PPNYTRALWRVAANSYVEVRRVGDFHYITGATEDGLKCPCQVPATEFFTEVDGVRIHRYAPPCRPLLRDEITFMVGLNSY
SQ  AIGSQLPCEPEPDVSVLTSMLRDPSHITAETAARRLARGSPPSEASSSASQLSAPSLKATCQTHRPHPDAELVDANLLWR
SQ  QEMGSNITRVESETKVVILDSFEPLRAETDDAELSAAAECFKKPPKYPPALPIWARPDYNPPLLDRWKSPDYVPPTVHGC
SQ  ALPPKGAPPVPPPRRKRTIQLDGSNVSAALAALAEKSFPSSKPQEENSSSSGVDTQSSTASKVLPSPGEESDSESCSSMP
SQ  PLEGEPGDPDLSCDSWSTVSDSEEQSVVCCSMSYSWTGALITPCSAEEEKLPISPLSNSLLRHHNLVYSTSSRSASQRQK
SQ  KVTFDRLQVLDDHYKTALQEVKERASRVKARMLSIEEACALVPPHSARSKFGYSAKDVRSLSSKAINQIRSVWEDLLEDT
SQ  TTPIPTTIMAKNEVFCVDPAKGGRKAARLIVYPDLGVRVCEKRALYDVIQRLSIETMGSAYGFQYSPRQRVERLLKMWTS
SQ  KKTPLGFSYDTRCFDSTVTGQDIRVEEAVYQCCNLEPEPGQAISSLTERLYCGGPMNNSKGAQCGYLRCRASGVLPTSFG
SQ  NTITCYIKATAAARAAGLRNPDFLVCGDDLVVVAESDGVDEDRATLRAFTEAMTRYSAPPGDAPQPTYDLELITSCSSNV
SQ  SVARDDKGKRYYYLTRDATTPLARAAWETARHTPVNSWLGSIIMYAPTIWVRMVMMTHFFSILQSQEILDRPLDFEMYGA
SQ  TYSVTPLDLPAIIERLHGLSAFSVHSYSPVELNRVAGTLRKLGCPPLRAWRHRARAVRAKLIAQGGRAKICGLYLFNWAV
SQ  RTKTKLTPLPAAGQLDLSSWFTVGVGGNDIYHSVSRARTRYLLLCLLLLTVGVGIFLLPAR
//
ID  Q81258;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356415;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000269|PubMed:17188392}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q81258;
DR  PDB: 6P6S;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (PubMed:17188392). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:17188392, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTLPKPQRKTKRNTIRRPQDVKFPGGGQIVGGVYVLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRSEGRSWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPSWGPNDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPVGGVARALAHGVRALED
SQ  GINFATGNLPGCSFSIFLLALFSCLIHPAASLEWRNTSGLYVLTNDCSNSSIVYEADDVILHTPGCVPCVQDGNTSTCWT
SQ  PVTPTVAVRYVGATTASIRSHVDLLVGAATMCSALYVGDMCGAVFLVGQAFTFRPRRHQTVQTCNCSLYPGHLSGHRMAW
SQ  DMMMNWSPAVGMVVAHVLRLPQTLFDIMAGAHWGILAGLAYYSMQGNWAKVAIIMVMFSGVDAHTYTTGGTASRHTQAFA
SQ  GLFDIGPQQKLQLVNTNGSWHINSTALNCNESINTGFIAGLFYYHKFNSTGCPQRLSSCKPITFFRQGWGPLTDANITGP
SQ  SDDRPYCWHYAPRPCDIVPASSVCGPVYCFTPSPVVVGTTDARGVPTYTWGENEKDVFLLKSQRPPSGRWFGCSWMNSTG
SQ  FLKTCGAPPCNIYGGEGNPHNESDLFCPTDCFRKHPETTYSRCGAGPWLTPRCMVDYPYRLWHYPCTVDFRLFKVRMFVG
SQ  GFEHRFTAACNWTRGERCDIEDRDRSEQHPLLHSTTELAILPCSFTPMPALSTGLIHLHQNIVDVQYLYGVGSGMVGWAL
SQ  KWEFVILVFLLLADARVCVALWLMLMISQTEAALENLVTLNAVAAAGTHGIGWYLVAFCAAWYVRGKLVPLVTYSLTGLW
SQ  SLALLVLLLPQRAYAWSGEDSATLGAGVLVLFGFFTLSPWYKHWIGRLMWWNQYTICRCESALHVWVPPLLARGSRDGVI
SQ  LLTSLLYPSLIFDITKLLMAVLGPLYLIQATITTTPYFVRAHVLVRLCMLVRSVIGGKYFQMIILSIGRWFNTYLYDHLA
SQ  PMQHWAAAGLKDLAVATEPVIFSPMEIKVITWGADTAACGDILCGLPVSARLGREVLLGPADDYREMGWRLLAPITAYAQ
SQ  QTRGLLGTIVTSLTGRDKNVVTGEVQVLSTATQTFLGTTVGGVIWTVYHGAGSRTLAGAKHPALQMYTNVDQDLVGWPAP
SQ  PGAKSLEPCACGSSDLYLVTRDADVIPARRRGDSTASLLSPRPLACLKGSSGGPVMCPSGHVAGIFRAAVCTRGVAKSLQ
SQ  FIPVETLSTQARSPSFSDNSTPPAVPQSYQVGYLHAPTGSGKSTKVPAAYVAQGYNVLVLNPSVAATLGFGSFMSRAYGI
SQ  DPNIRTGNRTVTTGAKLTYSTYGKFLADGGCSGGAYDVIICDECHAQDATSILGIGTVLDQAETAGVRLTVLATATPPGS
SQ  ITVPHSNIEEVALGSEGEIPFYGKAIPIALLKGGRHLIFCHSKKKCDEIASKLRGMGLNAVAYYRGLDVSVIPTTGDVVV
SQ  CATDALMTGFTGDFDSVIDCNVAVEQYVDFSLDPTFSIETRTAPQDAVSRSQRRGRTGRGRLGTYRYVASGERPSGMFDS
SQ  VVLCECYDAGCSWYDLQPAETTVRLRAYLSTPGLPVCQDHLDFWESVFTGLTHIDAHFLSQTKQQGLNFSYLTAYQATVC
SQ  ARAQAPPPSWDEMWKCLVRLKPTLHGPTPLLYRLGPVQNETCLTHPITKYLMACMSADLEVTTSTWVLLGGVLAALAAYC
SQ  LSVGCVVIVGHIELEGKPALVPDKEVLYQQYDEMEECSQAAPYIEQAQVIAHQFKEKILGLLQRATQQQAVIEPIVTTNW
SQ  QKLEAFWHKHMWNFVSGIQYLAGLSTLPGNPAVASLMAFTASVTSPLTTNQTMFFNILGGWVATHLAGPQSSSAFVVSGL
SQ  AGAAIGGIGLGRVLLDILAGYGAGVSGALVAFKIMGGECPTAEDMVNLLPAILSPGALVVGVICAAILRRHVGPGEGAVQ
SQ  WMNRLIAFASRGNHVSPTHYVPESDAAARVTALLSSLTVTSLLRRLHQWINEDYPSPCSDDWLRTIWDWVCSVLADFKAW
SQ  LSAKIMPALPGLPFISCQKGYKGVWRGDGVMSTRCPCGAAITGHVKNGSMRLAGPRTCANMWHGTFPINEYTTGPSTPCP
SQ  SPNYTRALWRVAANSYVEVRRVGDFHYITGATEDELKCPCQVPAAEFFTEVDGVRLHRYAPPCKPLLRDDITFMVGLHSY
SQ  TIGSQLPCEPEPDVSVLTSMLRDPSHITAETAARRLARGSPPSEASSSASQLSAPSLKATCQTHRPHPDAELVDANLLWR
SQ  QEMGSNITRVESETKVVVLDSFEPLRAETDDVEPSVAAECFKKPPKYPPALPIWARPDYNPPLLDRWKAPDYVPPTVHGC
SQ  ALPPRGAPPVPPPRRKRTIQLDGSNVSAALAALAEKSFPSSKPQEENSSSSGVDTQSSTTSKVPPSPGGESDSESCSSMP
SQ  PLEGEPGDPDLSCDSWSTVSDSEEQSVVCCSMSYSWTGALITPCSAEEEKLPISPLSNSLLRHHNLVYSTSSRSASQRQK
SQ  KVTFDRLQVLDDHYKTALKEVKERASRVKARMLTIEEACALVPPHSARSKFGYSAKDVRSLSSRAINQIRSVWEDLLEDT
SQ  TTPIPTTIMAKNEVFCVDPAKGGRKPARLIVYPDLGVRVCEKRALYDVIQKLSIETMGPAYGFQYSPQQRVERLLKMWTS
SQ  KKTPLGFSYDTRCFDSTVTEQDIRVEEEIYQCCNLEPEARKVISSLTERLYCGGPMFNSKGAQCGYRRCRASGVLPTSFG
SQ  NTITCYIKATAAAKAANLRNPDFLVCGDDLVVVAESDGVDEDRAALRAFTEAMTRYSAPPGDAPQATYDLELITSCSSNV
SQ  SVARDDKGRRYYYLTRDATTPLARAAWETARHTPVNSWLGNIIMYAPTIWVRMVMMTHFFSILQSQEILDRPLDFEMYGA
SQ  TYSVTPLDLPAIIERLHGLSAFTLHSYSPVELNRVAGTLRKLGCPPLRAWRHRARAVRAKLIAQGGKAKICGLYLFNWAV
SQ  RTKTNLTPLPAAGQLDLSSWFTVGVGGNDIYHSVSRARTRHLLLCLLLLTVGVGIFLLPAR
//
ID  Q913V3;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  421879;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q913V3;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: P07948; IntAct: EBI-710808; Score: 0.40
DE  Interaction: O88942; IntAct: EBI-10053076; Score: 0.52
DE  Interaction: Q09472; IntAct: EBI-10052962; Score: 0.40
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0051525;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:1990216;
GO  GO:0035066;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQPEGRAWAQPG
SQ  YPWPLYGNEGMGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGVARALAHGVRVVED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNVSGIYHVTNDCSNSSIVYEAADMIMHTPGCVPCVREGNSSRCWV
SQ  ALTPTLAARNASVPTTAIRRHVDLLVGAAAFCSAMYVGDLCGSVFLVSQLFTFSPRRHETIQDCNCSIYPGHVSGHRMAW
SQ  DMMMNWSPTTALVVSQLLRIPQAIVDMVAGAHWGVLAGLAYYSMVGNWAKVLIVMLLFAGVDGETRVTGGQIARNAYSLT
SQ  TLFSSGSAQNIQLINTNGSWHINRTALNCNDSLNTGFLAALFYTHKFNASGCPERLASCRPIDKFDQGWGPITYAEQGGQ
SQ  DQRPYCWHYAPKPCGIVSASKVCGPVYCFTPSPVVVGTTDRFGVPTYSWGENETDVLLLNNTRPPQGNWFGCTWMNGTGF
SQ  TKTCGGPPCNIGGGGNNTLTCPTDCFRKHPAATYTKCGSGPWLTPRCLVDYPYRLWHYPCTANFTIFKVRMYVGGVEHRL
SQ  DAACNWTRGERCNLEDRDRLELSPLLLSTTEWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGIGSAVVSFAIKWDYIV
SQ  ILFLLLADARVCACLWMMLLIAQAEAALENLVVLNAASVAGAHGILSFLVFFCAAWYIKGKLVPGAAYAFYGVWPLLLLL
SQ  LALPPRAYAMEREMAASCGGAVFVGLVLLTLSPYYKEFLARLIWWLQYFITRAEAHLQVWIPPLNIRGGRDAIILLACVV
SQ  HPELIFDITKLLLAILGPLMVLQASITQVPYFVRAQGLIRACMLVRKVAGGHYVQMAFVKLTALTGTYVYDHLTPLRDWA
SQ  HAGLRDLAVAVEPVVFSDMETKVITWGADTAACGDIILGLPVSARRGREILLGPADSLEGQGWRLLAPITAYSQQTRGLL
SQ  GCIITSLTGRDKNQVEGEVQVVSTATQSFLATCVNGACWTVFHGAGSKTLAGPKGPITQMYTNVDLDLVGWQAPPGSRSL
SQ  TPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSRHAVGIFRAAVCTRGVAKAVDFIPVES
SQ  METTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRT
SQ  GVRAITTGAPITYSTYGKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHP
SQ  NIEEVALSNAGEIPFYGKAIPIEVIKGGRHLIFCHSKKKYDELAAKLSALGLNAVAYYRGLDVSVIPTNGDVVVVATDAL
SQ  MTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVARSQRRGRTGRGRRGIYRFVTPGERPSGMFDSSVLCEC
SQ  YDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVSTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAP
SQ  PPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPMTKFIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSV
SQ  VIVGRIILSGRPAVIPDREVLYREFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRALETF
SQ  WAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLSTQNTLLFNIWGGWVAAQLAPPSAASAFVGAGIAGAAVG
SQ  SIGLGKVLVDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI
SQ  AFASRGNHVSPAHYVPESDAAARVTQILSGLTITQLLKRLHHWINEDCSTPCSGSWLRDVWDWICTVLTDFKTWLQSKLL
SQ  PRLPGVPFFSCQRGYKGVWRGDGIMQTTCPCGAQITGHVKNGSMRIVGPKTCSSTWHGTFPINAYTTGPCAPSPAPNYSR
SQ  ALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPACKPLLREEVTFQVGLNQYLVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHDSPDVDLIEANLLWRQEMGGN
SQ  ITRVESENKVVILDSFDPLRAEEDEREPSVAAEILRKTKRFPPAMPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPPTK
SQ  APPIPPPRRKRTVVLTESTVSSALAELATKTFGSSGSSAVDSGTATAPPDQASDDGDQGSDVESYSSMPPLEGEPGDPDL
SQ  SDGSWSTVSEEAGEDVICCSMSYTWTGALITPCAAEESKLPINPLSNSLLRHHNMVYATTSRSAGLRQKKVTFDRLQVLD
SQ  DHYRDVLKEMKAKASTVKAKLLSIEEACKLTPPHSARSKFGYGAKDVRNLSSKAVNHIRSVWKDLLEDTETPIDTTVMAK
SQ  SEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPGQRVEFLVNAWKSKKCPMGFSYDT
SQ  RCFDSTVTESDIRVEESIYQCCDLAPEARQAIKSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKASA
SQ  ACRAAKLRDCTMLVNGDDLVVICESAGTQEDEANLRVFTEAMTRYSAPPGDPPRPEYDLELITSCSSNVSVAHDASGKRV
SQ  YYLTRDPSTPLARAAWETARHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQ
SQ  IIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRAKLLSQGGRAATCGKYLFNWAVRTKLKLTPIPA
SQ  ASQLDLSSWFVAGYSGGDIYHSLSRARPRWFMLCLLLLSVGVGIYLLPNR
//
ID  O91936;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356390;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: O91936;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQPTGRSWGQPG
SQ  YPWPLYANEGLGWAGWLLSPRGSRPNWGPNDPRRKSRNLGKVIDTLTCGFADLMGYIPLVGGPVGGVARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFILALLSCLTVPTSAVPYRNASGVYHVTNDCPNSSIVYEAEDLILHAPGCVPCVRQGNVSRCWV
SQ  QITPTLSAPSLGAVTAPLRRAVDYLAGGAALCSALYVGDACGAVFLVGQMFTYSPRRHNVVQDCNCSIYSGHITGHRMAW
SQ  DMMMNWSPTTALVMAQLLRIPQVVIDIIAGAHWGVLFAAAYYASAANWAKVVLVLFLFAGVDANTRTVGGSAAQGARGLA
SQ  SLFTPGPQQNLQLINTNGSWHINRTALNCNDSLQTGFVAGLLYYHKFNSTGCPQRMASCRPLAAFDQGWGTISYAAVSGP
SQ  SDDKPYCWHYPPRPCGIVPARGVCGPVYCFTPSPVVVGTTDRKGNPTYSWGENETDIFLLNNTRPPTGNWFGCTWMNSTG
SQ  FVKTCGAPPCNLGPTGNNSLKCPTDCFRKHPDATYTKCGSGPWLTPRCLVHYPYRLWHYPCTLNYTIFKVRMYIGGLEHR
SQ  LEVACNWTRGERCDLEDRDRAELSPLLHTTTQWAILPCSFTPTPALSTGLIHLHQNIVDTQYLYGLSSSIVSWAVKWEYI
SQ  VLAFLLLADARICTCLWIMLLVCQAEAALENVIVLNAAAAAGTHGFFWGLLVICFAWHFKGRLVPGATYLCLGIWPLLLL
SQ  LFLLPQRALALDSSDGGTVGCLVLTILTIFTLTPGYKKMVVLVIWWLQYFIARVEAFIHVWVPPLQVRGGRDAIIMLTCL
SQ  FHPALGFEVTKILLGILGPLYLLQYSLIKLPYFIRARALLRACLLAKHLACGRYVQAALLHLGRLTGTYIYDHLAPMKDW
SQ  AASGLRDLAVATEPIIFSPMETKVITWGADTAACGDILAGLPVSARRGHEIFLGPADDIREAGWRLLAPITAYAQQTRGV
SQ  LGAIIVSLTGRDKNEAEGEVQVLSTATQTFLGTCINGVMWTVFHGAGAKTLAGPKGPVVQMYTNVDKDLVGWPTPPGTRS
SQ  LTPCTCGSADLYLVTRHADVVPARRRGDTRASLLSPRPISYLKGSSGGPVMCPSGHVVGVFRAAVCTRGVAKALDFIPVE
SQ  NLETTMRSPVFTDNSTPPAVPHEFQVGHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSRAYGVDPNIR
SQ  TGVRTVTTGAAITYSTYGKFLADGGCSGGAYDVIICDECHSQDATTILGIGTVLDQAETAGARLVVLATATPPGSVTTPH
SQ  PNIEEVALPSEGEIPFYGRAIPLALIKGGRHLIFCHSKKKCDELAKQLTSQGVNAVAYYRGLDVAVIPATGDVVVCSTDA
SQ  LMTGFTGDFDSVIDCNTTVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRHGIYRYVSSGERPSGIFDSVVLCE
SQ  CYDAGCAWYDLTPAETTVRLRAYLNTPGLPVCQDHLEFWEGVFTGLTNIDAHMLSQTKQGGENFPYLVAYQATVCVRAKA
SQ  PPPSWDTMWKCMLRLKPTLTGPTPLLYRLGAVQNEITLTHPITKYIMACMSADLEVITSTWVLVGGVVAALAAYCLTVGS
SQ  VAIVGRIILSGRPAIIPDREVLYQQFDEMEECSASLPYMDEARAIAEQFKEKVLGLIGTAGQKAETLKPAATSMWNRAEQ
SQ  FWAKHMWNFVSGIQYLAGLSTLPGNPAVATLMSFTAAVTSPLTTQQTLLFNILGGWVASQIAPPTAATAFVVSGMAGAAV
SQ  GSIGLGRVLIDILAGYGAGVAGALVAFKIMCGEKPTAEDLVNLLPSILCPGALVVGVICAAVLRRHIGPGEGAVQWMNRL
SQ  IAFASRGNHVSPTHYVPETDASAKVTQLLSSLTVTSLLKRLHTWIGEDYSTPCDGTWLRAIWDWVCTALTDFKAWLQAKL
SQ  LPQLPGVPFLSCQRGYRGVWRGDGVNSTKCPCGATISGHVKNGTMRIVGPKLCSNTWHGTFPINATTTGPSVPAPAPNYK
SQ  FALWRVGAADYAEVRRVGDYHYITGVTQDNLKCPCQVPSPEFFTELDGVRIHRYAPPCNPLLREEVCFSVGLHSFVVGSQ
SQ  LPCEPEPDVTVLTSMLSDPAHITAETAKRRLDRGSPPSLASSSASQLSAPSLKATCTTQGHHPDADLIEANLLWRQCMGG
SQ  NITRVEAENKVVILDSFEPLKADDDDREISVSADCFRRGPAFPPALPIWARPGYDPPLLETWKQPDYDPPQVSGCPLPPA
SQ  GLPPVPPPRRKRKPVVLSDSNVSQVLADLAHARFKADTQSIEGQDSAVGTSSQPDSGPEEKRDDDSDAASYSSMPPLEGE
SQ  PGDPDLSSGSWSTVSDEDSVVCCSMSYSWTGALITPCSAEEEKLPINPLSNTLLRHHNLVYSTSSRSAGQRQKKVTFDRL
SQ  QVLDDHYREVVDEMKRLASKVKARLLPLEEACGLTPPHSARSKYGYGAKEVRSLDKKALNHIKGVWQDLLDDSDTPLPTT
SQ  IMAKNEVFAVEPSKGGKKPARLIVYPDLGVRVCEKRALYDIAQKLPTALMGPSYGFQYSPAQRVEFLLKTWRSKKTPMAF
SQ  SYDTRCFDSTVTEHDIMTEESIYQSCDLQPEARAAIRSLTQRLYCGGPMYNSKGQQCGYRRCRASGVFTTSMGNTMTCYI
SQ  KALASCRAAKLRDCTLLVCGDDLVAICESQGTHEDEASLRAFTEAMTRYSAPPGDPPVPAYDLELVTSCSSNVSVAHDAS
SQ  GNRVYYLTRDPQVPLARAAWETAKHSPVNSWLGNIIMYAPTLWARIVLMTHFFSVLQSQEQLEKALAFEMYGSVYSVTPL
SQ  DLPAIIQRLHGLSAFTLHSYSPSEINRVSSCLRKLGVPPLRAWRHRARAVRAKLIAQGGKAAICGIYLFNWAVKTKRKLT
SQ  PLADADRLDLSSWFTVGAGGGDIYHSMSRARPRCILLCLLLLTVGVGIFLLPAR
//
ID  O92529;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356421;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: O92529;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTLPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARPSQGRTWGQPG
SQ  YPWPLYGNEGCGWAGWLMSPRGSRPSWGPNDPRRRSRNLGKVIDTLTCGLADLMGYIPVVGGPLGGVAAALAHGVRAIED
SQ  GINYATGNLPGCSFSIFILALLSCLTTPASALTYGNSSGLYHLTNDCPRSSIVLEAEAMILHLAGCVPCVRAGNISRCWH
SQ  PVSPTLAVPNASVPASGFRKHVDLLAGAAVVCSSMYIGDLCGAVFLAGQLATFSPRIHDITQDCNCSVYTGHVTGHRMAW
SQ  DMMMNWSPTTTLVLSSILRVPEIVLEVFAGGHWGVLIAIAYFGMSGNWLKVIAVLFLFAGVEATTTVGRAAGRSAYLFTS
SQ  IFSSGPNQKIQLINTNGSWHINRTALNCIDSLQTGFLSALFYRSNFNSTGCSERLGACKPLEHFQQGWGPITHKSNITGP
SQ  SEDRPYCWHYAPRECSVVPASSVCGPVYCFTPSPVVVGTTDRLGNPTYNWGENETDVFMLESLRPPQGGWFGCTWMNSTG
SQ  FTKTCGAPPCQLIPGDYNSSSNQLLCPTDCFRKHPEATYQKCGSGPWLTPRCLVDYPYRLWHYPCTVNYTIHKVRMFIGG
SQ  VEHRFDAACNWTRGDRCDLYDRDRIEMSPLLFSTTQLAILPCSFTTMPALSTGLIHLHQNIVDVQYLYGVSSSIVSWAVK
SQ  WEYVVLMFLVLADARICTCLWLMLLVGKVEAALERLVVLNAASAAGTAGWCWTLIFLCCVWHVKGRLVPACTYTALGMWP
SQ  ILLVILALPQRAYAWDNSQAASLGVVALLVLTIFTLSPMYKQLLTHAIWWNQYMLARAEAMIHDWVPDLRVRGGRDAIIL
SQ  LTCLLHPHLGFEVTKILLAILAPLYILQHSLLKVPYFVRAHILLRACMFFRKVAAGKYVQACLLRLGAWTGTYIYDHLAP
SQ  LSEWASDGLRDLAVAVEPVIFSPMEKKIITWGADTAACGDILRGLPVSARLGDLVLLGPADDMRHGGWKLLAPITAYAQQ
SQ  TRGLVGTIVTSLTGRDKNEAEGEVQVVSTATQSFLATTINGVLWTVYHGAGSKNLAGPKGPVCQMYTNVDQDLVGWPAPL
SQ  GARSLAPCTCGSSDLYLVTRGADVIPARRRGDTRAALLSPRPISTLKGSSGGPLMCPSGHVVGLFRAAVCTRGVAKALDF
SQ  IPVENMDTTMRSPVFTDNSSPPAVPQTYQVGYLHAPTGSGKSTRVPAAYATQGYKVLVLNPSVAATLSFGAYMSKAHGID
SQ  PNIRTGVRTITTGGPVTYSTYGKFLADGGCSGGAYDIIICDECHSTDPTTVLGIGTVLDQAETAGVRLTVLATATPPGSV
SQ  TVPHPNITETALPTTGEIPFYGKCIPLEFIKGGRHLIFCHSKKKCDELSKQLTSLGLNAVAFYRGVDVAVIPTSGDVVVC
SQ  ATDALMTGYTGDFDSVIDCNVAVTQVVDFSLDPTFSIETTTVPQDAVSRSQRRGRTGRGKPGVYRFVSQGERPSGMFDSV
SQ  VLCEAYDTGCAWYELTPAETTVRLRAYLNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQGGENFAYLVAYQATVCA
SQ  RAKAPPPSWDVMWKCLTRLKPTLTGPTPLLYRLGAVQNEIVTTHPITKYIMTCMSADLEVITSTWVIVGGVLAALAAYCL
SQ  TVGCVVICGRIVTSGKPAVVPDREVLYQQFDEMEECSKHIPYLVEGQQIAEQFKQKVLGLLQAGTKHAEELKPAIHSTWP
SQ  RVEEFWRKHMWNFVSGIQYLAGLSTLPGSPAVASLMSFTASLTSPLRTSQTLLLNILGGWIASQVAPPSASTAFVVSGLA
SQ  GATVASIGLGRVIVDILAGYGAGVAGALVAFKIMSGECPSTEDMVNLLPALLSPGALVVGVVCAAILRRHVGPSEGANQW
SQ  MNRLIAFASRGNHVSPTHYVPETDASNKVTQILSSLTITSLLRRLHQWIHEDTSTPCASSWLRDVWDWVCTVLSDFKTWL
SQ  KAKITPRIPGIPFISCQAGYRGVWAGDGVCHTTCSCGAQIAGHVKNGSMKITGPRMCSNTWHGTFPINATTTSPSVPVPA
SQ  PNYKRALWRVSAEEYVEVERHGDRHYVVGVTADGLKCPCQVPGPEFFTEVDGVRIHRYAPPCKPLLRDEVSFSVGLLEFV
SQ  VGSQLPCEPEPDVTVVTSMLTDPSHITAETASRRLKRGSPPSLASSSASQLSAPSLKATCTANGDHPDAELIEANLLWRQ
SQ  EMGSNITRVESETKVVILDSFDPLVAEYDDREISVSAECHRPPRPKFPPALPIWARPDYNPPLLQKWQMPGYEPPVVSGC
SQ  ALPPAKPTPIPPPRRKRLIQLDESAVSQALQQLADKVFVEDTSTSEPSSGLGGSIAGPSSPDPTTADDTCSDAGSFSSMP
SQ  PLEGEPGDPDLSTGSWSTVSEEDDVVCCSMSYTWTGALITPCAAEEEKLPINPLSNSLIRHHNMVYSTTSRSAGLRQKKV
SQ  TFDRLQVVDQHYQDVLKEIKLRASTVHARLLSTEEACSLTPPHSARSRYGYGARDVRSHTSKAVKHIDSVWEDLLEDNAT
SQ  PIPTTIMAKNEVFCVDPSKGGRKPARLIVYPDLSVRVCEKMALYDVTQKLPKTVMGSAYGFQYSPSQRVEYLLKMWRSKK
SQ  TPMGFSYDTRCFDSTVTERDIRTEEDIYQSCQLDPTARKAISSLTERLYCGGPMFNSKGESCGYRRCRASGVLTTSLGNT
SQ  LTCYLKAQAACRAANIKNFDMLVCGDDLVVICESAGVQEDVVALRAFTDAMIRYSAPPGDAPQPTYDLELITSCSSNVSV
SQ  AHDGTGQRYYYLTRDCTTPLARAAWETARHTPVNSWLGNIIMYAPTIWVRMVLMTHFFSILQCQEQLEAALNFDMYGVTY
SQ  SVTPLDLPAIIQRLHGMAAFSLHGYSPTELNRVGASLRKLGAPPLRAWRHRARAVRAKLIAQGGKAAICGKYLFNWAVKT
SQ  KLKLTPLAAASQLDLSGWFVAGYDGGDIYHSVSRARPRLLLLGLLLLTVGVGIFLLPAR
//
ID  Q81487;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  357355;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q81487;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTLPKPKRQTKRNTLRRPKNVKFPAGGQIVGEVYVLPRRGPQLGVREVRKTSERSQPRGRRQPTPKARPREGRSWAQPG
SQ  YPWPLYGNEGCGWAGWLLPPRGSRPSWGQNDPRRRSRNLGKVIDTLTCGFADLMGYIPLIGAPVGGVARALAHGVRALED
SQ  GVNYATGNLPGCSFSIFLLALFSCLTCPASSLEYRNASGLYLLTNDCSNRSIVYEADDVILHLPGCVPCVETDNNNTSCW
SQ  TPISPTVAVKHPGVTTASIRNHVNMLVAPPTLCSALYVEDAFGAVSLVGQAFTFRPRQHKTVQTCNCSIYPGHVSGHRMA
SQ  WDMMMNWSPAIGLVISHLMRLPQTFFDLVVGAHWGVMAGLAYFSMQGNWAKVVIVLIMFSGVDATTHTTGGSAAQATAGF
SQ  TSFFTRGPSQNLQLVNSNGSWHINSTALNCNDSLNTGFIAGLFYYHKFNSSGCPERMSSCKPITYFNQGWGPLTDANING
SQ  PSEDRPYCWHYPPRPCNITKPLNVCGPVYCFTPSPVVVGTTDIKGLPTYRFGVNESDVFLLTSLRPPQGRWFGCVWMNST
SQ  GFVKTCGAPPCNIYGGMKDIEANQTHLKCPTDCFRKHHDATFTRCGSGPWLTPRCLVDYPYRLWHYPCTVNFSIFKVRMF
SQ  VGGHEHRFSAACNWTRGERCDLEDRDRSEQQPLLHSTTDSLILPCSFTPMRRLSTGLIHLHQNIVDVQYLYGVGSAVVGW
SQ  ALKWEFVVLVFLLLADARVCVALWMMLLISQAEAAMENLVMLNALSAAGQQGYVWYLVAFCAAWHIRGKLVPLITYGLTG
SQ  LWPLALLDLLLPQRAYAWTGEDDATIGAGVLLLLGFFTLSPWYKHWIGRLIWWNQYAICRGEAALQVWVPPLLVRGSRDS
SQ  VILLASLLYPSLIFDITKLLIAVLGPLYLIQAALTSTPYFVRAHVLIRICMLVRSAMGGKYVQMAVLTVGRWFNTYLYDH
SQ  LSPIQDWAAEGLKGLAVATEPVIFSPMEIKVITWGADTAACGDILCGLPVSARLGRELLLGPADDYKKMGWRLLSPISAY
SQ  AQQTRGLFGTIVTSLTGRDKNVVTGEVQVLSTATQTFLGTTVGGVMWTVYHGAGSRTLAGNKRPALQMYTNVDQDLVGWP
SQ  APAGTKSLDPCTCGSSDLYLVTREADVLPARRRGDSTASLLSTRPLSCLKGSSGGPVMCPSGHVVGIFRAAVCTRGVAKA
SQ  LQFIPVETLSTQVRSPSFSDNSTPPAVPESYQVGYLHAPTGSGKSTKVPAAYVAQGYSVLVLNPSVAATLGFGTYMSKAY
SQ  GIDPNIRTGTRTITTGAKLTYSTYGKFLADGGCSGGAYDVIICDECHAQDATSILGIGTVLDQAETAGVRLTVLATATPP
SQ  GSITVPHPNIEEVGLTSDGEIPFYGKALPLAMIKGGRHLVFCHSKEKCDELASKLRGMGVNAVAFYRGLDVSVIPVSGDV
SQ  VVCATDALMTGYTGDFDTVIDCNVAVEQYVDFSLDPTFSIETRTVPQDAVSRSQRRGRTGRGRPGIYRFVTPGERPSGMF
SQ  DSVVLCECYDAGCSWYDLQPAETTVRLRAYLSTPGLPVCQDHLDFWERVFTGLTHIDAHFLSQAKQQGLNFAYLVAYQAT
SQ  VCARAKASPPCWDEMWKCLIRLKPTLQGPTPLLYRLGAIQNDICMTHPITKYIMACMSADLEVTTSAWVLVGGVLAALAA
SQ  YCLSVGCVVIVGHIELGGKPALVPDRQVLYQQYDEMEECSQSAPYIEQAQAIAQQFKDKVLGLLQRASQQEAEIRPIVQS
SQ  QWQKAEAFWQQHMWNFVSGIQYLAGLSTLPGNPAVASLMAFTASVTSPLTTNQTMFFNILGGWVATHLAGPAASSAFVVS
SQ  GLAGAAVGGIGIGRVLLDVLAGYGAGVSGALVAFKIMGGELPTTEDMVNLLPAILSPGALVVGVICAAVLRRHVGPGEGA
SQ  VQWMNRLIAFASRGNHVSPTHYVPESDAAAKVTALLSSLTVTRLLRRLHQWINEDYPSPCNGDWLHDIWDWVCIVLSDFK
SQ  TWLSAKIMPKVPGIPFLSCQKGYKGVWRGDGVMTTRCPCGEDFTGHVRNGSMRIAGSGLCANMWHGTFPINEYTTGPSTP
SQ  VPAHNYSRALWRVTSDSYVEVRRVGDTHYVVGATNDGLKIPCQVPAPEFFTELDGVRLHRYAPPCKPLLRDEITFSVGLH
SQ  SYANGSQLSCEPEPDVAVLTSMLRDPAHITAATAARRLARGSPPSEASSSASQLSAPSLKATCQTHRPHPDAELIDANLL
SQ  WRQEMGSNITRVESETKVVILDSFEPLRAEEDDTELSIPAECFKKPPKYPPALPIWARPDYNPPLLPSWKDPTYEPPAVH
SQ  GCALPPTRPAPVPPPRRKRTIKLDGSNVSAALLALAERSFPSTKPEGTGTSSSGVGTESTAESGDSPETGEESDVESYSS
SQ  MPPLEGEPGDPDLDADSWSTVSDSEEQSVVCCSMSYSWTGAIITPCSAEEEKLPISPLSNSLLRHHNLVYSTSSRSAAAR
SQ  QKKVTFDRLQVLDDHYKNVLKEVKERASGVKGRLLSFEEACSLVPPHSGRSKYGYSAKDVRSLSSKAMNQIRSVWEDLLE
SQ  DNSTPIPTTIMAKNEVFSVNPAKGGRKPARLIVYPDLGVRVCEKRALYDVIQKLSIATMGPAYGFQYSPKQRVEHLLKMW
SQ  TSKKTPLGFSYDTRCFDSTVTEHDIRTEEGIYQCCDLEPEARKAISALTERLYIGGPMYNSKGLQCGYRRCRASGVLPTS
SQ  FGNTITCYIKATAASRAAGLKNPSFLVCGDDLVVISESCGVEEDRTALRAFTEAMTRYSAPPGDAPQPTYDLELISSCSS
SQ  NVSVACDGAGKRYYYLTRDPETPLARAAWETARHTPVNSWLGNIIMFAPTIWVRMVLITHFFSILQAQEQLERALDFEMY
SQ  GATYSVTPLDLPAIIERLHGLSAFSLHGYSPTELNRVAGALRKLGIPPLRAWRHRARAVRAKLIAQGGKARICGLYLFNW
SQ  AVRTKTKLTPLPTAGQLDLSSWFTVGVGGNDIYHSVSRARTRHLLLCLLLLTVGVGIFLLPAR
//
ID  P29846;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  31645;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: P29846;
DR  UNIPROT: A7YCU9;
DR  PDB: 1N64;
DR  PDB: 2ZJO;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (PubMed:12208879). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF- induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:12208879, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (PubMed:9557650). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2, ECO:0000269|PubMed:9557650}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
DE  Interaction: O43889; IntAct: EBI-909649; Score: 0.59
DE  Interaction: P29846; IntAct: EBI-9303365; Score: 0.54
DE  Interaction: P61978; IntAct: EBI-8849316; Score: 0.64
DE  Interaction: P36941; IntAct: EBI-9099695; Score: 0.62
DE  Interaction: P08107; IntAct: EBI-9293903; Score: 0.62
DE  Interaction: P11142; IntAct: EBI-9293821; Score: 0.35
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0043433;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNGKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTWERSQPRGRRQPIPKARQPEGRAWAQPG
SQ  YPWPLYGNEGLGWAGWLVSPRGSRPNWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGVARALAHGVRVLED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVHNVSGIYHVTNDCSNSSIVYEAADMIMHTPGCVPCVRENNSSRCWV
SQ  ALTPTLAARNNSVPTATIRRHVDLLVGAAAFCSAMYVGDLCGSVFLVSQLFTFSPRRYETVQDCNCSIYPGHVTGHRMAW
SQ  DMMMNWSPTTALVVSQLLRIPQAVVDMVGGAHWGVLAGLAYYSMVGNWAKVLIVMLLFAGVDGSTIVSGGTVARTTHSLA
SQ  SLFTQGASQKIQLINTNGSWHINRTALNCNDSLQTGFLASLFYAHRFNASGCPERMASCRSIDKFDQGWGPITYTEADIQ
SQ  DQRPYCWHYAPRPCGIVPASQVCGPVYCFTPSPVVVGTTDRFGAPTYSWGENETDVLILNNTRPPQGNWFGCTWMNSTGF
SQ  TKTCGGPPCNIGGGGNNTLVCPTDCFRKHPEATYTKCGSGPWLTPRCMVDYPYRLWHYPCTVNFTIFKVRMYVGGVEHRL
SQ  NAACNWTRGERCDLEDRDRSELSPLLLSTTEWQILPCSFTGLPALSTGLIHLHQNVVDVQYLYGIGSAVVSFAIKWEYIL
SQ  LLFLLLADARVCACLWMMLLIAQAEAALENLVVFNAASVAGMHGTLSFLVFFCAAWYIKGRLVPGAAYALYGVWPLLLLL
SQ  LALPPRAYAMDREMAASCGGAVFVGLVLLTLSPHYKMFLARLIWWLQYFITRAEAHLQVWIPPLNVRGGRDAIILLTCAA
SQ  YPELIFDITKILLAILGPLMVLQAGLTRIPYFVRAQGLIRACMLVRKAAGGHYVQMALMKLAALTGTYVYDHLTPLQDWA
SQ  HTGLRDLAVAVEPVVFSDMETKIITWGADTAACGDIILGLPVSARRGREILLGPADSLEGRGWRLLAPITAYAQQTRGLF
SQ  GCIITSLTGRDKNQVEGEVQVVSTATQSFLATCINGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWHAPQGARSL
SQ  TPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPSGHVVGIFRAAVCTRGVAKAVDFVPVES
SQ  METTMRSPVFTDNSSPPAVPQAFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGVDPNIRT
SQ  GVRTITTGAPITYSTYGKFLADGGCSGGAYDIIMCDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHP
SQ  NIEEIALSNTGEIPFYGKAIPIETIKGGRHLIFCHSKKKCDELAAKLSALGIHAVAYYRGLDVSVIPASGNVVVVATDAL
SQ  MTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTMPQDAVSRSQRRGRTSRGRRGIYRFVTPGERPSGMFDSSVLCEC
SQ  YDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAP
SQ  PPSWDQMWKCLTRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSV
SQ  VIVGRIILSGKPAVVPDREVLYQEFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRTLEAF
SQ  WANDMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQSTLLFNILGGWVAAQLAPPGAASAFVGAGIAGAAVG
SQ  SIGLGKVLVDMVAGYGAGVAGALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVDPGEGAVQWMNRLI
SQ  AFASRGNHVSPTHYVPESDAAARVTQILSGLTITQLLRRLHQWINEDCSTPCSGSWLRDVWDWICTVLADFKTWLQSKLL
SQ  PRLPGVPFFSCQRGYKGVWRGDGIMQTTCPCGAQLTGHVKNGSMRIWGPKTCSNTWHGTFPINAYTTGPCTPSPAPNYSR
SQ  ALWRVAAEEYVEVRRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPACKPLLREEVSFQVGLNQYVVGSQL
SQ  PCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSALSLKAACTTRHTPPDADLIEANLLWRQEMGGN
SQ  ITRVESENKVVILDSFDPLRAEEDEREVSVPAEILRKSRKFPPALPVWARPDYNPPLLEPWKDPDYVPPVVHGCPLPPVK
SQ  APPIPPPRRKRTVVLTESTVSSALAELATKTFGSSESSAAGSGTATAPPDQPSDDGDAGSDVESCSSMPPLEGEPGDPDL
SQ  SDGSWSTVSEEDGEGVICCSMSYTWTGALITPCAAEESKLPINALSNSLLRHHNMVYATTSRSASQRQKKVTIDRLQVLD
SQ  DHYRDVLKEMKAKASTVKAKLLSVEEACKLTPPHSARSKFGYGAKDVRNLSGKAINHIRSVWKDLLEDTETPIDTTIMAK
SQ  NEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPGQRVEFLVNAWKSKKCPMGFSYDT
SQ  RCFDSTVTESDIRVEESIYQCCDLAPEARQAIRSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKASA
SQ  ACRAAKLQDCTMLVCGDDLVVICESAGTQEDAASLRVFTEAMTRYSAPPGDLPQPEYDQELITSCSSNVSVAHDASGKRV
SQ  YYLTRDPTTPLARAAWATARHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQ
SQ  IIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRAWRHRARSVRAKLLSQGGRAATCGRYLFNWAVKTKLKLTPIPA
SQ  ASQLDLSKWFVAGYGGGDIYHSLSRARPRWFMLCLLLLSVGVGIYLLPNR
//
ID  Q9QAX1;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356414;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: Q9QAX1;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKDRRSAGKSWGRPG
SQ  YPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRHRSRNLGKVIDTLTCGFADLMGYIPVVGAPVGGVARALAHGVRVLED
SQ  GINYATGNLPGCSFSIFLLALLSCMSVPVSAVEVKNTSQIYMATNDCSNNSITWQLEGAVLHVPGCVPCESTGNISRCWI
SQ  PVTPNVAVRERGALTKGLRTHIDLIVVSATFCSALYIGDVCGAIMIAAQATIISPQHHTFVQDCNCSIYPGHVTGHRMAW
SQ  DMMMNWSPATTMIMAYFMRVPEVVLDIITGAHWGVMFGLAYFSMQGAWAKVVVILLLTAGVDAQTHTISGHAARTTHGLV
SQ  SLFTPGSQQNIQLVNTNGSWHINRTALNCNDSLKTGFIAALFYSHKFNSSGCPQRMSSCRSIEEFRIGWGNLEYEENVTN
SQ  DDNMRPYCWHYPPRPCGIVPAQTVCGPVYCFTPSPVVVGTTDRRGVPTYTWGENDTDVFLLNSTRPPRGAWFGCTWMNST
SQ  GFTKTCGAPPCRIRPDFNSSEDLLCPTDCFRKHSEATYTRCGAGPWLTPKCLFHYPYRLWHYPCTINFTIHKIRMFIGGV
SQ  EHRLEAACNFTRGDRCNLEDRDRSQLSPLLHSTTEWAILPCTFSDMPALSTGLLHLHQNIVDVQYLYGLSPAITKYIVKW
SQ  EWVVLLFLLLADARVCACLWMLLLLGQAEAALEKLVILHAASAASSHGMLCFIIFFIAAWYIKGRVTPLVTYSYLGMWSF
SQ  SLLLLALPQQAYALDTTEQGQIGLVLLVVISVFTLSPAYKILLCRSLWWLSYLLVRAEALIQDWVPPWQARGGRDGIIWA
SQ  ATIFCPGVLFDITNWLLAILGPGYLLRSVLTSTPYFVRAQALLRICAAVRHLSGGKYVQMMLLTLGKWTGTYIYDHLSPM
SQ  SGWAASGLRDLAVAVEPIVFSPMEKKVIVWGAETAACGDILHGLPVSARLGQEVLLGPADEYTSKGWKLLAPITAYAQQT
SQ  RGLLGTIVVSMTGRDKTEQAGEIQVLSTVTQSFLGTTISGILWTVFHGAGNKTLAGSRGPVTQMYSSAEGDLVGWPSPPG
SQ  TRSLDPCTCGAVDLYLVTRNADVIPARRQGDRRGALLSPRPLSSLKGSSGGPVLCPRGHAVGIFRAAICTRGAAKSIDFI
SQ  PIESLDVIIRSPNFTDNSSPPAVPQTYQVGYLHAPTGSGKSTKVPASYAAQGYKVLVLNPSVAATLGFGAYMSKAHGINP
SQ  NIRTGVRTVTTGESITYSTYGKFLADGGCSGGAYDVIICDECHSVDATTILGIGTVLDQAETAGARLTVLATATPPGSVT
SQ  TPHPNIEEVALGHEGEIPFYGKAIPLSQIKGGRHLIFCHSKKKCDELAAALRGMGLNAVAYYRGLDVSVIPTQGDVVVVA
SQ  TDALMTGFTGDFDSVVDCNVAVTQTVDFSLDPTFTVTTQTVPQDAVSRSQRRGRTGRGRLGIYRYVSSGERASGMFDSVV
SQ  LCECYDAGAAWYELTPAETTVRLRAYFNTPGLPVCQDHLEFWEAVFTGLTHIDAHFLSQTKQAGENFPYLVAYQATVCAR
SQ  AKAPPPSWDVMWKCLIRLKPTLTGPTPLLYRLGPVTNETTLTHPVTKYIATCMQADLEIMTSTWVLAGGVLAAIAAYCLA
SQ  TGCVVCIGRVNINQKTIVAPDKEVLYEAFDEMEECASRALLLEEGQRIAEMLKSKIQGLLQQATKQAQDIQPAVQATWPK
SQ  LEQFWAKHMWNFISGIQYLAGLSTLPGNPAVAAMMAFSAALTSPLPTSTTILLNIMGGWLASQIAPAAGATGFVVSGLVG
SQ  AAVGSIGLGKILVDVLAGYGAGISGALVAFKIMSGEKPSVEDVVNLLPGILSPGALVVGVICAAILRRHVGQGEGAVQWM
SQ  NRLIAFASRGNHVAPTHYVAESDASQRVTQLLGSLTITSLLRRLHTWITEDCPVPCAGSWLRDIWDWACTILTDFKNWLS
SQ  TKLLPKMPGLPFISCQRGHKGAWTGTGIMTTRCPCGAVVSGNVRHGSMRITGPKTCMNTWQGTFPINCYTEGQCAPQPTH
SQ  NYKTAIWKVAAAEYAEVTRHGSYAYVTGLTNDNLKVPCQLPAPEFFSWVDGVQIHRFAPTPKPFIRDEVSFTVGLNSFVV
SQ  GSQLPCEPEPDTEVLASMLTDPSHITAEAAARRLARGSPPSEASSSASQLSAPSLRATCTAHAKNYAVEMVDANFFMGSD
SQ  VTRIESETKVLILDSLDPSVEEEDEREPSVPSEYLLPKKKFPQALPVWARPDYNPPVVETWKRPDYDPPTVSGCALPPRV
SQ  TAPTPPPRRRRALVLSQSNVGEALQALAIKSFGQLPPSCDSGRSTGMDTTDATDQPALKESTDSEAGSDSSMPPLEGEPG
SQ  DPDLESGSVEYHPSSQEGEAAPDLDSGSWSTCSEEGGSEVCCSMSYSWTGALITPCGPEEEKLPINPLSNSLLRYHNKVY
SQ  STTSRSASQRAKKVTFDRVQLLDSHYDQVLKDIKLAASKVSANLLSIEEACALTPPHSARSKYGFGAKEVRSLSRKAVDH
SQ  IKSVWKDLLEDQQTPIPTTIMAKNEVFCIDPTKGGKKAARLIVFPDLGVRVCEKMALYDITQKLPQAVMGASYGFQYSPA
SQ  QRVDFLLRAWKEKKDPMGFSYDTRCFDSTVTERDIRTEESIYLACSLPEEARVAIHSLTERLYVGGPMMNSKGQSCGYRR
SQ  CRASGVLTTSMGNTITCYVKALAACKAAGIVAPTMLVCGDDLVVISESQGAEEDERNLRVFTEAMTRYSAPPGDPPKPEY
SQ  DLELITSCSSNVSVALDQHGRRMYYLTRDPSTPLARAAWETARHSPVNSWLGNIIQYAPTIWVRMVLMTHFFSVLMAQET
SQ  LDQDLNFEMYGAVYSVNPLDLPAIIERLHGLEAFSLHGYSPTELTRVAAALRKLGAPPLRAWKSRARAVRASLISQGGRA
SQ  ATCGFYLFNWAVRTKRKLTPLPAARRLDLSGWFTVGAGGGDIYHSVSRARPRFLLLCLLLLSVGVGIFLLPAR
//
ID  O92530;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356422;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: O92530;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTLPKPQKRNQRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRQTGRTWAQPG
SQ  YPWPLYGNEGCGWMGWLLSPRGSRPHWGPNDPRRRSRNLGKVIDTLTCGFADLMGYIPVVGAPLGGVAAALAHGVRAVED
SQ  GINYATGNLPGCSFSIFLLALLSCLTTPASAVHYANKSGIYHLTNDCPNSSIVYEAEDFIMHLPGCVPCIKSGNGSSCWL
SQ  PATLTIAVPNASIPVRGFRRHVDLMVGAAAFCSAMYVGDLCGGIFLVGQLFSFNPRRHWVVQDCNCSIYVGHITGHRMAW
SQ  DMMMNWSPTATLVLSYVMRIPQVIMDIFTGGHWGILAGILYYSMVANWAKVLCILFLFAGVDATTRTTGAQAARATLGFT
SQ  GLFQTGAKQNIHLINTNGSWHINRTALNCNDSLNTGFMAALFYLHKFNSTGCPERLSACKSITQFAQGWGPVTYANVSGS
SQ  SEDRPYCWHYAPRPCGVVSARSVCGPVYCFTPSPVVVGTTDRRGVPTYTWGENESDVFLLESLRPPAGAWYGCTWMNSTG
SQ  YTKTCGAPPCHIGPPDQFCPTDCFRKHPEATYRKCGSGPWLTPRCLVDYPYRLWHYPCTVNYTIHKVRLFINGLEHRFDA
SQ  ACNWTRGERCELEDRDRIEMSPLLFSTTELAILPCSFTTMPALSTGLVHLHQNIVDIQYLYGLAPALVSWAVRWEYVVLA
SQ  FLLLADARICACLWMVLLISQVEAALENLIVLNAASAASSQGWIYCLVFICCAWYIKGRVVPGATYAILHLWPLLLLVLA
SQ  LPQRAYAQDREQGASIGVVVIAAITIFTLTPAYKTMLVHFLWWNQYFIARSEALIQQWVPSLRVRGGRDAVILLTCLLHP
SQ  SLGFDITKMLLALLGPLYLLQVSLLRVPYYVRAHALLRVCILVRRVAGGKYIQAALLKLGAWTGTYIYDHLAPLSTWASD
SQ  GLRDLAVAVEPVTFSPMEKKIITWGADTAACGDILAGLPVSARLGHLLFLGPADDMKSMGWRLLAPITAYCQQTRGLLGT
SQ  IVTSLTGRDRNVVEGEIQVLSTATQSFLGTAINGVMWTVYHGAGSKTLAGPKGPVCQMYTNVDQDMVGWPAPPGTRSLTP
SQ  CTCGASDLYLVTRNADVIPARRRGDTRAGLLSPRPLSTLKGSSGGPLMCPSDHVVGLFRAAVCTRGVAKALDFVPVENME
SQ  TTMRSPVFTDNSTPPAVPQTYQVGYLHAPTGSGKSTKVPAAYASQGYKVLVLNPSVAATLGFGSYMSTAHGIDPNIRTGV
SQ  RTITTGGPITYSTYGKFLADGGCSGGAYDIIICDECHSTDPTTVLGIGTVLDQAETAGVRLTVLATATPPGSVTVPHPNI
SQ  TETALPSTGEVPFYGKAIPLECIKGGRHLIFCHSKKKCDELAKQLRTLGLNAVAFYRGVDVSVIPTAGDVVVCATDALMT
SQ  GYTGDFDSVIDCNVAVTQIVDFSLDPTFSIETTTVPQDAVARSQRRGRTGRGKPGVYRYVSQGERPSGMFDTVVLCEAYD
SQ  VGCAWYELTPSETTVRLRAYLNTPGLPVCQDHLEFWEGVFTGMTHIDAHFLSQTKQGGENFAYLVAYQATVCARAKAPPP
SQ  SWDTMWKCLIRLKPMLTGPTPLLYRLGAVQNEIITTHPITKYIMTCMAADLEVITSTWVLAGGIVAALAAYCLTVGSVVI
SQ  CGRIVTSGKPVPLPDREVLYRQFDEMEECSRHIPYLAEGQQIAEQFKQKILGLLQNTAKQAEDLKPAVQSAWPKLEQFWQ
SQ  KHLWNFVSGVQYLAGLSTLPGNPAVASLMSFSAALTSPLSTSTTLLLNILGGWVASQLAPPTASTAFVVSGLAGAAVGSI
SQ  GLGKVIIDILAGYGAGVSGALVAFKIMSGEAPAVEDMVNLLPALLSPGALVVGVVCAAVLRRHVGPSEGATQWMNRLIAF
SQ  ASRGNHVSPTHYVPETDASRAVTTILSSLTITSLLRRLHEWISGDWSAPCSCSWLKDVWDWVCTVLSDFKTWLRAKLVPT
SQ  LPGIPFISCQRGFRGVWRGDGVNYTTCSCGANITGHVKNGSMKIVGPKMCSNVWNNRFPINAITTGPSVPVPEPNYHKAL
SQ  WRVSAEDYVEVVRVNDHHYIVGATADNLKCPCQVPAPEFFTEVDGVRLHRFAPPCRPLMRDDITFSVGLSTYVVGSQLPC
SQ  EPEPDVVILTSMLTDPDHITAETAARRLARGSPPSLASSSASQLSAPSLKATCTTAGKHPDAELIEANLLWRQEVGGNIT
SQ  RVESENKIIVLDSFDPLIAETDDREISVGAECFNPPRPKFPPALPVWARPDYNPPLLQPWKAPDYEPPLVHGCALPPKGL
SQ  PPVPPPRKKRVVQLDEGSAKRALAELAQTSFPPSTATLSEDSGRETSTLSSDMTPPREEADRASDDGSYSSMPPLEGEPG
SQ  DPDLSSGSWSTVSEDHDSVVCCSMSYSWTGALITPCAAEEEKLPISPLSNALIRHHNLVYSTTSRSASLRQKKVTFDRVQ
SQ  VVDQHYYDVLKEIKTKASGVSAKLLSVEEACALTPPHSARSKFGYGAKEVRGLASKAVNHINSVWEDLLEDNSTPIPTTI
SQ  MAKNEVFCVDAQKGGRKPARLIVYPDLGVRVCEKRALYDVTQKLPIAVMGAAYGFQYSPKQRVDYLLKMWRSKKTPMGFS
SQ  YDTRCFDSTVTERDIRTEEDIYQCCQLDPVAKKAITSLTERLYCGGPMYNSRGQSCGYRRCRASGVLTTSLGNTLTCYLK
SQ  AQAACRAAKLKDFDMLVCGDDLVVISESMGVAEDASALRAFTEAMTRYSAPPGDDPQPEYDLELITSCSSNVSVAHDGAG
SQ  QRYYYLTRDPLTPLSRAAWETARHTPVNSWLGNIIMYAPTIWVRMVLMTHFFAILQSQEILHKALDFDMYGVTYSVTPLD
SQ  LPYIIQRLHGMAAFSLHGYSPGELNRVASCLRKLGAPPLRAWRHRARAVRAKLIAQGGKHAICGKYLFNWAVRTKLKLTP
SQ  LRGAANLDLSGWFVSGGSGGDIFHSVSRARPRNLLLCLLLLTVGVGIFLLPAR
//
ID  O92531;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356425;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: O92531;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTLPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQSQGRHWAQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPNWGPNDPRRRSRNLGKVIDTLTCGFADLMGYIPVVGAPLGGVAAALAHGVRAIED
SQ  GINYATGNLPGCSFSIFLLALLSCLTTPASAVHYRNISGIYHLTNDCPNSSIIYEADNIIMHTPGCVPCVKTGNKSQCWV
SQ  PVAPTLAVANASVPIRGFRSHVDLLVGSAAACSALYIGDLCGGVFLVGQLFTFRPRQHTTVQECNCSIYTGHITGHRMAW
SQ  DMMMNWSPTVTFITSSLLRVPQLLLEIALEGHWGVIGALLYYSMVANWAKVFAVLLLFAGVDATTHIGSSASATTNRLTS
SQ  FFSPGSKQNVQLIKTNGSWHINRTALNCNDSLHTGFIAGLLYAHRFNSSGCPERLSSCRPLHAFEQGWGPLTYANISGPS
SQ  NDKPYCWHYPPRPCDIVPARSVCGPVYCFTPSPVVVGTTDRKGLPTYTWGANESDVFLLRSTRPPRGSWFGCTWMNSTGF
SQ  VKTCGAPPCNTRPVGSGNDTLVCPTDCFRKHPEATYARCGSGPWLTPRCLVNYPYRLWHYPCTVNYTIHKVRMFVGGIEH
SQ  RFEAACNWTRGERCELDDRDRVEMSPLLFSTTQLSILPCSFTTMPALSTGLIHLHQNIVDVQYLYGVSSAVVSWAVKWEY
SQ  IVLAFLVLAVARVCACLWLMFLVGQAEAALENLIVLNATSAAGSQGWVWGVVFICAAWYIRGRAAPITTYAILQLWPLLL
SQ  LVLALPRRAYAYNGEEAASLGMLAIVIITIFTLTPAYKTLLISTLWWIQYYIARAEAMLYVWVPSLQVRGGRDAVILLTC
SQ  LLHPQLGFEVTKAILALLGPLYILQYSLLKTPYFVRAHILLRVCMFLRGVAGGKYVQAALLRLGAWTGTYIYDHLTPLSD
SQ  WACDGLRDLAVAVEPVVFSPMEKKVITWGADTVACGDIISGLPVSARRGNLIFLGPADDIRDGGWRLLAPITAYAQQTRG
SQ  LVGTIVTSLTGRDKNEVEGEIQVVSTATQSFLATTVNGVLWTVYHGAGSKTLAGPKGPICQMYTNVDQDLVGWPAPPGAR
SQ  SLTPCTCGSSDLYLVTRNADVIPARRRGDTRAALLSPRPISTLKGSSGGPMLCPSGHVAGIFRAAVCTRGVAKSLDFVPV
SQ  ENMQSTARSPSFSDNTTPPAVPQTYQVGYLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGSYMSTAHGIDPNI
SQ  RTGVRTITTGGAITYSTYGKFLADGGCSGGAYDIIICDECHSTDPTTVLGIGTVLDQAETAGVRLTVLATATPPGSVTVP
SQ  HPNITEVALSSTGEVPFYGKAIPLEYIKGGRHLIFCHSKKKCDELAKQLTSLGLNAVAFYRGVDVSVIPTSGDVVVCATD
SQ  ALMTGYTGDFDSVIDCNVSVTQVVDFSLDPTFTIETTTMPQDAVSRSQRRGRTGRGKHGVYRYVSQGERPSGIFDTVVLC
SQ  EAYDTGCAWYELTPSETTVRLRAYLNTPGLPVCQDHLEFWEGVFTGLTHIDAHLLSQTKQGGENFAYLVAYQATVCARAK
SQ  APPPSWDTMWKCLIRLKPMLTGPTPLLYRLGAVQNEITTTHPITKYIMTCMSADLEVITSTWVLVGGVLAALAAYCLSVG
SQ  CVVVCGRISTTGKPVLIPDREVLYQQFDEMEECSRHIPYLVEGQHLAEQFKQKVLGLIQTTTRQAEEIEPVVHSAWPKLE
SQ  QFWQKHLWNFVSGIQYLAGLSTLPGNPAVASLMSFSASLTSPLSTSTTLLLNILGGWVASQLANPTASTAFVVSGLAGAT
SQ  VGSIGLGRVLVDIIAGYGAGVSGALVAFKIMSGETPSAEDMVNLLPALLSPGALVVGVVCAAILRRHAGPAEGATQWMNR
SQ  LIAFASRGNHVSPTHYVPETDTSRQVMAILSSLTVTSLLRKLHEWINSDWSTPCSGSWLRDIWDWVCTVLSDFKVWLKSK
SQ  LVPALPGVPFLSCQRGFRGVWRGDGICRTTCPCGADIVGHVKNGSMRISGSRWCSNIWHGTFPINATTTGPSVPIPEPNY
SQ  KRALWRVSAEEYVEVARVGDSHFVVGATNQDLKCPCQVPAPEFFTEVDGVRLHRFAPACKPLLRDEISFLVGLNSYAIGS
SQ  QLPCEPEPDVTVVTSMLVDPSHLTAEAAARRLARGSPPSCASSLASQLSAPSLKATCTTHCAHPDADLIEANLLWRQEVG
SQ  GNITRVESENKVIVLDSFDPLVPEYDDREPSVPAECHRPNRPKFPPALPIWARPDYNPPLLETWKKPDYAPPLVHGCALP
SQ  SPVQPPVPPPRRKSVVHLDDSTVATALAELAEKSFPTQPASTPDSDSGHPTTSKSSDQADEGEDTPSEAGSYSSMPPLEG
SQ  EPGDPDLSSGSWSTVSEEGDSVVCCSMSYSWTGALVTPCAAEEEKLPINPLSNSLIRHHNLVYSTTTRSAAMRQKKVTFD
SQ  RLQILDQHYNNVVKEVKLRASGVTAKLLSVEEACSLTPPHSARSKFGYGAKDVRSHTSKAINHINSVWEDLLEDNQTPIP
SQ  TTIMAKNEVFCADVSKGGRKPARLIVYPDLGVRVCEKRALYDVTRKLPTAIMGDAYGFQYSPKQRVDQLLKMWRSKKTPM
SQ  GFSYDTRCFDSTVTEHDIKTERDVYLSCKLDPVARKAIESLTERLYIGGPMYNSRGQLCGTRRCRASGVLTTSLGNTMTC
SQ  FIKAEAACRAAGLTNYDMLVCGDDLVVIAESAGVQEDASNLRAFTEAMTRYSAPPGDEPHPAYDLELITSCSSNVSVAHD
SQ  HTGQRYYYLTRDPTTPLSRAAWETARHTPVNSWLGNIIMYAPAIWVRMVLMTHFFQILQAQEQLDKVLDFDMYGVTYSVS
SQ  PLQLPAIIQRLHGMAAFSLHGYSPTELNRVGACLRKLGAPPLRAWRHRARAVRAKLIAQGGGAAICGKYLFNWAVKTKLK
SQ  LTPIPDAARLDLSGWFISGFSGGDIYHSVSRARPRIFLLCLLLLSVGVGIFLLPAR
//
ID  O92532;
PN  RNA-directed RNA polymerase;
GN  POLG;
OS  356424;
SL  Nucleus Position: SL-0382;
SL  Comments: [Core protein precursor]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein {ECO:0000255}. Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. [Mature core protein]: Virion {ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm {ECO:0000250|UniProtKB:Q99IB8}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E1]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). {ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P27958}. Host cell membrane {ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane domain acts as a signal sequence (By similarity). After cleavage by host signal peptidase, the membrane sequence is retained at the C- terminus of the protein, serving as ER membrane anchor (By similarity). ER retention of p7 is leaky and a small fraction reaches the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P27958}. [Protease NS2]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}. [Serine protease/helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=NS3 is associated to the ER membrane through its binding to NS4A. {ECO:0000305}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Host membrane insertion occurs after processing by the NS3 protease. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N- terminus into the ER lumen occurs post-translationally. {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion {ECO:0000250|UniProtKB:P26662}. Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host nucleus {ECO:0000250|UniProtKB:P26662}. Host lipid droplet {ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs after processing by the NS3 protease (By similarity). Localizes at the surface of lipid droplets (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}. Note=Host membrane insertion occurs after processing by the NS3 protease. {ECO:0000250|UniProtKB:P27958}.
DR  UNIPROT: O92532;
DR  Pfam: PF07652;
DR  Pfam: PF01543;
DR  Pfam: PF01542;
DR  Pfam: PF01539;
DR  Pfam: PF01560;
DR  Pfam: PF01538;
DR  Pfam: PF01006;
DR  Pfam: PF01001;
DR  Pfam: PF01506;
DR  Pfam: PF08300;
DR  Pfam: PF08301;
DR  Pfam: PF12941;
DR  Pfam: PF02907;
DR  Pfam: PF00998;
DR  PROSITE: PS51693;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51822;
DR  PROSITE: PS50507;
DE  Function: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). {ECO:0000250|UniProtKB:P27958}. [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). The interaction between E2 and host amino acid transporter complex formed by SLC3A2 and SLC7A5/LAT1 may facilitate viral entry into host cell (By similarity). {ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}. [Viroporin p7]: Ion channel protein that acts as a viroporin and plays an essential role in the assembly, envelopment and secretion of viral particles (By similarity). Regulates the host cell secretory pathway, which induces the intracellular retention of viral glycoproteins and favors assembly of viral particles (By similarity). Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the cytoplasm of infected cells, leading to a productive viral infection (By similarity). High levels of cytoplasmic Ca(2+) may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (Probable). This ionic imbalance induces the assembly of the inflammasome complex, which triggers the maturation of pro-IL-1beta into IL-1beta through the action of caspase-1 (By similarity). Targets also host mitochondria and induces mitochondrial depolarization (By similarity). In addition of its role as a viroporin, acts as a lipid raft adhesion factor (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000305}. [Protease NS2]: Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3 (By similarity). The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3) (By similarity). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins (By similarity). {ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}. [Serine protease/helicase NS3]: Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B- NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand (By similarity). Binds a single ATP and catalyzes the unzipping of a single base pair of dsRNA (By similarity). Inhibits host antiviral proteins TBK1 and IRF3 thereby preventing the establishment of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state (By similarity). Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and preventing the establishment of an antiviral state (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4A]: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease (By similarity). The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state (By similarity). The NS3/NS4A complex induces host amino acid transporter component SLC3A2, thus contributing to HCV propagation (By similarity). {ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}. [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity). NS4B self-interaction contributes to its function in membranous web formation (By similarity). Promotes host TRIF protein degradation in a CASP8-dependent manner thereby inhibiting host TLR3- mediated interferon signaling (By similarity). Disrupts the interaction between STING and TBK1 contributing to the inhibition of interferon signaling (By similarity). {ECO:0000250|UniProtKB:P27958}. [Non-structural protein 5A]: Phosphorylated protein that is indispensable for viral replication and assembly (By similarity). Both hypo- and hyperphosphorylated states are required for the viral life cycle (By similarity). The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity). Involved in RNA-binding and especially in binding to the viral genome (By similarity). Zinc is essential for RNA-binding (By similarity). Participates in the viral particle production as a result of its interaction with the mature viral core protein (By similarity). Its interaction with host VAPB may target the viral replication complex to vesicles (By similarity). Down- regulates viral IRES translation initiation (By similarity). Mediates interferon resistance, presumably by interacting with and inhibiting host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By similarity). Acts as a transcriptional activator of some host genes important for viral replication when localized in the nucleus (By similarity). Via the interaction with host PACSIN2, modulates lipid droplet formation in order to promote virion assembly (By similarity). Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By similarity). {ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}. [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication. {ECO:0000250|UniProtKB:P27958}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044186;
GO  GO:0044191;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:1990904;
GO  GO:0019031;
GO  GO:0019013;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0005216;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0017124;
GO  GO:0005198;
GO  GO:0008270;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039645;
GO  GO:0039707;
GO  GO:0051259;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039547;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019087;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P27958};
SQ  MSTLPKPQRKTKRNTNRRPMDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQPIGRSWGQPG
SQ  YPWPLYGNEGCGWAGWLLSPRGSRPNWGPNDPRRRSRNLGKVIDTLTCGLADLMGYIPVLGGPLGGVAAALAHGVRAIED
SQ  GVNYATGNLPGCSFSIFLLALLSCLTTPASAIQVRNASGIYHLTNDCSNNSIVFEAETIILHLPGCVPCIKVGNGSRCWL
SQ  SVSPTLAVPNSSVPIHGFRRHVDLLVGAAAFCSAMYIGDLCGSVFLVGQLFTFRPKHHQVTQDCNCSIYAGHITGHRMAW
SQ  DMMLNWSPTVSYVVSSALRVPQLLLEVITGAHWGVLGALLYFSMVANWAKVIAVLFLFAGADATTYTGSAVSSTTGAFVS
SQ  LFSPGPTQNLQLVNSNGSWHINRTALNCNDSLQTGFIAGLFARYKFNSTGCPERMSKCRPLHSFEQGWGPISYVNISGSS
SQ  EDKPYCWHYAPRPCGIVPARNVCGPVYCFTPSPVVVGTTDQRGIPTYTWGENVSDVFLLHSARPPLGAWFGCTWMNSSGF
SQ  VKTCGAPPCRIKPTINETDLVCPTDCFRKHPDASFVKCGSGPWLTPRCMVDYPYRLWHYPCTVNFTIHKVRVFVGGVEHR
SQ  FNAACNWTRGDRCELDDRDRFEMSPLLFSTTQLAILPCSFTTMPALSTGLIHLHQNIVDIQYLYGVSTAVVSWAMKWEYV
SQ  VLAFLVLADARVCACLWLMFLVGQAEAALENVIVLNAASAASCQGLLWGLIFICCAWHVRGRAVPVTTYALLQLWPLLLL
SQ  ILALPRRAYAFDSEQAASAGLLVLGLITIFTLTPAYKQLLISMLWWIQYFIALTEAQLHQWVPSLLVRGGRDAVILLACL
SQ  FHPQLGFEVTKILLALLGPLYLLQYSLLKTPYFVRAHILLRACMFFRGMARGRYAQAILLRIGAWTGTYIYDHLAPLSDW
SQ  ACDGLRDLAVAVEPVVFSPMEKKVITWGADTAACGDIIAGLPVAARRGNLLFLGPADDVKGKGWRLLAPITAYAQQTRGI
SQ  VGTIVTSLTGRDKNEVEGEIQVVSTATQSFLATAVNGVLWTVYYGAGSKTLAGPKGPVCQMYTNVDQDLVGWPAPAGARS
SQ  LTPCSCGSSDLYLVTRNADVIPARRRGDNRAALLSPRPISTLKGSSGGPMLCPSGHVAGIFRAAVCTRGVAKSLDFAPVE
SQ  SMQSSQRSPSFSDNTSPPAVPQTYQVGYLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGSYMSTSHGIDPNIR
SQ  TGVRTITTGGAITYSTYGKFLADGGCSGGAYDVIICDECHSTDPTTVSGIGTVLDQAETSGVRLTVLATATPPGSVTVPH
SQ  PNITESALPTTGEIPFYGKAVPLEYIKGGRHLIFCHPKKKCDELAKQLVSLGLNAVAFYRGVDVSVIPTSGDVVVCATDA
SQ  LMTGYTGDFDSVIDCNVTVTQVVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGKHGVYRYVSQGERPSGMFDSVILCE
SQ  AYDTGCAWYELTPAETTVRLRAYLNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQAEENFAYLVAYQATVCARAKA
SQ  PPPSWDTMWKCLIRLKPMLTGPTPLLYRLGPVQNEVVTTHPITKYIMTCMSADLEVITSTWVLVGGVVAALAAYCLSVGC
SQ  VVICGRISTSGKPVLIPDREVLYQQFDEMEECSRHIPYLAEGHLIAEQFKQKVLGLIQSTSKQAEELKPAVHAAWPKLEQ
SQ  FWQKQLWNFVSGIQYLAGLSTLPGNPAIASLMSFSASLTSPLSTHQTLLLNILGGWVASQLANPTASTAFVVSGLAGAAV
SQ  GSIGLGRVIVDVLAGYGAGVSGALVAFKIMCGETPSAEDMVNLLPALLSPGALVVGVVCAAILRRHAGPSEGATQWMNRL
SQ  IAFASRGNHVSPTHYVPETDTSRQIMTILSSLTVTSLLRKLHEWINTDWSTPCSSSWLRDIWDWVCEVLSDFKTWLKAKL
SQ  VPALPGVPFLSCQRGFRGTWRGDGICHTTCPCGSEITGHVKNGTMKISGPRWCSNVSHRTFPINATTTGPSVPIPEPNYT
SQ  RALWRVSAEEYVEVKRVGDSHFVVGATTDNLKCPCQVPAPEFFTEVDGVRLHRYAPRCKPLLRDEVSFSVGLSSYAVGSQ
SQ  LPCEPEPDVTVVTSMLIDPSHVTAEAAARRLARGSPPSLASSSASQLSAPSLKATCTMHGAHPDAELIEANLLWRQEMGG
SQ  NITRVESENKVVILDSFDPLVPEFEEREMSVPAECHRPRRPKFPPALPIWATPGYNPPVLETWKSPTYEPPVVHGCALPP
SQ  SGPPPIPPPRRKKVVQLDSSNVSAALAQLAAKTFETPSSPTTGYGSDQPDHSTESSEHDRDDGVASEAESYSSMPPLEGE
SQ  PGDPDLSSGSWSTVSEEGDSVVCCSYSYSWTGALVTPCAAEEEKLPINPLSNSLIRHHNLVYSTSSRSAATRQKKVTFDR
SQ  VQLLDQHYYDTVKEIKLRASHVKAQLLSTEEACDLTPPHSARSKFGYGAKDVRSHASKAINHINSVWADLLEDTQTPIPT
SQ  TIMAKNEVFCVDASKGGRKSARLIVYPDLGVRVCEKRALFDVTRKLPTAIMGDAYGFQYSPQQRVDRLLKMWRSKKTPMG
SQ  FSYDTRCFDSTVTERDIRTEQDIYLSCQLDPEARKVIESLTERLYVGGPMYNSKGQLCGQRRCRASGVLPTSMGNTVTCF
SQ  LKATAACRAAGFTDYDMLVCGDDLVVVTESAGVNEDIANLRAFTEAMTRYSATPGDEPSPTYDLELITSCSSNVSVAHDG
SQ  DGRRYYYLTRDPVTPLARAAWETARHTPVNSWLGNIIMYAPTIWVRMVLMTHFFQILQAQETLDRALDFDIYGVTYSITP
SQ  LDLPVIIQRLHGMAAFSLHGYSPDELNRVASCLRKLGAPPLRAWRHRARAVRAKLIAQGGKAAVCGKYLFNWAIKTKLRL
SQ  TPLRGASALDLSGWFTSGYGGGDVYHSASRARPRFLLLCLLLLSVGVGIFLLPAR
//
ID  Q32ZD7;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  59563;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q32ZD7;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKKPGKSAAKRTVNMLKRLASVSPSRGRRTIRRMLDVRGAPRLILALMAFFRFAAIKPTLGLKKRWRSVNKTVAVKHLT
SQ  NFKKELTTMLDSVNKRKEKKKSFSTALLWITMITAVAGLKISSHRDRPLLMVNKTDVSDAIPVPSVKGTNMCTIRALDVG
SQ  YTCAYDTTYECPHLEVTMDPEDIDCWCTLESVYVNYGLCKQNHHVRRGRRAINIPHHGESHLENRATPWMDTTKTTKYLT
SQ  KVENWVIRNPGYALVALATAWMLGSNTPQRVVFMIMMMLIAPAYSLNCLGISNRDFVEGLSGGTWVDIVLEGGSCVTVMA
SQ  KDKPTLDIKLIRMEAKDLATVRSYCYQATVTDSSTEARCPTMGEAHNSKSLDASYVCKSSYVDRGWGNGCGLFGKGSIQT
SQ  CVKFSCPGKATGKSIQRENLNYDVAVYVHGPISAAAHGNYTAQLTGKYAAKFSITPSAPTYTANLGEYGEATMECEPRAA
SQ  LDIDNYYVMSLNNKHWLVNRDWFHDLDLPWTGPATESWKNRESLIEFEEPHATRQTVVALGNQEGALHTALAGAIPVEVS
SQ  STTLTLNSGHLKCRLKLDKLKIKGTTYAMCKGTFAFAQTPVDTGHGTIVAELTYTGTDGPCKIPISMTADLRDMTPIGRL
SQ  VTVNPIIPSSAKSQKILVELEPPFGSSFILVGQENNQIKYQWHKTGSTIGNALKTTWKGAQRFAVLGDTAWDFGSVGGIF
SQ  NSIGKTIHGVFGTAFRSLFGGMSWVTQALMGALLLWLGISARERTVSLIMLSVGGILLFLAVNVHADTGCAIDMARRELK
SQ  CGSGIFIHNDVETWRNNYKYHPLTPRGFAKVIQMSKDKGVCGIRSVGRLEHEMWEAIAPELNAIFEDNGVDLSVVVKGQT
SQ  GIYKRAPKRLTETKDEMSFGWKNWGKSFIFSTETANSTFIVDGPESKECPTSDRAWNSLELEDFGFGIISTKIFLKVNEQ
SQ  RGNSCDSAVIGTAVKGNEAVHSDLGFWIQSTKNESWQLERAVLGEVKSCTWPESHTLWGDGVEESDLIIPITLAGPKSHH
SQ  NMRPGYKTQTKGPWHEETPLVIEFAECPGTTVTQEESCGGRGPSIRTTTASGRTIRNWCCKNCTLPPLRFMAGENCWYGV
SQ  EVRPKRENEETLIKSKVSAGNGQTIEPFQLGILMAFVFTQEVLRRRWTANLALPTSALLMACFIFGGFTYLDLFRYFILV
SQ  GAAFAEANSGGDVVHLAMIAAFNIQPVALVTTFFRKNWTNRENMILIIAAACTQMACMELKIELFHVMNSLSLAWMILKA
SQ  LTTGTTSTLAMPFLAALSPPMNWLGLDVVRCLLIMAGVAALISERRESLAKKKGALLISAALALTGAFSPLVLQGALMFT
SQ  QSLGKRGWPASEVLTAVGMTFALAGSVARLDGGTMAIPLATMAILAVAYVLSGKSTDMWLERCADISWINEAEITGTSPR
SQ  LDVELDSNGDFKMINDPGVPMWMWTCRMGLMAMAAYNPVLIPVSMAGYWMTVKIHKRGGVMWDVPAPKQFGKTELKPGVY
SQ  RVMTMGILGRYQSGVGVMWDGVFHTMWHVTQGAALRNGEGRLNPTWGSVRDDLISYGGKWKLSATWNGSEEVQMIAVEPG
SQ  KAAKNYQTKPGVFKTPAGEIGAITLDFPKGTSGSPIINKAGEITGLYGNGIVLERGAYVSAITQGERQEEETPEAFTPDM
SQ  LKKRRLTILDLHPGAGKTRRVIPQIVRECVKARLRTVILVPTRVVAAEMAEALRGLPIRYQTSAVKAEHSGNEIVDAMRH
SQ  ATLTQRLLTPAKVPNYNVFVMDEAHFTDPASIAARGYISTKVELGEAAAIFMTATPPGTTDPFPDSNAPIIDQEAEIPDR
SQ  AWNSGFEWITEYTGKTVWFVPSVRMGNEIAMCLTKAGKKVIQLNRKSYDSEYQKCKGNDWDFVITTDISEMGANFGAHRV
SQ  IDSRKCVKPVILDGDDRVLMNGPAPITPASAAQRRGRIGRDPTQSGDEYFYGGPTTTDDTGHAHWIEAKILLDNIQLQNG
SQ  LVAQLYGPERDKVFTTDGEYRLRSEQKKNFVEFLRTGDLPVWLSYKVAEAGYAYTDRRWCFDGPANNTILEVRGDPEVWT
SQ  RQGEKRILRPRWSDARVYCDNQALRSFKEFAAGKRSAGSVMEVMGRMPDYFWTKTLNAADNLYVLATANKGGRAHQAALE
SQ  ELPDTVETILLMTMMCVASLGMFTLMVHRRGLGKTGLGTLVLATVTVLLWISDVPAPKIAGVLLIAFLLMIVLIPEPEKQ
SQ  RSQTDNHLAIFLVCVLLLIGAVSANEMGWLETTKKDIGKLFRSSGDTQEQSTWQSWAPEVRAATAWAGYAGLTVFLTPLF
SQ  RHLITTQYVSFSLTAITAQASALFGLSAGYPFVGIDLAVGFLLLGCYGQYNLPTAVATGLLLLAHYGYMIPGWQAEAMRA
SQ  AQKRTAAGVMKNAVVDGIVATDIPEVDTATPITEKKLGQILLILLCGASLLVKFDTMVLVEAGVLTTSAMATLIEGNANT
SQ  VWNSTVAVGVCHLMRGAWLAGPSIGWTIVRNLENPKLKRGGGSAPTLGEIWKAQLNQLTREEFMAYRRDGILEVDRTQAR
SQ  RARQSGITTGGHPVSRGTAKLRWMVERGFVRPIGKVVDLGCGRGGWSYYCATLRHVQEVRGYTKGGPGHEEPVMMQSYGW
SQ  NIVTMKSGVDVFYKPTESCDTLLCDIGESSSSVGVEEARTLRVLDMVEPWLRAANSFCIKVLCPYTPKVIERLERLQRAY
SQ  GGGLVRVPLSRNSTHEMYWVSGASSNIINAVTVTSQILVQRMNKGCRHGPRYEEDVCLGSGTRAVATQASPSDHTKIKHR
SQ  LERLRKEFSATWHIDLEHPYRTWHYHGSYEVQPTGSANSMVNGVVRLLSKPWDAITSVVTMAMTDTTPFGQQRVFKEKVD
SQ  TRAPDPAVGVAQALDITTGWLWTFLARSKKPRMCTREEFIAKVNSNAALGAVFDEQNQWSTAREAVEDPAFWNLVDEERK
SQ  AHLAGRCETCIYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMSRENSLGGVEGQGLQKLGYILR
SQ  DISHLEGGNMFADDTAGWDTRITRADLENEAKVMNMMDGEHKQLAKAIIELTYRHKVVKVMRPARGGKTVMDIISREDQR
SQ  GSGQVVTYALNTFTNLAAQLVRCMEGEELLTESDVHGLSPKKKQAVRNWLIQNGRERLSRMAVSGDDCVVKPIDDRFASA
SQ  LHFLNGMAKIRKDTQEWKPSVGWSNWQEVPFGSHHFNELLMKDGRTIVVPCRSQDELVGRARVSPGSGWSLRETACLSKA
SQ  YAQMWLLMYFHRRDLRLMANAICSAVPVDWVPTGRTTWSIHGKGEWMTTEDMLQVWNRVWIEDNEHMEDKTPITSWTDIP
SQ  YIGKREDQWCGSLIGTRQRATWAENIYTPIMQIRNLIGDEKYVDCMVSQHRFETPSPVLFTGAI
//
ID  P27395;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11073;
SL  Nucleus Position: SL-0382;
SL  Comments: [Genome polyprotein]: Host endoplasmic reticulum membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Host cell surface {ECO:0000269|PubMed:28053106}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000269|PubMed:16699025}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P27395;
DR  UNIPROT: Q82920;
DR  UNIPROT: Q82921;
DR  UNIPROT: Q82922;
DR  UNIPROT: Q82923;
DR  UNIPROT: Q82924;
DR  UNIPROT: Q82925;
DR  UNIPROT: Q82926;
DR  UNIPROT: Q82927;
DR  UNIPROT: Q82928;
DR  PDB: 2Z83;
DR  PDB: 3P54;
DR  PDB: 4HDG;
DR  PDB: 4HDH;
DR  PDB: 4K6M;
DR  PDB: 4MTP;
DR  PDB: 5MV1;
DR  PDB: 5MV2;
DR  PDB: 5O19;
DR  PDB: 5O36;
DR  PDB: 5OW2;
DR  PDB: 5WSN;
DR  PDB: 5YWO;
DR  PDB: 5YWP;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HSPA5 (PubMed:28053106). Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3 (PubMed:7897348). May have membrane- destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:7897348}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase (PubMed:18201743, PubMed:7897348). NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5 (Probable). NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). {ECO:0000255|PROSITE- ProRule:PRU00860, ECO:0000269|PubMed:18201743, ECO:0000269|PubMed:7897348, ECO:0000305|PubMed:7897348}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN- alpha/beta pathway (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome (PubMed:24293643). Performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:16731929). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:16731929). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:16731929, ECO:0000269|PubMed:24293643}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044228;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWKAVEKSVAMKH
SQ  LTSFKRELGTLIDAVNKRGRKQNKRGGNEGSIMWLASLAVVIACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENR
SQ  CWVRAIDVGYMCEDTITYECPKLTMGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLD
SQ  STKATRYLMKTENWIIRNPGYAFLAAVLGWMLGSNNGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLE
SQ  GDSCLTIMANDKPTLDVRMINIEASQLAEVRSYCYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTDRGWGNGCG
SQ  LFGKGSIDTCAKFSCTSKAIGRTIQPENIKYEVGIFVHGTTTSENHGNYSAQVGASQAAKFTVTPNAPSITLKLGDYGEV
SQ  TLDCEPRSGLNTEAFYVMTVGSKSFLVHREWFHDLALPWTSPSSTAWRNRELLMEFEGAHATKQSVVALGSQEGGLHQAL
SQ  AGAIVVEYSSSVKLTSGHLKCRLKMDKLALKGTTYGMCTEKFSFAKNPVDTGHGTVVIELSYSGSDGPCKIPIVSVASLN
SQ  DMTPVGRLVTVNPFVATSSANSKVLVEMEPPFGDSYIVVGRGDKQINHHWHKAGSTLGKAFSTTLKGAQRLAALGDTAWD
SQ  FGSIGGVFNSIGRAVHQVFGGAFRTLFGGMSWITQGLMGALLLWMGVNARDRSIALAFLATGGVLVFLATNVHADTGCAI
SQ  DITRKEMRCGSGIFVHNDVEAWVDRYKYLPETPRSLAKIVHKAHKEGVCGVRSVTRLEHQMWEAVRDELNVLLKENAVDL
SQ  SVVVNKPVGRYRSAPKRLSMTQEKFEMGWKAWGKSILFAPELANSTFVVDGPETKECPDEHRAWNSMQIEDFGFGITSTR
SQ  VWLKIREESTDECDGAIIGTAVKGHVAVHSDLSYWIESRYNDTWKLERAVFGEVKSCTWPETHTLWGDDVEESELIIPHT
SQ  IAGPKSKHNRREGYKTQNQGPWDENGIVLDFDYCPGTKVTITEDCSKRGPSVRTTTDSGKLITDWCCRSCSLPPLRFRTE
SQ  NGCWYGMEIRPVMHDETTLVRSQVDAFKGEMVDPFQLGLLVMFLATQEVLRKRWTARLTIPAVLGVLLVLMLGGITYTDL
SQ  ARYVVLVAAAFAEANSGGDVLHLALIAVFKIQPAFLVMNMLSTRWTNQENVILVLGAAFFQLASVDLQIGVHGILNAAAI
SQ  AWMIVRAITFPTTSSVTMPVLALLTPGMRALYLDTYRIILLVIGICSLLHERKKTMAKKKGAVLLGLALTSTGWFSPTTI
SQ  AAGLMVCNPNKKRGWPATEFLSAVGLMFAIVGGLAELDIESMSIPFMLAGLMAVSYVVSGKATDMWLERAADISWEMDAA
SQ  ITGSSRRLDVKLDDDGDFHLIDDPGVPWKVWVLRMSCIGLAALTPWAIVPAAFGYWLTLKTTKRGGVFWDTPSPKPCSKG
SQ  DTTTGVYRIMARGILGTYQAGVGVMYENVFHTLWHTTRGAAIMSGEGKLTPYWGSVREDRIAYGGPWRFDRKWNGTDDVQ
SQ  VIVVEPGKAAVNIQTKPGVFRTPFGEVGAVSLDYPRGTSGSPILDSNGDIIGLYGNGVELGDGSYVSAIVQGDRQEEPVP
SQ  EAYTPNMLRKRQMTVLDLHPGSGKTRKILPQIIKDAIQQRLRTAVLAPTRVVAAEMAEALRGLPVRYQTSAVQREHQGNE
SQ  IVDVMCHATLTHRLMSPNRVPNYNLFVMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTTDPFPDSNAPIHDL
SQ  QDEIPDRAWSSGYEWITEYAGKTVWFVASVKMGNEIAMCLQRAGKKVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGA
SQ  NFGASRVIDCRKSVKPTILEEGEGRVILGNPSPITSASAAQRRGRVGRNPNQVGDEYHYGGATSEDDSNLAHWTEAKIML
SQ  DNIHMPNGLVAQLYGPEREKAFTMDGEYRLRGEEKKNFLELLRTADLPVWLAYKVASNGIQYTDRKWCFDGPRTNAILED
SQ  NTEVEIVTRMGERKILKPRWLDARVYADHQALKWFKDFAAGKRSAVSFIEVLGRMPEHFMGKTREALDTMYLVATAEKGG
SQ  KAHRMALEELPDALETITLIVAITVMTGGFFLLMMQRKGIGKMGLGALVLTLATFFLWAAEVPGTKIAGTLLIALLLMVV
SQ  LIPEPEKQRSQTDNQLAVFLICVLTVVGVVAANEYGMLEKTKADLKSMFGGKTQASGLTGLPSMALDLRPATAWALYGGS
SQ  TVVLTPLLKHLITSEYVTTSLASINSQAGSLFVLPRGVPFTDLDLTVGLVFLGCWGQITLTTFLTAMVLATLHYGYMLPG
SQ  WQAEALRAAQRRTAAGIMKNAVVDGMVATDVPELERTTPLMQKKVGQVLLIGVSVAAFLVNPNVTTVREAGVLVTAATLT
SQ  LWDNGASAVWNSTTATGLCHVMRGSYLAGGSIAWTLIKNADKPSLKRGRPGGRTLGEQWKEKLNAMSREEFFKYRREAII
SQ  EVDRTEARRARRENNIVGGHPVSRGSAKLRWLVEKGFVSPIGKVIDLGCGRGGWSYYAATLKKVQEVRGYTKGGAGHEEP
SQ  MLMQSYGWNLVSLKSGVDVFYKPSEPSDTLFCDIGESSPSPEVEEQRTLRVLEMTSDWLHRGPREFCIKVLCPYMPKVIE
SQ  KMEVLQRRFGGGLVRLPLSRNSNHEMYWVSGAAGNVVHAVNMTSQVLLGRMDRTVWRGPKYEEDVNLGSGTRAVGKGEVH
SQ  SNQEKIKKRIQKLKEEFATTWHKDPEHPYRTWTYHGSYEVKATGSASSLVNGVVELMSKPWDAIANVTTMAMTDTTPFGQ
SQ  QRVFKEKVDTKAPEPPAGAKEVLNETTNWLWAHLSREKRPRLCTKEEFIKKVNSNAALGAVFAEQNQWSTAREAVDDPRF
SQ  WEMVDEERENHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARYLEFEALGFLNEDHWLSRENSGGGVEGSG
SQ  VQKLGYILRDIAGKQGGKMYADDTAGWDTRITRTDLENEAKVLELLDGEHRMLARAIIELTYRHKVVKVMRPAAEGKTVM
SQ  DVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEGVIGPQHLEQLPRKTKIAVRTWLFENGEERVTRMAISGDDCVVK
SQ  PLDDRFATALHFLNAMSKVRKDIQEWKPSHGWHDWQQVPFCSNHFQEIVMKDGRSIVVPCRGQDELIGRARISPGAGWNV
SQ  KDTACLAKAYAQMWLLLYFHRRDLRLMANAICSAVPVDWVPTGRTSWSIHSKGEWMTTEDMLQVWNRVWIEENEWMMDKT
SQ  PITSWTDVPYVGKREDIWCGSLIGTRSRATWAENIYAAINQVRAVIGKENYVDYMTSLRRYEDVLIQEDRVI
//
ID  P19110;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11074;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Host cell surface {ECO:0000250|UniProtKB:P03314}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P19110;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HSPA5. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN- alpha/beta pathway (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome (By similarity). Performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:P27395, ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044228;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWKAVEKSVAMKH
SQ  LTSFKRELGTLIDAVNKRGRKQNKRGGNEGSIMWLASLAVVIACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENR
SQ  CWVRAIDVGYMCEDTITYECPKLTMGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLD
SQ  STKATRYLMKTENWIIRNPGYAFLAAVLGWMLGSNNGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLE
SQ  GDSCLTIMANDKPTLDVRMINIEASQLAEVRSYCYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTDRGWGNGCG
SQ  LFGKGSIDTCAKFSCTSKAIGRTIQPENIKYEVGIFVHGTTTSENHGNYSAQVGASQAAKFTVTPNAPSITLKLGDYGEV
SQ  TLDCEPRSGLNTEAFYVMTVGSKSFLVHREWFHDLALPWTSPSSTAWRNRELLMEFEGAHATKQSVVALGSQEGGLHQAL
SQ  AGAIVVEYSSSVKLTSGHLKCRLKMDKLALKGTTYGMCTEKFSFAKNPADTGHGTVVIELSYSGSDGSCKIPIVSVASLN
SQ  DMTPVGRLVTVNPFVATSSANSKVLVEMEPPFGDSYIVVGRGDKQINHHWHKAGSTLGKAFSTTLKGAQRLAALGDTAWD
SQ  FGSIGGVFNSIGKAVHQVFGGAFRTLFGGMSWITQGLMGALLLWMGVNARDRSIALAFLATGGVLVFLATNVHADTGCAI
SQ  DITRKEMRCGSGIFVHNDVEAWVDRYKYLPETPRSLAKIVHKAHKEGVCGVRSVTRLEHQMWEAVRDELNVLLKENAVDL
SQ  SVVVNKPVGRYRSAPKRLSMTQEKFEMGWKAWGKSILFAPELANSTFVVDGPETKECPDEHRAWNSMQIEDFGFGITSTR
SQ  VWLKIREESTDECDGAIIGTAVKGHVAVHSDLSYWIESRYNDTWKLERAVFGEVKSCTWPETHTLWGDDVEESELIIPHT
SQ  IAGPKSKHNRREGYKTQNQGPWDENGIVLDFDYCPGTKVTITEDCGKRGPSVRTTTDSGKLITDWCCRSCSLPPLRFRTE
SQ  NGCWYGMEIRPVRHDETTLVRSQVDAFNGEMVDPFQLGLLVMFLATQEVLRKRWTARLTIPAVLGALLVLMLGGITYTDL
SQ  ARYVVLVAAAFAEANSGGDVLHLALIAVFKIQPAFLVMNMLSTRWTNQENVVLVLGAAFFQLASVDLQIGVHGILNAAAI
SQ  AWMIVRAITFPTTSSVTMPVLALLTPGMRALYLDTYRIILLVIGICSLLHERKKTMAKKKGAVLLGLALTSTGWFSPTTI
SQ  AAGLMVCNPNKKRGWPATEFLSAVGLMFAIVGGLAELDIESMSIPFMLAGLMAVSYVVSGKATDMWLERAADISWEMDAA
SQ  ITGSSRRLDVKLDDDGDFHLIDDPGVPWKVWVLRMSCIGLAALTPWAIVPAAFGYWLTLKTTKRGGVFWDTPSPKPCSKG
SQ  DTTTGVYRIMARGILGTYQAGVGVMYENVFHTLWHTTRGAAIMSGEGKLTPYWGSVREDRIAYGGPWRFDRKWNGTDDVQ
SQ  VIVVEPGKAAVNIQTKPGVFRTPFGEVGAVSLDYPRGTSGSPILDSNGDIIGLYGNGVELGDGSYVSAIVQGDRQEEPVP
SQ  EAYTPNMLRKRQMTVLDLHPGSGKTRKILPQIIKDAIQQRLRTAVLAPTRVVAAEMAEVLRGLPVRYQTSAVQREHQGNE
SQ  IVDVMCHATLTHRLMSPNRVPNYNLFVMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTTDPFPDSNAPIHDL
SQ  QDEIPDRAWSSGYEWITEYAGKTVWFVASVKMGNEIAMCLQRAGKKVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGA
SQ  NFGASRVIDCRKSVKPTILEEGEGRVILGNPSPITSASAAQRRGRVGRNPNQVGDEYHYGGATSEDDSNLAHWTEAKIML
SQ  DNIHMPNGLVAQLYGPEREKAFTMDGEYRLRGEEKKNFLELLRTADLPVWLAYKVASNGIQYTDRKWCFDGPRTNAILED
SQ  NTEVEIVTRMGERKILKPRWLDARVYADHQALKWFKDFAAGKRSAVSFIEVLGRMPEHFMGKTREALDTMYLVATAEKGG
SQ  KAHRMALEELPDALETITLIVAITVMTGGFFLLMMQRKGIGKMGLGALVLTLATFFLWAAEVPGTKIAGTLLIALLLMVV
SQ  LIPEPEKQRSQTDNQLAVFLICVLTVVGVVAANEYGMLEKTKADLKSMFGGKTQASGLTGLPSMALDLRPATAWALYGGS
SQ  TVVLTPLLKHLITSEYVTTSLASINSQAGSLFVLPRGVPFTDLDLTVGLVFLGCWGQITLTTFLTAMVLATLHYGYMLPG
SQ  WQAEALRAAQRRTAAGIMKNAVVDGMVATDVPELERTTPLMQKKVGQVLLIGVSVAAFLVNPNVTTVREAGVLVTAATLT
SQ  LWDNGASAVWNSTTATGLCHVMRGSYLAGGSIAWTLIKNADKPSLKRGRPGGRTLGEQWKEKLNAMSREEFFKYRREAII
SQ  EVDRTEARRARRENNIVGGHPVSRGSAKLRWLVEKGFVSPIGKVIDLGCGRGGWSYYAATLKKVQEVRGYTKGGAGHEEP
SQ  MLMQSYGWNLVSLKSGVDVFYKPSEPSDTLFCDIGESSPSPEVEEQRTLRVLEMTSDWLHRGPREFCIKVLCPYMPKVIE
SQ  KMEVLQRRFGGGLVRLPLSRNSNHEMYWVSGAAGNVVHAVNMTSQVLLGRMDRTVWRGPKYEEDVNLGSGTRAVGKGEVH
SQ  SNQEKIKKRIQKLKEEFATTWHKDPEHPYRTWTYHGSYEVKATGSASSLVNGVVKLMSKPWDAIANVTTMAMTDTTPFGQ
SQ  QRVFKEKVDTKAPEPPAGAKEVLNETTNWLWAHLSREKRPRLCTKEEFIKKVNSNAALGAVFAEQNQWSTAREAVDDPRF
SQ  WEMVDEERENHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARYLEFEALGFLNEDHWLSRENSGGGVEGSG
SQ  VQKLGYILRDIAGKQGGKMYADDTAGWDTRITRTDLENEAKVLELLDGEHRMLARAIIELTYRHKVVKVMRPAAEGKTVM
SQ  DVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEGVIGPQHLEQLPRKNKIAVRTWLFENGEERVTRMAISGDDCVVK
SQ  PLDDRFATALHFLNAMSKVRKDIQEWKPSHGWHDWQQVPFCSNHFQEIVMKDGRSIVVPCRGQDELIDRARISPGAGWNV
SQ  KDTACLAKAYAQMWLLLYFHRRDLRLMANAICSAVPVDWVPTGRTSWSIHSKGEWMTTEDMLQVWNRVWIEENEWMMDKT
SQ  PITSWTDVPYVGKREDIWCGSLIGTRSRATWAENIYAAINQVRAVIGKENYVDYMTSLRRYEDVLIQEDRVI
//
ID  P32886;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11075;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Host cell surface {ECO:0000250|UniProtKB:P03314}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P32886;
DR  UNIPROT: P08769;
DR  PDB: 5YWO;
DR  PDB: 5YWP;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HSPA5. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane- destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P27395, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase (By similarity). NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A- NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5 (By similarity). NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000250|UniProtKB:P27395, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN- alpha/beta pathway (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:P27395, ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044228;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWKAVEKSVAMKH
SQ  LTSFKRELGTLIDAVNKRGRKQNKRGGNEGSIMWLASLAVVIAYAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENR
SQ  CWVRAIDVGYMCEDTITYECPKLTMGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLD
SQ  STKATRYLMKTENWIIRNPGYAFLAATLGWMLGSNNGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLE
SQ  GDSCLTIMANDKPTLDVRMINIEASQLAEVRSYCYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTDRGWGNGCG
SQ  LFGKGSIDTCAKFSCTSKAIGRTIQPENIKYEVGIFVHGTTTSENHGNYSAQVGASQAAKFTITPNAPSITLKLGDYGEV
SQ  TLDCEPRSGLNTEAFYVMTVGSKSFLVHREWFHDLALPWTSPSSTAWRNRELLMEFEEAHATKQSVVALGSQEGGLHQAL
SQ  AGAIVVEYSSSVKLTSGHLKCRLKMDKLALKGTTYGMCTEKFSFAKNPADTGHGTVVIELSYSGSDGPCKIPIVSVASLN
SQ  DMTPVGRLVTVNPFVATSSANSKVLVEMEPPFGDSYIVVGRGDKQINHHWHKAGSTLGKAFSTTLKGAQRLAALGDTAWD
SQ  FGSIGGVFNSIGKAVHQVFGGAFRTLFGGMSWITQGLMGALLLWMGVNARDRSIALAFLATGGVLVFLATNVHADTGCAI
SQ  DITRKEMRCGSGIFVHNDVEAWVDRYKYLPETPRSLAKIVHKAHKEGVCGVRSVTRLEHQMWEAVRDELNVLLKENAVDL
SQ  SVVVNKPVGRYRSAPKRLSMTQEKFEMGWKAWGKSILFAPELANSTFVVDGPETKECPDEHRAWNSMQIEDFGFGITSTR
SQ  VWLKIREESTDECDGAIIGTAVKGHVAVHSDLSYWIESRYNDTWKLERAVFGEVKSCTWPETHTLWGDGVEESELIIPHT
SQ  IAGPKSKHNRREGYKTQNQGPWDENGIVLDFDYCPGTKVTITEDCGKRGPSVRTTTDSGKLITDWCCRSCSLPPLRFRTE
SQ  NGCWYGMEIRPVRHDETTLVRSQVDAFNGEMVDPFQLGLLVMFLATQEVLRKRWTARLTIPAVLGALLVLMLGGITYTDL
SQ  ARYVVLVAAAFAEANSGGDVLHLALIAVFKIQPAFLVMNMLSTRWTNQENVVLVLGAALFQLASVDLQIGVHGILNAAAI
SQ  AWMIVRAITFPTTSSVTMPVLALLTPGMRALYLDTYRIILLVIGICSLLQERKKTMAKKKGAVLLGLALTSTGWFSPTTI
SQ  AAGLMVCNPNKKRGWPATEFLSAVGLMFAIVGGLAELDIESMSIPFMLAGLMAVSYVVSGKATDMWLERAADISWEMDAA
SQ  ITGSSRRLDVKLDDDGDFHLIDDPGVPWKVWVLRMSCIGLAALTPWAIVPAAFGYWLTLKTTKRGGVFWDTPSPKPCSKG
SQ  DTTTGVYRIMARGILGTYQAGVGVMYENVFHTLWHTTRGAAIMSGEGKLTPYWGSVKEDRIAYGGPWRFDRKWNGTDDVQ
SQ  VIVVEPGKAAVNIQTKPGVFRTPFGEVGAVSLDYPRGTSGSPILDSNGDIIGLYGNGVELGDGSYVSAIVQGDRQEEPVP
SQ  EAYTPNMLRKRQMTVLDLHPGSGKTRKILPQIIKDAIQQRLRTAVLAPTRVVAAEMAEALRGLPVRYQTSAVQREHQGNE
SQ  IVDVMCHATLTHRLMSPNRVPNYNLFVMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTTDPFPDSNAPIHDL
SQ  QDEIPDRAWSSGYEWITEYAGKTVWFVASVKMGNEIAMCLQRAGKKVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGA
SQ  NFGASRVIDCRKSVKPTILEEGEGRVILGNPSPITSASAAQRRGRVGRNPNQVGDEYHYGGATSEDDSNLAHWTEAKIML
SQ  DNIHMPNGLVAQLYGPEREKAFTMDGEYRLRGEEKKNFLELLRTADLPVWLAYKVASNGIQYTDRRWCFDGPRTNAILED
SQ  NTEVEIVTRMGERKILKPRWLDARVYADHQALKWFKDFAAGKRSAISFIEVLGRMPEHFMGKTREALDTMYLVATAEKGG
SQ  KAHRMALEELPDALETITLIVAITVMTGGFFLLMMQRKGIGKMGLGALVLTLATFFLWAAEVPGTKIAGTLLIALLLMVV
SQ  LIPEPEKQRSQTDNQLAVFLICVLTVVGVVAANEYGMLEKTKADLKSMFVGKTQASGLTGLPSMALDLRPATAWALYGGS
SQ  TVVLTPLLKHLITSEYVTTSLASINSQAGSLFVLPRGVPFTDLDLTVGLVFLGCWGQITLTTFLTAMVLATLHYGYMLPG
SQ  WQAEALRAAQRRTAAGIMKNAVVDGMVATDVPELERTTPLMQKKVGQVLLIGVSVAAFLVNPNVTTVREAGVLVTAATLT
SQ  LWDNGASAVWNSTTATGLCHVMRGSYLAGGSIAWTLIKNADKPSLKRGRPGGRTLGEQWKEKLNAMSREEFFKYRREAII
SQ  EVDRTEARRARRENNIVGGHPVSRGSAKLRWLVEKGFVSPIGKVIDLGCGRGGWSYYAATLKKVQEVRGYTKGGAGHEEP
SQ  MLMQSYGRNLVSLKSGVDVFYKPSEPSDTLFCDIGESSPSPEVEEQRTLRVLEMTSDWLHRGPREFCIKVLCPYMPKVIE
SQ  KMEVLQRRFGGGLVRLPLSRNSNHEMYWVSGAAGNVVHAVNMTSQVLLGRMDRTVWRGPKYEEDVNLGSGTRAVGKGEVH
SQ  SNQEKIKKRIQKLKEEFATTWHKDPEHPYRTWTYHGSYEVKATGSASSLVNGVVKLMSKPWDAIANVTTMAMTDTTPFGQ
SQ  QRVFKEKVDTKAPEPPAGAKEVLNETTNWLWAHLSREKRPRLCTKEEFIKKVNSNAALGAVFAEQNQWSTAREAVDDPRF
SQ  WEMVDEERENHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARYLEFEALGFLNEDHWLSRENSGGGVEGSG
SQ  VQKLGYILRDIAGKQGGKMYADDTAGWDTRITRTDLENEAKVLELLDGEHRMLARAIIELTYRHKVVKVMRPAAEGKTVM
SQ  DVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEGVIGPQHLEQLPRKTKIAVRTWLFENGEERVTRMAISGDDCVVK
SQ  PLDDRFATALHFLNAMSKVRKDIQEWKPSHGWHDWQQVPFCSNHFQEIVMKDGRSIVVPCRGQDELIGRARISPGAGWNV
SQ  KDTACLAKAYAQMWLLLYFHRRDLRLMANAICSAVPVDWVPTGRTSWSIHSKGEWMTTEDMLQVWNRVWIEENEWMMDKT
SQ  PITSWTDVPYVGKREDIWCGSLIGTRSRATWAENIYAAINQVRAVIGKENYVDYMTSLRRYEDVLIQEDRVI
//
ID  G3FEX6;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  2555554;
SL  Nucleus Position: SL-0382;
SL  Comments: [Genome polyprotein]: Host endoplasmic reticulum membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Host cell surface {ECO:0000250|UniProtKB:P03314}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P27395}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: G3FEX6;
DR  UNIPROT: A0A165GB83;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HSPA5. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane- destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P27395}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN- alpha/beta pathway (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome (By similarity). Performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:P27395, ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044228;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWRAVEKSVAMKH
SQ  LTSFKRELGTLIDAVNKRGKKQNKRGGNESSIMWLASLAIVIACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENR
SQ  CWVRAIDVGYMCEDTITYECPKLAVGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLD
SQ  STKATRYLMKTENWIIRNPGYAFLAAALGWMLGSNSGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLE
SQ  GDSCLTIMANDKPTLDVRMINIEASQLAEVRSYCYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTDRGWGNGCG
SQ  LFGKGSIDTCAKFSCTSKAIGRTIQPENIKYEVGVFVHGTTTSENHGNYSAQVGASQAAKFTVTPNAPSITLKLGDYGEV
SQ  TLDCEPRSGLNTEAFYVMTVGSKSFLVHREWFHDLSLPWTSPSSTAWRNRELLMEFEEAHATKQSVVALGSQEGGLHQAL
SQ  AGAIVVEYSSSVKLTSGHLKCRLKMDKLALKGTTYGMCTEKFSFAKNPADTGHGTVVIELTYSGSDGPCKIPIVSVASLN
SQ  DMTPVGRLVTVNPFVATSSSNSKVLVEMEPPFGDSYIVVGRGDKQINHHWYKAGSTLGKAFSTTLKGAQRLAALGDTAWD
SQ  FGSIGGVFNSIGKAVHQVFGGAFRTLFGGMSWITQGLMGALLLWMGVNARDRSIALAFLATGGVLVFLATNVHADTGCAI
SQ  DITRKEMRCGSGIFVHNDVEAWVDRYKYLPETPRSLAKIVHKAHQEGVCGVRSVTRLEHQMWESVRDELNVLLKENAVDL
SQ  SVVVNKPVGRYRSAPKRLSMTQEKFEMGWKAWGKSILFAPELANSTFVVDGPETKECPDERRAWNSMQIEDFGFGITSTR
SQ  VWLKIREENTDECDGAIIGTAVKGHVAVHSDLSYWIESRLNDTWKLERAVFGEVKSCTWPETHTLWGDGVEESELIIPHT
SQ  IAGPRSKHNRREGYKTQNQGPWDENGIVLDFDYCPGTKVTITEDCGKRGPSIRTTTDSGKLITDWCCRSCSLPPLRFRTE
SQ  NGCWYGMEIRPVRHDETTLVRSQVDAFNGEMIDPFQLGLLVMFLATQEVLRKRWTARLTIPAVLGALLVLMLGGITYIDL
SQ  ARYVVLVAAAFAEANSGGDVLHLALIAVFKIQPAFLVMNMLSARWTNQENMVLVLGAAFFQLASVDLQIGVHGILNAAAI
SQ  AWMIVRAITFPTTSTVAMPVLALLTPGMRALYLDTYRIILLVIGICSLLQERRKTMAKKKGAVLLGLALTSTGWFSPTTI
SQ  AAGLMVCNPNKKRGWPATEFLSAVGLMFAIVGGLAELDIESMSIPFMLAGLMAVSYVISGKATDMWLDRAADISWEMEAA
SQ  ITGSSRRLDVKLDDDGDFHLIDDPGVPWKVWLLRMSCIGLAALTPWAIVPAAFGYWLTLKTTKRGGVFWDTPSPKPCLKG
SQ  DTTTGVYRIMARGILGTYQAGVGVMYENVFHTLWHTTRGAAIMSGEGKLTPYWGSVKEDRISYGGPWRFDRKWNGTDDVQ
SQ  VIVVEPGKPAVNIQTKPGVFRTPFGEIGAVSLDYPRGTSGSPILDSNGDIIGLYGNGVELGDGSYVSAIVQGDRQEEPVP
SQ  DAYTPSMLKKRQMTVLDLHPGSGKTRKILPQIIKDAIQQRLRTAVLAPTRVVAAEMAEALRGLPVRYQTSAVQREHQGNE
SQ  IVDVMCHATLTHRLMSPNRVPNYNLFVMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTTDPFPDSNAPIHDL
SQ  QDEIPDRAWSSGYEWITEYAGKTVWFVASVKMGNEIAMCLQRAGKKVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGA
SQ  NFGASRVIDCRKSVKPTILEEGEGRVILGNPSPITSASAAQRRGRVGRNPNQVGDEYHYGGATSEDDSNLAHWTEAKIML
SQ  DNIHMPNGLVAQLYGPEREKAFTMDGEYRLRGEEKKNFLELLRTADLPVWLAYKVASNGIQYTDRKWCFDGPRTNAILED
SQ  NTEVEIVTRMGERKILKPRWLDARVYADHQALKWFKDFAAGKRSAVSFIEVLGRMPEHFMGKTREALDTMYLVATAEKGG
SQ  KAHRMALEELPDALETITLIVAITVMTGGFFLLMMQRKGIGKMGLGALVLTLATFFLWAAEVPGTKIAGTLLVALLLMVV
SQ  LIPEPEKQRSQTDNQLAVFLICVLTVVGVVAANEYGMLEKTKADLKSMFGGRTQAPGLTGLPSMALDLRPATAWALYGGS
SQ  TVVLTPLLKHLITSEYVTTSLASISSQAGSLFVLPRGVPFTDLDLTVGLVFLGCWGQITLTTFLTAMVLVTLHYGYMLPG
SQ  WQAEALRAAQRRTAAGIMKNAVVDGMVATDVPELERTTPLMQKKVGQVLLIGVSVAAFLVNPNVTTVREAGVLVTAATLT
SQ  LWDNGASAVWNSTTATGLCHVMRGSYLAGGSIAWTLIKNADKPSLKRGRPGGRTLGEQWKEKLNAMSRDEFFKYRREAII
SQ  EVDRTEARRARRENNIVGGHPVSRGSAKLRWLVEKGFVSPIGKVIDLGCGRGGWSYYAATLKKVQEVKGYTKGGAGHEEP
SQ  MLMQSYGWNLVSLKSGVDVFYKPSEPSDTLFCDIGESSPSPEVEEQRTLRVLEMTSDWLHRGPREFCIKVLCPYMPKVIE
SQ  KMEVLQRRFGGGLVRLPLSRNSNHEMYWVSGAAGNVVHAVNMTSQVLLGRMDRTVWRGPKYEEDVNLGSGTRAVGKGEVH
SQ  SNQEKIRKRIQKLREEFATTWHQDPEHPYRTWTYHGSYEVKATGSASSLVNGVVKLMSKPWDAIANVTTMAMTDTTPFGQ
SQ  QRVFKEKVDTKAPEPPAGVKEVLNETTNWLWAHLSREKRPRLCTKEEFIKKVNSNAALGAVFAEQNQWSTAREAVGDPLF
SQ  WEMVDEERENHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARYLEFEALGFLNEDHWLSRENSGGGVEGSG
SQ  VQKLGYILRDIAGKQGGKMYADDTAGWDTRITRTDLENEAKVLELLDGEHRMLARAIIELTYRHKVVKVMRPAAGGKTVM
SQ  DVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEGVIGPQHLEQLPRKNKIAVRTWLFENGEERVTRMAISGDDCVVK
SQ  PLDDRFATALHFLNAMSKVRKDIQEWKPSHGWHDWQQVPFCSNHFQEIVMKDGRSIVVPCRGQDELIGRARISPGAGWNV
SQ  KDTACLAKAYAQMWLLLYFHRRDLRLMANAICSAVPVDWVPTGRTSWSIHSKGEWMTTEDMLQVWNRVWIEENEWMMDKT
SQ  PITSWTDVPYVGKREDIWCGSLIGTRSRATWAENIYAAINQVRAVIGKENYVDYMSSLRRYEDVLIQEDRVI
//
ID  P14403;
PN  Serine protease NS3;
GN  POLG;
OS  11076;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}.
DR  UNIPROT: P14403;
DR  UNIPROT: P08769;
DR  PDB: 4R8T;
DR  Pfam: PF01003;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01570;
DR  PROSITE: PS51527;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. Non-structural protein 4B: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN- alpha/beta pathway (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}. RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) RNA genome (By similarity). Performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:P27395, ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  SVAMKHLTSFKRELGTLIDAVNKRGRKQNKRGGNEGSIMWLASLAVVIACAGAMKLSNFQGKLLMTVNNTDIADVIVIPN
SQ  PSKGENRCWVRAIDVGYMCEDTITYECPKLTMGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVN
SQ  KKEAWLDSTKATRYLMKTENWIVRNPGYAFLAAILGWMLGSNNGQRRWYFTILLLLVAPAYSFNCLGMGNRDFIEGASGA
SQ  TWVDLVLEGDSCLTIMANDKPTLDVRMINIEAVQLAEVRSYCYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTD
SQ  RGWGNGCGLFGKGSIDTCAKFSCTSKAIGRTIQPENIKYEVGIFVHGTTTSENHGNYSAQVGASQAAKFTVTPNAPSITL
SQ  KLGDYGEVTLDCEPRSGLNTEAFYVMTVGSKSFLVHREWFHDLALPWTPPSSTAWRNRELLMEFEEAHATKQSVVALGSQ
SQ  EGGLHQALAGAIVVEYSSSVKLTSGHLKCRLKMDKLALKGTTYGMCTEKFSFAKNPADTGHGTVVIELSYSGSDGPCKIP
SQ  IVSVASLNDMTPVGRLVTVNPFVATSSANSKVLVEMEPPFGDSYIVVGRGDKQINHHWHKAGSTLGKAFSTTLKGAQRLA
SQ  ALGDTAWDFGSIGGVFNSIGKAVHQVFGGAFRTLFGGMSWITQGLMGALLLWMGVNARDRSIALAFLATGGVLVFLATNV
SQ  HADTGCAIDITRKEMRCGSGIFVHNDVEAWVDRYKYLPETPRSLAKIVHKAHKEGVCGVRSVTRLEHQMWEAVRDELNVL
SQ  LKENAVDLSVVVNKPVGRYRSAPKRLSMTQEKFEMGWKAWGKSILFAPELANSTFVVDGPETKECPDEHRAWNSIEIEDF
SQ  GFGITSTRVWLKIREESTDECDGAIIGTAVKGHVAVHSDLSYWIESRYNDTWKLERAVFGEVKSCTWPETHTLWGDGVEE
SQ  SELIIPHTIAGPKSKHNRREGYKTQNQGPWDENGIVLDFDYCPGTKVTITEDCGKRGPSVRTTTDSGKLITDWCCRSCSL
SQ  PPLRFRTENGCWYGMEIRPVRHDETTLVRSQVDAFNGEMVDPFQLGLLVMFLATQEVLRKRWTARLTIPAVLGALLVLML
SQ  GGITYTDLARYVVLVAAAFAEANSGGDVLHLALIAVFKIQPAFLVMNMLSTRWTNQENVVLVLGAAFFHLASVDLQIGVH
SQ  GILNAAAIAWMIVRAITFPTTSSVTMPVLALLTPGMRALYLDTYRIILLVIGICSLLQERKKTMAKKKGAVLLGLALTST
SQ  GWFSPTTIAAGLMVCNPNKKRGWPATEFLSAVGLMFAIVGGLAELDIESMSIPFMLAGLMAVSYVVSGKATDMWLERAAD
SQ  ISWEMDAAITGSSRRLDVKLDDDGDFHLIDDPGVPWKVWVLRMSCIGLAALTPWAIVPAAFGYWLTLKTTKRGGVFWDTP
//
ID  D7RF80;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  33743;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: D7RF80;
DR  UNIPROT: B1PMU9;
DR  UNIPROT: H8Y6L3;
DR  UNIPROT: H8Y6L4;
DR  UNIPROT: H8Y6L5;
DR  UNIPROT: Q14F58;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0046718;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKGAVLKGKGGGPPRRVPKETAKKTRQGPGRLPNGLVLMRMMGVLWHMVAGTARNPILKRFWATVPVRQAIAALRKIRK
SQ  TVGLLLDSLNKRRGKRRSTTGLLTPILLACLATLVFSATVRRERTGNMVIRAEGKDAATQVEVMNGTCTILATDMGSWCD
SQ  DSIMYECVTIDSGEEPVDVDCFCKGVERVSLEYGRCGKPAGGRNRRSVSIPVHAHSDLTGRGHKWLKGDSVKTHLTRVEG
SQ  WVWKNKFLTAAFCAVVWMVTDSLPTRFIVITVALCLAPTYATRCTHLQNRDFVSGTQGTTRVSLVLELGGCVTLTAEGKP
SQ  SVDVWLDDIHQENPAKTREYCLHAKLANSKVAARCPAMGPATLPEEHQASTVCRRDQSDRGWGNHCGLFGKGSIVACAKF
SQ  SCEAKKKATGYVYDVNKITYVVKVEPHTGDYLAANESHSNRKTASFTTQSEKTILTLGDYGDISLTCRVTSGVDPAQTVV
SQ  LELDKTAEHLPKAWQVHRDWFEDLSLPWRHGGAQEWNHADRLVEFGEPHAVKMDIFNLGDQTGILLKSLAGVPVANIEGS
SQ  KYHLQSGHVTCDVGLEKLKMKGMTYTVCEGSKFAWKRPPTDSGHDTVVMEVTYTGSKPCRIPVRAVAHGEPNVNVASLIT
SQ  PNPSMETTGGGFVELQLPPGDNIIYVGELSHQWFQKGSTIGRVLEKTRRGIERLTVVGEHAWDFGSVGGMLSSVGKALHT
SQ  AFGAAFNTIFGGVGFLPRILLGVALAWLGLNSRNPTLSVGFLITGGLVLTMTLGVGADMGCAIDANRMELRCGEGLVVWR
SQ  EVTDWYDGYAFHPESPSVLAASLKEAYEEGICGIVPQNRLEMAMWRRVEAVLNLALAESDANLTVVVDKRDPSDYRGGKV
SQ  GTLRRSGKEMKTSWKGWSQSFVWSVPEAPRRFMVGVEGAGECPLDKRRTGVFTVAEFGMGMRTKVFLDLRETASSDCDTG
SQ  VMGAAVKSGHAVHTDQSLWMRSHRNATGVFISELIVTDLRNCTWPASHTLDNAGVVDSKLFLPAGLAGPRSHYNHIPGYA
SQ  EQVKGPWSQTPLRVVREPCPGTAVKIDQSCDKRGASLRSTTESGKAIPEWCCRTCELPPVTFRSGTDCWYAMEIRPVHQQ
SQ  GGLVRSMVLADNGAMLSEGGVPGIVAVFVVLELVIRRRPTTGSSVVWCGMVVLGLVVTGLVTIEGLCRYVVAVGILMSME
SQ  LGPEIVALVLLQAVFDMRTGLLVAFAVKRAYTTREAVATYFLLLVLELGFPEASLSNIWKWADSLAMGALILQACGQEGR
SQ  TRVGYLLAAMMTQKDMVIIHTGLTIFLSAATAMAVWSMIKGQRDQKGLSWATPLAGLLGGEGVGLRLLAFRKLAERRNRR
SQ  SFSEPLTVVGVMLTVASGMVRHTSQEALCALVAGAFLLLMMVLGTRKMQLTAEWCGEVEWNPDLVNEGGEVNLKVRQDAM
SQ  GNLHLTEVEKEERAMALWLLAGLVASAFHWAGILIVLAVWTLFEMLGSGRRSELVFSGQETRTERNRPFEIKDGAYRIYS
SQ  PGLLWGHRQIGVGYGAKGVLHTMWHVTRGAALVVDEAISGPYWADVREDVVCYGGAWSLESRWRGETVQVHAFPPGRPQE
SQ  THQCQPGELILENGRKLGAVPIDLSKGTSGSPIINAQGEVVGLYGNGLKTNEAYVSSIAQGEAEKSRPEIPLSVQGTGWM
SQ  SKGQITVLDMHPGSGKTHRVLPELVRQCADRGMRTLVLAPTRVVLKEMERALAGKKVRFHSPAVEGQTTAGAIVDVMCHA
SQ  TYVHRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSLAKENRCALVLMTATPPGRGDPFPESNGAIMSEERAIPDGE
SQ  WREGFDWITEYEGRTAWFVPSISKGGAVARTLRQRGKSVICLNSKTFEKDYLRVREEKPDFVVTTDISEMGANLDVSRVI
SQ  DGRTNIKPEEVDGKVELTGTRKVTTASAAQRRGRVGRTSGRTDEYIYSGQCDDDDTSLVQWKEAQILLDNITTLRGPVAT
SQ  FYGPEQVKMPEVAGHYRLNEEKRKHFRHLMTQCDFTPWLAWHVATNTSNVLDRSWTWQGPEENAIDGADGDLVRFKTPGG
SQ  SERVLQPVWKDCRMFREGRDVKDFILYASGRRSVGDVLGGLAGVPGLLRHRCASALDVVYTLLNENPGSRAMRMAERDAP
SQ  EAFLTIVEVAVLGVATLGILWCFVARASVSRMFLGTVVLFAALFLLWIGGVDYGHMAGIALIFYTLLTVLQPEPGKQRSS
SQ  DDNRLAYFLLGLFSLAGLVTANEMGMLDKTKADLAGLVWRGEQRHPAWEEWTNVDIQPARSWGTYVLIVSLFTPYMLHQL
SQ  QTKIQQLVNSSVASGAQAMRDLGGGTPFFGVAGHVIALGVTSLVGATPMSLGLGVALAAFHLAIVASGLEAELTQRAHRV
SQ  FFSAMVKNPMVDGDVINPFPDGETKPALYERRMSLILAIALCMGSVVLNRTAASMTEAGAVGLAALGQLVHPETETLWTM
SQ  PMACGMAGLVRGSFWGLLPMGHRLWLRTTGTRRGGAEGETLGDIWKRRLNGCSREEFFQYRRSGVMETERDKARELLKRG
SQ  ETNMGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMGVKAYTIGGKGHEVPRLITSLGWNLIKFR
SQ  TGMDVYSLEAHRADTILCDIGESSPDPLAEGERSRRVILLMEKWKLRNPDASCVFKVLAPYRPEVLEALHRFQLQWGGGL
SQ  VRVPFSRNSTHEMYFSTAISGNIINSVNTQSRKLLARFGDQRGPTKVPEVDLGTGTRCVVLAEDKVREADVAERIAALKT
SQ  QYGDSWHVDKEHPYRTWQYWGSYKTEATGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKEKVDTKAQEP
SQ  QVGTKIIMRAVNDWIFERLAGKKTPRLCTREEFIAKVRSNAALGAWSDEQNRWPNAREAVEDPEFWRLVDEERERHLGGR
SQ  CAQCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRYLEFEALGFLNEDHWASRDLSGAGVEGTSLNYLGWHLKKLSELE
SQ  GGLFYADDTAGWDTRITNADLEDEEQILRYLEGEHRTLAKTILEKAYHAKVVKVARPSSSGGCVMDIITRRDQRGSGQVV
SQ  TYALNTLTNIKVQLIRMMEGEGVIGPSDSQDPRLLRVEAWLKEHGEERLTRMLVSGDDCVVRPIDDRFGKALYFLNDMAK
SQ  VRKDIGEWEPSEGYSSWEEVPFCSHHFHELTMKDGRVIIVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSY
SQ  FHRRDLRTLGLAICSAVPIDWVPQGRTTWSIHASGAWMTTEDMLEVWNRVWILDNPFMGDKGKVREWRDIPYLPKSQDGL
SQ  CSSLVGRRERAEWAKNIWGSVEKVRRMIGPERYADYLSCMDRHELHWDLKLESNII
//
ID  Q32ZD5;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  44024;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q32ZD5;
DR  PDB: 2V6I;
DR  PDB: 2V6J;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (PubMed:18004778). {ECO:0000255|PROSITE-ProRule:PRU00860, ECO:0000269|PubMed:18004778}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0046718;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTKKPGRPGRNRAVNMLKRGASRALGPMIKLKRMLFGLLDGRGPLRMVLAILAFFRFTALKPTAGLLKRWGMMDKVHALS
SQ  LLKGFKKDLASMTDFVHLPKKKSGVSIIGRMLVFSFTAAVRVTLENGMSLMKIQKADVGKVITIRTDRGENRCIVQAMDV
SQ  GEDCEDTMKYLCPAIENPSEPDDIDCWCDKADAMVTYGRCSKTRHSRRSRRSTNIAGHADSRLDSRGSVWMDTKKATSYL
SQ  TKAESWALRNPGYALVAAVLGWSLGTSNAQKVIFTVMILLIAPAYSIRCVGVENRDFIEGVSGGTWVDVVLEHGGCVTIM
SQ  APDKPTIDLELTSTIAKSMAVTRTYCVQAQVSELSVETRCPTMGEAHNSKSSDAAYVCKKGFSDRGWGNGCGLFGKGSME
SQ  TCAKFSCQTKAEGRIIQRENLEYTIHMNVHASQETGHFMNDTIASENKHGAKISITATGPSRTADLGDYGMVTLDCEPRA
SQ  GLDFDNLYLLTLGRNSWLVNRDWFHDVNLPWIGGAEGHWKNRESLVEFGKTHATKREVLALGSQEGTLQVALAGAMIAKF
SQ  GSNVATINSGHLKCRLKLDKLKIKGTTYHMCKGSFAFTKTPSDTGHGTVLLELTYSGSDGPCRVPISMSVSLSNIEPVGR
SQ  MVTVNPIVLSSSPQKTIMIEVEPPFGDSFIIAGTGEPRAHYHWRKSGSSIGAAFATTIKGARRLAVIGDDAWDFGSVGGI
SQ  LNSVGKALHQIFGGMFRTLFGGMSWFTQIMIGALCCWLGINARDRTIAVTFLAVGGVLVFLATSVNADSGCALDLKRKEF
SQ  KCGNGIFVFNDAEAWSHSYRYHPSTPKKLAGSIVRAIEEGQCGVRSVGRLEHEMWRANAREINAILLENEKNLSVVVLES
SQ  EYYRKAKNLMPIGDEMPFGWKSWGKKFFEEPQLQNQTFVVDGRVGKECPEEKRSWNNFRIEDFGFGVFTTSVWMEQRTEY
SQ  TEDCDQKVIGAAVKGELAAHSDLGYWIESRSKNGSWELERAYLLESKSCSWPATHTLWNGGVEESELIIPKSRAGPVSHH
SQ  NTRKGYHNQIKGPWHLTPLEIRFESCPGTTVVTTEECGNRGPSLRTTTTSGKVISEWCCRSCTMPPLSFRTADGCWYGME
SQ  IRPLKEREETMVKSHVSAGRGDGVDNLSLGLLVLTIALQEVMRKRILGRHITWMVIAVFMAMILGGLSYRDLGRYLVLVG
SQ  AAFAERNSGGDLLHLVLVATFKVKPMALLGFVLGGRWCRRQSLLLSIGAVLVNFALEFQGGYFELVDSLALALLFVKAVV
SQ  QTDTTSVSLPLLAALAPAGCYTVLGTHRFIMLTLVLVTFLGCKKTASVKKAGTAAVGVVLGMVGMKTIPMLGMLMVTSRA
SQ  RRSWPLHEAMAAVGILCALFGALAETEVDLAGPLAAAGLIVMAYVISGRSNDLSIKKVEDVKWSDEAEVTGESVSYHVSL
SQ  DVRGDPTLTEDSGPGLEKVLLKVGLMAISGIYPVAIPFALGAWFFLEKRCKRAGALWDIPSPREAKPAKVEDGVYRIFSR
SQ  KLFGESQIGAGVMVKGTFHTMWHVTRGAVLKAGEGLLEPAWADVRKDLICYGGNWKLEEHWDGNEEVQLIALEPGKKVRH
SQ  IQTKPGIFKTSEGEIGALDLDCMAGTSGSPIVNKNGEVVGLYGNGVLIKGDRYVSAISQKENVGQEDGAEIEDNWFRKRE
SQ  LTVLDLHPGAGKTRRVLPQLVREAVKKRLRTVILAPTRVVASEMYEALRGEPIRYMTPAVQSERTGNEIVDFMCHSTFTM
SQ  KLFQGVRVPNYNLYIMDEAHFLDPASVAARGYIETRVSMGDAGAIFMTATPPGTTEAFPPSNSPIIDEETRIPDKAWNSG
SQ  YEWIIEFDGRTVWFVHSIKQGAEIGTCLQKAGKKVLYLNRKTFESEYPKCKSEKWDFVITTDISEMGANFKADRVIDPRK
SQ  TIKPILLDGRVSMQGPIAITPASAAQRRGRIGRNPEKLGDIYAYSGNVSSDNEGHVSWTEARMLLDNVHVQGGVVAQLYT
SQ  PEREKTEAYEGEFKLKTNQRKVFSELIRTGDLPVWLAFQVASANVEYHDRKWCFDGPNEHLLLENNQEIEVWTRQGQRRV
SQ  LKPRWLDGRITSDHLNLKSFKEFASGKRSALSILDLIAVLPSHLNLRLQEALDTAAILSRSEPGSRSYKAALENSPEMIE
SQ  TFLLCALVCLMTIGLVVVLVRGKGPGKLAFGMVSIGVMTWLLWSAGVDPGKIAAAVILVFLLLVVLIPEPEKQRSVQDNQ
SQ  LAMLMLLIATILGGVAANEMGWLEKTKADLSWVVRGRSSTTTPVVELDMKPATAWTLYALATTLLTPLFQHLIVTKYANI
SQ  SLMAIASQAGTLFSMDSGIPFSSIELSVPLLALGCWTQITPCSLILACVLLSTHYAILLPGMQAQAARDAQRRTAAGIMK
SQ  NAVVDGIVATDIPPLDGAGPLTEKKLGQLLLFAAAVTGVVITRSPRSWSELGVLGSAVGSTLIEGSAGKFWNATTVTAMC
SQ  NLFRGSYLAGVPLTYTIIRNSNPSNKRGGGIGETLGEKWKARLNQMNTLEFHRYRRSHIMEVDREPARAALKSGDFTRGA
SQ  AVSRGSAKLRWMHERGYIRLHDKVVDLGCGRGGWCYYSATVKEVKEVKGYTKGGRGHEEPVLTQSYGWNIVQMKSGVDVF
SQ  YKEAEPCDVVLCDIGECSSSPAVEADRSTKVLELAERWLERNDGADFCIKVLCPYMPEVVEKLSKLQLRYGGCLVRNPLS
SQ  RNSTHEMYWVSGYKGNLIGVINSTSALLLRRMEIKFAEPRYEEDVNLSCGTRAVSIAPPKFDYKKIGQRVERLKAEHMST
SQ  WHYDCEHPYRTWAYHGSYVVKPSGSASSQVNGVVKLLSKPWDVSSEVTGMSMTDTTPFGQQRVFKEKVDTKAPEPPAGAE
SQ  MASVIVSEWLWKRLNREKKPRLCTKEEFVRKVRGNAALGPVFEEENQWKDAAEAVQDPGFWNLVDMERKNHLEGKCETCV
SQ  YNMMGKREKKRGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMSRGNSGGGVEGLGIQKLGYVMREIGEKGGILYA
SQ  DDTAGWDTRITECDLRNEAHIMEYMENEHRKLARAIFELTYKHKVVKVMRPGKGVPLMDIISREDQRGSGQVVTYALNTF
SQ  TNLVVQLIRMAEAECVLTPEDLHEMSQSAKLRLLKWLKEEGWERLTRMAVSGDDCVVAAPDARFGAALTFLNAMSKIRKD
SQ  IKEWTPSKGWKNWEEVPFCSHHFHRLQMKDGRELVVPCRSQDELIGRARVTQGPGDLMSSACLAKAYAQMWQLLYFHRRD
SQ  LRLMGNAICSAVPVDWVPTGRTTWSIHGKGEWMTSENMLEVWNRVWIEENEHMEDKTPVREWTDIPYLGKREDPWCGSYI
SQ  GYRPRSTWAENIKVPVNVIRVKIGGNKYQDYLGTQKRYESEKRVEFRGVL
//
ID  P14335;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11078;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000269|PubMed:17376919}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:9636360}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease/Helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non- covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:9636360}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000269|PubMed:29582535}. Host cytoplasm {ECO:0000269|PubMed:29582535}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles (By similarity). Shuttles between the cytoplasm and nucleus (PubMed:29582535). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:29582535}.
DR  UNIPROT: P14335;
DR  UNIPROT: Q7T4P4;
DR  UNIPROT: Q7T4P5;
DR  UNIPROT: Q82983;
DR  PDB: 1SFK;
DR  PDB: 2HCN;
DR  PDB: 2HCS;
DR  PDB: 2HFZ;
DR  PDB: 2OF6;
DR  PDB: 2QEQ;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response (PubMed:15507609, PubMed:18337583). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15650219). {ECO:0000269|PubMed:15507609, ECO:0000269|PubMed:15650219, ECO:0000269|PubMed:18337583}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15650219). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE- ProRule:PRU00859, ECO:0000269|PubMed:15650219}. [Serine protease/Helicase NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A- NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). NS3 supports the separation of RNA daughter and template strands during viral replication. The helicase part is involved in the inhibition of phosphorylation of host STAT1, and thereby inhibition of host type-I IFN signaling (By similarity). In addition, NS3 assists the initiation of replication by unwinding the RNA secondary structure in the 3' non- translated region (NTR). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15650219). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000255|PROSITE-ProRule:PRU00860, ECO:0000269|PubMed:15650219}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Induces host ER membrane rearrangements to provide a compartment where viral replication can take part (PubMed:16611922, PubMed:25771497). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15650219). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15650219, ECO:0000269|PubMed:16611922, ECO:0000269|PubMed:25771497}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN- alpha/beta pathway (PubMed:15650219). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15650219). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15650219}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:20106931, PubMed:15650160). Inhibits host JAK1 and TYK2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:15650160). May transcriptionally regulate host genes involved in antiviral response when localized in the nucleus (PubMed:33866234). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15650160, ECO:0000269|PubMed:20106931, ECO:0000269|PubMed:33866234}.
DE  Reference Proteome: No;
DE  Interaction: P02760; IntAct: EBI-11422579; Score: 0.37
DE  Interaction: Q7Z5R6; IntAct: EBI-11422628; Score: 0.37
DE  Interaction: Q9H6S1; IntAct: EBI-11422725; Score: 0.37
DE  Interaction: P54259; IntAct: EBI-11422698; Score: 0.37
DE  Interaction: Q5JU67; IntAct: EBI-11422787; Score: 0.37
DE  Interaction: Q9BZR8; IntAct: EBI-11422755; Score: 0.37
DE  Interaction: O94983; IntAct: EBI-11422832; Score: 0.37
DE  Interaction: Q96S94; IntAct: EBI-11422864; Score: 0.37
DE  Interaction: P30622; IntAct: EBI-11422942; Score: 0.37
DE  Interaction: Q12873; IntAct: EBI-11422934; Score: 0.37
DE  Interaction: Q96MT8; IntAct: EBI-11422926; Score: 0.37
DE  Interaction: Q8WXU2; IntAct: EBI-11422982; Score: 0.37
DE  Interaction: O14641; IntAct: EBI-11422974; Score: 0.37
DE  Interaction: P06733; IntAct: EBI-11423022; Score: 0.37
DE  Interaction: P63241; IntAct: EBI-11422998; Score: 0.37
DE  Interaction: Q99848; IntAct: EBI-11422990; Score: 0.37
DE  Interaction: Q03112; IntAct: EBI-11423054; Score: 0.37
DE  Interaction: Q9UJY5; IntAct: EBI-11423106; Score: 0.37
DE  Interaction: Q6ZTR7; IntAct: EBI-11423082; Score: 0.37
DE  Interaction: Q76N89; IntAct: EBI-11423138; Score: 0.37
DE  Interaction: P08238; IntAct: EBI-11423162; Score: 0.37
DE  Interaction: P08727; IntAct: EBI-11423220; Score: 0.37
DE  Interaction: Q9NPJ6; IntAct: EBI-11423284; Score: 0.37
DE  Interaction: P25963; IntAct: EBI-11423364; Score: 0.37
DE  Interaction: Q5M9Q1; IntAct: EBI-11423386; Score: 0.37
DE  Interaction: Q13232; IntAct: EBI-11423402; Score: 0.37
DE  Interaction: P11940; IntAct: EBI-11423450; Score: 0.37
DE  Interaction: Q96CV9; IntAct: EBI-11423434; Score: 0.37
DE  Interaction: Q9Y3T9; IntAct: EBI-11423418; Score: 0.37
DE  Interaction: Q9Y6X2; IntAct: EBI-11423514; Score: 0.37
DE  Interaction: Q6NSJ2; IntAct: EBI-11423498; Score: 0.37
DE  Interaction: Q5VV67; IntAct: EBI-11423538; Score: 0.37
DE  Interaction: Q9NVW2; IntAct: EBI-11423578; Score: 0.37
DE  Interaction: Q9UNM6; IntAct: EBI-11423562; Score: 0.37
DE  Interaction: Q9UIK5; IntAct: EBI-11423690; Score: 0.37
DE  Interaction: O94842; IntAct: EBI-11423743; Score: 0.37
DE  Interaction: Q9BUZ4; IntAct: EBI-11423759; Score: 0.37
DE  Interaction: P14335; IntAct: EBI-25691260; Score: 0.44
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039576;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKKPGGPGKSRAVNMLKRGMPRVLSLTGLKRAMLSLIDGRGPTRFVLALLAFFRFTAIAPTRAVLDRWRSVNKQTAMKH
SQ  LLSFKKELGTLTSAINRRSSKQKKRGGKTGIAFMIGLIAGVGAVTLSNFQGKVMMTVNATDVTDIITIPPAAGKNLCIVR
SQ  AMDVGHMCDDTITYECPVLSAGNDPEDIDCWCTKLAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLSNKKGAWMDSTKA
SQ  TRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSC
SQ  VTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSELSTKAACPTMGEAHNDKRADPSFVCKQGVVDRGWGNGCGLFGK
SQ  GSIDTCAKFACSTKATGRTILKENIKYEVAIFVHGPTTVESHGNYFTQTGAAQAGRFSITPAAPSYTLKLGEYGEVTVDC
SQ  EPRSGIDTSAYYVMTVGTKTFLVHREWFMDLNLPWSSAESNVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAI
SQ  PVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFRFLGTPADTGHGTVVLELQYTGTDGPCKIPISSVASLNDLT
SQ  PVGRLVTVNPFVSVSTANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTATLKGAQRLAALGDTAWDFGS
SQ  VGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDIS
SQ  RQELRCGSGVFIHNDVEAWIDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSIV
SQ  VEKQEGMYKSAPRRLTATTEKLEIGWKAWGKSILFAPELANNTFVIDGPETKECPTQNRAWNNLEVEDFGFGLTSTRMFL
SQ  RVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRFNDTWKLERAVLGEVKSCTWPETHTLWGDGVLESDLIIPITLAG
SQ  PRSNHNRRPGYKTQSQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDNGC
SQ  WYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRY
SQ  VILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAAFFQMAYYDARQILLWEMPDVLNSLA
SQ  VAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGFFNPMI
SQ  LAAGLVACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWEGDA
SQ  EITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMACLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKR
SQ  GDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEV
SQ  QMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPV
SQ  PAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVAREHNGN
SQ  EIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTRVELGEAAAIFMTATPPGTSDPFPESNAPISD
SQ  LQTEIPDRAWNSGYEWITEYIGKTVWFVPSVKMGNEIALCLQRAGKKVIQLNRKSYETEYPKCKNDDWDFVVTTDISEMG
SQ  ANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRTGRNPSQAGDEYCYGGHTNEDDSNCAHWTEARIM
SQ  LDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILE
SQ  DNNEVEVITKLGERKILRPRWIDARVYSDHQALKSFKDFASGKRSQIGFIEVLGKMPEHFMGKTWEALDTMYVVATAEKG
SQ  GRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGVVLGAATFFCWMAEVPGTKIAGMLLLSLLLMI
SQ  VLIPEPEKQRSQTDNQLAVFLICVLTLVGAVAANEMGWLDKTKSDISGLFGQRIETKENFSIGEFLLDLRPATAWSLYAV
SQ  TTAVLTPLLKHLITSDYITTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTSATLLFCHYAYMVP
SQ  GWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQVMLILVSLAALVVNPSVKTVREAGILITAAAV
SQ  TLWENGASSVWNATTAIGLCHIMRGGWLSCLSITWTLVKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFIRYRKEAI
SQ  TEVDRSAAKHARKERNITGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEE
SQ  PQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTLRVLEMVEDWLHRGPKEFCVKVLCPYMPKVI
SQ  EKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKKTWKGPQYEEDVNLGSGTRAVGKPLL
SQ  NSDTSKIKNRIERLRREYSSTWHHDENHPYRTWNYHGSYEVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFG
SQ  QQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPK
SQ  FWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGL
SQ  GLQKLGYILREVGTRPGGRIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTV
SQ  MDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLSENGEERLSRMAVSGDDCVV
SQ  KPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVTPCRGQDELVGRARISPGAGWN
SQ  VRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDK
SQ  TPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRSIIGDEKYVDYMSSLKRYEDTTLVEDTVL
//
ID  P29837;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  31638;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P29837;
DR  PDB: 1Z66;
DR  PDB: 2GG1;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration in host cytoplasm after hemifusion induced by surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network. Presumably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M extodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane- destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:16188985). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:16188985). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:16188985}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039651;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039576;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGKAVLKGKGGGPPRRASKVAPKKTRQLRVQMPNGLVLMRMLGVLWHALTGTARSPVLKAFWKVVPLKQATLALRKIKR
SQ  TVSTLMVGLHRRGSRRTTIDWMTPLLITVMLGMCLTATVRRERDGSMVIRAEGRDAATQVRVENGTCVILATDMGSWCDD
SQ  SLAYECVTIDQGEEPVDVDCFCRGVEKVTLEYGRCGRREGSRSRRSVLIPSHAQRDLTGRGHQWLEGEAVKAHLTRVEGW
SQ  VWKNKLFTLSLVMVAWLMVDGLLPRILIVVVALALVPAYASRCTHLENRDFVTGVQGTTRLTLVLELGGCVTVTADGKPS
SQ  LDVWLDSIYQESPAQTREYCLHAKLTGTKVAARCPTMGPATLPEEHQSGTVCKRDQSDRGWGNHCGLFGKGSIVTCVKFT
SQ  CEDKKKATGHVYDVNKITYTIKVEPHTGEFVAANETHSGRKSASFTVSSEKTILTLGDYGDVSLLCRVASGVDLAQTVVL
SQ  ALDKTHEHLPTAWQVHRDWFNDLALPWKHDGAEAWNEAGRLVEFGTPHAVKMDVFNLGDQTGVLLKSLAGVPVASIEGTK
SQ  YHLKSGHVTCEVGLEKLKMKGLTYTVCDKTKFTWKRAPTDSGHDTVVMEVGFSGTRPCRIPVRAVAHGVPEVNVAMLITP
SQ  NPTMENNGGGFIEMQLPPGDNIIYVGDLNHQWFQKGSSIGRVLQKTRKGIERLTVLGEHAWDFGSVGGVMTSIGRAMHTV
SQ  LGGAFNTLLGGVGFLPKILLGVAMAWLGLNMRNPTLSMGFLLSGGLVLAMTLGVGADVGCAVDTERMELRCGEGLVVWRE
SQ  VSEWYDNYVFHPETPAVLASAVQRAYEEEICGIVPQNRLEMAMWRSSLVELNLALAEGEANLTVVVDKADPSDYRGGVPG
SQ  LLNKGKDIKVSWRSWGRSMLWSVPEAPRRFMIGVEGGRECPFARRKTGVMTVAEFGIGLRTKVFMDLRQELTTECDTGVM
SQ  GAAVKNGMAVHTDQSLWMKSIKNDTTVTIVELIVTDLRNCTWPASHTIDNAGVVNSKLFLPASLAGPRSTYNVIPGYAEQ
SQ  VRGPWAHTPVRIKREECPGTRVTIDKACDKRGASVRSTTESGKVIPEWCCRTCELPPVTYRTGTDCWYAMEIRPVHTQGG
SQ  LVRSMVVADNGALLSEGGVPGVVALFVVLELVIRRRPATGGTVIWGGIAILALLVTGLVSVESLFRYLVAVGLVFQLELG
SQ  PEAVAMVLLQAVFEMRTCLLSGFVLRRSITTREIVTVYFLLLVLEMGIPVKGLEHLWRWTDALAMGAIIFRACTAEGKTG
SQ  IGLLLAAFMTQSDMNIIHDGLTAFLCVATTMAIWRYIRGQGERKGLTWIVPLAGILGGEGSGVRLLAFWELAASRGRRSF
SQ  NEPMTVIGVMLTLASGMMRHTSQEAVCAMALAAFLLLMLTLGTRKMQLLAEWSGNIEWNPELTSEGGEVSLRVRQDALGN
SQ  LHLTELEKEERMMAFWLVVGLIASAFHWSGILIVMGLWTISEMLGSPRRTDLVFSGCSEGRSDSRPLDVKNGVYRIYTPG
SQ  LLWGQRQIGVGYGAKGVLHTMWHVTRGAALLVDGVAVGPYWADVREDVVCYGGAWSLESRWRGETVQVHAFPPGRAHETH
SQ  QCQPGELILENGRKMGAIPIDLAKGTSGSPIMNSQGEVVGLYGNGLKTNDTYVSSIAQGEVEKSRPNLPQSVVGTGWTAK
SQ  GQITVLDMHPGSGKTHRVLPELIRQCVERRLRTLVLAPTRVVLREMERALSGKNVRFHSPAVTEQHANGAIVDVMCHATY
SQ  VNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSLAKENRCAFVLMTATPPGKSEPFPESNGAIASEERQIPDGEWR
SQ  DGFDWITEYEGRTAWFVPSIARGGAIARALRQRGKSVICLNSKTFDKEYSRVKDEKPDFVVTTDISEMGANLDVTRVIDG
SQ  RTNIKPEEVDGRIELTGTRRVTTASAAQRRGRVGRQGGRTDEYIYSGQCDDDDSGLVQWKEAQILLDNITTARGPVATFY
SQ  GPEQERMTETAGHYRLPEEKRKHFRHLLAQCDFTPWLAWHVAANVASVTDRSWTWEGPEENAVDENNGELVTFRSPNGAE
SQ  RTLRPVWRDARMFREGRDIREFVSYASGRRSVGDVLMGMSGVPALLRQRCTSAMDVFYTLMHEEPGSRAMRIGERDAPEA
SQ  FLTAVEMLVLGLATLGVVWCFVVRTSVSRMVLGTLVLATSLIFLWAGGVGYGNMAGVALVFYTLLTVLQPETGKQRSSDD
SQ  NKLAYFLLTLCGLAGMVAANEMGLLEKTKADLAALFARDQGETVRWGEWTNLDIQPARSWGTYVLVVSLFTPYMLHQLQT
SQ  RIQQLVNSAVASGAQAMRDLGGGTPFFGVAGHVLALGVASLVGATPTSLILGVGLAAFHLAIVVSGLEAELTQRAHKVFF
SQ  SAMVRNPMVDGDVINPFGDGEAKPALYERKLSLILALVLCLASVVMNRTFVAVTEAGAVGVAAAMQLLRPEMDVLWTMPV
SQ  ACGMSGVVRGSLWGLLPLGHRLWLRTTGTRRGGSEGDTLGDMWKARLNSCTKEEFFAYRRAGVMETDREKARELLKRGET
SQ  NMGLAVSRGTSKLAWMEERGYVTLKGEVVDLGCGRGGWSYYAASRPAVMSVRAYTIGGKGHESPRMVTSLGWNLIKFRAG
SQ  MDVFSMEPHRADAILCDIGESNPDAVVEGERSRRVILLMEQWKNRNPTATCVFKVLAPYRPEVIEALHRFQLQWGGGLVR
SQ  TPFSRNSTHEMYFSTAITGNIVNSVNIQSRKLLARFGDQRGPTRVPEIDLGVGTRSVVLAEDKVKEKDVMERIQALKDQY
SQ  CDTWHEDHEHPYRTWQYWGSYKTAATGSSASLLNGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKDKVDTKAQEPQP
SQ  GTKIIMRAVNDWLLERLVKKSRPRMCSREEFIAKVRSNAALAAWSDEQNKWKSAREAVEDPEFWSLVEAERERHLQGRCA
SQ  HCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRFLEFEALGFLNEDHWASRASSGAGVEGISLNYLGWHLKKLASLSGG
SQ  LFYADDTAGWDTRITNADLDDEEQILRYMDGDHKKLAATVLRKAYHAKVVRVARPSREGGCVMDIITRRDQRGSGQVVTY
SQ  ALNTITNIKVQLVRMMEGEGVIEVADSHNPRLLRVEKCVEEHGEERLSRMLVSGDDCVVRPVDDRFSKALYFLNDMAKTR
SQ  KDTGEWEPSTGFASWEEVPFCSHHFHELVMKDGRALVVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSYFH
SQ  RRDLRTLGFAICSAVPVDWVPTGRTTWSIHASGAWMTTEDMLEVWNRVWIYDNPFMEDKTRVDEWRDTPYLPKSQDILCS
SQ  SLVGRGERAEWAKNIWGAVEKVRRMIGPEHYRDYLSSMDRHDLHWELKLESSIF
//
ID  P22338;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11086;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P22338;
DR  UNIPROT: O10383;
DR  PDB: 6J5C;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGRKTILKGKGGGPPRRVSKETATKTRQSRVQMPNGLVLMRMMGILWHAVAGTARNPVLKAFWNSVPLRQATAALRKIKR
SQ  TVSALMVGLQRRGKRRSVTNWMNWLLVIALLGMTLAATVRKEGDGTTVIRAEGRDAATQVRVENGTCVILATDMGSWCDD
SQ  SLSYECVTIEQGEEPVDVDCFCRNVDGVYLEYGRCGKQEGSRTRRSVLIPTHAQGELTGRGRKWLEGDSLRTHLTRVEGW
SQ  VWKNKLLALAMVAVVWLALESVVTRVAVLVVLLCLAPVYASRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPS
SQ  MDVWLDAIYQESPAKTREYCLHAKLSETKVAARCPTMGPAVLTEERQIGTVCKRDQSDRGWGNHCGLFGKGSIVACVKAA
SQ  CEAKKKATGYVYDANKIVYTVKVEPHTGDYVAANETHKGRKTATFTVSSEKTILTLGEYGDVSLLCRVASGVDLAQTIIL
SQ  ELDKTAEHLPTAWQVHRDWFNDLALPWKHDGNPHWNNAERLVEFGAPHAVKMDVYNLGDQTGVLLRALAGVPVAHIEGNK
SQ  YHLKSGHVTCEVGLEKLKMKGLTYTMCDKSKFAWKRTPTDSGHDTVVMEVTFSGSKPCRIPVRAVAHGSPDVNVAMLITP
SQ  NPTIENDGGGFIEMQLPPGDNIIYVGELSHQWFQTGSSIGRVFQTTRKGIERLTVIGEHAWDFGSAGGFFGSIGKAVHTV
SQ  LGGAFNSIFGGVGFLPKLLMGVALAWLGLNTRNPTMSMSFLLAGGLVLAMTLGVGADVGCAVDTERMELRCGEGLVVWRE
SQ  VSEWYDNYAYYPETPGALASAVKEAFEEGSCGVVPQNRLEMAMWRSSVTELNLALVEGDANLTVVVDKNDPTDYRGGVPG
SQ  TLKKGKDMKVSWRSWGHSMIWSIPEAPRRFMVGTEGQSECPLERRKTGVFTVAEFGVGLRTKVFLDFRQEPTHECDTGVM
SQ  GAAVKNDMAVHTDQSLWMKSMRNDTGTYIVELLVTDLRNCSWPASHTIDNADVVNSELFLPASLRGPRSWYNRIPGYSEQ
SQ  VKGPWKHTPLRVIREECPGTTVTINAKCEKRGASVRSTTESGKVIPEWCCRACTMPPVTFRTGTDCWYAMEIRPVHAQGG
SQ  LVRSMVVADNGELLSEGGVPGIVALFVVLECIIRRRPSTGVTVVWGGVVVLALLVTGMVRIESLVRYVVAVGIAFHLELG
SQ  PETVALMLLQAVFELRVGLLSAFALRRGLTVREMVTTYFLLLVLELGLSSAGLGDLWKWSDALAMGALIFRACTAEGKTG
SQ  TGLLLIALMTQRDVVTVHHGLVCFLAAAAACSVWRLLRGHREQKGLTWIIPLARLLGGEGSVIRLLAFWELAAHRGRRSF
SQ  SEPLTVVVVMLTLASGMMRHTSQEALCALAVASFFLLMLVSGTRKMQLVAEWSGCVEWHPETVNEGGEISLRVRQDSMGN
SQ  FHLTELEKEERMMAFWLLAGLVASALHWSGILGVMGLWTLTEIMRSSRRSDLVYSGQGGQERGDRPFEVKDGVYRIFSPG
SQ  LFWGQRQVGVGYGHKGVLHTMWHVTRGAALSIDDAVAGPYWADVKEDVVCYGGAWSLEEKWKGETVQVHAFPPGRAHEVH
SQ  QCQPGELILDTGKRLGAIPIDLAKGTSGSPILNAQGVVVGLYGNGPKTNESYVSSIAQGEAEKSRPNLPQAVVGTGWTSK
SQ  GQITVLDMHPGSGKTHRVLPELIRQCIDRRLSTLVLAPTRVVLKEMERALSGKRVRFHSPAVSDQQAGGAIVDVMCHATY
SQ  VNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYTLAKENKCALVLMTATPPGKSEPFPESNGAITSEERQIPDGEWR
SQ  DGFDWITEYEGRTAWFVPSIAKGGVIARTLRQKGKSVICLNSKTFEKDYSRVREEKPDFVVTTDISEMGANLDVSRVIDG
SQ  RTNIKPEEVDGKVELTGTRRVTTASAAQRRGRVGRQDGRTDEYIYSGQCDDDDSGLVQWKEAQILLDNITTLRGPVATFY
SQ  GPEQDKMPEVAGHFRLTEEKRKHFRHLLTHCDFTPWLAWHVAANVSSVTDRSWTWEGPEANAVDEASGDLVTFRSPNGAE
SQ  RTLRPVWRDARMFREGRDIKEFVAYASGRRSFGDVLTGMSGVPELLRHRCVNALDVFYTLMHEEPGSRAMKMAERDAPEA
SQ  FLTVVEMMVLGLATLGVVWCFVVRTSISRMMLGTLVLLASLLLLWAGGVGYGNMAGVALIFYTLLTVLQPETGKQRSSDD
SQ  NKLAYFLLTLCSLAGLVAANEMGFLEKTKADLSAMLWSGHEEHRQWSEWTNVDIQPARSWGTYVLVVSLFTPYIIHQLQT
SQ  KIQQLVNSAVASGAQAMRDLGGGAPFFGVAGHVMTLGVVSLVGATPTSLIVGIGLAAFHLAIVVSGLEAELTQRAHKVFF
SQ  SAMVRNPMVDGDVINPFGEGEAKPALYERKMSLVLAIVLCLVSVVMNRTVASMTEAAAVGLAATGQLLRPEADTLWTMPV
SQ  ACGMSGVVRGSLWGFLPLGHRLWLRASGGRRGGSDGDTLGDLWKRRLNNCTKEEFFVYRRTGILETERDKARELLRRGET
SQ  NMGLAVSRGTAKLAWLEERGYRTLKGEVVDLGCGRGGWSYYAASRPAVMSVRAYTIGGRGHEVPKMVTSLGWNLIRFRSG
SQ  MDVFSMQPHRADTIMCDIGESNPDAAVEGERTRKVISLMEQWKIRNPAAACVFKVLAPYRPEVIEALHRFQLQWGGGLVR
SQ  TPFSRNSTHEMYYSTAVTGNIVNSVNIQSRKLLARFGDQRGPTKVPEADLGVGTRCVVLAEDKVKEQDVQERIRALRKQY
SQ  SETWHMDEEHPYRTWQYWGTSRTAPTGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKEKVDTKAQEPQP
SQ  GTRVITRAVNDWILERLAQKSKPRMCSREEFIAKVRSNAALGAWSDEQNRWASAREAVVVPAFWALVDEVRERHLVGWCA
SQ  HCVYIMMGMREKKLGEFGVAKGSRAIWYMWLGSRFLEFEALGFLNKDHWASRESSGGGVEGISLNYLGWHLKKLTTLNGG
SQ  LFYADDTAGWDTKGTNSDPEDEEQILRYMEGEHKQLATTIMQKAYHAKVVKVARPSRDGGCIMDVITRRDQRGSGQVVTY
SQ  ALNTLTNIKVQSTRMMEGEGVIEAEDAHNPRLLRVERWLKEHGEERLGRMLVSGDDCVVRPIDDRFGKALYFLNDMAKTR
SQ  KDMGEWEPSAGFSSWEEVPFCSHHFHELVMKDGRTLVVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSYFH
SQ  RRDLRTLGFAISPAVPVDWVPTGRTTWSIHASGAWMTTEDMLDVWNRVWILDNPFMQNKERIMEWRDVPYLPKTQDMICS
SQ  SLVGRKERAEWAKNIWGAVEKVRKMIGPERFKDYLSCMDRHDLHWELKLESSII
//
ID  P05769;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  301478;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P05769;
DR  UNIPROT: Q9Q9F7;
DR  PDB: 2PX2;
DR  PDB: 2PX4;
DR  PDB: 2PX5;
DR  PDB: 2PX8;
DR  PDB: 2PXA;
DR  PDB: 2PXC;
DR  PDB: 2V8O;
DR  PDB: 2WV9;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860, ECO:0000269|PubMed:19793813}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKKPGGPGKPRVVNMLKRGIPRVFPLVGVKRVVMNLLDGRGPIRFVLALLAFFRFTALAPTKALMRRWKSVNKTTAMKH
SQ  LTSFKKELGTLIDVVNKRGKKQKKRGGSETSVLMLIFMLIGFAAALKLSTFQGKIMMTVNATDIADVIAIPTPKGPNQCW
SQ  IRAIDIGFMCDDTITYECPKLESGNDPEDIDCWCDKQAVYVNYGRCTRARHSKRSRRSITVQTHGESTLVNKKDAWLDST
SQ  KATRYLTKTENWIIRNPGYALVAVVLGWMLGSNTGQKVIFTVLLLLVAPAYSFNCLGMSSRDFIEGASGATWVDLVLEGD
SQ  SCITIMAADKPTLDIRMMNIEATNLALVRNYCYAATVSDVSTVSNCPTTGESHNTKRADHNYLCKRGVTDRGWGNGCGLF
SQ  GKGSIDTCAKFTCSNSAAGRLILPEDIKYEVGVFVHGSTDSTSHGNYSTQIGANQAVRFTISPNAPAITAKMGDYGEVTV
SQ  ECEPRSGLNTEAYYVMTIGTKHFLVHREWFNDLLLPWTSPASTEWRNREILVEFEEPHATKQSVVALGSQEGALHQALAG
SQ  AIPVEFSSSTLKLTSGHLKCRVKMEKLKLKGTTYGMCTEKFTFSKNPADTGHGTVVLELQYTGSDGPCKIPISSVASLND
SQ  MTPVGRMVTANPYVASSTANAKVLVEIEPPFGDSYIVVGRGDKQINHHWHKEGSSIGKAFSTTLKGAQRLAALGDTAWDF
SQ  GSVGGVFNSIGKAVHQVFGGAFRTLFGGMSWISPGLLGALLLWMGVNARDKSIALAFLATGGVLLFLATNVHADTGCAID
SQ  ITRRELKCGSGIFIHNDVEAWIDRYKYLPETPKQLAKVVENAHKSGICGIRSVNRFEHQMWESVRDELNALLKENAIDLS
SQ  VVVEKQKGMYRAAPNRLRLTVEELDIGWKAWGKSLLFAAELANSTFVVDGPETAECPNSKRAWNSFEIEDFGFGITSTRG
SQ  WLKLREENTSECDSTIIGTAVKGNHAVHSDLSYWIESGLNGTWKLERAIFGEVKSCTWPETHTLWGDAVEETELIIPVTL
SQ  AGPRSKHNRREGYKVQVQGPWDEEDIKLDFDYCPGTTVTVSEHCGKRGPSVRTTTDSGKLVTDWCCRSCTLPPLRFTTAS
SQ  GCWYGMEIRPMKHDESTLVKSRVQAFNGDMIDPFQLGLLVMFLATQEVLRKRWTARLTLPAAVGALLVLLLGGITYTDLV
SQ  RYLILVGSAFAESNNGGDVIHLALIAVFKVQPAFLVASLTRSRWTNQENLVLVLGAAFFQMAASDLELTIPGLLNSAATA
SQ  WMVLRAMAFPSTSAIAMPMLAMLAPGMRMLHLDTYRIVLLLIGICSLLNERRRSVEKKKGAVLIGLALTSTGYFSPTIMA
SQ  AGLMICNPNKKRGWPATEVLTAVGLMFAIVGGLAELDIDSMSVPFTIAGLMLVSYVISGKATDMWLERAADVSWEAGAAI
SQ  TGTSERLDVQLDDDGDFHLLNDPGVPWKIWVLRMTCLSVAAITPRAILPSAFGYWLTLKYTKRGGVFWDTPSPKVYPKGD
SQ  TTPGVYRIMARGILGRYQAGVGVMHEGVFHTLWHTTRGAAIMSGEGRLTPYWGNVKEDRVTYGGPWKLDQKWNGVDDVQM
SQ  IVVEPGKPAINVQTKPGIFKTAHGEIGAVSLDYPIGTSGSPIVNSNGEIIGLYGNGVILGNGAYVSAIVQGERVEEPVPE
SQ  AYNPEMLKKRQLTVLDLHPGAGKTRRILPQIIKDAIQKRLRTAVLAPTRVVAAEMAEALRGLPVRYLTPAVQREHSGNEI
SQ  VDVMCHATLTHRLMSPLRVPNYNLFVMDEAHFTDPASIAARGYIATRVEAGEAAAIFMTATPPGTSDPFPDTNSPVHDVS
SQ  SEIPDRAWSSGFEWITDYAGKTVWFVASVKMSNEIAQCLQRAGKRVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGAN
SQ  FGASRVIDCRKSVKPTILDEGEGRVILSVPSAITSASAAQRRGRVGRNPSQIGDEYHYGGGTSEDDTMLAHWTEAKILLD
SQ  NIHLPNGLVAQLYGPERDKTYTMDGEYRLRGEERKTFLELIKTADLPVWLAYKVASNGIQYNDRKWCFDGPRSNIILEDN
SQ  NEVEIITRIGERKVLKPRWLDARVYSDHQSLKWFKDFAAGKRSAIGFFEVLGRMPEHFAGKTREALDTMYLVATSEKGGK
SQ  AHRMALEELPDALETITLIAALGVMTAGFFLLMMQRKGIGKLGLGALVLVVATFFLWMSDVSGTKIAGVLLLALLMMVVL
SQ  IPEPEKQRSQTDNQLAVFLICVLLVVGLVAANEYGMLERTKTDIRNLFGKSLIEENEVHIPPFDFFTLDLKPATAWALYG
SQ  GSTVVLTPLIKHLVTSQYVTTSLASINAQAGSLFTLPKGIPFTDFDLSVALVFLGCWGQVTLTTLIMATILVTLHYGYLL
SQ  PGWQAEALRAAQKRTAAGIMKNAVVDGIVATDVPELERTTPQMQKRLGQILLVLASVAAVCVNPRITTIREAGILCTAAA
SQ  LTLWDNNASAAWNSTTATGLCHVMRGSWIAGASIAWTLIKNAEKPAFKRGRAGGRTLGEQWKEKLNAMGKEEFFSYRKEA
SQ  ILEVDRTEARRARREGNKVGGHPVSRGTAKLRWLVERRFVQPIGKVVDLGCGRGGWSYYAATMKNVQEVRGYTKGGPGHE
SQ  EPMLMQSYGWNIVTMKSGVDVFYKPSEISDTLLCDIGESSPSAEIEEQRTLRILEMVSDWLSRGPKEFCIKILCPYMPKV
SQ  IEKLESLQRRFGGGLVRVPLSRNSNHEMYWVSGASGNIVHAVNMTSQVLIGRMDKKIWKGPKYEEDVNLGSGTRAVGKGV
SQ  QHTDYKRIKSRIEKLKEEYAATWHTDDNHPYRTWTYHGSYEVKPSGSASTLVNGVVRLLSKPWDAITGVTTMAMTDTTPF
SQ  GQQRVFKEKVDTKAPEPPQGVKTVMDETTNWLWAYLARNKKARLCTREEFVKKVNSHAALGAMFEEQNQWKNAREAVEDP
SQ  KFWEMVDEERECHLRGECRTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWMSRENSGGGVEG
SQ  AGIQKLGYILRDVAQKPGGKIYADDTAGWDTRITQADLENEAKVLELMEGEQRTLARAIIELTYRHKVVKVMRPAAGGKT
SQ  VMDVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEAVIGPDDIESIERKKKFAVRTWLFENAEERVQRMAVSGDDCV
SQ  VKPLDDRFSTALHFLNAMSKVRKDIQEWKPSQGWYDWQQVPFCSNHFQEVIMKDGRTLVVPCRGQDELIGRARISPGSGW
SQ  NVRDTACLAKAYAQMWLVLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLSVWNRVWILENEWMED
SQ  KTTVSDWTEVPYVGKREDIWCGSLIGTRTRATWAENIYAAINQVRSVIGKEKYVDYVQSLRRYEETHVSEDRVL
//
ID  Q7T6D2;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  12542;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q7T6D2;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0046718;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGKAILKGKGGGPPRRVSKETAKKTRQRVVQMPNGLVLKRIMEILWHAMVGTARSPLLKSFWKVVPLKQAMAALRKIKK
SQ  AVSTLMIGLQKRGKRRSTTDWTGWLLVAMLLSIALAATVRKEGDGTTVIRAEGKDAATQVRVENGTCVILATDMGAWCED
SQ  SLSYECVTIDQGEEPVDVDCFCRNVDRVYLEYGRCGKQEGTRSRRSVLIPSHAQKDLTGRGQRWLEGDTIRSHLTRVEGW
SQ  VWKNKSLTLAVVVIVWMTVESAVTRIVIVSALLCLAPAYASRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPS
SQ  MDVWLDSIYQENPAKTREYCLHAKLSNTKVAARCPAMGPATLDEEHQSGTVCKRDQSDRGWGNHCGLFGKGSIVTCVKAS
SQ  CEAKKKATGHVYDANKIVYTVKVEPHTGNYVAANETHSGRKTALFTVSSEKTILTMGEYGDVSLMCRVASGVDLAQTVVL
SQ  ELDKTAEHLPTAWQVHRDWFNDLALPWKHEGMVGWNNAERLVEFGVPHAVKMDVYNLGDQTGVLLKSLAGAPLAHIEGTK
SQ  YHLKSGHVTCEVGLEKLKMKGLTYTMCDKAKFTWKRAPTDSGHDTVVMEVAFSGTKPCRIPVRAVAHGSPDVDVAMLITP
SQ  NPTIENNGGGFIEMQLPPGDNIIYVGELKHQWFQKGSSIGRVFQKTRKGIERLTVLGEHAWDFGSTGGFLSSIGKALHTV
SQ  LGGAFNSVFGGVGFLPRILLGISLAWLGLNMRNPTMSMSFLLAGGLVLTMTLGVGADVGCAVDTERMELRCGEGLVVWRE
SQ  VSEWYDNYAFYPETPAALASALKEMVEEGDCGIVPQNRLEMAMWRSSVSELNLALAEGDANLTVVVDKHDPTDYRGGVPG
SQ  LLKKGKDMKISWKSWGQSMIWSVPEAPRRFLVGTEGSSECPLAKRRTGVFTVAEFGMGLRTKVFLDFRQEITRECDTGVM
SQ  GAAVKNGIAVHTDQSLWMKSIRNETGTYIVELLVTDLRNCSWPASHTIDNADVVDSELFLPASLAGPRSWYNRIPGYSEQ
SQ  VRGPWKYTPIKITREECPGTKVAIDASCDKRGASVRSTSESGKIIPEWCCRKCTLPPVTFRTGTDCWYAMEIRPVHDQGG
SQ  LVRSMVVADNGELLSEGGIPGIVAVFVVLEYIIRKRPSAGLTVVWGGVVVLALLVTGMVTLQSMLRYVIAVGVTFHLELG
SQ  PEIVALMLLQAVFELRVGLLGAFVLRRSLTTREVVTIYFLLLVLELGLPSANLEALWGWADALAMGAMIFRACTAEGKTG
SQ  LGLLLVALMTQQNAVIVHQGLVIFLSVASACSVWKLLRGQREQKGLSWIVPLAGRLGGKGSGIRLLAFWELASRRDRRSF
SQ  SEPLTVVGVMLTLASGMMRHTSQEALCALAAASFLLLMLVLGTRKMQLVAEWSGCVEWHPDLADEGGEISLRVRQDALGN
SQ  FHLTELEKEERMMAFWLLAGLTASALHWTGILVVMGLWTMSEMLRSARRSDLVFSGQSGSERGSQPFEVRDGVYRILSPG
SQ  LLWGHRQVGVGFGSKGVLHTMWHVTRGAAIFIDNAVAGPYWADVKEDVVCYGGAWSLEEKWKGEKVQVHAFPPGRAHEVH
SQ  QCQPGELVLDTGRRIGAIPIDLAKGTSGSPILNAQGAVVGLYGNGLRTNETYVSSIAQGEVEKSRPNLPQAVVGTGWTSK
SQ  GTITVLDMHPGSGKTHRVLPELIRQCIDKRLRTLVLAPTRVVLKEMERALSGKRVRFHSPAVGDQQTGNAIVDVMCHATY
SQ  VNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSMAKENKCALVLMTATPPGKSEPFPESNGAITSEERQIPEGEWR
SQ  DGFDWITEYEGRTAWFVPSIAKGGVIARTLRQKGKSVICLNSKTFEKDYSRVRDEKPDFVVTTDISEMGANLDVSRVIDG
SQ  RTNIKPEEVDGKVELTGTRRVTTASAAQRRGRVGRHDGRTDEYIYSGQCDDDDSGLVQWKEAQILLDNITTLRGPVATFY
SQ  GPEQDKMPEVAGHFRLTEERRKHFRHLLTHCDFTPWLAWHVAANVSNVTSRSWTWEGPEENAVDEANGDLVTFKSPNGAE
SQ  RTLRPVWRDARMFKEGRDIREFVAYASGRRSLGDMLTGMSGVPELLRHRCMSAMDVFYTLLYEEPGSRAMKMAERDAPEA
SQ  FLTMVEMVVLGLATLGAVWCLVLRTSISRMMLGTMVLLVSLALLWAGGVGYGSMAGVALVFYTLLTVLQPEAGKQRSSDD
SQ  NKLAYFLLTLCSLAGLVAANEMGFLEKTKADLSAVLWSEREEPRVWSEWTNIDIQPAKSWGTYVLVVSLFTPYIIHQLQT
SQ  RIQQLVNSAVASGAQAMRDLGGGTPFFGVAGHVLTLGVVSLVGATPTSLVVGVGLAAFHLAIVVSGLEAELTQRAHKVFF
SQ  SAMVRNPMVDGDVINPFGDGEVKPALYERKMSLILAMILCFMSVVLNRTVPAVTEASAVGLAAAGQLIRPEADTLWTMPV
SQ  ACGLSGVVRGSLWGFLPLGHRLWLRTSGTRRGGSEGDTLGDLWKRRLNNCTKEEFFAYRRTGILETERDKARELLKKGET
SQ  NMGLAVSRGTAKLAWLEERGYVNLKGEVVDLGCGRGGWSYYAASRPAVMGVKAYTIGGKGHEVPRMVTSLGWNLIKFRAG
SQ  MNVFTMQPHRADTVMCDIGESSPDAAIEGERTRKVILLMEQWKNRNPTAACVFKVLAPYRPEVIEALHRFQLQWGGGLVR
SQ  TPFSRNSTHEMYYSTAISGNIVNSVNVQSRKLLARFGDQRGPIRVPEMDLGVGTRCVVLAEDKVKEHDVQERIKALQEQY
SQ  SDTWHVDREHPYRTWQYWGSYRTAPTGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKDKVDTKAQEPQP
SQ  GTRVIMRAVNDWMFERLARRSRPRMCSREEFIAKVKANAALGAWSDEQNKWASAKEAVEDPAFWHLVDEERERHLKGRCA
SQ  HCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRFLEFEALGFLNEDHWASRESSGAGVEGISLNYLGWHLKKLSLLEGG
SQ  LFYADDTAGWDTRVTNADLEDEEQILRYMEGEHKQLAATVMQKAYHAKVVKVARPSRDGGCIMDVITRRDQRGSGQVVTY
SQ  ALNTLTNIKVQLIRMMEGEGVIEATDSHNPRLLRVERWLRDHGEERLGRMLISGDDCVVRPIDDRFSKALYFLNDMAKTR
SQ  KDIGEWEHSAGFSSWEEVPFCSHHFHELVMKDGRTLVVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSYFH
SQ  RRDLRTLGFAICSAVPKDWVPTGRTTWSVHASGAWMTTENMLDVWNRVWILDNPFMENKEKVGEWRDIPYLPKSQDMMCS
SQ  SLVGRRERAEWAKNIWGAVEKVRKMLGPERYSDYLSCMDRHELHWELKVESSII
//
ID  Q04538;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  39008;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q04538;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MMTTSKGKGGGPPRRKLKVTANKSRPATSPMPKGFVLSRMLGILWHAVTGTARPPVLKMFWKTVPLRQAEAVLKKIKRVI
SQ  GNLMQSLHMRGRRRSGVDWTWIFLTMALMTMAMATTIHRDREGYMVMRASGRDAASQVRVQNGTCVILATDMGEWCEDSI
SQ  TYSCVTIDQEEEPVDVDCFCRGVDRVKLEYGRCGRQAGSRGKRSVVIPTHAQKDMVGRGHAWLKGDNIRDHVTRVEGWMW
SQ  KNKLLTAAIVALAWLMVDSWMARVTVILLALSLGPVYATRCTHLENRDFVTGTQGTTRVSLVLELGGCVTITAEGKPSID
SQ  VWLEDIFQESPAETREYCLHAKLTNTKVEARCPTTGPATLPEEHQANMVCKRDQSDRGWGNHCGFFGKGSIVACAKFECE
SQ  EAKKAVGHVYDSTKITYVVKVEPHTGDYLAANETNSNRKSAQFTVASEKVILRLGDYGDVSLTCKVASGIDVAQTVVMSL
SQ  DSSKDHLPSAWQVHRDWFEDLALPWKHKDNQDWNSVEKLVEFGPPHAVKMDVFNLGDQTAVLLKSLAGVPLASVEGQKYH
SQ  LKSGHVTCDVGLEKLKLKGTTYSMCDKAKFKWKRVPVDSGHDTVVMEVSYTGSDKPCRIPVRAVAHGVPAVNVAMLITPN
SQ  PTIETNGGGFIEMQLPPGDNIIYVGDLSQQWFQKGSTIGRMFEKTRRGLERLSVVGEHAWDFGSVGGVLSSVGKAIHTVL
SQ  GGAFNTLFGGVGFIPKMLLGVALVWLGLNARNPTMSMTFLAVGALTLMMTMGVGADYGCAIDPERMEIRCGEGLVVWKEV
SQ  SEWYDGYAYHPESPDTLAQALREAFERGVCGVVPQNRLEMAMWRSTAPELNLVLSEGEANLTIVVDKTDPADYRGGTPMV
SQ  LKKTGKESKVSWKSWGKSILWSVPDSPRRMMMGVDGVGECPLYRRATGVFTVAEFGVGLRTKVFLDLRGEASKECDTGVM
SQ  GAAVKNGKAIHTDQSMWMSSFRNDTGTYIHELILTDLRNCTWPASHTIDNDGVLDSHLFLPVTLAGPRSKYNRIPGYSEQ
SQ  VRGPWDQTPLRVVRDHCPGTSVRIDSHCDKRGASVRSTTESGKIIPEWCCRACELPPVTFRSGTDCWYAMEIRPVHSQGG
SQ  LVRSMVVADNGALLSEGGVPGLVAVFVLMEFLLRRRPGSVTSILWGGILMLGLLVTGLVRVEEIVRYVIAVGVTFHLELG
SQ  PETMVLVMLQAVFNMRTCYLMGFLVKRVITTREVVTVYFLLLVLEMGIPEMNFGHLWEWADALAMGLLIIKASAMEDRRG
SQ  LGFLLAGLMTQRHLVAVHHGLMVFLTVALAVVGRNIYNGQKERKGLCFTVPLASLLGGSGSGLRMLALWECLGGRGRRSL
SQ  SEPLTVVGVMLAMASGLLRHSSQEALLALSAGSFLILMLILGTRRLQLTAEWAGVVEWNPELVNEGGEVSLKVRQDAMGN
SQ  LHLTEVEREERRLALWLVFGLLASAYHWSGILVTMGAWTVYELFSSTRRTDLVFSGQLPDQGEKRSFDIKEGVYRIYAPG
SQ  LFWGYRQIGVGYGTKGVLHTMWHVTRGAALSVEGATSGPYWADVREDVVCYGGAWGLDKKWGGEVVQVHAFPPDSGHKIH
SQ  QCQPGKLNLEGGRVLGAIPIDLPRGTSGSPIINAQGDVLGLYGNGLKSNDVYISSIAQGNVEKSRPEMPLAVQGGKWTSK
SQ  GSITVLDMHPGSGKTHRVLPELIRECIDKRLRTVVLAPTRVVLKEMERALQGKRVKFHSAAVDNASSSSGAIVDVMCHAT
SQ  YVNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSLAKENRCALVLMTATPPGKSEAFPESKGAIVSEEKPIPEGEW
SQ  RDGFDWITEFEGRTAWFVPSIAKGGAIARTLRQKGKSVICLNSKTFDKDYGRVHEEKPDFVVTTDISEMGANLDVNRVID
SQ  GRTNIKPEEIDGKVELIGTRRVTTASAAQRRGRVGRHEGRTDLYVYSGQCDDDDSSLVQWKEAQILLDNITTVRGPVATF
SQ  YGPEQGKMLEVAGHFRLTEEKRKHFRHLLTNCDFTPWLAWHVAANTACVTDRKWTWEGPDENAIDGPGGELVTFRSPNGA
SQ  ERKLKPIWKDSRMFREGRDVADFIQYASGRRSAVDILTGLGGVPDLLRLRCTAAWDVVYTLLNETPGSRAMKMAERDAPE
SQ  AMLTLLEVAVLGIATLGVVWCFIVRTSVSRMVLGTLVLAVALILLWLGGMDYGTMAGVALIFYLLLTVLQPEPGKQRSGE
SQ  DNRLAFLLIGLGSVVGLVAANELGYLEQTKTDISGLFRREDQGGMVWDAWTNIDIQPARSWGTYVLIVSLFTPYMLHQLQ
SQ  TKIQRLVNSSVAAGTQAMRDLGGGTPFFGVAGHVVALGVTSLVGATPTSLALGVALAALHLAVVTSGLEAELTQRAHRAF
SQ  FSAMVKNPMVDGEIINPIPDGDPKPALYERKMSLFLAIGLCIAAVALNRTAAAMTEAGAVAVAALGQLLRPEEESWWTMP
SQ  MACGMAGLVRGSLWGLLPVLHRIWLRTQGARRGGAEGSTLGDIWKQRLNSCTKEEFFAYRRTGVMETNRDQARELLRRGE
SQ  TNMGLAVSRGCAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPSVMAVRAYTIGGKGHEAPRLVTSLGWNLIKFRS
SQ  GMDVFSMATTRADTILCDIGESSPDPEKEGARSRRVILLMEQWKARNPDAAAVFKVLAPYRPEVLEALHRFQLQWGGGLV
SQ  RVPFSRNSTHEMYYSTAVTGNLVNSVNVLSRKLLARFGETRGPIQVPEIDLGTGTRCVTLAEDKVKPRDVAERIGALREQ
SQ  YSESWHEDKEHPYRTWQYWGSYRTPATGSAASLINGVVKLLSWPWNAREDVTRMAMTDTTAFGQQRVFKEKVDTKAQEPQ
SQ  PGTRVIMRAVSDWLLEHLSRRAKVRMCTKDEFIAKVRSNAALGAWSDEQNKWSSAKEAVEDPEFWKLVDEERSRHLKGQC
SQ  RHCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRFLEFEVLGFLNEEHWASREVSGAGVEGTSLNYLGWLLRELGMKDG
SQ  GKLYADDTAGWDTRITNADLEDEEQILRYMEGEHHVLAKTILEKAYHAKVVKVARPSPQGGCVMDVITRRDQRGSGQVVT
SQ  YALNTITNMKVQLIRMMEGEGVIGPADSQDPRLKRVETWLKEHGVERLGRMLVSGDDCVVKPIDDRFGKALYFLNDMAKV
SQ  RKDVGEWEPSMGFTEWEEVPFCSHHFHELVMKDGRSLIVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLNYF
SQ  HRRDLRTLGFAICSAVPVSWVPMGRTTWSIHASGEWMTTEDMLRIWNKVWILDNPHMEDKQTVDEWRDIPYLPKTQDLVC
SQ  SSLVGRKERAEWAKNIWGSVEKVRKLIGPEDYRDYLSSMDRHDLHWELKLESSII
//
ID  Q32ZD4;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  64315;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q32ZD4;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKKPGGPAGRRVVNMLKRPASVSPIKGIKRLIGNLTDGRGPLRVVLAFIAFFRFAAIMPTQGLLRRWRVMNKSEALKHL
SQ  TSFKKEISNMLNIINRRKAKRGNGSVLLWIALVTGSMALRLGTYQGKVLMSINKTDVAEIIPIPTTKGDNLCTVRAMDVG
SQ  YMCQNDITYECPRLEPGMDPEDIDCWCDREAIYVHYGLCTKNHRERRGRRSVNIPSHGESQLENRGTPWLDTAKTTKYLT
SQ  KVENWMIRNPGYAIVAVAAAWMLGSNTSQKVIFTIMLLLIAPAYSINCLGVTNRDFVEGMSGGTWVDIVLEGDGCVTIMA
SQ  KDKPTLDIRLLKMEAKDLATVRSYCYHATVTSVSSEARCPTMGEAHNPKALDSNYLCKSTYVDRGWGNGCGLFGKGSLQT
SQ  CVKFGCTQKAMGMTIQRENLDYELAIYVHGPTSVAAHGNYTTQLGAKHAAKFSITPSSPSFTANLGEYGEATVDCEPRAA
SQ  LDIDNYYVMSMNNKHWLVNRDWFHDLDLPWTGPATDVWKYRESLVEFEEAHVTRQTVVALAAQEGELHIVLAGAIPVTVA
SQ  GTTLTLTSGHLKCRMKLDKLKIKGSTYLMCKDKFAFAKNPVDTGHGTIVTEVQYAGSDGPCRIPITMTENLHDLTPIGRL
SQ  VTVNPFVPSSETAQKILIELEPPFGTSFILVGTGPNQVKYQWHKSGSVIGSAFKTTIKGAQRMAVLGETAWDFGSVGGVF
SQ  NSIGKGIHGLFGGAFRTLFGGMSWVTQALMGALLLWLGVSSRERTVSITLLATGGILLFLAMNVHADTGCAIDITRRELK
SQ  CGSGIFIHNDVETWRDNYKYHPSTPKNFAKIIHKAYKEGICGVRSASRLEHEMWKHIAPELNAILEDNEVDLSVVVEEHK
SQ  GIYKKAPLRLENTSDEMHFGWKNWGKSFLFKTQMANSTFVVDGPETKECPTERRAWNSLEIEDFGVGIMSTKVFLKVNGD
SQ  KTEVCDSMVMGTAIKGNRAVHSDLGYWIESGKNTSWRLERAVLGEVRSCTWPESHTLWNEGVEDSDLIIPPTLGGPRTHH
SQ  NKREGYKTQLKGPWNEEGPIIIEFGECPGTKVTQEESCRNRAASARTTTASGKVIRDWCCKNCTMPPLRFTTKNGCWYGM
SQ  EIRPKHESEETLIKSKVTAGTGNDICRFQLGLLMAFVFTQEVLRKRWTARLALPTAALLLACFVLGAFTYSDMIRYFVLV
SQ  GCAFAESNSGGDVIHLALIAVFNIQPAALVSTFFRNRWTNRENLLLVIAAAMAQMAWSDVGIEIMPIMNAMALAWMILKA
SQ  VSIGTVSTIAMPILSGLAPPMEWFGLDVLRCLLLIVGVAALIKERKENLAKKKGALLISAGLALTGAFSPLVLQGALMLS
SQ  ECATKRGWPASEVLTAIGMTIALAGSVARLDSGTMAIPLATTSILFVSYVLSGKSTDMWIERCADVTWEEEAEITGTSPR
SQ  LDVELDDNGDFKMINDPGVPMWMWASRMGLMCMAAYNPVLIPVSVAGYWMTRKIHKRGGVLWDLPAPKQMGRSDMKPGVY
SQ  RVMTSGVLGSYQSGVGVMYDGVFHTMWHVTQGAALRNGEGRLNPTWGSVRDDLITYGGKWKLSATWDGTEEVQLIAAEPG
SQ  KPVKNFQTRPGVFKTPAGEVGAITLDFPKGTSGSPIVNKAGAVIGLYGNGLVLSHGAYVSAISQGERQEEEAPEAFTPEM
SQ  LRKRQLTILDLHPGAGKTRRVIPQIVREAVKQRLRTVILAPSRVVAAEIAEALRGLPVRFQTSAVKAEHSGTEIVDVMCH
SQ  ATLTQRLMTPMRVPNYNVFVMDEAHFTDPASIAARGYISTKVESGEAAAIFMTATPPGTIDPFPDSNSPIIDQEAEIPDR
SQ  AWNSGFEWITDYTGKTVWFVPSVRSGNEIAMCLTKAGKKVIQLNRKSYETEYQKCKGNDWDYVVTTDISEMGANFGAHRV
SQ  IDSRKCVKPVIINDGEGRVQLNGPLPITASSAAQRRGRVGRDPTQSGDEYYYGGPITNDDTGHAHWIEAKMLLDNIQLQN
SQ  GLVAQLYKPERDKVFATDGEYRLRGEQKKHFVELMRTGELPVWLSYKVAEAGINYTDRRWCFDGPHNNTILEDNTEVEIW
SQ  TRQGERKVLRPRWSDARVYSDNQALRAFKEFAAGKRSAGSMMDVMARMPDYFWTKTMNAADNLYVLATTEKGGRAHRAAL
SQ  EELPDTLETVLLIAMMSLASCGMLALMMQRKGIGKTGMGTAVLTAVTILLWMADVPAPKIAGVLLISFLLMIVLIPEPEK
SQ  QRSQTDNHLAVFLICALLLVSAVSANEMGWLDTTKRDLGKLFSGPSAVTTSRWEPLKLALALKPATAWAGYAGMTMLLTP
SQ  LFRHLITTQYISFSLTAITSQASALFGLNSGYPFVGVDLSVVFLLVGCYGQYNLPTTMATIGLLVGHYAFMIPGWQAEAM
SQ  RAAQRRTAAGVMKNAVVDGIVATDIPEMDTATPIVEKKMGQVMLLIISALAILLNPDTMTVVEGGVLITAALATLLEGNA
SQ  NTVWNSTVAVGVCHLMRGGWAAGPSIGWTIIRNLEAPKVKRGGIAAPTLGEIWKSRLNQLTREQFMEYRKDGIIEVDRTA
SQ  ARRARREGNRTGGHPVSRGTAKLRWLVERGFAKPLGKVVDLGCGRGGWSYYCATLRHVQEVRGYTKGGPGHEEPMLMQSY
SQ  GWNIVSMKSGIDVFYRPTEACDTVLCDIGESSPSPGVEEARTLRVLEMIEPWLRTANQYCVKVLCPYTPKVIERLEKLQR
SQ  KYGGGLVRVPLSRNSNHEMYWVSEASSNLINAVNATSQVLLQRLEKDHRKGPRYEEDVDLGSGTRSVARRSPFMDTRKIH
SQ  HRIERLKSEFSTTWHYDCEHPYRTWNYHGSYEVKPTGSASSMVNGVVKLMSKPWDSIQSVLTMAMTDTTPFGQQRVFKEK
SQ  VDTKAPEPAPGVKAVLDLTTDWLWAVLCRRKKPRMCTKEEFIAKVNSHAALGAIFEEQNQWASAREAVEDPGFWNFVDKE
SQ  RQAHLEGRCETCIYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMSRENSYGGVEGKGLQKLGYI
SQ  LQEISRKEGGHMFADDTAGWDTRVTLTDLENEAKITRWMEPEHRKLAEAMIELTYKNKVVKVTRPGKEGKTVMDIISRND
SQ  QRGSGQVVTYALNTYTNLAVQLIRCMEGEGLLEEEETMRISDAKRRAVQAWLDTNGTERLTPMAVSGDDCVVKPIDNRFA
SQ  TALHFLNGMSKVRKDIQEWKPSTGWTNWQEVPFCSHHFNELVMRDGRKIVVPCRAQDELIGRARVSPGSGWSLRETACLG
SQ  KAYAQMWLLMYFHRRDLRLMANAICSAVPIDWVPTGRTTWSIHGKGEWMTTEDMLAVWNRVWIFENEHMEDKTPVYSWTD
SQ  VPYIGKREDQWCGSLIGHRSRATWAENIYTPIMQVRNLIGAERYVDYMPAQTRFAHEAELQGGVL
//
ID  P09732;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11081;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P09732;
DR  UNIPROT: A3EZ58;
DR  UNIPROT: Q88781;
DR  UNIPROT: Q88782;
DR  UNIPROT: Q88783;
DR  UNIPROT: Q88784;
DR  UNIPROT: Q88785;
DR  UNIPROT: Q88786;
DR  UNIPROT: Q88787;
DR  UNIPROT: Q88788;
DR  PDB: 4FG0;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKKPGKPGRNRVVNMLKRGVSRVNPLTGLKRILGSLLDGRGPVRFILAILTFFRFTALQPTEALKRRWRAVDKRTALKH
SQ  LNGFKRDLGSMLDTINRRPSKKRGGTRSLLGLAALIGLASSLQLSTYQGKVLMSINKTDAQSAINIPSANGANTCIVRAL
SQ  DVGVMCKNDITYLCPVLSAGNDPEDIDCWCDVEEVWVHYGRCTRMGHSRRSRRSISVQHHGDSTLATKNTPWLDTVKTTK
SQ  YLTKVENWVLRNPGYALVALAIGWMLGSNNTQRVVFVIMLMLIAPAYSFNCLGTSNRDFVEGASGATWIDLVLEGGSCVT
SQ  VMAPEKPTLDFKVMKMEATELATVREYCYEATLDTLSTVARCPTTGEAHNTKRSDPTFVCKRDVVDRGWGNGCGLFGKGS
SQ  IDTCAKFTCKNKATGKTILRENIKYEVAIFVHGSTDSTSHGNYFEQIGKNQAARFTISPQAPSFTANMGEYGTVTIDCEA
SQ  RSGINTEDYYVFTVKEKSWLVNRDWFHDLNLPWTSPATTDWRNRETLVEFEEPHATKQTVVALGSQEGALHTALAGAIPA
SQ  TVSSSTLTLQSGHLKCRAKLDKVKIKGTTYGMCDSAFTFSKNPADTGHGTVIVELQYTGSNGPCRVPISVTANLMDLTPV
SQ  GRLVTVNPFISTGGANNKVMIEVEPPFGDSYIVVGRGTTQINYHWHKEGSSIGKALATTWKGAQRLAVLGDTAWDFGSIG
SQ  GVFNSIGKAVHQVFGGAFRTLFGGMSWITQGLLGALLLWMGLQARDRSISLTLLAVGGILIFLATSVQADSGCAIDLQRR
SQ  ELKCGGGIFVYNDVEKWKSDYKYFPLTPTGLAHVIQEAHANGICGIRSTSRLEHLMWENIQRELNAIFEDNEIDLSVVVQ
SQ  EDPKYYKRAPRRLKKLEDELDYGWKKWGKTLFVEPRLGNNTFVVDGPETKECPTANRAWNSFKVEDFGFGMVFTRLWLTI
SQ  REENTTECDSAIIGTAIKGDRAVHSDLSYWIESKKNETWQLERAVMGEVKSCTWPETHTLWGDGVVESEMIIPVTLGGPK
SQ  SHHNKRNGYHTQTKGPWSEGEITLDFDYCPGTTVTVTEHCGNRGASLRTTTASGKLVTDWCCRSCSLPPLRYTTKDGCWY
SQ  GMEIRPVKEEEAKLVKSRVTAGVAGGMEPFQLGLLVAFIATQEVLKRRWTGKLTLTSLAVCLALLIFGNLTYMDLVRYLV
SQ  LVGTAFAEMNTGGDVIHLALVAVFKVQPAFLAGLFLRMQWSNQENILMVIGAAFLQMAANDLKLEVLPILNAMSIAWMLI
SQ  RAMKEGKVAMYALPILCALTPGMRMAGLDVIRCLLLIIGIVTLLNERRESVAKKKGGYLLAAALCQAGVCSPLIMMGGLI
SQ  LAHPNGKRSWPASEVLTGVGLMCALAGGLLEFEETSMVVPFAIAGLMYITYTVSGKAAEMWIEKAADITWEQNAEITGTS
SQ  PRLDVDLDSHGNFKLLNDPGAPVHLFALRFILLGLSARFHWFIPFGVLGFWLLGKHSKRGGALWDVPSPKVYPKCETKPG
SQ  IYRIMTRGILGTFQAGVGVMHEGVFHTMWHATEGAVLRNGEGRLDPYAGDVRNDLISYGGPWKLSATWDGTEEVQMIAVA
SQ  PGKPAINVQTTPGVFKTPFGTIGAVTLDFPKGTSGSPIINKKGEIIGLYGNGVLIGQGEYVSGIIQGERTEEPIPDAYNE
SQ  EMLRKRKLTVLELHPGAGKTRKVLPQIIKDCIQKRLRTAVLAPTRVVACEIAEALKGLPIRYLTPAVRNEHQGNEIVDVM
SQ  CHATLTQKLLTPTRVPNYQVYIMDEAHFIDPASIAARGYISTKVELGEAAAIFMTATPPGTNDPFPDSNSPILDVEAQVP
SQ  DKAWSTGYEWITNFTGRTVWFVPSVKSGNEIAICLQKAGKRVIQLNRKSFDTEYPKTKNNEWDFVVTTDISEMGANFGAH
SQ  RVIDSRKCVKPVILEDDDRVILNGPMAITSASAAQRRGRIGRNPSQIGDEYHYGGATNEDDHDLANWTEAKILLDNIYLP
SQ  NGLVAQMYQPERDKVFTMDGEFRLRGEERKNFVELMRNGDLPVWLAYKVASNGHSYQDRSWCFTGQTNNTILEDNNEVEV
SQ  FTKTGDRKILRPKWMDARVCCDYQALKSFKEFAAGKRSALGMMEVMGRMPNHFWEKTVAAADTLYLLGTSEANSRAHKEA
SQ  LAELPDSLETLLLIGMLCVMSMGTFIFLMNRKGVGKMGLGAFVMTLATALLWAAEVPGTQIAGVLLIVFLLMIVLIPEPE
SQ  KQRSQTDNQLAVFLICIMTLMGVVAANEMGLLEKTKSDIAKLFGSQPGSVGFATRTTPWDISLDIKPATAWALYAAATMV
SQ  MTPLIKHLITTQYVNFSLTAIASQAGVLLGLTNGMPFTAMDLSVPLLVLGCWNQMTLPSLAVAVMLLAIHYAFMIPGWQA
SQ  EAMRAAQRRTAAGIMKNAVVDGIVATDIPDLSPATPMTEKKMGQILLIAAAVLAVLVRPGICSIKEFGVLGSAALVTLIE
SQ  GTAGVVWNCTTAVGLCNLMRGGWLAGMSITWTVYKNVDKPKGKRGGGKGATLGEIWKSRLNQLTRAEFMAYRKDGIVEVD
SQ  RAPARKARREGRLTGGHPVSRGSAKLRWITERGFVKPMGKVVDLGCGRGGWSYYCATLKHVQEVKGFTKGGPGHEEPQLM
SQ  QSYGWNLVHMKSGVDVFHKPAEPADTVLCDIGESNPSCEVEEARTARVLDMVEEWLKKGATEFCIKVLCPYTPKIIEKLE
SQ  KLQRKYGGGLVRVPLSRNSTHEMYWVSGAAGNIIHAVSMTSQVLMGRMDKQNRSGPRYEEDVNLGSGTRSVGKLTEKPDL
SQ  RKVGERIRRLREEYQQTWTYDHNNPYRTWNYHGSYEVKPTGSASSMVNGVVRLLSKPWDMITNVTTMAMTDTTPFGQQRV
SQ  FKEKVDTKAPEPPLGVAQIMDVTTDWLWDFVAREKKPRVCTPEEFKAKVNSHAALGAMFEEQNQWSSAREAVEDPKFWEM
SQ  VDEEREAHLKGECHTCIYNMMGKREKKTGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMSRENSYGGVEGKGLQK
SQ  LGYILQEISQIPGGKMYADDTAGWDTRITKEDLKNEAKITKRMEERHRKLAEAIIDLTYRHKVVKVMRPGPDGKTYMDVI
SQ  SREDQRGSGQVVTYALNTFTNLAVQLIRCMEAEGVVDEDDITRVRLGRLAKAVEWLRKNGPERLSRMAVSGDDCVVKPID
SQ  DRFATALHFLNNMSKIRKDIQEWKPSTGWHNWQEVPFCSHHFNELMLKDGRTIVVPCRSQDELIGRARISPGAGWNVKET
SQ  ACLSKSYAQMWLLMYFHRRDLRMMANAICSAVPVNWVPTGRTTWSIHGKGEWMTTEDMLSVWNRVWIEENEYMKDKTPLA
SQ  AWNDIPYLGKREDIWCGSLIGTRTRATWAENIYAPIMQIRNLIGEEEYRDYM
//
ID  Q01299;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  70733;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q01299;
DR  PDB: 5O6A;
DR  PDB: 5O6V;
DR  PDB: 7JNO;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane- destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:18042258). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:18042258). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:18042258}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVKKAILKGKGGGPPRRVSKETATKTRQPRVQMPNGLVLMRMMGILWHAVAGTARNPVLKAFWNSVPLKQATAALRKIKR
SQ  TVSALMVGLQKRGKRRSATDWMSWLLVITLLGMTIAATVRKERDGSTVIRAEGKDAATQVRVENGTCVILATDMGSWCDD
SQ  SLSYECVTIDQGEEPVDVDCFCRNVDGVYLEYGRCGKQEGSRTRRSVLIPSHAQGELTGRGHKWLEGDSLRTHLTRVEGW
SQ  VWKNRLLALAMVTVVWLTLESVVTRVAVLVVLLCLAPVYASRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPS
SQ  MDVWLDAIYQENPAQTREYCLHAKLSDTKVAARCPTMGPATLAEEHQGGTVCKRDQSDRGWGNHCGLFGKGSIVACVKAA
SQ  CEAKKKATGHVYDANKIVYTVKVEPHTGDYVAANETHSGRKTASFTVSSEKTILTMGEYGDVSLLCRVASGVDLAQTVIL
SQ  ELDKTVEHLPTAWQVHRDWFNDLALPWKHEGARNWNNAERLVEFGAPHAVKMDVYNLGDQTGVLLKALAGVPVAHIEGTK
SQ  YHLKSGHVTCEVGLEKLKMKGLTYTMCDKTKFTWKRAPTDSGHDTVVMEVTFSGTKPCRIPVRAVAHGSPDVNVAMLITP
SQ  NPTIENNGGGFIEMQLPPGDNIIYVGELSYQWFQKGSSIGRVFQKTKKGIERLTVIGEHAWDFGSAGGFLSSIGKALHTV
SQ  LGGAFNSIFGGVGFLPKLLLGVALAWLGLNMRNPTMSMSFLLAGVLVLAMTLGVGADVGCAVDTERMELRCGEGLVVWRE
SQ  VSEWYDNYAYYPETPGALASAIKETFEEGSCGVVPQNRLEMAMWRSSVTELNLALAEGEANLTVMVDKFDPTDYRGGVPG
SQ  LLKKGKDIKVSWKSWGHSMIWSIPEAPRRFMVGTEGQSECPLERRKTGVFTVAEFGVGLRTKVFLDFRQEPTHECDTGVM
SQ  GAAVKNGMAIHTDQSLWMRSMKNDTGTYIVELLVTDLRNCSWPASHTIDNADVVDSELFLPASLAGPRSWYNRIPGYSEQ
SQ  VKGPWKHTPIRVIREECPGTTVTINAKCDKRGASVRSTTESGKVIPEWCCRACTMPPVTFRTGTDCWYAMEIRPVHDQGG
SQ  LVRSMVVADNGELLSEGGVPGIVALFVVLEYIIRRRPSTGSTVVWGGIVVLALLVTGMVRMESLVRYVVAVGITFHLELG
SQ  PEIVALMLLQAVFELRVGLLSAFALRRSLTVREMVTTYFLLLVLELGLPSANLEDFWKWGDALAMGALIFRACTAEGKTG
SQ  AGLLLMALMTQQDVVTVHHGLVCFLSAASACSIWRLLRGHREQKGLTWIVPLARLLGGEGSGIRLLAFWELSAHRGRRSF
SQ  SEPLTVVGVMLTLASGMMRHTSQEALCALAVASFLLLMLVLGTRKMQLVAEWSGCVEWHPELVNEGGEVSLRVRQDAMGN
SQ  FHLTELEKEERMMAFWLIAGLAASAIHWSGIIGVMGLWTLTKMLRSSRRSDLVFSGQGGRERGDRPFEVKDGVYRIFSPG
SQ  LFWGQNQVGVGYGSKGVLHTMWHVTRGAALSIDDAVAGPYWADVREDVVCYGGAWSLEEKWKGETVQVHAFPPGKAHEVH
SQ  QCQPGELILDTGRKLGAIPIDLVKGTSGSPILNAQGVVVGLYGNGLKTNETYVSSIAQGEAEKSRPNLPQAVVGTGWTSK
SQ  GQITVLDMHPGSGKTHRVLPELIRQCIDRRLRTLVLAPTRVVLKEMERALNGKRVRFHSPAVSDQQAGGAIVDVMCHATY
SQ  VNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYTLAKENKCALVLMTATPPGKSEPFPESNGAITSEERQIPNGEWR
SQ  DGFDWITEYEGRTAWFVPSIAKGGAIARTLRQKGKSVICLNSKTFEKDYSRVRDEKPDFVVTTDISEMGANLDVSRVIDG
SQ  RTNIKPEEVDGKVELTGTRRVTTASAAQRRGRVGRQDGRTDEYIYSGQCDDDDSGLVQWKEAQILLDNITTLRGPVATFY
SQ  GPEQDKMPEVAGHFRLTEEKRKHFRHLLTHCDFTPWLAWHVAANVSSVTDRSWTWEGPEANAVDEASGGLVTFRSPNGAE
SQ  RTLRPVWKDARMFKEGRDIKEFVAYASGRRSFGDVLTGMSGVPELLRHRCVSALDVFYTLMHEKPDSRAMRMAERDAPEA
SQ  FLTMVEMMVLGLATLGVIWCFVVRTSISRMMLGTLVLLASLLLLWAGGVGYGNMAGVALIFYTLLTVLQPEAGKQRSSDD
SQ  NKLAYFLLTLCSLAGLVAANEMGFLEKTKADLSTVLWSEREEPRPWSEWTNVDIQPARSWGTYVLVVSLFTPYIIHQLQT
SQ  KIQQLVNSAVASGAQAMRDLGGGAPFFGVAGHVMTLGVVSLIGATPTSLMVGVGLAALHLAIVVSGLEAELTQRAHKVFF
SQ  SAMVRNPMVDGDVINPFGEGEAKPALYERRMSLVLAIVLCLMSVVMNRTVASITEASAVGLAAAGQLLRPEADTLWTMPV
SQ  ACGMSGVVRGSLWGFLPLGHRLWLRASGGRRGGSEGDTLGDLWKRRLNNCTREEFFVYRRTGILETERDKARELLRRGET
SQ  NMGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMSVRAYTIGGRGHEAPKMVTSLGWNLIKFRSG
SQ  MDVFSMQPHRADTVMCDIGESSPDAAVEGERTRKVILLMEQWKNRNPTAACVFKVLAPYRPEVIEALHRFQLQWGGGLVR
SQ  TPFSRNSTHEMYYSTAVTGNIVNSVNVQSRKLLARFGDQRGPTRVPELDLGVGTRCVVLAEDKVKEQDVQERIKALREQY
SQ  SETWHMDEEHPYRTWQYWGSYRTAPTGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKDKVDTKAQEPQP
SQ  GTRVIMRAVNDWILERLAQKSKPRMCSREEFIAKVKSNAALGAWSDEQNRWASAREAVEDPAFWHLVDEERERHLMGRCA
SQ  HCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRFLEFEALGFLNEDHWASRESSGAGVEGISLNYLGWHLKKLSTLNGG
SQ  LFYADDTAGWDTKVTNADLEDEEQILRYMEGEHKQLATTIMQKAYHAKVVKVARPSRDGGCIMDVITRRDQRGSGQVVTY
SQ  ALNTLTNIKVQLIRMMEGEGVIEAADAHNPRLLRVERWLKEHGEERLGRMLVSGDDCVVRPLDDRFGKALYFLNDMAKTR
SQ  KDIGEWEHSAGLSSWEEVPFCSHHFHELVMKDGRTLVVPCRDQDELVGRARISPGCGWSVRETACLSKAYGQMWLLSYFH
SQ  RRDLRTLGLAINSAVPVDWVPTGRTTWSIHASGAWMTTEDMLDVWNRVWILDNPFMQNKGKVMEWRDVPYLPKAQDMLCS
SQ  SLVGRKERAEWAKNIWGAVEKVRKMIGPEKFKDYLSCMDRHDLHWELRLESSII
//
ID  P07720;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11087;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P07720;
DR  UNIPROT: P07721;
DR  UNIPROT: Q88475;
DR  UNIPROT: Q88476;
DR  UNIPROT: Q88477;
DR  UNIPROT: Q88478;
DR  UNIPROT: Q88479;
DR  UNIPROT: Q88877;
DR  UNIPROT: Q88878;
DR  UNIPROT: Q88879;
DR  PDB: 1K4R;
DR  PDB: 7LSE;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane- destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon- alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGKAILKGKGGGPPRRVSKETAKKTRQSRVQMPNGLVLMRMMGILWHAVAGTARSPVLKSFWKSVPLKQATAALRKIKK
SQ  AVSTLMVGLQRRGKRRSAVDWTGWLLVVVLLGVTLAATVRKERDGTTVIRAEGKDAATQVRVENGTCVILATDMGSWCDD
SQ  SLTYECVTIDQGEEPVDVDCSCRNVDGVYLEYGRCGKQEGSRTRRSVLIPSHAQGDLTGRGHKWLEGDSLRTHLTRVEGW
SQ  VWKNKVLTLAVIAVVWLTVESVVTRVAVVVVLLCLAPVYASRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPS
SQ  MDVWLDSIYQENPAKTREYCLHAKLSDTKVAARCPTMGPATLAEEHQSGTVCKRDQSDRGWGNHCGLFGKGSIVTCVKAS
SQ  CEAKKKATGHVYDANKIVYTVKVEPHTGDYVAANETHSGRKTASFTVSSERTILTMGDYGDVSLLCRVASGVDLAQTVIL
SQ  ELDKTSEHLPTAWQVHRDWFNDLALPWKHEGAQNWNNAERLVEFGAPHAVKMDVYNLGDQTGVLLKSLAGVPVAHIDGTK
SQ  YHLKSGHVTCEVGLEKLKMKGLTYTMCDKTKFTWKRIPTDSGHDTVVMEVAFSGTKPCRIPVRAVAHGSPDVNVAMLMTP
SQ  NPTIENNGGGFIEMQLPPGDNIIYVGELSHQWFQKGSSIGRVFQKTRKGIERLTVIGEHAWDFGSTGGFLTSVGKALHTV
SQ  LGGAFNSLFGGVGFLPKILVGVVLAWLGLNMRNPTMSMSFLLAGGLVLAMTLGVGADVGCAVDTERMELRCGEGLVVWRE
SQ  VSEWYDNYAYYPETLGALASAIKETFEEGTCGIVPQNRLEMAMWRSSATELNLALVEGDANLTVVVDKLDPTDYRGGIPS
SQ  LLKKGKDIKVSWKSWGHSMIWSVPEAPRLFMVGTEGSSECPLERRKTGVFTVAEFGVGLRTKVFLDFRQESTHECDTGVM
SQ  GAAVKNGMAVHTDQSLWMKSVRNDTGTYIVELLVTDLRNCSWPASHTIDNAEVVDSELFLPASLAGPRSWYNRIPGYSEQ
SQ  VKGPWKYSPIRVTREECPGTRVTINADCDKRGASVRSTTESGKVIPEWCCRTCTLPPVTFRTGTDCWYAMEIRPVHDQGG
SQ  LVRSMVVADNGELLSEGGIPGIVALFVVLEYVIRRRPATGTTAMWGGIVVLALLVTGLVKIESLVRYVVAVGITFHLELG
SQ  PEIVALTLLQAVFELRVGLLSAFALRSNLTVREMVTIYFLLLVLELGLPSEGLGALWKWGDALAMGALIFRACTAEEKTG
SQ  VGLLLMALMTQQDLATVHYGLMLFLGVASCCSIWKLIRGHREQKGLTWIVPLAGLLGGEGSGVRLVAFWELTVHGRRRSF
SQ  SEPLTVVGVMLTLASGMIRHTSQEALCALAVASFLLLMLVLGTRKMQLVAEWSGCVEWHPELMNEGGEVSLRVRQDSMGN
SQ  FHLTELEKEERVMAFWLLAGLAASAFHWSGILGVMGLWTLSEMLRTARRSGLVFSGQGGRERGDRPFEVKDGVYRIFSPG
SQ  LLWGQRQVGVGYGSKGVLHTMWHVTRGAALSIDDAVAGPYWADVKEDVVCYGGAWSLEEKWKGETVQVHAFPPGRAHEVH
SQ  QCQPGELLLDTGRRIGAVPIDLAKGTSGSPILNSQGVVVGLYGNGLKTNETYVSSIAQGEAEKSRPNLPPAVTGTGWTAK
SQ  GQITVLDMHPGSGKTHRVLPELIRQCIDRRLRTLVLAPTRVVLKEMERALNGKRVRFHSPAVGDQQVGGSIVDVMCHATY
SQ  VNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYTLAKENKCALVLMTATPPGKSEPFPESNGAISSEEKQIPDGEWR
SQ  DGFDWITEYEGRTAWFVPSSAKGGIIARTLIQKGKSVICLNSKTFEKDYSRVRDEKPDFVVTTDISEMGANLDVSRVIDG
SQ  RTNIKPEEVDGRVELTGTRRVTTASAAQRRGRVGRQEGRTDEYIYSGQCDDDDSGLVQWKEAQILLDNITTLRGPVATFY
SQ  GPEQDKMPEVAGHFRLTEEKRKHFRHLLTHCDFTPWLAWHVAANVSSVTSRNWTWEGPEENTVDEANGDLVTFRSPNGAE
SQ  RTLRPVWRDARMFREGRDIREFVAYASGRRSFGDVLSGMSGVPELLRHRCVSAMDVFYTLMHEEPGSRAMKMAERDAPEA
SQ  FLTVVEMMVLGLATLGVVWCFVVRTSISRMMLGTLVLLASLALLWAGGVSYGNMAGVALIFYTLLTVLQPEAGKQRSSDD
SQ  NKLAYFLLTLCSLAGLVAANEMGFLEKTKADLSTVLWSEHEELRSWEEWTNIDIQPARSWGTYVLVVSLFTPYIIHQLQT
SQ  KIQQLVNSAVATGAQAMRDLGGGAPFFGVAGHVMALGVVSLVGATPTSLVVGVGLAAFHLAIVVSGLEAELTQRAHKVFF
SQ  SAMVRNPMVDGDVINPFGEGEAKPALYERKMSLVLAIVLCLMSVVMNRTVPSTPRLLLWDWRQRDNCSNQRRTPFGRCQA
SQ  CGLSGVVRGSLWGFCPLGHRLWLRASGSRRGGSEGDTLGDLWKRKLNGCTKEEFFAYRRTGILETERDKARELLKRGETN
SQ  MGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMSVKACAIAGKGHETPKMVTSLGWNLIKFRAGM
SQ  DVFSMQPHRADTIMCDIGESNPDAVVEGERTRKVILLMEQWKNRNPTATCVFKALAPYRPEVTEALHRFQLQWGGGLVRT
SQ  PFSRNSTHEMYYSTAITGNIVNSVNIQSRKLLARFGDQRGPTRVPELDLGVGTRCVVLAEDKVKEKDVQERISALREQYG
SQ  ETWHMDREHPYRTWQYWAATACANRVGGALINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKEKVDTKAQEPQPGT
SQ  KVIMRAVNDWILERLARKSKPRMCSREEFIAKVKSNAALGAWSDEQNRWSSAKEAVEDPAFWQLVDEERERHLAGRCAHC
SQ  VYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRFLEFEALGFLNEDHWASRGSSGSGVEGISLNYLGWHLKGLSTLEGGLF
SQ  YADDTAGWDTKVTNADLEDEEQLLRYMEGEHKQLAATIMQKAYHAKVVKVARPSRDGGCIMDVITRRDQRGSGQVVTYAL
SQ  NTLTNIKVQLIRMMEGEGVIEASDAHNPRLLRVERWLRDHGEERLGRMLVSGDDCVVRPVDDRFSGALYFLNDMAKTRKD
SQ  IGEWDHSVGFSNWEEVPFCSHHFHELVMKDGRTLIVPCRDQDELVGRARVSPGCGRSVRETACLSKAYGQMWLLSYFHRR
SQ  DLRTLGLAICSAVPVDWVPAGRTTWSIHASGAWMTTEDMLDVWNRVWILDNPFMHSKEKIAEWRDVPYLPKSHDMLCSSL
SQ  VGRKERAEWAKNIWGAVEKVRKMIGQEKFKDYLSCMDRHDLHWESKLESSII
//
ID  P14336;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11088;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P14336;
DR  UNIPROT: Q88493;
DR  PDB: 1N6G;
DR  PDB: 1NA4;
DR  PDB: 1SVB;
DR  PDB: 1URZ;
DR  PDB: 6J5G;
DR  PDB: 6S8C;
DR  PDB: 7LSF;
DR  PDB: 7LSG;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane- destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon- alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVKKAILKGKGGGPPRRVSKETATKTRQPRVQMPNGLVLMRMMGILWHAVAGTARNPVLKAFWNSVPLKQATAALRKIKR
SQ  TVSALMVGLQKRGKRRSATDWMSWLLVITLLGMTLAATVRKERDGSTVIRAEGKDAATQVRVENGTCVILATDMGSWCDD
SQ  SLSYECVTIDQGEEPVDVDCFCRNVDGVYLEYGRCGKQEGSRTRRSVLIPSHAQGELTGRGHKWLEGDSLRTHLTRVEGW
SQ  VWKNKLLALAMVTVVWLTLESVVTRVAVLVVLLCLAPVYASRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPS
SQ  MDVWLDAIYQENPAKTREYCLHAKLSDTKVAARCPTMGPATLAEEHQGGTVCKRDQSDRGWGNHCGLFGKGSIVACVKAA
SQ  CEAKKKATGHVYDANKIVYTVKVEPHTGDYVAANETHSGRKTASFTISSEKTILTMGEYGDVSLLCRVASGVDLAQTVIL
SQ  ELDKTVEHLPTAWQVHRDWFNDLALPWKHEGAQNWNNAERLVEFGAPHAVKMDVYNLGDQTGVLLKALAGVPVAHIEGTK
SQ  YHLKSGHVTCEVGLEKLKMKGLTYTMCDKTKFTWKRAPTDSGHDTVVMEVTFSGTKPCRIPVRAVAHGSPDVNVAMLITP
SQ  NPTIENNGGGFIEMQLPPGDNIIYVGELSHQWFQKGSSIGRVFQKTKKGIERLTVIGEHAWDFGSAGGFLSSIGKAVHTV
SQ  LGGAFNSIFGGVGFLPKLLLGVALAWLGLNMRNPTMSMSFLLAGGLVLAMTLGVGADVGCAVDTERMELRCGEGLVVWRE
SQ  VSEWYDNYAYYPETPGALASAIKETFEEGSCGVVPQNRLEMAMWRSSVTELNLALAEGEANLTVVVDKFDPTDYRGGVPG
SQ  LLKKGKDIKVSWKSWGHSMIWSIPEAPRRFMVGTEGQSECPLERRKTGVFTVAEFGVGLRTKVFLDFRQEPTHECDTGVM
SQ  GAAVKNGMAIHTDQSLWMRSMKNDTGTYIVELLVTDLRNCSWPASHTIDNADVVDSELFLPASLAGPRSWYNRIPGYSEQ
SQ  VKGPWKYTPIRVIREECPGTTVTINAKCDKRGASVRSTTESGKVIPEWCCRACTMPPVTFRTGTDCWYAMEIRPVHDQGG
SQ  LVRSMVVADNGELLSEGGVPGIVALFVVLEYIIRRRPSTGTTVVWGGIVVLALLVTGMVRIESLVRYVVAVGITFHLELG
SQ  PEIVALMLLQAVFELRVGLLSAFALRRSLTVREMVTTYFLLLVLELGLPGASLEEFWKWGDALAMGALIFRACTAEGKTG
SQ  AGLLLMALMTQQDVVTVHHGLVCFLSVASACSVWRLLKGHREQKGLTWVVPLAGLLGGEGSGIRLLAFWELSAHRGRRSF
SQ  SEPLTVVGVMLTLASGMMRHTSQEALCALAVASFLLLMLVLGTRKMQLVAEWSGCVEWYPELVNEGGEVSLRVRQDAMGN
SQ  FHLTELEKEERMMAFWLIAGLAASAIHWSGILGVMGLWTLTEMLRSSRRSDLVFSGQGGRERGDRPFEVKDGVYRIFSPG
SQ  LFWGQNQVGVGYGSKGVLHTMWHVTRGAALSIDDAVAGPYWADVREDVVCYGGAWSLEEKWKGETVQVHAFPPGRAHEVH
SQ  QCQPGELILDTGRKLGAIPIDLVKGTSGSPILNAQGVVVGLYGNGLKTNETYVSSIAQGEAEKSRPNLPQAVVGTGWTSK
SQ  GQITVLDMHPGSGKTHRVLPELIRQCIDRRLRTLVLAPTRVVLKEMERALNGKRVRFHSPAVSDQQAGGAIVDVMCHATY
SQ  VNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYTLAKENKCALVLMTATPPGKSEPFPESNGAITSEERQIPDGEWR
SQ  DGFDWITEYEGRTAWFVPSIAKGGAIARTLRQKGKSVICLNSKTFEKDYSRVRDEKPDFVVTTDISEMGANLDVSRVIDG
SQ  RTNIKPEEVDGKVELTGTRRVTTASAAQRRGRVGRQDGRTDEYIYSGQCDDDDSGLVQWKEAQILLDNITTLRGPVATFY
SQ  GPEQDKMPEVAGHFRLTEEKRKHFRHLLTHCDFTPWLAWHVAANVSSVTDRSWTWEGPEANAVDEASGDLVTFRSPNGAE
SQ  RTLRPVWKDARMFKEGRDIKEFVAYASGRRSFGDVLTGMSGVPELLRHRCVSALDVFYTLMHEEPGSRAMRMAERDAPEA
SQ  FLTMVEMMVLGLATLGVIWCFVVRTSISRMMLGTLVLLASLLLLWAGGVGYGNMAGVALIFYTLLTVLQPEAGKQRSSDD
SQ  NKLAYFLLTLCSLAGLVAANEMGFLEKTKADLSTALWSEREEPRPWSEWTNVDIQPARSWGTYVLVVSLFTPYIIHQLQT
SQ  KIQQLVNSAVASGAQAMRDLGGGAPFFGVAGHVMTLGVVSLIGATPTSLMVGVGLAALHLAIVVSGLEAELTQRAHKVFF
SQ  SAMVRNPMVDGDVINPFGEGEAKPALYERKMSLVLATVLCLMSVVMNRTVASITEASAVGLAAAGQLLRPEADTLWTMPV
SQ  ACGMSGVVRGSLWGFLPLGHRLWLRASGGRRGGSEGDTLGDLWKRRLNNCTREEFFVYRRTGILETERDKARELLRRGET
SQ  NVGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMSVRAYTIGGKGHEAPKMVTSLGWNLIKFRSG
SQ  MDVFSMQPHRADTVMCDIGESSPDAAVEGERTRKVILLMEQWKNRNPTAACVFKVLAPYRPEVIEALHRFQLQWGGGLVR
SQ  TPFSRNSTHEMYYSTAVTGNIVNSVNVQSRKLLARFGDQRGPTKVPELDLGVGTRCVVLAEDKVKEQDVQERIRALREQY
SQ  SETWHMDEEHPYRTWQYWGSYRTAPTGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKDKVDTKAQEPQP
SQ  GTRVIMRAVNDWILERLAQKSKPRMCSREEFIAKVKSNAALGAWSDEQNRWASAREAVEDPAFWRLVDEERERHLMGRCA
SQ  HCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRFLEFEALGFLNEDHWASRESSGAGVEGISLNYLGWHLKKLSTLNGG
SQ  LFYADDTAGWDTKVTNADLEDEEQILRYMEGEHKQLATTIMQKAYHAKVVKVARPSRDGGCIMDVITRRDQRGSGQVVTY
SQ  ALNTLTNIKVQLIRMMEGEGVIEAADAHNPRLLRVERWLKEHGEERLGRMLVSGDDCVVRPLDDRFGKALYFLNDMAKTR
SQ  KDIGEWEHSAGFSSWEEVPFCSHHFHELVMKDGRTLVVPCRDQDELVGRARISPGCGWSVRETACLSKAYGQMWLLSYFH
SQ  RRDLRTLGLAINSAVPADWVPTGRTTWSIHASGAWMTTEDMLDVWNRVWILDNPFMQNKERVMEWRDVPYLPKAQDMLCS
SQ  SLVGRRERAEWAKNIWGAVEKVRKMIGPEKFKDYLSCMDRHDLHWELRLESSII
//
ID  Q5WPU5;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  64286;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q5WPU5;
DR  PDB: 6A0P;
DR  PDB: 6S92;
DR  PDB: 6S93;
DR  PDB: 6S94;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK- STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKKPGGPGRNRAINMLKRGIPRVFPLVGVKRVVMGLLDGRGPVRFVLALMTFFKFTALAPTKALLGRWKRINKTTAMKH
SQ  LTSFKKELGTMINVVNNRGTKKKRGNNGPGLVMIITLMTVVSMVSSLKLSNFQGKVMMTINATDMADVIVVPTQHGKNQC
SQ  WIRAMDVGYMCDDTITYECPKLDAGNDPEDIDCWCDKQPMYVHYGRCTRTRHSKRSRRSIAVQTHGESMLANKKDAWLDS
SQ  TKASRYLMKTENWIIRNPGYAFVAVLLGWMLGSNNGQRVVFVVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDVVLEG
SQ  DSCITIMAKDKPTIDIKMMETEATNLAEVRSYCYLATVSDVSTVSNCPTTGEAHNPKRAEDTYVCKSGVTDRGWGNGCGL
SQ  FGKGSIDTCANFTCSLKAMGRMIQPENVKYEVGIFIHGSTSSDTHGNYSSQLGASQAGRFTITPNSPAITVKMGDYGEIS
SQ  VECEPRNGLNTEAYYIMSVGTKHFLVHREWFNDLALPWTSPASSNWRNREILLEFEEPHATKQSVVALGSQEGALHQALA
SQ  GAVPVSFSGSVKLTSGHLKCRVKMEKLTLKGTTYGMCTEKFSFAKNPADTGHGTVVLELQYTGSDGPCKIPISIVASLSD
SQ  LTPIGRMVTANPYVASSEANAKVLVEMEPPFGDSYIVVGRGDKQINHHWHKAGSSIGKAFITTIKGAQRLAALGDTAWDF
SQ  GSVGGIFNSVGKAVHQVFGGAFRTLFGGMSWITQGLMGALLLWMGVNARDRSIALVMLATGGVLLFLATNVHADSGCAID
SQ  VGRRELRCGQGIFIHNDVEAWVDRYKFMPETPKQLAKVIEQAHAKGICGLRSVSRLEHVMWENIRDELNTLLRENAVDLS
SQ  VVVEKPKGMYKSAPQRLALTSEEFEIGWKAWGKSLVFAPELANHTFVVDGPETKECPDAKRAWNSLEIEDFGFGIMSTRV
SQ  WLKVREHNTTDCDSSIIGTAVKGDIAVHSDLSYWIESHKNTTWRLERAVFGEIKSCTWPETHTLWSDGVVESDLVVPVTL
SQ  AGPKSNHNRREGYKVQSQGPWDEEDIVLDFDYCPGTTVTITEACGKRGPSIRTTTSSGRLVTDWCCRSCTLPPLRYRTKN
SQ  GCWYGMEIRPMKHDETTLVKSSVSAHRSDMIDPFQLGLLVMFLATQEVLRKRWTARLTVPAIVGALLVLILGGITYTDLL
SQ  RYVLLVGAAFAEANSGGDVVHLALIAAFKIQPGFLAMTFLRGKWTNQENILLALGAAFFQMAATDLNFSLPGILNATATA
SQ  WMLLRAATQPSTSAIVMPLLCLLAPGMRLLYLDTYRITLIIIGICSLIGERRRAAAKKKGAVLLGLALTSTGQFSASVMA
SQ  AGLMACNPNKKRGWPATEVLTAVGLMFAIVGGLAELDVDSMSIPFVLAGLMAVSYTISGKSTDLWLERAADITWETDAAI
SQ  TGTSQRLDVKLDDDGDFHLINDPGVPWKIWVIRMTALGFAAWTPWAIIPAGIGYWLTVKYAKRGGVFWDTPAPRTYPKGD
SQ  TSPGVYRIMSRYILGTYQAGVGVMYEGVLHTLWHTTRGAAIRSGEGRLTPYWGSVKEDRITYGGPWKFDRKWNGLDDVQL
SQ  IIVAPGKAAINIQTKPGIFKTPQGEIGAVSLDYPEGTSGSPILDKNGDIVGLYGNGVILGNGSYVSAIVQGEREEEPVPE
SQ  AYNADMLRKKQLTVLDLHPGAGKTRRILPQIIKDAIQRRLRTAVLAPTRVVAAEMAEALKGLPVRYLTPAVNREHSGTEI
SQ  VDVMCHATLTHRLMSPLRAPNYNLFVMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTHDPFPDTNAPVTDIQ
SQ  AEVPDRAWSSGFEWITEYTGKTVWFVASVKMGNEIAQCLQRAGKKVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGAN
SQ  FGASRVIDCRKSVKPTILEEGEGRVILSNPSPITSASAAQRRGRVGRNPSQIGDEYHYGGGTSEDDTIAAHWTEAKIMLD
SQ  NIHLPNGLVAQMYGPERDKAFTMDGEYRLRGEERKTFLELLRTADLPVWLAYKVASNGIQYTDRKWCFDGPRSNIILEDN
SQ  NEVEIVTRTGERKMLKPRWLDARVYADHQSLKWFKDFAAGKRSAVGFLEVLGRMPEHFAGKTREAFDTMYLVATAEKGGK
SQ  AHRMALEELPDALETITLIVALAVMTAGVFLLLVQRRGIGKLGLGGMVLGLATFFLWMADVSGTKIAGTLLLALLMMIVL
SQ  IPEPEKQRSQTDNQLAVFLICVLLVVGVVAANEYGMLERTKSDLGKIFSSTRQPQSALPLPSMNALALDLRPATAWALYG
SQ  GSTVVLTPLIKHLVTSEYITTSLASISAQAGSLFNLPRGLPFTELDFTVVLVFLGCWGQVSLTTLITAAALATLHYGYML
SQ  PGWQAEALRAAQRRTAAGIMKNAVVDGLVATDVPELERTTPLMQKKVGQILLIGVSAAALLVNPCVTTVREAGILISAAL
SQ  LTLWDNGAIAVWNSTTATGLCHVIRGNWLAGASIAWTLIKNADKPACKRGRPGGRTLGEQWKEKLNGLSKEDFLKYRKEA
SQ  ITEVDRSAARKARRDGNKTGGHPVSRGSAKLRWMVERQFVKPIGKVVDLGCGRGGWSYYAATLKGVQEVRGYTKGGPGHE
SQ  EPMLMQSYGWNLVTMKSGVDVYYKPSEPCDTLFCDIGESSSSAEVEEQRTLRILEMVSDWLQRGPREFCIKVLCPYMPRV
SQ  MERLEVLQRRYGGGLVRVPLSRNSNHEMYWVSGAAGNIVHAVNMTSQVLIGRMEKRTWHGPKYEEDVNLGSGTRAVGKPQ
SQ  PHTNQEKIKARIQRLKEEYAATWHHDKDHPYRTWTYHGSYEVKPTGSASSLVNGVVRLMSKPWDAILNVTTMAMTDTTPF
SQ  GQQRVFKEKVDTKAPEPPSGVREVMDETTNWLWAFLAREKKPRLCTREEFKRKVNSNAALGAMFEEQNQWSSAREAVEDP
SQ  RFWEMVDEERENHLKGECHTCIYNMMGKREKKLGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEG
SQ  LGVQKLGYILREMSHHSGGKMYADDTAGWDTRITRADLDNEAKVLELMEGEHRQLARAIIELTYKHKVVKVMRPGTDGKT
SQ  VMDVISREDQRGSGQVVTYALNTFTNIAVQLIRLMEAEGVIGQEHLESLPRKTKYAVRTWLFENGEERVTRMAVSGDDCV
SQ  VKPLDDRFANALHFLNSMSKVRKDVPEWKPSSGWHDWQQVPFCSNHFQELIMKDGRTLVVPCRGQDELIGRARVSPGSGW
SQ  NVRDTACLAKAYAQMWLLLYFHRRDLRLMANAICSAVPSNWVPTGRTSWSVHATGEWMTTDDMLEVWNKVWIQDNEWMLD
SQ  KTPVQSWTDIPYTGKREDIWCGSLIGTRTRATWAENIYAAINQVRAIIGQEKYRDYMLSLRRYEEVNVQEDRVL
//
ID  P06935;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11082;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:19889084}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease/Helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non- covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000269|PubMed:16699025}. Host cytoplasm {ECO:0000250|UniProtKB:P14335}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles (By similarity). Shuttles between the cytoplasm and nucleus (By similarity). {ECO:0000250|UniProtKB:P14335, ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P06935;
DR  PDB: 2FP7;
DR  PDB: 2GGV;
DR  PDB: 2IJO;
DR  PDB: 2P5P;
DR  PDB: 2YOL;
DR  PDB: 3E90;
DR  PDB: 3I50;
DR  PDB: 5IDK;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins (By similarity). Can migrate to the cell nucleus where it modulates host functions (By similarity). Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed:23522008). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:23522008}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes (PubMed:15367621). Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM (By similarity). They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E (By similarity). The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers (By similarity). prM-E cleavage is inefficient, and many virions are only partially matured (By similarity). These uncleaved prM would play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease/Helicase NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A- NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). NS3 supports the separation of RNA daughter and template strands during viral replication. The helicase part is involved in the inhibition of phosphorylation of host STAT1, and thereby inhibition of host type-I IFN signaling (By similarity). In addition, NS3 assists the initiation of replication by unwinding the RNA secondary structure in the 3' non- translated region (NTR). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). {ECO:0000250|UniProtKB:P14335, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:17267492). NS5 methylates viral RNA cap at guanine N- 7 and ribose 2'-O positions (PubMed:17267492). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:17267492}.
DE  Reference Proteome: No;
DE  Interaction: P05106; IntAct: EBI-981079; Score: 0.63
DE  Interaction: Q17NZ6; IntAct: EBI-2912467; Score: 0.58
DE  Interaction: Q16K62; IntAct: EBI-2912591; Score: 0.27
DE  Interaction: Q9BRP8; IntAct: EBI-11687809; Score: 0.40
GO  GO:0039714;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0032993;
GO  GO:1990904;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003677;
GO  GO:1990814;
GO  GO:0003725;
GO  GO:0140272;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008233;
GO  GO:0046983;
GO  GO:0003723;
GO  GO:0140691;
GO  GO:0003724;
GO  GO:0033592;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0045070;
GO  GO:0006508;
GO  GO:0106005;
GO  GO:0043489;
GO  GO:0019050;
GO  GO:0039574;
GO  GO:0039576;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKKPGGPGKNRAVNMLKRGMPRGLSLIGLKRAMLSLIDGKGPIRFVLALLAFFRFTAIAPTRAVLDRWRGVNKQTAMKH
SQ  LLSFKKELGTLTSAINRRSTKQKKRGGTAGFTILLGLIACAGAVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVR
SQ  AMDVGYLCEDTITYECPVLAAGNDPEDIDCWCTKSSVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWLDSTKA
SQ  TRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAILLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSC
SQ  VTIMSKDKPTIDVKMMNMEAANLADVRSYCYLASVSDLSTRAACPTMGEAHNEKRADPAFVCKQGVVDRGWGNGCGLFGK
SQ  GSIDTCAKFACTTKATGWIIQKENIKYEVAIFVHGPTTVESHGKIGATQAGRFSITPSAPSYTLKLGEYGEVTVDCEPRS
SQ  GIDTSAYYVMSVGEKSFLVHREWFMDLNLPWSSAGSTTWRNRETLMEFEEPHATKQSVVALGSQEGALHQALAGAIPVEF
SQ  SSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFKFARTPADTGHGTVVLELQYTGTDGPCKVPISSVASLNDLTPVGR
SQ  LVTVNPFVSVATANSKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTTTLRGAQRLAALGDTAWDFGSVGGV
SQ  FTSVGKAIHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIAMTFLAVGGVLLFLSVNVHADTGCAIDIGRQEL
SQ  RCGSGVFIHNDVEAWMDRYKFYPETPQGLAKIIQKAHAEGVCGLRSVSRLEHQMWEAIKDELNTLLKENGVDLSVVVEKQ
SQ  NGMYKAAPKRLAATTEKLEMGWKAWGKSIIFAPELANNTFVIDGPETEECPTANRAWNSMEVEDFGFGLTSTRMFLRIRE
SQ  TNTTECDSKIIGTAVKNNMAVHSDLSYWIESGLNDTWKLERAVLGEVKSCTWPETHTLWGDGVLESDLIIPITLAGPRSN
SQ  HNRRPGYKTQNQGPWDEGRVEIDFDYCPGTTVTISDSCEHRGPAARTTTESGKLITDWCCRSCTLPPLRFQTENGCWYGM
SQ  EIRPTRHDEKTLVQSRVNAYNADMIDPFQLGLMVVFLATQEVLRKRWTAKISIPAIMLALLVLVFGGITYTDVLRYVILV
SQ  GAAFAEANSGGDVVHLALMATFKIQPVFLVASFLKARWTNQESILLMLAAAFFQMAYYDAKNVLSWEVPDVLNSLSVAWM
SQ  ILRAISFTNTSNVVVPLLALLTPGLKCLNLDVYRILLLMVGVGSLIKEKRSSAAKKKGACLICLALASTGVFNPMILAAG
SQ  LMACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADITWESDAEITG
SQ  SSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMACLAISAYTPWAILPSVIGFWITLQYTKRGGVLWDTPSPKEYKKGDTT
SQ  TGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGHDEVQMIV
SQ  VEPGKNVKNVQTKPGVFKTPEGEIGAVTLDYPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMEEPAPAGF
SQ  EPEMLRKKQITVLDLHPGAGKTRKILPQIIKEAINKRLRTAVLAPTRVVAAEMSEALRGLPIRYQTSAVHREHSGNEIVD
SQ  VMCHATLTHRLMSPHRVPNYNLFIMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTSDPFPESNAPISDMQTE
SQ  IPDRAWNTGYEWITEYVGKTVWFVPSVKMGNEIALCLQRAGKKVIQLNRKSYETEYPKCKNDDWDFVITTDISEMGANFK
SQ  ASRVIDSRKSVKPTIIEEGDGRVILGEPSAITAASAAQRRGRIGRNPSQVGDEYCYGGHTNEDDSNFAHWTEARIMLDNI
SQ  NMPNGLVAQLYQPEREKVYTMDGEYRLRGEERKNFLEFLRTADLPVWLAYKVAAAGISYHDRKWCFDGPRTNTILEDNNE
SQ  VEVITKLGERKILRPRWADARVYSDHQALKSFKDFASGKRSQIGLVEVLGRMPEHFMVKTWEALDTMYVVATAEKGGRAH
SQ  RMALEELPDALQTIVLIALLSVMSLGVFFLLMQRKGIGKIGLGGVILGAATFFCWMAEVPGTKIAGMLLLSLLLMIVLIP
SQ  EPEKQRSQTDNQLAVFLICVLTLVGAVAANEMGWLDKTKNDIGSLLGHRPEARETTLGVESFLLDLRPATAWSLYAVTTA
SQ  VLTPLLKHLITSDYINTSLTSINVQASALFTLARGFPFVDVGVSALLLAVGCWGQVTLTVTVTAAALLFCHYAYMVPGWQ
SQ  AEAMRSAQRRTAAGIMKNVVVDGIVATDVPELERTTPVMQKKVGQIILILVSMAAVVVNPSVRTVREAGILTTAAAVTLW
SQ  ENGASSVWNATTAIGLCHIMRGGWLSCLSIMWTLIKNMEKPGLKRGGAKGRTLGEVWKERLNHMTKEEFTRYRKEAITEV
SQ  DRSAAKHARREGNITGGHPVSRGTAKLRWLVERRFLEPVGKVVDLGCGRGGWCYYMATQKRVQEVKGYTKGGPGHEEPQL
SQ  VQSYGWNIVTMKSGVDVFYRPSEASDTLLCDIGESSSSAEVEEHRTVRVLEMVEDWLHRGPKEFCIKVLCPYMPKVIEKM
SQ  ETLQRRYGGGLIRNPLSRNSTHEMYWVSHASGNIVHSVNMTSQVLLGRMEKKTWKGPQFEEDVNLGSGTRAVGKPLLNSD
SQ  TSKIKNRIERLKKEYSSTWHQDANHPYRTWNYHGSYEVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQR
SQ  VFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLARDKKPRMCSREEFIGKVNSNAALGAMFEEQNQWKNAREAVEDPKFWE
SQ  MVDEEREAHLRGECNTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQ
SQ  KLGYILKEVGTKPGGKVYADDTAGWDTRITKADLENEAKVLELLDGEHRRLARSIIELTYRHKVVKVMRPAADGKTVMDV
SQ  ISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLGKGKGPKVRTWLFENGEERLSRMAVSGDDCVVKPL
SQ  DDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVVPCRGQDELIGRARISPGAGWNVRD
SQ  TACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPANWVPTGRTTWSIHAKGEWMTTEDMLAVWNRVWIEENEWMEDKTPV
SQ  ERWSDVPYSGKREDIWCGSLIGTRTRATWAENIHVAINQVRSVIGEEKYVDYMSSLRRYEDTIVVEDTVL
//
ID  Q9Q6P4;
PN  RNA-directed RNA polymerase NS5;
GN  GP1;
OS  1968826;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000269|PubMed:24928049}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:24465392}; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000269|PubMed:24465392}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease/Helicase NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non- covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:24465392}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000269|PubMed:24465392, ECO:0000269|PubMed:29117567}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:24465392}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000269|PubMed:24465392}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}. Host cytoplasm {ECO:0000250|UniProtKB:P14335}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles (By similarity). Shuttles between the cytoplasm and nucleus (By similarity). {ECO:0000250|UniProtKB:P14335, ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q9Q6P4;
DR  PDB: 2OY0;
DR  PDB: 3I50;
DR  PDB: 3IYW;
DR  PDB: 3J0B;
DR  PDB: 3LKZ;
DR  PDB: 4O6C;
DR  PDB: 4O6D;
DR  PDB: 4OIE;
DR  PDB: 4OII;
DR  PDB: 6UTE;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000269|PubMed:17132743, ECO:0000269|PubMed:24245822, ECO:0000269|PubMed:24465392, ECO:0000269|PubMed:24889229, ECO:0000269|PubMed:24928049}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease/Helicase NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A- NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). NS3 supports the separation of RNA daughter and template strands during viral replication. The helicase part is involved in the inhibition of phosphorylation of host STAT1, and thereby inhibition of host type-I IFN signaling (PubMed:29099073). In addition, NS3 assists the initiation of replication by unwinding the RNA secondary structure in the 3' non-translated region (NTR). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). {ECO:0000250|UniProtKB:P14335, ECO:0000255|PROSITE-ProRule:PRU00860, ECO:0000269|PubMed:29099073}. [Non-structural protein 4A]: Facilitates host membrane remodelling necessary for viral replication by interacting with host RTN3. Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000269|PubMed:19474250, ECO:0000269|PubMed:29117567}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (PubMed:24465392). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN- alpha/beta pathway (PubMed:15956546). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15956546). {ECO:0000269|PubMed:15956546, ECO:0000269|PubMed:24465392}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm (PubMed:19850911). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed:19850911, PubMed:20685660). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) signaling pathway (PubMed:20106931). Inhibits host JAK1 and TYK2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:15650160). {ECO:0000269|PubMed:15650160, ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20106931, ECO:0000269|PubMed:20685660}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0039690;
GO  GO:0006508;
GO  GO:0039573;
GO  GO:0039503;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0046718;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKKPGGPGKSRAVNMLKRGMPRVLSLIGLKRAMLSLIDGKGPIRFVLALLAFFRFTAIAPTRAVLDRWRGVNKQTAMKH
SQ  LLSFKKELGTLTSAINRRSSKQKKRGGKTGIAVMIGLIASVGAVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVR
SQ  AMDVGYMCDDTITYECPVLSAGNDPEDIDCWCTKSAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWMDSTKA
SQ  TRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFVVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSC
SQ  VTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSDLSTKAACPTMGEAHNDKRADPAFVCRQGVVDRGWGNGCGLFGK
SQ  GSIDTCAKFACSTKAIGRTILKENIKYEVAIFVHGPTTVESHGNYSTQVGATQAGRFSITPAAPSYTLKLGEYGEVTVDC
SQ  EPRSGIDTNAYYVMTVGTKTFLVHREWFMDLNLPWSSAGSTVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAI
SQ  PVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFKFLGTPADTGHGTVVLELQYTGTDGPCKVPISSVASLNDLT
SQ  PVGRLVTVNPFVSVATANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTTTLKGAQRLAALGDTAWDFGS
SQ  VGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDIS
SQ  RQELRCGSGVFIHNDVEAWMDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSVV
SQ  VEKQEGMYKSAPKRLTATTEKLEIGWKAWGKSILFAPELANNTFVVDGPETKECPTQNRAWNSLEVEDFGFGLTSTRMFL
SQ  KVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRLNDTWKLERAVLGEVKSCTWPETHTLWGDGILESDLIIPVTLAG
SQ  PRSNHNRRPGYKTQNQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDSGC
SQ  WYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRY
SQ  VILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAVFFQMAYHDARQILLWEIPDVLNSLA
SQ  VAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGLFNPMI
SQ  LAAGLIACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWESDA
SQ  EITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMVCLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKK
SQ  GDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEV
SQ  QMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPI
SQ  PAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVPREHNGN
SQ  EIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTKVELGEAAAIFMTATPPGTSDPFPESNSPISD
SQ  LQTEIPDRAWNSGYEWITEYTGKTVWFVPSVKMGNEIALCLQRAGKKVVQLNRKSYETEYPKCKNDDWDFVITTDISEMG
SQ  ANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRIGRNPSQVGDEYCYGGHTNEDDSNFAHWTEARIM
SQ  LDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILE
SQ  DNNEVEVITKLGERKILRPRWIDARVYSDHQALKAFKDFASGKRSQIGLIEVLGKMPEHFMGKTWEALDTMYVVATAEKG
SQ  GRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGAVLGVATFFCWMAEVPGTKIAGMLLLSLLLMI
SQ  VLIPEPEKQRSQTDNQLAVFLICVMTLVSAVAANEMGWLDKTKSDISSLFGQRIEVKENFSMGEFLLDLRPATAWSLYAV
SQ  TTAVLTPLLKHLITSDYINTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTAATLLFCHYAYMVP
SQ  GWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQIMLILVSLAAVVVNPSVKTVREAGILITAAAV
SQ  TLWENGASSVWNATTAIGLCHIMRGGWLSCLSITWTLIKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFTRYRKEAI
SQ  IEVDRSAAKHARKEGNVTGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEE
SQ  PQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTIRVLEMVEDWLHRGPREFCVKVLCPYMPKVI
SQ  EKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKRTWKGPQYEEDVNLGSGTRAVGKPLL
SQ  NSDTSKIKNRIERLRREYSSTWHHDENHPYRTWNYHGSYDVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFG
SQ  QQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPK
SQ  FWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGL
SQ  GLQKLGYILREVGTRPGGKIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTV
SQ  MDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLFENGEERLSRMAVSGDDCVV
SQ  KPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVVPCRGQDELVGRARISPGAGWN
SQ  VRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDK
SQ  TPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRAIIGDEKYVDYMSSLKRYEDTTLVEDTVL
//
ID  C5H431;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  164416;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: C5H431;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0046718;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATKGMNKSRARSRGVNMVAARVKNLAVKVKNKTKQSARGLRGFLLFLVAQIFWARKLTPQVKRLWRMVDKVQGLRILKN
SQ  IRNIVTNLMKGLAGRKKKRSLTVPLVLLLIPLIAYSATVTRQRGLGLLLNVTFADVGKTYEVEGGNCSVNTLDAGKWCED
SQ  YVEYECVTLSEGEEPDDLDCWCYGVDNVRVTYGRCKSGGSRRSRRSAVITPHVDKGLTTRQEKWLPTKIGEQQLQKVEKW
SQ  IMRNPLYALGAVALAYFVGTSNVQRVVIAILLLGIGPAYSTHCLGIPKRDFIRGLDGNTWVSVVLEQGSCVTLIADNKPS
SQ  VDIWLSSIVVDTPTLVRKVCYASSVTGSKATGACPTMGDAHMSEEGNEEWECKRSYSDRGWGNGCGLFGKGSIVACAKFS
SQ  CTHEMEVYQIDATKIEYTISAQVHSGAKKDDWENHTKLVTFVPTTGTSTVAFTGYGNFGLECHVQMMVDLSNSYLVKVGT
SQ  DAWLVNKQWVHDITLPWQSGTGGHWRDKHFMVDFEEPHAVTMKALVLGSQEGALRTALSGAMVVELNSNRYSLKGGHVTC
SQ  KAYMNNLILKGSTYSMCKRGMSFAKQPVETDHGTAVMQIKVTTGAPCRIPVIAADSMAGTENRGSVITTNPIAASNNDEV
SQ  LVEISPPFGESYIIVGNGDDKLTYHWQRSGSTIGNLFTETMKGAQRMIITGEHSWDFGSTGGFFSSIAKAVHTVFGAAFH
SQ  AIFGGLSWITKILIGGLLIWLGLNSRSSSMSMGFICIGALLLVLATGVGAEVGCSLSWKQREMKCGDGVFVFKDSDDWFS
SQ  KYQYIPEDPKTMATLIHQAHQDGLCGLSSVSDLEHRMWYSRVDEINAILDENEVDLTVVVQESDAVYLRGSHAFPRPKSE
SQ  LKYGWKTWGKNIIFNPSRKNGTFIIDGKSKAECPFNKRVWNSIRVEEFGTGVYQTRVFMRPEFDYTKLCDTGTLGAAVKG
SQ  SVSAHGDPMFWMESEEINGTWMITTLEALNYRECEWPSSHTLDGAKVVESDMFMPRSLAGPISKHNHIPGYKVQTSGPWH
SQ  NVPLEIKREECPGTTVVVDEKCDDRAKSVRSTTDSGKIIPEWCCRSCTMPPVSFWGPDGCWYSMEVRPKHTNEAHLVKSW
SQ  VVASKGDVDPFSLGLLMLFLCSDMFLMKRFSMRAILVGSLVMLGAMTLGSLSYLDLLRYAITVGMYMAEINSGGDVTHLA
SQ  LLAVFRVRAGFVSMLALKRLWSPREGFVATCGIVMVQLALGDILSTDIMEWLNAAGMAVLIIKSIVEPKRCNAVLPLLCL
SQ  LTPLTVAEIQRAVMFVCSIVIFVTVWQTDSVSTRKTIPLVALTVCSFFKWTSPFLGIVCYLAFTRLPQRSWPLGETMAAV
SQ  GLVGVLAGMGLKDMNGMLGPVAVGGVLLIVMSLSGKVDGLVIKKVADVTWDEDAEISGASHRYDVEQTDTGEFKLRNEEP
SQ  APWIQVAVLTIAILSAATHPACLAVVTIGWFAWQKTTTRSGVLWDIPTVVPPEEVSYLEDGVYTINQNSFLGLAQKGVGV
SQ  VKDGVFHTMWHVTRGAFLLHAGKRMTPSWANVKEDLISYGGGWKLDAKWDGSEEVQLIAVSPGKVPVNVQTTPSVFQLKN
SQ  GKEIGAVNLDYPSGTSGSPILNKNGDVIGLYGNGILIGNNTYVSAIAQSDSVEEGGTEQLQDIPTMLKKGMLTVLDFHPG
SQ  AGKTRIYLPQILKECEKLKLKTLVLAPTRVVLSEMREAMPKMSIKYHTQAFSNTSTGKEIIDAMCHATLTHRMLEPTRVT
SQ  NWEVVIMDEAHFMDPASIAARGWAAHRSRARECATIFMSATPPGTSNEFPESNGMIEDVKKDVPSEPWTKGHEWILEDRR
SQ  PTAWFLPSIRIANSIANCLRKADRTVVVLNRKTFEKEYPTIKSKKPDFILATDIAEMGANLKVERVIDCRTAYKPILVDD
SQ  ATKVMVKGPLRISASSAAQRRGRIGRDPNRDTDTYIYGDSTTEDNGHYVCWTEGSMLLDNMEIRNGMIAPLYGVEGTKTT
SQ  TSPGETRLREDQRKVFRELVKRLDMPVWFSWQVAKAGLKVQDRSWCFDGEDDNTLLNDNGEPILARSPGGAKKPLKPRWV
SQ  DTRVCSDNASLIDFIKFAEGRRSASGILLGLQGFPEFLSGKMREAIDTVTVLYTSDTGSRAYKHALAMMPEATTIFLLVM
SQ  LAIICTSGVIMFFLAPKGLSRMSMAMMTMLVSAYLMSLGGMNPVQISCVMLVFFIFMVVLIPEPGTQRSTYDNQIIYLLV
SQ  GVLSLILLVAANEMELLEKTKRDIFGAVVVEEAKRWTFPEFDLRPGAAWTVYVGLVTPGNPMLHHWIKIDYGNISLSGIT
SQ  QNAQVLGLMDRGIPFIKMNMSVVILLLSAWNGITLLPLFAGMGAAALHWGFILPGLRAQAAKAAQKRVYHGVAKNPVVDG
SQ  NPTVDIDDAPGMPAMYEKKLALVILLALSILNLVLTRTPFATAEMVVLGSAAVGPLIEGDTNAYWNGPIAVAFSGLMRGN
SQ  YYATIGLAYNGWLAKQTRRGKAAGVTLGEVWKRQLNMLGKQEFERYKVPDITEVDRTAARRYLKEGRTDVGISVSRGAAK
SQ  IRWLHERGYLRITGRVLDLGCGRGGWSYYAAAQKEVMSVKGYTLGIEGHEKPIHMQTLGWNIVKFKDKSNVFTMPTEPSD
SQ  TLLCDIGESSSNPLVERDRTMKVLENFERWKHVNTENFCVKVLAPYHPDVIEKLERLQLRFGGGIVRVPFSRNSTHEMYY
SQ  ISGARNNITHMVNTTSRSLLRRMTRPSGKAIIEGDVFLPTGTRSVASEAGTIDHEALKLRVDQIKAEYSKTWTHDSNHPY
SQ  RTWHYLGSYLCKATGSSSSMINGIVKMLSMPWDKFESVTLLAMTDTTPFGQQRVFKEKVDTKAPPPPPGTRAIMRVVNAW
SQ  LFQHLARKKKPRICTREEFVAKVRSHAALGAYLEEQDKWKSASEAVQDPQFWKLVDDERKLHLQGQCRTCVYNMMGKREK
SQ  KPSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWVSRENSGGGVEGTGLQYLGYILKELGGKTGGNMYADDTAGWDT
SQ  RITEEDLEDEQEILKYMDEKHKKLAWAVTELAYKNKVVKVMRPGPGGLTFMDIISRRDQRGSGQVVTYALNTVTNLKVQL
SQ  IRMAEAEHVITNFDVDTVSQKTLQDLRCWLDRFGADRLSRMAVSGDDCVVKPIDDQFADALTHLNSMSKIRKDIDDWKPS
SQ  QGWASWEDVPFCSHHFHELILKDGRSIIAPCRDQDELIGRARVSPGNGWMIRETACLSKAYAQMWLLMYFHRRDLRVMAN
SQ  AINSTVPVDWVPTGRTTWSIHGKGEWMTTEDMLQVWNRVWIEDNPHQTDKTPITEWRDIPYLPKSIDKTCNSLVGTTQRA
SQ  SWARDIKHTVHRIRGLVGNEKYTDYLATMDRFRELDESGPGEVLW
//
ID  P03314;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  11090;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000269|PubMed:15507646}; Multi-pass membrane protein {ECO:0000269|PubMed:15507646}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:15507646}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000269|PubMed:15507646}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000269|PubMed:15507646}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:3008425}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000269|PubMed:15507646}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P03314;
DR  UNIPROT: O42028;
DR  UNIPROT: O91857;
DR  UNIPROT: P19901;
DR  UNIPROT: Q102J3;
DR  UNIPROT: Q45RQ2;
DR  UNIPROT: Q89275;
DR  UNIPROT: Q89276;
DR  UNIPROT: Q9W878;
DR  UNIPROT: Q9YWN0;
DR  UNIPROT: Q9YWN1;
DR  UNIPROT: Q9YWN2;
DR  PDB: 1NA4;
DR  PDB: 1YKS;
DR  PDB: 3EVA;
DR  PDB: 3EVB;
DR  PDB: 3EVC;
DR  PDB: 3EVD;
DR  PDB: 3EVE;
DR  PDB: 3EVF;
DR  PDB: 5FFM;
DR  PDB: 5N6B;
DR  PDB: 6EPK;
DR  PDB: 6IW0;
DR  PDB: 6IW1;
DR  PDB: 6IW2;
DR  PDB: 6IW4;
DR  PDB: 6QSN;
DR  PDB: 6SS7;
DR  PDB: 6SS8;
DR  PDB: 6SS9;
DR  PDB: 6SSA;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000269|PubMed:27849599}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:9371625}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (PubMed:18199634). {ECO:0000255|PROSITE-ProRule:PRU00860, ECO:0000269|PubMed:18199634}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway (PubMed:15956546). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15956546}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:19850911). NS5 methylates viral RNA cap at guanine N- 7 and ribose 2'-O positions (PubMed:19850911). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:25211074). IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition (PubMed:25211074). {ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:25211074}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0140533;
GO  GO:0046762;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRRGVRSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKITAHLKRLWKMLDPRQGLAV
SQ  LRKVKRVVASLMRGLSSRKRRSHDVLTVQFLILGMLLMTGGVTLVRKNRWLLLNVTSEDLGKTFSVGTGNCTTNILEAKY
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGKCDSAGRSRRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQ
SQ  KIERWFVRNPFFAVTALTIAYLVGSNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQDKCVTVMA
SQ  PDKPSLDISLETVAIDRPAEVRKVCYNAVLTHVKINDKCPSTGEAHLAEENEGDNACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNTDIKTLKFDALSGSQEVEFIGYGKATLECQVQTAVDFGNSYI
SQ  AEMETESWIVDRQWAQDLTLPWQSGSGGVWREMHHLVEFEPPHAATIRVLALGNQEGSLKTALTGAMRVTKDTNDNNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKICTDKMFFVKNPTDTGHGTVVMQVKVSKGAPCRIPVIVADDLTAAINKGILVTVNPI
SQ  ASTNDDEVLIEVNPPFGDSYIIVGRGDSRLTYQWHKEGSSIGKLFTQTMKGVERLAVMGDTAWDFSSAGGFFTSVGKGIH
SQ  TVFGSAFQGLFGGLNWITKVIMGAVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAINFGKRELKCGDGIFIF
SQ  RDSDDWLNKYSYYPEDPVKLASIVKASFEEGKCGLNSVDSLEHEMWRSRADEINAIFEENEVDISVVVQDPKNVYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLVFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGTGVFTTRVYMDAVFEYTIDCDGS
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMIHTLEALDYKECEWPLTHTIGTSVEESEMFMPRSIGGPVSSHNHIPGYKV
SQ  QTNGPWMQVPLEVKREACPGTSVIIDGNCDGRGKSTRSTTDSGKVIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPRKTHE
SQ  SHLVRSWVTAGEIHAVPFGLVSMMIAMEVVLRKRQGPKQMLVGGVVLLGAMLVGQVTLLDLLKLTVAVGLHFHEMNNGGD
SQ  AMYMALIAAFSIRPGLLIGFGLRTLWSPRERLVLTLGAAMVEIALGGVMGGLWKYLNAVSLCILTINAVASRKASNTILP
SQ  LMALLTPVTMAEVRLAAMFFCAVVIIGVLHQNFKDTSMQKTIPLVALTLTSYLGLTQPFLGLCAFLATRIFGRRSIPVNE
SQ  ALAAAGLVGVLAGLAFQEMENFLGPIAVGGLLMMLVSVAGRVDGLELKKLGEVSWEEEAEISGSSARYDVALSEQGEFKL
SQ  LSEEKVPWDQVVMTSLALVGAALHPFALLLVLAGWLFHVRGARRSGDVLWDIPTPKIIEECEHLEDGIYGIFQSTFLGAS
SQ  QRGVGVAQGGVFHTMWHVTRGAFLVRNGKKLIPSWASVKEDLVAYGGSWKLEGRWDGEEEVQLIAAVPGKNVVNVQTKPS
SQ  LFKVRNGGEIGAVALDYPSGTSGSPIVNRNGEVIGLYGNGILVGDNSFVSAISQTEVKEEGKEELQEIPTMLKKGMTTVL
SQ  DFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGREVIDAMCHATLTYRMLE
SQ  PTRVVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWNTGHDWI
SQ  LADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEREYPTIKQKKPDFILATDIAEMGANLCVERVLDCRTAFKP
SQ  VLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSENNAHHVCWLEASMLLDNMEVRGGMVAPLYGVE
SQ  GTKTPVSPGEMRLRDDQRKVFRELVRNCDLPVWLSWQVAKAGLKTNDRKWCFEGPEEHEILNDSGETVKCRAPGGAKKPL
SQ  RPRWCDERVSSDQSALSEFIKFAEGRRGAAEVLVVLSELPDFLAKKGGEAMDTISVFLHSEEGSRAYRNALSMMPEAMTI
SQ  VMLFILAGLLTSGMVIFFMSPKGISRMSMAMGTMAGCGYLMFLGGVKPTHISYVMLIFFVLMVVVIPEPGQQRSIQDNQV
SQ  AYLIIGILTLVSAVAANELGMLEKTKEDLFGKKNLIPSSASPWSWPDLDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYGN
SQ  LSLSGIAQSASVLSFMDKGIPFMKMNISVIMLLVSGWNSITVMPLLCGIGCAMLHWSLILPGIKAQQSKLAQRRVFHGVA
SQ  ENPVVDGNPTVDIEEAPEMPALYEKKLALYLLLALSLASVAMCRTPFSLAEGIVLASAALGPLIEGNTSLLWNGPMAVSM
SQ  TGVMRGNHYAFVGVMYNLWKMKTGRRGSANGKTLGEVWKRELNLLDKRQFELYKRTDIVEVDRDTARRHLAEGKVDTGVA
SQ  VSRGTAKLRWFHERGYVKLEGRVIDLGCGRGGWCYYAAAQKEVSGVKGFTLGRDGHEKPMNVQSLGWNIITFKDKTDIHR
SQ  LEPVKCDTLLCDIGESSSSSVTEGERTVRVLDTVEKWLACGVDNFCVKVLAPYMPDVLEKLELLQRRFGGTVIRNPLSRN
SQ  STHEMYYVSGARSNVTFTVNQTSRLLMRRMRRPTGKVTLEADVILPIGTRSVETDKGPLDKEAIEERVERIKSEYMTSWF
SQ  YDNDNPYRTWHYCGSYVTKTSGSAASMVNGVIKILTYPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRKI
SQ  MKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAIGAYLEEQEQWKTANEAVQDPKFWELVDEERKLHQQGRCRTCVYN
SQ  MMGKREKKLSEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIRDLAAMDGGGFYAD
SQ  DTAGWDTRITEADLDDEQEILNYMSPHHKKLAQAVMEMTYKNKVVKVLRPAPGGKAYMDVISRRDQRGSGQVVTYALNTI
SQ  TNLKVQLIRMAEAEMVIHHQHVQDCDESVLTRLEAWLTEHGCDRLKRMAVSGDDCVVRPIDDRFGLALSHLNAMSKVRKD
SQ  ISEWQPSKGWNDWENVPFCSHHFHELQLKDGRRIVVPCREQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHKR
SQ  DMRLLSLAVSSAVPTSWVPQGRTTWSIHGKGEWMTTEDMLEVWNRVWITNNPHMQDKTMVKKWRDVPYLTKRQDKLCGSL
SQ  IGMTNRATWASHIHLVIHRIRTLIGQEKYTDYLTVMDRYSVDADLQLGELI
//
ID  P29165;
PN  Non-structural protein 2A;
GN  POLG;
OS  31641;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P29165;
DR  Pfam: PF01003;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01570;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0004386;
GO  GO:0016787;
GO  GO:0046983;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRQGVRSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNVLTGRKITAHLKKLWRMLDPRQGLAV
SQ  LKKVKRVVASLMRGLSSRKRRSYEVLTVQFLILGMLLMTGGVTLVRKSRWLLLNVTSEDLGKTFSVGTGNCTTNILEAKN
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGKCDSAGRSRRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQ
SQ  KIERWLVRNPFFAVTALAIAYLVGSNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQDKCVTVMA
SQ  PDKPSLDISLETVAIDGPAEARKVCYSAVLTHVKINDKCPSTGEAHLAEENEGDHACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNADIKTLKFDALSGSQEAEFTGYGKATLECQVQTAVDFSNSYI
SQ  AEMEKESWIVDRQWAQDLTLPWQSGSGGVWREMHHLVEFEPPHAATIKVLALGNQEGSLKTALTGAMRVTKDTNGSNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTAVMQVKVPKGAPCRIPVMVADDLTASVNKGILVTVNPI
SQ  ASTNEDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGFFTSVGKGIH
SQ  MVFGSAFQGLFGGLSWITKVIMGAVLIWVGINMRNMTMSMSMILVGVIMMFLSLGVGADQGCAINFGKRELKCGDGVFIF
SQ  RDSDDWLNKYSYYPEDPVKLASIVKASFEEGKCGLNSVDSLEHEMWRSRADEINAILEENEVDISVVVQDPKNIYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLVFSPGRKNGSFIIDGKSRKECPFSNRVWNSLQIEEFGTGVFTTRVYMDAVFEYTMDCDGS
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMIHTLETLDYKECEWPLTHTIGTSVEESDMFMPRSIGGPVSSHNHIPGYKV
SQ  QTNGPWMQVPLEVKREACPGTSVVVDGGCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPRKTHD
SQ  NHLVRSWVTAGEVHAVPFGLVSMMIAMEVFLKKRQGPKQILVG
//
ID  Q6DV88;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  407134;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q6DV88;
DR  UNIPROT: Q89278;
DR  PDB: 2JQM;
DR  PDB: 2JV6;
DR  PDB: 6EPK;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRRGVRSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKITAHLKRLWKMLDPRQGLAV
SQ  LRKVKRVVASLMRGLSSRKRRSHDVLTVQFLILGMLLMTGGVTLVRKNRWLLLNVTSEDLGKTFSVGTGNCTTNILEAKY
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGKCDSAGRSRRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQ
SQ  KIERWLVRNPFFAVTALTIAYLVGSNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQDKCVTVMA
SQ  PDKPSLDISLETVAIDGPAEARKVCYNAVLTHVKINDKCPSTGEAHLAEENEGDNACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNTDIKTLKFDALSGSQEAEFTGYGKATLECQVQTAVDFGNSYI
SQ  AEMEKESWIVDRQWAQDLTLPWQSGSGGVWREMHHLVEFEPPHAATIRVLALGNQEGSLKTALTGAMRVTKDTNDNNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTVVMQVKVPKGAPCKIPVIVADDLTAAINKGILVTVNPI
SQ  ASTNDDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGFFTSVGKGIH
SQ  TVFGSAFQGLFGGLNWITKVIMGAVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAINFGKRELKCGDGIFIF
SQ  RDSDDWLNKYSYYPEDPVKLASIVKASFEEGKCGLNSVDSLEHEMWRSRADEINAILEENEVDISVVVQDPKNVYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLVFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGTGVFTTRVYMDAVFEYTIDCDGS
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMIHTLEALDYKECEWPLTHTIGTSVEESEMFMPRSIGGPVSSHNHIPGYKV
SQ  QTNGPWMQVPLEVKREACPGTSVIIDGNCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPRKTHE
SQ  SHLVRSWVTAGEIHAVPFGLVSMMIAMEVVLRKRQGPKQMLVGGVVLLGAMLVGQVTLLDLLKLTVAVGLHFHEMNNGGD
SQ  AMYMALIAAFSIRPGLLIGFGLRTLWSPRERLVLTLGAAMVEIALGGMMGGLWKYLNAVSLCILTINAVASRKASNTILP
SQ  LMALLTPVTMAEVRLATMLFCTVVIIGVLHQNSKDTSMQKTIPLVALTLTSYLGLTQPFLGLCAFLATRIFGRRSIPVNE
SQ  ALAAAGLVGVLAGLAFQEMENFLGPIAVGGILMMLVSVAGRVDGLELKKLGEVSWEEEAEISGSSARYDVALSEQGEFKL
SQ  LSEEKVPWDQVVMTSLALVGAAIHPFALLLVLAGWLFHVRGARRSGDVLWDIPTPKIIEECEHLEDGIYGIFQSTFLGAS
SQ  QRGVGVAQGGVFHTMWHVTRGAFLVRNGKKLIPSWASVKEDLVAYGGSWKLEGRWDGEEEVQLIAAVPGKNVVNVQTKPS
SQ  LFKVRNGGEIGAVALDYPSGTSGSPIVNRNGEVIGLYGNGILVGDNSFVSAISQTEVKEEGKEELQEIPTMLKKGMTTIL
SQ  DFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGREVIDAMCHATLTYRMLE
SQ  PTRVVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWNTGHDWI
SQ  LADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEREYPTIKQKKPDFILATDIAEMGANLCVERVLDCRTAFKP
SQ  VLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGVE
SQ  GTKTPVSPGEMRLRDDQRKVFRELVRNCDLPVWLSWQVAKAGLKTNDRKWCFEGPEEHEILNDSGETVKCRAPGGAKKPL
SQ  RPRWCDERVSSDQSALSEFIKFAEGRRGAAEVLVVLSELPDFLAKKGGEAMDTISVFLHSEEGSRAYRNALSMMPEAMTI
SQ  VMLFILAGLLTSGMVIFFMSPKGISRMSMAMGTMAGCGYLMFLGGVKPTHISYIMLIFFVLMVVVIPEPGQQRSIQDNQV
SQ  AYLIIGILTLVSVVAANELGMLEKTKEDLFGKKNLIPSSASPWSWPDLDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYGN
SQ  LSLSGIAQSASVLSFMDKGIPFMKMNISVIILLVSGWNSITVMPLLCGIGCAMLHWSLILPGIKAQQSKLAQRRVFHGVA
SQ  KNPVVDGNPTVDIEEAPEMPALYEKKLALYLLLALSLASVAMCRTPFSLAEGIVLASAALGPLIEGNTSLLWNGPMAVSM
SQ  TGVMRGNYYAFVGVMYNLWKMKTGRRGSANGKTLGEVWKRELNLLDKQQFELYKRTDIVEVDRDTARRHLAEGKVDTGVA
SQ  VSRGTAKLRWFHERGYVKLEGRVIDLGCGRGGWCYYAAAQKEVSGVKGFTLGRDGHEKPMNVQSLGWNIITFKDKTDIHR
SQ  LEPVKCDTLLCDIGESSSSSVTEGERTVRVLDTVEKWLACGVDNFCVKVLAPYMPDVLEKLELLQRRFGGTVIRNPLSRN
SQ  STHEMYYVSGARSNVTFTVNQTSRLLMRRMRRPTGKVTLEADVILPIGTRSVETDKGPLDKEAIEERVERIKSEYMTSWF
SQ  YDNDNPYRTWHYCGSYVTKTSGSAASMVNGVIKILTYPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRKI
SQ  MKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAIGAYLEEQEQWKTANEAVQDPKFWELVDEERKLHQQGRCRTCVYN
SQ  MMGKREKKLSEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIRDLAAMDGGGFYAD
SQ  DTAGWDTRITEADLDDEQEILNYMSPHHKKLAQAVMEMTYKNKVVKVLRPAPGGKAYMDVISRRDQRGSGQVVTYALNTI
SQ  TNLKVQLIRMAEAEMVIHHQHVQDCDESVLTRLEAWLTEHGCNRLKRMAVSGDDCVVRPIDDRFGLALSHLNAMSKVRKD
SQ  ISEWQPSKGWNDWENVPFCSHHFHELQLKDGRRIVVPCREQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHKR
SQ  DMRLLSLAVSSAVPTSWVPQGRTTWSIHGKGEWMTTEDMLEVWNRVWITNNPHMQDKTMVKEWRDVPYLTKRQDKLCGSL
SQ  IGMTNRATWASHIHLVIHRIRTLIGQEKYTDYLTVMDRYSVDADLQPGELI
//
ID  Q6J3P1;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  407136;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q6J3P1;
DR  UNIPROT: Q6PX46;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRRGVRSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKITAHLKRLWKMLDPRQGLAV
SQ  LRKVKRVVASLMRGLSSRKRRSHDALAVQFLILGMLLMAGGVTLVRKNRWLLLNVTSEDLGKTFSVGAGNCTTNILEAKY
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGKCDSAGRSRRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQ
SQ  KIERWLVRNPFFAVTALTIAYLVGSNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQDKCVTVMA
SQ  PDKPSLDISLETVAIDGPAEARKVCYNAVLTHVKINDKCPSTGEAHLAEENEGDNACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNTDIKTLKFDALSGSQEAEFTGYGKATLECQVQTAVDFGNSYI
SQ  AEMEKESWIVDRQWAQDLTLPWQSGSGGVWREMHHLVEFEPPHAATIRVLALGNQEGSLKTALTGAMRVTKDTNDNNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTVVMQVKVPKGAPCKIPVIVADDLTAAINKGILVTVNPI
SQ  ASTNDDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGFLTSVGKGIH
SQ  TVFGSAFQGLFGGLSWITKVIMGAVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAINFGKRELKCGDGIFIF
SQ  RDSDDWLNKYSYYPEDPVKLASIVKASFEEGKCGLNSVDSLEHEMWRSRADEINAILEENEVDISVVVQDPKNVYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLVFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGTGVFTTRVYMDAVFEYTIDCDGS
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMIHTLEALDYKECEWPLTHTIGTSVEESEMFMPRSIGGPVSSHNHIPGYKV
SQ  QTNGPWMQVPLEVRREACPGTSVIIDGNCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPRKTHE
SQ  SHLVRSWVTAGEIHAVPFGLVSMMIAMEVVLRKRQGPKQMLVGGVVLLGAMLVGQVTLLDLLKLTVAVGLHFHEMNNGGD
SQ  AMYMALIAAFSIRPGLLIGFGLRTLWSPRERLVLTLGAAMVEIALGGMMGGLWKYLNAVSLCILTINAVASRKASNTILP
SQ  LMALLTPVTMAEVRLAAMLFCTVVIIGVLHQNSKDTSMQKTIPLVALTLTSYLGLTQPFLGLCAFLATRLFGRRSIPVNE
SQ  ALAAAGLVGVLAGLAFQEMENFLGPIAVGGILMMLVSVAGRVDGLELRKLGEVSWEEEAEISGSSARYDVALSEQGEFKL
SQ  LSEEKVPWDQVVMTSLALVGAAIHPFALLLVLAGWLFHVKGARRSGDVLWDIPTPKIIEECEHLEDGIYGIFQSTFLGAS
SQ  QRGVGVAQGGVFHTMWHVTRGAFLVRNGKKLIPSWASVKEDLVAYGGSWKLEGRWDGEEEVQLIAAVPGKNVVNVQTKPS
SQ  LFKVRNGGEIGAVALDYPSGTSGSPIVNRNGEVIGLYGNGILVGDNSFVSAISQTEVKEEGKEELQEIPTMLKKGMTTIL
SQ  DFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGREVIDAMCHATLTYRMLE
SQ  PTRIVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWNTGHDWI
SQ  LADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEREYPTIKQKKPDFILATDIAEMGANLCVERVLDCRTAFKP
SQ  VLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGVE
SQ  GTKTPVSPGEMRLRDDQRKVFRELVRNCDQPVWLSWQVAKAGLKTNDRKWCFEGPDEHEILNDSGETVKCRAPGGAKKPL
SQ  RPRWCDERVSSDQSALADFIKFAEGRRGAAEVLVVLSELPDFLAKKGGEAMDTISVFLHSEEGSRAYRNALSMMPEAMTI
SQ  AMLFILAGLLTSGMVIFFMSPKGISRMSMAMGTMAGCGYLMFLGGVKPTHISYIMLIFFVLMVVVIPEPGQQRSIQDNQV
SQ  AYLIIGILTLVSVVAANELGMLEKTKEDLFGKKDLIPSSASPWSWPDLDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYGN
SQ  LSLSGIAQSASVLSFMDKGIPFMKMNISVIILLVSGWNSITVMPLLCGIGCAMLHWSLILPGIKAQQSKLAQRRVFHGVA
SQ  KNPVVDGNPTVDIEEAPEMPALYEKKLALYLLLALSLASVAMCRTPFSLAEGIVLASAALGPLIEGNTSLLWNGPMAVSM
SQ  TGVMRGNYYAFVGVMYNLWKMKTGRRGRANGKTLGEVWKRELNLLDKQQFELYKRTDIVEVDRDTARRHLAEGKVDTGVA
SQ  VSRGTAKLRWFHERGYVKLEGRVTDLGCGRGGWCYYAAAQKEVSGVKGFTLGRDGHEKPMNVQSLGWNIITFKDKTDIHR
SQ  LEPMKCDTLLCDIGESSSSSVTEGERTMRVLDTVEKWLACGVDNFCVKVLAPYMPDVLEKLELLQRRFGGTVIRNPLSRN
SQ  STHEMYYVSGARSNVTFTVNQTSRLLMRRMRRPTGKVTLEADVILPIGTRSVETDKGPLDREAIEERVERIKSEYMTTWF
SQ  YDNDNPYRTWHYCGSYVTKTSGSAASMVNGVIKILTYPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRKI
SQ  MKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAIGAYLEEQEQWKTANEAVQDPKFWELVDEERKLHQQGRCRTCVYN
SQ  MMGKREKKLSEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIRDLAAMDGGGFYAD
SQ  DTAGWDTRITEADLDDEQEILNYMSPHHKKLAQAVMEMTYKNKVVKVLRPAPGGKAYMDVISRRDQRGSGQVVTYALNTI
SQ  TNLKVQLIRMAEAEMVIHHQHVQDCDESALARLEAWLTEHGCDRLKRMAVSGDDCVVRPIDDRFGLALSHLNAMSKVRKD
SQ  ISEWQPSKGWNDWENVPFCSHHFHELHLKDGRRIVVPCREQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHKR
SQ  DMRLLSLAVSSAVPTSWVPQGRTTWSIHGKGEWMTTEDMLGVWNRVWITNNPHMQDKTVVKEWRDVPYLTKRQDKLCGSL
SQ  IGMTNRATWASHIHLVIHRIRTLIGQEKYTDYLTVMDRYSVDADLQPGELI
//
ID  Q074N0;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  407141;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q074N0;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRRGARSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKLTTHLKRLWRMLDPRQGLAV
SQ  LRKVKRVVASLMIGLSSRKRRSNEMAMMPLLILSMVILAGGVTLVRKNRWLLLNVTAEDLGKTFSLGTGNCTTNILEAKY
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGRCDAVGRSKRSRRAIDLPTHENHGLKTRQEKWMAGRMGERQLQ
SQ  KIERWLVRNPFFAITALAIAYLVGNNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQGKCVTVMA
SQ  PDKPSLDISLQTVAIDGPAEARKVCYSAVLTHVKINDKCPSTGEAHLAEENDGDNACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNTDIKTLKFDALSGSQEAEFTGYGKATLECQVQTAVDFGNSYI
SQ  AEMEKDSWIVDRQWAQDLTLPWQSGSGGIWREMHHLVEFEPPHAATIRVLALGNQEGSLKTALTGAMRVTKDENDNNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTVVMQVKVPKGAPCKIPVIVADDLTAAVNKGILVTVNPI
SQ  ASTNDDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGFFTSVGKGIH
SQ  TVFGSAFQGLFGGLSWITKVIMGAVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAVNFGKRELKCGDGIFVF
SQ  RDSDDWLTKYSYYPEDPVKLASIIKASHEEGKCGLNSVDSLEHEMWRSRADEINAIFEENEVDISVVVQDPKNIYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLIFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGMGVFTTRVFMDAVFDYSVDCDGA
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMVHTLETLDYKECEWPLTHTIGTSVEESDMFMPRSIGGPVSSHNHIPGYKV
SQ  QTNGPWMQVPLEVRREPCPGTSVVLDTGCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPMKTHE
SQ  SHLVRSWVTAGEVHAVPFGLVSMMIAMEVVLRKRQGPKQMLVGGIILLGAMLVGQVTVLDLVKLIVAVGLHFHEINNGGD
SQ  AMYMALIASFSIRPGLLVGFGLRTLWSPRERLVMAFGAAMVEVALGGMMGGLWQYLNAVSLCVLTINAISSRKASNAVLP
SQ  LMALLTPVTMHEVRMATMLFCTVVIVGVLHQNAKDTSMQKTIPIVALTLTSYMGLTQPFLGLCAYMSTQVFGRRSIPVNE
SQ  ALAAAGLVGVLAGLAFQDMENFLGPIAVGGILMMLVSVAGKVDGLELKKLGEVSWEEEAEISGSSSRYDVALSEQGEFKL
SQ  LSEDKVPWDQIVMTSLALVGAAIHPFALLLVLGGWVLHIKGARRSGDVLWDIPTPKVIEECEYLEDGIYGIFQSTFLGAS
SQ  QRGVGVAQGGVFHTMWHVTRGAFLLRNGKKLVPSWASVKEDLVAYGGSWKLDGKWDGEEEVQLIAAVPGKAVVNVQTKPS
SQ  VFKVRNGGEIGAVALDYPSGTSGSPIVNRSGEVVGLYGNGILVGDNSFVSAISQTEVKEESKEELQEIPTMLKKGMTTIL
SQ  DFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGKEVIDAMCHATLTYRMLE
SQ  PTRAVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWTSGHEWI
SQ  LADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEKEYPTIKQKRPDFILATDIAEMGANLCVERVLDCRTAYKP
SQ  VLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGIE
SQ  GTKTPVSPGEMRLRDDQRRVFRELVRGCDLPVWLSWQVAKPGLKTNDRKWCFEGPEEHEILNDNGETVKCRSPGGAKKAL
SQ  RPRWCDERVSSDQSALADFIKFAEGRRGAAEMLVVLTELPDFLAKKGGEAMDTISVFLHSEEGSRAYRNALSMMPEAMTI
SQ  VMLFILAGLLTSGMVIFFMSPKGMSRMSMAMGTMAGSGYLMFLGGVKPTHISYVMLIFFVLMVVIIPEPGQQRTIQDNQV
SQ  AYLIIGILTLLSIVAANELGMLEKTKEDFFGRRNIATSGGTIPWSWPDLDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYG
SQ  NLSLSGIAQSASVLSFMDKGIPFMKMNISVVILLVSGWNSITVIPLLCGVGGAMLHWTLILPGIKAQQSKLAQKRVFHGV
SQ  AKNPVVDGNPTADIEEAPEMPALYEKKLALYLLLALSLMSVAMCRTPFSLAEGIVLSSAALGPLIEGNTSLLWNGPMAVS
SQ  MTGVMRGNYYAFVGVMYNLWKMKTGRRGSASGKTLGEVWKRELNLLDKQQFELYKRTDITEVDRDMARRHLAEGKVDTGV
SQ  AVSRGTAKLRWFHERGYVKLEGRVMDLGCGRGGWCYYAAAQKEVSGVKGYTLGRDGHEKPMNVQSLGWNIVTFKDKTDIH
SQ  RLEPAKCETLLCDIGESSPSSVTEGERTLRVLETIEKWLACGVDNFCVKVLAPYMPDVIEKLELLQRRFGGTIIRNPLSR
SQ  NSTHEMYYVSGARSNITFTVNQTSRLLMRRMRRPTGKVTLEPDVILPIGTRSVETDKGPLDRDAIEERVERIKTEYAATW
SQ  FYDNDNPYRTWHYCGSYITKTSGSAASMINGVIKILTFPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRK
SQ  IMKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAVGAFLEEQEQWKTANEAVQDPKFWEMVDAERKLHQQGRCQSCVY
SQ  NMMGKREKKLSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIKDLSTKEGGGFYA
SQ  DDTAGWDTRITEADLDDEQEIMSYMNAEQRKLAWAVMEMTYKNKVVKVLRPAPGGKAFMDIISRRDQRGSGQVVTYALNT
SQ  ITNLKVQLIRMAEAEMVINHQHVNECDEGVLARLDAWLAENGCDRLARMAVSGDDCVVRPVDDRFGLALSHLNAMSKVRK
SQ  DISEWQPSKEWTDWENVPFCSHHFHELVLKDGRKVVVPCRDQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHK
SQ  RDMRLLSFAVSSAVPMAWVPSGRTTWSVHGKGEWMTTQDMLDVWNRVWVLNNPHMKDKTTVKEWRDVPYLTKRQDKLCGS
SQ  LIGMTNRATWASHIHLVIHRIRTLIGQEKYTDYLTVMDRYSVDADLQPGELI
//
ID  Q89277;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  407135;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q89277;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRRGVRSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKITAHLKRLWKMLDPRQGLAA
SQ  LRKVKRVVAGLMRGLSSRKRRSHDVLTVQFLILGMLLMTGGVTLVRKNRWLLLNVTSEDLGKTFSMGTGNCTTNILEAKY
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGKCDSAGRSRRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQ
SQ  KIERWFVRNPFFAVTALTIAYLVGSNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQDKCVTVMA
SQ  PDKPSLDISLETVAIDGPVEARKVCYNAVLTHVKINDKCPSTGEAHLAEENEGDNACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIRARLHVGAKQENWKTDIKTLKFDALSGSQEAEFTGYGKATLECQVQTAVDFGNSYI
SQ  AEMEKESWIVDRQWAQDLTLPWQSGSGGVWREMHHLVEFEPPHAATIRVLALGDQEGSLKTALTGAMRVTKDTNDNNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTVVMQVKVPKGAPCRIPVIVADDLTAAINKGILVTVNPI
SQ  ASTNDDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGFFTSVGKGIH
SQ  TVFGSAFQGLFGGLNWITKVIIGAVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAINFAKRELKCGDGIFIF
SQ  RDSDDWLNKYSYYPEDPVKLASIVKASFEEGKCGLNSVDSLEHEMWRSRADEINAILEENEVDISVVVQDPKNVYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLVFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGTGVFTTRVYMDAVFEYTIDCDGS
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMIHTLEALDYKECEWPLTHTIGTSVEESEMFMPRSIGGPVSSHNHIPGYKV
SQ  QTNGPWMQVPLEVKREACPGTSVIIDGNCDGRGKSARSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPRKTHE
SQ  SHLVRSWVTAGEIHAVPFGLVSMMIALEVVLRKRQGPKQMLVGGVVLLGAMLVGQVTLLDLLKLTVAVGLHFHEMNNGGD
SQ  AMYMALIAAFSVRPGLLIGFGLRTLWSPRERLVLALGAAMVEIALGGMMGGLWKYLNAVSLCILTINAVASRKASNTILP
SQ  LMALLTPVTMAEVRLATMLFCTVVIIGVLYQNSKDTSMQKTIPLVALTLTSYLGLTQPFLGLCAFLATRIFGRRSIPVNE
SQ  ALAAAGLVGVLAGLAFQEMENFLGPIAVGGILMMLVSVAGRVDGLELKKLGEVAWEEEAEISGSSARYDVALSEQGEFKL
SQ  LSEEKVPWDQVVMTSLALVGAAIHPFALLLVLAGWLFHVRGARRSGDVLWDIPTPKVIEECEHLEDGIYGIFQSTFLGAS
SQ  QRGVGVAQGGVFHTMWHVTRGAFLVRNGKKLIPSWASVKEDLVAYGGSWKLEGRWDGEEEVQLIAAVPGKNVVNVQTKPS
SQ  LFKVRNGGEIGAVALDYPSGTSGSPIVNRNGEVIGLYGNGILVGDNSFVSAISQTEVKEEGKEELQEIPTMLKKGKTTIL
SQ  DFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGREVIDAMCHATLTYRMLE
SQ  PTRIVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWNTGHDWI
SQ  LADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEREYPTIKQKKPDFILATDIAEMGANLCVERVLDCRTAFKP
SQ  VLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGVE
SQ  GTKTPVSPGEMRLRDDQRKVFRELVRNCDLPVWLSWQVAKAGLKTNDRKWCFEGPEEHEILNDSGETVKCRTPGGAKKPL
SQ  RPRWCDERVSSDQSALSEFIKFAEGRRGAAEVLVVLSELPDFLAKKGGEAMDTISVLLHSEEGSRAYRNALSMMPEAMTI
SQ  VMLFILAGLLTSGMVIFFMSPKGISRMSMAMGTMAGCGYLMFLGGVKPTHISYIMLIFFVLMVVVIPEPGQQRSIQDNQV
SQ  AFLIIGILTLVSVVAANELGMLEKTKEDLFGKKNSIPSSASPWSWPDLDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYGN
SQ  LSLSGIAQSASVLSFMDKGIPFMKMNISVIMLLISGWNSITVMPLLCGIGCAMLHWSLILPGIKAQQSKLAQRRVFHGVA
SQ  KNPVVDGNPTVDIEEAPEMPVLYEKKLALYLLLALSLASVAMCRTPFSLAEGIVLASAALGPLIEGNTSLLWNGPMAVSM
SQ  TGVMRGNYYAFVGVMYNLWKMKTGRRGTANGKTLGEVWKRELNLLDKQQFELYKRTDIVEVDRDTARRHLAEGKVDTGVA
SQ  VSRGTAKLRWFHERGYVKLEGRVIDLGCGRGGWCYYAAAQKEVSGVKGFTLGRDGHEKPMNVQSLGWNIITFKDKTDIHR
SQ  LEPVKCDTLLCDIGESSSSSVTEGERTVRVLDTVEKWLACGVDNFCVKVLAPYMPDVLEKLELLQRRFGGTVIRNPLSRN
SQ  STHEMYYVSGARSNVTFTVNQTSRLLMRRMRRPTGKVTLEADVTLPIGTRSVETDKGPLDKEAIEERVERIKSEYMTSWF
SQ  YDNDNPYRTWHYCGSYVTKTSGSAASMVNGVIKILTYPWDKIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRKI
SQ  MKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAIGAYLEEQEQWKTANEAVQDPKFWELVDEERKLHQQGRCRTCVYN
SQ  MMGKREKKLSEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIRDLAAMDGGGFYAD
SQ  DTAGWDTRITEADLDDEQEILNYMSPHHKKLAQAVMEMTYKNKVVKVLRPAPGGKAYMDVISRRDQRGSGQVVTYALNTI
SQ  TNLKVQLIRMAEAEMVIHHQHVQDCDESVLTRLEAWLTEHGCNRLRRMAVSGDDCVVRPIDDRFGLALSHLNAMSKVRKD
SQ  ISEWQPSKGWNDWENVPFCSHHFHELQLKDGRRIVVPCREQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHKR
SQ  DMRLLSLAVSSAVPTSWVPQGRTTWSIHGKGEWMTTEDMLEVWNRVWITNNPHMQDKTMVKEWRDVPYLTKRQDKLCGSL
SQ  IGMTNRATWASHIHLVIHRIRTLVGQEKYTDYLTVMDRYSVDADLQPGELI
//
ID  Q98803;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  407138;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q98803;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRRGVRSLSNKIKQKTKQIGNRPGPSRGVQGFISFFSFNILTGKKITAHLKRLWKMLDPRQGLAV
SQ  LRKVKRVVAGLMRGLSSRKRRSHDVLTVQFLILGMLLMAGGVTLVRKNRWLLLNVTSEDLGKTFSVGTGNCTTNILEAKY
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGKCDSAGRSRRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQ
SQ  KIERWLVRNPFFAVTALAIAYLVGSNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQDKCVTVMA
SQ  PDKPSLDISLETVAIDGPAEARKVCYNAVLTHVKINDKCPSTGEAHLAEENEGDNACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNTDIKTLKFDALSGSQEAEFTGYGKATLECRVQTAVDFGNSYI
SQ  AEMEKESWIVDRQWAQDLTLPWQSGSGGVWREMHHLVEFEPPHAATIRVLALGNQEGSLKTALTGAMRVTKDTNDNNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTDHGTVVMQVKVPKGAPCKIPVIVADDLTAAINKGILVTVNPI
SQ  ASTNDDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGLFTSIGKGSH
SQ  TVFGSAFQGLFGGLSWITKVIMGAVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAINFGKRELKCGDGIFIF
SQ  RDSDDWLNKYSYYPEDPVKLASIVKASFEEGKCGLNSVDSLDHEMWRSRADEINAILEENEVDISVVVQDPKNVYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLVFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGTGVFTTRVYMDAVFEYTIDCDGS
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMIHTLETLDYKECEWPLTHTIGTSVEESDMFMPRSIGGPVSSHNHIPGYKV
SQ  QTNGPWMQVPLEVKREACPGTSVIIDGNCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGNDGCWYPMEIRPRKTHE
SQ  SHLVRSWVTAGEIHAVPFGLVSMMIAMEVVLRKRQGPKQMLVGGMVLLGAMLVGQVTLLDLLKLTMAVGLHFHEMNNGGD
SQ  AMYMALIAAFSIRPGLLIGFGLRTLWSPRERLVLTLGAAMVEIALGGMMGGLWKYLNAVSLCILTINAVASRKASNTILP
SQ  LMALLTPVTMAEVRLATMLLCAVVIIGVLHQNSKDTSMQKTIPLVALTLTSYLGLTQPFLGLCAFLATRIFGRRSIPVNE
SQ  ALAAAGLVGVLAGLAFQEMENFLGPIAVGGILMMLVSVAGRVDGLELKKLGEVSWEEEAEISGSSARYDVALSEQGEFKL
SQ  LSEEKVPWDQVVMTSLALVGAAIHPSALLLVLAGWLFHVKGARRSGDVLWDIPTPKIIEECEHLEDGIYGIFQSTFLGAS
SQ  QRGVGVAQGGVFHTMWHVTRGAFLVRNGKKLIPSWASVKEDLVAYGGSWKLEGRWDGEEEVQLIAAVPGKNVVNVQTKPS
SQ  LFKVRNGGEIGAVALDYPSGTSGSPIVNRNGEVIGLYGNGILVGDNSFVSAISQTEVKEEGKEELQEIPTMLKKGMTTIL
SQ  DYHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGREVIDAMCHATLTYRMLE
SQ  PTRIVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWNTGHDWI
SQ  LADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEKEYPTIKQKKPDFILATDIAEMGANLCVDRVLDCRTAFKP
SQ  VLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGIE
SQ  GTKTPVSPGEMRLRDDQRRVSRELVRNCDLPVWLSWQVAKAGLKTNDRKWCFDGPKEHEILNDSGETVKCRAPGGAKRPL
SQ  RPRWCDERVSSDQSALADFIKFAEGRRGAAEILVVLSELPDFLAKKGGEAMDTISVFLHSEEGSRAYRNALSMMPEAMTI
SQ  VMLFILAGLLTSGMVIFFMSPKGISRMSMAMGTMAGCGYLMFLGGAKPTHISYIMLIFFVLMVVVIPEPGQQRSIQDNQV
SQ  AYLIIGILTLVSVVAANELGMLERTKEDLFGKKNLIPSSASPWSWPDLDLKPGAAWTVYVGIVTILSPMLHHWIKVEYGN
SQ  LSLSGIAQSASVLSFMDKGIPFMKMNISVIILLVSGWNSITVMPLLCGIGCAMLHWTLILPGIKAQQSKLPQRRVFHGVA
SQ  KNPVVDGNPTVDIEEAPEMPALYEKKLALYLLLALSLASVAMCRTPFSLAEGIVLASAALGPLIEGNTSLLWNGPMAVSM
SQ  TGVMRGNYYAFVGVMYNLWKMETGRRGRANGKTLGEVWKRELNLLDRQQFELYKRTDIVEVDRDTARRHLAEGKVDTGVA
SQ  VSRGTAKLRWFHERGYVKLEGRVTDLGCGRGGWCYYAAAQKEVSGVKGFTLGREGHEKPMNVRSLGWNIITFKDKTDIHH
SQ  LEPVKCDTLLCDIGESSSSSVTEGERTMRVLDTVEKWLACGVDNFCVKVLAPYMPDVLEKLELLQRRFGGTVIRNPLSRN
SQ  STHEMYYVSGARSNVTFTVNQTSRLLMRRMRRPTGKVTLEADVILPIGTRSVETDKGPLNREAIEERVERIKSEYMTTWF
SQ  YDNDNPYRTWHYCGSYVTKTSGSAASMVNGVIKILTYPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRKI
SQ  MKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAIGAYLEEQEQWKTANEAVQDPKFWELVDEERRLHQQGRCRTCVYN
SQ  MMGKREKKLSEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIRDLAAMDGGGFYAD
SQ  DTAGWDTRITEADLDDEQEILNYMSSHHKKLAQAVMEMTYKNKVVKVLRPTPGGKAYMDVISRRDQRGSGQVVTYALNTI
SQ  TNLKVQLIRMAEAEMVIHHHHVQDCDDSTLVRLEAWLIEHGCDRLNRMAVNGDDCVVRPIDDRFGMALSHLNAMSKVRKD
SQ  ISEWQPSKGWNDWENVPFCSHHFHELQLKDGRRIVVPCREQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHKR
SQ  DMRLLSLAVSSAVPTSWVPQGRTTWSIHGKGEWMTTEDMLEVWNRVWITNNPHMQDKTVVKEWRDVPYLTKRQDKLCGSL
SQ  IGMTNRATWASHIHLVIHRIRTLIGQEKYTDYLTVMDRYSVDADLQPGELI
//
ID  Q1X881;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  407140;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q1X881;
DR  PDB: 5YXA;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRRGVRSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKLTAHLKKLWRMLDPRQGLAV
SQ  LRKVKRVVASLMRGLSSRKRRSNEMALFPLLLLGLLALSGGVTLVRKNRWLLLNVTAEDLGKTFSVGTGNCTTNILEAKY
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGRCDAVGRSKRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQ
SQ  KIERWLVRNPFFAVTALAIAYLVGNNTTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQDKCVTVMA
SQ  PDKPSLDISLQTVAIDGPAEARKVCYSAVLTHVKINDKCPSTGEAHLAEENDGDNACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNTDIKTLKFDALSGSQEAEFTGYGKATLECQVQTAVDFGNSYI
SQ  AEMEKDSWIVDRQWAQDLTLPWQSGSGGIWREMHHLVEFEPPHAATIRVLALGNQEGSLKTALTGAMRVTKDENDNNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTVVMQVKVPKGAPCKIPVIVADDLTAAVNKGILVTVNPI
SQ  ASTNDDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGFFTSVGKGIH
SQ  TVFGSAFQGLFGGLSWITKVIMGAVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAVNFGKRELKCGDGIFVF
SQ  RDSDDWLTKYSYYPEDPVKLASIIKASHEEGKCGLNSVDSLEHEMWRSRADEINAIFEENEVDISVVVQDPKNIYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLVFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGMGVFTTRVFMDATFDYSVDCDGA
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMIHTLETLDYKECEWPLTHTIGTSVEESDMFMPRSIGGPVSSHNRIPGYKV
SQ  QTNGPWMQVPLEVKREVCPGTSVVVDSNCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPMKTSD
SQ  SHLVRSWVTAGEVHAVPFGLVSMMIAMEVVLRRRQGPKQMLVGGVVLLGAMLVGQVTVLDLVKFVVAVGLHFHEINNGGD
SQ  AMYMALIASFSIRPGLLMGFGLRTLWSPRERLVMAFGAAMVEIALGGMMGGLWQYLNAVSLCVLTINAISSRKASNMILP
SQ  LMALMTPMTMHEVRMATMLFCTVVIIGVLHQNSKDTSMQKTIPIVALTLTSYMGLTQPFLGLCAYMSTQVFGRRSIPVNE
SQ  ALAAAGLVGVLAGLAFQDMENFLGPIAVGGILMMLVSVAGRVDGLELKKLGEISWEEEAEISGSSSRYDVALSEQGEFKL
SQ  LSEDKVPWDQIVMTSLALVGAAIHPFALLLVLGGWILHIKGARRSGDVLWDIPTPKVIEECEHLEDGIYGIFQSTFLGAS
SQ  QRGVGVAQGGVFHTMWHVTRGAFLLRNGKKLVPSWASVKEDLVAYGGSWKLDGRWDGEEEVQLIAAVPGKSVVNVQTKPS
SQ  LFRVKNGGEIGAVALDYPSGTSGSPIVNRNGEVVGLYGNGILVGDNSFVSAISQTELKEESKEELQEIPTMLKKGMTTIL
SQ  DFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFQGLDVKFHTQAFSAHGSGKEVIDAMCHATLTYRMLE
SQ  PTRVVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWTAGHEWI
SQ  LADKRPTAWFLPSIRAANVMAASLRKAGKNVVVLNRKTFEKEYPTIKQKKPDFILATDIAEMGANLCVERVLDCRTAYKP
SQ  VLVDEGKKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGIE
SQ  GTKTPVSPGEMRLRDDQRRVFRELVRGCDLPVWLAWQVAKAGLKTNDRKWCFEGPEEHEILNDNGETVKCRSPGGAKRAL
SQ  RPRWCDERVSSDQSALADFIKFAEGRRGAAEMLVILTELPDFLAKKGGEAMDTISVFLHSEEGSRAYRNALSMMPEAMTI
SQ  VMLFLLAGLLTSGAVIFFMSPKGMSRMSMAMGTMAGSGYLMFLGGVKPTHISYVMLIFFVLMVVVIPEPGQQRTIQDNQV
SQ  AYLIIGILTLLSVVAANELGMLEKTKEDFFGKRDITTPSGAIPWSWPDLDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYG
SQ  NLSLSGIAQSASVLSFMDKGIPFMKMNISVVILLVSGWNSITVIPLLCGIGGAMLHWTLILPGIKAQQSKLAQKRVFHGV
SQ  AKNPVVDGNPTADIEEAPEMPALYEKKLALYLLLALSLMSVAMCRTPFSLAEGIVLSSAALGPLIEGNTSLLWNGPMAVS
SQ  MTGVMRGNYYAFVGVMYNLWKMKTERRGSASGKTLGEVWKRELNLLDKQQFEMYKRTDIIEVDRDMARRHLAEGKVDTGV
SQ  AVSRGTAKLRWFHERGYVKLEGRVTDLGCGRGGWCYYAAAQKEVSGVKGYTLGRDGHEKPMNVQSLGWNIVTFKDKTDVH
SQ  RLEPLKCETLLCDIGESSPSSATEGERTLRVLDTVEKWLACGVDNFCIKVLAPYMPDVIEKLELLQRRFGGTVIRNPLSR
SQ  NSTHEMYYVSGARSNITFTVNQTSRLLMRRMRRPTGKVTLEADVILPIGTRSVETDKGPLDKDAIEERVERIKNEYATTW
SQ  FYDNDNPYRTWHYCGSYVTKTSGSAASMINGVIKILTFPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRK
SQ  IMKVVNRWLFRHLSREKNPRLCTKEEFIAKVRSHAAVGAFLEEQEQWKTANEAVQDPKFWEMVDAERKLHQQGRCQSCVY
SQ  NMMGKREKKLSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWASRENSGGGVEGTGLQYLGYVIRDLSAKEGGGFYA
SQ  DDTAGWDTRITEADLDDEQEIMSYMSPEQRKLAWAIMEMTYKNKVVKVLRPAPGGKAFMDIISRRDQRGSGQVVTYALNT
SQ  ITNLKVQLIRMAEAEMVINHQHVQECGENVLERLETWLAENGCDRLSRMAVSGDDCVVRPVDDRFGLALSHLNAMSKVRK
SQ  DISEWQPSKGWTDWENVPFCSHHFHELVLKDGRKIVVPCRDQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHK
SQ  RDMRLLSFAVSSAVPTAWVPSGRTTWSVHGRGEWMTTEDMLDVWNRVWVLNNPHMTDKTTIKEWRDVPYLTKRQDKLCGS
SQ  LIGMTNRATWASHIHLVIHRIRTLIGQEKFTDYLTVMDRYSVDADLQPGELI
//
ID  Q9YRV3;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  407137;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q9YRV3;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRRGVRSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKITAQLKRLWKMLDPRQGLAA
SQ  LRKVKRVVAGLMRGLSSRKRRSHDVLTVQFLILGMLLMTGGVTLMRKNRWLLLNVTSEDLGKTFSIGTGNCTTNILEAKY
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVTYGKCDSAGRSRRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQ
SQ  KIERWFVRNPFFAVTALTIAYLVGSNMTQRVVIALLVLAVGPAYSAHCIGVADRDFIEGVHGGTWVSATLEQDKCVTVMA
SQ  PDKPSLDISLETVAIDGPVEARKVCYNAVLTHVKIDDKCPSTGEAHLAEENEGDNACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIKAQLHVGAKQEDWKTDIKTLKFDVLSGSQEAEFTGYGKVTLECQVQTAVDFGNSYI
SQ  AEMEKESWIVDRQWAQDLTLPWQSGSGGVWREMHHLVEFEPPHAATIRVLALGDQEGSLKTALTGAMRVTKDTNDNNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTVVMQVKVPKGAPCKIPVIVADDLTAAINKGILVTVNPI
SQ  ASTNDDEVLIEVNPPFGDSYIIIGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGFFTSVGKGIH
SQ  TVFGSAFQGLFGGLNWITKVIMGAVLIWVGFNTRNMTMSMSMILVGVIMMFLSLGVGADQGCAINFGKRELKCGDGIFIF
SQ  RDSDDWLNKYSYYPEDPVKLASIVKASFEEGKCGLNSVDSLEHEMWRSRADEINAILEENEVDISVVVQDPKNVYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLVFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGTGVFTTRVYMDAVFEYTIDCDGS
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMIHTLEALDYKECEWPLTHTIGTSVEESEMFMPRSIGGPVSSHNHIPGYKV
SQ  QTNGPWMQVPLEVKREACPGTSVIIDGNCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPMKTHE
SQ  SHLVRSWVTAGEIHAVPFGLVSMMIAMEVVLRKRQGPKQVLVGGVVLLGAMLVGQVTLLDLLELTVAVGLHFHEMNNGGD
SQ  AMYMALIAAFSVRPGLLIGFGLRTLWSPRERLVLALGAAMVEIALGGMMGGLWKYLNAVSLCILTINAVASRKASNAILP
SQ  LMALLTPVTMAEVRLATMLFCTVVIIGVLHQNSKDTSMQKTIPLVALTLTSYLGLTQPFLGLCAFLATRIFGRRSIPVNE
SQ  ALAATGLVGVLAGLAFQEMENFLGPIAVGGILMMLVSVAGRVDGLELKKLGEVSWEEEAEISGSSARYDVALSEQGEFKL
SQ  LSEEKVPWDQVVMTSLALVGAAIHPFALLLVLAGWLFHVRRARRSGDVLWDIPTPKIIEECEHLEDGIYGIFQSTFLGAS
SQ  QRGVGVAQGGVFHTMWHVTRGAFLVWNGKKLIPSWASVKEDLVAYGGSWKLEGRWDGEEEVQLIAAAPGKNVVNVQTKPS
SQ  LFKVRNGGEIGAVALDYPSGTSGSPIVNRNGEVIGLYGNGILVGDNSFVSAISQTEVKEEGKEELQEIPTMLKKGKTTIL
SQ  DFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGREVIDVMCHATLTYRMLE
SQ  PTRIVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWNTGHDWI
SQ  LADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEREYPTIKQKKPDFILATDIAEMGANLCVERVLDCRTAFKP
SQ  VLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGVE
SQ  GIKTPVSPGEMRLRDDQRKVFRELVRNCDLPVWLSWQVAKAGLKTNDRKWCFEGPEEHEILNDSGETVKCRAPGGAKKPL
SQ  RPRWCDERVSSDQSALSEFIKFAEGRRGAADVLVVLSELPDFLAKKGGEAMDTISVFLHSEEGSRAYRNALSMMPEAMTI
SQ  VMLFLLAGLLTSGMVIFFMSPKGISRMSMAKGTMAGCGYLMFLGGVEPTHISYIMLIFFVLMVVVIPEPGQQRSIQDNQV
SQ  AFLIIGILTLVSVVAANELGMLEKTKEDLFGKKNLIPSGASPWSWPDLDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYGN
SQ  LSLSGIAQSASVLSFMDKGIPFMKMNISVIMLLVSGWNSITVMPLLCGIGCAMLHWSLILPGIKAQQSKLAQRRVFHGVA
SQ  KNPVVDGNPTVDIEEAPEMPALYEKKLALYLLLALSLASVAMCRTPFSLDEGIVLASAALGPLIEGNTSLLWNGPMAVSM
SQ  TGVMRGNYYAFVGVAYNLWKMKTARRGTANGKTLGEVWKRELNLLDKQQFELYKRTDIVEVDRDTARRHLAEGKVDTGVA
SQ  VSRGTAKLRWFHERGYVKLEGRVIDLGCGRGGWCYYAAAQKEVSGVKGFTLGRDGHEKPMNVQSLGWNIITFKDKTDVHP
SQ  LEPVKCDTLLCDIGESSSSSVTEGERTVRVLDTVEKWLACGVDNFCVKVLAPYMRDVLEKLELLQRRFGGTVIRNPLSRN
SQ  STHEMYYVSGARSNVTFTVNQTSRLLMRRMRRPTGKVTLEADVTLPIGTRSVETDKGPLDKEAIKERVERIKSEYMTSWF
SQ  YDNDNPYRTWHYCGSYVTKTSGSAASMVNGVIKLLTYPWDKIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRKI
SQ  MKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAIGAYLEEQDQWKTANEAVQDPKFWELVDEERKLHQQGRCRTCVYN
SQ  MMGKREKKLSEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIRDLAAMDGGGLYAD
SQ  DTAGWDTRITEADLDDEQEILNYMSPHHKKLAQAVMEMTYKNKVVKVLRPAPGGKAYMDVISRRDQRGSGQVVTYALNTI
SQ  TNLKVQLIRMAEAEMVIHHQHVQDCDESVLTRLEAWLTEHGCDRLRRMAVSGDDCVVRPIDDRFGLALSHLNAMSKVRKD
SQ  ISEWQPSKGWNDWENVPFCSHHFHELQLKDGRRIVVPCREQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHKR
SQ  DMRLLSLAVSSAVPTSWVPQGRTTWSIHGKGEWMTTEDRLEVWNRVWITNNPHMQDKTMVKEWRDVPYLTKRQDKLCGSL
SQ  IGMTNRATWASNIHLVIHRIRTLVGQEKYTDYLTVMDRYSVDADLQPGELI
//
ID  Q1X880;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  407139;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q1X880;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRRGVRSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKLTTHLKRLWRMLDPRQGLTV
SQ  LRKVKRVVASLMRGLSSRKRRSSEMTMMPLLILSMVILGGGVTLVRKNRWLLLNVTAEDLGKTFSVGTGNCTTNILEAKY
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGRCDAVGRSKRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQ
SQ  KIERWLVRNPFFAVTALAIAYLVGNNKTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSASLEQDKCVTVMA
SQ  PDKPSLDISLQTVAIDGPAEARKVCYSAVLTHVKINDKCPSTGEAHLAEENDGDNACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNTDIKTLKFDALSGSQEAEFTGYGKATLECQVQTAVDFGNSYI
SQ  AEMEKDSWIVDRQWAQDLTLPWQSGSGGIWREMHHLVEFEPPHAATIRVLALGNQEGSLKTALTGAMRVTKDENDNNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTVVMQVKVPKGAPCKIPVIVADDLTAAVNKGILVTVNPI
SQ  ASTNDDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGVERLAVMGDAAWDFSSAGGFFTSVGKGIH
SQ  TVFGSAFQGLFGGLSWITKVIMGAVLIWVGINTRNMTMSMSMILVGVIMMFLSLGVGADQGCAVNFGKRELKCGDGIFVF
SQ  RDSDDWLTKYSYYPEDPVKLASIIKASYEEGKCGLNSVDSLEHEMWRSRADEINAIFEENEVDISIVVQDPKNIYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLIFSPGRKNGSFIIDGKSRKECPFSNRVWNSFQIEEFGMGVFTTRVFMDAVFDYSVDCDGA
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMMHTLETLDYKECEWPLTHTIGTSVEESDMFMPRSIGGPVSSHNHIPGYKV
SQ  QTNGPWMQVPLEVRREPCPGTSVVVDTSCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPMKTHE
SQ  SHLVRSWVTAGEVHAVPFGLVSMMIAMEVVLRKRQGPKQMLVGGIILLGAMLVGQVTMLDLVKLIVAVGLHFHEINNGGD
SQ  AMYMALIASFSIRPGLLIGFGLRTLWSPRERLVMAFGAAMVEVALGGMMGGLWQYLNAVSLCVLTINAISSRKASNTILP
SQ  LMALLTPVTMYEVRMATMLFCTVVIVGVLHQNSKDTSMQKTIPIVALTLTSYMGLTQPFLGLCAYMSTQVFGRRSIPVNE
SQ  ALAAAGLVGVLAGLAFQDMENFLGPIAVGGILMMLVSVAGKVDGLELKKLGEVSWEEEAEISGSSSRYDVALSEQGEFKL
SQ  LSEDKVPWDQIVMTSLALVGAAIHPFALLLVLGGWVLHIKGARRSGDVLWDIPTPKVIEECEHLEDGIYGIFQSTFLGAS
SQ  QRGVGVAQGGVFHTMWHVTRGAFLLRNGKKLVPSWASVKEDLVAYGGSWKLDGKWDGEEEVQLIAAVPGKAVVNVQTKPS
SQ  LFKVRNGGEIGAVALDYPSGTSGSPIVNRSGEVVGLYGNGILVGDNSFVSAISQTEVKEESKEELQEIPTMLKKGMTTIL
SQ  DFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGKEVIDAMCHATLTYRMLE
SQ  PTRVVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWTSGHEWI
SQ  LADKRPTAWFLPSIRAANVMAASLRKAGKNVVVLNRKTFEKEYPTIKQKRPDFILATDIAEMGANLCVERVLDCRTAYKP
SQ  VLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSEDNAHHVCWLEASMLLDNMEVRGGMVAPLYGIE
SQ  GTKTPVSPGEMRLRDDQRRVFRELVRGCDLPVWLSWQVAKAGLKTNDRKWCFEGPEEHEILNDNGETVKCRSPGGAKKAL
SQ  RPRWCDERVSSDQSALADFIKFAEGRRGAAEMLVVLTELPDFLAKKGGEAMDTISVFLHSEEGSRAYRNALSMMPEAMTI
SQ  VMLFILAGLLTSGMVIFFMSPKGMSRMSMAMGTMAGSGYLMFLGGVKPTHISYVMLIFFVLMVVIIPEPGQQRSIQDNQV
SQ  AYLIIGILTLLSVVAANELGMLEKTKEDFFGKRNIATSGGTIPWSWPDLDLKPGAAWTVYVGIVTMLSPMLHHWIKVEYG
SQ  NLSLSGIAQSASVLSFMDKGVPFMKMNISVVILLVSGWNSITVIPLLCGVGGAMLHWTLILPGIKAQQSKLAQKRVFHGV
SQ  AKNPVVDGNPTADIEEAPEMPALYEKKLALYLLLALSLMSVAMCRTPFSLAEGIVLSSAALGPLIEGNTSLLWNGPMAVS
SQ  MTGVMRGNYYAFVGVMYNLWKMKTGRRGSANGKTLGEVWKRELNLLDKQQFELYKRTDITEVDRDMARRHLAEGKVDTGV
SQ  AVSRGTAKLRWFHERGYVKLEGRVMDLGCGRGGWCYYAAAQKEVSGVKGYTLGRDGHEKPMNVQSLGWNIVTFKDKTDIH
SQ  RLEPAKCETLLCDIGESSPSSVTEGERTLRVLETVEKWLACGVDNFCVKVLAPYMPDVIEKLELLQRRFGGTVIRNPLSR
SQ  NSTHEMYYVSGARSNITFTVNQTSRLLMRRMRRPTGKVTLEPDVILPIGTRSVETDKGPLDRGAIEERVERIKTEYAATW
SQ  FHDNDNPYRTWHYCGSYITKTSGSAASMINGVIKILTFPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRK
SQ  IMRVVNRWLFRHLAREKKPRLCTKEEFIAKVRSHAAIGAFLEEQEQWKTANEAVQDPKFWEMVDAERKLHQQGRCQSCVY
SQ  NMMGKREKKLSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIKDLSTKEGGGFYA
SQ  DDTAGWDTRITEADLDDEQEIMSYMNAEQRKLAWAVMEMTYKNKVVKVLRPAPGGKAFMDIISRRDQRGSGQVVTYALNT
SQ  ITNLKVQLIRMAEAEMVINHQHVNECDESALARLDAWLAENGCDRLARMAVSGDDCVVKPVDDRFGLALSHLNAMSKVRK
SQ  DISEWQPSKGWTDWESVPFCSHHFHELVLKDGRKVVVPCRDQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHK
SQ  RDMRLLSFAVSSAVPTAWVPSGRTTWSVHGKGEWMTTEDMLDVWNRVWVLNNPHMKDKTTVKEWRDVPYLTKRQDKLCGS
SQ  LIGMTNRATWASHIHLVIHRIRNLIGQEKYTDYLTVMDRYSVDADLQPGELI
//
ID  Q32ZE1;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  64320;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host cytoplasm {ECO:0000269|PubMed:32150556}. Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000269|PubMed:27212660, ECO:0000269|PubMed:30848123, ECO:0000269|PubMed:31090058, ECO:0000269|PubMed:31690057}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: Q32ZE1;
DR  PDB: 5GJ4;
DR  PDB: 5GPI;
DR  PDB: 5GXJ;
DR  PDB: 5JPS;
DR  PDB: 5JRZ;
DR  PDB: 5K6K;
DR  PDB: 5RHG;
DR  PDB: 5RHH;
DR  PDB: 5RHI;
DR  PDB: 5RHJ;
DR  PDB: 5RHK;
DR  PDB: 5RHL;
DR  PDB: 5RHM;
DR  PDB: 5RHO;
DR  PDB: 5RHP;
DR  PDB: 5RHQ;
DR  PDB: 5RHR;
DR  PDB: 5RHS;
DR  PDB: 5RHT;
DR  PDB: 5RHU;
DR  PDB: 5RHV;
DR  PDB: 5RHW;
DR  PDB: 5RHX;
DR  PDB: 5RHY;
DR  PDB: 5T1V;
DR  PDB: 5TFN;
DR  PDB: 5TFO;
DR  PDB: 5TFR;
DR  PDB: 5TMH;
DR  PDB: 5U04;
DR  PDB: 5U0B;
DR  PDB: 5U0C;
DR  PDB: 5VI7;
DR  PDB: 5VIM;
DR  PDB: 5W41;
DR  PDB: 5Y4Z;
DR  PDB: 5YOD;
DR  PDB: 5YOF;
DR  PDB: 5Z0R;
DR  PDB: 5Z0V;
DR  PDB: 5ZMQ;
DR  PDB: 5ZMS;
DR  PDB: 5ZOB;
DR  PDB: 6ADW;
DR  PDB: 6ADX;
DR  PDB: 6ADY;
DR  PDB: 6JPW;
DR  PDB: 6KK2;
DR  PDB: 6KK3;
DR  PDB: 6KK4;
DR  PDB: 6KK5;
DR  PDB: 6KK6;
DR  PDB: 6KPQ;
DR  PDB: 6L50;
DR  PDB: 6MH3;
DR  PDB: 6UX2;
DR  PDB: 6WCZ;
DR  PDB: 6Y3B;
DR  PDB: 7O55;
DR  PDB: 7OBV;
DR  PDB: 7OC2;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the host cell membrane and packages the viral RNA into a nucleocapsid that forms the core of the mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptors and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HAVCR1 in a cell-type specific manner (By similarity). In addition, host NCAM1 can also be used as entry receptor (By similarity). Interaction with host HSPA5 plays an important role in the early stages of infection as well (By similarity). Envelope protein is synthesized in the endoplasmic reticulum and forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Plays a role in the inhibition of host RLR-induced interferon-beta activation by targeting TANK-binding kinase 1/TBK1 (PubMed:28373913). In addition, recruits the host deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn, stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability to recognize mitochondrial DNA release and initiate type I interferon signaling (PubMed:28373913). {ECO:0000269|PubMed:28373913}. [Non-structural protein 2A]: Component of the viral RNA replication complex that recruits genomic RNA, the structural protein prM/E complex, and the NS2B/NS3 protease complex to the virion assembly site and orchestrates virus morphogenesis (By similarity). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (PubMed:31882898, PubMed:31581385). May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex (PubMed:28826723). {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000269|PubMed:28826723, ECO:0000269|PubMed:31581385, ECO:0000269|PubMed:31882898}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. {ECO:0000255|PROSITE- ProRule:PRU00859}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Leads to translation arrest when expressed ex vivo (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). By inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly (PubMed:30550790). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (PubMed:31581385). Leads to translation arrest when expressed ex vivo (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440, ECO:0000269|PubMed:30550790, ECO:0000269|PubMed:31581385}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Also plays a role in the inhibition of host RLR-induced interferon-beta production at TANK-binding kinase 1/TBK1 level (PubMed:28373913). Cooperatively with NS4A suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440, ECO:0000269|PubMed:28373913}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:31090058). Methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to the cap-proximal structure and inhibits further translation of the viral genome (PubMed:32313955). Besides its role in RNA genome replication, also prevents the establishment of a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway (PubMed:31690057, PubMed:30530224). Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway (PubMed:27212660, PubMed:27797853). Within the host nucleus, disrupts host SUMO1 and STAT2 co-localization with PML, resulting in PML degradation (By similarity). May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000269|PubMed:27212660, ECO:0000269|PubMed:27797853, ECO:0000269|PubMed:30530224, ECO:0000269|PubMed:31690057, ECO:0000269|PubMed:32313955}.
DE  Reference Proteome: Yes;
DE  Interaction: Q32ZE1; IntAct: EBI-20717490; Score: 0.52
DE  Interaction: Q96CW1; IntAct: EBI-26353258; Score: 0.40
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039722;
GO  GO:0039502;
GO  GO:0039723;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKNPKEEIRRIRIVNMLKRGVARVNPLGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEI
SQ  IKKFKKDLAAMLRIINARKERKRRGADTSIGIIGLLLTTAMAAEITRRGSAYYMYLDRSDAGKAISFATTLGVNKCHVQI
SQ  MDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREY
SQ  TKHLIKVENWIFRNPGFALVAVAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGC
SQ  VTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGK
SQ  GSLVTCAKFTCSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIGYETDEDRAKVEVTPNSPRAEATLGGFGSLGLDCEPRT
SQ  GLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALE
SQ  AEMDGAKGRLFSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKVPAETLHGTVTVEVQYAGTDGPCKIPVQMAVDMQTLTP
SQ  VGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGDKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSV
SQ  GGVFNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLVWLGLNTKNGSISLTCLALGGVMIFLSTAVSADVGCSVDFSK
SQ  KETRCGTGVFIYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEEGICGISSVSRMENIMWKSVEGELNAILEENGVQLTVVV
SQ  GSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLEHRAWNSFLVEDHGFGVFHTSVWLK
SQ  VREDYSLECDPAVIGTAVKGREAAHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGVEESDLIIPKSLAGP
SQ  LSHHNTREGYRTQVKGPWHSEELEIRFEECPGTKVYVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCW
SQ  YGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIMSTSMAVLVVMILGGFSMSDLAKLV
SQ  ILMGATFAEMNTGGDVAHLALVAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLA
SQ  IRAMAVPRTDNIALPILAALTPLARGTLLVAWRAGLATCGGIMLLSLKGKGSVKKNLPFVMALGLTAVRVVDPINVVGLL
SQ  LLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSP
SQ  RLDVALDESGDFSLVEEDGPPMREIILKVVLMAICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGV
SQ  YRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGLSEVQLLAVPP
SQ  GERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKREEETPVECFEPS
SQ  MLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKKRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMC
SQ  HATFTSRLLQPIRVPNYNLNIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPE
SQ  RAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKNQEWDFVITTDISEMGANFKADR
SQ  VIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYMYGGGCAETDEGHAHWLEARMLLDNIYLQDG
SQ  LIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWT
SQ  KYGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAALGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAA
SQ  AQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEK
SQ  QRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKNDIAHLMGRREEGATMGFSMDIDLRPASAWAIYAALTTLITPAVQ
SQ  HAVTTSYNNYSLMAMATQAGVLFGMGKGMPFMHGDLGVPLLMMGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAA
SQ  QKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAISSAVLLRTAWGWGEAGALITAATSTLWEGSPNKYW
SQ  NSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRAL
SQ  KDGVATGGHAVSRGSAKIRWLEERGYLQPYGKVVDLGCGRGGWSYYAATIRKVQEVRGYTKGGPGHEEPMLVQSYGWNIV
SQ  RLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEETRTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETMERLQRRHGG
SQ  GLVRVPLCRNSTHEMYWVSGAKSNIIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVASCAEAPNMKIIGRRIER
SQ  IRNEHAETWFLDENHPYRTWAYHGSYEAPTQGSASSLVNGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRV
SQ  PDPQEGTRQVMNIVSSWLWKELGKRKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDREREHHL
SQ  RGECHSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYILEEMN
SQ  RAPGGKMYADDTAGWDTRISKFDLENEALITNQMEEGHRTLALAVIKYTYQNKVVKVLRPAEGGKTVMDIISRQDQRGSG
SQ  QVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRKPEKVTRWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLN
SQ  DMGKVRKDTQEWKPSTGWSNWEEVPFCSHHFNKLYLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMW
SQ  QLLYFHRRDLRLMANAICSAVPVDWVPTGRTTWSIHGKGEWMTTEDMLMVWNRVWIEENDHMEDKTPVTKWTDIPYLGKR
SQ  EDLWCGSLIGHRPRTTWAENIKDTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL
//
ID  A0A024B7W1;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  2043570;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q32ZE1}. Host nucleus {ECO:0000269|PubMed:32699085}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: A0A024B7W1;
DR  PDB: 5GOZ;
DR  PDB: 5GP1;
DR  PDB: 5H30;
DR  PDB: 5H32;
DR  PDB: 5H37;
DR  PDB: 5IRE;
DR  PDB: 5IZ7;
DR  PDB: 5JMT;
DR  PDB: 5KQR;
DR  PDB: 5KQS;
DR  PDB: 5KVE;
DR  PDB: 5LBS;
DR  PDB: 5LBV;
DR  PDB: 5LCV;
DR  PDB: 5M5B;
DR  PDB: 5MRK;
DR  PDB: 5NJU;
DR  PDB: 5NJV;
DR  PDB: 5U4W;
DR  PDB: 5UHY;
DR  PDB: 5ULP;
DR  PDB: 5Y0A;
DR  PDB: 5Y6M;
DR  PDB: 5Y6N;
DR  PDB: 6CO8;
DR  PDB: 6I7P;
DR  PDB: 6JFH;
DR  PDB: 6JFI;
DR  PDB: 6LD1;
DR  PDB: 6LD2;
DR  PDB: 6LD3;
DR  PDB: 6LD4;
DR  PDB: 6LD5;
DR  PDB: 6NIP;
DR  PDB: 6NIU;
DR  PDB: 6PLK;
DR  PDB: 6RWZ;
DR  PDB: 6S0J;
DR  PDB: 6UM3;
DR  PDB: 7BSD;
DR  PDB: 7BU8;
DR  PDB: 7BUA;
DR  PDB: 7M1V;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptors and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HAVCR1 in a cell-type specific manner (By similarity). In addition, host NCAM1 can also be used as entry receptor (By similarity).Interaction with host HSPA5 plays an important role in the early stages of infection as well (By similarity). Envelope protein is synthesized in the endoplasmic reticulum and forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Plays a role in the inhibition of host RLR-induced interferon-beta activation by targeting TANK-binding kinase 1/TBK1. In addition, recruits the host deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn, stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability to recognize mitochondrial DNA release and initiate type I interferon signaling. {ECO:0000250|UniProtKB:Q32ZE1}. [Non-structural protein 2A]: Component of the viral RNA replication complex that recruits genomic RNA, the structural protein prM/E complex, and the NS2B/NS3 protease complex to the virion assembly site and orchestrates virus morphogenesis (By similarity). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex (By similarity). {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:Q32ZE1}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. {ECO:0000250|UniProtKB:Q32ZE1}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). Leads to translation arrest when expressed ex vivo (PubMed:28592527). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:28592527}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). By inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly (PubMed:30550790). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). Leads to translation arrest when expressed ex vivo (PubMed:28592527). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440, ECO:0000269|PubMed:28592527, ECO:0000269|PubMed:30550790}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Also plays a role in the inhibition of host RLR-induced interferon-beta production at TANK-binding kinase 1/TBK1 level (By similarity). Cooperatively with NS4A suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:30951555). Methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to the cap-proximal structure and inhibits further translation of the viral genome (By similarity). Besides its role in RNA genome replication, also prevents the establishment of a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway (By similarity). Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway (By similarity). Within the host nucleus, disrupts host SUMO1 and STAT2 co-localization with PML, resulting in PML degradation (PubMed:32699085). May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (PubMed:30550790). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:30550790, ECO:0000269|PubMed:30951555, ECO:0000269|PubMed:32699085}.
DE  Reference Proteome: No;
DE  Interaction: A0A0B4L3F2; IntAct: EBI-22275699; Score: 0.32
DE  Interaction: A0A024B7W1; IntAct: EBI-26607668; Score: 0.32
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0051539;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0140272;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039574;
GO  GO:0039563;
GO  GO:0039564;
GO  GO:0039653;
GO  GO:0039502;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEI
SQ  IKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQI
SQ  MDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREY
SQ  TKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGC
SQ  VTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGK
SQ  GSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDC
SQ  EPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALA
SQ  GALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQ
SQ  TLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWD
SQ  FGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSV
SQ  DFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQL
SQ  TVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTS
SQ  VWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKS
SQ  LAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAK
SQ  DGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDL
SQ  AKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFAL
SQ  AWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINV
SQ  VGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVT
SQ  GNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGET
SQ  TDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLL
SQ  AVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVEC
SQ  FEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIV
SQ  DLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEV
SQ  EVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANF
SQ  KADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIY
SQ  LQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPA
SQ  EVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPY
SQ  KAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIP
SQ  EPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFIT
SQ  PAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAA
SQ  ARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSP
SQ  NKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEA
SQ  RRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYG
SQ  WNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQR
SQ  RYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGN
SQ  RIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKV
SQ  DTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKER
SQ  EHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVL
SQ  EEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQ
SQ  RGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHAL
SQ  RFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSY
SQ  AQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPY
SQ  LGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL
//
ID  A0A142I5B9;
PN  RNA-directed RNA polymerase NS5;
GN  POLG;
OS  2316109;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host cell surface {ECO:0000269|PubMed:33432092}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE- ProRule:PRU00860}. [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q32ZE1}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: A0A142I5B9;
DR  UNIPROT: H9A910;
DR  PDB: 6UTA;
DR  PDB: 7BPK;
DR  PDB: 7BQ5;
DR  Pfam: PF01003;
DR  Pfam: PF07652;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01005;
DR  Pfam: PF01002;
DR  Pfam: PF01350;
DR  Pfam: PF01349;
DR  Pfam: PF00972;
DR  Pfam: PF01570;
DR  Pfam: PF01728;
DR  Pfam: PF00949;
DR  PROSITE: PS51527;
DR  PROSITE: PS51528;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50507;
DR  PROSITE: PS51591;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptors and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HAVCR1 in a cell-type specific manner (PubMed:32641828). In addition, host NCAM1 can also be used as entry receptor (PubMed:32753727). Interaction with host HSPA5 plays an important role in the early stages of infection as well (PubMed:33432092). Envelope protein is synthesized in the endoplasmic reticulum and forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:32641828, ECO:0000269|PubMed:32753727, ECO:0000269|PubMed:33432092}. [Non-structural protein 1]: Plays a role in the inhibition of host RLR-induced interferon-beta activation by targeting TANK-binding kinase 1/TBK1. In addition, recruits the host deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn, stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability to recognize mitochondrial DNA release and initiate type I interferon signaling. {ECO:0000250|UniProtKB:Q32ZE1}. [Non-structural protein 2A]: Component of the viral RNA replication complex that recruits genomic RNA, the structural protein prM/E complex, and the NS2B/NS3 protease complex to the virion assembly site and orchestrates virus morphogenesis (PubMed:31662457). Antagonizes also the host alpha/beta interferon antiviral response (By similarity). May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex (By similarity). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:31662457}. [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. {ECO:0000250|UniProtKB:Q32ZE1}. [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). Leads to translation arrest when expressed ex vivo (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q32ZE1}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation (By similarity). By inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly (By similarity). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). Leads to translation arrest when expressed ex vivo (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4}. [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 4B]: Induces the formation of ER- derived membrane vesicles where the viral replication takes place (By similarity). Also plays a role in the inhibition of host RLR-induced interferon-beta production at TANK-binding kinase 1/TBK1 level (By similarity). Cooperatively with NS4A suppresses the Akt-mTOR pathway and leads to cellular dysregulation (By similarity). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4}. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (By similarity). Methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to the cap-proximal structure and inhibits further translation of the viral genome (By similarity). Besides its role in RNA genome replication, also prevents the establishment of a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway (By similarity). Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway (By similarity). Within the host nucleus, disrupts host SUMO1 and STAT2 co-localization with PML, resulting in PML degradation (By similarity). May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon- responsive genes (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q32ZE1}.
DE  Reference Proteome: No;
DE  Interaction: P35251; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q01105; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BSC4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q7Z7F7; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q6P161; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NRX2; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9H5H4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9UEG4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q969S3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q96ME7; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q96KR1; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q6NZY4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q7Z2W4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O43592; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9H269; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O15240; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q93008; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q13509; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q12899; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P11387; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9UM00; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q15633; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O75683; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q13243; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BXP5; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q96SB4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q13501; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q16637; IntAct: EBI-20625330; Score: 0.50
DE  Interaction: Q9NTJ3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O95347; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P53007; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8NC51; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NVU7; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O76021; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q5JTH9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P08865; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P46781; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62241; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62081; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P46782; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62701; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P61247; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P23396; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62273; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62857; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62854; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62851; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62847; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P63220; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P60866; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P39019; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62269; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P08708; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62249; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62244; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62841; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62277; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P25398; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P46783; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P04843; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P05387; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q6FG99; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P05388; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P32969; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62917; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62424; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P18124; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q02878; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P46777; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P36578; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P63173; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q969Q0; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y3U8; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P18077; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P42766; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P49207; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62910; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62899; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62888; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P39023; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P47914; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P46779; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P46776; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P61353; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9UNX3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P61254; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P83731; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62750; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62829; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P35268; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P46778; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P84098; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q02543; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q07020; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P18621; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P61313; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P50914; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P40429; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P26373; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P30050; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62913; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q14257; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P42696; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NW13; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q96EY7; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P56730; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P78527; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O15355; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NQ55; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q99575; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P40855; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O00408; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BW27; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q12769; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9H6R4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BYG3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8NEJ9; IntAct: EBI-20625330; Score: 0.50
DE  Interaction: P19338; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9H0A0; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q99733; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: F8W118; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P55209; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BQG0; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q86UE4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P52701; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9UKD2; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82933; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y2R9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82932; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82675; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82673; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82930; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y291; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q92665; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NP92; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y2Q9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q92552; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BYN8; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82663; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y3D9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82650; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82921; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y399; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y3D3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82914; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O60783; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82912; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P82664; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BYD2; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9HD33; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BRJ2; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y6G3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8IXM3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NYK5; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q96DV4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BZE1; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NZE8; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P09001; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q13084; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q96A35; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q16540; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NWU5; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q7Z2W9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q5T653; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P49406; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9H0U6; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NX20; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BYD1; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y3B7; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q7Z7H8; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BYD6; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y5V3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NX58; IntAct: EBI-20625330; Score: 0.50
DE  Interaction: Q9BRT6; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q4G0J3; IntAct: EBI-20625330; Score: 0.50
DE  Interaction: Q6PKG0; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q13601; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8N9T8; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q15397; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q96P70; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O95373; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q14197; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q5SSJ5; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q00341; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P55084; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P40939; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9P035; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q92522; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BZE4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8WUA4; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BQ67; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q5JY77; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: A0A024R2Z6; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q13823; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P63244; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8WXD5; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9HBB9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8IY81; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62861; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q06265; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NPD3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q01780; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9Y3B2; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O75616; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NR50; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q99848; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8WXX5; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O60884; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P31689; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O60832; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9UNQ2; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q6P158; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BQ39; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O15523; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9GZR7; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NR30; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9UHI6; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9NVP1; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q13206; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q16531; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P51398; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BQ75; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: B2R5U7; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q6PK04; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q13555; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P62158; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q9BRJ6; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q8TDN6; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q14137; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q14692; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O95831; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: Q6NT76; IntAct: EBI-20625829; Score: 0.40
DE  Interaction: O60613; IntAct: EBI-20626156; Score: 0.35
DE  Interaction: O14967; IntAct: EBI-20626156; Score: 0.35
DE  Interaction: Q13315; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: P04350; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: Q9NZ01; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: Q02978; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: Q29RF7; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: B3KY51; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: Q92604; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: A0A024R3R5; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: Q8WVX9; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: O95864; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: O94905; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: O75477; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: P11532; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: Q96MT8; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: P58397; IntAct: EBI-20626076; Score: 0.35
DE  Interaction: Q13442; IntAct: EBI-20626135; Score: 0.35
DE  Interaction: Q9UGN5; IntAct: EBI-20626135; Score: 0.35
DE  Interaction: Q9HCK8; IntAct: EBI-20626135; Score: 0.35
DE  Interaction: Q9BV73; IntAct: EBI-20626135; Score: 0.35
DE  Interaction: Q9BSJ8; IntAct: EBI-20626240; Score: 0.40
DE  Interaction: P45880; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: O14925; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: O15260; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: P46977; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: Q9UNL2; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: O15269; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: P60468; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: O00767; IntAct: EBI-20626197; Score: 0.50
DE  Interaction: Q99623; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: P35232; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: O60725; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: Q86UL3; IntAct: EBI-20626197; Score: 0.35
DE  Interaction: P62877; IntAct: EBI-20626169; Score: 0.35
DE  Interaction: Q13126; IntAct: EBI-20626169; Score: 0.35
DE  Interaction: O14681; IntAct: EBI-20626169; Score: 0.35
DE  Interaction: Q969M3; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9H2V7; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P00403; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9Y6C9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9GZP9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9NWW5; IntAct: EBI-20626314; Score: 0.54
DE  Interaction: O95070; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q8NBI6; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9Y277; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q96IX5; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: B1AH87; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9NS69; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q96JJ7; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q5BJD5; IntAct: EBI-20626314; Score: 0.50
DE  Interaction: P57088; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9HC07; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9H061; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9HD45; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q99805; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9NPL8; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q3ZCQ8; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O60830; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q7L0J3; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9UJZ1; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9NXE4; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q01650; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P08195; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: C4N9M8; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9H2H9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P11166; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P12236; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9H936; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9UJS0; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O75746; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q15758; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P53985; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q96EP9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9BWM7; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P61619; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q86SK9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q8TAC9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O14828; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O75845; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9NTJ5; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q96ER3; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P04844; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O43251; IntAct: EBI-20626314; Score: 0.50
DE  Interaction: Q14964; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9NP72; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O60831; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O15173; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O00264; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q15070; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P01111; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9BTX1; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O75352; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q13015; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O95490; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q8NF37; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q8N6L1; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q8TEX9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q16891; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q53GQ0; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q8TCT9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P04439; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O00165; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O75367; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P08754; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9H0Q3; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q86VR2; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9BW60; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q15125; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O75165; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9UBM7; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q15392; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P39656; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9UBF2; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q07065; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9NX63; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9Y6K0; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q8N111; IntAct: EBI-20626314; Score: 0.50
DE  Interaction: O95674; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O14735; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q96A33; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P35613; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9Y679; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q01814; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: O14983; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P05026; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P13637; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9BVK2; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9NP58; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9Y312; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: Q99653; IntAct: EBI-20639074; Score: 0.50
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044228;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003725;
GO  GO:0005525;
GO  GO:0046872;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0046983;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0005198;
GO  GO:0039654;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0039564;
GO  GO:0039502;
GO  GO:0046718;
GO  GO:0039694;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEI
SQ  IKKFKKDLAAMLRIINARKEKKRRGTDTSVGIVGLLLTTAMAVEVTRRGNAYYMYLDRSDAGEAISFPTTMGMNKCYIQI
SQ  MDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREY
SQ  TKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGC
SQ  VTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGK
SQ  GSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDC
SQ  EPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALA
SQ  GALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQ
SQ  TLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWD
SQ  FGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLVWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSV
SQ  DFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQL
SQ  TVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTS
SQ  VWLKVREDYSLECDPAVIGTAAKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKS
SQ  LAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAK
SQ  DGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDL
SQ  AKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVPINGFAL
SQ  AWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINV
SQ  VGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVT
SQ  GNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMAICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGET
SQ  TDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLL
SQ  AVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVEC
SQ  FEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIV
SQ  DLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEV
SQ  EVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANF
SQ  KADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIY
SQ  LQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPA
SQ  EVWTRYGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPY
SQ  KAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIP
SQ  EPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFIT
SQ  PAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAA
SQ  ARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSP
SQ  NKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEA
SQ  RRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYG
SQ  WNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQR
SQ  RYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGN
SQ  RIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKV
SQ  DTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKER
SQ  EHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVL
SQ  EEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQ
SQ  RGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHAL
SQ  RFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSY
SQ  AQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPY
SQ  LGKREDLWCGSLIGHRPRTTWAENIKNTVNMMRRIIGDEEKYVDYLSTQVRYLGEEGSTPGVL
//
ID  Q9LTX4;
PN  Probable ion channel POLLUX;
GN  K9P8;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9LTX4;
DR  Pfam: PF06241;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006811;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPIHTPRRTSLFQRSKTLPTNSYRRFTSPVIPTFRYDDGDTVSYDGDDSSNLPTVPNPEEKPVPVPSQSPSQRITRLWTQ
SQ  FSLTHCLKFICSCSFTYVMFLRSKVSRLEAENIILLTRCNSSSDNNEMEETNSRAVVFFSVIITFVLPFLLYMYLDDLSH
SQ  VKNLLRRTNQKKEDVPLKKRLAYSLDVCFSVYPYAKLLALLLATVVLIVYGGLALYAVSDCGVDEALWLSWTFVADSGSH
SQ  ADRVGVGARIVSVAISAGGMLIFATMLGLISDAISKMVDSLRKGKSEVLESNHILILGWSDKLGSLLKQLAIANKSIGGG
SQ  VVVVLAERDKEEMETDIAKFEFDLMGTSVICRSGSPLILADLKKVSVSNARAIIVLGSDENADQSDARALRVVLSLTGVK
SQ  EGWKGHVVVEMCDLDNEPLVKLVGGERIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIKKWPQLDGYCFED
SQ  VLISFPNAIPCGVKVAADGKIVLNPSDDYVLKEGDEILVIAEDDDTYAPGSLPEVRMCHFPKMQDPPKYPEKILFCGWRR
SQ  DIDDMIKVLEALLAPGSELWMFNEVPDQEREKKLTDAGLNISKLVNIKLVHRQGNAVIRRHLESLPLETFDSILILAEQS
SQ  LENSIVHSDSRSLATLLLIRDIQSKRLPYKDAKSSALRISGFPNCCWIRKMQQASDKSIVISEILDSRTKNLVSVSRISD
SQ  YVLSNELVSMALAMVAEDKQINRVLKELFAEKGNELCIRPAEFYIYDQEEVCFYDIMRRARQRQEIIIGYRLAGMEQAVI
SQ  NPTDKSKLTKWSLDDVFVVIASSQ
//
ID  Q5H8A5;
PN  Ion channel POLLUX;
GN  POLLUX;
OS  34305;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15616514, ECO:0000269|PubMed:19106374}; Multi-pass membrane protein {ECO:0000269|PubMed:15616514, ECO:0000269|PubMed:19106374}. Note=The chloroplastic localization proposed by PubMed:15616514 is probably an overexpression artifact.
DR  UNIPROT: Q5H8A5;
DR  Pfam: PF06241;
DE  Function: Ion channel with permeability for potassium. Involved in perinuclear calcium spiking but not in cytosolic calcium influx. Required for early signal transduction events leading to endosymbiosis. Acts early in a signal transduction chain leading from the perception of Nod factor to the activation of calcium spiking. Also involved in fungal entry into root epidermal cells during the establishment of the arbuscular mycorrhizal symbiosis. {ECO:0000269|PubMed:16903357, ECO:0000269|PubMed:19106374}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006811;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIPLPVAAANSNSNSNSNSNDEESPNLSTVIKPPLKKTKTLLPPPSSSSSNRPLHLRVSIDNNNNNNAPPPPADFSDHQW
SQ  NYPSFLGTTTRKRRPSSVKPPSTSNLRFDTIPKTKTKTKTNTNTNTNTNTNTNTNTDLPPPPVPSSSPVARPQHHNHRSP
SQ  PIFYLLIITCIIFVPYSSYLQYKLAKLEDHKLHLCRQSQIHFSSGHGNGKISIPIHDASFSYILSRKAALYIVLFTLILP
SQ  FLLYKYLDYLPQIINFLRRTHNNKEDVPLKKRIAYMLDVFFSIYPYAKLLALLFATLFLIGFGGLALYAVTGGSLAEALW
SQ  HSWTYVADSGNHAETQGTGQRVVSVSISSGGMLIFAMMLGLVSDAISEKVDSLRKGKCEVIERNHILILGWSDKLGSLLK
SQ  QLAIANKSVGGGVIVVLAEKEKEEMEMDITKLEFDFMGTSVICRSGSPLILADLKKVSVSKARAIIVLASDENADQSDAR
SQ  ALRVVLSLTGVKEGLRGHVVVEMSDLDNEPLVKLVGGELIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIK
SQ  RWPELDGLSFKDILISFPDAIPCGVKVAADGGKIVINPDDSYVMRDGDEVLVIAEDDDTYSPGSLPEVLKGFFPRIPDAP
SQ  KYPEKILFCGWRRDIDDMIMVLEAFLAPGSELWMFNEVPEKEREKKLAAGGLDVFGLENIKLVHREGNAVIRRHLESLPL
SQ  ETFDSILILADESVEDSVAHSDSRSLATLLLIRDIQSRRLPYKDTKSTSLRLSGFSHNSWIREMQQASDKSIIISEILDS
SQ  RTRNLVSVSRISDYVLSNELVSMALAMVAEDKQINRVLEELFAEQGNEMCIKPAEFYLFDQEELCFYDIMIRGRARQEII
SQ  IGYRLANQERAIINPSEKLVARKWSLGDVFVVIASGD
//
ID  Q5N941;
PN  Probable ion channel POLLUX;
GN  P0039A07;
OS  39947;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q5N941;
DR  UNIPROT: Q0JHD3;
DR  UNIPROT: Q5N940;
DR  Pfam: PF06241;
DE  Function: Required for mycorrhizal symbiosis. {ECO:0000269|PubMed:18852152, ECO:0000269|PubMed:18978069}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006811;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAESDGGEASPSGGGGGEGSPDPRRPPARPQLTKSRTISGSAASAFDRWGTSNSSSSILVRRSSTAPLPPGAAPRGLLTV
SQ  AVDEPSYAAPNGGAAMLDRDWCYPSFLGPHASRPRPPRSQQQTPTTTAAAAADSRSPTPAAPPQTASVSQREEEKSLASV
SQ  VKRPMLLDERRSLSPPPPQQRAPRFDLSPYLVLMLVVTVISFSLAIWQWMKATVLQEKIRSCCSVSTVDCKTTTEAFKIN
SQ  GQHGSDFINSADWNLASCSRMLVFAIPVFLVKYIDQLRRRNTDSIRLRSTEEEVPLKKRIAYKVDVFFSGHPYAKLLALL
SQ  LATIILIASGGIALYVVSGSGFLEALWLSWTFVADSGNHADQVGLGPRIVSVSISSGGMLVFATMLGLVSDAISEKVDSW
SQ  RKGKSEVIEVNHILILGWSDKLGSLLKQLAIANKSIGGGVVVVLAERDKEEMEMDIGKLEFDFMGTSVICRSGSPLILAD
SQ  LKKVSVSKARAIIVLASDENADQSDARALRVVLSLTGVKEGLRGHVVVEMSDLDNEPLVKLVGGELIETVVAHDVIGRLM
SQ  IQCALQPGLAQIWEDILGFENAEFYIKRWPELDGMRFGDVLISFPDAVPCGVKIASKAGKILMNPDNDYVLQEGDEVLVI
SQ  AEDDDTYVPASLPQVRKGFLPNIPTPPKYPEKILFCGWRRDIHDMIMVLEAFLAPGSELWMFNEVPEKERERKLTDGGMD
SQ  IYGLTNIKLVHKEGNAVIRRHLESLPLETFDSILILADESVEDSIVHSDSRSLATLLLIRDIQSKRLPSKELKSPLRYNG
SQ  FCHSSWIREMQHASDKSIIISEILDSRTRNLVSVSKISDYVLSNELVSMALAMVAEDKQINRVLEELFAEEGNEMCIRSA
SQ  EFYLYEQEELSFFDIMVRARERDEVVIGYRLANDDQAIINPEQKSEIRKWSLDDVFVVISKAGNATYFVKTTVMRSNPVV
SQ  YSSTF
//
ID  Q6X2U4;
PN  RNA-directed RNA polymerase p90;
GN  POLN;
OS  376262;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (By similarity). At 72 hpi, localizes to filamentous structures in the host cytoplasm (By similarity). {ECO:0000250|UniProtKB:P13889, ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000250|UniProtKB:Q86500}.
DR  UNIPROT: Q6X2U4;
DR  Pfam: PF01661;
DR  Pfam: PF05407;
DR  Pfam: PF00978;
DR  Pfam: PF12601;
DR  Pfam: PF01443;
DR  PROSITE: PS51743;
DR  PROSITE: PS51154;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51889;
DE  Function: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products. Together with RNA- directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation. {ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive- strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present. {ECO:0000250|UniProtKB:Q86500}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016020;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0046872;
GO  GO:0008174;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0006396;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVTAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHW
SQ  IEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETAGEAWHADYVCALRGAPSGPFYVHPEDVPRG
SQ  GRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRP
SQ  CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE
SQ  VGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
SQ  LAGIMKGAKRCAADSLSVAGWLDTIWDAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGHHLDTVQPPKPLPRPEI
SQ  AATWIVHAASADRHCACAPRCDVPRERPSAPAGPPDDEALIPPWLFAERRTLRCREWDFEALRARADTAATPAPLAPRPA
SQ  RYPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGART
SQ  WAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDANAVTAAVRADPGQLALT
SQ  SPPPDNPPPPRRARRSQRHADARGPPPPAPVRDPPPLPPSPPAPRRAGDPASPISAEPADRARDAEPEVACEPGGPATPT
SQ  RADPDSDIVESYARAAGPVHLRVRNIMDPPPGCKVVVNAANEGLLAGSGVCGAIFASAAATLAEDCRRLAPCPTGEAVAT
SQ  PGHGCGYTHIIHAVAPRRPQDPAALEQSEALLERAYRSVVALAAARRWACVACPLLGAGIYGWSAAESLRAALAAARTEP
SQ  AERVSLHICHPDRATLMHASVLVGAGLAARRVSPPPTEPLASCPADDPGRSTQRTASPPAAPPGDAAAPESRGCQGCELC
SQ  RYTRVTNDRAYVNLWLERDRGATGWAMRIPEVVVYGPEHLAAHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGMPQV
SQ  RCTPSNAHAALCRIGIPPRVSTRGDERDPNTCWLRAAANVAQAARACGAYTSAGCPKCAYGRALSEARTHEAFAALSQRW
SQ  IASHADASLDGTGDPLDPLMETVGCACSRVWVGSEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGG
SQ  GPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIKVWNMAAGAGKTT
SQ  RILAAFTREDLYVCPTNALLHEIQAKLRARDIDIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
SQ  VGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDVEGEHAGTFACNLWDGRQVDLHLAFSRETVR
SQ  RLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAE
SQ  LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
SQ  HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAAR
SQ  ELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKI
SQ  IMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
SQ  ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPSEVGLFGFHIPVKH
SQ  VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVR
SQ  ELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD
//
ID  Q6X2U2;
PN  RNA-directed RNA polymerase p90;
GN  POLN;
OS  376263;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (By similarity). At 72 hpi, localizes to filamentous structures in the host cytoplasm (By similarity). {ECO:0000250|UniProtKB:P13889, ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000250|UniProtKB:Q86500}.
DR  UNIPROT: Q6X2U2;
DR  Pfam: PF01661;
DR  Pfam: PF05407;
DR  Pfam: PF00978;
DR  Pfam: PF12601;
DR  Pfam: PF01443;
DR  PROSITE: PS51743;
DR  PROSITE: PS51154;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51889;
DE  Function: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products. Together with RNA- directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation. {ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive- strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present. {ECO:0000250|UniProtKB:Q86500}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016020;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0046872;
GO  GO:0008174;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0006396;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVTAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHW
SQ  IEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETAGEAWHADYVCALRGAPSGPFYVHPEDVPRG
SQ  GRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPMPGYTRP
SQ  CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE
SQ  VGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
SQ  LAGVMKGAKRCAADSLSVAGWLGTVWDAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGHHLDTVQPPKPLPRPEI
SQ  AATWIVHAASADRHCACAPRCDVPRERPSAPAGPPDDEAIIPPWLFAECRTLRCREWDFEALRARADTAATPAPLAPRPA
SQ  RHPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAVGAHMCAQARGLQAFVRVVPPPERPWADGGART
SQ  WAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDANAVTAAVRADPGQLALT
SQ  SPPPDNPPPPRRARRSQRHADARGPPPPAPARDPPPPAPSPPAPPRAGDPASPISAEPADRARDAEPEVACEPGGPATPA
SQ  RADPDSDIVESYARAAGPVHLRVRNIMDPPPGCKVVVNAANEGLLAGSGVCGAIFASAAASLAEDCRRLAPCPTGEAVAT
SQ  PGHGCGYAHIIHAVAPRRPQDPAALEQSEALLERAYRSIVALAAARRWTCVACPLLGAGIYGWSAAESLRAALAAARTEP
SQ  AERVSLHICHPDRATLMHASVLVGAGLAARRVSPPPTEPPASRPADDPGRSAQRTAPPPAAPPGDAAAPELRGCQGCELC
SQ  RYTRVTNDRAYVNLWLERDRGATGWAMRIPEVVVYGPEHLAAHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGMPQV
SQ  RCTPSNAHAALCRIGIPPRVSTRGDERDPNTCWLRAAANVAQAARACGAYTSAGCPKCAYGRALSEARTHEDFAALSQRW
SQ  IASHADASLDGTGDPLDPLMATVGCACSRVWVGSEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGG
SQ  GPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIKVWNMAAGAGKTT
SQ  RILAAFTREDLYVCPTNALLHEIQAKLRARDIDIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
SQ  VGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDVEGEHAGTFACNLWDGRQVDLHLAFSRETVR
SQ  RLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAE
SQ  LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
SQ  HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAAR
SQ  ELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKI
SQ  IMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
SQ  ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPSEVGLFGSHIPVKH
SQ  VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVR
SQ  ELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD
//
ID  Q9J6K9;
PN  RNA-directed RNA polymerase p90;
GN  POLN;
OS  376266;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (By similarity). At 72 hpi, localizes to filamentous structures in the host cytoplasm (By similarity). {ECO:0000250|UniProtKB:P13889, ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000250|UniProtKB:Q86500}.
DR  UNIPROT: Q9J6K9;
DR  Pfam: PF01661;
DR  Pfam: PF05407;
DR  Pfam: PF00978;
DR  Pfam: PF12601;
DR  Pfam: PF01443;
DR  PROSITE: PS51743;
DR  PROSITE: PS51154;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51889;
DE  Function: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products. Together with RNA- directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation. {ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive- strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present. {ECO:0000250|UniProtKB:Q86500}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016020;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0046872;
GO  GO:0008174;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0006396;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVTAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHW
SQ  IEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHG
SQ  GRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRP
SQ  CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE
SQ  VGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
SQ  LAGIMKGAKRCAADSLSVAGWLDTIWDAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEI
SQ  AATWIVHAASADRHCACAPRCDVPRERPSAPAGQPDDEALIPPWLFAERRALRCREWDFEALRARADTAAAPAPLAPRPA
SQ  RYPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARA
SQ  WAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDANAVTAAVRAGPGQLAAT
SQ  SPPPGDPPPPRRARRSQRHSDARGTPPPAPVRDPPPPAPSPPAPPRAGDPVPPTPAEPADRARDAELEVAYEPSGPPTST
SQ  KADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAADCRRLAPCPTGEAVAT
SQ  PGHGCGYTHIIHAVAPRRPRDPAALEEGEALLERAYRSIVALAAARRWAYVACPLLGAGVYGWSAAESLRAALAATRAEP
SQ  VERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGGPGRPAQRSASPPATPLGDATAPEPRGCQGCELC
SQ  RHTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGMPQV
SQ  RCTPSNAHAALCRTGVPPRVSTRGGELDPNTCWLRAAANVAQVARACGAYTSAGCPKCAYGRALSEARTHEDFAALSQRW
SQ  SASHADASPDGTGDPLDPLMETVGCACSRVWVGSEQEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGG
SQ  GPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIRVWNMAAGAGKTT
SQ  RILAAFTREDLYVCPTNALLHEIQAKLRARDIDIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
SQ  VGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGIFACNLWDGRQVDLHLAFSRETVR
SQ  RLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAE
SQ  LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
SQ  HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAAR
SQ  ELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKI
SQ  IMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
SQ  ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPAEVGLFGFHIPVKH
SQ  VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVR
SQ  ELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD
//
ID  Q86500;
PN  RNA-directed RNA polymerase p90;
GN  POLN;
OS  11043;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural polyprotein p200]: Host membrane {ECO:0000269|PubMed:19539969}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:22491463}. Host cytoplasm {ECO:0000269|PubMed:19539969}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000269|PubMed:19539969}. [Protease/methyltransferase p150]: Host membrane {ECO:0000269|PubMed:19539969, ECO:0000269|PubMed:25056903}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:20696450, ECO:0000269|PubMed:22491463}. Host cytoplasm {ECO:0000269|PubMed:19539969, ECO:0000269|PubMed:25056903}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (By similarity). At 72 hpi, localizes to filamentous structures in the host cytoplasm (PubMed:25056903). {ECO:0000250|UniProtKB:P13889, ECO:0000269|PubMed:25056903}. [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000269|PubMed:19539969}. Host cytoplasm {ECO:0000269|PubMed:19539969}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000269|PubMed:19539969}.
DR  UNIPROT: Q86500;
DR  Pfam: PF01661;
DR  Pfam: PF05407;
DR  Pfam: PF00978;
DR  Pfam: PF12601;
DR  Pfam: PF01443;
DR  PROSITE: PS51743;
DR  PROSITE: PS51154;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51889;
DE  Function: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000269|PubMed:11289813, ECO:0000269|PubMed:12076835}. [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products (PubMed:10823845, PubMed:9557742). Together with RNA-directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins (PubMed:11289813, PubMed:12076835). Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation (PubMed:20696450). {ECO:0000269|PubMed:10823845, ECO:0000269|PubMed:11289813, ECO:0000269|PubMed:12076835, ECO:0000269|PubMed:20696450, ECO:0000269|PubMed:9557742, ECO:0000305|PubMed:1518855}. [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive- strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins (PubMed:11289813, PubMed:12076835). A helicase activity is probably also present (PubMed:8599224). {ECO:0000269|PubMed:11289813, ECO:0000269|PubMed:12076835, ECO:0000269|PubMed:8599224}.
DE  Reference Proteome: Yes;
DE  Interaction: P06400; IntAct: EBI-2568715; Score: 0.52
DE  Interaction: Q9NUM4; IntAct: EBI-11478462; Score: 0.40
DE  Interaction: O14633; IntAct: EBI-11478489; Score: 0.40
DE  Interaction: Q9NS67; IntAct: EBI-11478512; Score: 0.40
DE  Interaction: P18847; IntAct: EBI-11478523; Score: 0.40
DE  Interaction: Q96D21; IntAct: EBI-11478529; Score: 0.40
DE  Interaction: P06732; IntAct: EBI-11478535; Score: 0.40
DE  Interaction: P02647; IntAct: EBI-11478541; Score: 0.40
DE  Interaction: Q9NV12; IntAct: EBI-11478547; Score: 0.40
DE  Interaction: Q96L50; IntAct: EBI-11478553; Score: 0.40
DE  Interaction: O43505; IntAct: EBI-11478559; Score: 0.40
DE  Interaction: O95707; IntAct: EBI-11478565; Score: 0.40
DE  Interaction: Q96C92; IntAct: EBI-11478571; Score: 0.40
DE  Interaction: O60224; IntAct: EBI-11478577; Score: 0.40
DE  Interaction: Q9P2N6; IntAct: EBI-11478583; Score: 0.40
DE  Interaction: P01562; IntAct: EBI-11478636; Score: 0.40
DE  Interaction: P08218; IntAct: EBI-11478662; Score: 0.40
DE  Interaction: Q96BM9; IntAct: EBI-11478668; Score: 0.52
DE  Interaction: Q8TAD8; IntAct: EBI-11478675; Score: 0.40
DE  Interaction: P60842; IntAct: EBI-11478682; Score: 0.40
DE  Interaction: Q8IWU5; IntAct: EBI-11478688; Score: 0.40
DE  Interaction: Q6P161; IntAct: EBI-11478694; Score: 0.40
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016020;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0046872;
GO  GO:0008174;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0006396;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVTAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHW
SQ  IEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHG
SQ  GRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRP
SQ  CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE
SQ  VGWWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
SQ  LAGIMKSAKRCAADSLSVAGWLDTIWDAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEI
SQ  AATWIVHAASADRHCACAPRCDVPRERPSAPAGPPDDEALIPPWLFAERRALRCREWDFEALRARADTAAAPAPLAPRPA
SQ  RYPTVLYRHPAHHGPWLTLDEPGGADAALVLCDPLGQPLRGPERHYAAGAHMCAQARGLQAFVRVVPPPERPWADGGARA
SQ  WAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPKLIALALRTLAQQGAALALSVRDLPRGTAFEANAVTAAVRAGPGQLAAT
SQ  SPPPGDPPPPRRARRSQRHSDARGTPPPAPVRDPPRPQPSPPAPPRVGDPVPPTTAEPADRARHAELEVVYEPSGPPTST
SQ  KADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAADCRRLAPCPIGEAVAT
SQ  PGHGCGYTHIIHAVAPRRPRDPAALEEGEALLERAYRSIVALAAARRWARVACPLLGAGVYGWSAAESLRAALAATRAEP
SQ  AERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGDPGRPAQRSASPPATPLGDATAPEPRGCQGCELC
SQ  RYTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGMPQV
SQ  RCTPSNAHAALCRTGVPPRVSTRGGELDPNTCWLRAAANVAQAARACGAYTSAGCPKCAYGRALSEARTHEDFAALSQWW
SQ  SASHADASPDGTGDPLDPLMETVGCACSRVWVGSEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGG
SQ  GPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASIQRPRKGPYNIRVWNMAAGAGKTT
SQ  RILAAFTREDLYVCPTNALLHEIQAKLRARDIDIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
SQ  VGDRDQCGPHYANNCRTPVPDRWPTGRSRHTWRFPDCWAARLRAGLDYDIEGERTGTFACNLWDGRQVDLHLAFSRETVR
SQ  RLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGLLRAAGLSAFLDAGALAE
SQ  LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
SQ  HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAAR
SQ  ELTDRYTRRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKI
SQ  IMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
SQ  ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARNAALKWTPAEVGLFGFHIPVKH
SQ  VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVR
SQ  ELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD
//
ID  Q8BCR0;
PN  RNA-directed RNA polymerase p90;
GN  POLN;
OS  376267;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (By similarity). At 72 hpi, localizes to filamentous structures in the host cytoplasm (By similarity). {ECO:0000250|UniProtKB:P13889, ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000250|UniProtKB:Q86500}.
DR  UNIPROT: Q8BCR0;
DR  UNIPROT: Q8VA11;
DR  UNIPROT: Q8VA13;
DR  Pfam: PF01661;
DR  Pfam: PF05407;
DR  Pfam: PF00978;
DR  Pfam: PF12601;
DR  Pfam: PF01443;
DR  PROSITE: PS51743;
DR  PROSITE: PS51154;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51889;
DE  Function: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products. Together with RNA- directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation. {ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive- strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present. {ECO:0000250|UniProtKB:Q86500}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016020;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0046872;
GO  GO:0008174;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0006396;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVSAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHW
SQ  IEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHG
SQ  GRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRP
SQ  CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE
SQ  VGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
SQ  LAGIMKSAKRCAADSLSVAGWLDTIWDAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEI
SQ  AATWIVHAASADRHCACAPRCDVPRERPSAPACPPDDEALIPPWLFAERRALRCREWDFEALRARADTAAAPAPLAPRPA
SQ  RYPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARA
SQ  WAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPKLIALALRTLAQQGAALALSVRDLPGGAAFDANAVTAAVRAGPGQFAAT
SQ  SPPPGDPPPPRRARRSQRHSDARGTPPPAPARDPPPPAPSPPAPPRAGDPDSPTSAEPADRARHAELEVVYEPSGPPTST
SQ  KADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAADCRRLAPCPTGEAVAT
SQ  PGHGCGYTHIIHAVAPRRPRDPAALEEGEALLERAYRSIVALAAARRWACVACPLLGAGVYGWSAAESLRAALAATRTEP
SQ  AERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGDLGRPAQRSASPPATPLGDATAPEPRGCQGCELC
SQ  RCTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGMPQV
SQ  RCTPSNAHAALCRTGVPPRVSTRGGELDPNTCWLRAAANVAQAARACGAYTSAGCPKCAYGRALSEARTHEDFAALSQRW
SQ  SASHADASPDGTGDPLDPLMETVGCACSRVWVGTEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGG
SQ  GPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIRVWNMAAGAGKTT
SQ  RILAAFTREDLYVCPTNALLHEIQAKLRARDIDIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
SQ  VGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGTFACNLWDGRQVDLHLAFSRETVR
SQ  RLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAE
SQ  LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
SQ  HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAAR
SQ  ELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKI
SQ  IMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
SQ  ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPAEVGLFGFHIPVKH
SQ  VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVR
SQ  ELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD
//
ID  Q99IE7;
PN  RNA-directed RNA polymerase p90;
GN  POLN;
OS  376265;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (By similarity). At 72 hpi, localizes to filamentous structures in the host cytoplasm (By similarity). {ECO:0000250|UniProtKB:P13889, ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000250|UniProtKB:Q86500}.
DR  UNIPROT: Q99IE7;
DR  Pfam: PF01661;
DR  Pfam: PF05407;
DR  Pfam: PF00978;
DR  Pfam: PF12601;
DR  Pfam: PF01443;
DR  PROSITE: PS51743;
DR  PROSITE: PS51154;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51889;
DE  Function: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products. Together with RNA- directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation. {ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive- strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present. {ECO:0000250|UniProtKB:Q86500}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016020;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0046872;
GO  GO:0008174;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0006396;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVTAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHW
SQ  IEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHG
SQ  GRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRP
SQ  CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE
SQ  VGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
SQ  LAGIMKSAKRCAADSLSVAGWLDTIWDAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEI
SQ  AATWIVHAASADRHCACAPRRDAPRERPSAPAGPPDDEALIPPWLFAERRALRCREWDFEALRARADTAAAPAPLAPRPA
SQ  RCPTVLYRHPAHYGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARA
SQ  WAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDANAVTAAVRAGPGQSAAT
SQ  SPPPGDPPPPRRARRSQRHLDARGTPPPAPARDPPPPAPSPPAPPRAGDPVLPTSAGPADRARHAELEVAYEPSDPPTPT
SQ  KADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAADCRRLAPCPTGEAVAT
SQ  PGHGCGYTHIIHAVAPRRPRDPAALEEGEALLERAYRSIVALAAARRWACVACPLLGAGVYGWSAAESLRAALAATRAEP
SQ  AERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGDPGRPAQRSASPPATPLGDATAPEPRGCQGCELC
SQ  RYTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGMPQV
SQ  RCTPSNAHAALCRTGVPPRVSTRGGELDPNTCWLRAAASVAQAARACGAYTSAGCPKCAYGRALSEARTHEDFAALSQRW
SQ  SASHADASPDGTGDPLDPLMETVGCACSRVWVGSEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGG
SQ  GPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIRVWDMAAGAGKTT
SQ  RILAAFTREDLYVCPTNALLHEIQAKLRARDIDIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
SQ  VGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGTFACNLWDGRQVDLHLAFSRETVR
SQ  RLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAE
SQ  LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
SQ  HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAAR
SQ  ELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKI
SQ  IMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
SQ  ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPAEVGLFGFHIPVKH
SQ  VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVR
SQ  ELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD
//
ID  O40955;
PN  RNA-directed RNA polymerase p90;
GN  POLN;
OS  11044;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (By similarity). At 72 hpi, localizes to filamentous structures in the host cytoplasm (By similarity). {ECO:0000250|UniProtKB:P13889, ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000250|UniProtKB:Q86500}.
DR  UNIPROT: O40955;
DR  Pfam: PF01661;
DR  Pfam: PF05407;
DR  Pfam: PF00978;
DR  Pfam: PF12601;
DR  Pfam: PF01443;
DR  PROSITE: PS51743;
DR  PROSITE: PS51154;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51889;
DE  Function: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products. Together with RNA- directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation. {ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive- strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present. {ECO:0000250|UniProtKB:Q86500}.
DE  Reference Proteome: No;
DE  Interaction: Q9MZE0; IntAct: EBI-6378260; Score: 0.56
DE  Interaction: Q07021; IntAct: EBI-6378072; Score: 0.50
DE  Interaction: Q9NU22; IntAct: EBI-6378072; Score: 0.35
DE  Interaction: Q92616; IntAct: EBI-6378072; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-6378072; Score: 0.35
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016020;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0046872;
GO  GO:0008174;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0006396;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVSAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHW
SQ  IEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHG
SQ  GRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRP
SQ  CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE
SQ  VGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
SQ  LAGIMKSAKRCAADSLSVAGWLDTIWGAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEI
SQ  AATWIVHAASADRHCACAPRCDVPRERPSAPAGPPDDEALIPPWLFAEHRALRCREWDFEVLRARADTAAAPAPLAPRPA
SQ  RYPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARA
SQ  WAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDANAVTAAVRAGPGQSAAT
SQ  SSPPGDPPPPRCARRSQRHSDARGTPPPAPARDPPPPAPSPPAPPRAGDPVPPTSAGPADRARDAELEVAYEPSGPPTST
SQ  KADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAADCRRLAPCPTGEAVAT
SQ  PGHGCGYTHIIHAVAPRRPRDPAALEEGEALLERAYRSIVALAAARRWARVACPLLGAGVYGWSAAESLRAALAATRTEP
SQ  AERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGDPGRPAQRSASPPATPLGDATAPEPRGCQGCELC
SQ  RYTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGVPQV
SQ  RCTPSNAHAALCRTGVPPRVSTRGGELDPNTCWLRAAANVAQAARACGAYTSAGCPRCAYGRALSEARTHKDFAALSQRW
SQ  SASHADASSDGTGDPLDPLMETVGCACSRVWVGSEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGG
SQ  GPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIRVWNMAAGAGKTT
SQ  RILAAFTREDLYVCPTNALLHEIQAKLRARDIEIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
SQ  VGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGTFACNLWDGRQVDLHLAFSRETVR
SQ  RLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAE
SQ  LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
SQ  HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAAR
SQ  ELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKI
SQ  IMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
SQ  ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPAEVGLFGFHIPVKH
SQ  VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVR
SQ  ELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD
//
ID  P13889;
PN  RNA-directed RNA polymerase p90;
GN  POLN;
OS  11045;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (PubMed:10438871, PubMed:8128633). At 72 hpi, localizes to filamentous structures in the host cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q86500, ECO:0000269|PubMed:10438871, ECO:0000269|PubMed:8128633}. [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000250|UniProtKB:Q86500}.
DR  UNIPROT: P13889;
DR  Pfam: PF01661;
DR  Pfam: PF05407;
DR  Pfam: PF00978;
DR  Pfam: PF12601;
DR  Pfam: PF01443;
DR  PROSITE: PS51743;
DR  PROSITE: PS51154;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51889;
DE  Function: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products. Together with RNA- directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation. {ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive- strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present. {ECO:0000250|UniProtKB:Q86500}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016020;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0046872;
GO  GO:0008174;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0006396;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVTAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHW
SQ  IEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHG
SQ  GRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRP
SQ  CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAE
SQ  VGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALCHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
SQ  LAGIMKGAKRCAADSLSVAGWLDTIWDAIKRFLGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEI
SQ  AATWIVHAASEDRHCACAPRCDVPRERPSAPAGQPDDEALIPPWLFAERRALRCREWDFEALRARADTAAAPAPPAPRPA
SQ  RYPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARA
SQ  WAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDANAVTAAVRAGPRQSAAA
SQ  SPPPGDPPPPRRARRSQRHSDARGTPPPAPARDPPPPAPSPPAPPRAGDPVPPIPAGPADRARDAELEVACEPSGPPTST
SQ  RADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAANCRRLAPCPTGEAVAT
SQ  PGHGCGYTHIIHAVAPRRPRDPAALEEGEALLERAYRSIVALAAARRWACVACPLLGAGVYGWSAAESLRAALAATRTEP
SQ  VERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGDPGRPAQRSASPPATPLGDATAPEPRGCQGCELC
SQ  RYTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWHGMPQV
SQ  RCTPSNAHAALCRTGVPPRASTRGGELDPNTCWLRAAANVAQAARACGAYTSAGCPKCAYGRALSEARTHEDFAALSQRW
SQ  SASHADASPDGTGDPLDPLMETVGCACSRVWVGSEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGG
SQ  GPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIRVWNMAAGAGKTT
SQ  RILAAFTREDLYVCPTNALLHEIQAKLRARDIDIKNAATYERRLTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
SQ  VGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGTFACNLWDGRQVDLHLAFSRETVR
SQ  RLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALTRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAE
SQ  LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
SQ  HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAAR
SQ  ELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKI
SQ  IMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
SQ  ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPAEVGLFGFHIPVKH
SQ  VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVR
SQ  ELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD
//
ID  Q99IE5;
PN  RNA-directed RNA polymerase p90;
GN  POLN;
OS  376264;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural polyprotein p200]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to cytoplasmic foci at 24 hpi. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=At 36 hpi, localizes to the host cytoplasm, probably in vesicles inside host vacuoles of endosomal and lysosomal origin (By similarity). At 72 hpi, localizes to filamentous structures in the host cytoplasm (By similarity). {ECO:0000250|UniProtKB:P13889, ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Host membrane {ECO:0000250|UniProtKB:Q86500}. Host cytoplasm {ECO:0000250|UniProtKB:Q86500}. Note=Localizes to the cytoplasm and to the cytoplasmic fibers formed by protease/methyltransferase p150. {ECO:0000250|UniProtKB:Q86500}.
DR  UNIPROT: Q99IE5;
DR  Pfam: PF01661;
DR  Pfam: PF05407;
DR  Pfam: PF00978;
DR  Pfam: PF12601;
DR  Pfam: PF01443;
DR  PROSITE: PS51743;
DR  PROSITE: PS51154;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51889;
DE  Function: [Non-structural polyprotein p200]: Probable principal replicase for the negative-strand DNA, which replicates the 40S (+) genomic RNA into (-) antigenomic RNA. It cannot replicate the (-) into (+) until cleaved into p150 and p90 mature proteins. {ECO:0000250|UniProtKB:Q86500}. [Protease/methyltransferase p150]: Protease that cleaves the precursor polyprotein into two mature products. Together with RNA- directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation. {ECO:0000250|UniProtKB:Q86500}. [RNA-directed RNA polymerase p90]: Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive- strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present. {ECO:0000250|UniProtKB:Q86500}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016020;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0046872;
GO  GO:0008174;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0006396;
GO  GO:0039694;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKLLDEVLAPGGPYNLTVGSWVRDHVRSIVEGAWEVRDVVTAAQKRAIVAVIPRPVFTQMQVSDHPALHAISRYTRRHW
SQ  IEWGPKEALHVLIDPSPGLLREVARVERRWVALCLHRTARKLATALAETASEAWHADYVCALRGAPSGPFYVHPEDVPHG
SQ  GRAVADRCLLYYTPMQMCELMRTIDATLLVAVDLWPVALAAHVGDDWDDLGIAWHLDHDGGCPADCRGAGAGPTPGYTRP
SQ  CTTRIYQVLPDTAHPGRLYRCGPRLWTRDCAVAELSWEVAQHCGHQARVRAVRCTLPIRHVRSLQPSARVRLPDLVHLAA
SQ  VGRWRWFSLPRPVFQRMLSYCKTLSPDAYYSERVFKFKNALSHSITLAGNVLQEGWKGTCAEEDALCAYVAFRAWQSNAR
SQ  LAGIMKSAKRCAADSLSVAGWLDTIWDAIKRFFGSVPLAERMEEWEQDAAVAAFDRGPLEDGGRHLDTVQPPKSPPRPEI
SQ  AATWIVHAASADRHCACAPRCDAPRERPSAPAGPPDDEALIPPWLFAERRALRCREWDFEALRARADTAAAPAPLAPRPA
SQ  RCPTVLYRHPAHHGPWLTLDEPGEADAALVLCDPLGQPLRGPERHFAAGAHMCAQARGLQAFVRVVPPPERPWADGGARA
SQ  WAKFFRGCAWAQRLLGEPAVMHLPYTDGDVPQLIALALRTLAQQGAALALSVRDLPGGAAFDAHAVTAAVRAGPGQSAAT
SQ  SPPPGDPPPPRRARRSQRHLDARGTPPPAPARDPPPPAPSPPAPPRAGDPVLPTSAGPADRARHAELEVAYEPSDPPTPT
SQ  KADPDSDIVESYARAAGPVHLRVRDIMDPPPGCKVVVNAANEGLLAGSGVCGAIFANATAALAADCRRLAPCPTGEAVAT
SQ  PGHGCGYTHIIHAVAPRRPRDPAALEEGEALLERAYRSIVALAAARRWACVACPLLGAGVYGWSAAESLRAALAATRAEP
SQ  AERVSLHICHPDRATLTHASVLVGAGLAARRVSPPPTEPLASCPAGDPGRPAQRSASPPATPLGDATAPEPRGCQGCELC
SQ  RYTRVTNDRAYVNLWLERDRGATSWAMRIPEVVVYGPEHLATHFPLNHYSVLKPAEVRPPRGMCGSDMWRCRGWQGMPQV
SQ  RCTPSNAHAALCRTGVPPRVSTRGGELDPNTCWFRAAANVAQAARACGAYTSAGCPKCAYGRALSEARTHEDFAALSQRW
SQ  SASHADASPDGTGDPLDPLMETVGCACSRVWVGSEHEAPPDHLLVSLHRAPNGPWGVVLEVRARPEGGNPTGHFVCAVGG
SQ  GPRRVSDRPHLWLAVPLSRGGGTCAATDEGLAQAYYDDLEVRRLGDDAMARAALASVQRPRKGPYNIRVWNMAAGAGKTT
SQ  RILAAFTREDLYVCPTNALLHEIQAKLRARDIDIKNAATYERALTKPLAAYRRIYIDEAFTLGGEYCAFVASQTTAEVIC
SQ  VGDRDQCGPHYANNCRTPVPDRWPTERSRHTWRFPDCWAARLRAGLDYDIEGERTGTFACNLWDGRQVDLHLAFSRETVR
SQ  RLHEAGIRAYTVREAQGMSVGTACIHVGRDGTDVALALVRDLAIVSLTRASDALYLHELEDGSLRAAGLSAFLDAGALAE
SQ  LKEVPAGIDRVVAVEQAPPPLPPADGIPEAQDVPPFCPRTLEELVFGRAGHPHYADLNRVTEGEREVRYMRISRHLLNKN
SQ  HTEMPGTERVLSAVCAVRRYRAGEDGSTLRTAVARQHPRPFRQIPPPRVTAGVAQEWRMTYLRERIDLTDVYTQMGVAAR
SQ  ELTDRYARRYPEIFAGMCTAQSLSVPAFLKATLKCVDAALGPRDTEDCHAAQGKAGLEIRAWAKEWVQVMSPHFRAIQKI
SQ  IMRALRPQFLVAAGHTEPEVDAWWQAHYTTNAIEVDFTEFDMNQTLATRDVELEISAALLGLPCAEDYRALRAGSYCTLR
SQ  ELGSTETGCERTSGEPATLLHNTTVAMCMAMRMVPKGVRWAGIFQGDDMVIFLPEGARSAALKWTPAEVGLFGFHIPVKH
SQ  VSTPTPSFCGHVGTAAGLFHDVMHQAIKVLCRRFDPDVLEEQQVALLDRLRGVYAALPDTVAANAAYYDYSAERVLAIVR
SQ  ELTAYARGRGLDHPATIGALEEIQTPYARANLHDAD
//
ID  G0S6T0;
PN  Nucleoporin POM33;
GN  POM33;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q12164}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12164}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q12164}.
DR  UNIPROT: G0S6T0;
DR  UNIPROT: G0ZGV8;
DR  Pfam: PF03661;
DE  Function: Contributes to proper distribution and/or efficient assembly of nuclear pores. {ECO:0000250|UniProtKB:Q12164}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPPPPSADVPLAERLQRLASTLQFAWFSGHALLLLCVFRYAFSWIRFNYYSGMARFCYRFAFIAAAATYGIVVYKTWRA
SQ  RQKTGVKTSGIKDYLRDENIQYLVLALVWLFMPQYPLALLPYGIYSVFHVATYVRANLIPTLVPPQRINAPAGASPNAKP
SQ  QYTQHPASEAIGVFVKKYYDSSMSMVARLEIMLWLRLILSVILFQRRSWILFAIYTTFLRTRFSQSIHVQNAFALLEARI
SQ  DNLIGAQGTPPQARQVWDNVKTAARQFYAVTDLNKYESGVAAPKKSS
//
ID  Q12164;
PN  Pore membrane protein of 33 kDa;
GN  POM33;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus, nuclear pore complex.
DR  UNIPROT: Q12164;
DR  UNIPROT: D6VXY1;
DR  Pfam: PF03661;
DE  Function: Contributes to proper distribution and/or efficient assembly of nuclear pores. Required for normal pore density in the daughter nucleus during telophase. {ECO:0000269|PubMed:20498018}.
DE  Reference Proteome: Yes;
DE  Interaction: P32793; IntAct: EBI-7294869; Score: 0.62
DE  Interaction: P43603; IntAct: EBI-489021; Score: 0.00
DE  Interaction: Q03012; IntAct: EBI-7737153; Score: 0.40
DE  Interaction: P43132; IntAct: EBI-8228578; Score: 0.22
DE  Interaction: P39743; IntAct: EBI-7294890; Score: 0.50
DE  Interaction: P10591; IntAct: EBI-3681182; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3699913; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3718362; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3808883; Score: 0.35
DE  Interaction: Q02785; IntAct: EBI-20814983; Score: 0.37
DE  Interaction: P33302; IntAct: EBI-20815291; Score: 0.37
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0031309;
GO  GO:0005643;
GO  GO:0071786;
GO  GO:0061024;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSRPANNQGPPNLPARDKSLVQRFMAVAKSLQFAWFTGHSVVLISSILYLLKMSEFYYRSAYLGVIESFGIIIYQQFFT
SQ  RNEPLQTQDAAATKASIKSRVAGLLKSEDVLYLVLANFWLFTPRFSFSLIPFFAFAVFHVLIYVEKVLLPKVFHLSSKDS
SQ  SKILSFIDKFVVQYNDLCMHWVGTAELLIFILVLFRAILCFQRSWIILVVYAIFIKLRYENSKYMKAAFAQWRVRMDGII
SQ  SHPSIPPFVKRAYNAIKMSLIRLSEYRLSGAPQVTKKQN
//
ID  G0S7R3;
PN  Nucleoporin POM34;
GN  POM34;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q12445}. Nucleus membrane {ECO:0000250|UniProtKB:Q12445}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12445}. Note=Central core structure of the nuclear pore complex. {ECO:0000250|UniProtKB:Q12445}.
DR  UNIPROT: G0S7R3;
DR  UNIPROT: G0ZGV6;
DR  Pfam: PF08058;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000250|UniProtKB:Q12445}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0015031;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSTLSVAKAASTPVKQITSAVGPVKESPGNWKHPRLAEITRRQSRNIFGEKNVRQIVYNVAAIVLLEIFRVFASPSIPS
SQ  QLILPSLRPYSLWIHAVFLVIPLTNIVIALLPLFRPVDDLSDIPLTPAQRKLLGLPPSSKPATPNSVYSTPPRYSRTPSL
SQ  AGSPASIKSYTSSTLPTASSPTPGAAGIGAGSPAAPIYLSPSKFTTSTSSQQFSPSPSGASPLLHRAISNTSTASGVSPY
SQ  GSPNSPSKFGASTNSTLAASTISTSTFSVSTTSSIAHVLNNSRLRESVIEGVPATPTPVGKGASVKANSKWLYQRGRRTS
SQ  SNNWVY
//
ID  Q12445;
PN  Nucleoporin POM34;
GN  POM34;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Multi-pass membrane protein. Note=Central core structure of the nuclear pore complex.
DR  UNIPROT: Q12445;
DR  UNIPROT: D6VY20;
DR  UNIPROT: E9P8U3;
DR  UNIPROT: Q7LGY6;
DR  Pfam: PF08058;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. {ECO:0000269|PubMed:10684247}.
DE  Reference Proteome: Yes;
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P49018; IntAct: EBI-7764055; Score: 0.37
DE  Interaction: P38356; IntAct: EBI-7764142; Score: 0.37
DE  Interaction: P38298; IntAct: EBI-7764388; Score: 0.37
DE  Interaction: P35206; IntAct: EBI-7764456; Score: 0.37
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: P11484; IntAct: EBI-3782274; Score: 0.35
GO  GO:0031309;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0070762;
GO  GO:0017056;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0006606;
GO  GO:0030474;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKIQAGQLGLDDNDVPGPLPDTDSKPSSQSQNDTPMFKLGNFESPVLKELSRRTVNKEMETQRIMTNVIAFAFWNLLVKF
SQ  IKFFWNNTHVGRQFCNRLSRIHLYMLTFHTLKKANIIYHTTFSWLNAELLDYLFHLLISLNILFSLWKLLSTVKVSDLNL
SQ  TDRQKKLLGVDMQSSVDTGLQPQHPHYVSTSKISQMAQNKTHIPQTNLKNHPAYLFKGLETPLKARQREMAEEQTKLQSQ
SQ  SLHTKNVFGTLQRHSGISSTLVSANNDNNSPHTPVTRKGYIPSSKYAYMMNSQSPRGKI
//
ID  P42001;
PN  Protection of telomeres homolog 1;
GN  pot;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:23390606, ECO:0000269|PubMed:24297748, ECO:0000305|PubMed:18329362}. Nucleus envelope {ECO:0000269|PubMed:24297748}. Chromosome, telomere {ECO:0000269|PubMed:23390606, ECO:0000305|PubMed:18329362}. Note=More highly expressed in meiotic pachytene nuclei than in diakinesis-stage oocyte nuclei (PubMed:23390606). Also expressed in mitotic nuclei (PubMed:23390606). {ECO:0000269|PubMed:23390606}.
DR  UNIPROT: P42001;
DR  UNIPROT: A0A2K5ATS5;
DR  UNIPROT: A0A2K5ATS9;
DR  UNIPROT: A0A2K5ATU9;
DE  Function: Telomeric DNA-binding protein, which binds to single-stranded C-rich repeat sequences, with high specificity to the 5'-GCCTAA-3' sequence (PubMed:18329362, PubMed:23390606). Repeat sequence binding can be at the 5' or 3' telomeric end (PubMed:18329362). May have a role in protecting the 5' end of the C-rich strand of the telomere (PubMed:23390606). Acts redundantly with pot-2 to negatively regulate telomerase-mediated telomere extension (PubMed:18329362, PubMed:23390606, PubMed:24297748). Also regulates telomere length by the telomerase-independent telomere maintenance pathway called ALT (alternative lengthening of telomeres) (PubMed:23390606, PubMed:22547822, PubMed:24297748). Through sun-1, anchors telomeres to the nuclear envelope in embryos (PubMed:24297748). {ECO:0000269|PubMed:18329362, ECO:0000269|PubMed:22547822, ECO:0000269|PubMed:23390606, ECO:0000269|PubMed:24297748}.
DE  Reference Proteome: Yes;
GO  GO:0000781;
GO  GO:0005635;
GO  GO:0043047;
GO  GO:1904357;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQYTYQHIQDLVPGPTPQNFYGKIIFIKKKINQIVVLIKDETQSIYLRVIPKEDQELEFQLRQVVRVHRCKIQSILNSKE
SQ  GIAQIGLFGCHLIAWSQSGKVDNPVIISSRSWTKSDEDSERLQTLRKLGKSRRKSGRKTSVDTMANKLIERREAMFADTF
SQ  IKSLFNKIALSRKEHLSRNARELFYHRPGDIVETQNLLEIDDSWFNDENSEQFVQYVLNCTTCHVEYNHVEYAQNNIPTN
SQ  CRFCQEAMESFHAAFRIRISIETYGVFLTIPLELIKTELDICEDWDSESNIVEEEEKVTRFKKNIQEKVRDASIVHIKGI
SQ  SSLLLIIMLNINSISLVNNITENKRILLQKSNVPSSLQLKILITPFVIVVVRFFGITWIYSGSSCIEEVLNLIDNCSRRR
//
ID  Q08358;
PN  p5;
GN  CP2475L;
OS  10498;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp220]: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:9032369}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000269|PubMed:9032369}. [p34]: Virion {ECO:0000269|PubMed:30185597}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12525602}. Note=Localizes to the viral factory at 16 hpi (PubMed:33429879). In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope (PubMed:12438573). {ECO:0000269|PubMed:12438573, ECO:0000269|PubMed:33429879}. [p14]: Virion {ECO:0000269|PubMed:30185597}. Host cytoplasm, host perinuclear region. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA- containing nucleoid and the inner envelope (PubMed:12438573). {ECO:0000269|PubMed:12438573}. [p37]: Virion {ECO:0000269|PubMed:30185597}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:17580096}. Host nucleus {ECO:0000269|PubMed:17580096}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA- containing nucleoid and the inner envelope (PubMed:12438573). {ECO:0000269|PubMed:12438573}. [p150]: Virion {ECO:0000269|PubMed:12438573, ECO:0000269|PubMed:30185597}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12525602}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope (PubMed:12438573). {ECO:0000269|PubMed:12438573}. [p5]: Virion {ECO:0000269|PubMed:30185597}.
DR  UNIPROT: Q08358;
DR  UNIPROT: Q65287;
DE  Function: [Polyprotein pp220]: Essential for the core assembly. Its myristoyl moiety may function as a membrane-anchoring signal to bind the developing core shell to the inner viral envelope. {ECO:0000269|PubMed:11861832}. [p34]: The structural protein p34 is a component of the virus core shell. {ECO:0000269|PubMed:12438573}. [p14]: The structural protein p14 is a component of the virus core shell. {ECO:0000269|PubMed:12438573}. [p37]: The structural protein p37 is a component of the virus core shell. {ECO:0000269|PubMed:12438573}. [p150]: The structural protein p150 is a component of the virus core shell. {ECO:0000269|PubMed:12438573}.
DE  Reference Proteome: Yes;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044423;
GO  GO:0019069;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8335009};
SQ  MGNRGSSTSSRPPLSSEANLYAKLQDHIQRQTRPFSGGGYFNGGGDKNPVQHIKDYHIDSVSSKAKLRVIEGIIRAIAKI
SQ  GFKVDTKQPIEDILKDIKKQLPDPRAGSTFVKNAEKQETVCKMIADAINQEFIDLGQDKLIDTTDGAASICRQIVLYINS
SQ  LTHGLRAEYLDVHGSIENTLENIKLLNDAIKQLHERMVTEVTKAAPNEEVINAVTMIEAVYRRLLNEQNLQINILTNFID
SQ  NILTPTQKELDKLQTDEVDIIKLLNDTNSVLGTKNFGKVLSYTLCNLGIAASVANKINKALQKVGLKVEQYLQSKNWAEF
SQ  DKELDLKRFSGLVSAENIAEFEKAVNLLRQTFNERHKILENSCAKKGGDEEKTPLDRRIEAQRLDRKHILMEFLNKSTQA
SQ  YNDFLENVKKIGIKLVKEIALTPNITRLRDALSRINDMGTIALDLSLIGFYTNAAAREERETFLTQFMLVKNVLEEQSKI
SQ  DPNFKNLYDSCSRLLQIIDFYTDIVQKKYGGGEDCECTRVGGAALTVEELGLSKAARSQVDLNQAINTFMYYYYVAQIYS
SQ  NLTHNKQEFQSYEENYATILGDAIAGRLMQLDTEKNARINSPAVDLARGHVGPNPGGAQEADWKAAVSAIELEYDVKRRF
SQ  YRALEGLDLYLKNITKTFVNNIDSIQTVQQMLDGVRIIGRWFTEATGDTLAQVFESFPTSAGNDSNVFTDNAPAGHYYEK
SQ  VAAEIQQGRSVGTLRPVRASQAKNIRDLIGRSLSNFQALKNIINAFARIGDMLGGEELRQMVPMSPLQIYKTLLEYIQHS
SQ  ALSVGLKNLNQSEIGGQRVALARTPEEAAQRVYLSTVRVNDALSTRWETEDVFFTFMLKSMAAKIFIVLGIYDMFERPEP
SQ  VYKLIPTRMILGGADELEPEVIPEAAELYFRLPRLAEFYQKLFSFRDENVQISMLPELEGIFSGLIRIIFMRPIELINIG
SQ  DYSETEIRQLIKEINVIYQHFNLEYGEQEATKKALIHFVNEINRRFGVITRTEWEKFQRIVQEARTMNDFGMMNQTNYSI
SQ  LPDEDGYTQSSQLLPSDRFISPSTQPTPKWRPALYNIDSVDVQTGMLQPNSQWDLVQKFRKQLSEMFEDPSLQQELGKVS
SQ  YQELIRQAINELKKEHTDKIQIVSKLIQGSESLADTDVNKIFLFHETVITGLNLLSAIYVLLNNFRNNIKGLDLDTIQKS
SQ  IIEWLRETQAANVNRANLIDWLGRKHGAISEIRNPGLVVKENDVRLSRVYPDPTTNATAPQDQNLVTETLFAWIVPYVGI
SQ  PAGGGVRAEQELAARYLVDNQRIMQLLLTNIFEMTSSFNKMVQVRFPETSTAQVHLDFTGLISLIDSLMADTKYFLNLLR
SQ  PHIDKNIIQYYENRSNPGSFYWLEEHLIDKLIKPPTDAGGRPLPGGELGLEGVNQIINKTYILLTKPYNVLQLRGGVQRR
SQ  DAANIQINNNPQPSERFEQYGRVFSRLVFYDALENNSGLRVEQVVLGDFRLSNLIRTNNAQEENTLSYWDNMAPRTYANV
SQ  NDAANNLRRYRLYGSDYGIQNNRSMMMVFNQLVASYIARFYDAPSGKIYLNLINAFANGNFSQAVMELGYTHPDLARDNI
SQ  AFGHRGDPTEQSVLLLSLGLMLQRLIKDTNRQGLSQHLISTLTEIPIYLKENYRANLPLFNKMFNILISQGELLKQFIQY
SQ  TNVQLARPNLMGLLGANNDSVIYYNNNINVPMTGLSVGQAALRGIGGVFRPNVTLMPLGDAQNNTSDVVRKRLVAVIDGI
SQ  IRGSHTLADSAMEVLHELTDHPIYLETEEHFIQNYMSRYNKEPLMPFSLSLYYLRDLRIENNEVYDPLLYPNLESGSPEF
SQ  KLLYGTRKLLGNDPVQLSDMPGVQLIMKNYNETVVAREQITPTRFEHFYTHAIQALRFIVNIRSFKTVMMYNENTFGGVN
SQ  LISENRDDKPIITAGIGMNAVYSLRKTLQDVISFVESSYQEEQINHIHKIVSPKGQTRTLGSNRERERIFNLFDMNIIPI
SQ  NVNALMRSIPLANIYNYDYSFEEIACLMYGISAEKVRSLNTAAPQPDIAEVLNIPNRPPMNTREFMLKLLINPYVSVSIT
SQ  QYGNELMSKGSAGYMSRIFRGDNALNMGRPKFLSDQIFNKVLFGSLYPTQFDYDEAGPGLAAGIQRGREQWGQPLSEYIN
SQ  QALHELVRTIRIPQKLRVLRNIIVKNQLIADLTTIREQLVSMRREVENMIQTPEIQNNPTPEVIAAAQNWTQQYRARVDT
SQ  LINFIGNIGQPNSMLDLIQTITPVTVRAQLGVIFNRHGIPVPHPRQILQTDDEATQWFMTNILNIPAIIMTPFTDLANDL
SQ  RTFLETLERYVFNVPRWLGPSTGRVARAPVRMAPRDMRHPISYTENSVLTYITEQNREEGPWSIVKQVGVGIQKPTLVQI
SQ  GKDRFDTRLIRNLIFITNIQRLLRLRLNLELSQFRNVLVSPDHIINPSITEYGFSITGPSETFSDKQYDSDIRIL
//
ID  P0CA01;
PN  p5;
GN  Ken;
OS  561445;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp220]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000250|UniProtKB:Q08358}. [p34]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Localizes to the viral factory at 16 hpi. In the virion, located in the core shell, which functions like a matrix between the DNA- containing nucleoid and the inner envelope. {ECO:0000250|UniProtKB:Q08358}. [p14]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. {ECO:0000250|UniProtKB:Q08358}. [p37]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Host nucleus {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA- containing nucleoid and the inner envelope. {ECO:0000250|UniProtKB:Q08358}. [p150]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. {ECO:0000250|UniProtKB:Q08358}. [p5]: Virion {ECO:0000250|UniProtKB:Q08358}.
DR  UNIPROT: P0CA01;
DE  Function: [Polyprotein pp220]: Essential for the core assembly. Its myristoyl moiety may function as a membrane-anchoring signal to bind the developing core shell to the inner viral envelope. {ECO:0000250|UniProtKB:Q08358}. [p34]: The structural protein p34 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p14]: The structural protein p14 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p37]: The structural protein p37 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p150]: The structural protein p150 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}.
DE  Reference Proteome: No;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044423;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q08358};
SQ  MGNRGSSTSSRPPLSSEANLYAKLQDHIQRQTRPFSGGGYFNGGGDKNPVQHIKDYHIDSVSSKAKLRIIEGIIKAISKI
SQ  GFKVDTKQPIEDILKDIKKQLPDPRAGSTFVKNAEKQETICKMIADAINQEFIDLGQDKLIDTTEGAASICRQIVLYINS
SQ  LTHGLRAEYLDVHGSIENTLENIKLLSDAIKQLHERMVTEVTKAAPNEEVINAVTMIEAVYRRLLNEQNLQINILTNFID
SQ  NILTPTQKELDKLKTDEVDIIKILNDTNSVLGTKNFGKVLSYTLCNLGIAATVANKINKALQRVGLKVEQYLHSKNWAEF
SQ  DKELDLKRFSGLVSAENIAEFEKAVNLLRQTFNERHKILENNCAKKGGDGEKTPLDKRMEAQRLDRKHILMEFLNKSTQA
SQ  YNDFLENVKKIGMKLVKEIALTPNITKLRDALSRINDMGTIALDLSLIGFYNNAAAREERETFLIQLTLVKNVLEELAKT
SQ  DPNFKNLYDSCFRLLQIIDFYTDIVQKKYGGGEDCECTKVGGAALTVEELGLSKAARSQVDLNQAINTFMYYYYVAQIYS
SQ  NLTHNKQEFQSYEENYATILGDAIAGRLMQLDTEKNARINSPAVDLARGHVGPNPGGAQEVDWKATISAIELEYDVKRRF
SQ  YRALEGLDLYLKNITKTFVNNIDSIQTVQQMLDGVRIIGRWFTEATGDTLAQVFESFPTSAGNDSNVFTDNAPAGHYYEK
SQ  VAAEIQQGRGVGTLRPVRASQAKNIRDLIGRSLSNFQALKNIINAFARIGDMLGGEELRQTVPMSPLQIYKTLLEYIQHS
SQ  ALSVGLKNLNQTQIGGQRVALAQTAEEASQRVYLSTVRVNDALSTRWETEDVFFTFMLKSMAAKIFIVLGIYDMFERPEP
SQ  VYKLIPTRMILGGADELEPEVIPEAAGLYFRLPRLAEFYQKLFSFRDENVQISMLPELEGIFSGLIRVIFMRPIELINIG
SQ  DYSETEIRQLIKEINVIYQHFNLEYGEQEAVKKALIHFVNEINRRFGVITRTEWEKFQRIVQEARTMNDFGMMNQTNYSI
SQ  LPDEDGYTQSSQLLPSDRFIGPSSQPTPKWRPALYNIDSVDVQTGMLQPNSQWDLVQKFRKQLSEMFEDPSLQQELGKVS
SQ  YQELIQQATNELKKEHTDKIQIVSKLIQGSESLADTDVNKIFLFHETVITGLNLLSAIYVLLNTFRNNIKALDLDTIQKS
SQ  IIEWLRETQAANVNRANLIDWLGRRHGDISEIRNPGLVIKANDARLSEVYPDPTTDATAPLDRNLVTETLFAWFTRFVGI
SQ  PADGAVRPEQELAARYLVDNQRIMQLLLTNIFEMTSSFNKLVQVRFPETSTAHVHLDFTGLISLIDSLMADTKYFLDLLR
SQ  PHIDKNIIQYYENRSNPGSFYWLEEHLIDKLIKPPTDAGGRPLPGGELGLEGVNQIINKTYILLTKPYNVLQLRGGAQRG
SQ  NAANIQINNNPEFSERYEQYGRVFSRLVFYDALIENSGLRVEQVALGDFRLSNLIRTNNAQEENALSFWTAVAPRAYANV
SQ  NDAANNLRRYRLYGSDYGIRNNRSMMMVFNQLVASYIARFYDAPSGKIYLNLINTFANGNFSQAVMELGYAHPDLARDNT
SQ  AFGHRGDPTEQSVLLLSLGLMLQRLIKDTNRQGLSQHLISTLTEIPIYLKENYRANLPLFNKMFNILISQGELLKQFIQY
SQ  TKVQLARPNLTALLGANNDSIIYYNNNNVPNTGLTVGQAALRGIGSVFRPDITLMPLGNAQNNTNDVVRKRLIAVINGII
SQ  RGSLTLANSAMEVLHELTDHPIYFETEEHFIQNYMSRYNKEPLMPFSLSLYYLRDLRIENNEVYDPLLYPNLESGSPEFK
SQ  ILYGTRKLLGNDPVQLSDMPGVQLIMKNYNETVVAREQITPTRFEHFYIHAIQALRFIINIRSFKTVMTYNENTFGGVNL
SQ  IGEDRDDKPIITEGIGMNAVYSLRKTLQDVISFVESSYQEEQINNIHKIVSPRSQTRSLGSNRERERIFNLFDMNIMPIN
SQ  VNALMRSIPLANIYNYDYSFEEIACLMYGISAEKVRSLDTAAPQPDVAQVLNIPNRPPMNTREFMLKLLINPYVTVSITQ
SQ  YGNELLFRGNAGYMSRIFRGDNALNMGRPKFLSDQIFNKVLFGSLYPTQFDYDEAGPGLAAGIQRGREQWGQPLSDYINQ
SQ  ALHELVRTIRIIPQNIRVLRNIMVKNQLIADLAAIREQLVRMRREVENMVQTPEIQNNPTPEVIAAAQTWTQQYRARVDF
SQ  LINFIGNAQQPNSLIQLIQNITPLTVRAQLTTVFIRHGLPVPDPDQALQTDDEATQWFMTNIINQPITMIIPFTDLADDL
SQ  RIFLETMERYVFNVPRWLGPSTGRVARVPVNMAPGNIRYRTSYTENNVLTYIAEQNQEEGPWSIVKQVGVGIQKPALIQI
SQ  GKDRFDTRLIRNLIFITNIQRLLRLRLNLELSQFRNVLVSPNHIINPSITEYGFSITGPSETFSDKQYDSDIRIL
//
ID  P0CA02;
PN  p5;
GN  Mal;
OS  10500;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp220]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000250|UniProtKB:Q08358}. [p34]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly (By similarity). In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope (By similarity). {ECO:0000250|UniProtKB:Q08358}. [p14]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. {ECO:0000250|UniProtKB:Q08358}. [p37]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Host nucleus {ECO:0000250|UniProtKB:Q08358}. Note=Nuclear at early stages of infection. Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. {ECO:0000250|UniProtKB:Q08358}. [p150]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. {ECO:0000250|UniProtKB:Q08358}. [p5]: Virion {ECO:0000250|UniProtKB:Q08358}.
DR  UNIPROT: P0CA02;
DE  Function: [Polyprotein pp220]: Essential for the core assembly. Its myristoyl moiety may function as a membrane-anchoring signal to bind the developing core shell to the inner viral envelope. {ECO:0000250|UniProtKB:Q08358}. [p34]: The structural protein p34 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p14]: The structural protein p14 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p37]: The structural protein p37 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p150]: The structural protein p150 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}.
DE  Reference Proteome: No;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044423;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q08358};
SQ  MGNRGSSTSSRPPLSSEANIYAKLQDHIQRQTRPFSGGGYFNGGGDKNPVQHIKDYHIDSVSSKAKLRIIEGIIKAISKI
SQ  GFKIDTKQPIEDILKDIKKQLPDPRAGSTFVKNAEKQETVCKMIADAINQEFIDLGQDKLIDTTEGAASICRQIVLYINS
SQ  LTHGLRAEYLDVHGSIENTLENIKLLNDAIKQLHERMVTEVTKAAPNEEVINAVTMIEAVYRRLLNEQNLQISILTNFID
SQ  NILTPTQKELDKLQTDEVDIIKLLNDTNSVLGTKNFGKVLSYTLCNLGIAASVANKINKALQRVGLKVEQYLQSKNWAEF
SQ  DKELDLKRFSGLVSAENIAEFEKAVNLLRQTFNERHKILENNCAKKGGDEVKTPLDKRIEAQRLDRKHILMEFLNKSTQA
SQ  YNDFLENVKKIGIKLVKEIALTPNITRLRDALSRINDMGTIALDLSLIGFYTNAAAREERETFLTQLTLVKNVLEEISKT
SQ  DPNFKNLYDSCFRLLQIIDFYTDIVQKKYGGGEDCECTRVGGAALTVEELGLSKAARSQVDLNQAINTFMYYYYVAQIYS
SQ  NLTHNKQEFQSYEENYATILGDAIAGRLMQLDTEKNARINSPAVDLARGHVGPNPGGAQEVDWKAAVSAIELEYDVKRRF
SQ  YRALEGLDLYLKNITKTFVNNIDSIQTVQQMLDGVRIIGRWFTEATGDTLAQVFESFPTSAGNDSNVFTDNAPAGHYYEK
SQ  VAAEIQQGRSVGTLRPVRASQAKNIRDLIGRSLSNFQALKNIINAFARIGDMLGGEELRQMVPMSPLQIYKTLLEYLQHS
SQ  ALSVGLKNLNQSEIGGQRMALAQTAEEAAQRVYLSTVRVNDALSSRWETEDMFFTFMLKSMAAKIFIVLGIYDMFERPEP
SQ  VYKLIPTRMILGGADELEPEVIPEAAELYFRLPRLAEFYQKLFSFRDGNVQISMLPELEGIFSGLIRIIFMRPIELINIG
SQ  DYSETEIRQLIKEINVIYQHFNLEYGEQEATKKALIHFVNEINRRFGVITRTEWEKFQRIVQEARTMNDFGMMNQTNYSI
SQ  LPDEDGYTQSSQLLPSDRFIGPSSQPTPKWRPALYNIDSVDVQTGMLQPNSQWDLVQKFRKQLSEMFEDPSLQQELGKIS
SQ  YQELIRQAINELKKEHTDKIQIVSKLIQGSESLADTDVNKIFLFHETVITGLNLLSAIYVLLNNFRNNIKGLDLDTIQKS
SQ  IIEWLRETQPPDVNHANLLDWLGRKHGAISEIRNPGLVVKANNARLSEVYPDPTTDANTPQDRNLTTETLFAWIVQYVGI
SQ  PAGGGVRPEQELAARYLVDNQRIMQLLLTNIFEITSSFNKMIQVRFPETSTAHVHLDFTGLISLIDSLMADTKYFLDLLR
SQ  PHIDKNIIQYYENRSNPGSFYWLEEHLIDKLIKPPTDARGRPLPGGELGLEGVNQIINKTYTLLTKPYNVLQLRGGAQRR
SQ  DAANIQINNNPQSSERFEQYGRVFSKLVFYDALENNSGLRVEQVALGDFRLSNLIRTNNAQEENTLSYWDNIALRTYANV
SQ  NDAANNLRRYRLYGSDYGIQNNRSMMMVFNQLIASYITRFYDAPSGKIYLNLINAFANGNFSQAVMEMGYAHPDLARNNN
SQ  AFGHRGDPTEQSVLLLSLGLILQRLIKDTNRQGLSQHLISTLTEIPIYLKENYRANLPLFNKMFNILISQGELLKQFIQY
SQ  TNVQLARPNLTALLRANNDSVIYYNNNNVPMTGLSIGQAAMRGIGGVFRPNVTLMPLGDAQNNTSDIVRKRLVAVIDGII
SQ  RGSHTLADSAMEVLHELTDHPIYLETEEHFIQNYMSRYNKEPLMPFSLSLYYLRDLRIENNEVYDPLLYPNLESGSPEFK
SQ  LLYGTRKLLGNDPVQLSDMPGVQLIMKNYNETVVAREQITPTRFEHFYTHAIQALRFIVNIRSFKTVMTYNENTFGGVNL
SQ  ISEDRNDKPIITAGIGMNAVYSLRKTLQDVISFVESSYQEEQINNIHKIVSPKGQTRTLGSNRERERIFNLFDMNIIPIN
SQ  VNALMRSIPLANIYNYDYSFEEIACLMYGISAEKVRSLNTAAPQPDVAEVLNIPNRPPINTREFMLKLLINPYVSVSITQ
SQ  YGNELLSKGNAGYMSRIFRGDNALNMGRPKFLSDQIFNKVLFGSLYPTQFDYDEAGPSLAAGIQRGRERWGHPMSIYINQ
SQ  ALHEIVRTIRLAETVRGLRNVIDRNQIIGELNAFRTQLEDTLREVNNLVQTPEIQNNPTPEIIAAVQNWGQQYRAQITDL
SQ  IDLIGNAGQANSMISLIQNINVQTAGAQLTALFNRRGLPAPPPRQVLQNDIEAIQWFMTIVINHPPILIAPFMLLVNNLK
SQ  EFLNTLERYVYKTPRWLGPGTARIAQPPVGMAPGINMRHHTSYTENSVLTYITEQNREEGPWSIVKQVGVGIQKPTLVQI
SQ  GKDRFDTRLIRNLIFITNVQRLLRLRLNLELSQFRNVLVSPDHIINPSITEYGFSITGPSETFSDKQYDSDIRIL
//
ID  P0CA03;
PN  p5;
GN  Pret;
OS  561443;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp220]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000250|UniProtKB:Q08358}. [p34]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly (By similarity). In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope (By similarity). {ECO:0000250|UniProtKB:Q08358}. [p14]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. {ECO:0000250|UniProtKB:Q08358}. [p37]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Host nucleus {ECO:0000250|UniProtKB:Q08358}. Note=Nuclear at early stages of infection. Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. {ECO:0000250|UniProtKB:Q08358}. [p150]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope. {ECO:0000250|UniProtKB:Q08358}. [p5]: Virion {ECO:0000250|UniProtKB:Q08358}.
DR  UNIPROT: P0CA03;
DE  Function: [Polyprotein pp220]: Essential for the core assembly. Its myristoyl moiety may function as a membrane-anchoring signal to bind the developing core shell to the inner viral envelope. {ECO:0000250|UniProtKB:Q08358}. [p34]: The structural protein p34 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p14]: The structural protein p14 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p37]: The structural protein p37 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p150]: The structural protein p150 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}.
DE  Reference Proteome: No;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044423;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q08358};
SQ  MGNRGSSTSSRPPPSSEANIYAKLQDHIQRQTRPFSGGGYFNGGGDKNPVQHIKDYHIDSVSSKAKLRIIEGIIRAIAKI
SQ  GFKVDTKQPIEDILKDIKKQLPDPRAGSTFVKNAEKQETVCKMIADAINQEFIDLGQDKLIDTTEGAASICRQIVLYINS
SQ  LTHGLRAEYLDVHGSIENTLENIKLLNDAIKQLHERMVTEVTKAAPNEEVINAVTMIEAVYRRLLNEQNLQINILTNFID
SQ  NILTPTQKELDKLQTDEVDIIKLLNDTNSVLGTKNFGKVLSYTLCNLGIAASVANKINKALQKVGLKVEQYLQSKNWEEF
SQ  DKELDLKRFSGLVSAENIAEFEKAVNLLRQTFNERHKILENSCAKKGGDEEKTPLDRRIEAQRLDRKHILMEFLNKSTQA
SQ  YNDFLENVKKIGIKLVKEIALTPNITRLRDALSRINDMGTIALDLSLIGFYTNAAAREERETFLTQFMLVKNVLEEQSKT
SQ  DPNFKNLYDSCSRLLQIIDFYTDIVQKKYGGEEDCECTRVGGAALTVEELGLSKAARSQVDLNQAINTFMYYYYVAQIYS
SQ  NLTHNKQEFQSYEENYATILGDAIAGRLMQLDTEKNARINSPAVDLARGHVGPNPGGAQEVDWKAAVSAIELEYDVKRRF
SQ  YRALEGLDLYLKNITKTFVNNIDSIQTVQQMLDGVRIIGRWFTEATGDTLAQVFESFPTSAGNDSNVFTDNAPAGHYYEK
SQ  VAAEIQQGRSVGTLRPVRASQAKNIRDLIGRSLSNFQALKNIINAFARIGDMLGGEELRQMVPMSPLQIYKTLLEYIQHS
SQ  ALSVGLKNLNQSEIGGQRVALARTPEEAAQRVYLSTVRVNDALSTRWETEDVFFTFMLKSMAAKIFIVLGIYDMFERPEP
SQ  VYKLIPTRMILGGADELEPEVIPEAAELYFRLPRLAEFYQKLFSFRDENVQISMLPELEGIFSGLIRIIFMRPIELINIG
SQ  DYSETEIRQLIKEINVIYQHFNLEYGEQEATKKALIHFVNEINRRFGVITRTEWEKFQRIVQEARTMNDFGMMNQTNYSI
SQ  LPDEDGYTQSSQLLPSDRFISPSSQPTPKWRPALYNIDSVDVQTGMLQPNSQWDLVQKFRKQLSEMFEDPSLQQELGKVS
SQ  YQELIRQAINELKKDHTDKIQIVSKLIQGSESLADTDVNKIFLFHETVITGLNLLSAIYVLLNNFRNNIKGLDLDTIQKS
SQ  IIEWLRETPANVNHANLIDWLGRKHGAISEIRNPGLVIKEINMRLSEVYPDPTTEANVPQDRNLTTETLFAWIVPYVGIP
SQ  AGGGVRAEQELAARYLVDNQRIMQLLLTNIFEMTSSFNKMVQVRFPETSTAQVHLDFTGLISLIDSLMADTKYFLNLLRP
SQ  HIDKNIIQYYENRSNPGSFYWLEEHLIDKLIKPPTDAGGRPLPGGELGLEGVNQIINKTYTLLTKPYNVLQLRGGAQRRD
SQ  AANIQINNNPQPSERFEQYGRVFSRLVFYDALENNSGLRVEQVVLGDFRLSNLIRTNNAQEENALSYWDNIALRTYANVN
SQ  DAANNLRRYRLYGSDHGIQNNRSMMMVFNQLVASYIARFYDAPSGKIYLNLINAFANGNFSQAVMEMGYAHPDLARNNNA
SQ  FGHRGDPTEQSVLLLSLGLILQRLIKDTNRQGLSQHLISTLTEIPIYLKENYRANLPLFNKMFNILISQGELLKQFIQYT
SQ  NVQLARPNLTALLGANNDSVIYYNNNINVPMTGLSVGQAAMRGIGGVFRPNVTLMPLGDAQSNTSDIVRKRLVAVIDGII
SQ  RGSHTLADSAMEVLHELTDHPIYLETEEHFIQNYMSRYNKEPLMPFSLSLYYLRDLRIENNEVYDPLLYPNLESGSPEFK
SQ  LLYGTRKLLGNDPVQLSDMPGVQLIMKNYNETVVAREQITPTRFEHFYTHAIQALRFIINIRSFKTVMMYNENTFGGVNL
SQ  ISENRDDKPIITAGIGMNAVYSLRKTLQDVISFVESSYQEEQINHIHKIVSPKGQTRTLGSNRERERIFNLFDMNIIPIN
SQ  VNALMRSIPLANIYNYDYSFEEIACLMYGISAEKVRSLNTAAPQPDIAEVLNIPNRPPMNTREFMLKLLINPYVSVSITQ
SQ  YGNELLSKGNAGYMSRIFRGDNALNMGRPKFLSDQIFNKVLFGSLYPTQFDYDEAGPSLAAGIQRGRERWGHPMSIYINQ
SQ  ALHEIVRTIRLAETVRGLRNVIDRNQIIGELNAFRTQLEDTRREVNNLIQTPEIRNNPTPEIIAAVQNWGQQYRGQITDL
SQ  IDLIGNVGQANSMINLIQNITPQTAGAQLIALFNIRGLPAPPPRQVIQNDIEAMQWFMTMVINHPPILIAPFMLLVNNLK
SQ  EFLNTLERYVYKTPRWLGPGTARIAQPPVGMAPGINMRHHTSYTENSVLTYITEQNREEGPWSIVKQVGVGIQKPTLVQI
SQ  GKDRFDTRLIRNLIFITNIQRLLRLRLNLELSQFRNVLVSPDHIINPSITEYGFSITGPSETFSDKQYDSDIRIL
//
ID  P0CA04;
PN  p5;
GN  War;
OS  561444;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp220]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000250|UniProtKB:Q08358}. [p34]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Localizes to the viral factory at 16 hpi (By similarity). In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope (By similarity). {ECO:0000250|UniProtKB:Q08358}. [p14]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA- containing nucleoid and the inner envelope (By similarity). {ECO:0000250|UniProtKB:Q08358}. [p37]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Host nucleus {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA- containing nucleoid and the inner envelope (By similarity). {ECO:0000250|UniProtKB:Q08358}. [p150]: Virion {ECO:0000250|UniProtKB:Q08358}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q08358}. Note=Found in perinuclear cytoplasmic viral factories during assembly. In the virion, located in the core shell, which functions like a matrix between the DNA-containing nucleoid and the inner envelope (By similarity). {ECO:0000250|UniProtKB:Q08358}. [p5]: Virion {ECO:0000250|UniProtKB:Q08358}.
DR  UNIPROT: P0CA04;
DE  Function: [Polyprotein pp220]: Essential for the core assembly. Its myristoyl moiety may function as a membrane-anchoring signal to bind the developing core shell to the inner viral envelope. {ECO:0000250|UniProtKB:Q08358}. [p34]: The structural protein p34 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p14]: The structural protein p14 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p37]: The structural protein p37 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}. [p150]: The structural protein p150 is a component of the virus core shell. {ECO:0000250|UniProtKB:Q08358}.
DE  Reference Proteome: No;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044423;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGNRGSSTSSRPPPSSEANIYAKLQDHIQRQTRPFSGGGYFNGGGDKNPVQHIKDYHIDSVSSKAKLRIIEGIIRAIAKI
SQ  GFKVDTKQPIEDILKDIKKQLPDPRAGSTFVKNAEKQETVCKMIADAINQEFIDLGQDKLIDTTEGAASICRQIVLYINS
SQ  LTHGLRAEYLDVHGSIENTLENIKLLNDAIKQLHERMVTEVTKAAPNEEVINAVTMIEAVYRRLLNEQNLQINILTNFID
SQ  NILTPTQKELDKLQTDEVDIIKLLNDTNSVLGTKNFGKVLSYTLCNLGIAASVANKINKALQKVGLKVEQYLQSKNWAEF
SQ  DKELDLKRFSGLVSAENIAEFEKAVNLLRQTFNERHKILENSCAKKGGDEEKTPLDRRIEAQRLDRKHILMEFLNKSTQA
SQ  YNDFLENVKKIGIKLVKEIALTPNITRLRDALSRINDMGTIALDLSLIGFYTNAAAREERETFLTQFMLVKNVLEEQSKI
SQ  DPNFKNLYDSCSRLLQIIDFYTDIVQKKYGGGEDCECTRVGGAALTVEELGLSKAARSQVDLNQAINTFMYYYYVAQIYS
SQ  NLTHNKQEFQSYEENYATILGDAIAGRLMQLDTEKNARINSPAVDLARGHVGPNPGGAQEEDWKATVSAIELEYDVKRRF
SQ  YRALEGLDLYLKNITKTFVNNIDSIQTVQQMLDGVRIIGRWFTEATGDTLAQVFESFPTSAGNDSNVFTDNAPAGHYYEK
SQ  VAAEIQQGRSVGTLRPVRASQAKNIRDLIGRSLSNFQALKNIINAFARIGDMLGGEELRQMVPMSPLQIYKTLLEYIQHS
SQ  ALSVGLKNLNQSEIGGQRVALARTPEEAAQRVYLSTVRVNDALSTRWETEDVFFTFMLKSMAAKIFIVLGIYDMFERPEP
SQ  VYKLIPTRMILGGADELEPEVIPEAAELYFRLPRLAEFYQKLFSFRDENVQISMLPELEGIFSGLIRIIFMRPIELINIG
SQ  DYSETEIRQLIKEINVIYQHFNLEYGEQEATKKALIHFVNEINRRFGVITRTEWEKFQRIVQEARTMNDFGMMNQTNYSI
SQ  LPDEDGYTQSSQLLPSDRFISPSSQPTPKWRPALYNIDSVDVQTGMLQPNSQWDLVQKFRKQLSEMFEDPSLQQELGKVS
SQ  YQELIRQAINELKKDHTDKIQIVSKLIQGSESLADTDVNKIFLFHETVITGLNLLSAIYVLLNNFRNNIKGLDLDTIQKS
SQ  IIEWLRETQAANVNHANLIDWLGRKHGAISEIRNPGLVVKENDARLSRVYPDPTTNATAPQDQNLVTETLFAWIVPYVGI
SQ  PAGGGVRAEQELAARYLVDNQRIMQLLLTNIFEMTSSFNKMVQVRFPETSTAQVHLDFTGLISLIDSLMADTKYFLNLLR
SQ  PHIDKNIIQYYENRSNPGSFYWLEEHLIDKLIKPPTDAGGRPLPGGELGLEGVNQIINKTYTLLTKPYNVLQLQGGAQRR
SQ  DAANIQINNNPQPSERFEQYGRVFSRLVFYDALENNSGLRVEQVVLGDFRLSNLIRTNNAQEENALSYWDNIALRTYANV
SQ  NDAANNLRRYRLYGSDHGIQNNRSMMMVFNQLVASYIARFYDAPSGKIYLNLINAFANGNFSQAVMEMGYAHPDLARNNN
SQ  AFGHRGDPTEQSVLLLSLGLILQRLIKDTNRQGLSQHLISTLTEIPIYLKENYRANLPLFNKMFNILISQGELLKQFIQY
SQ  TNVQLARPNLMGLLGANNDSIIYYNNNNVPTTGLSVGQAALRGIGGVFRPNVTLMPLGDAQNNTSDIVRKRLVAVIDGII
SQ  RGSHTLADSAMEVLHELTDHPIYLETEEHFIQNYMSRYNKEPLMPFSLSLYYLRDLRIENNEVYDPLLYPNLESGSPEFK
SQ  LLYGTRKLLGNDPVQLSDMPGVQLIMKNYNETVVAREQITPTRFEHFYTHAIQALRFIINIRSFKTVMMYNENTFGGVNL
SQ  ISENRDDKPIITAGIGMNAVYSLRKTLQDVISFVESSYQEEQINHIHKIVSPKGQTRTLGSNRERERIFNLFDMNIIPIN
SQ  VNALMRSIPLANIYNYDYSFEEIACLMYGISAEKVRSLDTTAPQPDVAEVLNIPNRPPINTREFMLKLLINPYVSVSITQ
SQ  YGNELLSKGNAGYMSRIFRGDNALNMGRPKFLSDQIFNKVLFGSLYPTQFDYDEAGPGLAAGIQRGRERWGHPMSIYINQ
SQ  ALHEIVRTIRLAETVRGLRNVIDRNQIIGELNAFRTQLEDTRREVNNLIQTPEIQNNPTPEIIAAIQNWVQQYRGQITNL
SQ  IDLIGNAGQANSMINLIQNITPQTAGAQLTALFNIRGLPAPPPRQPLQNDIEAMQWFMTIVINHPPILIAPFMLLVNNLK
SQ  EFLNTLERYVYKTPRWLGPGTARIAQPPVGMAPGINMRHHTSYTENSVLTYITEQNREEGPWSIVKQVGVGIQKPTLVHI
SQ  GKDRFDTRLIRNLIFITNIQRLLRLRLNLELSQFRNVLVSPDHIINPSITEYGFSITGPSETFSDKQYDSDIRIL
//
ID  Q65179;
PN  p8;
GN  CP530R;
OS  10498;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp62]: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:9223468}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000269|PubMed:9223468}. [p35]: Virion {ECO:0000269|PubMed:30185597, ECO:0000269|PubMed:33629764}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000269|PubMed:33629764}. [p15]: Virion {ECO:0000269|PubMed:30185597, ECO:0000269|PubMed:33629764}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000269|PubMed:33629764}. [p8]: Virion {ECO:0000269|PubMed:30185597}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000303|PubMed:30185597}.
DR  UNIPROT: Q65179;
DR  UNIPROT: Q86851;
DR  PDB: 6LNL;
DR  PDB: 6NLN;
DR  PDB: 7BQ9;
DR  PDB: 7BQA;
DR  PDB: 7CP2;
DE  Function: [Polyprotein pp62]: Essential for the correct assembly and maturation of the core of the virion. {ECO:0000269|PubMed:19846532}. [p35]: Component of the core shell (PubMed:30185597). Binds to phosphatidylserine, which may enable the core shell binding with the inner membrane (PubMed:32519301). {ECO:0000269|PubMed:30185597, ECO:0000269|PubMed:32519301}. [p15]: Component of the core shell (PubMed:30185597). Binds to phosphatidylserine and DNA, which may link the core shell to the inner membrane and to the viral nucleoid (PubMed:32451720). {ECO:0000269|PubMed:30185597, ECO:0000269|PubMed:32451720}. [p8]: Component of the core shell. {ECO:0000269|PubMed:30185597}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0044423;
GO  GO:0019069;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSNMKQFCKISVWLQQHDPDLLEIINNLCMLGNLSAAKYKHGVTFIYPKQAKIRDEIKKHAYSNDPSQAIKTLESLILP
SQ  FYIPTPAEFTGEIGSYTGVKLEVEKTEANKVILKNGEAVLVPAADFKPFPDRRLAVWIMESGSMPLEGPPYKRKKEGGGN
SQ  DPPVPKHISPYTPRTRIAIEVEKAFDDCMRQNWCSVNNPYLAKSVSLLSFLSLNHPTEFIKVLPLIDFDPLVTFYLLLEP
SQ  YKTHGDDFLIPETILFGPTGWNGTDLYQSAMLEFKKFFTQITRQTFMDIADSATKEVDVPICYSDPETVHSYTNHVRTEI
SQ  LHHNAVNKVTTPNLVVQAYNELEQTNTIRHYGPIFPESTINALRFWKKLWQDEQRFVIHGLHRTLMDQPTYETSEFAEIV
SQ  RNLRFSRPGNNYINELNITSPAMYGDKHTTGDIAPNDRFAMLVAFINSTDFLYTAIPEEKVGGNETQTSSLTDLVPTRLH
SQ  SFLNHNLSKLKILNRAQQTVRNILSNDCLNQLKHYVKHTGKNEILKLLQE
//
ID  P0CA05;
PN  p8;
GN  Ken;
OS  561445;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp62]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q65179}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000250|UniProtKB:Q65179}. [p35]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}. [p15]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}.
DR  UNIPROT: P0CA05;
DE  Function: [Polyprotein pp62]: Essential for the correct assembly and maturation of the core of the virion. {ECO:0000250|UniProtKB:Q65179}. [p35]: Component of the core shell (By similarity). Binds to phosphatidylserine, which may enable the core shell binding with the inner membrane (By similarity). {ECO:0000250|UniProtKB:Q65179}. [p15]: Component of the core shell (By similarity). Binds to phosphatidylserine and DNA, which may link the core shell to the inner membrane and to the viral nucleoid (By similarity). {ECO:0000250|UniProtKB:Q65179}. [p8]: Component of the core shell. {ECO:0000250|UniProtKB:Q65179}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0044423;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSNMKQFCKISVWLQQHDPDLLEIINNLCMLGNLSAAKYKHGVTFIYPKQAKIRDEIKKHAYSNDPSQAIKTLESLILP
SQ  FYIPTPMEFTGEIGSYTGVKLEVEKKEANKVILKNGEAVLIPAADFKPFPDRRLAVWIMESGSMPLEGPPYKRKKEGGGN
SQ  DPPVSKHISPYTPRTRIAIEVEKAFDECMRQNWCSVNNPYLAKSVSLLSFLSLNHPTEFIKVLPLIDFDPLVTFYLLLEP
SQ  YKTHGDDFLIPETILFGPTGWNGTDLYQSAMLEFKKFFTQITRQTFMDIADTATKEVDVPICYSDPETVHSYANHVRTEI
SQ  LHHNMVNKVTTPNLVVQAYNELEQTNTIRHYGPIFPESTINALRFWKKLWQDEQRFVIHGLHRTLMDQPTYETSEFAEIV
SQ  RNLRFSRPGNNYINELNITSPAMYGDKHTTGDIAPNDRFAMLVAFINSTDFLYTAIPEEKVGGNDTQTGSQTSSLTDLVP
SQ  TRLHSFLNHNLSKLKILNRAQQTVKNILSNDCLNQLKHYVKHTGKNEILKLLQE
//
ID  P0CA06;
PN  p8;
GN  Mal;
OS  10500;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp62]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q65179}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000250|UniProtKB:Q65179}. [p35]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}. [p15]: Virion {ECO:0000269|PubMed:7853518}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}. [p8]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}.
DR  UNIPROT: P0CA06;
DE  Function: [Polyprotein pp62]: Essential for the correct assembly and maturation of the core of the virion. {ECO:0000250|UniProtKB:Q65179}. [p35]: Component of the core shell (By similarity). Binds to phosphatidylserine, which may enable the core shell binding with the inner membrane (By similarity). {ECO:0000250|UniProtKB:Q65179}. [p15]: Component of the core shell (By similarity). Binds to phosphatidylserine and DNA, which may link the core shell to the inner membrane and to the viral nucleoid (By similarity). {ECO:0000250|UniProtKB:Q65179}. [p8]: Component of the core shell. {ECO:0000250|UniProtKB:Q65179}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0044423;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSNMKQFCKISVWLQQHDPDLLEIINNLCMLGNLSAAKYKHGVTFIYPKQAKIRDEIKKHAYSNDPSQAIKTLESLILP
SQ  FYIPTPAEFTGEIGSYTGVKLEVEKTEANKVILKNGEAVLIPAADFKPFPDRRLAVWIMESGSMPLEGPPYKRKKEGGGN
SQ  DPPVPKHISPYTPRTRIAIEVEKAFDDCMRQNWCSVNNPYLAKSVSLLSFLSLNHPTEFIKVLPLIDFDPLVTFYLLLEP
SQ  YKTHGDDFLIPETVLFGPTGWNGTDLYQSAMLEFKKFFTQITRQTFMDIADTATKEVDVPICYSDPETVHSYANHVRTEI
SQ  LHHNMVNKVTTPNLVVQAYNELEQTNTIRHYGPIFPESTINALRFWKKLWQDEQRFVIHGLHRTLMDQPTYETSEFAEIV
SQ  RNLRFSRPGNNYINELNITSPAMYGDKHTTGDIAPNDRFAMLVAFINSTDFLYTAIPEEKVGGNDTQTSSLTDLVPTRLH
SQ  SFLNHNLSKLKILNRAQQTVRNILSNDCLNQLKHYVKHTGKNEILKLLQD
//
ID  P0CA07;
PN  p8;
GN  Pret;
OS  561443;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp62]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q65179}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000250|UniProtKB:Q65179}. [p35]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}. [p15]: Virion {ECO:0000250|UniProtKB:P0CA06}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}. [p8]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}.
DR  UNIPROT: P0CA07;
DE  Function: [Polyprotein pp62]: Essential for the correct assembly and maturation of the core of the virion. {ECO:0000250|UniProtKB:Q65179}. [p35]: Component of the core shell (By similarity). Binds to phosphatidylserine, which may enable the core shell binding with the inner membrane (By similarity). {ECO:0000250|UniProtKB:Q65179}. [p15]: Component of the core shell (By similarity). Binds to phosphatidylserine and DNA, which may link the core shell to the inner membrane and to the viral nucleoid (By similarity). {ECO:0000250|UniProtKB:Q65179}. [p8]: Component of the core shell. {ECO:0000250|UniProtKB:Q65179}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0044423;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSNMKQFCKISVWLQQHDPDLLEIINNLCMLGNLSAAKYKHGVTFIYPKQAKIRDEIKKHAYSNDPSQAIKTLESLILP
SQ  FYIPTPAEFTGEIGSYTGVKLEVEKTEANKVILKNGEAVLVPAADFKPFPDRRLAVWIMESGSMPLEGPPYKRKKEGGGN
SQ  DPPVPKHISPYTPRTRIAIEVEKAFDDCMRQNWCSVNNPYLAKSVSLLSFLSLNHPTEFIKVLPLIDFDPLVTFYLLLEP
SQ  YKTHGDDFLIPETILFGPTGWNGTDLYQSAMLEFKKFFTQITRQTFMDIADSATKEVDVPICYSDPETVHSYTNHVRTEI
SQ  LHHNAVNKVTTPNLVVQAYNELEQTNTIRHYGPIFPESTINALRFWKKLWQDEQRFVIHGLHRTLMDQPTYETSEFAEIV
SQ  RNLRFSRPGNNYINELNITSPAMYGDKHTTGDIAPNDRFAMLVAFINSTDFLYTAIPEEKVGGNETQTSSLTDLVPTRLH
SQ  SFLNHNLSKLKILNRAQQTVRNILSNDCLNQLKHYVKHTGKNEILKILQE
//
ID  P0CA08;
PN  p8;
GN  War;
OS  561444;
SL  Nucleus Position: SL-0382;
SL  Comments: [Polyprotein pp62]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q65179}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000250|UniProtKB:Q65179}. [p35]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}. [p15]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}. [p8]: Virion {ECO:0000250|UniProtKB:Q65179}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000250|UniProtKB:Q65179}.
DR  UNIPROT: P0CA08;
DE  Function: [Polyprotein pp62]: Essential for the correct assembly and maturation of the core of the virion. {ECO:0000250|UniProtKB:Q65179}. [p35]: Component of the core shell (By similarity). Binds to phosphatidylserine, which may enable the core shell binding with the inner membrane (By similarity). {ECO:0000250|UniProtKB:Q65179}. [p15]: Component of the core shell (By similarity). Binds to phosphatidylserine and DNA, which may link the core shell to the inner membrane and to the viral nucleoid (By similarity). {ECO:0000250|UniProtKB:Q65179}. [p8]: Component of the core shell. {ECO:0000250|UniProtKB:Q65179}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0044423;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPSNMKQFCKISVWLQQHDPDLLEIINNLCMLGNLSAAKYKHGVTFIYPKQAKIRDEIKKHAYSNDPSQAIKTLESLILP
SQ  FYIPTPAEFTGEIGSYTGVKLEVEKTEANKVILKNGEAVLVPAADFKPFPDRRLAVWIMESGSMPLEGPPYKRKKEGGGN
SQ  DPPVPKHISPYTPRTRIAIEVEKAFDDCMRQNWCSVNNPYLAKSVSLLSFLSLNHPTEFIKVLPLIDFDPLVTFYLLLEP
SQ  YKTHGDDFLIPETILFGPTGWNGTDLYQSAMLEFKKFFTQITRQTFMDIADSATKEVDVPICYSDPETVHSYTNHVRTEI
SQ  LHHNAVNKVTTPNLVVQAYNELEQTNTIRHYGPIFPESTINALRFWKKLWQDEQRFVIHGLHRTLMDQPTYETSEFAEIV
SQ  RNLRFSRPGNNYINELNITSPAMYGDKHTTGDIAPNDRFAMLVAFINSTDFLYTAIPEEKVGGNETQTSSLTDLVPTRLH
SQ  SFLNHNLSKLKILNRAQQTVRNILSNDCLNQLKHYVKHTGKNEILKLLQE
//
ID  O43586;
PN  Proline-serine-threonine phosphatase-interacting protein 1;
GN  PSTPIP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:9857189}. Cell membrane {ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:9857189}; Peripheral membrane protein {ECO:0000269|PubMed:9857189}. Cell projection, uropodium {ECO:0000269|PubMed:18480402}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P97814}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P97814}. Cleavage furrow {ECO:0000250|UniProtKB:P97814}. Note=Mainly cytoplasmic in T-cells (PubMed:9857189). Colocalizes in cluster with CD2 near the cell surface membrane in activated T-cells (PubMed:9857189). In monocytes, forms a branched filamentous network in the cytoplasm (PubMed:19584923). In transfected cells, forms relatively straight filaments radiating out from the nucleus (PubMed:19584923). Filament formation requires an intact tubulin cytoskeleton (PubMed:19584923). In migrating neutrophils, colocalizes with PIP5K1C and DNM2 to the trailing edge of the uropod in a actin-dependent manner (PubMed:18480402). Colocalized with PTPN12 in the cytoplasm and the perinuclear region. During interphase, colocalizes with F-actin in the cortical cytoskeleton, lamellipodia, and stress fibers. In dividing cells, colocalizes with the F-actin rich cytokinetic cleavage furrow. Colocalized with CD2AP and WAS in the actin cytoskeleton within the cytoplasm. Colocalized with CD2, CD2AP and WAS at the site of T-cell:APC contact (By similarity). {ECO:0000250|UniProtKB:P97814, ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:9857189}.
DR  UNIPROT: O43586;
DR  UNIPROT: B5BU74;
DR  UNIPROT: B5BUK4;
DR  UNIPROT: O43585;
DR  UNIPROT: O95657;
DR  PDB: 2DIL;
DR  PDB: 7AAL;
DR  PDB: 7AAM;
DR  PDB: 7AAN;
DR  Pfam: PF00611;
DR  Pfam: PF14604;
DR  PROSITE: PS51741;
DR  PROSITE: PS50002;
DR  OMIM: 604416;
DR  OMIM: 606347;
DR  DisGeNET: 9051;
DE  Function: Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T- cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils. {ECO:0000250, ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:9857189}.
DE  Disease: PAPA syndrome (PAPAS) [MIM:604416]: Characterized by autosomal dominant inheritance of early-onset, primarily affecting skin and joint tissues. Recurring inflammatory episodes lead to accumulation of sterile, pyogenic, neutrophil-rich material within the affected joints, ultimately resulting in significant destruction. {ECO:0000269|PubMed:11971877, ECO:0000269|PubMed:14595024, ECO:0000269|PubMed:22161697}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P06729; IntAct: EBI-8661989; Score: 0.74
DE  Interaction: P18031; IntAct: EBI-8662139; Score: 0.40
DE  Interaction: Q05209; IntAct: EBI-7086193; Score: 0.78
DE  Interaction: P42768; IntAct: EBI-7086234; Score: 0.46
DE  Interaction: P35831; IntAct: EBI-7833624; Score: 0.40
DE  Interaction: Q53ZZ1; IntAct: EBI-7833641; Score: 0.56
DE  Interaction: Q15058; IntAct: EBI-1074843; Score: 0.00
DE  Interaction: Q9Y3U8; IntAct: EBI-1074867; Score: 0.00
DE  Interaction: Q75MH1; IntAct: EBI-1075090; Score: 0.00
DE  Interaction: Q7L1Q6; IntAct: EBI-1076117; Score: 0.00
DE  Interaction: Q8IZX4; IntAct: EBI-1076263; Score: 0.00
DE  Interaction: Q02543; IntAct: EBI-1076932; Score: 0.00
DE  Interaction: P83881; IntAct: EBI-1077069; Score: 0.00
DE  Interaction: Q9Y6E2; IntAct: EBI-1077189; Score: 0.00
DE  Interaction: P18077; IntAct: EBI-1077313; Score: 0.00
DE  Interaction: P37268; IntAct: EBI-1077329; Score: 0.00
DE  Interaction: P62899; IntAct: EBI-1077641; Score: 0.00
DE  Interaction: P39023; IntAct: EBI-1077784; Score: 0.00
DE  Interaction: Q76P68; IntAct: EBI-1077945; Score: 0.00
DE  Interaction: Q99996; IntAct: EBI-1078222; Score: 0.00
DE  Interaction: P15924; IntAct: EBI-1078302; Score: 0.00
DE  Interaction: P62910; IntAct: EBI-1079276; Score: 0.00
DE  Interaction: P31939; IntAct: EBI-1079436; Score: 0.00
DE  Interaction: Q9UMN6; IntAct: EBI-1080161; Score: 0.00
DE  Interaction: Q9UBS9; IntAct: EBI-1080330; Score: 0.00
DE  Interaction: Q9BVP2; IntAct: EBI-1080978; Score: 0.00
DE  Interaction: Q9UKX3; IntAct: EBI-1081139; Score: 0.00
DE  Interaction: P47914; IntAct: EBI-1081333; Score: 0.00
DE  Interaction: P46779; IntAct: EBI-1081646; Score: 0.00
DE  Interaction: Q9NR30; IntAct: EBI-1082024; Score: 0.00
DE  Interaction: P62750; IntAct: EBI-1083637; Score: 0.00
DE  Interaction: P61254; IntAct: EBI-1084016; Score: 0.00
DE  Interaction: Q9Y265; IntAct: EBI-1084371; Score: 0.00
DE  Interaction: Q9UJX6; IntAct: EBI-1084500; Score: 0.00
DE  Interaction: Q96LW2; IntAct: EBI-1085766; Score: 0.00
DE  Interaction: P49207; IntAct: EBI-1085840; Score: 0.00
DE  Interaction: P05408; IntAct: EBI-1085888; Score: 0.00
DE  Interaction: P42766; IntAct: EBI-1085896; Score: 0.00
DE  Interaction: P61513; IntAct: EBI-1085944; Score: 0.00
DE  Interaction: Q9H204; IntAct: EBI-6966600; Score: 0.40
DE  Interaction: P48023; IntAct: EBI-7908782; Score: 0.70
DE  Interaction: Q9ULH1; IntAct: EBI-8492005; Score: 0.44
DE  Interaction: Q96B02; IntAct: EBI-8652722; Score: 0.67
DE  Interaction: Q99952; IntAct: EBI-8674047; Score: 0.60
DE  Interaction: Q9Y2R2; IntAct: EBI-9635611; Score: 0.59
DE  Interaction: Q8WWY3; IntAct: EBI-10177198; Score: 0.81
DE  Interaction: O00560; IntAct: EBI-10179805; Score: 0.56
DE  Interaction: O43684; IntAct: EBI-10185162; Score: 0.56
DE  Interaction: O75386; IntAct: EBI-10188060; Score: 0.72
DE  Interaction: Q14D33; IntAct: EBI-10234854; Score: 0.72
DE  Interaction: Q86YD7; IntAct: EBI-10260742; Score: 0.72
DE  Interaction: Q96D16; IntAct: EBI-10284292; Score: 0.56
DE  Interaction: Q9H788; IntAct: EBI-10308355; Score: 0.56
DE  Interaction: Q9UQ90; IntAct: EBI-10324798; Score: 0.56
DE  Interaction: Q9Y228; IntAct: EBI-10325346; Score: 0.56
DE  Interaction: Q9Y473; IntAct: EBI-10328034; Score: 0.56
DE  Interaction: Q9Y4Z0; IntAct: EBI-10328518; Score: 0.72
DE  Interaction: Q9Y5E9; IntAct: EBI-10329011; Score: 0.72
DE  Interaction: Q9ULZ3; IntAct: EBI-10687267; Score: 0.35
DE  Interaction: X5D7R7; IntAct: EBI-21250457; Score: 0.37
DE  Interaction: X5DP17; IntAct: EBI-21250665; Score: 0.37
DE  Interaction: Q06630; IntAct: EBI-11535799; Score: 0.56
DE  Interaction: Q12446; IntAct: EBI-11537414; Score: 0.56
DE  Interaction: O15169; IntAct: EBI-16433147; Score: 0.56
DE  Interaction: P28702; IntAct: EBI-16433157; Score: 0.56
DE  Interaction: A0A0S2Z5X4; IntAct: EBI-16433167; Score: 0.56
DE  Interaction: Q15287; IntAct: EBI-24284068; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-24284949; Score: 0.56
DE  Interaction: P00540; IntAct: EBI-24284835; Score: 0.56
DE  Interaction: P17752; IntAct: EBI-24289405; Score: 0.56
DE  Interaction: O75031; IntAct: EBI-24292215; Score: 0.56
DE  Interaction: Q96GM5; IntAct: EBI-24293673; Score: 0.56
DE  Interaction: Q9BWG6; IntAct: EBI-24314943; Score: 0.56
DE  Interaction: Q8IX18; IntAct: EBI-24324802; Score: 0.56
DE  Interaction: Q03014; IntAct: EBI-24335840; Score: 0.56
DE  Interaction: Q53FD0; IntAct: EBI-24343226; Score: 0.56
DE  Interaction: Q9UK33; IntAct: EBI-25244547; Score: 0.56
DE  Interaction: Q09161; IntAct: EBI-25257106; Score: 0.56
DE  Interaction: Q9GZV7; IntAct: EBI-24487515; Score: 0.56
DE  Interaction: P0CG20; IntAct: EBI-24493428; Score: 0.56
DE  Interaction: Q14005; IntAct: EBI-24503632; Score: 0.56
DE  Interaction: P32969; IntAct: EBI-24399253; Score: 0.56
DE  Interaction: Q96GY3; IntAct: EBI-24405719; Score: 0.56
DE  Interaction: Q3SY00; IntAct: EBI-24420123; Score: 0.56
DE  Interaction: Q96T60; IntAct: EBI-24424643; Score: 0.56
DE  Interaction: Q08426; IntAct: EBI-24429413; Score: 0.56
DE  Interaction: Q96EZ8; IntAct: EBI-24473920; Score: 0.56
DE  Interaction: Q9H9D4; IntAct: EBI-24475818; Score: 0.56
DE  Interaction: Q63ZY3; IntAct: EBI-24476422; Score: 0.56
DE  Interaction: O43586; IntAct: EBI-14036224; Score: 0.59
DE  Interaction: O15553; IntAct: EBI-14036141; Score: 0.58
DE  Interaction: P16403; IntAct: EBI-20919468; Score: 0.40
DE  Interaction: O43390; IntAct: EBI-20927592; Score: 0.40
DE  Interaction: O14672; IntAct: EBI-21225540; Score: 0.40
GO  GO:0005884;
GO  GO:0032154;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001931;
GO  GO:0051015;
GO  GO:0042802;
GO  GO:0030041;
GO  GO:0007155;
GO  GO:0006897;
GO  GO:0006954;
GO  GO:0045087;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:9857189};
SQ  MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSL
SQ  KQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFER
SQ  ISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSM
SQ  QCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPK
SQ  TTSLAASAASTETLTPTPERNEGVYTAIAVQEIQGNPASPAQEYRALYDYTAQNPDELDLSAGDILEVILEGEDGWWTVE
SQ  RNGQRGFVPGSYLEKL
//
ID  P97814;
PN  Proline-serine-threonine phosphatase-interacting protein 1;
GN  Pstpip1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12530983}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11711533}. Cell projection, lamellipodium {ECO:0000269|PubMed:9265651}. Cleavage furrow {ECO:0000269|PubMed:9265651}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}. Cell membrane {ECO:0000250|UniProtKB:O43586}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43586}. Cell projection, uropodium {ECO:0000250|UniProtKB:O43586}. Note=Colocalized with PTPN12 in the cytoplasm and the perinuclear region (PubMed:11711533). During interphase, colocalizes with F-actin in the cortical cytoskeleton, lamellipodia, and stress fibers (PubMed:9265651). In dividing cells, colocalizes with the F-actin rich cytokinetic cleavage furrow (PubMed:9265651). Colocalized with CD2AP and WAS in the actin cytoskeleton within the cytoplasm (PubMed:12530983, PubMed:9488710). Colocalized with CD2, CD2AP and WAS at the site of T-cell:APC contact (PubMed:12530983). Mainly cytoplasmic in T cells. Colocalizes in cluster with CD2 near the cell surface membrane in activated T-cells. In monocytes, forms a branched filamentous network in the cytoplasm. In transfected cells, forms relatively straight filaments radiating out from the nucleus. Filament formation requires an intact tubulin cytoskeleton. In migrating neutrophils, colocalizes with PIP5K1C and DNM2 to the trailing edge of the uropod in a actin-dependent manner (By similarity). {ECO:0000250|UniProtKB:O43586, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12530983, ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}.
DR  UNIPROT: P97814;
DR  UNIPROT: Q4V9R4;
DR  Pfam: PF00611;
DR  Pfam: PF14604;
DR  PROSITE: PS51741;
DR  PROSITE: PS50002;
DE  Function: Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T- cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation. Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils. {ECO:0000269|PubMed:11163214, ECO:0000269|PubMed:11711533, ECO:0000269|PubMed:12530983, ECO:0000269|PubMed:9265651, ECO:0000269|PubMed:9488710}.
DE  Reference Proteome: Yes;
DE  Interaction: P70315; IntAct: EBI-8678726; Score: 0.60
DE  Interaction: P41047; IntAct: EBI-7833774; Score: 0.63
DE  Interaction: Q53ZZ1; IntAct: EBI-7833845; Score: 0.60
DE  Interaction: P35831; IntAct: EBI-7834118; Score: 0.78
DE  Interaction: P00520; IntAct: EBI-7484569; Score: 0.66
DE  Interaction: P70602; IntAct: EBI-7484657; Score: 0.40
DE  Interaction: Q61152; IntAct: EBI-8654066; Score: 0.44
DE  Interaction: P29352; IntAct: EBI-8654312; Score: 0.44
GO  GO:0005884;
GO  GO:0005826;
GO  GO:0032154;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001725;
GO  GO:0001931;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0042802;
GO  GO:0019903;
GO  GO:0030041;
GO  GO:0007155;
GO  GO:0006897;
GO  GO:0006954;
GO  GO:0045087;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O43586};
SQ  MMAQLQFRDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDVEELLRQRAQAEERYGKELVQIARKAGGQTEMNSLRTSFDSL
SQ  KQQTENVGSAHIQLALALREELRSLEEFRERQKEQRKKYEAIMDRVQKSKLSLYKKTMESKKAYDQKCRDADDAEQAFER
SQ  VSANGHQKQVEKSQNKAKQCKESATEAERVYRQNIEQLERARTEWEQEHRTTCEAFQLQEFDRLTILRNALWVHCNQLSM
SQ  QCVKDDELYEEVRLTLEGCDVEGDINGFIQSKSTGREPPAPVPYQNYYDREVTPLIGSPSIQPSCGVIKRFSGLLHGSPK
SQ  TTPSAPAASTETLTPTPERNELVYASIEVQATQGNLNSSAQDYRALYDYTAQNSDELDISAGDILAVILEGEDGWWTVER
SQ  NGQRGFVPGSYLEKL
//
ID  Q84XU2;
PN  Serine/threonine-protein phosphatase 5;
GN  PAPP5;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. [Isoform 2]: Cytoplasm. Nucleus, nucleoplasm. Nucleus speckle. Note=Cytoplasmic in darkness, but translocated to the nucleus upon illumination, when associated with phytochromes into speckles.
DR  UNIPROT: Q84XU2;
DR  UNIPROT: Q56X87;
DR  UNIPROT: Q8RXU0;
DR  UNIPROT: Q8W581;
DR  UNIPROT: Q9SJH5;
DR  PDB: 5JJT;
DR  PDB: 7OBE;
DR  Pfam: PF00149;
DR  Pfam: PF08321;
DR  Pfam: PF00515;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Isoform 2 dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms, and enhances phytochrome-mediated photoresponses, probably by enhancing their stability and their binding affinity for light signal transducers such as NDPK2. Can use para- nitrophenylphosphate (pNPP) as substrate. {ECO:0000269|PubMed:15707897}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9LE38; IntAct: EBI-4495648; Score: 0.37
DE  Interaction: D6RUV9; IntAct: EBI-7498180; Score: 0.50
DE  Interaction: Q93YQ1; IntAct: EBI-21138374; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030176;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0009506;
GO  GO:0046872;
GO  GO:0017018;
GO  GO:0004721;
GO  GO:0004722;
GO  GO:0046906;
GO  GO:0010019;
GO  GO:1902325;
GO  GO:0006913;
GO  GO:0010017;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  METKNENSDVSRAEEFKSQANEAFKGHKYSSAIDLYTKAIELNSNNAVYWANRAFAHTKLEEYGSAIQDASKAIEVDSRY
SQ  SKGYYRRGAAYLAMGKFKDALKDFQQVKRLSPNDPDATRKLKECEKAVMKLKFEEAISVPVSERRSVAESIDFHTIGNKP
SQ  RSSSMPTKTALAAVVAAVMVVAVRGFATTEILMVLVSVVLGTFWWGSFSGKVEPQYSGARIEGEEVTLDFVKTMMEDFKN
SQ  QKTLHKRYAYQIVLQTRQILLALPSLVDISVPHGKHITVCGDVHGQFYDLLNIFELNGLPSEENPYLFNGDFVDRGSFSV
SQ  EIILTLFAFKCMCPSSIYLARGNHESKSMNKIYGFEGEVRSKLSEKFVDLFAEVFCYLPLAHVINGKVFVVHGGLFSVDG
SQ  VKLSDIRAIDRFCEPPEEGLMCELLWSDPQPLPGRGPSKRGVGLSFGGDVTKRFLQDNNLDLLVRSHEVKDEGYEVEHDG
SQ  KLITVFSAPNYCDQMGNKGAFIRFEAPDMKPNIVTFSAVPHPDVKPMAYANNFLRMFN
//
ID  Q84K11;
PN  Serine/threonine-protein phosphatase 5;
GN  PP5;
OS  4081;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. [Isoform 2]: Cytoplasm. Nucleus, nucleoplasm. Nucleus speckle. Note=Cytoplasmic in darkness, but translocated to the nucleus upon illumination, when associated with phytochromes into speckles. {ECO:0000250}.
DR  UNIPROT: Q84K11;
DR  UNIPROT: Q8H1H4;
DR  Pfam: PF00149;
DR  Pfam: PF08321;
DR  Pfam: PF00515;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Isoform 2 dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms, and enhances phytochrome-mediated photoresponses (By similarity). Can use para-nitrophenylphosphate (pNPP) and phosphorylated casein as substrate at pH 7.5 and 5.0. {ECO:0000250, ECO:0000269|PubMed:12972652}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0046872;
GO  GO:0017018;
GO  GO:0004722;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPGMEAENSNASRAEELKQLANEAFKGHKYSQAIDLYTQAIELNGENAVYYANRAFAHTKLEEYGSAIQDGTRAIEIDPR
SQ  YSKGYYRRGAAYLAMGKFKDALKDFQQVKKLCPNDPDATKKLKECEKAVMKLKFEEAISVPESQRRSVADSIDYRSVGSG
SQ  PGSSYVPTKTTAVSAAAALMGVLVVYMGTKAATMVAAAASAALLVVLITFLWGRCSDGFFTKSRTLELEVEPQYAGARIE
SQ  GDVVTLDFVKKMLDDFKNQKNLHKRYAYQIVLQTREMLRALPSLVDIVVPEGKHFTVCGDVHGQFYDLLNIFELNGLPSE
SQ  DNPYLFNGDFVDRGSFSLEVILTLFAFKCMCPSAIHLARGNHESKSMNKIYGFEGEVRSKLSEIFVELFAEVFCCLPLAH
SQ  VINEKVFVVHGGLFSVDGVKLSDIRAIDRFCEPPEEGLMCELLWSDPQPQPGRGPSKRGVGLSFGGDVTKRFLQENNLDL
SQ  VVRSHEVKDEGYEIEHDGKLITVFSAPNYCDQMGNKGAFIRFEAPDMKPNIVTFSAVPHPDVKPMAYANNFLRMFS
//
ID  Q96MT3;
PN  Prickle-like protein 1;
GN  PRICKLE1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:14645515}. Cytoplasm, cytosol {ECO:0000269|PubMed:14645515}. Note=A smaller amount is detected in the cytosol.
DR  UNIPROT: Q96MT3;
DR  UNIPROT: Q14C83;
DR  UNIPROT: Q71QF8;
DR  UNIPROT: Q96N00;
DR  Pfam: PF00412;
DR  Pfam: PF06297;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS51303;
DR  OMIM: 182940;
DR  OMIM: 608500;
DR  OMIM: 612437;
DR  DisGeNET: 144165;
DE  Function: Involved in the planar cell polarity pathway that controls convergent extension during gastrulation and neural tube closure. Convergent extension is a complex morphogenetic process during which cells elongate, move mediolaterally, and intercalate between neighboring cells, leading to convergence toward the mediolateral axis and extension along the anteroposterior axis. Necessary for nuclear localization of REST. May serve as nuclear receptor. {ECO:0000269|PubMed:21901791}.
DE  Disease: Epilepsy, progressive myoclonic 1B (EPM1B) [MIM:612437]: A form of progressive myoclonic epilepsy, a clinically and genetically heterogeneous group of disorders defined by the combination of action and reflex myoclonus, other types of epileptic seizures, and progressive neurodegeneration and neurocognitive impairment. EPM1B is an autosomal recessive form characterized by myoclonus that progressed in severity over time, tonic-clonic seizures and ataxia. {ECO:0000269|PubMed:18976727, ECO:0000269|PubMed:21276947}. Note=The disease is caused by variants affecting the gene represented in this entry. Neural tube defects (NTD) [MIM:182940]: Congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy. Failure of neural tube closure can occur at any level of the embryonic axis. Common NTD forms include anencephaly, myelomeningocele and spina bifida, which result from the failure of fusion in the cranial and spinal region of the neural tube. NTDs have a multifactorial etiology encompassing both genetic and environmental components. {ECO:0000269|PubMed:21901791}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A2A5Z6; IntAct: EBI-2348682; Score: 0.40
DE  Interaction: O14641; IntAct: EBI-2348709; Score: 0.40
DE  Interaction: Q9Z101; IntAct: EBI-2348721; Score: 0.40
DE  Interaction: A6NK89; IntAct: EBI-6912271; Score: 0.35
DE  Interaction: Q92997; IntAct: EBI-8850502; Score: 0.40
DE  Interaction: Q8WWY3; IntAct: EBI-10177598; Score: 0.72
DE  Interaction: Q08E77; IntAct: EBI-10226027; Score: 0.56
DE  Interaction: Q8VIG1; IntAct: EBI-10684914; Score: 0.59
DE  Interaction: Q9HAQ2; IntAct: EBI-24796299; Score: 0.56
DE  Interaction: O75564; IntAct: EBI-24396853; Score: 0.56
DE  Interaction: Q13895; IntAct: EBI-24790662; Score: 0.56
DE  Interaction: Q5TAP6; IntAct: EBI-22147248; Score: 0.37
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0008270;
GO  GO:0035904;
GO  GO:0060976;
GO  GO:0090090;
GO  GO:2000691;
GO  GO:0045892;
GO  GO:0001843;
GO  GO:0032436;
GO  GO:0031398;
GO  GO:0006606;
GO  GO:0060071;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:14645515,};
SQ  MPLEMEPKMSKLAFGCQRSSTSDDDSGCALEEYAWVPPGLRPEQIQLYFACLPEEKVPYVNSPGEKHRIKQLLYQLPPHD
SQ  NEVRYCQSLSEEEKKELQVFSAQRKKEALGRGTIKLLSRAVMHAVCEQCGLKINGGEVAVFASRAGPGVCWHPSCFVCFT
SQ  CNELLVDLIYFYQDGKIHCGRHHAELLKPRCSACDEIIFADECTEAEGRHWHMKHFCCLECETVLGGQRYIMKDGRPFCC
SQ  GCFESLYAEYCETCGEHIGVDHAQMTYDGQHWHATEACFSCAQCKASLLGCPFLPKQGQIYCSKTCSLGEDVHASDSSDS
SQ  AFQSARSRDSRRSVRMGKSSRSADQCRQSLLLSPALNYKFPGLSGNADDTLSRKLDDLSLSRQGTSFASEEFWKGRVEQE
SQ  TPEDPEEWADHEDYMTQLLLKFGDKSLFQPQPNEMDIRASEHWISDNMVKSKTELKQNNQSLASKKYQSDMYWAQSQDGL
SQ  GDSAYGSHPGPASSRRLQELELDHGASGYNHDETQWYEDSLECLSDLKPEQSVRDSMDSLALSNITGASVDGENKPRPSL
SQ  YSLQNFEEMETEDCEKMSNMGTLNSSMLHRSAESLKSLSSELCPEKILPEEKPVHLPVLRRSKSQSRPQQVKFSDDVIDN
SQ  GNYDIEIRQPPMSERTRRRVYNFEERGSRSHHHRRRRSRKSRSDNALNLVTERKYSPKDRLRLYTPDNYEKFIQNKSARE
SQ  IQAYIQNADLYGQYAHATSDYGLQNPGMNRFLGLYGEDDDSWCSSSSSSSDSEEEGYFLGQPIPQPRPQRFAYYTDDLSS
SQ  PPSALPTPQFGQRTTKSKKKKGHKGKNCIIS
//
ID  Q3U5C7;
PN  Prickle-like protein 1;
GN  Prickle1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=A smaller amount is detected in the cytosol. {ECO:0000250}.
DR  UNIPROT: Q3U5C7;
DR  Pfam: PF00412;
DR  Pfam: PF06297;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS51303;
DE  Function: Involved in the planar cell polarity pathway that controls convergent extension during gastrulation and neural tube closure (By similarity). Convergent extension is a complex morphogenetic process during which cells elongate, move mediolaterally, and intercalate between neighboring cells, leading to convergence toward the mediolateral axis and extension along the anteroposterior axis. Necessary for nuclear localization of REST. May serve as nuclear receptor (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
DE  Interaction: Q8VIG1; IntAct: EBI-34578740; Score: 0.40
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0008270;
GO  GO:0035904;
GO  GO:0060976;
GO  GO:0090090;
GO  GO:2000691;
GO  GO:0045892;
GO  GO:0001843;
GO  GO:0032436;
GO  GO:0031398;
GO  GO:0006606;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MPLEMEPKMSKLVFGCQRSSTSDDDSGCALEEYAWVPPGLRPEQIQLYFACLPEEKVPYVNSPGEKHRIKQLLYQLPPHD
SQ  NEVRYCQSLSEEEKKELQVFSAQRKKEALGRGTIKLLSRAVMHAVCEQCGLQMNGGEVAVFASRAGPGVCWHPSCFVCFT
SQ  CNELLVDLIYFYQDGKIHCGRHHAELLKPRCSACDEIIFADECTEAEGRHWHMKHFCCLECETVLGGQRYIMKDGRPFCC
SQ  GCFESLYAEYCETCGEHIGVDHAQMTYDGQHWHATEACFSCAQCKASLLGCPFLPKQGQIYCSKTCSLGEDIHASDSSDS
SQ  AFQSARSRDSRRSVRMGRSSRSADQCRQSLLLSPALNYKFPGLSGNADDTLSRKLDDVSLASRQGAGFANEEFWKARVEQ
SQ  EASEDPEEWAEHEDYMTQLLLKFGDKNLFQQQSSEVDPRASEHWIPDNMVTNKPEVKPNHQGLASKKYQSDMYWAQSQDG
SQ  LGDSAYGSHPGPASSRRLQELDLDHGAAGYTHDQSQWYEDSLECLSDLKPEQSIRDSMDSLALSNITGASVDGESKPRPS
SQ  LYSLQNFEEIEAEDCEKMSNMGTLNSSMLHRSAESLQSLNSGLCPEKILPEEKPAHLPVLRRSKSQSRPQQVKFSDDVID
SQ  NGSYDIEIRQPPMSERTRRRAYHFEERGSRPHHHRHRRSRKSRSDNALNLVTERKYSAKDRLRLYTPDNYEKFIQNKSAR
SQ  ELQAYMQNANLYSQYAHATSDYALQNPGMNRFLGLCGEDDDSWCSSSTSSSDSEEEGYFLGQPIPQPRPQRFTYYTDDLS
SQ  SPASALPTPQFTQRTTKSKKKKGHKGKNCIIS
//
ID  Q71QF9;
PN  Prickle-like protein 1;
GN  Prickle1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=A smaller amount is detected in the cytosol. {ECO:0000250}.
DR  UNIPROT: Q71QF9;
DR  Pfam: PF00412;
DR  Pfam: PF06297;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS51303;
DE  Function: Involved in the planar cell polarity pathway that controls convergent extension during gastrulation and neural tube closure (By similarity). Convergent extension is a complex morphogenetic process during which cells elongate, move mediolaterally, and intercalate between neighboring cells, leading to convergence toward the mediolateral axis and extension along the anteroposterior axis. Necessary for nuclear localization of REST. May serve as nuclear receptor (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8VIG1; IntAct: EBI-10685002; Score: 0.37
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0008270;
GO  GO:0035904;
GO  GO:0060976;
GO  GO:0090090;
GO  GO:2000691;
GO  GO:0045892;
GO  GO:0001843;
GO  GO:0032436;
GO  GO:0031398;
GO  GO:0006606;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MPLEMEPKMSKLAFGCQRSSTSDDDSGCALEEYAWVPPGLRPEQIQLYFACLPEEKVPYVNSPGEKHRIKQLLYQLPPHD
SQ  NEVRYCQSLSEEEKKELQVFSAQRKKEALGRGTIKLLSRAMMHAVCEQCGLQMNGGEVAVFASRAGPGVCWRPSCFVCFT
SQ  CNELLVDLIYFYQDGKIHCGRHHAELLKPRCSACDEIIFADECTEAEGRHWHMKHFCCLECETVLGGQRYIMKDGRPFCC
SQ  GCFESLYAEYCETCGEHIGVDHAQMTYDGQHWHATEACFSCAQCKASLLGCPFLPKQGQIYCSKTCSLGEDIHASDSSDS
SQ  AFQSARSRDSRRSVRMGRSSRSADQCRQSLLLSPALNYKFPGLSGSADDTLSRKLDDVSLSGQGAGFAHEEFWKARVDQE
SQ  ASEDPEEWAEHEDYMTQLLLKFGDKNLFQQPPSEVDMRASEHWIPDNMVTNKPEAKQNHQSLASKKYQSDMYWAQSQDGL
SQ  GDSAYGSHPGPASSRRLQELDLDHGAAGYNHDQTQWYEDSLECLSDLKPEQSVRDSMDSLALSNITGASVDGESKPRPSL
SQ  YSLQNFEEIEAEDCEKMSNMGTLNSSMLHRSAESLKSLNSELCPEKIIPEEKPVHLPVLRRSKSQSRPQQVKFSDDVIDN
SQ  GSYDIEIRQPPMSERTRRRVYHFEERGSRPHHHRHRRSRKSRSDNALNLVTERKYSAKDRLRLYTPDNYEKFIQSKGARE
SQ  LQAYMQNANLYGQYAHTTSDYALQNPGMTRFLGLYGDDDDSWCSSSTSSSDSEEEGYFLGQPIPQPRPQRFTYYTDDLSS
SQ  PASALPTPQFNQRTTKSKKKKGHRGKNCIIS
//
ID  Q7Z3G6;
PN  Prickle-like protein 2;
GN  PRICKLE2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}.
DR  UNIPROT: Q7Z3G6;
DR  UNIPROT: Q0VF44;
DR  Pfam: PF00412;
DR  Pfam: PF06297;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS51303;
DR  OMIM: 608501;
DR  DisGeNET: 166336;
DE  Function: 
DE  Disease: Note=PRICKLE2 mutations have been found in patients with myoclonic epilepsy but involvement of this gene in pathogenesis is under debate since some of the patients also carry POLG mutations. {ECO:0000269|PubMed:21276947, ECO:0000269|PubMed:26942291, ECO:0000269|PubMed:26942292}.
DE  Reference Proteome: Yes;
DE  Interaction: A2A5Z6; IntAct: EBI-2349039; Score: 0.40
DE  Interaction: Q9UGN5; IntAct: EBI-7054206; Score: 0.44
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0008270;
GO  GO:0060071;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17411337};
SQ  MVTVMPLEMEKTISKLMFDFQRNSTSDDDSGCALEEYAWVPPGLKPEQVHQYYSCLPEEKVPYVNSPGEKLRIKQLLHQL
SQ  PPHDNEVRYCNSLDEEEKRELKLFSSQRKRENLGRGNVRPFPVTMTGAICEQCGGQINGGDIAVFASRAGHGVCWHPPCF
SQ  VCTVCNELLVDLIYFYQDGKIYCGRHHAECLKPRCAACDEIIFADECTEAEGRHWHMKHFCCFECETVLGGQRYIMKEGR
SQ  PYCCHCFESLYAEYCDTCAQHIGIDQGQMTYDGQHWHATETCFCCAHCKKSLLGRPFLPKQGQIFCSRACSAGEDPNGSD
SQ  SSDSAFQNARAKESRRSAKIGKNKGKTEEPMLNQHSQLQVSSNRLSADVDPLSLQMDMLSLSSQTPSLNRDPIWRSREEP
SQ  YHYGNKMEQNQTQSPLQLLSQCNIRTSYSPGGQGAGAQPEMWGKHFSNPKRSSSLAMTGHAGSFIKECREDYYPGRLRSQ
SQ  ESYSDMSSQSFSETRGSIQVPKYEEEEEEEGGLSTQQCRTRHPISSLKYTEDMTPTEQTPRGSMESLALSNATGLSADGG
SQ  AKRQEHLSRFSMPDLSKDSGMNVSEKLSNMGTLNSSMQFRSAESVRSLLSAQQYQEMEGNLHQLSNPIGYRDLQSHGRMH
SQ  QSFDFDGGMAGSKLPGQEGVRIQPMSERTRRRATSRDDNRRFRPHRSRRSRRSRSDNALHLASEREAISRLKDRPPLRAR
SQ  EDYDQFMRQRSFQESMGHGSRRDLYGQCPRTVSDLALQNAFGDRWGPYFAEYDWCSTCSSSSESDNEGYFLGEPIPQPAR
SQ  LRYVTSDELLHKYSSYGLPKSSTLGGRGQLHSRKRQKSKNCIIS
//
ID  Q80Y24;
PN  Prickle-like protein 2;
GN  Prickle2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}.
DR  UNIPROT: Q80Y24;
DR  UNIPROT: A6H652;
DR  Pfam: PF00412;
DR  Pfam: PF06297;
DR  PROSITE: PS00478;
DR  PROSITE: PS50023;
DR  PROSITE: PS51303;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q5NEC5; IntAct: EBI-22301317; Score: 0.37
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0016327;
GO  GO:0005737;
GO  GO:0016328;
GO  GO:0031965;
GO  GO:0008270;
GO  GO:0045197;
GO  GO:0031175;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTVMPLEMEKTISKLMFDFQRSSTSDDDSGCALEEYAWVPPGLKPEQVHQYYSCLPEEKVPYVNSAGEKLRIKQLLHQL
SQ  PPHDNEVRYCNSLDEEEKRELKLFSNQRKRENLGRGNVRPFPVTMTGAICEQCGGQIKGGDIAVFASRAGHGICWHPPCF
SQ  VCTVCNELLVDLIYFYQDGKIYCGRHHAECLKPRCAACDEIIFADECTEAEGRHWHMRHFCCFECETVLGGQRYIMKEGR
SQ  PYCCHCFESLYAEYCDTCAQHIGIDQGQMTYDGQHWHATETCFCCAHCKKSLLGRPFLPKQGQIFCSRACSAGEDPNGSD
SQ  SSDSAFQNARAKESRRSAKIGKNKGKTEEAMLNQHSQLQVSSNRLSADVDPLSVQMDLLSLSSQTPSLNRDPIWRSREEP
SQ  FHYGNKMEQNQSQSPLQLLSQCNIRTSYSPGGQGAGAQPDMWAKHFSNPKRSSSMALKGHGGSFIQECREDYYPGRLMSQ
SQ  ESYSDMSSQSFNETRGSIPVPKYEEEEEEEEGGISTQQCRPRRPLSSLKYTEDMTPTEQTPRGSMESLALSNATGLSAEG
SQ  GAKRQEHLSRFSMPDLSKDSGMNVSEKLSNMGTLNSSMQFRSAESVRSLLSAQQYQEMEGNLHQLSNPLGYRDLQSHGRM
SQ  HQSFDFDGGIASSKLPGQEGVHIQPMSERTRRRTTSRDDNRRFRPHRSRRSRRSRSDNALHLASEREVIARLKERPPLRA
SQ  REDYDQFMRQRSFQESLGQGSRRDLYSQCPRTVSDLALQNAFGERWGPYFTEYDWCSTCSSSSESDNEGYFLGEPIPQPA
SQ  RLRYVTSDELLHKYSSYGVPKSSTLGGRGQLHSRKRQKSKNCIIS
//
ID  Q7ZYA5;
PN  Interferon-inducible double-stranded RNA-dependent protein kinase activator A homolog A;
GN  prkra;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.
DR  UNIPROT: Q7ZYA5;
DR  Pfam: PF00035;
DR  Pfam: PF16482;
DR  PROSITE: PS50137;
DE  Function: Activates eif2ak2/pkr in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of eif2s1/efi2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by dicer1 and for subsequent siRNA-mediated post- transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by dicer1 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003725;
GO  GO:0008047;
GO  GO:0030422;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQERFPAAPKMSSEKPTSLDAMRATNPCETPIQLLHEFGTKTGNHPVYTLEKAEGQAHNPSFTFRLVIGDITSLGEGPS
SQ  KKTAKQKAAEFALNILRGDTSKCLPVTDTLRDPKKPPNQMQENPVGSLQELAVQKGWRLPEYTVAQESGPPHKREFTITC
SQ  RVETFVETGSGTSKQVAKRVAAEKLLTKFKTISTDNIPLNKLIGNKMGCTWDSMRNSSGEKISMLKRSPLSIPNTDYVKM
SQ  LKDVAEELDFNLTYLDIDELSVNGQYQCLAELSTNPITVCHGTGISCGNAHNDAAHNALQYLKIMCIKK
//
ID  Q91836;
PN  Interferon-inducible double-stranded RNA-dependent protein kinase activator A homolog B;
GN  prkra;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000269|PubMed:9230068}. Nucleus, nucleolus {ECO:0000269|PubMed:9230068}.
DR  UNIPROT: Q91836;
DR  PDB: 1DI2;
DR  Pfam: PF00035;
DR  Pfam: PF16482;
DR  PROSITE: PS50137;
DE  Function: Activates eif2ak2/pkr in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of eif2s1/efi2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by dicer1 and for subsequent siRNA-mediated post- transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by dicer1 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0003725;
GO  GO:0008047;
GO  GO:0030422;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSEKPTSLNAMRATNPCETPIQLLHEFGTKTGNHPVYTLEKAEGQAHNPSFTFRLVIGDITSLGEGPSKKTPKQKAAEF
SQ  ALNILRGDTSKCLPVTDTLRDPKKPPNQMQENPVGSLQELAVQKGWRLPEYTVAQESGPPHKREFTITCRVETFVETGSG
SQ  TSKQVAKRVAAEKLLTKFKTISTDNIPLNKLIGNKMGCTWDSMRNSSGEKISMLKRSPLSIPNTDYVKMLKDVAEELDFN
SQ  LTYLDIDELSVNGQYQCLAELSTNPITVCHGTGISCGNAHNDAAHNALQYLKIMCIKK
//
ID  Q2HJ92;
PN  Interferon-inducible double-stranded RNA-dependent protein kinase activator A;
GN  PRKRA;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}.
DR  UNIPROT: Q2HJ92;
DR  Pfam: PF00035;
DR  Pfam: PF16482;
DR  PROSITE: PS50137;
DE  Function: Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post- transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys- 386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005622;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0070883;
GO  GO:0042803;
GO  GO:0035197;
GO  GO:0034599;
GO  GO:0042474;
GO  GO:0042473;
GO  GO:2001244;
GO  GO:0031054;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:0070920;
GO  GO:0030422;
GO  GO:0048705;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQSRHRAAAPPMEREDSGTFSLGKMITAKPGKTPIQVLHEYGMKTKNIPVYECERSDVQIHVPTFTFRVTVGDITCTGE
SQ  GTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYT
SQ  TICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNMVGHSLGCTWHSLRNSPGEKINLLKRSLLSIPNTD
SQ  YIQLLSEIAKEQGFNITYLDIEELSANGQYQCLAELSTSPITVCHGSGISCSSAQSDAAHNALQYLKIIAERK
//
ID  B0V3F8;
PN  Interferon-inducible double-stranded RNA-dependent protein kinase activator A homolog;
GN  prkra;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: B0V3F8;
DR  UNIPROT: A4IGC9;
DR  Pfam: PF00035;
DR  Pfam: PF16482;
DR  PROSITE: PS50137;
DR  PROSITE: PS50835;
DE  Function: Activates eif2ak2/pkr in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of eif2s1/efi2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by dicer1 and for subsequent siRNA-mediated post- transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by dicer1 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0008047;
GO  GO:0035197;
GO  GO:0070920;
GO  GO:0030422;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPQRSQDKTPIQLLHEYGIKISSAPKYELIHADGDAHQPSFMFSVTIGEVTCKGRGSTKKAAKHEAAEAALKLLKRDSQ
SQ  IIDQRDNNGLSPEAGEASNPVGILQELAMQRVWCLPEYVVFMETGPGHMKEFTIACRLEGLEETGSGSSKKLARRAAAEN
SQ  MIAKLQSLSGSSEITWSPPSRVYVESLRNSTGEKVSLLKRTPLSLPNTDYIQMLLEISLELGFQVTYIDIDELTVNGQYQ
SQ  CLVELSTRPVTVCHGSGVTSSNAHNAAAHNALQYIKMVASKH
//
ID  O75569;
PN  Interferon-inducible double-stranded RNA-dependent protein kinase activator A;
GN  PRKRA;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Cytoplasm.
DR  UNIPROT: O75569;
DR  UNIPROT: A8K3I6;
DR  UNIPROT: Q53G24;
DR  UNIPROT: Q6X7T5;
DR  UNIPROT: Q8NDK4;
DR  PDB: 2DIX;
DR  Pfam: PF00035;
DR  Pfam: PF16482;
DR  PROSITE: PS50137;
DR  OMIM: 603424;
DR  OMIM: 612067;
DR  DisGeNET: 8575;
DE  Function: Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post- transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys- 386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner (By similarity). {ECO:0000250, ECO:0000269|PubMed:10336432, ECO:0000269|PubMed:11238927, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:16982605, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:9687506}.
DE  Disease: Dystonia 16 (DYT16) [MIM:612067]: An early-onset dystonia- parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYT16 patients have progressive, generalized dystonia with axial muscle involvement, oro-mandibular (sardonic smile) and laryngeal dystonia and, in some cases, parkinsonian features. {ECO:0000269|PubMed:18243799, ECO:0000269|PubMed:18420150}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q7L5N1; IntAct: EBI-730597; Score: 0.00
DE  Interaction: O60383; IntAct: EBI-730600; Score: 0.00
DE  Interaction: O75569; IntAct: EBI-7321838; Score: 0.80
DE  Interaction: Q15047; IntAct: EBI-730606; Score: 0.00
DE  Interaction: Q9UPY3; IntAct: EBI-8031519; Score: 0.74
DE  Interaction: Q9UKV8; IntAct: EBI-8031692; Score: 0.56
DE  Interaction: Q15633; IntAct: EBI-8031712; Score: 0.89
DE  Interaction: O60506; IntAct: EBI-1079593; Score: 0.00
DE  Interaction: Q14558; IntAct: EBI-1080077; Score: 0.00
DE  Interaction: Q9NZI8; IntAct: EBI-1081716; Score: 0.00
DE  Interaction: Q9Y3U8; IntAct: EBI-1082209; Score: 0.00
DE  Interaction: P03496; IntAct: EBI-2548060; Score: 0.67
DE  Interaction: P03485; IntAct: EBI-2548065; Score: 0.37
DE  Interaction: P03495; IntAct: EBI-2549290; Score: 0.37
DE  Interaction: A0A6L7H2I0; IntAct: EBI-2827043; Score: 0.00
DE  Interaction: Q92731; IntAct: EBI-2880601; Score: 0.35
DE  Interaction: Q9NX58; IntAct: EBI-8650565; Score: 0.74
DE  Interaction: P62487; IntAct: EBI-3912312; Score: 0.37
DE  Interaction: Q03701; IntAct: EBI-7321210; Score: 0.37
DE  Interaction: Q9P2H0; IntAct: EBI-7321354; Score: 0.37
DE  Interaction: O15226; IntAct: EBI-7321570; Score: 0.67
DE  Interaction: P29353; IntAct: EBI-7321982; Score: 0.37
DE  Interaction: Q9Y5X3; IntAct: EBI-7322110; Score: 0.37
DE  Interaction: Q8NHY6; IntAct: EBI-7322487; Score: 0.37
DE  Interaction: Q6NUN9; IntAct: EBI-7322704; Score: 0.37
DE  Interaction: Q7Z6M1; IntAct: EBI-7333491; Score: 0.37
DE  Interaction: P19525; IntAct: EBI-6116026; Score: 0.80
DE  Interaction: Q0HD54; IntAct: EBI-6155110; Score: 0.35
DE  Interaction: O56264; IntAct: EBI-6157161; Score: 0.35
DE  Interaction: Q9UPE1; IntAct: EBI-6381422; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: O95786; IntAct: EBI-9819981; Score: 0.69
DE  Interaction: Q05127; IntAct: EBI-9821212; Score: 0.52
DE  Interaction: Q9HA38; IntAct: EBI-10309853; Score: 0.56
DE  Interaction: P61965; IntAct: EBI-11057137; Score: 0.35
DE  Interaction: Q8TES7; IntAct: EBI-11374846; Score: 0.27
DE  Interaction: Q9E7P0; IntAct: EBI-11423546; Score: 0.37
DE  Interaction: P38732; IntAct: EBI-11529314; Score: 0.61
DE  Interaction: B2BTY8; IntAct: EBI-11510524; Score: 0.40
DE  Interaction: Q67020; IntAct: EBI-11514536; Score: 0.57
DE  Interaction: Q20MH3; IntAct: EBI-11520013; Score: 0.37
DE  Interaction: Q0A2H0; IntAct: EBI-11520168; Score: 0.37
DE  Interaction: Q2PJP0; IntAct: EBI-11520378; Score: 0.37
DE  Interaction: Q6DP93; IntAct: EBI-11520593; Score: 0.37
DE  Interaction: O92551; IntAct: EBI-11520760; Score: 0.37
DE  Interaction: O95793; IntAct: EBI-24279170; Score: 0.56
DE  Interaction: Q08426; IntAct: EBI-24301154; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-24316818; Score: 0.56
DE  Interaction: Q96SI9; IntAct: EBI-24342019; Score: 0.56
DE  Interaction: O75928; IntAct: EBI-24515412; Score: 0.56
DE  Interaction: P78563; IntAct: EBI-24416410; Score: 0.56
DE  Interaction: Q9H898; IntAct: EBI-24638962; Score: 0.60
DE  Interaction: P56945; IntAct: EBI-15099463; Score: 0.35
DE  Interaction: Q96LZ2; IntAct: EBI-21533913; Score: 0.35
DE  Interaction: P42696; IntAct: EBI-21605193; Score: 0.35
DE  Interaction: Q12905; IntAct: EBI-21665924; Score: 0.35
DE  Interaction: Q12926; IntAct: EBI-21666158; Score: 0.35
DE  Interaction: Q8WYQ5; IntAct: EBI-21679517; Score: 0.35
DE  Interaction: B0UZZ8; IntAct: EBI-21740634; Score: 0.35
DE  Interaction: P62888; IntAct: EBI-21742373; Score: 0.35
DE  Interaction: Q02543; IntAct: EBI-21743296; Score: 0.35
DE  Interaction: Q86SE5; IntAct: EBI-21774934; Score: 0.35
DE  Interaction: Q92737; IntAct: EBI-21797176; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-16798663; Score: 0.27
DE  Interaction: P60953; IntAct: EBI-16881098; Score: 0.37
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: P59595; IntAct: EBI-25639357; Score: 0.54
DE  Interaction: P03416; IntAct: EBI-25639368; Score: 0.54
DE  Interaction: Q9BYX4; IntAct: EBI-25639395; Score: 0.50
DE  Interaction: K9N4V0; IntAct: EBI-26375098; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-26948704; Score: 0.71
DE  Interaction: P43405; IntAct: EBI-28935283; Score: 0.35
DE  Interaction: Q9Y2H9; IntAct: EBI-28948459; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0070883;
GO  GO:0042803;
GO  GO:0003723;
GO  GO:0035197;
GO  GO:0034599;
GO  GO:0006955;
GO  GO:0042474;
GO  GO:0035196;
GO  GO:0008285;
GO  GO:0042473;
GO  GO:2001244;
GO  GO:0031054;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:0070920;
GO  GO:0009615;
GO  GO:0030422;
GO  GO:0048705;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQSRHRAEAPPLEREDSGTFSLGKMITAKPGKTPIQVLHEYGMKTKNIPVYECERSDVQIHVPTFTFRVTVGDITCTGE
SQ  GTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYT
SQ  TICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSIPNTD
SQ  YIQLLSEIAKEQGFNITYLDIDELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK
//
ID  Q9WTX2;
PN  Interferon-inducible double-stranded RNA-dependent protein kinase activator A;
GN  Prkra;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}.
DR  UNIPROT: Q9WTX2;
DR  UNIPROT: Q9CZB7;
DR  Pfam: PF00035;
DR  Pfam: PF16482;
DR  PROSITE: PS50137;
DE  Function: Required for siRNA production by DICER1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1 (By similarity). Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Promotes UBC9- p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner. {ECO:0000250, ECO:0000269|PubMed:10336432, ECO:0000269|PubMed:22214662}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6NZM9; IntAct: EBI-26472137; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0070883;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0035197;
GO  GO:0034599;
GO  GO:0043583;
GO  GO:0042474;
GO  GO:0035196;
GO  GO:0042473;
GO  GO:0008284;
GO  GO:2001244;
GO  GO:0031054;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:0070920;
GO  GO:0030422;
GO  GO:0048705;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSHSRHRAEAPPLQREDSGTFSLGKMITAKPGKTPIQVLHEYGMKTKNIPVYECERSDVQVHVPTFTFRVTVGDITCTGE
SQ  GTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYT
SQ  TICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSLPNTD
SQ  YIQLLSEIASEQGFNITYLDIEELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK
//
ID  Q4V8C7;
PN  Interferon-inducible double-stranded RNA-dependent protein kinase activator A;
GN  Prkra;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}.
DR  UNIPROT: Q4V8C7;
DR  Pfam: PF00035;
DR  Pfam: PF16482;
DR  PROSITE: PS50137;
DE  Function: Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post- transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association, sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR- dependent manner (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0008047;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0070883;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0035197;
GO  GO:0034599;
GO  GO:0043583;
GO  GO:0042474;
GO  GO:0035196;
GO  GO:0042473;
GO  GO:0008284;
GO  GO:2001244;
GO  GO:0031054;
GO  GO:0006468;
GO  GO:0050821;
GO  GO:0070920;
GO  GO:0070922;
GO  GO:0030422;
GO  GO:0048705;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSHSRHRAEAPPLQREDSGTFSLGKMITAKPGKTPIQVLHEYGTKTKNIPVYECERSDVQVHVPTFTFRVTVGDITCTGE
SQ  GTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYT
SQ  TICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSLPNTD
SQ  YIQLLSEIAKEQGFSITYLDIEELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK
//
ID  Q08931;
PN  Pheromone-regulated membrane protein 3;
GN  PRM3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane; Single-pass membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
DR  UNIPROT: Q08931;
DR  UNIPROT: D6W3H6;
DE  Function: Required for the fusion of nuclear envelopes during mating, ensuring proper karyogamy. Plays a role in the initiation of outer nuclear envelope fusion. {ECO:0000269|PubMed:12514182, ECO:0000269|PubMed:19297527, ECO:0000269|PubMed:19570912}.
DE  Reference Proteome: Yes;
DE  Interaction: P38987; IntAct: EBI-391647; Score: 0.37
DE  Interaction: Q08931; IntAct: EBI-392676; Score: 0.37
DE  Interaction: P38555; IntAct: EBI-392733; Score: 0.37
DE  Interaction: P32602; IntAct: EBI-394017; Score: 0.37
DE  Interaction: Q99260; IntAct: EBI-394311; Score: 0.37
DE  Interaction: P38074; IntAct: EBI-856087; Score: 0.00
DE  Interaction: P40857; IntAct: EBI-856585; Score: 0.00
DE  Interaction: P47088; IntAct: EBI-856681; Score: 0.00
GO  GO:0005737;
GO  GO:0031316;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005816;
GO  GO:0000742;
GO  GO:0048288;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTAMKEDNAALITLKKNNDQEKLRVHKLTDASSNSADGFVINKAKNGGPLNKKSLVNNEQHIKKAVSPGRVRKHKTTTSS
SQ  TKSRTKSKKKDASESKVQRENKGSFYQGAIFGSFLGAAVTTVLSNLAVKALQN
//
ID  Q0VBZ8;
PN  Proline-rich protein 14;
GN  PRR14;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Chromosome {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus lamina {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9BWN1}. Note=During interphase, associated with peripheral heterochromatin at the nuclear lamina. Released from the nuclear lamina in mitotic prophase and remains highly dispersed in metaphase. Associates with chromatin at the onset of anaphase and relocalizes to the nuclear lamina in telophase. {ECO:0000250|UniProtKB:Q9BWN1}.
DR  UNIPROT: Q0VBZ8;
DR  UNIPROT: Q58D02;
DR  Pfam: PF15386;
DE  Function: Functions in tethering peripheral heterochromatin to the nuclear lamina during interphase, possibly through the interaction with heterochromatin protein CBX5/HP1 alpha. Might play a role in reattaching heterochromatin to the nuclear lamina at mitotic exit. Promotes myoblast differentiation during skeletal myogenesis, possibly by stimulating transcription factor MyoD activity via binding to CBX5/HP1 alpha. Involved in the positive regulation of the PI3K-Akt- mTOR signaling pathway and in promoting cell proliferation, possibly via binding to GRB2 (By similarity). {ECO:0000250|UniProtKB:Q9BWN1}.
DE  Reference Proteome: Yes;
GO  GO:0005694;
GO  GO:0005652;
GO  GO:0005654;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLPGDSSTPGRQRLCRQPHAGALWGAKSPKRPKLQPLGAPSPLEKASRRVLAVVLEDVMAARMVPLEPQEESSTPRHHS
SQ  NHRDSVRSQPPASPPRQAMWSPQARPPDPLHLCREPLSRIRRPPSTPRRQSRTTPGPDEGPSQKVDQVHQPTLVVMLQDI
SQ  ASSRPRAEGFADEAPNFIIPARRAEPKVMVHQPKPPSRDLPAPSRPSALSANPLASPPPAPDPVLEPPSTPPPSSLLRPR
SQ  LSPWGLAPLFHSVRSKLESFADIFLTPNKAPRPPPPSPPMKLELKIAISEAGQPGASEGTVTVSPRPPIRQWRAQDQNPS
SQ  ATLTKPSLGRSHSCPDLGPPGPDPCSWPPVPAPSSRPRPRRHTVGGGEMAKAPPPPRPCLRKEVFPLGGVGASPPLVTSC
SQ  SSTASTSSFSEPAEPRLSSTKRKEPRAPEDQVLPDSETKTIGKVSRFRIRRTPARSQINLTPMGLPRPVRLNKKEFSLEE
SQ  IYTNKNYQSPTTRRTFETIFEEPRERNGTLIFTSSRKLRRTVEFRDSSLPRSRRPSRGARATAGRTLPPSLAPSPDVEPL
SQ  LQQRLQELDASLLEEEEEGDQDQPHRT
//
ID  Q9BWN1;
PN  Proline-rich protein 14;
GN  PRR14;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Chromosome {ECO:0000269|PubMed:24209742}. Nucleus {ECO:0000269|PubMed:25906157}. Nucleus lamina {ECO:0000269|PubMed:24209742}. Nucleus, nucleoplasm {ECO:0000269|PubMed:24209742}. Note=During interphase, associated with peripheral heterochromatin at the nuclear lamina. Released from the nuclear lamina in mitotic prophase and remains highly dispersed in metaphase. Associates with chromatin at the onset of anaphase and relocalizes to the nuclear lamina in telophase. {ECO:0000269|PubMed:24209742}.
DR  UNIPROT: Q9BWN1;
DR  UNIPROT: Q8WTX2;
DR  Pfam: PF15386;
DR  OMIM: 617423;
DR  DisGeNET: 78994;
DE  Function: Functions in tethering peripheral heterochromatin to the nuclear lamina during interphase, possibly through the interaction with heterochromatin protein CBX5/HP1 alpha (PubMed:24209742). Might play a role in reattaching heterochromatin to the nuclear lamina at mitotic exit (PubMed:24209742). Promotes myoblast differentiation during skeletal myogenesis, possibly by stimulating transcription factor MyoD activity via binding to CBX5/HP1 alpha (PubMed:25906157). Involved in the positive regulation of the PI3K-Akt-mTOR signaling pathway and in promoting cell proliferation, possibly via binding to GRB2 (PubMed:27041574). {ECO:0000269|PubMed:24209742, ECO:0000269|PubMed:25906157, ECO:0000269|PubMed:27041574}.
DE  Reference Proteome: Yes;
DE  Interaction: P45973; IntAct: EBI-756307; Score: 0.89
DE  Interaction: Q9P0V3; IntAct: EBI-2654051; Score: 0.00
DE  Interaction: Q99962; IntAct: EBI-7387644; Score: 0.37
DE  Interaction: P83916; IntAct: EBI-8831269; Score: 0.53
DE  Interaction: Q13185; IntAct: EBI-8831531; Score: 0.67
DE  Interaction: Q76MZ3; IntAct: EBI-10991736; Score: 0.35
DE  Interaction: P83917; IntAct: EBI-11012671; Score: 0.35
DE  Interaction: P30153; IntAct: EBI-11055988; Score: 0.64
DE  Interaction: Q5SZD1; IntAct: EBI-21545147; Score: 0.35
DE  Interaction: Q9UNI1; IntAct: EBI-21546011; Score: 0.35
DE  Interaction: O43291; IntAct: EBI-21587968; Score: 0.35
DE  Interaction: O14595; IntAct: EBI-21619731; Score: 0.35
DE  Interaction: Q6UWN0; IntAct: EBI-21625737; Score: 0.35
DE  Interaction: P62714; IntAct: EBI-21762711; Score: 0.35
DE  Interaction: Q9Y2E5; IntAct: EBI-21862823; Score: 0.35
DE  Interaction: Q13362; IntAct: EBI-21862823; Score: 0.35
DE  Interaction: Q16537; IntAct: EBI-21862823; Score: 0.35
DE  Interaction: Q15172; IntAct: EBI-21862823; Score: 0.35
DE  Interaction: Q14738; IntAct: EBI-21862823; Score: 0.35
DE  Interaction: P67775; IntAct: EBI-21862823; Score: 0.35
DE  Interaction: P30154; IntAct: EBI-21862823; Score: 0.35
DE  Interaction: P46108; IntAct: EBI-30821175; Score: 0.44
GO  GO:0005694;
GO  GO:0005652;
GO  GO:0005654;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLPGDSSPPGQPRLCRQPLTRALWGARSPKRPRLQLPGAPSPLEKASRRVLAVVLEDVMAVHMVPVVPSKQTSIPQHHS
SQ  YHQDPVHRQPPASPPRQAGWSSQARPPDPLCLCREPLSRIHRTSSTLRRRSRTTPGPEEGPSQKVDRAPQPTLVVMLEDI
SQ  ASPRPPAEGFIDETPNFIIPAQRAEPMRIVRQPTPPPGDLEPPFQPSALPADPLESPPTAPDPALELPSTPPPSSLLRPR
SQ  LSPWGLAPLFRSVRSKLESFADIFLTPNKTPQPPPPSPPMKLELKIAISEAEQSGAAEGTASVSPRPPIRQWRTQDHNTP
SQ  ALLPKPSLGRSYSCPDLGPPGPGTCTWPPAPPQPSRPRPRRHTVGGGEMARAPPPPRPCLRKEVFPLGGVGASPSLTTSC
SQ  SSTASTSFSEPAEPRLGSTKGKEPRASKDQVLSEPETKTMGKVSRFRIRRTPARPQLNLTPMGLPRPIRLNKKEFSLEEI
SQ  YTNKNYQSPTTRRTFETIFEEPRERNGTLIFTSSRKLRRAVEFRDSSLPRSRRPSRGVRAAGGRTVPPNVAPSPDVGPLL
SQ  QQRLEELDALLLEEETVDREQPHWT
//
ID  Q7TPN9;
PN  Proline-rich protein 14;
GN  Prr14;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Chromosome {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus lamina {ECO:0000250|UniProtKB:Q9BWN1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9BWN1}. Note=During interphase, associated with peripheral heterochromatin at the nuclear lamina. Released from the nuclear lamina in mitotic prophase and remains highly dispersed in metaphase. Associates with chromatin at the onset of anaphase and relocalizes to the nuclear lamina in telophase. {ECO:0000250|UniProtKB:Q9BWN1}.
DR  UNIPROT: Q7TPN9;
DR  UNIPROT: Q922N8;
DR  Pfam: PF15386;
DE  Function: Functions in tethering peripheral heterochromatin to the nuclear lamina during interphase, possibly through the interaction with heterochromatin protein CBX5/HP1 alpha (By similarity). Might play a role in reattaching heterochromatin to the nuclear lamina at mitotic exit (By similarity). Promotes myoblast differentiation during skeletal myogenesis, possibly by stimulating transcription factor MyoD activity via binding to CBX5/HP1 alpha (PubMed:25906157) (By similarity). Involved in the positive regulation of the PI3K-Akt-mTOR signaling pathway and in promoting cell proliferation, possibly via binding to GRB2 (By similarity). {ECO:0000250|UniProtKB:Q9BWN1, ECO:0000269|PubMed:25906157}.
DE  Reference Proteome: Yes;
GO  GO:0005694;
GO  GO:0005652;
GO  GO:0005654;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLPGNSSPFTQPSLCRQPLSRASWEARSPKRPRLQPLGTPSSLEKASRRVLAVVLEDVMTTNRVPLTHKEDTPSPLTHN
SQ  HHQDPVCTQSPALPSQQVKWSMQARPPDPLHLCREPLTRARQSSPALRMRSRAASGPEESPSKKTDQVPQPTLVVVLEDI
SQ  ASGRQPAEGFDEDQPNLIVPAQSTFRSLKGPGKHCHRRGLDLEARPTLTLSLHPRAEPVTKAGQPMPTPSDLEPPFQLST
SQ  LPADPPESPVPDPALETPVIPTSSSLLRPRLSPWGLAPLFRSVRSKLESFADIFFTPNKTPQPPPPSPPMKLELKIAISE
SQ  AEQSRATEKITSVSPRPPIRQWRTQCNSLAPVSKSSLGRSYSCPDLGPPDPGSWPPVPSQPSQSRPRRHTVGCGEMARTP
SQ  PPPRPCLRKEVFPLGGVGVSPSLTTSCSANAPASFFCEPAEPRLGSTKGKELRASKDKVFSDPETKTMGKVSRFRIRRTP
SQ  VRLQPNLTPMGLPRPIRLNKKEFTLEEIYTNKNYQSPTTRRTFETIFEEPRERNGTLIFTSSRKLRRAVEFRDSSLPRSR
SQ  RPSRGVRTAASRTLTPNLAPSQDVGSLLQERLRELDALLLEEETDKEHPCHL
//
ID  Q8TB68;
PN  Proline-rich protein 7;
GN  PRR7;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:21460222}; Single-pass type III membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P0C6T3}; Single-pass type III membrane protein {ECO:0000305}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P0C6T3}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21460222}. Synapse {ECO:0000269|PubMed:27458189}. Cell projection, dendrite {ECO:0000269|PubMed:27458189}. Nucleus {ECO:0000269|PubMed:27458189}. Note=Enriched in postsynaptic plasma membrane and postsynaptic densities (PSD). Accumulates in spines along with synapse maturation and colocalizes with DLG4 in a punctate pattern. Translocates from synapses to nuclei following NMDA receptor activity (By similarity). {ECO:0000250|UniProtKB:P0C6T3}.
DR  UNIPROT: Q8TB68;
DR  UNIPROT: Q8WU53;
DR  UNIPROT: Q9BTA7;
DR  OMIM: 618306;
DR  DisGeNET: 80758;
DE  Function: Acts as a synapse-to-nucleus messenger to promote NMDA receptor-mediated excitotoxicity in neurons in a JUN-dependent manner (By similarity). Inhibits ubiquitination-mediated degradation and promotes phosphorylation and transcriptional activity of transcription factor JUN (PubMed:27458189). Might play a redundant role in the regulation of T cell receptor signaling (PubMed:21460222). Might promote apoptosis in T cells (PubMed:21460222). {ECO:0000250|UniProtKB:P0C6T3, ECO:0000250|UniProtKB:Q3V0I2, ECO:0000269|PubMed:21460222, ECO:0000269|PubMed:27458189}.
DE  Reference Proteome: Yes;
DE  Interaction: A8K8V0; IntAct: EBI-3925408; Score: 0.37
DE  Interaction: P46934; IntAct: EBI-30833480; Score: 0.44
DE  Interaction: P46937; IntAct: EBI-30847770; Score: 0.44
GO  GO:0070161;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0098978;
GO  GO:0016021;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098839;
GO  GO:0099092;
GO  GO:0036041;
GO  GO:1990782;
GO  GO:0044877;
GO  GO:0044389;
GO  GO:0002250;
GO  GO:0046632;
GO  GO:0031397;
GO  GO:0043065;
GO  GO:0010942;
GO  GO:2001269;
GO  GO:0099527;
GO  GO:0033077;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVMSQGTYTFLTCFAGFWLIWGLIVLLCCFCSFLRRRLKRRQEERLREQNLRALELEPLELEGSLAGSPPGLAPPQPPPH
SQ  RSRLEAPAHAHSHPHVHVHPLLHHGPAQPHAHAHPHPHHHALPHPPPTHLSVPPRPWSYPRQAESDMSKPPCYEEAVLMA
SQ  EPPPPYSEVLTDTRGLYRKIVTPFLSRRDSAEKQEQPPPSYKPLFLDRGYTSALHLPSAPRPAPPCPALCLQADRGRRVF
SQ  PSWTDSELSSREPLEHGAWRLPVSIPLFGRTTAV
//
ID  Q3V0I2;
PN  Proline-rich protein 7;
GN  Prr7;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8TB68}; Single-pass type III membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P0C6T3}; Single-pass type III membrane protein {ECO:0000305}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P0C6T3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TB68}. Synapse {ECO:0000250|UniProtKB:P0C6T3}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0C6T3}. Nucleus {ECO:0000250|UniProtKB:P0C6T3}. Note=Enriched in postsynaptic plasma membrane and postsynaptic densities (PSD). Accumulates in spines along with synapse maturation and colocalizes with DLG4 in a punctate pattern. Translocates from synapses to nuclei following NMDA receptor activity (By similarity). {ECO:0000250|UniProtKB:P0C6T3}.
DR  UNIPROT: Q3V0I2;
DE  Function: Acts as a synapse-to-nucleus messenger to promote NMDA receptor-mediated excitotoxicity in neurons in a JUN-dependent manner (By similarity). Inhibits ubiquitination-mediated degradation and promotes phosphorylation and transcriptional activity of transcription factor JUN (By similarity). Might play a redundant role in the regulation of T cell receptor signaling (PubMed:27657535). Might promote apoptosis in T cells (By similarity). {ECO:0000250|UniProtKB:P0C6T3, ECO:0000250|UniProtKB:Q8TB68, ECO:0000269|PubMed:27657535}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0070161;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0098978;
GO  GO:0016021;
GO  GO:0043005;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098839;
GO  GO:0099092;
GO  GO:0045202;
GO  GO:0036041;
GO  GO:1990782;
GO  GO:0044877;
GO  GO:0044389;
GO  GO:0002250;
GO  GO:0046632;
GO  GO:0031397;
GO  GO:0043065;
GO  GO:0010942;
GO  GO:2001269;
GO  GO:0099527;
GO  GO:0033077;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVMSQGTYTFLTCFAGFWLIWGLIVLLCCFCSFLRRRLKRRQEERLREQNLRALELEPLELEGSLAGSPPGLAPPPPPHR
SQ  SRLEAPVHAHSHVHVHPLLHHGPAPPHAHPHPHHHALPHPPPPHLAVPPRPWSYPRQAESDMSKPPCYEEAVLMAEPPPP
SQ  YSEVLTDTRGLYRKIVTPFLSRRDSAEKQEQPPPSYKPLFLDRGYTSALHLPSAPRPAAPCPALCLQAERSRRVFPSWTD
SQ  SELSSREPLEHGAWRLPVSIPLFGRTTAV
//
ID  P0C6T3;
PN  Proline-rich protein 7;
GN  Prr7;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8TB68}; Single-pass type III membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000269|PubMed:15629447}; Single-pass type III membrane protein {ECO:0000305}. Postsynaptic density membrane {ECO:0000269|PubMed:15629447, ECO:0000269|PubMed:27458189}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TB68}. Synapse {ECO:0000269|PubMed:27458189}. Cell projection, dendrite {ECO:0000269|PubMed:27458189}. Nucleus {ECO:0000269|PubMed:27458189}. Note=Enriched in postsynaptic plasma membrane and postsynaptic densities (PSD) (PubMed:15629447, PubMed:27458189). Accumulates in spines along with synapse maturation and colocalizes with DLG4 in a punctate pattern (PubMed:15629447). Translocates from synapses to nuclei following NMDA receptor activity (PubMed:27458189). {ECO:0000269|PubMed:15629447, ECO:0000269|PubMed:27458189}.
DR  UNIPROT: P0C6T3;
DE  Function: Acts as a synapse-to-nucleus messenger to promote NMDA receptor-mediated excitotoxicity in neurons in a JUN-dependent manner (PubMed:27458189). Inhibits ubiquitination-mediated degradation and promotes phosphorylation and transcriptional activity of transcription factor JUN (PubMed:27458189). Might play a redundant role in the regulation of T cell receptor signaling (By similarity). Might promote apoptosis in T cells (By similarity). {ECO:0000250|UniProtKB:Q8TB68, ECO:0000269|PubMed:27458189}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0098978;
GO  GO:0016021;
GO  GO:0043005;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0098839;
GO  GO:0099092;
GO  GO:0045202;
GO  GO:0036041;
GO  GO:1990782;
GO  GO:0044877;
GO  GO:0044389;
GO  GO:0002250;
GO  GO:0046632;
GO  GO:0031397;
GO  GO:0043065;
GO  GO:0010942;
GO  GO:2001269;
GO  GO:0099527;
GO  GO:0033077;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVMSQGTYTFLTCFAGFWLIWGLIVLLCCFCSFLRRRLKRRQEERLREQNLRALELEPLELEGSLAGSPPGLAPPPPPHR
SQ  SRLEAPVHAHSHVHVHPLLHHGPAQPHAHPHPHHHALPHPPPSHLSVPPRPWSYPRQAESDMSKPPCYEEAVLMAEPPPP
SQ  YSEVLTDTRGLYRKIVTPFLSRRDSAEKQEQPPPSYKPLFLDRGYTSALHLPSAPRPAAPCPALCLQADRSRRVFPSWTD
SQ  SELSSREPLEHGAWRLPVSIPLFGRTTAV
//
ID  Q9UTB5;
PN  Phosphatidylserine decarboxylase 2 alpha chain;
GN  psd2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: [Phosphatidylserine decarboxylase 2 beta chain]: Mitochondrion {ECO:0000305|PubMed:16823372, ECO:0000305|PubMed:34818062}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Nucleus envelope {ECO:0000269|PubMed:16823372}. [Phosphatidylserine decarboxylase 2 alpha chain]: Mitochondrion {ECO:0000305|PubMed:16823372, ECO:0000305|PubMed:34818062}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Nucleus envelope {ECO:0000269|PubMed:16823372}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}. Lipid droplet {ECO:0000269|PubMed:34818062}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:34818062}.
DR  UNIPROT: Q9UTB5;
DR  Pfam: PF02666;
DE  Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Together with psd1 and psd3, responsible for the majority of phosphatidylethanolamine synthesis (PubMed:19286980). Plays a role in lipid droplet biogenesis at the endoplasmic reticulum membrane (PubMed:34818062). {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:19286980, ECO:0000269|PubMed:34818062}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0031305;
GO  GO:0005811;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0004609;
GO  GO:0140042;
GO  GO:0006656;
GO  GO:0006646;
GO  GO:0016540;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03208};
SQ  MRPRQRFRRFHPRWSKVNLRGFGGVGALKGVKALNGMNVRVSMRLKWISNRIHRIRRSRRLGRLSISVRPNGSWQVYLLS
SQ  SLPLRSLSRVWGQFNRAHLPTFLRTPGFKLYAWVFGCNLSELKDPDLTHYRNFQDFFCRELRPETRPVDPVSPVVSPVDG
SQ  RIVCQGVVDNNRIQHVKGLSYSLEALLGGISSSNPLVVNFEDEITPDLIQKHEQFAEQHSISLNSNNRYRKADASAAVVD
SQ  EHSDEEALLCAFTDHPHFYLNDSRNSLNYFCPFSAFEDISNSVRSSCGKRLSPSSNFDLNNLGGDDDLRSESSSDFESAP
SQ  ASILEHEPTNWDDWVQEADVTDIDSLPWHNIRPGNKLFYSVIYLAPGDYHRFHSPADWVIESRRHFSGELFSVSPFLARR
SQ  LHNLFVLNERVALLGRYEHGFMSMIPVGATNVGSIVINCDPTLSTNRLVLRKKSLGTFQEAVYKNASPVLDGMPVSRGEQ
SQ  VGGFQLGSTVVLVFEAPADFEFSTYQGQYVRVGEAL
//
ID  F4HXY7;
PN  CDP-diacylglycerol--serine O-phosphatidyltransferase 1;
GN  PSS1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21554450}; Multi-pass membrane protein {ECO:0000269|PubMed:21554450}. Nucleus envelope {ECO:0000269|PubMed:21554450}. Note=Mainly localized in nuclei and ER membranes during pollen development.
DR  UNIPROT: F4HXY7;
DR  UNIPROT: Q9XI59;
DR  Pfam: PF03034;
DE  Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Is essential for phosphatidylserine (PS) biosynthesis and PE seems to be the most plausible substrate. Plays an important role in microspore maturation. {ECO:0000269|PubMed:21554450}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003882;
GO  GO:0106245;
GO  GO:0009556;
GO  GO:0006646;
GO  GO:0006659;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEPNGYRKERRKEQHLGRMNGGGGDVETDLDPWTAWAYKPRTISLLLIGACFLIWASGALDPDSTTSDDLVTSVKRGVWA
SQ  MIAVFLAYSLLQAPSTVLIRPHPAIWRLVHGMAVIYLVALTFLLFQRRDDARQFMKFLHPDLGIELPEKSYGADCRIYVP
SQ  DHPTNRFKNLYDTVFDEFFLAHIFGWWGKAILIRNQPLLWVLSIGFELLEVTFRHMLPNFNECWWDSIVLDILICNWFGI
SQ  WAGMYTVRYFDGKTYEWVGISRQPNIIGKVKRTLGQFTPAHWDKDEWHPLQGPWRFIQVLTLCIIFLTVELNTFFLKFSL
SQ  WIPPRNPVILYRLILWWLIAIPTTREYNSYLQDRKPVKKVGAFCWLSLGICIVELLICIKFGSGLYPTEMPLWVVTLWGS
SQ  VGLGLVAFLLSWTWKIQKILAQKRR
//
ID  O02853;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: O02853;
DR  UNIPROT: A2VDW5;
DR  UNIPROT: A5PJE8;
DR  Pfam: PF00061;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation (PubMed:9510973). Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non- substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222, ECO:0000269|PubMed:9510973}.
DE  Reference Proteome: Yes;
DE  Interaction: P29128; IntAct: EBI-11292082; Score: 0.37
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0043303;
GO  GO:0044793;
GO  GO:0045071;
GO  GO:0001516;
GO  GO:0045187;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATPNRLWMALLLLGVLGVLQTPAPAQAALQPNFEEDKFLGRWFTSGLASNSSWFLEKKKVLSMCKSVVAPAADGGLNLT
SQ  STFLRKDQCETRTLLLRPAGPPGCYSYTSPHWSSTHEVSVAETDYETYALLYTEGVRGPGQDFRMATLYSRSQNPRAEVK
SQ  EHFTTFAKSLGFTEEGIVFLPKTDKCMEEHP
//
ID  Q9XS65;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: Q9XS65;
DR  Pfam: PF00061;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0043303;
GO  GO:0001516;
GO  GO:0045187;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGALCTLWLGLVLLGVLGALQTSAQAQVSLQPNFQQDKFLGRWFTSGLASNSSWFREKKNVLSMCMSVVAPTADGGLNLT
SQ  STFLRKDQCETRTLLLRPAGTPGCYSYTSPHWGSTHDVWVVATNYEEYALLYTAGSKGLGQDFHMATLYSRTQTPKAEIK
SQ  EKFSTFAKTQGFTEDAIVFLPQTDKCMEENK
//
ID  Q29487;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9685;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: Q29487;
DR  Pfam: PF00061;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0043303;
GO  GO:0001516;
GO  GO:0045187;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALHTLWMGLVLLGVLGVLQTRAQAQVSRQPNFQQDKFLGRWFTSGLASNSSWFREKKNALSMCISVVAPSAEGGLNLT
SQ  TTFLRKDQCETRTLLLRPAETPGCYSYTSPHWGSTHDVWVVATDYEEYALLYTAGTKSPGQDFHMATLYSRTQTPRAEVK
SQ  EKFSTFAKTRGFTEDAIVFLPKTERCMEEHR
//
ID  Q8WNM1;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9595;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: Q8WNM1;
DR  Pfam: PF00061;
DR  PROSITE: PS00213;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0043303;
GO  GO:0001516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKAALSMCKSVVAPAADGGLNLT
SQ  STFLRKNQCETRTMLLQTAGSLGSYSYRSPHWGSTYSVSVVETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELK
SQ  EKFTAFCKAQGFTEDTIVFLPQTDKCLTEQ
//
ID  O97921;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9796;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: O97921;
DR  Pfam: PF00061;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0043303;
GO  GO:0001516;
GO  GO:0045187;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASHTLWMGLVLLGVLGVLQTRAQAQPSLQPNFQQDKFLGRWFTSGLASNSSWFREKKKVLSMCTSVVAPTADGGFNLT
SQ  STFLRKDQCETRTLLLQPAGPPGCYSYTSPHWGMVHEVSVVETDYEEYALLYTHAESTKGLGGQDFRMATLYSRVQSPRP
SQ  EVKEKFSTFAKAQGFTEDAIVFLPQTDKCMEEHN
//
ID  P41222;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000269|PubMed:9065498}. Nucleus membrane {ECO:0000269|PubMed:9065498}. Golgi apparatus {ECO:0000269|PubMed:9065498}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9065498}. Secreted {ECO:0000269|PubMed:9065498}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted.
DR  UNIPROT: P41222;
DR  UNIPROT: B2R727;
DR  UNIPROT: Q5SQ10;
DR  UNIPROT: Q7M4P3;
DR  UNIPROT: Q9UC22;
DR  UNIPROT: Q9UCC9;
DR  UNIPROT: Q9UCD9;
DR  PDB: 2WWP;
DR  PDB: 3O19;
DR  PDB: 3O22;
DR  PDB: 3O2Y;
DR  PDB: 4IMN;
DR  PDB: 4IMO;
DR  PDB: 4ORR;
DR  PDB: 4ORS;
DR  PDB: 4ORU;
DR  PDB: 4ORW;
DR  PDB: 4ORX;
DR  PDB: 4ORY;
DR  PDB: 4OS0;
DR  PDB: 4OS3;
DR  PDB: 4OS8;
DR  PDB: 5WY9;
DR  Pfam: PF00061;
DR  PROSITE: PS00213;
DR  OMIM: 176803;
DR  DisGeNET: 5730;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation (PubMed:20667974). Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non- substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (PubMed:20667974, PubMed:9475419). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250|UniProtKB:O09114, ECO:0000269|PubMed:20667974, ECO:0000269|PubMed:9475419}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-4397184; Score: 0.55
DE  Interaction: P54253; IntAct: EBI-25975530; Score: 0.67
DE  Interaction: Q4R5M2; IntAct: EBI-7552882; Score: 0.27
DE  Interaction: Q4R4P0; IntAct: EBI-7552924; Score: 0.27
DE  Interaction: Q5NGW2; IntAct: EBI-2798376; Score: 0.00
DE  Interaction: A0A6L8P1I7; IntAct: EBI-2809743; Score: 0.00
DE  Interaction: Q81K97; IntAct: EBI-2826871; Score: 0.00
DE  Interaction: P40692; IntAct: EBI-2932395; Score: 0.37
DE  Interaction: O00555; IntAct: EBI-3867481; Score: 0.37
DE  Interaction: O15382; IntAct: EBI-3927332; Score: 0.37
DE  Interaction: P31749; IntAct: EBI-9063831; Score: 0.37
DE  Interaction: P60409; IntAct: EBI-10208427; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-24276790; Score: 0.56
DE  Interaction: Q9UHD9; IntAct: EBI-24305877; Score: 0.56
DE  Interaction: P60328; IntAct: EBI-24314278; Score: 0.56
DE  Interaction: Q9BWT7; IntAct: EBI-24398818; Score: 0.56
DE  Interaction: P02763; IntAct: EBI-21854886; Score: 0.35
DE  Interaction: P52757; IntAct: EBI-21873773; Score: 0.40
DE  Interaction: P07550; IntAct: EBI-20801889; Score: 0.37
DE  Interaction: P55212; IntAct: EBI-25834727; Score: 0.56
DE  Interaction: P13473; IntAct: EBI-25872987; Score: 0.56
DE  Interaction: Q9Y371; IntAct: EBI-25921966; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25959160; Score: 0.56
DE  Interaction: P07949; IntAct: EBI-32719411; Score: 0.35
GO  GO:0005789;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0005504;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0019371;
GO  GO:0010467;
GO  GO:0043303;
GO  GO:2000255;
GO  GO:0001516;
GO  GO:0045187;
GO  GO:0051384;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKAALSMCKSVVAPATDGGLNLT
SQ  STFLRKNQCETRTMLLQPAGSLGSYSYRSPHWGSTYSVSVVETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELK
SQ  EKFTAFCKAQGFTEDTIVFLPQTDKCMTEQ
//
ID  Q9TUI1;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9543;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: Q9TUI1;
DR  Pfam: PF00061;
DR  PROSITE: PS00213;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0043303;
GO  GO:0001516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATHHTLWMGLVLLGLLGGLQAAPEAQVSVQPNFQPDKFLGRWFSAGLASNSSWLQEKKAALSMCKSVVAPATDGGLNLT
SQ  STFLRKNQCETRTMLLQPGESLGSYSYGSPHWGSTYSVSVVETDYDHYALLYSQGSKGPGEDFRMATLYSRTQTPRAELK
SQ  EKFSAFCKAQGFTEDSIVFLPQTDKCMTEQ
//
ID  O09114;
PN  Prostaglandin-H2 D-isomerase;
GN  Ptgds;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: O09114;
DR  UNIPROT: O09157;
DR  UNIPROT: O35091;
DR  UNIPROT: Q3V2G5;
DR  UNIPROT: Q62169;
DR  PDB: 2CZT;
DR  PDB: 2CZU;
DR  PDB: 2E4J;
DR  PDB: 2KTD;
DR  PDB: 2RQ0;
DR  Pfam: PF00061;
DR  PROSITE: PS00213;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (PubMed:10781097, PubMed:11751991, PubMed:12077186, PubMed:17715133, PubMed:19546224, PubMed:19833210, PubMed:8922532, PubMed:9892701). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (PubMed:23624557). {ECO:0000269|PubMed:10781097, ECO:0000269|PubMed:11751991, ECO:0000269|PubMed:12077186, ECO:0000269|PubMed:17715133, ECO:0000269|PubMed:19546224, ECO:0000269|PubMed:19833210, ECO:0000269|PubMed:23624557, ECO:0000269|PubMed:8922532, ECO:0000269|PubMed:9892701}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0005504;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0010467;
GO  GO:0043303;
GO  GO:2000255;
GO  GO:0001516;
GO  GO:0045187;
GO  GO:0051384;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALRMLWMGLVLLGLLGFPQTPAQGHDTVQPNFQQDKFLGRWYSAGLASNSSWFREKKAVLYMCKTVVAPSTEGGLNLT
SQ  STFLRKNQCETKIMVLQPAGAPGHYTYSSPHSGSIHSVSVVEANYDEYALLFSRGTKGPGQDFRMATLYSRTQTLKDELK
SQ  EKFTTFSKAQGLTEEDIVFLPQPDKCIQE
//
ID  Q29095;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: Q29095;
DR  Pfam: PF00061;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0043303;
GO  GO:0001516;
GO  GO:0045187;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATPSSLWLGLALLGTLGVLQTPAQASLQPNFQEDKFLGRWFTSGLASNSSWFLEKKKVLSMCKSLVAPAPDGGFNLTST
SQ  FLRKDQCVTRTLMLRPAGPPGCYSYTSPHGGSNLEVSVVETDYKNYALLHTESGPSPGPAFRMATLYSRSQAPGAAVREK
SQ  FTAFAKARGFTEDGIVFLPRNEKCLEEHE
//
ID  Q8WNM0;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9600;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: Q8WNM0;
DR  Pfam: PF00061;
DR  PROSITE: PS00213;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0043303;
GO  GO:0001516;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATHHTLWMGLALLGVLGGLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKAALSMCKSVVAPAADGGLNLT
SQ  STFLRKNQCETRTMLLQPAGSLGSYSYRSPHWGSTYSVSVVETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELK
SQ  EKFTAFCKAQGFTEDTIVFLPQTDKCMTEQ
//
ID  P22057;
PN  Prostaglandin-H2 D-isomerase;
GN  Ptgds;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: P22057;
DR  Pfam: PF00061;
DR  PROSITE: PS00213;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (PubMed:10387044, PubMed:10650953, PubMed:11058225, PubMed:9188476). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250|UniProtKB:O09114, ECO:0000269|PubMed:10387044, ECO:0000269|PubMed:10650953, ECO:0000269|PubMed:11058225, ECO:0000269|PubMed:9188476}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0005504;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0010467;
GO  GO:0043303;
GO  GO:2000255;
GO  GO:0001516;
GO  GO:0045187;
GO  GO:0051384;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALPMLWTGLVLLGLLGFPQTPAQGHDTVQPNFQQDKFLGRWYSAGLASNSSWFREKKELLFMCQTVVAPSTEGGLNLT
SQ  STFLRKNQCETKVMVLQPAGVPGQYTYNSPHWGSFHSLSVVETDYDEYAFLFSKGTKGPGQDFRMATLYSRAQLLKEELK
SQ  EKFITFSKDQGLTEEDIVFLPQPDKCIQE
//
ID  Q9XSM0;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9940;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: Q9XSM0;
DR  Pfam: PF00061;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222, ECO:0000269|PubMed:11804963}.
DE  Reference Proteome: Yes;
GO  GO:0005576;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0043303;
GO  GO:0001516;
GO  GO:0045187;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATPNRPWMGLLLLGVLGVLQTPAPTEAALQPNFEEDKFLGRWFTSGLASNSSWFLEKRKVLSMCKSEVAPAADGGLNVT
SQ  STFLRKDQCETRTLLLRPAGPPGCYSYTSPHWSSTHEVSVAETDYETYALLYTESVRGPGPDSLMATLYSRTQTPRAEVK
SQ  EKFTTFARSLGFTEEGIVFLPKTDKCMEVRT
//
ID  Q29562;
PN  Prostaglandin-H2 D-isomerase;
GN  PTGDS;
OS  9644;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
DR  UNIPROT: Q29562;
DR  Pfam: PF00061;
DE  Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114, ECO:0000250|UniProtKB:P41222}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005791;
GO  GO:0004667;
GO  GO:0005501;
GO  GO:0036094;
GO  GO:0043303;
GO  GO:0001516;
GO  GO:0045187;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAALHTLWMGLVLLGVLGVLQTQAQVQVSLQPNFQQDKFLGRWFTSGLASNSSWFREKKKVLSMCVSVVAPSADGGLNLT
SQ  STFLRKEQCETRTLLLRPAGTPGCYSYTSPHWGSTHDVWVAMTDYDEYALLYTTGTKGLGQDFHMATLYSRTQTPRAEIK
SQ  EKFTTFAKTQGFTEDAIVFLPQTDKCMEEHK
//
ID  Q95L14;
PN  Prostaglandin E synthase;
GN  PTGES;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:O14684}; Multi- pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}.
DR  UNIPROT: Q95L14;
DR  UNIPROT: Q0P5C8;
DR  Pfam: PF01124;
DE  Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15- hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4- dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity). {ECO:0000250|UniProtKB:O14684, ECO:0000250|UniProtKB:Q9JM51}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005641;
GO  GO:0048471;
GO  GO:0043295;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0004667;
GO  GO:0050220;
GO  GO:0008283;
GO  GO:0071347;
GO  GO:0008285;
GO  GO:0032308;
GO  GO:0001516;
GO  GO:0031620;
GO  GO:0050727;
GO  GO:0019233;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O14684};
SQ  MPPSGLELMNGQVLPAFLLCSALLVIKMYVVAVITGQVRLRKKAFANPEDAQRHGGLQYCRNDPDVERCLRAHRNDMETI
SQ  YPFLFLGFVYSFLGPNPFVARMHFLVFFLGRMVHTVAYLGKLRAPTRSLAYTLAQLPCASMALQIVWEAARHL
//
ID  A0SYQ0;
PN  Prostaglandin E synthase;
GN  PTGES;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:O14684}; Multi- pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}.
DR  UNIPROT: A0SYQ0;
DR  Pfam: PF01124;
DE  Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15- hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4- dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity). {ECO:0000250|UniProtKB:O14684, ECO:0000250|UniProtKB:Q9JM51}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005641;
GO  GO:0048471;
GO  GO:0043295;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0004667;
GO  GO:0050220;
GO  GO:0008283;
GO  GO:0008285;
GO  GO:0032308;
GO  GO:0001516;
GO  GO:0031620;
GO  GO:0050727;
GO  GO:0019233;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O14684};
SQ  MPPPVLALVSGQALPAFLLCSTLLVIKMYVVAVITGQVRLRKKAFANPEDALRHGGLQYCRSDQDVDRCLRAHRNDMETI
SQ  YPFLFLGFVYSFLGPDPFIAQMHFLVFFLGRMVHTVAYLGKLRAPTRSLAYTVAQLPCASMALQIVWEAACHL
//
ID  Q8HZJ2;
PN  Prostaglandin E synthase;
GN  PTGES;
OS  9796;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:O14684}; Multi- pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}.
DR  UNIPROT: Q8HZJ2;
DR  Pfam: PF01124;
DE  Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15- hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4- dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity). {ECO:0000250|UniProtKB:O14684, ECO:0000250|UniProtKB:Q9JM51}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005641;
GO  GO:0048471;
GO  GO:0043295;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0004667;
GO  GO:0050220;
GO  GO:0008283;
GO  GO:0008285;
GO  GO:0032308;
GO  GO:0001516;
GO  GO:0031620;
GO  GO:0050727;
GO  GO:0019233;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O14684};
SQ  MPPPSLAMVSGQALPAFLLCSTLLVIKMYAVAVITGQVRLRKKAFANPEDALRHGGLQFHRDDQDVERCLRAHRNDMETI
SQ  YPFLFLGLVYSFLGPDPFVAQMHFLVFFLGRMVHTVAYLGKLRAPTRSLAYTVAQLPCASMALQIVWEAARHL
//
ID  O14684;
PN  Prostaglandin E synthase;
GN  PTGES;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000269|PubMed:10377395, ECO:0000269|PubMed:16439136, ECO:0000269|PubMed:18682561, ECO:0000269|PubMed:27684486}; Multi-pass membrane protein {ECO:0000303|PubMed:18682561}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10869354}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000269|PubMed:10869354}.
DR  UNIPROT: O14684;
DR  UNIPROT: O14900;
DR  UNIPROT: Q5SZC0;
DR  PDB: 3DWW;
DR  PDB: 4AL0;
DR  PDB: 4AL1;
DR  PDB: 4BPM;
DR  PDB: 4WAB;
DR  PDB: 4YK5;
DR  PDB: 4YL0;
DR  PDB: 4YL1;
DR  PDB: 4YL3;
DR  PDB: 5BQG;
DR  PDB: 5BQH;
DR  PDB: 5BQI;
DR  PDB: 5K0I;
DR  PDB: 5T36;
DR  PDB: 5T37;
DR  PDB: 5TL9;
DR  PDB: 6VL4;
DR  Pfam: PF01124;
DR  OMIM: 605172;
DR  DisGeNET: 9536;
DE  Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (PubMed:18682561, PubMed:10377395, PubMed:12672824, PubMed:12460774, PubMed:10869354, PubMed:12244105). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2 (PubMed:12244105, PubMed:12672824). In addition, displays low glutathione transferase and glutathione- dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (PubMed:12672824). {ECO:0000250|UniProtKB:Q9JM51, ECO:0000269|PubMed:10377395, ECO:0000269|PubMed:10869354, ECO:0000269|PubMed:12244105, ECO:0000269|PubMed:12460774, ECO:0000269|PubMed:12672824, ECO:0000269|PubMed:18682561}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q9H0R3; IntAct: EBI-24674609; Score: 0.56
DE  Interaction: Q04941; IntAct: EBI-24686270; Score: 0.56
DE  Interaction: Q9NRQ5; IntAct: EBI-23722140; Score: 0.56
DE  Interaction: Q96IW7; IntAct: EBI-23723397; Score: 0.56
DE  Interaction: Q6PI78; IntAct: EBI-24690855; Score: 0.56
DE  Interaction: Q96F15; IntAct: EBI-23780523; Score: 0.56
DE  Interaction: Q8N6R1; IntAct: EBI-23798787; Score: 0.56
DE  Interaction: O95070; IntAct: EBI-23825176; Score: 0.56
DE  Interaction: Q08426; IntAct: EBI-24755804; Score: 0.56
DE  Interaction: O95292; IntAct: EBI-24784464; Score: 0.56
DE  Interaction: Q8WWP7; IntAct: EBI-24641110; Score: 0.56
DE  Interaction: O15155; IntAct: EBI-24644551; Score: 0.56
DE  Interaction: O75379; IntAct: EBI-24799716; Score: 0.56
DE  Interaction: Q96HH6; IntAct: EBI-25213278; Score: 0.56
DE  Interaction: Q15836; IntAct: EBI-25224808; Score: 0.56
DE  Interaction: Q8WVX3; IntAct: EBI-25273998; Score: 0.56
DE  Interaction: P19739; IntAct: EBI-25685423; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005641;
GO  GO:0048471;
GO  GO:0043295;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0004667;
GO  GO:0050220;
GO  GO:0008283;
GO  GO:0008285;
GO  GO:0032308;
GO  GO:0001516;
GO  GO:0006693;
GO  GO:0031620;
GO  GO:0050727;
GO  GO:0019233;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Curator Inference {ECO:0000305|PubMed:23431194};
SQ  MPAHSLVMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCRSDPDVERCLRAHRNDMETIY
SQ  PFLFLGFVYSFLGPNPFVAWMHFLVFLVGRVAHTVAYLGKLRAPIRSVTYTLAQLPCASMALQILWEAARHL
//
ID  Q6PWL6;
PN  Prostaglandin E synthase;
GN  PTGES;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:O14684}; Multi- pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}.
DR  UNIPROT: Q6PWL6;
DR  Pfam: PF01124;
DE  Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15- hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4- dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity). {ECO:0000250|UniProtKB:O14684, ECO:0000250|UniProtKB:Q9JM51}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0043295;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0050220;
GO  GO:0001516;
GO  GO:0050727;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O14684};
SQ  MPAHSLAMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCRSDPDVERCLRAHRNDMETIY
SQ  PFLFLGFVYSFLGPNPFVAWMHFLVFLLGRVVHTVAYLGKLRAPIRSVTYTLAQLPCASMALQILWEAARHL
//
ID  Q9JM51;
PN  Prostaglandin E synthase;
GN  Ptges;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000269|PubMed:11795891}; Multi- pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}.
DR  UNIPROT: Q9JM51;
DR  UNIPROT: Q3T9C5;
DR  Pfam: PF01124;
DE  Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway (PubMed:10869354, PubMed:11795891). Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (PubMed:11795891, PubMed:10869354). Plays a key role in inflammation response, fever and pain (PubMed:12835414, PubMed:14566340). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4- dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity). {ECO:0000250|UniProtKB:O14684, ECO:0000269|PubMed:10869354, ECO:0000269|PubMed:11795891, ECO:0000269|PubMed:12835414, ECO:0000269|PubMed:14566340}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005641;
GO  GO:0048471;
GO  GO:0043295;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0004667;
GO  GO:0050220;
GO  GO:0008283;
GO  GO:0008285;
GO  GO:0032308;
GO  GO:0001516;
GO  GO:0006693;
GO  GO:0031620;
GO  GO:0050727;
GO  GO:0019233;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O14684};
SQ  MPSPGLVMESGQVLPAFLLCSTLLVIKMYAVAVITGQMRLRKKAFANPEDALKRGGLQYYRSDPDVERCLRAHRNDMETI
SQ  YPFLFLGFVYSFLGPNPLIAWIHFLVVLTGRVVHTVAYLGKLNPRLRSGAYVLAQFSCFSMALQILWEVAHHL
//
ID  Q9JHF3;
PN  Prostaglandin E synthase;
GN  Ptges;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000269|PubMed:11067848}; Multi- pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}.
DR  UNIPROT: Q9JHF3;
DR  Pfam: PF01124;
DE  Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (PubMed:10869354, PubMed:11067848). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5- hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity). {ECO:0000250|UniProtKB:O14684, ECO:0000250|UniProtKB:Q9JM51, ECO:0000269|PubMed:10869354, ECO:0000269|PubMed:11067848}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005641;
GO  GO:0048471;
GO  GO:0043295;
GO  GO:0004602;
GO  GO:0004364;
GO  GO:0004667;
GO  GO:0050220;
GO  GO:0002526;
GO  GO:0008283;
GO  GO:0002544;
GO  GO:0008285;
GO  GO:0032308;
GO  GO:0001516;
GO  GO:0006693;
GO  GO:0031620;
GO  GO:0050727;
GO  GO:0051592;
GO  GO:0034097;
GO  GO:0032496;
GO  GO:0014070;
GO  GO:0032526;
GO  GO:0019233;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O14684};
SQ  MTSLGLVMENSQVLPAFLLCSTLLVIKMYAVAVITGQVRLRKKAFANPEDALKRGGLQYCRSDPDVERCLRAHRNDMETI
SQ  YPFLFLGFVYSFLGPNPLIAWIHFLVVLTGRVVHTVAYLGKMNPRIRSGAYVLAQFACFSMALQILWEVAHHL
//
ID  P35233;
PN  Tyrosine-protein phosphatase non-receptor type 2;
GN  Ptpn2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Targeted to the endoplasmic reticulum by its C-terminal hydrophobic region. {ECO:0000250}. [Isoform 1]: Endoplasmic reticulum {ECO:0000269|PubMed:8900155}. Nucleus membrane {ECO:0000269|PubMed:8900155}. [Isoform 2]: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Predominantly localizes to chromatin. Able to shuttle between the nucleus and the cytoplasm and to dephosphorylate plasma membrane receptors. Recruited by activated ITGA1 at the plasma membrane (By similarity). {ECO:0000250}.
DR  UNIPROT: P35233;
DR  Pfam: PF00102;
DR  PROSITE: PS00383;
DR  PROSITE: PS50056;
DR  PROSITE: PS50055;
DE  Function: Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3 and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T- cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. In addition to the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Also plays an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. May also bind DNA (By similarity). {ECO:0000250|UniProtKB:P17706}.
DE  Reference Proteome: Yes;
DE  Interaction: Q63584; IntAct: EBI-4409899; Score: 0.27
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0003677;
GO  GO:0005178;
GO  GO:0004726;
GO  GO:0019901;
GO  GO:0004725;
GO  GO:0030971;
GO  GO:0097677;
GO  GO:0019905;
GO  GO:0030183;
GO  GO:0030218;
GO  GO:0042593;
GO  GO:0008286;
GO  GO:0008285;
GO  GO:0050922;
GO  GO:0042059;
GO  GO:0070373;
GO  GO:0050728;
GO  GO:0046627;
GO  GO:0060336;
GO  GO:1902206;
GO  GO:1902215;
GO  GO:0070104;
GO  GO:0010888;
GO  GO:1902227;
GO  GO:0045650;
GO  GO:2000587;
GO  GO:1902233;
GO  GO:0061099;
GO  GO:0046426;
GO  GO:0050860;
GO  GO:0000122;
GO  GO:0010804;
GO  GO:0060339;
GO  GO:0042532;
GO  GO:0035335;
GO  GO:1902237;
GO  GO:0045722;
GO  GO:1903899;
GO  GO:0006470;
GO  GO:1902202;
GO  GO:0030217;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSATIEREFEELDAQCRWQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSAENDYINASLVDIEEAQ
SQ  RSYILTQGPLPNTCCHFWLMVWQQKTRAVVMLNRTVEKESVKCAQYWPTDDREMVFKETGFSVKLLSEDVKSYYTVHLLQ
SQ  LENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGE
SQ  DVNVKQILLSMRKYRMGLIQTPDQLRFSYMAIIEGAKYTKGDSNIQKRWKELSKEDLSPVCRHSQNRTMTEKYNGKRIGS
SQ  EDEKLTGLSSKVPDTVEESSESILRKRIREDRKATTAQKVQQMRQRLNETERKRKRWLYWQPILTKMGFVSVILVGALVG
SQ  WTLLFQLNVLPRLTDT
//
ID  A4IFC9;
PN  Prostate tumor-overexpressed gene 1 protein homolog;
GN  PTOV1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q86YD1}. Nucleus {ECO:0000250|UniProtKB:Q86YD1}. Cell membrane {ECO:0000250|UniProtKB:Q86YD1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86YD1}. Note=Translocates from the cytoplasm to the nucleus at the onset of S-phase. Also localizes to lipid rafts. {ECO:0000250|UniProtKB:Q86YD1}.
DR  UNIPROT: A4IFC9;
DR  Pfam: PF11232;
DE  Function: May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation. {ECO:0000250|UniProtKB:Q86YD1}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005667;
GO  GO:0045944;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRPRRAPHRSGAGGPLGGRGRPLRPFTARAARSRSWPASPRGPQPPRIRARSAPPMQGARVFGALGPIGPSSPGLALGG
SQ  LAVGEHRLSNKLLAWSGVLEWQEKRRPYSDSTAKLKRALPCQAYVNQGENLETDQWPQKLIMQLIPQQLLTTLGPLFRNS
SQ  QLAQFHFTNRDCDSLKGLCRVMGNGFAGCMLFPHISPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVNAIRQVITTRKQAV
SQ  GPGGVAGPVQIVNNKFLAWSGVMEWQEPRPEPHSRSKRWLPSHIYVNQGEILRTEQWPRKLYMQLIPQQLLTTLVPLFRN
SQ  SRLVQFHFTKDLETLKSLCRIMDNGFAGCVHFSYKASCEVRVLMLLYSSEKKIFIGLIPHDQSNFVNGIRRVIANQQQVL
SQ  QRNLEQEQQQRGMGG
//
ID  Q86YD1;
PN  Prostate tumor-overexpressed gene 1 protein;
GN  PTOV1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12598323, ECO:0000269|PubMed:16639697}. Nucleus {ECO:0000269|PubMed:12598323, ECO:0000269|PubMed:15713644}. Cell membrane {ECO:0000269|PubMed:15713644}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11313889}. Note=Translocates from the cytoplasm to the nucleus at the onset of S-phase (PubMed:12598323). Also localizes to lipid rafts (PubMed:15713644). {ECO:0000269|PubMed:12598323, ECO:0000269|PubMed:15713644}.
DR  UNIPROT: Q86YD1;
DR  UNIPROT: Q6UXX7;
DR  UNIPROT: Q96BU3;
DR  UNIPROT: Q9HBN4;
DR  UNIPROT: Q9NYL1;
DR  Pfam: PF11232;
DR  OMIM: 610195;
DR  DisGeNET: 53635;
DE  Function: May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation. {ECO:0000269|PubMed:12598323, ECO:0000269|PubMed:15713644, ECO:0000269|PubMed:17641689}.
DE  Reference Proteome: Yes;
DE  Interaction: Q08495; IntAct: EBI-735504; Score: 0.00
DE  Interaction: Q13526; IntAct: EBI-735507; Score: 0.00
DE  Interaction: Q13813; IntAct: EBI-735510; Score: 0.00
DE  Interaction: O75069; IntAct: EBI-737468; Score: 0.00
DE  Interaction: P31947; IntAct: EBI-7544614; Score: 0.40
DE  Interaction: Q14457; IntAct: EBI-3257986; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: O75901; IntAct: EBI-6912184; Score: 0.35
DE  Interaction: Q16659; IntAct: EBI-12502733; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-11003456; Score: 0.35
DE  Interaction: O94776; IntAct: EBI-11903853; Score: 0.00
DE  Interaction: Q13547; IntAct: EBI-11912782; Score: 0.00
DE  Interaction: P48380; IntAct: EBI-11921171; Score: 0.00
DE  Interaction: Q9H1B5; IntAct: EBI-11931253; Score: 0.00
DE  Interaction: Q9Y3I0; IntAct: EBI-11940521; Score: 0.00
DE  Interaction: Q8IYS4; IntAct: EBI-21565697; Score: 0.35
DE  Interaction: Q9Y2U9; IntAct: EBI-21781475; Score: 0.35
DE  Interaction: P40855; IntAct: EBI-21782948; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-21902679; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: P51679; IntAct: EBI-20804528; Score: 0.37
DE  Interaction: P0DTC9; IntAct: EBI-27127583; Score: 0.35
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005667;
GO  GO:0045944;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRPRRAPYRSGAGGPLGGRGRPPRPLVVRAVRSRSWPASPRGPQPPRIRARSAPPMEGARVFGALGPIGPSSPGLTLGG
SQ  LAVSEHRLSNKLLAWSGVLEWQEKRRPYSDSTAKLKRTLPCQAYVNQGENLETDQWPQKLIMQLIPQQLLTTLGPLFRNS
SQ  QLAQFHFTNRDCDSLKGLCRIMGNGFAGCMLFPHISPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVSAIRQVITTRKQAV
SQ  GPGGVNSGPVQIVNNKFLAWSGVMEWQEPRPEPNSRSKRWLPSHVYVNQGEILRTEQWPRKLYMQLIPQQLLTTLVPLFR
SQ  NSRLVQFHFTKDLETLKSLCRIMDNGFAGCVHFSYKASCEIRVLMLLYSSEKKIFIGLIPHDQGNFVNGIRRVIANQQQV
SQ  LQRNLEQEQQQRGMGG
//
ID  Q91VU8;
PN  Prostate tumor-overexpressed gene 1 protein homolog;
GN  Ptov1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q86YD1}. Nucleus {ECO:0000250|UniProtKB:Q86YD1}. Cell membrane {ECO:0000250|UniProtKB:Q86YD1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86YD1}. Note=Translocates from the cytoplasm to the nucleus at the onset of S-phase. Also localizes to lipid rafts. {ECO:0000250|UniProtKB:Q86YD1}.
DR  UNIPROT: Q91VU8;
DR  UNIPROT: Q9CTC2;
DR  Pfam: PF11232;
DE  Function: May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation. {ECO:0000250|UniProtKB:Q86YD1}.
DE  Reference Proteome: Yes;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005667;
GO  GO:0045944;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRPRRAPHRSGAGGPLGGRGRPPRPLVVRAVRSRSWPGGPRGPQPPRIRARSAPPMEGARVFGALGPIGPSSPGLTLGG
SQ  LAVNEHRLSNKLLAWSGVLEWQEKRRPFSDSTAKLKRTLPCQAYVNQGENLETDQWPQKLIMQLIPQQLLTTLGPLFRNS
SQ  QLAQFHFTNRDCDSLKGLCRIMGNGFAGCMLFPHISPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVNAIRQVITTRKQAV
SQ  GPGGVHSGPVQIVNNKFLAWSGVMEWQEPRPEPNSRSKRWLPSHVYVNQGEILRTDQWPRRLFMQLIPQQLLTTLVPLFR
SQ  NSRLVQFHFTKDMETLKSLCRIMDNGFAGCVHFSYKASCEVRVLMLLYSSEKKIFIGLIPHDQSNFVNGIRRVIANQQQV
SQ  LQRSLEQEQQQRGMGG
//
ID  Q15256;
PN  Receptor-type tyrosine-protein phosphatase R;
GN  PTPRR;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: [Isoform Alpha]: Cell membrane; Single-pass type I membrane protein. [Isoform Delta]: Cytoplasm, perinuclear region. Note=Locates to the perinuclear areas within the cytoplasm. [Isoform Gamma]: Cytoplasm, perinuclear region. Note=Locates to the perinuclear areas within the cytoplasm.
DR  UNIPROT: Q15256;
DR  UNIPROT: B2R5Z7;
DR  UNIPROT: B7Z3J1;
DR  UNIPROT: F5GXR7;
DR  UNIPROT: O00342;
DR  UNIPROT: Q92682;
DR  UNIPROT: Q9UE65;
DR  PDB: 2A8B;
DR  Pfam: PF00102;
DR  PROSITE: PS00383;
DR  PROSITE: PS50056;
DR  PROSITE: PS50055;
DR  OMIM: 602853;
DR  DisGeNET: 5801;
DE  Function: Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-20980716; Score: 0.37
DE  Interaction: P02545; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-20977323; Score: 0.51
DE  Interaction: P42704; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q15256; IntAct: EBI-7670318; Score: 0.31
DE  Interaction: P19022; IntAct: EBI-2265623; Score: 0.00
DE  Interaction: P09619; IntAct: EBI-2265708; Score: 0.00
DE  Interaction: Q16539; IntAct: EBI-16067405; Score: 0.65
DE  Interaction: P28482; IntAct: EBI-7157244; Score: 0.58
DE  Interaction: Q9H0R8; IntAct: EBI-24684656; Score: 0.56
DE  Interaction: P06213; IntAct: EBI-21132493; Score: 0.51
DE  Interaction: Q8IWU2; IntAct: EBI-20979781; Score: 0.37
DE  Interaction: Q6ZMQ8; IntAct: EBI-20980062; Score: 0.37
DE  Interaction: Q15303; IntAct: EBI-20980546; Score: 0.37
DE  Interaction: P21860; IntAct: EBI-20980866; Score: 0.37
DE  Interaction: Q02763; IntAct: EBI-20981106; Score: 0.37
DE  Interaction: Q01973; IntAct: EBI-20981500; Score: 0.37
DE  Interaction: P07949; IntAct: EBI-20981400; Score: 0.37
DE  Interaction: P34925; IntAct: EBI-20981440; Score: 0.37
DE  Interaction: Q01974; IntAct: EBI-20981640; Score: 0.37
DE  Interaction: P08069; IntAct: EBI-20981970; Score: 0.37
DE  Interaction: Q13308; IntAct: EBI-20982240; Score: 0.37
DE  Interaction: P29317; IntAct: EBI-20982664; Score: 0.37
DE  Interaction: Q62190; IntAct: EBI-21223151; Score: 0.37
DE  Interaction: P04629; IntAct: EBI-21224974; Score: 0.37
DE  Interaction: P21802; IntAct: EBI-21226905; Score: 0.37
DE  Interaction: P22455; IntAct: EBI-21227046; Score: 0.37
DE  Interaction: P35968; IntAct: EBI-21227083; Score: 0.37
DE  Interaction: P17987; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: P19338; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: P78371; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: Q13610; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: Q5VZ46; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: Q6P5R6; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: Q9BQ67; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: Q9NSD9; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: Q9NUL7; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: Q9NVI7; IntAct: EBI-25383510; Score: 0.35
DE  Interaction: O60783; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: O75688; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P07237; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P23528; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P31153; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P42166; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P56134; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P63261; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P82650; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P82673; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P82675; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P82914; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: P82930; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q02978; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q15149; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q16875; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q7L014; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q8NCE2; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q92552; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q92665; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q96EY1; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q96EY7; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9BU76; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9GZT3; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9H3K6; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9NWB6; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9NXV2; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9ULV4; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9Y291; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9Y2Q9; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9Y2R9; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9Y399; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q9Y3D9; IntAct: EBI-25393868; Score: 0.35
DE  Interaction: Q96F44; IntAct: EBI-27115100; Score: 0.35
DE  Interaction: Q9UL42; IntAct: EBI-27115100; Score: 0.42
DE  Interaction: P27361; IntAct: EBI-27115100; Score: 0.35
DE  Interaction: P49366; IntAct: EBI-27115100; Score: 0.35
DE  Interaction: P54886; IntAct: EBI-27115100; Score: 0.35
DE  Interaction: Q9UNH7; IntAct: EBI-27116713; Score: 0.27
DE  Interaction: O75165; IntAct: EBI-27116713; Score: 0.27
DE  Interaction: Q92609; IntAct: EBI-27116713; Score: 0.27
DE  Interaction: Q12768; IntAct: EBI-27116713; Score: 0.27
GO  GO:0030054;
GO  GO:0005829;
GO  GO:0005615;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0019901;
GO  GO:0004725;
GO  GO:0005001;
GO  GO:0038128;
GO  GO:0001701;
GO  GO:0010633;
GO  GO:0070373;
GO  GO:0035335;
GO  GO:0006470;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRAVCFPALCLLLNLHAAGCFSGNNDHFLAINQKKSGKPVFIYKHSQDIEKSLDIAPQKIYRHSYHSSSEAQVSKRHQI
SQ  VNSAFPRPAYDPSLNLLAMDGQDLEVENLPIPAANVIVVTLQMDVNKLNITLLRIFRQGVAAALGLLPQQVHINRLIGKK
SQ  NSIELFVSPINRKTGISDALPSEEVLRSLNINVLHQSLSQFGITEVSPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFVI
SQ  IVTCLMILYRLKERFQLSLRQDKEKNQEIHLSPITLQPALSEAKTVHSMVQPEQAPKVLNVVVDPQGRGAPEIKATTATS
SQ  VCPSPFKMKPIGLQERRGSNVSLTLDMSSLGNIEPFVSIPTPREKVAMEYLQSASRILTRSQLRDVVASSHLLQSEFMEI
SQ  PMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMV
SQ  WQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDS
SQ  AQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFV
SQ  HHALCLYESRLSAETVQ
//
ID  Q5U2W6;
PN  Prostate tumor-overexpressed gene 1 protein homolog;
GN  Ptov1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q86YD1}. Nucleus {ECO:0000250|UniProtKB:Q86YD1}. Cell membrane {ECO:0000250|UniProtKB:Q86YD1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86YD1}. Note=Translocates from the cytoplasm to the nucleus at the onset of S-phase. Also localizes to lipid rafts. {ECO:0000250|UniProtKB:Q86YD1}.
DR  UNIPROT: Q5U2W6;
DR  Pfam: PF11232;
DE  Function: May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation. {ECO:0000250|UniProtKB:Q86YD1}.
DE  Reference Proteome: Yes;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005667;
GO  GO:0045944;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVRPRRAPHRSGAGGPLGGRGRPPRPLVVRAVRSRSWPAGPRGPQPPRIRARSAPPMEGARVFGALGPIGPSSPGLTLGG
SQ  LAVNEHRLSNKLLAWSGVLEWQEKRRPFSDSAAKLKRTLPCQAYVNQGENLETDQWPQKLIMQLIPQQLLTTLGPLFRNS
SQ  QLAQFHFTNRDCDSLKGLCRIMGNGFAGCMLFPHISPCEVRVLMLLYSSKKKIFMGLIPYDQSGFVNAIRQVITTRKQAV
SQ  GPGGVHSGPVQIVNNKFLAWSGVMEWQEPRPEPNSRSKRWLPSHVYVNQGEILRTDQWPRRLFMQLIPQQLLTTLVPLFR
SQ  NSRLVQFHFTKDMETLKSLCRIMDNGFAGCVHFSYKASCEVRVLMLLYSSEKKIFIGLIPHDQSNFVNGIRRVIANQQQV
SQ  LQRSLEQEQQQRGMGG
//
ID  Q8TB72;
PN  Pumilio homolog 2;
GN  PUM2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000305|PubMed:19168546}. Cytoplasmic granule {ECO:0000269|PubMed:25340845}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19168546}. Note=The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS3 in the stress granules. Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ cells. {ECO:0000269|PubMed:25340845}.
DR  UNIPROT: Q8TB72;
DR  UNIPROT: B3KSL0;
DR  UNIPROT: B4E2B6;
DR  UNIPROT: D6W527;
DR  UNIPROT: O00234;
DR  UNIPROT: Q53TV7;
DR  UNIPROT: Q8WY43;
DR  UNIPROT: Q9HAN2;
DR  PDB: 3Q0Q;
DR  PDB: 3Q0R;
DR  PDB: 3Q0S;
DR  Pfam: PF00806;
DR  PROSITE: PS50302;
DR  PROSITE: PS50303;
DR  OMIM: 607205;
DR  DisGeNET: 23369;
DE  Function: Sequence-specific RNA-binding protein that acts as a post- transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'- UGUANAUA-3', that is related to the Nanos Response Element (NRE) (, PubMed:21397187). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation- independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:22345517). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm (PubMed:26724866). May regulate DCUN1D3 mRNA levels (PubMed:25349211). May support proliferation and self-renewal of stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A expression at a postranscriptional level (PubMed:28431233). {ECO:0000269|PubMed:18776931, ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:22345517, ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26724866, ECO:0000269|PubMed:28431233}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9ULK4; IntAct: EBI-311679; Score: 0.37
DE  Interaction: Q9NQZ3; IntAct: EBI-997951; Score: 0.51
DE  Interaction: Q8ZJF3; IntAct: EBI-2860212; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q9H1Y0; IntAct: EBI-3622507; Score: 0.35
DE  Interaction: Q9Q2G4; IntAct: EBI-6174875; Score: 0.56
DE  Interaction: Q6SPF0; IntAct: EBI-11160311; Score: 0.35
DE  Interaction: Q8IUH3; IntAct: EBI-11161115; Score: 0.35
DE  Interaction: P47902; IntAct: EBI-21581572; Score: 0.35
DE  Interaction: O43251; IntAct: EBI-21595758; Score: 0.35
DE  Interaction: Q99732; IntAct: EBI-21643847; Score: 0.35
DE  Interaction: Q12905; IntAct: EBI-21665924; Score: 0.35
DE  Interaction: Q12926; IntAct: EBI-21666158; Score: 0.35
DE  Interaction: Q8N2M8; IntAct: EBI-21714908; Score: 0.35
DE  Interaction: Q8N6W0; IntAct: EBI-21727590; Score: 0.35
DE  Interaction: Q96SI9; IntAct: EBI-21752787; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q92904; IntAct: EBI-27095486; Score: 0.37
DE  Interaction: Q8N9W6; IntAct: EBI-27095489; Score: 0.51
DE  Interaction: Q8TB72; IntAct: EBI-27095542; Score: 0.40
DE  Interaction: Q9BZB8; IntAct: EBI-29014562; Score: 0.27
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0106222;
GO  GO:0035198;
GO  GO:0003730;
GO  GO:0003729;
GO  GO:0062104;
GO  GO:0003723;
GO  GO:0060612;
GO  GO:0051276;
GO  GO:0001942;
GO  GO:0035196;
GO  GO:0007005;
GO  GO:2000637;
GO  GO:1900246;
GO  GO:0010608;
GO  GO:0051983;
GO  GO:0060964;
GO  GO:0043488;
GO  GO:0006417;
GO  GO:0022904;
GO  GO:0001501;
GO  GO:0034063;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNHDFQALALESRGMGELLPTKKFWEPDDSTKDGQKGIFLGDDEWRETAWGASHHSMSQPIMVQRRSGQGFHGNSEVNAI
SQ  LSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRG
SQ  LPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYP
SQ  GNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPG
SQ  TDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQG
SQ  QQGQQAESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAA
SQ  AAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLG
SQ  AAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPS
SQ  LSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFP
SQ  NLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIR
SQ  GHVLPLALQMYGCRVIQKALESISSDQQVISEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVL
SQ  STHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASN
SQ  VVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHI
SQ  LAKLEKYYLKNSPDLGPIGGPPNGML
//
ID  Q80U58;
PN  Pumilio homolog 2;
GN  Pum2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000305|PubMed:19861488}. Cytoplasmic granule {ECO:0000269|PubMed:19861488}. Cytoplasm, perinuclear region {ECO:0000250}. Note=The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ cells (By similarity). Colocalizes with NANOS3 in the stress granules (PubMed:19861488). {ECO:0000250|UniProtKB:Q8TB72, ECO:0000269|PubMed:19861488}.
DR  UNIPROT: Q80U58;
DR  UNIPROT: Q80UZ9;
DR  UNIPROT: Q91YW4;
DR  UNIPROT: Q925A0;
DR  UNIPROT: Q9ERC7;
DR  PDB: 3GVO;
DR  PDB: 3GVT;
DR  Pfam: PF00806;
DR  PROSITE: PS50302;
DR  PROSITE: PS50303;
DE  Function: Sequence-specific RNA-binding protein that acts as a post- transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'- UGUANAUA-3', that is related to the Nanos Response Element (NRE). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Also mediates deadenylation-independent repression by promoting accessibility of miRNAs. Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation. Plays a role in cytoplasmic sensing of viral infection. Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm. May regulate DCUN1D3 mRNA levels. May support proliferation and self-renewal of stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A expression at a postranscriptional level (By similarity). {ECO:0000250|UniProtKB:Q8TB72}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NQZ3; IntAct: EBI-998084; Score: 0.40
DE  Interaction: Q80Z64; IntAct: EBI-8820601; Score: 0.35
DE  Interaction: Q8CJG0; IntAct: EBI-9030750; Score: 0.35
DE  Interaction: P35637; IntAct: EBI-25423814; Score: 0.35
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0106222;
GO  GO:0035198;
GO  GO:0003730;
GO  GO:0003729;
GO  GO:0062104;
GO  GO:0003723;
GO  GO:0060612;
GO  GO:0051276;
GO  GO:0001942;
GO  GO:0035196;
GO  GO:0007005;
GO  GO:2000637;
GO  GO:1900246;
GO  GO:0010608;
GO  GO:0051983;
GO  GO:0043488;
GO  GO:0006417;
GO  GO:0022904;
GO  GO:0001501;
GO  GO:0034063;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNHDFQALALESRGMGELLPTKKFWEPDDSTKDGQKGIFLGDDEWRETAWGTSHHSMSQPIMVQRRSGQSFHGNSEVNAI
SQ  LSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGTFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQDDEDSKINGRGL
SQ  PNGMDADCKDFNRTPGSRQASPTEVVERLGPSTNPPEGLGPLPNPTANKPLVEEFSNPETQNLDAMDQVGLDSLQFDYPG
SQ  NQVPMDSSGATVGLFDYNSQQQLFQRTSALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGT
SQ  DPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAASNTANQQAASQAQPGQQQVLRPGAGQRPITPSQGQ
SQ  QGQQAESLAAAANPTLAFGQSLAAGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSTAAQAAAAAA
SQ  AAGGTANSLTGSTNGLFRPIGTQPPQQQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSASLGFGSGSSLG
SQ  AAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPS
SQ  LSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFP
SQ  NLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQIVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIR
SQ  GHVLPLALQMYGCRVIQKALESISSDQQVISEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVL
SQ  STHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASN
SQ  VVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHI
SQ  LAKLEKYYLKNSPDLGPIGGPPNGML
//
ID  Q9H0J4;
PN  Glutamine-rich protein 2;
GN  QRICH2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q3V2A7}. Nucleus {ECO:0000250|UniProtKB:Q3V2A7}. Cytoplasm {ECO:0000250|UniProtKB:Q3V2A7}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:30683861}. Note=Localization varies during spermatozoa development. The protein is distributed in the nuclear membrane of the spermatogonia, in the nucleus of round spermatids, in the nucleus and cytoplasm of early elongating spermatids, in the cytoplasm of late elongating spermatids, and in the flagella of epididymal spermatozoa. {ECO:0000250|UniProtKB:Q3V2A7}.
DR  UNIPROT: Q9H0J4;
DR  UNIPROT: A2RRE1;
DR  UNIPROT: Q96LM3;
DR  Pfam: PF16043;
DR  OMIM: 618304;
DR  OMIM: 618341;
DR  DisGeNET: 84074;
DE  Function: Has an essential role in the formation of sperm flagella and flagellar structure maintainance. It acts as a suppressor of ubiquitination and degradation of proteins involved in flagellar development and motility. {ECO:0000269|PubMed:30683861}.
DE  Disease: Spermatogenic failure 35 (SPGF35) [MIM:618341]: An autosomal recessive infertility disorder caused by spermatogenesis defects that result in multiple abnormalities of sperm flagellum and severely impaired spermatozoa motility. {ECO:0000269|PubMed:30683861}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P04406; IntAct: EBI-1078469; Score: 0.00
DE  Interaction: P52948; IntAct: EBI-1065782; Score: 0.00
DE  Interaction: Q05397; IntAct: EBI-30836888; Score: 0.44
DE  Interaction: O75352; IntAct: EBI-1062069; Score: 0.00
DE  Interaction: Q9BZ23; IntAct: EBI-1065962; Score: 0.00
DE  Interaction: Q53HC9; IntAct: EBI-1069347; Score: 0.00
DE  Interaction: O15479; IntAct: EBI-1072707; Score: 0.00
DE  Interaction: O60232; IntAct: EBI-1077857; Score: 0.00
DE  Interaction: O95863; IntAct: EBI-1084094; Score: 0.00
DE  Interaction: Q9UMN6; IntAct: EBI-16072132; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21390114; Score: 0.00
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0036126;
GO  GO:0030031;
GO  GO:0030317;
GO  GO:2000059;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKDAAEELSFARVLLQRVDELEKLFKDREQFLELVSRKLSLVPGAEEVTMVTWEELEQAITDGWRASQAGSETLMGFSKH
SQ  GGFTSLTSPEGTLSGDSTKQPSIEQALDSASGLGPDRTASGSGGTAHPSDGVSSREQSKVPSGTGRQQQPRARDEAGVPR
SQ  LHQSSTFQFKSDSDRHRSREKLTSTQPRRNARPGPVQQDLPLARDQPSSVPASQSQVHLRPDRRGLEPTGMNQPGLVPAS
SQ  TYPHGVVPLSMGQLGVPPPEMDDRELIPFVVDEQRMLPPSVPGRDQQGLELPSTDQHGLVSVSAYQHGMTFPGTDQRSME
SQ  PLGMDQRGCVISGMGQQGLVPPGIDQQGLTLPVVDQHGLVLPFTDQHGLVSPGLMPISADQQGFVQPSLEATGFIQPGTE
SQ  QHDLIQSGRFQRALVQRGAYQPGLVQPGADQRGLVRPGMDQSGLAQPGADQRGLVWPGMDQSGLAQPGRDQHGLIQPGTG
SQ  QHDLVQSGTGQGVLVQPGVDQPGMVQPGRFQRALVQPGAYQPGLVQPGADQIDVVQPGADQHGLVQSGADQSDLAQPGAV
SQ  QHGLVQPGVDQRGLAQPRADHQRGLVPPGADQRGLVQPGADQHGLVQPGVDQHGLAQPGEVQRSLVQPGIVQRGLVQPGA
SQ  VQRGLVQPGAVQRGLVQPGVDQRGLVQPGAVQRGLVQPGAVQHGLVQPGADQRGLVQPGVDQRGLVQPGVDQRGLVQPGM
SQ  DQRGLIQPGADQPGLVQPGAGQLGMVQPGIGQQGMVQPQADPHGLVQPGAYPLGLVQPGAYLHDLSQSGTYPRGLVQPGM
SQ  DQYGLRQPGAYQPGLIAPGTKLRGSSTFQADSTGFISVRPYQHGMVPPGREQYGQVSPLLASQGLASPGIDRRSLVPPET
SQ  YQQGLMHPGTDQHSPIPLSTGLGSTHPDQQHVASPGPGEHDQVYPDAAQHGHAFSLFDSHDSMYPGYRGPGYLSADQHGQ
SQ  EGLDPNRTRASDRHGIPAQKAPGQDVTLFRSPDSVDRVLSEGSEVSSEVLSERRNSLRRMSSSFPTAVETFHLMGELSSL
SQ  YVGLKESMKDLDEEQAGQTDLEKIQFLLAQMVKRTIPPELQEQLKTVKTLAKEVWQEKAKVERLQRILEGEGNQEAGKEL
SQ  KAGELRLQLGVLRVTVADIEKELAELRESQDRGKAAMENSVSEASLYLQDQLDKLRMIIESMLTSSSTLLSMSMAPHKAH
SQ  TLAPGQIDPEATCPACSLDVSHQVSTLVRRYEQLQDMVNSLAVSRPSKKAKLQRQDEELLGRVQSAILQVQGDCEKLNIT
SQ  TSNLIEDHRQKQKDIAMLYQGLEKLEKEKANREHLEMEIDVKADKSALATKVSRVQFDATTEQLNHMMQELVAKMSGQEQ
SQ  DWQKMLDRLLTEMDNKLDRLELDPVKQLLEDRWKSLRQQLRERPPLYQADEAAAMRRQLLAHFHCLSCDRPLETPVTGHA
SQ  IPVTPAGPGLPGHHSIRPYTVFELEQVRQHSRNLKLGSAFPRGDLAQMEQSVGRLRSMHSKMLMNIEKVQIHFGGSTKAS
SQ  SQIIRELLHAQCLGSPCYKRVTDMADYTYSTVPRRCGGSHTLTYPYHRSRPQHLPRGLYPTEEIQIAMKHDEVDILGLDG
SQ  HIYKGRMDTRLPGILRKDSSGTSKRKSQQPRPHVHRPPSLSSNGQLPSRPQSAQISAGNTSER
//
ID  Q3V2A7;
PN  Glutamine-rich protein 2;
GN  Qrich2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:30683861}. Nucleus {ECO:0000269|PubMed:30683861}. Cytoplasm {ECO:0000269|PubMed:30683861}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:30683861}. Note=Localization varies during spermatozoa development. The protein is distributed in the nuclear membrane of the spermatogonia, in the nucleus of round spermatids, in the nucleus and cytoplasm of early elongating spermatids, in the cytoplasm of late elongating spermatids, and in the flagella of epididymal spermatozoa. {ECO:0000269|PubMed:30683861}.
DR  UNIPROT: Q3V2A7;
DR  UNIPROT: B9EKM0;
DR  Pfam: PF16043;
DE  Function: Has an essential role in the formation of sperm flagella and flagellar structure maintainance. It acts as a suppressor of ubiquitination and degradation of proteins involved in flagellar development and motility. {ECO:0000269|PubMed:30683861}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0036126;
GO  GO:0030031;
GO  GO:0030317;
GO  GO:2000059;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENSVSEASLYLQDQLDKLRTIIESMLGSSSTLLSMSITPHKSTACLVPGQIDPEATCPACSLDVSHQVSLLVQRYEQLQ
SQ  DMVSGLAASRPSKKAKLQGQDEELLGHVQSAILQVQGDCEKLNITTSNLIEDHRQKQKDIEVLYQGIERLDKEKANREHL
SQ  EMEIDEKADKSALASKVSRIQFDATTEQLNHMMQELVAKMSGQEQDWQKLLDKLLAEMDSKLDRLELDPLKQMLEDRWKS
SQ  LRQQLKERPPLYQADEAAAMRRQLLAHFHCLSCDRPLETTVTGQVISVTPIISSMPGHRSVRPYTVFELEQIRQQSRNLK
SQ  LGSSFPRVDMSQMERSVGRLHSMHSRMLMDMEKVQVHFGGSVKASSQMIRELLHTQCLSHPCYKRGADTADYSYSTVSRR
SQ  CGGSHTLTYPYRRNRPQHLSPLEEIQIAMKHDEVDILGLDGHIYKGRMDTRLPGILGKDAPGVTKHNKAKLQQLQQLQQL
SQ  QQLQQLQQLQQAQHARPHAHRQPSLGNMISPPSRPQSAQMIADSKAVPSGQKKDRPVSSEGRLLQSNVSHSSIPTDIASL
SQ  QGSQQGLNMHIDVPPGEGLEEPTRGPRSTAAH
//
ID  Q6ZRP7;
PN  Sulfhydryl oxidase 2;
GN  QSOX2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000269|PubMed:14633699}; Single- pass membrane protein {ECO:0000269|PubMed:14633699}. Secreted {ECO:0000269|PubMed:14633699}. Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000305}; Single- pass membrane protein {ECO:0000305}. Note=Seems to be predominantly targeted to the nuclear and outer plasma membrane.
DR  UNIPROT: Q6ZRP7;
DR  UNIPROT: A2CEE0;
DR  UNIPROT: A6NLB0;
DR  UNIPROT: Q5TB37;
DR  UNIPROT: Q7Z7B6;
DR  UNIPROT: Q86VV7;
DR  UNIPROT: Q8N3G2;
DR  Pfam: PF04777;
DR  Pfam: PF18371;
DR  Pfam: PF18108;
DR  Pfam: PF00085;
DR  PROSITE: PS51324;
DR  PROSITE: PS51352;
DR  OMIM: 612860;
DR  DisGeNET: 169714;
DE  Function: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. Also seems to play a role in regulating the sensitization of neuroblastoma cells for interferon-gamma-induced apoptosis. {ECO:0000269|PubMed:14633699}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: P0C6X7; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q99614; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q5VYS8; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q9C0F1; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q8IZH2; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q86YS7; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q12824; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q9UBD5; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: F8VY35; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q9P2X3; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q9Y6K0; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q8TB52; IntAct: EBI-11127397; Score: 0.35
DE  Interaction: Q20MH8; IntAct: EBI-12586007; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: P20036; IntAct: EBI-21511890; Score: 0.35
DE  Interaction: Q9NRD5; IntAct: EBI-21519718; Score: 0.35
DE  Interaction: P05161; IntAct: EBI-16720078; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: Q9H5K3; IntAct: EBI-28948637; Score: 0.35
DE  Interaction: P08069; IntAct: EBI-32718669; Score: 0.35
DE  Interaction: P06213; IntAct: EBI-32718777; Score: 0.35
DE  Interaction: Q16288; IntAct: EBI-32719212; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-32719373; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-32719716; Score: 0.35
GO  GO:0005615;
GO  GO:0005794;
GO  GO:0030173;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005886;
GO  GO:0016971;
GO  GO:0003756;
GO  GO:0006457;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAAGAAVARSPGIGAGPALRARRSPPPRAARLPRLLVLLAAAAVGPGAGGAARLYRAGEDAVWVLDSGSVRGATANSSA
SQ  AWLVQFYSSWCGHCIGYAPTWRALAGDVRDWASAIRVAALDCMEEKNQAVCHDYDIHFYPTFRYFKAFTKEFTTGENFKG
SQ  PDRELRTVRQTMIDFLQNHTEGSRPPACPRLDPIQPSDVLSLLDNRGSHYVAIVFESNSSYLGREVILDLIPYESIVVTR
SQ  ALDGDKAFLEKLGVSSVPSCYLIYPNGSHGLINVVKPLRAFFSSYLKSLPDVRKKSLPLPEKPHKEENSEIVVWREFDKS
SQ  KLYTVDLESGLHYLLRVELAAHKSLAGAELKTLKDFVTVLAKLFPGRPPVKKLLEMLQEWLASLPLDRIPYNAVLDLVNN
SQ  KMRISGIFLTNHIKWVGCQGSRSELRGYPCSLWKLFHTLTVEASTHPDALVGTGFEDDPQAVLQTMRRYVHTFFGCKECG
SQ  EHFEEMAKESMDSVKTPDQAILWLWKKHNMVNGRLAGHLSEDPRFPKLQWPTPDLCPACHEEIKGLASWDEGHVLTFLKQ
SQ  HYGRDNLLDTYSADQGDSSEGGTLARGEEEEKRLTPPEVSHGDRDTQSVRPPGALGPRPALPESLHHSLDGKLQSLDGPG
SQ  AHKEVGGAAPFLGVDFSSLDMSLCVVLYVASSLFLMVMYFFFRVRSRRWKVKHHHPAV
//
ID  P0C6W1;
PN  2'-O-methyltransferase;
GN  rep;
OS  389230;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W1;
DR  UNIPROT: Q0Q4F3;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:19264783}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLSKAGVTTQGARGKYRAELYNEKRSDHVACTVPLCDTEDMASKLTPWFEDGETAFNQVSSILKEKGKILFVPMHMQRAM
SQ  KFLPGPRVYLVERLTGGMLSKHFLVNQLAYKDHVGAAMMRTTLNVKPLGMFFPYDSSLETGEHTFLLRKNGLGGQLFRER
SQ  PWDRKETPYVEILDDLEADPTGKYSQNLLKKLIGGDCIPVDQYMCGKNGKPIADYAKIVAKEGLTTLADIEVDVKSRMDS
SQ  DRFIVLNKKLYRVVWNVTRRNVPYSKQTAFTVVSVIQCDDKESVPEHTFTIGSQILMVSPLKATNNKNFNLKQRLLHTFY
SQ  GKEAVQQPGYIYHSAYVDCNACGRGTWCTGNAIQGFACDCGANYSANDVDLQSSGLVPKNALFLANCPCANNGACSHNAA
SQ  QVYSILDGKACVEVGGKSFTLTFGGVVYAYMGCCDGTMYFVPRAKSCVSRIGDAIFTGCTGTWDKVVETANLFLEKAQHS
SQ  LNFCQQFALTEVVLAILSGTTSTFEELRDLCHNASYEKVRDHLVNHGFVVTIGDYIRDAINIGANGVCNATINAPFIAFT
SQ  GLGESFKKVAAIPWKICSNLKSALDYYCSNIMFRVFPYDIPCDVNDFVELLLDCGKLTVATSYFVLRYLDEKFDTVLGTV
SQ  SNACQTALSSFLNACVAASRATAGFISDMFKLFKVLMHKLYVYTSCGYVAVAEHSSKIVQQVLDIMSKAMKLLHTNVSWA
SQ  GTKLSAIIYEGREALLFNSGTYFCLSTKAKTLQDQMNLVLPGDYNKKTLGILDPVPNADTIDVTANSTVVDVVHGQLEPT
SQ  NEHGPSMIVGNYVLVSDKLFVRTDDEEFYPLCINGKVVSTLFRLKGGMPSKKVTFGDVNTVEVTAYRSVSITYDIHPVLD
SQ  ALLSSSKLATFTVEKDLLVEDFVDVIKDEVLTLLTPLLRGYDIDGFDVEDFIDVPCYVYNQDGDCAWSSNMTFSINPVED
SQ  VEEVEEFIEDDYLSDELPIADDEEAWTRAVEEVMPLDDILVAEIELEEDLPLETALESVEAEVGESISDELCVVETAKAQ
SQ  EPSVESTDSTPSTSTVVSENDLSVKPMSRVAETGDVLEVETAVVGGPVSDVTASVVTNDIVSVEQAQQCGVSSLPIQDEA
SQ  SENQVHQVPDLQCTSETKVEIVQPRQDLRPRRLRKSKVDLSKYKHTVINNSVTLVLGDAIQIASLLPKCVLVNAANRHLK
SQ  HGGGIAGAINKASGGDVQEESDEYISNSGPLHVGDSVLLKGYGLADAILRVVGPDARNNEDAALLKRCYKTFNKHTIVVT
SQ  PLISSGIFSVDPKVSFEYLLANVTTTTYVVVNNEDIYNTLATPSKPDGLVYSFEGWRGTVRTAKNYGFTCFICTEYSANV
SQ  KFLRTKGVDTTKKIQTVDGVSYYLYSARDALTDVIAAANGCPGICAMPFGYVTHGLDLAQSGNYVRQVKVPYVCLLASKE
SQ  QIPIMNSDVAIQTPETAFINNVTSNGGYHSWHLVSGDLIVKDVCYKKLLHWSGQTICYADNKFYVVKNDVALPFSDLEAC
SQ  RAYLTSRAAQQVNIEVLVTIDGVNFRTVILNDATTFRKQLGATFYKGVDISDALPTVKMGGESLFVADNLSESEEVVLKE
SQ  YYGTSDVTFLQRYYSLQPLVQQWKFVVHDGVKSLKLSNYNCYINATIMMIDMLHDIKFVVPALQNAYLRYKGGDPYDFLA
SQ  LIMAYGDCTFDNPDDEAKLLHTLLAKAELTVSAKMVWREWCTVCGIRDIEYTGMRACVYAGVNSMEELQSVFNETCVCGS
SQ  VKHRQLVEHSTPWLLVSGLNEVKVSTSTDPVYRAFNVFQGVETSVGHYVHVRVKDGLFYKYDSGSLTKTSDMKCKMTSVW
SQ  YPKVRYTADCNVVVYDLDGVTKVEVNPDLSNYYMKDGKYYTSKPTIKYSPATILPGSVYSNSCLVGVDGTPGSDTISKFF
SQ  NDLLGFDETKPISKKLTYSLLPNEDGDVLLSEFNNYNPVYKKGVMLKGKPILWVNNGVCDSALNKPNRASLRQLYDVAPI
SQ  VLDNKYTVLQDNTSQLIEPNVPVVEDVSITTRKLIEVKCKGLNKPFVKGNFSFVNDPNGVTVVDTLGLTELRALYVDINT
SQ  RYIVLRDNNWSSLFKLHTVESGDLQIVANGGSVTRRARVLLGASSLFASFAKITVTATTAACKTAGRSFCKFVVNYGVLQ
SQ  NMFLFLKMLFFLPFNYLWPKKQPTVDVGVSGLRTAGVVTTNIVKQCGTAAYYMLLGKFKRVDWKATLRLFLLLCTTILLL
SQ  SSIYHLVIFNQVLSSDVMLEDATGILAMYKEVRSYLGIRTLCDGLAVEYRNTSFDVVDFCSNRSVLCQWCLIGQDSLTRY
SQ  SALQMLQTHITSYVLNIDWIWFALEFFLAYVLYTSSFNVLLLVVTAQYFFAYTSAFVNWRAYNYIVSGLFFLVTHIPLHG
SQ  LVRVYNFLACLWFLRKFYSHVINGCKDTACLLCYKRNRLTRVEASTIVCGTKRTFYIAANGGTSYCCKHNWNCVECDTAG
SQ  VGNTFICTEVANDLTTTLRRLIKPTDQSHYYVDSVVVKDAVVELHYNRDGSSCYERYPLCYFTNLEKLKFKEVCKTPTGI
SQ  PEHNFLIYDTNDRGQENLARSACVYYSQVLCKPMLLVDVNLVTTVGDSREIAIKMLDSFINSFISLFSVSRDKLEKLINT
SQ  ARDCVRRGDDFQTVLKTFTDAARGHAGVESDVETTMVVDALQYAHKNDIQLTTECYNNYVPGYIKPDSINTLDLGCLIDL
SQ  KAASVNQTSMRNANGACVWNSGDYMKLSDSFKRQIRIACRKCNIPFRLTTSKLRAADNILSVKFSATKIVGGAPSWLLRV
SQ  RDLTVKGYCILTLFVFTVAVLSWFCLPSYSIATVNFNDDRILTYKVIENGIVRDIAPNDACFANKYGHFSKWFNENHGGV
SQ  YRNSVDCPITIAVIAGVAGARVANVPATLAWVGRQIVLFVSRVFANTNVCFTPTNEIPYDTFSDSGCVLSSECTLFRDAE
SQ  GNLNPFCYDPTVLPGASSYADMKPHVRYDMYDSDMYIKFPEVIFESTLRITKTLATQYCRFGSCEESAAGVCISTNGSWA
SQ  LYNQNYSTRPGIYCGDDYFDIVRRLAVSLFQPVTYFQLSTSLAMGLVLCVFLTAAFYYINKVKRALADYTQCAVVAVVAA
SQ  LLNSLCLCFIVANPLLVAPYTAMYYYATFYLTGEPAFIMHISWYVMFGTVVPIWMLASYTVGVMLRHLFWVLAYFSKKHV
SQ  DVFTDGKLNCSFQDAASNIFVIGKDTYVALRNAITQDSFVRYLSLFNKYKYYSGAMDTASYREACAAHLCKALQTYSETG
SQ  SDILYQPPNCSVTSSVLQSGLVKMSAPSGAVENCIVQVTCGSMTLNGLWLDNTVWCPRHIMCPADQLTDPNYDALLISKT
SQ  NHSFIVQKHIGAQANLRVVAHSMVGVLLKLTVDVANPSTPAYTFSTVKPGASFSVLACYNGKPTGVFTVNLRHNSTIKGS
SQ  FLCGSCGSVGYTENGGVLNFVYMHQMELSNGTHTGSSFDGVMYGAFEDKQTHQLQLTDKYCTINVVAWLYAAVLNGCKWF
SQ  VKPTRVGIVTYNEWALSNQFTEFVGTQSIDMLAHRTGVSVEQMLAAIQSLHAGFQGKTILGQSTLEDEFTPDDVNMQVMG
SQ  VVMQSGVKRISYGFMHWLMSTLVLAYVSVMQLTKFTMWTYLFETIPTQMTPLLFGFMACVMFTVKHKHTFLSLFLLPVAL
SQ  CLTYANIVYEPQTLVSSTLIAVANWLTPTSVYMRTTHLDFGLYISLSFVLAIIVRRLYRPSMSNLALALCSGVMWFYTYV
SQ  IGDHSSPITYLMFITTLTSDYTITVFATVNLAKFISGLVFLYAPHLGFILPEVKLVLLIYLCLGYMCTMYFGVFSLLNLK
SQ  LRVPLGVYDYSVSTQEFRFLTGNGLHAPRNSWEALILNFKLLGIGGTPCIKVATVQSKLTDLKCTSVVLLTVLQQLHLES
SQ  NSKAWSYCVKLHNEILAAVDPTEAFERFVCLFATLMSFSANVDLDALANDLFENSSVLQATLTEFSHLATYAELETAQSS
SQ  YQKALNSGDASPQVLKALQKAVNVAKNAYEKDKAVARKLERMAEQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDN
SQ  DVLNGVIANARNGCVPLSIVPLCASNKLRVVIPDISVWNKVVNWPSVSYAGSLWDVTVINNVDNEVVKPTDVVETNESLT
SQ  WPLVIECSRASSSAVKLQNNEIHPKGLKTMVVTAGIDQVNCSSSAVAYYEPVQGHRMVMGLLSENAHLKWAKVEGKDGFI
SQ  NIELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQLLGHIAATVRLQAGANTEFASNSTVLTLVAFAVDPAKAYLDYVG
SQ  SGGTPLSNYVKMLAPKTGTGVAISVKPEATADQETYGGASVCLYCRAHIEHPDVSGVCKYKTRFVQIPAHVRDPVGFLLK
SQ  NVPCNVCQYWVGYGCNCDALRNNTVPQSKDTNFLNRVRGSSVNARLEPCSSGLTTDVVYRAFDICNFKARVAGIGKYYKT
SQ  NTCRFVQVDDEGHKLDSYFIVKRHTMSNYELEKRCYDLLKDCDAVAIHDFFIFDVDKTKTPHIVRQSLTEYTMMDLVYAL
SQ  RHFDQNNCEVLKSILVKYGCCEQSYFDNKLWFDFVENPSVIGVYHKLGERIRQAMLNTVKMCDHMVKSGLVGVLTLDNQD
SQ  LNGKWYDFGDFVITQPGAGVAIVDSYYSYLMPVLSMTNCLAAETHKDCDFNKPLIEWLLLEYDYTDYKIGLFNKYFKHWD
SQ  QTYHPNCVNCGDDRCILHCANFNVLFSMVLPNTSFGPIVRKIFVDGVPFIVSCGYHYKELGLVMNMDVNIHRHRLALKEL
SQ  MMYAADPAMHIASASALWDLRTPCFSVAALTTGLTFQTVRPGNFNKDFYDFVVSRGFFKEGSSVTLKHFFFAQDGHAAIT
SQ  DYSYYAYNLPTMVDIKQMLFCMEVVDKYFDIYDGGCLNASEVIVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAVT
SQ  KRNVLPTITQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGATCVIGTTKFYGGWDFMLKTLYKDVES
SQ  PHLMGWDYPKCDRAMPNMCRILASLILARKHSTCCTNSDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYAN
SQ  SVFNILQATTANVSALMSANGNTIIDREIKDMQFDLYINVYRKVVPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYA
SQ  AKGYVASIQNFKETLYYQNNVFMSEAKCWVETNLEKGPHEFCSQHTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTD
SQ  GTVMMERYVSLAIDAYPLTKHDDTEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDDSAKFWEEGFYRDLYSSPTTL
SQ  QAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATTHKMVLSVSPYVCNAPGCDVSDVTKLYLGGMSYYCNDHRPVC
SQ  SFPLCANGLVFGLYKNMCTGSSSIMEFNRLATCDWSDSGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVG
SQ  ERELILVWEVGKSKPPLNRNYVFTGYHLTKNSKVQLGEYVFERIDYSDAVSYKSSTTYKLAVGDIFVLTSHSVATLSAPT
SQ  IVNQERYLKITGIYPTITVPEEFANHVVNFQKAGFSKYVTVQGPPGTGKSHFAIGLAIYYPTARIVYTACSHAAVDALCA
SQ  KAFKYLNIAKCSRIIPAKARVECYDRFKVNDTNAQYLFSTVNALPEISVDILVVDEVSMCTNYDLSIINSRVKAKHIVYV
SQ  GDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSVCYRCPKEIVNTVSALVYNNKLSAKKDASGQCFKILFKGS
SQ  VTHDASSAINRPQLNFVKTFIAANPNWSKAVFISPYNSQNAVARSMLGLTTQTVDSSQGSEYPYVIFCQTADTAHANNLN
SQ  RFNVAVTRAQKGILCVMTSQVLFDSLEFAELSLNNYKLQSQIVTGLFKDCSREDVGLPPAYAPTYLSVDAKYKTTDELCV
SQ  NLNITPNVTYSRVISRMGFKLDATIPGYPKLFITRDEAIRQVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQP
SQ  VGVVDTEWGSMLTTISARPPPGEQFKHLVPLMNKGATWPIVRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKI
SQ  GKEQRCCMCSRRASTFSSPLQSYACWSHSSGYDYVYNPFFVDVQQWGYVGNLATNHDRYCGIHAGAHVASSDAIMTRCLA
SQ  IYDCFIERVDWDVTYPYISHEQKLNSCCRTVERNVVRSAVLSGKFDKIYDIGNPKGIPIISEPVEWHFYDAQPLSNKVKK
SQ  LFYTDDVAKQFEDGLCLFWNCNVSKYPSNAVVCRFDTRVHSEFNLPGCNGGSLYVNKHAFHTPAYDINAFRDLKPLPFFY
SQ  YSTTPCEVHGSGNMLEDIDYVPLKSAVCITACNLGGAVCRKHAAEYRDYMEAYNIVSAAGFRLWVYKTFDIYNLWSTFVK
SQ  VQGLENIAFNVIKQGHFTGVDGELPVAVVNDKIFTKNGTDDVCIFKNETALPTNVAFELYAKRAVRSHPDLNLLRNLEVD
SQ  VCYNFVLWDYDRNNIYGTTTIGVCKYTDIDVNPNLNMCFDIRDKGSLERFMSMPNGVLISDRKIKNYPCIIGPKHAYFNG
SQ  AILRNIDAKQPITFYLYKKVNNEFVSFSDTFYTCGRTVNDFTALTPMEEDFLVLDSDVFIKKYSLEDYAFEHVVYGDFSH
SQ  TTLGGLHLLIGLYKKMRDGHILMEEMLKDRATVHNYFITDSNTASYKAVCSVIDLRLDDFVNIIKEMDLDVVSKVVKVPI
SQ  DLTMIEFMLWCKDGKVQTFYPRLQATNDWKPGLTMPSLFKVQQMNLEPCLLANYKQSIPMPNGVHMNVAKYMQLCQYLNT
SQ  CTLAVPANMRVIHFGAGCEKGVAPGTSVLRQWLPLDAVLIDNDLNEFVSDADITIFGDCVTVHVGQQVDLLISDMYDPCT
SQ  KAVGEVNQTKALFFVYLCNFIKNNLALGGSVAIKITEHSWSADLYKIMGRFAYWTVFCTNANASSSEGFLIGINFLGELK
SQ  EEIDGNVMHANYIFWRNSTPMNLSTYSLFDLSRFPLKLKGTPVLQLKESQINELVISLLSQGKLLIRDNDTLNVSTDVLV
SQ  NFRKRL
//
ID  P0C6V9;
PN  2'-O-methyltransferase;
GN  rep;
OS  389167;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6V9;
DR  UNIPROT: Q0Q476;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF12379;
DR  Pfam: PF12124;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51940;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESLALGVSEKTHVQLSLPVLQVRDVLVRGFGDSVEEALAEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDAQGTN
SQ  HGYKVVELVAELDGIQYGRSGTTLGVLVPHVGETPVAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGVELGTDPIEDYEQN
SQ  WNTKHGGGVLRELIRELNGGAFTRYVDNNFCGPDGYPLECIKDLLARAGKSMCTLSEQLDYIESKRGVYCCREHEHEIVW
SQ  FTERSEKSYERQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVATPQECNDMHLSTL
SQ  MKCNHCDEVSWQTCDFLKATCEQCGTENLVCEGPTTCGYLPANAVVKMPCPACQDPEVGPEHSVADYHNHSNIETRLRKG
SQ  GRTKCFGGCVFAYVGCYNKRAYWVPRASANIGASHTGITGDNVETLNEDLMEILNRDRVNINIVGDFHLNEEVAIILASF
SQ  SASTCAFVDTVKGLDYKTFKDIVESCGNFKVTRGRAKKGAWNIGQEKSILTPLYGFPSQAAGVIRSIFTRALDTANHSIP
SQ  DLQRAAITILDGISEQSLRLIDAMVYTSDLLTNSVIVMAYVTGGLVQQITQWLSNMLGTTVDKLKPVFTWVEAKLSAGIE
SQ  FLRDAWEILKFLVTGVFDIVKGQIQVASDNLKECVKAFLDVLNKALEMCIDQVIIAGAKLRTLNLGEVFIAQSKGLYRQC
SQ  IRGKEQLQLLMPLRAPKEVTFFEGDSHDTVFTSEEVVLKNGELEALETPVDSFTNGAVIGTPVCVNGLMLLELKDKEQYC
SQ  ALSPGLLATNNVFSLKGGAPVKGVTFGEDTVLEVQGYKNVKITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAV
SQ  VKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEEKLSSRMYCSFYPPDEEEDCEEYEDEEEIPEETCEHEYGTEDDYKG
SQ  LPLEFGASTEIQQVDEEEEEDWLEEAIAAKPEPEPLPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQHAKPTVIVNAANVH
SQ  LKHGGGVAGALNKATNGAMQQESDDYIKKNGPLTVGGSCLLSGHNLAKKCMHVVGPNLNAGEDVQLLKAAYANFNSQDVL
SQ  LAPLLSAGIFGAKPLQSLKMCVETVRTQVYFAVNDQDLYDHVVLGYLDSLKPKVETPTQENLELKEQPAVETLTQENLEL
SQ  EELPVIEKPVDVKFKARIEEVNTSLEETKFLTSRLLLFADINGKLYQDSQNMLRGEDMFFLEKDAPYIVGDVISSGDITC
SQ  VIIPAKKAGGTTEMLAKALKKVPVSEYITTYPGQGCAGYTLEEAKTALRKCKSVFYVLPSKTPNDKEEILGTVSWNLREM
SQ  LAHAEETRKLMLICMDVKALMSTIHRRYKGIKVQEGIVDYGVRFFFYTSKEPVASIITKLNLLNEPLVTMPIGYVTHGLN
SQ  LEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFIETVSLAGMYRDWSYSGQRTELGVEFLKRGDKVVYHT
SQ  VGSPIQFHLDGEVLLLDKLKSLLSLREVRTIKVFTTVDNTNLHTQIVDMSMTYGQQFGPTYLDGADVTKIKPHAKHEGKT
SQ  FFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQIGGLTSIKWADNNCYLSSVLLALQQIEVKFNAPALQE
SQ  AYYRARAGDAANFCALILAYSNRTVGELGDVRETMTHLLQHANLESAKRVLNVVCKTCGQKSTTLTGVEAVMYMGTLSYE
SQ  ELKTGVTIPCICGRDATQYLVQQESSFVMMSAPPSEYTLQQGAFLCANEYTGSYQCGHYTHVTVKETLYRIDGAYLTKMS
SQ  EYKGPVTDVFYKEISYTTTIKPVSYKLDGVIYTEIQPKLDEYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKF
SQ  ADDLNQMTGFKKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIIWHINQTTNKTTYKPNTWCLRCLWSTK
SQ  PVETSNSFEVLEVEDTQGMDNLACESQTPTSEEVVENPTIQKEVIECDVKTIEVVGNVILKPSEEGVKVTQELGHEDLMA
SQ  AYVEETSITIKKPNELSLALGLRTLATHGAAAINSVPWSKILAYVKPFLGQAAVTTTNCIKRCVQRVFNNYMPYVITLLF
SQ  QLCTFTRSTNSRIRASLPTTIAKNSVKSVAKLCLDVCINYVKSPKFSKLFTIAMWLLLLSICLGSLIYVTAAFGVLLSNL
SQ  GIPSYCDGVRESYVNSSNVTTMDFCEGSFLCSVCLNGLDSLDSYPALETIQVTISSYKLDLTSLGLAAEWFLAYMLFTKF
SQ  FYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFAFCYYVWKSYVHIMDGCTSSTCMMCYKRNR
SQ  ATRVECTTIVNGMKRSFYVYANGGRGFCKAHNWNCLNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYVVDSVAVK
SQ  NGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESAAKSASVYYSQLMCQPILLLDQALV
SQ  SDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKL
SQ  SHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNN
SQ  IPFRLTCATTRQVVNAITTKISLKGGKIVSTWFKLMLKATLLCVLAALFCYIIMPVHSLSVHDGYTNEIIGYKAIQDGVT
SQ  RDIMATDDCFANKHAGFDSWFSQRGGSYRNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICY
SQ  TPSKLIEYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVT
SQ  TFDAEYCRHGTCERSEAGVCLSTSGRWVLNNEHYRALPGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILV
SQ  TCAAYYFMKFRRAFGEYNHVVAANALLFLMSFTILCLAPAYSFLPGVYSIFYLYLTFYFTNDVSFLAHLQWFAMFSPIVP
SQ  FWITAIYVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYF
SQ  SGALDTTSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDD
SQ  TVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSV
SQ  LACYNGSPSGVYQCAMRPNYTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAA
SQ  GTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQN
SQ  GMNGRTILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLG
SQ  IMAIAACAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLVLMTA
SQ  RTVYDDAARRVWTLMNVITLVYKVYYGNSLDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQ
SQ  CIMLVYCFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVAT
SQ  VQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDN
SQ  RATLQAIASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQAR
SQ  SEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWE
SQ  IQQVVDADSKIVQLSEINMDNSQNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKG
SQ  GRFVLALLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPRGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNA
SQ  TEVPANSAVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHP
SQ  NPKGFCDLKGKYVQIPATCANDPVGFTLKNTVCTVCGTWKGYGCSCDQLREPMMQSADASTFLNRVCGVSAARLTPCGTG
SQ  TSTDVVYRAFDIYNERVAGFAKFLKTNCCRFQEKDEEGNLLDSYFVVKRHTMSNYQHEETIYNLVKECPAVAVHDFFKFR
SQ  VDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQA
SQ  LLKTVQFCDAMRDAGIVGVLTLDNQDLNGNWYDFGDFVQVAPGCGVPIVDSYYSLLMPILTLTKALAAESHMDADLAKPL
SQ  IKWDLLKYDFTEERLCLFDRYFKYWDQTYHPNCINCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTG
SQ  YHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVS
SQ  KGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFP
SQ  FNKWGKARLYYDSMSYEDQDVLFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGA
SQ  TVVIGTSKFYGGWHNMLKTVYSDVETPHLMGWDYPKCDRAMPNMLRIMASLVLARKHSTCCNLSHRFYRLANECAQVLSE
SQ  MVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDHEFVDEF
SQ  YAYLRKHFSMMILSDDAVVCYNSNYAAQGLVASIKNFKAVHYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDD
SQ  YVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSV
SQ  MLTNDNTSRYWEPEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAP
SQ  GCDVTDVTQLYLGGMSYYCKLHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLF
SQ  AAETLKATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRG
SQ  TTTYKLNVGDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAI
SQ  GLALYYPSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVF
SQ  DEISMATNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVS
SQ  ALVYDNKLKAHKEKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTV
SQ  DSSQGSEYDYVIFTQTTETAHSCNVNRFNVAITRAKIGILCIMSDRDLYDKLQFTSLEVPRRNVATLQAENVTGLFKDCS
SQ  KIITGLHPTQAPTHLSVDTKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFITREEAIRHVRAWIGFDVE
SQ  GCHATRDAVGTNLPLQLGFSTGVNLVAVPTGYVDTENNTEFTRVNAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSD
SQ  TLKGLSDRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDRRATCFSTSSDTYACWNHSVGFDYVYNPFMIDVQQWGFTGN
SQ  LQSNHDQHCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWSVEYPIIGDELKINAACRKVQHMVVKSALLADKFSVLHDI
SQ  GNPKAIKCVPQAEVDWKFYDAQPCSDKAYKIEELFYSYATHHDKFTDGVCLFWNCNVDRYPANAIVCRFDTRVLSNLNLP
SQ  GCDGGSLYVNKHAFHTPAFDKSAFTYLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRRHANEYR
SQ  QYLDAYNMMISAGFSLWIYKQFDTYNLWNTFTRLQSLENVAYNVVNKGHFDGQIGEAPVSIINNAVYTKVDGNDVEIFEN
SQ  KTTLPVNVAFELWAKRNIKPVPEIKILNNLGVDIAANTVIWDYKREAPAHVSTIGVCTMTDIAKKPTESACSSLTVLFDG
SQ  RVEGQVDLFRNARNGVLITEGSVKGLTPSKGPAQASVNGVTLIGESVKTQFNYFKKVDGIIQQLPETYFTQSRDLEDFKP
SQ  RSKMETDFLELAMDEFIQRYKLEGYAFEHIVYGDFSHGQLGGLHLMIGLAKRSQDSPLKLEDFIPTDSTVKNYFITDAQT
SQ  GSSKCVCSVIDLLLDDFVEIIKSQDLSVISKVVKVTIDYAEISFMLWCKDGHVETFYPKLQASQAWQPGVAMPNLYKMQR
SQ  MLLEKCDLQNYGENAVIPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGTAVLRQWLPTGALLVDSD
SQ  LNDFVSDADSTLIGDCATVHTANKWDLIISDMYDPKTKHVTKENDSKEGFFTYLCGFIKQKLALGGSVAVKITEHSWNAD
SQ  LYKLMGHFSWWTAFVTNVNASSSEAFLIGVNYLGKLREQIDGYTMHANYIFWRNTNPIQLSSYSLFDMSKFPLKLRGTAV
SQ  MSLKENQINDMIYSLLENGRLIIRENNRVVVSSDILVNN
//
ID  P0C6W0;
PN  Putative 2'-O-methyl transferase;
GN  rep;
OS  693999;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W0;
DR  UNIPROT: Q0Q467;
DR  Pfam: PF13087;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity). {ECO:0000250}. The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. {ECO:0000250}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039548;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASNHISLAFANDEEISAIGFGSVEEAVSYYSDAAVNGFDQCRFVSLGLQDAVVGVEDDDVVMLITGVTQLRAYLGTFGD
SQ  RPLNLRGWLLFSNCNYFLEELDLVFGRCGGTTIPVDQFMCGADGAPVIQEGDWTFMDYFQDSNQFTLNGITYVKAWDVDR
SQ  KPNDYAKQNVTCIRRITYITDHRHVLADGTTMKTARHPKVNKSVVLDSPFDQIYKEVGSPFMGNGSTFVEMLKDPAFFHA
SQ  LITCECGRSEWTVGDWKGYNSLCCNIKCKPITIVTPKAVPGAVVITKAGIGAGLKCYNNVFLKHIIDLVVPGTNLGWGVW
SQ  RIAKVQSKDDVATSGNVLVDDPEDRLDPCYFGNDGPFATKFKFQLLANSFDDEVKGAIVQGVVHVNTAICDVVKDILGLP
SQ  WFVKKLGSLVTVMWDQFVAGVQSMKICTLKVVQLAKALSCATMSVVKGVITLVAEVPEIFKRLFYTLTSALKSLCTSSCD
SQ  ALVVAGKSFAKIGDYVLLPSALVRLVSSKVKGKAQSGIKQLQFATVVLGDTHKVESDRVEFSSVNLKMVDEEFPLNPVGH
SQ  TVAVGNQAFFCSDGLYRFMADRDLVITSPIFKPELELEPIFECDAIPGFPKVAASNVAELCVKVDTLLFNYDKIYKKYST
SQ  IIKGDRCYIQCTHTFKAPSYYFDDDEFVELCTKYYKLPDFDAFYNAVHAATDMDQFCALCTSGFEVFIPRVPDCPPILND
SQ  IDGGSIWTSFILSVRSATDFIKTLKIDLGLNGVVVFVTKKFRKAGALLQKLYNAFLDTVTSFIKVAGVAFKYCATCVPKI
SQ  VINGCYHTVTRLFAKDLQIPTEDGVADFNTFNHCVFPVNPTRIETDSLELEEVDFVEPGVDGKLVILDDYSFYSDGTNYY
SQ  PSDGKGVVASCFKKKGGGVVTISDEVQVRTIDPVYKVRLEYEFEDETLVKVCEKAIGTKLKVTGDWSNLLETLEKAMDVV
SQ  RQHLDVPDYFVYDEEGGTDLNLTIMVSQWPLSSDSEDDFKAVDDEPNANTDETVDTFAEDVAETQNVQQDVTQDEVEAVC
SQ  DLVVKATEEGPIEHEELSEDQKEVQQALAFIEDKPVVVKPDVFAFSYASYGGLKVLNQSSNNCWVSSALVQLQLTGLLDS
SQ  DEMQLFNAGRVSPMVKRCYESQRAIFGSLGDVSACLESLLKDRDGMSITCTIDCGCGPGVRVYENAIFRFTPLKTAFPMG
SQ  RCLICSKTLMHTITQMKGTGIFCRDATALDVDTLVVKPLCAAVYVGAQDGGHYLTNMYDANMAVDGHGRHPIKFNTINTL
SQ  CYKDVDWEVSNGSCDVKPFLTYKNIEFYQGELSALLSVNHDFVVNAANEQLSHGGGIAKALDDLTKGELQVLSNQYVSRN
SQ  GSIKVGSGVLIKCKEHSILNVVGPRKGKHAAELLTKAYTFVFKQKGVPLMPLLSVGIFKVPITESLAAFLACVGDRVCKC
SQ  FCYTDKERLAIQNFVTSFQTEQPVEPLPVIQEVKGVQLEKPVPDVKVENPCEPFRIEGDAKFYDLTPSMVQSLQVTRLVS
SQ  FTNSDLCLGSFVRDCDGYVQGSLGGAIANYKKSNPVLPAGNCVTLKCDGFISFTFVILPKEGDTNYEKNFNRAIAKFLKL
SQ  KGSLLVVVEDSSVFNKISHASVAGYVAKPALVDTLFEAKPVQVVVTQDQRSFHTVELSTSQTYGQQLGDCVVEDKKVTNL
SQ  KPVSKDKVVSVVPNVDWDKHYGFVDAGIFHTLDHTMFVFDNNVVNGKRVLRTSDNNCWINAVCLQLQFANAKFKPKGLQQ
SQ  LWESYCTGDVAMFVHWLYWITGVEKGEPSDAENTLNIISRFLKPQGSVEMLRATSTTCDGTCSTKRVVSTPVVNASVLKV
SQ  GLDDGNCVHGLPLVDRVVSVNGTVIITNVGDTPGKPVVATENLLLDGVSYTVFQDSTTGVGHYTVFDKEAKLMFDGDVLK
SQ  PCDLNVSPVTSVVVCNNKKIVVQDPVKRVELDASKFLDTMNVASEKFFTFGDFVSRNIIVLIVYLFSLLAICFRALKKRD
SQ  MKVMAGVPERTGIILKRSVKYNYKALKFFFRLKFQYIKVFLKFSLVLYTLYALMFMFIRFTPVGTPICKRYTDGYANSTF
SQ  DKNDYCGNVLCKICLYGYEELSDFTHTRVIWQHLKDPLIGNILPLFYLVFLIIFGGFFVRIGITYFIMQYINAAGVALGY
SQ  QDNVWLLHLLPFNSMGNIIVVAFIVTRILLFLKHVLFGCDKPSCIACSKSAKLTRVPLQTILQGVTKSFYVNANGGKKFC
SQ  KKHNFFCVDCDSYGYGCTFINDVIAPELSNVTKLNVIPTGPATIIIDKVEFSNGFYYLYSGSTFWKYNFDITEAKYACKD
SQ  VLKNCNILTDFVVFNNSGSNVTQVKNACVYFSQLLCKPIKLVDSALLASLNVDFSANLHKAFVEVLSNSFGKDLSNCSNM
SQ  NECRESLGLSDVPEEEFSAAVSEAHRYDVLISDVSFNNLIVSYAKPEEKLAVHDIANCMRVGAKVVNHNVLTKDNVPVVW
SQ  LAKDFIALSEEARKYIVRTTKTKGINFMLTFNDRRMHLTIPTISVANKKGAGLPSLFTRLYSFFWHLCVLIVVLFVATSL
SQ  LDFSAQVTSDTQYDFKYIENGVLKVFEKPLDCVHNAFVNFNEWHNAKFGSIPTNSRRCPIVVGTSDEVRYIPGVPAGVFL
SQ  YGKSLIFAMSTIFGTSGLCFDDRGLTDPDSCIFNSACTTLSGIGGRNVYCYREGVVDNAKLYSSLLPHSYYRLMDGNHIV
SQ  LPEIITRGFGIRTIKTQAMTYCRTGECIDSQAGVCVGLDRFFVYSKTPGSDYVCGTGFFSLLFNVIGMFSNSIPVTVMSG
SQ  QILLNCVVAFTAVMACFAFTKFKRLFGDMSFGVLSVGLCTVVNNLSYVVTQNSIGMLAYATLYFLCTKGVRYSWVWHVGF
SQ  AISYCFLAPWWVVLAYLICALLEFLPNLFKLKVSTQLFEGDKFVGSFESAASGTFVLDMHSYQKLANSISTEKLKQYCAS
SQ  YNRYKYYSGSASEADYRLACFAHLAKAMSDFANDHMDKLYTPPTVSYNSTLQAGLRKMAQPSGIVEGCIVRVSYGNLTLN
SQ  GLWLGDTVICPRHVIASNTTNVIDYDHAMSLVRLHNFSISSGNMFLGVISASMRGTLLHIKVNQSNVNTPNYTYKVLKPG
SQ  DSFNILACYDGSAAGVYGVNMRTNYTIRGSFISGACGSPGYNINNGVVEFCYMHHLELGSGCHVGSDMDGTMYGKYEDQP
SQ  TLQIEGASNLVTENVCSWLYGALINGDRWWLSSVSVGVDTYNEWALRNGMTALKNVDCFSLLVAKTGVDVGRLLASIQKL
SQ  HGNFGGKSILGCTSLCDEFTLSEVVKQMYGVTLQSGKVSRAFRNASIVCCLLFLFLSEMLNHSKLFWINPGYITPVFLAI
SQ  IVASSALMLLVKHKLLFLQLYLLPSLCIVSGYNIFKDYHFYTYMLEEFDYKVPFGGFNVTGVLNISLCCFVMGLHTFRFL
SQ  QTPNKIFSYVVAVLTVLYTYYYSTDVLGLILTSMSGFTNYWFIGTATYKLATYVLPHTSLLDSFDAIKAVVFLYLLLGYC
SQ  NCVYYGSLYWINRFCKLTLGCYEFKVSAAEFKYMVANGLRAPTGVFDALILSLKLIGVGGRKTIKISSVQSKLTDLKCTN
SQ  VVLLGCLSNMNIAANSREWAYCVDLHNKINLCNDAEAAQEMLLALLAFFLSKNSAFGVDELLDSYFNDSSVLQSVAATYV
SQ  NLPSYLAYETARQSYEDALANGSPPQLVKQLRHAMNVAKSEFDREASTQRKLDRMAEQAASQMYKEARAVNRKSKVVSAM
SQ  HSLLFGMLRRLDMSSVDTILSLAKDGVVPLSIIPAVSATKLNIVVSDIESYSKIQREGCVHYAGVIWSVVDIKDNDGKPV
SQ  HAKEVVTSNVESLAWPLFLNCERIIKLQNNEIIPSKIKQRPIKAEGEGVVADGNALYSNEGGRTFMYAFISDKPDLKVVK
SQ  WEFDGGSNAIELEPPCKFLVEAPSGPVVKYLYFVRNLNNLRRGAVLGFIGATVRLQAGKQTEQATNSSLLTLCAFAVDPP
SQ  KTYLDAVKSGHRPVGNCVKMLANGSGNGQAITNGVEASTNQDSYGGASVCLYCRAHVEHPDMDGFCKLRGKYVQVPLGTL
SQ  DPIRFVLENTVCKVCGCWQANGCTCDRAVIQSVDSGYLNRVRGSSAARLEPLNGSDTHHVFRAFDVYNRDVACISKFLKV
SQ  NCVRLKNLDKHDAFWIVKKCTKSVMEHEQSIYNLISDCGAVAKHDFFTWKEGRSVYGNVCRQDLTEYTMMDLCYALRNFD
SQ  ENNCETLKKILVVVGACDESYFDNKLWFDPVENEDVHRVYAKLGTIVARAMLKCVKYCDAMVEQGIVGVITLDNQDLNGD
SQ  FYDFGDFVTSVKGMGVPICTSYYSYMMPVMGMTNCLASECFIKSDIFGEDFRTFDLLAYDFTEHKVNLFNKYFKHWGQTY
SQ  HPNCEDCHDESCIVHCANFNTLFATTIPITAFGPLCRKCWIDGVPLVTTAGYHFKQLGIVWNKDLNLHSSRLTINELLQF
SQ  CADPSLLIASSPALVDKRTVCFSVAALGTGMTNQTVKPGHFNREFYDFLRSQGFFEEGSELTLKHFFFAQKGDAAVRDFD
SQ  YYRYNRTTVLDICQARVVYQIVQCYFGMYEGGCITAKEVIVNNLNKSAGYPFNKFGKAGLYYDSLSYEEQDDLYAYTKRN
SQ  IIPTMTQLNLKYAISGKDRARTVGGVSLLSTMTTRQYHQKHLKSIVNTRGASVVIGTTKFYGGWDNMLKTLIKDVENPHL
SQ  MGWDYPKCDRALPNMIRMISAMILGSKHVNCCSSSDRYYRLCNELAQVLTEMVYSNGGFYVKPGGTTSGDATTAYANSVF
SQ  NIFQATSANVNRLLSVDSNTCNNIEVKQLQRKLYDCCYRSSSVDQSFVEEYFGYLRKHFSMMILSDDGVVCYNSEYAALG
SQ  YVADLNAFKAVLYYQNNVFMSASKCWIEPDINKGPHEFCSQHTMQIVDKDGTYYLPYPDPSRILSAGVFVDDIVKTDPVI
SQ  LLERYVSLAIDAYPLSKHDNPEYRRVFTVMLDWVKHLYKTLNQGVLDSFSVTLLEDATAKFWDESFYASMYEQSSVLQSA
SQ  GLCVVCSSQTVLRCGDCIRRPMLCTKCAYDHVVSTSHKFILAITPYVCCSSGCGVSDVTKLYLGGLSYWCVDHKPRLSFP
SQ  LCSSGNVFGLYKNSATGSPDVDDFNTLATSDWTDVKDYKLANDVKDSLRLFAAETIKAKEESVKSSYACATIHEVVGPKE
SQ  LVLKWEVGKPRPPLSRNSVFTCYHITKNTKFQVGEFTFEKLDYDNDAVSYKSTATTKLVPGMVFVLTSHNVQPLRAPTII
SQ  NQERYSTLHKLRPAFNIHEDYSNLIPYYQLIGKQKLTTIQGPPGSGKSHCVIGLGLYFPGARIVFTACSHAAVDSLCVKA
SQ  ATAYSSDRCSRIIPQKARIECYDGFKSNNTSAQYLFSTVNALPEVNADICVVDEVSMCTNYDLSVINQRVNYRHIVYVGD
SQ  PQQLPAPRVMITRGVLVPEDYNVVTRRMCVLKPDIFLHKCYRCPAEIVNTVSEMVYENQFVPVKSESKECFKIYCRGNVQ
SQ  VDNGSSINRRQLEVVRMFLAKNPKWAKAVFISPYNSQNYVAGRVLGLQIQTVDSSQGSEYDYVIYTQTSDTAHASNVNRF
SQ  NVAITRAKKGILCIMCDRELFDILKFYELKLSDLQVGDGCGLFKDCYKGEDNLPPSHAPTFMSLSDNFKTDKDLAVQIGV
SQ  NGPVKYEHVISFMGFRFDINVPNQHTLFCTRDFAMRNARGWLGFDVEGAHVIGSNVGTNVPLQLGFSNGVDFVVRPEGCV
SQ  STEVGDVIQPVRARAPPGDQFTHLLPLLRKGQPWSVIRRRIVQMCSDYLANLSDTLIFVLWSGGLELTTMRYFVKLGPVQ
SQ  TCDCGKRATCYNSTNHTFSCFRHALGSDYIYNCYCIDIQQWGYTGSLSMNHHEVCNIHRNEHVASGDAAMTRCLAIHDCF
SQ  VKNVDWSITYPFIANEQAINKSGRLVQSHVMRAVLKLYNPKAIHDVGNPKGIRCVVTDASWYCYDKNPTNTNVKMLEYDY
SQ  ITHGQLDGLCLFWNCNVDMYPEFSVVCRFDTRMRSTLNLEGCNGGSLYVNNHAFHTPAYDKRAFAKLKAMPFFFYDDSEC
SQ  EKLQDAVNYVPLRASNCITRCNVGGAVCSKHCALYHNYVMAYNTFTTAGFTIWVPNSFDMFNLWQTFKNSNVQGLENIAY
SQ  NVVKKGSFVGVEGELPVAVVNDKVMVRDGVSDNVVFVNNTSLPTNVAFELYAKRKVGLTPPLTILKNLGVVCTSKCVLWD
SQ  YEASRPLTTFTKDVCKYTDFDGDVCTLFDNSVPGAFERFTVTKNAVLISLTAVKKLTAIKLTYGYLNGVPVFTHEDKPFT
SQ  WYIYTRKDGAFVEYPDGYFTQGRVISDFQPRSNMEEDFLNMDMGLFISKYGLEDYGFEHVVFGDVSKTTLGGLHLLISQI
SQ  RLSKIGVLKVEDFVSSSDSTLKSCTVTYVDNPSSKMVCTYVDLLLDDFVNILKSVDLSVVSKVHEVVIDCKVWRWMLWCK
SQ  DHKVQTFYPQLQSAEWKCGYSMPSIYKIQRMCLEPCNLYNYGSGLKLPDGIMFNVVKYTQLCQYLNSTTMCVPHHMRVLH
SQ  LGAGSDKGVAPGTAVLRRWLPLDAVIVDNDVNDYVSDADFSYTGDCASMYLTDKFDLVISDMYDGRTKSCDGDNVSKEGF
SQ  FPYINGVITEKLALGGTVAIKITEFSWNKKLYELIQKFEYWTLFCTSVNTSSSEAFLIGVHFLGDFSTNAIIDGNIMHAN
SQ  YIFWRNSTIMTMSYNSVLDLSKFSCKHKATVVVNLKDSSVTDLVLGLLKNGKLLIRNNGVVCGFSNHLVNSTK
//
ID  P0C6W2;
PN  2'-O-methyltransferase;
GN  rep;
OS  442736;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W2;
DR  UNIPROT: Q3LZX2;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF12379;
DR  Pfam: PF12124;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51940;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTN
SQ  HGHKVVELVAELDGIQFGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSFGIDLKSYDLGDELGTDPIEDYEQN
SQ  WNTKHGSGALRELTRELNGGVVTRYVDNNFCGPDGYPLECIKDFLARAGKSMCTLSEQLDYIESKRGVYCCREHEHEIVW
SQ  FTERSEKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVATPQECNDMHLSTL
SQ  MKCNHCDEVSWQTCDFLKATCEQCGTENLVCEGPTTCGYLPTNAVVKMPCPACQDPEVGPEHSVADYHNHSNIETRLRKG
SQ  GRTKCFGGCVFSYVGCYNKRAYWVPRASANIGANHTGITGENVETLNEDLLEILNRERVNINIVGDFRFNEEVAIILASF
SQ  SASPSAFIETVKGLDYKSFKVIVESCGNYKVTNGKPVTGAWNIGQQRSILTPLCGFPSQAAGVIRSIFSRTLDAANHSIL
SQ  DLQRAAVTTLDGISEQSLRLVDAMVYTSDLLTNSVVVMAYVTGGLVQQTMQWLSNMLGTAVDKLKPVFTWVEAKLSAGVE
SQ  FLRDAWEILKFLITGVFDVIKGQIQVATDNIKECVKIFLGVVNKALEMCLDQVTIAGTKLRALNLGEVFIAQSRGLYRQC
SQ  IRGKEQLQLLMPLKAPKEVTFLEGDAHDTVLTSEEVVLKSGELEALETPIDSFTSGAVVGTPVCINGLMLLELENKEQYC
SQ  ALSPGLLATNNVFRLKGGAPVKGVTFGEDTVLEVQGYKNVKITFELDVRVDKVLNEKCSVYTVESGTEVTEFACVVAEAV
SQ  VKTLQPVSDLLTPMGIDLDEWSVATFYLFDDAGEEKLSSRMYCSFYPPDEEEDCEECEDEEETCEHEYGTEDDYKGLPLE
SQ  FGASTETPHVEEEEEEEDWLDDAIEAEPEPEPLPEEPVNQFVGYLKLTDNVAIKCIDIVKEAQSAKPTVIVNAANTHLKH
SQ  GGGVAGALNKATNGAMQNESDEYIRQNGPLTVGGSCLLSGHNLAEKCLHVVGPNLNAGEDVQLLKRAYENFNSQDVLLAP
SQ  LLSAGIFGAKPLQSLKMCVEIVRTQVYLAVNDKSLYDQIVLDYLDSLKPKVESPNKEEEPKLEEPKAVQPVAEKPVDVKP
SQ  KIKACIDEVTTTLEETKFLTNKLLLFADINGKLYQDSQNMLRGEDMSFLEKDAPYIVGDVITSGDITCVIIPAKKSGGTT
SQ  EMLARALKEVPVAEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSETPNEKEEVLGTVSWNLREMLAHAEETRKLMP
SQ  ICLDVRAIMATIQRKYKGIKVQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGLNLEEAARCMRSLK
SQ  APAVVSVSSPDAVTAYNGYLTSSSKTPEEYFVETTSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTTGSPIEFHLDGE
SQ  VLPLDKLKSLLSLREVKTIKVFTTVDNTNLHTHIVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRS
SQ  EAFEYYHTIDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQVEVKFNAPALQEAYYRARAGDAAN
SQ  FCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLKGVEAVMYMGTLSYDELKTGVSIPCVC
SQ  GRNATQYLVQQESSFVMMSAPPAEYKLQQGAFLCANEYTGNYQCGHYTHITAKETLYRVDGAHLTKMSEYKGPVTDVFYK
SQ  ETSYTTAIKPVSYKLDGVTYTEIEPKLDGYYKKGNAYYTEQPIDLVPTQPMPNASFDNFKLTCSNTKFADDLNQMTGFKK
SQ  PASRELTVTFFPDLNGDVVAIDYRHYSTSFKKGAKLVHKPILWHINQTTNKTTYKPNIWCLRCLWSTKPVDTSNSFEVLV
SQ  VEDTQGMDNLACESQTTTSEEVVENPTVQKEIIECDVKTTEVVGNVILKPSEEGVKVTQELGHEDLMAAYVEETSITIKK
SQ  PNELSLALGLKTLATHGAAAINSVPWSKILAYVKPFLGQTAVITSNCIKKCVQRVFSNYMPYVITLLFQLCTFTKSTNSR
SQ  IKASLPTTIAKNSVKSVAKLCLDVCINYVKSPKFSKLFTIVMWLLLLSICLGSLTYVTAVLGVCLSSLGVPSYCDGVREL
SQ  YINSSNVTTMDFCQGYFPCSVCLSGLDSLDSYPALETIQVTISSYKLDLTFLGLAAEWLLAYMLFTKFFYLLGLSAIMQA
SQ  FFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYVWKSYVHIMDGCTSSTCMMCYKRNRATRVECTTIVNG
SQ  VKRSFYVYANGGRGFCKAHNWNCLNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSAYVVDSVTVKNGALHLYFDKAG
SQ  QKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESAAKSASVYYSQLMCQPILLLDQALVSDVGDSTEVSVK
SQ  MFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDIEVTGDS
SQ  CNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLVWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCATTRQ
SQ  VVNVITTKISLKGGKVVSTWFKLLLKVTLLCVLAALFCYVIMPVHSLSVHDGYTNEIIGYKAIQDGVTRDIVSTDDCFAN
SQ  KHAGFDSWFSQRGGSYRNDKNCPVVAAIITREIGFIVPGLPGTVLRALNGDFLHFLPRVFSAVGNICYTPSKLIEYSDFA
SQ  TSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEYCRHGTC
SQ  ERSEVGVCLSTSGRWVLNNEHYRALPGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFMKFRR
SQ  AFGEYNHVVAANALLFLMSFTILCLAPAYSFLPGVYSIFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYVFCIS
SQ  LKHFHWFFSNYLKKRVMFNGVTFSTFEEAALCTFLLNKEMYLRLRSETLLPLTQYNRYLALYNKYKYFSGALDTTSYREA
SQ  ACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVVCTA
SQ  EDMLNPNYDDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVY
SQ  QCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLA
SQ  WLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTI
SQ  LEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFALGIMAVAACAMLLV
SQ  KHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDDAARRVW
SQ  TLMNVITLVYKVYYGNSLDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCFLGYC
SQ  CCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDVKCTS
SQ  VVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIASEFS
SQ  SLPSYAAYATAQEAYEQAVSNGDSEVVLKKLKKSLNVAKSEFDHDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAM
SQ  QTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDADSKIV
SQ  QLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNAKGGRFVLALLSDHQ
SQ  DLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSF
SQ  CAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKY
SQ  VQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPMMQSADASTFLNRVCGVSAARLTPCGTGTSTDVVYRAFDI
SQ  YNEKVAGFAKFLKTNCCRFQEKDEEGNLLDSYFVVKRHTMSNYQHEETIYNLIKECPAVAVHDFFKFRVDGDMVPHISRQ
SQ  RLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDNYFNKKDWYDFVENPDVLRVYANLGERVRRALLKTVQFCDAMR
SQ  DAGIVGVLTLDNQDLNGNWYDFGDFVQVAPGCGVPIVDSYYSLLMPILTLTKALAAESHMDADLAKPLVKWDLLKYDFTE
SQ  ERLCLFDRYFKYWDQTYHPNCINCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQ
SQ  DVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVEL
SQ  KHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYD
SQ  SMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGG
SQ  WHNMLKTVYSDVESPHLMGWDYPKCDRAMPNMLRIMASLILARKHSTCCNLSHRFYRLANECAQVLSEMVMCGGSLYVKP
SQ  GGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDHEFVDEFYAYLRKHFSMMI
SQ  LSDDAVVCYNSNYAAQGLVASIKNFKAVLYYQNNVFMSEAKCWTETDLTRGPHEFCSQHTMLVKQGDDYVYLPYPDPSRI
SQ  LGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYWE
SQ  PEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYL
SQ  GGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETF
SQ  KLSYGIATVREVLSDRELYLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYF
SQ  VLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISNEFSSNVANYQKIGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIV
SQ  YTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATNYDLS
SQ  VVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHK
SQ  EKSAQCFKMYYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEYDYVI
SQ  FTQTTETAHSCNVNRFNVAITRAKIGILCIMSDRDLYDKLQFTSLEVPRRNVATLQAENVTGLFKDCSKIITGLHPTQAP
SQ  THLSVDTKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFITREEAIRHVRAWIGFDVEGCHATRDAVGTN
SQ  LPLQLGFSTGVNLVAVPTGYVDTENSTEFTRVNAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSDTLKGLSDRVVFV
SQ  LWAHGFELTSMKYFVKIGPERTCCLCDKRATCFSTSSDTYACWNHSVGFDYVYNPFMIDVQQWGFTGNLQSNHDQHCQVH
SQ  GNAHVASCDAIMTRCLAVHECFVKRVDWSVEYPIIGDELKINAACRKVQHMVVKSALLADKFTVLHDIGNPKAIRCVPQA
SQ  EVDWKFYDAQPCSDKAYKIEELFYSYATHHDKFTDGVCLFWNCNVDRYPANAIVCRFDTRVLSNLNLPGCDGGSLYVNKH
SQ  AFHTPAFDKSAFTHLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRHHANEYRQYLDAYNMMISA
SQ  GFSLWIYKQFDTYNLWNTFTKLQSLENVAYNVVNKGHFDGQSGEAPVSIINNAVYTKVDGIDVEIFENKTTLPVNVAFEL
SQ  WAKRNIKPVPEIKILNNLGVDIAANNVIWDYKREAPAHVSTIGVCTMTDIAKKPTESACSSLIVLFDGRVEGQVDFFRNA
SQ  RNGVLITEGSVKGLTPSKGPAQASVNGVTLIGESVKTQFNYFKKVDGIIQQLPETYFTQSRDLEDFKPRSQMETDFLELA
SQ  MDEFIQRYKLEGYAFEHIVYGDFSHGQLGGLHLMIGLAKRSQDSLLKLEDFIPMDSTVKNYFITDAQTGSSKCVCSVIDL
SQ  LLDDFVEIIKSQDLSVVSKVVKVTIDYAEISFMLWCKDGHVETFYPKLQASQAWQPGVAMPNLYKMQRMLLEKCDLQNYG
SQ  ENAVIPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGTAVLRQWLPTGTLLVDSDLNDFVSDADSTL
SQ  IGDCATVHTANKWDLIISDMYDPKTKHVLKDNDSKEGFFTYLCGFIKQKLALGGSVAVKITEHSWNADLYKLMGHFSWWT
SQ  AFVTNVNASSSEAFLIGVNYLGKPKEQIDGYTMHANYIFWRNTNPIQLSSYSLFDMSKFPLKLRGTAVMSLKENQINDMI
SQ  YSLLEKGRLIIRENNRVVVSSDILVNN
//
ID  P0C6W3;
PN  2'-O-methyltransferase;
GN  rep;
OS  694007;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W3;
DR  UNIPROT: A3EX93;
DR  PDB: 4YO9;
DR  PDB: 4YOG;
DR  PDB: 4YOI;
DR  PDB: 4YOJ;
DR  PDB: 6MEA;
DR  PDB: 6MEB;
DR  PDB: 6MEN;
DR  PDB: 6MWM;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLSKASVTTQGARGKYRAELYNEKRSDHVACTVPLCDTDDMACKLTPWFEDGETAFNQVSSILKEKGKILFVPMHMQRAM
SQ  KFLPGPRVYLVERLTGGMLSKHFLVNQLAYKDQVGAAMMRTTLNAKPLGMFFPYDSSLETGEYTFLLRKNGLGGQLFRER
SQ  PWDRKETPYVEILDDLEADPTGKYSQNLLKKLIGGDCIPIDQYMCGKNGKPIADYAKIVAKEGLTTLADIEVDVKSRMDS
SQ  DRFIVLNKKLYRVVWNVTRRNVPYPKQTAFTIVSVVQCDDKDSVPEHTFTIGSQILMVSPLKATNNKNFNLKQRLLYTFY
SQ  GKDAVQQPGYIYHSAYVDCNACGRGTWCTGNAIQGFACDCGANYSANDVDLQSSGLVPRNALFLANCPCANNGACSHSAA
SQ  QVYNILDGKACVEVGGKSFTLTFGGVVYAYMGCCDGTMYFVPRAKSCVSRIGDAIFTGCTGTWDKVVETANLFLEKAQRS
SQ  LNFCQQFALTEVVLAILSGTTSTFEELRDLCHNASYEKVRDHLVNHGFVVTIGDYIRDAINIGANGVCNATINAPFIAFT
SQ  GLGESFKKVSAIPWKICSNLKSALDYYSSNIMFRVFPYDIPCDVSNFVELLLDCGKLTVATSYFVLRYLDEKFDTVLGTV
SQ  SSACQTALSSFLNACVAASRATAGFINDMFKLFKVLMHKLYVYTSCGYVAVAEHSSKIVQQVLDIMSKAMKLLHTNVSWA
SQ  GTKLSAIIYEGREALLFNSGTYFCLSTKAKTLQGQMNLVLPGDYNKKTLGILDPVPNADTIDVNANSTVVDVVHGQLEPT
SQ  NEHGPSMIVGNYVLVSDKLFVRTEDEEFYPLCTNGKVVSTLFRLKGGMPSKKVTFGDVNTVEVTAYRSVSITYDIHPVLD
SQ  ALLSSSKLATFTVEKDLLVEDFVDVIKDEVLTLLTPLLRGYDIDGFDVEDFIDVPCYVYNQDGDCAWSSNMTFSINPVED
SQ  VEEVEEFIEDDYLSDELPIADDEEAWARAVEEVMPLDDILVAEIELEEDPPLETALESVEAEVVETAEAQEPSVESIDST
SQ  PSTSTVVGENDLSVKPMSRVAETDDVLELETAVVGGPVSDVTAIVTNDIVSVEQAQQCGVSSLPIQDEASENQVHQVSDL
SQ  QGNELLCSETKVEIVQPRQDLKPRRSRKSKVDLSKYKHTVINNSVTLVLGDAIQIASLLPKCILVNAANRHLKHGGGIAG
SQ  VINKASGGDVQEESDEYISNNGPLHVGDSVLLKGHGLADAILHVVGPDARNNEDAALLKRCYKAFNKHTIVVTPLISAGI
SQ  FSVDPKVSFEYLLANVTTTTYVVVNNEDIYNTLATPSKPDGLVYSFEGWRGTVRTAKNYGFTCFICTEYSANVKFLRTKG
SQ  VDTTKKIQTVDGVSYYLYSARDALTDVIAAANGCSGICAMPFGYVTHGLDLAQSGNYVRQVKVPYVCLLASKEQIPIMNS
SQ  DVAIQTPETAFINNVTSNGGYHSWHLVSGDLIVKDVCYKKLLHWSGQTICYADNKFYVVKNDVALPFSDLEACRAYLTSR
SQ  AAQQVNIEVLVTIDGVNFRTVILNDTTTFRKQLGATFYKGVDISDAFPTVKMGGESLFVADNLSESEKVVLKEYYGTSDV
SQ  TFLQRYYSLQPLVQQWKFVVHDGVKSLKLSNYNCYINATIMMIDMLHDIKFVVPALQNAYLRYKGGDPYDFLALIMAYGD
SQ  CTFDNPDDEAKLLHTLLAKAELTVSAKMVWREWCTVCGIRDIEYTGMRACVYAGVNSMEELQSVFNETCVCGSVKHRQLV
SQ  EHSAPWLLVSGLNEVKVSTSTDPIYRAFNVFQGVETSVGHYVHIRVKDGLFYKYDSGSLTKTSDMKCKMTSVWYPTVRYT
SQ  ADCNVVVYDLDGVTKVEVNPDLSNYYMKDGKYYTSKPTIKYSPATILPGSVYSNSCLVGVDGTPGSDTISKFFNDLLGFD
SQ  ETKPISKKLTYSLLPNEDGDVLLSEFSNYNPVYKKGVMLKGKPILWVNNGVCDSALNKPNRASLRQLYDVAPIVLDNKYT
SQ  VLQDNTSQLVEHNVPVVDDVPITTRKLIEVKCKGLNKPFVKGNFSFVNDPNGVTVVDTLGLTELRALYVDINTRYIVLRD
SQ  NNWSSLFKLHTVESGDLQIVAAGGSVTRRARVLLGASSLFASFAKITVTATTAACKTAGRGFCKFVVNYGVLQNMFVFLK
SQ  MLFFLPFNYLWPKKQPTVDIGVSGLRTAGIVTTNIVKQCGTAAYYMLLGKFKRVDWKATLRLFLLLCTTILLLSSIYHLV
SQ  LFNQVLSSDVMLEDATGILAIYKEVRSYLGIRTLCDGLVVEYRNTSFDVMEFCSNRSVLCQWCLIGQDSLTRYSALQMLQ
SQ  THITSYVLNIDWIWFALEFFLAYVLYTSSFNVLLLVVTAQYFFAYTSAFVNWRAYNYIVSGLFFLVTHIPLHGLVRVYNF
SQ  LACLWFLRKFYSHVINGCKDTACLLCYKRNRLTRVEASTIVCGTKRTFYIAANGGTSYCCKHNWNCVECDTAGVGNTFIC
SQ  TEVANDLTTTLRRLIKPTDQSHYYVDSVVVKDAVVELHYNRDGSSCYERYPLCYFTNLEKLKFKEVCKTPTGIPEHNFLI
SQ  YDTNDRGQENLARSACVYYSQVLCKPMLLVDVNLVTTVGDSREIAIKMLDSFINSFISLFSVSRDKLEKLINTARDCVRR
SQ  GDDFQNVLKTFTDAARGHAGVESDVETTMVVDALQYAHKNDIQLTTECYNNYVPGYIKPDSINTLDLGCLIDLKAASVNQ
SQ  TSMRNANGACVWNSGDYMKLSDSFKRQIRIACRKCNIPFRLTTSKLRAADNILSVKFSATKIVGGAPSWLLRVRDLTVKG
SQ  YCILTLFVFTVAVLSWFCLPSYSIATVNFNDDRILTYKVIENGIVRDIAPNDVCFANKYGHFSKWFNENHGGVYRNSMDC
SQ  PITIAVIAGVAGARVANVPANLAWVGKQIVLFVSRVFANTNVCFTPINEIPYDTFSDSGCVLSSECTLFRDAEGNLNPFC
SQ  YDPTVLPGASSYADMKPHVRYDMYDSDMYIKFPEVIVESTLRITKTLATQYCRFGSCEESAAGVCISTNGSWALYNQNYS
SQ  TRPGIYCGDDYFDIVRRLAISLFQPVTYFQLSTSLAMGLVLCVFLTAAFYYINKVKRALADYTQCAVVAVVAALLNSLCL
SQ  CFIVANPLLVAPYTAMYYYATFYLTGEPAFIMHISWYVMFGAVVPIWMLASYTVGVMLRHLFWVLAYFSKKHVDVFTDGK
SQ  LNCSFQDAASNIFVIGKDTYVALRNAITQDSFVRYLSLFNKYKYYSGAMDTASYREACAAHLCKALQTYSETGSDILYQP
SQ  PNCSVTSSVLQSGLVKMSAPSGAVENCIVQVTCGSMTLNGLWLDNTVWCPRHIMCPADQLTDPNYDALLISKTNHSFIVQ
SQ  KHIGAQANLRVVAHSMVGVLLKLTVDVANPSTPAYTFSTVKPGASFSVLACYNGKPTGVFTVNLRHNSTIKGSFLCGSCG
SQ  SVGYTENGGVINFVYMHQMELSNGTHTGSSFDGVMYGAFEDKQTHQLQLTDKYCTINVVAWLYAAVLNGCKWFVKPTRVG
SQ  IVTYNEWALSNQFTEFVGTQSIDMLAHRTGVSVEQMLAAIQSLHAGFQGKTILGQSTLEDEFTPDDVNMQVMGVVMQSGV
SQ  KRISYGFIHWLISTFVLAYVSVMQLTKFTMWTYLFETIPTQMTPLLLGFMACVMFTVKHKHTFMSLFLLPVALCLTYANI
SQ  VYEPQTLISSTLIAVANWLTPTSVYMRTTHFDFGLYISLSFVLAIIVRRLYRPSMSNLALALCSGVMWFYTYVIGDHSSP
SQ  ITYLMFITTLTSDYTITVFATVNLAKFISGLVFFYAPHLGFILPEVKLVLLIYLGLGYMCTMYFGVFSLLNLKLRVPLGV
SQ  YDYSVSTQEFRFLTGNGLHAPRNSWEALILNFKLLGIGGTPCIKVATVQSKLTDLKCTSVVLLTVLQQLHLESNSKAWSY
SQ  CVKLHNEILAAVDPTEAFERFVCLFATLMSFSANVDLDALANDLFENSSVLQATLTEFSHLATYAELETAQSSYQKALNS
SQ  GDASPQVLKALQKAVNVAKNAYEKDKAVARKLERMAEQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGVI
SQ  ANARNGCVPLSIVPLCASNKLRVVIPDISVWNKVVNWPSVSYAGSLWDITVINNVDNEVVKPTDVVETNESLTWPLVIEC
SQ  SRSSSSAVKLQNNEIHPKGLKTMVITAGVDQVNCNSSAVAYYEPVQGHRMVMGLLSENAHLKWAKVEGKDGFINIELQPP
SQ  CKFLIAGPKGPEIRYLYFVKNLNNLHRGQLLGHIAATVRLQAGANTEFASNSTVLTLVAFAVDPAKAYLDYVGSGGTPLS
SQ  NYVKMLAPKTGTGVAISVKPEATADQETYGGASVCLYCRAHIEHPDVSGVCKYKTRFVQIPAHVRDPVGFLLKNVPCNVC
SQ  QYWVGYGCNCDALRNNTVPQSKDTNFLNRVRGSSVNARLEPCSSGLTTDVVYRAFDICNFKARVAGIGKYYKTNTCRFVQ
SQ  VDDEGHKLDSYFIVKRHTMSNYELEKRCYDLLKDCDAVAIHDFFIFDVDKTKTPHIVRQSLTEYTMMDLVYALRHFDQNN
SQ  CEVLKSILVKYGCCEQSYFDNKLWFDFVENPSVIGVYHKLGERIRQAMLNTVKMCDHMVKSGLVGVLTLDNQDLNGKWYD
SQ  FGDFVITQPGAGVAIVDSYYSYLMPVLSMTNCLAAETHKDCDFNKPLIEWPLLEYDYTDYKIGLFNKYFKYWDQTYHPNC
SQ  VNCSDDRCILHCANFNVLFSMVLPNTSFGPIVRKIFVDGVPFIVSCGYHYKELGLVMNMDFNIHRHRLALKELMMYAADP
SQ  AMHIASASALWDLRTPCFSVAALTTGLTFQTVRPGNFNKDFYDFVVSRGFFKEGSSVTLKHFFFAQDGHAAITDYSYYAY
SQ  NLPTMVDIKQMLFCMEVVDKYFDIYDGGCLNASEVIVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAVTKRNVLPT
SQ  ITQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGATCVIGTTKFYGGWDFMLKTLYKDVESPHLMGWD
SQ  YPKCDRAMPNMCRILASLILARKHSTCCTNSDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQ
SQ  ATTANVSALMSANGNTIIDREIKDMQFDLYINVYRKVVPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYVAS
SQ  IQNFKETLYYQNNVFMSEAKCWVETNLEKGPHEFCSQHTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTVMMER
SQ  YVSLAIDAYPLTKHDDTEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDDSAKFWEEGFYRDLYSSPTTLQAVGSCV
SQ  VCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVCNAPGCDVSDVTKLYLGGMSYYCNDHRPVCSFPLCAN
SQ  GLVFGLYKNMCTGSSSIMEFNRLATCDWSDSGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERELILV
SQ  WEVGKSKPPLNRNYVFTGYHLTKNSKVQLGEYVFERIDYSDAVSYKSSTTYKLAVGDIFVLTSHSVATLSAPTIVNQERY
SQ  LKITGIYPTITVPEEFANHVVNFQKAGFSKYVTVQGPPGTGKSHFAIGLAIYYPTARIVYTACSHAAVDALCEKAFKYLN
SQ  IAKCSRIIPAKARVECYDRFKVNDTNSQYLFSTVNALPEISVDILVVDEVSMCTNYDLSIINSRVKAKHIVYVGDPAQLP
SQ  APRTLLIRGTLEPENFNSVTRLMCNLGPDIFLSVCYRCPKEIVSTVSALVYNNKLSAKKDASGQCFKILFKGSVTHDASS
SQ  AINRPQLNFVKTFIAANPNWSKAVFISPYNSQNAVARSMLGLTTQTVDSSQGSEYPYVIFCQTADTAHANNLNRFNVAVT
SQ  RAQKGILCVMTSQVLFDSLEFAELSLNNYKLQSQIVTGLFKDCSREDTGLPPAYAPTYLSVDAKYKTTDELCVNLNITPN
SQ  VTYSRVISRMGFKLDATIPGYPKLFITRDEAIRQVRSWVGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTE
SQ  WGSMLTTISARPPPGEQFKHLVPLMNKGATWPIVRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQRCS
SQ  MCSRRASTFSSPLQSYACWSHSSGYDYVYNPFFVDVQQWGYVGNLATNHDRYCGIHAGAHVASSDAIMTRCLAIYDCFIE
SQ  RVDWDVTYPYISHEQKLNSCCRTVERNVVRSAVLSGKFEKIYDIGNPKGIAIISEPVEWHFYDAQPLSNKVKKLFYTDDV
SQ  SKQFEDGLCLFWNCNVSKYPSNAVVCRFDTRVHSEFNLPGCNGGSLYVNKHAFHTPAYDINAFRDLKPLPFFYYSTTPCE
SQ  VHGSGNMLEDIDYVPLKSAVCITACNLGGAVCRKHAAEYRDYMEAYNIVSAAGFRLWVYKTFDIYNLWSTFVKVQGLENI
SQ  AFNVIKQGHFTGVDGELPVAVVNDKIFTKNGTDDVCIFKNETALPTNVAFELYAKRAVRSHPDLNLLRNLEVDVCYNFVL
SQ  WDYDRNNIYGTTTIGVCKYTDIDVNPNLNMCFDIRDKGSLERFMSMPNGVLISDRKIKNYPCISGPKHAYFNGAILRNID
SQ  AKQPVIFYLYKKVNNEFVSFSDTFYTCGRTVGDFTVLTPMEEDFLVLDSDVFIKKYGLEDYAFEHVVYGDFSHTTLGGLH
SQ  LLIGLYKKMREGHILMEEMLKDRATVHNYFITDSNTASYKAVCSVIDLRLDDFVTIIKEMDLDVVSKVVKVPIDLTMIEF
SQ  MLWCRDGKVQTFYPRLQATNDWKPGLTMPSLFKVQQMNLEPCLLANYKQSIPMPNGVHMNVAKYMQLCQYLNTCTLAVPA
SQ  NMRVIHFGAGCEKGVAPGTSVLRQWLPLDAVLIDNDLNEFVSDADITIFGDCVTVHVGQQVDLLISDMYDPCTKAVGEVN
SQ  QTKALFFVYLCNFIKNNLALGGSVAIKITEHSWSADLYKIMGRFAYWTVFCTNANASSSEGFLIGINFLGELKEEIDGNV
SQ  MHANYIFWRNSTPMNLSTYSLFDLSRFPLKLKGTPVLQLKESQINELVISLLSQGKLLIRDNDTLNVSTDVLVNFRKRL
//
ID  P0C6W4;
PN  2'-O-methyltransferase;
GN  rep;
OS  694008;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W4;
DR  UNIPROT: A3EXC9;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9GZQ8; IntAct: EBI-29445734; Score: 0.44
DE  Interaction: Q9H492; IntAct: EBI-29451709; Score: 0.44
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFVAGVAPQGARGKYRAELNTEKRTDHVSLKASLCDAGDLVLKISPWFMDGESAYKHVSEQLSKGSKLLFVPQTLKGFI
SQ  RHLPGPRVYLVERLTGGTYSDPFMVNQLAYQNAAGEGVIGTTLQGKRVGMFFPFDADLVTGEFQFLLRKKGFGGNRFRDA
SQ  PWDYNWTPYSDLMDALEADPCGKYSQSLLKKLVGGDFTPIDQYMCGKNGKPIAEFAALMASEGITKLADVEAEVKSRTDS
SQ  DRYIVFKNKLYRIVWNVQRKDVAYSKQSAFTMNSIVQLDTMEDVPRHSFTIGSEIQVIAPSTAVQANGHLNLKQRLLYAF
SQ  YGKQAVSEPNYIYHSAYVDCTSCGKGSWLTGNAVQGFACDCGAHYCANDVDLQSSGLVRKNAVLLTTCPCNKDGECKHTL
SQ  PQLVSMMTDKCDVEVVGKTFILTYGGVIYAYMGCSGGTMHFIPRAKSCVSKIGDAIFTGCTGTWSKVCETANLFLERAQH
SQ  AINFVNEFVLTETVVALLSGTTSSIEELRDLCRNATFEKVRDYLTPRGWIVTMGSYIEGVINVGAAGVCNAALNAPFIVL
SQ  SGLGESFKKVAATPWKLCSSLRETLDHYADSITYRVFPYDIPCDVTDYTALLLDCAVLTGASAYFVARYVDEKVEQLTNL
SQ  VFSSCQSAVAAFVQACMSTYKATAKFISDMFTLIKVVSERLYVYTSVGFVVVGDYSSQLLKQFMHILSKAMQLLHTTVSW
SQ  AGSKLPSVVYNGRDSLVFPSGTYYCVSTQGRSLQDQFDLVIPGDLSKKQIGILEPTPNSTTVDKKINTNVVEVVVGQLEP
SQ  TKEHSPELVVGDYVIISNKIFVRSVEDSETVFYPLCTDGKIVPTLFRLKGGAPPKGVKFGGEQTKEITAVRSVSVDYDVH
SQ  PVLDALLAGSELATFTVEKDLPVKDFVDVVKDEVIELLSKLLRGYNVDGFDLEDFADTPCYVYNAEGDLAWSSTMTFSVN
SQ  PVEEVEEECDDDYVEDEYLSEEMLVEEDENSWAAAVEAVIPMEDVQLDTLVAEIDVSEPADDVAEQASTEEVEVPSACVL
SQ  EASQVANAAEVESCEAEVSSSIPLHEDANAAKANDCAEGMPALDSTETVSKLSVDTPVGDVTQDDATSSNATVISEDVHT
SQ  ATHSKGLVAVPEVVPEKALGTSVERMRSTSEWTVVETSLKQETAVIVKNDSSAKPQRVKKPKAENPLKNFKHIVLNNDVT
SQ  LVFGDAIAVARATEDCILVNAANTHLKHGGGIAAAIDRASGGLVQAESDDYVNFYGPLNVGDSTLLKGHGLATGILHVVG
SQ  PDARANQDIQLLKRCYKAFNKYPLVVSPLISAGIFCVEPRVSLEYLLSVVHTKTYVVVNSEKVYNDLAAPKPPTGLTYSH
SQ  EGWRGIIRNAKSFGFTCFICTDQSANAKLLKGRGVDLTKKTQTVDGVKYYLYSSKDPLTDIITAANACKGICAMPIGYVT
SQ  HGLDLAQAGQQVKKITVPYVCLLASKDQVPILNSDVAVQTPEQSFINTVIANGGYHCWHLVTGELIVKGVSYRKLLNWSD
SQ  QTICYADNKFYVVKGQIALPFDSLEKCRTYLTSRAAQQKNVDVLVTIDGVNFRTVVLNNTTTYRVQLGSVFYKGSDISDT
SQ  IPTEKMSGEAVYLADNLSEAEKAVLSEVYGTADTAFLHRYYSLLALVKKWKYTVHDGVKSLKLNSNNCYVNVTMLMLDML
SQ  KEIKFIVPALQAAYLKHKGGDSTEFIALIMAYGDCTYGEPDDASRLLHTILSKAELTTQAKMVWRQWCNVCGVQDTTTTG
SQ  LKACIYVGMNSLDELHATHEECCQCGDVRKRQLVEHNAPWLLLSGLNEAKVMTPTSQSAGPDYTAFNVFQGVETSVGHYL
SQ  HVRVKDNLLYKYDSGSLSKTSDMKCKMTDVYYPKQRYSADCNVVVYSLDGNTWADVDPDLSAFYMKDGKYFTKKPVIEYS
SQ  PATILSGSVYTNSCLVGHDGTIGSDAISSSFNNLLGFDNSKPVSKKLTYSFFPDFEGDVILTEYSTYDPIYKNGAMLHGK
SQ  PILWVNNSKFDSALNKFNRATLRQVYDIAPVTLENKYTVLQDNQIQQVEVEAPKEDAKPQSPVQVAEDIDNKLPIIKCKG
SQ  LKKPFVKDGYSFVNDPQGVNVIDTLGIDDLRALYVDRNLRLIVLKENNWSALFNIHTVEKGDLSVIAASGSITRRVKILL
SQ  GASSLFAQFASVTVNVTTAMGKALGRMTRNVITNTGIIGQGFALLKMLLILPFTFWKSKNQSTVKVEVGALRTAGIVTTN
SQ  VVKQCASAAYDVLVVKFKRIDWKSTLRLLFLICTTGLLLSSLYYLFLFHQVLTSDVMLDGAEGMLATYRELRSYLGIHSL
SQ  CDGMVEAYRNVSYDVNDFCSNRSALCNWCLIGQDSLTRYSAFQMIQTHVTSYVINIDWVWFVMEFALAYVLYTSTFNVLL
SQ  LVVSSQYFFSYTGAFVNWRSYNYLVSGYFFCVTHIPLLGLVRIYNFLACLWFLRRFYNHVINGCKDTACLLCYKRNRLTR
SQ  VEASTVVCGSKRTFYIVANGGTSFCCRHNWNCVDCDTAGIGNTFICEEVANDLTTSLRRLVKPTDKSHYYVESVTVKDSV
SQ  VQLHYSREGASCYERYPLCYFTNLDKLKFKEVCKTPTGIPEHNFLIYDSSDRGQENLARSACVYYSQVLSKPMLLVDSNM
SQ  VTTVGDSREIASKMLDSYVNSFISLFGVNRDKLDKLVATARDCVKRGDDFQTVIKTFTDAARGPAGVESDVETSSIVDAL
SQ  QYAYKHDLQLTTEGFNNYVPSYIKPDSVATADLGCLIDLNAASVNQTSIRNANGACIWNSSDYMKLSDSLKRQIRIACRK
SQ  CNIPFRLTTSRLRSADNILSVKFSATKLSGGAPKWLLKLRDFTWKSYCVVTLVVFAMAVLSYLCLPAFNMSQVSFHEDRI
SQ  LTYKVVENGIIRDITPSDTCFANKYQSFSKWFNEHYGGLFNNDISCPVTVAVIAGVAGARVPNLPANVAWVGRQIVLFVS
SQ  RVFASSNNVCYTPTAEIPYERFSDSGCVLASECTLFRDAEGKINPYCYDPTVLPGASAYDQMKPHVRYDMYDSDMYIKFP
SQ  EVVFESTLRITKTLATRYCRFGSCEDANEGVCITTNGSWAIYNDHYANKPGVYCGDNYFDIVRRLGLSLFQPVTYFQLST
SQ  SLALGVMLCIFLTIAFYYVNKVKRALADYTQCAVVAVAAALLNSLCLCFVVSNPLLVLPYTALYYYATFYLTGEPAFVMH
SQ  VSWFVMFGTVVPIWMVFAYIVGVCLRHLLWVMAYFSKKHVEVFTDGKLNCSFQDAAANIFVINKDTYVALRNSITQDSYN
SQ  RYLSMFNKYKYYSGAMDTASYREASAAHLCKALQVYSETGSDVLFQPPNCSVTSSVLQSGLVKMAAPSGVVENCMVQVTC
SQ  GSMTLNGLWLDNYVWCPRHVMCPADQLSDPNYDALLVSKTNLSFIVQKNVGAPANLRVVGHTMVGTLLKLTVESANPQTP
SQ  AYTFTTVKPGASFSVLACYNGRPTGVFMVNMRQNSTIKGSFLCGSCGSVGYTQEGNVINFCYMHQMELSNGTHTGCAFDG
SQ  VMYGAFEDRQVHQVQLSDKYCTINIVAWLYAAILNGCNWFVKPNKTGIATFNEWAMSNQFTEFIGTQSVDMLAHKTGVSV
SQ  EQLLYAIQTLHKGFQGKTILGNSMLEDEFTPDDVNMQVMGVVMQSGVKRISYGLVHWLFTTLLLAYVATLQLTKFTIWNY
SQ  LFEVIPLQLTPLVLCVMACVMLTVKHKHTFLTLFLLPTAICLTYANIVYEPQTPVSSALIAVANWLNPASVYMRTTHTDL
SQ  GVYLSLCFALAVVVRRLYRPNASNLALALGSAMVWFYTYTTGDCSSPLTYLMFLTTLTSDYTVTVFLAVNVAKFFARVVF
SQ  LYAPHAGFIFPEVKLVLLMYLAVGYFCTVYFGVFSLLNLKLRVPLGVYDYTVSTQEFRYLTGNGLHAPRNSWEALRLNMK
SQ  LIGIGGTPCIKIASVQSKLTDLKCTSVVLLSVLQQLHLEANSKAWAHCVKLHNDILAATDPTEAFDNFVCLFATLMSFSA
SQ  NVDLEALASDLLDHPSVLQATLSEFSHLASYAELEAAQSSYQKALNSGDASPQVLKALQKAVNIAKNAYEKDKAVARKLE
SQ  RMAEQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGVISNARNGCVPLSVVPLCASNKLRVVIPDITIWNK
SQ  VVTWPSLSYAGALWDISLINNVDGEVVKSSDVTETNESLTWPLVLECTRAASSAVTLQNNEIRPSGLKTMVVSAGIDHAN
SQ  CNTSSLAYYEPVEGRKMLMGILSENAHLKWAKVEGRDGFVNIELQPPCKFLIAGPKGPEVRYLYFVKNLNNLHRGQLLGH
SQ  IAATVRLQAGSNTEFAINSSVLSAVTFSVDPGKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAVSVKPEANADQDTYGGAS
SQ  VCLYCRAHIEHPDVTGVCKFKGKFVQVPLHIRDPVGFCLQNTPCNVCQFWIGHGCNCDALRGTTIPQSKDSNFLNRVRGS
SQ  IVNARIEPCASGLTTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVEVDDEGHRLDSFFVVKRHTMENYELEKRCYDLVK
SQ  DCDAVAVHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNNCEVLKSILVKYGCCDASYFDNKLWFDFVENPNV
SQ  ISVYHKLGERIRQAVLNTVKFCDQMVKSGLVGVLTLDNQDLNGKWYDFGDFVITQPGAGVAIVDSYYSYLMPVLSMTNCL
SQ  AAETHRDCDLTKPLIEWPLLEYDYTDYKIGLFEKYFKXWDQQYHPNCVNCTDDRCVLHCANFNVLFSMTLPGTSFGPIVR
SQ  KIFVDGVPFVISCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASASALWDLRTPCFSVAALTTGLTFQTVR
SQ  PGNFNKDFYDFVVSKGFFKEGSSVTLRHFFFAQDGHAAITDYSYYAYNLPTMCDIKQMLFCMEVVDRYFEIYDGGCLNAS
SQ  EVIVNNLDKSAGHPFNKFGKARVYYESLSYQEQDELFAMTKRNVLPTITQMNLKYAISAKNRARTVAGVSILSTMTNRQY
SQ  HQKMLKSMAATRGSTCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHSTCCTNTDR
SQ  FYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNTIVDEEVKDMQFELYVNV
SQ  YRKSQPDPKFVDRYYAFLNKHFSMMILSDDGVVCYNSDYATKGYIASIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHE
SQ  FCSQHTLFIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHDDPEYQNVFWVYLQYIEKL
SQ  YKDLTGHMLDSYSVMLCGDNSAKFWEESFYRDLYTAPTTLQAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPH
SQ  KMVLSVSPYVCNAPGCDVADVTKLYLGGMSYFCIDHRPVCSFPLCANGLVFGLYKNMCTGSPSVTEFNRLATCDWTESGD
SQ  YTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERELLLVWEAGKAKPPLNRNYVFTGYHITKNSKVQLGEYV
SQ  FERIDYSDAVSYKSSTTYKLAVGDIFVLTSHSVATLQAPTIVNQERYVKITGLYPTLTVPEEFANHVANFQKAGFSKFVT
SQ  VQGPPGTGKSHFAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDQFKVNETNSQYLFST
SQ  INALPETSADILVVDEVSMCTNYDLSVINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLS
SQ  VCYRCPEEIVNTVSALVYNNKLVAKKPASGQCFKILYKGSVTHDASSAINRPQLNFVKSFIAANPNWSKAVFISPYNSQN
SQ  AVARSVLGLTTQTVDSSQGSEYPYVIFCQTADTAHANNINRFNVAVTRAQKGILCVMTSQALFDSLEFAEVSLNNYKLQS
SQ  QIVTGLYKDCSRESSGLHPAYAPTYVSVDDKYKTSDELCVNLNVPANVPYSRVISRMGFKLDASIPNYPKLFITRDEAIR
SQ  QVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGSMLTSIAARPPPGEQFKHLVPLMNKGAAWPI
SQ  VRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQRCCMCNRRASTYSSPLHSYACWSHSSGYDYVYNPFF
SQ  VDVQQWGYIGNLATNHDRYCSVHQGAHVASNDAVMTRCLAIHDCFIERVEWDITYPYISHEKRLNSCCRAVERNVVRAAL
SQ  LAGRFERVYDIGNPKGIPIVDDPVVDWHYYDAQPLSKKVQQLFYTEDCAKNFSDGLCLFWNCNVPRYPNNAIVCRFDTRV
SQ  HSEFNLPGCDGGSLYVNKHAFHTPAYDASAFRDLKPLPFFYYSTTPCEVHGNGNMLEDIDYVPLKSAVCITACNLGGAVC
SQ  RKHAAEYRDYMEAYNLVSASGFRLWCYKTFDVYNLWSTFTKIQGLENIAYNVIKQGHFTGVEGELPVAVVNDKIYTKSDV
SQ  NDVCIFENKTTLPTNIAFELYAKRAVRSHPDFNLLRNLEVDVCYKFVLWDYERSNIYGSATIGVCKYTDIDVNSALNICF
SQ  DIRDNGSLERFMSLPNGILISDRKVKNYPCIVSSNYAYFNGTLIRDNTGNSQSSDGEVKQPVTFYIYKKVNNEFVQFTDT
SQ  YYTLGRTVSDFTPVSEMEKDFLALDSDVFIKKYKLEAYAFEHVVYGDFSRTTLGGLHLLIGLYKKHQEGHIIMEEMLKER
SQ  ATVHNYFVTESNTASFKAVCSVIDLKLDDFVDIIKAMDLSVVSKVVKIPIDLTMIEFMLWCKDGQVQTFYPRLQAINDWK
SQ  PGLAMPSLFKVQNSNLEPCMLPNYKQSIPMPQGVHMNIAKYMQLCQYLNTCTIAVPANMRVMHFGAGSDKGVAPGSSVLR
SQ  QWLPTDAILIDNDLNEYVSDADITLFGDCVTVRVGQQVDLLISDMYDPSTKVVGETNEAKALFFVYLCNFIKNNLALGGS
SQ  VAIKITEHSWSAELYELMGRFAWWTVFCTNANASSSEGFLIGINYLGELKEVIDGNVMHANYIFWRNTTLMNLSTYSLFD
SQ  LSRFPLKLKGTPVLQLKESQINELVISLLSQGKLIIRDNDTLSVSTDVLVNFYRKPHKRSKC
//
ID  P0C6W5;
PN  2'-O-methyltransferase;
GN  rep;
OS  694006;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W5;
DR  UNIPROT: A3EXG5;
DR  PDB: 5UTV;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:19264783}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UNP9; IntAct: EBI-29486867; Score: 0.44
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGVPDPPKLKSMVVTTLKWCDPFANPNVTGWDIPIEEALEYAKQQLRTPEPQLVFVPYYLSHAPGISGDRVVITDSIWY
SQ  ATNFGWQPIRELAMDKDGVRYGRGGTHGVLLPMQDPSFIMGDIDIQIRKYGIGANSPPDVLPLWDGFSDPGPDVGPYLDF
SQ  PDNCCPTKPKAKRGGDVYLSDQYGFDNNGILVEPVMKLLGVIKSDFTLEQLLAALGKYRTEDGYDLPDGYVKVAIKVGRK
SQ  AVPVLKQSIFTVVGVTEQLVPGYYYPFSTSSVVEHTKPTRGGPVGKTVEAVMLSLYGTNNYNPATPVARLKCSYCDYYGW
SQ  TPLKDIGTVNCLCGAEFQLTSSCVDAESAGVIKPGCVMLLDKSPGMRLIPGNRTYVSFGGAIWSPIGKVNGVTVWVPRAY
SQ  SIVAGEHSGAVGSGDTVAINKELVEYLIEGIRVDADTLDNPTCATFIANLDCDTKAPVVHTVESLQGLCLANKIMLGDKP
SQ  LPTDEFHPFIVGLAYHVQRACWYGALASRTFEAFRDFVRTEEERFAQFFGKVCAPINGCVYLAYTTGRVTLFSAYQVLNT
SQ  AIAKSKDAFGGVAAIVVDMLKPILEWVLKKMSIAKGAWLPYAEGLLALFKAQFTVVKGKFQFLRASLNSKCHSLCDLLTT
SQ  IMSKLLTSVKWAGCKVDALYTGTYYYFSRKGVLTEVQLCAKRLGLLLTPKQQKMEVEVLDGDFDAPVTLTDLELEECTGV
SQ  LEEVFGASDVKLVKGTLVSLASKLFVRTEDGFLYRYVKSGGVLGKAFRLRGGGVSKVTFGDEEVHTIPNTVTVNFSYDVC
SQ  EGLDAILDKVMAPFQVEEGTKLEDLACVVQKAVYERLSDLFSDCPAELRPINLEDFLTSECFVYSKDYEKILMPEMYFSL
SQ  EDAVPVDDEMVDDIEDTVEQASDSDDQWLGDEGAEDCDNTIQDVDVATSMTTPCGYTKIAEHVYIKCADIVQEARNYSYA
SQ  VLVNAANVNLHHGGGVAGALNRATNNAMQKESSEYIKANGSLQPGGHVLLSSHGLASHGILHVVGPDKRLGQDLALLDAV
SQ  YAAYTGFDSVLTPLVSAGIFGFTVEESLCSLVKNVACTTYVVVYDRQLYERALATSFDVPGPQSSVQHVPAIDWAEAVEV
SQ  QESIVDQVETPSLGAVDTVDSNADSGLNETARSPENVVGSVPDDVVADVESCVRDLVRQVVKKVKRDKRPPPIVPQQTVE
SQ  QQPQEISSPGDCNTVLVDVVSMSFSAMVNFGKEKGLLIPVVIDYPAFLKVLKRFSPKEGLFSSNGYEFYGYSRDKPLHEV
SQ  SKDLNSLGRPLIMIPFGFIVNGQTLAVSAVSMRGLTVPHTVVVPSESSVPLYRAYFNGVFSGDTTAVQDFVVDILLNGAR
SQ  DWDVLQTTCTVDRKVYKTICKRGNTYLCFDDTNLYAITGDVVLKFATVSKARAYLETKLCAPEPLIKVLTTVDGINYSTV
SQ  LVSTAQSYRAQIGTVFCDGHDWSNKNPMPTDEGTHLYKQDNFSSAEVTAIREYYGVDDSNIIARAMSIRKTVQTWPYTVV
SQ  DGRVLLAQRDSNCYLNVAISLLQDIDVSFSTPWVCRAYDALKGGNPLPMAEVLIALGKATPGVSDDAHMVLSAVLNHGTV
SQ  TARRVMQTVCEHCGVSQMVFTGTDACTFYGSVVLDDLYAPVSVVCQCGRPAIRYVSEQKSPWLLMSCTPTQVPLDTSGIW
SQ  KTAIVFRGPVTAGHYMYAVNGTLISVYDANTRRRTSDLKLPATDILYGPTSFTSDSKVETYYLDGVKRTTIDPDFSKYVK
SQ  RGDYYFTTAPIEVVAAPKLVTSYDGFYLSSCQNPQLAESFNKAINATKTGPMKLLTMYPNVAGDVVAISDDNVVAHPYGS
SQ  LHMGKPVLFVTRPNTWKKLVPLLSTVVVNTPNTYDVLAVDPLPVNNETSEEPISVKAPIPLYGLKATMVLNGTTYVPGNK
SQ  GHLLCLKEFTLTDLQTFYVEGVQPFVLLKASHLSKVLGLRVSDSSLHVNHLSKGVVYAYAATRLTTRVTTSLLGGLVTRS
SQ  VRKTADFVRSTNPGSKCVGLLCLFYQLFMRFWLLVKKPPIVKVSGIIAYNTGCGVTTCVLNYLRSRCGNISWSRLLKLLR
SQ  YMLYIWFVWTCLTICGVWLSEPYAPSLVTRFKYFLGIVMPCDYVLVNETGTGWLHHLCMAGMDSLDYPALRMQQHRYGSP
SQ  YNYTYILMLLEAFFAYLLYTPALPIVGILAVLHLIVLYLPIPLGNSWLVVFLYYIIRLVPFTSMLRMYIVIAFLWLCYKG
SQ  FLHVRYGCNNVACLMCYKKNVAKRIECSTVVNGVKRMFYVNANGGTHFCTKHNWNCVSCDTYTVDSTFICRQVALDLSAQ
SQ  FKRPIIHTDEAYYEVTSVEVRNGYVYCYFESDGQRSYERFPMDAFTNVSKLHYSELKGAAPAFNVLVFDATNRIEENAVK
SQ  TAAIYYAQLACKPILLVDKRMVGVVGDDATIARAMFEAYAQNYLLKYSIAMDKVKHLYSTALQQISSGMTVESVLKVFVG
SQ  STRAEAKDLESDVDTNDLVSCIRLCHQEGWEWTTDSWNNLVPTYIKQDTLSTLEVGQFMTANAKYVNANIAKGAAVNLIW
SQ  RYADFIKLSESMRRQLKVAARKTGLNLLVTTSSLKADVPCMVTPFKIIGGHRRIVSWRRVLIHVFMLLVVLNPQWFTPWY
SQ  IMRPIEYNVVDFKVIDNAVIRDITSADQCFANKFSAFENWYSNRYGSYVNSRGCPMVVGVVSDIVGSLVPGLPARFLRVG
SQ  TTLLPLVNYGLGAVGSVCYTPHYAINYDVFDTSACVLAATCTLFSSASGERMPYCADAALIQNASRYDMLKPHVMYPFYE
SQ  HSGYIRFPEVISAGVHIVRTMAMEYCKVGRCDVSEAGLCMSLQPRWVVNNAYFRQQSGVYCGTSAFDLFMNMLLPIFTPV
SQ  GAVDITTSILMGALLAVVVSMSLYYLLRFRRAFGDYSGVIFTNILAFVLNVIVLCLEGPYPMLPSIYAMVFLYATCYFGS
SQ  DIACMMHVSFLIMFAGVVPLWVTVLYIVVVLSRHILWFASLCTKRTVQVGDLAFHSFQDAALQTFMLDKEVFLRLKREIS
SQ  SDAYFKYLAMYNKYKYYSGPMDTAAYREAACSHLVMALEKYSNGGGDTIYQPPRCSVASAALQAGLTRMAHPSGLVEPCL
SQ  VKVNYGSMTLNGIWLDNFVICPRHVMCSRDELANPDYPRLSMRAANYDFHVSQNGHNIRVIGHTMEGSLLKLTVDVNNPK
SQ  TPAYSFIRVSTGQAMSLLACYDGLPTGVYTCTLRSNGTMRASFLCGSCGSPGFVMNGKEVQFCYLHQLELPNGTHTGTDF
SQ  SGVFYGPFEDKQVPQLAAPDCTITVNVLAWLYAAVLSGENWFLTKSSISPAEFNNCAVKYMCQSVTSESLQVLQPLAAKT
SQ  GISVERMLSALKVLLSAGFCGRTIMGSCSLEDEHTPYDIGRQMLGVKLQGKFQSMFRWTLQWFAIIFVLTILILLQLAQW
SQ  TFVGALPFTLLLPLIGFVAVCVGFVSLLIKHKHTYLTVYLLPVAMVTAYYNFQYTPEGVQGYLLSLYNYVNPGRIDVIGT
SQ  DLLTMLIISVACTLLSVRMVRTDAYSRIWYVCTAVGWLYNCWTGSADTVAISYLTFMVSVFTNYTGVACASLYAAQFMVW
SQ  VLKFLDPTILLLYGRFRCVLVCYLLVGYLCTCYFGVFNLINRLFRCTLGNYEYVVSSQELRYMNSHGLLPPTNSWQALML
SQ  NIKLAGIGGIPIYRVSTIQSNMTDLKCTSVVLLSVLQQLRVESSSKLWALCVKLHNEILASNSPTEAFEAFVSLLSVLLS
SQ  LPGAINLDELCSSILENNSVLQAVASEFSNLSSYVDYENAQKAYDTAVATGAPASTVNALKKAMNVAKSVLDKDVATTRK
SQ  LERMSELAMTAMYKQARAEDRRSKVTAAMQTMLFNMIRRLDSDALSNILNNARNGVVPLGVIPRTAANKLLLVVPDFSVY
SQ  TATITMPTLTYAGSAWDVMQVADADGKTVNATDITRENSVNLAWPLVVTAQRQQATSPVKLQNNELMPQTVKRMNVVAGV
SQ  SQTACVTDAVAYYNATKEGRHVMAILADTDGLAFAKVEKSTGDGFVILELEPPCKFMVDTPKGPALKYLYFTKGLKNLCR
SQ  GTVLGTLACTVRLHAGSATEVASNSSILSLCSFSVDPEATYKDYLDNGGSPIGNCVKMLTPHTGTGLAITAKPDANIDQE
SQ  SFGGASCCLYCRCHIEHPGASGVCKYKGKFVQIPLVGVNDPIGFCIRNVVCAVCNMWQGYGCPCSSLREINLQARDECFL
SQ  NRVRGTSGVARLVPLGSGVQPDIVLRAFDICNTKVAGFGLHLKNNCCRYQELDADGTQLDSYFVVKRHTESNYLLEQRCY
SQ  EKLKDCGVVARHDFFKFNIEGVMTPHVSRERLTKYTMADLVYSLRHFDNNNCDTLKEILVLRGCCTADYFDRKDWYDPVE
SQ  NPDIIRVYHNLGETVRKAVLSAVKMADSMVEQGLIGVLTLDNQDLNGQWYDFGDFIEGPAGAGVAVMDTYYSLAMPVYTM
SQ  TNMLAAECHVDGDFSKPKRVWDICKYDYTQFKYSLFSKYFKYWDMQYHPNCVACADDRCILHCANFNILFSMVLPNTSFG
SQ  PLVQKIYVDGVPFVVSTGYHYRELGVVMNQDIRQHAQRLSLRELLVYAADPAMHVAASNALADKRTVCMSVAAMTTGVTF
SQ  QTVKPGQFNEDFYNFAVKCGFFKEGSTISFKHFFYAQDGNAAISDYDYYRYNLPTMCDIKQLLFSLEVVDKYFDCYDGGC
SQ  LQASQVVVANYDKSAGFPFNKFGKARLYYESLSYADQDELFAYTKRNVLPTITQMNLKYAISAKNRARTVAGVSIASTMT
SQ  NRQFHQKMLKSIAAARGASVVIGTTKFYGGWNRMLRTLCEGVENPHLMGWDYPKCDRAMPNLLRIFASLILARKHATCCN
SQ  ASERFYRLANECAQVLSEMVLCGGGFYVKPGGTSSGDSTTAYANSVFNICQAVSANLNTFLSIDGNKIYTTYVQELQRRL
SQ  YLGIYRSNTVDNELVLDYYNYLRKHFSMMILSDDGVVCYNADYAQKGYVADIQGFKELLYFQNNVFMSESKCWVEPDITK
SQ  GPHEFCSQHTMLVDMKGEQVYLPYPDPSRILGAGCFVDDLLKTDGTLMMERYVSLAIDAYPLTKHPDPEYQNVFWCYLQY
SQ  IKKLHEELTGHLLDTYSVMLASDNASKYWEVEFYENMYMESATLQSVGTCVVCNSQTSLRCGGCIRRPFLCCKCCYDHVV
SQ  STTHKLVLSVTPYVCNNPSCDVADVTQLYLGGMSYYCRDHRPPISFPLCANGQVFGLYKNICTGSPDVADFNSLATCDWS
SQ  NSKDYVLANTATERLKLFAAETLRATEENAKQAYASAVVKEVLSDRELVLSWETGKTRPPLNRNYVFTGFHITKNSKVQL
SQ  GEYIFEKGDYGDVVNYRSSTTYKLQVGDYFVLTSHSVQPLSSPTLLPQERYTKLVGLYPAMNVPESFASNVVHYQRVGMS
SQ  RYTTVQGPPGTGKSHLSIGLALYYPSAKIVYTACSHAAVDALCEKAHKNLPINRCSRIVPAKARVECFSKFKVNDVGAQY
SQ  VFSTINALPETTADILVVDEVSMCTNYDLSMINARVRAKHIVYVGDPAQLPAPRTLLTKGTLAPEHFNSVCRLMVAVGPD
SQ  IFLATCYRCPKEIVDTVSALVYDKKLKANKVTTGECYKCYYKGSVTHDSSSAINKPQLGLVKEFLIKNPKWQSAVFISPY
SQ  NSQNSVARRMLGLQTQTVDSSQGSEFDYVIYCQTSDTAHALNVNRFNVAITRAKKGILCVMSDSTLYESLEFTPLDVNDY
SQ  VKPKMQSEVTVGLFKDCAKAEPLGPAYAPTFVSVNDKFKLNESLCVHFDTTELQMPYNRLISKMGFKFDLNIPGYSKLFI
SQ  TREQAIREVRGWVGFDVEGAHACGPNIGTNLPLQIGFSTGVNFVVTPSGYIDTESGSRLANVVSKAPPGDQFKHLIPLMR
SQ  KGEPWSVVRKRIVEMLCDTLDGVSDTVTFVTWAHGFELTTLHYFAKVGPERKCFMCPRRATLFSSVYGAYSCWSHHRHIG
SQ  GADFVYNPFLVDVQQWGYVGNLQVNHDNVCDVHKGAHVASCDAIMTRCLAIHDCFCGEVNWDVEYPIIANELAINRACRS
SQ  VQRVVLKAAVKALHIETIYDIGNPKAIKVYGVNVNNWNFYDTNPVVEGVKQLHYVYDVHRDQFKDGLAMFWNCNVDCYPH
SQ  NALVCRFDTRVLSKLNLAGCNGGSLYVNQHAFHTDAFNKNAFVNLKPLPFFYYSDTACENATGVSTNYVSEVDYVPLKSN
SQ  VCITRCNLGGAVCKKHADEYRNFLESYNTMVSAGFTLWVDKTFDVFNLWSTFVKLQSLENVAYNVLKSGHFTAVAGELPV
SQ  AILNDRLYIKEDGADKLLFTNNTCLPTNVAFELWAKRSVNVVPEVKLLRNLGVTCTYNLVIWDYESNAPLVPNTVGICTY
SQ  TDLTKLDDQVVLVDGRQLDAYSKFCQLKNAIYFSPSKPKCVCTRGPTHASINGVVVEAPDRGTAFWYAMRKDGAFVQPTD
SQ  GYFTQSRTVDDFQPRTQLEIDFLDLEQSCFLDKYDLHDLGLEHIVYGQFDGTIGGLHLLIGAVRRKRTAHLVMETVLGTD
SQ  TVTSYAVIDQPTASSKQVCSVVDIILDDFIALIKAQDRSVVSKVVQCCLDFKVFRFMLWCKGGKISTFYPQLQAKQDWKP
SQ  GYSMPALYKVQNAVLEPCLLHNYGQAARLPSGTLMNVAKYTQLCQYLNTCSLAVPAKMRVMHFGAGSDKGVCPGTAVLKQ
SQ  WLPADAYLVDNDLCYCASDADSTYVGSCETFFSVNKWDFIFSDMYDARTKNTSGDNTSKEGFFTYLTGFIRSKLALGGSI
SQ  AIKITEHSWSADLYAIMGHFNWWTCFCTSVNSSSSEAFLIGVNYIGVGALLDGWQMHANYVFWRNSTVMQLSSYSLYDLQ
SQ  RFPLRLKGTPVMSLKEDQLNELVLNLIRAGRLIVRDAVDIGVRGVACSGV
//
ID  P0C6W6;
PN  2'-O-methyltransferase;
GN  rep;
OS  349344;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W6;
DR  UNIPROT: Q3I5J6;
DR  UNIPROT: Q3I5J7;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF12379;
DR  Pfam: PF12124;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51940;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESLVLGINEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKSGTCGIVELEKGVLPQPEQPYVFIKRSDAQGTD
SQ  HGHRVRELVAELDGVQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSFGIDLKSYDLGDELGTDPIEDYEQN
SQ  WNTKHGSGVLRELTRELNGGALTRYVDNNFCGPDGYPLECIKDLLARAGKSMCTLSEQLDYIESKRGVYCCRDHGHEIAW
SQ  FTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVATPQECNNMHLSTL
SQ  MKCNHCDEVSWQTCDFLKATCEQCGTENLVSEGPNTCGYLPTNAVVKMPCPACQDPEIGPEHSAADYHNHSNIETRLRKG
SQ  GRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFQLNEEVAIILASF
SQ  SASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPIKGAWNIGQHRSVLTPLCGFPSQAAGVIRSIFSRTLDAANHSIP
SQ  DLQRAAVTILDSISEQSLRLVDAMVYTSNLLTNSVIIMAYVTGGLVQQTSQWLSNLLDTTVEKLRPIFAWIEAKLSAGVE
SQ  FLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFVDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQC
SQ  IRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAVVGTPVCINGLMLLEIKANEQYC
SQ  ALSPGLLATNNVFRLKGGAPTKGVTFGEDTVVEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAV
SQ  VKTLQPVSDLLTNMGIDLDEWSVATFYLFDDSGEEKLSSRMYCSFYPPDEEEDCEEYEEEEEVSERTCEHEYGTEEDYKG
SQ  LPLEFGASTDIIQVEEQEEEDWLDDAVEAEPEPEPLHEEPVNQLTGYLKLTDNVAIKCVDIVEEAQNANPMVIVNAANIH
SQ  LKHGGGVAGALNKATNGAMQKESDHYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDIL
SQ  LAPLLSAGIFGAKPLQSLQMCVQTVRTQVYIVVNDKVLYEQVVMDYLDSLKPKVEAPKQEVLPKAEYPKVDEKSVVQKTI
SQ  DVKPKIKACIDEVTTTLEETKFLTNKLLLFTDINGKLYQDSKNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKA
SQ  GGTTEMLSRALKKVPINEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSETPNAKEEILGTVSWNLREMLAHAEETR
SQ  KLMPVCMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCM
SQ  RSLKAPAIVSVSSPDAVTTYNGYLTSSSKTSEDHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGEKIVYHTLESPVKFH
SQ  LDGEVLPLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQLGPTYLEGADVTKIKPHVNHEGKTFFVLPSDD
SQ  TLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQIEVKFNAPALQEAYYRARAG
SQ  DAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKMGVSI
SQ  PCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTD
SQ  VFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLIPTQPLPNASFDNFKLTCSNTKFADDLNQMT
SQ  GFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSF
SQ  EVLAVEDTQGMDNLACESQQPTPEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELDHEDLMAAYVENTSI
SQ  TIKKPNELSLALGLKTIATHGIAAINSVPWGKILAYVKPFLGQAAVTTSNCAKRLVQRMFNNYMPYVLTLLFQLCTFTKS
SQ  TNSRIRASLPTTIAKNSVRGIVRLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLIYVTAALGVLLSNFGAPSYCSG
SQ  VRESYLNSSNVTTMDFCEGSFPCSVCLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWFFAYMLFTKFFYLLGLSA
SQ  IMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVECTT
SQ  IVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYVVDSVAVKNGALHLYF
SQ  DKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESAAKSASVYYSQLMCQPILLLDQALVSDVGDSTE
SQ  VSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSASRQGVVDTDVDTKDVIECLKLSHHSDLEV
SQ  TGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVARSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCA
SQ  TTRQVVNVITTKISLKGGKIVSTWFKIMLKATLLCVLAALVCYIVMPVHILSVHGGYTNEIIGYKAIQDGVTRDIVSTDD
SQ  CFANKHAGFDSWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLIEY
SQ  SDFSTSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNAYLEGSVRVVTTFDAEYCR
SQ  HGTCERSEAGICLSTSGRWVLNNEHYRALPGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFM
SQ  KFRRAFGEYNHVVAANAPLFLMSFTILCLAPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYV
SQ  FCISLKHFHWFFNNYLRKRVVFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDTTS
SQ  YREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHV
SQ  ICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSP
SQ  SGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTEVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITL
SQ  NVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTIL
SQ  GSTILEDEFTPFDVVRQCSGVTFQGKFKRIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAVAACA
SQ  MLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLVLMTARTVYDDAA
SQ  RRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCF
SQ  LGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDV
SQ  KCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIA
SQ  SEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRNAAMQRKLEKMADQAMTQMYKQARSEDKRAKV
SQ  TSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDAD
SQ  SKIVQLSEINMENSSNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALL
SQ  SDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLHFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANST
SQ  VLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDL
SQ  KGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPMMQSADASTFLNRVCGVSAARLTPCGTGISTDVVYR
SQ  AFDIYNEKVAGFAKFLKTNCCRFQEKDEEGNLLDSYFVVKRHTMSNYQHEETIYNLVKDCPAVAVHDFFKFRVDGDMVPH
SQ  ISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQALLKTVQFC
SQ  DAMRDAGIVGVLTLDNQDLNGNWYDFGDFVQVAPGCGVPIVDSYYSLLMPILTLTRALAAESHMDADLAKPLIKWDLLKY
SQ  DFTAERLCLFDRYFKYWDQTYHPNCINCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGV
SQ  VHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGS
SQ  SVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKAR
SQ  LYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSK
SQ  FYGGWHNMLKTVYSDVETPHLMGWDYPKCDRAMPNMLRIMASLVLARKHSTCCNLSHRFYRLANECAQVLSEMVMCGGSL
SQ  YVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDHEFVGEFYAYLRKHF
SQ  SMMILSDDAVVCYNSNYAAQGLVASIKNFKAVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPD
SQ  PSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTS
SQ  RYWEPEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVT
SQ  QLYLGGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKAT
SQ  EETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNI
SQ  GDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPS
SQ  ARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATN
SQ  YDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKL
SQ  KAHKEKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEY
SQ  DYVIFTQTTETAHSCNVNRFNVAITRAKIGILCIMSDRDLYDKLQFTSLEVPRRNVATLQAENVTGLFKDCSKIITGLHP
SQ  TQAPTHLSVDTKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFITREEAIRHVRAWIGFDVEGCHATRDA
SQ  VGTNLPLQLGFSTGVNLVAIPTGYVDTENNTEFTRVNAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSDTLKGLSDR
SQ  VVFVLWAHGFELTSMKYFVKIGPERTCCLCDKRATCFSTSSDTYACWNHSVGFDYVYNPFMIDVQQWGFTGNLQSNHDQH
SQ  CQVHGNAHVASCDAIMTRCLAVHECFVKRVDWSVEYPIIGDELKINSACRKVQHMVVKSALLADKFPVLHDIGNPKAIKC
SQ  VPQAEVEWKFYDAQPCSDKAYKIEELFYSYATHHDKFTDGVCLFWNCNVDRYPANAIVCRFDTRVLSNLNLPGCDGGSLY
SQ  VNKHAFHTPAFDKSAFTNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRHHANEYRQYLDAYNM
SQ  MISAGFSLWIYKQFDTYNLWNTFTRLQSLENVAYNVVNKGHFDGQAGETPVSIINNAVYTKVDGFDVEIFENKTTLPVNV
SQ  AFELWAKRNIKSVPEIKILNNLGVDIAANTVIWDHKREAPVHMSTIGVCTMTDIAKKPTESACSSLTVLFDGRVEGQVDL
SQ  FRNARNGVLITEGSVKGLTPSKGPAQASVNGVTLIGESVKTQFNYFKKVDGIIQQLPETYFTQSRDLEDFKPRSQMETDF
SQ  LELAMDEFIQRYKLEGYAFEHIVYGDFSHGQLGGLHLMIGLAKRSRDSPLKLEDFIPMDSTVKNYFITDAQTGSSKCVCS
SQ  VIDLLLDDFVEIIKSQDLSVVSKVVKVTIDYAEISFMLWCKDGHVETFYPKLQASQAWQPGVAMPNLYKMQRMLLEKCDL
SQ  QNYGENAVIPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGTAVLRQWLPTGTLLVDSDLNDFVSDA
SQ  DSTLIGDCATVHTANKWDLIVSDMYDPKAKHVTKENDSKEGFFTYLCGFIKQKLALGGSVAVKITEHSWNADLYKLMGHF
SQ  SWWTAFVTNVNASSSEAFLIGVNYLGKPKEQIDGYTMHANYIFWRNTNPIQLSSYSLFDMSKFPLKLRGTAVMSLKENQI
SQ  NDMIYSLLEKGRLIIRENNRVVVSSDILVNN
//
ID  P0C6W7;
PN  2'-O-methyltransferase;
GN  rep;
OS  233262;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W7;
DR  UNIPROT: Q91A28;
DR  UNIPROT: Q91A29;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDIVCSTTAQKLETGGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNTRPYDLEVLLQDALQSREAVLVTPPLGMSLEACYVRGCNPNGWTMGLFRRRSVCNTGRCAVNKHVAYQLYMIDPAGV
SQ  CFGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKCGEKGAYNKDHKRGGFEHVYNFKVEDAYDLVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGGLADGLEAYADKTLQEMKALFPIWSQELPFDVTVAWHVVRDPRYVMRLQSASTIRSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQHNLVDIMSCFYMEADAVVNAFYGVDLKDCGFVMQFGYIDCEQDLCDFK
SQ  GWVPGNMIDGFACTTCGHVYETGDLLAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDGLVYTGVVGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLLNRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYADKICHAVVSKSKELLDVSLDSLSAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFRSVAKVVLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGSKIYEVERGLLHSSQLPLDVYDLTMPSQVQKAKQKPIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDGHVGLLDQAWRVPCAGRRVTFKEQPTVNEIASTPKTIKVFYELD
SQ  KDFNTILNTACGVFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNSLFLFDEAGEEVLASKLYCA
SQ  FTAPEDDDFLEESGVEEDDVEGEETDLTVTSAGEPCVASEQEESSEILEDTLDDGPCVETSDSQVEEDVEMSDFADLESV
SQ  IQDYENVCFEFYTTEPEFVKVLDLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVVPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHVCKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRSVYKAACVVDVNDSHSMAVVDGKQIDDHRVTSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKRVKAEVVVNPANGHMAHGGGVAKAIAVAAGQQFVKETTDMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYALLERVYKHLNKYDCVVTTLISAGIFSVPSDVSLTYLLGTAEKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAERLSFNVGRSIVYETDANKLILSNDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVVPEGWRVVNKFYQINGV
SQ  RTVKYFECPGGIDICSQDKVFGYVQQGSFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCSKWQVVFNGKYFTFKQANNNCFVNVSCLML
SQ  QSLNLKFKIVQWQEAWLEFRSGRPARFVSLVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  VDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFKGDKVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGNLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYNPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTICDILNAKLGFDSSKEFVEYKVTEWPTATGDVVLATDDLYVKRYERGCITFGKPVIWLSHEQASLNSLTYF
SQ  NRPLLVDENKFDVLKVDDVDDGGDISESDAKESKEINIIKLSGVKKPFKVEDSVIVNDDTSEIKYVKSLSIVDVYDMWLT
SQ  GCRYVVRTANALSMAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPVFNVVKAVRNKISACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEVASKLTCKLVALAFKNAFLTFKWSVVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQW
SQ  IKSTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELFMLSTLHWSVRLLVSLANMLPAHVFMRFYIIIASFIKLFILFRHVAYGCSKPGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDVMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCYMRLFYERDGQRTYDDVNASLFVDYSNLLHSKVKGVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  NLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKGDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKAC
SQ  CKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFLLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVVDQDLGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFAMADGSPQPYCYTEGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVR
SQ  IVRTRSMSYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLVFYYLIKLKRAFGDYTSIVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYISVVVSNHAFWVFAYCRRLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLDD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  VQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLVKGIVCWIMASTFLFSCIITAFVKWTMFMYVTTNMLSITFCALCV
SQ  ISLAMLLVKHKHLYLTMYIIPVLFTLLYNNYLVVYKQTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLIGMVFVTLRSI
SQ  NHDLFSFIMFVGRVISVVSLWYMGSNLEEEILLMLASLFGTYTWTTALSMAAAKVIAKWVAVNVLYFTDIPQIKIVLVCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANVVLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEARSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVW
SQ  QIQTIQDSDGTNKQLNEISDDCNWPLVIIANRHNEVSATVLQNNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSNNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTNQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQSKDTNFLNRVRGTSVDARLVPCASGLSTDVQ
SQ  LRAFDICNASVAGIGLHLKVNCCRFQRVDENGDKLDQFFVVKRTDLTIYNREMECYERVKDCKFVAEHDFFTFDVEGSRV
SQ  PHIVRKDLTKYTMLDLCYALRHFDRNDCMLLCDILSIYAGCEQSYFTKKDWYDFVENPDIINVYKKLGPIFNRALVSATE
SQ  FADKLVEVGLVGILTLDNQDLNGKWYDFGDYVIAAPGCGVAIADSYYSYMMPMLTMCHALDCELYVNNAYRLFDLVQYDF
SQ  TDYKLELFNKYFKHWSMPYHPNTVDCQDDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGIVM
SQ  NMDVDTHRYRLSLKDLLLYAADPALHVASASALYDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYDFILSKGLLKEGSSV
SQ  DLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLY
SQ  YEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFY
SQ  GGWDDMLRRLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLVLARKHEACCSQSDRFYRLANECAQVLSEIVMCGGCYYV
SQ  KPGGTSSGDATTAFANSVFNICQAVSANVCALMSCNGNKIEDLSIRALQKRLYSHVYRSDMVDSTFVTEYYEFLNKHFSM
SQ  MILSDDGVVCYNSDYASKGYIANISAFQQVLYYQNNVFMSESKCWVENDINNGPHEFCSQHTMLVKMDGDDVYLPYPDPS
SQ  RILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENEEYQKVFRVYLEYIKKLYNDLGNQILDSYSVILSTCDGQKF
SQ  TDESFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATDHKYVLSVSPYVCNAPGCDVNDVTKL
SQ  YLGGMSYYCEDHKPQYSFKLVMNGMVFGLYKQSCTGSPYIDDFNRIASCKWTDVDDYILANECTERLKLFAAETQKATEE
SQ  AFKQSYASATIQEIVSERELILSWEIGKVKPPLNKNYVFTGYHFTKNGKTVLGEYVFDKSELTNGVYYRATTTYKLSVGD
SQ  VFVLTSHSVANLSAPTLVPQENYSSIRFASVYSVLETFQNNVVNYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYYCTARV
SQ  VYTAASHAAVDALCEKAYKFLNINDCTRIVPAKVRVECYDKFKINDTTRKYVFTTINALPEMVTDIVVVDEVSMLTNYEL
SQ  SVINARIRAKHYVYIGDPAQLPAPRVLLSKGTLEPKYFNTVTKLMCCLGPDIFLGTCYRCPKEIVDTVSALVYENKLKAK
SQ  NESSSLCFKVYYKGVTTHESSSAVNMQQIYLINKFLKANPLWHKAVFISPYNSQNFAAKRVLGLQTQTVDSAQGSEYDYV
SQ  IYSQTAETAHSVNVNRFNVAITRAKKGILCVMSNMQLFEALQFTTLTLDKVPQAVETRVQCSTNLFKDCSKSYSGYHPAH
SQ  APSFLAVDDKYKATGDLAVCLGIGDSAVTYSRLISLMGFKLDVTLDGYCKLFITKEEAVKRVRAWVGFDAEGAHATRDSI
SQ  GTNFPLQLGFSTGIDFVVEATGLFADRDGYSFKKAVAKAPPGEQFKHLIPLMTRGQRWDVVRPRIVQMFADHLIDLSDCV
SQ  VLVTWAANFELTCLRYFAKVGREISCNVCTKRATAYNSRTGYYGCWRHSVTCDYLYNPLIVDIQQWGYIGSLSSNHDLYC
SQ  SVHKGAHVASSDAIMTRCLAVYDCFCNNINWNVEYPIISNELSINTSCRVLQRVMLKAAMLCNRYTLCYDIGNPKAIACV
SQ  KDFDFKFYDAQPIVKSVKTLLYSFEAHKDSFKDGLCMFWNCNVDKYPPNAVVCRFDTRVLNNLNLPGCNGGSLYVNKHAF
SQ  HTKPFSRAAFEHLKPMPFFYYSDTPCVYMDGMDAKQVDYVPLKSATCITRCNLGGAVCLKHAEEYREYLESYNTATTAGF
SQ  TFWVYKTFDFYNLWNTFTKLQSLENVVYNLVKTGHYTGQAGEMPCAIINDKVVAKIDKEDVVIFINNTTYPTNVAVELFA
SQ  KRSIRHHPELKLFRNLNIDVCWKHVIWDYARESIFCSNTYGVCMYTDLKFIDKLNVLFDGRDNGALEAFKRSNNGVYIST
SQ  TKVKSLSMIKGPPRAELNGVVVDKVGDTDCVFYFAVRKEGQDVIFSQFDSLRVSSNQSPQGNLGSNEPGNVGGNDALATS
SQ  TIFTQSRVISSFTCRTDMEKDFIALDQDLFIQKYGLEDYAFEHIVYGNFNQKIIGGLHLLIGLYRRQQTSNLVIQEFVSY
SQ  DSSIHSYFITDEKSGGSKSVCTVIDILLDDFVALVKSLNLNCVSKVVNVNVDFKDFQFMLWCNDEKVMTFYPRLQAASDW
SQ  KPGYSMPVLYKYLNSPMERVSLWNYGKPVTLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSEKGVAPGSAVL
SQ  RQWLPAGTILVDNDLYPFVSDSVATYFGDCITLPFDCQWDLIISDMYDPITKNIGEYNVSKDGFFTYICHMIRDKLALGG
SQ  SVAIKITEFSWNAELYKLMGYFAFWTVFCTNANASSSEGFLIGINYLGKPKVEIDGNVMHANYLFWRNSTVWNGGAYSLF
SQ  DMAKFPLKLAGTAVINLRADQINDMVYSLLEKGKLLVRDTNKEVFVGDSLVNVI
//
ID  P0C6W8;
PN  2'-O-methyltransferase;
GN  rep;
OS  233264;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W8;
DR  UNIPROT: Q8V439;
DR  UNIPROT: Q8V440;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDIVCSTTAQKLETGGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNTRPYDLEVLLQDALQSREAVLVTPPLGMSLEACYVRGCNPNGWTMGLFRRRSVCNTGRCAVNKHVAYQLYMIDPAGV
SQ  CFGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKCGEKGAYNKDHKRGGFEHVYNFKVEDAYDLVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGGLADGLEAYADKTLQEMKALFPIWSQELPFDVTVAWHVVRDPRYVMRLQSASTIRSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQHNLVDIMSCFYMEADAVVNAFYGVDLKDCGFVMQFGYIDCEQDLCDFK
SQ  GWVPGNMIDGFACTTCGHVYETGDLLAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDGLVYTGVVGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLLNRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYADKICHAVVSKSKELLDVSLDSLSAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFRSVAKVVLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGSKIYEVERGLLHSSQLPLDVYDLTMPSQVQKAKQKPIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDGHVGLLDQAWRVPCAGRRVTFKEQPTVNEIASTPKTIKVFYELD
SQ  KDFNTILNTACGVFEVDDTVDMEEFYAVVVDAIEEKLSPCKELEGVGAKVSAFLQKLEDNSLFLFDEAGEEVLASKLYCA
SQ  FTAPEDDDFLEESGVEEDDVEGEETDLTVTSAGEPCVASEQEESSEILEDTLDDGPCVETSDSQVEEDVEMSDFADLESV
SQ  IQDYENVCFEFYTTEPEFVKVLDLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVVPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHVCKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRSVYKAACVVDVNDSHSMAVVDGKQIDDHRVTSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKRVKAEVVVNPANGHMAHGGGVAKAIAVAAGQQFVKETTDMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYALLERVYKHLNKYDCVVTTLISAGIFSVPSDVSLTYLLGTAEKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAERLSFNVGRSIVYETDANKLILSNDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVVPEGWRVVNKFYQINGV
SQ  RTVKYFECPGGIDICSQDKVFGYVQQGSFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGENFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCSKWQVVFNGKYFTFKQANNNCFVNVSCLML
SQ  QSLNLKFKIVQWQEAWLEFRSGRPARFVSLVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  VDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFKGDKVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGNLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYKPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTICDILNAKLGFDSSKEFVEYKVTEWPTATGDVVLATDDLYVKRYERGCITFGKPVIWLSHEQASLNSLTYF
SQ  NRPLLVDENKFDVLKVDDVDDGGDISESDAKESKEINIIKLSGVKKPFKVEDSVIVNDDTSEIKYVKSLSIVDVYDMWLT
SQ  GCRYVVRTANDLSMAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPVFNVVKAVRNKISACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEVASKLTCKLVALAFKNAFLTFKWSVVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQW
SQ  IKSTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELFMLSTLHWSVRLLVSLANMLPAHVFMRFYIIIASFIKLFSLFRHVAYGCSKPGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDVMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCYMRLFYERDGQRTYDDVNASLFVDYSNLLHSKVKGVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  NLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKGDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKAC
SQ  CKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFLLSLVCFIGLWCLMPTYTVHKSDFQLPVYTSYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVVDQDLGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFAMADGSPQPYCYTEGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVR
SQ  IVRTRSMSYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLVFYYLIKLKRAFGDYTSIVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYISVVVSNHAFWVFAYCRRLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLDD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  VQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLVKGIVCWIMASTFLFSCIITAFVKWTMFMYVTTNMLSITFCALCV
SQ  ISLAMLLVKHKHLYLTMYIIPVLFTLLYNNYLVVYKQTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLIGMVFVTLRSI
SQ  NHDLFSFIMFVGRVISVVSLWYMGSNLEEEILLMLASLFGTYTWTTALSMAAAKVIAKWVAVNVLYFTDIPQIKIVLVCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANVVLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEARSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVW
SQ  QIQTIQDSDGTNKQLNEISDDCNWPLVIIANRHNEVSATVLQNNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSNNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTNQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQSKDTNFLNRVRGTSVDARLVPCASGLSTDVQ
SQ  LRAFDICNASVAGIGLHLKVNCCRFQRVDENGDKLDQFFVVKRTDLTIYNREMECYERVKDCKFVAEHDFFTFDVEGSRV
SQ  PHIVRKDLTKYTMLDLCYALRHFDRNDCMLLCDILSIYAGCEQSYFTKKDWYDFVENPDIINVYKKLGPIFNRALVSATE
SQ  FADKLVEVGLVGILTLDNQDLNGKWYDFGDYVIAAPGCGVAIADSYYSYMMPMLTMCHALDCELYVNNAYRLFDLVQYDF
SQ  TDYKLELFNKYFKHWSMPYHPNTVDCQDDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGIVM
SQ  NMDVDTHRYRLSLKDLLLYAADPALHVASASALYDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYDFILSKGLLKEGSSV
SQ  DLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLY
SQ  YEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFY
SQ  GGWDDMLRRLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLVLARKHEACCSQSDRFYRLANECAQVLSEIVMCGGCYYV
SQ  KPGGTSSGDATTAFANSVFNICQAVSANVCALMSCNGNKIEDLSIRALQKRLYSHVYRSDMVDSTFVTEYYEFLNKHFSM
SQ  MILSDDGVVCYNSDYASKGYIANISAFQQVLYYQNNVFMSESKCWVENDINNGPHEFCSQHTMLVKMDGDDVYLPYPDPS
SQ  RILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENEEYQKVFRVYLEYIKKLYNDLGNQILDSYSVILSTCDGQKF
SQ  TDESFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATDHKYVLSVSPYVCNAPGCDVNDVTKL
SQ  YLGGMSYYCEDHKPQYSFKLVMNGMVFGLYKQSCTGSPYIDDFNRIASCKWTDVDDYILANECTERLKLFAAETQKATEE
SQ  AFKQSYASATIQEIVSERELILSWEIGKVKPPLNKNYVFTGYHFTKNGKTVLGEYVFDKSELTNGVYYRATTTYKLSVGD
SQ  VFVLTSHSVANLSAPTLVPQENYSSIRFASVYSVLETFQNNVVNYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYYCTARV
SQ  VYTAASHAAVDALCEKAYKFLNINDCTRIVPAKVRVECYDKFKINDTTRKYVFTTINALPEMVTDIVVVDEVSMLTNYEL
SQ  SVINARIRAKHYVYIGDPAQLPAPRVLLSKGTLEPKYFNTVTKLMCCLGPDIFLGTCYRCPKEIVDTVSALVYENKLKAK
SQ  NESSSLCFKVYYKGVTTHESSSAVNMQQIYLINKFLKANPLWHKAVFISPYNSQNFAAKRVLGLQTQTVDSAQGSEYDYV
SQ  IYSQTAETAHSVNVNRFNVAITRAKKGILCVMSNMQLFEALQFTTLTLDKVPQAVETRVQCSTNLFKDCSKSYSGYHPAH
SQ  APSFLAVDDKYKATGDLAVCLGIGDSAVTYSRLISLMGFKLDVTLDGYCKLFITKEEAVKRVRAWVGFDAEGAHATRDSI
SQ  GTNFPLQLGFSTGIDFVVEATGLFADRDGYSFKKAVAKAPPGEQFKHLIPLMTRGQRWDVVRPRIVQMFADHLIDLSDCV
SQ  VLVTWAANFELTCLRYFAKVGREISCNVCTKRATAYNSRTGYYGCWRHSVTCDYLYNPLIVDIQQWGYIGSLSSNHDLYC
SQ  SVHKGAHVASSDAIMTRCLAVYDCFCNNINWNVEYPIISNELSINTSCRVLQRVMLKAAMLCNRYTLCYDIGNPKAIACV
SQ  KDFDFKFYDAQPIVKSVKTLLYSFEAHKDSFKDGLCMFWNCNVDKYPPNAVVCRFDTRVLNNLNLPGCNGGSLYVNKHAF
SQ  HTKPFSRAAFEHLKPMPFFYYSDTPCVYMDGMDAKQVDYVPLKSATCITRCNLGGAVCLKHAEEYREYLESYNTATTAGF
SQ  TFWVYKTFDFYNLWNTFTKLQSLENVVYNLVKTGHYTGQAGEMPCAIINDKVVAKIDKEDVVIFINNTTYPTNVAVELFA
SQ  KRSIRHHPELKLFRNLNIDVCWKHVIWDYARESIFCSNTYGVCMYTDLKFIDKLNVLFDGRDNGALEAFKRSNNGVYIST
SQ  TKVKSLSMIKGPPRAELNGVVVDKVGDTDCVFYFAVRKEGQDVIFSQFDSLRVSSNQSPQGNLGSNEPGNVGGNDALATS
SQ  TIFTQSRVISSFTCRTDMEKDFIALDQDLFIQKYGLEDYAFEHIVYGNFNQKIIGGLHLLIGLYRRQQTSNLVIQEFVSY
SQ  DSSIHSYFITDEKSGGSKSVCTVIDILLDDFVALVKSLNLNCVSKVVNVNVDFKDFQFMLWCNDEKVMTFYPRLQAASDW
SQ  KPGYSMPVLYKYLNSPMERVSLWNYGKPVTLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSEKGVAPGSAVL
SQ  RQWLPAGTILVDNDLYPFVSDSVATYFGDCITLPFDCQWDLIISDMYDPITKNIGEYNVSKDGFFTYICHMIRDKLALGG
SQ  SVAIKITEFSWNAELYKLMGYFAFWTVFCTNANASSSEGFLIGINYLGKPKVEIDGNVMHANYLFWRNSTVWNGGAYSLF
SQ  DMAKFPLKLAGTAVINLRADQINDMVYSLLEKGKLLVRDTNKEVFVGDSLVNVI
//
ID  P0C6W9;
PN  2'-O-methyltransferase;
GN  rep;
OS  11132;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6W9;
DR  UNIPROT: Q66198;
DR  UNIPROT: Q9WQ81;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDIVCSTTAQKLETGGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNTRPYDLEVLLQDALQSREAVLVTPPLGMSLEACYVRGCNPNGWTMGLFRRRSVCNTGRCAVNKHVAYQLYMIDPAGV
SQ  CFGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKCGEKGAYNKDHKRGGFEHVYNFKVEDAYDLVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGGLADGLEAYADKTLQEMKALFPIWSQELPFDVTVAWHVVRDPRYVMRLQSASTIRSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQHNLVDIMSCFYMEADAVVNAFYGVDLKDCGFVMQFGYIDCEQDLCDFK
SQ  GWVPGNMIDGFACTTCGHVYETGDLLAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDGLVYTGVVGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLLNRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYAGKICHAVVSKSKELLDVSLDSLGAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFRSVAKVVLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGSKIYEVERGLLHSSQLPLDVYDLTMPSQVQKTKQKPIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDGHVGLLDQAWRVPCAGRCVTFKEQPTVNEIASTPKTIKVFYELD
SQ  KDFNTILNTACGVFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNSLFLFDEAGEEVLAPKLYCA
SQ  FTAPEDDDFLEESGVEEDDVEGEETDLTVTSAGEPCVASEQEESSEILEDTLDDGPCVETSDSQVEEDVQMSDFVDLESV
SQ  IQDYENVCFEFYTTEPEFVKVLDLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVVPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHVCKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRSVYKAACVVDVNDSHSMAVVDGKQIDDHRITSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKRVKAEVVVNPANGHMAHGGGVAKAIAVAAGQQFVKETTDMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYALLERVYKHLNKYDCVVTTLISAGIFSVPSDVSLTYLLGTAKKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAERLSFNVGRSIVYETDANKLILSNDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVVPEGWRVVNKFYQINGV
SQ  RTVKYFECPGGIDICSQDKVFGYVQQGSFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCSKWQVVFNGKYFTFKQANNNCFVNVSCLML
SQ  QSLNLKFKIVQWQEAWLEFRSGRPARFVSLVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  VDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFKGDKVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGNLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYKPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTVCDILNAKLGFDSSKEFVEYKVTEWPTATGDVVLATDDLYVKRYERGCITFGKPVIWLSHEQASLNSLTYF
SQ  NRPLLVDENKFDVLKVDDVDDGGDISESDAKEPKEINIIKLSGVKKPFKVEDSVIVNDDTSEIKYVKSLSIVDVYDMWLT
SQ  GCRCVVRTANALSRAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPVFNVVKAVRNKISACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEVASKLTCKLVALAFKNAFLTFKWSVVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQW
SQ  IKNTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELFMLSTLHWSVRLLVSLANMLPAHVFMRFYIIIASFIKLFSLFRHVAYGCSKSGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDAMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCYMRLFYDRDGQRTYDDVNASLFVDYSNLLHSKVKSVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  NLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKGDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKAC
SQ  CKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFVLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVVDQDFGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFAMADGSPQPYCYTDGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVR
SQ  IVRTRSMPYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLVFYYLIKLKRAFGDYTSIVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYISVVVSNHAFWVFSYCRQLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLGD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVVYVIMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  VQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKHLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLVKGIVCWIMASTFLFSCIITAFVKWTMFMYVTTNMLSITFCALCV
SQ  ISLTMLLVKHKHLYLTMYIIPVLFTLLYNNYLVVYKQTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLIGMVFVTLRSI
SQ  NQYLFSFIMFVGRVISVVSLWYMGSNLEEEILLMLASLFGTYTWTTALSMAAAKVIAKWVAVNVLYFTDIPQIKIVLVCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANVVLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEACSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVW
SQ  QIQTIQDSDGTNKQLHEISDDCNWPLVIIANRHNEVSATALQNNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSYNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTSQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQSKDTNFLNRVRGTSVDARLVPCASGLSTDVQ
SQ  LRAFDICNASVAGIGLHLKVNCCRFQRVDENGDKLDQFFVVKRTDLTIYNREMECYERVKDCKFVAEHDFFTFDVEGSRV
SQ  PHIVRKDLTKYTMLDLCYALRHFDRNDCMLLCDILSIYAGCEQSYFTKKDWYDFVENPDIINVYKKLGPIFNRALVSATE
SQ  FADKLVEVGLVGILTLDNQDLNGKWYDFGDYVIAAPGCGVAIADSYYSYMMPMLTMCHALDCELYVNNAYRLFDLVQYDF
SQ  TDYKLELFNKYFKHWSMPYHPNTVDCQDDRCIIRCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGIVM
SQ  NMDVDTHRYRLSLKDLLLYAADPALHVASASALYDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYDFILSKGLLKEGSSV
SQ  DLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLY
SQ  YEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFY
SQ  GGWDDMLRRLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLVLARKHEACCSQSDRFYRLANEYAQVLSEIVMCGGCYYV
SQ  KPGGTSSGDATTAFANSVFNICQAVSANVCALMSCNGNKIEDLSIRALQKRLYSHVYRSDMVDSTFVTEYYEFLNKHFSM
SQ  MILSDDGVVCYNSDYASKGYIANISAFQQVLYYQNNVFMSESKCWVENDINNGPHEFCSQHTMLVKMDGDDVYLPYPDPS
SQ  RILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENEEYQKVFRVYLEYIKKLYNELGNQILDSYSVILSTCDGQKF
SQ  TDESFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATDHKYVLSVSPYVCNAPGCDVNDVTKL
SQ  YLGGMSYYCEDHKPQYSFKLVMNGMVFGLYKQSCTGSPYIDDFNRIASCKWTDVDDYILANECTERLKLFAAETQKATEE
SQ  AFKQSYASATIQEIVSERELILSWEIGKVKPPLNKNYVFTGYHFTKNGKTVLGEYVFDKSELTNGVYYRATTTYKLSVGD
SQ  VFVLTSHSVANLSAPTLVPQENYSSIRFASVYSVLETFQNNVVNYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYYCTARV
SQ  VYTAASHAAVDALCEKAYKFLNINDCTRIVPAKVRVECYDKFKINDTTRKYVFTTINALPEMVTDIVVVDEVSMLTNYEL
SQ  SVINARIRAKHYVYIGDPAQLPAPRVLLSKGTLEPKYFNTVTKLMCCLGPDIFLGTCYRCPKEIVDTVSALVYENKLKAK
SQ  NESSSLCFKVYYKGVTTHESSSAVNMQQIYLINKFLKANPLWHKAVFISPYNSQNFAARRVLGLQTQTVDSAQGSEYDYV
SQ  IYSQTAETAHSVNVNRFNVAITRAKKGILCVMSNMQLFEALQFTTLTVDKVPQAVETRVQCSTNLFKDCSKSYSGYHPAH
SQ  APSFLAVDDKYKATGDLAVCLGIGDSAVTYSRLTSLMGFKLDVTLDGYCKLFITKEEAVKRVRAWVGFDAEGAHATRDSI
SQ  GTNFPLQLGFSTGIDFVVEATGLFADRDGYSFKKAVAKAPPGEQFKHLIPLMTRGQRWDVVRPRIVQMFADHLIDLSDCV
SQ  VLVTWAANFELTCLRYFAKVGREISCNVCTKRATAYNSRTGYYGCWRHSVTCDYLYNPLIVDIQQWGYIGSLSSNHDLYC
SQ  SVHKGAHVASSDAIMTRCLAVYDCFCNNINWNVEYPIISNELSINTSCRVLQRVMLKAAMLCNRYTLCYDIGNPKAIACV
SQ  KDFDFKFYDAQPIVKSVKTLLYFFEAHKDSFKDGLCMFWNCNVDKYPPNAVVCRFDTRVLNNLNLPGCNGGSLYVNKHAF
SQ  HTKPFSRAAFEHLKPMPFFYYSDTPCVYMDGMDAKQVDYVPLKSATCITRCNLVGAVCLKHAEEYREYLNSYNTATTAGF
SQ  TFWVYKTFDFYNLWNTFTKLQSLENVVYNLVKTGHYTGQAGEMPCAIINDKVVAKIDKEDVVIFINNTTYPTNVAVELFA
SQ  KRSIRHHPELKLFRNLNIDVCWKHVIWDYARESIFCSNTYGVCMYTDLKFIDKLNVLFDGRDNGALEAFKRSNNGVYIST
SQ  TKVKSLSMIRGPPRAELNGVVVDKVGDTDCVFYFAVRKEGQDVIFSQFDSLRVSSNQSPQGNLGSNEPGNVGGNDALATS
SQ  TIFTQSRVISSFTCRTDMEKDFIALDQDVFIQKYGLEDYAFEHIVYGNFNQKIIGGLHLLIGLYRRQQTSNLVIQEFVSY
SQ  DSSIHSYFITDEKSGGSKSVCTVIDILLDDFVALVKSLNLNCVSKVVNVNVDFKDFQFMLWCNDEKVMTFYLRLQAASDW
SQ  KPGYSMPVLYKYLNSPMERVSLWNYGKPVTLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSEKGVAPGSAVL
SQ  RQWLPAGTILVDNDLYPFVSDSVATYFGDCITLPFDCQWDLIISDMYDPITKNIGEYNVSKDGFFTYICHMIRDKLALGG
SQ  SVAIKITEFSWNAELYKLMGYFAFWTVFCTNANASSSEGFLIGINYLGKPKVEIDGNVMHANYLFWRNSTVWNGGAYSLF
SQ  DMAKFPLKLAGTAVINLRADQINDMVYSLLEKGKLLVRDTNKEVFVGDSMVNVI
//
ID  P0C6X0;
PN  2'-O-methyltransferase;
GN  rep;
OS  11133;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X0;
DR  UNIPROT: Q8V6W6;
DR  UNIPROT: Q8V6W7;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
DE  Interaction: Q9Y566; IntAct: EBI-29477564; Score: 0.44
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDIVCSTTAQKLETGGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNTRPYDLEVLLQDALQSREAVLVTPPLGMSLEACYVRGCNPNGWTMGLFRRRSVCNTGRCAVNKHVAYQLYMIDPAGV
SQ  CFGAGQFVGWVIPLAFMPVQSRKFIAPWVMYLRKCGEKGAYIKDYKRGGFEHVYNFKVEDAYDLVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGGLADGLEAYADKTLQEMKALFPIWSQELPFDVTVAWHVVRDPRYVMRLQSASTIRSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQHNLVDIMSCFYMEADAVVNAFYGVDLKDCGFVMQFGYIDCEQDLCDFK
SQ  GWVPGNMIDGFACTTCGHVYETGDLLAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDGLVYTGVVGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLLNRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYAGKICHAVVSKSKELLDVSVDSLGAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFGKNIPRYASAVAQAFRSGAKVGLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGSKIYEVERGLLHSSQLPLDVYDLTMPSQVQKTKQKGIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDGHVGLLDQAWRVPCAGRCVTFKEQPTVNEIASTPKTIKVFYELD
SQ  KDFNTILNTACGEFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNSLFLFDEAGEEVLAPKLYCA
SQ  FTAPEDDDFLEESGVEEDDVEGEETDLTVTSAGEPCVASEQEESSEILEDTLDDGPCVETSDSQVEEDVQMSDFGDLESV
SQ  IQDYENVCFEFYTTEPEFVKVLDLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVVPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHVCKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRSVYKAACVVDVNDSHSMAVVDGKQIDDHRITSITSDKFDFIIGHGTSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKRVKAEVVVNPANGHMAHGGGVAKAIAVAAGQQFVKETTDMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYALLERVYKHLNKYDCVVTTLISAGIFSVPSDVSLTYLLGTAKKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAERLSFNVGRSIVYETDANKLILSNDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVVPEGWRVVNKFYQINGV
SQ  RPVKYFECPGGIDICSQDKVFGYVQQGSFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCSKWQVVFNGKYFTFKQANNNCFVNVSCLML
SQ  QSLNLKFKIVQWQEAWLEFRSGRPARFVSLVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  VDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFKGDKVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGNLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYKPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTVCDILNAKLGFDSSKEFVEYKVTEWPTATGDVVLATDDLYVKRYERGCITFGKPVIWLSHEQASLNSLTYF
SQ  NRPLLVDENKFDVLKVDDVDDGGDISESDAKEPKEINIIKLSGVKKPFKVEDSVIVNDDTSEIKYVKSLSIVDVYDMWLT
SQ  GCRCVVRTANALSRAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPVFNVVKAVRNKISACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEVASKLTCKLVALAFKNAFLTFKWSVVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIVQW
SQ  IKNTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELLMLSTLHWSVRLLVSLANMLPAHVFMRFYIIIASFIKLFSLFRHVAYGCSKSGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDVMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCYMRLFYDRDGQRTYDDVNASLFVDYSNLLHSKVKSVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  ILITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKGDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKAC
SQ  CKTGLKLELTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFVLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVVDQDFGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFAMADGSPQPYCYTDGLMQNASLYSSLVPHVRYNLANAKGFIRLPEVLREGLVR
SQ  IVRTRSMSYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLGFYYLIKLKRAFGDYTSIVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYISVVVSNHAFWVFSYCRQLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLDD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVIMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  VQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLVKGIVCWIMASTFLFSCIITAFVKWTMFMYVTTNMLSITFCALCV
SQ  ISLAMLLVKHKHLYLTMYIIPVLFTLLYNNYLVVYKQTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLIGMVFVTLRSI
SQ  NHDLFSFIMFVGRVISVVSLWYMGSNLEEEILLMLASLFGTYTWTTALSMAAAKVIAKWVAVNVLYFTDIPQIKIVLVCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANGGLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEACSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVW
SQ  QIQTIQDSDGTNKQLHEISDDCNWPLVIIANRHNEVSATVLQNNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSYNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTSQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQSKDTNFLNRVRGTSVDARLVPCASGLSTDVQ
SQ  LRAFDICNASVAGIGLHLKVNCCRFQRVDENGDKLDQFFVVKRTDLTIYNREMECYERVKDCKFVAEHDFFTFDVEGSRV
SQ  PHIVRKDLTKYTMLDLCYALRHFDRNDCMLLCDILSIYAGCEQSYFTKKDWYDFVENPDIINVYKKLGPIFNRALVSATE
SQ  FADKLVEVGLVGILTLDNQDLNGKWYDFGDYVIAAPGCGVAIADSYYSYMMPMLTMCHALDCELYVNNAYRLFDLVQYDF
SQ  TDYKLELFNKYFKHWSMPYHPNTVDCQDDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGIVM
SQ  NMDVDTHRYRLSLKDLLLYAADPALHVASASALYDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYDFILSKGLLKEGSSV
SQ  DLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPAAQVIVNNYDKSAGYPFNKFGKARLY
SQ  YEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFY
SQ  GGWDDMLRRLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLVLARKHEACCSQSDRFYRLANECAQVLSEIVMCGGCYYV
SQ  KPGGTSSGDATTAFANSVFNICQAVSANVCALMSCNGNKIEDLSIRALQKRLYSHVYRSDMVDSTFVTEYYEFLNKHFSM
SQ  MILSDDGVVCYNSDYASKGYIANISAFQQVLYYQNNVFMSESKCWVENDINNGPHEFCSQHTMLVKMDGDDVYLPYPVPS
SQ  RILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENEEYQKVFRVYLEYIKKLYNELGNQILDSYSVILSTCDGQKF
SQ  TDESFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATDHKYVLSVSPYVCNAPGCDVNDVTKL
SQ  YLGGMSYYCEDHKPQYSFKLVMNGMVFGLYKQSCTGSPYIDDFNRIASCKWTDVDDYILANECTERLKLFAAETQKATEE
SQ  AFKQSYASATIQEIVSERELILSWEIGKVKPPLNKNYVFTGYHFTKNGKTVLGEYVFDKSELTNGVYYRATTTYKLSVGD
SQ  VFVLTSHSVANLSAPTLVPQENYSSIRFASVYSVLETFQNNVVNYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYYCTARV
SQ  VYTAASHAAVDALCEKAYKFLNINDCTRIVPAKVRVECYDKFKINDTTRKYVFTTINALPEMVTDIVVVDEVSMLTNYEL
SQ  SVINARIRAKHYVYIGDPAQLPAPRVLLSKGTLEPKYFNTVTKLMCCLGPDIFLGTCYRCPKEIVDTVSALVYENKLKAK
SQ  NESSSLCFKVYYKGVTTHESSSAVNMQQIYLINKFLKANPLWHKAVFISPYNSQNFAAKRVLGLQTQTVDSAQGSEYDYV
SQ  IYSQTAETAHSVNVNRFNVAITRAKKGILCVMSNMQLFEALQFTTLTVDKVPQAVETRVQCSTNLFKDCSKSYSGYHPAH
SQ  APSFLAVDDKYKATGDLAVCLGIGDSAVTYSRLISLMGFKLDVTLDGYCKLFITKEEAVKRVRAWVGFDAEGAHATRDSI
SQ  GTNFPLQLGFSTGIDFVVEATGLFADRDGYSFKKAVAKAPPGEQFKHLIPLMTRGQRWDVVRPRIVQMFADHLIDLSDCV
SQ  VLVTWAANFELTCLRYFAKVGREISCNVSTKRATAYNSRTGYYGCWRHSVTCDYLYNPLIVDIQQWGYIGSLSSNHDLYC
SQ  SVHKGAHVASSDAIMTRCLAVYDCFCNNINWNVEYPIISNELSINTSCRVLQRVMLKAAMLCNRYTLCYDIGNPKAIACV
SQ  KDFDFKFYDAQPIVKSVKTLLYFFEAHKDSFKDGLCMFWNCNVDKYPPNAVVCRFDTRVLNNLNLPGCNGGSLYVNKHAF
SQ  HTKPFSRAAFEHLKPMPFFYYSDTPCVYMDGMDAKQVDYVPLKSATCITRCNLGGAVCLKHAEEYREYLESYNTATTAGF
SQ  TFWVYKTFDFYNLWNTFTKLQSLENVVYNLVKTGHYTGQAGEMPCAIINDKVVAKIDKEDVVIFINNTTYPTNVAVELFA
SQ  KRSIRHHPELKLFRNLNIDVCWKHVIWDYARESIFCSNTYGVCMYTDLKLIDKLNVLFDGRDNGALEAFKRSNNGVYIST
SQ  TKVKSLSMIRGPPRAELNGVVVDKVGDTDCVFYFAVRKEGQDVIFSQFDSLRVSSNQSPQGNLGSNEPGNVGGNDALATS
SQ  TIFTQSRVISSFTCRTDMEKDFIALDQDVFIQKYGLEDYAFEHIVYGNFNQKIIGGLHLLIGLYRRQQTSNLVIQEFVSY
SQ  DSSIHSYFITDEKSGGSKSVCTVIDILLDDFVALVKSLNLNCVSKVVNVNVDFKDFQFMLWCNDEKVMTFYPRLQAASDW
SQ  KPGYSMPVLYKYLNSPMERVSLWNYGKPVTLPTGCMMNVAKYTQLCQYLNTTTLAVPVNTRVLHLGAGSEKGVAPGSAVL
SQ  RQWLPAGTILRQWLPAGTILVHNDLYPFVSDSVATYFGDCITLPFDCQWDLIISDMYDLLLDIGVHVVRCSYIHCHMIRD
SQ  KLALGGSVAIKITEFSWNAELYKLMGYFAFWTVFCTNANASSSEGFLIGINYLGKPKVEIDGNVMHAIICFGEIPQFGTG
SQ  VLIACLIWLNSRLSWLVMP
//
ID  P0C6X1;
PN  Putative 2'-O-methyl transferase;
GN  rep;
OS  11137;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X1;
DR  UNIPROT: Q05002;
DR  UNIPROT: Q9DLN0;
DR  UNIPROT: Q9DLN1;
DR  PDB: 1P9S;
DR  PDB: 2J97;
DR  PDB: 2J98;
DR  PDB: 3EJG;
DR  PDB: 4RS4;
DR  PDB: 4S1T;
DR  Pfam: PF13087;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G). The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. {ECO:0000250}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: P62937; IntAct: EBI-25637353; Score: 0.37
DE  Interaction: P0C6X1; IntAct: EBI-25708571; Score: 0.61
DE  Interaction: P0C6Y4; IntAct: EBI-26366740; Score: 0.44
DE  Interaction: Q96C36; IntAct: EBI-27129560; Score: 0.46
DE  Interaction: P32322; IntAct: EBI-27129560; Score: 0.46
DE  Interaction: O75717; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q93008; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q9HA64; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P19447; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q9ULT8; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q92759; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P28715; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P32780; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q13889; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q7Z4H7; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q14247; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q9H9G7; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q13546; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P41229; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: A3KMH1; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q2NKX8; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q9Y5X1; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q15003; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q504Q3; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q8WV41; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P45974; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q15418; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q86UV5; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P54727; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P49642; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q14181; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q03426; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q9UKK9; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P45973; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q9H706; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P51946; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P27144; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: Q14008; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-27129362; Score: 0.35
DE  Interaction: P78344; IntAct: EBI-27129362; Score: 0.35
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039548;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MACNRVTLAVASDSEISANGCSTIAQAVRRYSEAASNGFRACRFVSLDLQDCIVGIADDTYVMGLHGNQTLFCNIMKFSD
SQ  RPFMLHGWLVFSNSNYLLEEFDVVFGKRGGGNVTYTDQYLCGADGKPVMSEDLWQFVDHFGENEEIIINGHTYVCAWLTK
SQ  RKPLDYKRQNNLAIEEIEYVHGDALHTLRNGSVLEMAKEVKTSSKVVLSDALDKLYKVFGSPVMTNGSNILEAFTKPVFI
SQ  SALVQCTCGTKSWSVGDWTGFKSSCCNVISNKLCVVPGNVKPGDAVITTQQAGAGIKYFCGMTLKFVANIEGVSVWRVIA
SQ  LQSVDCFVASSTFVEEEHVNRMDTFCFNVRNSVTDECRLAMLGAEMTSNVRRQVASGVIDISTGWFDVYDDIFAESKPWF
SQ  VRKAEDIFGPCWSALASALKQLKVTTGELVRFVKSICNSAVAVVGGTIQILASVPEKFLNAFDVFVTAIQTVFDCAVETC
SQ  TIAGKAFDKVFDYVLLDNALVKLVTTKLKGVRERGLNKVKYATVVVGSTEEVKSSRVERSTAVLTIANNYSKLFDEGYTV
SQ  VIGDVAYFVSDGYFRLMASPNSVLTTAVYKPLFAFNVNVMGTRPEKFPTTVTCENLESAVLFVNDKITEFQLDYSIDVID
SQ  NEIIVKPNISLCVPLYVRDYVDKWDDFCRQYSNESWFEDDYRAFISVLDITDAAVKAAESKAFVDTIVPPCPSILKVIDG
SQ  GKIWNGVIKNVNSVRDWLKSLKLNLTQQGLLGTCAKRFKRWLGILLEAYNAFLDTVVSTVKIGGLTFKTYAFDKPYIVIR
SQ  DIVCKVENKTEAEWIELFPHNDRIKSFSTFESAYMPIADPTHFDIEEVELLDAEFVEPGCGGILAVIDEHVFYKKDGVYY
SQ  PSNGTNILPVAFTKAAGGKVSFSDDVEVKDIEPVYRVKLCFEFEDEKLVDVCEKAIGKKIKHEGDWDSFCKTIQSALSVV
SQ  SCYVNLPTYYIYDEEGGNDLSLPVMISEWPLSVQQAQQEATLPDIAEDVVDQVEEVNSIFDIETVDVKHDVSPFEMPFEE
SQ  LNGLKILKQLDNNCWVNSVMLQIQLTGILDGDYAMQFFKMGRVAKMIERCYTAEQCIRGAMGDVGLCMYRLLKDLHTGFM
SQ  VMDYKCSCTSGRLEESGAVLFCTPTKKAFPYGTCLNCNAPRMCTIRQLQGTIIFVQQKPEPVNPVSFVVKPVCSSIFRGA
SQ  VSCGHYQTNIYSQNLCVDGFGVNKIQPWTNDALNTICIKDADYNAKVEISVTPIKNTVDTTPKEEFVVKEKLNAFLVHDN
SQ  VAFYQGDVDTVVNGVDFDFIVNAANENLAHGGGLAKALDVYTKGKLQRLSKEHIGLAGKVKVGTGVMVECDSLRIFNVVG
SQ  PRKGKHERDLLIKAYNTINNEQGTPLTPILSCGIFGIKLETSLEVLLDVCNTKEVKVFVYTDTEVCKVKDFVSGLVNVQK
SQ  VEQPKIEPKPVSVIKVAPKPYRVDGKFSYFTEDLLCVADDKPIVLFTDSMLTLDDRGLALDNALSGVLSAAIKDCVDINK
SQ  AIPSGNLIKFDIGSVVVYMCVVPSEKDKHLDNNVQRCTRKLNRLMCDIVCTIPADYILPLVLSSLTCNVSFVGELKAAEA
SQ  KVITIKVTEDGVNVHDVTVTTDKSFEQQVGVIADKDKDLSGAVPSDLNTSELLTKAIDVDWVEFYGFKDAVTFATVDHSA
SQ  FAYESAVVNGIRVLKTSDNNCWVNAVCIALQYSKPHFISQGLDAAWNKFVLGDVEIFVAFVYYVARLMKGDKGDAEDTLT
SQ  KLSKYLANEAQVQLEHYSSCVECDAKFKNSVASINSAIVCASVKRDGVQVGYCVHGIKYYSRVRSVRGRAIIVSVEQLEP
SQ  CAQSRLLSGVAYTAFSGPVDKGHYTVYDTAKKSMYDGDRFVKHDLSLLSVTSVVMVGGYVAPVNTVKPKPVINQLDEKAQ
SQ  KFFDFGDFLIHNFVIFFTWLLSMFTLCKTAVTTGDVKIMAKAPQRTGVVLKRSLKYNLKASAAVLKSKWWLLAKFTKLLL
SQ  LIYTLYSVVLLCVRFGPFNFCSETVNGYAKSNFVKDDYCDGSLGCKMCLFGYQELSQFSHLDVVWKHITDPLFSNMQPFI
SQ  VMVLLLIFGDNYLRCFLLYFVAQMISTVGVFLGYKETNWFLHFIPFDVICDELLVTVIVIKVISFVRHVLFGCENPDCIA
SQ  CSKSARLKRFPVNTIVNGVQRSFYVNANGGSKFCKKHRFFCVDCDSYGYGSTFITPEVSRELGNITKTNVQPTGPAYVMI
SQ  DKVEFENGFYRLYSCETFWRYNFDITESKYSCKEVFKNCNVLDDFIVFNNNGTNVTQVKNASVYFSQLLCRPIKLVDSEL
SQ  LSTLSVDFNGVLHKAYIDVLRNSFGKDLNANMSLAECKRALGLSISDHEFTSAISNAHRCDVLLSDLSFNNFVSSYAKPE
SQ  EKLSAYDLACCMRAGAKVVNANVLTKDQTPIVWHAKDFNSLSAEGRKYIVKTSKAKGLTFLLTINENQAVTQIPATSIVA
SQ  KQGAGDAGHSLTWLWLLCGLVCLIQFYLCFFMPYFMYDIVSSFEGYDFKYIENGQLKNFEAPLKCVRNVFENFEDWHYAK
SQ  FGFTPLNKQSCPIVVGVSEIVNTVAGIPSNVYLVGKTLIFTLQAAFGNAGVCYDIFGVTTPEKCIFTSACTRLEGLGGNN
SQ  VYCYNTALMEGSLPYSSIQANAYYKYDNGNFIKLPEVIAQGFGFRTVRTIATKYCRVGECVESNAGVCFGFDKWFVNDGR
SQ  VANGYVCGTGLWNLVFNILSMFSSSFSVAAMSGQILLNCALGAFAIFCCFLVTKFRRMFGDLSVGVCTVVVAVLLNNVSY
SQ  IVTQNLVTMIAYAILYFFATRSLRYAWIWCAAYLIAYISFAPWWLCAWYFLAMLTGLLPSLLKLKVSTNLFEGDKFVGTF
SQ  ESAAAGTFVIDMRSYEKLANSISPEKLKSYAASYNRYKYYSGNANEADYRCACYAYLAKAMLDFSRDHNDILYTPPTVSY
SQ  GSTLQAGLRKMAQPSGFVEKCVVRVCYGNTVLNGLWLGDIVYCPRHVIASNTTSAIDYDHEYSIMRLHNFSIISGTAFLG
SQ  VVGATMHGVTLKIKVSQTNMHTPRHSFRTLKSGEGFNILACYDGCAQGVFGVNMRTNWTIRGSFINGACGSPGYNLKNGE
SQ  VEFVYMHQIELGSGSHVGSSFDGVMYGGFEDQPNLQVESANQMLTVNVVAFLYAAILNGCTWWLKGEKLFVEHYNEWAQA
SQ  NGFTAMNGEDAFSILAAKTGVCVERLLHAIQVLNNGFGGKQILGYSSLNDEFSINEVVKQMFGVNLQSGKTTSMFKSISL
SQ  FAGFFVMFWAELFVYTTTIWVNPGFLTPFMILLVALSLCLTFVVKHKVLFLQVFLLPSIIVAAIQNCAWDYHVTKVLAEK
SQ  FDYNVSVMQMDIQGFVNIFICLFVALLHTWRFAKERCTHWCTYLFSLIAVLYTALYSYDYVSLLVMLLCAISNEWYIGAI
SQ  IFRICRFGVAFLPVEYVSYFDGVKTVLLFYMLLGFVSCMYYGLLYWINRFCKCTLGVYDFCVSPAEFKYMVANGLNAPNG
SQ  PFDALFLSFKLMGIGGPRTIKVSTVQSKLTDLKCTNVVLMGILSNMNIASNSKEWAYCVEMHNKINLCDDPETAQELLLA
SQ  LLAFFLSKHSDFGLGDLVDSYFENDSILQSVASSFVGMPSFVAYETARQEYENAVANGSSPQIIKQLKKAMNVAKAEFDR
SQ  ESSVQKKINRMAEQAAAAMYKEARAVNRKSKVVSAMHSLLFGMLRRLDMSSVDTILNMARNGVVPLSVIPATSAARLVVV
SQ  VPDHDSFVKMMVDGFVHYAGVVWTLQEVKDNDGKNVHLKDVTKENQEILVWPLILTCERVVKLQNNEIMPGKMKVKATKG
SQ  EGDGGITSEGNALYNNEGGRAFMYAYVTTKPGMKYVKWEHDSGVVTVELEPPCRFVIDTPTGPQIKYLYFVKNLNNLRRG
SQ  AVLGYIGATVRLQAGKQTEFVSNSHLLTHCSFAVDPAAAYLDAVKQGAKPVGNCVKMLTNGSGSGQAITCTIDSNTTQDT
SQ  YGGASVCIYCRAHVAHPTMDGFCQYKGKWVQVPIGTNDPIRFCLENTVCKVCGCWLNHGCTCDRTAIQSFDNSYLNRVRG
SQ  SSAARLEPCNGTDIDYCVRAFDVYNKDASFIGKNLKSNCVRFKNVDKDDAFYIVKRCIKSVMDHEQSMYNLLKGCNAVAK
SQ  HDFFTWHEGRTIYGNVSRQDLTKYTMMDLCFALRNFDEKDCEVFKEILVLTGCCSTDYFEMKNWFDPIENEDIHRVYAAL
SQ  GKVVANAMLKCVAFCDEMVLKGVVGVLTLDNQDLNGNFYDFGDFVLCPPGMGIPYCTSYYSYMMPVMGMTNCLASECFMK
SQ  SDIFGQDFKTFDLLKYDFTEHKEVLFNKYFKYWGQDYHPDCVDCHDEMCILHCSNFNTLFATTIPNTAFGPLCRKVFIDG
SQ  VPVVATAGYHFKQLGLVWNKDVNTHSTRLTITELLQFVTDPTLIVASSPALVDKRTVCFSVAALSTGLTSQTVKPGHFNK
SQ  EFYDFLRSQGFFDEGSELTLKHFFFTQKGDAAIKDFDYYRYNRPTMLDIGQARVAYQVAARYFDCYEGGCITSREVVVTN
SQ  LNKSAGWPLNKFGKAGLYYESISYEEQDAIFSLTKRNILPTMTQLNLKYAISGKERARTVGGVSLLATMTTRQFHQKCLK
SQ  SIVATRNATVVIGTTKFYGGWDNMLKNLMADVDDPKLMGWDYPKCDRAMPSMIRMLSAMILGSKHVTCCTASDKFYRLSN
SQ  ELAQVLTEVVYSNGGFYFKPGGTTSGDATTAYANSVFNIFQAVSSNINCVLSVNSSNCNNFNVKKLQRQLYDNCYRNSNV
SQ  DESFVDDFYGYLQKHFSMMILSDDSVVCYNKTYAGLGYIADISAFKATLYYQNGVFMSTAKCWTEEDLSIGPHEFCSQHT
SQ  MQIVDENGKYYLPYPDPSRIISAGVFVDDITKTDAVILLERYVSLAIDAYPLSKHPKPEYRKVFYALLDWVKHLNKTLNE
SQ  GVLESFSVTLLDEHESKFWDESFYASMYEKSTVLQAAGLCVVCGSQTVLRCGDCLRRPMLCTKCAYDHVFGTDHKFILAI
SQ  TPYVCNTSGCNVNDVTKLYLGGLNYYCVDHKPHLSFPLCSAGNVFGLYKSSALGSMDIDVFNKLSTSDWSDIRDYKLAND
SQ  AKESLRLFAAETVKAKEESVKSSYAYATLKEIVGPKELLLLWESGKAKPPLNRNSVFTCFQITKDSKFQVGEFVFEKVDY
SQ  GSDTVTYKSTATTKLVPGMLFILTSHNVAPLRAPTMANQEKYSTIYKLHPSFNVSDAYANLVPYYQLIGKQRITTIQGPP
SQ  GSGKSHCSIGIGVYYPGARIVFTACSHAAVDSLCAKAVTAYSVDKCTRIIPARARVECYSGFKPNNNSAQYVFSTVNALP
SQ  EVNADIVVVDEVSMCTNYDLSVINQRISYKHIVYVGDPQQLPAPRVLISKGVMEPIDYNVVTQRMCAIGPDVFLHKCYRC
SQ  PAEIVNTVSELVYENKFVPVKEASKQCFKIFERGSVQVDNGSSINRRQLDVVKRFIHKNSTWSKAVFISPYNSQNYVAAR
SQ  LLGLQTQTVDSAQGSEYDYVIFAQTSDTAHACNANRFNVAITRAKKGIFCIMSDRTLFDALKFFEITMTDLQSESSCGLF
SQ  KDCARNPIDLPPSHATTYLSLSDRFKTSGDLAVQIGNNNVCTYEHVISYMGFRFDVSMPGSHSLFCTRDFAMRHVRGWLG
SQ  MDVEGAHVTGDNVGTNVPLQVGFSNGVDFVAQPEGCVLTNTGSVVKPVRARAPPGEQFTHIVPLLRKGQPWSVLRKRIVQ
SQ  MIADFLAGSSDVLVFVLWAGGLELTTMRYFVKIGAVKHCQCGTVATCYNSVSNDYCCFKHALGCDYVYNPYVIDIQQWGY
SQ  VGSLSTNHHAICNVHRNEHVASGDAIMTRCLAVYDCFVKNVDWSITYPMIANENAINKGGRTVQSHIMRAAIKLYNPKAI
SQ  HDIGNPKGIRCAVTDAKWYCYDKNPINSNVKTLEYDYMTHGQMDGLCLFWNCNVDMYPEFSIVCRFDTRTRSTLNLEGVN
SQ  GGSLYVNNHAFHTPAYDKRAMAKLKPAPFFYYDDGSCEVVHDQVNYVPLRATNCITKCNIGGAVCSKHANLYRAYVESYN
SQ  IFTQAGFNIWVPTTFDCYNLWQTFTEVNLQGLENIAFNVVNKGSFVGADGELPVAISGDKVFVRDGNTDNLVFVNKTSLP
SQ  TNIAFELFAKRKVGLTPPLSILKNLGVVATYKFVLWDYEAERPLTSFTKSVCGYTDFAEDVCTCYDNSIQGSYERFTLST
SQ  NAVLFSATAVKTGGKSLPAIKLNFGMLNGNAIATVKSEDGNIKNINWFVYVRKDGKPVDHYDGFYTQGRNLQDFLPRSTM
SQ  EEDFLNMDIGVFIQKYGLEDFNFEHVVYGDVSKTTLGGLHLLISQVRLSKMGILKAEEFVAASDITLKCCTVTYLNDPSS
SQ  KTVCTYMDLLLDDFVSVLKSLDLTVVSKVHEVIIDNKPWRWMLWCKDNAVATFYPQLQSAEWKCGYSMPGIYKTQRMCLE
SQ  PCNLYNYGAGLKLPSGIMFNVVKYTQLCQYFNSTTLCVPHNMRVLHLGAGSDYGVAPGTAVLKRWLPHDAIVVDNDVVDY
SQ  VSDADFSVTGDCATVYLEDKFDLLISDMYDGRTKAIDGENVSKEGFFTYINGFICEKLAIGGSIAIKVTEYSWNKKLYEL
SQ  VQRFSFWTMFCTSVNTSSSEAFVVGINYLGDFAQGPFIDGNIIHANYVFWRNSTVMSLSYNSVLDLSKFNCKHKATVVVQ
SQ  LKDSDINEMVLSLVRSGKLLVRGNGKCLSFSNHLVSTK
//
ID  P0C6X2;
PN  2'-O-methyltransferase;
GN  rep;
OS  443239;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X2;
DR  UNIPROT: Q5MQD2;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIKTSKYGLGFKWAPEFRWLLPDAAEELASPMKSDEGGLCPSTGQAMESVGFVYDNHVKIDCRCILGQEWHVQSNLIRDI
SQ  FVHEDLHVVEVLTKTAVKSGTAILIKSPLHSLGGFPKGYVMGLFRSYKTKRYVVHHLSMTTSTTNFGEDFLGWIVPFGFM
SQ  PSYVHKWFQFCRLYIEESDLIISNFKFDDYDFSVEDAYAEVHAEPKGKYSQKAYALLRQYRGIKPVLFVDQYGCDYSGKL
SQ  ADCLQAYGHYSLQDMRQKQSVWLANCDFDIVVAWHVVRDSRFVMRLQTIATICGIKYVAQPTEDVVDGDVVIREPVHLLS
SQ  ADAIVLKLPSLMKVMTHMDDFSIKSIYNVDLCDCGFVMQYGYVDCFNDNCDFYGWVSGNMMDGFSCPLCCTVYDSSEVKA
SQ  QSSGVIPENPVLFTNSTDTVNHDSFNLYGYSVTPFGSCIYWSPRPGLWIPIIKSSVKSYDDLVYSGVVGCKSIVKETALI
SQ  THALYLDYVQCKCGNLEQNHILGVNNSWCRQLLLNRGDYNMLLKNIDLFVKRRADFACKFAVCGDGFVPFLLDGLIPRSY
SQ  YLIQSGIFFTSLMSQFSQEVSDMCLKMCILFMDRVSVATFYIEHYVNRLVTQFKLLGTTLVNKMVNWFNTMLDASAPATG
SQ  WLLYQLLNGLFVVSQANFNFVALIPDYAKILVNKFYTFFKLLLECVTVDVLKDMPVLKTINGLVCIVGNKFYNVSTGLIP
SQ  GFVLPCNAQEQQIYFFEGVAESVIVEDDVIENVKSSLSSYEYCQPPKSVEKICIIDNMYMGKCGDKFFPIVMNDKNICLL
SQ  DQAWRFPCAGRKVNFNEKPVVMEIPSLMTVKVMFDLDSTFDDILGKVCSEFEVEKGVTVDDFVAVVCDAIENALNSCKEH
SQ  PVVGYQVRAFLNKLNENVVYLFDEAGDEAMASRMYCTFAIEDVEDVISSEAVEDTIDGVVEDTINDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNNDEEIVTGDNDDQIVVTGDDVDDIESIYDFDTYKA
SQ  LLVFNDVYNDALFVSYGSSVETETYFKVNGLWSPTITHTNCWLRSVLLVMQKLPFKFKDLAIENMWLSYKVGYNQSFVDY
SQ  LLTTIPKAIVLPQGGFVADFAYWFLNQFDINAYANWCCLKCGFSFDLNGLDALFFYGDIVSHVCKCGHNMTLIAADLPCT
SQ  LHFSLFDDNFCAFCTPKKIFIAACAVDVNVCHSVAVIGDEQIDGKFVTKFSGDKFDFIVGYGMSFSMSSFELPQLYGLCI
SQ  TPNVCFVKGDIINVARLVKADVIVNPANGHMLHGGGVAKAIAVAAGKKFSKETAAMVKSKGVCQVGDCYVSTGGKLCKTI
SQ  LNIVGPDARQDGRQSYVLLARAYKHLNNYDCCLSTLISAGIFSVPADVSLTYLLGVVDKQVILVSNNKEDFDIIQKCQIT
SQ  SVVGTKALAVRLTANVGRVIKFETDAYKLFLSGDDCFVSNSSVIQEVLLLRHDIQLNNDVRDYLLSKMTSLPKDWRLINK
SQ  FDVINGVKTVKYFECPNSIYICSQGKDFGYVCDGSFYKATVNQVCVLLAKKIDVLLTVDGVNFKSISLTVGEVFGKILGN
SQ  VFCDGIDVTKLKCSDFYADKILYQYENLSLADISAVQSSFGFDQQQLLAYYNFLTVCKWSVVVNGPFFSFEQSHNNCYVN
SQ  VACLMLQHINLKFNKWQWQEAWYEFRAGRPHRLVALVLAKGHFKFDEPSDATDFIRVVLKQADLSGAICELELICDCGIK
SQ  QESRVGVDAVMHFGTLAKTDLFNGYKIGCNCAGRIVHCTKLNVPFLICSNTPLSKDLPDDVVAANMFMGVGVGHYTHLKC
SQ  GSPYQHYDACSVKKYTGVSGCLTDCLYLKNLTQTFTSMLTNYFLDDVEMVAYNPDLSQYYCDNGKYYTKPIIKAQFKPFA
SQ  KVDGVYTNFKLVGHDICAQLNDKLGFNVDLPFVEYKVTVWPVATGDVVLASDDLYVKRYFKGCETFGKPVIWFCHDEASL
SQ  NSLTYFNKPSFKSENRYSVLSVDSVSEESQGNVVTSVMESQISTKEVKLKGVRKTVKIEDAIIVNDENSSIKVVKSLSLV
SQ  DVWDMYLTGCDYVVWVANELSRLVKSPTVREYIRYGIKPITIPIDLLCLRDDNQTLLVPKIFKARAIEFYGFLKWLFIYV
SQ  FSLLHFTNDKTIFYTTEIASKFTFNLFCLALKNAFQTFRWSIFIKGFLVVATVFLFWFNFLYINVIFSDFYLPNISVFPI
SQ  FVGRIVMWIKATFGLVTICDFYSKLGVGFTSHFCNGSFICELCHSGFDMLDTYAAIDFVQYEVDRRVLFDYVSLVKLIVE
SQ  LVIGYSLYTVWFYPLFCLIGLQLFTTWLPDLFMLETMHWLIRFIVFVANMLPAFVLLRFYIVVTAMYKVVGFIRHIVYGC
SQ  NKAGCLFCYKRNCSVRVKCSTIVGGVIRYYDITANGGTGFCVKHQWNCFNCHSFKPGNTFITVEAAIELSKELKRPVNPT
SQ  DASHYVVTDIKQVGCMMRLFYDRDGQRVYDDVDASLFVDINNLLHSKVKVVPNLYVVVVESDADRANFLNAVVFYAQSLY
SQ  RPILLVDKKLITTACNGISVTQTMFDVYVDTFMSHFDVDRKSFNNFVNIAHASLREGVQLEKVLDTFVGCVRKCCSIDSD
SQ  VETRFITKSMISAVAAGLEFTDENYNNLVPTYLKSDNIVAADLGVLIQNGAKHVQGNVAKAANISCIWFIDAFNQLTADL
SQ  QHKLKKACVKTGLKLKLTFNKQEASVPILTTPFSLKGGVVLSNLLYILFFVSLICFILLWALLPTYSVYKSDIHLPAYAS
SQ  FKVIDNGVVRDISVNDLCFANKFFQFDQWYESTFGSVYYHNSMDCPIVVAVMDEDIGSTMFNVPTKVLRHGFHVLHFLTY
SQ  AFASDSVQCYTPHIQISYNDFYASGCVLSSLCTMFKRGDGTPHPYCYSDGVMKNASLYTSLVPHTRYSLANSNGFIRFPD
SQ  VISEGIVRIVRTRSMTYCRVGACEYAEEGICFNFNSSWVLNNDYYRSMPGTFCGRDLFDLFYQFFSSLIRPIDFFSLTAS
SQ  SIFGAILAIVVVLVFYYLIKLKRAFGDYTSVVVINVVVWCINFLMLFVFQVYPICACVYACFYFYVTLYFPSEISVIMHL
SQ  QWIVMYGAIMPFWFCVTYVAMVIANHVLWLFSYCRKIGVNVCSDSTFEETSLTTFMITKDSYCRLKNSVSDVAYNRYLSL
SQ  YNKYRYYSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVSTSFLQSGIVKMVSPTSKIEPCIVSVTYGSMT
SQ  LNGLWLDDKVYCPRHVICSSSNMNEPDYSALLCRVTLGDFTIMSGRMSLTVVSYQMQGCQLVLTVSLQNPYTPKYTFGNV
SQ  KPGETFTVLAAYNGRPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLTGDSVKFVYMHQLELSTGCHTGTDFTGNFYGPYR
SQ  DAQVVQLPVKDYVQTVNVIAWLYAAILNNCAWFVQNDVCSTEDFNVWAMANGFSQVKADLVLDALASMTGVSIETLLAAI
SQ  KRLYMGFQGRQILGSCTFEDELAPSDVYQQLAGVKLQSKTKRFIKETIYWILISTFLFSCIISAFVKWTIFMYINTHMIG
SQ  VTLCVLCFVSFMMLLVKHKHFYLTMYIIPVLCTLFYVNYLVVYKEGFRGFTYVWLSYFVPAVNFTYVYEVFYGCILCVFA
SQ  IFITMHSINHDIFSLMFLVGRIVTLISMWYFGSNLEEDVLLFITAFLGTYTWTTILSLAIAKIVANWLSVNIFYFTDVPY
SQ  IKLILLSYLFIGYILSCYWGFFSLLNSVFRMPMGVYNYKISVQELRYMNANGLRPPRNSFEAILLNLKLLGIGGVPVIEV
SQ  SQIQSKLTDVKCANVVLLNCLQHLHVASNSKLWQYCSVLHNEILSTSDLSVAFDKLAQLLIVLFANPAAVDTKCLASIDE
SQ  VSDDYVQDSTVLQALQSEFVNMASFVEYEVAKKNLADAKNSGSVNQQQIKQLEKACNIAKSVYERDKAVARKLERMADLA
SQ  LTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLSAIPALAANTLTIVIPDKQVFDKVVDNVY
SQ  VTYAGSVWHIQTVQDADGINKQLTDISVDSNWPLVIIANRYNEVANAVMQNNELMPHKLKIQVVNSGSDMNCNIPTQCYY
SQ  NNGSSGRIVYAVLSDVDGLKYTKIMKDDGNCVVLELDPPCKFSIQDVKGLKIKYLYFIKGCNTLARGWVVGTLSSTIRLQ
SQ  AGVATEYAANSSILSLCAFSVDPKKTYLDYIQQGGVPIINCVKMLCDHAGTGMAITIKPEATINQDSYGGASVCIYCRAR
SQ  VEHPDVDGICKLRGKFVQVPLGIKDPILYVLTHDVCQVCGFWRDGSCSCVGSSVAVQSKDLNFLNRVRGTSVNARLVPCA
SQ  SGLSTDVQLRAFDICNTNRAGIGLYYKVNCCRFQRIDDDGNKLDKFFVVKRTNLEVYNKEKTYYELTKSCGVVAEHDFFT
SQ  FDIDGSRVPHIVRRNLSKYTMLDLCYALRHFDRNDCSILCEILCEYADCKESYFSKKDWYDFVENPDIINIYKKLGPIFN
SQ  RALLNTVIFADTLVEVGLVGVLTLDNQDLYGQWYDFGDFIQTAPGFGVAVADSYYSYMMPMLTMCHVLDCELFVNDSYRQ
SQ  FDLVQYDFTDYKLELFNKYFKYWGMKYHPNTVDCDNDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYH
SQ  YKELGVVMNLDVDTHRYRLSLKDLLLYAADPAMHVASASALLDLRTCCFSVAAITSGIKFQTVKPGNFNQDFYEFVKSKG
SQ  LFKEGSTVDLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFN
SQ  KFGKARLYYEALSFEEQNEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPV
SQ  VIGTTKFYGGWDDMLRHLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLVLARKHEFCCSHGDRFYRLANECAQVLSEIV
SQ  MCGGCYYVKPGGTSSGDATTAFANSVFNICQAVTANVCSLMACNGHKIEDLSIRNLQKRLYSNVYRTDYVDYTFVNEYYE
SQ  FLCKHFSMMILSDDGVVCYNSDYASKGYIANISVFQQVLYYQNNVFMSESKCWVENDITNGPHEFCSQHTMLVKIDGDYV
SQ  YLPYPDPSRILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVHHENEEYQKVFRVYLEYIKKLYNDLGTQILDSYSVIL
SQ  STCDGLKFTEESFYKNMYLKSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATNHKYVLSVSPYVCNAPNC
SQ  DVSDVTKLYLGGMSYYCENHKPHYSFKLVMNGMVFGLYKQSCTGSPYIDDFNKIASCKWTEVDDYVLANECIERLKLFAA
SQ  ETQKATEEAFKQSYASATIQEIVSDREVILCWETGKVKPPLNKNYVFTGYHFTSTGKTVLGEYVFDKSELTNGVYYRATT
SQ  TYKLSIGDVFVLTSHSVASLSAPTLVPQENYASIRFSSVYSVPLVFQNNVANYQHIGMKRYCTVQGPPGTGKSHLAIGLA
SQ  VYYYTARVVYTAASHAAVDALCEKAYKFLNINDCTRIIPAKVRVDCYDKFKINDTTCKYVFTTINALPELVTDIVVVDEV
SQ  SMLTNYELSVINARIKAKHYVYIGDPAQLPAPRVLLSKGSLEPRHFNSITKIMCCLGPDIFLGNCYRCPKEIVETVSALV
SQ  YDNKLKAKNDNSSLCFKVYFKGQTTHESSSAVNIQQIYLISKFLKANPVWNSAVFISPYNSQNYVAKRVLGVQTQTVDSA
SQ  QGSEYDYVIYSQTAETAHSVNVNRFNVAITRAKKGIFCVMSNMQLFESLNFITLPLDKIQNQTLPRLHCTTNLFKDCSKS
SQ  CLGYHPAHAPSFLAVDDKYKVNENLAVNLNICEPVLTYSRLISLMGFKLDLTLDGYSKLFITKDEAIKRVRGWVGFDVEG
SQ  AHATRENIGTNFPLQIGFSTGVDFVVEATGLFAERDCYTFKKTVAKAPPGEKFKHLIPLMSKGQKWDIVRIRIVQMLSDY
SQ  LLDLSDSVVFITWSASFELTCLRYFAKLGRELNCNVCSNRATCYNSRTGYYGCWRHSYTCDYVYNPLIVDIQQWGYTGSL
SQ  TSNHDIICNVHKGAHVASADAIMTRCLAIYDCFCKSVNWNLEYPIISNEVSINTSCRLLQRVMLKAAMLCNRYNLCYDIG
SQ  NPKGLACVKDYEFKFYDAFPVAKSVKQLFYVYDVHKDNFKDGLCMFWNCNVDKYPSNSIVCRFDTRVLNKLNLPGCNGGS
SQ  LYVNKHAFHTNPFTRTVFENLKPMPFFYYSDTPCVYVDGLESKQVDYVPLRSATCITRCNLGGAVCSKHAEEYCNYLESY
SQ  NIVTTAGFTFWVYKNFDFYNLWNTFTTLQSLENVIYNLVNVGHYDGRTGELPCAIMNDKVVVKINNVDTVIFKNNTSFPT
SQ  NIAVELFTKRSIRHHPELKILRNLNIDICWKHVLWDYVKDSLFCSSTYGVCKYTDLKFIENLNILFDGRDTGALEAFRKA
SQ  RNGVFISTEKLSRLSMIKGPQRADLNGVIVDKVGELKVEFWFAMRKDGDDVIFSRTDSLCSSHYWSPQGNLGGNCAGNVI
SQ  GNDALTRFTIFTQSRVLSSFEPRSDLERDFIDMDDNLFIAKYGLEDYAFDHIVYGSFNHKVIGGLHLLIGLFRRKKKSNL
SQ  LIQEFLQYDSSIHSYFITDQECGSSKSVCTVIDLLLDDFVSIVKSLNLSCVSKVVNINVDFKDFQFMLWCNDNKIMTFYP
SQ  KMQATNDWKPGYSMPVLYKYLNVPLERVSLWNYGKPINLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSDKE
SQ  VAPGSAVLRQWLPSGSILVDNDLNPFVSDSLVTYFGDCMTLPFDCHWDLIISDMYDPLTKNIGDYNVSKDGFFTYICHLI
SQ  RDKLSLGGSVAIKITEFSWNADLYKLMSCFAFWTVFCTNVNASSSEGFLIGINYLGKSSFEIDGNVMHANYLFWRNSTTW
SQ  NGGAYSLFDMTKFSLKLAGTAVVNLRPDQLNDLVYSLIERGKLLVRDTRKEIFVGDSLVNTC
//
ID  P0C6X3;
PN  2'-O-methyltransferase;
GN  rep;
OS  443240;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X3;
DR  UNIPROT: Q14EB2;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIKTSKYGLGFKWAPEFRWLLPDAAEELASPMKSDEGGLCPSTGQAMESVGFVYDNHVKIDCRCILGQEWHVQSNLIRDI
SQ  FVHEDLHVVEVLTKTAVKSGTAILIKSPLHSLGGFPKGYVMGLFRSYKTKRYVVHHLSMTTSTTNFGEDFLGWIVPFGFM
SQ  PSYVHKWFQFCRLYIEESDLIISNFKFDDYDFSVEDAYAEVHAEPKGKYSQKAYALLRQYRGIKPVLFVDQYGCDYSGKL
SQ  ADCLQAYGHYSLQDMRQKQSVWLANCDFDIVVAWHVVRDSRFVMRLQTIATICGIKYVAQPTEDVVDGAVVIREPVHLLS
SQ  ADAIVLKLPSLMKVMTHMDDFSIKSIYNVDLCDCGFVMQYGYVDCFNDNCDFYGWVSGNMMDGFSCPLCCTVYDSSEVKA
SQ  QSSGVIPENPVLFTNSTDTVNPDSFNLYGYSVTPFGSCIYWSPRPGLWIPIIKSSVKSYDDLVYSGVVGCKSIVKETALI
SQ  THALYLDYVQCKCGNLEQNHILGVNNSWCRQLLLNRGDYNMLLKNIDLFVKRRADFACKFAVCGDGFVPFLLDGLIPRSY
SQ  YLIQSGIFFTSLMSQFSQEVSDMCLKMCILFMDRVSVATFYIEHYVNRLVTQFKLLGTTLVNKMVNWFNTMLDASAPATG
SQ  WLLYQLLNGLFVVSQANFNFVALIPDYAKILVNKFYTFFKLLLECVTVDVLKDMPVLKTINGLVCIVGNKFYNVSTGLIP
SQ  GFVLPCNAQEQQIYFFEGVAESVIVEDDVIENVKSSLSSYEYCQPPKSVEKICIIDNMYMGKCGDKFFPIVMNDKNICLL
SQ  DQAWRFPCAGRKVNFNEKPVVMEIPSLMTVKVMFDLDSTFDDILGKVCSEFEVEKGVTVDDFVAVVCDAIENALNSCKDH
SQ  PVVGYQVRAFLNKLNENVVYLFDEAGDEAMASRMYCTFAIEDVEDVISSEAVEDTIDGVVEDTINDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEEIVTGDNDDQIVVTGDDVDDIESVYDFDTYKALLVFNDVYNDALFVSYGSSVETETYFKVNG
SQ  LWSPTITHTNCWLRSVLLVMQKLPFKFKDLAIENMWLSYKVGYNQSFVDYLLTTIPKAIVLPQGGYVADFAYWFLNQFDI
SQ  NAYANWCCLKCGFSFDLNGLDAVFFYGDIVSHVCKCGHNMTLIAADLPCTLHFSLFDDNFCAFCTPKKIFIAACAVDVNV
SQ  CHSVAVIGDEQIDGKFVTKFSGDKFDFIVGYGMSFSMSSFELAQLYGLCITPNVCFVKGDIINVARLVKADVIVNPANGH
SQ  MLHGGGVAKAIAVAAGKKFSKETAAMVKSKGVCQVGDCYVSTGGKLCKTILNIVGPDARQDGRQSYVLLARAYKHLNNYD
SQ  CCLSTLISAGIFSVPADVSLTYLLGVVDKQVILVSNNKEDFDIIQKCQITSVVGTKALAVRLTANVGRVIKFETDAYKLF
SQ  LSGDDCFVSNSSVIQEVLLLRHDIQLNNDVRDYLLSKMTSLPKDWRLINKFDVINGVKTVKYFECPNSIYICSQGKDFGY
SQ  VCDGSFYKATVNQVCVLLAKKIDVLLTVDGVNFKSISLTVGEVFGKILGNVFCDGIDVTKLKCSDFYADKILYQYENLSL
SQ  ADISAVQSSFGFDQQQLLAYYNFLTVCKWSVVVNGPFFSFEQSHNNCYVNVACLMLQHINLKFNKWQWQEAWYEFRAGRP
SQ  HRLVALVLAKGHFKFDEPSDATDFIRVVLKQADLSGAICELELICDCGIKQESRVGVDAVMHFGTLAKTDLFNGYKIGCN
SQ  CAGRIVHCTKLNVPFLICSNTPLSKDLPDDVVAANMFMGVGVGHYTHLKCGSPYQHYDACSVKKYTGVSGCLTDCLYLKN
SQ  LTQTFTSMLTNYFLDDVEMVAYNPDLSQYYCDNGKYYTKPIIKAQFKPFAKVDGVYTNFKLVGHDICAQLNDKLGFNVDL
SQ  PFVEYKVTVWPVATGDVVLASDDLYVKRYFKGCETFGKPVIWLCHDEASLNSLTYFNKPSFKSENRYSVLSVDSVSEESQ
SQ  GNVVTSVMESQISTKEVKLKGVRKTVKIEDAIIVNDENSSIKVVKSLSLVDVWDMYLTGCDYVVWVANELSRLVKSPTVR
SQ  EYIRYGIKPITIPIDLLCLRDDNQTLLVPKIFKARAIEFYGFLKWLFIYVFSLLHFTNDKTIFYTTEIASKFTFNLFCLA
SQ  LKNAFQTFRWSIFIKGFLVVATVFLFWFNFLYINVIFSDFYLPNISVFPIFVGRIVMWIKATFGLVTICDFYSKLGVGFT
SQ  SHFCNGSFICELCYSGFDMLDTYAAIDFVQYEVDRRVLFDYVSLVKLIVELVIGYSLYTVWFYPLFCLIGLQLFTTWLPD
SQ  LFMLETMHWLIRFIVFVANMLPAFVLLRFYIVVTAMYKVVGFIRHIVYGCNKAGCLFCYKRNCSVRVKCSTIVGGVIRYY
SQ  DITANGGTGFCVKHQWNCFNCHSFKPGNTFITVEAAIELSKELKRPVNPTDASHYVVTDIKQVGCMMRLFYDRDGQRVYD
SQ  DVDASLFVDINNLLHSKVKVVPNLYVVVVESDADRANFLNAVVFYAQSLYRPILLVDKKLITTACNGISVTQTMFDVYVD
SQ  TFMSHFDVDRKSFNNFVNIAHASLREGVQLEKVLDTFVGCVRKCCSIDSDVETRFITKSMISAVAAGLEFTDENYNNLVP
SQ  TYLKSDNIVAADLGVLIQNGAKHVQGNVAKAANISCIWFIDTFNQLTADLQHKLKKACVKTGLKLKLTFNKQEASVPILT
SQ  TPFSLKGGVVLSNLLYILFFISLICFILLWALLPTYSVYKSDIHLPAYASFKVIDNGVVRDISVNDLCFANKFFQFDQWY
SQ  ESTFGSFYYHNSMDCPIVVAVMDEDIGSTMFNVPTKVLRHGFHVLHFLTYAFASDSVQCYTPHIQISYNDFYASGCVLSS
SQ  LCTMFKRGDGTPHPYCYSDGVMKNASLYTSLVPHTRYSLANSNGFIRFPDVISEGIVRIVRTRSMTYCRVGACEYAEEGI
SQ  CFNFNSSWVLNNDYYRSMPGTFCGRDLFDLFYQFFSSLIRPIDFFSLTASSIFGAILAIVVVLVFYYLIKLKRAFGDYTS
SQ  VVVINVIVWCINFLMLFVFQVYPICACVYACFYFYVTLYFPSEISVIMHLQWIVMYGAIMPFWFCVTYVAMVIANHVLWL
SQ  FSYCRKIGVNVCNDSTFEETSLTTFMITKDSYCRLKNSVSDVAYNRYLSLYNKYRYYSGKMDTAAYREAACSQLAKAMET
SQ  FNHNNGNDVLYQPPTASVSTSFLQSGIVKMVSPTSKIEPCIVSVTYGSMTLNGLWLDDKVYCPRHVICLSSNMNEPDYSA
SQ  LLCRVTLGDFTIMSGRMSLTVVSYQMQGCQLVLTVSLQNPYTPKYTFGVVKPGETFTVLAAYNGRPQGAFHVTMRSSYTI
SQ  KGSFLCGSCGSVGYVLTGDSVKFVYMHQLELSTGCHTGTDFTGNFYGPYRDAQVVQLPVKDYVQTVNVIAWLYAAILNNC
SQ  AWFVQNDVCSIEDFNVWAMTNGFSQVKADLVLDALASMTGVSIETLLAAIKRLYMGFQGRQILGSCTFEDELAPSDVYQQ
SQ  LAGVKLQSKTKRFIKETIYWILISTFLFSCIISAFVKWTIFMYINTHMIGVTLCVLCFVSFMMLLVKHKHFYLTMYIIPV
SQ  LCTLFYVNYLVVYKEGFRGLTYVWLSYFVPAVNFTYVYEVFYGCILCVFAIFITMHSINHDIFSLMFLVGRIVTLISMWY
SQ  FGSNLEEDVLLFITAFLGTYTWTTILSLAIAKIVANWLSVNIFYFTDVPYIKLILLSYLFIGYILSCYWGFFSLLNSVFR
SQ  MPMGVYNYKISVQELRYMNANGLRPPRNSFEAILLNLKLLGIGGVPVIEVSQIQSKLTDVKCANVVLLNCLQHLHVASNS
SQ  RLWQYCSILHNEILSTSDLSVAFDKLAQLLIVLFANPAAVDTKCLASIDEVSDDYVQDSTVLQALQSEFVNMASFVEYEV
SQ  AKKNLADAKNSGSVNQQQIKQLEKACNIAKSVYERDKAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMVR
SQ  KLDNQALNSILDNAVKGCVPLNAIPALAANTLTIIIPDKQVFDKVVDNVYVAYAGSVWHIQTVQDADGINKQLTDISVDS
SQ  NWPLVIIANRYNEVANAVMQNNELMPHKLKIQVVNSGSDMNCNIPTQCYYNNGSSGRIVYAVLSDVDGLKYTKIIKDDGN
SQ  CVVLELDPPCKFSIQDVKGLKIKYLYFIKGCNTLARGWVVGTLSSTIRLQAGVATEYAANSSILSLCAFSVDPKKTYLDY
SQ  IQQGGVPIINCVKMLCDHAGTGMAITIKPEATINQDSYGGASVCIYCRARVEHPDVDGLCKLRGKFVQVPLGIKDPILYV
SQ  LTHDVCQVCGFWRDGSCSCVGSGVAVQSKDLNFLNRVRGTSVNARLVPCASGLSTDVQLRAFDICNTNRAGIGLYYKVNC
SQ  CRFQRIDDDGNKLDKFFVVKRTNLEVYNKEKTYYELTKSCGVVAEHDFFTFDIDGSRVPHIVRKNLSKYTMLDLCYALRH
SQ  FDCNDCSVLCEILCEYADCKESYFSKKDWYDFVENPDIINIYKKLGPIFNRALLNTVSFADTLVKVGLVGVLTLDNQDLY
SQ  GQWYDFGDFIQTAPGFGVAVADSYYSYMMPMLTMCHVLDCELFVNDSYRQFDLVQYDFTDYKLELFNKYFKYWGMKYHPN
SQ  TVDCDNDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGVVMNLDVDTHRYRLSLKDLLLYAAD
SQ  PAMHVASASALLDLRTCCFSVAAITSGIKFQTVKPGNFNQDFYEFVKSKGLFKEGSTVDLKHFFFTQDGNAAITDYNYYK
SQ  YNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLYYEALSFEEQNEIYAYTKRNVLP
SQ  TLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFYGGWDDMLRHLIKDVDNPVLMGW
SQ  DYPKCDRAMPNILRIVSSLVLARKHEFCCSHGDRFYRLANECAQVLSEIVMCGGCYYVKPGGTSSGDATTAFANSVFNIC
SQ  QAVTANVCSLMACNGHKIEDLSIRNLQKRLYSNVYRTDYVDYTFVNEYYEFLCKHFSMMILSDDGVVCYNSDYASKGYIA
SQ  NISVFQQVLYYQNNVFMSESKCWVENDITNGPHEFCSQHTMLVKIDGDYVYLPYPDPSRILGAGCFVDDLLKTDSVLLIE
SQ  RFVSLAIDAYPLVHHENEEYQKVFRVYLEYIKKLYNDLGNQILDSYSVILSTCDGLKFTDESFYKNMYLKSAVMQSVGAC
SQ  VVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATNHKYVLSVSPYVCNAPNCDVSDVTKLYLGGMSYYCENHKPHYSFKLVM
SQ  NGMVFGLYKQSCTGSPYIDDFNKIASCKWTEVDDYVLANECIERLKLFAAETQKATEEAFKQSYASATIQEIVSDREIIL
SQ  CWETGKVKPPLNKNYVFTGYHFTSTGKTVLGEYVFDKSELTNGVYYRATTTYKLSIGDVFVLTSHSVANLSAPTLVPQEN
SQ  YASIRFSSVYSVPLLFQTNVANYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYYYTARVVYTAASHAAVDALCEKAYKFLN
SQ  INDCTRIIPAKVRVDCYDKFKINDTTCKYVFTTINALPELVTDIVVVDEVSMLTNYELSVINARVKAKHYVYIGDPAQLP
SQ  APRVLLSKGSLEPRHFNSITKIMCCLGPDIFLGNCYRCPKEIVETVSALVYDNKLKAKNDNSSLCFKVYFKGQTTHESSS
SQ  AVNIQQIYLISKFLKANPVWNSAVFISPYNSQNYVAKRILGVQTQTVDSAQGSEYDYVIYSQTAETAHSINVNRFNVAIT
SQ  RAKKGIFCVMSNMQLFESLNFITLPLDKIQNQTLSRLHCTTNLFKDCSKNFLGYHPAHAPSFLSVDDKYKVNEDLAVCLN
SQ  ICEPVLTYSRLISLMGFKLDLTLDGYSKFFITKDEAIKRVRGWVGFDVEGAHATRDNIGTNFPLQIGFSTGVDFVVEATG
SQ  LFAERDCYIFKRTVAKAPPGDNFKHLIPLMSKGQKWDVVRIRIVQMLSDYLLDLSDSVVFITWSASFELTCLRYFAKLGR
SQ  ELNCDVCPNRATCYNSRTGYYGCWRHSYTCDYVYNPLIVDIQQWGYTGSLTSNHDIICNVHKGAHVASSDAIMTRCLAIY
SQ  DCFCKSVNWNLEYPIISNEVSINTSCRLLQRVMLKAAMLCNRYNLCYDIGNPKGIACVKDYEFKFYDASPVVKSVKQLFY
SQ  VYDVHKDNFKDGLCMFWNCNVDKYPSNSIVCRFDTRVLNKLNLPGCNGGSLYVNKHAFHTNPFTRTVFENLKPMPFFYYS
SQ  DTPCVYVDGLESKQVDYVPLRSATCITRCNLGGAVCSKHAEDYCKYLESYNVATTAGFTFWVYKTFDFYNLWNTFTMLQS
SQ  LENVIYNLVNAGHYDGRIGELPCAIMNDKVVVKINNVDTVIFKNNTSLPTNIAVELFTKRSIRHHPELKILRNLNIDICW
SQ  KHVLWDYVKDSLFCSSTYGVCKYTDLNFIENLNVLFDGRDNGALEAFRKARNGVFISTGKLSSLSMIKGPQRADLNGVIV
SQ  DKVGELNVEFWFAMRKDGDDVIFSRADSLSPSHYWSPQGNLGGNCAGNASGNDALARFTIFTQSRVLSTFEPRSDLERDF
SQ  IDMEDSLFIAKYGLEDYAFDHIVYGSFNYKVIGGLHLLIGLFRRLKKSNLVIQEFLQYDSSIHSYFITDQECGSSKSVCT
SQ  VIDLLLDDFVVIVKSLNLNCVSKVVNINVDFKDFQFMLWCNDNKIMTFYPKMQATSDWKPGYSMPVLYKYLNVPLERVSL
SQ  WNYGKAINLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSDKEVAPGSAVLRQWLPSGSILVDNDLNPFVSDS
SQ  LVTYFGDCMTLPFDCHWDLIISDMYDPLTKNIGDYNVSKDGFFTYICYLIRDKLSLGGSVAIKITEFSWNADLYKLMSYF
SQ  AFWTVFCTNVNASSSEGFLIGINYLGKSCFEIDGNVMHANYLFWRNSTTWNGGAYSLFDMSKFSLKLAGTAVVNLRPDQL
SQ  NDLVYSLIERGKLLVRDTRKEIFVGDSLVNTC
//
ID  P0C6X4;
PN  2'-O-methyltransferase;
GN  rep;
OS  443241;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X4;
DR  UNIPROT: Q0ZME9;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: Q96C36; IntAct: EBI-27129547; Score: 0.46
DE  Interaction: P32322; IntAct: EBI-27129547; Score: 0.46
DE  Interaction: O75717; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q5T4S7; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q6XZF7; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q08499; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q9HCS4; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q8IYU2; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P09884; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P49848; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q5T5X7; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q0D2I5; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q9ULT8; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q14247; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q5VZ89; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P41229; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q14999; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q9Y5X1; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q15003; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q504Q3; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q8WV41; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q96RF0; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q9Y376; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: O96006; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q86UV5; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P54727; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: O75879; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q8IYT2; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q8N3Y1; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q9P2F8; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q8N2Y8; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P54725; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P27144; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q13362; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q7Z494; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q9H9G7; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q13546; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q93008; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q9HA64; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q13889; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: A3KMH1; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q2NKX8; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P45974; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q15418; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P49643; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q14181; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q03426; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q14008; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P49642; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q7Z4H7; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: P78344; IntAct: EBI-27128759; Score: 0.35
DE  Interaction: Q9Y566; IntAct: EBI-29484590; Score: 0.44
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIKTSKYGLGFKWAPEFRWLLPDAAEELASPMKSDEGGLCPSTGQAMESVGFVYDNHVKIDCRCILGQEWHVQSNLIRDI
SQ  FVHEDLHVVEVLTKTAVKSGTAILIKSPLHSLGGFPKGYVMGLFRSYKTKRYVVHHLSMTTSTTNFGEDFFGWIVPFGFM
SQ  PSYVHKWFQFCRLYIEESDLIISNFKFDDYDFSVEAAYAEVHAEPKGKYSQKAYALLRQYRGIKPVLFVDQYGCDYSGKL
SQ  ADCLQAYGHYSLQDMRQKQSVWLANCDFDIVVAWHVVRDSRFVMRLQTIATICGIKYVAQPTEDVVDGDVVIREPVHLLS
SQ  ADAIVLKLPSLMKVMTHMDDFSIKSIYNVDLCDCGFVMQYGYVDCFNDNCDFYGWVSGNMMDGFSCPLCCTVYDSSEVKA
SQ  QSSGVIPENPVLFTNSTDTVNPDSFNLYGYSVTPFGSCIYWSPRPGLWIPIIKSSVKSYDDLVYSGVVGCKSIVKETALI
SQ  THALYLDYVQCKCGNLEQNHILGVNNSWCRQLLLNRGDYNMLLKNIDLFVKRRADFACKFAVCGDGFVPFLLDGLIPRSY
SQ  YLIQSGIFFTSLMSQFSQEVSDMCLKMCILFMDRVSVATFYIEHYVNRLVTQFKLLGTTLVNKMVNWFNTMLDASAPATG
SQ  WLLYQLLNGFFVVSQANLNFVALIPDYAKILVNKFYTFFKLLLECVTVDVLKDMPVLKTINGLVCIVGNKFYNVSTGLIP
SQ  GFVLPCNAQEQQIYFFEGVAESVIVEDDVIENVKSSLSSYEYCQPPKSVEKICIIDNMYMGKCGDKFFPIVMNDKNICLL
SQ  DHAWRFPCAGRKVNFNEKPVVMEIPSLMTVKVMFDLDSTFDDILGKVCSEFEVEKGVTVDDFVAVVCDAIENALNSCKEH
SQ  PVVGYQVRAFLNKLNENVVYLFDEAGDEAMASRMYCTFAIEDVEDVISSEAVEDTIDGVVEDTINDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNNDEDVVTGDNNDEES
SQ  VTGDNDDQIVVTGDDVDDIESIYDFDTYKALLVFNDVYNDALFVSYGSSVETETYFKVNGLWSPTITHTNCWLRSVLLVM
SQ  QKLPFKFKDLAIENMWLSYKVGYNQSFVDYLLTTIPKAIVLPQGGYVADFAYWFLNQFDINAYANWCCLKCGFSFDLNGL
SQ  DAVFFYGDIVSHVCKCGHNMTLIAADLPCTLHFSLFDDNFCAFCTPKKIFIAACAVDVNVCHSVAVIGDEQIDGKFVTKF
SQ  SGDKFDFIVGYGMSFSMSSFELAQLYGLCITPNVCFVKGDIINVARLVKADVIVNPANGHMLHGGGVAKAIAVAAGKKFS
SQ  KETAAMVKSKGVCQVGDCYVSTGGKLCKTILNIVGPDARQDGRQSYVLLARAYKHLNNYDCCLSTLISAGIFSVPADVSL
SQ  TYLLGVVDKQVILVSNNKEDFDIIQKCQITSVVGTKALAVRLTANVGRVIKFETDAYKLFLSGDDCFVSNSSVIQEVLLL
SQ  RHDIQLNNDVRDYLLSKMTSLPKDWRLINKFDVINGVKTVKYFECPNSIYICSQGKDFGYVCDGSFYKATVNQVCVLLAK
SQ  KIDVLLTVDGVNFKSISLTVGEVFGKILGNVFCDGIDVTKLKCSDFYADKILYQYENLSLADISAVQSSFGFDQQQLLAY
SQ  YNFLTVCKWSVVVNGPFFSFEQSHNNCYVNVACLMLQHINLKFNKWQWQEAWYEFRAGRPHRLVALVLAKGHFKFDEPSD
SQ  ATDFIRVVLKQADLSGAICELELICDCGIKQESRVGVDAVMHFGTLAKTDLFNGYKIGCNCAGRIVHCTKLNVPFLICSN
SQ  TPLSKDLPDDVVAANMFMGVGVGHYTHLKCGSPYQHYDACSVKKYTGVSGCLTDCLYLKNLTQTFTSMLTNYFLDDVEMV
SQ  AYNPDLSQYYCDNGKYYTKPIIKAQFKPFAKVDGVYTNFKLVGHDICAQLNDKLGFNVDLPFVEYKVTVWPVATGDVVLA
SQ  SDDLYVKRYFKGCETFGKPVIWFCHDEASLNSLTYFNKPSFKSENRYSVLSVDSVSEESQGNVVTSVMESQISTKEVKLK
SQ  GVRKTVKIEDAIIVNDENSSIKVVKSLSLVDVWDMYLTGCDYVVWVANELSRLVKSPTVREYIRYGIKPITIPIDLLCLR
SQ  DDNQTLLVPKIFKARAIEFYGFLKWLFIYVFSLLHFTNDKTIFYTTEIASKFTFNLFCLALKNAFQTFRWSIFIKGFLVV
SQ  ATVFLFWFNFLYINVIFSDFYLPNISVFPIFVGRIVMWIKATFGLVTICDFYSKLGVGFTSHFCNGSFICELCHSGFDML
SQ  DTYAAIDFVQYEVDRRVLFDYVSLVKLIVELVIGYSLYTVWFYPLFCLIGLQLFTTWLPDLFMLETMHWLIRFIVFVANM
SQ  LPAFVLLRFYIVVTAMYKVVGFIRHIVYGCNKAGCLFCYKRNCSVRVKCSTIVGGVIRYYDITANGGTGFCVKHQWNCFN
SQ  CHSFKPGNTFITVEAAIELSKELKRPVNPTDASHYVVTDIKQVGCMMRLFYDRDGQRVYDDVDASLFVDINNLLHSKVKV
SQ  VPNLYVVVVESDADRANFLNAVVFYAQSLYRPILLVDKKLITTACNGISVTQIMFDVYVDTFMSHFDVDRKSFNNFVNIA
SQ  HASLREGVQLEKVLDTFVGCVRKCCSIDSDVETRFITKSMISAVAAGLEFTDENYNNLVPTYLKSDNIVAADLGVLIQNG
SQ  AKHVQGNVAKVANISCIWFIDAFNQLTADLQHKLKKACVKTGLKLKLTFNKQEASVPILTTPFSLKGGVVLSNLLYILFF
SQ  ISLICFILLWALLPTYSVYKSDIHLPAYASFKVIDNGVVRDISVNDLCFANKFFQFDQWYESTFGSVYYHNSMDCPIVVA
SQ  VMDEDIGSTMFNVPTKVLRYGFHVLHFLTYAFASDSVQCYTPHIQISYNDFYASGCVLSSLCTMFKRGDGTPHPYCYTDG
SQ  VMKNASLYTSLVPHTRYSLANSNGFIRFPDVISEGIVRIVRTRSMTYCRVGACEYAEEGICFNFNSSWVLNNDYYRSMPG
SQ  TFCGRDFFDLFYQFFSSLIRPIDFFSLTASSIFGAILAIVVVLVFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQ
SQ  VYPICACVYACFYFYVTLYFPSEISVIMHLQWIVMYGAIMPFWFCVTYVAMVIANHVLWLFSYCRKIGVNVCSDSTFEET
SQ  SLTTFMITKDSYCRLKNSVSDVAYNRYLSLYNKYRYYSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVST
SQ  SFLQSGIVKMVSPTSKIEPCLVSVTYGSMTLNGLWLDDKVYCPRHVICLSSNMNEPDYSALLCRVTLGDFTIMSGRMSLT
SQ  VVSYQMQGCQLVLTVSLQNPYTPKYTFGVVKPGETFTVLAAYNGRPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLTGDS
SQ  VKFVYMHQLELSTGCHTGTDFNGNFYGPYRDAQVVQLPVKDYVQTVNVIAWLYAAILNNCAWFVQNDVCSIEDFNVWAMT
SQ  NGFSQVKADLVLDALASMTGVSIETLLAAIKRLYMGFQGRQILGSCTFEDELAPSDVYQQLAGVKLQSKTKRFIKETIYW
SQ  ILISTFLFSCIISAFVKWTIFMYINTHMIGVTLCVLCFVSFMMLLVKHKHFYLTMYIIPVLCTLFYVNYLVVYKEGFRGF
SQ  TYVWLSHFVPAVNFTYVYEVFYGCILCVFAIFITMHSINHDIFSLMFLVGRIVTLISMWYFGSNLEEDVLLFITAFLGTY
SQ  TWTTILSLAIAKIVANWLSVNIFYFTDVPYIKLILLSYLFIGYILSCYWGFFSLLNSVFRMPMGVYNYKISVQELRYMNA
SQ  NGLRPPRNSFEAILLNLKLLGIGGVPVIEVSQIQSKLTDVKCANVVLLNCLQHLHVASNSKLWQYCSVLHNEILSTSDLS
SQ  VAFDKLAQLLIVLFSNPAAVDTKCLASIDEVSDDYVQDSTVLQALQSEFVNMASFVEYEVAKKNLADAKNSGSVNQQQIK
SQ  QLEKACNIAKSVYERDKAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVP
SQ  LSAIPALAANTLTIIIPDKQVFDKVVDNVYVTYAGSVWHIQTVQDADGINKQLTDISVDSNWPLVIIANRYNEVANAVMQ
SQ  NNELMPHKLKIQVVNSGSDINCNIPTQCYYNNVSSGRIVYAVLSDVDGLKYTKIMKDDGNCVVLELDPPCKFSIQDVKGL
SQ  KIKYLYFIKGCNTLARGWVVGTLSSTIRLQAGVATEYAANSSILSLCAFSVDPKKTYLDYIQQGGVPIINCVKMLCDHAG
SQ  TGMAITIKPEATINQDSYGGASVCIYCRARVEHPDVDGICKLRGKFVQVPLGIKDPILYVLTHDVCQVCGFWRDGSCSCV
SQ  GSSVAVQSKDLNFLNRVRGTSVNARLVPCASGLSTDVQLRAFDICNTNRAGIGLYYKVNCCRFQRIDDDGNKLDKFFVVK
SQ  RTNLEVYNKEKTYYELTKSCGVVAEHDFFTFDIDGSRVPHIVRRNLSKYTMLDLCYALRHFDRNDCSILCEILCEYADCK
SQ  ESYFSKKDWYDFVENPDIINIYKKLGPIFNRALLNTVIFADTLVEVGLVGVLTLDNQDLYGQWYDFGDFIQTAPGFGVAV
SQ  ADSYYSYMMPMLTMCHVLDCELFVNDSYRQFDLVQYDFTDYKLELFNKYFKYWGMKYHPNTVDCDNDRCIIHCANFNILF
SQ  SMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGVVMNLDVDTHRYRLSLKDLLLYAADPAMHVASASALLDLRTCCFS
SQ  VAAITSGIKFQTVKPGNFNQDFYEFVKSKGLFKEGSTVDLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVY
SQ  KYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLYYEALSFEEQNEIYAYTKRNVLPTLTQMNLKYAISAKNRARTV
SQ  AGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFYGGWDDMLRHLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLV
SQ  LARKHEFCCSHGDRFYRLANECAQVLSEIVMCGGCYYVKPGGTSSGDATTAFANSVFNICQAVTANVCSLMACNGHKIED
SQ  LSIRNLQKRLYSNVYRTDYVDYTFVNEYYEFLCKHFSMMILSDDGVVCYNSDYANKGYIANISAFQQVLYYQNNVFMSES
SQ  KCWVENDITNGPHEFCSQHTMLVKIDGDYVYLPYPDPSRILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENEEY
SQ  QKVFRVYLEYIKKLYNDLGTQILDSYSVILSTCDGLKFTEESFYKNMYLKSAVMQSVGACVVCSSQTSLRCGSCIRKPLL
SQ  CCKCCYDHVMATNHKYVLSVSPYVCNAPNCDVSDVTKLYLGGMSYYCENHKPHYSFKLVMNGMVFGLYKQSCTGSPYIDD
SQ  FNKIASCKWTEVDDYVLANECIERLKLFAAETQKATEEAFKQSYASATIQEIVSDREVILCWETGKVKPPLNKNYVFTGY
SQ  HFTSTGKTVLGEYVFDKSELTNGVYYRATTTYKLSIGDVFVLTSHSVASLSAPTLVPQENYASIRFSSVYSVPLVFQNNV
SQ  ANYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYYYTARVVYTAASHAAVDALCEKAYKFLNINDCTRIIPAKVRVDCYDKF
SQ  KINDTTCKYVFTTINALPELVTDIVVVDEVSMLTNYELSVINARIKAKHYVYIGDPAQLPAPRVLLSKGSLEPRHFNSIT
SQ  KIMCCLGPDIFLGNCYRCPKEIVETVSALVYDNKLKAKNDNSSLCFKVYFKGQTTHESSSAVNIQQIYLISKFLKANPVW
SQ  NSAVFISPYNSQNYVAKRVLGVQTQTVDSAQGSEYDYVIYSQTAETAHSVNVNRFNVAITRAKKGIFCVMSNMQLFESLN
SQ  FITLPLDKIQNQTLPRLHCTTNLFKDCSKSCLGYHPAHAPSFLAVDDKYKVNENLAVNLNICEPVLTYSRLISLMGFKLD
SQ  LTLDGYSKLFITKDEAIKRVRGWVGFDVEGAHATRENIGTNFPLQIGFSTGVDFVVEATGLFAERDCYTFKKTVAKAPPG
SQ  EKFKHLIPLMSKGQKWDIVRIRIVQMLSDYLLDLSDSVVFITWSASFELTCLRYFAKLGRELNCNVCSNRATCYNSRTGY
SQ  YGCWRHSYTCDYVYNPLIVDIQQWGYTGSLTSNHDIICNVHKGAHVASADAIMTRCLAIYDCFCKSVNWNLEYPIISNEV
SQ  SINTSCRLLQRVMLKAAMLCNRYNLCYDIGNPKGLACVKDYEFKFYDAFPVAKSVKQLFYVYDVHKDNFKDGLCMFWNCN
SQ  VDKYPSNSIVCRFDTRVLNKLNLPGCNGGSLYVNKHAFHTNPFTRTVFENLKPMPFFYYSDTPCVYVDGLESKQVDYVPL
SQ  RSATCITRCNLGGAVCSKHAEEYCNYLESYNIVTTAGFTFWVYKTFDFYNLWNTFTTLQSLENVIYNLVNVGHYDGRTGE
SQ  LPCAIMNDKVVVKINNVDTVIFKNNTSFPTNIAVELFTKRSIRHHPELKILRNLNIDICWKHVLWDYVKDSLFCSSTYGV
SQ  CKYTDLKFIENLNILFDGRDTGALEAFRKARNGVFISTEKLSRLSMIKGPQRADLNGVIVDKVGELKVEFWFAMRKDGDD
SQ  VIFSRTDSLCSSHYWSPQGNLGGNCAGNVIGNDALTRFTIFTQSRVLSSFEPRSDLERDFIDMDDNLFIAKYGLEDYAFD
SQ  HIVYGSFNHKVIGGLHLLIGLFRRLKKSNLLIQEFLQYDSSIHSYFITDQECGSSKSVCTVIDLLLDDFVSIVKSLNLSC
SQ  VSKVVNINVDFKDFQFMLWCNDNKIMTFYPKMQATNDWKPGYSMPVLYKYLNVPLERVSLWNYGKPINLPTGCMMNVAKY
SQ  TQLCQYLNTTTLAVPVNMRVLHLGAGSDKEVAPGSAVLRQWLPSGSILVDNDLNPFVSDSLVTYFGDCMTLPFDCHWDLI
SQ  ISDMYDPLTKNIGDYNVSKDGFFTYICHLIRDKLSLGGSVAIKITEFSWNADLYKLMSCFAFWTVFCTNVNASSSEGFLI
SQ  GINYLGKSSFEIDGNVMHANYLFWRNSTTWNGGAYSLFDMTKFSLKLAGTAVVNLRPDQLNDLVYSLIERGKLLVRDTRK
SQ  EIFVGDSLVNTC
//
ID  P0C6X5;
PN  Putative 2'-O-methyl transferase;
GN  rep;
OS  277944;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X5;
DR  UNIPROT: Q6Q1S3;
DR  PDB: 5NH0;
DR  PDB: 6FV1;
DR  PDB: 6FV2;
DR  Pfam: PF13087;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000269|PubMed:20181693}. The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G). {ECO:0000269|PubMed:20181693}. The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. {ECO:0000250}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
DE  Interaction: Q86WV6; IntAct: EBI-25622122; Score: 0.46
DE  Interaction: Q9GZQ8; IntAct: EBI-25753355; Score: 0.40
DE  Interaction: Q14457; IntAct: EBI-25753431; Score: 0.40
DE  Interaction: Q00987; IntAct: EBI-25763692; Score: 0.46
DE  Interaction: Q96PM5; IntAct: EBI-25826841; Score: 0.51
DE  Interaction: Q9BYX4; IntAct: EBI-26895258; Score: 0.40
DE  Interaction: Q96C36; IntAct: EBI-27129534; Score: 0.46
DE  Interaction: P32322; IntAct: EBI-27129534; Score: 0.46
DE  Interaction: O75717; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q96CT2; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9P2P5; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P98164; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q3LIE5; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q86X02; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: O00418; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q96G74; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P07954; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q99767; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9UKK9; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q8TBZ6; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9P2D6; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9ULQ0; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q01850; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q8IXT5; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P45973; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9Y2G2; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9H706; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9UKK3; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q5T4S7; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q8IYU2; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q6XZF7; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P09884; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q08499; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9ULT8; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q14247; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q5VZ89; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P41229; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q14999; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9Y5X1; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q15003; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q504Q3; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q8WV41; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q96RF0; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9Y376; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: O96006; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q86UV5; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P54727; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: O75879; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q8IYT2; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q8N3Y1; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9P2F8; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q8N2Y8; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P27144; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q13362; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q7Z494; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9H9G7; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q13546; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q93008; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q9HA64; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q13889; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: A3KMH1; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q2NKX8; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P45974; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q15418; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P49643; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q14181; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q03426; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q14008; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P49642; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: Q7Z4H7; IntAct: EBI-27128956; Score: 0.35
DE  Interaction: P78344; IntAct: EBI-27128956; Score: 0.35
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039548;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFYNQVTLAVASDSEISGFGFAIPSVAVRTYSEAAAQGFQACRFVAFGLQDCVTGINDDDYVIALTGTNQLCAKILPFSD
SQ  RPLNLRGWLIFSNSNYVLQDFDVVFGHGAGSVVFVDKYMCGFDGKPVLPKNMWEFRDYFNNNTDSIVIGGVTYQLAWDVI
SQ  RKDLSYEQQNVLAIESIHYLGTTGHTLKSGCKLTNAKPPKYSSKVVLSGEWNAVYRAFGSPFITNGMSLLDIIVKPVFFN
SQ  AFVKCNCGSESWSVGAWDGYLSSCCGTPAKKLCVVPGNVVPGDVIITSTSAGCGVKYYAGLVVKHITNITGVSLWRVTAV
SQ  HSDGMFVASSSYDALLHRNSLDPFCFDVNTLLSNQLRLAFLGASVTEDVKFAASTGVIDISAGMFGLYDDILTNNKPWFV
SQ  RKASGLFDAIWDAFVAAIKLVPTTTGVLVRFVKSIASTVLTVSNGVIIMCADVPDAFQSVYRTFTQAICAAFDFSLDVFK
SQ  IGDVKFKRLGDYVLTENALVRLTTEVVRGVRDARIKKAMFTKVVVGPTTEVKFSVIELATVNLRLVDCAPVVCPKGKIVV
SQ  IAGQAFFYSGGFYRFMVDPTTVLNDPVFTGDLFYTIKFSGFKLDGFNHQFVTASSATDAIIAVELLLLDFKTAVFVYTCV
SQ  VDGCSVIVRRDATFATHVCFKDCYNVWEQFCIDNCGEPWFLTDYNAILQSNNPQCAIVQASESKVLLERFLPKCPEILLS
SQ  IDDGHLWNLFVEKFNFVTDWLKTLKLTLTSNGLLGNCAKRFRRVLVKLLDVYNGFLETVCSVAYTAGVCIKYYAVNVPYV
SQ  VISGFVSRVIRRERCDMTFPCVSCVTFFYEFLDTCFGVSKPNAIDVEHLELKETVFVEPKDGGQFFVSGDYLWYVVDDIY
SQ  YPASCNGVLPVAFTKLAGGKISFSDDVIVHDVEPTHKVKLIFEFEDDVVTSLCKKSFGKSIIYTGDWEGLHEVLTSAMNV
SQ  IGQHIKLPQFYIYDEEGGYDVSKPVMISQWPISNDSNGCVVEASTDFHQLECIVDDSVREEVDIIEQPFEEVEHVLSIKQ
SQ  PFSFSFRDELGVRVLDQSDNNCWISTTLVQLQLTKLLDDSIEMQLFKVGKVDSIVQKCYELSHLISGSLGDSGKLLSELL
SQ  KEKYTCSITFEMSCDCGKKFDDQVGCLFWIMPYTKLFQKGECCICHKMQTYKLVSMKGTGVFVQDPAPIDIDAFPVKPIC
SQ  SSVYLGVKGSGHYQTNLYSFNKAIDGFGVFDIKNSSVNTVCFVDVDFHSVEIEAGEVKPFAVYKNVKFYLGDISHLVNCV
SQ  SFDFVVNAANENLLHGGGVARAIDILTEGQLQSLSKDYISSNGPLKVGAGVMLECEKFNVFNVVGPRTGKHEHSLLVEAY
SQ  NSILFENGIPLMPLLSCGIFGVRIENSLKALFSCDINKPLQVFVYSSNEEQAVLKFLDGLDLTPVIDDVDVVKPFRVEGN
SQ  FSFFDCGVNALDGDIYLLFTNSILMLDKQGQLLDTKLNGILQQAALDYLATVKTVPAGNLVKLFVESCTIYMCVVPSIND
SQ  LSFDKNLGRCVRKLNRLKTCVIANVPAIDVLKKLLSSLTLTVKFVVESNVMDVNDCFKNDNVVLKITEDGINVKDVVVES
SQ  SKSLGKQLGVVSDGVDSFEGVLPINTDTVLSVAPEVDWVAFYGFEKAALFASLDVKPYGYPNDFVGGFRVLGTTDNNCWV
SQ  NATCIILQYLKPTFKSKGLNVLWNKFVTGDVGPFVSFIYFITMSSKGQKGDAEEALSKLSEYLISDSIVTLEQYSTCDIC
SQ  KSTVVEVKSAIVCASVLKDGCDVGFCPHRHKLRSRVKFVNGRVVITNVGEPIISQPSKLLNGIAYTTFSGSFDNGHYVVY
SQ  DAANNAVYDGARLFSSDLSTLAVTAIVVVGGCVTSNVPTIVSEKISVMDKLDTGAQKFFQFGDFVMNNIVLFLTWLLSMF
SQ  SLLRTSIMKHDIKVIAKAPKRTGVILTRSFKYNIRSALFVIKQKWCVIVTLFKFLLLLYAIYALVFMIVQFSPFNSLLCG
SQ  DIVSGYEKSTFNKDIYCGNSMVCKMCLFSYQEFNDLDHTSLVWKHIRDPILISLQPFVILVILLIFGNMYLRFGLLYFVA
SQ  QFISTFGSFLGFHQKQWFLHFVPFDVLCNEFLATFIVCKIVLFVRHIIVGCNNADCVACSKSARLKRVPLQTIINGMHKS
SQ  FYVNANGGTCFCNKHNFFCVNCDSFGPGNTFINGDIARELGNVVKTAVQPTAPAYVIIDKVDFVNGFYRLYSGDTFWRYD
SQ  FDITESKYSCKEVLKNCNVLENFIVYNNSGSNITQIKNACVYFSQLLCEPIKLVNSELLSTLSVDFNGVLHKAYVDVLCN
SQ  SFFKELTANMSMAECKATLGLTVSDDDFVSAVANAHRYDVLLSDLSFNNFFISYAKPEDKLSVYDIACCMRAGSKVVNHN
SQ  VLIKESIPIVWGVKDFNTLSQEGKKYLVKTTKAKGLTFLLTFNDNQAITQVPATSIVAKQGAGFKRTYNFLWYVCLFVVA
SQ  LFIGVSFIDYTTTVTSFHGYDFKYIENGQLKVFEAPLHCVRNVFDNFNQWHEAKFGVVTTNSDKCPIVVGVSERINVVPG
SQ  VPTNVYLVGKTLVFTLQAAFGNTGVCYDFDGVTTSDKCIFNSACTRLEGLGGDNVYCYNTDLIEGSKPYSTLQPNAYYKY
SQ  DAKNYVRFPEILARGFGLRTIRTLATRYCRVGECRDSHKGVCFGFDKWYVNDGRVDDGYICGDGLIDLLVNVLSIFSSSF
SQ  SVVAMSGHMLFNFLFAAFITFLCFLVTKFKRVFGDLSYGVFTVVCATLINNISYVVTQNLFFMLLYAILYFVFTRTVRYA
SQ  WIWHIAYIVAYFLLIPWWLLTWFSFAAFLELLPNVFKLKISTQLFEGDKFIGTFESAAAGTFVLDMRSYERLINTISPEK
SQ  LKNYAASYNKYKYYSGSASEADYRCACYAHLAKAMLDYAKDHNDMLYSPPTISYNSTLQSGLKKMAQPSGCVERCVVRVC
SQ  YGSTVLNGVWLGDTVTCPRHVIAPSTTVLIDYDHAYSTMRLHNFSVSHNGVFLGVVGVTMHGSVLRIKVSQSNVHTPKHV
SQ  FKTLKPGDSFNILACYEGIASGVFGVNLRTNFTIKGSFINGACGSPGYNVRNDGTVEFCYLHQIELGSGAHVGSDFTGSV
SQ  YGNFDDQPSLQVESANLMLSDNVVAFLYAALLNGCRWWLCSTRVNVDGFNEWAMANGYTSVSSVECYSILAAKTGVSVEQ
SQ  LLASIQHLHEGFGGKNILGYSSLCDEFTLAEVVKQMYGVNLQSGKVIFGLKTMFLFSVFFTMFWAELFIYTNTIWINPVI
SQ  LTPIFCLLLFLSLVLTMFLKHKFLFLQVFLLPTVIATALYNCVLDYYIVKFLADHFNYNVSVLQMDVQGLVNVLVCLFVV
SQ  FLHTWRFSKERFTHWFTYVCSLIAVAYTYFYSGDFLSLLVMFLCAISSDWYIGAIVFRLSRLIVFFSPESVFSVFGDVKL
SQ  TLVVYLICGYLVCTYWGILYWFNRFFKCTMGVYDFKVSAAEFKYMVANGLHAPHGPFDALWLSFKLLGIGGDRCIKISTV
SQ  QSKLTDLKCTNVVLLGCLSSMNIAANSSEWAYCVDLHNKINLCDDPEKAQSMLLALLAFFLSKHSDFGLDGLIDSYFDNS
SQ  STLQSVASSFVSMPSYIAYENARQAYEDAIANGSSSQLIKQLKRAMNIAKSEFDHEISVQKKINRMAEQAATQMYKEARS
SQ  VNRKSKVISAMHSLLFGMLRRLDMSSVETVLNLARDGVVPLSVIPATSASKLTIVSPDLESYSKIVCDGSVHYAGVVWTL
SQ  NDVKDNDGRPVHVKEITKENVETLTWPLILNCERVVKLQNNEIMPGKLKQKPMKAEGDGGVLGDGNALYNTEGGKTFMYA
SQ  YISNKADLKFVKWEYEGGCNTIELDSPCRFMVETPNGPQVKYLYFVKNLNTLRRGAVLGFIGATIRLQAGKQTELAVNSG
SQ  LLTACAFSVDPATTYLEAVKHGAKPVSNCIKMLSNGAGNGQAITTSVDANTNQDSYGGASICLYCRAHVPHPSMDGYCKF
SQ  KGKCVQVPIGCLDPIRFCLENNVCNVCGCWLGHGCACDRTTIQSVDISYLNRARGSSAARLEPCNGTDIDKCVRAFDIYN
SQ  KNVSFLGKCLKMNCVRFKNADLKDGYFVIKRCTKSVMEHEQSMYNLLNFSGALAEHDFFTWKDGRVIYGNVSRHNLTKYT
SQ  MMDLVYAMRNFDEQNCDVLKEVLVLTGCCDNSYFDSKGWYDPVENEDIHRVYASLGKIVARAMLKCVALCDAMVAKGVVG
SQ  VLTLDNQDLNGNFYDFGDFVVSLPNMGVPCCTSYYSYMMPIMGLTNCLASECFVKSDIFGSDFKTFDLLKYDFTEHKENL
SQ  FNKYFKHWSFDYHPNCSDCYDDMCVIHCANFNTLFATTIPGTAFGPLCRKVFIDGVPLVTTAGYHFKQLGLVWNKDVNTH
SQ  SVRLTITELLQFVTDPSLIIASSPALVDQRTICFSVAALSTGLTNQVVKPGHFNEEFYNFLRLRGFFDEGSELTLKHFFF
SQ  AQNGDAAVKDFDFYRYNKPTILDICQARVTYKIVSRYFDIYEGGCIKACEVVVTNLNKSAGWPLNKFGKASLYYESISYE
SQ  EQDALFALTKRNVLPTMTQLNLKYAISGKERARTVGGVSLLSTMTTRQYHQKHLKSIVNTRNATVVIGTTKFYGGWNNML
SQ  RTLIDGVENPMLMGWDYPKCDRALPNMIRMISAMVLGSKHVNCCTATDRFYRLGNELAQVLTEVVYSNGGFYFKPGGTTS
SQ  GDASTAYANSIFNIFQAVSSNINRLLSVPSDSCNNVNVRDLQRRLYDNCYRLTSVEESFIDDYYGYLRKHFSMMILSDDG
SQ  VVCYNKDYAELGYIADISAFKATLYYQNNVFMSTSKCWVEEDLTKGPHEFCSQHTMQIVDKDGTYYLPYPDPSRILSAGV
SQ  FVDDVVKTDAVVLLERYVSLAIDAYPLSKHPNSEYRKVFYVLLDWVKHLNKNLNEGVLESFSVTLLDNQEDKFWCEDFYA
SQ  SMYENSTILQAAGLCVVCGSQTVLRCGDCLRKPMLCTKCAYDHVFGTDHKFILAITPYVCNASGCGVSDVKKLYLGGLNY
SQ  YCTNHKPQLSFPLCSAGNIFGLYKNSATGSLDVEVFNRLATSDWTDVRDYKLANDVKDTLRLFAAETIKAKEESVKSSYA
SQ  FATLKEVVGPKELLLSWESGKVKPPLNRNSVFTCFQISKDSKFQIGEFIFEKVEYGSDTVTYKSTVTTKLVPGMIFVLTS
SQ  HNVQPLRAPTIANQEKYSSIYKLHPAFNVSDAYANLVPYYQLIGKQKITTIQGPPGSGKSHCSIGLGLYYPGARIVFVAC
SQ  AHAAVDSLCAKAMTVYSIDKCTRIIPARARVECYSGFKPNNTSAQYIFSTVNALPECNADIVVVDEVSMCTNYDLSVINQ
SQ  RLSYKHIVYVGDPQQLPAPRVMITKGVMEPVDYNVVTQRMCAIGPDVFLHKCYRCPAEIVNTVSELVYENKFVPVKPASK
SQ  QCFKVFFKGNVQVDNGSSINRKQLEIVKLFLVKNPSWSKAVFISPYNSQNYVASRFLGLQIQTVDSSQGSEYDYVIYAQT
SQ  SDTAHACNVNRFNVAITRAKKGIFCVMCDKTLFDSLKFFEIKHADLHSSQVCGLFKNCTRTPLNLPPTHAHTFLSLSDQF
SQ  KTTGDLAVQIGSNNVCTYEHVISFMGFRFDISIPGSHSLFCTRDFAIRNVRGWLGMDVESAHVCGDNIGTNVPLQVGFSN
SQ  GVNFVVQTEGCVSTNFGDVIKPVCAKSPPGEQFRHLIPLLRKGQPWLIVRRRIVQMISDYLSNLSDILVFVLWAGSLELT
SQ  TMRYFVKIGPIKYCYCGNSATCYNSVSNEYCCFKHALGCDYVYNPYAFDIQQWGYVGSLSQNHHTFCNIHRNEHDASGDA
SQ  VMTRCLAVHDCFVKNVDWTVTYPFIANEKFINGCGRNVQGHVVRAALKLYKPSVIHDIGNPKGVRCAVTDAKWYCYDKQP
SQ  VNSNVKLLDYDYATHGQLDGLCLFWNCNVDMYPEFSIVCRFDTRTRSVFNLEGVNGGSLYVNKHAFHTPAYDKRAFVKLK
SQ  PMPFFYFDDSDCDVVQEQVNYVPLRASSCVTRCNIGGAVCSKHANLYQKYVEAYNTFTQAGFNIWVPHSFDVYNLWQIFI
SQ  ETNLQSLENIAFNVVKKGCFTGVDGELPVAVVNDKVFVRYGDVDNLVFTNKTTLPTNVAFELFAKRKMGLTPPLSILKNL
SQ  GVVATYKFVLWDYEAERPFTSYTKSVCKYTDFNEDVCVCFDNSIQGSYERFTLTTNAVLFSTVVIKNLTPIKLNFGMLNG
SQ  MPVSSIKGDKGVEKLVNWYIYVRKNGQFQDHYDGFYTQGRNLSDFTPRSDMEYDFLNMDMGVFINKYGLEDFNFEHVVYG
SQ  DVSKTTLGGLHLLISQFRLSKMGVLKADDFVTASDTTLRCCTVTYLNELSSKVVCTYMDLLLDDFVTILKSLDLGVISKV
SQ  HEVIIDNKPYRWMLWCKDNHLSTFYPQLQSAEWKCGYAMPQIYKLQRMCLEPCNLYNYGAGIKLPSGIMLNVVKYTQLCQ
SQ  YLNSTTMCVPHNMRVLHYGAGSDKGVAPGTTVLKRWLPPDAIIIDNDINDYVSDADFSITGDCATVYLEDKFDLLISDMY
SQ  DGRIKFCDGENVSKDGFFTYLNGVIREKLAIGGSVAIKITEYSWNKYLYELIQRFAFWTLFCTSVNTSSSEAFLIGINYL
SQ  GDFIQGPFIAGNTVHANYIFWRNSTIMSLSYNSVLDLSKFECKHKATVVVTLKDSDVNDMVLSLIKSGRLLLRNNGRFGG
SQ  FSNHLVSTK
//
ID  P0C6X6;
PN  2'-O-methyltransferase;
GN  rep;
OS  31631;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X6;
DR  UNIPROT: Q4VID8;
DR  UNIPROT: Q4VIE7;
DR  UNIPROT: Q696Q1;
DR  UNIPROT: Q6TNG2;
DR  UNIPROT: Q9WAC3;
DR  PDB: 7NH7;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y605; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: Q5T9L3; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: Q9BQB6; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: Q9BTV4; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: P57088; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: P67812; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: Q99942; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: Q9NZB2; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: Q9UBM7; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: P39656; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: O14967; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: Q96C36; IntAct: EBI-27129572; Score: 0.46
DE  Interaction: P32322; IntAct: EBI-27129572; Score: 0.46
DE  Interaction: O75717; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q9ULT8; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q14247; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q5VZ89; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: P41229; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q14999; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: P98164; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q9Y5X1; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q15003; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q504Q3; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q8WV41; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q96RF0; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q9Y376; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q99767; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q86UV5; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: P54727; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: O75879; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q8IYT2; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q8N3Y1; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q9P2F8; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q8N2Y8; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q8TBZ6; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q9ULQ0; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q13362; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q7Z494; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q9H9G7; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q13546; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q93008; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q9HA64; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q13889; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: A3KMH1; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q2NKX8; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: P45974; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q15418; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: P49643; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q14181; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q03426; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q14008; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: P49642; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: Q7Z4H7; IntAct: EBI-27128688; Score: 0.35
DE  Interaction: P78344; IntAct: EBI-27128688; Score: 0.35
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDMICSTTAQKLETDGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNASPYHLEVLLQDALQSREAVLVTTPLGMSLEACYVRGCNPKGWTMGLFRRRSVCNTGRCTVNKHVAYQLYMIDPAGV
SQ  CLGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKRGEKGAYNKDHGCGGFGHVYDFKVEDAYDQVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGSLADGLEAYADKTLQEMKALFPTWSQELPFDVIVAWHVVRDPRYVMRLQSAATICSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQYNLFDIMSHFYMEADTVVNAFYGVALKDCGFVMQFGYIDCEQDSCDFK
SQ  GWIPGNMIDGFACTTCGHVYEVGDLIAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDSLVYTGVLGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLINRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYADKLCHAVVSKSKELLDVSLDSLGAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFQSVAKVVLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGRKIYEVERGLLHSSQLPLDVYDLTMPSQVQKAKQKPIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDDHVGLLDQAWRVPCAGRRVTFKEQPTVKEIISMPKIIKVFYELD
SQ  NDFNTILNTACGVFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNPLFLFDEAGEEVFAPKLYCA
SQ  FTAPEDDDFLEESDVEEDDVEGEETDLTITSAGQPCVASEQEESSEVLEDTLDDGPSVETSDSQVEEDVEMSDFVDLESV
SQ  IQDYENVCFEFYTTEPEFVKVLGLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVLPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHICKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRIVYKAACVVDVNDSHSMAVVDGKQIDDHRITSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKLVKAEVVVNPANGHMVHGGGVAKAIAVAAGQQFVKETTNMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYVLLERVYKHFNNYDCVVTTLISAGIFSVPSDVSLTYLLGTAKKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAARLSFNVGRSIVYETDANKLILINDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVLPEGWRVVNKFYQINGV
SQ  RTVKYFECTGGIDICSQDKVFGYVQQGIFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCFKWQVVVNGKYFTFKQANNNCFVNVSCLML
SQ  QSLHLTFKIVQWQEAWLEFRSGRPARFVALVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  LDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFIGDNVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGKLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYKPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTVCDSLNSKLGFDSSKEFVEYKITEWPTATGDVVLANDDLYVKRYERGCITFGKPVIWLSHEKASLNSLTYF
SQ  NRPLLVDDNKFDVLKVDDVDDSGDSSESGAKETKEINIIKLSGVKKPFKVEDSVIVNDDTSETKYVKSLSIVDVYDMWLT
SQ  GCKYVVRTANALSRAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPAVNVVKAVRNKTSACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEIASKLTCKLVALAFKNAFLTFKWSMVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQW
SQ  IKNTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELFMLSTLHWSFRLLVALANMLPAHVFMRFYIIIASFIKLFSLFKHVAYGCSKSGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDVMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCSMRLFYDRDGQRIYDDVNASLFVDYSNLLHSKVKSVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  NLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQIYKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKSDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQFSSDFQHKLKKAC
SQ  CKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFVLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVIDQDFGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFTMADGSPQPYCYTDGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVR
SQ  VVRTRSMSYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLVFYYLIKLKRAFGDYTSVVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYIAVVVSNHAFWVFSYCRKLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCVVSVTYGNMTLNGLWLDD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMRGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVIMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  IQDYIQSVNFLAWLYAAILNNCNWFIQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLFKGTVCWIMASTFLFSCIITAFVKWTMFMYVTTNMFSITFCALCV
SQ  ISLAMLLVKHKHLYLTMYITPVLFTLLYNNYLVVYKHTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLVGMVFVTLRSI
SQ  NHDLFSFIMFVGRLISVFSLWYKGSNLEEEILLMLASLFGTYTWTTVLSMAVAKVIAKWVAVNVLYFTDIPQIKIVLLCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANVVLLNCLQHLHVASNSKLWHYCSTLHNEILATSDLSVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEARFSGSANQQQLKQLEKACNIAKSAYERDRAVAKKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLNIIVPDKSVYDQIVDNIYVTYAGNVW
SQ  QIQTIQDSDGTNKQLNEISDDCNWPLVIIANRYNEVSATVLQNNELMPAKLKIQVVNSGPDQTCNTPTQCYYNNSNNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDAKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTSQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCRVCGFWRDGSCSCVSTDTTVQSKDTNFLNRVRGASVDARLVPCASGLSTDVQ
SQ  LRAFDIYNASVAGIGLHLKVNCCRFQRVDENGDKLDQFFVVKRTDLTIYNREMKCYERVKDCKFVAEHDFFTFDVEGSRV
SQ  PHIVRKDLTKYTMLDLCYALRHFDRNDCMLLCDILSIYAGCEQSYFTKKDWYDFVENPDIINVYKKLGPIFNRALVSATE
SQ  FADKLVEVGLVGVLTLDNQDLNGKWYDFGDYVIAAPGCGVAIADSYYSYIMPMLTMCHALDCELYVNNAYRLFDLVQYDF
SQ  TDYKLELFNKYFKHWSMPYHPNTVDCQDDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGIVM
SQ  NMDVDTHRYRLSLKDLLLYAADPALHVASASALYDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYDFVLSKGLLKEGSSV
SQ  DLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLY
SQ  YEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFY
SQ  GGWDDMLRRLIKDVDNPVLMGWDYPKCDRAMPNILRIVSSLVLARKHETCCSQSDRFYRLANECAQVLSEIVMCGGCYYV
SQ  KPGGTSSGDATTAFANSVFNICQAVSANVCALMSCNGNKIEDLSIRALQKRLYSHVYRSDKVDSTFVTEYYEFLNKHFSM
SQ  MILSDDGVVCYNSDYASKGYIANISAFQQVLYYQNNVFMSESKCWVEHDINNGPHEFCSQHTMLVKMDGDDVYLPYPNPS
SQ  RILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENEEYQKVFRVYLAYIKKLYNDLGNQILDSYSVILSTCDGQKF
SQ  TDESFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATDHKYVLSVSPYVCNAPGCDVNDVTKL
SQ  YLGGMSYYCEDHKPQYSFKLVMNGLVFGLYKQSCTGSPYIDDFNRIASCKWTDVDDYILANECTERLKLFAAETQKATEE
SQ  AFKQSYASATIQEIVSERELILSWEIGKVKPPLNKNYVFTGYHFTKNGKTVLGEYVFDKSELTNGVYYRATTTYKLSVGD
SQ  VFVLTSHSVANLSAPTLVPQENYSSIRFASVYSVLETFQNNVVNYQHIGMKRYCTVQGPPGTGKSHLAIGLAVFYCTARV
SQ  VYTAASHAAVDALCEKAYKFLNINDCTRIVPAKVRVECYDKFKINDTTRKYVFTTINALPEMVTDIVVVDEVSMLTNYEL
SQ  SVINARIRAKHYVYIGDPAQLPAPRVLLSKGTLEPKYFNTVTKLMCCLGPDIFLGTCYRCPKEIVDTVSALVYENKLKAK
SQ  NESSLLCFKVYYKGVTTHESSSAVNMQQIYLINKFLKANPLWHKAVFISPYNSQNFAAKRVLGLQTQTVDSAQGSEYDYV
SQ  IYSQTAETAHSVNVNRFNVAITRAKKGILCVMSNMQLFEALQFTTLTLDKVPQAVETKVQCSTNLFKDCSKSYSGYHPAH
SQ  APSFLAVDDKYKATGDLAVCLGIGDSAVTYSRLISLMGFKLDVTLDGYCKLFITKEEAVKRVRAWVGFDAEGAHATLDSI
SQ  GTNFPLQLGFSTGIDFVVEATGLFADRDGYSFKKAVAKAPPGEQFKHLIPLMTRGHRWDVVRPRIVQMFADHLIDLSDCV
SQ  VLVTWAANFELTCLRYFAKVGREISCNVCTKRATVYNSRTGYYGCWRHSVTCDYLYNPLIVDIQQWGYIGSLSSNHDLYC
SQ  SVHKGAHVASSDAIMTRCLAVYDCFCNNINWNVEYPIISNELSINTSCRVLQRVILKAAMLCNRYTLCYDIGNPKGIACV
SQ  KDFDFKFYDAQPIVKSVKTLLYSFEAHKDSFKDGLCMFWNCNVDKYPPNAVVCRFDTRVLNNLNLPGCNGGSLYVNKHAF
SQ  HTKPFARAAFEHLKPMPFFYYSDTPCVYMDGMDAKQVDYVPLKSATCITRCNLGGAVCLKHAEEYREYLESYNTATTAGF
SQ  TFWVYKTFDFYNLWNTFTKLQSLENVVYNLVKTGHYTGQAGEMPCAIINDKVVTKIDKEDVVIFINNTTYPTNVAVELFA
SQ  KRSVRHHPELKLFRNLNIDVCWKHVIWDYARESIFCSNTYGVCMYTDLKFIDKLNVLFDGRDNGAFEAFKRSNNGVYIST
SQ  TKVKSLSMIRGPPRAELNGVVVDKVGDTDCVFYFAVRKEGQDVIFSQFDSLGVSSNQSPQGNLGSNGKPGNVGGNDALSI
SQ  STIFTQSRVISSFTCRTDMEKDFIALDQDVFIQKYGLEDYAFEHIVYGNFNQKIIGGLHLLIGLYRRQQTSNLVVQEFVS
SQ  YDSSIHSYFITDEKSGGSKSVCTVIDILLDDFVTLVKSLNLNCVSKVVNVNVDFKDFQFMLWCNDEKVMTFYPRLQAASD
SQ  WKPGYSMPVLYKYLNSPMERVSLWNYGKPVTLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSEKGVAPGSAV
SQ  LRQWLPAGTILVDNDLYPFVSDSVATYFGDCITLPFDCQWDLIISDMYDPITKNIGEYNVSKDGFFTYICHMIRDKLALG
SQ  GSVAIKITEFSWNAELYKLMGYFAFWTVFCTNANASSSEGFLIGINYLCKPKVEIDGNVMHANYLFWRNSTVWNGGAYSL
SQ  FDMAKFPLKLAGTAVINLRADQINDMVYSLLEKGKLLIRDTNKEVFVGDSLVNVI
//
ID  P0C6X8;
PN  2'-O-methyltransferase;
GN  rep;
OS  76344;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X8;
DR  UNIPROT: Q9PYA2;
DR  UNIPROT: Q9PYA3;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKMGKYGLGFKWAPEFPWMLPNASEKLGSPERSEEDGFCPSAAQEPKTKGKTLINHVRVDCSRLPALECCVQSAIIRDI
SQ  FVDEDPLNVEASTMMALQFGSAVLVKPSKRLSIQAWAKLGVLPKTPAMGLFKRFCLCNTRECVCDAHVAFQLFTVQPDGV
SQ  CLGNGRFIGWFVPVTAIPAYAKQWLQPWSILLRKGGNKGSVTSGHFRRAVTMPVYDFNVEDACEEVHLNPKGKYSRKAYA
SQ  LLKGYRGVKSILFLDQYGCDYTGRLAKGLEDYGDCTLEEMKELFPVWCDSLDNEVVVAWHVDRDPRAVMRLQTLATIRSI
SQ  GYVGQPTEDLVDGDVVVREPAHLLAANAIVKRLPRLVETMLYTDSSVTEFCYKTKLCDCGFITQFGYVDCCGDACDFRGW
SQ  VPGNMMDGFLCPGCSKSYMPWELEAQSSGVIPKGGVLFTQSTDTVNRESFKLYGHAVVPFGSAVYWSPYPGMWLPVIWSS
SQ  VKSYADLTYTGVVGCKAIVQETDAICRSLYMDYVQHKCGNLEQRAILGLDDVYHRQLLVNRGDYSLLLENVDLFVKRRAE
SQ  FACKFATCGDGLVPLLLDGLVPRSYYLIKSGQAFTSMMVNFSHEVTDMCMDMALLFMHDVKVATKYVKKVTGKLAVRFKA
SQ  LGVAVVRKITEWFDLAVDTAASAAGWLCYQLVNGLFAVANGGITFLSDVPELVKNFVDKFKVFFKVLIDSMSVSVLSGLT
SQ  VVKTASNRVCLAGCKVYEVVQKRLSAYVMPVGCNEATCLVGEIEPAVVEDDVVDVVKAPLTYQGCCKPPTSFEKICVVDK
SQ  LYMAKCGDQFYPVVVDNDTIGVLDQCWRFPCAGKKVEFNDKPKVKEIPSTRKIKINFALDATFDSVLSKACSEFEVDKDV
SQ  TLDELLDVVLDAVESTLSPCKEHDVIGTKVCALLNRLAEDYVYLFDEGGEEVIAPKMYCSFSAPDDEDCVAADVVDADEN
SQ  QGDDADDSAALVTDTQEEDGVAKGQVGVAESDARLDQVEAFDIEKVEDPILNELSAELNAPADKTYEDVLAFDAIYSEAL
SQ  SAFYAVPGDETHFKVCGFYSPAIERTNCWLRSTLIVMQSLPLEFKDLEMQKLWLSYKSSYNKEFVDKLVKSVPKSIILPQ
SQ  GGYVADFAYFFLSQCSFKAYANWRCLKCDMDLKLQGLDAMFFYGDVVSHVCKCGTGMTLLSADIPYTLHFGLRDDKFCAF
SQ  YTPRKVFRAACVVDVNDCHSMAVVDGKQIDGKVVTKFNGDKYDFMVGHGMAFSMSAFEIAQLYGSCITPNVCFVKGDVIK
SQ  VLRRVGAEVIVNPANGRMAHGAGVAGAIAKAAGKSFIKETADMVKNQGVCQVGECYESTGGNLCKTVLNIVGPDARGHGK
SQ  QCYSFLERAYQHINKCDDVVTTLISAGIFSVPTDVSLTYLIGVVTKNVILVSNNKDDFDVIEKCQVTSIAGTKALSLQLA
SQ  KNLCRDVKFETNACDSLFSDSCFVSSYDVLQEVELLRHDIQLDDDARVFVQAHMDNLPADWRLVNKFDSVDGVRTVKYFE
SQ  CPGEIFVSSQGKKFGYVQNGSFKVASVSQIRALLANKVDVLCTVDGVNFRSCCVAEGEVFGKTLGSVFCDGINVTKVRCS
SQ  AIHKGKVFFQYSGLSAADLVAVTDAFGFDEPQLLKYYNMLGMCKWPVVVCGNYFAFKQSNNNCYINVACLMLQHLSLKFH
SQ  KWQWQEAWNEFRSGKPLRFVSLVLAKGSFKFNEPSDSTDFMRVVLREADLSGATCDFEFVCKCGVKQEQRKGVDAVMHFG
SQ  TLDKGDLAKGYTIACTCGNKLVHCTQLNVPFLICSNKPEGKKLPDDVVAANIFTGGSLGHYTHVKCKPKYQLYDACNVSK
SQ  VSEAKGNFTDCLYLKNLKQTFSSKLTTFYLDDVKCVEYNPDLSQYYCESGKYYTKPIIKAQFRTFEKVEGVYTNFKLVGH
SQ  SIAEKFNAKLGFDCNSPFTEYKITEWPTATGDVVLASDDLYVSRYSGGCVTFGKPVIWLGHEEASLKSLTYFNRPSVVCE
SQ  NKFNVLPVDVSEPTDKGPVPAAVLVTGALSGAATAPGTAKEQKVCASDSVVDQVVSGFLSDLSGATVDVKEVKLNGVKKP
SQ  IKVEDSVVVNDPTSETKVVKSLSIVDVYDMFLTGCRYVVWMANELSRLVNSPTVREYVKWGMTKIVIPAKLVLLRDEKQE
SQ  FVAPKVVKAKVIACYSAVKWFFLYCFSWIKFNTDNKVIYTTEVASKLTFNLCCLAFKNALQTFNWNVVSRGFFLVATVFL
SQ  LWFNFLYANVILSDFYLPNIGFFPTFVGQIVAWVKTTFGIFTLCDLYQVSDVGYRSSFCNGSMVCELCFSGFDMLDNYDA
SQ  INVVQHVVDRRVSFDYISLFKLVVELVIGYSLYTVCFYPLFGLIGMQLLTTWLPEFFMLETMHWSARFFVFVANMLPAFT
SQ  LLRFYIVVTAMYKIFCLCRHVMYGCSRPGCLFCYKRNRSVRVKCSTVVGGTLRYYDVMANGGTGFCAKHQWNCLNCSAFG
SQ  PGNTFITHEAAADLSKELKRPVNPTDSAYYLVTEVKQVGCSMRLFYERDGQRVYDDVSASLFVDMNGLLHSKVKGVPETH
SQ  VVVVENEADKAGFLNAAVFYAQSLYRPMLLVEKKLITTANTGLSVSQTMFDLYVDSLLGVLDVDRKSLTSFVNAAHNSLK
SQ  EGVQLEQVMDTFIGCARRKCAIDSDVETKSITKSIMSAVNAGVDFTDESCNNLVPTYVKSDTIVAADLGVLIQNNAKHVQ
SQ  ANVAKAANVACIWSVDAFNQLSADLQHRLRKACSKTGLKIKLTYNKQEANVPILTTPFSLKGGAVFSKVLQWLFVVNLIC
SQ  FIVLWALMPTYAVHKSDMQLPLYASFKVIDNGVLRDVTVTDACFANKFIQFDQWYESTFGLVYYRNSRACPVVVAVIDQD
SQ  IGYTLFNVPTKVLRYGFHVLHFITHAFATDSVQCYTPHMQIPYDNFYASGCVLSSLCTMLAHADGTPHPYCYTEGIMHNA
SQ  SLYDSLAPHVRYNLANSNGYIRFPEVVSEGIVRIVRTRSMTYCRVGLCEDAEEGVCFNFNSSWVLNNPYYRAMPGTFCGR
SQ  NAFDLIHQVLGGLVRPIDFFALTASSVAGAILAIIVVLAFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQVYPTL
SQ  SCLYACFYFYTTLYFPSEISVVMHLQWLVMYGAIMPLWFCIIYVAVVVSNHALWLFSYCRKLGTEVRSDGTFEEMSLTTF
SQ  MITKESYCKLKNSVSDVAFNRYLSLYNKYRYFSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVTTSFLQS
SQ  GIVKMVFPTSKVEPCVVSVTYGNMTLNGLWLDDKVYCPRHVICSSADMTDPDYSNLLCRVISSDFCVMSGRMSLTVMSYQ
SQ  MQGSLLVLTVTLQNPNTPKYSFGVVKPGETFTVLAAYNGKSQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLTGDSVRFVY
SQ  MHQLELSTGCHTGTDFSGNFYGPYRDAQVVQLPVQDYTQTVNVVAWLYAAILNRCNWFVQSDSCSLEEFNVWAMTNGFSS
SQ  IKADLVLDALASMTGVTVEQILAAIKRLYSGFQGKQILGSCVLEDELTPSDVYQQLAGVKLQSKRTRVVKGTCCWILAST
SQ  LLFCSIISAFVKWTMFMYVTTHMLGVTLCALCFVSFAMLLVKHKHLYLTMFIMPVLCTLFYTNYLVVYKQSFRGLAYAWL
SQ  SHFVPAVDYTYMDEVLYGVVLLVAMVFVTMRSINHDVFSVMFLVGRLVSLVSMWYFGANLEEEVLLFLTSLFGTYTWTTM
SQ  LSLATAKVIAKWLAVNVLYFTDVPQVKLVLLSYLCIGYVCCCYWGVLSLLNSIFRMPLGVYNYKISVQELRYMNANGLRP
SQ  PRNSFEALVLNFKLLGIGGVPVIEVSQIQSRLTDVKCVNVVLLNCLQHLHIASSSKLWQYCSTLHNEILATSDLSVAFDK
SQ  LAQLLVVLFANPAAVDSKCLASIEEVSDDYVRDSTVLQALQSEFVNMASFVEYELAKKNLDEAKASGSANQQQIKQLEKA
SQ  CNIAKSAYERDRAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMIRKLDNQALNSILDNAVKGCVPLNAIP
SQ  SLTSNTLTIIVPDKQVFDQVVDNVYVTYAGNVWHIQSIQDADGAVKQLNEIDVNITWPLVIAANRHNEVSSVVLQNNELM
SQ  PQKLRTQVVNSGSDMNCNTPTQCYYNTTGMGKIVYAILSDCDGLKYTKIVKEDGNCVVLELDPPCKFSVQDVKGLKIKYL
SQ  YFVKGCNTLARGWVVGTLSSTVRLQAGTATEYASNSAIRSLCAFSVDPKKTYLDYIQQGGAPVTNCVKMLCDHAGTGMAI
SQ  TIKPEATTNQDSYGGASVCIYCRSRVEHPDVDGLCKLRGKFVQVPLGIKDPVSYVLTHDVCQVCGFWRDGSCSCVGTGSQ
SQ  FQSKDTNFLNRVRGTSVNARLVPCASGLDTDVQLRAFDICNANRAGIGLYYKVNCCRFQRADEDGNTLDKFFVIKRTNLE
SQ  VYNKEKECYELTKECGVVAEHEFFTFDVEGSRVPHIVRKDLSKYTMLDLCYALRHFDRNDCSTLKEILLTYAECDESYFQ
SQ  KKDWYDFVENSDIINVYKKLGPIFNRALLNTAKFADTLVEAGLVGVLTLDNQDLYGQWYDFGDFVKTVPGCGVAVADSYY
SQ  SYMMPMLTMCHALDSELFINGTYREFDLVQYDFTDFKLELFNKYFKYWSMTYHPNTCECEDDRCIIHCANFNILFSMVLP
SQ  KTCFGPLVRQIFVDGVPFVVSIGYHYKELGVVMNMDVDTHRYRLSLKDLLLYAADPALHVASASALLDLRTCCFSVAAIT
SQ  SGVKFQTVKPGNFNQDFYEFILSKGLLKEGSSVDLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVNKYFEI
SQ  YDGGCIPATQVIVNNYDKSAGYPFNKFGKARLYYEALSFEEQDEVYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSI
SQ  LSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFYGGWDDMLRRLIKDVDSPVLMGWDYPKCDRAMPNILRIISSLVLARKH
SQ  DSCCSHTDRFYRLANECAQVLSEIVMCGGCYYVKPGGTSSGDATTAFANSVFNICQAVSANVCSLMACNGHKIEDLSIRE
SQ  LQKRLYSNVYRADHVDPAFVNEYYEFLNKHFSMMILSDDGVVCYNSEFASKGYIANISAFQQVLYYQNNVFMSEAKCWVE
SQ  TDIEKGPHEFCSQHTMLVKMDGDEVYLPYPDPSRILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENPEYQNVFR
SQ  VYLEYIKKLYNDLGNQILDSYSVILSTCDGQKFTDETFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCA
SQ  YDHVMSTDHKYVLSVSPYVCNSPGCDVNDVTKLYLGGMSYYCEDHKPQYSFKLVMNGMVFGLYKQSCTGSPYIEDFNKIA
SQ  SCKWTEVDDYVLANECTERLKLFAAETQKATEESFKQCYASATIREIVSDRELILSWEIGKVRPPLNKNYVFTGYHFTSN
SQ  GKTVLGEYVFDKSELTNGVYYRATTTYKLSVGDVFILTSHAVSSLSAPTLVPQENYTSIRFASVYSVPETFQNNVPNYQH
SQ  IGMKRYCTVQGPPGTGKSHLAIGLAVYYCTARVVYTAASHAAVDALCEKAYKFLNINDCTRIVPAKVRVDCYDKFKVNDT
SQ  TRKYVFTTINALPELVTDIIVVDEVSMLTNYELSVINSRVRAKHYVYIGDPAQLPAPRVLLNKGTLEPRYFNSVTKLMCC
SQ  LGPDIFLGTCYRCPKEIVDTVSALVYHNKLKAKNDNSSMCFKVYYKGQTTHESSSAVNMQQIYLISKFLKANPSWSNAVF
SQ  ISPYNSQNYVAKRVLGLQTQTVDSAQGSEYDFVIYSQTAETAHSVNVNRFNVAITRAKKGILCVMSSMQLFESLNFSTLT
SQ  LDKINNPRLQCTTNLFKDCSRSYAGYHPAHAPSFLAVDDKYKVGGDLAVCLNVADSAVTYSRLISLMGFKLDLTLDGYCK
SQ  LFITRDEAIRRVRAWVGFDAEGAHATRDSIGTNFPLQLGFSTGIDFVVEATGMFAERDGYVFKKAVARAPPGEQFKHLVP
SQ  LMSRGQKWDVVRIRIVQMLSDHLVDLADSVVLVTWAASFELTCLRYFAKVGKEVVCSVCNKRATCFNSRTGYYGCWRHSY
SQ  SCDYLYNPLIVDIQQWGYTGSLTSNHDLICSVHKGAHVASSDAIMTRCLAVHDCFCKSVNWSLEYPIISNEVSVNTSCRL
SQ  LQRVMFRAAMLCNRYDVCYDIGNPKGLACVKGYDFKFYDASPVVKSVKQFVYKYEAHKDQFLDGLCMFWNCNVDKYPANA
SQ  VVCRFDTRVLNKLNLPGCNGGSLYVNKHAFHTSPFTRAAFENLKPMPFFYYSDTPCVYMEGMESKQVDYVPLRSATCITR
SQ  CNLGGAVCLKHAEDYREYLESYNTATTAGFTFWVYKTFDFYNLWNTFTRLQSLENVVYNLVNAGHFDGRAGELPCAVIGE
SQ  KVIAKIQNEDVVVFKNNTPFPTNVAVELFAKRSIRPHPELKLFRNLNIDVCWSHVLWDYAKDSVFCSSTYKVCKYTDLQC
SQ  IESLNVLFDGRDNGALEAFKKCRDGVYINTTKIKSLSMIKGPQRADLNGVVVEKVGDSDVEFWFAMRRDGDDVIFSRTGS
SQ  LEPSHYRSPQGNPGGNRVGDLSGNEALARGTIFTQSRFLSSFAPRSEMEKDFMDLDEDVFIAKYSLQDYAFEHVVYGSFN
SQ  QKIIGGLHLLIGLARRQQKSNLVIQEFVPYDSSIHSYFITDENSGSSKSVCTVIDLLLDDFVDIVKSLNLNCVSKVVNVN
SQ  VDFKDFQFMLWCNEEKVMTFYPRLQAAADWKPGYVMPVLYKYLESPLERVNLWNYGKPITLPTGCLMNVAKYTQLCQYLN
SQ  TTTLAVPANMRVLHLGAGSDKDVAPGSAVLRQWLPAGSILVDNDINPFVSDSVASYYGNCITLPIACQWDLIISDMYDPL
SQ  TKNIGEYNVSKDGFFTYLCHLIRDKLALGGSVAIKITEFSWNAELYSLMGKFAFWTIFCTNVNASSSEGFLIGINWLNRT
SQ  RTEIDGKTMHANYLFWRNSTMWNGGAYSLFDMSKFPLKVAGTAVVSLKPDQINDLVLSLIEKGKLLVRDTRKEVFVGDSL
SQ  VNVK
//
ID  P0C6X9;
PN  2'-O-methyltransferase;
GN  rep;
OS  11142;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000269|PubMed:10400784}. [Uridylate-specific endoribonuclease nsp15]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X9;
DR  UNIPROT: O39225;
DR  UNIPROT: O39226;
DR  UNIPROT: P16342;
DR  UNIPROT: P19750;
DR  PDB: 2GTH;
DR  PDB: 2GTI;
DR  PDB: 3VC8;
DR  PDB: 3VCB;
DR  PDB: 4YPT;
DR  PDB: 5WFI;
DR  PDB: 6JIJ;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease nsp15]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (PubMed:32198201). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32198201}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: O88888; IntAct: EBI-25509102; Score: 0.37
DE  Interaction: P40337; IntAct: EBI-25507613; Score: 0.37
DE  Interaction: Q8TF42; IntAct: EBI-25507637; Score: 0.37
DE  Interaction: O95433; IntAct: EBI-25507641; Score: 0.37
DE  Interaction: Q14653; IntAct: EBI-25507645; Score: 0.37
DE  Interaction: Q9JJC6; IntAct: EBI-25508183; Score: 0.37
DE  Interaction: Q68EF0; IntAct: EBI-25508294; Score: 0.37
DE  Interaction: Q8BHK0; IntAct: EBI-25508313; Score: 0.37
DE  Interaction: P97434; IntAct: EBI-25508317; Score: 0.37
DE  Interaction: A2A870; IntAct: EBI-25508321; Score: 0.37
DE  Interaction: Q5I043; IntAct: EBI-25508325; Score: 0.37
DE  Interaction: Q8BHN3; IntAct: EBI-25508335; Score: 0.37
DE  Interaction: Q99JP6; IntAct: EBI-25508349; Score: 0.37
DE  Interaction: E9PW83; IntAct: EBI-25508365; Score: 0.37
DE  Interaction: Q80YT7; IntAct: EBI-25508369; Score: 0.37
DE  Interaction: Q80TL7; IntAct: EBI-25508399; Score: 0.37
DE  Interaction: Q8BMD2; IntAct: EBI-25508403; Score: 0.37
DE  Interaction: Q7TNM2; IntAct: EBI-25508407; Score: 0.37
DE  Interaction: O08992; IntAct: EBI-25508411; Score: 0.37
DE  Interaction: P55264; IntAct: EBI-25508427; Score: 0.37
DE  Interaction: Q8BIJ7; IntAct: EBI-25508435; Score: 0.37
DE  Interaction: Q9JIY5; IntAct: EBI-25508439; Score: 0.37
DE  Interaction: P12849; IntAct: EBI-25508937; Score: 0.37
DE  Interaction: Q8BJU0; IntAct: EBI-25508953; Score: 0.37
DE  Interaction: Q6P1G0; IntAct: EBI-25509000; Score: 0.37
DE  Interaction: O88907; IntAct: EBI-25509007; Score: 0.37
DE  Interaction: Q8C008; IntAct: EBI-25509017; Score: 0.37
DE  Interaction: Q8VHZ5; IntAct: EBI-25509023; Score: 0.37
DE  Interaction: Q9EQJ9; IntAct: EBI-25509027; Score: 0.37
DE  Interaction: Q8K296; IntAct: EBI-25509065; Score: 0.37
DE  Interaction: Q8BMJ7; IntAct: EBI-25509127; Score: 0.37
DE  Interaction: P59280; IntAct: EBI-25509153; Score: 0.37
DE  Interaction: Q05512; IntAct: EBI-25509163; Score: 0.37
DE  Interaction: Q8VHJ5; IntAct: EBI-25509167; Score: 0.37
DE  Interaction: Q03141; IntAct: EBI-25509171; Score: 0.37
DE  Interaction: Q8BMK0; IntAct: EBI-25509175; Score: 0.37
DE  Interaction: O35231; IntAct: EBI-25509183; Score: 0.37
DE  Interaction: Q8VHH5; IntAct: EBI-25509226; Score: 0.37
DE  Interaction: P00397; IntAct: EBI-25509264; Score: 0.37
DE  Interaction: P10639; IntAct: EBI-25509269; Score: 0.37
DE  Interaction: P03416; IntAct: EBI-25641946; Score: 0.40
DE  Interaction: Q9BYX4; IntAct: EBI-26895271; Score: 0.40
GO  GO:0039714;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKMGKYGLGFKWAPEFPWMLPNASEKLGNPERSEEDGFCPSAAQEPKVKGKTLVNHVRVNCSRLPALECCVQSAIIRDI
SQ  FVDEDPQKVEASTMMALQFGSAVLVKPSKRLSIQAWTNLGVLPKTAAMGLFKRVCLCNTRECSCDAHVAFHLFTVQPDGV
SQ  CLGNGRFIGWFVPVTAIPEYAKQWLQPWSILLRKGGNKGSVTSGHFRRAVTMPVYDFNVEDACEEVHLNPKGKYSCKAYA
SQ  LLKGYRGVKPILFVDQYGCDYTGCLAKGLEDYGDLTLSEMKELFPVWRDSLDSEVLVAWHVDRDPRAAMRLQTLATVRCI
SQ  DYVGQPTEDVVDGDVVVREPAHLLAANAIVKRLPRLVETMLYTDSSVTEFCYKTKLCECGFITQFGYVDCCGDTCDFRGW
SQ  VAGNMMDGFPCPGCTKNYMPWELEAQSSGVIPEGGVLFTQSTDTVNRESFKLYGHAVVPFGSAVYWSPCPGMWLPVIWSS
SQ  VKSYSGLTYTGVVGCKAIVQETDAICRSLYMDYVQHKCGNLEQRAILGLDDVYHRQLLVNRGDYSLLLENVDLFVKRRAE
SQ  FACKFATCGDGLVPLLLDGLVPRSYYLIKSGQAFTSMMVNFSHEVTDMCMDMALLFMHDVKVATKYVKKVTGKLAVRFKA
SQ  LGVAVVRKITEWFDLAVDIAASAAGWLCYQLVNGLFAVANGVITFVQEVPELVKNFVDKFKAFFKVLIDSMSVSILSGLT
SQ  VVKTASNRVCLAGSKVYEVVQKSLSAYVMPVGCSEATCLVGEIEPAVFEDDVVDVVKAPLTYQGCCKPPTSFEKICIVDK
SQ  LYMAKCGDQFYPVVVDNDTVGVLDQCWRFPCAGKKVEFNDKPKVRKIPSTRKIKITFALDATFDSVLSKACSEFEVDKDV
SQ  TLDELLDVVLDAVESTLSPCKEHDVIGTKVCALLDRLAGDYVYLFDEGGDEVIAPRMYCSFSAPDDEDCVAADVVDADEN
SQ  QDDDAEDSAVLVADTQEEDGVAKGQVEADSEICVAHTGSQEELAEPDAVGSQTPIASAEETEVGEASDREGIAEAKATVC
SQ  ADAVDACPDQVEAFEIEKVEDSILDELQTELNAPADKTYEDVLAFDAVCSEALSAFYAVPSDETHFKVCGFYSPAIERTN
SQ  CWLRSTLIVMQSLPLEFKDLEMQKLWLSYKAGYDQCFVDKLVKSVPKSIILPQGGYVADFAYFFLSQCSFKAYANWRCLE
SQ  CDMELKLQGLDAMFFYGDVVSHMCKCGNSMTLLSADIPYTLHFGVRDDKFCAFYTPRKVFRAACAVDVNDCHSMAVVEGK
SQ  QIDGKVVTKFIGDKFDFMVGYGMTFSMSPFELAQLYGSCITPNVCFVKGDVIKVVRLVNAEVIVNPANGRMAHGAGVAGA
SQ  IAEKAGSAFIKETSDMVKAQGVCQVGECYESAGGKLCKKVLNIVGPDARGHGKQCYSLLERAYQHINKCDNVVTTLISAG
SQ  IFSVPTDVSLTYLLGVVTKNVILVSNNQDDFDVIEKCQVTSVAGTKALSLQLAKNLCRDVKFVTNACSSLFSESCFVSSY
SQ  DVLQEVEALRHDIQLDDDARVFVQANMDCLPTDWRLVNKFDSVDGVRTIKYFECPGGIFVSSQGKKFGYVQNGSFKEASV
SQ  SQIRALLANKVDVLCTVDGVNFRSCCVAEGEVFGKTLGSVFCDGINVTKVRCSAIYKGKVFFQYSDLSEADLVAVKDAFG
SQ  FDEPQLLKYYTMLGMCKWPVVVCGNYFAFKQSNNNCYINVACLMLQHLSLKFPKWQWQEAWNEFRSGKPLRFVSLVLAKG
SQ  SFKFNEPSDSIDFMRVVLREADLSGATCNLEFVCKCGVKQEQRKGVDAVMHFGTLDKGDLVRGYNIACTCGSKLVHCTQF
SQ  NVPFLICSNTPEGRKLPDDVVAANIFTGGSVGHYTHVKCKPKYQLYDACNVNKVSEAKGNFTDCLYLKNLKQTFSSVLTT
SQ  FYLDDVKCVEYKPDLSQYYCESGKYYTKPIIKAQFRTFEKVDGVYTNFKLVGHSIAEKLNAKLGFDCNSPFVEYKITEWP
SQ  TATGDVVLASDDLYVSRYSSGCITFGKPVVWLGHEEASLKSLTYFNRPSVVCENKFNVLPVDVSEPTDKGPVPAAVLVTG
SQ  VPGADASAGAGIAKEQKACASASVEDQVVTEVRQEPSVSAADVKEVKLNGVKKPVKVEGSVVVNDPTSETKVVKSLSIVD
SQ  VYDMFLTGCKYVVWTANELSRLVNSPTVREYVKWGMGKIVTPAKLLLLRDEKQEFVAPKVVKAKAIACYCAVKWFLLYCF
SQ  SWIKFNTDNKVIYTTEVASKLTFKLCCLAFKNALQTFNWSVVSRGFFLVATVFLLWFNFLYANVILSDFYLPNIGPLPTF
SQ  VGQIVAWFKTTFGVSTICDFYQVTDLGYRSSFCNGSMVCELCFSGFDMLDNYDAINVVQHVVDRRLSFDYISLFKLVVEL
SQ  VIGYSLYTVCFYPLFVLIGMQLLTTWLPEFFMLETMHWSARLFVFVANMLPAFTLLRFYIVVTAMYKVYCLCRHVMYGCS
SQ  KPGCLFCYKRNRSVRVKCSTVVGGSLRYYDVMANGGTGFCTKHQWNCLNCNSWKPGNTFITHEAAADLSKELKRPVNPTD
SQ  SAYYSVTEVKQVGCSMRLFYERDGQRVYDDVNASLFVDMNGLLHSKVKGVPETHVVVVENEADKAGFLGAAVFYAQSLYR
SQ  PMLMVEKKLITTANTGLSVSRTMFDLYVDSLLNVLDVDRKSLTSFVNAAHNSLKEGVQLEQVMDTFIGCARRKCAIDSDV
SQ  ETKSITKSVMSAVNAGVDFTDESCNNLVPTYVKSDTIVAADLGVLIQNNAKHVQANVAKAANVACIWSVDAFNQLSADLQ
SQ  HRLRKACSKTGLKIKLTYNKQEANVPILTTPFSLKGGAVFSRMLQWLFVANLICFIVLWALMPTYAVHKSDMQLPLYASF
SQ  KVIDNGVLRDVSVTDACFANKFNQFDQWYESTFGLAYYRNSKACPVVVAVIDQDIGHTLFNVPTTVLRYGFHVLHFITHA
SQ  FATDSVQCYTPHMQIPYDNFYASGCVLSSLCTMLAHADGTPHPYCYTGGVMHNASLYSSLAPHVRYNLASSNGYIRFPEV
SQ  VSEGIVRVVRTRSMTYCRVGLCEEAEEGICFNFNRSWVLNNPYYRAMPGTFCGRNAFDLIHQVLGGLVRPIDFFALTASS
SQ  VAGAILAIIVVLAFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQVYPTLSCLYACFYFYTTLYFPSEISVVMHLQ
SQ  WLVMYGAIMPLWFCIIYVAVVVSNHALWLFSYCRKIGTEVRSDGTFEEMALTTFMITKESYCKLKNSVSDVAFNRYLSLY
SQ  NKYRYFSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVTTSFLQSGIVKMVSPTSKVEPCIVSVTYGNMTL
SQ  NGLWLDDKVYCPRHVICSSADMTDPDYPNLLCRVTSSDFCVMSGRMSLTVMSYQMQGCQLVLTVTLQNPNTPKYSFGVVK
SQ  PGETFTVLAAYNGRPQGAFHVTLRSSHTIKGSFLCGSCGSVGYVLTGDSVRFVYMHQLELSTGCHTGTDFSGNFYGPYRD
SQ  AQVVQLPVQDYTQTVNVVAWLYAAIFNRCNWFVQSDSCSLEEFNVWAMTNGFSSIKADLVLDALASMTGVTVEQVLAAIK
SQ  RLHSGFQGKQILGSCVLEDETPSDVYQQLAGVKLQSKRTRVIKGTCCWILASTFLFCSIISAFVKWTMFMYVTTHMLGVT
SQ  LCALCFVSFAMLLIKHKHLYLTMYIMPVLCTFYTNYLVVYKQSFRGLAYAWLSHFVPAVDYTYMDEVLYGVVLLVAMVFV
SQ  TMRSINHDVFSIMFLVGRLVSLVSMWYFGANLEEEVLLFLTSLFGTYTWTTMLSLATAKVIAKWLAVNVLYFTDVPQIKL
SQ  VLLSYLCIGYVCCCYWGILSLLNSIFRMPLGVYNYKISVQELRYMNANGLRPPRNSFEALMLNFKLLGIGGVPVIEVSQI
SQ  QSRLTDVKCANVVLLNCLQHLHIASNSKLWQYCSTLHNEILATSDLSMAFDKLAQLLVVLFANPAAVDSKCLASIEEVSD
SQ  DYVRDNTVLQALQSEFVNMASFVEYELAKKNLDEAKASGSANQQQIKQLEKACNIAKSAYERDRAVARKLERMADLALTN
SQ  MYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLTSNTLTIIVPDKQVFDQVVDNVYVTY
SQ  AGNVWHIQFIQDADGAVKQLNEIDVNSTWPLVIAANRHNEVSTVVLQNNELMPQKLRTQVVNSGSDMNCNTPTQCYYNTT
SQ  GTGKIVYAILSDCDGLKYTKIVKEDGNCVVLELDPPCKFSVQDVKGLKIKYLYFVKGCNTLARGWVVGTLSSTVRLQAGT
SQ  ATEYASNSAILSLCAFSVDPKKTYLDYIKQGGVPVTNCVKMLCDHAGTGMAITIKPEATTNQDSYGGASVCIYCRSRVEH
SQ  PDVDGLCKLRGKFVQVPLGIKDPVSYVLTHDVCQVCGFWRDGSCSCVGTGSQFQSKDTNFLNRIRGTSVNARLVPCASGL
SQ  DTDVQLRAFDICNANRAGIGLYYKVNCCRFQRVDEDGNKLDKFFVVKRTNLEVYNKEKECYELTKECGVVAEHEFFTFDV
SQ  EGSRVPHIVRKDLSKFTMLDLCYALRHFDRNDCSTLKEILLTYAECEESYFQKKDWYDFVENPDIINVYKKLGPIFNRAL
SQ  LNTAKFADALVEAGLVGVLTLDNQDLYGQWYDFGDFVKTVPGCGVAVADSYYSYMMPMLTMCHALDSELFVNGTYREFDL
SQ  VQYDFTDFKLELFTKYFKHWSMTYHPNTCECEDDRCIIHCANFNILFSMVLPKTCFGPLVRQIFVDGVPFVVSIGYHYKE
SQ  LGVVMNMDVDTHRYRLSLKDLLLYAADPALHVASASALLDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYEFILSKGLLK
SQ  EGSSVDLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVNKYFEIYEGGCIPATQVIVNNYDKSAGYPFNKFG
SQ  KARLYYEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIG
SQ  TTKFYGGWDDMLRRLIKDVDSPVLMGWDYPKCDRAMPNILRIVSSLVLARKHDSCCSHTDRFYRLANECAQVLSEIVMCG
SQ  GCYYVKPGGTSSGDATTAFANSVFNICQAVSANVCSLMACNGHKIEDLSIRELQKRLYSNVYRADHVDPAFVSEYYEFLN
SQ  KHFSMMILSDDGVVCYNSEFASKGYIANISAFQQVLYYQNNVFMSEAKCWVETDIEKGPHEFCSQHTMLVKMDGDEVYLP
SQ  YPDPSRILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENPEYQNVFRVYLEYIKKLYNDLGNQILDSYSVILSTC
SQ  DGQKFTDETFYKNMYLRSAVLQSVGACVVCSSQTSLRCGSCIRKPLLCCKCAYDHVMSTDHKYVLSVSPYVCNSPGCDVN
SQ  DVTKLYLGGMSYYCEDHKPQYSFKLVMNGMVFGLYKQSCTGSPYIEDFNKIASCKWTEVDDYVLANECTERLKLFAAETQ
SQ  KATEEAFKQCYASATIREIVSDRELILSWEIGKVRPPLNKNYVFTGYHFTNNGKTVLGEYVFDKSELTNGVYYRATTTYK
SQ  LSVGDVFILTSHAVSSLSAPTLVPQENYTSIRFASVYSVPETFQNNVPNYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYY
SQ  CTARVVYTAASHAAVDALCEKAHKFLNINDCTRIVPAKVRVDCYDKFKVNDTTRKYVFTTINALPELVTDIIVVDEVSML
SQ  TNYELSVINSRVRAKHYVYIGDPAQLPAPRVLLNKGTLEPRYFNSVTKLMCCLGPDIFLGTCYRCPKEIVDTVSALVYNN
SQ  KLKAKNDNSSMCFKVYYKGQTTHESSSAVNMQQIHLISKFLKANPSWSNAVFISPYNSQNYVAKRVLGLQTQTVDSAQGS
SQ  EYDFVIYSQTAETAHSVNVNRFNVAITRAKKGILCVMSSMQLFESLNFTTLTLDKINNPRLQCTTNLFKDCSRSYVGYHP
SQ  AHAPSFLAVDDKYKVGGDLAVCLNVADSAVTYSRLISLMGFKLDLTLDGYCKLFITRDEAIKRVRAWVGFDAEGAHAIRD
SQ  SIGTNFPLQLGFSTGIDFVVEATGMFAERDGYVFKKAAARAPPGEQFKHLIPLMSRGQKWDVVRIRIVQMLSDHLVDLAD
SQ  SVVLVTWAASFELTCLRYFAKVGREVVCSVCTKRATCFNSRTGYYGCWRHSYSCDYLYNPLIVDIQQWGYTGSLTSNHDP
SQ  ICSVHKGAHVASSDAIMTRCLAVHDCFCKSVNWNLEYPIISNEVSVNTSCRLLQRVMFRAAMLCNRYDVCYDIGNPKGLA
SQ  CVKGYDFKFYDASPVVKSVKQFVYKYEAHKDQFLDGLCMFWNCNVDKYPANAVVCRFDTRVLNKLNLPGCNGGSLYVNKH
SQ  AFHTSPFTRAAFENLKPMPFFYYSDTPCVYMEGMESKQVDYVPLRSATCITRCNLGGAVCLKHAEEYREYLESYNTATTA
SQ  GFTFWVYKTFDFYNLWNTFTRLQSLENVVYNLVNAGHFDGRAGELPCAVIGEKVIAKIQNEDVVVFKNNTPFPTNVAVEL
SQ  FAKRSIRPHPELKLFRNLNIDVCWSHVLWDYAKDSVFCSSTYKVCKYTDLQCIESLNVLFDGRDNGALEAFKKCRNGVYI
SQ  NTTKIKSLSMIKGPQRADLNGVVVEKVGDSDVEFWFAVRKDGDDVIFSRTGSLEPSHYRSPQGNPGGNRVGDLSGNEALA
SQ  RGTIFTQSRLLSSFTPRSEMEKDFMDLDDDVFIAKYSLQDYAFEHVVYGSFNQKIIGGLHLLIGLARRQQKSNLVIQEFV
SQ  TYDSSIHSYFITDENSGSSKSVCTVIDLLLDDFVDIVKSLNLKCVSKVVNVNVDFKDFQFMLWCNEEKVMTFYPRLQAAA
SQ  DWKPGYVMPVLYKYLESPLERVNLWNYGKPITLPTGCMMNVAKYTQLCQYLSTTTLAVPANMRVLHLGAGSDKGVAPGSA
SQ  VLRQWLPAGSILVDNDVNPFVSDSVASYYGNCITLPFDCQWDLIISDMYDPLTKNIGEYNVSKDGFFTYLCHLIRDKLAL
SQ  GGSVAIKITEFSWNAELYSLMGKFAFWTIFCTNVNASSSEGFLIGINWLNKTRTEIDGKTMHANYLFWRNSTMWNGGAYS
SQ  LFDMSKFPLKAAGTAVVSLKPDQINDLVLSLIEKGKLLVRDTRKEVFVGDSLVNVK
//
ID  P0C6Y0;
PN  2'-O-methyl transferase;
GN  rep;
OS  11144;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6Y0;
DR  UNIPROT: P19751;
DR  UNIPROT: P29982;
DR  UNIPROT: Q66194;
DR  UNIPROT: Q90045;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally- induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. 2'-O-methyltransferase: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7- methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-25758213; Score: 0.44
DE  Interaction: P0C6X7; IntAct: EBI-25758199; Score: 0.44
DE  Interaction: P0C6Y0; IntAct: EBI-25757578; Score: 0.44
DE  Interaction: P0C6Y5; IntAct: EBI-25758285; Score: 0.44
DE  Interaction: Q98VG9; IntAct: EBI-25758346; Score: 0.44
DE  Interaction: P0C6Y1; IntAct: EBI-25758438; Score: 0.44
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKMGKYGLGFKWAPEFPWMLPNASEKLGNPERSEEDGFCPSAAQEPKVKGKTLVNHVRVDCSRLPALECCVQSAIIRDI
SQ  FVDEDPQKVEASTMMALQFGSAVLVKPSKRLSVQAWAKLGVLPKTPAMGLFKRFCLCNTRECVCDAHVAFQLFTVQPDGV
SQ  CLGNGRFIGWFVPVTAIPEYAKQWLQPWSILLRKGGNKGSVTSGHFRRAVTMPVYDFNVEDACEEVHLNPRGKYSCKAYA
SQ  LLRGYRGVKPILFVDQYGCDYTGCLAKGLEDYGDLTLSEMKELSPVWRDSLDNEVVVAWHVDRDPRAVMRLQTLATVRSI
SQ  EYVGQPIEDMVDGDVVMREPAHLLAPNAIVKRLPRLVETMLYTDSSVTEFCYKTKLCDCGFITQFGYVDCCGDTCGFRGW
SQ  VPGNMMDGFPCPGCCKSYMPWELEAQSSGVIPEGGVLFTQSTDTVNRESFKLYGHAVVPFGGAAYWSPYPGMWLPVIWSS
SQ  VKSYSYLTYTGVVGCKAIVQETDAICRFLYMDYVQHKCGNLEQRAILGLDDVYHRQLLVNRGDYSLLLENVDLFVKRRAE
SQ  FACKFATCGDGLVPLLLDGLVPRSYYLIKSGQAFTSLMVNFSREVVDMCMDMALLFMHDVKVATKYVKKVTGKVAVRFKA
SQ  LGIAVVRKITEWFDLAVDTAASAAGWLCYQLVNGLFAVANGVITFIQEVPELVKNFVDKFKTFFKVLIDSMSVSILSGLT
SQ  VVKTASNRVCLAGSKVYEVVQKSLPAYIMPVGCSEATCLVGEIEPAVFEDDVVDVVKAPLTYQGCCKPPSSFEKICIVDK
SQ  LYMAKCGDQFYPVVVDNDTVGVLDQCWRFPCAGKKVVFNDKPKVKEVPSTRKIKIIFALDATFDSVLSKACSEFEVDKDV
SQ  TLDELLDVVLDAVESTLSPCKEHGVIGTKVCALLERLVDDYVYLFDEGGEEVIASRMYCSFSAPDEDCVATDVVYADENQ
SQ  DDDADDPVVLVADTQEEDGVAREQVDSADSEICVAHTGGQEMTEPDVVGSQTPIASAEETEVGEACDREGIAEVKATVCA
SQ  DALDACPDQVEAFDIEKVEDSILSELQTELNAPADKTYEDVLAFDAIYSETLSAFYAVPSDETHFKVCGFYSPAIERTNC
SQ  WLRSTLIVMQSLPLEFKDLGMQKLWLSYKAGYDQCFVDKLVKSAPKSIILPQGGYVADFAYFFLSQCSFKVHANWRCLKC
SQ  GMELKLQGLDAVFFYGDVVSHMCKCGNSMTLLSADIPYTFDFGVRDDKFCAFYTPRKVFRAACAVDVNDCHSMAVVDGKQ
SQ  IDGKVVTKFNGDKFDFMVGHGMTFSMSPFEIAQLYGSCITPNVCFVKGDVIKVLRRVGAEVIVNPANGRMAHGAGVAGAI
SQ  AKAAGKAFINETADMVKAQGVCQVGGCYESTGGKLCKKVLNIVGPDARGHGNECYSLLERAYQHINKCDNVVTTLISAGI
SQ  FSVPTDVSLTYLLGVVTKNVILVSNNQDDFDVIEKCQVTSVAGTKALSFQLAKNLCRDVKFVTNACSSLFSESSFVSSYD
SQ  VLQEVEALRHDIQLDDDARVFVQANMDCLPTDWRLVNKFDSVDGVRTIKYFECPGEVFVSSQGKKFGYVQNGSFKEASVS
SQ  QIRALLANKVDVLCTVDGVNFRSCCVAEGEVFGKTLGSVFCDGINVTKVRCSAIHKGKVFFQYSGLSAADLAAVKDAFGF
SQ  DEPQLLQYYSMLGMCKWPVVVCGNYFAFKQSNNNCYINVACLMLQHLSLKFPKWQWRRPGNEFRSGKPLRFVSLVLAKGS
SQ  FKFNEPSDSTDFIRVELREADLSGATCDLEFICKCGVKQEQRKGVDAVMHFGTLDKSGLVKGYNIACTCGDKLVHCTQFN
SQ  VPFLICSNTPEGKKLPDDVVAANIFTGGSVGHYTHVKCKPKYQLYDACNVSKVSEAKGNFTDCLYLKNLKQTFSSVLTTY
SQ  YLDDVKCVAYKPDLSQYYCESGKYYTKPIIKAQFRTFEKVEGVYTNFKLVGHDIAEKLNAKLGFDCNSPFMEYKITEWPT
SQ  ATGDVVLASDDLYVSRYSGGCVTFGKPVIWRGHEEASLKSLTYFNRPSVVCENKFNVLPVDVSEPTDRRPVPSAVLVTGA
SQ  ASGADASAISTEPGTAKEQKACASDSVEDQIVMEAQKKSSVTTVAVKEVKLNGVKKPVKWNCSVVVNDPTSETKVVKSLS
SQ  IVDVYDMFLTGCRYVVWTANELSRLINSPTVREYVKWGMSKLIIPANLLLLRDEKQEFVAPKVVKAKAIACYGAVKWFLL
SQ  YCFSWIKFNTDNKVIYTTEVASKLTFKLCCLAFKNALQTFNWSVVSRGFFLVATVFLLWFNFLYANVILSDFYLPNIGPL
SQ  PMFVGQIVAWVKTTFGVLTICDFYQVTDLGYRSSFCNGSMVCELCFSGFDMLDNYESINVVQHVVDRRVSFDYISLFKLV
SQ  VELVIGYSLYTVCFYPLFVLVGMQLLTTWLPEFFMLGTMHWSARLFVFVANMLPAFTLLRFYIVVTAMYKVYCLCRHVMY
SQ  GCSKPGCLFCYKRNRSVRVKCSTVVGGSLRYYDVMANGGTGFCTKHQWNCLNCNSWKPGNTFITHEAAADLSKELKRPVN
SQ  PTDSAYYSVIEVKQVGCSMRLFYERDGQRVYDDVSASLFVDMNGLLHSKVKGVPETHVVVVENEADKAGFLNAAVFYAQS
SQ  LYRPMLMVEKKLITTANTGLSVSRTMFDLYVYSLLRHLDVDRKSLTSFVNAAHNSLKEGVQLEQVMDTFVGCARRKCAID
SQ  SDVETKSITKSVMAAVNAGVEVTDESCNNLVPTYVKSDTIVAADLGVLIQNNAKHVQSNVAKAANVACIWSVDAFNQLSA
SQ  DLQHRLRKACVKTGLKIKLTYNKQEANVPILTTPFSLKGGAVFSRVLQWLFVANLICFIVLWALMPTYAVHKSDMQLPLY
SQ  ASFKVIDNGVLRDVSVTDACFANKFNQFDQWYESTFGLVYYRNSKACPVVVAVIDQDIGHTLFNVPTKVLRYGFHVLHFI
SQ  THAFATDRVQCYTPHMQIPYDNFYASGCVLSSLCTMLAHADGTPHPYCYTEGVMHNASLYSSLVPHVRYNLASSNGYIRF
SQ  PEVVSEGIVRVVRTRSMTYCRVGLCEEAEEGICFNFNSSWVLNNPYYRAMPGTFCGRNAFDLIHQVLGGLVQPIDFFALT
SQ  ASSVAGAILAIIVVLAFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQVYPTLSCLYACFYFYTTLYFPSEISVVM
SQ  HLQWLVMYGAIMPLWFCITYVAVVVSNHALWLFSYCRKIGTDVRSDGTFEEMALTTFMITKESYCKLKNSVSDVAFNRYL
SQ  SLYNKYRYFSGKMDTATYREAACSQLAKAMETFNHNNGNDVLYQPPTASVTTSFLQSGIVKMVSPTSKVEPCVVSVTYGN
SQ  MTLNGLWLDDKVYCPRHVICSSADMTDPDYPNLLCRVTSSDFCVMSDRMSLTVMSYQMQGSLLVLTVTLQNPNTPKYSFG
SQ  VVKPGETFTVLAAYNGRPQGAFHVVMRSSHTIKGSFLCGSCGSVGYVLTGDSVRFVYMHQLELSTGCHTGTDFSGNFYGP
SQ  YRDAQVVQLPVQDYTQTVNVVAWLYAAILNRCNWFVQSDSCSLEEFNVWAMTNGFSSIKADLVLDALASMTGVTVEQVLA
SQ  AIKRLHSGFQGKQILGSCVLEDELTPSDVYQQLAGVKLQSKRTRVIKGTCCWILASTFLFCSIISAFVKWTMFMYVTTHM
SQ  LGVTLCALCFVIFAMLLIKHKHLYLTMYIMPVLCTLFYTNYLVVGYKQSFRGLAYAWLSYFVPAVDYTYMDEVLYGVVLL
SQ  VAMVFVTMRSINHDVFSTMFLVGRLVSLVSMWYFGANLEEEVLLFLTSLFGTYTWTTMLSLATAKVIAKWLAVNVLYFTD
SQ  IPQIKLVLLSYLCIGYVCCCYWGVLSLLNSIFRMPLGVYNYKISVQELRYMNANGLRPPRNSFEALMLNFKLLGIGGVPV
SQ  IEVSQIQSRLTDVKCANVVLLNCLQHLHIASNSKLWQYCSTLHNEILATSDLSVAFDKLAQLLVVLFANPAAVDSKCLAS
SQ  IEEVSDDYVRDNTVLQALQSEFVNMASFVEYELAKKNLDEAKASGSANQQQIKQLEKACNIAKSAYERDRAVARKLERMA
SQ  DLALTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPPLTSNTLTIIVPDKQVFDQVVD
SQ  NVYVTYAPNVWHIQSIQDADGAVKQLNEIDVNSTWPLVISANRHNEVSTVVLQNNELMPQKLRTQVVNSGSDMNCNIPTQ
SQ  CYYNTTGTGKIVYAILSDCDGLKYTKIVKEDGNCVVLELDPPCKFSVQDVKGLKIKYLYFVKGCNTLARGWVVGTLSSTV
SQ  RLQAGTATEYASNSAILSLCAFSVDPKKTYLDYIQQGGVPVTNCVKMLCDHAGTGMAITIKPEATTNQDSYGGASVCIYC
SQ  RSRVEHPDVDGLCKLRGKFVQVPLGIKDPVSYVLTHDVCQVCGFWRDGSCSCVGTGSQFQSKDTNFLNRVRGTSVNARLV
SQ  PCASGLDTDVQLRAFDICNANRAGIGLYYKVNCFRFQRVDEEGNKLDKFFVVKRTNLEVYNKEKECYELTKDCGVVAEHE
SQ  FFTFDVEGSRVPHIVRKDLSKFTMLDLCYALRHFDRNDCSTLKEILLTYAECDESYFQKKDWYDFVENPDIINVYKKLGP
SQ  IFNRALLNTANFADTLVEAGLVGVLTLDNQDLYGQWYDFGDFVKTVPCCGVAVADSYYSYMMPMLTMCHALDSELFVNGT
SQ  YREFDLVQYDFTDFKLELFNKYFKHWSMTYHPNTSECEDDRCIIHCANFNILFSMVLPKTCFGPLVRQIFVDGVPFVVSI
SQ  GYHYKELGVVMNMDVDTHRYRLSLKDLLLYAADPALHVASASALLDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYEFIL
SQ  SKGLLKEGSSVDLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVVEVVNKYFEIYEGGCIPATQVIVNNYDKSAGY
SQ  PFNKFGKARLYYEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRG
SQ  VPVVIGTTKFYGGWDDMLRRLIKDVDSPVLMGWDYPKCDRAMPNILRIVSSLVLARKHDSCCSHTDRFYRLANECAQVLG
SQ  EIVMCGGCYYVKPGGTSSGDATTAFANSVFNICQAVSANVCSLMACNGHKIEDLSIRELQKRLYSNVYRADHVDPAFVSE
SQ  YYEFLNKHFSMIILSDDGVVCYNSEFASKGYIANISDFQQVLYYQNNVFMSEAKCWVETDIEKGPHEFCSQHTMLVKMDG
SQ  DEVYLPYPDPSRILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENPEYQNVFRVYLEYIKKLYNDLGNQILDSIS
SQ  VILSTCDGQKFTDETFYKNMYLRSAVMQSVGACVVCSSQTSLRCGSCIRKPLLCCKCAYDHVMSTDHKYVLSVSPYVCNS
SQ  PGCDVNDVTKLYLGGMSYYCEAHKPQYSFKLVMNGMVFGLYKQSCTGSPYIEDFNKIASCKWTEVDDYVLANECTERLKL
SQ  FAAETQKATEEAFKQCYASATIREIVSDRELILSWEIGKVRPPLNKNYVFTGYHFTNNGKTVLGEYVFDKSELTNGVYYR
SQ  ATTTYKLSVGDVFILTSHAVSSLSAPTLVPQENYTSVRFASAYSVPETFQNNVPNYQHIGIKRYCTVQGPPGTGKSHLAI
SQ  GHAVYYCTARVVYTAASHAAVDALCEKAHKFLNINDCARIVPAKLRVDCYDKFNVNDTTRKYVFTTINALPELVTDIIVV
SQ  DEVSMLTNYELSVINSRVRAKHYVYIGDPAQLPAPRVLLNKGTLEPRYFNSVTKLMCCLGPDIFLGTCYRCPKEIVDTVS
SQ  ALVYNNKLKAKNDNSAMCFKVYYKGQTTHESSSAVNMQQIHLISKLLKANPSWSNAVFISPYNSQNYVAKRVLGLQTQTA
SQ  DSAQGSAYDFVIYSQTAQTAHSVNVNRFNVAITRAKKGILCVMSSMQLIGVFNFTTLTLDKINNPRLQCTTNLFKDCSKS
SQ  YVGIPPCAFLLAVDDKYKVSGNLAVCLNVADSAVTYSRLISLMGFKLDLTLDGYCKLFITRDEAIKRVRAWVGFDAEGAH
SQ  ATRDSIGTNFPLQLGFSTGIDFVVEATGMFAERDGYVFKKAAARAPPGEQFKHLVPLMSRGQKWDVVRIRIVQMLSDHLV
SQ  DLADSVVLVTWAASFELTCLRYFAKVGKEVVCSVCNKRATCFNSRTGYYGCWRHSYSCDYLYNPLIVDIQQWGYTGSLTS
SQ  NHDPICSVHKGAHVASSDAIMTRCLAVHDCFCKSVNWNLEYPIISNEVSVNTSCRLLQRVMFRAAMLCNRYDVCYDIGNP
SQ  KGLACVKGYDFKFYDASPVVKSVKQFVYKYEAHKDQFLDGLCMFWNCNVDKYPANAVVCRFDTRVLSKLNLPGCNGGSLY
SQ  VNKHAFHTNPFTRAAFENLKPMPFFYYSDTPCVYMEGMESKQVDYVPLRSATCITRCNLGGAVCLKHAEEYREYLESYNT
SQ  ATTAGFTFWVYKTFDFYNLWNTFTRLQSLENVVYNLVNAGHFDGRAGELPCAVIGEKVIAKIQNEDVVVFKNNTPFPTNV
SQ  AVELFAERSIRPHPELKLFRSSNIHVCWNHVLWDYAKDSVFCSSTYKVCKYTDLQCIESLNVLFDGRDNGALEAFKKCRN
SQ  GVYINTTKIKSLSMIKGPQRADLNGVVVEKVGDSDVEFWFAMRRDGDDVIFSRTGSLEPSHYRSPQGNPGGNRVGDLSGN
SQ  EALARGTIFTQSRFLSSFSPRSEMEKDFMDLDEDVFIAKYSLQDYAFEHVVYGSFNQKIIGGLHLLIGLARRPKKSNLVI
SQ  QEFVPYDSSIHSYFITDENSGSSESVCTVIDLLLDDFVDIVKSLNLKCVSKVVNVNVDFKDFQFMLWCNEEKVMTFYPRL
SQ  QAAADWKPGYVMPVLYKYLESPMERVNLWNYGKPITLPTGCMMNVAKYTQLCQYLSTTTLAVPANMRVLHLGAGSDKGVA
SQ  PGSAVLRQWLPSGSILVDNDMNPFVSDSVASYYGNCITLPFDCQWDLIISDMYDPLTKNIGEYNVSKDGFFTYLCHLIRD
SQ  KLALGGSVAIKITEFSWNAELYSLMGKFAFWTIFCTNVNASSSEGFLIGINWLNRTRNEIDGKTMHANYLFWRNSTMWNG
SQ  GAYSLFDMTKFPLKAAGTAVVSLKPDQINDLVLSLIEKGKLLVRDTRKEVFVGDSLVNVK
//
ID  P0C6Y5;
PN  Putative 2'-O-methyl transferase;
GN  rep;
OS  11151;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6Y5;
DR  UNIPROT: Q88508;
DR  UNIPROT: Q9IW05;
DR  UNIPROT: Q9IW06;
DR  PDB: 1LVO;
DR  PDB: 1P9U;
DR  PDB: 2AMP;
DR  PDB: 6IVC;
DR  Pfam: PF13087;
DR  Pfam: PF16688;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000269|PubMed:21047955}. Non-structural protein 1 inhibits host translation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000269|PubMed:21047955}. The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SAGC]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. {ECO:0000269|PubMed:21047955}. The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G). {ECO:0000269|PubMed:21047955}. The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. {ECO:0000250}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-25758330; Score: 0.44
DE  Interaction: P0C6X7; IntAct: EBI-25758300; Score: 0.44
DE  Interaction: P0C6Y0; IntAct: EBI-25758285; Score: 0.44
DE  Interaction: P0C6Y1; IntAct: EBI-25758315; Score: 0.44
DE  Interaction: Q29099; IntAct: EBI-25684360; Score: 0.27
DE  Interaction: F2Z5F9; IntAct: EBI-25684386; Score: 0.27
DE  Interaction: P0C6Y5; IntAct: EBI-25757370; Score: 0.44
DE  Interaction: Q98VG9; IntAct: EBI-25758171; Score: 0.44
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSKQFKILVNEDYQVNVPSLPIRDVLQEIKYCYRNGFEGYVFVPEYCRDLVDCDRKDHYVIGVLGNGVSDLKPVLLTEP
SQ  SVMLQGFIVRANCNGVLEDFDLKIARTGRGAIYVDQYMCGADGKPVIEGDFKDYFGDEDIIEFEGEEYHCAWTTVRDEKP
SQ  LNQQTLFTIQEIQYNLDIPHKLPNCATRHVAPPVKKNSKIVLSEDYKKLYDIFGSPFMGNGDCLSKCFDTLHFIAATLRC
SQ  PCGSESSGVGDWTGFKTACCGLSGKVKGVTLGDIKPGDAVVTSMSAGKGVKFFANCVLQYAGDVEGVSIWKVIKTFTVDE
SQ  TVCTPGFEGELNDFIKPESKSLVACSVKRAFITGDIDDAVHDCIITGKLDLSTNLFGNVGLLFKKTPWFVQKCGALFVDA
SQ  WKVVEELCGSLTLTYKQIYEVVASLCTSAFTIVNYKPTFVVPDNRVKDLVDKCVKVLVKAFDVFTQIITIAGIEAKCFVL
SQ  GAKYLLFNNALVKLVSVKILGKKQKGLECAFFATSLVGATVNVTPKRTETATISLNKVDDVVAPGEGYIVIVGDMAFYKS
SQ  GEYYFMMSSPNFVLTNNVFKAVKVPSYDIVYDVDNDTKSKMIAKLGSSFEYDGDIDAAIVKVNELLIEFRQQSLCFRAFK
SQ  DDKSIFVEAYFKKYKMPACLAKHIGLWNIIKKDSCKRGFLNLFNHLNELEDIKETNIQAIKNILCPDPLLDLDYGAIWYN
SQ  CMPGCSDPSVLGSVQLLIGNGVKVVCDGCKGFANQLSKGYNKLCNAARNDIEIGGIPFSTFKTPTNTFIEMTDAIYSVIE
SQ  QGKALSFRDADVPVVDNGTISTADWSEPILLEPAEYVKPKNNGNVIVIAGYTFYKDEDEHFYPYGFGKIVQRMYNKMGGG
SQ  DKTVSFSEEVDVQEIAPVTRVKLEFEFDNEIVTGVLERAIGTRYKFTGTTWEEFEESISEELDAIFDTLANQGVELEGYF
SQ  IYDTCGGFDIKNPDGIMISQYDINITADEKSEVSASSEEEEVESVEEDPENEIVEASEGAEGTSSQEEVETVEVADITST
SQ  EEDVDIVEVSAKDDPWAAAVDVQEAEQFNPSLPPFKTTNLNGKIILKQGDNNCWINACCYQLQAFDFFNNEAWEKFKKGD
SQ  VMDFVNLCYAATTLARGHSGDAEYLLELMLNDYSTAKIVLAAKCGCGEKEIVLERAVFKLTPLKESFNYGVCGDCMQVNT
SQ  CRFLSVEGSGVFVHDILSKQTPEAMFVVKPVMHAVYTGTTQNGHYMVDDIEHGYCVDGMGIKPLKKRCYTSTLFINANVM
SQ  TRAEKPKQEFKVEKVEQQPIVEENKSSIEKEEIQSPKNDDLILPFYKAGKLSFYQGALDVLINFLEPDVIVNAANGDLKH
SQ  MGGVARAIDVFTGGKLTERSKDYLKKNKSIAPGNAVFFENVIEHLSVLNAVGPRNGDSRVEAKLCNVYKAIAKCEGKILT
SQ  PLISVGIFNVRLETSLQCLLKTVNDRGLNVFVYTDQERQTIENFFSCSIPVNVTEDNVNHERVSVSFDKTYGEQLKGTVV
SQ  IKDKDVTNQLPSAFDVGQKVIKAIDIDWQAHYGFRDAAAFSASSHDAYKFEVVTHSNFIVHKQTDNNCWINAICLALQRL
SQ  KPQWKFPGVRGLWNEFLERKTQGFVHMLYHISGVKKGEPGDAELMLHKLGDLMDNDCEIIVTHTTACDKCAKVEKFVGPV
SQ  VAAPLAIHGTDETCVHGVSVNVKVTQIKGTVAITSLIGPIIGEVLEATGYICYSGSNRNGHYTYYDNRNGLVVDAEKAYH
SQ  FNRDLLQVTTAIASNFVVKKPQAEERPKNCAFNKVAASPKIVQEQKLLAIESGANYALTEFGRYADMFFMAGDKILRLLL
SQ  EVFKYLLVLFMCLRSTKMPKVKVKPPLAFKDFGAKVRTLNYMRQLNKPSVWRYAKLVLLLIAIYNFFYLFVSIPVVHKLT
SQ  CNGAVQAYKNSSFIKSAVCGNSILCKACLASYDELADFQHLQVTWDFKSDPLWNRLVQLSYFAFLAVFGNNYVRCFLMYF
SQ  VSQYLNLWLSYFGYVEYSWFLHVVNFESISAEFVIVVIVVKAVLALKHIVFACSNPSCKTCSRTARQTRIPIQVVVNGSM
SQ  KTVYVHANGTGKFCKKHNFYCKNCDSYGFENTFICDEIVRDLSNSVKQTVYATDRSHQEVTKVECSDGFYRFYVGDEFTS
SQ  YDYDVKHKKYSSQEVLKSMLLLDDFIVYSPSGSALANVRNACVYFSQLIGKPIKIVNSDLLEDLSVDFKGALFNAKKNVI
SQ  KNSFNVDVSECKNLDECYRACNLNVSFSTFEMAVNNAHRFGILITDRSFNNFWPSKVKPGSSGVSAMDIGKCMTSDAKIV
SQ  NAKVLTQRGKSVVWLSQDFAALSSTAQKVLVKTFVEEGVNFSLTFNAVGSDDDLPYERFTESVSPKSGSGFFDVITQLKQ
SQ  IVILVFVFIFICGLCSVYSVATQSYIESAEGYDYMVIKNGIVQPFDDTISCVHNTYKGFGDWFKAKYGFIPTFGKSCPIV
SQ  VGTVFDLENMRPIPDVPAYVSIVGRSLVFAINAAFGVTNMCYDHTGNAVSKDSYFDTCVFNTACTTLTGLGGTIVYCAKQ
SQ  GLVEGAKLYSDLMPDYYYEHASGNMVKLPAIIRGLGLRFVKTQATTYCRVGECIDSKAGFCFGGDNWFVYDNEFGNGYIC
SQ  GNSVLGFFKNVFKLFNSNMSVVATSGAMLVNIIIACLAIAMCYGVLKFKKIFGDCTFLIVMIIVTLVVNNVSYFVTQNTF
SQ  FMIIYAIVYYFITRKLAYPGILDAGFIIAYINMAPWYVITAYILVFLYDSLPSLFKLKVSTNLFEGDKFVGNFESAAMGT
SQ  FVIDMRSYETIVNSTSIARIKSYANSFNKYKYYTGSMGEADYRMACYAHLGKALMDYSVNRTDMLYTPPTVSVNSTLQSG
SQ  LRKMAQPSGLVEPCIVRVSYGNNVLNGLWLGDEVICPRHVIASDTTRVINYENEMSSVRLHNFSVSKNNVFLGVVSARYK
SQ  GVNLVLKVNQVNPNTPEHKFKSIKAGESFNILACYEGCPGSVYGVNMRSQGTIKGSFIAGTCGSVGYVLENGILYFVYMH
SQ  HLELGNGSHVGSNFEGEMYGGYEDQPSMQLEGTNVMSSDNVVAFLYAALINGERWFVTNTSMSLESYNTWAKTNSFTELS
SQ  STDAFSMLAAKTGQSVEKLLDSIVRLNKGFGGRTILSYGSLCDEFTPTEVIRQMYGVNLQAGKVKSFFYPIMTAMTILFA
SQ  FWLEFFMYTPFTWINPTFVSIVLAVTTLISTVFVSGIKHKMLFFMSFVLPSVILVTAHNLFWDFSYYESLQSIVENTNTM
SQ  FLPVDMQGVMLTVFCFIVFVTYSVRFFTCKQSWFSLAVTTILVIFNMVKIFGTSDEPWTENQIAFCFVNMLTMIVSLTTK
SQ  DWMVVIASYRIAYYIVVCVMPSAFVSDFGFMKCISIVYMACGYLFCCYYGILYWVNRFTCMTCGVYQFTVSAAELKYMTA
SQ  NNLSAPKNAYDAMILSAKLIGVGGKRNIKISTVQSKLTEMKCTNVVLLGLLSKMHVESNSKEWNYCVGLHNEINLCDDPE
SQ  IVLEKLLALIAFFLSKHNTCDLSELIESYFENTTILQSVASAYAALPSWIALEKARADLEEAKKNDVSPQILKQLTKAFN
SQ  IAKSDFEREASVQKKLDKMAEQAAASMYKEARAVDRKSKIVSAMHSLLFGMLKKLDMSSVNTIIDQARNGVLPLSIIPAA
SQ  SATRLVVITPSLEVFSKIRQENNVHYAGAIWTIVEVKDANGSHVHLKEVTAANELNLTWPLSITCERTTKLQNNEIMPGK
SQ  LKERAVRASATLDGEAFGSGKALMASESGKSFMYAFIASDNNLKYVKWESNNDIIPIELEAPLRFYVDGANGPEVKYLYF
SQ  VKNLNTLRRGAVLGYIGATVRLQAGKPTEHPSNSSLLTLCAFSPDPAKAYVDAVKRGMQPVNNCVKMLSNGAGNGMAVTN
SQ  GVEANTQQDSYGGASVCIYCRCHVEHPAIDGLCRYKGKFVQIPTGTQDPIRFCIENEVCVVCGCWLNNGCMCDRTSMQSF
SQ  TVDQSYLNRVRGSSAARLEPCNGTDPDHVSRAFDIYNKDVACIGKFLKTNCSRFRNLDKHDAYYIVKRCTKTVMDHEQVC
SQ  YNDLKDSGAVAEHDFFTYKEGRCEFGNVARRNLTKYTMMDLCYAIRNFDEKNCEVLKEILVTVGACTEEFFENKDWFDPV
SQ  ENEAIHEVYAKLGPIVANAMLKCVAFCDAIVEKGYIGVITLDNQDLNGNFYDFGDFVKTAPGFGCACVTSYYSYMMPLMG
SQ  MTSCLESENFVKSDIYGSDYKQYDLLAYDFTEHKEYLFQKYFKYWDRTYHPNCSDCTSDECIIHCANFNTLFSMTIPMTA
SQ  FGPLVRKVHIDGVPVVVTAGYHFKQLGIVWNLDVKLDTMKLSMTDLLRFVTDPTLLVASSPALLDQRTVCFSIAALSTGI
SQ  TYQTVKPGHFNKDFYDFITERGFFEEGSELTLKHFFFAQGGEAAMTDFNYYRYNRVTVLDICQAQFVYKIVGKYFECYDG
SQ  GCINAREVVVTNYDKSAGYPLNKFGKARLYYETLSYEEQDALFALTKRNVLPTMTQMNLKYAISGKARARTVGGVSLLST
SQ  MTTRQYHQKHLKSIAATRNATVVIGSTKFYGGWDNMLKNLMRDVDNGCLMGWDYPKCDRALPNMIRMASAMILGSKHVGC
SQ  CTHNDRFYRLSNELAQVLTEVVHCTGGFYFKPGGTTSGDGTTAYANSAFNIFQAVSANVNKLLGVDSNACNNVTVKSIQR
SQ  KIYDNCYRSSSIDEEFVVEYFSYLRKHFSMMILSDDGVVCYNKDYADLGYVADINAFKATLYYQNNVFMSTSKCWVEPDL
SQ  SVGPHEFCSQHTLQIVGPDGDYYLPYPDPSRILSAGVFVDDIVKTDNVIMLERYVSLAIDAYPLTKHPKPAYQKVFYTLL
SQ  DWVKHLQKNLNAGVLDSFSVTMLEEGQDKFWSEEFYASLYEKSTVLQAAGMCVVCGSQTVLRCGDCLRRPLLCTKCAYDH
SQ  VMGTKHKFIMSITPYVCSFNGCNVNDVTKLFLGGLSYYCMNHKPQLSFPLCANGNVFGLYKSSAVGSEAVEDFNKLAVSD
SQ  WTNVEDYKLANNVKESLKIFAAETVKAKEESVKSEYAYAVLKEVIGPKEIVLQWEASKTKPPLNRNSVFTCFQISKDTKI
SQ  QLGEFVFEQSEYGSDSVYYKSTSTYKLTPGMIFVLTSHNVSPLKAPILVNQEKYNTISKLYPVFNIAEAYNTLVPYYQMI
SQ  GKQKFTTIQGPPGSGKSHCVIGLGLYYPQARIVYTACSHAAVDALCEKAAKNFNVDRCSRIIPQRIRVDCYTGFKPNNTN
SQ  AQYLFCTVNALPEASCDIVVVDEVSMCTNYDLSVINSRLSYKHIVYVGDPQQLPAPRTLINKGVLQPQDYNVVTKRMCTL
SQ  GPDVFLHKCYRCPAEIVKTVSALVYENKFVPVNPESKQCFKMFVKGQVQIESNSSINNKQLEVVKAFLAHNPKWRKAVFI
SQ  SPYNSQNYVARRLLGLQTQTVDSAQGSEYDYVIYTQTSDTQHATNVNRFNVAITRAKVGILCIMCDRTMYENLDFYELKD
SQ  SKIGLQAKPETCGLFKDCSKSEQYIPPAYATTYMSLSDNFKTSDGLAVNIGTKDVKYANVISYMGFRFEANIPGYHTLFC
SQ  TRDFAMRNVRAWLGFDVEGAHVCGDNVGTNVPLQLGFSNGVDFVVQTEGCVITEKGNSIEVVKARAPPGEQFAHLIPLMR
SQ  KGQPWHIVRRRIVQMVCDYFDGLSDILIFVLWAGGLELTTMRYFVKIGRPQKCECGKSATCYSSSQSVYACFKHALGCDY
SQ  LYNPYCIDIQQWGYTGSLSMNHHEVCNIHRNEHVASGDAIMTRCLAIHDCFVKRVDWSIVYPFIDNEEKINKAGRIVQSH
SQ  VMKAALKIFNPAAIHDVGNPKGIRCATTPIPWFCYDRDPINNNVRCLDYDYMVHGQMNGLMLFWNCNVDMYPEFSIVCRF
SQ  DTRTRSKLSLEGCNGGALYVNNHAFHTPAYDRRAFAKLKPMPFFYYDDSNCELVDGQPNYVPLKSNVCITKCNIGGAVCK
SQ  KHAALYRAYVEDYNIFMQAGFTIWCPQNFDTYMLWHGFVNSKALQSLENVAFNVVKKGAFTGLKGDLPTAVIADKIMVRD
SQ  GPTDKCIFTNKTSLPTNVAFELYAKRKLGLTPPLTILRNLGVVATYKFVLWDYEAERPFSNFTKQVCSYTDLDSEVVTCF
SQ  DNSIAGSFERFTTTRDAVLISNNAVKGLSAIKLQYGLLNDLPVSTVGNKPVTWYIYVRKNGEYVEQIDSYYTQGRTFETF
SQ  KPRSTMEEDFLSMDTTLFIQKYGLEDYGFEHVVFGDVSKTTIGGMHLLISQVRLAKMGLFSVQEFMNNSDSTLKSCCITY
SQ  ADDPSSKNVCTYMDILLDDFVTIIKSLDLNVVSKVVDVIVDCKAWRWMLWCENSHIKTFYPQLQSAEWNPGYSMPTLYKI
SQ  QRMCLERCNLYNYGAQVKLPDGITTNVVKYTQLCQYLNTTTLCVPHKMRVLHLGAAGASGVAPGSTVLRRWLPDDAILVD
SQ  NDLRDYVSDADFSVTGDCTSLYIEDKFDLLVSDLYDGSTKSIDGENTSKDGFFTYINGFIKEKLSLGGSVAIKITEFSWN
SQ  KDLYELIQRFEYWTVFCTSVNTSSSEGFLIGINYLGPYCDKAIVDGNIMHANYIFWRNSTIMALSHNSVLDTPKFKCRCN
SQ  NALIVNLKEKELNEMVIGLLRKGKLLIRNNGKLLNFGNHFVNTP
//
ID  Q98VG9;
PN  Putative 2'-O-methyl transferase;
GN  rep;
OS  33734;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: Q98VG9;
DR  UNIPROT: Q4U5G1;
DR  UNIPROT: Q4U5G2;
DR  UNIPROT: Q52PA4;
DR  PDB: 3ETI;
DR  PDB: 3EW5;
DR  PDB: 3GZF;
DR  PDB: 3JZT;
DR  PDB: 3UB0;
DR  PDB: 4ZRO;
DR  PDB: 5EU8;
DR  PDB: 6LP9;
DR  Pfam: PF13087;
DR  Pfam: PF16688;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity). {ECO:0000250}. The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. {ECO:0000250}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-25758376; Score: 0.44
DE  Interaction: P0C6X7; IntAct: EBI-25758361; Score: 0.44
DE  Interaction: P0C6Y0; IntAct: EBI-25758346; Score: 0.44
DE  Interaction: P0C6Y1; IntAct: EBI-25758391; Score: 0.44
DE  Interaction: P0C6Y5; IntAct: EBI-25758171; Score: 0.44
DE  Interaction: Q98VG9; IntAct: EBI-26365761; Score: 0.56
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSKQFKILVNEDYQVNVPSLPFRDALQEIKYCYRNGFDGYVFVPEYRRDLVDCNRKDHYVIGVLGNGISDLKPVLLTEP
SQ  SVMLQGFIVRANCNGVLEDFDLKFARTGNGAIYVDQYMCGADGKPVIEGEFKDYFGDEDVIIYEGEEYHCAWLTVRDEKP
SQ  LWQQTLLTIREIQYNLDIPHKLPNCAIREVAPPVKKNSKVVLSEEYRKLYDIFGSPFMGNGDSLNTCFDSLHFIAATLKC
SQ  PCGAESSGVGDWTGFKTACCGLHGKVKGVTLGAVKPGDAIVTSMSAGKGVKFFANSVLQYAGDVENVSVWKVIKTFTVNE
SQ  TVCTTDFEGELNDFIRPESTSPVSCSIKRAFITGEVDDAVHDCIIAGKLDLSTNLFGSANLLFKKMPWFVQKCGAIFADA
SQ  WKVVEELLCSLKLTYKQIYDVVASLCTSAFTIMDYKPVFVVSSNSVKDLVDKCVKILVKAFDVFTQTITIAGVEAKCFVL
SQ  GSKYLLFNNALVKLVSVKILGKRQKGLDSAFFATNLIGATVNVTPQRTESAYISLNKVDDVVTPGGGHIVIIGDMAFYKS
SQ  EEYYFMMASPDSVLVNNVFKAARVPSYNIVYDVNDDTKSKMVVKIGTSFDFDGDLDAAIAKVNDLLIEFRQEKLCFRALK
SQ  DGENILVEAYLKKYKMPVCLKNHVGLWDIIRQDSGKKGFLDTFNHLNELEDVKDIKIQTIKNIICPDLLLELDFGAIWYR
SQ  CMPACSDKSILGNVKIMLGNGVKVVCDGCHSFANRLTINYNKLCDTARKDIEIGGIPFSTFKTPSSSFIDMKDAIYSVVE
SQ  YGEALSFKTASVPVTNSGIITTDDWSDPILLEPADYVEPKDNGDVIVIAGYTFYKDEDDHFYPYGSGMVVQKMYNKMGGG
SQ  DKSVSFSDNVNVREIEPVTRVRLEFEFDNEVVTQVLEKVIGTKYKFIGTTWEEFEDSISEKLDKIFDTLAEQGVELEGYF
SQ  IYDTCGGFDINNPDGVMISQYDLNTAADDKSDSDASVEDISLISDNEDVEQIEEDNTSTDDAEDVSSVEGETVSVVDVED
SQ  FVEQVSLVEENNVLTPAVNPDEQLSSVEKKDEVSAKNDPWAAAVDEQEAEQPKPSLTPFKTTNLNGKIILKQQDNNCWIN
SQ  ACCYQLQAFDFFNHDLWDGFKKDDVMPFVDFCYAALTLKQGDSGDAEYLLETMLNDYSTAKVTLSAKCGCGVKEIVLERT
SQ  VFKLTPLRNEFKYGVCGDCKQINMCKFASVEGSGVFVHDRIEKQTPVSQFIVTPTMHAVYTGTTQSGHYMIEDCIHDYCV
SQ  DGMGIKPRKHKFYTSTLFLNANVMTAKSKTMVEPPVPVEDKCVEDCQSPKDLILPFYKAGKVSFYQGDLDVLINFLEPDV
SQ  LVNAANGDLRHVGGVARAIDVFTGGKLTKRSKEYLKSSKAIAPGNAVLFENVLEHLSVLNAVGPRNGDSRVEGKLCNVYK
SQ  AIAKCDGKILTPLISVGIFKVKLEVSLQCLLKTVTDRDLNVFVYTDQERVTIENFFNGTIPIKVTEDTVNQKRVSVALDK
SQ  TYGEQLKGTVVIKDKDVTNQLPSVSDVGEKVVKALDVDWNAYYGFPNAAAFSASSHDAYEFDVVTHNNFIVHKQTDNNCW
SQ  VNAICLALQRLKPTWKFPGVKSLWDAFLTRKTAGFVHMLYHISGLTKGQPGDAELTLHKLVDLMSSDSAVTVTHTTACDK
SQ  CAKVETFTGPVVAAPLLVCGTDEICVHGVHVNVKVTSIRGTVAITSLIGPVVGDVIDATGYICYTGLNSRGHYTYYDNRN
SQ  GLMVDADKAYHFEKNLLQVTTAIASNFVANTPKKEIMPKTQAKESKAKESNTARVFSEVEENPKNIVRKEKLLAIESGVD
SQ  YTITTLGKYADVFFMAGDKILRFLLEVFKYLLVVFMCLRKSKMPKVKVKPPHVFRNLGAKVRTLNYVRQLNKPALWRYIK
SQ  LVLLLIALYHFFYLFVSIPVVHKLACSGSVQAYSNSSFVKSEVCGNSILCKACLASYDELADFDHLQVSWDYKSDPLWNR
SQ  VIQLSYFIFLAVFGNNYVRCLLMYFVSQYLNLWLSYFGYVKYSWFLHVVNFESISVEFVIIVVVFKAVLALKHIFLPCNN
SQ  PSCKTCSKIARQTRIPIQVVVNGSMKTVYVHANGTGKLCKKHNFYCKNCDSYGFDHTFICDEIVRDLSNSIKQTVYATDR
SQ  SYQEVTKVECTDGFYRFYVGEEFTAYDYDVKHKKYSSQEVLKTMFLLDDFIVYNPSGSSLASVRNVCVYFSQLIGRPIKI
SQ  VNSELLEDLSVDFKGALFNAKKNVIKNSFNVDVSECKNLEECYKLCNLDVTFSTFEMAINNAHRFGILITDRSFNNFWPS
SQ  KIKPGSSGVSAMDIGKCMTFDAKIVNAKVLTQRGKSVVWLSQDFSTLSSTAQKVLVKTFVEEGVNFSLTFNAVGSDEDLP
SQ  YERFTESVSAKSGSGFFDVLKQLKQLFWCLVLFITLYGLCSVYSVATQSYIDSAEGYDYMVIKNGVVQSFDDSINCVHNT
SQ  YKGFAVWFKAKHGFVPTFDKSCPIVLGTVFDLGNMRPIPDVPAYVALVGRSLVFAINAAFGVTNVCYDHTGAAVSKNSYF
SQ  DTCVFNSACTTLTGIGGTVVYCAKQGLVEGAKLYSELLPDYYYEHASGNMVKIPAIIRSFGLRFVKTQATTYCRVGECTE
SQ  SQAGFCFGGDNWFVYDKEFGDGYICGSSTLGFFKNVFALFNSNMSVVATSGAMLANIVIACLAIAVCYGVLKFKKIFGDC
SQ  TLLVVMIIVTLVVNNVSYFVTQNTFFMIVYAIIYYFTTRKLAYPGVLDAGFIIAYLNMAPWYVLVLYIMVFLYDSLPSLF
SQ  KLKVTTNLFEGDKFVGSFESAAMGTFVIDMRSYETLVNSTSLDRIKSYANSFNKYKYYTGSMGEADYRMACYAHLGKALM
SQ  DYSVSRNDMLYTPPTVSVNSTLQSGLRKMAQPSGVVEPCIVRVAYGNNVLNGLWLGDEVICPRHVIASDTSRVINYENEL
SQ  SSVRLHNFSIAKNNAFLGVVSAKYKGVNLVLKVNQVNPNTPEHKFKSVRPGESFNILACYEGCPGSVYGVNMRSQGTIKG
SQ  SFIAGTCGSVGYVLENGTLYFVYMHHLELGNGSHVGSNLEGEMYGGYEDQPSMQLEGTNVMSSDNVVAFLYAALINGERW
SQ  FVTNTSMTLESYNAWAKTNSFTEIVSTDAFNMLAAKTGYSVEKLLECIVRLNKGFGGRTILSYGSLCDEFTPTEVIRQMY
SQ  GVNLQSGKVKSIFYPMMTAIAILFAFWLEFFMYTPFTWINPTFVSVVLAITTLVSVLLVAGIKHKMLFFMSFVMPSVILA
SQ  TAHNVVWDMTYYESLQVLVENVNTTFLPVDMQGVMLALFCVVVFVICTIRFFTCKQSWFSLFATTIFVMFNIVKLLGMIG
SQ  EPWTDDHFLLCLVNMLTMLISLTTKDWFVVFASYKVAYYIVVYVMQPAFVQDFGFVKCVSIIYMACGYLFCCYYGILYWV
SQ  NRFTCMTCGVYQFTVSPAELKYMTANNLSAPKTAYDAMILSFKLMGIGGGRNIKISTVQSKLTEMKCTNVVLLGLLSKMH
SQ  VESNSKEWNYCVGLHNEINLCDDPDAVLEKLLALIAFFLSKHNTCDLSDLIESYFENTTILQSVASAYAALPSWIAYEKA
SQ  RADLEEAKKNDVSPQLLKQLTKACNIAKSEFEREASVQKKLDKMAEQAAASMYKEARAVDRKSKIVSAMHSLLFGMLKKL
SQ  DMSSVNTIIEQARNGVLPLSIIPAASATRLIVVTPNLEVLSKVRQENNVHYAGAIWSIVEVKDANGAQVHLKEVTAANEL
SQ  NITWPLSITCERTTKLQNNEILPGKLKEKAVKASATIDGDAYGSGKALMASEGGKSFIYAFIASDSNLKYVKWESNNDVI
SQ  PIELEAPLRFYVDGVNGPEVKYLYFVKSLNTLRRGAVLGYIGATVRLQAGKPTEHPSNSGLLTLCAFAPDPAKAYVDAVK
SQ  RGMQPVTNCVKMLSNGAGNGMAITNGVESNTQQDSYGGASVCIYCRCHVEHPAIDGLCRFKGKFVQVPTGTQDPIRFCIE
SQ  NEVCVVCGCWLTNGCMCDRTSIQGTTIDQSYLNECGVLVQLDLEPCNGTDPDHVSRAFDIYNKDVACIGKFLKTNCSRFR
SQ  NLDKHDAYYVVKRCTKSVMDHEQVCYNDLKDSGVVAEHDFFLYKEGRCEFGNVARKDLTKYTMMDLCYAIRNFDEKNCEV
SQ  LKEILVTLGACNESFFENKDWFDPVENEAIHEVYARLGPIVANAMLKCVAFCDAIVEKGYIGIITLDNQDLNGNFYDFGD
SQ  FVKTTPGFGCACVTSYYSYMMPLMGMTSCLESENFVKSDIYGADYKQYDLLAYDFTDHKEKLFHKYFKHWDRTYHPNCSD
SQ  CTSDECIIHCANFNTLFSMTIPSTAFGPLVRKVHIDGVPVVVTAGYHFKQLGIVWNLDVKLDTMKLSMTDLLRFVTDPTL
SQ  LVASSPALLDQRTVCFSIAALSTGVTYQTVKPGHFNKDFYDFITERGFFEEGSELTLKHFFFAQGGEAAMTDFNYYRYNR
SQ  VTVLDICQAQFVYKIVGKYFECYDGGCINAREVVVTNYDKSAGYPLNKFGKARLYYETLSYEEQDALFALTKRNVLPTMT
SQ  QMNLKYAISGKARARTVGGVSLLSTMTTRQYHQKHLKSIAATRNATVVIGSTKFYGGWDNMLKNLMRDVDNGCLMGWDYP
SQ  KCDRALPNMIRMASAMILGSKHVGCCTHSDRFYRLSNELAQVLTEVVHCTGGFYFKPGGTTSGDGTTAYANSAFNIFQAV
SQ  SANVNKLLGVDSNACNNVTVKSIQRKIYDNCYRSSSIDEEFVVEYFSYLRKHFSMMILSDDGVVCYNKDYADLGYVADIN
SQ  AFKATLYYQNNVFMSTSKCWVEPDLSVGPHEFCSQHTLQIVGPDGDYYLPYPDPSRILSAGVFVDDIVKTDNVIMLERYV
SQ  SLAIDAYPLTKHPKPAYQKVFYTLLDWVKHLQKNLNAGVLDSFSVTMLEEGQDKFWSEEFYASLYEKSTVLQAAGMCVVC
SQ  GSQTVLRCGDCLRRPLLCTKCAYDHVMGTKHKFIMSITPYVCSFNGCNVNDVTKLFLGGLSYYCMDHKPQLSFPLCANGN
SQ  VFGLYKSSAVGSEDVEDFNKLAVSDWTNVEDYKLANNVKESLKIFAAETVKAKEESVKSEYAYAILKEVIGPKEIVLQWE
SQ  ASKTKPPLNRNSVFTCFQISKDTKIQLGEFVFEQSEYGSDSVYYKSTSTYKLTPGMIFVLTSHNVSPLKATILVNQEKYN
SQ  TISKLYPVFNIAEAYNTLVPYYQMIGKQKFTTIQGPPGSGKSHCVIGLGLYYPQARIVYTACSHAAVDALCEKAAKNFNV
SQ  DRCSRIIPQRIRVDCYTGFKPNNTNAQYLFCTVNALPEASCDIVVVDEVSMCTNYDLSVINSRLSYKHIVYVGDPQQLPA
SQ  PRTLINKGVLQPQDYNVVTQRVCTLGPDVFLHKCYRCPAEIVKTVSALVYENKFVPVNPESKQCFKMFVKGQVQIESNSS
SQ  INNKQLEVVKAFLAHNPKWRKAVFISPYNSQNYVARRLLGLQTQTVDSAQGSEYDYVIYTQTSDTQHATNVNRFNVAITR
SQ  AKVGILCIMCDRTMYENLDFYELKDSKIGLQAKPETCGLFKDCSKSEQYIPPAYATTYMSLSDNFKTSDGLAVNIGTKDV
SQ  KYANVISYMGFRFEANIPGYHTLFCTRDFAMRNVRAWLGFDVEGAHVCGDNVGTNVPLQLGFSNGVDFVVQTEGCVVTEK
SQ  GNSIEVVKARAPPGEQFAHLIPLMRKGQPWHIVRRRIVQMVCDYFDGLSDILIFVLWAGGLELTTMRYFVKIGRPQKCEC
SQ  GKSATCYSSSQCVYACFKHALGCDYLYNPYCIDIQQWGYTGSLSMNHHEVCNIHRNEHVASGDAIMTRCLAIHDCFVKRV
SQ  DWSIVYPFIDNEEKINKAGRIVQSHVMKAALKIFNPAAIHDVGNPKGIRCATTPIPWFCYDRDPINNNVRCLEYDYMVHG
SQ  QMNGLMLFWNCNVDMYPEFSIVCRFDTRTRSKLSLEGCNGGALYVNNHAFHTPAYDRRAFAKLKPMPFFYYDDSNCELVD
SQ  GQPNYVPLKSNVCITKCNIGGAVCKKHAALYRAYVEDYNMFMQAGFTIWCPQNFDTYMLWHGFVNSKALQSLENVAFNVV
SQ  KKGAFTGLKGDLPTAVIADKIMVRDGPTDKCIFTNKTSLPTNVAFELYAKRKLGLTPPLTILRNLGVVATYKFVLWDYEA
SQ  ECPFSNFTKQVCSYTDLDSEVVTCFDNSIAGSFERFTTTKDAVLISNNAVKGLSAIKLQYGFLNDLPVSTVGNKPVTWYI
SQ  YVRKNGEYVEQIDSYYTHGRTFETFKPRSTMEEDFLSMDTTLFIQKYGLEDYGFEHVVFGDVSKTTIGGMHLLISQVRLA
SQ  KMGLFSVQEFMTNSDSTLKSCCITYADDPSSKNVCTYMDILLDDFVTIIKSLDLNVVSKVVDVIVDCKAWRWMLWCENSQ
SQ  IKTFYPQLQSAEWNPGYSMPTLYKIQRMCLERCNLYNYGAQVRLPDGITTNVVKYTQLCQYLNTTTVCVPHKMRVLHLGA
SQ  AGASGVAPGSTVLRRWLPDDAILVDNDLRDYVSDADFSVTGDCTSLYIEDKFDLLISDLYDGSTKSIDGENTSKDGFFTY
SQ  INGFIKEKLSLGGSAAIKITEFSWNKDLYELIQRFEYWTVFCTSVNTSSSEGFLIGINYLGPYCDKAIVDGNIMHANYIF
SQ  WRNSTIMALSHNSVLDTPKFKCRCNNALIVNLKEKELNEMVVGLLRKGKLLIRNNGKLLNFGNHLVNVP
//
ID  P0C6Y1;
PN  2'-O-methyl transferase;
GN  rep;
OS  11122;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 4]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 6]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. [Proofreading exoribonuclease]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. [Uridylate-specific endoribonuclease]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}.
DR  UNIPROT: P0C6Y1;
DR  UNIPROT: P26314;
DR  UNIPROT: P27920;
DR  UNIPROT: Q4ZJT1;
DR  UNIPROT: Q4ZJT2;
DR  PDB: 3EJF;
DR  PDB: 3EKE;
DR  PDB: 4X2Z;
DR  PDB: 5BZ0;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF17896;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51961;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: [Isoform Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (By similarity). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like protease]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:25609249). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:25609249}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (By similarity). Alone is able to induce paired membranes (By similarity). Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (By similarity). {ECO:0000250|UniProtKB:P0C6Y3}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. {ECO:0000255|PROSITE-ProRule:PRU00772}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities (By similarity). Therefore plays an essential role in viral mRNAs cap methylation (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Proofreading exoribonuclease]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity (By similarity). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs (By similarity). Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyl transferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-25758616; Score: 0.44
DE  Interaction: P0C6X7; IntAct: EBI-25758560; Score: 0.44
DE  Interaction: P0C6Y0; IntAct: EBI-25758438; Score: 0.44
DE  Interaction: P0C6Y1; IntAct: EBI-25757817; Score: 0.44
DE  Interaction: P0C6Y5; IntAct: EBI-25758315; Score: 0.44
DE  Interaction: Q98VG9; IntAct: EBI-25758391; Score: 0.44
DE  Interaction: Q92499; IntAct: EBI-25826987; Score: 0.54
GO  GO:0044167;
GO  GO:0044172;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASSLKQGVSPKPRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRSLQTGKQFKFETVCGLFLLKGVDKIT
SQ  PGVPAKVLKATSKLADLEDIFGVSPLARKYRELLKTACQWSLTVEALDVRAQTLDEIFDPTEILWLQVAAKIHVSSMAMR
SQ  RLVGEVTAKVMDALGSNLSALFQIVKQQIARIFQKALAIFENVNELPQRIAALKMAFAKCARSITVVVVERTLVVKEFAG
SQ  TCLASINGAVAKFFEELPNGFMGSKIFTTLAFFKEAAVRVVENIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK
SQ  ADIPVEPEGWSAILDGHLCYVFRSGDRFYAAPLSGNFALSDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVSELVTA
SQ  LKKGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLRLFQSARVIAEDVWSSFTEKSFEFWKLAYGKVRNLEEFVKTYVC
SQ  KAQMSIVILAAVLGEDIWHLVSQVIYKLGVLFTKVVDFCDKHWKGFCVQLKRAKLIVTETFCVLKGVAQHCFQLLLDAIH
SQ  SLYKSFKKCALGRIHGDLLFWKGGVHKIVQDGDEIWFDAIDSVDVEDLGVVQEKSIDFEVCDDVTLPENQPGHMVQIEDD
SQ  GKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVPIKVSIECCGEPWNTIFKKAYKEPIEV
SQ  DTDLTVEQLLSVIYEKMCDDLKLFPEAPEPPPFENVALVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGEA
SQ  EECDTNSECEEEDEDTKVLALIQDPASIKYPLPLDEDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKPLPQKV
SQ  VDVLGDWGEAVDAQEQLCQQEPLQHTFEEPVENSTGSSKTMTEQVVVEDQELPVVEQDQDVVVYTPTDLEVAKETAEEVD
SQ  EFILIFAVPKEEVVSQKDGAQIKQEPIQVVKPQREKKAKKFKVKPATCEKPKFLEYKTCVGDLTVVIAKALDEFKEFCIV
SQ  NAANEHMTHGSGVAKAIADFCGLDFVEYCEDYVKKHGPQQRLVTPSFVKGIQCVNNVVGPRHGDNNLHEKLVAAYKNVLV
SQ  DGVVNYVVPVLSLGIFGVDFKMSIDAMREAFEGCTIRVLLFSLSQEHIDYFDVTCKQKTIYLTEDGVKYRSIVLKPGDSL
SQ  GQFGQVYAKNKIVFTADDVEDKEILYVPTTDKSILEYYGLDAQKYVIYLQTLAQKWNVQYRDNFLILEWRDGNCWISSAI
SQ  VLLQAAKIRFKGFLTEAWAKLLGGDPTDFVAWCYASCTAKVGDFSDANWLLANLAEHFDADYTNAFLKKRVSCNCGIKSY
SQ  ELRGLEACIQPVRATNLLHFKTQYSNCPTCGANNTDEVIEASLPYLLLFATDGPATVDCDEDAVGTVVFVGSTNSGHCYT
SQ  QAAGQAFDNLAKDRKFGKKSPYITAMYTRFAFKNETSLPVAKQSKGKSKSVKEDVSNLATSSKASFDNLTDFEQWYDSNI
SQ  YESLKVQESPDNFDKYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFIYKLTPDTDENSKAPVYYPVLDAISLKAIWVE
SQ  GNANFVVGHPNYYSKSLHIPTFWENAENFVKMGDKIGGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKLIG
SQ  KAATFIADKVGGGVVRNITDSIKGLCGITRGHFERKMSPQFLKTLMFFLFYFLKASVKSVVASYKTVLCKVVLATLLIVW
SQ  FVYTSNPVMFTGIRVLDFLFEGSLCGPYKDYGKDSFDVLRYCADDFICRVCLHDKDSLHLYKHAYSVEQVYKDAASGFIF
SQ  NWNWLYLVFLILFVKPVAGFVIICYCVKYLVLNSTVLQTGVCFLDWFVQTVFSHFNFMGAGFYFWLFYKIYIQVHHILYC
SQ  KDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVKPT
SQ  AYAYHVVDEACLVDDFVNLKYKAATPGKDSASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEAKN
SQ  AAIYYAQYLCKPILILDQALYEQLVVEPVSKSVIDKVCSILSSIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIFCH
SQ  NHDVDYTGDGFTNVIPSYGIDTGKLTPRDRGFLINADASIANLRVKNAPPVVWKFSELIKLSDSCLKYLISATVKSGVRF
SQ  FITKSGAKQVIACHTQKLLVEKKAGGIVSGTFKCFKSYFKWLLIFYILFTACCSGYYYMEVSKSFVHPMYDVNSTLHVEG
SQ  FKVIDKGVLREIVPEDTCFSNKFVNFDAFWGRPYDNSRNCPIVTAVIDGDGTVATGVPGFVSWVMDGVMFIHMTQTERKP
SQ  WYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVRLI
SQ  VPQQILHTPYVVKFVSDSYCRGSVCEYTRPGYCVSLNPQWVLFNDEYTSKPGVFCGSTVRELMFSMVSTFFTGVNPNIYM
SQ  QLATMFLILVVVVLIFAMVIKFQGVFKAYATTVFITMLVWVINAFILCVHSYNSVLAVILLVLYCYASLVTSRNTVIIMH
SQ  CWLVFTFGLIVPTWLACCYLGFIIYMYTPLFLWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGSEFVKLTNEIGDKF
SQ  EAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEIVYTPPRYSIGVSRLQSGFKKLVSPSSAVEKCIVSVS
SQ  YRGNNLNGLWLGDTIYCPRHVLGKFSGDQWNDVLNLANNHEFEVTTQHGVTLNVVSRRLKGAVLILQTAVANAETPKYKF
SQ  IKANCGDSFTIACAYGGTVVGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEFYG
SQ  GYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSLPKWLESTTVSVDDYNKWAGDNGFTPFSTSTAITKLSAITGV
SQ  DVCKLLRTIMVKNSQWGGDPILGQYNFEDELTPESVFNQIGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTAVP
SQ  LKFYVYAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPWMF
SQ  LPLVLYTAFKCVQGCYMNSFNTSLLMLYQFVKLGFVIYTSSNTLTAYTEGNWELFFELVHTTVLANVSSNSLIGLFVFKC
SQ  AKWMLYYCNATYLNNYVLMAVMVNCIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKINPPKTVWEVFST
SQ  NILIQGIGGDRVLPIATVQAKLSDVKCTTVVLMQLLTKLNVEANSKMHVYLVELHNKILASDDVGECMDNLLGMLITLFC
SQ  IDSTIDLSEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKNLYEKVLVDSKNGGVTQQELAAYRKAANIAKSVFDRDLA
SQ  VQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQASSGVVPLATVPIVCSNKLTLVIPD
SQ  PETWVKCVEGVHVTYSTVVWNIDTVIDADGTELHPTSTGSGLTYCISGANIAWPLKVNLTRNGHNKVDVVLQNNELMPHG
SQ  VKTKACVAGVDQAHCSVESKCYYTNISGNSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGVKVEVVYLYF
SQ  IKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFAIT
SQ  SKPSPTPDQDSYGGASVCLYCRAHIAHPGSVGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCDSL
SQ  RQPKSSVQSVAGASDFDKNYLNRVRGSSEARLIPLASGCDPDVVKRAFDVCNKESAGMFQNLKRNCARFQELRDTEDGNL
SQ  EYLDSYFVVKQTTPSNYEHEKSCYEDLKSEVTADHDFFVFNKNIYNISRQRLTKYTMMDFCYALRHFDPKDCEVLKEILV
SQ  TYGCIEDYHPKWFEENKDWYDPIENSKYYVMLAKMGPIVRRALLNAIEFGNLMVEKGYVGVITLDNQDLNGKFYDFGDFQ
SQ  KTAPGAGVPVFDTYYSYMMPIIAMTDALAPERYFEYDVHKGYKSYDLLKYDYTEEKQELFQKYFKYWDQEYHPNCRDCSD
SQ  DRCLIHCANFNILFSTLIPQTSFGNLCRKVFVDGVPFIATCGYHSKELGVIMNQDNTMSFSKMGLSQLMQFVGDPALLVG
SQ  TSNNLVDLRTSCFSVCALTSGITHQTVKPGHFNKDFYDFAEKAGMFKEGSSIPLKHFFYPQTGNAAINDYDYYRYNRPTM
SQ  FDICQLLFCLEVTSKYFECYEGGCIPASQVVVNNLDKSAGYPFNKFGKARLYYEMSLEEQDQLFEITKKNVLPTITQMNL
SQ  KYAISAKNRARTVAGVSILSTMTNRQFHQKILKSIVNTRNASVVIGTTKFYGGWDNMLRNLIQGVEDPILMGWDYPKCDR
SQ  AMPNLLRIAASLVLARKHTNCCSWSERIYRLYNECAQVLSETVLATGGIYVKPGGTSSGDATTAYANSVFNIIQATSANV
SQ  ARLLSVITRDIVYDNIKSLQYELYQQVYRRVNFDPAFVEKFYSYLCKNFSLMILSDDGVVCYNNTLAKQGLVADISGFRE
SQ  VLYYQNNVFMADSKCWVEPDLEKGPHEFCSQHTMLVEVDGEPKYLPYPDPSRILGACVFVDDVDKTEPVAVMERYIALAI
SQ  DAYPLVHHENEEYKKVFFVLLAYIRKLYQELSQNMLMDYSFVMDIDKGSKFWEQEFYENMYRAPTTLQSCGVCVVCNSQT
SQ  ILRCGNCIRKPFLCCKCCYDHVMHTDHKNVLSINPYICSQLGCGEADVTKLYLGGMSYFCGNHKPKLSIPLVSNGTVFGI
SQ  YRANCAGSENVDDFNQLATTNWSIVEPYILANRCSDSLRRFAAETVKATEELHKQQFASAEVREVFSDRELILSWEPGKT
SQ  RPPLNRNYVFTGYHFTRTSKVQLGDFTFEKGEGKDVVYYKATSTAKLSVGDIFVLTSHNVVSLVAPTLCPQQTFSRFVNL
SQ  RPNVMVPECFVNNIPLYHLVGKQKRTTVQGPPGSGKSHFAIGLAVYFSSARVVFTACSHAAVDALCEKAFKFLKVDDCTR
SQ  IVPQRTTVDCFSKFKANDTGKKYIFSTINALPEVSCDILLVDEVSMLTNYELSFINGKINYQYVVYVGDPAQLPAPRTLL
SQ  NGSLSPKDYNVVTNLMVCVKPDIFLAKCYRCPKEIVDTVSTLVYDGKFIANNPESRECFKVIVNNGNSDVGHESGSAYNT
SQ  TQLEFVKDFVCRNKQWREAIFISPYNAMNQRAYRMLGLNVQTVDSSQGSEYDYVIFCVTADSQHALNINRFNVALTRAKR
SQ  GILVVMRQRDELYSALKFTELDSETSLQGTGLFKICNKEFSGVHPAYAVTTKALAATYKVNDELAALVNVEAGSEITYKH
SQ  LISLLGFKMSVNVEGCHNMFITRDEAIRNVRGWVGFDVEATHACGTNIGTNLPFQVGFSTGADFVVTPEGLVDTSIGNNF
SQ  EPVNSKAPPGEQFNHLRVLFKSAKPWHVIRPRIVQMLADNLCNVSDCVVFVTWCHGLELTTLRYFVKIGKEQVCSCGSRA
SQ  TTFNSHTQAYACWKHCLGFDFVYNPLLVDIQQWGYSGNLQFNHDLHCNVHGHAHVASVDAIMTRCLAINNAFCQDVNWDL
SQ  TYPHIANEDEVNSSCRYLQRMYLNACVDALKVNVVYDIGNPKGIKCVRRGDVNFRFYDKNPIVRNVKQFEYDYNQHKDKF
SQ  ADGLCMFWNCNVDCYPDNSLVCRYDTRNLSVFNLPGCNGGSLYVNKHAFYTPKFDRISFRNLKAMPFFFYDSSPCETIQV
SQ  DGVAQDLVSLATKDCITKCNIGGAVCKKHAQMYAEFVTSYNAAVTAGFTFWVTNKLNPYNLWKSFSALQSIDNIAYNMYK
SQ  GGHYDAIAGEMPTVITGDKVFVIDQGVEKAVFVNQTTLPTSVAFELYAKRNIRTLPNNRILKGLGVDVTNGFVIWDYANQ
SQ  TPLYRNTVKVCAYTDIEPNGLVVLYDDRYGDYQSFLAADNAVLVSTQCYKRYSYVEIPSNLLVQNGMPLKDGANLYVYKR
SQ  VNGAFVTLPNTINTQGRSYETFEPRSDIERDFLAMSEESFVERYGKDLGLQHILYGEVDKPQLGGLHTVIGMYRLLRANK
SQ  LNAKSVTNSDSDVMQNYFVLSDNGSYKQVCTVVDLLLDDFLELLRNILKEYGTNKSKVVTVSIDYHSINFMTWFEDGSIK
SQ  TCYPQLQSAWTCGYNMPELYKVQNCVMEPCNIPNYGVGITLPSGILMNVAKYTQLCQYLSKTTICVPHNMRVMHFGAGSD
SQ  KGVAPGSTVLKQWLPEGTLLVDNDIVDYVSDAHVSVLSDCNKYNTEHKFDLVISDMYTDNDSKRKHEGVIANNGNDDVFI
SQ  YLSSFLRNNLALGGSFAVKVTETSWHEVLYDIAQDCAWWTMFCTAVNASSSEAFLIGVNYLGASEKVKVSGKTLHANYIF
SQ  WRNCNYLQTSAYSIFDVAKFDLRLKATPVVNLKTEQKTDLVFNLIKCGKLLVRDVGNTSFTSDSFVCTM
//
ID  P0C6Y2;
PN  2'-O-methyl transferase;
GN  rep;
OS  160235;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 4]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles (By similarity). Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER) (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 6]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. [Proofreading exoribonuclease]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. [Uridylate-specific endoribonuclease]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}.
DR  UNIPROT: P0C6Y2;
DR  UNIPROT: Q91QT2;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF17896;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51961;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: [Isoform Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (By similarity). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like protease]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (By similarity). Alone is able to induce paired membranes (By similarity). Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (By similarity). {ECO:0000250|UniProtKB:P0C6Y3}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. {ECO:0000255|PROSITE-ProRule:PRU00772}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities (By similarity). Therefore plays an essential role in viral mRNAs cap methylation (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Proofreading exoribonuclease]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity (By similarity). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs (By similarity). Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyl transferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044172;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASSLKQGVSPKPRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRSLQTGKQFKFETVCGLFLLKGVDKIT
SQ  PGVPAKVLKATSKLADLEDIFGVSPLARKYRELLKTACQWSLTVEALDVRAQTLDEIFDPTEILWLQVAAKIHVSSMAMR
SQ  RLVGEVTAKVMDALGSNLSALFQIVKQQIARIFQKALAIFENVNELPQRIAALKMAFAKCARSITVVVVERTLVVKEFAG
SQ  TCLASINGAVAKFFEELPNGFMGSKIFTTLAFFKEAAVRVVENIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK
SQ  ADIPVEPEGWSAILDGHLCYVFRSGDRFYAAPLSGNFALSDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVSELVTA
SQ  LKKGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLRLFQSARVIAEDVWSSFTEKSFEFWKLAYGKVRNLEEFVKTYVC
SQ  KAQMSIVILAAVLGEDIWHLVSQVIYKLGVLFTKVVDFCDKHWKGFCVQLKRAKLIVTETFCVLKGVAQHCFQLLLDAIH
SQ  SLYKSFKKCALGRIHGDLLFWKGGVHKIVQDGDEIWFDAIDSVDVEDLGVVQEKSIDFEVCDDVTLPENQPGHMVQIEDD
SQ  GKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVPIKVSIECCGEPWNTIFKKAYKEPIEV
SQ  DTDLTVEQLLSVIYEKMCDDLKLFPEAPEPPPFENVALVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGEA
SQ  EECDTNSECEEEDEDTKVLALIQDPASIKYPLPLDEDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKPLPQKV
SQ  VDVLGDWGEAVDAQEQLCQQEPLQHTFEEPVENSTGSSKTMTEQVVVEDQELPVVEQDQDVVVYTPTDLEVAKETAEEVD
SQ  EFILIFAVPKEEVVSQKDGAQIKQEPIQVVKPQREKKAKKFKVKPATCEKPKFLEYKTCVGDLTVVIAKALDEFKEFCIV
SQ  NAANEHMTHGSGVAKAIADFCGLDFVEYCEDYVKKHGPQQRLVTPSFVKGIQCVNNVVGPRHGDNNLHEKLVAAYKNVLV
SQ  DGVVNYVVPVLSLGIFGVDFKMSIDAMREAFEGCTIRVLLFSLSQEHIDYFDVTCKQKTIYLTEDGVKYRSIVLKPGDSL
SQ  GQFGQVYAKNKIVFTADDVEDKEILYVPTTDKSILEYYGLDAQKYVIYLQTLAQKWNVQYRDNFLILEWRDGNCWISSAI
SQ  VLLQAAKIRFKGFLTEAWAKLLGGDPTDFVAWCYASCTAKVGDFSDANWLLANLAEHFDADYTNAFLKKRVSCNCGIKSY
SQ  ELRGLEACIQPVRATNLLHFKTQYSNCPTCGANNTDEVIEASLPYLLLFATDGPATVDCDEDAVGTVVFVGSTNSGHCYT
SQ  QAAGQAFDNLAKDRKFGKKSPYITAMYTRFAFKNETSLPVAKQSKGKSKSVKEDVSNLATSSKASFDNLTDFEQWYDSNI
SQ  YESLKVQESPDNFDKYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFIYKLTPDTDENSKAPVYYPVLDAISLKAIWVE
SQ  GNANFVVGHPNYYSKSLHIPTFWENAENFVKMGDKIGGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKLIG
SQ  KAATFIADKVGGGVVRNITDSIKGLCGITRGHFERKMSPQFLKTLMFFLFYFLKASVKSVVASYKTVLCKVVLATLLIVW
SQ  FVYTSNPVMFTGIRVLDFLFEGSLCGPYKDYGKDSFDVLRYCADDFICRVCLHDKDSLHLYKHAYSVEQVYKDAASGFIF
SQ  NWNWLYLVFLILFVKPVAGFVIICYCVKYLVLNSTVLQTGVCFLDWFVQTVFSHFNFMGAGFYFWLFYKIYIQVHHILYC
SQ  KDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVKPT
SQ  AYAYHVVDEACLVDDFVNLKYKAATPGKDSASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEAKN
SQ  AAIYYAQYLCKPILILDQALYEQLVVEPVSKSVIDKVCSILSSIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIFCH
SQ  NHDVDYTGDGFTNVIPSYGIDTGKLTPRDRGFLINADASIANLRVKNAPPVVWKFSELIKLSDSCLKYLISATVKSGVRF
SQ  FITKSGAKQVIACHTQKLLVEKKAGGIVSGTFKCFKSYFKWLLIFYILFTACCSGYYYMEVSKSFVHPMYDVNSTLHVEG
SQ  FKVIDKGVLREIVPEDTCFSNKFVNFDAFWGRPYDNSRNCPIVTAVIDGDGTVATGVPGFVSWVMDGVMFIHMTQTERKP
SQ  WYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVRLI
SQ  VPQQILHTPYVVKFVSDSYCRGSVCEYTRPGYCVSLNPQWVLFNDEYTSKPGVFCGSTVRELMFSMVSTFFTGVNPNIYM
SQ  QLATMFLILVVVVLIFAMVIKFQGVFKAYATTVFITMLVWVINAFILCVHSYNSVLAVILLVLYCYASLVTSRNTVIIMH
SQ  CWLVFTFGLIVPTWLACCYLGFIIYMYTPLFLWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGSEFVKLTNEIGDKF
SQ  EAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEIVYTPPRYSIGVSRLQSGFKKLVSPSSAVEKCIVSVS
SQ  YRGNNLNGLWLGDTIYCPRHVLGKFSGDQWNDVLNLANNHEFEVTTQHGVTLNVVSRRLKGAVLILQTAVANAETPKYKF
SQ  IKANCGDSFTIACAYGGTVVGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEFYG
SQ  GYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSLPKWLESTTVSVDDYNKWAGDNGFTPFSTSTAITKLSAITGV
SQ  DVCKLLRTIMVKNSQWGGDPILGQYNFEDELTPESVFNQIGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTAVP
SQ  LKFYVYAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPWMF
SQ  LPLVLYTAFKCVQGCYMNSFNTSLLMLYQFVKLGFVIYTSSNTLTAYTEGNWELFFELVHTTVLANVSSNSLIGLFVFKC
SQ  AKWMLYYCNATYLNNYVLMAVMVNCIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKINPPKTVWEVFST
SQ  NILIQGIGGDRVLPIATVQAKLSDVKCTTVVLMQLLTKLNVEANSKMHVYLVELHNKILASDDVGECMDNLLGMLITLFC
SQ  IDSTIDLSEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKNLYEKVLVDSKNGGVTQQELAAYRKAANIAKSVFDRDLA
SQ  VQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQASSGVVPLATVPIVCSNKLTLVIPD
SQ  PETWVKCVEGVHVTYSTVVWNIDTVIDADGTELHPTSTGSGLTYCISGANIAWPLKVNLTRNGHNKVDVVLQNNELMPHG
SQ  VKTKACVAGVDQAHCSVESKCYYTNISGNSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGVKVEVVYLYF
SQ  IKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFAIT
SQ  SKPSPTPDQDSYGGASVCLYCRAHIAHPGSVGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCDSL
SQ  RQPKSSVQSVAGASDFDKNYLNRVRGSSEARLIPLASGCDPDVVKRAFDVCNKESAGMFQNLKRNCARFQELRDTEDGNL
SQ  EYLDSYFVVKQTTPSNYEHEKSCYEDLKSEVTADHDFFVFNKNIYNISRQRLTKYTMMDFCYALRHFDPKDCEVLKEILV
SQ  TYGCIEDYHPKWFEENKDWYDPIENSKYYVMLAKMGPIVRRALLNAIEFGNLMVEKGYVGVITLDNQDLNGKFYDFGDFQ
SQ  KTAPGAGVPVFDTYYSYMMPIIAMTDALAPERYFEYDVHKGYKSYDLLKYDYTEEKQELFQKYFKYWDQEYHPNCRDCSD
SQ  DRCLIHCANFNILFSTLIPQTSFGNLCRKVFVDGVPFIATCGYHSKELGVIMNQDNTMSFSKMGLSQLMQFVGDPALLVG
SQ  TSNNLVDLRTSCFSVCALTSGITHQTVKPGHFNKDFYDFAEKAGMFKEGSSIPLKHFFYPQTGNAAINDYDYYRYNRPTM
SQ  FDICQLLFCLEVTSKYFECYEGGCIPASQVVVNNLDKSAGYPFNKFGKARLYYEMSLEEQDQLFEITKKNVLPTITQMNL
SQ  KYAISAKNRARTVAGVSILSTMTNRQFHQKILKSIVNTRNASVVIGTTKFYGGWDNMLRNLIQGVEDPILMGWDYPKCDR
SQ  AMPNLLRIAASLVLARKHTNCCSWSERIYRLYNECAQVLSETVLATGGIYVKPGGTSSGDATTAYANSVFNIIQATSANV
SQ  ARLLSVITRDIVYDNIKSLQYELYQQVYRRVNFDPAFVEKFYSYLCKNFSLMILSDDGVVCYNNTLAKQGLVADISGFRE
SQ  VLYYQNNVFMADSKCWVEPDLEKGPHEFCSQHTMLVEVDGEPKYLPYPDPSRILGACVFVDDVDKTEPVAVMERYIALAI
SQ  DAYPLVHHENEEYKKVFFVLLAYIRKLYQELSQNMLMDYSFVMDIDKGSKFWEQEFYENMYRAPTTLQSCGVCVVCNSQT
SQ  ILRCGNCIRKPFLCCKCCYDHVMHTDHKNVLSINPYICSQLGCGEADVTKLYLGGMSYFCGNHKPKLSIPLVSNGTVFGI
SQ  YRANCAGSENVDDFNQLATTNWSIVEPYILANRCSDSLRRFAAETVKATEELHKQQFASAEVREVFSDRELILSWEPGKT
SQ  RPPLNRNYVFTGYHFTRTSKVQLGDFTFEKGEGKDVVYYKATSTAKLSVGDIFVLTSHNVVSLVAPTLCPQQTFSRFVNL
SQ  RPNVMVPECFVNNIPLYHLVGKQKRTTVQGPPGSGKSHFAIGLAVYFSSARVVFTACSHAAVDALCEKAFKFLKVDDCTR
SQ  IVPQRTTVDCFSKFKANDTGKKYIFSTINALPEVSCDILLVDEVSMLTNYELSFINGKINYQYVVYVGDPAQLPAPRTLL
SQ  NGSLSPKDYNVVTNLMVCVKPDIFLAKCYRCPKEIVDTVSTLVYDGKFIANNPESRECFKVIVNNGNSDVGHESGSAYNT
SQ  TQLEFVKDFVCRNKQWREAIFISPYNAMNQRAYRMLGLNVQTVDSSQGSEYDYVIFCVTADSQHALNINRFNVALTRAKR
SQ  GILVVMRQRDELYSALKFTELDSETSLQGTGLFKICNKEFSGVHPAYAVTTKALAATYKVNDELAALVNVEAGSEITYKH
SQ  LISLLGFKMSVNVEGCHNMFITRDEAIRNVRGWVGFDVEATHACGTNIGTNLPFQVGFSTGADFVVTPEGLVDTSIGNNF
SQ  EPVNSKAPPGEQFNHLRVLFKSAKPWHVIRPRIVQMLADNLCNVSDCVVFVTWCHGLELTTLRYFVKIGKEQVCSCGSRA
SQ  TTFNSHTQAYACWKHCLGFDFVYNPLLVDIQQWGYSGNLQFNHDLHCNVHGHAHVASVDAIMTRCLAINNAFCQDVNWDL
SQ  TYPHIANEDEVNSSCRYLQRMYLNACVDALKVNVVYDIGNPKGIKCVRRGDVNFRFYDKNPIVRNVKQFEYDYNQHKDKF
SQ  ADGLCMFWNCNVDCYPDNSLVCRYDTRNLSVFNLPGCNGGSLYVNKHAFYTPKFDRISFRNLKAMPFFFYDSSPCETIQV
SQ  DGVAQDLVSLATKDCITKCNIGGAVCKKHAQMYAEFVTSYNAAVTAGFTFWVTNKLNPYNLWKSFSALQSIDNIAYNMYK
SQ  GGHYDAIAGEMPTVITGDKVFVIDQGVEKAVFVNQTTLPTSVAFELYAKRNIRTLPNNRILKGLGVDVTNGFVIWDYANQ
SQ  TPLYRNTVKVCAYTDIEPNGLVVLYDDRYGDYQSFLAADNAVLVSTQCYKRYSYVEIPSNLLVQNGMPLKDGANLYVYKR
SQ  VNGAFVTLPNTINTQGRSYETFEPRSDIERDFLAMSEESFVERYGKDLGLQHILYGEVDKPQLGGLHTVIGMYRLLRANK
SQ  LNAKSVTNSDSDVMQNYFVLSDNGSYKQVCTVVDLLLDDFLELLRNILKEYGTNKSKVVTVSIDYHSINFMTWFEDGSIK
SQ  TCYPQLQSAWTCGYNMPELYKVQNCVMEPCNIPNYGVGITLPSGILMNVAKYTQLCQYLLKTTICVPHNMRVMHFGAGSD
SQ  KGVAPGSTVLKQWLPEGTLLVDNDIVDYVSDAHVSVLSDCNKYNTEHKFDLVISDMYTDNDSKRKHEGVIANNGNDDVFI
SQ  YLSSFLRNNLALGGSFAVKVTETSWHEVLYDIAQDCAWWTMFCTAVNASSSEAFLIGVNYLGASEKVKVSGKTLHANYIF
SQ  WRNCNYLQTSAYSIFDVAKFDLRLKATPVVNLKTEQKTDLVFNLIKCGKLLVRDVGNTSFTSDSFVCTM
//
ID  P0C6Y3;
PN  2'-O-methyl transferase;
GN  rep;
OS  11127;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000305|PubMed:30200673}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000305|PubMed:30200673}. [Non-structural protein 4]: Host endoplasmic reticulum membrane {ECO:0000305|PubMed:30200673}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000305|PubMed:30200673}. [Non-structural protein 6]: Host endoplasmic reticulum membrane {ECO:0000305|PubMed:30200673}; Multi-pass membrane protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000305|PubMed:30200673}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. [Proofreading exoribonuclease]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. [Uridylate-specific endoribonuclease]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}.
DR  UNIPROT: P0C6Y3;
DR  UNIPROT: Q0GNB9;
DR  UNIPROT: Q0GNC0;
DR  UNIPROT: Q5I5Y0;
DR  UNIPROT: Q5I5Y1;
DR  PDB: 2Q6D;
DR  PDB: 2Q6F;
DR  PDB: 5C94;
DR  PDB: 7F52;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF17896;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51961;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: [Isoform Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (By similarity). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like protease]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:30200673). Alone is able to induce paired membranes (PubMed:30200673). Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (PubMed:30200673). {ECO:0000269|PubMed:30200673}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. {ECO:0000255|PROSITE-ProRule:PRU00772}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000269|PubMed:28257598}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities (By similarity). Therefore plays an essential role in viral mRNAs cap methylation (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Proofreading exoribonuclease]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity (By similarity). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs (By similarity). Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyl transferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
GO  GO:0044167;
GO  GO:0044172;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASSLKQGVSPKLRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRNLQTGKQFKFETVCGLFLLKGVDKIT
SQ  PGVPAKVLKATSKLADLEDIFGVSPFARKYRELLKTACQWSLTVETLDARAQTLDEIFDPTEILWLQVAAKIQVSAMAMR
SQ  RLVGEVTAKVMDALGSNMSALFQIFKQQIVRIFQKALAIFENVSELPQRIAALKMAFAKCAKSITVVVMERTLVVREFAG
SQ  TCLASINGAVAKFFEELPNGFMGAKIFTTLAFFREAAVKIVDNIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK
SQ  AEIPVESEGWSAILGGHLCYVFKSGDRFYAAPLSGNFALHDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVAELVAA
SQ  IKRGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLKLFQSARVKVEDVWSSLTEKSFEFWRLAYGKVRNLEEFVKTCFC
SQ  KAQMAIVILATVLGEGIWHLVSQVIYKVGGLFTKVVDFCEKYWKGFCAQLKRAKLIVTETLCVLKGVAQHCFQLLLDAIQ
SQ  FMYKSFKKCALGRIHGDLLFWKGGVHKIIQEGDEIWFDAIDSIDVEDLGVVQEKLIDFDVCDNVTLPENQPGHMVQIEDD
SQ  GKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVFIKVSIECCGEPWNTIFKKAYKEPIEV
SQ  ETDLTVEQLLSVVYEKMCDDLKLFPEAPEPPPFENVTLVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGDA
SQ  EECDTNLECEEEDEDTKVLALIQDPASNKYPLPLDDDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKALPQKV
SQ  IDVLGDWGEAVDAQEQLCQQESTRVISEKSVEGFTGSCDAMAEQAIVEEQEIVPVVEQSQDVVVFTPADLEVVKETAEEV
SQ  DEFILISAVPKEEVVSQEKEEPQVEQEPTLVVKAQREKKAKKFKVKPATCEKPKFLEYKTCVGDLAVVIAKALDEFKEFC
SQ  IVNAANEHMSHGGGVAKAIADFCGPDFVEYCADYVKKHGPQQKLVTPSFVKGIQCVNNVVGPRHGDSNLREKLVAAYKSV
SQ  LVGGVVNYVVPVLSSGIFGVDFKISIDAMREAFKGCAIRVLLFSLSQEHIDYFDATCKQKTIYLTEDGVKYRSVVLKPGD
SQ  SLGQFGQVFARNKVVFSADDVEDKEILFIPTTDKTILEYYGLDAQKYVTYLQTLAQKWDVQYRDNFVILEWRDGNCWISS
SQ  AIVLLQAAKIRFKGFLAEAWAKLLGGDPTDFVAWCYASCNAKVGDFSDANWLLANLAEHFDADYTNALLKKCVSCNCGVK
SQ  SYELRGLEACIQPVRAPNLLHFKTQYSNCPTCGASSTDEVIEASLPYLLLFATDGPATVDCDENAVGTVVFIGSTNSGHC
SQ  YTQADGKAFDNLAKDRKFGRKSPYITAMYTRFSLRSENPLLVVEHSKGKAKVVKEDVSNLATSSKASFDDLTDFEQWYDS
SQ  NIYESLKVQETPDNLDEYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFTYKLTPDTDENSKTPVYYPVLDSISLRAIW
SQ  VEGSANFVVGHPNYYSKSLRIPTFWENAESFVKMGYKIDGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKI
SQ  LVKAATYVADKVGDGVVRNITDRIKGLCGFTRGHFEKKMSLQFLKTLVFFFFYFLKASSKSLVSSYKIVLCKVVFATLLI
SQ  VWFIYTSNPVVFTGIRVLDFLFEGSLCGPYNDYGKDSFDVLRYCAGDFTCRVCLHDRDSLHLYKHAYSVEQIYKDAASGI
SQ  NFNWNWLYLVFLILFVKPVAGFVIICYCVKYLVLSSTVLQTGVGFLDWFVKTVFTHFNFMGAGFYFWLFYKIYVQVHHIL
SQ  YCKDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVK
SQ  PTAYAYHVVYEACVVDDFVNLKYKAAIPGKDNASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEA
SQ  KNAAVYYAQYLCKPILILDQALYEQLIVEPVSKSVIDKVCSILSNIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIF
SQ  CHNHEVEYTGDGFTNVIPSYGMDTDKLTPRDRGFLINADASIANLRVKNAPPVVWKFSDLIKLSDSCLKYLISATVKSGG
SQ  RFFITKSGAKQVISCHTQKLLVEKKAGGVINNTFKWFMSCFKWLFVFYILFTACCLGYYYMEMNKSFVHPMYDVNSTLHV
SQ  EGFKVIDKGVIREIVSEDNCFSNKFVNFDAFWGKSYENNKNCPIVTVVIDGDGTVAVGVPGFVSWVMDGVMFVHMTQTDR
SQ  RPWYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVR
SQ  LIVPQQILHTPYIVKFVSDSYCRGSVCEYTKPGYCVSLDSQWVLFNDEYISKPGVFCGSTVRELMFNMVSTFFTGVNPNI
SQ  YIQLATMFLILVVIVLIFAMVIKFQGVFKAYATIVFTIMLVWVINAFVLCVHSYNSVLAVILLVLYCYASMVTSRNTAII
SQ  MHCWLVFTFGLIVPTWLACCYLGFILYMYTPLVFWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGTEFVKLTNEIGD
SQ  KFEAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEVVYTPPRYSIGVSRLQAGFKKLVSPSSAVEKCIVS
SQ  VSYRGNNLNGLWLGDSIYCPRHVLGKFSGDQWGDVLNLANNHEFEVVTQNGVTLNVVSRRLKGAVLILQTAVANAETPKY
SQ  KFVKANCGDSFTIACSYGGTVIGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEF
SQ  YGGYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSQPKWLESTTVSIEDYNRWASDNGFTPFSTSTAITKLSAIT
SQ  GVDVCKLLRTIMVKSAQWGSDPILGQYNFEDELTPESVFNQVGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTA
SQ  VPLKFYVHAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPW
SQ  MLLPLVLYTAFKCVQGCYMNSFNTSLLMLYQFMKLGFVIYTSSNTLTAYTEGNWELFFELVHTIVLANVSSNSLIGLIVF
SQ  KCAKWMLYYCNATYFNNYVLMAVMVNGIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKVNPPKTVWEVF
SQ  TTNILIQGIGGDRVLPIATVQSKLSDVKCTTVVLMQLLTKLNVEANSKMHAYLVELHNKILASDDVGECMDNLLGMLITL
SQ  FCIDSTIDLGEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKSIYEKVLADSKNGGVTQQELAAYRKAANIAKSVFDRD
SQ  LAVQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQANSGVVPLATVPIVCSNKLTLVI
SQ  PDPETWVKCVEGVHVTYSTVVWNIDCVTDADGTELHPTSTGSGLTYCISGDNIAWPLKVNLTRNGHNKVDVALQNNELMP
SQ  HGVKTKACVAGVDQAHCSVESKCYYTSISGSSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGDKVEVVYL
SQ  YFIKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFA
SQ  ITSKPSPTPDQDSYGGASVCLYCRAHIAHPGGAGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCD
SQ  SLRQPKPSVQSVAVASGFDKNYLNRVRGSSEARLIPLANGCDPDVVKRAFDVCNKESAGMFQNLKRNCARFQEVRDTEDG
SQ  NLEYCDSYFVVKQTTPSNYEHEKACYEDLKSEVTADHDFFVFNKNIYNISRQRLTKYTMMDFCYALRHFDPKDCEVLKEI
SQ  LVTYGCIEDYHPKWFEENKDWYDPIENPKYYAMLAKMGPIVRRALLNAIEFGNLMVEKGYVGVITLDNQDLNGKFYDFGD
SQ  FQKTAPGAGVPVFDTYYSYMMPIIAMTDALAPERYFEYDVHKGYKSYDLLKYDYTEEKQDLFQKYFKYWDQEYHPNCRDC
SQ  SDDRCLIHCANFNILFSTLVPQTSFGNLCRKVFVDGVPFIATCGYHSKELGVIMNQDNTMSFSKMGLSQLMQFVGDPALL
SQ  VGTSNKLVDLRTSCFSVCALASGITHQTVKPGHFNKDFYDFAEKAGMFKEGSSIPLKHFFYPQTGNAAINDYDYYRYNRP
SQ  TMFDIRQLLFCLEVTSKYFECYEGGCIPASQVVVNNLDKSAGYPFNKFGKARLYYEMSLEEQDQLFESTKKNVLPTITQM
SQ  NLKYAISAKNRARTVAGVSILSTMTNRQFHQKILKSIVNTRNAPVVIGTTKFYGGWDNMLRNLIQGVEDPILMGWDYPKC
SQ  DRAMPNLLRIAASLVLARKHTNCCTWSERVYRLYNECAQVLSETVLATGGIYVKPGGTSSGDATTAYANSVFNIIQATSA
SQ  NVARLLSVITRDIVYDDIKSLQYELYQQVYRRVNFDPAFVEKFYSYLCKNFSLMILSDDGVVCYNNTLAKQGLVADISGF
SQ  REVLYYQNNVFMADSKCWVEPDLEKGPHEFCSQHTMLVEVDGEPRYLPYPDPSRILCACVFVDDLDKTESVAVMERYIAL
SQ  AIDAYPLVHHENEEYKKVFFVLLSYIRKLYQELSQNMLMDYSFVMDIDKGSKFWEQEFYENMYRAPTTLQSCGVCVVCNS
SQ  QTILRCGNCIRKPFLCCKCCYDHVMHTDHKNVLSINPYICSQPGCGEADVTKLYLGGMSYFCGNHKPKLSIPLVSNGTVF
SQ  GIYRANCAGSENVDDFNQLATTNWSTVEPYILANRCVDSLRRFAAETVKATEELHKQQFASAEVREVLSDRELILSWEPG
SQ  KTRPPLNRNYVFTGFHFTRTSKVQLGDFTFEKGEGKDVVYYRATSTAKLSVGDIFVLTSHNVVSLIAPTLCPQQTFSRFV
SQ  NLRPNVMVPACFVNNIPLYHLVGKQKRTTVQGPPGSGKSHFAIGLAAYFSNARVVFTACSHAAVDALCEKAFKFLKVDDC
SQ  TRIVPQRTTIDCFSKFKANDTGKKYIFSTINALPEVSCDILLVDEVSMLTNYELSFINGKINYQYVVYVGDPAQLPAPRT
SQ  LLNGSLSPKDYNVVTNLMVCVKPDIFLAKCYRCPKEIVDTVSTLVYDGKFIANNPESRQCFKVIVNNGNSDVGHESGSAY
SQ  NITQLEFVKDFVCRNKEWREATFISPYNAMNQRAYRMLGLNVQTVDSSQGSEYDYVIFCVTADSQHALNINRFNVALTRA
SQ  KRGILVVMRQRDELYSALKFIELDSVASLQGTGLFKICNKEFSGVHPAYAVTTKALAATYKVNDELAALVNVEAGSEITY
SQ  KHLISLLGFKMSVNVEGCHNMFITRDEAIRNVRGWVGFDVEATHACGTNIGTNLPFQVGFSTGADFVVTPEGLVDTSIGN
SQ  NFEPVNSKAPPGEQFNHLRALFKSAKPWHVVRPRIVQMLADNLCNVSDCVVFVTWCHGLELTTLRYFVKIGKDQVCSCGS
SQ  RATTFNSHTQAYACWKHCLGFDFVYNPLLVDIQQWGYSGNLQFNHDLHCNVHGHAHVASADAIMTRCLAINNAFCQDVNW
SQ  DLTYPHIANEDEVNSSCRYLQRMYLNACVDALKVNVVYDIGNPKGIKCVRRGDLNFRFYDKNPIVPNVKQFEYDYNQHKD
SQ  KFADGLCMFWNCNVDCYPDNSLVCRYDTRNLSVFNLPGCNGGSLYVNKHAFHTPKFDRTSFRNLKAMPFFFYDSSPCETI
SQ  QLDGVAQDLVSLATKDCITKCNIGGAVCKKHAQMYADFVTSYNAAVTAGFTFWVTNNFNPYNLWKSFSALQSIDNIAYNM
SQ  YKGGHYDAIAGEMPTIVTGDKVFVIDQGVEKAVFFNQTILPTSVAFELYAKRNIRTLPNNRILKGLGVDVTNGFVIWDYT
SQ  NQTPLYRNTVKVCAYTDIEPNGLIVLYDDRYGDYQSFLAADNAVLVSTQCYKRYSYVEIPSNLLVQNGIPLKDGANLYVY
SQ  KRVNGAFVTLPNTLNTQGRSYETFEPRSDVERDFLDMSEESFVEKYGKELGLQHILYGEVDKPQLGGLHTVIGMCRLLRA
SQ  NKLNAKSVTNSDSDVMQNYFVLADNGSYKQVCTVVDLLLDDFLELLRNILKEYGTNKSKVVTVSIDYHSINFMAWFEDGI
SQ  IKTCYPQLQSAWTCGYNMPELYKVQNCVMEPCNIPNYGVGIALPSGIMMNVAKYTQLCQYLSKTTMCVPHNMRVMHFGAG
SQ  SDKGVAPGSTVLKQWLPEGTLLVDNDIVDYVSDAHVSVLSDCNKYKTEHKFDLVISDMYTDNDSKRKHEGVIANNGNDDV
SQ  FIYLSSFLRNNLALGGSFAVKVTETSWHEVLYDIAQDCAWWTMFCTAVNASSSEAFLVGVNYLGASEKVKVSGKTLHANY
SQ  IFWRNCNYLQTSAYSIFDVAKFDLRLKATPVVNLKTEQKTDLVFNLIKCGKLLVRDVGNTSFTSDSFVCTM
//
ID  K9N7C7;
PN  2'-O-methyltransferase;
GN  rep;
OS  1263720;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: K9N7C7;
DR  PDB: 4WUR;
DR  PDB: 5HOL;
DR  PDB: 5KO3;
DR  Pfam: PF13087;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000269|PubMed:26311885}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B. signaling. {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:25142582}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}. [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}. [Guanine-N7 methyltransferase]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. [2'-O-methyltransferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
DE  Interaction: K9N7C7; IntAct: EBI-25568763; Score: 0.56
DE  Interaction: P0C6Y0; IntAct: EBI-25758213; Score: 0.44
DE  Interaction: P0C6X7; IntAct: EBI-25758227; Score: 0.44
DE  Interaction: P0C6Y5; IntAct: EBI-25758330; Score: 0.44
DE  Interaction: Q98VG9; IntAct: EBI-25758376; Score: 0.44
DE  Interaction: P0C6Y1; IntAct: EBI-25758616; Score: 0.44
DE  Interaction: Q96PM5; IntAct: EBI-25826816; Score: 0.51
DE  Interaction: Q9C026; IntAct: EBI-26374603; Score: 0.35
DE  Interaction: Q9BZH6; IntAct: EBI-26374603; Score: 0.35
DE  Interaction: P28330; IntAct: EBI-26374603; Score: 0.35
DE  Interaction: Q05516; IntAct: EBI-26374629; Score: 0.35
DE  Interaction: P42345; IntAct: EBI-26374629; Score: 0.35
DE  Interaction: P40763; IntAct: EBI-26374629; Score: 0.35
DE  Interaction: O60220; IntAct: EBI-26374629; Score: 0.35
DE  Interaction: P17612; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q9UPN4; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q9Y2I6; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q9UNZ2; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q9C0B0; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q9BV73; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q9BQS8; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q99996; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q96SN8; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q8TD10; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q8NDN9; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q8N4C6; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q8IWJ2; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q8IUD2; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q66GS9; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q5VU43; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q16881; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q15154; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q12965; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q08378; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: P67936; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: P49454; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: P31323; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: P14649; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: P13861; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: P09493; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: O95613; IntAct: EBI-26374676; Score: 0.35
DE  Interaction: Q92878; IntAct: EBI-26374745; Score: 0.35
DE  Interaction: Q9NQX3; IntAct: EBI-26374745; Score: 0.35
DE  Interaction: Q96EN8; IntAct: EBI-26374745; Score: 0.35
DE  Interaction: Q5T9A4; IntAct: EBI-26374745; Score: 0.35
DE  Interaction: Q5QP82; IntAct: EBI-26374745; Score: 0.35
DE  Interaction: P63151; IntAct: EBI-26374745; Score: 0.35
DE  Interaction: P49959; IntAct: EBI-26374745; Score: 0.35
DE  Interaction: P30153; IntAct: EBI-26374745; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-26374745; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-26374745; Score: 0.35
DE  Interaction: A0A0B4J1Y9; IntAct: EBI-26374774; Score: 0.40
DE  Interaction: Q96IV0; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q9UBV2; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q9Y305; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q9ULA0; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q9P209; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q96RU2; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q96DZ1; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q92995; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q8IWR1; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q6PJI9; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q15796; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q13438; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: P54802; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: P51659; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: P43686; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: P11717; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: O95835; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: A3KMH1; IntAct: EBI-26374786; Score: 0.35
DE  Interaction: Q8TF46; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q8WVC6; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q7L2H7; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q9UPQ9; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q9UH62; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q9HD20; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q9H1I8; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q9BQ70; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q99613; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q96D09; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q96B26; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q96A26; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q8NBU5; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q8N9N2; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q8N3C0; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q6Y7W6; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q6NUN9; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q5VT66; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q5SZL2; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q15650; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q13423; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q10471; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: P16435; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: P15954; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: P00387; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: O00746; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: O00186; IntAct: EBI-26374831; Score: 0.35
DE  Interaction: Q92643; IntAct: EBI-26374899; Score: 0.35
DE  Interaction: Q96S52; IntAct: EBI-26374899; Score: 0.35
DE  Interaction: Q969N2; IntAct: EBI-26374899; Score: 0.35
DE  Interaction: Q8NFQ8; IntAct: EBI-26374899; Score: 0.35
DE  Interaction: Q8NBJ7; IntAct: EBI-26374899; Score: 0.35
DE  Interaction: Q13586; IntAct: EBI-26374899; Score: 0.35
DE  Interaction: P49257; IntAct: EBI-26374899; Score: 0.35
DE  Interaction: P13674; IntAct: EBI-26374899; Score: 0.35
DE  Interaction: Q15032; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: Q15118; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: Q8NHV4; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: Q8NBN7; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: Q8IX12; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: Q7KZI7; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: Q6ZRY4; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: Q14244; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: Q12948; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: P52952; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: P29558; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: P19447; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: P15923; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: P15170; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: O75629; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: O15014; IntAct: EBI-26374923; Score: 0.35
DE  Interaction: Q9UDY4; IntAct: EBI-26374950; Score: 0.35
DE  Interaction: P25685; IntAct: EBI-26374950; Score: 0.35
DE  Interaction: Q9Y5J7; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q9NX40; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q9H7Z7; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q9BQE4; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q8WUY8; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q8N9F7; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q8N2K0; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q6ZRP7; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q6P1Q0; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q6P1M0; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q53H12; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: Q13724; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: O95573; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: O95159; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: O94766; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: O14975; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: A8MTT3; IntAct: EBI-26374966; Score: 0.35
DE  Interaction: P10644; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q9Y3A4; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q9BSC4; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q9Y3B2; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q9NY61; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q99848; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q96GQ7; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q8IY81; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q15050; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q13823; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q9ULX6; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q9UHG3; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q9NTK5; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q9H6R4; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q9GZL7; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q99547; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q8TC07; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q8NI36; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q8N5D0; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q8IX01; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q7Z4Q2; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q76FK4; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q16531; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q15269; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q14146; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q13206; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q12788; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q03701; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: P51116; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: P51114; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: P42285; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: O95707; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: O95373; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: O60287; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: O15381; IntAct: EBI-26375013; Score: 0.35
DE  Interaction: Q9BU61; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: Q8IWP9; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: Q86YT6; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: Q6SZW1; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: Q5SW79; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: P62310; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: P49419; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: P41250; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: P38606; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: P21281; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: O00233; IntAct: EBI-26375055; Score: 0.35
DE  Interaction: P0CG48; IntAct: EBI-26585537; Score: 0.44
DE  Interaction: Q64339; IntAct: EBI-26585746; Score: 0.44
DE  Interaction: P05161; IntAct: EBI-26602927; Score: 0.65
DE  Interaction: Q9BYX4; IntAct: EBI-26895245; Score: 0.40
DE  Interaction: Q9BZS1; IntAct: EBI-26996646; Score: 0.44
DE  Interaction: P07225; IntAct: EBI-26996673; Score: 0.44
DE  Interaction: Q96C36; IntAct: EBI-27129521; Score: 0.46
DE  Interaction: P32322; IntAct: EBI-27129521; Score: 0.46
DE  Interaction: Q93008; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q9HA64; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q9ULT8; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q7Z4H7; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q5VZ89; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q9H9G7; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q13546; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: P41229; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q14999; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: P98164; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q15003; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q504Q3; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: P45974; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q8IYU2; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: P54727; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q9P2F8; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q8N2Y8; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: P54725; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q13362; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q7Z494; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q14008; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: P78344; IntAct: EBI-27129420; Score: 0.35
DE  Interaction: Q96CW1; IntAct: EBI-30798570; Score: 0.40
GO  GO:1905369;
GO  GO:1902555;
GO  GO:1905354;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0031381;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:1902680;
GO  GO:0045070;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0016485;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039503;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039653;
GO  GO:0039604;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0046786;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHT
SQ  RHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHY
SQ  ERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEG
SQ  FITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYG
SQ  KESLENPTYIYHSAFIECGSCGNDSWLTGNAIQGFACGCGASYTANDVEVQSSGMIKPNALLCATCPFAKGDSCSSNCKH
SQ  SVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGCEEGTMYFVPRAKSVVSRIGDSIFTGCTGSWNKVTQIANMFLEQT
SQ  QHSLNFVGEFVVNDVVLAILSGTTTNVDKIRQLLKGVTLDKLRDYLADYDVAVTAGPFMDNAINVGGTGLQYAAITAPYV
SQ  VLTGLGESFKKVATIPYKVCNSVKDTLTYYAHSVLYRVFPYDMDSGVSSFSELLFDCVDLSVASTYFLVRLLQDKTGDFM
SQ  STIITSCQTAVSKLLDTCFEATEATFNFLLDLAGLFRIFLRNAYVYTSQGFVVVNGKVSTLVKQVLDLLNKGMQLLHTKV
SQ  SWAGSNISAVIYSGRESLIFPSGTYYCVTTKAKSVQQDLDVILPGEFSKKQLGLLQPTDNSTTVSVTVSSNMVETVVGQL
SQ  EQTNMHSPDVIVGDYVIISEKLFVRSKEEDGFAFYPACTNGHAVPTLFRLKGGAPVKKVAFGGDQVHEVAAVRSVTVEYN
SQ  IHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFS
SQ  LHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIA
SQ  QVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVIT
SQ  ECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNIL
SQ  HVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSL
SQ  TFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPL
SQ  GYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLL
SQ  HWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGAD
SQ  ISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMT
SQ  LDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDV
SQ  VLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHY
SQ  VHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTY
SQ  SPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKG
SQ  KPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVS
SQ  FVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFAT
SQ  RTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVD
SQ  LSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRAN
SQ  SFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQ
SQ  TSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGK
SQ  RTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQP
SQ  FYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIA
SQ  TKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQIT
SQ  NESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSK
SQ  LRANDNILSVRFTANKIVGGAPTWFNALRDFTLKGYVLATIIVFLCAVLMYLCLPTFSMVPVEFYEDRILDFKVLDNGII
SQ  RDVNPDDKCFANKHRSFTQWYHEHVGGVYDNSITCPLTVAVIAGVAGARIPDVPTTLAWVNNQIIFFVSRVFANTGSVCY
SQ  TPIDEIPYKSFSDSGCILPSECTMFRDAEGRMTPYCHDPTVLPGAFAYSQMRPHVRYDLYDGNMFIKFPEVVFESTLRIT
SQ  RTLSTQYCRFGSCEYAQEGVCITTNGSWAIFNDHHLNRPGVYCGSDFIDIVRRLAVSLFQPITYFQLTTSLVLGIGLCAF
SQ  LTLLFYYINKVKRAFADYTQCAVIAVVAAVLNSLCICFVASIPLCIVPYTALYYYATFYFTNEPAFIMHVSWYIMFGPIV
SQ  PIWMTCVYTVAMCFRHFFWVLAYFSKKHVEVFTDGKLNCSFQDAASNIFVINKDTYAALRNSLTNDAYSRFLGLFNKYKY
SQ  FSGAMETAAYREAAACHLAKALQTYSETGSDLLYQPPNCSITSGVLQSGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLD
SQ  NTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGA
SQ  AFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQV
SQ  HQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLY
SQ  TGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQSGVRKVTYGTAHWLFATLVSTYVIILQATKFTLWNYLFETIPTQLFP
SQ  LLFVTMAFVMLLVKHKHTFLTLFLLPVAICLTYANIVYEPTTPISSALIAVANWLAPTNAYMRTTHTDIGVYISMSLVLV
SQ  IVVKRLYNPSLSNFALALCSGVMWLYTYSIGEASSPIAYLVFVTTLTSDYTITVFVTVNLAKVCTYAIFAYSPQLTLVFP
SQ  EVKMILLLYTCLGFMCTCYFGVFSLLNLKLRAPMGVYDFKVSTQEFRFMTANNLTAPRNSWEAMALNFKLIGIGGTPCIK
SQ  VAAMQSKLTDLKCTSVVLLSVLQQLHLEANSRAWAFCVKCHNDILAATDPSEAFEKFVSLFATLMTFSGNVDLDALASDI
SQ  FDTPSVLQATLSEFSHLATFAELEAAQKAYQEAMDSGDTSPQVLKALQKAVNIAKNAYEKDKAVARKLERMADQAMTSMY
SQ  KQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGIISNARNGCIPLSVIPLCASNKLRVVIPDFTVWNQVVTYPSLNYAG
SQ  ALWDITVINNVDNEIVKSSDVVDSNENLTWPLVLECTRASTSAVKLQNNEIKPSGLKTMVVSAGQEQTNCNTSSLAYYEP
SQ  VQGRKMLMALLSDNAYLKWARVEGKDGFVSVELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQVLGHIAATVRLQAGS
SQ  NTEFASNSSVLSLVNFTVDPQKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAISVKPESTADQETYGGASVCLYCRAHIEH
SQ  PDVSGVCKYKGKFVQIPAQCVRDPVGFCLSNTPCNVCQYWIGYGCNCDSLRQAALPQSKDSNFLKRVRGSIVNARIEPCS
SQ  SGLSTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVELDDQGHHLDSYFVVKRHTMENYELEKHCYDLLRDCDAVAPHDF
SQ  FIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNSEVLKAILVKYGCCDVTYFENKLWFDFVENPSVIGVYHKLGERV
SQ  RQAILNTVKFCDHMVKAGLVGVLTLDNQDLNGKWYDFGDFVITQPGSGVAIVDSYYSYLMPVLSMTDCLAAETHRDCDFN
SQ  KPLIEWPLTEYDFTDYKVQLFEKYFKYWDQTYHANCVNCTDDRCVLHCANFNVLFAMTMPKTCFGPIVRKIFVDGVPFVV
SQ  SCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASSNAFLDLRTSCFSVAALTTGLTFQTVRPGNFNQDFYDF
SQ  VVSKGFFKEGSSVTLKHFFFAQDGNAAITDYNYYSYNLPTMCDIKQMLFCMEVVNKYFEIYDGGCLNASEVVVNNLDKSA
SQ  GHPFNKFGKARVYYESMSYQEQDELFAMTKRNVIPTMTQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAAT
SQ  RGATCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQV
SQ  LSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFV
SQ  DKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYIAGIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLYIKD
SQ  GDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHEDIEYQNVFWVYLQYIEKLYKDLTGHMLDS
SQ  YSVMLCGDNSAKFWEEAFYRDLYSSPTTLQAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVC
SQ  NAPGCGVSDVTKLYLGGMSYFCVDHRPVCSFPLCANGLVFGLYKNMCTGSPSIVEFNRLATCDWTESGDYTLANTTTEPL
SQ  KLFAAETLRATEEASKQSYAIATIKEIVGERQLLLVWEAGKSKPPLNRNYVFTGYHITKNSKVQLGEYIFERIDYSDAVS
SQ  YKSSTTYKLTVGDIFVLTSHSVATLTAPTIVNQERYVKITGLYPTITVPEEFASHVANFQKSGYSKYVTVQGPPGTGKSH
SQ  FAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDRFKVNETNSQYLFSTINALPETSADI
SQ  LVVDEVSMCTNYDLSIINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSMCYRCPKEIVS
SQ  TVSALVYNNKLLAKKELSGQCFKILYKGNVTHDASSAINRPQLTFVKNFITANPAWSKAVFISPYNSQNAVARSMLGLTT
SQ  QTVDSSQGSEYQYVIFCQTADTAHANNINRFNVAITRAQKGILCVMTSQALFESLEFTELSFTNYKLQSQIVTGLFKDCS
SQ  RETSGLSPAYAPTYVSVDDKYKTSDELCVNLNLPANVPYSRVISRMGFKLDATVPGYPKLFITREEAVRQVRSWIGFDVE
SQ  GAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGNMLTGIAARPPPGEQFKHLVPLMHKGAAWPIVRRRIVQMLSD
SQ  TLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQKCCMCNRRAAAYSSPLQSYACWTHSCGYDYVYNPFFVDVQQWGYVGN
SQ  LATNHDRYCSVHQGAHVASNDAIMTRCLAIHSCFIERVDWDIEYPYISHEKKLNSCCRIVERNVVRAALLAGSFDKVYDI
SQ  GNPKGIPIVDDPVVDWHYFDAQPLTRKVQQLFYTEDMASRFADGLCLFWNCNVPKYPNNAIVCRFDTRVHSEFNLPGCDG
SQ  GSLYVNKHAFHTPAYDVSAFRDLKPLPFFYYSTTPCEVHGNGSMIEDIDYVPLKSAVCITACNLGGAVCRKHATEYREYM
SQ  EAYNLVSASGFRLWCYKTFDIYNLWSTFTKVQGLENIAFNFVKQGHFIGVEGELPVAVVNDKIFTKSGVNDICMFENKTT
SQ  LPTNIAFELYAKRAVRSHPDFKLLHNLQADICYKFVLWDYERSNIYGTATIGVCKYTDIDVNSALNICFDIRDNGSLEKF
SQ  MSTPNAIFISDRKIKKYPCMVGPDYAYFNGAIIRDSDVVKQPVKFYLYKKVNNEFIDPTECIYTQSRSCSDFLPLSDMEK
SQ  DFLSFDSDVFIKKYGLENYAFEHVVYGDFSHTTLGGLHLLIGLYKKQQEGHIIMEEMLKGSSTIHNYFITETNTAAFKAV
SQ  CSVIDLKLDDFVMILKSQDLGVVSKVVKVPIDLTMIEFMLWCKDGQVQTFYPRLQASADWKPGHAMPSLFKVQNVNLERC
SQ  ELANYKQSIPMPRGVHMNIAKYMQLCQYLNTCTLAVPANMRVIHFGAGSDKGIAPGTSVLRQWLPTDAIIIDNDLNEFVS
SQ  DADITLFGDCVTVRVGQQVDLVISDMYDPTTKNVTGSNESKALFFTYLCNLINNNLALGGSVAIKITEHSWSVELYELMG
SQ  KFAWWTVFCTNANASSSEGFLLGINYLGTIKENIDGGAMHANYIFWRNSTPMNLSTYSLFDLSKFQLKLKGTPVLQLKES
SQ  QINELVISLLSQGKLLIRDNDTLSVSTDVLVNTYRKLR
//
ID  P0C6Y4;
PN  Putative 2'-O-methyl transferase;
GN  rep;
OS  229032;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 1]: Host cytoplasm {ECO:0000269|PubMed:26773386}. Host nucleus {ECO:0000269|PubMed:26773386}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6Y4;
DR  UNIPROT: Q91AV2;
DR  PDB: 5HIY;
DR  PDB: 5HIZ;
DR  Pfam: PF13087;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  PROSITE: PS51961;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DE  Function: The non-structural protein 1 (nsp1) protein plays a role in the inhibition of host interferon and pro-inflammatory cytokines production. Suppresses host RELA/p65 activation by blocking NFKBIA phosphorylation (PubMed:28715653). Targets also the RLR pathway downstream of the IRF3 activation by targeting host CREBBP to proteasomal degradation (PubMed:26773386). {ECO:0000269|PubMed:26773386, ECO:0000269|PubMed:28715653}. The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity). {ECO:0000250}. The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. {ECO:0000250}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
DE  Interaction: P0C6X1; IntAct: EBI-26366740; Score: 0.44
DE  Interaction: P0C6Y4; IntAct: EBI-25590339; Score: 0.56
GO  GO:0030430;
GO  GO:0044172;
GO  GO:0033644;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0000175;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039644;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASNHVTLAFANDAEISAFGFCTASEAVSYYSEAAASGFMQCRFVSLDLADTVEGLLPEDYVMVVIGTTKLSAYVDTFGS
SQ  RPRNICGWLLFSNCNYFLEELELTFGRRGGNIVPVDQYMCGADGKPVLQESEWEYTDFFADSEDGQLNIAGITYVKAWIV
SQ  ERSDVSYASQNLTSIKSITYCSTYEHTFLDGTAMKVARTPKIKKNVVLSEPLATIYREIGSPFVDNGSDARSIIRRPVFL
SQ  HAFVKCKCGSYHWTVGDWTSYVSTCCGFKCKPVLVASCSAMPGSVVVTRAGAGTGVKYYNNMFLRHVADIDGLAFWRILK
SQ  VQSKDDLACSGKFLEHHEEGFTDPCYFLNDSSLATKLKFDILSGKFSDEVKQAIIAGHVVVGSALVDIVDDALGQPWFIR
SQ  KLGDLASAPWEQLKAVVRGLGLLSDEVVLFGKRLSCATLSIVNGVFEFLADVPEKLAAAVTVFVNFLNEFFESACDCLKV
SQ  GGKTFNKVGSYVLFDNALVKLVKAKARGPRQAGICEVRYTSLVVGSTTKVVSKRVENANVNLVVVDEDVTLNTTGRTVVV
SQ  DGLAFFESDGFYRHLADADVVIEHPVYKSACELKPVFECDPIPDFPLPVAASVAELCVQTDLLLKNYNTPYKTYSCVVRG
SQ  DKCCITCTLQFKAPSYVEDAVNFVDLCTKNIGTAGFHEFYITAHEQQDLQGFLTTCCTMSGFECFMPTIPQCPAVLEEID
SQ  GGSIWRSFITGLNTMWDFCKRLKVSFGLDGIVVTVARKFKRLGALLAEMYNTYLSTVVENLVLAGVSFKYYATSVPKIVL
SQ  GGCFHSVKSVFASVFQIPVQAGIEKFKVFLNCVHPVVPRVIETSFVELEETTFKPPALNGGIAIVDGFAFYYDGTLYYPT
SQ  DGNSVVPICFKKKGGGDVKFSDEVSVKTIDPVYKVSLEFEFESETIMAVLNKAVGNRIKVTGGWDDVVEYINVAIEVLKD
SQ  HVEVPKYYIYDEEGGTDPNLPVMVSQWPLNDDTISQDLLDVEVVTDAPIDSEGDEVDSSAPEKVADVANSEPGDDGLPVA
SQ  PETNVESEVEEVAATLSFIKDTPSTVTKDPFAFDFVSYGGLKVLRQSHNNCWVTSTLVQLQLLGIVDDPAMELFSAGRVG
SQ  PMVRKCYESQKAILGSLGDVSACLESLTKDLHTLKITCSVVCGCGTGERIYEGCAFRMTPTLEPFPYGACAQCAQVLMHT
SQ  FKSIVGTGIFCRDTTALSLDSLVVKPLCAAAFIGKDSGHYVTNFYDAAMAIDGYGRHQIKYDTLNTICVKDVNWTAPLVP
SQ  AVDSVVEPVVKPFYSYKNVDFYQGDFSDLVKLPCDFVVNAANEKLSHGGGIAKAIDVYTKGMLQKCSNDYIKAHGPIKVG
SQ  RGVMLEALGLKVFNVVGPRKGKHAPELLVKAYKSVFANSGVALTPLISVGIFSVPLEESLSAFLACVGDRHCKCFCYGDK
SQ  EREAIIKYMDGLVDAIFKEALVDTTPVQEDVQQVSQKPVLPNFEPFRIEGAHAFYECNPEGLMSLGADKLVLFTNSNLDF
SQ  CSVGKCLNDVTSGALLEAINVFKKSNKTVPAGNCVTLDCANMISITMVVLPFDGDANYDKNYARAVVKVSKLKGKLVLAV
SQ  DDATLYSKLSHLSVLGFVSTPDDVERFYANKSVVIKVTEDTRSVKAVKVESTATYGQQIGPCLVNDTVVTDNKPVVADVV
SQ  AKVVPNANWDSHYGFDKAGEFHMLDHTGFTFPSEVVNGRRVIKTTDNNCWVNVTCLQLQFARFRFKSAGLQAMWESYCTG
SQ  DVAMFVHWLYWLTGVDKGQPSDSENALNMLSKYIVPAGSVTIERVTHDGCCCSKRVVTAPVVNASVLKLGVEDGLCPHGL
SQ  NYIGKVVVVKGTTIVVNVGKPVVAPSHLFLKGVSYTTFLDNGNGVVGHYTVFDHGTGMVHDGDAFVPGDLNVSPVTNVVV
SQ  SEQTAVVIKDPVKKAELDATKLLDTMNYASERFFSFGDFMSRNLITVFLYILSILGLCFRAFRKRDVKVLAGVPQRTGII
SQ  LRKSMRYNAKALGVFFKLKLYWFKVLGKFSLGIYALYALLFMTIRFTPIGSPVCDDVVAGYANSSFDKNEYCNSVICKVC
SQ  LYGYQELSDFSHTQVVWQHLRDPLIGNVMPFFYLAFLAIFGGVYVKAITLYFIFQYLNSLGVFLGLQQSIWFLQLVPFDV
SQ  FGDEIVVFFIVTRVLMFIKHVCLGCDKASCVACSKSARLKRVPVQTIFQGTSKSFYVHANGGSKFCKKHNFFCLNCDSYG
SQ  PGCTFINDVIATEVGNVVKLNVQPTGPATILIDKVEFSNGFYYLYSGDTFWKYNFDITDSKYTCKEALKNCSIITDFIVF
SQ  NNNGSNVNQVKNACVYFSQMLCKPVKLVDSALLASLSVDFGASLHSAFVSVLSNSFGKDLSSCNDMQDCKSTLGFDDVPL
SQ  DTFNAAVAEAHRYDVLLTDMSFNNFTTSYAKPEEKFPVHDIATCMRVGAKIVNHNVLVKDSIPVVWLVRDFIALSEETRK
SQ  YIIRTTKVKGITFMLTFNDCRMHTTIPTVCIANKKGAGLPSFSKVKKFFWFLCLFIVAAFFALSFLDFSTQVSSDSDYDF
SQ  KYIESGQLKTFDNPLSCVHNVFINFDQWHDAKFGFTPVNNPSCPIVVGVSDEARTVPGIPAGVYLAGKTLVFAINTIFGT
SQ  SGLCFDASGVADKGACIFNSACTTLSGLGGTAVYCYKNGLVEGAKLYSELAPHSYYKMVDGNAVSLPEIISRGFGIRTIR
SQ  TKAMTYCRVGQCVQSAEGVCFGADRFFVYNAESGSDFVCGTGLFTLLMNVISVFSKTVPVTVLSGQILFNCIIAFVAVAV
SQ  CFLFTKFKRMFGDMSVGVFTVGACTLLNNVSYIVTQNTLGMLGYATLYFLCTKGVRYMWIWHLGFLISYILIAPWWVLMV
SQ  YAFSAIFEFMPNLFKLKVSTQLFEGDKFVGSFENAAAGTFVLDMHAYERLANSISTEKLRQYASTYNKYKYYSGSASEAD
SQ  YRLACFAHLAKAMMDYASNHNDTLYTPPTVSYNSTLQAGLRKMAQPSGVVEKCIVRVCYGNMALNGLWLGDIVMCPRHVI
SQ  ASSTTSTIDYDYALSVLRLHNFSISSGNVFLGVVSATMRGALLQIKVNQNNVHTPKYTYRTVRPGESFNILACYDGAAAG
SQ  VYGVNMRSNYTIRGSFINGACGSPGYNINNGTVEFCYLHQLELGSGCHVGSDLDGVMYGGYEDQPTLQVEGASSLFTENV
SQ  LAFLYAALINGSTWWLSSSRIAVDRFNEWAVHNGMTTVGNTDCFSILAAKTGVDVQRLLASIQSLHKNFGGKQILGHTSL
SQ  TDEFTTGEVVRQMYGVNLQGGYVSRACRNVLLVGSFLTFFWSELVSYTKFFWVNPGYVTPMFACLSLLSSLLMFTLKHKT
SQ  LFFQVFLIPALIVTSCINLAFDVEVYNYLAEHFDYHVSLMGFNAQGLVNIFVCFVVTILHGTYTWRFFNTPASSVTYVVA
SQ  LLTAAYNYFYASDILSCAMTLFASVTGNWFVGAVCYKVAVYMALRFPTFVAIFGDIKSVMFCYLVLGYFTCCFYGILYWF
SQ  NRFFKVSVGVYDYTVSAAEFKYMVANGLRAPTGTLDSLLLSAKLIGIGGERNIKISSVQSKLTDIKCSNVVLLGCLSSMN
SQ  VSANSTEWAYCVDLHNKINLCNDPEKAQEMLLALLAFFLSKNSAFGLDDLLESYFNDNSMLQSVASTYVGLPSYVIYENA
SQ  RQQYEDAVNNGSPPQLVKQLRHAMNVAKSEFDREASTQRKLDRMAEQAAAQMYKEARAVNRKSKVVSAMHSLLFGMLRRL
SQ  DMSSVDTILNLAKDGVVPLSVIPAVSATKLNIVTSDIDSYNRIQREGCVHYAGTIWNIIDIKDNDGKVVHVKEVTAQNAE
SQ  SLSWPLVLGCERIVKLQNNEIIPGKLKQRSIKAEGDGIVGEGKALYNNEGGRTFMYAFISDKPDLRVVKWEFDGGCNTIE
SQ  LEPPRKFLVDSPNGAQIKYLYFVRNLNTLRRGAVLGYIGATVRLQAGKQTEQAINSSLLTLCAFAVDPAKTYIDAVKSGH
SQ  KPVGNCVKMLANGSGNGQAVTNGVEASTNQDSYGGASVCLYCRAHVEHPSMDGFCRLKGKYVQVPLGTVDPIRFVLENDV
SQ  CKVCGCWLSNGCTCDRSIMQSTDMAYLNRVRGSSAARLEPCNGTDTQHVYRAFDIYNKDVACLGKFLKVNCVRLKNLDKH
SQ  DAFYVVKRCTKSAMEHEQSIYSRLEKCGAIAEHDFFTWKDGRAIYGNVCRKDLTEYTMMDLCYALRNFDENNCDVLKSIL
SQ  IKVGACEESYFNNKVWFDPVENEDIHRVYALLGTIVARAMLKCVKFCDAMVEQGIVGVVTLDNQDLNGDFYDFGDFTCSI
SQ  KGMGVPICTSYYSYMMPVMGMTNCLASECFVKSDIFGEDFKSYDLLEYDFTEHKTALFNKYFKYWGLQYHPNCVDCSDEQ
SQ  CIVHCANFNTLFSTTIPITAFGPLCRKCWIDGVPLVTTAGYHFKQLGIVWNNDLNLHSSRLSINELLQFCSDPALLIASS
SQ  PALVDQRTVCFSVAALGTGMTNQTVKPGHFNKEFYDFLLEQGFFSEGSELTLKHFFFAQKVDAAVKDFDYYRYNRPTVLD
SQ  ICQARVVYQIVQRYFDIYEGGCITAKEVVVTNLNKSAGYPLNKFGKAGLYYESLSYEEQDELYAYTKRNILPTMTQLNLK
SQ  YAISGKERARTVGGVSLLSTMTTRQYHQKHLKSIVNTRGASVVIGTTKFYGGWDNMLKNLIDGVENPCLMGWDYPKCDRA
SQ  LPNMIRMISAMILGSKHTTCCSSTDRFFRLCNELAQVLTEVVYSNGGFYLKPGGTTSGDATTAYANSVFNIFQAVSANVN
SQ  KLLSVDSNVCHNLEVKQLQRKLYECCYRSTIVDDQFVVEYYGYLRKHFSMMILSDDGVVCYNNDYASLGYVADLNAFKAV
SQ  LYYQNNVFMSASKCWIEPDINKGPHEFCSQHTMQIVDKEGTYYLPYPDPSRILSAGVFVDDVVKTDAVVLLERYVSLAID
SQ  AYPLSKHENPEYKKVFYVLLDWVKHLYKTLNAGVLESFSVTLLEDSTAKFWDESFYANMYEKSAVLQSAGLCVVCGSQTV
SQ  LRCGDCLRRPMLCTKCAYDHVIGTTHKFILAITPYVCCASDCGVNDVTKLYLGGLSYWCHEHKPRLAFPLCSAGNVFGLY
SQ  KNSATGSPDVEDFNRIATSDWTDVSDYRLANDVKDSLRLFAAETIKAKEESVKSSYACATLHEVVGPKELLLKWEVGRPK
SQ  PPLNRNSVFTCYHITKNTKFQIGEFVFEKAEYDNDAVTYKTTATTKLVPGMVFVLTSHNVQPLRAPTIANQERYSTIHKL
SQ  HPAFNIPEAYSSLVPYYQLIGKQKITTIQGPPGSGKSHCVIGLGLYYPGARIVFTACSHAAVDSLCVKASTAYSNDKCSR
SQ  IIPQRARVECYDGFKSNNTSAQYLFSTVNALPECNADIVVVDEVSMCTNYDLSVINQRISYRHVVYVGDPQQLPAPRVMI
SQ  SRGTLEPKDYNVVTQRMCALKPDVFLHKCYRCPAEIVRTVSEMVYENQFIPVHPDSKQCFKIFCKGNVQVDNGSSINRRQ
SQ  LDVVRMFLAKNPRWSKAVFISPYNSQNYVASRLLGLQIQTVDSSQGSEYDYVIYAQTSDTAHASNVNRFNVAITRAKKGI
SQ  LCIMCDRSLFDLLKFFELKLSDLQANEGCGLFKDCSRGDDLLPPSHANTFMSLADNFKTDQYLAVQIGVNGPIKYEHVIS
SQ  FMGFRFDINIPNHHTLFCTRDFAMRNVRGWLGFDVEGAHVVGSNVGTNVPLQLGFSNGVDFVVRPEGCVVTESGDYIKPV
SQ  RARAPPGEQFAHLLPLLKRGQPWDVVRKRIVQMCSDYLANLSDILIFVLWAGGLELTTMRYFVKIGPSKSCDCGKVATCY
SQ  NSALHTYCCFKHALGCDYLYNPYCIDIQQWGYKGSLSLNHHEHCNVHRNEHVASGDAIMTRCLAIHDCFVKNVDWSITYP
SQ  FIGNEAVINKSGRIVQSHTMRSVLKLYNPKAIYDIGNPKGIRCAVTDAKWFCFDKNPTNSNVKTLEYDYITHGQFDGLCL
SQ  FWNCNVDMYPEFSVVCRFDTRCRSPLNLEGCNGGSLYVNNHAFHTPAFDKRAFAKLKPMPFFFYDDTECDKLQDSINYVP
SQ  LRASNCITKCNVGGAVCSKHCAMYHSYVNAYNTFTSAGFTIWVPTSFDTYNLWQTFSNNLQGLENIAFNVLKKGSFVGDE
SQ  GELPVAVVNDKVLVRDGTVDTLVFTNKTSLPTNVAFELYAKRKVGLTPPITILRNLGVVCTSKCVIWDYEAERPLTTFTK
SQ  DVCKYTDFEGDVCTLFDNSIVGSLERFSMTQNAVLMSLTAVKKLTGIKLTYGYLNGVPVNTHEDKPFTWYIYTRKNGKFE
SQ  DYPDGYFTQGRTTADFSPRSDMEKDFLSMDMGLFINKYGLEDYGFEHVVYGDVSKTTLGGLHLLISQVRLACMGVLKIDE
SQ  FVSSNDSTLKSCTVTYADNPSSKMVCTYMDLLLDDFVSILKSLDLSVVSKVHEVMVDCKMWRWMLWCKDHKLQTFYPQLQ
SQ  ASEWKCGYSMPSIYKIQRMCLEPCNLYNYGAGVKLPDGIMFNVVKYTQLCQYLNSTTMCVPHHMRVLHLGAGSDKGVAPG
SQ  TAVLRRWLPLDAIIVDNDSVDYVSDADYSVTGDCSTLYLSDKFDLVISDMYDGKIKSCDGENVSKEGFFPYINGVITEKL
SQ  ALGGTVAIKVTEFSWNKKLYELIQKFEYWTMFCTSVNTSSSEAFLIGVHYLGDFASGAVIDGNTMHANYIFWRNSTIMTM
SQ  SYNSVLDLSKFNCKHKATVVVNLKDSSISDVVLGLLKNGKLLVRNNDAICGFSNHLVNVNK
//
ID  P0C6X7;
PN  2'-O-methyltransferase nsp16;
GN  rep;
OS  694009;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 2]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endosome {ECO:0000250|UniProtKB:P0DTD1}. [Papain-like protease nsp3]: Host membrane {ECO:0000305}; Multi-pass membrane protein. Host cytoplasm {ECO:0000269|PubMed:23943763}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000269|PubMed:23943763}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles. {ECO:0000269|PubMed:17855519, ECO:0000269|PubMed:21345958, ECO:0000269|PubMed:23943763}. [3C-like proteinase nsp5]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host Golgi apparatus {ECO:0000250|UniProtKB:P0DTD1}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:17532020}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Helicase nsp13]: Host endoplasmic reticulum- Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. [Proofreading exoribonuclease nsp14]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. [Uridylate-specific endoribonuclease nsp15]: Host cytoplasm, host perinuclear region {ECO:0000250}.
DR  UNIPROT: P0C6X7;
DR  UNIPROT: P59641;
DR  UNIPROT: Q6WGN0;
DR  UNIPROT: Q7T697;
DR  UNIPROT: Q808C0;
DR  UNIPROT: Q80BV7;
DR  UNIPROT: Q80BV8;
DR  UNIPROT: Q80E51;
DR  PDB: 1Q2W;
DR  PDB: 1QZ8;
DR  PDB: 1UJ1;
DR  PDB: 1UK2;
DR  PDB: 1UK3;
DR  PDB: 1UK4;
DR  PDB: 1UW7;
DR  PDB: 1WOF;
DR  PDB: 1YSY;
DR  PDB: 1Z1I;
DR  PDB: 1Z1J;
DR  PDB: 2A5A;
DR  PDB: 2A5I;
DR  PDB: 2A5K;
DR  PDB: 2ACF;
DR  PDB: 2AHM;
DR  PDB: 2ALV;
DR  PDB: 2AMD;
DR  PDB: 2AMQ;
DR  PDB: 2BX3;
DR  PDB: 2BX4;
DR  PDB: 2C3S;
DR  PDB: 2D2D;
DR  PDB: 2DUC;
DR  PDB: 2FAV;
DR  PDB: 2FE8;
DR  PDB: 2FYG;
DR  PDB: 2G9T;
DR  PDB: 2GA6;
DR  PDB: 2GDT;
DR  PDB: 2GRI;
DR  PDB: 2GT7;
DR  PDB: 2GT8;
DR  PDB: 2GTB;
DR  PDB: 2GX4;
DR  PDB: 2GZ7;
DR  PDB: 2GZ8;
DR  PDB: 2GZ9;
DR  PDB: 2H2Z;
DR  PDB: 2H85;
DR  PDB: 2HOB;
DR  PDB: 2HSX;
DR  PDB: 2IDY;
DR  PDB: 2JZD;
DR  PDB: 2JZE;
DR  PDB: 2JZF;
DR  PDB: 2K7X;
DR  PDB: 2K87;
DR  PDB: 2OP9;
DR  PDB: 2OZK;
DR  PDB: 2PWX;
DR  PDB: 2Q6G;
DR  PDB: 2QC2;
DR  PDB: 2QCY;
DR  PDB: 2QIQ;
DR  PDB: 2RHB;
DR  PDB: 2RNK;
DR  PDB: 2V6N;
DR  PDB: 2VJ1;
DR  PDB: 2XYQ;
DR  PDB: 2XYR;
DR  PDB: 2XYV;
DR  PDB: 2Z3C;
DR  PDB: 2Z3D;
DR  PDB: 2Z3E;
DR  PDB: 2Z94;
DR  PDB: 2Z9G;
DR  PDB: 2Z9J;
DR  PDB: 2Z9K;
DR  PDB: 2Z9L;
DR  PDB: 3D62;
DR  PDB: 3E9S;
DR  PDB: 3EBN;
DR  PDB: 3R24;
DR  PDB: 4TWW;
DR  PDB: 4TWY;
DR  PDB: 4WY3;
DR  PDB: 4ZUH;
DR  PDB: 5B6O;
DR  PDB: 5C5N;
DR  PDB: 5C5O;
DR  PDB: 5C8S;
DR  PDB: 5C8T;
DR  PDB: 5C8U;
DR  PDB: 5E6J;
DR  PDB: 5F22;
DR  PDB: 5N19;
DR  PDB: 5N5O;
DR  PDB: 5NFY;
DR  PDB: 6JYT;
DR  PDB: 6LNQ;
DR  PDB: 6NUR;
DR  PDB: 6NUS;
DR  PDB: 6W79;
DR  PDB: 6WCO;
DR  PDB: 7LCP;
DR  PDB: 7LCQ;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF12379;
DR  Pfam: PF12124;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51653;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51940;
DE  Function: [Isoform Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371). {ECO:0000269|PubMed:23035226, ECO:0000269|PubMed:30943371}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (PubMed:19640993). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (PubMed:19640993). {ECO:0000269|PubMed:19640993}. [Papain-like protease nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein (PubMed:16306590). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:16306590, PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF- kappa-B signaling (PubMed:19369340, PubMed:24622840). {ECO:0000269|PubMed:16306590, ECO:0000269|PubMed:17692280, ECO:0000269|PubMed:19369340, ECO:0000269|PubMed:23943763, ECO:0000269|PubMed:24622840, ECO:0000303|PubMed:24410069}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes. Nsp3, nsp4 and nsp6 together are sufficient to form DMV. {ECO:0000269|PubMed:23943763, ECO:0000303|PubMed:24410069}. [3C-like proteinase nsp5]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH. {ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:16226257}. [Non-structural protein 6]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:24991833, PubMed:24410069). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24991833, PubMed:24410069). Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (PubMed:24991833). {ECO:0000269|PubMed:24991833, ECO:0000303|PubMed:24410069}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000269|PubMed:22039154}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000269|PubMed:22039154}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000269|PubMed:19153232}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000269|PubMed:22022266, ECO:0000269|PubMed:22635272}. [RNA-directed RNA polymerase nsp12]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000269|PubMed:22791111}. [Helicase nsp13]: Multi-functional protein with a zinc- binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000269|PubMed:12917423, ECO:0000269|PubMed:22615777}. [Proofreading exoribonuclease nsp14]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity (PubMed:16549795, PubMed:20421945, PubMed:22635272). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (PubMed:23966862, PubMed:29511076, PubMed:21593585). {ECO:0000269|PubMed:16549795, ECO:0000269|PubMed:20421945, ECO:0000269|PubMed:21593585, ECO:0000269|PubMed:22635272, ECO:0000269|PubMed:23966862, ECO:0000269|PubMed:29511076}. [Uridylate-specific endoribonuclease nsp15]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (PubMed:28158275, PubMed:18045871). Acts by degrading the 5'- polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (PubMed:16828802). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (PubMed:28158275, PubMed:18045871). {ECO:0000269|PubMed:16828802, ECO:0000269|PubMed:18045871, ECO:0000269|PubMed:28158275}. [2'-O-methyltransferase nsp16]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs (PubMed:18417574, PubMed:22022266, PubMed:20421945). N7- methyl guanosine cap is a prerequisite for binding of nsp16 (PubMed:18417574). Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system (PubMed:18417574, PubMed:22022266, PubMed:20421945). {ECO:0000269|PubMed:18417574, ECO:0000269|PubMed:20421945, ECO:0000269|PubMed:22022266, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N638; IntAct: EBI-26366798; Score: 0.44
DE  Interaction: K9N7C7; IntAct: EBI-25758227; Score: 0.44
DE  Interaction: O15182; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: O75821; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: P0C6U8; IntAct: EBI-25492630; Score: 0.51
DE  Interaction: O75348; IntAct: EBI-7843859; Score: 0.66
DE  Interaction: P0C6X7; IntAct: EBI-25490398; Score: 0.89
DE  Interaction: P62937; IntAct: EBI-25488476; Score: 0.51
DE  Interaction: Q9UQN3; IntAct: EBI-25488518; Score: 0.51
DE  Interaction: Q5SQN1; IntAct: EBI-25488935; Score: 0.51
DE  Interaction: Q9Y4W2; IntAct: EBI-25488511; Score: 0.51
DE  Interaction: Q9UKA8; IntAct: EBI-25488504; Score: 0.51
DE  Interaction: O43447; IntAct: EBI-25488497; Score: 0.51
DE  Interaction: Q13427; IntAct: EBI-25488490; Score: 0.51
DE  Interaction: P62942; IntAct: EBI-25488483; Score: 0.51
DE  Interaction: O95299; IntAct: EBI-25489287; Score: 0.40
DE  Interaction: Q8TD31; IntAct: EBI-25488553; Score: 0.55
DE  Interaction: P20231; IntAct: EBI-25488546; Score: 0.37
DE  Interaction: P30876; IntAct: EBI-25488539; Score: 0.37
DE  Interaction: Q15661; IntAct: EBI-25489276; Score: 0.40
DE  Interaction: Q99471; IntAct: EBI-25489298; Score: 0.40
DE  Interaction: Q99426; IntAct: EBI-25488574; Score: 0.37
DE  Interaction: P51948; IntAct: EBI-25488581; Score: 0.37
DE  Interaction: Q13064; IntAct: EBI-25488700; Score: 0.51
DE  Interaction: P09630; IntAct: EBI-25488588; Score: 0.37
DE  Interaction: Q8N488; IntAct: EBI-25488595; Score: 0.51
DE  Interaction: P27448; IntAct: EBI-25488602; Score: 0.37
DE  Interaction: Q7KZI7; IntAct: EBI-25488609; Score: 0.37
DE  Interaction: O96017; IntAct: EBI-25488616; Score: 0.51
DE  Interaction: P05155; IntAct: EBI-25488644; Score: 0.51
DE  Interaction: Q56VL3; IntAct: EBI-25488630; Score: 0.37
DE  Interaction: Q92802; IntAct: EBI-25488637; Score: 0.37
DE  Interaction: Q13561; IntAct: EBI-25488651; Score: 0.37
DE  Interaction: Q8WXF8; IntAct: EBI-25488665; Score: 0.37
DE  Interaction: Q9H000; IntAct: EBI-25488693; Score: 0.51
DE  Interaction: Q7Z3Q1; IntAct: EBI-25488686; Score: 0.37
DE  Interaction: Q7Z494; IntAct: EBI-25488679; Score: 0.37
DE  Interaction: Q13564; IntAct: EBI-25488825; Score: 0.37
DE  Interaction: A9UHW6; IntAct: EBI-25488818; Score: 0.51
DE  Interaction: P62258; IntAct: EBI-25488811; Score: 0.37
DE  Interaction: Q9HCD5; IntAct: EBI-25488804; Score: 0.37
DE  Interaction: P49703; IntAct: EBI-25488797; Score: 0.37
DE  Interaction: Q92560; IntAct: EBI-25488790; Score: 0.37
DE  Interaction: Q8TEB7; IntAct: EBI-25488783; Score: 0.37
DE  Interaction: O95865; IntAct: EBI-25488776; Score: 0.51
DE  Interaction: O14498; IntAct: EBI-25488769; Score: 0.37
DE  Interaction: Q9GZN8; IntAct: EBI-25488762; Score: 0.37
DE  Interaction: P23025; IntAct: EBI-25488755; Score: 0.37
DE  Interaction: P08949; IntAct: EBI-25488727; Score: 0.37
DE  Interaction: Q96GS6; IntAct: EBI-25489377; Score: 0.40
DE  Interaction: Q86VK4; IntAct: EBI-25488707; Score: 0.37
DE  Interaction: Q53GL0; IntAct: EBI-25488844; Score: 0.37
DE  Interaction: P13796; IntAct: EBI-25488851; Score: 0.37
DE  Interaction: Q6P587; IntAct: EBI-25488921; Score: 0.37
DE  Interaction: P23588; IntAct: EBI-25488893; Score: 0.37
DE  Interaction: P54274; IntAct: EBI-25488879; Score: 0.51
DE  Interaction: Q9P0M6; IntAct: EBI-25488872; Score: 0.51
DE  Interaction: Q9Y6E2; IntAct: EBI-25488865; Score: 0.37
DE  Interaction: P69849; IntAct: EBI-25488858; Score: 0.51
DE  Interaction: Q9BUV0; IntAct: EBI-25488907; Score: 0.37
DE  Interaction: P06733; IntAct: EBI-25488928; Score: 0.37
DE  Interaction: P23284; IntAct: EBI-25475813; Score: 0.40
DE  Interaction: P20290; IntAct: EBI-25487623; Score: 0.37
DE  Interaction: P03901; IntAct: EBI-25487628; Score: 0.37
DE  Interaction: P00403; IntAct: EBI-25487633; Score: 0.37
DE  Interaction: Q9Y2D1; IntAct: EBI-25487647; Score: 0.37
DE  Interaction: P59632; IntAct: EBI-25492642; Score: 0.51
DE  Interaction: P59636; IntAct: EBI-25492804; Score: 0.51
DE  Interaction: Q7TFA0; IntAct: EBI-25492912; Score: 0.37
DE  Interaction: P59637; IntAct: EBI-25635717; Score: 0.54
DE  Interaction: Q80H93; IntAct: EBI-25492945; Score: 0.37
DE  Interaction: Q7TLC7; IntAct: EBI-25493011; Score: 0.37
DE  Interaction: P59635; IntAct: EBI-25493519; Score: 0.37
DE  Interaction: Q19QW5; IntAct: EBI-25635410; Score: 0.61
DE  Interaction: P08865; IntAct: EBI-25507413; Score: 0.37
DE  Interaction: P62879; IntAct: EBI-25507431; Score: 0.37
DE  Interaction: Q15047; IntAct: EBI-25507450; Score: 0.37
DE  Interaction: Q9NY15; IntAct: EBI-25507454; Score: 0.37
DE  Interaction: Q9BW92; IntAct: EBI-25507458; Score: 0.37
DE  Interaction: P40337; IntAct: EBI-25507462; Score: 0.60
DE  Interaction: O95433; IntAct: EBI-25507466; Score: 0.37
DE  Interaction: Q8TF42; IntAct: EBI-25507481; Score: 0.37
DE  Interaction: Q0VD86; IntAct: EBI-25507485; Score: 0.37
DE  Interaction: Q14653; IntAct: EBI-25498708; Score: 0.66
DE  Interaction: Q5JRX3; IntAct: EBI-25507493; Score: 0.37
DE  Interaction: Q99873; IntAct: EBI-25507497; Score: 0.37
DE  Interaction: P62487; IntAct: EBI-25507501; Score: 0.37
DE  Interaction: Q9BTC0; IntAct: EBI-25507472; Score: 0.35
DE  Interaction: Q93009; IntAct: EBI-25507472; Score: 0.35
DE  Interaction: Q6IEG0; IntAct: EBI-25507472; Score: 0.35
DE  Interaction: P78345; IntAct: EBI-25507472; Score: 0.35
DE  Interaction: P35250; IntAct: EBI-25507472; Score: 0.35
DE  Interaction: O75131; IntAct: EBI-25507472; Score: 0.35
DE  Interaction: Q14008; IntAct: EBI-25507472; Score: 0.53
DE  Interaction: Q6Y7W6; IntAct: EBI-25507801; Score: 0.53
DE  Interaction: P21796; IntAct: EBI-25507801; Score: 0.35
DE  Interaction: Q9UJZ1; IntAct: EBI-25507801; Score: 0.64
DE  Interaction: Q96T58; IntAct: EBI-25507801; Score: 0.35
DE  Interaction: Q15758; IntAct: EBI-25507801; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-25507801; Score: 0.64
DE  Interaction: P35232; IntAct: EBI-25507801; Score: 0.64
DE  Interaction: Q15154; IntAct: EBI-25507801; Score: 0.35
DE  Interaction: O14686; IntAct: EBI-25507801; Score: 0.35
DE  Interaction: O60573; IntAct: EBI-25507801; Score: 0.64
DE  Interaction: Q7L2H7; IntAct: EBI-25507801; Score: 0.53
DE  Interaction: Q15751; IntAct: EBI-25688256; Score: 0.40
DE  Interaction: Q9BRX9; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: Q9NZM4; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: Q9H9G7; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: Q9BT78; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: Q99798; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: Q8TDY2; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: Q6NWY9; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: Q15631; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: Q15532; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: Q13228; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: P55786; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: P52756; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: P49903; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: P40925; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: P28066; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: P25789; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: P07954; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: O76064; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: O15498; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: O14979; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: O14732; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: O00268; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: P09525; IntAct: EBI-25688210; Score: 0.35
DE  Interaction: A6NHR9; IntAct: EBI-25688210; Score: 0.35
DE  Interaction: O75781; IntAct: EBI-25688221; Score: 0.35
DE  Interaction: P07858; IntAct: EBI-25688221; Score: 0.35
DE  Interaction: Q16719; IntAct: EBI-25688245; Score: 0.35
DE  Interaction: O43570; IntAct: EBI-25688245; Score: 0.35
DE  Interaction: Q86TG7; IntAct: EBI-25688201; Score: 0.40
DE  Interaction: P06400; IntAct: EBI-25684934; Score: 0.56
DE  Interaction: Q86WV6; IntAct: EBI-25751009; Score: 0.40
DE  Interaction: Q9UHD2; IntAct: EBI-25751044; Score: 0.40
DE  Interaction: AY394850.2; IntAct: EBI-25752076; Score: 0.44
DE  Interaction: P0C6Y0; IntAct: EBI-25758199; Score: 0.44
DE  Interaction: P0C6Y5; IntAct: EBI-25758300; Score: 0.44
DE  Interaction: Q98VG9; IntAct: EBI-25758361; Score: 0.44
DE  Interaction: P0C6Y1; IntAct: EBI-25758560; Score: 0.44
DE  Interaction: Q9Y657; IntAct: EBI-25762307; Score: 0.35
DE  Interaction: Q96K19; IntAct: EBI-25762307; Score: 0.35
DE  Interaction: Q9UBN7; IntAct: EBI-25762307; Score: 0.35
DE  Interaction: O94905; IntAct: EBI-25762307; Score: 0.35
DE  Interaction: O75477; IntAct: EBI-25762307; Score: 0.35
DE  Interaction: P51798; IntAct: EBI-25762307; Score: 0.35
DE  Interaction: Q8N4V1; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: P62699; IntAct: EBI-25762541; Score: 0.53
DE  Interaction: Q9H7D7; IntAct: EBI-25762541; Score: 0.53
DE  Interaction: Q9BQB6; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q99942; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q9H871; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q96S59; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q6VN20; IntAct: EBI-25762541; Score: 0.53
DE  Interaction: Q9UKZ9; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: O75592; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q9UL63; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q7L5Y9; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q13907; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q15011; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q9NWU2; IntAct: EBI-25762541; Score: 0.53
DE  Interaction: P0C2W1; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q9ULG6; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q8IUR7; IntAct: EBI-25762541; Score: 0.35
DE  Interaction: Q13557; IntAct: EBI-25825454; Score: 0.57
DE  Interaction: Q96PM5; IntAct: EBI-25825454; Score: 0.59
DE  Interaction: P04637; IntAct: EBI-25825787; Score: 0.35
DE  Interaction: Q92499; IntAct: EBI-25827273; Score: 0.40
DE  Interaction: P49643; IntAct: EBI-26376937; Score: 0.53
DE  Interaction: P49642; IntAct: EBI-26376937; Score: 0.53
DE  Interaction: P09884; IntAct: EBI-26376937; Score: 0.53
DE  Interaction: Q14181; IntAct: EBI-26376937; Score: 0.53
DE  Interaction: Q969X5; IntAct: EBI-26376953; Score: 0.35
DE  Interaction: Q6Q0C0; IntAct: EBI-26376953; Score: 0.35
DE  Interaction: O15078; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q9HCJ0; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q9HAU0; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q9H2H8; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q96M11; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q96IZ5; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q92908; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q92615; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q8IWR0; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q86SQ0; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q70EL1; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q6ZRI6; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q6UUV7; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q5VUA4; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q5EBL8; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q4KMZ1; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q2T9J0; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q2NL68; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q13948; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q13615; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q13546; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: Q13033; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: O95391; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: O75506; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: O43303; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: O15014; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: A3KN83; IntAct: EBI-26376977; Score: 0.35
DE  Interaction: P17612; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9Y2I6; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q8WWI1; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q8N4C6; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9Y608; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9Y4I1; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9UPQ0; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9UPN4; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9UM54; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9ULV0; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9H0E2; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9BZF9; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9BV73; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9BV19; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9BQQ3; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q99996; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q96SN8; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q96N16; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q96II8; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q92995; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q8WXW3; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q8TD10; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q8IUD2; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q7Z406; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q6ZVM7; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q66GS9; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q5VUJ6; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q5VU43; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q5VT06; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q14789; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q13045; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q12965; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q08378; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q04726; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q04724; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: P67936; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: P35241; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: P28289; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: P14649; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: P13861; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: P09493; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: P06396; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: O95684; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: O95613; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: O75381; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: O60784; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: O60237; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: O14908; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: O14639; IntAct: EBI-26377017; Score: 0.35
DE  Interaction: Q9NXA8; IntAct: EBI-26377088; Score: 0.35
DE  Interaction: Q96JN8; IntAct: EBI-26377088; Score: 0.35
DE  Interaction: P12268; IntAct: EBI-26377088; Score: 0.35
DE  Interaction: P06280; IntAct: EBI-26377088; Score: 0.35
DE  Interaction: O95714; IntAct: EBI-26377088; Score: 0.35
DE  Interaction: P62330; IntAct: EBI-26377105; Score: 0.40
DE  Interaction: Q9Y2S7; IntAct: EBI-26377113; Score: 0.35
DE  Interaction: Q9UKF6; IntAct: EBI-26377113; Score: 0.35
DE  Interaction: Q8TEM1; IntAct: EBI-26377113; Score: 0.35
DE  Interaction: Q5SVZ6; IntAct: EBI-26377113; Score: 0.35
DE  Interaction: Q567U6; IntAct: EBI-26377113; Score: 0.35
DE  Interaction: P28838; IntAct: EBI-26377113; Score: 0.35
DE  Interaction: O60232; IntAct: EBI-26377113; Score: 0.35
DE  Interaction: Q13347; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: P55884; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: O15371; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: Q9Y262; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: Q9UBQ5; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: Q9C037; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: Q99613; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: Q86UK7; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: Q6NUN9; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: Q14152; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: P60228; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: P52306; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: O75822; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: O15372; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: O00303; IntAct: EBI-26377128; Score: 0.35
DE  Interaction: P14735; IntAct: EBI-26377154; Score: 0.35
DE  Interaction: P07203; IntAct: EBI-26377169; Score: 0.35
DE  Interaction: Q9NXH9; IntAct: EBI-26377169; Score: 0.35
DE  Interaction: Q99720; IntAct: EBI-26377180; Score: 0.40
DE  Interaction: Q9Y3D7; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q9NYP7; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q9H7Z7; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q9BQE4; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q96KC8; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q96ER9; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q96A26; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q8WUY8; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q8WTV0; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q8NBX0; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q8IUR0; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q7LGA3; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q6ZRP7; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q6P1Q0; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q5VT66; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q2TAA5; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q12907; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: P61006; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: P00387; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: O94766; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: A8MTT3; IntAct: EBI-26377188; Score: 0.35
DE  Interaction: Q9BSC4; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q9Y3B7; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q9NQT5; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q9NQT4; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q8NEJ9; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: P82675; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q9ULT8; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q9UL40; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q9UGI8; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q9NY61; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q9H6F5; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q96FK6; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q96B26; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q8N983; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q8IY37; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q7L2J0; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q4G0J3; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q15397; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q14692; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: Q13206; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: P09132; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: O95260; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: O76094; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: O00566; IntAct: EBI-26377216; Score: 0.35
DE  Interaction: P35556; IntAct: EBI-26377247; Score: 0.35
DE  Interaction: Q8TD19; IntAct: EBI-26377247; Score: 0.35
DE  Interaction: Q8N1G2; IntAct: EBI-26377247; Score: 0.35
DE  Interaction: Q8N0X7; IntAct: EBI-26377247; Score: 0.35
DE  Interaction: Q86YT6; IntAct: EBI-26377247; Score: 0.35
DE  Interaction: Q14232; IntAct: EBI-26377247; Score: 0.35
DE  Interaction: P61962; IntAct: EBI-26377247; Score: 0.35
DE  Interaction: O00142; IntAct: EBI-26377247; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-26451065; Score: 0.40
DE  Interaction: Q64339; IntAct: EBI-26583749; Score: 0.56
DE  Interaction: P0CG48; IntAct: EBI-26585786; Score: 0.56
DE  Interaction: P31151; IntAct: EBI-26584254; Score: 0.35
DE  Interaction: P05109; IntAct: EBI-26584254; Score: 0.35
DE  Interaction: P59665; IntAct: EBI-26584254; Score: 0.35
DE  Interaction: P07339; IntAct: EBI-26584254; Score: 0.35
DE  Interaction: P47929; IntAct: EBI-26584254; Score: 0.35
DE  Interaction: Q96P63; IntAct: EBI-26584254; Score: 0.35
DE  Interaction: P48594; IntAct: EBI-26584254; Score: 0.35
DE  Interaction: P29508; IntAct: EBI-26584254; Score: 0.35
DE  Interaction: P06702; IntAct: EBI-26584254; Score: 0.35
DE  Interaction: P05161; IntAct: EBI-26584341; Score: 0.54
DE  Interaction: P25963; IntAct: EBI-26585885; Score: 0.44
DE  Interaction: Q13616; IntAct: EBI-26585276; Score: 0.44
DE  Interaction: Q9BYX4; IntAct: EBI-26895226; Score: 0.40
DE  Interaction: Q96C36; IntAct: EBI-27129499; Score: 0.46
DE  Interaction: P32322; IntAct: EBI-27129499; Score: 0.46
DE  Interaction: Q96CT2; IntAct: EBI-27128638; Score: 0.35
DE  Interaction: Q93008; IntAct: EBI-27128638; Score: 0.35
DE  Interaction: Q9HA64; IntAct: EBI-27128638; Score: 0.35
DE  Interaction: A3KMH1; IntAct: EBI-27128638; Score: 0.35
DE  Interaction: Q9UKK9; IntAct: EBI-27128638; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-27128638; Score: 0.35
DE  Interaction: Q7Z4H7; IntAct: EBI-27128638; Score: 0.35
DE  Interaction: P78344; IntAct: EBI-27128638; Score: 0.35
DE  Interaction: Q96CW1; IntAct: EBI-30605858; Score: 0.40
GO  GO:0039714;
GO  GO:0062243;
GO  GO:1905369;
GO  GO:1902555;
GO  GO:1905354;
GO  GO:0030430;
GO  GO:0044165;
GO  GO:0044172;
GO  GO:0044174;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0031533;
GO  GO:0031381;
GO  GO:0000175;
GO  GO:0032574;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0003725;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0004386;
GO  GO:0042802;
GO  GO:0019785;
GO  GO:0016829;
GO  GO:1990380;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0046983;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006370;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0080009;
GO  GO:1902680;
GO  GO:2000158;
GO  GO:0045070;
GO  GO:0039690;
GO  GO:0016540;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0016485;
GO  GO:0006508;
GO  GO:0090503;
GO  GO:0001172;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039722;
GO  GO:0039547;
GO  GO:0039604;
GO  GO:0039501;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019082;
GO  GO:0046786;
GO  GO:0039694;
GO  GO:0019083;
TP  Membrane Topology: Transmembrane; Source: UniProt - Curator Inference {ECO:0000305|PubMed:18842706};
SQ  MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTN
SQ  HGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELGTDPIEDYEQN
SQ  WNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAW
SQ  FTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVASPQECNNMHLSTL
SQ  MKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKG
SQ  GRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFHLNEEVAIILASF
SQ  SASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIP
SQ  DLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAYVTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVE
SQ  FLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQC
SQ  IRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYC
SQ  ALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAV
SQ  VKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGL
SQ  PLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAAN
SQ  IHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQD
SQ  ILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQK
SQ  PVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSK
SQ  KAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEE
SQ  TRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAAR
SQ  CMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVE
SQ  FHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPS
SQ  DDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRAR
SQ  AGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGV
SQ  SIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPV
SQ  TDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQ
SQ  MTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSN
SQ  SFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENT
SQ  SITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFT
SQ  KSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYC
SQ  NGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGL
SQ  SAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVEC
SQ  TTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHL
SQ  YFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDS
SQ  TEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDL
SQ  EVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLT
SQ  CATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIIST
SQ  DDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLI
SQ  EYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEY
SQ  CRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYY
SQ  FMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAI
SQ  YVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDT
SQ  TSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPR
SQ  HVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNG
SQ  SPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTI
SQ  TLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRT
SQ  ILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAA
SQ  CAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDD
SQ  AARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVY
SQ  CFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMS
SQ  DVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINRLCEEMLDNRATLQA
SQ  IASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRA
SQ  KVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVD
SQ  ADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLA
SQ  LLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPAN
SQ  STVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFC
SQ  DLKGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPLMQSADASTFLNRVCGVSAARLTPCGTGTSTDVV
SQ  YRAFDIYNEKVAGFAKFLKTNCCRFQEKDEEGNLLDSYFVVKRHTMSNYQHEETIYNLVKDCPAVAVHDFFKFRVDGDMV
SQ  PHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQSLLKTVQ
SQ  FCDAMRDAGIVGVLTLDNQDLNGNWYDFGDFVQVAPGCGVPIVDSYYSLLMPILTLTRALAAESHMDADLAKPLIKWDLL
SQ  KYDFTEERLCLFDRYFKYWDQTYHPNCINCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFREL
SQ  GVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKE
SQ  GSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGK
SQ  ARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGT
SQ  SKFYGGWHNMLKTVYSDVETPHLMGWDYPKCDRAMPNMLRIMASLVLARKHNTCCNLSHRFYRLANECAQVLSEMVMCGG
SQ  SLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDHEFVDEFYAYLRK
SQ  HFSMMILSDDAVVCYNSNYAAQGLVASIKNFKAVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPY
SQ  PDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDN
SQ  TSRYWEPEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTD
SQ  VTQLYLGGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLK
SQ  ATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKL
SQ  NVGDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYY
SQ  PSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMA
SQ  TNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDN
SQ  KLKAHKDKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGS
SQ  EYDYVIFTQTTETAHSCNVNRFNVAITRAKIGILCIMSDRDLYDKLQFTSLEIPRRNVATLQAENVTGLFKDCSKIITGL
SQ  HPTQAPTHLSVDIKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFITREEAIRHVRAWIGFDVEGCHATR
SQ  DAVGTNLPLQLGFSTGVNLVAVPTGYVDTENNTEFTRVNAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSDTLKGLS
SQ  DRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDKRATCFSTSSDTYACWNHSVGFDYVYNPFMIDVQQWGFTGNLQSNHD
SQ  QHCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWSVEYPIIGDELRVNSACRKVQHMVVKSALLADKFPVLHDIGNPKAI
SQ  KCVPQAEVEWKFYDAQPCSDKAYKIEELFYSYATHHDKFTDGVCLFWNCNVDRYPANAIVCRFDTRVLSNLNLPGCDGGS
SQ  LYVNKHAFHTPAFDKSAFTNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRHHANEYRQYLDAY
SQ  NMMISAGFSLWIYKQFDTYNLWNTFTRLQSLENVAYNVVNKGHFDGHAGEAPVSIINNAVYTKVDGIDVEIFENKTTLPV
SQ  NVAFELWAKRNIKPVPEIKILNNLGVDIAANTVIWDYKREAPAHVSTIGVCTMTDIAKKPTESACSSLTVLFDGRVEGQV
SQ  DLFRNARNGVLITEGSVKGLTPSKGPAQASVNGVTLIGESVKTQFNYFKKVDGIIQQLPETYFTQSRDLEDFKPRSQMET
SQ  DFLELAMDEFIQRYKLEGYAFEHIVYGDFSHGQLGGLHLMIGLAKRSQDSPLKLEDFIPMDSTVKNYFITDAQTGSSKCV
SQ  CSVIDLLLDDFVEIIKSQDLSVISKVVKVTIDYAEISFMLWCKDGHVETFYPKLQASQAWQPGVAMPNLYKMQRMLLEKC
SQ  DLQNYGENAVIPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGTAVLRQWLPTGTLLVDSDLNDFVS
SQ  DADSTLIGDCATVHTANKWDLIISDMYDPRTKHVTKENDSKEGFFTYLCGFIKQKLALGGSIAVKITEHSWNADLYKLMG
SQ  HFSWWTAFVTNVNASSSEAFLIGANYLGKPKEQIDGYTMHANYIFWRNTNPIQLSSYSLFDMSKFPLKLRGTAVMSLKEN
SQ  QINDMIYSLLEKGRLIIRENNRVVVSSDILVNN
//
ID  P0DTD1;
PN  2'-O-methyltransferase nsp16;
GN  rep;
OS  2697049;
SL  Nucleus Position: SL-0382;
SL  Comments: [Host translation inhibitor nsp1]: Host cytoplasm {ECO:0000269|PubMed:33060197}. [Non-structural protein 2]: Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endosome {ECO:0000269|PubMed:33060197}. [Papain-like protease nsp3]: Host membrane {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32763915}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32763915}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase nsp5]: Host cytoplasm {ECO:0000269|PubMed:33060197}. Host Golgi apparatus {ECO:0000269|PubMed:33060197}. [Non-structural protein 6]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:33080218}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:33080218}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. [Proofreading exoribonuclease nsp14]: Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum. [Helicase nsp13]: Host endoplasmic reticulum- Golgi intermediate compartment {ECO:0000250|UniProtKB:P0C6X7}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250|UniProtKB:P0C6X9}. [Uridylate-specific endoribonuclease nsp15]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. [2'-O-methyltransferase nsp16]: Host nucleus. Host cytoplasm {ECO:0000269|PubMed:33080218}.
DR  UNIPROT: P0DTD1;
DR  PDB: 5R7Y;
DR  PDB: 5R7Z;
DR  PDB: 5R80;
DR  PDB: 5R81;
DR  PDB: 5R82;
DR  PDB: 5R83;
DR  PDB: 5R84;
DR  PDB: 5R8T;
DR  PDB: 5RE4;
DR  PDB: 5RE5;
DR  PDB: 5RE6;
DR  PDB: 5RE7;
DR  PDB: 5RE8;
DR  PDB: 5RE9;
DR  PDB: 5REA;
DR  PDB: 5REB;
DR  PDB: 5REC;
DR  PDB: 5RED;
DR  PDB: 5REE;
DR  PDB: 5REF;
DR  PDB: 5REG;
DR  PDB: 5REH;
DR  PDB: 5REI;
DR  PDB: 5REJ;
DR  PDB: 5REK;
DR  PDB: 5REL;
DR  PDB: 5REM;
DR  PDB: 5REN;
DR  PDB: 5REO;
DR  PDB: 5REP;
DR  PDB: 5RER;
DR  PDB: 5RES;
DR  PDB: 5RET;
DR  PDB: 5REU;
DR  PDB: 5REV;
DR  PDB: 5REW;
DR  PDB: 5REX;
DR  PDB: 5REY;
DR  PDB: 5REZ;
DR  PDB: 5RF0;
DR  PDB: 5RF1;
DR  PDB: 5RF2;
DR  PDB: 5RF3;
DR  PDB: 5RF4;
DR  PDB: 5RF5;
DR  PDB: 5RF6;
DR  PDB: 5RF7;
DR  PDB: 5RF8;
DR  PDB: 5RF9;
DR  PDB: 5RFA;
DR  PDB: 5RFB;
DR  PDB: 5RFC;
DR  PDB: 5RFD;
DR  PDB: 5RFE;
DR  PDB: 5RFF;
DR  PDB: 5RFG;
DR  PDB: 5RFH;
DR  PDB: 5RFI;
DR  PDB: 5RFJ;
DR  PDB: 5RFK;
DR  PDB: 5RFL;
DR  PDB: 5RFM;
DR  PDB: 5RFN;
DR  PDB: 5RFO;
DR  PDB: 5RFP;
DR  PDB: 5RFQ;
DR  PDB: 5RFR;
DR  PDB: 5RFS;
DR  PDB: 5RFT;
DR  PDB: 5RFU;
DR  PDB: 5RFV;
DR  PDB: 5RFW;
DR  PDB: 5RFX;
DR  PDB: 5RFY;
DR  PDB: 5RFZ;
DR  PDB: 5RG0;
DR  PDB: 5RG1;
DR  PDB: 5RG2;
DR  PDB: 5RG3;
DR  PDB: 5RGG;
DR  PDB: 5RGH;
DR  PDB: 5RGI;
DR  PDB: 5RGJ;
DR  PDB: 5RGK;
DR  PDB: 5RGL;
DR  PDB: 5RGM;
DR  PDB: 5RGN;
DR  PDB: 5RGO;
DR  PDB: 5RGP;
DR  PDB: 5RGQ;
DR  PDB: 5RGR;
DR  PDB: 5RGS;
DR  PDB: 5RGT;
DR  PDB: 5RGU;
DR  PDB: 5RGV;
DR  PDB: 5RGW;
DR  PDB: 5RGX;
DR  PDB: 5RGY;
DR  PDB: 5RGZ;
DR  PDB: 5RH0;
DR  PDB: 5RH1;
DR  PDB: 5RH2;
DR  PDB: 5RH3;
DR  PDB: 5RH4;
DR  PDB: 5RH5;
DR  PDB: 5RH6;
DR  PDB: 5RH7;
DR  PDB: 5RH8;
DR  PDB: 5RH9;
DR  PDB: 5RHA;
DR  PDB: 5RHB;
DR  PDB: 5RHC;
DR  PDB: 5RHD;
DR  PDB: 5RHE;
DR  PDB: 5RHF;
DR  PDB: 5RL0;
DR  PDB: 5RL1;
DR  PDB: 5RL2;
DR  PDB: 5RL3;
DR  PDB: 5RL4;
DR  PDB: 5RL5;
DR  PDB: 5RL6;
DR  PDB: 5RL7;
DR  PDB: 5RL8;
DR  PDB: 5RL9;
DR  PDB: 5RLB;
DR  PDB: 5RLC;
DR  PDB: 5RLD;
DR  PDB: 5RLE;
DR  PDB: 5RLF;
DR  PDB: 5RLG;
DR  PDB: 5RLH;
DR  PDB: 5RLI;
DR  PDB: 5RLJ;
DR  PDB: 5RLK;
DR  PDB: 5RLL;
DR  PDB: 5RLM;
DR  PDB: 5RLN;
DR  PDB: 5RLO;
DR  PDB: 5RLP;
DR  PDB: 5RLQ;
DR  PDB: 5RLR;
DR  PDB: 5RLS;
DR  PDB: 5RLT;
DR  PDB: 5RLU;
DR  PDB: 5RLV;
DR  PDB: 5RLW;
DR  PDB: 5RLY;
DR  PDB: 5RLZ;
DR  PDB: 5RM0;
DR  PDB: 5RM1;
DR  PDB: 5RM2;
DR  PDB: 5RM3;
DR  PDB: 5RM4;
DR  PDB: 5RM5;
DR  PDB: 5RM6;
DR  PDB: 5RM7;
DR  PDB: 5RM8;
DR  PDB: 5RM9;
DR  PDB: 5RMA;
DR  PDB: 5RMB;
DR  PDB: 5RMC;
DR  PDB: 5RMD;
DR  PDB: 5RME;
DR  PDB: 5RMF;
DR  PDB: 5RMG;
DR  PDB: 5RMH;
DR  PDB: 5RMI;
DR  PDB: 5RMJ;
DR  PDB: 5RMK;
DR  PDB: 5RML;
DR  PDB: 5RMM;
DR  PDB: 5ROB;
DR  PDB: 5RS7;
DR  PDB: 5RS8;
DR  PDB: 5RS9;
DR  PDB: 5RSB;
DR  PDB: 5RSC;
DR  PDB: 5RSD;
DR  PDB: 5RSE;
DR  PDB: 5RSF;
DR  PDB: 5RSG;
DR  PDB: 5RSH;
DR  PDB: 5RSI;
DR  PDB: 5RSJ;
DR  PDB: 5RSK;
DR  PDB: 5RSL;
DR  PDB: 5RSM;
DR  PDB: 5RSN;
DR  PDB: 5RSO;
DR  PDB: 5RSP;
DR  PDB: 5RSQ;
DR  PDB: 5RSR;
DR  PDB: 5RSS;
DR  PDB: 5RST;
DR  PDB: 5RSU;
DR  PDB: 5RSV;
DR  PDB: 5RSW;
DR  PDB: 5RSX;
DR  PDB: 5RSY;
DR  PDB: 5RSZ;
DR  PDB: 5RT0;
DR  PDB: 5RT1;
DR  PDB: 5RT2;
DR  PDB: 5RT3;
DR  PDB: 5RT4;
DR  PDB: 5RT5;
DR  PDB: 5RT6;
DR  PDB: 5RT7;
DR  PDB: 5RT8;
DR  PDB: 5RT9;
DR  PDB: 5RTA;
DR  PDB: 5RTB;
DR  PDB: 5RTC;
DR  PDB: 5RTD;
DR  PDB: 5RTE;
DR  PDB: 5RTF;
DR  PDB: 5RTG;
DR  PDB: 5RTH;
DR  PDB: 5RTI;
DR  PDB: 5RTJ;
DR  PDB: 5RTK;
DR  PDB: 5RTL;
DR  PDB: 5RTM;
DR  PDB: 5RTN;
DR  PDB: 5RTO;
DR  PDB: 5RTP;
DR  PDB: 5RTQ;
DR  PDB: 5RTR;
DR  PDB: 5RTS;
DR  PDB: 5RTT;
DR  PDB: 5RTU;
DR  PDB: 5RTV;
DR  PDB: 5RTW;
DR  PDB: 5RTX;
DR  PDB: 5RTY;
DR  PDB: 5RTZ;
DR  PDB: 5RU0;
DR  PDB: 5RU1;
DR  PDB: 5RU2;
DR  PDB: 5RU3;
DR  PDB: 5RU4;
DR  PDB: 5RU5;
DR  PDB: 5RU6;
DR  PDB: 5RU7;
DR  PDB: 5RU8;
DR  PDB: 5RU9;
DR  PDB: 5RUA;
DR  PDB: 5RUC;
DR  PDB: 5RUD;
DR  PDB: 5RUE;
DR  PDB: 5RUF;
DR  PDB: 5RUG;
DR  PDB: 5RUH;
DR  PDB: 5RUI;
DR  PDB: 5RUJ;
DR  PDB: 5RUK;
DR  PDB: 5RUL;
DR  PDB: 5RUM;
DR  PDB: 5RUN;
DR  PDB: 5RUO;
DR  PDB: 5RUP;
DR  PDB: 5RUQ;
DR  PDB: 5RUR;
DR  PDB: 5RUS;
DR  PDB: 5RUT;
DR  PDB: 5RUU;
DR  PDB: 5RUV;
DR  PDB: 5RUW;
DR  PDB: 5RUX;
DR  PDB: 5RUY;
DR  PDB: 5RUZ;
DR  PDB: 5RV0;
DR  PDB: 5RV1;
DR  PDB: 5RV2;
DR  PDB: 5RV3;
DR  PDB: 5RV4;
DR  PDB: 5RV5;
DR  PDB: 5RV6;
DR  PDB: 5RV7;
DR  PDB: 5RV8;
DR  PDB: 5RV9;
DR  PDB: 5RVA;
DR  PDB: 5RVB;
DR  PDB: 5RVC;
DR  PDB: 5RVD;
DR  PDB: 5RVE;
DR  PDB: 5RVF;
DR  PDB: 5RVG;
DR  PDB: 5RVH;
DR  PDB: 5RVI;
DR  PDB: 5RVJ;
DR  PDB: 5RVK;
DR  PDB: 5RVL;
DR  PDB: 5RVM;
DR  PDB: 5RVN;
DR  PDB: 5RVO;
DR  PDB: 5RVP;
DR  PDB: 5RVQ;
DR  PDB: 5RVR;
DR  PDB: 5RVS;
DR  PDB: 5RVT;
DR  PDB: 5RVU;
DR  PDB: 5RVV;
DR  PDB: 5S18;
DR  PDB: 5S1A;
DR  PDB: 5S1C;
DR  PDB: 5S1E;
DR  PDB: 5S1G;
DR  PDB: 5S1I;
DR  PDB: 5S1K;
DR  PDB: 5S1M;
DR  PDB: 5S1O;
DR  PDB: 5S1Q;
DR  PDB: 5S1S;
DR  PDB: 5S1U;
DR  PDB: 5S1W;
DR  PDB: 5S1Y;
DR  PDB: 5S20;
DR  PDB: 5S22;
DR  PDB: 5S24;
DR  PDB: 5S26;
DR  PDB: 5S27;
DR  PDB: 5S28;
DR  PDB: 5S29;
DR  PDB: 5S2A;
DR  PDB: 5S2B;
DR  PDB: 5S2C;
DR  PDB: 5S2D;
DR  PDB: 5S2E;
DR  PDB: 5S2F;
DR  PDB: 5S2G;
DR  PDB: 5S2H;
DR  PDB: 5S2I;
DR  PDB: 5S2J;
DR  PDB: 5S2K;
DR  PDB: 5S2L;
DR  PDB: 5S2M;
DR  PDB: 5S2N;
DR  PDB: 5S2O;
DR  PDB: 5S2P;
DR  PDB: 5S2Q;
DR  PDB: 5S2R;
DR  PDB: 5S2S;
DR  PDB: 5S2T;
DR  PDB: 5S2U;
DR  PDB: 5S2V;
DR  PDB: 5S2W;
DR  PDB: 5S2X;
DR  PDB: 5S2Y;
DR  PDB: 5S2Z;
DR  PDB: 5S30;
DR  PDB: 5S31;
DR  PDB: 5S32;
DR  PDB: 5S33;
DR  PDB: 5S34;
DR  PDB: 5S35;
DR  PDB: 5S36;
DR  PDB: 5S37;
DR  PDB: 5S38;
DR  PDB: 5S39;
DR  PDB: 5S3A;
DR  PDB: 5S3B;
DR  PDB: 5S3C;
DR  PDB: 5S3D;
DR  PDB: 5S3E;
DR  PDB: 5S3F;
DR  PDB: 5S3G;
DR  PDB: 5S3H;
DR  PDB: 5S3I;
DR  PDB: 5S3J;
DR  PDB: 5S3K;
DR  PDB: 5S3L;
DR  PDB: 5S3M;
DR  PDB: 5S3N;
DR  PDB: 5S3O;
DR  PDB: 5S3P;
DR  PDB: 5S3Q;
DR  PDB: 5S3R;
DR  PDB: 5S3S;
DR  PDB: 5S3T;
DR  PDB: 5S3U;
DR  PDB: 5S3V;
DR  PDB: 5S3W;
DR  PDB: 5S3X;
DR  PDB: 5S3Y;
DR  PDB: 5S3Z;
DR  PDB: 5S40;
DR  PDB: 5S41;
DR  PDB: 5S42;
DR  PDB: 5S43;
DR  PDB: 5S44;
DR  PDB: 5S45;
DR  PDB: 5S46;
DR  PDB: 5S47;
DR  PDB: 5S48;
DR  PDB: 5S49;
DR  PDB: 5S4A;
DR  PDB: 5S4B;
DR  PDB: 5S4C;
DR  PDB: 5S4D;
DR  PDB: 5S4E;
DR  PDB: 5S4F;
DR  PDB: 5S4G;
DR  PDB: 5S4H;
DR  PDB: 5S4I;
DR  PDB: 5S4J;
DR  PDB: 5S4K;
DR  PDB: 5S6X;
DR  PDB: 5S6Y;
DR  PDB: 5S6Z;
DR  PDB: 5S70;
DR  PDB: 5S71;
DR  PDB: 5S72;
DR  PDB: 5S73;
DR  PDB: 5S74;
DR  PDB: 5SA4;
DR  PDB: 5SA5;
DR  PDB: 5SA6;
DR  PDB: 5SA7;
DR  PDB: 5SA8;
DR  PDB: 5SA9;
DR  PDB: 5SAA;
DR  PDB: 5SAB;
DR  PDB: 5SAC;
DR  PDB: 5SAD;
DR  PDB: 5SAE;
DR  PDB: 5SAF;
DR  PDB: 5SAG;
DR  PDB: 5SAH;
DR  PDB: 5SAI;
DR  PDB: 5SBF;
DR  PDB: 5SKW;
DR  PDB: 5SKX;
DR  PDB: 5SKY;
DR  PDB: 5SKZ;
DR  PDB: 5SL0;
DR  PDB: 5SL1;
DR  PDB: 5SL2;
DR  PDB: 5SL3;
DR  PDB: 5SL4;
DR  PDB: 5SL5;
DR  PDB: 5SL6;
DR  PDB: 5SL7;
DR  PDB: 5SL8;
DR  PDB: 5SL9;
DR  PDB: 5SLA;
DR  PDB: 5SLB;
DR  PDB: 5SLC;
DR  PDB: 5SLD;
DR  PDB: 5SLE;
DR  PDB: 5SLF;
DR  PDB: 5SLG;
DR  PDB: 5SLH;
DR  PDB: 5SLI;
DR  PDB: 5SLJ;
DR  PDB: 5SLK;
DR  PDB: 5SLL;
DR  PDB: 5SLM;
DR  PDB: 5SLN;
DR  PDB: 5SLO;
DR  PDB: 5SLP;
DR  PDB: 5SLQ;
DR  PDB: 5SLR;
DR  PDB: 5SLS;
DR  PDB: 5SLT;
DR  PDB: 5SLU;
DR  PDB: 5SLV;
DR  PDB: 5SLW;
DR  PDB: 5SLX;
DR  PDB: 5SLY;
DR  PDB: 5SLZ;
DR  PDB: 5SM0;
DR  PDB: 5SM1;
DR  PDB: 5SM2;
DR  PDB: 5SM3;
DR  PDB: 5SM4;
DR  PDB: 5SM5;
DR  PDB: 5SM6;
DR  PDB: 5SM7;
DR  PDB: 5SM8;
DR  PDB: 5SM9;
DR  PDB: 5SMA;
DR  PDB: 5SMB;
DR  PDB: 5SMC;
DR  PDB: 5SMD;
DR  PDB: 5SME;
DR  PDB: 5SMF;
DR  PDB: 5SMG;
DR  PDB: 5SMH;
DR  PDB: 5SMI;
DR  PDB: 5SMK;
DR  PDB: 6LU7;
DR  PDB: 6LZE;
DR  PDB: 6M03;
DR  PDB: 6M0K;
DR  PDB: 6M2N;
DR  PDB: 6M2Q;
DR  PDB: 6M71;
DR  PDB: 6VWW;
DR  PDB: 6VXS;
DR  PDB: 6W01;
DR  PDB: 6W02;
DR  PDB: 6W4B;
DR  PDB: 6W4H;
DR  PDB: 6W61;
DR  PDB: 6W63;
DR  PDB: 6W6Y;
DR  PDB: 6W75;
DR  PDB: 6W9C;
DR  PDB: 6W9Q;
DR  PDB: 6WC1;
DR  PDB: 6WCF;
DR  PDB: 6WEN;
DR  PDB: 6WEY;
DR  PDB: 6WIQ;
DR  PDB: 6WJT;
DR  PDB: 6WKQ;
DR  PDB: 6WKS;
DR  PDB: 6WLC;
DR  PDB: 6WNP;
DR  PDB: 6WOJ;
DR  PDB: 6WQ3;
DR  PDB: 6WQD;
DR  PDB: 6WQF;
DR  PDB: 6WRH;
DR  PDB: 6WRZ;
DR  PDB: 6WTC;
DR  PDB: 6WTJ;
DR  PDB: 6WTK;
DR  PDB: 6WTM;
DR  PDB: 6WTT;
DR  PDB: 6WUU;
DR  PDB: 6WVN;
DR  PDB: 6WX4;
DR  PDB: 6WXC;
DR  PDB: 6WXD;
DR  PDB: 6WZU;
DR  PDB: 6X1B;
DR  PDB: 6X4I;
DR  PDB: 6XA4;
DR  PDB: 6XA9;
DR  PDB: 6XAA;
DR  PDB: 6XB0;
DR  PDB: 6XB1;
DR  PDB: 6XB2;
DR  PDB: 6XBG;
DR  PDB: 6XBH;
DR  PDB: 6XBI;
DR  PDB: 6XCH;
DR  PDB: 6XDH;
DR  PDB: 6XFN;
DR  PDB: 6XG3;
DR  PDB: 6XHM;
DR  PDB: 6XHU;
DR  PDB: 6XIP;
DR  PDB: 6XKF;
DR  PDB: 6XKH;
DR  PDB: 6XKM;
DR  PDB: 6XMK;
DR  PDB: 6XOA;
DR  PDB: 6XQS;
DR  PDB: 6XQT;
DR  PDB: 6XQU;
DR  PDB: 6XR3;
DR  PDB: 6Y2E;
DR  PDB: 6Y2F;
DR  PDB: 6Y2G;
DR  PDB: 6Y84;
DR  PDB: 6YB7;
DR  PDB: 6YNQ;
DR  PDB: 6YVA;
DR  PDB: 6YVF;
DR  PDB: 6YWK;
DR  PDB: 6YWL;
DR  PDB: 6YWM;
DR  PDB: 6YYT;
DR  PDB: 6YZ1;
DR  PDB: 6Z2E;
DR  PDB: 6Z5T;
DR  PDB: 6Z6I;
DR  PDB: 6Z72;
DR  PDB: 6ZCT;
DR  PDB: 6ZLW;
DR  PDB: 6ZM7;
DR  PDB: 6ZME;
DR  PDB: 6ZMI;
DR  PDB: 6ZMO;
DR  PDB: 6ZMT;
DR  PDB: 6ZN5;
DR  PDB: 6ZOJ;
DR  PDB: 6ZOK;
DR  PDB: 6ZON;
DR  PDB: 6ZP4;
DR  PDB: 6ZPE;
DR  PDB: 6ZRT;
DR  PDB: 6ZRU;
DR  PDB: 6ZSL;
DR  PDB: 7A1U;
DR  PDB: 7ABU;
DR  PDB: 7ADW;
DR  PDB: 7AEG;
DR  PDB: 7AEH;
DR  PDB: 7AF0;
DR  PDB: 7AGA;
DR  PDB: 7AHA;
DR  PDB: 7AK4;
DR  PDB: 7AKU;
DR  PDB: 7ALH;
DR  PDB: 7ALI;
DR  PDB: 7AMJ;
DR  PDB: 7ANS;
DR  PDB: 7AOL;
DR  PDB: 7AP6;
DR  PDB: 7APH;
DR  PDB: 7AQE;
DR  PDB: 7AQI;
DR  PDB: 7AQJ;
DR  PDB: 7AR5;
DR  PDB: 7AR6;
DR  PDB: 7ARF;
DR  PDB: 7AU4;
DR  PDB: 7AVD;
DR  PDB: 7AWR;
DR  PDB: 7AWS;
DR  PDB: 7AWU;
DR  PDB: 7AWW;
DR  PDB: 7AX6;
DR  PDB: 7AXM;
DR  PDB: 7AXO;
DR  PDB: 7AY7;
DR  PDB: 7B2J;
DR  PDB: 7B2U;
DR  PDB: 7B3E;
DR  PDB: 7B5Z;
DR  PDB: 7B77;
DR  PDB: 7B83;
DR  PDB: 7BAJ;
DR  PDB: 7BAK;
DR  PDB: 7BAL;
DR  PDB: 7BB2;
DR  PDB: 7BE7;
DR  PDB: 7BF3;
DR  PDB: 7BF4;
DR  PDB: 7BF5;
DR  PDB: 7BF6;
DR  PDB: 7BFB;
DR  PDB: 7BGP;
DR  PDB: 7BIJ;
DR  PDB: 7BQ7;
DR  PDB: 7BQY;
DR  PDB: 7BRO;
DR  PDB: 7BRP;
DR  PDB: 7BTF;
DR  PDB: 7BUY;
DR  PDB: 7BV1;
DR  PDB: 7BV2;
DR  PDB: 7BWQ;
DR  PDB: 7BZF;
DR  PDB: 7C2I;
DR  PDB: 7C2J;
DR  PDB: 7C2K;
DR  PDB: 7C2Q;
DR  PDB: 7C2Y;
DR  PDB: 7C6S;
DR  PDB: 7C6U;
DR  PDB: 7C7P;
DR  PDB: 7C8B;
DR  PDB: 7C8R;
DR  PDB: 7C8T;
DR  PDB: 7C8U;
DR  PDB: 7CA8;
DR  PDB: 7CAM;
DR  PDB: 7CB7;
DR  PDB: 7CBT;
DR  PDB: 7CJD;
DR  PDB: 7CJM;
DR  PDB: 7CMD;
DR  PDB: 7COM;
DR  PDB: 7CUT;
DR  PDB: 7CUU;
DR  PDB: 7CWB;
DR  PDB: 7CWC;
DR  PDB: 7CX9;
DR  PDB: 7D1M;
DR  PDB: 7D1O;
DR  PDB: 7D7K;
DR  PDB: 7D7L;
DR  PDB: 7DDC;
DR  PDB: 7DG6;
DR  PDB: 7DIY;
DR  PDB: 7DVX;
DR  PDB: 7DVY;
DR  PDB: 7DW0;
DR  PDB: 7DW6;
DR  PDB: 7E18;
DR  PDB: 7E19;
DR  PDB: 7E5X;
DR  PDB: 7E6K;
DR  PDB: 7EQ4;
DR  PDB: 7JFQ;
DR  PDB: 7JHE;
DR  PDB: 7JIB;
DR  PDB: 7JKV;
DR  PDB: 7JME;
DR  PDB: 7JOY;
DR  PDB: 7JP0;
DR  PDB: 7JP1;
DR  PDB: 7JPE;
DR  PDB: 7JPY;
DR  PDB: 7JPZ;
DR  PDB: 7JQ0;
DR  PDB: 7JQ1;
DR  PDB: 7JQ2;
DR  PDB: 7JQ3;
DR  PDB: 7JQ4;
DR  PDB: 7JQ5;
DR  PDB: 7JQB;
DR  PDB: 7JQC;
DR  PDB: 7JR3;
DR  PDB: 7JR4;
DR  PDB: 7JST;
DR  PDB: 7JSU;
DR  PDB: 7JT0;
DR  PDB: 7JT7;
DR  PDB: 7JU7;
DR  PDB: 7JUN;
DR  PDB: 7JVZ;
DR  PDB: 7JW8;
DR  PDB: 7JYC;
DR  PDB: 7JYY;
DR  PDB: 7JZ0;
DR  PDB: 7K0E;
DR  PDB: 7K0F;
DR  PDB: 7K0R;
DR  PDB: 7K1L;
DR  PDB: 7K1O;
DR  PDB: 7K3N;
DR  PDB: 7K3T;
DR  PDB: 7K40;
DR  PDB: 7K5I;
DR  PDB: 7K6D;
DR  PDB: 7K6E;
DR  PDB: 7K7P;
DR  PDB: 7K9P;
DR  PDB: 7KAG;
DR  PDB: 7KEG;
DR  PDB: 7KEH;
DR  PDB: 7KF4;
DR  PDB: 7KFI;
DR  PDB: 7KG3;
DR  PDB: 7KHP;
DR  PDB: 7KOA;
DR  PDB: 7KPH;
DR  PDB: 7KQO;
DR  PDB: 7KQP;
DR  PDB: 7KQW;
DR  PDB: 7KR0;
DR  PDB: 7KR1;
DR  PDB: 7KRI;
DR  PDB: 7KVL;
DR  PDB: 7KVR;
DR  PDB: 7KX5;
DR  PDB: 7KXB;
DR  PDB: 7KYU;
DR  PDB: 7L0D;
DR  PDB: 7L10;
DR  PDB: 7L11;
DR  PDB: 7L12;
DR  PDB: 7L13;
DR  PDB: 7L14;
DR  PDB: 7L1F;
DR  PDB: 7L5D;
DR  PDB: 7L6R;
DR  PDB: 7L6T;
DR  PDB: 7L8I;
DR  PDB: 7L8J;
DR  PDB: 7LB7;
DR  PDB: 7LBN;
DR  PDB: 7LBR;
DR  PDB: 7LBS;
DR  PDB: 7LCO;
DR  PDB: 7LCS;
DR  PDB: 7LCT;
DR  PDB: 7LDL;
DR  PDB: 7LDX;
DR  PDB: 7LFE;
DR  PDB: 7LFP;
DR  PDB: 7LFZ;
DR  PDB: 7LG2;
DR  PDB: 7LG3;
DR  PDB: 7LG7;
DR  PDB: 7LGO;
DR  PDB: 7LHQ;
DR  PDB: 7LKD;
DR  PDB: 7LKE;
DR  PDB: 7LKR;
DR  PDB: 7LKS;
DR  PDB: 7LKT;
DR  PDB: 7LKU;
DR  PDB: 7LKV;
DR  PDB: 7LKW;
DR  PDB: 7LKX;
DR  PDB: 7LLF;
DR  PDB: 7LLZ;
DR  PDB: 7LMD;
DR  PDB: 7LME;
DR  PDB: 7LMF;
DR  PDB: 7LOS;
DR  PDB: 7LTJ;
DR  PDB: 7LTN;
DR  PDB: 7LW3;
DR  PDB: 7LW4;
DR  PDB: 7LYH;
DR  PDB: 7LYI;
DR  PDB: 7LZT;
DR  PDB: 7LZU;
DR  PDB: 7LZV;
DR  PDB: 7LZW;
DR  PDB: 7LZX;
DR  PDB: 7LZY;
DR  PDB: 7LZZ;
DR  PDB: 7M00;
DR  PDB: 7M01;
DR  PDB: 7M02;
DR  PDB: 7M03;
DR  PDB: 7M04;
DR  PDB: 7M2P;
DR  PDB: 7M8M;
DR  PDB: 7M8N;
DR  PDB: 7M8O;
DR  PDB: 7M8P;
DR  PDB: 7M8X;
DR  PDB: 7M8Y;
DR  PDB: 7M8Z;
DR  PDB: 7M90;
DR  PDB: 7M91;
DR  PDB: 7MBG;
DR  PDB: 7MBI;
DR  PDB: 7MC5;
DR  PDB: 7MC6;
DR  PDB: 7ME0;
DR  PDB: 7MGR;
DR  PDB: 7MGS;
DR  PDB: 7MHF;
DR  PDB: 7MHG;
DR  PDB: 7MHH;
DR  PDB: 7MHI;
DR  PDB: 7MHJ;
DR  PDB: 7MHK;
DR  PDB: 7MHL;
DR  PDB: 7MHM;
DR  PDB: 7MHN;
DR  PDB: 7MHO;
DR  PDB: 7MHP;
DR  PDB: 7MHQ;
DR  PDB: 7MLF;
DR  PDB: 7MLG;
DR  PDB: 7MNG;
DR  PDB: 7MPB;
DR  PDB: 7MRR;
DR  PDB: 7MSW;
DR  PDB: 7MSX;
DR  PDB: 7N06;
DR  PDB: 7N0B;
DR  PDB: 7N0C;
DR  PDB: 7N0D;
DR  PDB: 7N33;
DR  PDB: 7N3K;
DR  PDB: 7N44;
DR  PDB: 7N5Z;
DR  PDB: 7N6N;
DR  PDB: 7N7R;
DR  PDB: 7N7U;
DR  PDB: 7N7W;
DR  PDB: 7N7Y;
DR  PDB: 7N83;
DR  PDB: 7N89;
DR  PDB: 7N8C;
DR  PDB: 7NBR;
DR  PDB: 7NBS;
DR  PDB: 7NBT;
DR  PDB: 7NBY;
DR  PDB: 7NEO;
DR  PDB: 7NEV;
DR  PDB: 7NF5;
DR  PDB: 7NFV;
DR  PDB: 7NG3;
DR  PDB: 7NG6;
DR  PDB: 7NIO;
DR  PDB: 7NN0;
DR  PDB: 7NNG;
DR  PDB: 7NT4;
DR  PDB: 7NTS;
DR  PDB: 7O46;
DR  PDB: 7O7Y;
DR  PDB: 7O7Z;
DR  PDB: 7O80;
DR  PDB: 7O81;
DR  PDB: 7ORR;
DR  PDB: 7ORU;
DR  PDB: 7ORV;
DR  PDB: 7ORW;
DR  PDB: 7QBB;
DR  PDB: 7QGI;
DR  PDB: 7QIF;
DR  PDB: 7R2V;
DR  PDB: 7R7H;
DR  PDB: 7RB0;
DR  PDB: 7RB2;
DR  PDB: 7RBZ;
DR  PDB: 7RC0;
DR  PDB: 7RFR;
DR  PDB: 7RFS;
DR  PDB: 7RFU;
DR  PDB: 7RFW;
DR  PDB: 7RLS;
DR  PDB: 7RM2;
DR  PDB: 7RMB;
DR  PDB: 7RME;
DR  PDB: 7RMT;
DR  PDB: 7RMZ;
DR  PDB: 7RN0;
DR  PDB: 7RN1;
DR  PDB: 7RN4;
DR  PDB: 7RNH;
DR  PDB: 7RNK;
DR  PDB: 7RNW;
DR  PDB: 7RQG;
DR  PDB: 7S3K;
DR  PDB: 7S3S;
DR  PDB: 7S4B;
DR  PDB: 7S82;
DR  PDB: 7SI9;
DR  PDB: 7T42;
DR  PDB: 7T43;
DR  PDB: 7T44;
DR  PDB: 7T45;
DR  PDB: 7T46;
DR  PDB: 7T48;
DR  PDB: 7T49;
DR  PDB: 7T4A;
DR  PDB: 7T4B;
DR  PDB: 7T9W;
DR  PDB: 7TDU;
DR  PDB: 7TE0;
DR  PDB: 7TEH;
DR  PDB: 7TFR;
DR  PDB: 7THH;
DR  PDB: 7TI9;
DR  PDB: 7TJ2;
DR  PDB: 7TQ5;
DR  PDB: 7TQ6;
DR  PDB: 7TQV;
DR  PDB: 7TWF;
DR  PDB: 7TWG;
DR  PDB: 7TWH;
DR  PDB: 7TWI;
DR  PDB: 7TWJ;
DR  PDB: 7TWN;
DR  PDB: 7TWO;
DR  PDB: 7TWP;
DR  PDB: 7TWQ;
DR  PDB: 7TWR;
DR  PDB: 7TWS;
DR  PDB: 7TWT;
DR  PDB: 7TWV;
DR  PDB: 7TWW;
DR  PDB: 7TWX;
DR  PDB: 7TWY;
DR  PDB: 7TX0;
DR  PDB: 7TX1;
DR  PDB: 7TX3;
DR  PDB: 7TX4;
DR  PDB: 7TX5;
DR  PDB: 7ULT;
DR  PDB: 7VAH;
DR  PDB: 7WOH;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF12379;
DR  Pfam: PF12124;
DR  Pfam: PF11633;
DR  Pfam: PF06471;
DR  Pfam: PF06460;
DR  Pfam: PF09401;
DR  Pfam: PF19215;
DR  Pfam: PF19216;
DR  Pfam: PF19219;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF06478;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51961;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51954;
DR  PROSITE: PS51962;
DR  PROSITE: PS52000;
DR  PROSITE: PS51948;
DR  PROSITE: PS51960;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS00867;
DR  PROSITE: PS51653;
DR  PROSITE: PS00213;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51955;
DR  PROSITE: PS51953;
DR  PROSITE: PS51124;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DR  PROSITE: PS51940;
DE  Function: [Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by associating with the open head conformation of the 40S subunit (PubMed:33479166, PubMed:33080218, PubMed:32680882, PubMed:32908316). The C-terminus binds to and obstructs ribosomal mRNA entry tunnel (PubMed:33479166, PubMed:33080218, PubMed:32680882, PubMed:32908316). Thereby inhibits antiviral response triggered by innate immunity or interferons (PubMed:33080218, PubMed:32680882, PubMed:32979938). The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation (By similarity). Viral mRNAs less susceptible to nsp1-mediated inhibition of translation, because of their 5'-end leader sequence (PubMed:32908316, PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32680882, ECO:0000269|PubMed:32908316, ECO:0000269|PubMed:32979938, ECO:0000269|PubMed:33080218, ECO:0000269|PubMed:33479166}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like protease nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication (By similarity). Forms a molecular pore spanning the double membrane of the coronavirus replication organelle (PubMed:32763915). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:32733001). Prevents also host NF-kappa-B signaling (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:32726803). Cleaves preferentially ISG15 from antiviral protein IFIH1 (MDA5), but not DDX58 (RIG-I) (PubMed:33727702). Can play a role in host ADP-ribosylation by binding ADP-ribose (PubMed:32578982). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32578982, ECO:0000269|PubMed:32726803, ECO:0000269|PubMed:32733001, ECO:0000269|PubMed:32763915, ECO:0000269|PubMed:33727702}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase nsp5]: Cleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481). Also able to bind an ADP-ribose- 1''-phosphate (ADRP) (By similarity) (PubMed:32198291, PubMed:32272481). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481, ECO:0000269|PubMed:32321856}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic (By similarity). Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (By similarity). Binds to host TBK1 without affecting TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32979938}. [Non-structural protein 7]: Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}. [Non-structural protein 8]: Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity). Interacts with ribosome signal recognition particle RNA (SRP) (PubMed:33080218). Together with NSP9, suppress protein integration into the cell membrane, thereby disrupting host immune defenses (PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33080218}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein (By similarity). Interacts with ribosome signal recognition particle RNA (SRP) (PubMed:33080218). Together with NSP9, suppress protein integration into the cell membrane, thereby disrupting host immune defenses (PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:33080218}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. [RNA-directed RNA polymerase nsp12]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000305|PubMed:32277040, ECO:0000305|PubMed:32358203, ECO:0000305|PubMed:32438371, ECO:0000305|PubMed:32526208}. [Helicase nsp13]: Multi-functional protein with a zinc- binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium (By similarity). Binds to host TBK1 and inhibits TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32979938}. [Proofreading exoribonuclease nsp14]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens. {ECO:0000250|UniProtKB:P0C6X7}. [Uridylate-specific endoribonuclease nsp15]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs (PubMed:33504779, PubMed:33564093). Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (PubMed:33504779, PubMed:33564093). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:33504779}. [2'-O-methyltransferase nsp16]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs (By similarity). N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system (By similarity). May disrupt host mRNA splicing in nucleus by interacting with pre-mRNA Recognition Domains ofthe U1 and U2 snRNAs (PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:33080218}.
DE  Reference Proteome: Yes;
DE  Interaction: A0PK00; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O14657; IntAct: EBI-27050247; Score: 0.35
DE  Interaction: O75312; IntAct: EBI-27128112; Score: 0.27
DE  Interaction: O75569; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: O75821; IntAct: EBI-27128043; Score: 0.27
DE  Interaction: O95831; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: P04406; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: P0DTC7; IntAct: EBI-25508859; Score: 0.62
DE  Interaction: Q14181; IntAct: EBI-25490637; Score: 0.67
DE  Interaction: P49643; IntAct: EBI-25490637; Score: 0.64
DE  Interaction: P49642; IntAct: EBI-25490637; Score: 0.64
DE  Interaction: P09884; IntAct: EBI-25490637; Score: 0.67
DE  Interaction: Q99959; IntAct: EBI-25490637; Score: 0.53
DE  Interaction: Q8NBJ5; IntAct: EBI-25490637; Score: 0.53
DE  Interaction: Q9HAV7; IntAct: EBI-25490661; Score: 0.53
DE  Interaction: Q96CW1; IntAct: EBI-25490661; Score: 0.53
DE  Interaction: Q969X5; IntAct: EBI-25490661; Score: 0.53
DE  Interaction: P55789; IntAct: EBI-25490661; Score: 0.53
DE  Interaction: O94973; IntAct: EBI-25490661; Score: 0.53
DE  Interaction: Q9HAU0; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q9H2H8; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q99081; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q96IZ5; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q92615; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q8IWR0; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q70EL1; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q6UUV7; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q5VUA4; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q5T6F2; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q5JSZ5; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q5EBL8; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q2T9J0; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q14157; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: Q13546; IntAct: EBI-25490691; Score: 0.72
DE  Interaction: O95391; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: O75592; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: O43823; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: O14874; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: A3KN83; IntAct: EBI-25490691; Score: 0.53
DE  Interaction: P17612; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: O14578; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q9Y2I6; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q9UJC3; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q9UHD2; IntAct: EBI-25490757; Score: 0.82
DE  Interaction: Q9BV73; IntAct: EBI-26950012; Score: 0.56
DE  Interaction: Q9BV19; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q9BQS8; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q9BQQ3; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q99996; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q96SN8; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q96N16; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q96CN9; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q92995; IntAct: EBI-25490757; Score: 0.67
DE  Interaction: Q8TD10; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q8N8E3; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q8N4C6; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q8N3C7; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q8IWJ2; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q8IUD2; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q7Z7A1; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q76N32; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q66GS9; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q5VU43; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q5VT06; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q4V328; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q14789; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q08379; IntAct: EBI-26950045; Score: 0.56
DE  Interaction: Q08378; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q08117; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q04726; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q04724; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: P49454; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: P35241; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: P31323; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: P13861; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: O95684; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: O95613; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: O75506; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: A7MCY6; IntAct: EBI-25490757; Score: 0.53
DE  Interaction: Q9NXA8; IntAct: EBI-25490883; Score: 0.64
DE  Interaction: P12268; IntAct: EBI-25490883; Score: 0.53
DE  Interaction: P06280; IntAct: EBI-25490883; Score: 0.53
DE  Interaction: P07203; IntAct: EBI-25490979; Score: 0.53
DE  Interaction: Q9NXH9; IntAct: EBI-25490979; Score: 0.53
DE  Interaction: Q9H7F0; IntAct: EBI-25490993; Score: 0.73
DE  Interaction: Q99720; IntAct: EBI-25490993; Score: 0.73
DE  Interaction: Q15904; IntAct: EBI-25490993; Score: 0.83
DE  Interaction: O75964; IntAct: EBI-25490993; Score: 0.53
DE  Interaction: Q92769; IntAct: EBI-25490970; Score: 0.59
DE  Interaction: Q8WVC6; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q9NP72; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q9H7Z7; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q9BQE4; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q96DA6; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q96A26; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q8WUY8; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q8WTV0; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q8NBX0; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q8N183; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q7LGA3; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q6ZRP7; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q5VT66; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q5JTV8; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q13724; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q12907; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P63218; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P62873; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P62820; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P61586; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P61106; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P61026; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P61019; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P61006; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P51149; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P51148; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P21964; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P11233; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P00387; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: O95573; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: O43169; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: O00116; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q9H4P4; IntAct: EBI-25490898; Score: 0.53
DE  Interaction: P62330; IntAct: EBI-25490898; Score: 0.53
DE  Interaction: P61970; IntAct: EBI-25490898; Score: 0.53
DE  Interaction: Q6Y7W6; IntAct: EBI-25490913; Score: 0.64
DE  Interaction: Q5T1M5; IntAct: EBI-25490913; Score: 0.64
DE  Interaction: Q2M389; IntAct: EBI-25490913; Score: 0.53
DE  Interaction: P52306; IntAct: EBI-25490913; Score: 0.78
DE  Interaction: P16435; IntAct: EBI-25490913; Score: 0.53
DE  Interaction: O60573; IntAct: EBI-25490913; Score: 0.53
DE  Interaction: O14975; IntAct: EBI-25490913; Score: 0.53
DE  Interaction: Q9Y5J7; IntAct: EBI-25490940; Score: 0.53
DE  Interaction: Q9Y5J6; IntAct: EBI-25490940; Score: 0.53
DE  Interaction: Q9NVH1; IntAct: EBI-25490940; Score: 0.53
DE  Interaction: Q9BSF4; IntAct: EBI-25490940; Score: 0.53
DE  Interaction: Q8TEM1; IntAct: EBI-25490940; Score: 0.53
DE  Interaction: Q2TAA5; IntAct: EBI-25490940; Score: 0.53
DE  Interaction: P62072; IntAct: EBI-25490940; Score: 0.53
DE  Interaction: P14735; IntAct: EBI-25490940; Score: 0.53
DE  Interaction: Q9HD40; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q9BSC4; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q92552; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q13868; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: P82675; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q9Y399; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q9ULT8; IntAct: EBI-25491113; Score: 0.64
DE  Interaction: Q9NY61; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q9NQT5; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q9NQT4; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q9H6F5; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q96I59; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q96B26; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q8NEJ9; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q7L2J0; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q4G0J3; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: Q13206; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: P82663; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: P61011; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: P09132; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: O96028; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: O95260; IntAct: EBI-25491113; Score: 0.64
DE  Interaction: O76094; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: O00566; IntAct: EBI-25491113; Score: 0.53
DE  Interaction: P35556; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: Q9UBX5; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: Q9NZL9; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: Q9BVL2; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: Q99567; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: Q96F45; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: Q8TD19; IntAct: EBI-25491191; Score: 0.64
DE  Interaction: Q8N0X7; IntAct: EBI-25491191; Score: 0.64
DE  Interaction: Q86YT6; IntAct: EBI-25491191; Score: 0.67
DE  Interaction: Q7Z3B4; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: Q15056; IntAct: EBI-25491191; Score: 0.64
DE  Interaction: P61962; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: P37198; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: P35658; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: P35555; IntAct: EBI-25491191; Score: 0.53
DE  Interaction: P13984; IntAct: EBI-25491191; Score: 0.73
DE  Interaction: P0DTD1; IntAct: EBI-25506373; Score: 0.99
DE  Interaction: P0DTD8; IntAct: EBI-25508759; Score: 0.55
DE  Interaction: P0DTC9; IntAct: EBI-27052424; Score: 0.66
DE  Interaction: P0DTC3; IntAct: EBI-26953433; Score: 0.49
DE  Interaction: P0DTC6; IntAct: EBI-26953705; Score: 0.49
DE  Interaction: P0DTC8; IntAct: EBI-25508863; Score: 0.37
DE  Interaction: O15226; IntAct: EBI-25508881; Score: 0.50
DE  Interaction: P55884; IntAct: EBI-25508895; Score: 0.53
DE  Interaction: P08865; IntAct: EBI-25508895; Score: 0.53
DE  Interaction: P60228; IntAct: EBI-25508895; Score: 0.53
DE  Interaction: P35251; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: P46782; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: P46783; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: O76021; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: Q9BUJ2; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: Q9BZE4; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: O95757; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: P82650; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: P53007; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: P26599; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: P05023; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: P34932; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: O00411; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: Q9UNQ2; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: Q9H0A0; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: Q96CS3; IntAct: EBI-25508903; Score: 0.35
DE  Interaction: P63244; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P06576; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: P31689; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P25705; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P25205; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P22314; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P53621; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P61158; IntAct: EBI-25509935; Score: 0.40
DE  Interaction: Q16875; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: Q9UM54; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: Q06787; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: P62195; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: P62269; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: Q96N67; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: P19105; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: P60660; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: P35998; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: Q9NTJ3; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: Q9NZ01; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: Q16891; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: Q9P035; IntAct: EBI-25509444; Score: 0.35
DE  Interaction: P09012; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: P35250; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q9NXF1; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q9H5H4; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: P16989; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: P25398; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q14498; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q9UHX1; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q9NW13; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: O43660; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q7Z2T5; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: O15381; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q9NX58; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: O43395; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q13610; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q9UKD2; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: P11387; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q86UE4; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q9UJV9; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q13523; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: P42696; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: O95104; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q8N5C6; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q9GZR7; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q12788; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: P40938; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q9HC36; IntAct: EBI-25509501; Score: 0.35
DE  Interaction: Q8NC51; IntAct: EBI-25509548; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-25509566; Score: 0.35
DE  Interaction: P57088; IntAct: EBI-25509566; Score: 0.35
DE  Interaction: P55786; IntAct: EBI-25509566; Score: 0.35
DE  Interaction: O43592; IntAct: EBI-25509566; Score: 0.35
DE  Interaction: O14980; IntAct: EBI-25509566; Score: 0.35
DE  Interaction: P30043; IntAct: EBI-25509566; Score: 0.35
DE  Interaction: Q99460; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: P53396; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: P22234; IntAct: EBI-27092549; Score: 0.44
DE  Interaction: Q9NNW5; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: P06733; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: O95347; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: P47756; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: Q13200; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: P52907; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: Q9ULV4; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: Q9NYL9; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: P00338; IntAct: EBI-25509603; Score: 0.35
DE  Interaction: P11586; IntAct: EBI-25509669; Score: 0.53
DE  Interaction: Q07021; IntAct: EBI-25509669; Score: 0.35
DE  Interaction: Q14315; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: Q16576; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: O00148; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: Q15366; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: Q15942; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: Q92945; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: Q99615; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: P51570; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: P67936; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: Q9NRN7; IntAct: EBI-25509687; Score: 0.35
DE  Interaction: P25789; IntAct: EBI-25509767; Score: 0.35
DE  Interaction: P08621; IntAct: EBI-25509767; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-25509767; Score: 0.35
DE  Interaction: P06753; IntAct: EBI-25509767; Score: 0.35
DE  Interaction: Q5JWF2; IntAct: EBI-25509767; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-25509811; Score: 0.35
DE  Interaction: O75688; IntAct: EBI-25509811; Score: 0.35
DE  Interaction: P04075; IntAct: EBI-25509811; Score: 0.35
DE  Interaction: Q15365; IntAct: EBI-25509845; Score: 0.35
DE  Interaction: P17987; IntAct: EBI-25509845; Score: 0.35
DE  Interaction: P46109; IntAct: EBI-25509845; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-25509845; Score: 0.35
DE  Interaction: P13797; IntAct: EBI-25509845; Score: 0.35
DE  Interaction: P49327; IntAct: EBI-25509845; Score: 0.35
DE  Interaction: P59998; IntAct: EBI-25509845; Score: 0.35
DE  Interaction: Q9NWT1; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q9H0D6; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q01081; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q15024; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q9Y383; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: P62263; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q96SB4; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: P46087; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: P08708; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: P42285; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q99848; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q12789; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q9P015; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q13243; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q1KMD3; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: O60293; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: O60832; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q2NL82; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q8N9T8; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q15020; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: O75934; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q5SSJ5; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q14137; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q92974; IntAct: EBI-25509874; Score: 0.35
DE  Interaction: Q8IY21; IntAct: EBI-26495688; Score: 0.40
DE  Interaction: P54132; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q9BVQ7; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q14146; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q6P1X5; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q13427; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: P19878; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q9NYV4; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q12873; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: P30414; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q9BRT6; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q8IZ69; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: O60287; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q8N4N8; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q9GZR2; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q96C57; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q14241; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: P49711; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q8N3C0; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q9UPE1; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q9H9Y6; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: P20042; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q49A26; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q8NFW8; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q15397; IntAct: EBI-26495696; Score: 0.35
DE  Interaction: Q9Y6C9; IntAct: EBI-26495704; Score: 0.35
DE  Interaction: P20674; IntAct: EBI-26495704; Score: 0.35
DE  Interaction: Q9BVT8; IntAct: EBI-26495704; Score: 0.35
DE  Interaction: P10606; IntAct: EBI-26495704; Score: 0.35
DE  Interaction: P28331; IntAct: EBI-26495704; Score: 0.35
DE  Interaction: P85037; IntAct: EBI-26495704; Score: 0.35
DE  Interaction: P13073; IntAct: EBI-26495704; Score: 0.35
DE  Interaction: Q9UJZ1; IntAct: EBI-26495704; Score: 0.35
DE  Interaction: Q01831; IntAct: EBI-26495709; Score: 0.35
DE  Interaction: P54725; IntAct: EBI-26495709; Score: 0.35
DE  Interaction: Q14232; IntAct: EBI-26495714; Score: 0.35
DE  Interaction: Q9P0M6; IntAct: EBI-26495714; Score: 0.35
DE  Interaction: Q8IYD1; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: P49588; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q9UJV3; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: P52701; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q86X55; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q8WU90; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q9NPF4; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: O43837; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q15654; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: P28340; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: P04183; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q96D46; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: O60518; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q9BW92; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q9UGI8; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: P52790; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q9BRX2; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q9Y2L1; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q9HAV4; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: P11802; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: P49419; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: P54886; IntAct: EBI-26495747; Score: 0.35
DE  Interaction: P62633; IntAct: EBI-26495753; Score: 0.35
DE  Interaction: P35237; IntAct: EBI-26495753; Score: 0.35
DE  Interaction: P30044; IntAct: EBI-26495753; Score: 0.35
DE  Interaction: Q9NYU2; IntAct: EBI-26495753; Score: 0.35
DE  Interaction: Q9Y2T4; IntAct: EBI-26495753; Score: 0.35
DE  Interaction: Q13162; IntAct: EBI-26495753; Score: 0.35
DE  Interaction: O60826; IntAct: EBI-26495758; Score: 0.67
DE  Interaction: P13489; IntAct: EBI-26495758; Score: 0.35
DE  Interaction: O15269; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: P43686; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-26495763; Score: 0.53
DE  Interaction: P35232; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: Q9BTV4; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: Q9UBV2; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: P04844; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: O15260; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: O75947; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: O94905; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: Q9Y277; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: P24539; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: Q96DZ1; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: P36542; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: P48047; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: P45880; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: P17480; IntAct: EBI-26495768; Score: 0.35
DE  Interaction: Q9NVI1; IntAct: EBI-26495768; Score: 0.35
DE  Interaction: Q9Y4B6; IntAct: EBI-26495768; Score: 0.35
DE  Interaction: Q9H000; IntAct: EBI-26495768; Score: 0.67
DE  Interaction: P07205; IntAct: EBI-26495768; Score: 0.35
DE  Interaction: Q96PM5; IntAct: EBI-26495768; Score: 0.35
DE  Interaction: P51116; IntAct: EBI-26495768; Score: 0.67
DE  Interaction: P51114; IntAct: EBI-26495768; Score: 0.74
DE  Interaction: P22061; IntAct: EBI-26495773; Score: 0.56
DE  Interaction: Q96EY7; IntAct: EBI-26495783; Score: 0.35
DE  Interaction: Q9BXT6; IntAct: EBI-26495783; Score: 0.35
DE  Interaction: Q8TC07; IntAct: EBI-26496082; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-26496082; Score: 0.35
DE  Interaction: A6NEC2; IntAct: EBI-26496082; Score: 0.35
DE  Interaction: P55060; IntAct: EBI-26496082; Score: 0.35
DE  Interaction: P53618; IntAct: EBI-26496082; Score: 0.35
DE  Interaction: Q5T160; IntAct: EBI-26496082; Score: 0.35
DE  Interaction: Q93084; IntAct: EBI-26496082; Score: 0.35
DE  Interaction: Q15751; IntAct: EBI-26496082; Score: 0.53
DE  Interaction: Q14573; IntAct: EBI-26496082; Score: 0.35
DE  Interaction: Q92616; IntAct: EBI-26496082; Score: 0.35
DE  Interaction: Q53GL7; IntAct: EBI-25619194; Score: 0.44
DE  Interaction: Q9H3R2; IntAct: EBI-25686027; Score: 0.35
DE  Interaction: O60524; IntAct: EBI-25686027; Score: 0.35
DE  Interaction: Q86TG7; IntAct: EBI-25686016; Score: 0.35
DE  Interaction: P15622; IntAct: EBI-25686016; Score: 0.35
DE  Interaction: O76064; IntAct: EBI-25686007; Score: 0.40
DE  Interaction: O00238; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: Q9UHN6; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: Q969N2; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: Q92820; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: Q30201; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: Q16658; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: P51690; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: P10321; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: O75354; IntAct: EBI-25686038; Score: 0.35
DE  Interaction: Q5VW36; IntAct: EBI-25686238; Score: 0.35
DE  Interaction: P00846; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: O43264; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9UPQ8; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q96B96; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: O94919; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: Q9Y5Z9; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9Y561; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9Y3P4; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9UBU6; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9UBF2; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9P0I2; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: Q9NWS8; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9NUT2; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9H490; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9H2J7; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: Q9C0H2; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9BVG9; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9BT76; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9BSR8; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9BRR6; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q96S52; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q96Q80; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q96HV5; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q96GC9; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q96G23; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q96ES6; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q96CP7; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q96C19; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q969E2; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q92536; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q8WY22; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q8WVQ1; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q8WUD6; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q8WTW3; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q8N357; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q8N0U8; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q7Z3C6; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q6Y1H2; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q6SZW1; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: Q6P1A2; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q5UCC4; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q5J8M3; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: Q5HYI8; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q5BJH7; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q15800; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q15392; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q15125; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q15043; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q15006; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q14746; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q14596; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q14019; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q13637; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q03135; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: P83436; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: P58658; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: P56381; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: P51636; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: P30049; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: P28328; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: P28068; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: P26038; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: P04114; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: P04035; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: P03905; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: P00167; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: O95395; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: O76024; IntAct: EBI-25686067; Score: 0.53
DE  Interaction: O60779; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: O43402; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: O43292; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: O00151; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: B7ZAQ6; IntAct: EBI-25686067; Score: 0.35
DE  Interaction: Q9BYW2; IntAct: EBI-25686251; Score: 0.35
DE  Interaction: Q86VP1; IntAct: EBI-25686251; Score: 0.35
DE  Interaction: P42226; IntAct: EBI-25686251; Score: 0.35
DE  Interaction: J3QS39; IntAct: EBI-25691145; Score: 0.62
DE  Interaction: P05161; IntAct: EBI-25691177; Score: 0.91
DE  Interaction: Q64339; IntAct: EBI-25691525; Score: 0.79
DE  Interaction: Q9UBQ5; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: Q96CT7; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: Q9BY44; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: O15372; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: Q7L2H7; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: Q13347; IntAct: EBI-25765840; Score: 0.48
DE  Interaction: P68104; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: O00303; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: P41091; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: P61221; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: O15371; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: Q9Y262; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: Q99613; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: Q14152; IntAct: EBI-25765840; Score: 0.35
DE  Interaction: Q9BYX4; IntAct: EBI-26895043; Score: 0.52
DE  Interaction: Q5RKT7; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62945; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62280; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62277; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62841; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P62244; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62249; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P39019; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P60866; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P63220; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62266; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62847; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62851; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62854; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P42677; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62857; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62273; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P15880; IntAct: EBI-25828920; Score: 0.53
DE  Interaction: P62861; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P23396; IntAct: EBI-25828920; Score: 0.53
DE  Interaction: P61247; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62701; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P62753; IntAct: EBI-25828920; Score: 0.53
DE  Interaction: P62081; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P62241; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: P46781; IntAct: EBI-25828920; Score: 0.32
DE  Interaction: Q9H0H0; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: O75564; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: O14972; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q96LT9; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9Y6G5; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9Y2K2; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9Y2D8; IntAct: EBI-26375521; Score: 0.67
DE  Interaction: Q9UN81; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9UKF6; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9UHP3; IntAct: EBI-26375521; Score: 0.76
DE  Interaction: Q9UBI1; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9P2S5; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9P2D0; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9P000; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9NX08; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9NVH2; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9H4B6; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q9GZQ3; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q96II8; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q96HP0; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q8N668; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q86X10; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q86W92; IntAct: EBI-26375521; Score: 0.67
DE  Interaction: Q86SQ0; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q7Z4G1; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q7Z3J2; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q6ZWJ1; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q6ZU80; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q6IEG0; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q6GYQ0; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q63ZY3; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q5VUJ6; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q5SZL2; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q5SVZ6; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q567U6; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q53EZ4; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q15345; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q13188; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q13049; IntAct: EBI-26375521; Score: 0.67
DE  Interaction: Q13043; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q12923; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q05086; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: P51530; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: P28838; IntAct: EBI-26375521; Score: 0.62
DE  Interaction: O95754; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: O95714; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: O75665; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: O75382; IntAct: EBI-26375521; Score: 0.67
DE  Interaction: O43933; IntAct: EBI-26375521; Score: 0.35
DE  Interaction: Q14653; IntAct: EBI-26583175; Score: 0.44
DE  Interaction: Q15750; IntAct: EBI-26583273; Score: 0.44
DE  Interaction: P59046; IntAct: EBI-26583398; Score: 0.44
DE  Interaction: E9Q5R7; IntAct: EBI-26583416; Score: 0.44
DE  Interaction: P0CG48; IntAct: EBI-26583643; Score: 0.56
DE  Interaction: P37837; IntAct: EBI-26584235; Score: 0.35
DE  Interaction: P38646; IntAct: EBI-26584235; Score: 0.35
DE  Interaction: P09382; IntAct: EBI-26584235; Score: 0.35
DE  Interaction: P61978; IntAct: EBI-26584235; Score: 0.35
DE  Interaction: P78527; IntAct: EBI-26584235; Score: 0.35
DE  Interaction: P25963; IntAct: EBI-26585856; Score: 0.44
DE  Interaction: Q13616; IntAct: EBI-26585236; Score: 0.44
DE  Interaction: O02741; IntAct: EBI-26601418; Score: 0.44
DE  Interaction: B2LUG8; IntAct: EBI-26601473; Score: 0.44
DE  Interaction: A0A5N4DAX7; IntAct: EBI-26601486; Score: 0.44
DE  Interaction: Q9GKP4; IntAct: EBI-26602287; Score: 0.44
DE  Interaction: L5LC70; IntAct: EBI-26602296; Score: 0.44
DE  Interaction: A0A1S2ZWT3; IntAct: EBI-26602342; Score: 0.44
DE  Interaction: R9QB93; IntAct: EBI-26602358; Score: 0.44
DE  Interaction: O75360; IntAct: EBI-26949889; Score: 0.56
DE  Interaction: Q2TAC2; IntAct: EBI-26950001; Score: 0.56
DE  Interaction: P53675; IntAct: EBI-26950023; Score: 0.56
DE  Interaction: Q9Y2V7; IntAct: EBI-26950034; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-26950056; Score: 0.56
DE  Interaction: Q9Y6K9; IntAct: EBI-26950067; Score: 0.56
DE  Interaction: O60229; IntAct: EBI-26950078; Score: 0.56
DE  Interaction: P52954; IntAct: EBI-26950089; Score: 0.56
DE  Interaction: Q9Y6D9; IntAct: EBI-26950100; Score: 0.56
DE  Interaction: Q5JR59; IntAct: EBI-26950111; Score: 0.56
DE  Interaction: A8MTQ0; IntAct: EBI-26950122; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-26950144; Score: 0.56
DE  Interaction: Q15427; IntAct: EBI-26950155; Score: 0.56
DE  Interaction: Q9BXI9; IntAct: EBI-26949990; Score: 0.60
DE  Interaction: P14373; IntAct: EBI-26950199; Score: 0.56
DE  Interaction: Q12933; IntAct: EBI-26950188; Score: 0.56
DE  Interaction: Q13077; IntAct: EBI-26950177; Score: 0.56
DE  Interaction: Q86XT4; IntAct: EBI-26950210; Score: 0.56
DE  Interaction: Q96R06; IntAct: EBI-26950166; Score: 0.56
DE  Interaction: Q9H257; IntAct: EBI-26950823; Score: 0.56
DE  Interaction: Q8WWH4; IntAct: EBI-26950812; Score: 0.60
DE  Interaction: Q4VCS5; IntAct: EBI-26950801; Score: 0.56
DE  Interaction: O95273; IntAct: EBI-26950835; Score: 0.63
DE  Interaction: P08670; IntAct: EBI-26951264; Score: 0.56
DE  Interaction: Q9BYV2; IntAct: EBI-26951242; Score: 0.56
DE  Interaction: Q9C040; IntAct: EBI-26951198; Score: 0.60
DE  Interaction: Q9H5L6; IntAct: EBI-26951187; Score: 0.56
DE  Interaction: Q8WW24; IntAct: EBI-26951176; Score: 0.56
DE  Interaction: Q8N0S2; IntAct: EBI-26951165; Score: 0.56
DE  Interaction: Q9UHV2; IntAct: EBI-26951132; Score: 0.56
DE  Interaction: Q96QF0; IntAct: EBI-26951110; Score: 0.60
DE  Interaction: Q8TBN0; IntAct: EBI-26951099; Score: 0.56
DE  Interaction: P11217; IntAct: EBI-26951088; Score: 0.56
DE  Interaction: P41219; IntAct: EBI-26951077; Score: 0.56
DE  Interaction: Q8ND90; IntAct: EBI-26951044; Score: 0.56
DE  Interaction: Q9HBI0; IntAct: EBI-26951033; Score: 0.56
DE  Interaction: Q6UWW0; IntAct: EBI-26950989; Score: 0.56
DE  Interaction: Q6A163; IntAct: EBI-26950967; Score: 0.56
DE  Interaction: Q14532; IntAct: EBI-26950956; Score: 0.56
DE  Interaction: Q15323; IntAct: EBI-26950945; Score: 0.56
DE  Interaction: Q7Z3Y8; IntAct: EBI-26950934; Score: 0.56
DE  Interaction: P13646; IntAct: EBI-26950923; Score: 0.56
DE  Interaction: Q9UKT9; IntAct: EBI-26950901; Score: 0.56
DE  Interaction: Q8IX15; IntAct: EBI-26950890; Score: 0.60
DE  Interaction: Q04446; IntAct: EBI-26950857; Score: 0.56
DE  Interaction: Q9UGI0; IntAct: EBI-26951286; Score: 0.56
DE  Interaction: Q8N1B4; IntAct: EBI-26951275; Score: 0.56
DE  Interaction: Q8IYX8; IntAct: EBI-26952645; Score: 0.56
DE  Interaction: Q13064; IntAct: EBI-26952689; Score: 0.56
DE  Interaction: P60880; IntAct: EBI-26952878; Score: 0.56
DE  Interaction: O95429; IntAct: EBI-26952867; Score: 0.56
DE  Interaction: Q86Y26; IntAct: EBI-26953109; Score: 0.56
DE  Interaction: P15884; IntAct: EBI-26953260; Score: 0.56
DE  Interaction: P23497; IntAct: EBI-26953249; Score: 0.56
DE  Interaction: P56192; IntAct: EBI-26949366; Score: 0.49
DE  Interaction: Q9NXS3; IntAct: EBI-26949355; Score: 0.49
DE  Interaction: A8MW99; IntAct: EBI-26949411; Score: 0.49
DE  Interaction: Q9NR56; IntAct: EBI-26949575; Score: 0.49
DE  Interaction: A8MRT5; IntAct: EBI-26949601; Score: 0.49
DE  Interaction: Q9H361; IntAct: EBI-26949612; Score: 0.49
DE  Interaction: P23759; IntAct: EBI-26949623; Score: 0.49
DE  Interaction: Q8TE12; IntAct: EBI-26949564; Score: 0.49
DE  Interaction: Q9BQ66; IntAct: EBI-26949553; Score: 0.49
DE  Interaction: Q96D03; IntAct: EBI-26949542; Score: 0.49
DE  Interaction: Q8N684; IntAct: EBI-26949531; Score: 0.49
DE  Interaction: Q96NS8; IntAct: EBI-26949520; Score: 0.49
DE  Interaction: Q96P56; IntAct: EBI-26949498; Score: 0.49
DE  Interaction: Q96B67; IntAct: EBI-26949487; Score: 0.49
DE  Interaction: Q09666; IntAct: EBI-26949476; Score: 0.49
DE  Interaction: Q9NX63; IntAct: EBI-26949509; Score: 0.49
DE  Interaction: Q7Z3I7; IntAct: EBI-26949711; Score: 0.49
DE  Interaction: Q96AQ6; IntAct: EBI-26949634; Score: 0.49
DE  Interaction: Q9NP87; IntAct: EBI-26949645; Score: 0.49
DE  Interaction: Q9BRQ0; IntAct: EBI-26949656; Score: 0.49
DE  Interaction: Q9NTJ5; IntAct: EBI-26949667; Score: 0.49
DE  Interaction: P50453; IntAct: EBI-26949678; Score: 0.49
DE  Interaction: Q9BXI2; IntAct: EBI-26949689; Score: 0.49
DE  Interaction: P17023; IntAct: EBI-26949700; Score: 0.49
DE  Interaction: Q8WWN8; IntAct: EBI-26949911; Score: 0.49
DE  Interaction: Q9Y2M5; IntAct: EBI-26949933; Score: 0.49
DE  Interaction: Q96CW7; IntAct: EBI-26949922; Score: 0.49
DE  Interaction: P49765; IntAct: EBI-26949944; Score: 0.49
DE  Interaction: Q92546; IntAct: EBI-26950485; Score: 0.49
DE  Interaction: Q6IC83; IntAct: EBI-26950463; Score: 0.49
DE  Interaction: Q6PF05; IntAct: EBI-26950529; Score: 0.49
DE  Interaction: Q8N7C3; IntAct: EBI-26950518; Score: 0.49
DE  Interaction: Q96N21; IntAct: EBI-26950507; Score: 0.49
DE  Interaction: Q86T65; IntAct: EBI-26951858; Score: 0.49
DE  Interaction: Q96JB2; IntAct: EBI-26951847; Score: 0.49
DE  Interaction: Q8WXK4; IntAct: EBI-26951825; Score: 0.49
DE  Interaction: Q8N2N9; IntAct: EBI-26951814; Score: 0.49
DE  Interaction: Q8WXI4; IntAct: EBI-26951792; Score: 0.49
DE  Interaction: Q6KB66; IntAct: EBI-26951913; Score: 0.49
DE  Interaction: P00488; IntAct: EBI-26951891; Score: 0.49
DE  Interaction: Q14562; IntAct: EBI-26951869; Score: 0.49
DE  Interaction: Q8TAG9; IntAct: EBI-26951880; Score: 0.49
DE  Interaction: P61758; IntAct: EBI-26952089; Score: 0.49
DE  Interaction: Q5W5X9; IntAct: EBI-26952067; Score: 0.49
DE  Interaction: Q96H20; IntAct: EBI-26952034; Score: 0.49
DE  Interaction: Q86VW0; IntAct: EBI-26952023; Score: 0.49
DE  Interaction: Q6NUQ1; IntAct: EBI-26952012; Score: 0.49
DE  Interaction: A6NK89; IntAct: EBI-26952001; Score: 0.49
DE  Interaction: Q6IN85; IntAct: EBI-26951979; Score: 0.49
DE  Interaction: Q07869; IntAct: EBI-26951968; Score: 0.49
DE  Interaction: P17568; IntAct: EBI-26951957; Score: 0.49
DE  Interaction: A9UHW6; IntAct: EBI-26951946; Score: 0.49
DE  Interaction: P26842; IntAct: EBI-26952961; Score: 0.56
DE  Interaction: P25942; IntAct: EBI-26952972; Score: 0.49
DE  Interaction: Q6UWB1; IntAct: EBI-26952983; Score: 0.49
DE  Interaction: Q16553; IntAct: EBI-26952994; Score: 0.56
DE  Interaction: Q6UWN5; IntAct: EBI-26953005; Score: 0.49
DE  Interaction: P54274; IntAct: EBI-26953131; Score: 0.49
DE  Interaction: A0A663DJA2; IntAct: EBI-26953397; Score: 0.49
DE  Interaction: P0DTD2; IntAct: EBI-26954139; Score: 0.49
DE  Interaction: P0DTC2; IntAct: EBI-26954338; Score: 0.49
DE  Interaction: P13533; IntAct: EBI-26996222; Score: 0.44
DE  Interaction: P07225; IntAct: EBI-26996294; Score: 0.44
DE  Interaction: Q9BZS1; IntAct: EBI-26996969; Score: 0.44
DE  Interaction: Q15303; IntAct: EBI-26997123; Score: 0.44
DE  Interaction: Q8N0Z8; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q96P11; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9BXP2; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9Y692; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q2M1P5; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9UI30; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9HCS7; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9H1D9; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q13813; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9ULC4; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P60900; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q13505; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q8WVS4; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q53H82; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O95249; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9NQC7; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O75494; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O00469; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9Y312; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9H1P3; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O14936; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9NQR4; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O60763; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9BZG8; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q7Z5K2; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q8NB91; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q14186; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9Y285; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q86VN1; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q96E39; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q13492; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9BTU6; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q8WVV9; IntAct: EBI-27030072; Score: 0.52
DE  Interaction: Q68E01; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9NZZ3; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9BSH4; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P12694; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O75191; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O60812; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O75179; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9NUL3; IntAct: EBI-27030072; Score: 0.52
DE  Interaction: P21281; IntAct: EBI-27030072; Score: 0.52
DE  Interaction: Q9P2K6; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q8IYQ7; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q6P5R6; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O94761; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O75915; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O95985; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P40222; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: O14727; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q13888; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9Y4L1; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9NX46; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P12883; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P22681; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q16629; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9BTE3; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q8IXB1; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q53H12; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q6PJT7; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q16630; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P04083; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P50750; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9Y2R9; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q96Q05; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P00750; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9Y3X0; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q96P48; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q12792; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q13395; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q13232; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: P42167; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q9HAQ2; IntAct: EBI-27050247; Score: 0.35
DE  Interaction: O00571; IntAct: EBI-27050247; Score: 0.35
DE  Interaction: P42336; IntAct: EBI-27050247; Score: 0.35
DE  Interaction: P23193; IntAct: EBI-27050247; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-27050247; Score: 0.35
DE  Interaction: P23528; IntAct: EBI-27050247; Score: 0.35
DE  Interaction: P20742; IntAct: EBI-27050247; Score: 0.35
DE  Interaction: P47929; IntAct: EBI-27050247; Score: 0.35
DE  Interaction: P12829; IntAct: EBI-27050247; Score: 0.35
DE  Interaction: Q9Y6K5; IntAct: EBI-27050631; Score: 0.35
DE  Interaction: Q9Y3Z3; IntAct: EBI-27050631; Score: 0.35
DE  Interaction: P09913; IntAct: EBI-27050631; Score: 0.35
DE  Interaction: P09914; IntAct: EBI-27050631; Score: 0.35
DE  Interaction: P33993; IntAct: EBI-27050631; Score: 0.35
DE  Interaction: P0DTC4; IntAct: EBI-27052479; Score: 0.37
DE  Interaction: P0DTC5; IntAct: EBI-27052648; Score: 0.37
DE  Interaction: P35754; IntAct: EBI-27072957; Score: 0.56
DE  Interaction: Q9H307; IntAct: EBI-27092400; Score: 0.44
DE  Interaction: P12931; IntAct: EBI-27092586; Score: 0.44
DE  Interaction: Q7Z434; IntAct: EBI-27094247; Score: 0.54
DE  Interaction: O95786; IntAct: EBI-27094255; Score: 0.72
DE  Interaction: O88522; IntAct: EBI-27121653; Score: 0.44
DE  Interaction: Q96C36; IntAct: EBI-27126032; Score: 0.46
DE  Interaction: Q03426; IntAct: EBI-27126032; Score: 0.35
DE  Interaction: P32322; IntAct: EBI-27126032; Score: 0.46
DE  Interaction: Q8NEC7; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: Q9NX70; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: P49795; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: G9CGD6; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: P23142; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: Q9NPH0; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: P51687; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: Q02952; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: Q8IVE3; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: Q96AX9; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: Q9NR28; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: Q5T447; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: Q15773; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: O43149; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: Q6DKK2; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: O43447; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: P83111; IntAct: EBI-27126088; Score: 0.35
DE  Interaction: P81605; IntAct: EBI-27126148; Score: 0.40
DE  Interaction: P10809; IntAct: EBI-27126652; Score: 0.40
DE  Interaction: P68363; IntAct: EBI-27126663; Score: 0.40
DE  Interaction: P21108; IntAct: EBI-27126674; Score: 0.40
DE  Interaction: Q99558; IntAct: EBI-27126696; Score: 0.40
DE  Interaction: Q96AY3; IntAct: EBI-27126707; Score: 0.35
DE  Interaction: Q9NQH7; IntAct: EBI-27126707; Score: 0.35
DE  Interaction: P48594; IntAct: EBI-27126721; Score: 0.40
DE  Interaction: P51784; IntAct: EBI-27126732; Score: 0.35
DE  Interaction: Q5W0V3; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9HD23; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: O94830; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9UQ90; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q12979; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q15021; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: O60512; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9HB07; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9H920; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9HCN3; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q96NR8; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q8IUH4; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9BUJ0; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q86WT1; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: P04920; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9Y375; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q06323; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9ULF5; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9UJJ9; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: P18859; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9NRY5; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9NPA0; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q7L7V1; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q3T906; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: O95873; IntAct: EBI-27126745; Score: 0.35
DE  Interaction: Q9C0C2; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: A5YKK6; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: Q96LI5; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: Q96FV9; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: O14640; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: Q9H1K0; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: A6NHR9; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: Q92997; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: Q9UNZ2; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: Q9NZN8; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: Q8TD16; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: O75175; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: O43432; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: Q5W0B1; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: O14641; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: Q86W42; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: Q7Z478; IntAct: EBI-27126939; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-27127026; Score: 0.35
DE  Interaction: Q6FI81; IntAct: EBI-27127026; Score: 0.35
DE  Interaction: O76003; IntAct: EBI-27127026; Score: 0.35
DE  Interaction: Q6PEY2; IntAct: EBI-27128059; Score: 0.27
DE  Interaction: Q8NHA4; IntAct: EBI-27128073; Score: 0.27
DE  Interaction: P17661; IntAct: EBI-27128105; Score: 0.27
DE  Interaction: P30086; IntAct: EBI-27128112; Score: 0.27
DE  Interaction: O15143; IntAct: EBI-27128112; Score: 0.27
DE  Interaction: P08758; IntAct: EBI-27128112; Score: 0.27
DE  Interaction: Q5TFE4; IntAct: EBI-27128112; Score: 0.27
DE  Interaction: P08133; IntAct: EBI-27128112; Score: 0.27
DE  Interaction: O75367; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: Q9NRL2; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: Q9Y5B9; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: P45973; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: O75475; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: Q13111; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: P51608; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: P51532; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: Q9UIG0; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: Q99986; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: P35659; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: Q08945; IntAct: EBI-27128132; Score: 0.27
DE  Interaction: Q03518; IntAct: EBI-27128155; Score: 0.27
DE  Interaction: Q14676; IntAct: EBI-27128162; Score: 0.27
DE  Interaction: P38398; IntAct: EBI-27128162; Score: 0.27
DE  Interaction: P00374; IntAct: EBI-27128172; Score: 0.27
DE  Interaction: Q3SXY7; IntAct: EBI-27128172; Score: 0.27
DE  Interaction: Q9UK32; IntAct: EBI-27128172; Score: 0.27
DE  Interaction: Q92771; IntAct: EBI-27128209; Score: 0.27
DE  Interaction: P59534; IntAct: EBI-27128216; Score: 0.27
DE  Interaction: Q96RG2; IntAct: EBI-27128243; Score: 0.27
DE  Interaction: Q9H9G7; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: Q93008; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: Q9HA64; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: Q13889; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: A3KMH1; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: Q2NKX8; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: P45974; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: Q15418; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: Q9UKK9; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: Q14008; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: Q7Z4H7; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: P78344; IntAct: EBI-27128476; Score: 0.35
DE  Interaction: Q00987; IntAct: EBI-30810800; Score: 0.40
DE  Interaction: Q13283; IntAct: EBI-30814306; Score: 0.57
GO  GO:0039714;
GO  GO:0062243;
GO  GO:1905369;
GO  GO:1902555;
GO  GO:1905354;
GO  GO:0030430;
GO  GO:0044165;
GO  GO:0044172;
GO  GO:0044174;
GO  GO:0044177;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0044385;
GO  GO:0005845;
GO  GO:0031533;
GO  GO:0031381;
GO  GO:0000175;
GO  GO:0032574;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008234;
GO  GO:0003678;
GO  GO:0016892;
GO  GO:0002151;
GO  GO:0004386;
GO  GO:0042802;
GO  GO:0019785;
GO  GO:0016829;
GO  GO:0004482;
GO  GO:0004483;
GO  GO:0008242;
GO  GO:0046983;
GO  GO:0042803;
GO  GO:0003723;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0006370;
GO  GO:0006351;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039519;
GO  GO:0039648;
GO  GO:0080009;
GO  GO:1902680;
GO  GO:0045070;
GO  GO:0039690;
GO  GO:0016540;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0016485;
GO  GO:0006508;
GO  GO:0090503;
GO  GO:0001172;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039722;
GO  GO:0039547;
GO  GO:0039604;
GO  GO:0039501;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0039723;
GO  GO:0019082;
GO  GO:0046786;
GO  GO:0039694;
GO  GO:0019083;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAP
SQ  HGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQEN
SQ  WNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAW
SQ  YTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTL
SQ  MKCDHCGETSWQTGDFVKATCEFCGTENLTKEGATTCGYLPQNAVVKIYCPACHNSEVGPEHSLAEYHNESGLKTILRKG
SQ  GRTIAFGGCVFSYVGCHNKCAYWVPRASANIGCNHTGVVGEGSEGLNDNLLEILQKEKVNINIVGDFKLNEEIAIILASF
SQ  SASTSAFVETVKGLDYKAFKQIVESCGNFKVTKGKAKKGAWNIGEQKSILSPLYAFASEAARVVRSIFSRTLETAQNSVR
SQ  VLQKAAITILDGISQYSLRLIDAMMFTSDLATNNLVVMAYITGGVVQLTSQWLTNIFGTVYEKLKPVLDWLEEKFKEGVE
SQ  FLRDGWEIVKFISTCACEIVGGQIVTCAKEIKESVQTFFKLVNKFLALCADSIIIGGAKLKALNLGETFVTHSKGLYRKC
SQ  VKSREETGLLMPLKAPKEIIFLEGETLPTEVLTEEVVLKTGDLQPLEQPTSEAVEAPLVGTPVCINGLMLLEIKDTEKYC
SQ  ALAPNMMVTNNTFTLKGGAPTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVI
SQ  KTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPL
SQ  EFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYI
SQ  KNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGP
SQ  NVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVE
SQ  QKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLK
SQ  KDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSII
SQ  SNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLND
SQ  LNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQS
SQ  TQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLD
SQ  GADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATAL
SQ  LTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQT
SQ  TLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHIT
SQ  SKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPY
SQ  PNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNK
SQ  ATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPA
SQ  NNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRC
SQ  LNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCL
SQ  GSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTA
SQ  FGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHV
SQ  VDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRP
SQ  INPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVY
SQ  YSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQG
SQ  FVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMS
SQ  LSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHT
SQ  DFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGD
SQ  FLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGS
SQ  IIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGA
SQ  LDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDV
SQ  SFLAHIQWMVMFTPLVPFWITIAYIICISTKHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLP
SQ  LTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCM
SQ  VQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPK
SQ  TPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDL
SQ  EGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQT
SQ  GIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQSAVKRTIKGTHHWLLLTILTSLLVLVQSTQW
SQ  SLFFFLYENAFLPFAMGIIAMSAFAMMFVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLDMVDTSLSGFKLK
SQ  DCVMYASAVVLLILMTARTVYDDGARRVWTLMNVLTLVYKVYYGNALDQAISMWALIISVTSNYSGVVTTVMFLARGIVF
SQ  MCVEYCPIFFITGNTLQCIMLVYCFLGYFCTCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKNSIDAFKL
SQ  NIKLLGVGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLS
SQ  MQGAVDINKLCEEMLDNRATLQAIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRK
SQ  LEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVIPDYNTY
SQ  KNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQ
SQ  TACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRG
SQ  MVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQES
SQ  FGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQSADAQSFL
SQ  NRVCGVSAARLTPCGTGTSTDVVYRAFDIYNDKVAGFAKFLKTNCCRFQEKDEDDNLIDSYFVVKRHTFSNYQHEETIYN
SQ  LLKDCPAVAKHDFFKFRIDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVEN
SQ  PDILRVYANLGERVRQALLKTVQFCDAMRNAGIVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDSYYSLLMPILTLT
SQ  RALTAESHVDTDLTKPYIKWDLLKYDFTEERLKLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVLFSTVFPPTSFGP
SQ  LVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQ
SQ  TVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCI
SQ  NANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTN
SQ  RQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASLVLARKHTTCCSL
SQ  SHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLY
SQ  ECLYRNRDVDTDFVNEFYAYLRKHFSMMILSDDAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSEAKCWTETDLTKG
SQ  PHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYI
SQ  RKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVIS
SQ  TSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTN
SQ  AGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIG
SQ  EYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQK
SQ  YSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYV
SQ  FCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDM
SQ  FLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYN
SQ  SQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNVNRFNVAITRAKVGILCIMSDRDLYDKLQFTSLEIPRRN
SQ  VATLQAENVTGLFKDCSKVITGLHPTQAPTHLSVDTKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFIT
SQ  REEAIRHVRAWIGFDVEGCHATREAVGTNLPLQLGFSTGVNLVAVPTGYVDTPNNTDFSRVSAKPPPGDQFKHLIPLMYK
SQ  GLPWNVVRIKIVQMLSDTLKNLSDRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDRRATCFSTASDTYACWHHSIGFDY
SQ  VYNPFMIDVQQWGFTGNLQSNHDLYCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWTIEYPIIGDELKINAACRKVQHM
SQ  VVKAALLADKFPVLHDIGNPKAIKCVPQADVEWKFYDAQPCSDKAYKIEELFYSYATHSDKFTDGVCLFWNCNVDRYPAN
SQ  SIVCRFDTRVLSNLNLPGCDGGSLYVNKHAFHTPAFDKSAFVNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCIT
SQ  RCNLGGAVCRHHANEYRLYLDAYNMMISAGFSLWVYKQFDTYNLWNTFTRLQSLENVAFNVVNKGHFDGQQGEVPVSIIN
SQ  NTVYTKVDGVDVELFENKTTLPVNVAFELWAKRNIKPVPEVKILNNLGVDIAANTVIWDYKRDAPAHISTIGVCSMTDIA
SQ  KKPTETICAPLTVFFDGRVDGQVDLFRNARNGVLITEGSVKGLQPSVGPKQASLNGVTLIGEAVKTQFNYYKKVDGVVQQ
SQ  LPETYFTQSRNLQEFKPRSQMEIDFLELAMDEFIERYKLEGYAFEHIVYGDFSHSQLGGLHLLIGLAKRFKESPFELEDF
SQ  IPMDSTVKNYFITDAQTGSSKCVCSVIDLLLDDFVEIIKSQDLSVVSKVVKVTIDYTEISFMLWCKDGHVETFYPKLQSS
SQ  QAWQPGVAMPNLYKMQRMLLEKCDLQNYGDSATLPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGT
SQ  AVLRQWLPTGTLLVDSDLNDFVSDADSTLIGDCATVHTANKWDLIISDMYDPKTKNVTKENDSKEGFFTYICGFIQQKLA
SQ  LGGSVAIKITEHSWNADLYKLMGHFAWWTAFVTNVNASSSEAFLIGCNYLGKPREQIDGYVMHANYIFWRNTNPIQLSSY
SQ  SLFDMSKFPLKLRGTAVMSLKEGQINDMILSLLSKGRLIIRENNRVVISSDVLVNN
//
ID  P0C6F7;
PN  Non-structural protein 11;
GN  1a;
OS  389230;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6F7;
DR  UNIPROT: Q0Q4F3;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3. {ECO:0000269|PubMed:19264783}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000269|PubMed:19264783}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0008242;
GO  GO:0003727;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLSKAGVTTQGARGKYRAELYNEKRSDHVACTVPLCDTEDMASKLTPWFEDGETAFNQVSSILKEKGKILFVPMHMQRAM
SQ  KFLPGPRVYLVERLTGGMLSKHFLVNQLAYKDHVGAAMMRTTLNVKPLGMFFPYDSSLETGEHTFLLRKNGLGGQLFRER
SQ  PWDRKETPYVEILDDLEADPTGKYSQNLLKKLIGGDCIPVDQYMCGKNGKPIADYAKIVAKEGLTTLADIEVDVKSRMDS
SQ  DRFIVLNKKLYRVVWNVTRRNVPYSKQTAFTVVSVIQCDDKESVPEHTFTIGSQILMVSPLKATNNKNFNLKQRLLHTFY
SQ  GKEAVQQPGYIYHSAYVDCNACGRGTWCTGNAIQGFACDCGANYSANDVDLQSSGLVPKNALFLANCPCANNGACSHNAA
SQ  QVYSILDGKACVEVGGKSFTLTFGGVVYAYMGCCDGTMYFVPRAKSCVSRIGDAIFTGCTGTWDKVVETANLFLEKAQHS
SQ  LNFCQQFALTEVVLAILSGTTSTFEELRDLCHNASYEKVRDHLVNHGFVVTIGDYIRDAINIGANGVCNATINAPFIAFT
SQ  GLGESFKKVAAIPWKICSNLKSALDYYCSNIMFRVFPYDIPCDVNDFVELLLDCGKLTVATSYFVLRYLDEKFDTVLGTV
SQ  SNACQTALSSFLNACVAASRATAGFISDMFKLFKVLMHKLYVYTSCGYVAVAEHSSKIVQQVLDIMSKAMKLLHTNVSWA
SQ  GTKLSAIIYEGREALLFNSGTYFCLSTKAKTLQDQMNLVLPGDYNKKTLGILDPVPNADTIDVTANSTVVDVVHGQLEPT
SQ  NEHGPSMIVGNYVLVSDKLFVRTDDEEFYPLCINGKVVSTLFRLKGGMPSKKVTFGDVNTVEVTAYRSVSITYDIHPVLD
SQ  ALLSSSKLATFTVEKDLLVEDFVDVIKDEVLTLLTPLLRGYDIDGFDVEDFIDVPCYVYNQDGDCAWSSNMTFSINPVED
SQ  VEEVEEFIEDDYLSDELPIADDEEAWTRAVEEVMPLDDILVAEIELEEDLPLETALESVEAEVGESISDELCVVETAKAQ
SQ  EPSVESTDSTPSTSTVVSENDLSVKPMSRVAETGDVLEVETAVVGGPVSDVTASVVTNDIVSVEQAQQCGVSSLPIQDEA
SQ  SENQVHQVPDLQCTSETKVEIVQPRQDLRPRRLRKSKVDLSKYKHTVINNSVTLVLGDAIQIASLLPKCVLVNAANRHLK
SQ  HGGGIAGAINKASGGDVQEESDEYISNSGPLHVGDSVLLKGYGLADAILRVVGPDARNNEDAALLKRCYKTFNKHTIVVT
SQ  PLISSGIFSVDPKVSFEYLLANVTTTTYVVVNNEDIYNTLATPSKPDGLVYSFEGWRGTVRTAKNYGFTCFICTEYSANV
SQ  KFLRTKGVDTTKKIQTVDGVSYYLYSARDALTDVIAAANGCPGICAMPFGYVTHGLDLAQSGNYVRQVKVPYVCLLASKE
SQ  QIPIMNSDVAIQTPETAFINNVTSNGGYHSWHLVSGDLIVKDVCYKKLLHWSGQTICYADNKFYVVKNDVALPFSDLEAC
SQ  RAYLTSRAAQQVNIEVLVTIDGVNFRTVILNDATTFRKQLGATFYKGVDISDALPTVKMGGESLFVADNLSESEEVVLKE
SQ  YYGTSDVTFLQRYYSLQPLVQQWKFVVHDGVKSLKLSNYNCYINATIMMIDMLHDIKFVVPALQNAYLRYKGGDPYDFLA
SQ  LIMAYGDCTFDNPDDEAKLLHTLLAKAELTVSAKMVWREWCTVCGIRDIEYTGMRACVYAGVNSMEELQSVFNETCVCGS
SQ  VKHRQLVEHSTPWLLVSGLNEVKVSTSTDPVYRAFNVFQGVETSVGHYVHVRVKDGLFYKYDSGSLTKTSDMKCKMTSVW
SQ  YPKVRYTADCNVVVYDLDGVTKVEVNPDLSNYYMKDGKYYTSKPTIKYSPATILPGSVYSNSCLVGVDGTPGSDTISKFF
SQ  NDLLGFDETKPISKKLTYSLLPNEDGDVLLSEFNNYNPVYKKGVMLKGKPILWVNNGVCDSALNKPNRASLRQLYDVAPI
SQ  VLDNKYTVLQDNTSQLIEPNVPVVEDVSITTRKLIEVKCKGLNKPFVKGNFSFVNDPNGVTVVDTLGLTELRALYVDINT
SQ  RYIVLRDNNWSSLFKLHTVESGDLQIVANGGSVTRRARVLLGASSLFASFAKITVTATTAACKTAGRSFCKFVVNYGVLQ
SQ  NMFLFLKMLFFLPFNYLWPKKQPTVDVGVSGLRTAGVVTTNIVKQCGTAAYYMLLGKFKRVDWKATLRLFLLLCTTILLL
SQ  SSIYHLVIFNQVLSSDVMLEDATGILAMYKEVRSYLGIRTLCDGLAVEYRNTSFDVVDFCSNRSVLCQWCLIGQDSLTRY
SQ  SALQMLQTHITSYVLNIDWIWFALEFFLAYVLYTSSFNVLLLVVTAQYFFAYTSAFVNWRAYNYIVSGLFFLVTHIPLHG
SQ  LVRVYNFLACLWFLRKFYSHVINGCKDTACLLCYKRNRLTRVEASTIVCGTKRTFYIAANGGTSYCCKHNWNCVECDTAG
SQ  VGNTFICTEVANDLTTTLRRLIKPTDQSHYYVDSVVVKDAVVELHYNRDGSSCYERYPLCYFTNLEKLKFKEVCKTPTGI
SQ  PEHNFLIYDTNDRGQENLARSACVYYSQVLCKPMLLVDVNLVTTVGDSREIAIKMLDSFINSFISLFSVSRDKLEKLINT
SQ  ARDCVRRGDDFQTVLKTFTDAARGHAGVESDVETTMVVDALQYAHKNDIQLTTECYNNYVPGYIKPDSINTLDLGCLIDL
SQ  KAASVNQTSMRNANGACVWNSGDYMKLSDSFKRQIRIACRKCNIPFRLTTSKLRAADNILSVKFSATKIVGGAPSWLLRV
SQ  RDLTVKGYCILTLFVFTVAVLSWFCLPSYSIATVNFNDDRILTYKVIENGIVRDIAPNDACFANKYGHFSKWFNENHGGV
SQ  YRNSVDCPITIAVIAGVAGARVANVPATLAWVGRQIVLFVSRVFANTNVCFTPTNEIPYDTFSDSGCVLSSECTLFRDAE
SQ  GNLNPFCYDPTVLPGASSYADMKPHVRYDMYDSDMYIKFPEVIFESTLRITKTLATQYCRFGSCEESAAGVCISTNGSWA
SQ  LYNQNYSTRPGIYCGDDYFDIVRRLAVSLFQPVTYFQLSTSLAMGLVLCVFLTAAFYYINKVKRALADYTQCAVVAVVAA
SQ  LLNSLCLCFIVANPLLVAPYTAMYYYATFYLTGEPAFIMHISWYVMFGTVVPIWMLASYTVGVMLRHLFWVLAYFSKKHV
SQ  DVFTDGKLNCSFQDAASNIFVIGKDTYVALRNAITQDSFVRYLSLFNKYKYYSGAMDTASYREACAAHLCKALQTYSETG
SQ  SDILYQPPNCSVTSSVLQSGLVKMSAPSGAVENCIVQVTCGSMTLNGLWLDNTVWCPRHIMCPADQLTDPNYDALLISKT
SQ  NHSFIVQKHIGAQANLRVVAHSMVGVLLKLTVDVANPSTPAYTFSTVKPGASFSVLACYNGKPTGVFTVNLRHNSTIKGS
SQ  FLCGSCGSVGYTENGGVLNFVYMHQMELSNGTHTGSSFDGVMYGAFEDKQTHQLQLTDKYCTINVVAWLYAAVLNGCKWF
SQ  VKPTRVGIVTYNEWALSNQFTEFVGTQSIDMLAHRTGVSVEQMLAAIQSLHAGFQGKTILGQSTLEDEFTPDDVNMQVMG
SQ  VVMQSGVKRISYGFMHWLMSTLVLAYVSVMQLTKFTMWTYLFETIPTQMTPLLFGFMACVMFTVKHKHTFLSLFLLPVAL
SQ  CLTYANIVYEPQTLVSSTLIAVANWLTPTSVYMRTTHLDFGLYISLSFVLAIIVRRLYRPSMSNLALALCSGVMWFYTYV
SQ  IGDHSSPITYLMFITTLTSDYTITVFATVNLAKFISGLVFLYAPHLGFILPEVKLVLLIYLCLGYMCTMYFGVFSLLNLK
SQ  LRVPLGVYDYSVSTQEFRFLTGNGLHAPRNSWEALILNFKLLGIGGTPCIKVATVQSKLTDLKCTSVVLLTVLQQLHLES
SQ  NSKAWSYCVKLHNEILAAVDPTEAFERFVCLFATLMSFSANVDLDALANDLFENSSVLQATLTEFSHLATYAELETAQSS
SQ  YQKALNSGDASPQVLKALQKAVNVAKNAYEKDKAVARKLERMAEQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDN
SQ  DVLNGVIANARNGCVPLSIVPLCASNKLRVVIPDISVWNKVVNWPSVSYAGSLWDVTVINNVDNEVVKPTDVVETNESLT
SQ  WPLVIECSRASSSAVKLQNNEIHPKGLKTMVVTAGIDQVNCSSSAVAYYEPVQGHRMVMGLLSENAHLKWAKVEGKDGFI
SQ  NIELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQLLGHIAATVRLQAGANTEFASNSTVLTLVAFAVDPAKAYLDYVG
SQ  SGGTPLSNYVKMLAPKTGTGVAISVKPEATADQETYGGASVCLYCRAHIEHPDVSGVCKYKTRFVQIPAHVRDPVGFLLK
SQ  NVPCNVCQYWVGYGCNCDALRNNTVPQSKDTNFLNESGVLV
//
ID  P0C6F5;
PN  Non-structural protein 11;
GN  1a;
OS  389167;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6F5;
DR  UNIPROT: Q0Q476;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF12379;
DR  Pfam: PF12124;
DR  Pfam: PF11633;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DR  PROSITE: PS51940;
DE  Function: The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0008242;
GO  GO:0003727;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESLALGVSEKTHVQLSLPVLQVRDVLVRGFGDSVEEALAEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDAQGTN
SQ  HGYKVVELVAELDGIQYGRSGTTLGVLVPHVGETPVAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGVELGTDPIEDYEQN
SQ  WNTKHGGGVLRELIRELNGGAFTRYVDNNFCGPDGYPLECIKDLLARAGKSMCTLSEQLDYIESKRGVYCCREHEHEIVW
SQ  FTERSEKSYERQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVATPQECNDMHLSTL
SQ  MKCNHCDEVSWQTCDFLKATCEQCGTENLVCEGPTTCGYLPANAVVKMPCPACQDPEVGPEHSVADYHNHSNIETRLRKG
SQ  GRTKCFGGCVFAYVGCYNKRAYWVPRASANIGASHTGITGDNVETLNEDLMEILNRDRVNINIVGDFHLNEEVAIILASF
SQ  SASTCAFVDTVKGLDYKTFKDIVESCGNFKVTRGRAKKGAWNIGQEKSILTPLYGFPSQAAGVIRSIFTRALDTANHSIP
SQ  DLQRAAITILDGISEQSLRLIDAMVYTSDLLTNSVIVMAYVTGGLVQQITQWLSNMLGTTVDKLKPVFTWVEAKLSAGIE
SQ  FLRDAWEILKFLVTGVFDIVKGQIQVASDNLKECVKAFLDVLNKALEMCIDQVIIAGAKLRTLNLGEVFIAQSKGLYRQC
SQ  IRGKEQLQLLMPLRAPKEVTFFEGDSHDTVFTSEEVVLKNGELEALETPVDSFTNGAVIGTPVCVNGLMLLELKDKEQYC
SQ  ALSPGLLATNNVFSLKGGAPVKGVTFGEDTVLEVQGYKNVKITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAV
SQ  VKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEEKLSSRMYCSFYPPDEEEDCEEYEDEEEIPEETCEHEYGTEDDYKG
SQ  LPLEFGASTEIQQVDEEEEEDWLEEAIAAKPEPEPLPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQHAKPTVIVNAANVH
SQ  LKHGGGVAGALNKATNGAMQQESDDYIKKNGPLTVGGSCLLSGHNLAKKCMHVVGPNLNAGEDVQLLKAAYANFNSQDVL
SQ  LAPLLSAGIFGAKPLQSLKMCVETVRTQVYFAVNDQDLYDHVVLGYLDSLKPKVETPTQENLELKEQPAVETLTQENLEL
SQ  EELPVIEKPVDVKFKARIEEVNTSLEETKFLTSRLLLFADINGKLYQDSQNMLRGEDMFFLEKDAPYIVGDVISSGDITC
SQ  VIIPAKKAGGTTEMLAKALKKVPVSEYITTYPGQGCAGYTLEEAKTALRKCKSVFYVLPSKTPNDKEEILGTVSWNLREM
SQ  LAHAEETRKLMLICMDVKALMSTIHRRYKGIKVQEGIVDYGVRFFFYTSKEPVASIITKLNLLNEPLVTMPIGYVTHGLN
SQ  LEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFIETVSLAGMYRDWSYSGQRTELGVEFLKRGDKVVYHT
SQ  VGSPIQFHLDGEVLLLDKLKSLLSLREVRTIKVFTTVDNTNLHTQIVDMSMTYGQQFGPTYLDGADVTKIKPHAKHEGKT
SQ  FFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQIGGLTSIKWADNNCYLSSVLLALQQIEVKFNAPALQE
SQ  AYYRARAGDAANFCALILAYSNRTVGELGDVRETMTHLLQHANLESAKRVLNVVCKTCGQKSTTLTGVEAVMYMGTLSYE
SQ  ELKTGVTIPCICGRDATQYLVQQESSFVMMSAPPSEYTLQQGAFLCANEYTGSYQCGHYTHVTVKETLYRIDGAYLTKMS
SQ  EYKGPVTDVFYKEISYTTTIKPVSYKLDGVIYTEIQPKLDEYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKF
SQ  ADDLNQMTGFKKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIIWHINQTTNKTTYKPNTWCLRCLWSTK
SQ  PVETSNSFEVLEVEDTQGMDNLACESQTPTSEEVVENPTIQKEVIECDVKTIEVVGNVILKPSEEGVKVTQELGHEDLMA
SQ  AYVEETSITIKKPNELSLALGLRTLATHGAAAINSVPWSKILAYVKPFLGQAAVTTTNCIKRCVQRVFNNYMPYVITLLF
SQ  QLCTFTRSTNSRIRASLPTTIAKNSVKSVAKLCLDVCINYVKSPKFSKLFTIAMWLLLLSICLGSLIYVTAAFGVLLSNL
SQ  GIPSYCDGVRESYVNSSNVTTMDFCEGSFLCSVCLNGLDSLDSYPALETIQVTISSYKLDLTSLGLAAEWFLAYMLFTKF
SQ  FYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFAFCYYVWKSYVHIMDGCTSSTCMMCYKRNR
SQ  ATRVECTTIVNGMKRSFYVYANGGRGFCKAHNWNCLNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYVVDSVAVK
SQ  NGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESAAKSASVYYSQLMCQPILLLDQALV
SQ  SDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKL
SQ  SHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNN
SQ  IPFRLTCATTRQVVNAITTKISLKGGKIVSTWFKLMLKATLLCVLAALFCYIIMPVHSLSVHDGYTNEIIGYKAIQDGVT
SQ  RDIMATDDCFANKHAGFDSWFSQRGGSYRNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICY
SQ  TPSKLIEYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVT
SQ  TFDAEYCRHGTCERSEAGVCLSTSGRWVLNNEHYRALPGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILV
SQ  TCAAYYFMKFRRAFGEYNHVVAANALLFLMSFTILCLAPAYSFLPGVYSIFYLYLTFYFTNDVSFLAHLQWFAMFSPIVP
SQ  FWITAIYVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYF
SQ  SGALDTTSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDD
SQ  TVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSV
SQ  LACYNGSPSGVYQCAMRPNYTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAA
SQ  GTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQN
SQ  GMNGRTILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLG
SQ  IMAIAACAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLVLMTA
SQ  RTVYDDAARRVWTLMNVITLVYKVYYGNSLDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQ
SQ  CIMLVYCFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVAT
SQ  VQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDN
SQ  RATLQAIASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQAR
SQ  SEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWE
SQ  IQQVVDADSKIVQLSEINMDNSQNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKG
SQ  GRFVLALLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPRGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNA
SQ  TEVPANSAVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHP
SQ  NPKGFCDLKGKYVQIPATCANDPVGFTLKNTVCTVCGTWKGYGCSCDQLREPMMQSADASTFLNGFAV
//
ID  P0C6F6;
PN  Non-structural protein 11;
GN  1a;
OS  693999;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6F6;
DR  UNIPROT: Q0Q467;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASNHISLAFANDEEISAIGFGSVEEAVSYYSDAAVNGFDQCRFVSLGLQDAVVGVEDDDVVMLITGVTQLRAYLGTFGD
SQ  RPLNLRGWLLFSNCNYFLEELDLVFGRCGGTTIPVDQFMCGADGAPVIQEGDWTFMDYFQDSNQFTLNGITYVKAWDVDR
SQ  KPNDYAKQNVTCIRRITYITDHRHVLADGTTMKTARHPKVNKSVVLDSPFDQIYKEVGSPFMGNGSTFVEMLKDPAFFHA
SQ  LITCECGRSEWTVGDWKGYNSLCCNIKCKPITIVTPKAVPGAVVITKAGIGAGLKCYNNVFLKHIIDLVVPGTNLGWGVW
SQ  RIAKVQSKDDVATSGNVLVDDPEDRLDPCYFGNDGPFATKFKFQLLANSFDDEVKGAIVQGVVHVNTAICDVVKDILGLP
SQ  WFVKKLGSLVTVMWDQFVAGVQSMKICTLKVVQLAKALSCATMSVVKGVITLVAEVPEIFKRLFYTLTSALKSLCTSSCD
SQ  ALVVAGKSFAKIGDYVLLPSALVRLVSSKVKGKAQSGIKQLQFATVVLGDTHKVESDRVEFSSVNLKMVDEEFPLNPVGH
SQ  TVAVGNQAFFCSDGLYRFMADRDLVITSPIFKPELELEPIFECDAIPGFPKVAASNVAELCVKVDTLLFNYDKIYKKYST
SQ  IIKGDRCYIQCTHTFKAPSYYFDDDEFVELCTKYYKLPDFDAFYNAVHAATDMDQFCALCTSGFEVFIPRVPDCPPILND
SQ  IDGGSIWTSFILSVRSATDFIKTLKIDLGLNGVVVFVTKKFRKAGALLQKLYNAFLDTVTSFIKVAGVAFKYCATCVPKI
SQ  VINGCYHTVTRLFAKDLQIPTEDGVADFNTFNHCVFPVNPTRIETDSLELEEVDFVEPGVDGKLVILDDYSFYSDGTNYY
SQ  PSDGKGVVASCFKKKGGGVVTISDEVQVRTIDPVYKVRLEYEFEDETLVKVCEKAIGTKLKVTGDWSNLLETLEKAMDVV
SQ  RQHLDVPDYFVYDEEGGTDLNLTIMVSQWPLSSDSEDDFKAVDDEPNANTDETVDTFAEDVAETQNVQQDVTQDEVEAVC
SQ  DLVVKATEEGPIEHEELSEDQKEVQQALAFIEDKPVVVKPDVFAFSYASYGGLKVLNQSSNNCWVSSALVQLQLTGLLDS
SQ  DEMQLFNAGRVSPMVKRCYESQRAIFGSLGDVSACLESLLKDRDGMSITCTIDCGCGPGVRVYENAIFRFTPLKTAFPMG
SQ  RCLICSKTLMHTITQMKGTGIFCRDATALDVDTLVVKPLCAAVYVGAQDGGHYLTNMYDANMAVDGHGRHPIKFNTINTL
SQ  CYKDVDWEVSNGSCDVKPFLTYKNIEFYQGELSALLSVNHDFVVNAANEQLSHGGGIAKALDDLTKGELQVLSNQYVSRN
SQ  GSIKVGSGVLIKCKEHSILNVVGPRKGKHAAELLTKAYTFVFKQKGVPLMPLLSVGIFKVPITESLAAFLACVGDRVCKC
SQ  FCYTDKERLAIQNFVTSFQTEQPVEPLPVIQEVKGVQLEKPVPDVKVENPCEPFRIEGDAKFYDLTPSMVQSLQVTRLVS
SQ  FTNSDLCLGSFVRDCDGYVQGSLGGAIANYKKSNPVLPAGNCVTLKCDGFISFTFVILPKEGDTNYEKNFNRAIAKFLKL
SQ  KGSLLVVVEDSSVFNKISHASVAGYVAKPALVDTLFEAKPVQVVVTQDQRSFHTVELSTSQTYGQQLGDCVVEDKKVTNL
SQ  KPVSKDKVVSVVPNVDWDKHYGFVDAGIFHTLDHTMFVFDNNVVNGKRVLRTSDNNCWINAVCLQLQFANAKFKPKGLQQ
SQ  LWESYCTGDVAMFVHWLYWITGVEKGEPSDAENTLNIISRFLKPQGSVEMLRATSTTCDGTCSTKRVVSTPVVNASVLKV
SQ  GLDDGNCVHGLPLVDRVVSVNGTVIITNVGDTPGKPVVATENLLLDGVSYTVFQDSTTGVGHYTVFDKEAKLMFDGDVLK
SQ  PCDLNVSPVTSVVVCNNKKIVVQDPVKRVELDASKFLDTMNVASEKFFTFGDFVSRNIIVLIVYLFSLLAICFRALKKRD
SQ  MKVMAGVPERTGIILKRSVKYNYKALKFFFRLKFQYIKVFLKFSLVLYTLYALMFMFIRFTPVGTPICKRYTDGYANSTF
SQ  DKNDYCGNVLCKICLYGYEELSDFTHTRVIWQHLKDPLIGNILPLFYLVFLIIFGGFFVRIGITYFIMQYINAAGVALGY
SQ  QDNVWLLHLLPFNSMGNIIVVAFIVTRILLFLKHVLFGCDKPSCIACSKSAKLTRVPLQTILQGVTKSFYVNANGGKKFC
SQ  KKHNFFCVDCDSYGYGCTFINDVIAPELSNVTKLNVIPTGPATIIIDKVEFSNGFYYLYSGSTFWKYNFDITEAKYACKD
SQ  VLKNCNILTDFVVFNNSGSNVTQVKNACVYFSQLLCKPIKLVDSALLASLNVDFSANLHKAFVEVLSNSFGKDLSNCSNM
SQ  NECRESLGLSDVPEEEFSAAVSEAHRYDVLISDVSFNNLIVSYAKPEEKLAVHDIANCMRVGAKVVNHNVLTKDNVPVVW
SQ  LAKDFIALSEEARKYIVRTTKTKGINFMLTFNDRRMHLTIPTISVANKKGAGLPSLFTRLYSFFWHLCVLIVVLFVATSL
SQ  LDFSAQVTSDTQYDFKYIENGVLKVFEKPLDCVHNAFVNFNEWHNAKFGSIPTNSRRCPIVVGTSDEVRYIPGVPAGVFL
SQ  YGKSLIFAMSTIFGTSGLCFDDRGLTDPDSCIFNSACTTLSGIGGRNVYCYREGVVDNAKLYSSLLPHSYYRLMDGNHIV
SQ  LPEIITRGFGIRTIKTQAMTYCRTGECIDSQAGVCVGLDRFFVYSKTPGSDYVCGTGFFSLLFNVIGMFSNSIPVTVMSG
SQ  QILLNCVVAFTAVMACFAFTKFKRLFGDMSFGVLSVGLCTVVNNLSYVVTQNSIGMLAYATLYFLCTKGVRYSWVWHVGF
SQ  AISYCFLAPWWVVLAYLICALLEFLPNLFKLKVSTQLFEGDKFVGSFESAASGTFVLDMHSYQKLANSISTEKLKQYCAS
SQ  YNRYKYYSGSASEADYRLACFAHLAKAMSDFANDHMDKLYTPPTVSYNSTLQAGLRKMAQPSGIVEGCIVRVSYGNLTLN
SQ  GLWLGDTVICPRHVIASNTTNVIDYDHAMSLVRLHNFSISSGNMFLGVISASMRGTLLHIKVNQSNVNTPNYTYKVLKPG
SQ  DSFNILACYDGSAAGVYGVNMRTNYTIRGSFISGACGSPGYNINNGVVEFCYMHHLELGSGCHVGSDMDGTMYGKYEDQP
SQ  TLQIEGASNLVTENVCSWLYGALINGDRWWLSSVSVGVDTYNEWALRNGMTALKNVDCFSLLVAKTGVDVGRLLASIQKL
SQ  HGNFGGKSILGCTSLCDEFTLSEVVKQMYGVTLQSGKVSRAFRNASIVCCLLFLFLSEMLNHSKLFWINPGYITPVFLAI
SQ  IVASSALMLLVKHKLLFLQLYLLPSLCIVSGYNIFKDYHFYTYMLEEFDYKVPFGGFNVTGVLNISLCCFVMGLHTFRFL
SQ  QTPNKIFSYVVAVLTVLYTYYYSTDVLGLILTSMSGFTNYWFIGTATYKLATYVLPHTSLLDSFDAIKAVVFLYLLLGYC
SQ  NCVYYGSLYWINRFCKLTLGCYEFKVSAAEFKYMVANGLRAPTGVFDALILSLKLIGVGGRKTIKISSVQSKLTDLKCTN
SQ  VVLLGCLSNMNIAANSREWAYCVDLHNKINLCNDAEAAQEMLLALLAFFLSKNSAFGVDELLDSYFNDSSVLQSVAATYV
SQ  NLPSYLAYETARQSYEDALANGSPPQLVKQLRHAMNVAKSEFDREASTQRKLDRMAEQAASQMYKEARAVNRKSKVVSAM
SQ  HSLLFGMLRRLDMSSVDTILSLAKDGVVPLSIIPAVSATKLNIVVSDIESYSKIQREGCVHYAGVIWSVVDIKDNDGKPV
SQ  HAKEVVTSNVESLAWPLFLNCERIIKLQNNEIIPSKIKQRPIKAEGEGVVADGNALYSNEGGRTFMYAFISDKPDLKVVK
SQ  WEFDGGSNAIELEPPCKFLVEAPSGPVVKYLYFVRNLNNLRRGAVLGFIGATVRLQAGKQTEQATNSSLLTLCAFAVDPP
SQ  KTYLDAVKSGHRPVGNCVKMLANGSGNGQAITNGVEASTNQDSYGGASVCLYCRAHVEHPDMDGFCKLRGKYVQVPLGTL
SQ  DPIRFVLENTVCKVCGCWQANGCTCDRAVIQSVDSGYLNECGALVQLD
//
ID  P0C6F8;
PN  Non-structural protein 11;
GN  1a;
OS  442736;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6F8;
DR  UNIPROT: Q3LZX2;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF12379;
DR  Pfam: PF12124;
DR  Pfam: PF11633;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DR  PROSITE: PS51940;
DE  Function: The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0008242;
GO  GO:0003727;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTN
SQ  HGHKVVELVAELDGIQFGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSFGIDLKSYDLGDELGTDPIEDYEQN
SQ  WNTKHGSGALRELTRELNGGVVTRYVDNNFCGPDGYPLECIKDFLARAGKSMCTLSEQLDYIESKRGVYCCREHEHEIVW
SQ  FTERSEKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVATPQECNDMHLSTL
SQ  MKCNHCDEVSWQTCDFLKATCEQCGTENLVCEGPTTCGYLPTNAVVKMPCPACQDPEVGPEHSVADYHNHSNIETRLRKG
SQ  GRTKCFGGCVFSYVGCYNKRAYWVPRASANIGANHTGITGENVETLNEDLLEILNRERVNINIVGDFRFNEEVAIILASF
SQ  SASPSAFIETVKGLDYKSFKVIVESCGNYKVTNGKPVTGAWNIGQQRSILTPLCGFPSQAAGVIRSIFSRTLDAANHSIL
SQ  DLQRAAVTTLDGISEQSLRLVDAMVYTSDLLTNSVVVMAYVTGGLVQQTMQWLSNMLGTAVDKLKPVFTWVEAKLSAGVE
SQ  FLRDAWEILKFLITGVFDVIKGQIQVATDNIKECVKIFLGVVNKALEMCLDQVTIAGTKLRALNLGEVFIAQSRGLYRQC
SQ  IRGKEQLQLLMPLKAPKEVTFLEGDAHDTVLTSEEVVLKSGELEALETPIDSFTSGAVVGTPVCINGLMLLELENKEQYC
SQ  ALSPGLLATNNVFRLKGGAPVKGVTFGEDTVLEVQGYKNVKITFELDVRVDKVLNEKCSVYTVESGTEVTEFACVVAEAV
SQ  VKTLQPVSDLLTPMGIDLDEWSVATFYLFDDAGEEKLSSRMYCSFYPPDEEEDCEECEDEEETCEHEYGTEDDYKGLPLE
SQ  FGASTETPHVEEEEEEEDWLDDAIEAEPEPEPLPEEPVNQFVGYLKLTDNVAIKCIDIVKEAQSAKPTVIVNAANTHLKH
SQ  GGGVAGALNKATNGAMQNESDEYIRQNGPLTVGGSCLLSGHNLAEKCLHVVGPNLNAGEDVQLLKRAYENFNSQDVLLAP
SQ  LLSAGIFGAKPLQSLKMCVEIVRTQVYLAVNDKSLYDQIVLDYLDSLKPKVESPNKEEEPKLEEPKAVQPVAEKPVDVKP
SQ  KIKACIDEVTTTLEETKFLTNKLLLFADINGKLYQDSQNMLRGEDMSFLEKDAPYIVGDVITSGDITCVIIPAKKSGGTT
SQ  EMLARALKEVPVAEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSETPNEKEEVLGTVSWNLREMLAHAEETRKLMP
SQ  ICLDVRAIMATIQRKYKGIKVQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGLNLEEAARCMRSLK
SQ  APAVVSVSSPDAVTAYNGYLTSSSKTPEEYFVETTSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTTGSPIEFHLDGE
SQ  VLPLDKLKSLLSLREVKTIKVFTTVDNTNLHTHIVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRS
SQ  EAFEYYHTIDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQVEVKFNAPALQEAYYRARAGDAAN
SQ  FCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLKGVEAVMYMGTLSYDELKTGVSIPCVC
SQ  GRNATQYLVQQESSFVMMSAPPAEYKLQQGAFLCANEYTGNYQCGHYTHITAKETLYRVDGAHLTKMSEYKGPVTDVFYK
SQ  ETSYTTAIKPVSYKLDGVTYTEIEPKLDGYYKKGNAYYTEQPIDLVPTQPMPNASFDNFKLTCSNTKFADDLNQMTGFKK
SQ  PASRELTVTFFPDLNGDVVAIDYRHYSTSFKKGAKLVHKPILWHINQTTNKTTYKPNIWCLRCLWSTKPVDTSNSFEVLV
SQ  VEDTQGMDNLACESQTTTSEEVVENPTVQKEIIECDVKTTEVVGNVILKPSEEGVKVTQELGHEDLMAAYVEETSITIKK
SQ  PNELSLALGLKTLATHGAAAINSVPWSKILAYVKPFLGQTAVITSNCIKKCVQRVFSNYMPYVITLLFQLCTFTKSTNSR
SQ  IKASLPTTIAKNSVKSVAKLCLDVCINYVKSPKFSKLFTIVMWLLLLSICLGSLTYVTAVLGVCLSSLGVPSYCDGVREL
SQ  YINSSNVTTMDFCQGYFPCSVCLSGLDSLDSYPALETIQVTISSYKLDLTFLGLAAEWLLAYMLFTKFFYLLGLSAIMQA
SQ  FFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYVWKSYVHIMDGCTSSTCMMCYKRNRATRVECTTIVNG
SQ  VKRSFYVYANGGRGFCKAHNWNCLNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSAYVVDSVTVKNGALHLYFDKAG
SQ  QKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESAAKSASVYYSQLMCQPILLLDQALVSDVGDSTEVSVK
SQ  MFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDIEVTGDS
SQ  CNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLVWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCATTRQ
SQ  VVNVITTKISLKGGKVVSTWFKLLLKVTLLCVLAALFCYVIMPVHSLSVHDGYTNEIIGYKAIQDGVTRDIVSTDDCFAN
SQ  KHAGFDSWFSQRGGSYRNDKNCPVVAAIITREIGFIVPGLPGTVLRALNGDFLHFLPRVFSAVGNICYTPSKLIEYSDFA
SQ  TSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEYCRHGTC
SQ  ERSEVGVCLSTSGRWVLNNEHYRALPGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFMKFRR
SQ  AFGEYNHVVAANALLFLMSFTILCLAPAYSFLPGVYSIFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYVFCIS
SQ  LKHFHWFFSNYLKKRVMFNGVTFSTFEEAALCTFLLNKEMYLRLRSETLLPLTQYNRYLALYNKYKYFSGALDTTSYREA
SQ  ACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVVCTA
SQ  EDMLNPNYDDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVY
SQ  QCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLA
SQ  WLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTI
SQ  LEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFALGIMAVAACAMLLV
SQ  KHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDDAARRVW
SQ  TLMNVITLVYKVYYGNSLDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCFLGYC
SQ  CCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDVKCTS
SQ  VVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIASEFS
SQ  SLPSYAAYATAQEAYEQAVSNGDSEVVLKKLKKSLNVAKSEFDHDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAM
SQ  QTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDADSKIV
SQ  QLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNAKGGRFVLALLSDHQ
SQ  DLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSF
SQ  CAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKY
SQ  VQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPMMQSADASTFLNGFAV
//
ID  P0C6T4;
PN  Non-structural protein 11;
GN  1a;
OS  694007;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6T4;
DR  UNIPROT: A3EX93;
DR  PDB: 2YNA;
DR  PDB: 2YNB;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0008242;
GO  GO:0003727;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLSKASVTTQGARGKYRAELYNEKRSDHVACTVPLCDTDDMACKLTPWFEDGETAFNQVSSILKEKGKILFVPMHMQRAM
SQ  KFLPGPRVYLVERLTGGMLSKHFLVNQLAYKDQVGAAMMRTTLNAKPLGMFFPYDSSLETGEYTFLLRKNGLGGQLFRER
SQ  PWDRKETPYVEILDDLEADPTGKYSQNLLKKLIGGDCIPIDQYMCGKNGKPIADYAKIVAKEGLTTLADIEVDVKSRMDS
SQ  DRFIVLNKKLYRVVWNVTRRNVPYPKQTAFTIVSVVQCDDKDSVPEHTFTIGSQILMVSPLKATNNKNFNLKQRLLYTFY
SQ  GKDAVQQPGYIYHSAYVDCNACGRGTWCTGNAIQGFACDCGANYSANDVDLQSSGLVPRNALFLANCPCANNGACSHSAA
SQ  QVYNILDGKACVEVGGKSFTLTFGGVVYAYMGCCDGTMYFVPRAKSCVSRIGDAIFTGCTGTWDKVVETANLFLEKAQRS
SQ  LNFCQQFALTEVVLAILSGTTSTFEELRDLCHNASYEKVRDHLVNHGFVVTIGDYIRDAINIGANGVCNATINAPFIAFT
SQ  GLGESFKKVSAIPWKICSNLKSALDYYSSNIMFRVFPYDIPCDVSNFVELLLDCGKLTVATSYFVLRYLDEKFDTVLGTV
SQ  SSACQTALSSFLNACVAASRATAGFINDMFKLFKVLMHKLYVYTSCGYVAVAEHSSKIVQQVLDIMSKAMKLLHTNVSWA
SQ  GTKLSAIIYEGREALLFNSGTYFCLSTKAKTLQGQMNLVLPGDYNKKTLGILDPVPNADTIDVNANSTVVDVVHGQLEPT
SQ  NEHGPSMIVGNYVLVSDKLFVRTEDEEFYPLCTNGKVVSTLFRLKGGMPSKKVTFGDVNTVEVTAYRSVSITYDIHPVLD
SQ  ALLSSSKLATFTVEKDLLVEDFVDVIKDEVLTLLTPLLRGYDIDGFDVEDFIDVPCYVYNQDGDCAWSSNMTFSINPVED
SQ  VEEVEEFIEDDYLSDELPIADDEEAWARAVEEVMPLDDILVAEIELEEDPPLETALESVEAEVVETAEAQEPSVESIDST
SQ  PSTSTVVGENDLSVKPMSRVAETDDVLELETAVVGGPVSDVTAIVTNDIVSVEQAQQCGVSSLPIQDEASENQVHQVSDL
SQ  QGNELLCSETKVEIVQPRQDLKPRRSRKSKVDLSKYKHTVINNSVTLVLGDAIQIASLLPKCILVNAANRHLKHGGGIAG
SQ  VINKASGGDVQEESDEYISNNGPLHVGDSVLLKGHGLADAILHVVGPDARNNEDAALLKRCYKAFNKHTIVVTPLISAGI
SQ  FSVDPKVSFEYLLANVTTTTYVVVNNEDIYNTLATPSKPDGLVYSFEGWRGTVRTAKNYGFTCFICTEYSANVKFLRTKG
SQ  VDTTKKIQTVDGVSYYLYSARDALTDVIAAANGCSGICAMPFGYVTHGLDLAQSGNYVRQVKVPYVCLLASKEQIPIMNS
SQ  DVAIQTPETAFINNVTSNGGYHSWHLVSGDLIVKDVCYKKLLHWSGQTICYADNKFYVVKNDVALPFSDLEACRAYLTSR
SQ  AAQQVNIEVLVTIDGVNFRTVILNDTTTFRKQLGATFYKGVDISDAFPTVKMGGESLFVADNLSESEKVVLKEYYGTSDV
SQ  TFLQRYYSLQPLVQQWKFVVHDGVKSLKLSNYNCYINATIMMIDMLHDIKFVVPALQNAYLRYKGGDPYDFLALIMAYGD
SQ  CTFDNPDDEAKLLHTLLAKAELTVSAKMVWREWCTVCGIRDIEYTGMRACVYAGVNSMEELQSVFNETCVCGSVKHRQLV
SQ  EHSAPWLLVSGLNEVKVSTSTDPIYRAFNVFQGVETSVGHYVHIRVKDGLFYKYDSGSLTKTSDMKCKMTSVWYPTVRYT
SQ  ADCNVVVYDLDGVTKVEVNPDLSNYYMKDGKYYTSKPTIKYSPATILPGSVYSNSCLVGVDGTPGSDTISKFFNDLLGFD
SQ  ETKPISKKLTYSLLPNEDGDVLLSEFSNYNPVYKKGVMLKGKPILWVNNGVCDSALNKPNRASLRQLYDVAPIVLDNKYT
SQ  VLQDNTSQLVEHNVPVVDDVPITTRKLIEVKCKGLNKPFVKGNFSFVNDPNGVTVVDTLGLTELRALYVDINTRYIVLRD
SQ  NNWSSLFKLHTVESGDLQIVAAGGSVTRRARVLLGASSLFASFAKITVTATTAACKTAGRGFCKFVVNYGVLQNMFVFLK
SQ  MLFFLPFNYLWPKKQPTVDIGVSGLRTAGIVTTNIVKQCGTAAYYMLLGKFKRVDWKATLRLFLLLCTTILLLSSIYHLV
SQ  LFNQVLSSDVMLEDATGILAIYKEVRSYLGIRTLCDGLVVEYRNTSFDVMEFCSNRSVLCQWCLIGQDSLTRYSALQMLQ
SQ  THITSYVLNIDWIWFALEFFLAYVLYTSSFNVLLLVVTAQYFFAYTSAFVNWRAYNYIVSGLFFLVTHIPLHGLVRVYNF
SQ  LACLWFLRKFYSHVINGCKDTACLLCYKRNRLTRVEASTIVCGTKRTFYIAANGGTSYCCKHNWNCVECDTAGVGNTFIC
SQ  TEVANDLTTTLRRLIKPTDQSHYYVDSVVVKDAVVELHYNRDGSSCYERYPLCYFTNLEKLKFKEVCKTPTGIPEHNFLI
SQ  YDTNDRGQENLARSACVYYSQVLCKPMLLVDVNLVTTVGDSREIAIKMLDSFINSFISLFSVSRDKLEKLINTARDCVRR
SQ  GDDFQNVLKTFTDAARGHAGVESDVETTMVVDALQYAHKNDIQLTTECYNNYVPGYIKPDSINTLDLGCLIDLKAASVNQ
SQ  TSMRNANGACVWNSGDYMKLSDSFKRQIRIACRKCNIPFRLTTSKLRAADNILSVKFSATKIVGGAPSWLLRVRDLTVKG
SQ  YCILTLFVFTVAVLSWFCLPSYSIATVNFNDDRILTYKVIENGIVRDIAPNDVCFANKYGHFSKWFNENHGGVYRNSMDC
SQ  PITIAVIAGVAGARVANVPANLAWVGKQIVLFVSRVFANTNVCFTPINEIPYDTFSDSGCVLSSECTLFRDAEGNLNPFC
SQ  YDPTVLPGASSYADMKPHVRYDMYDSDMYIKFPEVIVESTLRITKTLATQYCRFGSCEESAAGVCISTNGSWALYNQNYS
SQ  TRPGIYCGDDYFDIVRRLAISLFQPVTYFQLSTSLAMGLVLCVFLTAAFYYINKVKRALADYTQCAVVAVVAALLNSLCL
SQ  CFIVANPLLVAPYTAMYYYATFYLTGEPAFIMHISWYVMFGAVVPIWMLASYTVGVMLRHLFWVLAYFSKKHVDVFTDGK
SQ  LNCSFQDAASNIFVIGKDTYVALRNAITQDSFVRYLSLFNKYKYYSGAMDTASYREACAAHLCKALQTYSETGSDILYQP
SQ  PNCSVTSSVLQSGLVKMSAPSGAVENCIVQVTCGSMTLNGLWLDNTVWCPRHIMCPADQLTDPNYDALLISKTNHSFIVQ
SQ  KHIGAQANLRVVAHSMVGVLLKLTVDVANPSTPAYTFSTVKPGASFSVLACYNGKPTGVFTVNLRHNSTIKGSFLCGSCG
SQ  SVGYTENGGVINFVYMHQMELSNGTHTGSSFDGVMYGAFEDKQTHQLQLTDKYCTINVVAWLYAAVLNGCKWFVKPTRVG
SQ  IVTYNEWALSNQFTEFVGTQSIDMLAHRTGVSVEQMLAAIQSLHAGFQGKTILGQSTLEDEFTPDDVNMQVMGVVMQSGV
SQ  KRISYGFIHWLISTFVLAYVSVMQLTKFTMWTYLFETIPTQMTPLLLGFMACVMFTVKHKHTFMSLFLLPVALCLTYANI
SQ  VYEPQTLISSTLIAVANWLTPTSVYMRTTHFDFGLYISLSFVLAIIVRRLYRPSMSNLALALCSGVMWFYTYVIGDHSSP
SQ  ITYLMFITTLTSDYTITVFATVNLAKFISGLVFFYAPHLGFILPEVKLVLLIYLGLGYMCTMYFGVFSLLNLKLRVPLGV
SQ  YDYSVSTQEFRFLTGNGLHAPRNSWEALILNFKLLGIGGTPCIKVATVQSKLTDLKCTSVVLLTVLQQLHLESNSKAWSY
SQ  CVKLHNEILAAVDPTEAFERFVCLFATLMSFSANVDLDALANDLFENSSVLQATLTEFSHLATYAELETAQSSYQKALNS
SQ  GDASPQVLKALQKAVNVAKNAYEKDKAVARKLERMAEQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGVI
SQ  ANARNGCVPLSIVPLCASNKLRVVIPDISVWNKVVNWPSVSYAGSLWDITVINNVDNEVVKPTDVVETNESLTWPLVIEC
SQ  SRSSSSAVKLQNNEIHPKGLKTMVITAGVDQVNCNSSAVAYYEPVQGHRMVMGLLSENAHLKWAKVEGKDGFINIELQPP
SQ  CKFLIAGPKGPEIRYLYFVKNLNNLHRGQLLGHIAATVRLQAGANTEFASNSTVLTLVAFAVDPAKAYLDYVGSGGTPLS
SQ  NYVKMLAPKTGTGVAISVKPEATADQETYGGASVCLYCRAHIEHPDVSGVCKYKTRFVQIPAHVRDPVGFLLKNVPCNVC
SQ  QYWVGYGCNCDALRNNTVPQSKDTNFLNESGVLV
//
ID  P0C6T5;
PN  Non-structural protein 11;
GN  1a;
OS  694008;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6T5;
DR  UNIPROT: A3EXC9;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9BXW4; IntAct: EBI-29441340; Score: 0.44
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0008242;
GO  GO:0003727;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFVAGVAPQGARGKYRAELNTEKRTDHVSLKASLCDAGDLVLKISPWFMDGESAYKHVSEQLSKGSKLLFVPQTLKGFI
SQ  RHLPGPRVYLVERLTGGTYSDPFMVNQLAYQNAAGEGVIGTTLQGKRVGMFFPFDADLVTGEFQFLLRKKGFGGNRFRDA
SQ  PWDYNWTPYSDLMDALEADPCGKYSQSLLKKLVGGDFTPIDQYMCGKNGKPIAEFAALMASEGITKLADVEAEVKSRTDS
SQ  DRYIVFKNKLYRIVWNVQRKDVAYSKQSAFTMNSIVQLDTMEDVPRHSFTIGSEIQVIAPSTAVQANGHLNLKQRLLYAF
SQ  YGKQAVSEPNYIYHSAYVDCTSCGKGSWLTGNAVQGFACDCGAHYCANDVDLQSSGLVRKNAVLLTTCPCNKDGECKHTL
SQ  PQLVSMMTDKCDVEVVGKTFILTYGGVIYAYMGCSGGTMHFIPRAKSCVSKIGDAIFTGCTGTWSKVCETANLFLERAQH
SQ  AINFVNEFVLTETVVALLSGTTSSIEELRDLCRNATFEKVRDYLTPRGWIVTMGSYIEGVINVGAAGVCNAALNAPFIVL
SQ  SGLGESFKKVAATPWKLCSSLRETLDHYADSITYRVFPYDIPCDVTDYTALLLDCAVLTGASAYFVARYVDEKVEQLTNL
SQ  VFSSCQSAVAAFVQACMSTYKATAKFISDMFTLIKVVSERLYVYTSVGFVVVGDYSSQLLKQFMHILSKAMQLLHTTVSW
SQ  AGSKLPSVVYNGRDSLVFPSGTYYCVSTQGRSLQDQFDLVIPGDLSKKQIGILEPTPNSTTVDKKINTNVVEVVVGQLEP
SQ  TKEHSPELVVGDYVIISNKIFVRSVEDSETVFYPLCTDGKIVPTLFRLKGGAPPKGVKFGGEQTKEITAVRSVSVDYDVH
SQ  PVLDALLAGSELATFTVEKDLPVKDFVDVVKDEVIELLSKLLRGYNVDGFDLEDFADTPCYVYNAEGDLAWSSTMTFSVN
SQ  PVEEVEEECDDDYVEDEYLSEEMLVEEDENSWAAAVEAVIPMEDVQLDTLVAEIDVSEPADDVAEQASTEEVEVPSACVL
SQ  EASQVANAAEVESCEAEVSSSIPLHEDANAAKANDCAEGMPALDSTETVSKLSVDTPVGDVTQDDATSSNATVISEDVHT
SQ  ATHSKGLVAVPEVVPEKALGTSVERMRSTSEWTVVETSLKQETAVIVKNDSSAKPQRVKKPKAENPLKNFKHIVLNNDVT
SQ  LVFGDAIAVARATEDCILVNAANTHLKHGGGIAAAIDRASGGLVQAESDDYVNFYGPLNVGDSTLLKGHGLATGILHVVG
SQ  PDARANQDIQLLKRCYKAFNKYPLVVSPLISAGIFCVEPRVSLEYLLSVVHTKTYVVVNSEKVYNDLAAPKPPTGLTYSH
SQ  EGWRGIIRNAKSFGFTCFICTDQSANAKLLKGRGVDLTKKTQTVDGVKYYLYSSKDPLTDIITAANACKGICAMPIGYVT
SQ  HGLDLAQAGQQVKKITVPYVCLLASKDQVPILNSDVAVQTPEQSFINTVIANGGYHCWHLVTGELIVKGVSYRKLLNWSD
SQ  QTICYADNKFYVVKGQIALPFDSLEKCRTYLTSRAAQQKNVDVLVTIDGVNFRTVVLNNTTTYRVQLGSVFYKGSDISDT
SQ  IPTEKMSGEAVYLADNLSEAEKAVLSEVYGTADTAFLHRYYSLLALVKKWKYTVHDGVKSLKLNSNNCYVNVTMLMLDML
SQ  KEIKFIVPALQAAYLKHKGGDSTEFIALIMAYGDCTYGEPDDASRLLHTILSKAELTTQAKMVWRQWCNVCGVQDTTTTG
SQ  LKACIYVGMNSLDELHATHEECCQCGDVRKRQLVEHNAPWLLLSGLNEAKVMTPTSQSAGPDYTAFNVFQGVETSVGHYL
SQ  HVRVKDNLLYKYDSGSLSKTSDMKCKMTDVYYPKQRYSADCNVVVYSLDGNTWADVDPDLSAFYMKDGKYFTKKPVIEYS
SQ  PATILSGSVYTNSCLVGHDGTIGSDAISSSFNNLLGFDNSKPVSKKLTYSFFPDFEGDVILTEYSTYDPIYKNGAMLHGK
SQ  PILWVNNSKFDSALNKFNRATLRQVYDIAPVTLENKYTVLQDNQIQQVEVEAPKEDAKPQSPVQVAEDIDNKLPIIKCKG
SQ  LKKPFVKDGYSFVNDPQGVNVIDTLGIDDLRALYVDRNLRLIVLKENNWSALFNIHTVEKGDLSVIAASGSITRRVKILL
SQ  GASSLFAQFASVTVNVTTAMGKALGRMTRNVITNTGIIGQGFALLKMLLILPFTFWKSKNQSTVKVEVGALRTAGIVTTN
SQ  VVKQCASAAYDVLVVKFKRIDWKSTLRLLFLICTTGLLLSSLYYLFLFHQVLTSDVMLDGAEGMLATYRELRSYLGIHSL
SQ  CDGMVEAYRNVSYDVNDFCSNRSALCNWCLIGQDSLTRYSAFQMIQTHVTSYVINIDWVWFVMEFALAYVLYTSTFNVLL
SQ  LVVSSQYFFSYTGAFVNWRSYNYLVSGYFFCVTHIPLLGLVRIYNFLACLWFLRRFYNHVINGCKDTACLLCYKRNRLTR
SQ  VEASTVVCGSKRTFYIVANGGTSFCCRHNWNCVDCDTAGIGNTFICEEVANDLTTSLRRLVKPTDKSHYYVESVTVKDSV
SQ  VQLHYSREGASCYERYPLCYFTNLDKLKFKEVCKTPTGIPEHNFLIYDSSDRGQENLARSACVYYSQVLSKPMLLVDSNM
SQ  VTTVGDSREIASKMLDSYVNSFISLFGVNRDKLDKLVATARDCVKRGDDFQTVIKTFTDAARGPAGVESDVETSSIVDAL
SQ  QYAYKHDLQLTTEGFNNYVPSYIKPDSVATADLGCLIDLNAASVNQTSIRNANGACIWNSSDYMKLSDSLKRQIRIACRK
SQ  CNIPFRLTTSRLRSADNILSVKFSATKLSGGAPKWLLKLRDFTWKSYCVVTLVVFAMAVLSYLCLPAFNMSQVSFHEDRI
SQ  LTYKVVENGIIRDITPSDTCFANKYQSFSKWFNEHYGGLFNNDISCPVTVAVIAGVAGARVPNLPANVAWVGRQIVLFVS
SQ  RVFASSNNVCYTPTAEIPYERFSDSGCVLASECTLFRDAEGKINPYCYDPTVLPGASAYDQMKPHVRYDMYDSDMYIKFP
SQ  EVVFESTLRITKTLATRYCRFGSCEDANEGVCITTNGSWAIYNDHYANKPGVYCGDNYFDIVRRLGLSLFQPVTYFQLST
SQ  SLALGVMLCIFLTIAFYYVNKVKRALADYTQCAVVAVAAALLNSLCLCFVVSNPLLVLPYTALYYYATFYLTGEPAFVMH
SQ  VSWFVMFGTVVPIWMVFAYIVGVCLRHLLWVMAYFSKKHVEVFTDGKLNCSFQDAAANIFVINKDTYVALRNSITQDSYN
SQ  RYLSMFNKYKYYSGAMDTASYREASAAHLCKALQVYSETGSDVLFQPPNCSVTSSVLQSGLVKMAAPSGVVENCMVQVTC
SQ  GSMTLNGLWLDNYVWCPRHVMCPADQLSDPNYDALLVSKTNLSFIVQKNVGAPANLRVVGHTMVGTLLKLTVESANPQTP
SQ  AYTFTTVKPGASFSVLACYNGRPTGVFMVNMRQNSTIKGSFLCGSCGSVGYTQEGNVINFCYMHQMELSNGTHTGCAFDG
SQ  VMYGAFEDRQVHQVQLSDKYCTINIVAWLYAAILNGCNWFVKPNKTGIATFNEWAMSNQFTEFIGTQSVDMLAHKTGVSV
SQ  EQLLYAIQTLHKGFQGKTILGNSMLEDEFTPDDVNMQVMGVVMQSGVKRISYGLVHWLFTTLLLAYVATLQLTKFTIWNY
SQ  LFEVIPLQLTPLVLCVMACVMLTVKHKHTFLTLFLLPTAICLTYANIVYEPQTPVSSALIAVANWLNPASVYMRTTHTDL
SQ  GVYLSLCFALAVVVRRLYRPNASNLALALGSAMVWFYTYTTGDCSSPLTYLMFLTTLTSDYTVTVFLAVNVAKFFARVVF
SQ  LYAPHAGFIFPEVKLVLLMYLAVGYFCTVYFGVFSLLNLKLRVPLGVYDYTVSTQEFRYLTGNGLHAPRNSWEALRLNMK
SQ  LIGIGGTPCIKIASVQSKLTDLKCTSVVLLSVLQQLHLEANSKAWAHCVKLHNDILAATDPTEAFDNFVCLFATLMSFSA
SQ  NVDLEALASDLLDHPSVLQATLSEFSHLASYAELEAAQSSYQKALNSGDASPQVLKALQKAVNIAKNAYEKDKAVARKLE
SQ  RMAEQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGVISNARNGCVPLSVVPLCASNKLRVVIPDITIWNK
SQ  VVTWPSLSYAGALWDISLINNVDGEVVKSSDVTETNESLTWPLVLECTRAASSAVTLQNNEIRPSGLKTMVVSAGIDHAN
SQ  CNTSSLAYYEPVEGRKMLMGILSENAHLKWAKVEGRDGFVNIELQPPCKFLIAGPKGPEVRYLYFVKNLNNLHRGQLLGH
SQ  IAATVRLQAGSNTEFAINSSVLSAVTFSVDPGKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAVSVKPEANADQDTYGGAS
SQ  VCLYCRAHIEHPDVTGVCKFKGKFVQVPLHIRDPVGFCLQNTPCNVCQFWIGHGCNCDALRGTTIPQSKDSNFLNESGVL
SQ  L
//
ID  P0C6T6;
PN  Non-structural protein 11;
GN  1a;
OS  694006;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6T6;
DR  UNIPROT: A3EXG5;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000269|PubMed:19264783}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0008242;
GO  GO:0003727;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGVPDPPKLKSMVVTTLKWCDPFANPNVTGWDIPIEEALEYAKQQLRTPEPQLVFVPYYLSHAPGISGDRVVITDSIWY
SQ  ATNFGWQPIRELAMDKDGVRYGRGGTHGVLLPMQDPSFIMGDIDIQIRKYGIGANSPPDVLPLWDGFSDPGPDVGPYLDF
SQ  PDNCCPTKPKAKRGGDVYLSDQYGFDNNGILVEPVMKLLGVIKSDFTLEQLLAALGKYRTEDGYDLPDGYVKVAIKVGRK
SQ  AVPVLKQSIFTVVGVTEQLVPGYYYPFSTSSVVEHTKPTRGGPVGKTVEAVMLSLYGTNNYNPATPVARLKCSYCDYYGW
SQ  TPLKDIGTVNCLCGAEFQLTSSCVDAESAGVIKPGCVMLLDKSPGMRLIPGNRTYVSFGGAIWSPIGKVNGVTVWVPRAY
SQ  SIVAGEHSGAVGSGDTVAINKELVEYLIEGIRVDADTLDNPTCATFIANLDCDTKAPVVHTVESLQGLCLANKIMLGDKP
SQ  LPTDEFHPFIVGLAYHVQRACWYGALASRTFEAFRDFVRTEEERFAQFFGKVCAPINGCVYLAYTTGRVTLFSAYQVLNT
SQ  AIAKSKDAFGGVAAIVVDMLKPILEWVLKKMSIAKGAWLPYAEGLLALFKAQFTVVKGKFQFLRASLNSKCHSLCDLLTT
SQ  IMSKLLTSVKWAGCKVDALYTGTYYYFSRKGVLTEVQLCAKRLGLLLTPKQQKMEVEVLDGDFDAPVTLTDLELEECTGV
SQ  LEEVFGASDVKLVKGTLVSLASKLFVRTEDGFLYRYVKSGGVLGKAFRLRGGGVSKVTFGDEEVHTIPNTVTVNFSYDVC
SQ  EGLDAILDKVMAPFQVEEGTKLEDLACVVQKAVYERLSDLFSDCPAELRPINLEDFLTSECFVYSKDYEKILMPEMYFSL
SQ  EDAVPVDDEMVDDIEDTVEQASDSDDQWLGDEGAEDCDNTIQDVDVATSMTTPCGYTKIAEHVYIKCADIVQEARNYSYA
SQ  VLVNAANVNLHHGGGVAGALNRATNNAMQKESSEYIKANGSLQPGGHVLLSSHGLASHGILHVVGPDKRLGQDLALLDAV
SQ  YAAYTGFDSVLTPLVSAGIFGFTVEESLCSLVKNVACTTYVVVYDRQLYERALATSFDVPGPQSSVQHVPAIDWAEAVEV
SQ  QESIVDQVETPSLGAVDTVDSNADSGLNETARSPENVVGSVPDDVVADVESCVRDLVRQVVKKVKRDKRPPPIVPQQTVE
SQ  QQPQEISSPGDCNTVLVDVVSMSFSAMVNFGKEKGLLIPVVIDYPAFLKVLKRFSPKEGLFSSNGYEFYGYSRDKPLHEV
SQ  SKDLNSLGRPLIMIPFGFIVNGQTLAVSAVSMRGLTVPHTVVVPSESSVPLYRAYFNGVFSGDTTAVQDFVVDILLNGAR
SQ  DWDVLQTTCTVDRKVYKTICKRGNTYLCFDDTNLYAITGDVVLKFATVSKARAYLETKLCAPEPLIKVLTTVDGINYSTV
SQ  LVSTAQSYRAQIGTVFCDGHDWSNKNPMPTDEGTHLYKQDNFSSAEVTAIREYYGVDDSNIIARAMSIRKTVQTWPYTVV
SQ  DGRVLLAQRDSNCYLNVAISLLQDIDVSFSTPWVCRAYDALKGGNPLPMAEVLIALGKATPGVSDDAHMVLSAVLNHGTV
SQ  TARRVMQTVCEHCGVSQMVFTGTDACTFYGSVVLDDLYAPVSVVCQCGRPAIRYVSEQKSPWLLMSCTPTQVPLDTSGIW
SQ  KTAIVFRGPVTAGHYMYAVNGTLISVYDANTRRRTSDLKLPATDILYGPTSFTSDSKVETYYLDGVKRTTIDPDFSKYVK
SQ  RGDYYFTTAPIEVVAAPKLVTSYDGFYLSSCQNPQLAESFNKAINATKTGPMKLLTMYPNVAGDVVAISDDNVVAHPYGS
SQ  LHMGKPVLFVTRPNTWKKLVPLLSTVVVNTPNTYDVLAVDPLPVNNETSEEPISVKAPIPLYGLKATMVLNGTTYVPGNK
SQ  GHLLCLKEFTLTDLQTFYVEGVQPFVLLKASHLSKVLGLRVSDSSLHVNHLSKGVVYAYAATRLTTRVTTSLLGGLVTRS
SQ  VRKTADFVRSTNPGSKCVGLLCLFYQLFMRFWLLVKKPPIVKVSGIIAYNTGCGVTTCVLNYLRSRCGNISWSRLLKLLR
SQ  YMLYIWFVWTCLTICGVWLSEPYAPSLVTRFKYFLGIVMPCDYVLVNETGTGWLHHLCMAGMDSLDYPALRMQQHRYGSP
SQ  YNYTYILMLLEAFFAYLLYTPALPIVGILAVLHLIVLYLPIPLGNSWLVVFLYYIIRLVPFTSMLRMYIVIAFLWLCYKG
SQ  FLHVRYGCNNVACLMCYKKNVAKRIECSTVVNGVKRMFYVNANGGTHFCTKHNWNCVSCDTYTVDSTFICRQVALDLSAQ
SQ  FKRPIIHTDEAYYEVTSVEVRNGYVYCYFESDGQRSYERFPMDAFTNVSKLHYSELKGAAPAFNVLVFDATNRIEENAVK
SQ  TAAIYYAQLACKPILLVDKRMVGVVGDDATIARAMFEAYAQNYLLKYSIAMDKVKHLYSTALQQISSGMTVESVLKVFVG
SQ  STRAEAKDLESDVDTNDLVSCIRLCHQEGWEWTTDSWNNLVPTYIKQDTLSTLEVGQFMTANAKYVNANIAKGAAVNLIW
SQ  RYADFIKLSESMRRQLKVAARKTGLNLLVTTSSLKADVPCMVTPFKIIGGHRRIVSWRRVLIHVFMLLVVLNPQWFTPWY
SQ  IMRPIEYNVVDFKVIDNAVIRDITSADQCFANKFSAFENWYSNRYGSYVNSRGCPMVVGVVSDIVGSLVPGLPARFLRVG
SQ  TTLLPLVNYGLGAVGSVCYTPHYAINYDVFDTSACVLAATCTLFSSASGERMPYCADAALIQNASRYDMLKPHVMYPFYE
SQ  HSGYIRFPEVISAGVHIVRTMAMEYCKVGRCDVSEAGLCMSLQPRWVVNNAYFRQQSGVYCGTSAFDLFMNMLLPIFTPV
SQ  GAVDITTSILMGALLAVVVSMSLYYLLRFRRAFGDYSGVIFTNILAFVLNVIVLCLEGPYPMLPSIYAMVFLYATCYFGS
SQ  DIACMMHVSFLIMFAGVVPLWVTVLYIVVVLSRHILWFASLCTKRTVQVGDLAFHSFQDAALQTFMLDKEVFLRLKREIS
SQ  SDAYFKYLAMYNKYKYYSGPMDTAAYREAACSHLVMALEKYSNGGGDTIYQPPRCSVASAALQAGLTRMAHPSGLVEPCL
SQ  VKVNYGSMTLNGIWLDNFVICPRHVMCSRDELANPDYPRLSMRAANYDFHVSQNGHNIRVIGHTMEGSLLKLTVDVNNPK
SQ  TPAYSFIRVSTGQAMSLLACYDGLPTGVYTCTLRSNGTMRASFLCGSCGSPGFVMNGKEVQFCYLHQLELPNGTHTGTDF
SQ  SGVFYGPFEDKQVPQLAAPDCTITVNVLAWLYAAVLSGENWFLTKSSISPAEFNNCAVKYMCQSVTSESLQVLQPLAAKT
SQ  GISVERMLSALKVLLSAGFCGRTIMGSCSLEDEHTPYDIGRQMLGVKLQGKFQSMFRWTLQWFAIIFVLTILILLQLAQW
SQ  TFVGALPFTLLLPLIGFVAVCVGFVSLLIKHKHTYLTVYLLPVAMVTAYYNFQYTPEGVQGYLLSLYNYVNPGRIDVIGT
SQ  DLLTMLIISVACTLLSVRMVRTDAYSRIWYVCTAVGWLYNCWTGSADTVAISYLTFMVSVFTNYTGVACASLYAAQFMVW
SQ  VLKFLDPTILLLYGRFRCVLVCYLLVGYLCTCYFGVFNLINRLFRCTLGNYEYVVSSQELRYMNSHGLLPPTNSWQALML
SQ  NIKLAGIGGIPIYRVSTIQSNMTDLKCTSVVLLSVLQQLRVESSSKLWALCVKLHNEILASNSPTEAFEAFVSLLSVLLS
SQ  LPGAINLDELCSSILENNSVLQAVASEFSNLSSYVDYENAQKAYDTAVATGAPASTVNALKKAMNVAKSVLDKDVATTRK
SQ  LERMSELAMTAMYKQARAEDRRSKVTAAMQTMLFNMIRRLDSDALSNILNNARNGVVPLGVIPRTAANKLLLVVPDFSVY
SQ  TATITMPTLTYAGSAWDVMQVADADGKTVNATDITRENSVNLAWPLVVTAQRQQATSPVKLQNNELMPQTVKRMNVVAGV
SQ  SQTACVTDAVAYYNATKEGRHVMAILADTDGLAFAKVEKSTGDGFVILELEPPCKFMVDTPKGPALKYLYFTKGLKNLCR
SQ  GTVLGTLACTVRLHAGSATEVASNSSILSLCSFSVDPEATYKDYLDNGGSPIGNCVKMLTPHTGTGLAITAKPDANIDQE
SQ  SFGGASCCLYCRCHIEHPGASGVCKYKGKFVQIPLVGVNDPIGFCIRNVVCAVCNMWQGYGCPCSSLREINLQARDECFL
SQ  NESGVLVE
//
ID  P0C6T7;
PN  Non-structural protein 11;
GN  1a;
OS  349344;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6T7;
DR  UNIPROT: Q3I5J6;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF12379;
DR  Pfam: PF12124;
DR  Pfam: PF11633;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DR  PROSITE: PS51940;
DE  Function: The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0008242;
GO  GO:0003727;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESLVLGINEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKSGTCGIVELEKGVLPQPEQPYVFIKRSDAQGTD
SQ  HGHRVRELVAELDGVQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSFGIDLKSYDLGDELGTDPIEDYEQN
SQ  WNTKHGSGVLRELTRELNGGALTRYVDNNFCGPDGYPLECIKDLLARAGKSMCTLSEQLDYIESKRGVYCCRDHGHEIAW
SQ  FTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVATPQECNNMHLSTL
SQ  MKCNHCDEVSWQTCDFLKATCEQCGTENLVSEGPNTCGYLPTNAVVKMPCPACQDPEIGPEHSAADYHNHSNIETRLRKG
SQ  GRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFQLNEEVAIILASF
SQ  SASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPIKGAWNIGQHRSVLTPLCGFPSQAAGVIRSIFSRTLDAANHSIP
SQ  DLQRAAVTILDSISEQSLRLVDAMVYTSNLLTNSVIIMAYVTGGLVQQTSQWLSNLLDTTVEKLRPIFAWIEAKLSAGVE
SQ  FLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFVDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQC
SQ  IRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAVVGTPVCINGLMLLEIKANEQYC
SQ  ALSPGLLATNNVFRLKGGAPTKGVTFGEDTVVEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAV
SQ  VKTLQPVSDLLTNMGIDLDEWSVATFYLFDDSGEEKLSSRMYCSFYPPDEEEDCEEYEEEEEVSERTCEHEYGTEEDYKG
SQ  LPLEFGASTDIIQVEEQEEEDWLDDAVEAEPEPEPLHEEPVNQLTGYLKLTDNVAIKCVDIVEEAQNANPMVIVNAANIH
SQ  LKHGGGVAGALNKATNGAMQKESDHYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDIL
SQ  LAPLLSAGIFGAKPLQSLQMCVQTVRTQVYIVVNDKVLYEQVVMDYLDSLKPKVEAPKQEVLPKAEYPKVDEKSVVQKTI
SQ  DVKPKIKACIDEVTTTLEETKFLTNKLLLFTDINGKLYQDSKNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKA
SQ  GGTTEMLSRALKKVPINEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSETPNAKEEILGTVSWNLREMLAHAEETR
SQ  KLMPVCMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCM
SQ  RSLKAPAIVSVSSPDAVTTYNGYLTSSSKTSEDHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGEKIVYHTLESPVKFH
SQ  LDGEVLPLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQLGPTYLEGADVTKIKPHVNHEGKTFFVLPSDD
SQ  TLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQIEVKFNAPALQEAYYRARAG
SQ  DAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKMGVSI
SQ  PCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTD
SQ  VFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLIPTQPLPNASFDNFKLTCSNTKFADDLNQMT
SQ  GFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSF
SQ  EVLAVEDTQGMDNLACESQQPTPEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELDHEDLMAAYVENTSI
SQ  TIKKPNELSLALGLKTIATHGIAAINSVPWGKILAYVKPFLGQAAVTTSNCAKRLVQRMFNNYMPYVLTLLFQLCTFTKS
SQ  TNSRIRASLPTTIAKNSVRGIVRLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLIYVTAALGVLLSNFGAPSYCSG
SQ  VRESYLNSSNVTTMDFCEGSFPCSVCLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWFFAYMLFTKFFYLLGLSA
SQ  IMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVECTT
SQ  IVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYVVDSVAVKNGALHLYF
SQ  DKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESAAKSASVYYSQLMCQPILLLDQALVSDVGDSTE
SQ  VSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSASRQGVVDTDVDTKDVIECLKLSHHSDLEV
SQ  TGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVARSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCA
SQ  TTRQVVNVITTKISLKGGKIVSTWFKIMLKATLLCVLAALVCYIVMPVHILSVHGGYTNEIIGYKAIQDGVTRDIVSTDD
SQ  CFANKHAGFDSWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLIEY
SQ  SDFSTSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNAYLEGSVRVVTTFDAEYCR
SQ  HGTCERSEAGICLSTSGRWVLNNEHYRALPGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFM
SQ  KFRRAFGEYNHVVAANAPLFLMSFTILCLAPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYV
SQ  FCISLKHFHWFFNNYLRKRVVFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDTTS
SQ  YREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHV
SQ  ICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSP
SQ  SGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTEVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITL
SQ  NVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTIL
SQ  GSTILEDEFTPFDVVRQCSGVTFQGKFKRIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAVAACA
SQ  MLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLVLMTARTVYDDAA
SQ  RRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCF
SQ  LGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDV
SQ  KCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIA
SQ  SEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRNAAMQRKLEKMADQAMTQMYKQARSEDKRAKV
SQ  TSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDAD
SQ  SKIVQLSEINMENSSNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALL
SQ  SDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLHFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANST
SQ  VLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDL
SQ  KGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPMMQSADASTFLNGFAV
//
ID  P0C6T8;
PN  Non-structural protein 11;
GN  1a;
OS  233262;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6T8;
DR  UNIPROT: Q91A29;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDIVCSTTAQKLETGGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNTRPYDLEVLLQDALQSREAVLVTPPLGMSLEACYVRGCNPNGWTMGLFRRRSVCNTGRCAVNKHVAYQLYMIDPAGV
SQ  CFGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKCGEKGAYNKDHKRGGFEHVYNFKVEDAYDLVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGGLADGLEAYADKTLQEMKALFPIWSQELPFDVTVAWHVVRDPRYVMRLQSASTIRSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQHNLVDIMSCFYMEADAVVNAFYGVDLKDCGFVMQFGYIDCEQDLCDFK
SQ  GWVPGNMIDGFACTTCGHVYETGDLLAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDGLVYTGVVGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLLNRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYADKICHAVVSKSKELLDVSLDSLSAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFRSVAKVVLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGSKIYEVERGLLHSSQLPLDVYDLTMPSQVQKAKQKPIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDGHVGLLDQAWRVPCAGRRVTFKEQPTVNEIASTPKTIKVFYELD
SQ  KDFNTILNTACGVFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNSLFLFDEAGEEVLASKLYCA
SQ  FTAPEDDDFLEESGVEEDDVEGEETDLTVTSAGEPCVASEQEESSEILEDTLDDGPCVETSDSQVEEDVEMSDFADLESV
SQ  IQDYENVCFEFYTTEPEFVKVLDLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVVPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHVCKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRSVYKAACVVDVNDSHSMAVVDGKQIDDHRVTSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKRVKAEVVVNPANGHMAHGGGVAKAIAVAAGQQFVKETTDMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYALLERVYKHLNKYDCVVTTLISAGIFSVPSDVSLTYLLGTAEKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAERLSFNVGRSIVYETDANKLILSNDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVVPEGWRVVNKFYQINGV
SQ  RTVKYFECPGGIDICSQDKVFGYVQQGSFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCSKWQVVFNGKYFTFKQANNNCFVNVSCLML
SQ  QSLNLKFKIVQWQEAWLEFRSGRPARFVSLVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  VDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFKGDKVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGNLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYNPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTICDILNAKLGFDSSKEFVEYKVTEWPTATGDVVLATDDLYVKRYERGCITFGKPVIWLSHEQASLNSLTYF
SQ  NRPLLVDENKFDVLKVDDVDDGGDISESDAKESKEINIIKLSGVKKPFKVEDSVIVNDDTSEIKYVKSLSIVDVYDMWLT
SQ  GCRYVVRTANALSMAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPVFNVVKAVRNKISACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEVASKLTCKLVALAFKNAFLTFKWSVVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQW
SQ  IKSTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELFMLSTLHWSVRLLVSLANMLPAHVFMRFYIIIASFIKLFILFRHVAYGCSKPGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDVMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCYMRLFYERDGQRTYDDVNASLFVDYSNLLHSKVKGVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  NLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKGDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKAC
SQ  CKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFLLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVVDQDLGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFAMADGSPQPYCYTEGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVR
SQ  IVRTRSMSYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLVFYYLIKLKRAFGDYTSIVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYISVVVSNHAFWVFAYCRRLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLDD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  VQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLVKGIVCWIMASTFLFSCIITAFVKWTMFMYVTTNMLSITFCALCV
SQ  ISLAMLLVKHKHLYLTMYIIPVLFTLLYNNYLVVYKQTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLIGMVFVTLRSI
SQ  NHDLFSFIMFVGRVISVVSLWYMGSNLEEEILLMLASLFGTYTWTTALSMAAAKVIAKWVAVNVLYFTDIPQIKIVLVCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANVVLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEARSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVW
SQ  QIQTIQDSDGTNKQLNEISDDCNWPLVIIANRHNEVSATVLQNNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSNNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTNQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQSKDTNFLNGFGVRV
//
ID  P0C6T9;
PN  Non-structural protein 11;
GN  1a;
OS  233264;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6T9;
DR  UNIPROT: Q8V439;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDIVCSTTAQKLETGGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNTRPYDLEVLLQDALQSREAVLVTPPLGMSLEACYVRGCNPNGWTMGLFRRRSVCNTGRCAVNKHVAYQLYMIDPAGV
SQ  CFGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKCGEKGAYNKDHKRGGFEHVYNFKVEDAYDLVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGGLADGLEAYADKTLQEMKALFPIWSQELPFDVTVAWHVVRDPRYVMRLQSASTIRSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQHNLVDIMSCFYMEADAVVNAFYGVDLKDCGFVMQFGYIDCEQDLCDFK
SQ  GWVPGNMIDGFACTTCGHVYETGDLLAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDGLVYTGVVGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLLNRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYADKICHAVVSKSKELLDVSLDSLSAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFRSVAKVVLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGSKIYEVERGLLHSSQLPLDVYDLTMPSQVQKAKQKPIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDGHVGLLDQAWRVPCAGRRVTFKEQPTVNEIASTPKTIKVFYELD
SQ  KDFNTILNTACGVFEVDDTVDMEEFYAVVVDAIEEKLSPCKELEGVGAKVSAFLQKLEDNSLFLFDEAGEEVLASKLYCA
SQ  FTAPEDDDFLEESGVEEDDVEGEETDLTVTSAGEPCVASEQEESSEILEDTLDDGPCVETSDSQVEEDVEMSDFADLESV
SQ  IQDYENVCFEFYTTEPEFVKVLDLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVVPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHVCKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRSVYKAACVVDVNDSHSMAVVDGKQIDDHRVTSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKRVKAEVVVNPANGHMAHGGGVAKAIAVAAGQQFVKETTDMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYALLERVYKHLNKYDCVVTTLISAGIFSVPSDVSLTYLLGTAEKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAERLSFNVGRSIVYETDANKLILSNDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVVPEGWRVVNKFYQINGV
SQ  RTVKYFECPGGIDICSQDKVFGYVQQGSFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGENFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCSKWQVVFNGKYFTFKQANNNCFVNVSCLML
SQ  QSLNLKFKIVQWQEAWLEFRSGRPARFVSLVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  VDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFKGDKVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGNLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYKPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTICDILNAKLGFDSSKEFVEYKVTEWPTATGDVVLATDDLYVKRYERGCITFGKPVIWLSHEQASLNSLTYF
SQ  NRPLLVDENKFDVLKVDDVDDGGDISESDAKESKEINIIKLSGVKKPFKVEDSVIVNDDTSEIKYVKSLSIVDVYDMWLT
SQ  GCRYVVRTANDLSMAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPVFNVVKAVRNKISACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEVASKLTCKLVALAFKNAFLTFKWSVVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQW
SQ  IKSTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELFMLSTLHWSVRLLVSLANMLPAHVFMRFYIIIASFIKLFSLFRHVAYGCSKPGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDVMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCYMRLFYERDGQRTYDDVNASLFVDYSNLLHSKVKGVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  NLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKGDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKAC
SQ  CKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFLLSLVCFIGLWCLMPTYTVHKSDFQLPVYTSYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVVDQDLGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFAMADGSPQPYCYTEGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVR
SQ  IVRTRSMSYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLVFYYLIKLKRAFGDYTSIVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYISVVVSNHAFWVFAYCRRLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLDD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  VQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLVKGIVCWIMASTFLFSCIITAFVKWTMFMYVTTNMLSITFCALCV
SQ  ISLAMLLVKHKHLYLTMYIIPVLFTLLYNNYLVVYKQTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLIGMVFVTLRSI
SQ  NHDLFSFIMFVGRVISVVSLWYMGSNLEEEILLMLASLFGTYTWTTALSMAAAKVIAKWVAVNVLYFTDIPQIKIVLVCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANVVLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEARSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVW
SQ  QIQTIQDSDGTNKQLNEISDDCNWPLVIIANRHNEVSATVLQNNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSNNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTNQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQSKDTNFLNGFGVRV
//
ID  P0C6U0;
PN  Non-structural protein 11;
GN  1a;
OS  11132;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6U0;
DR  UNIPROT: Q66198;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
DE  Interaction: P10527; IntAct: EBI-25666661; Score: 0.40
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDIVCSTTAQKLETGGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNTRPYDLEVLLQDALQSREAVLVTPPLGMSLEACYVRGCNPNGWTMGLFRRRSVCNTGRCAVNKHVAYQLYMIDPAGV
SQ  CFGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKCGEKGAYNKDHKRGGFEHVYNFKVEDAYDLVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGGLADGLEAYADKTLQEMKALFPIWSQELPFDVTVAWHVVRDPRYVMRLQSASTIRSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQHNLVDIMSCFYMEADAVVNAFYGVDLKDCGFVMQFGYIDCEQDLCDFK
SQ  GWVPGNMIDGFACTTCGHVYETGDLLAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDGLVYTGVVGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLLNRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYAGKICHAVVSKSKELLDVSLDSLGAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFRSVAKVVLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGSKIYEVERGLLHSSQLPLDVYDLTMPSQVQKTKQKPIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDGHVGLLDQAWRVPCAGRCVTFKEQPTVNEIASTPKTIKVFYELD
SQ  KDFNTILNTACGVFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNSLFLFDEAGEEVLAPKLYCA
SQ  FTAPEDDDFLEESGVEEDDVEGEETDLTVTSAGEPCVASEQEESSEILEDTLDDGPCVETSDSQVEEDVQMSDFVDLESV
SQ  IQDYENVCFEFYTTEPEFVKVLDLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVVPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHVCKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRSVYKAACVVDVNDSHSMAVVDGKQIDDHRITSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKRVKAEVVVNPANGHMAHGGGVAKAIAVAAGQQFVKETTDMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYALLERVYKHLNKYDCVVTTLISAGIFSVPSDVSLTYLLGTAKKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAERLSFNVGRSIVYETDANKLILSNDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVVPEGWRVVNKFYQINGV
SQ  RTVKYFECPGGIDICSQDKVFGYVQQGSFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCSKWQVVFNGKYFTFKQANNNCFVNVSCLML
SQ  QSLNLKFKIVQWQEAWLEFRSGRPARFVSLVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  VDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFKGDKVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGNLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYKPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTVCDILNAKLGFDSSKEFVEYKVTEWPTATGDVVLATDDLYVKRYERGCITFGKPVIWLSHEQASLNSLTYF
SQ  NRPLLVDENKFDVLKVDDVDDGGDISESDAKEPKEINIIKLSGVKKPFKVEDSVIVNDDTSEIKYVKSLSIVDVYDMWLT
SQ  GCRCVVRTANALSRAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPVFNVVKAVRNKISACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEVASKLTCKLVALAFKNAFLTFKWSVVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQW
SQ  IKNTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELFMLSTLHWSVRLLVSLANMLPAHVFMRFYIIIASFIKLFSLFRHVAYGCSKSGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDAMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCYMRLFYDRDGQRTYDDVNASLFVDYSNLLHSKVKSVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  NLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKGDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKAC
SQ  CKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFVLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVVDQDFGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFAMADGSPQPYCYTDGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVR
SQ  IVRTRSMPYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLVFYYLIKLKRAFGDYTSIVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYISVVVSNHAFWVFSYCRQLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLGD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVVYVIMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  VQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKHLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLVKGIVCWIMASTFLFSCIITAFVKWTMFMYVTTNMLSITFCALCV
SQ  ISLTMLLVKHKHLYLTMYIIPVLFTLLYNNYLVVYKQTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLIGMVFVTLRSI
SQ  NQYLFSFIMFVGRVISVVSLWYMGSNLEEEILLMLASLFGTYTWTTALSMAAAKVIAKWVAVNVLYFTDIPQIKIVLVCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANVVLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEACSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVW
SQ  QIQTIQDSDGTNKQLHEISDDCNWPLVIIANRHNEVSATALQNNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSYNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTSQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQSKDTNFLNGFGVRV
//
ID  P0C6U1;
PN  Non-structural protein 11;
GN  1a;
OS  11133;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6U1;
DR  UNIPROT: Q8V6W7;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDIVCSTTAQKLETGGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNTRPYDLEVLLQDALQSREAVLVTPPLGMSLEACYVRGCNPNGWTMGLFRRRSVCNTGRCAVNKHVAYQLYMIDPAGV
SQ  CFGAGQFVGWVIPLAFMPVQSRKFIAPWVMYLRKCGEKGAYIKDYKRGGFEHVYNFKVEDAYDLVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGGLADGLEAYADKTLQEMKALFPIWSQELPFDVTVAWHVVRDPRYVMRLQSASTIRSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQHNLVDIMSCFYMEADAVVNAFYGVDLKDCGFVMQFGYIDCEQDLCDFK
SQ  GWVPGNMIDGFACTTCGHVYETGDLLAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDGLVYTGVVGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLLNRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYAGKICHAVVSKSKELLDVSVDSLGAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFGKNIPRYASAVAQAFRSGAKVGLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGSKIYEVERGLLHSSQLPLDVYDLTMPSQVQKTKQKGIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDGHVGLLDQAWRVPCAGRCVTFKEQPTVNEIASTPKTIKVFYELD
SQ  KDFNTILNTACGEFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNSLFLFDEAGEEVLAPKLYCA
SQ  FTAPEDDDFLEESGVEEDDVEGEETDLTVTSAGEPCVASEQEESSEILEDTLDDGPCVETSDSQVEEDVQMSDFGDLESV
SQ  IQDYENVCFEFYTTEPEFVKVLDLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVVPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHVCKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRSVYKAACVVDVNDSHSMAVVDGKQIDDHRITSITSDKFDFIIGHGTSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKRVKAEVVVNPANGHMAHGGGVAKAIAVAAGQQFVKETTDMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYALLERVYKHLNKYDCVVTTLISAGIFSVPSDVSLTYLLGTAKKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAERLSFNVGRSIVYETDANKLILSNDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVVPEGWRVVNKFYQINGV
SQ  RPVKYFECPGGIDICSQDKVFGYVQQGSFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCSKWQVVFNGKYFTFKQANNNCFVNVSCLML
SQ  QSLNLKFKIVQWQEAWLEFRSGRPARFVSLVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  VDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFKGDKVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGNLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYKPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTVCDILNAKLGFDSSKEFVEYKVTEWPTATGDVVLATDDLYVKRYERGCITFGKPVIWLSHEQASLNSLTYF
SQ  NRPLLVDENKFDVLKVDDVDDGGDISESDAKEPKEINIIKLSGVKKPFKVEDSVIVNDDTSEIKYVKSLSIVDVYDMWLT
SQ  GCRCVVRTANALSRAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPVFNVVKAVRNKISACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEVASKLTCKLVALAFKNAFLTFKWSVVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIVQW
SQ  IKNTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELLMLSTLHWSVRLLVSLANMLPAHVFMRFYIIIASFIKLFSLFRHVAYGCSKSGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDVMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCYMRLFYDRDGQRTYDDVNASLFVDYSNLLHSKVKSVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  ILITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKGDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKAC
SQ  CKTGLKLELTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFVLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVVDQDFGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFAMADGSPQPYCYTDGLMQNASLYSSLVPHVRYNLANAKGFIRLPEVLREGLVR
SQ  IVRTRSMSYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLGFYYLIKLKRAFGDYTSIVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYISVVVSNHAFWVFSYCRQLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLDD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVIMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  VQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLVKGIVCWIMASTFLFSCIITAFVKWTMFMYVTTNMLSITFCALCV
SQ  ISLAMLLVKHKHLYLTMYIIPVLFTLLYNNYLVVYKQTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLIGMVFVTLRSI
SQ  NHDLFSFIMFVGRVISVVSLWYMGSNLEEEILLMLASLFGTYTWTTALSMAAAKVIAKWVAVNVLYFTDIPQIKIVLVCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANGGLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEACSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVW
SQ  QIQTIQDSDGTNKQLHEISDDCNWPLVIIANRHNEVSATVLQNNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSYNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTSQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQSKDTNFLNGFGVRV
//
ID  P0C6U2;
PN  Non-structural protein 11;
GN  1a;
OS  11137;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6U2;
DR  UNIPROT: Q05002;
DR  PDB: 1P9S;
DR  PDB: 2ZU2;
DR  PDB: 3EWQ;
DR  PDB: 3EWR;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MACNRVTLAVASDSEISANGCSTIAQAVRRYSEAASNGFRACRFVSLDLQDCIVGIADDTYVMGLHGNQTLFCNIMKFSD
SQ  RPFMLHGWLVFSNSNYLLEEFDVVFGKRGGGNVTYTDQYLCGADGKPVMSEDLWQFVDHFGENEEIIINGHTYVCAWLTK
SQ  RKPLDYKRQNNLAIEEIEYVHGDALHTLRNGSVLEMAKEVKTSSKVVLSDALDKLYKVFGSPVMTNGSNILEAFTKPVFI
SQ  SALVQCTCGTKSWSVGDWTGFKSSCCNVISNKLCVVPGNVKPGDAVITTQQAGAGIKYFCGMTLKFVANIEGVSVWRVIA
SQ  LQSVDCFVASSTFVEEEHVNRMDTFCFNVRNSVTDECRLAMLGAEMTSNVRRQVASGVIDISTGWFDVYDDIFAESKPWF
SQ  VRKAEDIFGPCWSALASALKQLKVTTGELVRFVKSICNSAVAVVGGTIQILASVPEKFLNAFDVFVTAIQTVFDCAVETC
SQ  TIAGKAFDKVFDYVLLDNALVKLVTTKLKGVRERGLNKVKYATVVVGSTEEVKSSRVERSTAVLTIANNYSKLFDEGYTV
SQ  VIGDVAYFVSDGYFRLMASPNSVLTTAVYKPLFAFNVNVMGTRPEKFPTTVTCENLESAVLFVNDKITEFQLDYSIDVID
SQ  NEIIVKPNISLCVPLYVRDYVDKWDDFCRQYSNESWFEDDYRAFISVLDITDAAVKAAESKAFVDTIVPPCPSILKVIDG
SQ  GKIWNGVIKNVNSVRDWLKSLKLNLTQQGLLGTCAKRFKRWLGILLEAYNAFLDTVVSTVKIGGLTFKTYAFDKPYIVIR
SQ  DIVCKVENKTEAEWIELFPHNDRIKSFSTFESAYMPIADPTHFDIEEVELLDAEFVEPGCGGILAVIDEHVFYKKDGVYY
SQ  PSNGTNILPVAFTKAAGGKVSFSDDVEVKDIEPVYRVKLCFEFEDEKLVDVCEKAIGKKIKHEGDWDSFCKTIQSALSVV
SQ  SCYVNLPTYYIYDEEGGNDLSLPVMISEWPLSVQQAQQEATLPDIAEDVVDQVEEVNSIFDIETVDVKHDVSPFEMPFEE
SQ  LNGLKILKQLDNNCWVNSVMLQIQLTGILDGDYAMQFFKMGRVAKMIERCYTAEQCIRGAMGDVGLCMYRLLKDLHTGFM
SQ  VMDYKCSCTSGRLEESGAVLFCTPTKKAFPYGTCLNCNAPRMCTIRQLQGTIIFVQQKPEPVNPVSFVVKPVCSSIFRGA
SQ  VSCGHYQTNIYSQNLCVDGFGVNKIQPWTNDALNTICIKDADYNAKVEISVTPIKNTVDTTPKEEFVVKEKLNAFLVHDN
SQ  VAFYQGDVDTVVNGVDFDFIVNAANENLAHGGGLAKALDVYTKGKLQRLSKEHIGLAGKVKVGTGVMVECDSLRIFNVVG
SQ  PRKGKHERDLLIKAYNTINNEQGTPLTPILSCGIFGIKLETSLEVLLDVCNTKEVKVFVYTDTEVCKVKDFVSGLVNVQK
SQ  VEQPKIEPKPVSVIKVAPKPYRVDGKFSYFTEDLLCVADDKPIVLFTDSMLTLDDRGLALDNALSGVLSAAIKDCVDINK
SQ  AIPSGNLIKFDIGSVVVYMCVVPSEKDKHLDNNVQRCTRKLNRLMCDIVCTIPADYILPLVLSSLTCNVSFVGELKAAEA
SQ  KVITIKVTEDGVNVHDVTVTTDKSFEQQVGVIADKDKDLSGAVPSDLNTSELLTKAIDVDWVEFYGFKDAVTFATVDHSA
SQ  FAYESAVVNGIRVLKTSDNNCWVNAVCIALQYSKPHFISQGLDAAWNKFVLGDVEIFVAFVYYVARLMKGDKGDAEDTLT
SQ  KLSKYLANEAQVQLEHYSSCVECDAKFKNSVASINSAIVCASVKRDGVQVGYCVHGIKYYSRVRSVRGRAIIVSVEQLEP
SQ  CAQSRLLSGVAYTAFSGPVDKGHYTVYDTAKKSMYDGDRFVKHDLSLLSVTSVVMVGGYVAPVNTVKPKPVINQLDEKAQ
SQ  KFFDFGDFLIHNFVIFFTWLLSMFTLCKTAVTTGDVKIMAKAPQRTGVVLKRSLKYNLKASAAVLKSKWWLLAKFTKLLL
SQ  LIYTLYSVVLLCVRFGPFNFCSETVNGYAKSNFVKDDYCDGSLGCKMCLFGYQELSQFSHLDVVWKHITDPLFSNMQPFI
SQ  VMVLLLIFGDNYLRCFLLYFVAQMISTVGVFLGYKETNWFLHFIPFDVICDELLVTVIVIKVISFVRHVLFGCENPDCIA
SQ  CSKSARLKRFPVNTIVNGVQRSFYVNANGGSKFCKKHRFFCVDCDSYGYGSTFITPEVSRELGNITKTNVQPTGPAYVMI
SQ  DKVEFENGFYRLYSCETFWRYNFDITESKYSCKEVFKNCNVLDDFIVFNNNGTNVTQVKNASVYFSQLLCRPIKLVDSEL
SQ  LSTLSVDFNGVLHKAYIDVLRNSFGKDLNANMSLAECKRALGLSISDHEFTSAISNAHRCDVLLSDLSFNNFVSSYAKPE
SQ  EKLSAYDLACCMRAGAKVVNANVLTKDQTPIVWHAKDFNSLSAEGRKYIVKTSKAKGLTFLLTINENQAVTQIPATSIVA
SQ  KQGAGDAGHSLTWLWLLCGLVCLIQFYLCFFMPYFMYDIVSSFEGYDFKYIENGQLKNFEAPLKCVRNVFENFEDWHYAK
SQ  FGFTPLNKQSCPIVVGVSEIVNTVAGIPSNVYLVGKTLIFTLQAAFGNAGVCYDIFGVTTPEKCIFTSACTRLEGLGGNN
SQ  VYCYNTALMEGSLPYSSIQANAYYKYDNGNFIKLPEVIAQGFGFRTVRTIATKYCRVGECVESNAGVCFGFDKWFVNDGR
SQ  VANGYVCGTGLWNLVFNILSMFSSSFSVAAMSGQILLNCALGAFAIFCCFLVTKFRRMFGDLSVGVCTVVVAVLLNNVSY
SQ  IVTQNLVTMIAYAILYFFATRSLRYAWIWCAAYLIAYISFAPWWLCAWYFLAMLTGLLPSLLKLKVSTNLFEGDKFVGTF
SQ  ESAAAGTFVIDMRSYEKLANSISPEKLKSYAASYNRYKYYSGNANEADYRCACYAYLAKAMLDFSRDHNDILYTPPTVSY
SQ  GSTLQAGLRKMAQPSGFVEKCVVRVCYGNTVLNGLWLGDIVYCPRHVIASNTTSAIDYDHEYSIMRLHNFSIISGTAFLG
SQ  VVGATMHGVTLKIKVSQTNMHTPRHSFRTLKSGEGFNILACYDGCAQGVFGVNMRTNWTIRGSFINGACGSPGYNLKNGE
SQ  VEFVYMHQIELGSGSHVGSSFDGVMYGGFEDQPNLQVESANQMLTVNVVAFLYAAILNGCTWWLKGEKLFVEHYNEWAQA
SQ  NGFTAMNGEDAFSILAAKTGVCVERLLHAIQVLNNGFGGKQILGYSSLNDEFSINEVVKQMFGVNLQSGKTTSMFKSISL
SQ  FAGFFVMFWAELFVYTTTIWVNPGFLTPFMILLVALSLCLTFVVKHKVLFLQVFLLPSIIVAAIQNCAWDYHVTKVLAEK
SQ  FDYNVSVMQMDIQGFVNIFICLFVALLHTWRFAKERCTHWCTYLFSLIAVLYTALYSYDYVSLLVMLLCAISNEWYIGAI
SQ  IFRICRFGVAFLPVEYVSYFDGVKTVLLFYMLLGFVSCMYYGLLYWINRFCKCTLGVYDFCVSPAEFKYMVANGLNAPNG
SQ  PFDALFLSFKLMGIGGPRTIKVSTVQSKLTDLKCTNVVLMGILSNMNIASNSKEWAYCVEMHNKINLCDDPETAQELLLA
SQ  LLAFFLSKHSDFGLGDLVDSYFENDSILQSVASSFVGMPSFVAYETARQEYENAVANGSSPQIIKQLKKAMNVAKAEFDR
SQ  ESSVQKKINRMAEQAAAAMYKEARAVNRKSKVVSAMHSLLFGMLRRLDMSSVDTILNMARNGVVPLSVIPATSAARLVVV
SQ  VPDHDSFVKMMVDGFVHYAGVVWTLQEVKDNDGKNVHLKDVTKENQEILVWPLILTCERVVKLQNNEIMPGKMKVKATKG
SQ  EGDGGITSEGNALYNNEGGRAFMYAYVTTKPGMKYVKWEHDSGVVTVELEPPCRFVIDTPTGPQIKYLYFVKNLNNLRRG
SQ  AVLGYIGATVRLQAGKQTEFVSNSHLLTHCSFAVDPAAAYLDAVKQGAKPVGNCVKMLTNGSGSGQAITCTIDSNTTQDT
SQ  YGGASVCIYCRAHVAHPTMDGFCQYKGKWVQVPIGTNDPIRFCLENTVCKVCGCWLNHGCTCDRTAIQSFDNSYLNESGA
SQ  LVPLD
//
ID  P0C6U3;
PN  Non-structural protein 11;
GN  1a;
OS  443239;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
DR  UNIPROT: P0C6U3;
DR  UNIPROT: Q5MQD2;
DR  PDB: 3D23;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIKTSKYGLGFKWAPEFRWLLPDAAEELASPMKSDEGGLCPSTGQAMESVGFVYDNHVKIDCRCILGQEWHVQSNLIRDI
SQ  FVHEDLHVVEVLTKTAVKSGTAILIKSPLHSLGGFPKGYVMGLFRSYKTKRYVVHHLSMTTSTTNFGEDFLGWIVPFGFM
SQ  PSYVHKWFQFCRLYIEESDLIISNFKFDDYDFSVEDAYAEVHAEPKGKYSQKAYALLRQYRGIKPVLFVDQYGCDYSGKL
SQ  ADCLQAYGHYSLQDMRQKQSVWLANCDFDIVVAWHVVRDSRFVMRLQTIATICGIKYVAQPTEDVVDGDVVIREPVHLLS
SQ  ADAIVLKLPSLMKVMTHMDDFSIKSIYNVDLCDCGFVMQYGYVDCFNDNCDFYGWVSGNMMDGFSCPLCCTVYDSSEVKA
SQ  QSSGVIPENPVLFTNSTDTVNHDSFNLYGYSVTPFGSCIYWSPRPGLWIPIIKSSVKSYDDLVYSGVVGCKSIVKETALI
SQ  THALYLDYVQCKCGNLEQNHILGVNNSWCRQLLLNRGDYNMLLKNIDLFVKRRADFACKFAVCGDGFVPFLLDGLIPRSY
SQ  YLIQSGIFFTSLMSQFSQEVSDMCLKMCILFMDRVSVATFYIEHYVNRLVTQFKLLGTTLVNKMVNWFNTMLDASAPATG
SQ  WLLYQLLNGLFVVSQANFNFVALIPDYAKILVNKFYTFFKLLLECVTVDVLKDMPVLKTINGLVCIVGNKFYNVSTGLIP
SQ  GFVLPCNAQEQQIYFFEGVAESVIVEDDVIENVKSSLSSYEYCQPPKSVEKICIIDNMYMGKCGDKFFPIVMNDKNICLL
SQ  DQAWRFPCAGRKVNFNEKPVVMEIPSLMTVKVMFDLDSTFDDILGKVCSEFEVEKGVTVDDFVAVVCDAIENALNSCKEH
SQ  PVVGYQVRAFLNKLNENVVYLFDEAGDEAMASRMYCTFAIEDVEDVISSEAVEDTIDGVVEDTINDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNNDEEIVTGDNDDQIVVTGDDVDDIESIYDFDTYKA
SQ  LLVFNDVYNDALFVSYGSSVETETYFKVNGLWSPTITHTNCWLRSVLLVMQKLPFKFKDLAIENMWLSYKVGYNQSFVDY
SQ  LLTTIPKAIVLPQGGFVADFAYWFLNQFDINAYANWCCLKCGFSFDLNGLDALFFYGDIVSHVCKCGHNMTLIAADLPCT
SQ  LHFSLFDDNFCAFCTPKKIFIAACAVDVNVCHSVAVIGDEQIDGKFVTKFSGDKFDFIVGYGMSFSMSSFELPQLYGLCI
SQ  TPNVCFVKGDIINVARLVKADVIVNPANGHMLHGGGVAKAIAVAAGKKFSKETAAMVKSKGVCQVGDCYVSTGGKLCKTI
SQ  LNIVGPDARQDGRQSYVLLARAYKHLNNYDCCLSTLISAGIFSVPADVSLTYLLGVVDKQVILVSNNKEDFDIIQKCQIT
SQ  SVVGTKALAVRLTANVGRVIKFETDAYKLFLSGDDCFVSNSSVIQEVLLLRHDIQLNNDVRDYLLSKMTSLPKDWRLINK
SQ  FDVINGVKTVKYFECPNSIYICSQGKDFGYVCDGSFYKATVNQVCVLLAKKIDVLLTVDGVNFKSISLTVGEVFGKILGN
SQ  VFCDGIDVTKLKCSDFYADKILYQYENLSLADISAVQSSFGFDQQQLLAYYNFLTVCKWSVVVNGPFFSFEQSHNNCYVN
SQ  VACLMLQHINLKFNKWQWQEAWYEFRAGRPHRLVALVLAKGHFKFDEPSDATDFIRVVLKQADLSGAICELELICDCGIK
SQ  QESRVGVDAVMHFGTLAKTDLFNGYKIGCNCAGRIVHCTKLNVPFLICSNTPLSKDLPDDVVAANMFMGVGVGHYTHLKC
SQ  GSPYQHYDACSVKKYTGVSGCLTDCLYLKNLTQTFTSMLTNYFLDDVEMVAYNPDLSQYYCDNGKYYTKPIIKAQFKPFA
SQ  KVDGVYTNFKLVGHDICAQLNDKLGFNVDLPFVEYKVTVWPVATGDVVLASDDLYVKRYFKGCETFGKPVIWFCHDEASL
SQ  NSLTYFNKPSFKSENRYSVLSVDSVSEESQGNVVTSVMESQISTKEVKLKGVRKTVKIEDAIIVNDENSSIKVVKSLSLV
SQ  DVWDMYLTGCDYVVWVANELSRLVKSPTVREYIRYGIKPITIPIDLLCLRDDNQTLLVPKIFKARAIEFYGFLKWLFIYV
SQ  FSLLHFTNDKTIFYTTEIASKFTFNLFCLALKNAFQTFRWSIFIKGFLVVATVFLFWFNFLYINVIFSDFYLPNISVFPI
SQ  FVGRIVMWIKATFGLVTICDFYSKLGVGFTSHFCNGSFICELCHSGFDMLDTYAAIDFVQYEVDRRVLFDYVSLVKLIVE
SQ  LVIGYSLYTVWFYPLFCLIGLQLFTTWLPDLFMLETMHWLIRFIVFVANMLPAFVLLRFYIVVTAMYKVVGFIRHIVYGC
SQ  NKAGCLFCYKRNCSVRVKCSTIVGGVIRYYDITANGGTGFCVKHQWNCFNCHSFKPGNTFITVEAAIELSKELKRPVNPT
SQ  DASHYVVTDIKQVGCMMRLFYDRDGQRVYDDVDASLFVDINNLLHSKVKVVPNLYVVVVESDADRANFLNAVVFYAQSLY
SQ  RPILLVDKKLITTACNGISVTQTMFDVYVDTFMSHFDVDRKSFNNFVNIAHASLREGVQLEKVLDTFVGCVRKCCSIDSD
SQ  VETRFITKSMISAVAAGLEFTDENYNNLVPTYLKSDNIVAADLGVLIQNGAKHVQGNVAKAANISCIWFIDAFNQLTADL
SQ  QHKLKKACVKTGLKLKLTFNKQEASVPILTTPFSLKGGVVLSNLLYILFFVSLICFILLWALLPTYSVYKSDIHLPAYAS
SQ  FKVIDNGVVRDISVNDLCFANKFFQFDQWYESTFGSVYYHNSMDCPIVVAVMDEDIGSTMFNVPTKVLRHGFHVLHFLTY
SQ  AFASDSVQCYTPHIQISYNDFYASGCVLSSLCTMFKRGDGTPHPYCYSDGVMKNASLYTSLVPHTRYSLANSNGFIRFPD
SQ  VISEGIVRIVRTRSMTYCRVGACEYAEEGICFNFNSSWVLNNDYYRSMPGTFCGRDLFDLFYQFFSSLIRPIDFFSLTAS
SQ  SIFGAILAIVVVLVFYYLIKLKRAFGDYTSVVVINVVVWCINFLMLFVFQVYPICACVYACFYFYVTLYFPSEISVIMHL
SQ  QWIVMYGAIMPFWFCVTYVAMVIANHVLWLFSYCRKIGVNVCSDSTFEETSLTTFMITKDSYCRLKNSVSDVAYNRYLSL
SQ  YNKYRYYSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVSTSFLQSGIVKMVSPTSKIEPCIVSVTYGSMT
SQ  LNGLWLDDKVYCPRHVICSSSNMNEPDYSALLCRVTLGDFTIMSGRMSLTVVSYQMQGCQLVLTVSLQNPYTPKYTFGNV
SQ  KPGETFTVLAAYNGRPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLTGDSVKFVYMHQLELSTGCHTGTDFTGNFYGPYR
SQ  DAQVVQLPVKDYVQTVNVIAWLYAAILNNCAWFVQNDVCSTEDFNVWAMANGFSQVKADLVLDALASMTGVSIETLLAAI
SQ  KRLYMGFQGRQILGSCTFEDELAPSDVYQQLAGVKLQSKTKRFIKETIYWILISTFLFSCIISAFVKWTIFMYINTHMIG
SQ  VTLCVLCFVSFMMLLVKHKHFYLTMYIIPVLCTLFYVNYLVVYKEGFRGFTYVWLSYFVPAVNFTYVYEVFYGCILCVFA
SQ  IFITMHSINHDIFSLMFLVGRIVTLISMWYFGSNLEEDVLLFITAFLGTYTWTTILSLAIAKIVANWLSVNIFYFTDVPY
SQ  IKLILLSYLFIGYILSCYWGFFSLLNSVFRMPMGVYNYKISVQELRYMNANGLRPPRNSFEAILLNLKLLGIGGVPVIEV
SQ  SQIQSKLTDVKCANVVLLNCLQHLHVASNSKLWQYCSVLHNEILSTSDLSVAFDKLAQLLIVLFANPAAVDTKCLASIDE
SQ  VSDDYVQDSTVLQALQSEFVNMASFVEYEVAKKNLADAKNSGSVNQQQIKQLEKACNIAKSVYERDKAVARKLERMADLA
SQ  LTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLSAIPALAANTLTIVIPDKQVFDKVVDNVY
SQ  VTYAGSVWHIQTVQDADGINKQLTDISVDSNWPLVIIANRYNEVANAVMQNNELMPHKLKIQVVNSGSDMNCNIPTQCYY
SQ  NNGSSGRIVYAVLSDVDGLKYTKIMKDDGNCVVLELDPPCKFSIQDVKGLKIKYLYFIKGCNTLARGWVVGTLSSTIRLQ
SQ  AGVATEYAANSSILSLCAFSVDPKKTYLDYIQQGGVPIINCVKMLCDHAGTGMAITIKPEATINQDSYGGASVCIYCRAR
SQ  VEHPDVDGICKLRGKFVQVPLGIKDPILYVLTHDVCQVCGFWRDGSCSCVGSSVAVQSKDLNFLNGFGVLV
//
ID  P0C6U4;
PN  Non-structural protein 11;
GN  1a;
OS  443240;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
DR  UNIPROT: P0C6U4;
DR  UNIPROT: Q14EB2;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIKTSKYGLGFKWAPEFRWLLPDAAEELASPMKSDEGGLCPSTGQAMESVGFVYDNHVKIDCRCILGQEWHVQSNLIRDI
SQ  FVHEDLHVVEVLTKTAVKSGTAILIKSPLHSLGGFPKGYVMGLFRSYKTKRYVVHHLSMTTSTTNFGEDFLGWIVPFGFM
SQ  PSYVHKWFQFCRLYIEESDLIISNFKFDDYDFSVEDAYAEVHAEPKGKYSQKAYALLRQYRGIKPVLFVDQYGCDYSGKL
SQ  ADCLQAYGHYSLQDMRQKQSVWLANCDFDIVVAWHVVRDSRFVMRLQTIATICGIKYVAQPTEDVVDGAVVIREPVHLLS
SQ  ADAIVLKLPSLMKVMTHMDDFSIKSIYNVDLCDCGFVMQYGYVDCFNDNCDFYGWVSGNMMDGFSCPLCCTVYDSSEVKA
SQ  QSSGVIPENPVLFTNSTDTVNPDSFNLYGYSVTPFGSCIYWSPRPGLWIPIIKSSVKSYDDLVYSGVVGCKSIVKETALI
SQ  THALYLDYVQCKCGNLEQNHILGVNNSWCRQLLLNRGDYNMLLKNIDLFVKRRADFACKFAVCGDGFVPFLLDGLIPRSY
SQ  YLIQSGIFFTSLMSQFSQEVSDMCLKMCILFMDRVSVATFYIEHYVNRLVTQFKLLGTTLVNKMVNWFNTMLDASAPATG
SQ  WLLYQLLNGLFVVSQANFNFVALIPDYAKILVNKFYTFFKLLLECVTVDVLKDMPVLKTINGLVCIVGNKFYNVSTGLIP
SQ  GFVLPCNAQEQQIYFFEGVAESVIVEDDVIENVKSSLSSYEYCQPPKSVEKICIIDNMYMGKCGDKFFPIVMNDKNICLL
SQ  DQAWRFPCAGRKVNFNEKPVVMEIPSLMTVKVMFDLDSTFDDILGKVCSEFEVEKGVTVDDFVAVVCDAIENALNSCKDH
SQ  PVVGYQVRAFLNKLNENVVYLFDEAGDEAMASRMYCTFAIEDVEDVISSEAVEDTIDGVVEDTINDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEEIVTGDNDDQIVVTGDDVDDIESVYDFDTYKALLVFNDVYNDALFVSYGSSVETETYFKVNG
SQ  LWSPTITHTNCWLRSVLLVMQKLPFKFKDLAIENMWLSYKVGYNQSFVDYLLTTIPKAIVLPQGGYVADFAYWFLNQFDI
SQ  NAYANWCCLKCGFSFDLNGLDAVFFYGDIVSHVCKCGHNMTLIAADLPCTLHFSLFDDNFCAFCTPKKIFIAACAVDVNV
SQ  CHSVAVIGDEQIDGKFVTKFSGDKFDFIVGYGMSFSMSSFELAQLYGLCITPNVCFVKGDIINVARLVKADVIVNPANGH
SQ  MLHGGGVAKAIAVAAGKKFSKETAAMVKSKGVCQVGDCYVSTGGKLCKTILNIVGPDARQDGRQSYVLLARAYKHLNNYD
SQ  CCLSTLISAGIFSVPADVSLTYLLGVVDKQVILVSNNKEDFDIIQKCQITSVVGTKALAVRLTANVGRVIKFETDAYKLF
SQ  LSGDDCFVSNSSVIQEVLLLRHDIQLNNDVRDYLLSKMTSLPKDWRLINKFDVINGVKTVKYFECPNSIYICSQGKDFGY
SQ  VCDGSFYKATVNQVCVLLAKKIDVLLTVDGVNFKSISLTVGEVFGKILGNVFCDGIDVTKLKCSDFYADKILYQYENLSL
SQ  ADISAVQSSFGFDQQQLLAYYNFLTVCKWSVVVNGPFFSFEQSHNNCYVNVACLMLQHINLKFNKWQWQEAWYEFRAGRP
SQ  HRLVALVLAKGHFKFDEPSDATDFIRVVLKQADLSGAICELELICDCGIKQESRVGVDAVMHFGTLAKTDLFNGYKIGCN
SQ  CAGRIVHCTKLNVPFLICSNTPLSKDLPDDVVAANMFMGVGVGHYTHLKCGSPYQHYDACSVKKYTGVSGCLTDCLYLKN
SQ  LTQTFTSMLTNYFLDDVEMVAYNPDLSQYYCDNGKYYTKPIIKAQFKPFAKVDGVYTNFKLVGHDICAQLNDKLGFNVDL
SQ  PFVEYKVTVWPVATGDVVLASDDLYVKRYFKGCETFGKPVIWLCHDEASLNSLTYFNKPSFKSENRYSVLSVDSVSEESQ
SQ  GNVVTSVMESQISTKEVKLKGVRKTVKIEDAIIVNDENSSIKVVKSLSLVDVWDMYLTGCDYVVWVANELSRLVKSPTVR
SQ  EYIRYGIKPITIPIDLLCLRDDNQTLLVPKIFKARAIEFYGFLKWLFIYVFSLLHFTNDKTIFYTTEIASKFTFNLFCLA
SQ  LKNAFQTFRWSIFIKGFLVVATVFLFWFNFLYINVIFSDFYLPNISVFPIFVGRIVMWIKATFGLVTICDFYSKLGVGFT
SQ  SHFCNGSFICELCYSGFDMLDTYAAIDFVQYEVDRRVLFDYVSLVKLIVELVIGYSLYTVWFYPLFCLIGLQLFTTWLPD
SQ  LFMLETMHWLIRFIVFVANMLPAFVLLRFYIVVTAMYKVVGFIRHIVYGCNKAGCLFCYKRNCSVRVKCSTIVGGVIRYY
SQ  DITANGGTGFCVKHQWNCFNCHSFKPGNTFITVEAAIELSKELKRPVNPTDASHYVVTDIKQVGCMMRLFYDRDGQRVYD
SQ  DVDASLFVDINNLLHSKVKVVPNLYVVVVESDADRANFLNAVVFYAQSLYRPILLVDKKLITTACNGISVTQTMFDVYVD
SQ  TFMSHFDVDRKSFNNFVNIAHASLREGVQLEKVLDTFVGCVRKCCSIDSDVETRFITKSMISAVAAGLEFTDENYNNLVP
SQ  TYLKSDNIVAADLGVLIQNGAKHVQGNVAKAANISCIWFIDTFNQLTADLQHKLKKACVKTGLKLKLTFNKQEASVPILT
SQ  TPFSLKGGVVLSNLLYILFFISLICFILLWALLPTYSVYKSDIHLPAYASFKVIDNGVVRDISVNDLCFANKFFQFDQWY
SQ  ESTFGSFYYHNSMDCPIVVAVMDEDIGSTMFNVPTKVLRHGFHVLHFLTYAFASDSVQCYTPHIQISYNDFYASGCVLSS
SQ  LCTMFKRGDGTPHPYCYSDGVMKNASLYTSLVPHTRYSLANSNGFIRFPDVISEGIVRIVRTRSMTYCRVGACEYAEEGI
SQ  CFNFNSSWVLNNDYYRSMPGTFCGRDLFDLFYQFFSSLIRPIDFFSLTASSIFGAILAIVVVLVFYYLIKLKRAFGDYTS
SQ  VVVINVIVWCINFLMLFVFQVYPICACVYACFYFYVTLYFPSEISVIMHLQWIVMYGAIMPFWFCVTYVAMVIANHVLWL
SQ  FSYCRKIGVNVCNDSTFEETSLTTFMITKDSYCRLKNSVSDVAYNRYLSLYNKYRYYSGKMDTAAYREAACSQLAKAMET
SQ  FNHNNGNDVLYQPPTASVSTSFLQSGIVKMVSPTSKIEPCIVSVTYGSMTLNGLWLDDKVYCPRHVICLSSNMNEPDYSA
SQ  LLCRVTLGDFTIMSGRMSLTVVSYQMQGCQLVLTVSLQNPYTPKYTFGVVKPGETFTVLAAYNGRPQGAFHVTMRSSYTI
SQ  KGSFLCGSCGSVGYVLTGDSVKFVYMHQLELSTGCHTGTDFTGNFYGPYRDAQVVQLPVKDYVQTVNVIAWLYAAILNNC
SQ  AWFVQNDVCSIEDFNVWAMTNGFSQVKADLVLDALASMTGVSIETLLAAIKRLYMGFQGRQILGSCTFEDELAPSDVYQQ
SQ  LAGVKLQSKTKRFIKETIYWILISTFLFSCIISAFVKWTIFMYINTHMIGVTLCVLCFVSFMMLLVKHKHFYLTMYIIPV
SQ  LCTLFYVNYLVVYKEGFRGLTYVWLSYFVPAVNFTYVYEVFYGCILCVFAIFITMHSINHDIFSLMFLVGRIVTLISMWY
SQ  FGSNLEEDVLLFITAFLGTYTWTTILSLAIAKIVANWLSVNIFYFTDVPYIKLILLSYLFIGYILSCYWGFFSLLNSVFR
SQ  MPMGVYNYKISVQELRYMNANGLRPPRNSFEAILLNLKLLGIGGVPVIEVSQIQSKLTDVKCANVVLLNCLQHLHVASNS
SQ  RLWQYCSILHNEILSTSDLSVAFDKLAQLLIVLFANPAAVDTKCLASIDEVSDDYVQDSTVLQALQSEFVNMASFVEYEV
SQ  AKKNLADAKNSGSVNQQQIKQLEKACNIAKSVYERDKAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMVR
SQ  KLDNQALNSILDNAVKGCVPLNAIPALAANTLTIIIPDKQVFDKVVDNVYVAYAGSVWHIQTVQDADGINKQLTDISVDS
SQ  NWPLVIIANRYNEVANAVMQNNELMPHKLKIQVVNSGSDMNCNIPTQCYYNNGSSGRIVYAVLSDVDGLKYTKIIKDDGN
SQ  CVVLELDPPCKFSIQDVKGLKIKYLYFIKGCNTLARGWVVGTLSSTIRLQAGVATEYAANSSILSLCAFSVDPKKTYLDY
SQ  IQQGGVPIINCVKMLCDHAGTGMAITIKPEATINQDSYGGASVCIYCRARVEHPDVDGLCKLRGKFVQVPLGIKDPILYV
SQ  LTHDVCQVCGFWRDGSCSCVGSGVAVQSKDLNFLNGFGVLV
//
ID  P0C6U5;
PN  Non-structural protein 11;
GN  1a;
OS  443241;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
DR  UNIPROT: P0C6U5;
DR  UNIPROT: Q0ZME9;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIKTSKYGLGFKWAPEFRWLLPDAAEELASPMKSDEGGLCPSTGQAMESVGFVYDNHVKIDCRCILGQEWHVQSNLIRDI
SQ  FVHEDLHVVEVLTKTAVKSGTAILIKSPLHSLGGFPKGYVMGLFRSYKTKRYVVHHLSMTTSTTNFGEDFFGWIVPFGFM
SQ  PSYVHKWFQFCRLYIEESDLIISNFKFDDYDFSVEAAYAEVHAEPKGKYSQKAYALLRQYRGIKPVLFVDQYGCDYSGKL
SQ  ADCLQAYGHYSLQDMRQKQSVWLANCDFDIVVAWHVVRDSRFVMRLQTIATICGIKYVAQPTEDVVDGDVVIREPVHLLS
SQ  ADAIVLKLPSLMKVMTHMDDFSIKSIYNVDLCDCGFVMQYGYVDCFNDNCDFYGWVSGNMMDGFSCPLCCTVYDSSEVKA
SQ  QSSGVIPENPVLFTNSTDTVNPDSFNLYGYSVTPFGSCIYWSPRPGLWIPIIKSSVKSYDDLVYSGVVGCKSIVKETALI
SQ  THALYLDYVQCKCGNLEQNHILGVNNSWCRQLLLNRGDYNMLLKNIDLFVKRRADFACKFAVCGDGFVPFLLDGLIPRSY
SQ  YLIQSGIFFTSLMSQFSQEVSDMCLKMCILFMDRVSVATFYIEHYVNRLVTQFKLLGTTLVNKMVNWFNTMLDASAPATG
SQ  WLLYQLLNGFFVVSQANLNFVALIPDYAKILVNKFYTFFKLLLECVTVDVLKDMPVLKTINGLVCIVGNKFYNVSTGLIP
SQ  GFVLPCNAQEQQIYFFEGVAESVIVEDDVIENVKSSLSSYEYCQPPKSVEKICIIDNMYMGKCGDKFFPIVMNDKNICLL
SQ  DHAWRFPCAGRKVNFNEKPVVMEIPSLMTVKVMFDLDSTFDDILGKVCSEFEVEKGVTVDDFVAVVCDAIENALNSCKEH
SQ  PVVGYQVRAFLNKLNENVVYLFDEAGDEAMASRMYCTFAIEDVEDVISSEAVEDTIDGVVEDTINDDEDVVTGDNDDEDV
SQ  VTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNDDEDVVTGDNNDEDVVTGDNNDEES
SQ  VTGDNDDQIVVTGDDVDDIESIYDFDTYKALLVFNDVYNDALFVSYGSSVETETYFKVNGLWSPTITHTNCWLRSVLLVM
SQ  QKLPFKFKDLAIENMWLSYKVGYNQSFVDYLLTTIPKAIVLPQGGYVADFAYWFLNQFDINAYANWCCLKCGFSFDLNGL
SQ  DAVFFYGDIVSHVCKCGHNMTLIAADLPCTLHFSLFDDNFCAFCTPKKIFIAACAVDVNVCHSVAVIGDEQIDGKFVTKF
SQ  SGDKFDFIVGYGMSFSMSSFELAQLYGLCITPNVCFVKGDIINVARLVKADVIVNPANGHMLHGGGVAKAIAVAAGKKFS
SQ  KETAAMVKSKGVCQVGDCYVSTGGKLCKTILNIVGPDARQDGRQSYVLLARAYKHLNNYDCCLSTLISAGIFSVPADVSL
SQ  TYLLGVVDKQVILVSNNKEDFDIIQKCQITSVVGTKALAVRLTANVGRVIKFETDAYKLFLSGDDCFVSNSSVIQEVLLL
SQ  RHDIQLNNDVRDYLLSKMTSLPKDWRLINKFDVINGVKTVKYFECPNSIYICSQGKDFGYVCDGSFYKATVNQVCVLLAK
SQ  KIDVLLTVDGVNFKSISLTVGEVFGKILGNVFCDGIDVTKLKCSDFYADKILYQYENLSLADISAVQSSFGFDQQQLLAY
SQ  YNFLTVCKWSVVVNGPFFSFEQSHNNCYVNVACLMLQHINLKFNKWQWQEAWYEFRAGRPHRLVALVLAKGHFKFDEPSD
SQ  ATDFIRVVLKQADLSGAICELELICDCGIKQESRVGVDAVMHFGTLAKTDLFNGYKIGCNCAGRIVHCTKLNVPFLICSN
SQ  TPLSKDLPDDVVAANMFMGVGVGHYTHLKCGSPYQHYDACSVKKYTGVSGCLTDCLYLKNLTQTFTSMLTNYFLDDVEMV
SQ  AYNPDLSQYYCDNGKYYTKPIIKAQFKPFAKVDGVYTNFKLVGHDICAQLNDKLGFNVDLPFVEYKVTVWPVATGDVVLA
SQ  SDDLYVKRYFKGCETFGKPVIWFCHDEASLNSLTYFNKPSFKSENRYSVLSVDSVSEESQGNVVTSVMESQISTKEVKLK
SQ  GVRKTVKIEDAIIVNDENSSIKVVKSLSLVDVWDMYLTGCDYVVWVANELSRLVKSPTVREYIRYGIKPITIPIDLLCLR
SQ  DDNQTLLVPKIFKARAIEFYGFLKWLFIYVFSLLHFTNDKTIFYTTEIASKFTFNLFCLALKNAFQTFRWSIFIKGFLVV
SQ  ATVFLFWFNFLYINVIFSDFYLPNISVFPIFVGRIVMWIKATFGLVTICDFYSKLGVGFTSHFCNGSFICELCHSGFDML
SQ  DTYAAIDFVQYEVDRRVLFDYVSLVKLIVELVIGYSLYTVWFYPLFCLIGLQLFTTWLPDLFMLETMHWLIRFIVFVANM
SQ  LPAFVLLRFYIVVTAMYKVVGFIRHIVYGCNKAGCLFCYKRNCSVRVKCSTIVGGVIRYYDITANGGTGFCVKHQWNCFN
SQ  CHSFKPGNTFITVEAAIELSKELKRPVNPTDASHYVVTDIKQVGCMMRLFYDRDGQRVYDDVDASLFVDINNLLHSKVKV
SQ  VPNLYVVVVESDADRANFLNAVVFYAQSLYRPILLVDKKLITTACNGISVTQIMFDVYVDTFMSHFDVDRKSFNNFVNIA
SQ  HASLREGVQLEKVLDTFVGCVRKCCSIDSDVETRFITKSMISAVAAGLEFTDENYNNLVPTYLKSDNIVAADLGVLIQNG
SQ  AKHVQGNVAKVANISCIWFIDAFNQLTADLQHKLKKACVKTGLKLKLTFNKQEASVPILTTPFSLKGGVVLSNLLYILFF
SQ  ISLICFILLWALLPTYSVYKSDIHLPAYASFKVIDNGVVRDISVNDLCFANKFFQFDQWYESTFGSVYYHNSMDCPIVVA
SQ  VMDEDIGSTMFNVPTKVLRYGFHVLHFLTYAFASDSVQCYTPHIQISYNDFYASGCVLSSLCTMFKRGDGTPHPYCYTDG
SQ  VMKNASLYTSLVPHTRYSLANSNGFIRFPDVISEGIVRIVRTRSMTYCRVGACEYAEEGICFNFNSSWVLNNDYYRSMPG
SQ  TFCGRDFFDLFYQFFSSLIRPIDFFSLTASSIFGAILAIVVVLVFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQ
SQ  VYPICACVYACFYFYVTLYFPSEISVIMHLQWIVMYGAIMPFWFCVTYVAMVIANHVLWLFSYCRKIGVNVCSDSTFEET
SQ  SLTTFMITKDSYCRLKNSVSDVAYNRYLSLYNKYRYYSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVST
SQ  SFLQSGIVKMVSPTSKIEPCLVSVTYGSMTLNGLWLDDKVYCPRHVICLSSNMNEPDYSALLCRVTLGDFTIMSGRMSLT
SQ  VVSYQMQGCQLVLTVSLQNPYTPKYTFGVVKPGETFTVLAAYNGRPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLTGDS
SQ  VKFVYMHQLELSTGCHTGTDFNGNFYGPYRDAQVVQLPVKDYVQTVNVIAWLYAAILNNCAWFVQNDVCSIEDFNVWAMT
SQ  NGFSQVKADLVLDALASMTGVSIETLLAAIKRLYMGFQGRQILGSCTFEDELAPSDVYQQLAGVKLQSKTKRFIKETIYW
SQ  ILISTFLFSCIISAFVKWTIFMYINTHMIGVTLCVLCFVSFMMLLVKHKHFYLTMYIIPVLCTLFYVNYLVVYKEGFRGF
SQ  TYVWLSHFVPAVNFTYVYEVFYGCILCVFAIFITMHSINHDIFSLMFLVGRIVTLISMWYFGSNLEEDVLLFITAFLGTY
SQ  TWTTILSLAIAKIVANWLSVNIFYFTDVPYIKLILLSYLFIGYILSCYWGFFSLLNSVFRMPMGVYNYKISVQELRYMNA
SQ  NGLRPPRNSFEAILLNLKLLGIGGVPVIEVSQIQSKLTDVKCANVVLLNCLQHLHVASNSKLWQYCSVLHNEILSTSDLS
SQ  VAFDKLAQLLIVLFSNPAAVDTKCLASIDEVSDDYVQDSTVLQALQSEFVNMASFVEYEVAKKNLADAKNSGSVNQQQIK
SQ  QLEKACNIAKSVYERDKAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVP
SQ  LSAIPALAANTLTIIIPDKQVFDKVVDNVYVTYAGSVWHIQTVQDADGINKQLTDISVDSNWPLVIIANRYNEVANAVMQ
SQ  NNELMPHKLKIQVVNSGSDINCNIPTQCYYNNVSSGRIVYAVLSDVDGLKYTKIMKDDGNCVVLELDPPCKFSIQDVKGL
SQ  KIKYLYFIKGCNTLARGWVVGTLSSTIRLQAGVATEYAANSSILSLCAFSVDPKKTYLDYIQQGGVPIINCVKMLCDHAG
SQ  TGMAITIKPEATINQDSYGGASVCIYCRARVEHPDVDGICKLRGKFVQVPLGIKDPILYVLTHDVCQVCGFWRDGSCSCV
SQ  GSSVAVQSKDLNFLNGLGVLV
//
ID  P0C6U6;
PN  Non-structural protein 11;
GN  1a;
OS  277944;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6U6;
DR  UNIPROT: Q6Q1S3;
DR  PDB: 2VRI;
DR  PDB: 3TLO;
DR  PDB: 5GWY;
DR  PDB: 7E6L;
DR  PDB: 7E6M;
DR  PDB: 7E6N;
DR  PDB: 7E6R;
DR  PDB: 7EO7;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3. {ECO:0000269|PubMed:20181693}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFYNQVTLAVASDSEISGFGFAIPSVAVRTYSEAAAQGFQACRFVAFGLQDCVTGINDDDYVIALTGTNQLCAKILPFSD
SQ  RPLNLRGWLIFSNSNYVLQDFDVVFGHGAGSVVFVDKYMCGFDGKPVLPKNMWEFRDYFNNNTDSIVIGGVTYQLAWDVI
SQ  RKDLSYEQQNVLAIESIHYLGTTGHTLKSGCKLTNAKPPKYSSKVVLSGEWNAVYRAFGSPFITNGMSLLDIIVKPVFFN
SQ  AFVKCNCGSESWSVGAWDGYLSSCCGTPAKKLCVVPGNVVPGDVIITSTSAGCGVKYYAGLVVKHITNITGVSLWRVTAV
SQ  HSDGMFVASSSYDALLHRNSLDPFCFDVNTLLSNQLRLAFLGASVTEDVKFAASTGVIDISAGMFGLYDDILTNNKPWFV
SQ  RKASGLFDAIWDAFVAAIKLVPTTTGVLVRFVKSIASTVLTVSNGVIIMCADVPDAFQSVYRTFTQAICAAFDFSLDVFK
SQ  IGDVKFKRLGDYVLTENALVRLTTEVVRGVRDARIKKAMFTKVVVGPTTEVKFSVIELATVNLRLVDCAPVVCPKGKIVV
SQ  IAGQAFFYSGGFYRFMVDPTTVLNDPVFTGDLFYTIKFSGFKLDGFNHQFVTASSATDAIIAVELLLLDFKTAVFVYTCV
SQ  VDGCSVIVRRDATFATHVCFKDCYNVWEQFCIDNCGEPWFLTDYNAILQSNNPQCAIVQASESKVLLERFLPKCPEILLS
SQ  IDDGHLWNLFVEKFNFVTDWLKTLKLTLTSNGLLGNCAKRFRRVLVKLLDVYNGFLETVCSVAYTAGVCIKYYAVNVPYV
SQ  VISGFVSRVIRRERCDMTFPCVSCVTFFYEFLDTCFGVSKPNAIDVEHLELKETVFVEPKDGGQFFVSGDYLWYVVDDIY
SQ  YPASCNGVLPVAFTKLAGGKISFSDDVIVHDVEPTHKVKLIFEFEDDVVTSLCKKSFGKSIIYTGDWEGLHEVLTSAMNV
SQ  IGQHIKLPQFYIYDEEGGYDVSKPVMISQWPISNDSNGCVVEASTDFHQLECIVDDSVREEVDIIEQPFEEVEHVLSIKQ
SQ  PFSFSFRDELGVRVLDQSDNNCWISTTLVQLQLTKLLDDSIEMQLFKVGKVDSIVQKCYELSHLISGSLGDSGKLLSELL
SQ  KEKYTCSITFEMSCDCGKKFDDQVGCLFWIMPYTKLFQKGECCICHKMQTYKLVSMKGTGVFVQDPAPIDIDAFPVKPIC
SQ  SSVYLGVKGSGHYQTNLYSFNKAIDGFGVFDIKNSSVNTVCFVDVDFHSVEIEAGEVKPFAVYKNVKFYLGDISHLVNCV
SQ  SFDFVVNAANENLLHGGGVARAIDILTEGQLQSLSKDYISSNGPLKVGAGVMLECEKFNVFNVVGPRTGKHEHSLLVEAY
SQ  NSILFENGIPLMPLLSCGIFGVRIENSLKALFSCDINKPLQVFVYSSNEEQAVLKFLDGLDLTPVIDDVDVVKPFRVEGN
SQ  FSFFDCGVNALDGDIYLLFTNSILMLDKQGQLLDTKLNGILQQAALDYLATVKTVPAGNLVKLFVESCTIYMCVVPSIND
SQ  LSFDKNLGRCVRKLNRLKTCVIANVPAIDVLKKLLSSLTLTVKFVVESNVMDVNDCFKNDNVVLKITEDGINVKDVVVES
SQ  SKSLGKQLGVVSDGVDSFEGVLPINTDTVLSVAPEVDWVAFYGFEKAALFASLDVKPYGYPNDFVGGFRVLGTTDNNCWV
SQ  NATCIILQYLKPTFKSKGLNVLWNKFVTGDVGPFVSFIYFITMSSKGQKGDAEEALSKLSEYLISDSIVTLEQYSTCDIC
SQ  KSTVVEVKSAIVCASVLKDGCDVGFCPHRHKLRSRVKFVNGRVVITNVGEPIISQPSKLLNGIAYTTFSGSFDNGHYVVY
SQ  DAANNAVYDGARLFSSDLSTLAVTAIVVVGGCVTSNVPTIVSEKISVMDKLDTGAQKFFQFGDFVMNNIVLFLTWLLSMF
SQ  SLLRTSIMKHDIKVIAKAPKRTGVILTRSFKYNIRSALFVIKQKWCVIVTLFKFLLLLYAIYALVFMIVQFSPFNSLLCG
SQ  DIVSGYEKSTFNKDIYCGNSMVCKMCLFSYQEFNDLDHTSLVWKHIRDPILISLQPFVILVILLIFGNMYLRFGLLYFVA
SQ  QFISTFGSFLGFHQKQWFLHFVPFDVLCNEFLATFIVCKIVLFVRHIIVGCNNADCVACSKSARLKRVPLQTIINGMHKS
SQ  FYVNANGGTCFCNKHNFFCVNCDSFGPGNTFINGDIARELGNVVKTAVQPTAPAYVIIDKVDFVNGFYRLYSGDTFWRYD
SQ  FDITESKYSCKEVLKNCNVLENFIVYNNSGSNITQIKNACVYFSQLLCEPIKLVNSELLSTLSVDFNGVLHKAYVDVLCN
SQ  SFFKELTANMSMAECKATLGLTVSDDDFVSAVANAHRYDVLLSDLSFNNFFISYAKPEDKLSVYDIACCMRAGSKVVNHN
SQ  VLIKESIPIVWGVKDFNTLSQEGKKYLVKTTKAKGLTFLLTFNDNQAITQVPATSIVAKQGAGFKRTYNFLWYVCLFVVA
SQ  LFIGVSFIDYTTTVTSFHGYDFKYIENGQLKVFEAPLHCVRNVFDNFNQWHEAKFGVVTTNSDKCPIVVGVSERINVVPG
SQ  VPTNVYLVGKTLVFTLQAAFGNTGVCYDFDGVTTSDKCIFNSACTRLEGLGGDNVYCYNTDLIEGSKPYSTLQPNAYYKY
SQ  DAKNYVRFPEILARGFGLRTIRTLATRYCRVGECRDSHKGVCFGFDKWYVNDGRVDDGYICGDGLIDLLVNVLSIFSSSF
SQ  SVVAMSGHMLFNFLFAAFITFLCFLVTKFKRVFGDLSYGVFTVVCATLINNISYVVTQNLFFMLLYAILYFVFTRTVRYA
SQ  WIWHIAYIVAYFLLIPWWLLTWFSFAAFLELLPNVFKLKISTQLFEGDKFIGTFESAAAGTFVLDMRSYERLINTISPEK
SQ  LKNYAASYNKYKYYSGSASEADYRCACYAHLAKAMLDYAKDHNDMLYSPPTISYNSTLQSGLKKMAQPSGCVERCVVRVC
SQ  YGSTVLNGVWLGDTVTCPRHVIAPSTTVLIDYDHAYSTMRLHNFSVSHNGVFLGVVGVTMHGSVLRIKVSQSNVHTPKHV
SQ  FKTLKPGDSFNILACYEGIASGVFGVNLRTNFTIKGSFINGACGSPGYNVRNDGTVEFCYLHQIELGSGAHVGSDFTGSV
SQ  YGNFDDQPSLQVESANLMLSDNVVAFLYAALLNGCRWWLCSTRVNVDGFNEWAMANGYTSVSSVECYSILAAKTGVSVEQ
SQ  LLASIQHLHEGFGGKNILGYSSLCDEFTLAEVVKQMYGVNLQSGKVIFGLKTMFLFSVFFTMFWAELFIYTNTIWINPVI
SQ  LTPIFCLLLFLSLVLTMFLKHKFLFLQVFLLPTVIATALYNCVLDYYIVKFLADHFNYNVSVLQMDVQGLVNVLVCLFVV
SQ  FLHTWRFSKERFTHWFTYVCSLIAVAYTYFYSGDFLSLLVMFLCAISSDWYIGAIVFRLSRLIVFFSPESVFSVFGDVKL
SQ  TLVVYLICGYLVCTYWGILYWFNRFFKCTMGVYDFKVSAAEFKYMVANGLHAPHGPFDALWLSFKLLGIGGDRCIKISTV
SQ  QSKLTDLKCTNVVLLGCLSSMNIAANSSEWAYCVDLHNKINLCDDPEKAQSMLLALLAFFLSKHSDFGLDGLIDSYFDNS
SQ  STLQSVASSFVSMPSYIAYENARQAYEDAIANGSSSQLIKQLKRAMNIAKSEFDHEISVQKKINRMAEQAATQMYKEARS
SQ  VNRKSKVISAMHSLLFGMLRRLDMSSVETVLNLARDGVVPLSVIPATSASKLTIVSPDLESYSKIVCDGSVHYAGVVWTL
SQ  NDVKDNDGRPVHVKEITKENVETLTWPLILNCERVVKLQNNEIMPGKLKQKPMKAEGDGGVLGDGNALYNTEGGKTFMYA
SQ  YISNKADLKFVKWEYEGGCNTIELDSPCRFMVETPNGPQVKYLYFVKNLNTLRRGAVLGFIGATIRLQAGKQTELAVNSG
SQ  LLTACAFSVDPATTYLEAVKHGAKPVSNCIKMLSNGAGNGQAITTSVDANTNQDSYGGASICLYCRAHVPHPSMDGYCKF
SQ  KGKCVQVPIGCLDPIRFCLENNVCNVCGCWLGHGCACDRTTIQSVDISYLNEQGVLVQLD
//
ID  P0C6U7;
PN  Non-structural protein 11;
GN  1a;
OS  31631;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6U7;
DR  UNIPROT: Q9WAC3;
DR  PDB: 7NH7;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKINKYGLELHWAPEFPWMFEDAEEKLDNPSSSEVDMICSTTAQKLETDGICPENHVMVDCRRLLKQECCVQSSLIREI
SQ  VMNASPYHLEVLLQDALQSREAVLVTTPLGMSLEACYVRGCNPKGWTMGLFRRRSVCNTGRCTVNKHVAYQLYMIDPAGV
SQ  CLGAGQFVGWVIPLAFMPVQSRKFIVPWVMYLRKRGEKGAYNKDHGCGGFGHVYDFKVEDAYDQVHDEPKGKFSKKAYAL
SQ  IRGYRGVKPLLYVDQYGCDYTGSLADGLEAYADKTLQEMKALFPTWSQELPFDVIVAWHVVRDPRYVMRLQSAATICSVA
SQ  YVANPTEDLCDGSVVIKEPVHVYADDSIILRQYNLFDIMSHFYMEADTVVNAFYGVALKDCGFVMQFGYIDCEQDSCDFK
SQ  GWIPGNMIDGFACTTCGHVYEVGDLIAQSSGVLPVNPVLHTKSAAGYGGFGCKDSFTLYGQTVVYFGGCVYWSPARNIWI
SQ  PILKSSVKSYDSLVYTGVLGCKAIVKETNLICKALYLDYVQHKCGNLHQRELLGVSDVWHKQLLINRGVYKPLLENIDYF
SQ  NMRRAKFSLETFTVCADGFMPFLLDDLVPRAYYLAVSGQAFCDYADKLCHAVVSKSKELLDVSLDSLGAAIHYLNSKIVD
SQ  LAQHFSDFGTSFVSKIVHFFKTFTTSTALAFAWVLFHVLHGAYIVVESDIYFVKNIPRYASAVAQAFQSVAKVVLDSLRV
SQ  TFIDGLSCFKIGRRRICLSGRKIYEVERGLLHSSQLPLDVYDLTMPSQVQKAKQKPIYLKGSGSDFSLADSVVEVVTTSL
SQ  TPCGYSEPPKVADKICIVDNVYMAKAGDKYYPVVVDDHVGLLDQAWRVPCAGRRVTFKEQPTVKEIISMPKIIKVFYELD
SQ  NDFNTILNTACGVFEVDDTVDMEEFYAVVIDAIEEKLSPCKELEGVGAKVSAFLQKLEDNPLFLFDEAGEEVFAPKLYCA
SQ  FTAPEDDDFLEESDVEEDDVEGEETDLTITSAGQPCVASEQEESSEVLEDTLDDGPSVETSDSQVEEDVEMSDFVDLESV
SQ  IQDYENVCFEFYTTEPEFVKVLGLYVPKATRNNCWLRSVLAVMQKLPCQFKDKNLQDLWVLYKQQYSQLFVDTLVNKIPA
SQ  NIVLPQGGYVADFAYWFLTLCDWQCVAYWKCIKCDLALKLKGLDAMFFYGDVVSHICKCGESMVLIDVDVPFTAHFALKD
SQ  KLFCAFITKRIVYKAACVVDVNDSHSMAVVDGKQIDDHRITSITSDKFDFIIGHGMSFSMTTFEIAQLYGSCITPNVCFV
SQ  KGDIIKVSKLVKAEVVVNPANGHMVHGGGVAKAIAVAAGQQFVKETTNMVKSKGVCATGDCYVSTGGKLCKTVLNVVGPD
SQ  ARTQGKQSYVLLERVYKHFNNYDCVVTTLISAGIFSVPSDVSLTYLLGTAKKQVVLVSNNQEDFDLISKCQITAVEGTKK
SQ  LAARLSFNVGRSIVYETDANKLILINDVAFVSTFNVLQDVLSLRHDIALDDDARTFVQSNVDVLPEGWRVVNKFYQINGV
SQ  RTVKYFECTGGIDICSQDKVFGYVQQGIFNKATVAQIKALFLDKVDILLTVDGVNFTNRFVPVGESFGKSLGNVFCDGVN
SQ  VTKHKCDINYKGKVFFQFDNLSSEDLKAVRSSFNFDQKELLAYYNMLVNCFKWQVVVNGKYFTFKQANNNCFVNVSCLML
SQ  QSLHLTFKIVQWQEAWLEFRSGRPARFVALVLAKGGFKFGDPADSRDFLRVVFSQVDLTGAICDFEIACKCGVKQEQRTG
SQ  LDAVMHFGTLSREDLEIGYTVDCSCGKKLIHCVRFDVPFLICSNTPASVKLPKGVGSANIFIGDNVGHYVHVKCEQSYQL
SQ  YDASNVKKVTDVTGKLSDCLYLKNLKQTFKSVLTTYYLDDVKKIEYKPDLSQYYCDGGKYYTQRIIKAQFKTFEKVDGVY
SQ  TNFKLIGHTVCDSLNSKLGFDSSKEFVEYKITEWPTATGDVVLANDDLYVKRYERGCITFGKPVIWLSHEKASLNSLTYF
SQ  NRPLLVDDNKFDVLKVDDVDDSGDSSESGAKETKEINIIKLSGVKKPFKVEDSVIVNDDTSETKYVKSLSIVDVYDMWLT
SQ  GCKYVVRTANALSRAVNVPTIRKFIKFGMTLVSIPIDLLNLREIKPAVNVVKAVRNKTSACFNFIKWLFVLLFGWIKISA
SQ  DNKVIYTTEIASKLTCKLVALAFKNAFLTFKWSMVARGACIIATIFLLWFNFIYANVIFSDFYLPKIGFLPTFVGKIAQW
SQ  IKNTFSLVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEADRRAFVDYTGVLKIVIELIVSYALY
SQ  TAWFYPLFALISIQILTTWLPELFMLSTLHWSFRLLVALANMLPAHVFMRFYIIIASFIKLFSLFKHVAYGCSKSGCLFC
SQ  YKRNRSLRVKCSTIVGGMIRYYDVMANGGTGFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVT
SQ  DVKQVGCSMRLFYDRDGQRIYDDVNASLFVDYSNLLHSKVKSVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDK
SQ  NLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQIYKVLDTFLSCARKSCSIDSDVDTKCLAD
SQ  SVMSAVSAGLELTDESCNNLVPTYLKSDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQFSSDFQHKLKKAC
SQ  CKTGLKLKLTYNKQMANVSVLTTPFSLKGGAVFSYFVYVCFVLSLVCFIGLWCLMPTYTVHKSDFQLPVYASYKVLDNGV
SQ  IRDVSVEDVCFANKFEQFDQWYESTFGLSYYSNSMACPIVVAVIDQDFGSTVFNVPTKVLRYGYHVLHFITHALSADGVQ
SQ  CYTPHSQISYSNFYASGCVLSSACTMFTMADGSPQPYCYTDGLMQNASLYSSLVPHVRYNLANAKGFIRFPEVLREGLVR
SQ  VVRTRSMSYCRVGLCEEADEGICFNFNGSWVLNNDYYRSLPGTFCGRDVFDLIYQLFKGLAQPVDFLALTASSIAGAILA
SQ  VIVVLVFYYLIKLKRAFGDYTSVVFVNVIVWCVNFMMLFVFQVYPTLSCVYAICYFYATLYFPSEISVIMHLQWLVMYGT
SQ  IMPLWFCLLYIAVVVSNHAFWVFSYCRKLGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYS
SQ  GKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQSGIVKMVNPTSKVEPCVVSVTYGNMTLNGLWLDD
SQ  KVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMRGCMLVLTVTLQNSRTPKYTFGVVKPGETFTV
SQ  LAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVIMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLP
SQ  IQDYIQSVNFLAWLYAAILNNCNWFIQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQ
SQ  GRQIMGSCSFEDELTPSDVYQQLAGIKLQSKRTRLFKGTVCWIMASTFLFSCIITAFVKWTMFMYVTTNMFSITFCALCV
SQ  ISLAMLLVKHKHLYLTMYITPVLFTLLYNNYLVVYKHTFRGYVYAWLSYYVPSVEYTYTDEVIYGMLLLVGMVFVTLRSI
SQ  NHDLFSFIMFVGRLISVFSLWYKGSNLEEEILLMLASLFGTYTWTTVLSMAVAKVIAKWVAVNVLYFTDIPQIKIVLLCY
SQ  LFIGYIISCYWGLFSLMNSLFRMPLGVYNYKISVQELRYMNANGLRPPKNSFEALMLNFKLLGIGGVPIIEVSQFQSKLT
SQ  DVKCANVVLLNCLQHLHVASNSKLWHYCSTLHNEILATSDLSVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKD
SQ  NTVLQALQSEFVNMASFVEYEVAKKNLDEARFSGSANQQQLKQLEKACNIAKSAYERDRAVAKKLERMADLALTNMYKEA
SQ  RINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLNIIVPDKSVYDQIVDNIYVTYAGNVW
SQ  QIQTIQDSDGTNKQLNEISDDCNWPLVIIANRYNEVSATVLQNNELMPAKLKIQVVNSGPDQTCNTPTQCYYNNSNNGKI
SQ  VYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDAKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQAGTATEYA
SQ  SNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITVKPDATTSQDSYGGASVCIYCRARVEHPDVDG
SQ  LCKLRGKFVQVPVGIKDPVSYVLTHDVCRVCGFWRDGSCSCVSTDTTVQSKDTNFLNGFGVRV
//
ID  P0C6U9;
PN  Non-structural protein 11;
GN  1a;
OS  76344;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6U9;
DR  UNIPROT: Q9PYA3;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKMGKYGLGFKWAPEFPWMLPNASEKLGSPERSEEDGFCPSAAQEPKTKGKTLINHVRVDCSRLPALECCVQSAIIRDI
SQ  FVDEDPLNVEASTMMALQFGSAVLVKPSKRLSIQAWAKLGVLPKTPAMGLFKRFCLCNTRECVCDAHVAFQLFTVQPDGV
SQ  CLGNGRFIGWFVPVTAIPAYAKQWLQPWSILLRKGGNKGSVTSGHFRRAVTMPVYDFNVEDACEEVHLNPKGKYSRKAYA
SQ  LLKGYRGVKSILFLDQYGCDYTGRLAKGLEDYGDCTLEEMKELFPVWCDSLDNEVVVAWHVDRDPRAVMRLQTLATIRSI
SQ  GYVGQPTEDLVDGDVVVREPAHLLAANAIVKRLPRLVETMLYTDSSVTEFCYKTKLCDCGFITQFGYVDCCGDACDFRGW
SQ  VPGNMMDGFLCPGCSKSYMPWELEAQSSGVIPKGGVLFTQSTDTVNRESFKLYGHAVVPFGSAVYWSPYPGMWLPVIWSS
SQ  VKSYADLTYTGVVGCKAIVQETDAICRSLYMDYVQHKCGNLEQRAILGLDDVYHRQLLVNRGDYSLLLENVDLFVKRRAE
SQ  FACKFATCGDGLVPLLLDGLVPRSYYLIKSGQAFTSMMVNFSHEVTDMCMDMALLFMHDVKVATKYVKKVTGKLAVRFKA
SQ  LGVAVVRKITEWFDLAVDTAASAAGWLCYQLVNGLFAVANGGITFLSDVPELVKNFVDKFKVFFKVLIDSMSVSVLSGLT
SQ  VVKTASNRVCLAGCKVYEVVQKRLSAYVMPVGCNEATCLVGEIEPAVVEDDVVDVVKAPLTYQGCCKPPTSFEKICVVDK
SQ  LYMAKCGDQFYPVVVDNDTIGVLDQCWRFPCAGKKVEFNDKPKVKEIPSTRKIKINFALDATFDSVLSKACSEFEVDKDV
SQ  TLDELLDVVLDAVESTLSPCKEHDVIGTKVCALLNRLAEDYVYLFDEGGEEVIAPKMYCSFSAPDDEDCVAADVVDADEN
SQ  QGDDADDSAALVTDTQEEDGVAKGQVGVAESDARLDQVEAFDIEKVEDPILNELSAELNAPADKTYEDVLAFDAIYSEAL
SQ  SAFYAVPGDETHFKVCGFYSPAIERTNCWLRSTLIVMQSLPLEFKDLEMQKLWLSYKSSYNKEFVDKLVKSVPKSIILPQ
SQ  GGYVADFAYFFLSQCSFKAYANWRCLKCDMDLKLQGLDAMFFYGDVVSHVCKCGTGMTLLSADIPYTLHFGLRDDKFCAF
SQ  YTPRKVFRAACVVDVNDCHSMAVVDGKQIDGKVVTKFNGDKYDFMVGHGMAFSMSAFEIAQLYGSCITPNVCFVKGDVIK
SQ  VLRRVGAEVIVNPANGRMAHGAGVAGAIAKAAGKSFIKETADMVKNQGVCQVGECYESTGGNLCKTVLNIVGPDARGHGK
SQ  QCYSFLERAYQHINKCDDVVTTLISAGIFSVPTDVSLTYLIGVVTKNVILVSNNKDDFDVIEKCQVTSIAGTKALSLQLA
SQ  KNLCRDVKFETNACDSLFSDSCFVSSYDVLQEVELLRHDIQLDDDARVFVQAHMDNLPADWRLVNKFDSVDGVRTVKYFE
SQ  CPGEIFVSSQGKKFGYVQNGSFKVASVSQIRALLANKVDVLCTVDGVNFRSCCVAEGEVFGKTLGSVFCDGINVTKVRCS
SQ  AIHKGKVFFQYSGLSAADLVAVTDAFGFDEPQLLKYYNMLGMCKWPVVVCGNYFAFKQSNNNCYINVACLMLQHLSLKFH
SQ  KWQWQEAWNEFRSGKPLRFVSLVLAKGSFKFNEPSDSTDFMRVVLREADLSGATCDFEFVCKCGVKQEQRKGVDAVMHFG
SQ  TLDKGDLAKGYTIACTCGNKLVHCTQLNVPFLICSNKPEGKKLPDDVVAANIFTGGSLGHYTHVKCKPKYQLYDACNVSK
SQ  VSEAKGNFTDCLYLKNLKQTFSSKLTTFYLDDVKCVEYNPDLSQYYCESGKYYTKPIIKAQFRTFEKVEGVYTNFKLVGH
SQ  SIAEKFNAKLGFDCNSPFTEYKITEWPTATGDVVLASDDLYVSRYSGGCVTFGKPVIWLGHEEASLKSLTYFNRPSVVCE
SQ  NKFNVLPVDVSEPTDKGPVPAAVLVTGALSGAATAPGTAKEQKVCASDSVVDQVVSGFLSDLSGATVDVKEVKLNGVKKP
SQ  IKVEDSVVVNDPTSETKVVKSLSIVDVYDMFLTGCRYVVWMANELSRLVNSPTVREYVKWGMTKIVIPAKLVLLRDEKQE
SQ  FVAPKVVKAKVIACYSAVKWFFLYCFSWIKFNTDNKVIYTTEVASKLTFNLCCLAFKNALQTFNWNVVSRGFFLVATVFL
SQ  LWFNFLYANVILSDFYLPNIGFFPTFVGQIVAWVKTTFGIFTLCDLYQVSDVGYRSSFCNGSMVCELCFSGFDMLDNYDA
SQ  INVVQHVVDRRVSFDYISLFKLVVELVIGYSLYTVCFYPLFGLIGMQLLTTWLPEFFMLETMHWSARFFVFVANMLPAFT
SQ  LLRFYIVVTAMYKIFCLCRHVMYGCSRPGCLFCYKRNRSVRVKCSTVVGGTLRYYDVMANGGTGFCAKHQWNCLNCSAFG
SQ  PGNTFITHEAAADLSKELKRPVNPTDSAYYLVTEVKQVGCSMRLFYERDGQRVYDDVSASLFVDMNGLLHSKVKGVPETH
SQ  VVVVENEADKAGFLNAAVFYAQSLYRPMLLVEKKLITTANTGLSVSQTMFDLYVDSLLGVLDVDRKSLTSFVNAAHNSLK
SQ  EGVQLEQVMDTFIGCARRKCAIDSDVETKSITKSIMSAVNAGVDFTDESCNNLVPTYVKSDTIVAADLGVLIQNNAKHVQ
SQ  ANVAKAANVACIWSVDAFNQLSADLQHRLRKACSKTGLKIKLTYNKQEANVPILTTPFSLKGGAVFSKVLQWLFVVNLIC
SQ  FIVLWALMPTYAVHKSDMQLPLYASFKVIDNGVLRDVTVTDACFANKFIQFDQWYESTFGLVYYRNSRACPVVVAVIDQD
SQ  IGYTLFNVPTKVLRYGFHVLHFITHAFATDSVQCYTPHMQIPYDNFYASGCVLSSLCTMLAHADGTPHPYCYTEGIMHNA
SQ  SLYDSLAPHVRYNLANSNGYIRFPEVVSEGIVRIVRTRSMTYCRVGLCEDAEEGVCFNFNSSWVLNNPYYRAMPGTFCGR
SQ  NAFDLIHQVLGGLVRPIDFFALTASSVAGAILAIIVVLAFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQVYPTL
SQ  SCLYACFYFYTTLYFPSEISVVMHLQWLVMYGAIMPLWFCIIYVAVVVSNHALWLFSYCRKLGTEVRSDGTFEEMSLTTF
SQ  MITKESYCKLKNSVSDVAFNRYLSLYNKYRYFSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVTTSFLQS
SQ  GIVKMVFPTSKVEPCVVSVTYGNMTLNGLWLDDKVYCPRHVICSSADMTDPDYSNLLCRVISSDFCVMSGRMSLTVMSYQ
SQ  MQGSLLVLTVTLQNPNTPKYSFGVVKPGETFTVLAAYNGKSQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLTGDSVRFVY
SQ  MHQLELSTGCHTGTDFSGNFYGPYRDAQVVQLPVQDYTQTVNVVAWLYAAILNRCNWFVQSDSCSLEEFNVWAMTNGFSS
SQ  IKADLVLDALASMTGVTVEQILAAIKRLYSGFQGKQILGSCVLEDELTPSDVYQQLAGVKLQSKRTRVVKGTCCWILAST
SQ  LLFCSIISAFVKWTMFMYVTTHMLGVTLCALCFVSFAMLLVKHKHLYLTMFIMPVLCTLFYTNYLVVYKQSFRGLAYAWL
SQ  SHFVPAVDYTYMDEVLYGVVLLVAMVFVTMRSINHDVFSVMFLVGRLVSLVSMWYFGANLEEEVLLFLTSLFGTYTWTTM
SQ  LSLATAKVIAKWLAVNVLYFTDVPQVKLVLLSYLCIGYVCCCYWGVLSLLNSIFRMPLGVYNYKISVQELRYMNANGLRP
SQ  PRNSFEALVLNFKLLGIGGVPVIEVSQIQSRLTDVKCVNVVLLNCLQHLHIASSSKLWQYCSTLHNEILATSDLSVAFDK
SQ  LAQLLVVLFANPAAVDSKCLASIEEVSDDYVRDSTVLQALQSEFVNMASFVEYELAKKNLDEAKASGSANQQQIKQLEKA
SQ  CNIAKSAYERDRAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMIRKLDNQALNSILDNAVKGCVPLNAIP
SQ  SLTSNTLTIIVPDKQVFDQVVDNVYVTYAGNVWHIQSIQDADGAVKQLNEIDVNITWPLVIAANRHNEVSSVVLQNNELM
SQ  PQKLRTQVVNSGSDMNCNTPTQCYYNTTGMGKIVYAILSDCDGLKYTKIVKEDGNCVVLELDPPCKFSVQDVKGLKIKYL
SQ  YFVKGCNTLARGWVVGTLSSTVRLQAGTATEYASNSAIRSLCAFSVDPKKTYLDYIQQGGAPVTNCVKMLCDHAGTGMAI
SQ  TIKPEATTNQDSYGGASVCIYCRSRVEHPDVDGLCKLRGKFVQVPLGIKDPVSYVLTHDVCQVCGFWRDGSCSCVGTGSQ
SQ  FQSKDTNFLNGFGVQV
//
ID  P0C6V0;
PN  Non-structural protein 11;
GN  1a;
OS  11142;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
DR  UNIPROT: P0C6V0;
DR  UNIPROT: P16342;
DR  PDB: 2M0A;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: R9QB93; IntAct: EBI-25821276; Score: 0.44
DE  Interaction: E0D5D4; IntAct: EBI-25821334; Score: 0.44
DE  Interaction: Q64339; IntAct: EBI-25821362; Score: 0.44
DE  Interaction: P05161; IntAct: EBI-26603848; Score: 0.44
DE  Interaction: Q9H492; IntAct: EBI-29454962; Score: 0.44
GO  GO:0039714;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0097264;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKMGKYGLGFKWAPEFPWMLPNASEKLGNPERSEEDGFCPSAAQEPKVKGKTLVNHVRVNCSRLPALECCVQSAIIRDI
SQ  FVDEDPQKVEASTMMALQFGSAVLVKPSKRLSIQAWTNLGVLPKTAAMGLFKRVCLCNTRECSCDAHVAFHLFTVQPDGV
SQ  CLGNGRFIGWFVPVTAIPEYAKQWLQPWSILLRKGGNKGSVTSGHFRRAVTMPVYDFNVEDACEEVHLNPKGKYSCKAYA
SQ  LLKGYRGVKPILFVDQYGCDYTGCLAKGLEDYGDLTLSEMKELFPVWRDSLDSEVLVAWHVDRDPRAAMRLQTLATVRCI
SQ  DYVGQPTEDVVDGDVVVREPAHLLAANAIVKRLPRLVETMLYTDSSVTEFCYKTKLCECGFITQFGYVDCCGDTCDFRGW
SQ  VAGNMMDGFPCPGCTKNYMPWELEAQSSGVIPEGGVLFTQSTDTVNRESFKLYGHAVVPFGSAVYWSPCPGMWLPVIWSS
SQ  VKSYSGLTYTGVVGCKAIVQETDAICRSLYMDYVQHKCGNLEQRAILGLDDVYHRQLLVNRGDYSLLLENVDLFVKRRAE
SQ  FACKFATCGDGLVPLLLDGLVPRSYYLIKSGQAFTSMMVNFSHEVTDMCMDMALLFMHDVKVATKYVKKVTGKLAVRFKA
SQ  LGVAVVRKITEWFDLAVDIAASAAGWLCYQLVNGLFAVANGVITFVQEVPELVKNFVDKFKAFFKVLIDSMSVSILSGLT
SQ  VVKTASNRVCLAGSKVYEVVQKSLSAYVMPVGCSEATCLVGEIEPAVFEDDVVDVVKAPLTYQGCCKPPTSFEKICIVDK
SQ  LYMAKCGDQFYPVVVDNDTVGVLDQCWRFPCAGKKVEFNDKPKVRKIPSTRKIKITFALDATFDSVLSKACSEFEVDKDV
SQ  TLDELLDVVLDAVESTLSPCKEHDVIGTKVCALLDRLAGDYVYLFDEGGDEVIAPRMYCSFSAPDDEDCVAADVVDADEN
SQ  QDDDAEDSAVLVADTQEEDGVAKGQVEADSEICVAHTGSQEELAEPDAVGSQTPIASAEETEVGEASDREGIAEAKATVC
SQ  ADAVDACPDQVEAFEIEKVEDSILDELQTELNAPADKTYEDVLAFDAVCSEALSAFYAVPSDETHFKVCGFYSPAIERTN
SQ  CWLRSTLIVMQSLPLEFKDLEMQKLWLSYKAGYDQCFVDKLVKSVPKSIILPQGGYVADFAYFFLSQCSFKAYANWRCLE
SQ  CDMELKLQGLDAMFFYGDVVSHMCKCGNSMTLLSADIPYTLHFGVRDDKFCAFYTPRKVFRAACAVDVNDCHSMAVVEGK
SQ  QIDGKVVTKFIGDKFDFMVGYGMTFSMSPFELAQLYGSCITPNVCFVKGDVIKVVRLVNAEVIVNPANGRMAHGAGVAGA
SQ  IAEKAGSAFIKETSDMVKAQGVCQVGECYESAGGKLCKKVLNIVGPDARGHGKQCYSLLERAYQHINKCDNVVTTLISAG
SQ  IFSVPTDVSLTYLLGVVTKNVILVSNNQDDFDVIEKCQVTSVAGTKALSLQLAKNLCRDVKFVTNACSSLFSESCFVSSY
SQ  DVLQEVEALRHDIQLDDDARVFVQANMDCLPTDWRLVNKFDSVDGVRTIKYFECPGGIFVSSQGKKFGYVQNGSFKEASV
SQ  SQIRALLANKVDVLCTVDGVNFRSCCVAEGEVFGKTLGSVFCDGINVTKVRCSAIYKGKVFFQYSDLSEADLVAVKDAFG
SQ  FDEPQLLKYYTMLGMCKWPVVVCGNYFAFKQSNNNCYINVACLMLQHLSLKFPKWQWQEAWNEFRSGKPLRFVSLVLAKG
SQ  SFKFNEPSDSIDFMRVVLREADLSGATCNLEFVCKCGVKQEQRKGVDAVMHFGTLDKGDLVRGYNIACTCGSKLVHCTQF
SQ  NVPFLICSNTPEGRKLPDDVVAANIFTGGSVGHYTHVKCKPKYQLYDACNVNKVSEAKGNFTDCLYLKNLKQTFSSVLTT
SQ  FYLDDVKCVEYKPDLSQYYCESGKYYTKPIIKAQFRTFEKVDGVYTNFKLVGHSIAEKLNAKLGFDCNSPFVEYKITEWP
SQ  TATGDVVLASDDLYVSRYSSGCITFGKPVVWLGHEEASLKSLTYFNRPSVVCENKFNVLPVDVSEPTDKGPVPAAVLVTG
SQ  VPGADASAGAGIAKEQKACASASVEDQVVTEVRQEPSVSAADVKEVKLNGVKKPVKVEGSVVVNDPTSETKVVKSLSIVD
SQ  VYDMFLTGCKYVVWTANELSRLVNSPTVREYVKWGMGKIVTPAKLLLLRDEKQEFVAPKVVKAKAIACYCAVKWFLLYCF
SQ  SWIKFNTDNKVIYTTEVASKLTFKLCCLAFKNALQTFNWSVVSRGFFLVATVFLLWFNFLYANVILSDFYLPNIGPLPTF
SQ  VGQIVAWFKTTFGVSTICDFYQVTDLGYRSSFCNGSMVCELCFSGFDMLDNYDAINVVQHVVDRRLSFDYISLFKLVVEL
SQ  VIGYSLYTVCFYPLFVLIGMQLLTTWLPEFFMLETMHWSARLFVFVANMLPAFTLLRFYIVVTAMYKVYCLCRHVMYGCS
SQ  KPGCLFCYKRNRSVRVKCSTVVGGSLRYYDVMANGGTGFCTKHQWNCLNCNSWKPGNTFITHEAAADLSKELKRPVNPTD
SQ  SAYYSVTEVKQVGCSMRLFYERDGQRVYDDVNASLFVDMNGLLHSKVKGVPETHVVVVENEADKAGFLGAAVFYAQSLYR
SQ  PMLMVEKKLITTANTGLSVSRTMFDLYVDSLLNVLDVDRKSLTSFVNAAHNSLKEGVQLEQVMDTFIGCARRKCAIDSDV
SQ  ETKSITKSVMSAVNAGVDFTDESCNNLVPTYVKSDTIVAADLGVLIQNNAKHVQANVAKAANVACIWSVDAFNQLSADLQ
SQ  HRLRKACSKTGLKIKLTYNKQEANVPILTTPFSLKGGAVFSRMLQWLFVANLICFIVLWALMPTYAVHKSDMQLPLYASF
SQ  KVIDNGVLRDVSVTDACFANKFNQFDQWYESTFGLAYYRNSKACPVVVAVIDQDIGHTLFNVPTTVLRYGFHVLHFITHA
SQ  FATDSVQCYTPHMQIPYDNFYASGCVLSSLCTMLAHADGTPHPYCYTGGVMHNASLYSSLAPHVRYNLASSNGYIRFPEV
SQ  VSEGIVRVVRTRSMTYCRVGLCEEAEEGICFNFNRSWVLNNPYYRAMPGTFCGRNAFDLIHQVLGGLVRPIDFFALTASS
SQ  VAGAILAIIVVLAFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQVYPTLSCLYACFYFYTTLYFPSEISVVMHLQ
SQ  WLVMYGAIMPLWFCIIYVAVVVSNHALWLFSYCRKIGTEVRSDGTFEEMALTTFMITKESYCKLKNSVSDVAFNRYLSLY
SQ  NKYRYFSGKMDTAAYREAACSQLAKAMETFNHNNGNDVLYQPPTASVTTSFLQSGIVKMVSPTSKVEPCIVSVTYGNMTL
SQ  NGLWLDDKVYCPRHVICSSADMTDPDYPNLLCRVTSSDFCVMSGRMSLTVMSYQMQGCQLVLTVTLQNPNTPKYSFGVVK
SQ  PGETFTVLAAYNGRPQGAFHVTLRSSHTIKGSFLCGSCGSVGYVLTGDSVRFVYMHQLELSTGCHTGTDFSGNFYGPYRD
SQ  AQVVQLPVQDYTQTVNVVAWLYAAIFNRCNWFVQSDSCSLEEFNVWAMTNGFSSIKADLVLDALASMTGVTVEQVLAAIK
SQ  RLHSGFQGKQILGSCVLEDETPSDVYQQLAGVKLQSKRTRVIKGTCCWILASTFLFCSIISAFVKWTMFMYVTTHMLGVT
SQ  LCALCFVSFAMLLIKHKHLYLTMYIMPVLCTFYTNYLVVYKQSFRGLAYAWLSHFVPAVDYTYMDEVLYGVVLLVAMVFV
SQ  TMRSINHDVFSIMFLVGRLVSLVSMWYFGANLEEEVLLFLTSLFGTYTWTTMLSLATAKVIAKWLAVNVLYFTDVPQIKL
SQ  VLLSYLCIGYVCCCYWGILSLLNSIFRMPLGVYNYKISVQELRYMNANGLRPPRNSFEALMLNFKLLGIGGVPVIEVSQI
SQ  QSRLTDVKCANVVLLNCLQHLHIASNSKLWQYCSTLHNEILATSDLSMAFDKLAQLLVVLFANPAAVDSKCLASIEEVSD
SQ  DYVRDNTVLQALQSEFVNMASFVEYELAKKNLDEAKASGSANQQQIKQLEKACNIAKSAYERDRAVARKLERMADLALTN
SQ  MYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLTSNTLTIIVPDKQVFDQVVDNVYVTY
SQ  AGNVWHIQFIQDADGAVKQLNEIDVNSTWPLVIAANRHNEVSTVVLQNNELMPQKLRTQVVNSGSDMNCNTPTQCYYNTT
SQ  GTGKIVYAILSDCDGLKYTKIVKEDGNCVVLELDPPCKFSVQDVKGLKIKYLYFVKGCNTLARGWVVGTLSSTVRLQAGT
SQ  ATEYASNSAILSLCAFSVDPKKTYLDYIKQGGVPVTNCVKMLCDHAGTGMAITIKPEATTNQDSYGGASVCIYCRSRVEH
SQ  PDVDGLCKLRGKFVQVPLGIKDPVSYVLTHDVCQVCGFWRDGSCSCVGTGSQFQSKDTNFLNGFGVQV
//
ID  P0C6V1;
PN  Non-structural protein 11;
GN  1a;
OS  11144;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6V1;
DR  UNIPROT: P19751;
DR  Pfam: PF16251;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF11963;
DR  Pfam: PF01661;
DR  Pfam: PF01831;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}. [Non-structural protein 1]: Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0097264;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKMGKYGLGFKWAPEFPWMLPNASEKLGNPERSEEDGFCPSAAQEPKVKGKTLVNHVRVDCSRLPALECCVQSAIIRDI
SQ  FVDEDPQKVEASTMMALQFGSAVLVKPSKRLSVQAWAKLGVLPKTPAMGLFKRFCLCNTRECVCDAHVAFQLFTVQPDGV
SQ  CLGNGRFIGWFVPVTAIPEYAKQWLQPWSILLRKGGNKGSVTSGHFRRAVTMPVYDFNVEDACEEVHLNPRGKYSCKAYA
SQ  LLRGYRGVKPILFVDQYGCDYTGCLAKGLEDYGDLTLSEMKELSPVWRDSLDNEVVVAWHVDRDPRAVMRLQTLATVRSI
SQ  EYVGQPIEDMVDGDVVMREPAHLLAPNAIVKRLPRLVETMLYTDSSVTEFCYKTKLCDCGFITQFGYVDCCGDTCGFRGW
SQ  VPGNMMDGFPCPGCCKSYMPWELEAQSSGVIPEGGVLFTQSTDTVNRESFKLYGHAVVPFGGAAYWSPYPGMWLPVIWSS
SQ  VKSYSYLTYTGVVGCKAIVQETDAICRFLYMDYVQHKCGNLEQRAILGLDDVYHRQLLVNRGDYSLLLENVDLFVKRRAE
SQ  FACKFATCGDGLVPLLLDGLVPRSYYLIKSGQAFTSLMVNFSREVVDMCMDMALLFMHDVKVATKYVKKVTGKVAVRFKA
SQ  LGIAVVRKITEWFDLAVDTAASAAGWLCYQLVNGLFAVANGVITFIQEVPELVKNFVDKFKTFFKVLIDSMSVSILSGLT
SQ  VVKTASNRVCLAGSKVYEVVQKSLPAYIMPVGCSEATCLVGEIEPAVFEDDVVDVVKAPLTYQGCCKPPSSFEKICIVDK
SQ  LYMAKCGDQFYPVVVDNDTVGVLDQCWRFPCAGKKVVFNDKPKVKEVPSTRKIKIIFALDATFDSVLSKACSEFEVDKDV
SQ  TLDELLDVVLDAVESTLSPCKEHGVIGTKVCALLERLVDDYVYLFDEGGEEVIASRMYCSFSAPDEDCVATDVVYADENQ
SQ  DDDADDPVVLVADTQEEDGVAREQVDSADSEICVAHTGGQEMTEPDVVGSQTPIASAEETEVGEACDREGIAEVKATVCA
SQ  DALDACPDQVEAFDIEKVEDSILSELQTELNAPADKTYEDVLAFDAIYSETLSAFYAVPSDETHFKVCGFYSPAIERTNC
SQ  WLRSTLIVMQSLPLEFKDLGMQKLWLSYKAGYDQCFVDKLVKSAPKSIILPQGGYVADFAYFFLSQCSFKVHANWRCLKC
SQ  GMELKLQGLDAVFFYGDVVSHMCKCGNSMTLLSADIPYTFDFGVRDDKFCAFYTPRKVFRAACAVDVNDCHSMAVVDGKQ
SQ  IDGKVVTKFNGDKFDFMVGHGMTFSMSPFEIAQLYGSCITPNVCFVKGDVIKVLRRVGAEVIVNPANGRMAHGAGVAGAI
SQ  AKAAGKAFINETADMVKAQGVCQVGGCYESTGGKLCKKVLNIVGPDARGHGNECYSLLERAYQHINKCDNVVTTLISAGI
SQ  FSVPTDVSLTYLLGVVTKNVILVSNNQDDFDVIEKCQVTSVAGTKALSFQLAKNLCRDVKFVTNACSSLFSESSFVSSYD
SQ  VLQEVEALRHDIQLDDDARVFVQANMDCLPTDWRLVNKFDSVDGVRTIKYFECPGEVFVSSQGKKFGYVQNGSFKEASVS
SQ  QIRALLANKVDVLCTVDGVNFRSCCVAEGEVFGKTLGSVFCDGINVTKVRCSAIHKGKVFFQYSGLSAADLAAVKDAFGF
SQ  DEPQLLQYYSMLGMCKWPVVVCGNYFAFKQSNNNCYINVACLMLQHLSLKFPKWQWRRPGNEFRSGKPLRFVSLVLAKGS
SQ  FKFNEPSDSTDFIRVELREADLSGATCDLEFICKCGVKQEQRKGVDAVMHFGTLDKSGLVKGYNIACTCGDKLVHCTQFN
SQ  VPFLICSNTPEGKKLPDDVVAANIFTGGSVGHYTHVKCKPKYQLYDACNVSKVSEAKGNFTDCLYLKNLKQTFSSVLTTY
SQ  YLDDVKCVAYKPDLSQYYCESGKYYTKPIIKAQFRTFEKVEGVYTNFKLVGHDIAEKLNAKLGFDCNSPFMEYKITEWPT
SQ  ATGDVVLASDDLYVSRYSGGCVTFGKPVIWRGHEEASLKSLTYFNRPSVVCENKFNVLPVDVSEPTDRRPVPSAVLVTGA
SQ  ASGADASAISTEPGTAKEQKACASDSVEDQIVMEAQKKSSVTTVAVKEVKLNGVKKPVKWNCSVVVNDPTSETKVVKSLS
SQ  IVDVYDMFLTGCRYVVWTANELSRLINSPTVREYVKWGMSKLIIPANLLLLRDEKQEFVAPKVVKAKAIACYGAVKWFLL
SQ  YCFSWIKFNTDNKVIYTTEVASKLTFKLCCLAFKNALQTFNWSVVSRGFFLVATVFLLWFNFLYANVILSDFYLPNIGPL
SQ  PMFVGQIVAWVKTTFGVLTICDFYQVTDLGYRSSFCNGSMVCELCFSGFDMLDNYESINVVQHVVDRRVSFDYISLFKLV
SQ  VELVIGYSLYTVCFYPLFVLVGMQLLTTWLPEFFMLGTMHWSARLFVFVANMLPAFTLLRFYIVVTAMYKVYCLCRHVMY
SQ  GCSKPGCLFCYKRNRSVRVKCSTVVGGSLRYYDVMANGGTGFCTKHQWNCLNCNSWKPGNTFITHEAAADLSKELKRPVN
SQ  PTDSAYYSVIEVKQVGCSMRLFYERDGQRVYDDVSASLFVDMNGLLHSKVKGVPETHVVVVENEADKAGFLNAAVFYAQS
SQ  LYRPMLMVEKKLITTANTGLSVSRTMFDLYVYSLLRHLDVDRKSLTSFVNAAHNSLKEGVQLEQVMDTFVGCARRKCAID
SQ  SDVETKSITKSVMAAVNAGVEVTDESCNNLVPTYVKSDTIVAADLGVLIQNNAKHVQSNVAKAANVACIWSVDAFNQLSA
SQ  DLQHRLRKACVKTGLKIKLTYNKQEANVPILTTPFSLKGGAVFSRVLQWLFVANLICFIVLWALMPTYAVHKSDMQLPLY
SQ  ASFKVIDNGVLRDVSVTDACFANKFNQFDQWYESTFGLVYYRNSKACPVVVAVIDQDIGHTLFNVPTKVLRYGFHVLHFI
SQ  THAFATDRVQCYTPHMQIPYDNFYASGCVLSSLCTMLAHADGTPHPYCYTEGVMHNASLYSSLVPHVRYNLASSNGYIRF
SQ  PEVVSEGIVRVVRTRSMTYCRVGLCEEAEEGICFNFNSSWVLNNPYYRAMPGTFCGRNAFDLIHQVLGGLVQPIDFFALT
SQ  ASSVAGAILAIIVVLAFYYLIKLKRAFGDYTSVVVINVIVWCINFLMLFVFQVYPTLSCLYACFYFYTTLYFPSEISVVM
SQ  HLQWLVMYGAIMPLWFCITYVAVVVSNHALWLFSYCRKIGTDVRSDGTFEEMALTTFMITKESYCKLKNSVSDVAFNRYL
SQ  SLYNKYRYFSGKMDTATYREAACSQLAKAMETFNHNNGNDVLYQPPTASVTTSFLQSGIVKMVSPTSKVEPCVVSVTYGN
SQ  MTLNGLWLDDKVYCPRHVICSSADMTDPDYPNLLCRVTSSDFCVMSDRMSLTVMSYQMQGSLLVLTVTLQNPNTPKYSFG
SQ  VVKPGETFTVLAAYNGRPQGAFHVVMRSSHTIKGSFLCGSCGSVGYVLTGDSVRFVYMHQLELSTGCHTGTDFSGNFYGP
SQ  YRDAQVVQLPVQDYTQTVNVVAWLYAAILNRCNWFVQSDSCSLEEFNVWAMTNGFSSIKADLVLDALASMTGVTVEQVLA
SQ  AIKRLHSGFQGKQILGSCVLEDELTPSDVYQQLAGVKLQSKRTRVIKGTCCWILASTFLFCSIISAFVKWTMFMYVTTHM
SQ  LGVTLCALCFVIFAMLLIKHKHLYLTMYIMPVLCTLFYTNYLVVGYKQSFRGLAYAWLSYFVPAVDYTYMDEVLYGVVLL
SQ  VAMVFVTMRSINHDVFSTMFLVGRLVSLVSMWYFGANLEEEVLLFLTSLFGTYTWTTMLSLATAKVIAKWLAVNVLYFTD
SQ  IPQIKLVLLSYLCIGYVCCCYWGVLSLLNSIFRMPLGVYNYKISVQELRYMNANGLRPPRNSFEALMLNFKLLGIGGVPV
SQ  IEVSQIQSRLTDVKCANVVLLNCLQHLHIASNSKLWQYCSTLHNEILATSDLSVAFDKLAQLLVVLFANPAAVDSKCLAS
SQ  IEEVSDDYVRDNTVLQALQSEFVNMASFVEYELAKKNLDEAKASGSANQQQIKQLEKACNIAKSAYERDRAVARKLERMA
SQ  DLALTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPPLTSNTLTIIVPDKQVFDQVVD
SQ  NVYVTYAPNVWHIQSIQDADGAVKQLNEIDVNSTWPLVISANRHNEVSTVVLQNNELMPQKLRTQVVNSGSDMNCNIPTQ
SQ  CYYNTTGTGKIVYAILSDCDGLKYTKIVKEDGNCVVLELDPPCKFSVQDVKGLKIKYLYFVKGCNTLARGWVVGTLSSTV
SQ  RLQAGTATEYASNSAILSLCAFSVDPKKTYLDYIQQGGVPVTNCVKMLCDHAGTGMAITIKPEATTNQDSYGGASVCIYC
SQ  RSRVEHPDVDGLCKLRGKFVQVPLGIKDPVSYVLTHDVCQVCGFWRDGSCSCVGTGSQFQSKDTNFLNGFGVQV
//
ID  P0C6V2;
PN  Non-structural protein 11;
GN  1a;
OS  11151;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6V2;
DR  UNIPROT: Q9IW06;
DR  PDB: 1LVO;
DR  PDB: 1P9U;
DR  PDB: 2AMP;
DR  PDB: 3MP2;
DR  PDB: 3ZBD;
DR  PDB: 4F49;
DR  PDB: 6IVD;
DR  Pfam: PF16688;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SAGC]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSKQFKILVNEDYQVNVPSLPIRDVLQEIKYCYRNGFEGYVFVPEYCRDLVDCDRKDHYVIGVLGNGVSDLKPVLLTEP
SQ  SVMLQGFIVRANCNGVLEDFDLKIARTGRGAIYVDQYMCGADGKPVIEGDFKDYFGDEDIIEFEGEEYHCAWTTVRDEKP
SQ  LNQQTLFTIQEIQYNLDIPHKLPNCATRHVAPPVKKNSKIVLSEDYKKLYDIFGSPFMGNGDCLSKCFDTLHFIAATLRC
SQ  PCGSESSGVGDWTGFKTACCGLSGKVKGVTLGDIKPGDAVVTSMSAGKGVKFFANCVLQYAGDVEGVSIWKVIKTFTVDE
SQ  TVCTPGFEGELNDFIKPESKSLVACSVKRAFITGDIDDAVHDCIITGKLDLSTNLFGNVGLLFKKTPWFVQKCGALFVDA
SQ  WKVVEELCGSLTLTYKQIYEVVASLCTSAFTIVNYKPTFVVPDNRVKDLVDKCVKVLVKAFDVFTQIITIAGIEAKCFVL
SQ  GAKYLLFNNALVKLVSVKILGKKQKGLECAFFATSLVGATVNVTPKRTETATISLNKVDDVVAPGEGYIVIVGDMAFYKS
SQ  GEYYFMMSSPNFVLTNNVFKAVKVPSYDIVYDVDNDTKSKMIAKLGSSFEYDGDIDAAIVKVNELLIEFRQQSLCFRAFK
SQ  DDKSIFVEAYFKKYKMPACLAKHIGLWNIIKKDSCKRGFLNLFNHLNELEDIKETNIQAIKNILCPDPLLDLDYGAIWYN
SQ  CMPGCSDPSVLGSVQLLIGNGVKVVCDGCKGFANQLSKGYNKLCNAARNDIEIGGIPFSTFKTPTNTFIEMTDAIYSVIE
SQ  QGKALSFRDADVPVVDNGTISTADWSEPILLEPAEYVKPKNNGNVIVIAGYTFYKDEDEHFYPYGFGKIVQRMYNKMGGG
SQ  DKTVSFSEEVDVQEIAPVTRVKLEFEFDNEIVTGVLERAIGTRYKFTGTTWEEFEESISEELDAIFDTLANQGVELEGYF
SQ  IYDTCGGFDIKNPDGIMISQYDINITADEKSEVSASSEEEEVESVEEDPENEIVEASEGAEGTSSQEEVETVEVADITST
SQ  EEDVDIVEVSAKDDPWAAAVDVQEAEQFNPSLPPFKTTNLNGKIILKQGDNNCWINACCYQLQAFDFFNNEAWEKFKKGD
SQ  VMDFVNLCYAATTLARGHSGDAEYLLELMLNDYSTAKIVLAAKCGCGEKEIVLERAVFKLTPLKESFNYGVCGDCMQVNT
SQ  CRFLSVEGSGVFVHDILSKQTPEAMFVVKPVMHAVYTGTTQNGHYMVDDIEHGYCVDGMGIKPLKKRCYTSTLFINANVM
SQ  TRAEKPKQEFKVEKVEQQPIVEENKSSIEKEEIQSPKNDDLILPFYKAGKLSFYQGALDVLINFLEPDVIVNAANGDLKH
SQ  MGGVARAIDVFTGGKLTERSKDYLKKNKSIAPGNAVFFENVIEHLSVLNAVGPRNGDSRVEAKLCNVYKAIAKCEGKILT
SQ  PLISVGIFNVRLETSLQCLLKTVNDRGLNVFVYTDQERQTIENFFSCSIPVNVTEDNVNHERVSVSFDKTYGEQLKGTVV
SQ  IKDKDVTNQLPSAFDVGQKVIKAIDIDWQAHYGFRDAAAFSASSHDAYKFEVVTHSNFIVHKQTDNNCWINAICLALQRL
SQ  KPQWKFPGVRGLWNEFLERKTQGFVHMLYHISGVKKGEPGDAELMLHKLGDLMDNDCEIIVTHTTACDKCAKVEKFVGPV
SQ  VAAPLAIHGTDETCVHGVSVNVKVTQIKGTVAITSLIGPIIGEVLEATGYICYSGSNRNGHYTYYDNRNGLVVDAEKAYH
SQ  FNRDLLQVTTAIASNFVVKKPQAEERPKNCAFNKVAASPKIVQEQKLLAIESGANYALTEFGRYADMFFMAGDKILRLLL
SQ  EVFKYLLVLFMCLRSTKMPKVKVKPPLAFKDFGAKVRTLNYMRQLNKPSVWRYAKLVLLLIAIYNFFYLFVSIPVVHKLT
SQ  CNGAVQAYKNSSFIKSAVCGNSILCKACLASYDELADFQHLQVTWDFKSDPLWNRLVQLSYFAFLAVFGNNYVRCFLMYF
SQ  VSQYLNLWLSYFGYVEYSWFLHVVNFESISAEFVIVVIVVKAVLALKHIVFACSNPSCKTCSRTARQTRIPIQVVVNGSM
SQ  KTVYVHANGTGKFCKKHNFYCKNCDSYGFENTFICDEIVRDLSNSVKQTVYATDRSHQEVTKVECSDGFYRFYVGDEFTS
SQ  YDYDVKHKKYSSQEVLKSMLLLDDFIVYSPSGSALANVRNACVYFSQLIGKPIKIVNSDLLEDLSVDFKGALFNAKKNVI
SQ  KNSFNVDVSECKNLDECYRACNLNVSFSTFEMAVNNAHRFGILITDRSFNNFWPSKVKPGSSGVSAMDIGKCMTSDAKIV
SQ  NAKVLTQRGKSVVWLSQDFAALSSTAQKVLVKTFVEEGVNFSLTFNAVGSDDDLPYERFTESVSPKSGSGFFDVITQLKQ
SQ  IVILVFVFIFICGLCSVYSVATQSYIESAEGYDYMVIKNGIVQPFDDTISCVHNTYKGFGDWFKAKYGFIPTFGKSCPIV
SQ  VGTVFDLENMRPIPDVPAYVSIVGRSLVFAINAAFGVTNMCYDHTGNAVSKDSYFDTCVFNTACTTLTGLGGTIVYCAKQ
SQ  GLVEGAKLYSDLMPDYYYEHASGNMVKLPAIIRGLGLRFVKTQATTYCRVGECIDSKAGFCFGGDNWFVYDNEFGNGYIC
SQ  GNSVLGFFKNVFKLFNSNMSVVATSGAMLVNIIIACLAIAMCYGVLKFKKIFGDCTFLIVMIIVTLVVNNVSYFVTQNTF
SQ  FMIIYAIVYYFITRKLAYPGILDAGFIIAYINMAPWYVITAYILVFLYDSLPSLFKLKVSTNLFEGDKFVGNFESAAMGT
SQ  FVIDMRSYETIVNSTSIARIKSYANSFNKYKYYTGSMGEADYRMACYAHLGKALMDYSVNRTDMLYTPPTVSVNSTLQSG
SQ  LRKMAQPSGLVEPCIVRVSYGNNVLNGLWLGDEVICPRHVIASDTTRVINYENEMSSVRLHNFSVSKNNVFLGVVSARYK
SQ  GVNLVLKVNQVNPNTPEHKFKSIKAGESFNILACYEGCPGSVYGVNMRSQGTIKGSFIAGTCGSVGYVLENGILYFVYMH
SQ  HLELGNGSHVGSNFEGEMYGGYEDQPSMQLEGTNVMSSDNVVAFLYAALINGERWFVTNTSMSLESYNTWAKTNSFTELS
SQ  STDAFSMLAAKTGQSVEKLLDSIVRLNKGFGGRTILSYGSLCDEFTPTEVIRQMYGVNLQAGKVKSFFYPIMTAMTILFA
SQ  FWLEFFMYTPFTWINPTFVSIVLAVTTLISTVFVSGIKHKMLFFMSFVLPSVILVTAHNLFWDFSYYESLQSIVENTNTM
SQ  FLPVDMQGVMLTVFCFIVFVTYSVRFFTCKQSWFSLAVTTILVIFNMVKIFGTSDEPWTENQIAFCFVNMLTMIVSLTTK
SQ  DWMVVIASYRIAYYIVVCVMPSAFVSDFGFMKCISIVYMACGYLFCCYYGILYWVNRFTCMTCGVYQFTVSAAELKYMTA
SQ  NNLSAPKNAYDAMILSAKLIGVGGKRNIKISTVQSKLTEMKCTNVVLLGLLSKMHVESNSKEWNYCVGLHNEINLCDDPE
SQ  IVLEKLLALIAFFLSKHNTCDLSELIESYFENTTILQSVASAYAALPSWIALEKARADLEEAKKNDVSPQILKQLTKAFN
SQ  IAKSDFEREASVQKKLDKMAEQAAASMYKEARAVDRKSKIVSAMHSLLFGMLKKLDMSSVNTIIDQARNGVLPLSIIPAA
SQ  SATRLVVITPSLEVFSKIRQENNVHYAGAIWTIVEVKDANGSHVHLKEVTAANELNLTWPLSITCERTTKLQNNEIMPGK
SQ  LKERAVRASATLDGEAFGSGKALMASESGKSFMYAFIASDNNLKYVKWESNNDIIPIELEAPLRFYVDGANGPEVKYLYF
SQ  VKNLNTLRRGAVLGYIGATVRLQAGKPTEHPSNSSLLTLCAFSPDPAKAYVDAVKRGMQPVNNCVKMLSNGAGNGMAVTN
SQ  GVEANTQQDSYGGASVCIYCRCHVEHPAIDGLCRYKGKFVQIPTGTQDPIRFCIENEVCVVCGCWLNNGCMCDRTSMQSF
SQ  TVDQSYLNECGVLVQLD
//
ID  P0C6V3;
PN  Non-structural protein 11;
GN  1a;
OS  11122;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6U8}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 4]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6U8}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles (By similarity). Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER) (By similarity). {ECO:0000250|UniProtKB:P0C6U8, ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 6]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6U8}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
DR  UNIPROT: P0C6V3;
DR  UNIPROT: P27920;
DR  Pfam: PF09401;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF17896;
DR  Pfam: PF05409;
DR  PROSITE: PS51952;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: [Isoform Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (By similarity). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [Papain-like protease]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (By similarity). Alone is able to induce paired membranes (By similarity). Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. {ECO:0000255|PROSITE-ProRule:PRU00772}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities (By similarity). Therefore plays an essential role in viral mRNAs cap methylation (By similarity). {ECO:0000250|UniProtKB:P0C6U8}.
DE  Reference Proteome: Yes;
DE  Interaction: P0C6V3; IntAct: EBI-25618177; Score: 0.61
GO  GO:0044167;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004197;
GO  GO:0042802;
GO  GO:0016829;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASSLKQGVSPKPRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRSLQTGKQFKFETVCGLFLLKGVDKIT
SQ  PGVPAKVLKATSKLADLEDIFGVSPLARKYRELLKTACQWSLTVEALDVRAQTLDEIFDPTEILWLQVAAKIHVSSMAMR
SQ  RLVGEVTAKVMDALGSNLSALFQIVKQQIARIFQKALAIFENVNELPQRIAALKMAFAKCARSITVVVVERTLVVKEFAG
SQ  TCLASINGAVAKFFEELPNGFMGSKIFTTLAFFKEAAVRVVENIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK
SQ  ADIPVEPEGWSAILDGHLCYVFRSGDRFYAAPLSGNFALSDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVSELVTA
SQ  LKKGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLRLFQSARVIAEDVWSSFTEKSFEFWKLAYGKVRNLEEFVKTYVC
SQ  KAQMSIVILAAVLGEDIWHLVSQVIYKLGVLFTKVVDFCDKHWKGFCVQLKRAKLIVTETFCVLKGVAQHCFQLLLDAIH
SQ  SLYKSFKKCALGRIHGDLLFWKGGVHKIVQDGDEIWFDAIDSVDVEDLGVVQEKSIDFEVCDDVTLPENQPGHMVQIEDD
SQ  GKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVPIKVSIECCGEPWNTIFKKAYKEPIEV
SQ  DTDLTVEQLLSVIYEKMCDDLKLFPEAPEPPPFENVALVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGEA
SQ  EECDTNSECEEEDEDTKVLALIQDPASIKYPLPLDEDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKPLPQKV
SQ  VDVLGDWGEAVDAQEQLCQQEPLQHTFEEPVENSTGSSKTMTEQVVVEDQELPVVEQDQDVVVYTPTDLEVAKETAEEVD
SQ  EFILIFAVPKEEVVSQKDGAQIKQEPIQVVKPQREKKAKKFKVKPATCEKPKFLEYKTCVGDLTVVIAKALDEFKEFCIV
SQ  NAANEHMTHGSGVAKAIADFCGLDFVEYCEDYVKKHGPQQRLVTPSFVKGIQCVNNVVGPRHGDNNLHEKLVAAYKNVLV
SQ  DGVVNYVVPVLSLGIFGVDFKMSIDAMREAFEGCTIRVLLFSLSQEHIDYFDVTCKQKTIYLTEDGVKYRSIVLKPGDSL
SQ  GQFGQVYAKNKIVFTADDVEDKEILYVPTTDKSILEYYGLDAQKYVIYLQTLAQKWNVQYRDNFLILEWRDGNCWISSAI
SQ  VLLQAAKIRFKGFLTEAWAKLLGGDPTDFVAWCYASCTAKVGDFSDANWLLANLAEHFDADYTNAFLKKRVSCNCGIKSY
SQ  ELRGLEACIQPVRATNLLHFKTQYSNCPTCGANNTDEVIEASLPYLLLFATDGPATVDCDEDAVGTVVFVGSTNSGHCYT
SQ  QAAGQAFDNLAKDRKFGKKSPYITAMYTRFAFKNETSLPVAKQSKGKSKSVKEDVSNLATSSKASFDNLTDFEQWYDSNI
SQ  YESLKVQESPDNFDKYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFIYKLTPDTDENSKAPVYYPVLDAISLKAIWVE
SQ  GNANFVVGHPNYYSKSLHIPTFWENAENFVKMGDKIGGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKLIG
SQ  KAATFIADKVGGGVVRNITDSIKGLCGITRGHFERKMSPQFLKTLMFFLFYFLKASVKSVVASYKTVLCKVVLATLLIVW
SQ  FVYTSNPVMFTGIRVLDFLFEGSLCGPYKDYGKDSFDVLRYCADDFICRVCLHDKDSLHLYKHAYSVEQVYKDAASGFIF
SQ  NWNWLYLVFLILFVKPVAGFVIICYCVKYLVLNSTVLQTGVCFLDWFVQTVFSHFNFMGAGFYFWLFYKIYIQVHHILYC
SQ  KDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVKPT
SQ  AYAYHVVDEACLVDDFVNLKYKAATPGKDSASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEAKN
SQ  AAIYYAQYLCKPILILDQALYEQLVVEPVSKSVIDKVCSILSSIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIFCH
SQ  NHDVDYTGDGFTNVIPSYGIDTGKLTPRDRGFLINADASIANLRVKNAPPVVWKFSELIKLSDSCLKYLISATVKSGVRF
SQ  FITKSGAKQVIACHTQKLLVEKKAGGIVSGTFKCFKSYFKWLLIFYILFTACCSGYYYMEVSKSFVHPMYDVNSTLHVEG
SQ  FKVIDKGVLREIVPEDTCFSNKFVNFDAFWGRPYDNSRNCPIVTAVIDGDGTVATGVPGFVSWVMDGVMFIHMTQTERKP
SQ  WYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVRLI
SQ  VPQQILHTPYVVKFVSDSYCRGSVCEYTRPGYCVSLNPQWVLFNDEYTSKPGVFCGSTVRELMFSMVSTFFTGVNPNIYM
SQ  QLATMFLILVVVVLIFAMVIKFQGVFKAYATTVFITMLVWVINAFILCVHSYNSVLAVILLVLYCYASLVTSRNTVIIMH
SQ  CWLVFTFGLIVPTWLACCYLGFIIYMYTPLFLWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGSEFVKLTNEIGDKF
SQ  EAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEIVYTPPRYSIGVSRLQSGFKKLVSPSSAVEKCIVSVS
SQ  YRGNNLNGLWLGDTIYCPRHVLGKFSGDQWNDVLNLANNHEFEVTTQHGVTLNVVSRRLKGAVLILQTAVANAETPKYKF
SQ  IKANCGDSFTIACAYGGTVVGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEFYG
SQ  GYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSLPKWLESTTVSVDDYNKWAGDNGFTPFSTSTAITKLSAITGV
SQ  DVCKLLRTIMVKNSQWGGDPILGQYNFEDELTPESVFNQIGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTAVP
SQ  LKFYVYAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPWMF
SQ  LPLVLYTAFKCVQGCYMNSFNTSLLMLYQFVKLGFVIYTSSNTLTAYTEGNWELFFELVHTTVLANVSSNSLIGLFVFKC
SQ  AKWMLYYCNATYLNNYVLMAVMVNCIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKINPPKTVWEVFST
SQ  NILIQGIGGDRVLPIATVQAKLSDVKCTTVVLMQLLTKLNVEANSKMHVYLVELHNKILASDDVGECMDNLLGMLITLFC
SQ  IDSTIDLSEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKNLYEKVLVDSKNGGVTQQELAAYRKAANIAKSVFDRDLA
SQ  VQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQASSGVVPLATVPIVCSNKLTLVIPD
SQ  PETWVKCVEGVHVTYSTVVWNIDTVIDADGTELHPTSTGSGLTYCISGANIAWPLKVNLTRNGHNKVDVVLQNNELMPHG
SQ  VKTKACVAGVDQAHCSVESKCYYTNISGNSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGVKVEVVYLYF
SQ  IKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFAIT
SQ  SKPSPTPDQDSYGGASVCLYCRAHIAHPGSVGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCDSL
SQ  RQPKSSVQSVAGASDFDKNYLNGYGVAVRLG
//
ID  P0C6V4;
PN  Non-structural protein 11;
GN  1a;
OS  160235;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6U8}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 4]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6U8}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles (By similarity). Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER) (By similarity). {ECO:0000250|UniProtKB:P0C6U8, ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 6]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6U8}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
DR  UNIPROT: P0C6V4;
DR  UNIPROT: Q91QT2;
DR  Pfam: PF09401;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF17896;
DR  Pfam: PF05409;
DR  PROSITE: PS51952;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: [Isoform Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (By similarity). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [Papain-like protease]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (By similarity). Alone is able to induce paired membranes (By similarity). Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. {ECO:0000255|PROSITE-ProRule:PRU00772}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities (By similarity). Therefore plays an essential role in viral mRNAs cap methylation (By similarity). {ECO:0000250|UniProtKB:P0C6U8}.
DE  Reference Proteome: No;
GO  GO:0044167;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004197;
GO  GO:0016829;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASSLKQGVSPKPRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRSLQTGKQFKFETVCGLFLLKGVDKIT
SQ  PGVPAKVLKATSKLADLEDIFGVSPLARKYRELLKTACQWSLTVEALDVRAQTLDEIFDPTEILWLQVAAKIHVSSMAMR
SQ  RLVGEVTAKVMDALGSNLSALFQIVKQQIARIFQKALAIFENVNELPQRIAALKMAFAKCARSITVVVVERTLVVKEFAG
SQ  TCLASINGAVAKFFEELPNGFMGSKIFTTLAFFKEAAVRVVENIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK
SQ  ADIPVEPEGWSAILDGHLCYVFRSGDRFYAAPLSGNFALSDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVSELVTA
SQ  LKKGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLRLFQSARVIAEDVWSSFTEKSFEFWKLAYGKVRNLEEFVKTYVC
SQ  KAQMSIVILAAVLGEDIWHLVSQVIYKLGVLFTKVVDFCDKHWKGFCVQLKRAKLIVTETFCVLKGVAQHCFQLLLDAIH
SQ  SLYKSFKKCALGRIHGDLLFWKGGVHKIVQDGDEIWFDAIDSVDVEDLGVVQEKSIDFEVCDDVTLPENQPGHMVQIEDD
SQ  GKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVPIKVSIECCGEPWNTIFKKAYKEPIEV
SQ  DTDLTVEQLLSVIYEKMCDDLKLFPEAPEPPPFENVALVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGEA
SQ  EECDTNSECEEEDEDTKVLALIQDPASIKYPLPLDEDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKPLPQKV
SQ  VDVLGDWGEAVDAQEQLCQQEPLQHTFEEPVENSTGSSKTMTEQVVVEDQELPVVEQDQDVVVYTPTDLEVAKETAEEVD
SQ  EFILIFAVPKEEVVSQKDGAQIKQEPIQVVKPQREKKAKKFKVKPATCEKPKFLEYKTCVGDLTVVIAKALDEFKEFCIV
SQ  NAANEHMTHGSGVAKAIADFCGLDFVEYCEDYVKKHGPQQRLVTPSFVKGIQCVNNVVGPRHGDNNLHEKLVAAYKNVLV
SQ  DGVVNYVVPVLSLGIFGVDFKMSIDAMREAFEGCTIRVLLFSLSQEHIDYFDVTCKQKTIYLTEDGVKYRSIVLKPGDSL
SQ  GQFGQVYAKNKIVFTADDVEDKEILYVPTTDKSILEYYGLDAQKYVIYLQTLAQKWNVQYRDNFLILEWRDGNCWISSAI
SQ  VLLQAAKIRFKGFLTEAWAKLLGGDPTDFVAWCYASCTAKVGDFSDANWLLANLAEHFDADYTNAFLKKRVSCNCGIKSY
SQ  ELRGLEACIQPVRATNLLHFKTQYSNCPTCGANNTDEVIEASLPYLLLFATDGPATVDCDEDAVGTVVFVGSTNSGHCYT
SQ  QAAGQAFDNLAKDRKFGKKSPYITAMYTRFAFKNETSLPVAKQSKGKSKSVKEDVSNLATSSKASFDNLTDFEQWYDSNI
SQ  YESLKVQESPDNFDKYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFIYKLTPDTDENSKAPVYYPVLDAISLKAIWVE
SQ  GNANFVVGHPNYYSKSLHIPTFWENAENFVKMGDKIGGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKLIG
SQ  KAATFIADKVGGGVVRNITDSIKGLCGITRGHFERKMSPQFLKTLMFFLFYFLKASVKSVVASYKTVLCKVVLATLLIVW
SQ  FVYTSNPVMFTGIRVLDFLFEGSLCGPYKDYGKDSFDVLRYCADDFICRVCLHDKDSLHLYKHAYSVEQVYKDAASGFIF
SQ  NWNWLYLVFLILFVKPVAGFVIICYCVKYLVLNSTVLQTGVCFLDWFVQTVFSHFNFMGAGFYFWLFYKIYIQVHHILYC
SQ  KDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVKPT
SQ  AYAYHVVDEACLVDDFVNLKYKAATPGKDSASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEAKN
SQ  AAIYYAQYLCKPILILDQALYEQLVVEPVSKSVIDKVCSILSSIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIFCH
SQ  NHDVDYTGDGFTNVIPSYGIDTGKLTPRDRGFLINADASIANLRVKNAPPVVWKFSELIKLSDSCLKYLISATVKSGVRF
SQ  FITKSGAKQVIACHTQKLLVEKKAGGIVSGTFKCFKSYFKWLLIFYILFTACCSGYYYMEVSKSFVHPMYDVNSTLHVEG
SQ  FKVIDKGVLREIVPEDTCFSNKFVNFDAFWGRPYDNSRNCPIVTAVIDGDGTVATGVPGFVSWVMDGVMFIHMTQTERKP
SQ  WYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVRLI
SQ  VPQQILHTPYVVKFVSDSYCRGSVCEYTRPGYCVSLNPQWVLFNDEYTSKPGVFCGSTVRELMFSMVSTFFTGVNPNIYM
SQ  QLATMFLILVVVVLIFAMVIKFQGVFKAYATTVFITMLVWVINAFILCVHSYNSVLAVILLVLYCYASLVTSRNTVIIMH
SQ  CWLVFTFGLIVPTWLACCYLGFIIYMYTPLFLWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGSEFVKLTNEIGDKF
SQ  EAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEIVYTPPRYSIGVSRLQSGFKKLVSPSSAVEKCIVSVS
SQ  YRGNNLNGLWLGDTIYCPRHVLGKFSGDQWNDVLNLANNHEFEVTTQHGVTLNVVSRRLKGAVLILQTAVANAETPKYKF
SQ  IKANCGDSFTIACAYGGTVVGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEFYG
SQ  GYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSLPKWLESTTVSVDDYNKWAGDNGFTPFSTSTAITKLSAITGV
SQ  DVCKLLRTIMVKNSQWGGDPILGQYNFEDELTPESVFNQIGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTAVP
SQ  LKFYVYAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPWMF
SQ  LPLVLYTAFKCVQGCYMNSFNTSLLMLYQFVKLGFVIYTSSNTLTAYTEGNWELFFELVHTTVLANVSSNSLIGLFVFKC
SQ  AKWMLYYCNATYLNNYVLMAVMVNCIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKINPPKTVWEVFST
SQ  NILIQGIGGDRVLPIATVQAKLSDVKCTTVVLMQLLTKLNVEANSKMHVYLVELHNKILASDDVGECMDNLLGMLITLFC
SQ  IDSTIDLSEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKNLYEKVLVDSKNGGVTQQELAAYRKAANIAKSVFDRDLA
SQ  VQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQASSGVVPLATVPIVCSNKLTLVIPD
SQ  PETWVKCVEGVHVTYSTVVWNIDTVIDADGTELHPTSTGSGLTYCISGANIAWPLKVNLTRNGHNKVDVVLQNNELMPHG
SQ  VKTKACVAGVDQAHCSVESKCYYTNISGNSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGVKVEVVYLYF
SQ  IKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFAIT
SQ  SKPSPTPDQDSYGGASVCLYCRAHIAHPGSVGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCDSL
SQ  RQPKSSVQSVAGASDFDKNYLNGYGVAVRLG
//
ID  P0C6V5;
PN  Non-structural protein 11;
GN  1a;
OS  11127;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6U8}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 4]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6U8}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles (By similarity). Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER) (By similarity). {ECO:0000250|UniProtKB:P0C6U8, ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 6]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6U8}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
DR  UNIPROT: P0C6V5;
DR  UNIPROT: Q0GNB9;
DR  PDB: 3EWO;
DR  PDB: 3EWP;
DR  PDB: 3LD1;
DR  Pfam: PF09401;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF17896;
DR  Pfam: PF05409;
DR  PROSITE: PS51952;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: [Isoform Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (By similarity). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [Papain-like protease]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (By similarity). Alone is able to induce paired membranes (By similarity). Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. {ECO:0000255|PROSITE-ProRule:PRU00772}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities (By similarity). Therefore plays an essential role in viral mRNAs cap methylation (By similarity). {ECO:0000250|UniProtKB:P0C6U8}.
DE  Reference Proteome: Yes;
GO  GO:0044167;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004197;
GO  GO:0016829;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASSLKQGVSPKLRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRNLQTGKQFKFETVCGLFLLKGVDKIT
SQ  PGVPAKVLKATSKLADLEDIFGVSPFARKYRELLKTACQWSLTVETLDARAQTLDEIFDPTEILWLQVAAKIQVSAMAMR
SQ  RLVGEVTAKVMDALGSNMSALFQIFKQQIVRIFQKALAIFENVSELPQRIAALKMAFAKCAKSITVVVMERTLVVREFAG
SQ  TCLASINGAVAKFFEELPNGFMGAKIFTTLAFFREAAVKIVDNIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK
SQ  AEIPVESEGWSAILGGHLCYVFKSGDRFYAAPLSGNFALHDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVAELVAA
SQ  IKRGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLKLFQSARVKVEDVWSSLTEKSFEFWRLAYGKVRNLEEFVKTCFC
SQ  KAQMAIVILATVLGEGIWHLVSQVIYKVGGLFTKVVDFCEKYWKGFCAQLKRAKLIVTETLCVLKGVAQHCFQLLLDAIQ
SQ  FMYKSFKKCALGRIHGDLLFWKGGVHKIIQEGDEIWFDAIDSIDVEDLGVVQEKLIDFDVCDNVTLPENQPGHMVQIEDD
SQ  GKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVFIKVSIECCGEPWNTIFKKAYKEPIEV
SQ  ETDLTVEQLLSVVYEKMCDDLKLFPEAPEPPPFENVTLVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGDA
SQ  EECDTNLECEEEDEDTKVLALIQDPASNKYPLPLDDDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKALPQKV
SQ  IDVLGDWGEAVDAQEQLCQQESTRVISEKSVEGFTGSCDAMAEQAIVEEQEIVPVVEQSQDVVVFTPADLEVVKETAEEV
SQ  DEFILISAVPKEEVVSQEKEEPQVEQEPTLVVKAQREKKAKKFKVKPATCEKPKFLEYKTCVGDLAVVIAKALDEFKEFC
SQ  IVNAANEHMSHGGGVAKAIADFCGPDFVEYCADYVKKHGPQQKLVTPSFVKGIQCVNNVVGPRHGDSNLREKLVAAYKSV
SQ  LVGGVVNYVVPVLSSGIFGVDFKISIDAMREAFKGCAIRVLLFSLSQEHIDYFDATCKQKTIYLTEDGVKYRSVVLKPGD
SQ  SLGQFGQVFARNKVVFSADDVEDKEILFIPTTDKTILEYYGLDAQKYVTYLQTLAQKWDVQYRDNFVILEWRDGNCWISS
SQ  AIVLLQAAKIRFKGFLAEAWAKLLGGDPTDFVAWCYASCNAKVGDFSDANWLLANLAEHFDADYTNALLKKCVSCNCGVK
SQ  SYELRGLEACIQPVRAPNLLHFKTQYSNCPTCGASSTDEVIEASLPYLLLFATDGPATVDCDENAVGTVVFIGSTNSGHC
SQ  YTQADGKAFDNLAKDRKFGRKSPYITAMYTRFSLRSENPLLVVEHSKGKAKVVKEDVSNLATSSKASFDDLTDFEQWYDS
SQ  NIYESLKVQETPDNLDEYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFTYKLTPDTDENSKTPVYYPVLDSISLRAIW
SQ  VEGSANFVVGHPNYYSKSLRIPTFWENAESFVKMGYKIDGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKI
SQ  LVKAATYVADKVGDGVVRNITDRIKGLCGFTRGHFEKKMSLQFLKTLVFFFFYFLKASSKSLVSSYKIVLCKVVFATLLI
SQ  VWFIYTSNPVVFTGIRVLDFLFEGSLCGPYNDYGKDSFDVLRYCAGDFTCRVCLHDRDSLHLYKHAYSVEQIYKDAASGI
SQ  NFNWNWLYLVFLILFVKPVAGFVIICYCVKYLVLSSTVLQTGVGFLDWFVKTVFTHFNFMGAGFYFWLFYKIYVQVHHIL
SQ  YCKDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVK
SQ  PTAYAYHVVYEACVVDDFVNLKYKAAIPGKDNASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEA
SQ  KNAAVYYAQYLCKPILILDQALYEQLIVEPVSKSVIDKVCSILSNIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIF
SQ  CHNHEVEYTGDGFTNVIPSYGMDTDKLTPRDRGFLINADASIANLRVKNAPPVVWKFSDLIKLSDSCLKYLISATVKSGG
SQ  RFFITKSGAKQVISCHTQKLLVEKKAGGVINNTFKWFMSCFKWLFVFYILFTACCLGYYYMEMNKSFVHPMYDVNSTLHV
SQ  EGFKVIDKGVIREIVSEDNCFSNKFVNFDAFWGKSYENNKNCPIVTVVIDGDGTVAVGVPGFVSWVMDGVMFVHMTQTDR
SQ  RPWYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVR
SQ  LIVPQQILHTPYIVKFVSDSYCRGSVCEYTKPGYCVSLDSQWVLFNDEYISKPGVFCGSTVRELMFNMVSTFFTGVNPNI
SQ  YIQLATMFLILVVIVLIFAMVIKFQGVFKAYATIVFTIMLVWVINAFVLCVHSYNSVLAVILLVLYCYASMVTSRNTAII
SQ  MHCWLVFTFGLIVPTWLACCYLGFILYMYTPLVFWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGTEFVKLTNEIGD
SQ  KFEAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEVVYTPPRYSIGVSRLQAGFKKLVSPSSAVEKCIVS
SQ  VSYRGNNLNGLWLGDSIYCPRHVLGKFSGDQWGDVLNLANNHEFEVVTQNGVTLNVVSRRLKGAVLILQTAVANAETPKY
SQ  KFVKANCGDSFTIACSYGGTVIGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEF
SQ  YGGYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSQPKWLESTTVSIEDYNRWASDNGFTPFSTSTAITKLSAIT
SQ  GVDVCKLLRTIMVKSAQWGSDPILGQYNFEDELTPESVFNQVGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTA
SQ  VPLKFYVHAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPW
SQ  MLLPLVLYTAFKCVQGCYMNSFNTSLLMLYQFMKLGFVIYTSSNTLTAYTEGNWELFFELVHTIVLANVSSNSLIGLIVF
SQ  KCAKWMLYYCNATYFNNYVLMAVMVNGIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKVNPPKTVWEVF
SQ  TTNILIQGIGGDRVLPIATVQSKLSDVKCTTVVLMQLLTKLNVEANSKMHAYLVELHNKILASDDVGECMDNLLGMLITL
SQ  FCIDSTIDLGEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKSIYEKVLADSKNGGVTQQELAAYRKAANIAKSVFDRD
SQ  LAVQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQANSGVVPLATVPIVCSNKLTLVI
SQ  PDPETWVKCVEGVHVTYSTVVWNIDCVTDADGTELHPTSTGSGLTYCISGDNIAWPLKVNLTRNGHNKVDVALQNNELMP
SQ  HGVKTKACVAGVDQAHCSVESKCYYTSISGSSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGDKVEVVYL
SQ  YFIKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFA
SQ  ITSKPSPTPDQDSYGGASVCLYCRAHIAHPGGAGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCD
SQ  SLRQPKPSVQSVAVASGFDKNYLNGYGVAVRLG
//
ID  K9N638;
PN  Non-structural protein 11;
GN  1a;
OS  1263720;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like proteinase]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm. Note=Localizes in virally- induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: K9N638;
DR  PDB: 4R3D;
DR  PDB: 5DUS;
DR  PDB: 5HIH;
DR  PDB: 5WKJ;
DR  PDB: 5WKK;
DR  PDB: 5WKL;
DR  PDB: 5WKM;
DR  PDB: 7T3Y;
DR  PDB: 7T3Z;
DR  PDB: 7T40;
DR  PDB: 7T41;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF11633;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000269|PubMed:26311885}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B. signaling. {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:25142582}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: No;
DE  Interaction: Q53GL7; IntAct: EBI-25618963; Score: 0.44
DE  Interaction: P05161; IntAct: EBI-25821105; Score: 0.44
DE  Interaction: R9QB93; IntAct: EBI-25821183; Score: 0.44
DE  Interaction: E0D5D4; IntAct: EBI-25821283; Score: 0.44
DE  Interaction: Q64339; IntAct: EBI-25821343; Score: 0.56
DE  Interaction: A0A5N4DAX7; IntAct: EBI-25821368; Score: 0.44
DE  Interaction: Q9GKP4; IntAct: EBI-25821596; Score: 0.56
DE  Interaction: L5LC70; IntAct: EBI-25821608; Score: 0.44
DE  Interaction: K9N638; IntAct: EBI-26366109; Score: 0.44
DE  Interaction: P0C6X7; IntAct: EBI-26366798; Score: 0.44
DE  Interaction: O14734; IntAct: EBI-26374663; Score: 0.40
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0008242;
GO  GO:0003727;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHT
SQ  RHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHY
SQ  ERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEG
SQ  FITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYG
SQ  KESLENPTYIYHSAFIECGSCGNDSWLTGNAIQGFACGCGASYTANDVEVQSSGMIKPNALLCATCPFAKGDSCSSNCKH
SQ  SVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGCEEGTMYFVPRAKSVVSRIGDSIFTGCTGSWNKVTQIANMFLEQT
SQ  QHSLNFVGEFVVNDVVLAILSGTTTNVDKIRQLLKGVTLDKLRDYLADYDVAVTAGPFMDNAINVGGTGLQYAAITAPYV
SQ  VLTGLGESFKKVATIPYKVCNSVKDTLTYYAHSVLYRVFPYDMDSGVSSFSELLFDCVDLSVASTYFLVRLLQDKTGDFM
SQ  STIITSCQTAVSKLLDTCFEATEATFNFLLDLAGLFRIFLRNAYVYTSQGFVVVNGKVSTLVKQVLDLLNKGMQLLHTKV
SQ  SWAGSNISAVIYSGRESLIFPSGTYYCVTTKAKSVQQDLDVILPGEFSKKQLGLLQPTDNSTTVSVTVSSNMVETVVGQL
SQ  EQTNMHSPDVIVGDYVIISEKLFVRSKEEDGFAFYPACTNGHAVPTLFRLKGGAPVKKVAFGGDQVHEVAAVRSVTVEYN
SQ  IHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFS
SQ  LHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIA
SQ  QVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVIT
SQ  ECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNIL
SQ  HVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSL
SQ  TFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPL
SQ  GYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLL
SQ  HWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGAD
SQ  ISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMT
SQ  LDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDV
SQ  VLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHY
SQ  VHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTY
SQ  SPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKG
SQ  KPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVS
SQ  FVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFAT
SQ  RTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVD
SQ  LSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRAN
SQ  SFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQ
SQ  TSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGK
SQ  RTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQP
SQ  FYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIA
SQ  TKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQIT
SQ  NESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSK
SQ  LRANDNILSVRFTANKIVGGAPTWFNALRDFTLKGYVLATIIVFLCAVLMYLCLPTFSMVPVEFYEDRILDFKVLDNGII
SQ  RDVNPDDKCFANKHRSFTQWYHEHVGGVYDNSITCPLTVAVIAGVAGARIPDVPTTLAWVNNQIIFFVSRVFANTGSVCY
SQ  TPIDEIPYKSFSDSGCILPSECTMFRDAEGRMTPYCHDPTVLPGAFAYSQMRPHVRYDLYDGNMFIKFPEVVFESTLRIT
SQ  RTLSTQYCRFGSCEYAQEGVCITTNGSWAIFNDHHLNRPGVYCGSDFIDIVRRLAVSLFQPITYFQLTTSLVLGIGLCAF
SQ  LTLLFYYINKVKRAFADYTQCAVIAVVAAVLNSLCICFVASIPLCIVPYTALYYYATFYFTNEPAFIMHVSWYIMFGPIV
SQ  PIWMTCVYTVAMCFRHFFWVLAYFSKKHVEVFTDGKLNCSFQDAASNIFVINKDTYAALRNSLTNDAYSRFLGLFNKYKY
SQ  FSGAMETAAYREAAACHLAKALQTYSETGSDLLYQPPNCSITSGVLQSGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLD
SQ  NTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGA
SQ  AFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQV
SQ  HQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLY
SQ  TGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQSGVRKVTYGTAHWLFATLVSTYVIILQATKFTLWNYLFETIPTQLFP
SQ  LLFVTMAFVMLLVKHKHTFLTLFLLPVAICLTYANIVYEPTTPISSALIAVANWLAPTNAYMRTTHTDIGVYISMSLVLV
SQ  IVVKRLYNPSLSNFALALCSGVMWLYTYSIGEASSPIAYLVFVTTLTSDYTITVFVTVNLAKVCTYAIFAYSPQLTLVFP
SQ  EVKMILLLYTCLGFMCTCYFGVFSLLNLKLRAPMGVYDFKVSTQEFRFMTANNLTAPRNSWEAMALNFKLIGIGGTPCIK
SQ  VAAMQSKLTDLKCTSVVLLSVLQQLHLEANSRAWAFCVKCHNDILAATDPSEAFEKFVSLFATLMTFSGNVDLDALASDI
SQ  FDTPSVLQATLSEFSHLATFAELEAAQKAYQEAMDSGDTSPQVLKALQKAVNIAKNAYEKDKAVARKLERMADQAMTSMY
SQ  KQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGIISNARNGCIPLSVIPLCASNKLRVVIPDFTVWNQVVTYPSLNYAG
SQ  ALWDITVINNVDNEIVKSSDVVDSNENLTWPLVLECTRASTSAVKLQNNEIKPSGLKTMVVSAGQEQTNCNTSSLAYYEP
SQ  VQGRKMLMALLSDNAYLKWARVEGKDGFVSVELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQVLGHIAATVRLQAGS
SQ  NTEFASNSSVLSLVNFTVDPQKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAISVKPESTADQETYGGASVCLYCRAHIEH
SQ  PDVSGVCKYKGKFVQIPAQCVRDPVGFCLSNTPCNVCQYWIGYGCNCDSLRQAALPQSKDSNFLNESGVLL
//
ID  P0C6V6;
PN  Non-structural protein 11;
GN  1a;
OS  229032;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 1]: Host cytoplasm {ECO:0000269|PubMed:26773386}. Host nucleus {ECO:0000269|PubMed:26773386}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.
DR  UNIPROT: P0C6V6;
DR  UNIPROT: Q91AV2;
DR  PDB: 5GWZ;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: The non-structural protein 1 (nsp1) protein plays a role in the inhibition of host interferon and pro-inflammatory cytokines production. Suppresses host RELA/p65 activation by blocking NFKBIA phosphorylation (PubMed:28715653). Targets also the RLR pathway downstream of the IRF3 activation by targeting host CREBBP to proteasomal degradation (PubMed:26773386). {ECO:0000269|PubMed:26773386, ECO:0000269|PubMed:28715653}. The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N- terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}. Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0030430;
GO  GO:0033644;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039644;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASNHVTLAFANDAEISAFGFCTASEAVSYYSEAAASGFMQCRFVSLDLADTVEGLLPEDYVMVVIGTTKLSAYVDTFGS
SQ  RPRNICGWLLFSNCNYFLEELELTFGRRGGNIVPVDQYMCGADGKPVLQESEWEYTDFFADSEDGQLNIAGITYVKAWIV
SQ  ERSDVSYASQNLTSIKSITYCSTYEHTFLDGTAMKVARTPKIKKNVVLSEPLATIYREIGSPFVDNGSDARSIIRRPVFL
SQ  HAFVKCKCGSYHWTVGDWTSYVSTCCGFKCKPVLVASCSAMPGSVVVTRAGAGTGVKYYNNMFLRHVADIDGLAFWRILK
SQ  VQSKDDLACSGKFLEHHEEGFTDPCYFLNDSSLATKLKFDILSGKFSDEVKQAIIAGHVVVGSALVDIVDDALGQPWFIR
SQ  KLGDLASAPWEQLKAVVRGLGLLSDEVVLFGKRLSCATLSIVNGVFEFLADVPEKLAAAVTVFVNFLNEFFESACDCLKV
SQ  GGKTFNKVGSYVLFDNALVKLVKAKARGPRQAGICEVRYTSLVVGSTTKVVSKRVENANVNLVVVDEDVTLNTTGRTVVV
SQ  DGLAFFESDGFYRHLADADVVIEHPVYKSACELKPVFECDPIPDFPLPVAASVAELCVQTDLLLKNYNTPYKTYSCVVRG
SQ  DKCCITCTLQFKAPSYVEDAVNFVDLCTKNIGTAGFHEFYITAHEQQDLQGFLTTCCTMSGFECFMPTIPQCPAVLEEID
SQ  GGSIWRSFITGLNTMWDFCKRLKVSFGLDGIVVTVARKFKRLGALLAEMYNTYLSTVVENLVLAGVSFKYYATSVPKIVL
SQ  GGCFHSVKSVFASVFQIPVQAGIEKFKVFLNCVHPVVPRVIETSFVELEETTFKPPALNGGIAIVDGFAFYYDGTLYYPT
SQ  DGNSVVPICFKKKGGGDVKFSDEVSVKTIDPVYKVSLEFEFESETIMAVLNKAVGNRIKVTGGWDDVVEYINVAIEVLKD
SQ  HVEVPKYYIYDEEGGTDPNLPVMVSQWPLNDDTISQDLLDVEVVTDAPIDSEGDEVDSSAPEKVADVANSEPGDDGLPVA
SQ  PETNVESEVEEVAATLSFIKDTPSTVTKDPFAFDFVSYGGLKVLRQSHNNCWVTSTLVQLQLLGIVDDPAMELFSAGRVG
SQ  PMVRKCYESQKAILGSLGDVSACLESLTKDLHTLKITCSVVCGCGTGERIYEGCAFRMTPTLEPFPYGACAQCAQVLMHT
SQ  FKSIVGTGIFCRDTTALSLDSLVVKPLCAAAFIGKDSGHYVTNFYDAAMAIDGYGRHQIKYDTLNTICVKDVNWTAPLVP
SQ  AVDSVVEPVVKPFYSYKNVDFYQGDFSDLVKLPCDFVVNAANEKLSHGGGIAKAIDVYTKGMLQKCSNDYIKAHGPIKVG
SQ  RGVMLEALGLKVFNVVGPRKGKHAPELLVKAYKSVFANSGVALTPLISVGIFSVPLEESLSAFLACVGDRHCKCFCYGDK
SQ  EREAIIKYMDGLVDAIFKEALVDTTPVQEDVQQVSQKPVLPNFEPFRIEGAHAFYECNPEGLMSLGADKLVLFTNSNLDF
SQ  CSVGKCLNDVTSGALLEAINVFKKSNKTVPAGNCVTLDCANMISITMVVLPFDGDANYDKNYARAVVKVSKLKGKLVLAV
SQ  DDATLYSKLSHLSVLGFVSTPDDVERFYANKSVVIKVTEDTRSVKAVKVESTATYGQQIGPCLVNDTVVTDNKPVVADVV
SQ  AKVVPNANWDSHYGFDKAGEFHMLDHTGFTFPSEVVNGRRVIKTTDNNCWVNVTCLQLQFARFRFKSAGLQAMWESYCTG
SQ  DVAMFVHWLYWLTGVDKGQPSDSENALNMLSKYIVPAGSVTIERVTHDGCCCSKRVVTAPVVNASVLKLGVEDGLCPHGL
SQ  NYIGKVVVVKGTTIVVNVGKPVVAPSHLFLKGVSYTTFLDNGNGVVGHYTVFDHGTGMVHDGDAFVPGDLNVSPVTNVVV
SQ  SEQTAVVIKDPVKKAELDATKLLDTMNYASERFFSFGDFMSRNLITVFLYILSILGLCFRAFRKRDVKVLAGVPQRTGII
SQ  LRKSMRYNAKALGVFFKLKLYWFKVLGKFSLGIYALYALLFMTIRFTPIGSPVCDDVVAGYANSSFDKNEYCNSVICKVC
SQ  LYGYQELSDFSHTQVVWQHLRDPLIGNVMPFFYLAFLAIFGGVYVKAITLYFIFQYLNSLGVFLGLQQSIWFLQLVPFDV
SQ  FGDEIVVFFIVTRVLMFIKHVCLGCDKASCVACSKSARLKRVPVQTIFQGTSKSFYVHANGGSKFCKKHNFFCLNCDSYG
SQ  PGCTFINDVIATEVGNVVKLNVQPTGPATILIDKVEFSNGFYYLYSGDTFWKYNFDITDSKYTCKEALKNCSIITDFIVF
SQ  NNNGSNVNQVKNACVYFSQMLCKPVKLVDSALLASLSVDFGASLHSAFVSVLSNSFGKDLSSCNDMQDCKSTLGFDDVPL
SQ  DTFNAAVAEAHRYDVLLTDMSFNNFTTSYAKPEEKFPVHDIATCMRVGAKIVNHNVLVKDSIPVVWLVRDFIALSEETRK
SQ  YIIRTTKVKGITFMLTFNDCRMHTTIPTVCIANKKGAGLPSFSKVKKFFWFLCLFIVAAFFALSFLDFSTQVSSDSDYDF
SQ  KYIESGQLKTFDNPLSCVHNVFINFDQWHDAKFGFTPVNNPSCPIVVGVSDEARTVPGIPAGVYLAGKTLVFAINTIFGT
SQ  SGLCFDASGVADKGACIFNSACTTLSGLGGTAVYCYKNGLVEGAKLYSELAPHSYYKMVDGNAVSLPEIISRGFGIRTIR
SQ  TKAMTYCRVGQCVQSAEGVCFGADRFFVYNAESGSDFVCGTGLFTLLMNVISVFSKTVPVTVLSGQILFNCIIAFVAVAV
SQ  CFLFTKFKRMFGDMSVGVFTVGACTLLNNVSYIVTQNTLGMLGYATLYFLCTKGVRYMWIWHLGFLISYILIAPWWVLMV
SQ  YAFSAIFEFMPNLFKLKVSTQLFEGDKFVGSFENAAAGTFVLDMHAYERLANSISTEKLRQYASTYNKYKYYSGSASEAD
SQ  YRLACFAHLAKAMMDYASNHNDTLYTPPTVSYNSTLQAGLRKMAQPSGVVEKCIVRVCYGNMALNGLWLGDIVMCPRHVI
SQ  ASSTTSTIDYDYALSVLRLHNFSISSGNVFLGVVSATMRGALLQIKVNQNNVHTPKYTYRTVRPGESFNILACYDGAAAG
SQ  VYGVNMRSNYTIRGSFINGACGSPGYNINNGTVEFCYLHQLELGSGCHVGSDLDGVMYGGYEDQPTLQVEGASSLFTENV
SQ  LAFLYAALINGSTWWLSSSRIAVDRFNEWAVHNGMTTVGNTDCFSILAAKTGVDVQRLLASIQSLHKNFGGKQILGHTSL
SQ  TDEFTTGEVVRQMYGVNLQGGYVSRACRNVLLVGSFLTFFWSELVSYTKFFWVNPGYVTPMFACLSLLSSLLMFTLKHKT
SQ  LFFQVFLIPALIVTSCINLAFDVEVYNYLAEHFDYHVSLMGFNAQGLVNIFVCFVVTILHGTYTWRFFNTPASSVTYVVA
SQ  LLTAAYNYFYASDILSCAMTLFASVTGNWFVGAVCYKVAVYMALRFPTFVAIFGDIKSVMFCYLVLGYFTCCFYGILYWF
SQ  NRFFKVSVGVYDYTVSAAEFKYMVANGLRAPTGTLDSLLLSAKLIGIGGERNIKISSVQSKLTDIKCSNVVLLGCLSSMN
SQ  VSANSTEWAYCVDLHNKINLCNDPEKAQEMLLALLAFFLSKNSAFGLDDLLESYFNDNSMLQSVASTYVGLPSYVIYENA
SQ  RQQYEDAVNNGSPPQLVKQLRHAMNVAKSEFDREASTQRKLDRMAEQAAAQMYKEARAVNRKSKVVSAMHSLLFGMLRRL
SQ  DMSSVDTILNLAKDGVVPLSVIPAVSATKLNIVTSDIDSYNRIQREGCVHYAGTIWNIIDIKDNDGKVVHVKEVTAQNAE
SQ  SLSWPLVLGCERIVKLQNNEIIPGKLKQRSIKAEGDGIVGEGKALYNNEGGRTFMYAFISDKPDLRVVKWEFDGGCNTIE
SQ  LEPPRKFLVDSPNGAQIKYLYFVRNLNTLRRGAVLGYIGATVRLQAGKQTEQAINSSLLTLCAFAVDPAKTYIDAVKSGH
SQ  KPVGNCVKMLANGSGNGQAVTNGVEASTNQDSYGGASVCLYCRAHVEHPSMDGFCRLKGKYVQVPLGTVDPIRFVLENDV
SQ  CKVCGCWLSNGCTCDRSIMQSTDMAYLNEYGALVQLD
//
ID  P0C6U8;
PN  Non-structural protein 11;
GN  1a;
OS  694009;
SL  Nucleus Position: SL-0382;
SL  Comments: [Non-structural protein 2]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endosome {ECO:0000250|UniProtKB:P0DTD1}. [Papain-like protease nsp3]: Host membrane {ECO:0000305}; Multi-pass membrane protein. Host cytoplasm {ECO:0000269|PubMed:23943763}. [Non-structural protein 4]: Host membrane; Multi- pass membrane protein. Host cytoplasm {ECO:0000269|PubMed:23943763}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles. {ECO:0000269|PubMed:21345958, ECO:0000269|PubMed:23943763}. [3C-like proteinase nsp5]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host Golgi apparatus {ECO:0000250|UniProtKB:P0DTD1}. [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:17532020}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
DR  UNIPROT: P0C6U8;
DR  UNIPROT: P59641;
DR  PDB: 1Q2W;
DR  PDB: 1QZ8;
DR  PDB: 1UJ1;
DR  PDB: 1UK2;
DR  PDB: 1UK3;
DR  PDB: 1UK4;
DR  PDB: 1UW7;
DR  PDB: 1WOF;
DR  PDB: 1YSY;
DR  PDB: 1Z1I;
DR  PDB: 1Z1J;
DR  PDB: 2A5A;
DR  PDB: 2A5I;
DR  PDB: 2A5K;
DR  PDB: 2ACF;
DR  PDB: 2AHM;
DR  PDB: 2ALV;
DR  PDB: 2AMD;
DR  PDB: 2AMQ;
DR  PDB: 2BX3;
DR  PDB: 2BX4;
DR  PDB: 2C3S;
DR  PDB: 2D2D;
DR  PDB: 2DUC;
DR  PDB: 2FAV;
DR  PDB: 2FE8;
DR  PDB: 2FYG;
DR  PDB: 2G9T;
DR  PDB: 2GA6;
DR  PDB: 2GDT;
DR  PDB: 2GRI;
DR  PDB: 2GT7;
DR  PDB: 2GT8;
DR  PDB: 2GTB;
DR  PDB: 2GX4;
DR  PDB: 2GZ7;
DR  PDB: 2GZ8;
DR  PDB: 2GZ9;
DR  PDB: 2H2Z;
DR  PDB: 2HOB;
DR  PDB: 2HSX;
DR  PDB: 2IDY;
DR  PDB: 2KAF;
DR  PDB: 2KQV;
DR  PDB: 2KQW;
DR  PDB: 2KYS;
DR  PDB: 2LIZ;
DR  PDB: 2OP9;
DR  PDB: 2PWX;
DR  PDB: 2W2G;
DR  PDB: 2WCT;
DR  PDB: 2Z3C;
DR  PDB: 2Z3D;
DR  PDB: 2Z3E;
DR  PDB: 2ZU4;
DR  PDB: 2ZU5;
DR  PDB: 3ATW;
DR  PDB: 3AVZ;
DR  PDB: 3AW0;
DR  PDB: 3AW1;
DR  PDB: 3E91;
DR  PDB: 3EA7;
DR  PDB: 3EA8;
DR  PDB: 3EA9;
DR  PDB: 3EAJ;
DR  PDB: 3EE7;
DR  PDB: 3F9E;
DR  PDB: 3F9F;
DR  PDB: 3F9G;
DR  PDB: 3F9H;
DR  PDB: 3FZD;
DR  PDB: 3IWM;
DR  PDB: 3M3S;
DR  PDB: 3M3T;
DR  PDB: 3M3V;
DR  PDB: 3MJ5;
DR  PDB: 3R24;
DR  PDB: 3SN8;
DR  PDB: 3SNA;
DR  PDB: 3SNB;
DR  PDB: 3SNC;
DR  PDB: 3SND;
DR  PDB: 3SNE;
DR  PDB: 3SZN;
DR  PDB: 3TIT;
DR  PDB: 3TIU;
DR  PDB: 3TNS;
DR  PDB: 3TNT;
DR  PDB: 3V3M;
DR  PDB: 3VB3;
DR  PDB: 3VB4;
DR  PDB: 3VB5;
DR  PDB: 3VB6;
DR  PDB: 3VB7;
DR  PDB: 4HI3;
DR  PDB: 4M0W;
DR  PDB: 4MDS;
DR  PDB: 4MM3;
DR  PDB: 4OVZ;
DR  PDB: 4OW0;
DR  PDB: 5F22;
DR  PDB: 5Y3E;
DR  PDB: 5Y3Q;
DR  PDB: 6LNY;
DR  PDB: 6LO0;
DR  PDB: 6NUR;
DR  PDB: 6NUS;
DR  PDB: 6W2A;
DR  PDB: 6XHL;
DR  PDB: 6XHN;
DR  PDB: 6XHO;
DR  PDB: 6Y7M;
DR  PDB: 6YXJ;
DR  PDB: 7DQZ;
DR  PDB: 7EO8;
DR  PDB: 7K0G;
DR  PDB: 7K0H;
DR  PDB: 7LFU;
DR  PDB: 7LFV;
DR  PDB: 7LMG;
DR  PDB: 7LMH;
DR  PDB: 7LMI;
DR  PDB: 7LMJ;
DR  PDB: 7OPL;
DR  PDB: 7RC1;
DR  PDB: 7VLO;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF12379;
DR  Pfam: PF12124;
DR  Pfam: PF11633;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DR  PROSITE: PS51940;
DE  Function: [Isoform Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}. [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371). {ECO:0000269|PubMed:23035226, ECO:0000269|PubMed:30943371}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (PubMed:19640993). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (PubMed:19640993). {ECO:0000269|PubMed:19640993}. [Papain-like protease nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069, PubMed:23943763). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840). {ECO:0000269|PubMed:16271890, ECO:0000269|PubMed:17692280, ECO:0000269|PubMed:19369340, ECO:0000269|PubMed:23943763, ECO:0000269|PubMed:24622840, ECO:0000303|PubMed:24410069}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763, PubMed:24410069). Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). {ECO:0000269|PubMed:23943763, ECO:0000303|PubMed:24410069}. [3C-like proteinase nsp5]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH. {ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:16226257}. [Non-structural protein 6]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (PubMed:24991833). {ECO:0000269|PubMed:23943763, ECO:0000269|PubMed:24991833, ECO:0000303|PubMed:24410069}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000269|PubMed:22039154}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000269|PubMed:22039154}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000269|PubMed:19153232}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000269|PubMed:22635272}.
DE  Reference Proteome: Yes;
DE  Interaction: P62753; IntAct: EBI-15811015; Score: 0.40
DE  Interaction: P0C6X7; IntAct: EBI-25492630; Score: 0.51
DE  Interaction: P59637; IntAct: EBI-25492828; Score: 0.37
DE  Interaction: P0C6U8; IntAct: EBI-25610728; Score: 0.72
DE  Interaction: Q53GL7; IntAct: EBI-25619173; Score: 0.44
DE  Interaction: L5LC70; IntAct: EBI-25760958; Score: 0.62
DE  Interaction: P05161; IntAct: EBI-25760974; Score: 0.72
DE  Interaction: P62992; IntAct: EBI-25775419; Score: 0.56
DE  Interaction: R9QB93; IntAct: EBI-25821194; Score: 0.44
DE  Interaction: Q64339; IntAct: EBI-25821352; Score: 0.62
DE  Interaction: A0A5N4DAX7; IntAct: EBI-25821415; Score: 0.44
DE  Interaction: Q9GKP4; IntAct: EBI-25821587; Score: 0.56
DE  Interaction: Q9C0D3; IntAct: EBI-26376963; Score: 0.35
DE  Interaction: Q92624; IntAct: EBI-26376963; Score: 0.35
DE  Interaction: Q9H074; IntAct: EBI-26970949; Score: 0.68
DE  Interaction: P11940; IntAct: EBI-26971142; Score: 0.50
DE  Interaction: P15311; IntAct: EBI-30809805; Score: 0.40
DE  Interaction: Q8IZU9; IntAct: EBI-30809847; Score: 0.40
DE  Interaction: Q13283; IntAct: EBI-30810106; Score: 0.40
DE  Interaction: Q9UN86; IntAct: EBI-30810451; Score: 0.40
DE  Interaction: Q9BXW4; IntAct: EBI-30810678; Score: 0.40
DE  Interaction: Q00987; IntAct: EBI-30810755; Score: 0.40
GO  GO:0039714;
GO  GO:0062243;
GO  GO:0030430;
GO  GO:0044165;
GO  GO:0044174;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003725;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0019785;
GO  GO:0016829;
GO  GO:0008242;
GO  GO:0046983;
GO  GO:0003968;
GO  GO:0003727;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039519;
GO  GO:0039648;
GO  GO:0039690;
GO  GO:0016540;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039722;
GO  GO:0039547;
GO  GO:0039604;
GO  GO:0039501;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
GO  GO:0039694;
GO  GO:0019083;
TP  Membrane Topology: Transmembrane; Source: UniProt - Curator Inference {ECO:0000305|PubMed:18842706};
SQ  MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTN
SQ  HGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELGTDPIEDYEQN
SQ  WNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAW
SQ  FTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVASPQECNNMHLSTL
SQ  MKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKG
SQ  GRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFHLNEEVAIILASF
SQ  SASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIP
SQ  DLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAYVTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVE
SQ  FLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQC
SQ  IRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYC
SQ  ALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAV
SQ  VKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGL
SQ  PLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAAN
SQ  IHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQD
SQ  ILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQK
SQ  PVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSK
SQ  KAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEE
SQ  TRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAAR
SQ  CMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVE
SQ  FHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPS
SQ  DDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRAR
SQ  AGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGV
SQ  SIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPV
SQ  TDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQ
SQ  MTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSN
SQ  SFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENT
SQ  SITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFT
SQ  KSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYC
SQ  NGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGL
SQ  SAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVEC
SQ  TTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHL
SQ  YFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDS
SQ  TEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDL
SQ  EVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLT
SQ  CATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIIST
SQ  DDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLI
SQ  EYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEY
SQ  CRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYY
SQ  FMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAI
SQ  YVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDT
SQ  TSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPR
SQ  HVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNG
SQ  SPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTI
SQ  TLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRT
SQ  ILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAA
SQ  CAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDD
SQ  AARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVY
SQ  CFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMS
SQ  DVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINRLCEEMLDNRATLQA
SQ  IASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRA
SQ  KVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVD
SQ  ADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLA
SQ  LLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPAN
SQ  STVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFC
SQ  DLKGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPLMQSADASTFLNGFAV
//
ID  P0DTC1;
PN  Non-structural protein 11;
GN  R1A;
OS  2697049;
SL  Nucleus Position: SL-0382;
SL  Comments: [Host translation inhibitor nsp1]: Host cytoplasm {ECO:0000269|PubMed:33060197}. [Non-structural protein 2]: Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endosome {ECO:0000269|PubMed:33060197}. [Papain-like protease nsp3]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 4]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase nsp5]: Host cytoplasm {ECO:0000269|PubMed:33060197}. Host Golgi apparatus {ECO:0000269|PubMed:33060197}. [Non-structural protein 6]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:33080218}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:33080218}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}.
DR  UNIPROT: P0DTC1;
DR  PDB: 6Y2E;
DR  PDB: 6Y2F;
DR  PDB: 6Y2G;
DR  PDB: 6YHU;
DR  PDB: 6YYT;
DR  PDB: 7BV2;
DR  PDB: 7C33;
DR  PDB: 7CZ4;
DR  PDB: 7D3I;
DR  PDB: 7D47;
DR  PDB: 7D64;
DR  PDB: 7D6H;
DR  PDB: 7DAT;
DR  PDB: 7DAU;
DR  PDB: 7DAV;
DR  PDB: 7DCD;
DR  PDB: 7DGB;
DR  PDB: 7DGF;
DR  PDB: 7DGG;
DR  PDB: 7DGH;
DR  PDB: 7DGI;
DR  PDB: 7DHJ;
DR  PDB: 7DJR;
DR  PDB: 7DK1;
DR  PDB: 7DPP;
DR  PDB: 7DPU;
DR  PDB: 7DPV;
DR  PDB: 7E35;
DR  PDB: 7EIN;
DR  PDB: 7EIZ;
DR  PDB: 7EXM;
DR  PDB: 7FAY;
DR  PDB: 7FAZ;
DR  PDB: 7JIR;
DR  PDB: 7JIT;
DR  PDB: 7JIV;
DR  PDB: 7JIW;
DR  PDB: 7JN2;
DR  PDB: 7JRN;
DR  PDB: 7KOJ;
DR  PDB: 7KOK;
DR  PDB: 7KOL;
DR  PDB: 7KRX;
DR  PDB: 7M1Y;
DR  PDB: 7NT1;
DR  PDB: 7NT2;
DR  PDB: 7NT3;
DR  PDB: 7NTQ;
DR  PDB: 7NTT;
DR  PDB: 7NTV;
DR  PDB: 7NTW;
DR  PDB: 7NUK;
DR  PDB: 7NW2;
DR  PDB: 7NWX;
DR  PDB: 7NXH;
DR  PDB: 7OFS;
DR  PDB: 7OFT;
DR  PDB: 7OFU;
DR  PDB: 7P51;
DR  PDB: 7QCG;
DR  PDB: 7QCH;
DR  PDB: 7QCI;
DR  PDB: 7QCJ;
DR  PDB: 7QCK;
DR  PDB: 7QCM;
DR  PDB: 7RBR;
DR  PDB: 7RBS;
DR  PDB: 7RZC;
DR  PDB: 7SDR;
DR  PDB: 7SGU;
DR  PDB: 7SGV;
DR  PDB: 7SGW;
DR  PDB: 7SQE;
DR  PDB: 7TLL;
DR  PDB: 7TOB;
DR  PDB: 7TVS;
DR  PDB: 7TVX;
DR  PDB: 7TZJ;
DR  PDB: 7U28;
DR  PDB: 7U29;
DR  PDB: 7VFA;
DR  PDB: 7VFB;
DR  PDB: 7VH8;
DR  PDB: 7VIC;
DR  PDB: 7VJW;
DR  PDB: 7VJX;
DR  PDB: 7VJY;
DR  PDB: 7VJZ;
DR  PDB: 7VK0;
DR  PDB: 7VK1;
DR  PDB: 7VK2;
DR  PDB: 7VK3;
DR  PDB: 7VK4;
DR  PDB: 7VK5;
DR  PDB: 7VK6;
DR  PDB: 7VK7;
DR  PDB: 7VK8;
DR  PDB: 7VLP;
DR  PDB: 7VLQ;
DR  PDB: 7VTH;
DR  PDB: 7VU6;
DR  PDB: 7VVT;
DR  PDB: 7WO1;
DR  PDB: 7WO3;
DR  PDB: 7WOF;
DR  Pfam: PF16251;
DR  Pfam: PF11501;
DR  Pfam: PF12379;
DR  Pfam: PF12124;
DR  Pfam: PF11633;
DR  Pfam: PF09401;
DR  Pfam: PF19212;
DR  Pfam: PF19211;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF05409;
DR  PROSITE: PS51963;
DR  PROSITE: PS51942;
DR  PROSITE: PS51941;
DR  PROSITE: PS51994;
DR  PROSITE: PS51945;
DR  PROSITE: PS51952;
DR  PROSITE: PS51962;
DR  PROSITE: PS51991;
DR  PROSITE: PS51990;
DR  PROSITE: PS51989;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS00867;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DR  PROSITE: PS51940;
DE  Function: [Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000250|UniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Inhibits host translation by associating with the open head conformation of the 40S subunit (PubMed:33479166, PubMed:33080218, PubMed:32680882, PubMed:32908316). The C-terminus binds to and obstructs ribosomal mRNA entry tunnel (PubMed:33479166, PubMed:33080218, PubMed:32680882, PubMed:32908316). Thereby inhibits antiviral response triggered by innate immunity or interferons (PubMed:33080218, PubMed:32680882, PubMed:32979938). The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation (By similarity). Viral mRNAs less susceptible to nsp1-mediated inhibition of translation, because of their 5'-end leader sequence (PubMed:32908316, PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32680882, ECO:0000269|PubMed:32908316, ECO:0000269|PubMed:32979938, ECO:0000269|PubMed:33080218, ECO:0000269|PubMed:33479166}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}. [Papain-like protease nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication (By similarity). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:32733001). Prevents also host NF- kappa-B signaling (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:32726803). Cleaves preferentially ISG15 from antiviral protein IFIH1 (MDA5), but not DDX58 (RIG-I) (PubMed:33727702). Can play a role in host ADP-ribosylation by ADP-ribose (PubMed:32578982). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32578982, ECO:0000269|PubMed:32726803, ECO:0000269|PubMed:32733001, ECO:0000269|PubMed:33727702}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}. [3C-like proteinase nsp5]: Cleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481). Also able to bind an ADP-ribose- 1''-phosphate (ADRP) (By similarity) (PubMed:32198291, PubMed:32272481). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481, ECO:0000269|PubMed:32321856}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic (By similarity). Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (By similarity). Binds to host TBK1 without affecting TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32979938}. [Non-structural protein 7]: Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}. [Non-structural protein 8]: Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity). Interacts with ribosome signal recognition particle RNA (SRP) (PubMed:33080218). Together with NSP9, suppress protein integration into the cell membrane, thereby disrupting host immune defenses (PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33080218}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein (By similarity). Interacts with ribosome signal recognition particle RNA (SRP) (PubMed:33080218). Together with NSP9, suppress protein integration into the cell membrane, thereby disrupting host immune defenses (PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:33080218}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}.
DE  Reference Proteome: Yes;
DE  Interaction: O75347; IntAct: EBI-25490682; Score: 0.59
DE  Interaction: Q9UM54; IntAct: EBI-25509753; Score: 0.35
DE  Interaction: O43795; IntAct: EBI-25509753; Score: 0.35
DE  Interaction: P61158; IntAct: EBI-25509753; Score: 0.35
DE  Interaction: P24468; IntAct: EBI-25762295; Score: 0.35
DE  Interaction: Q14165; IntAct: EBI-25762295; Score: 0.35
DE  Interaction: P56270; IntAct: EBI-25762295; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-25762295; Score: 0.35
DE  Interaction: P85037; IntAct: EBI-25762295; Score: 0.35
DE  Interaction: Q5VV42; IntAct: EBI-25762295; Score: 0.35
DE  Interaction: Q8N4V1; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q9P0T4; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q9BQB6; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: P57088; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q99805; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q9BVV7; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: O15260; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q8TCJ2; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q92504; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: P62979; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q99942; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q96AA3; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: P78527; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q8NC67; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q9H0U3; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: P36776; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q96MM7; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: P30459; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q15011; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q7L5D6; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: O94905; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: O75477; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: P39656; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q9ULG6; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: O95816; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: Q53GL7; IntAct: EBI-26365343; Score: 0.44
DE  Interaction: Q9H074; IntAct: EBI-26971191; Score: 0.37
DE  Interaction: O95155; IntAct: EBI-27126133; Score: 0.40
DE  Interaction: Q16533; IntAct: EBI-27128066; Score: 0.27
DE  Interaction: P15311; IntAct: EBI-30809820; Score: 0.40
DE  Interaction: Q8IZU9; IntAct: EBI-30809884; Score: 0.40
DE  Interaction: Q13283; IntAct: EBI-30810056; Score: 0.40
DE  Interaction: Q9UN86; IntAct: EBI-30810408; Score: 0.40
DE  Interaction: Q9BXW4; IntAct: EBI-30810710; Score: 0.40
DE  Interaction: Q00987; IntAct: EBI-30810740; Score: 0.40
GO  GO:0039714;
GO  GO:0062243;
GO  GO:0030430;
GO  GO:0044165;
GO  GO:0044174;
GO  GO:0044177;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008234;
GO  GO:0004519;
GO  GO:0002151;
GO  GO:0042802;
GO  GO:0019785;
GO  GO:0008242;
GO  GO:0046983;
GO  GO:0042803;
GO  GO:0003727;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039595;
GO  GO:0039520;
GO  GO:0039519;
GO  GO:0039648;
GO  GO:0039690;
GO  GO:0016540;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0006508;
GO  GO:0039657;
GO  GO:0039579;
GO  GO:0039644;
GO  GO:0039722;
GO  GO:0039547;
GO  GO:0039604;
GO  GO:0039501;
GO  GO:0039502;
GO  GO:0039548;
GO  GO:0019079;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAP
SQ  HGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQEN
SQ  WNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAW
SQ  YTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTL
SQ  MKCDHCGETSWQTGDFVKATCEFCGTENLTKEGATTCGYLPQNAVVKIYCPACHNSEVGPEHSLAEYHNESGLKTILRKG
SQ  GRTIAFGGCVFSYVGCHNKCAYWVPRASANIGCNHTGVVGEGSEGLNDNLLEILQKEKVNINIVGDFKLNEEIAIILASF
SQ  SASTSAFVETVKGLDYKAFKQIVESCGNFKVTKGKAKKGAWNIGEQKSILSPLYAFASEAARVVRSIFSRTLETAQNSVR
SQ  VLQKAAITILDGISQYSLRLIDAMMFTSDLATNNLVVMAYITGGVVQLTSQWLTNIFGTVYEKLKPVLDWLEEKFKEGVE
SQ  FLRDGWEIVKFISTCACEIVGGQIVTCAKEIKESVQTFFKLVNKFLALCADSIIIGGAKLKALNLGETFVTHSKGLYRKC
SQ  VKSREETGLLMPLKAPKEIIFLEGETLPTEVLTEEVVLKTGDLQPLEQPTSEAVEAPLVGTPVCINGLMLLEIKDTEKYC
SQ  ALAPNMMVTNNTFTLKGGAPTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVI
SQ  KTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPL
SQ  EFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYI
SQ  KNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGP
SQ  NVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVE
SQ  QKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLK
SQ  KDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSII
SQ  SNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLND
SQ  LNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQS
SQ  TQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLD
SQ  GADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATAL
SQ  LTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQT
SQ  TLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHIT
SQ  SKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPY
SQ  PNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNK
SQ  ATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPA
SQ  NNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRC
SQ  LNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCL
SQ  GSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTA
SQ  FGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHV
SQ  VDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRP
SQ  INPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVY
SQ  YSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQG
SQ  FVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMS
SQ  LSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHT
SQ  DFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGD
SQ  FLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGS
SQ  IIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGA
SQ  LDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDV
SQ  SFLAHIQWMVMFTPLVPFWITIAYIICISTKHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLP
SQ  LTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCM
SQ  VQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPK
SQ  TPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDL
SQ  EGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQT
SQ  GIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQSAVKRTIKGTHHWLLLTILTSLLVLVQSTQW
SQ  SLFFFLYENAFLPFAMGIIAMSAFAMMFVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLDMVDTSLSGFKLK
SQ  DCVMYASAVVLLILMTARTVYDDGARRVWTLMNVLTLVYKVYYGNALDQAISMWALIISVTSNYSGVVTTVMFLARGIVF
SQ  MCVEYCPIFFITGNTLQCIMLVYCFLGYFCTCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKNSIDAFKL
SQ  NIKLLGVGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLS
SQ  MQGAVDINKLCEEMLDNRATLQAIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRK
SQ  LEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVIPDYNTY
SQ  KNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQ
SQ  TACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRG
SQ  MVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQES
SQ  FGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQSADAQSFL
SQ  NGFAV
//
ID  Q8R2J9;
PN  DNA repair protein RAD51 homolog 3;
GN  RAD51C;
OS  10029;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43502}. Cytoplasm {ECO:0000250|UniProtKB:O43502}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43502}. Mitochondrion {ECO:0000250|UniProtKB:O43502}. Note=DNA damage induces an increase in nuclear levels. Accumulates in DNA damage induced nuclear foci or RAD51C foci which is formed during the S or G2 phase of cell cycle. Accumulation at DNA lesions requires the presence of NBN/NBS1, ATM and RPA. {ECO:0000250|UniProtKB:O43502}.
DR  UNIPROT: Q8R2J9;
DR  UNIPROT: Q8VDE9;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DE  Function: Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD51 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1- BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single- stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA- dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross- link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis. {ECO:0000269|PubMed:11912211, ECO:0000269|PubMed:12000837, ECO:0000269|PubMed:17268176, ECO:0000269|PubMed:20471405}.
DE  Reference Proteome: No;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048476;
GO  GO:0005739;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0033063;
GO  GO:0033065;
GO  GO:0005657;
GO  GO:0005524;
GO  GO:0140664;
GO  GO:0008821;
GO  GO:0000400;
GO  GO:0006310;
GO  GO:0006281;
GO  GO:0000724;
GO  GO:0007066;
GO  GO:0007141;
GO  GO:0010971;
GO  GO:0007131;
GO  GO:0007062;
GO  GO:0007283;
GO  GO:0000722;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQRELVSFPLSPTVRVKLVAAGFQTAEDVLGVKPSELSKEVGISKEEALETLQIVRRESLTDKPRCAGASVAGKKYTALE
SQ  LLEQEHTQGFIITFCSALDNILGGGIPLMKTTEVCGVPGVGKTQLCMQLAVDVQIPECFGGVAGEAVFIDTEGSFMVDRV
SQ  VTLANACIQHLHLIAGTHKDEEHQKALEGFTLENILSHIYYFRCHDYTELLAQVYLLPDFLSNHSKVQLVIIDGIALPFR
SQ  HDLDDLSLRTRLLNGLAQQMISLANNHRLAVILTNQMTTKIDKNQALLVPALGESWGHAATIRLIFHWEQKQRFATLYKS
SQ  PSQKESTIPFQITPQGFRDAAVTASSSQTEGSSNLRKRSREPEEGC
//
ID  O43502;
PN  DNA repair protein RAD51 homolog 3;
GN  RAD51C;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:12966089, ECO:0000269|PubMed:16215984}. Cytoplasm {ECO:0000269|PubMed:16215984}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16215984}. Mitochondrion {ECO:0000269|PubMed:20413593}. Note=DNA damage induces an increase in nuclear levels. Accumulates in DNA damage induced nuclear foci or RAD51C foci which is formed during the S or G2 phase of cell cycle. Accumulation at DNA lesions requires the presence of NBN/NBS1, ATM and RPA.
DR  UNIPROT: O43502;
DR  UNIPROT: O43503;
DR  UNIPROT: Q3B783;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DR  OMIM: 602774;
DR  OMIM: 613390;
DR  OMIM: 613399;
DR  DisGeNET: 5889;
DE  Function: Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD51 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1- BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single- stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA- dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross- link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis. {ECO:0000269|PubMed:14716019, ECO:0000269|PubMed:16215984, ECO:0000269|PubMed:16395335, ECO:0000269|PubMed:19451272, ECO:0000269|PubMed:19783859, ECO:0000269|PubMed:20413593, ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.
DE  Disease: Fanconi anemia complementation group O (FANCO) [MIM:613390]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:20400963, ECO:0000269|PubMed:24141787}. Note=The disease is caused by variants affecting the gene represented in this entry. Breast-ovarian cancer, familial, 3 (BROVCA3) [MIM:613399]: A condition associated with familial predisposition to cancer of the breast and ovaries. Characteristic features in affected families are an early age of onset of breast cancer (often before age 50), increased chance of bilateral cancers (cancer that develop in both breasts, or both ovaries, independently), frequent occurrence of breast cancer among men, increased incidence of tumors of other specific organs, such as the prostate. {ECO:0000269|PubMed:20400964, ECO:0000269|PubMed:21990120, ECO:0000269|PubMed:24141787}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q06609; IntAct: EBI-7988560; Score: 0.66
DE  Interaction: Q8IZS8; IntAct: EBI-1076952; Score: 0.00
DE  Interaction: O00571; IntAct: EBI-1082433; Score: 0.00
DE  Interaction: Q86YZ3; IntAct: EBI-1084572; Score: 0.00
DE  Interaction: Q6NVH7; IntAct: EBI-5282255; Score: 0.52
DE  Interaction: Q86YC2; IntAct: EBI-9118380; Score: 0.61
DE  Interaction: P51587; IntAct: EBI-9118380; Score: 0.53
DE  Interaction: O43542; IntAct: EBI-9119744; Score: 0.94
DE  Interaction: O15315; IntAct: EBI-9118355; Score: 0.91
DE  Interaction: O75771; IntAct: EBI-9118355; Score: 0.77
DE  Interaction: O43543; IntAct: EBI-9118355; Score: 0.67
DE  Interaction: Q9NZD8; IntAct: EBI-24621755; Score: 0.56
DE  Interaction: Q8TBP5; IntAct: EBI-21502646; Score: 0.35
DE  Interaction: Q9UK85; IntAct: EBI-21531225; Score: 0.35
DE  Interaction: Q15768; IntAct: EBI-21537920; Score: 0.35
DE  Interaction: O75173; IntAct: EBI-21640424; Score: 0.35
DE  Interaction: Q9HBV2; IntAct: EBI-21670400; Score: 0.35
DE  Interaction: Q5T8I9; IntAct: EBI-21755295; Score: 0.35
DE  Interaction: Q6JEL2; IntAct: EBI-21868932; Score: 0.35
DE  Interaction: Q96MF4; IntAct: EBI-21868932; Score: 0.35
DE  Interaction: P43378; IntAct: EBI-21868932; Score: 0.35
DE  Interaction: Q8TDG4; IntAct: EBI-16072514; Score: 0.50
DE  Interaction: Q9UMX1; IntAct: EBI-30826134; Score: 0.44
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0005739;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0033063;
GO  GO:0033065;
GO  GO:0005657;
GO  GO:0005524;
GO  GO:0140664;
GO  GO:0008821;
GO  GO:0003677;
GO  GO:0006310;
GO  GO:0006281;
GO  GO:0000724;
GO  GO:0007066;
GO  GO:0007141;
GO  GO:0000707;
GO  GO:0010971;
GO  GO:0007131;
GO  GO:0007062;
GO  GO:0007283;
GO  GO:0000722;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRGKTFRFEMQRDLVSFPLSPAVRVKLVSAGFQTAEELLEVKPSELSKEVGISKAEALETLQIIRRECLTNKPRYAGTSE
SQ  SHKKCTALELLEQEHTQGFIITFCSALDDILGGGVPLMKTTEICGAPGVGKTQLCMQLAVDVQIPECFGGVAGEAVFIDT
SQ  EGSFMVDRVVDLATACIQHLQLIAEKHKGEEHRKALEDFTLDNILSHIYYFRCRDYTELLAQVYLLPDFLSEHSKVRLVI
SQ  VDGIAFPFRHDLDDLSLRTRLLNGLAQQMISLANNHRLAVILTNQMTTKIDRNQALLVPALGESWGHAATIRLIFHWDRK
SQ  QRLATLYKSPSQKECTVLFQIKPQGFRDTVVTSACSLQTEGSLSTRKRSRDPEEEL
//
ID  Q924H5;
PN  DNA repair protein RAD51 homolog 3;
GN  Rad51c;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43502}. Cytoplasm {ECO:0000250|UniProtKB:O43502}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43502}. Mitochondrion {ECO:0000250|UniProtKB:O43502}. Note=DNA damage induces an increase in nuclear levels. Accumulates in DNA damage induced nuclear foci or RAD51C foci which is formed during the S or G2 phase of cell cycle. Accumulation at DNA lesions requires the presence of NBN/NBS1, ATM and RPA. {ECO:0000250|UniProtKB:O43502}.
DR  UNIPROT: Q924H5;
DR  UNIPROT: B2KGK7;
DR  UNIPROT: Q5SX32;
DR  UNIPROT: Q8C653;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DE  Function: Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD51 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1- BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single- stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA- dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross- link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis. {ECO:0000269|PubMed:20471405}.
DE  Reference Proteome: Yes;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048476;
GO  GO:0043231;
GO  GO:0005739;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0033063;
GO  GO:0033065;
GO  GO:0005657;
GO  GO:0005524;
GO  GO:0140664;
GO  GO:0008821;
GO  GO:0000400;
GO  GO:0006310;
GO  GO:0006281;
GO  GO:0000724;
GO  GO:0007066;
GO  GO:0007141;
GO  GO:0000707;
GO  GO:0010971;
GO  GO:0007131;
GO  GO:0007283;
GO  GO:0000722;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQRELVGYPLSPAVRGKLVAAGFQTAEDVLEVKPSELSKEVGISKEEALETLQILRRECLTNKPRCAGTSVANEKCTALE
SQ  LLEQEHTQGFIITFCSALDNILGGGIPLMKTTEVCGVPGVGKTQLCMQLAVDVQIPECFGGVAGEAVFIDTEGSFMVDRV
SQ  VSLATACIQHLHLIAGTHTEEEHQKALKDFTLENILSHIYYFRCHDYTELLAQVYLLPDFLSDHPKVQLVIIDGIAFPFR
SQ  HDLEDLSLRTRLLNGLAQQMISLANNHRLAVILTNQMTTKIDKNQALLVPALGESWGHAATIRLIFHWEQKQRFATLYKS
SQ  PSQKESTIPFQITPQGFRDAVVTAASSQTESSLNFRKRSREPEEEC
//
ID  Q5ZIT5;
PN  Ras-related protein Rab-10;
GN  RAB10;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic vesicle membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}. Endosome membrane {ECO:0000250|UniProtKB:P61026}. Recycling endosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P24409}. Cell projection, cilium {ECO:0000250|UniProtKB:P61027}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61027}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P61027}. Note=Associates with SLC2A4/GLUT4 storage vesicles (By similarity). Localizes to the base of the cilium (By similarity). Transiently associates with phagosomes (By similarity). Localizes to the endoplasmic reticulum at domains of new tubule growth (By similarity). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61026, ECO:0000250|UniProtKB:P61027}.
DR  UNIPROT: Q5ZIT5;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Also plays a specific role in asymmetric protein transport to the plasma membrane within the polarized neuron and epithelial cells. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane while in epithelial cells, it regulates transport from the Golgi to the basolateral membrane. Moreover, may play a role in the basolateral recycling pathway and in phagosome maturation. Finally, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (By similarity). {ECO:0000250|UniProtKB:P61026, ECO:0000250|UniProtKB:P61027}.
DE  Reference Proteome: Yes;
GO  GO:0005929;
GO  GO:0005789;
GO  GO:0071782;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0032593;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0030670;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0055038;
GO  GO:0008021;
GO  GO:0005802;
GO  GO:0003925;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0031489;
GO  GO:0007409;
GO  GO:0032869;
GO  GO:0071786;
GO  GO:0016197;
GO  GO:0045200;
GO  GO:0097051;
GO  GO:0043001;
GO  GO:0006893;
GO  GO:0030859;
GO  GO:1903361;
GO  GO:0072659;
GO  GO:0009306;
GO  GO:0017157;
GO  GO:0006904;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDLKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYR
SQ  GAMGIMLVYDITNAKSFENISKWLRNIDEHANEDVERMLLGNKCDMEDKRVVPKAKGEQIAREHGIRFFETSAKANINIE
SQ  KAFLTLAEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC
//
ID  P61026;
PN  Ras-related protein Rab-10;
GN  RAB10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic vesicle membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:23263280}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}. Endosome membrane {ECO:0000269|PubMed:16641372}. Recycling endosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:30398148}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23263280}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:29212815}. Note=Associates with SLC2A4/GLUT4 storage vesicles (PubMed:22908308). Localizes to the base of the cilium when phosphorylated by LRRK2 on Thr-73 (PubMed:20576682, PubMed:30398148). Transiently associates with phagosomes (By similarity). Localizes to the endoplasmic reticulum at domains of new tubule growth (PubMed:23263280). {ECO:0000250|UniProtKB:P24409, ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:22908308, ECO:0000269|PubMed:23263280, ECO:0000269|PubMed:30398148}.
DR  UNIPROT: P61026;
DR  UNIPROT: D6W538;
DR  UNIPROT: O88386;
DR  UNIPROT: Q6IA52;
DR  UNIPROT: Q9D7X6;
DR  UNIPROT: Q9H0T3;
DR  PDB: 5LPN;
DR  PDB: 5SZJ;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DR  OMIM: 612672;
DR  DisGeNET: 10890;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:21248164). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:21248164). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane (PubMed:21248164). Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane (By similarity). In parallel, it regulates the transport of TLR4, a toll- like receptor to the plasma membrane and therefore may be important for innate immune response (By similarity). Also plays a specific role in asymmetric protein transport to the plasma membrane (PubMed:16641372). In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane (By similarity). In epithelial cells, it regulates transport from the Golgi to the basolateral membrane (PubMed:16641372). May play a role in the basolateral recycling pathway and in phagosome maturation (By similarity). May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (PubMed:23263280). Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis (PubMed:30398148). When phosphorylated by LRRK2 on Thr-73, binds RILPL1 and inhibits ciliogenesis (PubMed:30398148). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61027, ECO:0000269|PubMed:16641372, ECO:0000269|PubMed:21248164, ECO:0000269|PubMed:23263280, ECO:0000269|PubMed:30398148}. (Microbial infection) Upon Legionella pneumophila infection promotes endoplasmic reticulum recruitment and bacterial replication. Plays a role in remodeling the Legionella-containing vacuole (LCV) into an endoplasmic reticulum-like vacuole. {ECO:0000269|PubMed:31540829}.
DE  Reference Proteome: Yes;
DE  Interaction: O60271; IntAct: EBI-25436875; Score: 0.40
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P0DTD1; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: Q9HC74; IntAct: EBI-737213; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-1062133; Score: 0.00
DE  Interaction: P61966; IntAct: EBI-1064543; Score: 0.00
DE  Interaction: P61006; IntAct: EBI-1069273; Score: 0.00
DE  Interaction: O60496; IntAct: EBI-1078210; Score: 0.00
DE  Interaction: Q9H3U5; IntAct: EBI-1080105; Score: 0.00
DE  Interaction: O14965; IntAct: EBI-1085734; Score: 0.00
DE  Interaction: P11171; IntAct: EBI-1086219; Score: 0.00
DE  Interaction: P48039; IntAct: EBI-1188258; Score: 0.53
DE  Interaction: Q5NFA1; IntAct: EBI-2801878; Score: 0.00
DE  Interaction: Q9UHY7; IntAct: EBI-7330812; Score: 0.37
DE  Interaction: O95758; IntAct: EBI-7850130; Score: 0.35
DE  Interaction: B9VXK6; IntAct: EBI-6156496; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6191076; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: A0A8C0N5P9; IntAct: EBI-6466462; Score: 0.27
DE  Interaction: Q8N3F8; IntAct: EBI-8783637; Score: 0.37
DE  Interaction: Q96CV9; IntAct: EBI-10218281; Score: 0.56
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: P31150; IntAct: EBI-11035437; Score: 0.64
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q8N4P2; IntAct: EBI-12452567; Score: 0.51
DE  Interaction: Q5S007; IntAct: EBI-11820434; Score: 0.69
DE  Interaction: Q5EBL4; IntAct: EBI-11828480; Score: 0.53
DE  Interaction: P24386; IntAct: EBI-11828480; Score: 0.35
DE  Interaction: P47224; IntAct: EBI-11828480; Score: 0.35
DE  Interaction: P26374; IntAct: EBI-11828480; Score: 0.35
DE  Interaction: Q15286; IntAct: EBI-11828480; Score: 0.35
DE  Interaction: Q14964; IntAct: EBI-11828480; Score: 0.56
DE  Interaction: A4D1S5; IntAct: EBI-11828480; Score: 0.35
DE  Interaction: P50395; IntAct: EBI-11828480; Score: 0.35
DE  Interaction: Q7RTP6; IntAct: EBI-11828480; Score: 0.35
DE  Interaction: Q9H0N0; IntAct: EBI-11828480; Score: 0.35
DE  Interaction: Q6IQ22; IntAct: EBI-11829558; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: P31040; IntAct: EBI-20306992; Score: 0.35
DE  Interaction: Q9H082; IntAct: EBI-20906656; Score: 0.40
DE  Interaction: Q96CM3; IntAct: EBI-20934644; Score: 0.40
DE  Interaction: Q9H944; IntAct: EBI-25472954; Score: 0.35
DE  Interaction: Q969X0; IntAct: EBI-21006706; Score: 0.56
DE  Interaction: P54852; IntAct: EBI-21194717; Score: 0.45
DE  Interaction: P05067; IntAct: EBI-21132308; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q8N6Q3; IntAct: EBI-21402192; Score: 0.35
DE  Interaction: P97573; IntAct: EBI-22240534; Score: 0.35
DE  Interaction: D3ZEY4; IntAct: EBI-22240534; Score: 0.35
DE  Interaction: Q400C7; IntAct: EBI-22240534; Score: 0.35
DE  Interaction: Q9ULR3; IntAct: EBI-22223427; Score: 0.43
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9UPT6; IntAct: EBI-25437687; Score: 0.40
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: Q8NHP6; IntAct: EBI-25617558; Score: 0.35
DE  Interaction: P60033; IntAct: EBI-25646004; Score: 0.35
DE  Interaction: Q8TB24; IntAct: EBI-26518569; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0F6B1Q8; IntAct: EBI-27033383; Score: 0.46
DE  Interaction: A0A0F6B5H5; IntAct: EBI-27033770; Score: 0.35
DE  Interaction: A0A0F6B1M5; IntAct: EBI-27033901; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: A0A0H3NJM6; IntAct: EBI-27055677; Score: 0.35
DE  Interaction: O75582; IntAct: EBI-28931316; Score: 0.35
DE  Interaction: Q13131; IntAct: EBI-28939246; Score: 0.35
DE  Interaction: Q15746; IntAct: EBI-28941345; Score: 0.35
DE  Interaction: Q8NI60; IntAct: EBI-28943519; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q8NCE2; IntAct: EBI-27113554; Score: 0.35
DE  Interaction: P42695; IntAct: EBI-28951349; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-32724964; Score: 0.27
GO  GO:0005912;
GO  GO:0005929;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0071782;
GO  GO:0005768;
GO  GO:0070382;
GO  GO:0070062;
GO  GO:0005925;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0032593;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0030670;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0055038;
GO  GO:0030667;
GO  GO:0008021;
GO  GO:0005802;
GO  GO:0098641;
GO  GO:0003925;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0031489;
GO  GO:0019882;
GO  GO:0007409;
GO  GO:0032869;
GO  GO:0071786;
GO  GO:0016197;
GO  GO:0045200;
GO  GO:0097051;
GO  GO:0090150;
GO  GO:0043001;
GO  GO:0006893;
GO  GO:0030859;
GO  GO:1903361;
GO  GO:0072659;
GO  GO:0009306;
GO  GO:0045055;
GO  GO:0017157;
GO  GO:0006904;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYR
SQ  GAMGIMLVYDITNGKSFENISKWLRNIDEHANEDVERMLLGNKCDMDDKRVVPKGKGEQIAREHGIRFFETSAKANINIE
SQ  KAFLTLAEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC
//
ID  P61027;
PN  Ras-related protein Rab-10;
GN  Rab10;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic vesicle membrane {ECO:0000305}; Lipid-anchor {ECO:0000305|PubMed:20576682}; Cytoplasmic side {ECO:0000305|PubMed:20576682}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}. Endosome membrane {ECO:0000250|UniProtKB:P61026}. Recycling endosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:30398148}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20576682}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27354378}. Note=Associates with SLC2A4/GLUT4 storage vesicles (PubMed:27354378). Localizes to the base of the cilium when phosphorylated by LRRK2 on Thr-73 (PubMed:20576682, PubMed:27354378). Transiently associates with phagosomes (By similarity). Localizes to the endoplasmic reticulum at domains of new tubule growth (By similarity). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61026, ECO:0000269|PubMed:20576682, ECO:0000269|PubMed:27354378}.
DR  UNIPROT: P61027;
DR  UNIPROT: O88386;
DR  UNIPROT: Q9D7X6;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (By similarity). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane (By similarity). Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane (PubMed:17403373, PubMed:22908308, PubMed:27354378). In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response (PubMed:20643919). Also plays a specific role in asymmetric protein transport to the plasma membrane (By similarity). In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane (By similarity). In epithelial cells, it regulates transport from the Golgi to the basolateral membrane (By similarity). May play a role in the basolateral recycling pathway and in phagosome maturation (By similarity). May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (By similarity). Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis (By similarity). When phosphorylated by LRRK2 on Thr-73, it binds RILPL1 and inhibits ciliogenesis (By similarity). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P35281, ECO:0000250|UniProtKB:P61026, ECO:0000269|PubMed:17403373, ECO:0000269|PubMed:20643919, ECO:0000269|PubMed:22908308, ECO:0000269|PubMed:27354378}.
DE  Reference Proteome: Yes;
DE  Interaction: P62158; IntAct: EBI-911456; Score: 0.35
DE  Interaction: Q8CHW5; IntAct: EBI-7893516; Score: 0.40
DE  Interaction: Q9EPL2; IntAct: EBI-3869454; Score: 0.35
DE  Interaction: P50395; IntAct: EBI-6309640; Score: 0.54
DE  Interaction: P31150; IntAct: EBI-6309595; Score: 0.54
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q9DD03; IntAct: EBI-11567802; Score: 0.43
DE  Interaction: Q3UHA3; IntAct: EBI-11567802; Score: 0.35
DE  Interaction: O88990; IntAct: EBI-11567802; Score: 0.35
DE  Interaction: Q8C547; IntAct: EBI-11567802; Score: 0.35
DE  Interaction: Q9D289; IntAct: EBI-11567802; Score: 0.35
DE  Interaction: P33610; IntAct: EBI-11567802; Score: 0.35
DE  Interaction: Q6PHN9; IntAct: EBI-11567802; Score: 0.43
DE  Interaction: P55258; IntAct: EBI-11567802; Score: 0.43
DE  Interaction: P62823; IntAct: EBI-11567802; Score: 0.35
DE  Interaction: Q8BHC1; IntAct: EBI-11567802; Score: 0.35
DE  Interaction: Q3TTL0; IntAct: EBI-11567802; Score: 0.35
DE  Interaction: P62849; IntAct: EBI-11567802; Score: 0.35
DE  Interaction: Q9D1G1; IntAct: EBI-11571200; Score: 0.43
DE  Interaction: P61028; IntAct: EBI-11571565; Score: 0.27
DE  Interaction: Q8BMD2; IntAct: EBI-16153450; Score: 0.40
DE  Interaction: F6SEU4; IntAct: EBI-16733301; Score: 0.53
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0098993;
GO  GO:0005929;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005789;
GO  GO:0071782;
GO  GO:0005768;
GO  GO:0070382;
GO  GO:0005794;
GO  GO:0032593;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0030670;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0055038;
GO  GO:0008021;
GO  GO:0005802;
GO  GO:0003925;
GO  GO:0019003;
GO  GO:0051021;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0031489;
GO  GO:0019882;
GO  GO:0007409;
GO  GO:0032869;
GO  GO:0071786;
GO  GO:0016197;
GO  GO:0045200;
GO  GO:0097051;
GO  GO:0090150;
GO  GO:0043001;
GO  GO:0006893;
GO  GO:0006886;
GO  GO:0030859;
GO  GO:1903361;
GO  GO:0072659;
GO  GO:0009306;
GO  GO:0045055;
GO  GO:0017157;
GO  GO:0006904;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYR
SQ  GAMGIMLVYDITNGKSFENISKWLRNIDEHANEDVERMLLGNKCDMDDKRVVPKGKGEQIAREHGIRFFETSAKANINIE
SQ  KAFLTLAEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC
//
ID  Q5R5U1;
PN  Ras-related protein Rab-10;
GN  RAB10;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic vesicle membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}. Endosome membrane {ECO:0000250|UniProtKB:P61026}. Recycling endosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P24409}. Cell projection, cilium {ECO:0000250|UniProtKB:P61027}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61027}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P61027}. Note=Associates with SLC2A4/GLUT4 storage vesicles (By similarity). Localizes to the base of the cilium (By similarity). Transiently associates with phagosomes (By similarity). Localizes to the endoplasmic reticulum at domains of new tubule growth (By similarity). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61026, ECO:0000250|UniProtKB:P61027}.
DR  UNIPROT: Q5R5U1;
DR  UNIPROT: Q5RA43;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (By similarity). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane (By similarity). Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane (By similarity). In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response (By similarity). Also plays a specific role in asymmetric protein transport to the plasma membranes (By similarity). In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane. In epithelial cells, it regulates transport from the Golgi to the basolateral membrane (By similarity). May play a role in the basolateral recycling pathway and in phagosome maturation (By similarity). May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (By similarity). Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis (By similarity). When phosphorylated by LRRK2 on Thr-73, it binds RILPL1 and inhibits ciliogenesis (By similarity). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61026, ECO:0000250|UniProtKB:P61027}.
DE  Reference Proteome: Yes;
GO  GO:0005929;
GO  GO:0005789;
GO  GO:0071782;
GO  GO:0005768;
GO  GO:0070382;
GO  GO:0005794;
GO  GO:0032593;
GO  GO:0048471;
GO  GO:0030670;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0055038;
GO  GO:0005802;
GO  GO:0003925;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0031489;
GO  GO:0019882;
GO  GO:0007409;
GO  GO:0032869;
GO  GO:0071786;
GO  GO:0016197;
GO  GO:0045200;
GO  GO:0097051;
GO  GO:0043001;
GO  GO:0006893;
GO  GO:0030859;
GO  GO:1903361;
GO  GO:0072659;
GO  GO:0045055;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYR
SQ  GAMGIMLVYDITNGKSFENISKWLRNIDEHANEDVERMLLGNKCDMDDKRVVPKGKGEQIAREHGIRFFETSAKANINIE
SQ  KAFLTLAEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC
//
ID  P35281;
PN  Ras-related protein Rab-10;
GN  Rab10;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasmic vesicle membrane {ECO:0000305}; Lipid-anchor {ECO:0000305|PubMed:20576682}; Cytoplasmic side {ECO:0000305|PubMed:20576682}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}. Endosome membrane {ECO:0000250|UniProtKB:P61026}. Recycling endosome membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P24409}. Cell projection, cilium {ECO:0000269|PubMed:20576682}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61027}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P61027}. Note=Associates with SLC2A4/GLUT4 storage vesicles (By similarity). Localizes to the base of the cilium (PubMed:20576682). Transiently associates with phagosomes (By similarity). Localizes to the endoplasmic reticulum at domains of new tubule growth (By similarity). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61026, ECO:0000269|PubMed:20576682}.
DR  UNIPROT: P35281;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (By similarity). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane (By similarity). Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane (By similarity). In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response (By similarity). Also plays a specific role in asymmetric protein transport to the plasma membrane (By similarity). In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane (PubMed:21856246). In epithelial cells, it regulates transport from the Golgi to the basolateral membrane (By similarity). May play a role in the basolateral recycling pathway and in phagosome maturation (By similarity). May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (By similarity). Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis (By similarity). When phosphorylated by LRRK2 on Thr-73, it binds RILPL1 and inhibits ciliogenesis (By similarity). {ECO:0000250|UniProtKB:P24409, ECO:0000250|UniProtKB:P61026, ECO:0000250|UniProtKB:P61027, ECO:0000269|PubMed:21856246}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P07896; IntAct: EBI-8304928; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26440627; Score: 0.35
GO  GO:0098993;
GO  GO:0005929;
GO  GO:0005789;
GO  GO:0071782;
GO  GO:0005768;
GO  GO:0070382;
GO  GO:0005794;
GO  GO:0032593;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0030670;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0055038;
GO  GO:0008021;
GO  GO:0005802;
GO  GO:0003925;
GO  GO:0019003;
GO  GO:0051021;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0031489;
GO  GO:0019882;
GO  GO:0007409;
GO  GO:0071236;
GO  GO:0032869;
GO  GO:0071786;
GO  GO:0016197;
GO  GO:0045200;
GO  GO:0097051;
GO  GO:0090150;
GO  GO:0043001;
GO  GO:0006893;
GO  GO:0030859;
GO  GO:1903361;
GO  GO:0072659;
GO  GO:0009306;
GO  GO:0045055;
GO  GO:0017157;
GO  GO:0006904;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIEIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYR
SQ  GAMGIMLVYDITNGKSFENISKWLRNIDQHANEDVERMLLRNKCDMDHKRVVPKGKGEQIAREHRIRFFETSAKANINIE
SQ  KAFLTLPEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC
//
ID  Q2HJH2;
PN  Ras-related protein Rab-1B;
GN  RAB1B;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P10536}. Membrane {ECO:0000250|UniProtKB:P10536}; Lipid-anchor {ECO:0000250|UniProtKB:P10536}; Cytoplasmic side {ECO:0000250|UniProtKB:P10536}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000250|UniProtKB:P10536}; Cytoplasmic side {ECO:0000250|UniProtKB:P10536}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P10536}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm (By similarity). Co-localizes with MTMR6 to the endoplasmic reticulum- Golgi intermediate compartment and to the peri-Golgi region (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000250|UniProtKB:Q9H0U4}.
DR  UNIPROT: Q2HJH2;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (By similarity). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Required to modulate the compacted morphology of the Golgi. Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000250|UniProtKB:Q9H0U4}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0034045;
GO  GO:0003925;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000045;
GO  GO:0007030;
GO  GO:0006886;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9H0U4};
SQ  MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRG
SQ  AHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQ
SQ  AFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKQAGGGCC
//
ID  Q9H0U4;
PN  Ras-related protein Rab-1B;
GN  RAB1B;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11389151}. Membrane {ECO:0000269|PubMed:11389151}; Lipid-anchor {ECO:0000269|PubMed:11389151}; Cytoplasmic side {ECO:0000269|PubMed:11389151}. Preautophagosomal structure membrane {ECO:0000269|PubMed:20545908}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P10536}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments (PubMed:11389151). In the GDP-form, colocalizes with GDI in the cytoplasm (PubMed:11389151). Co-localizes with MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment and to the peri- Golgi region (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000269|PubMed:11389151}.
DR  UNIPROT: Q9H0U4;
DR  UNIPROT: A8K7S1;
DR  PDB: 3JZA;
DR  PDB: 3NKV;
DR  PDB: 4HLQ;
DR  PDB: 4I1O;
DR  PDB: 5O74;
DR  PDB: 5SZH;
DR  PDB: 5SZK;
DR  PDB: 6SKU;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DR  OMIM: 612565;
DR  DisGeNET: 81876;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:20545908, PubMed:9437002). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:9437002). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (PubMed:20545908). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments (By similarity). Required to modulate the compacted morphology of the Golgi (PubMed:26209634). Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000269|PubMed:20545908, ECO:0000269|PubMed:26209634, ECO:0000269|PubMed:9437002}.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-32718334; Score: 0.35
DE  Interaction: Q8TDZ2; IntAct: EBI-7566160; Score: 0.37
DE  Interaction: Q08379; IntAct: EBI-7566236; Score: 0.37
DE  Interaction: Q8N2Y8; IntAct: EBI-7566282; Score: 0.57
DE  Interaction: P40337; IntAct: EBI-1060209; Score: 0.00
DE  Interaction: P23508; IntAct: EBI-1064480; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1082004; Score: 0.00
DE  Interaction: A0A6H3AKP3; IntAct: EBI-2824082; Score: 0.00
DE  Interaction: Q8TAQ2; IntAct: EBI-3921327; Score: 0.37
DE  Interaction: Q969M1; IntAct: EBI-3925033; Score: 0.37
DE  Interaction: Q01968; IntAct: EBI-8603940; Score: 0.67
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: Q5ZSM7; IntAct: EBI-6666777; Score: 0.44
DE  Interaction: Q14CZ7; IntAct: EBI-11426979; Score: 0.35
DE  Interaction: Q9UKF7; IntAct: EBI-11687359; Score: 0.54
DE  Interaction: Q5S007; IntAct: EBI-11820797; Score: 0.59
DE  Interaction: P47224; IntAct: EBI-24554691; Score: 0.67
DE  Interaction: Q8WUD1; IntAct: EBI-21500361; Score: 0.35
DE  Interaction: Q92930; IntAct: EBI-21858952; Score: 0.35
DE  Interaction: Q92696; IntAct: EBI-21858952; Score: 0.35
DE  Interaction: P50395; IntAct: EBI-21858952; Score: 0.35
DE  Interaction: P31150; IntAct: EBI-21858952; Score: 0.35
DE  Interaction: P26374; IntAct: EBI-21858952; Score: 0.35
DE  Interaction: P24386; IntAct: EBI-21858952; Score: 0.35
DE  Interaction: P62820; IntAct: EBI-21858793; Score: 0.35
DE  Interaction: Q08484; IntAct: EBI-15592637; Score: 0.44
DE  Interaction: Q5ZWZ3; IntAct: EBI-15948833; Score: 0.62
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: P25786; IntAct: EBI-16797676; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798617; Score: 0.27
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20799058; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q8N6Q3; IntAct: EBI-21402192; Score: 0.35
DE  Interaction: Q9ULR3; IntAct: EBI-22223639; Score: 0.35
DE  Interaction: P51636; IntAct: EBI-25394431; Score: 0.35
DE  Interaction: O84232; IntAct: EBI-22302753; Score: 0.40
DE  Interaction: A0A0H3LG06; IntAct: EBI-25401076; Score: 0.35
DE  Interaction: Q29ST3; IntAct: EBI-25611201; Score: 0.40
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-26367302; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: P42695; IntAct: EBI-28951349; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-32719716; Score: 0.35
DE  Interaction: Q06124; IntAct: EBI-32723738; Score: 0.27
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0048471;
GO  GO:0034045;
GO  GO:0030133;
GO  GO:0003925;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000045;
GO  GO:0006888;
GO  GO:0007030;
GO  GO:0006886;
GO  GO:1903020;
GO  GO:2000785;
GO  GO:0019068;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8836150};
SQ  MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRG
SQ  AHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQ
SQ  AFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKPAGGGCC
//
ID  Q4R8X3;
PN  Ras-related protein Rab-1B;
GN  RAB1B;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P10536}. Membrane {ECO:0000250|UniProtKB:P10536}; Lipid-anchor {ECO:0000250|UniProtKB:P10536}; Cytoplasmic side {ECO:0000250|UniProtKB:P10536}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000250|UniProtKB:P10536}; Cytoplasmic side {ECO:0000250|UniProtKB:P10536}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P10536}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm (By similarity). Co-localizes with MTMR6 to the endoplasmic reticulum- Golgi intermediate compartment and to the peri-Golgi region (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000250|UniProtKB:Q9H0U4}.
DR  UNIPROT: Q4R8X3;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (By similarity). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Required to modulate the compacted morphology of the Golgi. Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000250|UniProtKB:Q9H0U4}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0034045;
GO  GO:0003925;
GO  GO:0005525;
GO  GO:0006914;
GO  GO:0007030;
GO  GO:0015031;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9H0U4};
SQ  MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRG
SQ  AHGIIVVYDVTDRESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQ
SQ  AFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKPAGGGCC
//
ID  Q9D1G1;
PN  Ras-related protein Rab-1B;
GN  Rab1b;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9H0U4}. Membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000250|UniProtKB:Q9H0U4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H0U4}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000250|UniProtKB:Q9H0U4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H0U4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P10536}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm (By similarity). Co-localizes with MTMR6 to the endoplasmic reticulum- Golgi intermediate compartment and to the peri-Golgi region (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000250|UniProtKB:Q9H0U4}.
DR  UNIPROT: Q9D1G1;
DR  UNIPROT: Q3U0N1;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (By similarity). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Required to modulate the compacted morphology of the Golgi. Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000250|UniProtKB:Q9H0U4}.
DE  Reference Proteome: Yes;
DE  Interaction: P61027; IntAct: EBI-11571200; Score: 0.43
DE  Interaction: P62821; IntAct: EBI-11568013; Score: 0.35
DE  Interaction: Q60809; IntAct: EBI-11571200; Score: 0.35
DE  Interaction: Q7SIG6; IntAct: EBI-11571200; Score: 0.35
DE  Interaction: Q8QZV4; IntAct: EBI-11571200; Score: 0.35
DE  Interaction: Q9DD03; IntAct: EBI-11571200; Score: 0.43
DE  Interaction: P56371; IntAct: EBI-11571200; Score: 0.35
DE  Interaction: Q8BHC1; IntAct: EBI-11571200; Score: 0.35
DE  Interaction: P62823; IntAct: EBI-11571200; Score: 0.35
DE  Interaction: Q6PHN9; IntAct: EBI-11571200; Score: 0.35
DE  Interaction: Q91V14; IntAct: EBI-11571200; Score: 0.35
DE  Interaction: P58389; IntAct: EBI-11571200; Score: 0.35
DE  Interaction: Q9Z179; IntAct: EBI-11571200; Score: 0.35
DE  Interaction: P61028; IntAct: EBI-11571997; Score: 0.27
DE  Interaction: P55258; IntAct: EBI-11571985; Score: 0.27
DE  Interaction: Q8BIZ1; IntAct: EBI-26595802; Score: 0.35
GO  GO:0005793;
GO  GO:0005794;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0034045;
GO  GO:0045202;
GO  GO:0003925;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000045;
GO  GO:0006888;
GO  GO:0007030;
GO  GO:0006886;
GO  GO:1903020;
GO  GO:2000785;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRG
SQ  AHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGVPFLETSAKNATNVEQ
SQ  AFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKPASGGCC
//
ID  Q06AU7;
PN  Ras-related protein Rab-1B;
GN  RAB1B;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P10536}. Membrane {ECO:0000250|UniProtKB:P10536}; Lipid-anchor {ECO:0000250|UniProtKB:P10536}; Cytoplasmic side {ECO:0000250|UniProtKB:P10536}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000250|UniProtKB:P10536}; Cytoplasmic side {ECO:0000250|UniProtKB:P10536}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P10536}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm (By similarity). Co-localizes with MTMR6 to the endoplasmic reticulum- Golgi intermediate compartment and to the peri-Golgi region (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000250|UniProtKB:Q9H0U4}.
DR  UNIPROT: Q06AU7;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (By similarity). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Required to modulate the compacted morphology of the Golgi. Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000250|UniProtKB:Q9H0U4}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0034045;
GO  GO:0003925;
GO  GO:0005525;
GO  GO:0006914;
GO  GO:0007030;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9H0U4};
SQ  MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERGRTITSSYYRG
SQ  AHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQ
SQ  AFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKQAGGGCC
//
ID  Q5RE13;
PN  Ras-related protein Rab-1B;
GN  RAB1B;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P10536}. Membrane {ECO:0000250|UniProtKB:P10536}; Lipid-anchor {ECO:0000250|UniProtKB:P10536}; Cytoplasmic side {ECO:0000250|UniProtKB:P10536}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000250|UniProtKB:P10536}; Cytoplasmic side {ECO:0000250|UniProtKB:P10536}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P10536}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm (By similarity). Co-localizes with MTMR6 to the endoplasmic reticulum- Golgi intermediate compartment and to the peri-Golgi region (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000250|UniProtKB:Q9H0U4}.
DR  UNIPROT: Q5RE13;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (By similarity). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Required to modulate the compacted morphology of the Golgi. Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment (By similarity). {ECO:0000250|UniProtKB:P10536, ECO:0000250|UniProtKB:Q9H0U4}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0034045;
GO  GO:0003925;
GO  GO:0005525;
GO  GO:0006914;
GO  GO:0007030;
GO  GO:0015031;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9H0U4};
SQ  MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRG
SQ  AHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQ
SQ  AFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKPAGGGCC
//
ID  P10536;
PN  Ras-related protein Rab-1B;
GN  Rab1b;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:1918138, ECO:0000269|PubMed:23188820}. Membrane {ECO:0000269|PubMed:1918138}; Lipid-anchor {ECO:0000269|PubMed:1918138}; Cytoplasmic side {ECO:0000269|PubMed:1918138}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23188820}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm (By similarity). Co-localizes with MTMR6 to the endoplasmic reticulum- Golgi intermediate compartment and to the peri-Golgi region (PubMed:23188820). {ECO:0000250|UniProtKB:Q9H0U4, ECO:0000269|PubMed:23188820}.
DR  UNIPROT: P10536;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (By similarity). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments (PubMed:1918138). Required to modulate the compacted morphology of the Golgi. Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum- Golgi intermediate compartment (PubMed:23188820). {ECO:0000250|UniProtKB:Q9H0U4, ECO:0000269|PubMed:1918138, ECO:0000269|PubMed:23188820}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26438079; Score: 0.35
GO  GO:0005793;
GO  GO:0048471;
GO  GO:0034045;
GO  GO:0045202;
GO  GO:0003925;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000045;
GO  GO:0006888;
GO  GO:0007030;
GO  GO:0006886;
GO  GO:1903020;
GO  GO:2000785;
GO  GO:0019068;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:1648736};
SQ  MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTVTSSYYRG
SQ  AHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGVPFLETSAKNATNVEQ
SQ  AFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKSASGGCC
//
ID  O14966;
PN  Ras-related protein Rab-7L1;
GN  RAB29;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24788816}. Golgi apparatus {ECO:0000269|PubMed:22042847}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}. Vacuole {ECO:0000269|PubMed:22042847}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22042847}. Note=Colocalizes with LRRK2 along tubular structures emerging from Golgi apparatus (PubMed:29212815). Colocalizes with GM130 at the Golgi apparatus (PubMed:22042847). Colocalizes with dynamic tubules emerging from and retracting to the Golgi apparatus (PubMed:22042847). Colocalizes with TGN46 at the trans- Golgi network (TGN) (PubMed:24788816). In Salmonella enterica serovar Typhi (S.Typhi) infected epithelial cells, is recruited and colocalized with both S.Typhi-containing vacuoles and dynamic tubules as well as those emerging from the vacuole toward the cell periphery (PubMed:22042847). {ECO:0000269|PubMed:22042847, ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}.
DR  UNIPROT: O14966;
DR  UNIPROT: B4E1K3;
DR  UNIPROT: C9JE77;
DR  PDB: 6HH2;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DR  OMIM: 603949;
DR  DisGeNET: 8934;
DE  Function: The small GTPases Rab are key regulators in vesicle trafficking (PubMed:24788816). Essential for maintaining the integrity of the endosome-trans-Golgi network structure (By similarity). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:24788816). Recruits LRRK2 to the Golgi complex and stimulates LRRK2 kinase activity (PubMed:29212815). Regulates neuronal process morphology in the intact central nervous system (CNS) (By similarity). May play a role in the formation of typhoid toxin transport intermediates during Salmonella enterica serovar Typhi (S.Typhi) epithelial cell infection (PubMed:22042847). {ECO:0000250|UniProtKB:Q63481, ECO:0000269|PubMed:22042847, ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UK45; IntAct: EBI-373977; Score: 0.00
DE  Interaction: A0A380PDF6; IntAct: EBI-2856699; Score: 0.00
DE  Interaction: Q5S007; IntAct: EBI-9247238; Score: 0.76
DE  Interaction: P11142; IntAct: EBI-9247728; Score: 0.35
DE  Interaction: O14976; IntAct: EBI-9247728; Score: 0.35
DE  Interaction: P14373; IntAct: EBI-24492416; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-24371046; Score: 0.56
DE  Interaction: O95751; IntAct: EBI-24414905; Score: 0.67
DE  Interaction: Q13049; IntAct: EBI-24451423; Score: 0.56
DE  Interaction: Q9NVJ2; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: Q96LI5; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: Q92696; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: Q5VSL9; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: Q14643; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: Q14573; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: Q14571; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: Q04656; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: P26374; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: P24386; IntAct: EBI-21858632; Score: 0.35
DE  Interaction: H9L447; IntAct: EBI-15950513; Score: 0.44
DE  Interaction: Q9H6J7; IntAct: EBI-22145198; Score: 0.37
DE  Interaction: Q9ULR3; IntAct: EBI-22223478; Score: 0.35
DE  Interaction: P57729; IntAct: EBI-22225674; Score: 0.40
DE  Interaction: Q8TEV9; IntAct: EBI-26618985; Score: 0.40
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0097708;
GO  GO:0042470;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0005773;
GO  GO:0070840;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0019894;
GO  GO:0031267;
GO  GO:0030154;
GO  GO:0007030;
GO  GO:0006886;
GO  GO:0032438;
GO  GO:0007005;
GO  GO:0044788;
GO  GO:0010977;
GO  GO:0090316;
GO  GO:0001921;
GO  GO:0050862;
GO  GO:1903441;
GO  GO:0072657;
GO  GO:1901214;
GO  GO:1905279;
GO  GO:0009617;
GO  GO:0042147;
GO  GO:0007416;
GO  GO:0042110;
GO  GO:1901998;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGSRDHLFKVLVVGDAAVGKTSLVQRYSQDSFSKHYKSTVGVDFALKVLQWSDYEIVRLQLWDIAGQERFTSMTRLYYRD
SQ  ASACVIMFDVTNATTFSNSQRWKQDLDSKLTLPNGEPVPCLLLANKCDLSPWAVSRDQIDRFSKENGFTGWTETSVKENK
SQ  NINEAMRVLIEKMMRNSTEDIMSLSTQGDYINLQTKSSSWSCC
//
ID  Q91YQ1;
PN  Ras-related protein Rab-7L1;
GN  Rab29;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O14966}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14966}. Golgi apparatus {ECO:0000250|UniProtKB:O14966}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O14966}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O14966}. Note=Colocalizes with GM130 at the Golgi apparatus (By similarity). Colocalizes with LRRK2 at dynamic tubules emerging from and retracting to the Golgi apparatus (By similarity). Colocalizes with TGN46 at the trans-Golgi network (TGN) (By similarity). {ECO:0000250|UniProtKB:O14966, ECO:0000250|UniProtKB:Q63481}.
DR  UNIPROT: Q91YQ1;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators in vesicle trafficking (By similarity). Essential for maintaining the integrity of endosome-trans-Golgi network structure (By similarity). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (By similarity). Recruits LRRK2 to the Golgi apparatus and stimulates LRRK2 kinase activity (By similarity). Regulates also neuronal process morphology in the intact central nervous system (CNS) (By similarity). {ECO:0000250|UniProtKB:O14966, ECO:0000250|UniProtKB:Q63481}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5S007; IntAct: EBI-6514227; Score: 0.46
DE  Interaction: Q5S006; IntAct: EBI-6558874; Score: 0.46
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005794;
GO  GO:0043231;
GO  GO:0097708;
GO  GO:0042470;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0005773;
GO  GO:0031982;
GO  GO:0070840;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0019894;
GO  GO:0031267;
GO  GO:0030154;
GO  GO:0060271;
GO  GO:0007030;
GO  GO:0006886;
GO  GO:0032438;
GO  GO:0007005;
GO  GO:0044788;
GO  GO:0010977;
GO  GO:0090316;
GO  GO:0001921;
GO  GO:0050862;
GO  GO:1903441;
GO  GO:0072657;
GO  GO:1901214;
GO  GO:1905279;
GO  GO:0009617;
GO  GO:0042147;
GO  GO:0007416;
GO  GO:0042110;
GO  GO:1901998;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGSRDHLFKVLVVGDAAVGKTSLVQRYSQDSFSKHYKSTVGVDFALKVLQWSDSEMVRLQLWDIAGQERFTSMTRLYYRD
SQ  ASACVIMFDVTNATTFSNSQRWKQDLDSKLTLPSGEPVPCLLLANKSDLSPWAVSRDQIDRFSKENGFTGWTETSVKENK
SQ  NINEAMRVLVEKMMNNSREDVMSLSTQGNYINLQAKPSSGWTCC
//
ID  Q5R7A4;
PN  Ras-related protein Rab-7L1;
GN  RAB29;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O14966}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14966}. Golgi apparatus {ECO:0000250|UniProtKB:O14966}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O14966}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O14966}. Note=Colocalizes with GM130 at the Golgi apparatus (By similarity). Colocalizes with LRRK2 at dynamic tubules emerging from and retracting to the Golgi apparatus (By similarity). Colocalizes with TGN46 at the trans-Golgi network (TGN) (By similarity). {ECO:0000250|UniProtKB:O14966, ECO:0000250|UniProtKB:Q63481}.
DR  UNIPROT: Q5R7A4;
DR  UNIPROT: Q5R6Z5;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators in vesicle trafficking (By similarity). Essential for maintaining the integrity of endosome-trans-Golgi network structure (By similarity). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (By similarity). Recruits LRRK2 to the Golgi apparatus and stimulates LRRK2 kinase activity (By similarity). Regulates also neuronal process morphology in the intact central nervous system (CNS) (By similarity). {ECO:0000250|UniProtKB:O14966, ECO:0000250|UniProtKB:Q63481}.
DE  Reference Proteome: Yes;
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0005773;
GO  GO:0070840;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0019894;
GO  GO:0031267;
GO  GO:0030154;
GO  GO:0007030;
GO  GO:0007005;
GO  GO:0044788;
GO  GO:0010977;
GO  GO:0090316;
GO  GO:0001921;
GO  GO:0050862;
GO  GO:0072657;
GO  GO:0015031;
GO  GO:0009617;
GO  GO:0042147;
GO  GO:0007416;
GO  GO:0042110;
GO  GO:1901998;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGSRDHLFKVLVVGDAAVGKTSLVQRYSQDSFSKHYKSTVGVDFALKVLQWSDYEIVRLQLWDIAGQERFTSMTRLYYRD
SQ  ASACVIMFDVTNATTFSNSQRWKQDLDSKLTLPNGEPVPCLLLANKCDLSPWAVSRDQIDRFSKENGFTGWTETSVKENK
SQ  NINEAMRVLIEKMMRNSTEDIMSLSTQGDYINLQTKSSSWSCC
//
ID  Q63481;
PN  Ras-related protein Rab-7L1;
GN  Rab29;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O14966}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14966}. Golgi apparatus {ECO:0000269|PubMed:23395371}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O14966}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23395371}. Note=Colocalizes with GM130 at the Golgi apparatus (By similarity). Colocalizes with dynamic tubules emerging from and retracting to the Golgi apparatus (By similarity). Colocalizes with TGN46 at the trans-Golgi network (TGN) (By similarity). Colocalized with LRRK2 along tubular structures emerging from Golgi apparatus (PubMed:23395371). {ECO:0000250|UniProtKB:O14966, ECO:0000269|PubMed:23395371}.
DR  UNIPROT: Q63481;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: The small GTPases Rab are key regulators in vesicle trafficking (PubMed:23395371). Essential for maintaining the integrity of endosome-trans-Golgi network structure (PubMed:23395371). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:23395371). Recruits LRRK2 to the Golgi apparatus and stimulates LRRK2 kinase activity (By similarity). Regulates also neuronal process morphology in the intact central nervous system (CNS) (PubMed:23395371). {ECO:0000250|UniProtKB:O14966, ECO:0000269|PubMed:23395371}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5S007; IntAct: EBI-6514548; Score: 0.46
DE  Interaction: Q08484; IntAct: EBI-15592913; Score: 0.44
GO  GO:0005801;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005794;
GO  GO:0097708;
GO  GO:0042470;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0005802;
GO  GO:0005773;
GO  GO:0031982;
GO  GO:0070840;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0019894;
GO  GO:0031267;
GO  GO:0030154;
GO  GO:0060271;
GO  GO:0007030;
GO  GO:0006886;
GO  GO:0032438;
GO  GO:0007005;
GO  GO:0044788;
GO  GO:0010977;
GO  GO:0090316;
GO  GO:0001921;
GO  GO:0050862;
GO  GO:1903441;
GO  GO:0072657;
GO  GO:1901214;
GO  GO:1905279;
GO  GO:0009617;
GO  GO:0042147;
GO  GO:0007416;
GO  GO:0042110;
GO  GO:1901998;
GO  GO:0039694;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGSRDHLFKVLVVGDAAVGKTSLVQRYSQDSFSKHYKSTVGVDFALKVLQWSDSEMVRLQLWDIAGQERFTSMTRLYYRD
SQ  ASACVIMFDVTNATTFSNSQRWKQDLDSKLTLPSGEPVPCLLLANKSDLSPWAVSRDQIDRFSKENGFTGWTETSVKENK
SQ  NINEAMRVLVEKMMNNSREDIMSSSTQGNYINLQTKPSPGWTCC
//
ID  Q9V8W3;
PN  Rab proteins geranylgeranyltransferase component A;
GN  Rep;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10082978}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10082978}. Note=Coordinated with the cell cycle, located around nuclei during prophase and telophase. Located to spindle poles during metaphase.
DR  UNIPROT: Q9V8W3;
DR  UNIPROT: O97142;
DR  Pfam: PF00996;
DE  Function: Binds unprenylated Rab proteins, presents it to the catalytic component B, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab to a protein acceptor (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A0B4K7J4; IntAct: EBI-249184; Score: 0.00
DE  Interaction: Q9VN77; IntAct: EBI-16092252; Score: 0.50
DE  Interaction: Q9W501; IntAct: EBI-16092228; Score: 0.50
GO  GO:0005818;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005968;
GO  GO:0000922;
GO  GO:0008021;
GO  GO:0005092;
GO  GO:0005096;
GO  GO:0007049;
GO  GO:0006886;
GO  GO:0007269;
GO  GO:1905552;
GO  GO:0018344;
GO  GO:0007264;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLDDLPEQFDLVVIGTGFTESCIAAAGSRIGKSVLHLDSNEYYGDVWSSFSMDALCARLDQEVEPHSALRNARYTWHSME
SQ  KESETDAQSWNRDSVLAKSRRFSLDLCPRILYAAGELVQLLIKSNICRYAEFRAVDHVCMRHNGEIVSVPCSRSDVFNTK
SQ  TLTIVEKRLLMKFLTACNDYGEDKCNEDSLEFRGRTFLEYLQAQRVTEKISSCVMQAIAMCGPSTSFEEGMQRTQRFLGS
SQ  LGRYGNTPFLFPMYGCGELPQCFCRLCAVYGGIYCLKRAVDDIALDSNSNEFLLSSAGKTLRAKNVVSAPGYTPVSKGIE
SQ  LKPHISRGLFISSSPLGNEELNKGGGGVNLLRLLDNEGGREAFLIQLSHYTGACPEGLYIFHLTTPALSEDPASDLAIFT
SQ  SQLFDQSDAQIIFSSYFTIAAQSSKSPAAEHIYYTDPPTYELDYDAAIANARDIFGKMFPDADFLPRAPDPEEIVVDGED
SQ  PSALNEHTLPEDLRAQLHDMQQATQEMDIQE
//
ID  P60763;
PN  Ras-related C3 botulinum toxin substrate 3;
GN  RAC3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Endomembrane system. Cell projection, lamellipodium. Cytoplasm, perinuclear region. Cell membrane. Cytoplasm, cytoskeleton. Note=Membrane-associated when activated. Colocalizes with NRBP to endomembranes and at the cell periphery in lamellipodia. Colocalized with CIB1 in the perinuclear area and at the cell periphery.
DR  UNIPROT: P60763;
DR  UNIPROT: O14658;
DR  UNIPROT: Q5U0M8;
DR  PDB: 2C2H;
DR  PDB: 2G0N;
DR  PDB: 2IC5;
DR  PDB: 2OV2;
DR  PDB: 2QME;
DR  PDB: 6TM1;
DR  Pfam: PF00071;
DR  PROSITE: PS51420;
DR  OMIM: 602050;
DR  OMIM: 618577;
DR  DisGeNET: 5881;
DE  Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner. {ECO:0000269|PubMed:11756406, ECO:0000269|PubMed:11956649}.
DE  Disease: Neurodevelopmental disorder with structural brain anomalies and dysmorphic facies (NEDBAF) [MIM:618577]: An autosomal dominant neurodevelopmental disorder characterized by global developmental delay, severe intellectual disability, poor language, seizures, dysmorphic features, and thin corpus callosum. {ECO:0000269|PubMed:29276006, ECO:0000269|PubMed:30293988}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UHY1; IntAct: EBI-767080; Score: 0.56
DE  Interaction: P07195; IntAct: EBI-2689000; Score: 0.00
DE  Interaction: P31629; IntAct: EBI-2689026; Score: 0.00
DE  Interaction: Q96IZ5; IntAct: EBI-2689013; Score: 0.00
DE  Interaction: Q9P013; IntAct: EBI-2690879; Score: 0.00
DE  Interaction: Q9Y5V0; IntAct: EBI-2690923; Score: 0.00
DE  Interaction: Q7L014; IntAct: EBI-2690936; Score: 0.00
DE  Interaction: P19338; IntAct: EBI-2693090; Score: 0.00
DE  Interaction: Q96IZ7; IntAct: EBI-2693142; Score: 0.00
DE  Interaction: Q9HB71; IntAct: EBI-2693103; Score: 0.00
DE  Interaction: P55209; IntAct: EBI-2693129; Score: 0.00
DE  Interaction: P07197; IntAct: EBI-2693116; Score: 0.00
DE  Interaction: Q9H446; IntAct: EBI-2693155; Score: 0.00
DE  Interaction: P03372; IntAct: EBI-3895691; Score: 0.64
DE  Interaction: P52565; IntAct: EBI-7335755; Score: 0.37
DE  Interaction: P52566; IntAct: EBI-7336081; Score: 0.37
DE  Interaction: P98170; IntAct: EBI-7581640; Score: 0.44
DE  Interaction: O95758; IntAct: EBI-7850130; Score: 0.35
DE  Interaction: Q62839; IntAct: EBI-7597856; Score: 0.27
DE  Interaction: P42768; IntAct: EBI-6285750; Score: 0.40
DE  Interaction: Q13153; IntAct: EBI-6285800; Score: 0.40
DE  Interaction: Q9BYG5; IntAct: EBI-22756502; Score: 0.56
DE  Interaction: P53365; IntAct: EBI-24777280; Score: 0.56
DE  Interaction: Q8WUI4; IntAct: EBI-24809361; Score: 0.56
DE  Interaction: P30825; IntAct: EBI-21505748; Score: 0.35
DE  Interaction: Q92581; IntAct: EBI-21548868; Score: 0.35
DE  Interaction: P52306; IntAct: EBI-21808615; Score: 0.35
DE  Interaction: P63000; IntAct: EBI-21873302; Score: 0.35
DE  Interaction: P15153; IntAct: EBI-21873252; Score: 0.35
DE  Interaction: P19793; IntAct: EBI-15666771; Score: 0.41
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9UF33; IntAct: EBI-32721019; Score: 0.27
GO  GO:0005938;
GO  GO:0071944;
GO  GO:0042995;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0005789;
GO  GO:0070062;
GO  GO:0031941;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0043020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0048306;
GO  GO:0003925;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0019901;
GO  GO:0030036;
GO  GO:0007015;
GO  GO:0030031;
GO  GO:0021894;
GO  GO:0030865;
GO  GO:0007163;
GO  GO:0048873;
GO  GO:0035556;
GO  GO:0050885;
GO  GO:0031175;
GO  GO:0033630;
GO  GO:1900026;
GO  GO:0032956;
GO  GO:0008360;
GO  GO:0014041;
GO  GO:0045730;
GO  GO:0007264;
GO  GO:0051932;
GO  GO:0016055;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLI
SQ  CFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDLRDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSAL
SQ  TQRGLKTVFDEAIRAVLCPPPVKKPGKKCTVF
//
ID  P60764;
PN  Ras-related C3 botulinum toxin substrate 3;
GN  Rac3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P60763}. Endomembrane system {ECO:0000250|UniProtKB:P60763}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P60763}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60763}. Cell membrane {ECO:0000250|UniProtKB:P60763}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60763}. Note=Membrane-associated when activated. Colocalizes with NRBP to endomembranes and at the cell periphery in lamellipodia. Colocalized with CIB1 in the perinuclear area and at the cell periphery. {ECO:0000250|UniProtKB:P60763}.
DR  UNIPROT: P60764;
DR  UNIPROT: O14658;
DR  Pfam: PF00071;
DR  PROSITE: PS51420;
DE  Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner. {ECO:0000250|UniProtKB:P60763}.
DE  Reference Proteome: Yes;
DE  Interaction: Q60749; IntAct: EBI-653444; Score: 0.37
DE  Interaction: Q99PT1; IntAct: EBI-653347; Score: 0.37
DE  Interaction: Q61599; IntAct: EBI-653366; Score: 0.37
DE  Interaction: Q8BIZ1; IntAct: EBI-26595802; Score: 0.35
GO  GO:0005938;
GO  GO:0071944;
GO  GO:0042995;
GO  GO:0031410;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0031941;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0048306;
GO  GO:0003925;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0019901;
GO  GO:0030036;
GO  GO:0007015;
GO  GO:0030031;
GO  GO:0021894;
GO  GO:0030865;
GO  GO:0007163;
GO  GO:0048873;
GO  GO:0050905;
GO  GO:0050885;
GO  GO:0031175;
GO  GO:0033630;
GO  GO:1900026;
GO  GO:0032956;
GO  GO:0022604;
GO  GO:0008360;
GO  GO:0014041;
GO  GO:0007264;
GO  GO:0051932;
GO  GO:0016055;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLI
SQ  CFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDLRDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSAL
SQ  TQRGLKTVFDEAIRAVLCPPPVKKPGKKCTVF
//
ID  P63243;
PN  Receptor of activated protein C kinase 1, N-terminally processed;
GN  RACK1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm {ECO:0000250|UniProtKB:P63244}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000250|UniProtKB:P63244}. Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite {ECO:0000250|UniProtKB:P68040}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery (By similarity). In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity). {ECO:0000250|UniProtKB:P63244, ECO:0000250|UniProtKB:P68040}.
DR  UNIPROT: P63243;
DR  UNIPROT: P25388;
DR  UNIPROT: P99049;
DR  UNIPROT: Q3T0R8;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (By similarity). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome- mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration (By similarity). Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63244}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:1990630;
GO  GO:0030496;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0001891;
GO  GO:0015935;
GO  GO:0051434;
GO  GO:0030332;
GO  GO:0008656;
GO  GO:0042803;
GO  GO:0005080;
GO  GO:0019903;
GO  GO:0030292;
GO  GO:0030971;
GO  GO:0043022;
GO  GO:0042169;
GO  GO:0035591;
GO  GO:0007049;
GO  GO:0071333;
GO  GO:0071363;
GO  GO:0007369;
GO  GO:0030308;
GO  GO:0010629;
GO  GO:1903208;
GO  GO:0033137;
GO  GO:0050765;
GO  GO:0032091;
GO  GO:0051898;
GO  GO:0045879;
GO  GO:0030178;
GO  GO:0043065;
GO  GO:0030335;
GO  GO:0051343;
GO  GO:2000543;
GO  GO:0042998;
GO  GO:0043547;
GO  GO:2001244;
GO  GO:0051901;
GO  GO:0032436;
GO  GO:0001934;
GO  GO:0031334;
GO  GO:0016567;
GO  GO:0051726;
GO  GO:0051302;
GO  GO:2000114;
GO  GO:0032880;
GO  GO:0006417;
GO  GO:0072344;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P63244};
SQ  MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALS
SQ  GSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNS
SQ  SNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALC
SQ  FSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
//
ID  P63247;
PN  Receptor of activated protein C kinase 1;
GN  RACK1;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm {ECO:0000250|UniProtKB:P63244}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000250|UniProtKB:P63244}. Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite {ECO:0000250|UniProtKB:P68040}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery (By similarity). In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity). {ECO:0000250|UniProtKB:P63244, ECO:0000250|UniProtKB:P68040}.
DR  UNIPROT: P63247;
DR  UNIPROT: A5HUK6;
DR  UNIPROT: P25388;
DR  UNIPROT: P99049;
DR  UNIPROT: Q5EVY1;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0015935;
GO  GO:0005080;
GO  GO:0043022;
GO  GO:0030178;
GO  GO:2000543;
GO  GO:0001934;
GO  GO:0016567;
GO  GO:0051302;
GO  GO:2000114;
GO  GO:0032880;
GO  GO:0072344;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P63244};
SQ  MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALS
SQ  GSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNS
SQ  SNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALC
SQ  FSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
//
ID  P63244;
PN  Receptor of activated protein C kinase 1, N-terminally processed;
GN  RACK1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:11312657, ECO:0000269|PubMed:17956333}; Peripheral membrane protein. Cytoplasm {ECO:0000269|PubMed:10849009, ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20573744}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12958311}. Nucleus {ECO:0000269|PubMed:10849009}. Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite {ECO:0000250|UniProtKB:P68040}. Cell projection, phagocytic cup {ECO:0000269|PubMed:21347310}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1 (PubMed:17956333). Also associated with the membrane in oncogene- transformed cells (PubMed:11884618). PKC activation induces translocation from the perinuclear region to the cell periphery (PubMed:11279199). In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity). Localized to phagocytic cups following infection by Y.pestis (PubMed:21347310). {ECO:0000250|UniProtKB:P68040, ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:21347310}.
DR  UNIPROT: P63244;
DR  UNIPROT: B3KTJ0;
DR  UNIPROT: D3DWS0;
DR  UNIPROT: P25388;
DR  UNIPROT: P99049;
DR  UNIPROT: Q53HU2;
DR  UNIPROT: Q5J8M6;
DR  UNIPROT: Q5VLR4;
DR  UNIPROT: Q6FH47;
DR  PDB: 4AOW;
DR  PDB: 4UG0;
DR  PDB: 4V6X;
DR  PDB: 5A2Q;
DR  PDB: 5AJ0;
DR  PDB: 5FLX;
DR  PDB: 5LKS;
DR  PDB: 5OA3;
DR  PDB: 5T2C;
DR  PDB: 5VYC;
DR  PDB: 6FEC;
DR  PDB: 6G18;
DR  PDB: 6G51;
DR  PDB: 6G53;
DR  PDB: 6G5H;
DR  PDB: 6G5I;
DR  PDB: 6IP5;
DR  PDB: 6IP6;
DR  PDB: 6IP8;
DR  PDB: 6OLE;
DR  PDB: 6OLF;
DR  PDB: 6OLG;
DR  PDB: 6OLI;
DR  PDB: 6OLZ;
DR  PDB: 6OM0;
DR  PDB: 6OM7;
DR  PDB: 6QZP;
DR  PDB: 6XA1;
DR  PDB: 6Y0G;
DR  PDB: 6Y2L;
DR  PDB: 6Y57;
DR  PDB: 6YBS;
DR  PDB: 6Z6L;
DR  PDB: 6Z6M;
DR  PDB: 6Z6N;
DR  PDB: 6ZLW;
DR  PDB: 6ZM7;
DR  PDB: 6ZME;
DR  PDB: 6ZMI;
DR  PDB: 6ZMO;
DR  PDB: 6ZMT;
DR  PDB: 6ZMW;
DR  PDB: 6ZN5;
DR  PDB: 6ZOJ;
DR  PDB: 6ZOL;
DR  PDB: 6ZON;
DR  PDB: 6ZP4;
DR  PDB: 6ZUO;
DR  PDB: 6ZV6;
DR  PDB: 6ZVH;
DR  PDB: 6ZVJ;
DR  PDB: 6ZXD;
DR  PDB: 6ZXE;
DR  PDB: 6ZXF;
DR  PDB: 6ZXG;
DR  PDB: 6ZXH;
DR  PDB: 7A09;
DR  PDB: 7K5I;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 176981;
DR  DisGeNET: 10399;
DE  Function: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome- mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158). {ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:12589061, ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17108144, ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:18621736, ECO:0000269|PubMed:19423701, ECO:0000269|PubMed:19674157, ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20541605, ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:20976005, ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:21347310, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:28132843, ECO:0000269|PubMed:9584165}. (Microbial infection) Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells. {ECO:0000269|PubMed:21347310}. (Microbial infection) Enhances phosphorylation of HIV-1 Nef by PKCs. {ECO:0000269|PubMed:11312657}. (Microbial infection) In case of poxvirus infection, remodels the ribosomes so that they become optimal for the viral mRNAs (containing poly-A leaders) translation but not for host mRNAs. {ECO:0000269|PubMed:28636603}. (Microbial infection) Contributes to the cap-independent internal ribosome entry site (IRES)-mediated translation by some RNA viruses. {ECO:0000269|PubMed:25416947}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: P00533; IntAct: EBI-9072870; Score: 0.40
DE  Interaction: P04626; IntAct: EBI-32721465; Score: 0.27
DE  Interaction: P07948; IntAct: EBI-9072792; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25509375; Score: 0.35
DE  Interaction: Q9Y561; IntAct: EBI-296801; Score: 0.51
DE  Interaction: Q9Y6K9; IntAct: EBI-361479; Score: 0.00
DE  Interaction: P60709; IntAct: EBI-353790; Score: 0.40
DE  Interaction: P21246; IntAct: EBI-728946; Score: 0.00
DE  Interaction: Q8NBJ4; IntAct: EBI-728949; Score: 0.00
DE  Interaction: P12236; IntAct: EBI-730822; Score: 0.00
DE  Interaction: P38936; IntAct: EBI-734149; Score: 0.00
DE  Interaction: Q9UMR2; IntAct: EBI-734245; Score: 0.00
DE  Interaction: Q9Y3Q8; IntAct: EBI-759787; Score: 0.37
DE  Interaction: Q1EHW4; IntAct: EBI-922367; Score: 0.35
DE  Interaction: P03255; IntAct: EBI-7140618; Score: 0.46
DE  Interaction: P48551; IntAct: EBI-958438; Score: 0.58
DE  Interaction: P13569; IntAct: EBI-1170380; Score: 0.53
DE  Interaction: P63167; IntAct: EBI-1769001; Score: 0.63
DE  Interaction: O43521; IntAct: EBI-1769058; Score: 0.40
DE  Interaction: O54918; IntAct: EBI-1769191; Score: 0.54
DE  Interaction: P22303; IntAct: EBI-1769965; Score: 0.53
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.55
DE  Interaction: Q8BT07; IntAct: EBI-2559310; Score: 0.40
DE  Interaction: Q8VD62; IntAct: EBI-2562857; Score: 0.40
DE  Interaction: Q5NHX0; IntAct: EBI-2806664; Score: 0.00
DE  Interaction: Q5NF74; IntAct: EBI-2806657; Score: 0.00
DE  Interaction: Q6KMS8; IntAct: EBI-2833445; Score: 0.00
DE  Interaction: A0A6L8PL93; IntAct: EBI-2833438; Score: 0.00
DE  Interaction: Q81UI7; IntAct: EBI-2833459; Score: 0.00
DE  Interaction: Q81U22; IntAct: EBI-2833452; Score: 0.00
DE  Interaction: A0A6L7H0W6; IntAct: EBI-2833466; Score: 0.00
DE  Interaction: Q8CZY2; IntAct: EBI-2847653; Score: 0.00
DE  Interaction: A0A0H2W269; IntAct: EBI-2847660; Score: 0.00
DE  Interaction: Q8CZR4; IntAct: EBI-2869177; Score: 0.00
DE  Interaction: Q8D1J6; IntAct: EBI-2869170; Score: 0.00
DE  Interaction: Q7CHU1; IntAct: EBI-2869212; Score: 0.00
DE  Interaction: Q8ZAR3; IntAct: EBI-2869205; Score: 0.00
DE  Interaction: A0A5P8YIB0; IntAct: EBI-2869184; Score: 0.00
DE  Interaction: A0A380PMW3; IntAct: EBI-2869191; Score: 0.00
DE  Interaction: A0A0H2W3W7; IntAct: EBI-2869198; Score: 0.00
DE  Interaction: Q92731; IntAct: EBI-2880601; Score: 0.35
DE  Interaction: P40337; IntAct: EBI-3507770; Score: 0.61
DE  Interaction: P00325; IntAct: EBI-3906988; Score: 0.37
DE  Interaction: P61586; IntAct: EBI-3927722; Score: 0.37
DE  Interaction: Q96GD4; IntAct: EBI-3935523; Score: 0.37
DE  Interaction: Q92615; IntAct: EBI-3941736; Score: 0.74
DE  Interaction: Q9HC52; IntAct: EBI-3951861; Score: 0.35
DE  Interaction: P42345; IntAct: EBI-4369732; Score: 0.35
DE  Interaction: Q6R327; IntAct: EBI-4369851; Score: 0.35
DE  Interaction: P61254; IntAct: EBI-4369851; Score: 0.64
DE  Interaction: P18124; IntAct: EBI-4369851; Score: 0.64
DE  Interaction: Q9UKV8; IntAct: EBI-8660720; Score: 0.50
DE  Interaction: P23396; IntAct: EBI-8660895; Score: 0.71
DE  Interaction: Q16659; IntAct: EBI-7208705; Score: 0.37
DE  Interaction: Q6QDQ4; IntAct: EBI-5276631; Score: 0.35
DE  Interaction: O75928; IntAct: EBI-7626183; Score: 0.40
DE  Interaction: Q8C5D8; IntAct: EBI-7626323; Score: 0.27
DE  Interaction: Q9NR09; IntAct: EBI-5654605; Score: 0.00
DE  Interaction: Q8IWX8; IntAct: EBI-7723227; Score: 0.37
DE  Interaction: Q8WWY3; IntAct: EBI-7733021; Score: 0.37
DE  Interaction: Q13123; IntAct: EBI-7738872; Score: 0.37
DE  Interaction: Q9BRX9; IntAct: EBI-7744956; Score: 0.37
DE  Interaction: Q96DF8; IntAct: EBI-7747320; Score: 0.37
DE  Interaction: P55795; IntAct: EBI-7760044; Score: 0.37
DE  Interaction: P12830; IntAct: EBI-6083772; Score: 0.27
DE  Interaction: Q77M19; IntAct: EBI-6156361; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q9JKL7; IntAct: EBI-6452273; Score: 0.35
DE  Interaction: Q08752; IntAct: EBI-6467805; Score: 0.59
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q4VGL6; IntAct: EBI-8759371; Score: 0.35
DE  Interaction: P0C090; IntAct: EBI-8759987; Score: 0.35
DE  Interaction: Q9NWQ8; IntAct: EBI-9072771; Score: 0.40
DE  Interaction: P05771; IntAct: EBI-9072870; Score: 0.40
DE  Interaction: P03206; IntAct: EBI-9347475; Score: 0.58
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.35
DE  Interaction: Q99497; IntAct: EBI-9685618; Score: 0.58
DE  Interaction: P63244; IntAct: EBI-9685865; Score: 0.40
DE  Interaction: Q16666; IntAct: EBI-9995438; Score: 0.35
DE  Interaction: P41218; IntAct: EBI-9996028; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-11322417; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: P23116; IntAct: EBI-11020127; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-11145880; Score: 0.35
DE  Interaction: Q96EQ0; IntAct: EBI-11152414; Score: 0.35
DE  Interaction: P48039; IntAct: EBI-11576149; Score: 0.37
DE  Interaction: Q70EL1; IntAct: EBI-24285633; Score: 0.56
DE  Interaction: Q9NZN8; IntAct: EBI-24339799; Score: 0.56
DE  Interaction: Q14694; IntAct: EBI-24503222; Score: 0.56
DE  Interaction: Q13895; IntAct: EBI-24793226; Score: 0.56
DE  Interaction: Q9H000; IntAct: EBI-24393937; Score: 0.56
DE  Interaction: Q14194; IntAct: EBI-24451162; Score: 0.56
DE  Interaction: Q96B67; IntAct: EBI-24535923; Score: 0.56
DE  Interaction: Q86UU5; IntAct: EBI-24569623; Score: 0.56
DE  Interaction: Q86WP2; IntAct: EBI-24635039; Score: 0.56
DE  Interaction: Q0P631; IntAct: EBI-24637360; Score: 0.56
DE  Interaction: O43309; IntAct: EBI-25272992; Score: 0.56
DE  Interaction: P35609; IntAct: EBI-12698011; Score: 0.56
DE  Interaction: P53041; IntAct: EBI-14023934; Score: 0.35
DE  Interaction: Q8NI37; IntAct: EBI-14026943; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-14035332; Score: 0.35
DE  Interaction: Q9NUD5; IntAct: EBI-21868538; Score: 0.35
DE  Interaction: Q9HCJ0; IntAct: EBI-21868538; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-21868538; Score: 0.35
DE  Interaction: P42694; IntAct: EBI-21868538; Score: 0.35
DE  Interaction: Q71RC2; IntAct: EBI-21877645; Score: 0.40
DE  Interaction: Q5MNZ9; IntAct: EBI-21877614; Score: 0.35
DE  Interaction: P54645; IntAct: EBI-16361875; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16362252; Score: 0.35
DE  Interaction: O75530; IntAct: EBI-15825729; Score: 0.53
DE  Interaction: Q9NY59; IntAct: EBI-15825773; Score: 0.40
DE  Interaction: P01375; IntAct: EBI-15825849; Score: 0.35
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: Q0VD86; IntAct: EBI-20620635; Score: 0.51
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: O96013; IntAct: EBI-26962273; Score: 0.35
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: P13693; IntAct: EBI-20992046; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-21255323; Score: 0.37
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9H3D4; IntAct: EBI-25300147; Score: 0.37
DE  Interaction: P46734; IntAct: EBI-25377403; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: Q9UKT8; IntAct: EBI-25594515; Score: 0.68
DE  Interaction: P0DTC2; IntAct: EBI-25509945; Score: 0.35
DE  Interaction: P0DTD3; IntAct: EBI-25510342; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.35
DE  Interaction: P46783; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P25398; IntAct: EBI-26597393; Score: 0.50
DE  Interaction: P62841; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P62249; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P08708; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P62269; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P39019; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P60866; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P62851; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P62979; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P62857; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P62273; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P46782; IntAct: EBI-26597393; Score: 0.61
DE  Interaction: P62906; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: Q96L21; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62913; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P26373; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P40429; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P50914; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P61313; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P18621; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: Q07020; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: Q02543; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P84098; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P46778; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P35268; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62829; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62750; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P83731; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P61353; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P46776; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P46779; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P47914; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62888; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62899; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62910; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P49207; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P42766; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P18077; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: Q9Y3U8; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P83881; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P61927; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P61513; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P63173; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62891; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P39023; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62987; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62945; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P36578; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P46777; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: Q02878; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62424; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62917; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P32969; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62280; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62277; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62263; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62244; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P63220; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62266; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62847; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62854; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P42677; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P15880; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62861; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P61247; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62701; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62753; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62081; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P62241; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P46781; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: P08865; IntAct: EBI-26359000; Score: 0.50
DE  Interaction: Q09161; IntAct: EBI-26396507; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-26399642; Score: 0.35
DE  Interaction: Q99608; IntAct: EBI-26955247; Score: 0.27
DE  Interaction: A0A0F6B2Z0; IntAct: EBI-27034162; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: O00311; IntAct: EBI-28930020; Score: 0.35
DE  Interaction: O43318; IntAct: EBI-28931001; Score: 0.35
DE  Interaction: P22612; IntAct: EBI-28934688; Score: 0.35
DE  Interaction: P36507; IntAct: EBI-28935019; Score: 0.35
DE  Interaction: P43405; IntAct: EBI-28935283; Score: 0.35
DE  Interaction: P53350; IntAct: EBI-28938281; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-28938584; Score: 0.35
DE  Interaction: Q05513; IntAct: EBI-28938998; Score: 0.35
DE  Interaction: Q16566; IntAct: EBI-28941485; Score: 0.35
DE  Interaction: Q16539; IntAct: EBI-28941466; Score: 0.35
DE  Interaction: Q2M2I8; IntAct: EBI-28941588; Score: 0.35
DE  Interaction: Q6PHR2; IntAct: EBI-28941815; Score: 0.35
DE  Interaction: Q86YV6; IntAct: EBI-28942265; Score: 0.35
DE  Interaction: Q8IY84; IntAct: EBI-28942464; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28944101; Score: 0.35
DE  Interaction: Q9H1R3; IntAct: EBI-28946206; Score: 0.35
DE  Interaction: Q9NQU5; IntAct: EBI-28946365; Score: 0.35
DE  Interaction: Q9Y2K2; IntAct: EBI-28947183; Score: 0.35
DE  Interaction: P78362; IntAct: EBI-28948274; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27105115; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-28955760; Score: 0.35
DE  Interaction: Q9BZB8; IntAct: EBI-29014562; Score: 0.27
DE  Interaction: Q8WV16; IntAct: EBI-30863977; Score: 0.35
DE  Interaction: P29376; IntAct: EBI-32718970; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: Q96Q04; IntAct: EBI-32723651; Score: 0.27
DE  Interaction: O15146; IntAct: EBI-32724025; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0022627;
GO  GO:0030425;
GO  GO:0070062;
GO  GO:1990630;
GO  GO:0030496;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0001891;
GO  GO:0015935;
GO  GO:0051434;
GO  GO:0045296;
GO  GO:0030332;
GO  GO:0008656;
GO  GO:0019899;
GO  GO:0008200;
GO  GO:0060090;
GO  GO:0042803;
GO  GO:0005080;
GO  GO:0019903;
GO  GO:0030292;
GO  GO:0030971;
GO  GO:0043022;
GO  GO:0003723;
GO  GO:0042169;
GO  GO:0035591;
GO  GO:0005102;
GO  GO:0006919;
GO  GO:0007049;
GO  GO:0071333;
GO  GO:0071363;
GO  GO:0002181;
GO  GO:0007369;
GO  GO:0030308;
GO  GO:1900102;
GO  GO:0010629;
GO  GO:1903208;
GO  GO:0033137;
GO  GO:0050765;
GO  GO:0032091;
GO  GO:0051898;
GO  GO:0045879;
GO  GO:0017148;
GO  GO:0030178;
GO  GO:0043473;
GO  GO:0043065;
GO  GO:0030335;
GO  GO:0051343;
GO  GO:2000543;
GO  GO:0042998;
GO  GO:0043547;
GO  GO:2001244;
GO  GO:0051901;
GO  GO:0032436;
GO  GO:0001934;
GO  GO:0031334;
GO  GO:0016567;
GO  GO:0051726;
GO  GO:0051302;
GO  GO:2000114;
GO  GO:0032880;
GO  GO:0072344;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALS
SQ  GSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNS
SQ  SNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALC
SQ  FSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
//
ID  P68040;
PN  Receptor of activated protein C kinase 1, N-terminally processed;
GN  Rack1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm {ECO:0000269|PubMed:20093473}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000269|PubMed:20093473}. Perikaryon {ECO:0000269|PubMed:16414032}. Cell projection, dendrite {ECO:0000269|PubMed:16414032}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. PKC activation induces translocation from the perinuclear region to the cell periphery (By similarity). In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (PubMed:16414032). {ECO:0000250|UniProtKB:P63244, ECO:0000269|PubMed:16414032}.
DR  UNIPROT: P68040;
DR  UNIPROT: P25388;
DR  UNIPROT: P99049;
DR  UNIPROT: Q3THP0;
DR  UNIPROT: Q3THY7;
DR  UNIPROT: Q3TKQ0;
DR  UNIPROT: Q3TW88;
DR  UNIPROT: Q5NCC5;
DR  UNIPROT: Q5NCC6;
DR  UNIPROT: Q9CSQ0;
DR  UNIPROT: Q9ERM6;
DR  PDB: 7CPU;
DR  PDB: 7CPV;
DR  PDB: 7LS1;
DR  PDB: 7LS2;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression. Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC- dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity). {ECO:0000250|UniProtKB:P63244, ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:20093473, ECO:0000269|PubMed:7968370}.
DE  Reference Proteome: Yes;
DE  Interaction: P05064; IntAct: EBI-494190; Score: 0.35
DE  Interaction: O88351; IntAct: EBI-655738; Score: 0.37
DE  Interaction: P68134; IntAct: EBI-1183981; Score: 0.40
DE  Interaction: P22303; IntAct: EBI-1770081; Score: 0.40
DE  Interaction: Q9JJP2; IntAct: EBI-1770199; Score: 0.35
DE  Interaction: O35177; IntAct: EBI-2642901; Score: 0.35
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: Q8CG73; IntAct: EBI-4284701; Score: 0.35
DE  Interaction: Q8C5D8; IntAct: EBI-7625880; Score: 0.53
DE  Interaction: Q9CQT7; IntAct: EBI-7769558; Score: 0.37
DE  Interaction: Q80V81; IntAct: EBI-6396445; Score: 0.37
DE  Interaction: Q99LX0; IntAct: EBI-9685844; Score: 0.46
DE  Interaction: P35294; IntAct: EBI-11567325; Score: 0.35
DE  Interaction: Q9CZE3; IntAct: EBI-11570633; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
DE  Interaction: Q9EP53; IntAct: EBI-16734894; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: P51637; IntAct: EBI-20565496; Score: 0.35
DE  Interaction: Q62470; IntAct: EBI-21016103; Score: 0.50
DE  Interaction: P68404; IntAct: EBI-21016124; Score: 0.40
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
DE  Interaction: P16056; IntAct: EBI-27118288; Score: 0.35
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:1990630;
GO  GO:0030496;
GO  GO:0005739;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0001891;
GO  GO:0015935;
GO  GO:0051434;
GO  GO:0030332;
GO  GO:0008656;
GO  GO:0019899;
GO  GO:0008200;
GO  GO:0042803;
GO  GO:0005080;
GO  GO:0019903;
GO  GO:0030292;
GO  GO:0030971;
GO  GO:0043022;
GO  GO:0042169;
GO  GO:0035591;
GO  GO:0038023;
GO  GO:0006919;
GO  GO:0007049;
GO  GO:0071333;
GO  GO:0071363;
GO  GO:0007369;
GO  GO:0035556;
GO  GO:0030308;
GO  GO:0010629;
GO  GO:1903208;
GO  GO:0033137;
GO  GO:0050765;
GO  GO:0032091;
GO  GO:0051898;
GO  GO:0045879;
GO  GO:0017148;
GO  GO:0030178;
GO  GO:0043473;
GO  GO:0043065;
GO  GO:0030335;
GO  GO:0051343;
GO  GO:2000543;
GO  GO:0042998;
GO  GO:0043547;
GO  GO:2001244;
GO  GO:0051901;
GO  GO:0032436;
GO  GO:0001934;
GO  GO:0031334;
GO  GO:0008104;
GO  GO:0016567;
GO  GO:0051726;
GO  GO:0051302;
GO  GO:2000114;
GO  GO:0032880;
GO  GO:1903076;
GO  GO:0072344;
GO  GO:0048511;
GO  GO:0006412;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P63244};
SQ  MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALS
SQ  GSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNS
SQ  SNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALC
SQ  FSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
//
ID  P63246;
PN  Receptor of activated protein C kinase 1, N-terminally processed;
GN  RACK1;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm {ECO:0000250|UniProtKB:P63244}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000250|UniProtKB:P63244}. Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite {ECO:0000250|UniProtKB:P68040}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery (By similarity). In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity). {ECO:0000250|UniProtKB:P63244, ECO:0000250|UniProtKB:P68040}.
DR  UNIPROT: P63246;
DR  UNIPROT: P25388;
DR  UNIPROT: P99049;
DR  PDB: 3J7P;
DR  PDB: 3J7R;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (By similarity). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome- mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration (By similarity). Regulates internalization of the muscarinic receptor CHRM2 (PubMed:20976005). Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63244, ECO:0000269|PubMed:20976005}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5U8X5; IntAct: EBI-12654472; Score: 0.55
DE  Interaction: Q9YS30; IntAct: EBI-12515533; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:1990630;
GO  GO:0030496;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0001891;
GO  GO:0015935;
GO  GO:0051434;
GO  GO:0030332;
GO  GO:0008656;
GO  GO:0042803;
GO  GO:0005080;
GO  GO:0019903;
GO  GO:0030292;
GO  GO:0030971;
GO  GO:0043022;
GO  GO:0042169;
GO  GO:0035591;
GO  GO:0007049;
GO  GO:0071333;
GO  GO:0071363;
GO  GO:0007369;
GO  GO:0030308;
GO  GO:0010629;
GO  GO:1903208;
GO  GO:0033137;
GO  GO:0050765;
GO  GO:0032091;
GO  GO:0051898;
GO  GO:0045879;
GO  GO:0030178;
GO  GO:0043065;
GO  GO:0030335;
GO  GO:0051343;
GO  GO:2000543;
GO  GO:0042998;
GO  GO:0043547;
GO  GO:2001244;
GO  GO:0051901;
GO  GO:0032436;
GO  GO:0001934;
GO  GO:0031334;
GO  GO:0016567;
GO  GO:0051726;
GO  GO:0051302;
GO  GO:2000114;
GO  GO:0032880;
GO  GO:0006417;
GO  GO:0072344;
GO  GO:0048511;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P63244};
SQ  MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALS
SQ  GSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNS
SQ  SNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALC
SQ  FSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
//
ID  P63245;
PN  Receptor of activated protein C kinase 1, N-terminally processed;
GN  Rack1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm {ECO:0000250|UniProtKB:P63244}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000250|UniProtKB:P63244}. Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite {ECO:0000250|UniProtKB:P68040}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery (By similarity). In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity). {ECO:0000250|UniProtKB:P63244, ECO:0000250|UniProtKB:P68040}.
DR  UNIPROT: P63245;
DR  UNIPROT: P25388;
DR  UNIPROT: P99049;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:15340087). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome- mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane. {ECO:0000250|UniProtKB:P63244, ECO:0000269|PubMed:15340087, ECO:0000269|PubMed:8302854}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P21708; IntAct: EBI-7620761; Score: 0.35
DE  Interaction: P54645; IntAct: EBI-16399805; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26439741; Score: 0.35
GO  GO:0044297;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:1990630;
GO  GO:0016020;
GO  GO:0030496;
GO  GO:0005739;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0001891;
GO  GO:0015935;
GO  GO:0051434;
GO  GO:0030332;
GO  GO:0008656;
GO  GO:0019899;
GO  GO:0008200;
GO  GO:0042803;
GO  GO:0005080;
GO  GO:0019903;
GO  GO:0030292;
GO  GO:0030971;
GO  GO:0043022;
GO  GO:0042169;
GO  GO:0035591;
GO  GO:0006919;
GO  GO:0007049;
GO  GO:0071333;
GO  GO:0071363;
GO  GO:0007369;
GO  GO:0030308;
GO  GO:0010629;
GO  GO:1903208;
GO  GO:0033137;
GO  GO:0050765;
GO  GO:0032091;
GO  GO:0051898;
GO  GO:0045879;
GO  GO:0017148;
GO  GO:0030178;
GO  GO:0001649;
GO  GO:0043473;
GO  GO:0043065;
GO  GO:0030335;
GO  GO:0051343;
GO  GO:2000543;
GO  GO:0042998;
GO  GO:0043547;
GO  GO:2001244;
GO  GO:0051901;
GO  GO:0032436;
GO  GO:0001934;
GO  GO:0031334;
GO  GO:0007205;
GO  GO:0016567;
GO  GO:0051726;
GO  GO:0051302;
GO  GO:2000114;
GO  GO:0032880;
GO  GO:1903076;
GO  GO:0072344;
GO  GO:0048511;
GO  GO:0006412;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P63244};
SQ  MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALS
SQ  GSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNS
SQ  SNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALC
SQ  FSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
//
ID  Q2KJ94;
PN  DNA repair protein RAD51 homolog 1;
GN  RAD51;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q06609}. Chromosome {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. Colocalizes with ERCC5/XPG to nuclear foci in S phase. Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner. {ECO:0000250|UniProtKB:Q06609}.
DR  UNIPROT: Q2KJ94;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DR  PROSITE: PS50163;
DE  Function: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2- scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross- link repair. {ECO:0000250|UniProtKB:Q06609}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005694;
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0009897;
GO  GO:0000800;
GO  GO:0001673;
GO  GO:0005815;
GO  GO:0005759;
GO  GO:0000228;
GO  GO:0000152;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0035861;
GO  GO:0005524;
GO  GO:0140664;
GO  GO:0003682;
GO  GO:0070182;
GO  GO:0000150;
GO  GO:0003690;
GO  GO:0042802;
GO  GO:0008022;
GO  GO:0019903;
GO  GO:0003697;
GO  GO:0017116;
GO  GO:0072757;
GO  GO:0006974;
GO  GO:0072711;
GO  GO:0071479;
GO  GO:0070192;
GO  GO:0000730;
GO  GO:0006268;
GO  GO:0000724;
GO  GO:0036297;
GO  GO:1990426;
GO  GO:0002769;
GO  GO:2000272;
GO  GO:0051106;
GO  GO:0010569;
GO  GO:0001932;
GO  GO:1990414;
GO  GO:0000722;
GO  GO:0010833;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILTEAAK
SQ  LVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYI
SQ  DTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSA
SQ  RQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCL
SQ  PEAEAMFAINADGVGDAKD
//
ID  Q8MKI8;
PN  DNA repair protein RAD51 homolog 1;
GN  RAD51;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q06609}. Chromosome {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. Colocalizes with ERCC5/XPG to nuclear foci in S phase. Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner. {ECO:0000250|UniProtKB:Q06609}.
DR  UNIPROT: Q8MKI8;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DR  PROSITE: PS50163;
DE  Function: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2- scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross- link repair. {ECO:0000250|UniProtKB:Q06609}.
DE  Reference Proteome: Yes;
DE  Interaction: P51587; IntAct: EBI-6957934; Score: 0.37
DE  Interaction: Q8MKI9; IntAct: EBI-6957976; Score: 0.37
DE  Interaction: Q8MKI8; IntAct: EBI-6958115; Score: 0.37
DE  Interaction: Q864S8; IntAct: EBI-6958082; Score: 0.37
GO  GO:0000785;
GO  GO:0005694;
GO  GO:0000781;
GO  GO:0000793;
GO  GO:0000794;
GO  GO:0005737;
GO  GO:0000800;
GO  GO:0001673;
GO  GO:0005815;
GO  GO:0005759;
GO  GO:0000228;
GO  GO:0000152;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0035861;
GO  GO:0005524;
GO  GO:0008094;
GO  GO:0140664;
GO  GO:0003682;
GO  GO:0070182;
GO  GO:0000150;
GO  GO:0003690;
GO  GO:0042802;
GO  GO:0008022;
GO  GO:0003697;
GO  GO:0017116;
GO  GO:0072757;
GO  GO:0006974;
GO  GO:0072711;
GO  GO:0071479;
GO  GO:0070192;
GO  GO:0000730;
GO  GO:0006268;
GO  GO:0000724;
GO  GO:0036297;
GO  GO:0051321;
GO  GO:0006312;
GO  GO:1990426;
GO  GO:0051106;
GO  GO:0007131;
GO  GO:0010569;
GO  GO:0001932;
GO  GO:1990414;
GO  GO:0042148;
GO  GO:0000722;
GO  GO:0010833;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELISIKGISEAKADKILTEAAK
SQ  LVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYI
SQ  DTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSA
SQ  RQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCL
SQ  PEAEAMFAINADGVGDAKD
//
ID  P70099;
PN  DNA repair protein RAD51 homolog 1;
GN  RAD51;
OS  10029;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q06609}. Chromosome {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. Colocalizes with ERCC5/XPG to nuclear foci in S phase. Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner. {ECO:0000250|UniProtKB:Q06609}.
DR  UNIPROT: P70099;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DR  PROSITE: PS50163;
DE  Function: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2- scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross- link repair. {ECO:0000250|UniProtKB:Q06609}.
DE  Reference Proteome: No;
GO  GO:0000785;
GO  GO:0005694;
GO  GO:0000781;
GO  GO:0000793;
GO  GO:0000794;
GO  GO:0005737;
GO  GO:0000800;
GO  GO:0001673;
GO  GO:0005815;
GO  GO:0005759;
GO  GO:0000228;
GO  GO:0000152;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0035861;
GO  GO:0005524;
GO  GO:0140664;
GO  GO:0003682;
GO  GO:0070182;
GO  GO:0000150;
GO  GO:0003690;
GO  GO:0042802;
GO  GO:0008022;
GO  GO:0003697;
GO  GO:0017116;
GO  GO:0072757;
GO  GO:0006974;
GO  GO:0072711;
GO  GO:0071479;
GO  GO:0070192;
GO  GO:0000730;
GO  GO:0006268;
GO  GO:0000724;
GO  GO:0036297;
GO  GO:0051321;
GO  GO:1990426;
GO  GO:0051106;
GO  GO:0010569;
GO  GO:0001932;
GO  GO:1990414;
GO  GO:0000722;
GO  GO:0010833;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMQMQLEANADTSVEEESFGPQPISRLEQCGISANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAK
SQ  LVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYI
SQ  DTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSA
SQ  RQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFTADPKKPIGGNIIAHASTTRLYLRKGRGETRICKVYDSPCL
SQ  PEAEAMFAINADGVGDAKD
//
ID  Q06609;
PN  DNA repair protein RAD51 homolog 1;
GN  RAD51;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:12442171, ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:18417535, ECO:0000269|PubMed:19783859, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:26681308, ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:9192668}. Cytoplasm {ECO:0000269|PubMed:16215984, ECO:0000269|PubMed:26681308}. Cytoplasm, perinuclear region. Mitochondrion matrix {ECO:0000269|PubMed:20413593}. Chromosome {ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:27797818, ECO:0000269|PubMed:31844045}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21276791}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage (PubMed:20154705). DNA damage induces an increase in nuclear levels (PubMed:20154705). Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment (PubMed:23754376). Accumulated at sites of DNA damage in a SPIDR- dependent manner (PubMed:23509288). Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner (PubMed:23401855). Colocalizes with ERCC5/XPG to nuclear foci in S phase (PubMed:26833090). Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner (PubMed:27797818, PubMed:31844045). {ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:23754376, ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:27797818, ECO:0000269|PubMed:31844045}.
DR  UNIPROT: Q06609;
DR  UNIPROT: B0FXP0;
DR  UNIPROT: B2R8T6;
DR  UNIPROT: Q6FHX9;
DR  UNIPROT: Q6ZNA8;
DR  UNIPROT: Q9BV60;
DR  PDB: 1B22;
DR  PDB: 1N0W;
DR  PDB: 5H1B;
DR  PDB: 5H1C;
DR  PDB: 5JZC;
DR  PDB: 5NP7;
DR  PDB: 5NWL;
DR  PDB: 7C9A;
DR  PDB: 7EJC;
DR  PDB: 7EJE;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DR  PROSITE: PS50163;
DR  OMIM: 114480;
DR  OMIM: 179617;
DR  OMIM: 614508;
DR  OMIM: 617244;
DR  DisGeNET: 5888;
DE  Function: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR) (PubMed:18417535, PubMed:20348101, PubMed:12205100, PubMed:20231364, PubMed:23754376, PubMed:23509288, PubMed:28575658, PubMed:26681308). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange (PubMed:18417535, PubMed:20348101, PubMed:12205100, PubMed:20231364, PubMed:23754376, PubMed:23509288, PubMed:28575658, PubMed:26681308). Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template (PubMed:18417535, PubMed:20348101, PubMed:12205100, PubMed:20231364, PubMed:23754376, PubMed:23509288, PubMed:28575658, PubMed:26681308). Recruited to resolve stalled replication forks during replication stress (PubMed:27797818, PubMed:31844045). Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR (PubMed:24141787, PubMed:12442171). Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3 (PubMed:20413593). Also involved in interstrand cross-link repair (PubMed:26253028). {ECO:0000269|PubMed:12205100, ECO:0000269|PubMed:12442171, ECO:0000269|PubMed:18417535, ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:20348101, ECO:0000269|PubMed:20413593, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:23754376, ECO:0000269|PubMed:24141787, ECO:0000269|PubMed:26253028, ECO:0000269|PubMed:26681308, ECO:0000269|PubMed:27797818, ECO:0000269|PubMed:28575658, ECO:0000269|PubMed:31844045}.
DE  Disease: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:10807537, ECO:0000269|PubMed:25539919}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Mirror movements 2 (MRMV2) [MIM:614508]: A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities. {ECO:0000269|PubMed:22305526}. Note=The disease is caused by variants affecting the gene represented in this entry. Fanconi anemia, complementation group R (FANCR) [MIM:617244]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:26253028, ECO:0000269|PubMed:26681308}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O43502; IntAct: EBI-7988560; Score: 0.66
DE  Interaction: O43542; IntAct: EBI-9249126; Score: 0.73
DE  Interaction: P00519; IntAct: EBI-6995587; Score: 0.40
DE  Interaction: P63165; IntAct: EBI-15819689; Score: 0.44
DE  Interaction: P51587; IntAct: EBI-297231; Score: 0.98
DE  Interaction: Q06609; IntAct: EBI-297242; Score: 0.92
DE  Interaction: P04637; IntAct: EBI-367003; Score: 0.40
DE  Interaction: Q12873; IntAct: EBI-729210; Score: 0.00
DE  Interaction: P08670; IntAct: EBI-730657; Score: 0.00
DE  Interaction: P43351; IntAct: EBI-706470; Score: 0.63
DE  Interaction: P94102; IntAct: EBI-930862; Score: 0.37
DE  Interaction: Q7Y1C5; IntAct: EBI-930894; Score: 0.37
DE  Interaction: Q7Y1C4; IntAct: EBI-944276; Score: 0.37
DE  Interaction: P41214; IntAct: EBI-1081745; Score: 0.00
DE  Interaction: Q9Y376; IntAct: EBI-1082450; Score: 0.00
DE  Interaction: Q9Y5L4; IntAct: EBI-1085852; Score: 0.00
DE  Interaction: P36601; IntAct: EBI-1109552; Score: 0.55
DE  Interaction: Q96B01; IntAct: EBI-1178705; Score: 0.79
DE  Interaction: Q6UWZ7; IntAct: EBI-1263592; Score: 0.27
DE  Interaction: Q96RL1; IntAct: EBI-1263606; Score: 0.27
DE  Interaction: Q9BQ15; IntAct: EBI-2121557; Score: 0.46
DE  Interaction: Q9UI08; IntAct: EBI-7203877; Score: 0.44
DE  Interaction: P60709; IntAct: EBI-3646976; Score: 0.37
DE  Interaction: P07737; IntAct: EBI-3646981; Score: 0.37
DE  Interaction: P27694; IntAct: EBI-3647003; Score: 0.37
DE  Interaction: P15927; IntAct: EBI-3647007; Score: 0.37
DE  Interaction: P35244; IntAct: EBI-3647015; Score: 0.37
DE  Interaction: P16104; IntAct: EBI-8589785; Score: 0.27
DE  Interaction: O60701; IntAct: EBI-3912761; Score: 0.37
DE  Interaction: Q9UBU9; IntAct: EBI-3914918; Score: 0.37
DE  Interaction: O14757; IntAct: EBI-4404023; Score: 0.52
DE  Interaction: Q6NVH7; IntAct: EBI-5281993; Score: 0.52
DE  Interaction: Q86YC2; IntAct: EBI-7615447; Score: 0.80
DE  Interaction: P38398; IntAct: EBI-7615501; Score: 0.72
DE  Interaction: Q96PU4; IntAct: EBI-6051513; Score: 0.40
DE  Interaction: Q9W157; IntAct: EBI-7677194; Score: 0.35
DE  Interaction: Q9NTI5; IntAct: EBI-7677915; Score: 0.35
DE  Interaction: P42574; IntAct: EBI-6592054; Score: 0.27
DE  Interaction: P07900; IntAct: EBI-9064637; Score: 0.37
DE  Interaction: Q8WX92; IntAct: EBI-9064611; Score: 0.37
DE  Interaction: P67870; IntAct: EBI-9064624; Score: 0.37
DE  Interaction: P11172; IntAct: EBI-9064689; Score: 0.37
DE  Interaction: Q9UPT6; IntAct: EBI-9064650; Score: 0.37
DE  Interaction: Q9UHG2; IntAct: EBI-9064663; Score: 0.37
DE  Interaction: Q8IXJ6; IntAct: EBI-9064676; Score: 0.37
DE  Interaction: Q14694; IntAct: EBI-9064702; Score: 0.37
DE  Interaction: P55290; IntAct: EBI-9070137; Score: 0.37
DE  Interaction: Q15828; IntAct: EBI-9070150; Score: 0.37
DE  Interaction: Q96KN1; IntAct: EBI-9070163; Score: 0.54
DE  Interaction: Q13007; IntAct: EBI-9070176; Score: 0.51
DE  Interaction: Q86UX2; IntAct: EBI-9070189; Score: 0.37
DE  Interaction: P11245; IntAct: EBI-9070202; Score: 0.54
DE  Interaction: Q9Y5Y6; IntAct: EBI-9070215; Score: 0.37
DE  Interaction: P04155; IntAct: EBI-9070228; Score: 0.37
DE  Interaction: Q9BZ95; IntAct: EBI-9070241; Score: 0.54
DE  Interaction: Q8IUH5; IntAct: EBI-9087924; Score: 0.37
DE  Interaction: Q9HAV2; IntAct: EBI-9368380; Score: 0.40
DE  Interaction: P58340; IntAct: EBI-9368358; Score: 0.40
DE  Interaction: Q96BE0; IntAct: EBI-9368402; Score: 0.40
DE  Interaction: A2AUM9; IntAct: EBI-10994361; Score: 0.35
DE  Interaction: Q9Z1B5; IntAct: EBI-10996176; Score: 0.35
DE  Interaction: A2APR8; IntAct: EBI-11001201; Score: 0.35
DE  Interaction: P60953; IntAct: EBI-11002356; Score: 0.35
DE  Interaction: Q6P1J9; IntAct: EBI-11014586; Score: 0.35
DE  Interaction: Q5FBB7; IntAct: EBI-11015316; Score: 0.35
DE  Interaction: Q91X51; IntAct: EBI-11015786; Score: 0.35
DE  Interaction: Q9CWL8; IntAct: EBI-11023129; Score: 0.35
DE  Interaction: Q3U410; IntAct: EBI-11026005; Score: 0.35
DE  Interaction: D3YY91; IntAct: EBI-11028850; Score: 0.35
DE  Interaction: P78318; IntAct: EBI-11039408; Score: 0.35
DE  Interaction: E9Q4K7; IntAct: EBI-11042417; Score: 0.35
DE  Interaction: Q9UGU5; IntAct: EBI-11042629; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P16298; IntAct: EBI-11047313; Score: 0.35
DE  Interaction: D6RA96; IntAct: EBI-11047357; Score: 0.35
DE  Interaction: Q8CIF6; IntAct: EBI-11072478; Score: 0.35
DE  Interaction: D6RI17; IntAct: EBI-11073846; Score: 0.35
DE  Interaction: Q9BSJ2; IntAct: EBI-11083048; Score: 0.35
DE  Interaction: O08586; IntAct: EBI-11086220; Score: 0.35
DE  Interaction: Q9NP66; IntAct: EBI-11087905; Score: 0.35
DE  Interaction: Q9H2H0; IntAct: EBI-11088370; Score: 0.35
DE  Interaction: Q6DFZ1; IntAct: EBI-11091172; Score: 0.35
DE  Interaction: Q8C8N2; IntAct: EBI-11092225; Score: 0.35
DE  Interaction: Q56A08; IntAct: EBI-11095792; Score: 0.35
DE  Interaction: Q8CAF4; IntAct: EBI-11096313; Score: 0.35
DE  Interaction: P35749; IntAct: EBI-11098041; Score: 0.35
DE  Interaction: Q6PJG2; IntAct: EBI-11106137; Score: 0.35
DE  Interaction: P35700; IntAct: EBI-11114197; Score: 0.35
DE  Interaction: O75792; IntAct: EBI-11115131; Score: 0.35
DE  Interaction: P46467; IntAct: EBI-11115954; Score: 0.35
DE  Interaction: Q96HR8; IntAct: EBI-11116990; Score: 0.35
DE  Interaction: Q14114; IntAct: EBI-11117560; Score: 0.35
DE  Interaction: Q9CQW0; IntAct: EBI-11121111; Score: 0.35
DE  Interaction: P51148; IntAct: EBI-11124397; Score: 0.35
DE  Interaction: Q9ET47; IntAct: EBI-11124608; Score: 0.35
DE  Interaction: P70335; IntAct: EBI-11124658; Score: 0.35
DE  Interaction: O00257; IntAct: EBI-11125021; Score: 0.35
DE  Interaction: Q9NYU2; IntAct: EBI-11127729; Score: 0.35
DE  Interaction: O00400; IntAct: EBI-11135399; Score: 0.35
DE  Interaction: Q7Z4S6; IntAct: EBI-11140402; Score: 0.35
DE  Interaction: Q9UBT6; IntAct: EBI-11141739; Score: 0.35
DE  Interaction: P51530; IntAct: EBI-21525688; Score: 0.35
DE  Interaction: Q14565; IntAct: EBI-21540407; Score: 0.35
DE  Interaction: Q96LI6; IntAct: EBI-21542067; Score: 0.35
DE  Interaction: Q86XE0; IntAct: EBI-21777996; Score: 0.35
DE  Interaction: Q6PIW4; IntAct: EBI-21840775; Score: 0.35
DE  Interaction: P28347; IntAct: EBI-21881702; Score: 0.40
DE  Interaction: Q14676; IntAct: EBI-15557704; Score: 0.52
DE  Interaction: O94761; IntAct: EBI-15710123; Score: 0.40
DE  Interaction: P54132; IntAct: EBI-15819727; Score: 0.44
DE  Interaction: O94762; IntAct: EBI-15710184; Score: 0.35
DE  Interaction: Q14191; IntAct: EBI-15710258; Score: 0.40
DE  Interaction: P61956; IntAct: EBI-15819708; Score: 0.44
DE  Interaction: O14980; IntAct: EBI-16073017; Score: 0.40
DE  Interaction: O75417; IntAct: EBI-16141075; Score: 0.60
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
DE  Interaction: Q92698; IntAct: EBI-22014998; Score: 0.37
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P15924; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: Q02413; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: P16403; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: P07477; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: Q96P63; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: P81605; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: Q01469; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: P68363; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: P62899; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: P62701; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: P39019; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: P01040; IntAct: EBI-25483457; Score: 0.35
DE  Interaction: Q14159; IntAct: EBI-26608253; Score: 0.66
DE  Interaction: Q9H9A7; IntAct: EBI-26616811; Score: 0.35
DE  Interaction: Q00341; IntAct: EBI-27122970; Score: 0.50
GO  GO:0000785;
GO  GO:0000781;
GO  GO:0000793;
GO  GO:0000794;
GO  GO:0005737;
GO  GO:0000800;
GO  GO:0001673;
GO  GO:0005815;
GO  GO:0005759;
GO  GO:0005739;
GO  GO:0000228;
GO  GO:0000152;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0032991;
GO  GO:0035861;
GO  GO:0005524;
GO  GO:0008094;
GO  GO:0140664;
GO  GO:0003682;
GO  GO:0070182;
GO  GO:0000150;
GO  GO:0003690;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0003676;
GO  GO:0008022;
GO  GO:0003697;
GO  GO:0017116;
GO  GO:0072757;
GO  GO:0072719;
GO  GO:0006974;
GO  GO:0071480;
GO  GO:0072711;
GO  GO:0071479;
GO  GO:0070192;
GO  GO:0000730;
GO  GO:0006310;
GO  GO:0006281;
GO  GO:0006268;
GO  GO:0000724;
GO  GO:0035518;
GO  GO:0036297;
GO  GO:0051321;
GO  GO:0006312;
GO  GO:1990426;
GO  GO:0051106;
GO  GO:0051865;
GO  GO:0007131;
GO  GO:2000001;
GO  GO:0010569;
GO  GO:0001932;
GO  GO:0031297;
GO  GO:1990414;
GO  GO:1904631;
GO  GO:0009636;
GO  GO:0010165;
GO  GO:0009410;
GO  GO:0042148;
GO  GO:0000722;
GO  GO:0010833;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAK
SQ  LVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYI
SQ  DTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSA
SQ  RQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCL
SQ  PEAEAMFAINADGVGDAKD
//
ID  Q08297;
PN  DNA repair protein RAD51 homolog 1;
GN  Rad51;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q06609}. Chromosome {ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471, ECO:0000269|PubMed:30760716, ECO:0000269|PubMed:30949703, ECO:0000269|PubMed:32463460}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. Colocalizes with ERCC5/XPG to nuclear foci in S phase. Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner. {ECO:0000250|UniProtKB:Q06609}.
DR  UNIPROT: Q08297;
DR  UNIPROT: Q3UAY5;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DR  PROSITE: PS50163;
DE  Function: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR) (PubMed:15834424). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair (By similarity). {ECO:0000250|UniProtKB:Q06609, ECO:0000269|PubMed:15834424}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8K396; IntAct: EBI-310417; Score: 0.37
GO  GO:0000785;
GO  GO:0005694;
GO  GO:0000781;
GO  GO:0000793;
GO  GO:0000794;
GO  GO:0005737;
GO  GO:0000800;
GO  GO:0001673;
GO  GO:0005815;
GO  GO:0005759;
GO  GO:0005739;
GO  GO:0000228;
GO  GO:0000152;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0032991;
GO  GO:0035861;
GO  GO:0000795;
GO  GO:0005524;
GO  GO:0008094;
GO  GO:0140664;
GO  GO:0003682;
GO  GO:0070182;
GO  GO:0000150;
GO  GO:0003690;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0008022;
GO  GO:0003697;
GO  GO:0017116;
GO  GO:0071312;
GO  GO:0072757;
GO  GO:0072719;
GO  GO:0006974;
GO  GO:0071480;
GO  GO:0072711;
GO  GO:0071479;
GO  GO:0070192;
GO  GO:0000730;
GO  GO:0006281;
GO  GO:0006268;
GO  GO:0000724;
GO  GO:0035518;
GO  GO:0036297;
GO  GO:0051321;
GO  GO:0006312;
GO  GO:1990426;
GO  GO:0051106;
GO  GO:0051865;
GO  GO:0007131;
GO  GO:2000001;
GO  GO:0010569;
GO  GO:0001932;
GO  GO:0031297;
GO  GO:1990414;
GO  GO:1904631;
GO  GO:0009636;
GO  GO:0010165;
GO  GO:0009410;
GO  GO:0042148;
GO  GO:0000722;
GO  GO:0010833;
GO  GO:0032200;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMQMQLEASADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGYHTVEAVAYAPKKELINIKGISEAKADKILTEAAK
SQ  LVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYI
SQ  DTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSA
SQ  RQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCL
SQ  PEAEAMFAINADGVGDAKD
//
ID  O77507;
PN  DNA repair protein RAD51 homolog 1;
GN  RAD51;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q06609}. Chromosome {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner. Colocalizes with ERCC5/XPG to nuclear foci in S phase (By similarity). {ECO:0000250|UniProtKB:Q06609}.
DR  UNIPROT: O77507;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DR  PROSITE: PS50163;
DE  Function: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2- scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross- link repair. {ECO:0000250|UniProtKB:Q06609}.
DE  Reference Proteome: Yes;
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005815;
GO  GO:0005759;
GO  GO:0000228;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0140664;
GO  GO:0000150;
GO  GO:0003690;
GO  GO:0003697;
GO  GO:0017116;
GO  GO:0072757;
GO  GO:0006974;
GO  GO:0071479;
GO  GO:0000730;
GO  GO:0006268;
GO  GO:0000724;
GO  GO:0036297;
GO  GO:1990426;
GO  GO:0010569;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAMQMQLEANADTSVEEESFGPQPVSRLEQCGINANDVKKLEEAGFHTEEAVAYAPKKELINIKGISEAKADKILTEAAK
SQ  LVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYI
SQ  DTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSA
SQ  RQMHLARFLRMLLRLADEFGVTVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCL
SQ  PEAEAMFAINADGVGDAKD
//
ID  P78406;
PN  mRNA export factor RAE1;
GN  RAE1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:9256445}. Nucleus {ECO:0000269|PubMed:9256445}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:17172455}. Nucleus envelope {ECO:0000269|PubMed:33360543}. Note=Recruited from interphase nuclei to spindle MTs during mitosis. {ECO:0000269|PubMed:17172455}.
DR  UNIPROT: P78406;
DR  UNIPROT: A8K882;
DR  UNIPROT: O15306;
DR  UNIPROT: Q3SYL7;
DR  UNIPROT: Q5TCH8;
DR  UNIPROT: Q6V708;
DR  UNIPROT: Q9H100;
DR  UNIPROT: Q9NQM6;
DR  PDB: 3MMY;
DR  PDB: 4OWR;
DR  PDB: 7VPG;
DR  PDB: 7VPH;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 603343;
DR  DisGeNET: 8480;
DE  Function: Acts as mRNA export factor involved in nucleocytoplasmic transport (PubMed:33849972, PubMed:20498086). Plays a role in mitotic bipolar spindle formation (PubMed:17172455). May function in attaching cytoplasmic mRNPs to the cytoskeleton both directly or indirectly (PubMed:17172455). {ECO:0000269|PubMed:17172455, ECO:0000269|PubMed:20498086, ECO:0000269|PubMed:33849972}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P03519; IntAct: EBI-7228174; Score: 0.53
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-15616283; Score: 0.90
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-7193130; Score: 0.54
DE  Interaction: Q9GZR7; IntAct: EBI-736592; Score: 0.00
DE  Interaction: P31947; IntAct: EBI-7545203; Score: 0.40
DE  Interaction: Q9BUJ2; IntAct: EBI-7228381; Score: 0.40
DE  Interaction: P51784; IntAct: EBI-2511298; Score: 0.40
DE  Interaction: Q93009; IntAct: EBI-2513133; Score: 0.40
DE  Interaction: Q80U93; IntAct: EBI-2555228; Score: 0.56
DE  Interaction: Q6ZQH8; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: O95758; IntAct: EBI-7850130; Score: 0.35
DE  Interaction: P21698; IntAct: EBI-6155965; Score: 0.35
DE  Interaction: O00418; IntAct: EBI-6255330; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P21860; IntAct: EBI-8770321; Score: 0.35
DE  Interaction: Q13188; IntAct: EBI-8796543; Score: 0.35
DE  Interaction: P46937; IntAct: EBI-8796643; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-9393294; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-11003456; Score: 0.35
DE  Interaction: P80314; IntAct: EBI-11019324; Score: 0.35
DE  Interaction: Q9WTX5; IntAct: EBI-11023218; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-11051725; Score: 0.35
DE  Interaction: Q08380; IntAct: EBI-11108487; Score: 0.53
DE  Interaction: Q07797; IntAct: EBI-11108624; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q15154; IntAct: EBI-11366535; Score: 0.27
DE  Interaction: O94986; IntAct: EBI-11381405; Score: 0.27
DE  Interaction: Q6UVJ0; IntAct: EBI-11388172; Score: 0.27
DE  Interaction: Q96Q45; IntAct: EBI-11396533; Score: 0.27
DE  Interaction: Q8WUM0; IntAct: EBI-11889630; Score: 0.37
DE  Interaction: E5LBS6; IntAct: EBI-14062727; Score: 0.50
DE  Interaction: Q8IVT5; IntAct: EBI-14035332; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q7Z5H3; IntAct: EBI-21621636; Score: 0.35
DE  Interaction: Q969H0; IntAct: EBI-21645852; Score: 0.35
DE  Interaction: O43683; IntAct: EBI-21701844; Score: 0.35
DE  Interaction: Q8N302; IntAct: EBI-21776220; Score: 0.35
DE  Interaction: P49643; IntAct: EBI-21776220; Score: 0.35
DE  Interaction: P49642; IntAct: EBI-21776220; Score: 0.35
DE  Interaction: O60566; IntAct: EBI-21776220; Score: 0.35
DE  Interaction: O15488; IntAct: EBI-21849880; Score: 0.35
DE  Interaction: Q14980; IntAct: EBI-15616283; Score: 0.62
DE  Interaction: Q82506; IntAct: EBI-15620563; Score: 0.35
DE  Interaction: Q14683; IntAct: EBI-15731279; Score: 0.58
DE  Interaction: Q9UQE7; IntAct: EBI-15731297; Score: 0.35
DE  Interaction: P46663; IntAct: EBI-20803253; Score: 0.37
DE  Interaction: P41595; IntAct: EBI-20808713; Score: 0.37
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: Q9NPJ6; IntAct: EBI-25472377; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-21132926; Score: 0.67
DE  Interaction: Q63358; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568044; Score: 0.35
DE  Interaction: P0DTC6; IntAct: EBI-25491317; Score: 0.92
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: P59634; IntAct: EBI-26377272; Score: 0.78
DE  Interaction: P48431; IntAct: EBI-26574619; Score: 0.35
DE  Interaction: A0A3Q8B233; IntAct: EBI-26955178; Score: 0.35
DE  Interaction: E0XIZ7; IntAct: EBI-26955195; Score: 0.35
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P29323; IntAct: EBI-32718255; Score: 0.35
DE  Interaction: Q12824; IntAct: EBI-34581136; Score: 0.35
GO  GO:0005737;
GO  GO:0001650;
GO  GO:0097431;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0008017;
GO  GO:0003723;
GO  GO:0043130;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0071407;
GO  GO:0006406;
GO  GO:0006913;
GO  GO:0060236;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLFGTTSGFGTSGTSMFGSATTDNHNPMKDIEVTSSPDDSIGCLSFSPPTLPGNFLIAGSWANDVRCWEVQDSGQTIPK
SQ  AQQMHTGPVLDVCWSDDGSKVFTASCDKTAKMWDLSSNQAIQIAQHDAPVKTIHWIKAPNYSCVMTGSWDKTLKFWDTRS
SQ  SNPMMVLQLPERCYCADVIYPMAVVATAERGLIVYQLENQPSEFRRIESPLKHQHRCVAIFKDKQNKPTGFALGSIEGRV
SQ  AIHYINPPNPAKDNFTFKCHRSNGTNTSAPQDIYAVNGIAFHPVHGTLATVGSDGRFSFWDKDARTKLKTSEQLDQPISA
SQ  CCFNHNGNIFAYASSYDWSKGHEFYNPQKKNYIFLRNAAEELKPRNKK
//
ID  Q38942;
PN  Protein RAE1;
GN  RAE1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:21189294}.
DR  UNIPROT: Q38942;
DR  UNIPROT: Q1LYY5;
DR  UNIPROT: Q9SAJ0;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9M0V3; IntAct: EBI-1632814; Score: 0.37
GO  GO:0080008;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0003723;
GO  GO:0043130;
GO  GO:0051028;
GO  GO:0015031;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATFGAPATANSNPNKSYEVTPSPADSISSLSFSPRADILVATSWDNQVRCWEISRSGASLASAPKASISHDQPVLCSAW
SQ  KDDGTTVFSGGCDKQAKMWPLLSGGQPVTVAMHEGPIAAMAWIPGMNLLATGSWDKTLKYWDTRQQNPVHTQQLPDKCYT
SQ  LSVKHPLMVVGTADRNLIVFNLQNPQTEFKRIQSPLKYQTRCVTAFPDQQGFLVGSIEGRVGVHHLDDSQQSKNFTFKCH
SQ  RDGNDIYSVNSLNFHPVHGTFATAGSDGAFNFWDKDSKQRLKAMSRCNQPIPCSSFNHDGSIYAYAACYDWSKGAENHNP
SQ  ATAKSSIFLHLPQESEVKAKPRVGATGRK
//
ID  Q93454;
PN  mRNA export factor rae-1;
GN  rae;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12937276}. Nucleus {ECO:0000269|PubMed:22357847}. Cell projection, axon {ECO:0000269|PubMed:22357847}. Synapse {ECO:0000269|PubMed:22357847}.
DR  UNIPROT: Q93454;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC) (PubMed:12937276). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity). It is specifically important for nuclear mRNA export (PubMed:12937276). Has a role in neuronal development, where it acts downstream of rpm-1 to control axon termination and synapse formation in anterior lateral microtubule (ALM) and posterior lateral microtubule (PLM) mechanosensory neurons (PubMed:22357847). {ECO:0000250|UniProtKB:P40066, ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:22357847}.
DE  Reference Proteome: Yes;
DE  Interaction: Q17551; IntAct: EBI-6920146; Score: 0.46
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0005643;
GO  GO:0045202;
GO  GO:0003723;
GO  GO:0043130;
GO  GO:0006406;
GO  GO:0015031;
GO  GO:0006405;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGSSGFGNKSMFGGSNISTSTTTPAANTTQNDDFLVDGAPEDTIQVIKFSPTPQDKPMLACGSWDGTIRVWMFNDANTF
SQ  EGKAQQNIPAPILDIAWIEDSSKIFIACADKEARLWDLASNQVAVVGTHDGPVKTCHWINGNNYQCLMTGSFDKTLRFWD
SQ  MKNLPNQTQMAQIQLPERVYAADVLYPMAVVALANKHIKVYNLENGPTEVKDIESQLKFQIRCISIFKDKSNQNPAGFAL
SQ  GSIEGRVAVQYVDVANPKDNFTFKCHRSAELVNGFQEIYAVNDICFHPQHGTLVTIGSDGRYSMWDKDARTKLKTSEPHP
SQ  MPLTCCDVHSSGAFLVYALGYDWSRGHEGNTQPGSKIVIHKCIEDMKPRPTKK
//
ID  Q9W2E7;
PN  Protein Rae1;
GN  Rae1;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:23788425, ECO:0000269|PubMed:27494403}. Nucleus {ECO:0000269|PubMed:27494403}. Nucleus envelope {ECO:0000269|PubMed:14729268, ECO:0000269|PubMed:23788425}. Chromosome {ECO:0000269|PubMed:23788425, ECO:0000269|PubMed:28554770}. Cytoplasm {ECO:0000269|PubMed:23788425, ECO:0000269|PubMed:27494403}. Note=Dynamic pattern of localization during the spermatocyte cell cycle. Perinuclear in young primary spermatocytes. In late meiotic prophase spermatocytes, localizes to the nucleus where it co-localizes with three major chromatin clumps, and is also associated with puncta in the cytoplasm. In anaphase I and telophase I, occurs at segregating chromatin and mitochondria localized between the two daughter nuclei. In post-meiotic onion stage spermatids, mainly associates with the Nebenkern (a mitochondrial formation in the sperm) but is not detected at the nucleus. {ECO:0000269|PubMed:23788425}.
DR  UNIPROT: Q9W2E7;
DR  UNIPROT: Q7JVX4;
DR  Pfam: PF00400;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Probable component of the nuclear pore complex (NPC) which regulates the nuclear export of specific mRNAs and promotes cell cycle progression during mitosis and male meiosis (PubMed:23788425, PubMed:14729268, PubMed:27494403). Acts with Nup98-96 to promote the nuclear export of specific mRNAs such as Moe, however it does not appear to be required for general nuclear mRNA transport (PubMed:14729268, PubMed:28554770). Essential mitotic and male meiotic cell cycle regulator with roles in many aspects of the cell cycle including chromatin organization and condensation, spindle assembly, chromosome segregation, and maintaining nuclear structure (PubMed:23788425, PubMed:14729268, PubMed:27494403). During male meiosis it is required for completion of meiosis I, as well as accurate cytokinesis of the secondary spermatocytes, and postmeiotic differentiation of spermatids (PubMed:23788425). Acts as a downstream regulatory target of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway to promote mitotic cell cycle progression and proliferation during wing and eye development, and thereby plays a key role in integrating the regulation of proliferation with organ size control (PubMed:27494403, PubMed:14729268). When the Hippo/SWH signaling pathway is inactive, Rae1 acts independently of yki to increase organ size by promoting mitotic S-phase entry and increase cellular proliferation (PubMed:27494403). When the Hippo/SWH signaling pathway is active it inhibits the activity of Rae1 in a Wts-dependent manner to restrict organ growth (PubMed:27494403). However, Rae1 is also able to negatively regulate the levels and activity of yki likely by activating the core kinases of the Hippo/SWH signaling pathway hpo and Wts and increasing the protein levels of hpo, Mer and Wts; it is therefore likely that it functions as part of a negative feedback loop with the Hippo/SWH signaling pathway to regulate pathway homeostasis and prevent organ overgrowth (PubMed:27494403). Promotes mitotic cell cycle progression, at least in part, by increasing the accumulation of mitotic cyclins such as CycB, possibly by directly up-regulating cyclin transcripts or by inhibiting the anaphase promoting complex/cyclosome (APC/C) activator fzy (PubMed:27494403). Also required in presynaptic, postmitotic motor neurons to restrain synaptic terminal growth (PubMed:21874015). Promotes the expression and stability of the an E3 ubiquitin ligase of hiw, and is likely to function in the regulation of synaptic growth by binding to hiw and protecting it from autophagy- mediated degradation (PubMed:21874015). {ECO:0000269|PubMed:14729268, ECO:0000269|PubMed:21874015, ECO:0000269|PubMed:23788425, ECO:0000269|PubMed:27494403, ECO:0000269|PubMed:28554770}.
DE  Reference Proteome: Yes;
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: P18431; IntAct: EBI-9925534; Score: 0.35
GO  GO:0071944;
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0016006;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0036126;
GO  GO:0003723;
GO  GO:0043130;
GO  GO:0030154;
GO  GO:0051301;
GO  GO:0035329;
GO  GO:0007141;
GO  GO:0000278;
GO  GO:0045886;
GO  GO:1900087;
GO  GO:0010628;
GO  GO:0035332;
GO  GO:0010506;
GO  GO:0042127;
GO  GO:0048638;
GO  GO:2000045;
GO  GO:0035330;
GO  GO:0006405;
GO  GO:0007283;
GO  GO:0000972;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGATQSTNRMNDFEVASPPDDSVSALEFSPSTVQKNFLVAGSWDSTVRCWEVEQNGATVPKSMKTMGGPVLDVCWSDDG
SQ  SKVFVASCDKQVKLWDLASDQVMQVAAHDGPVKTCHMVKGPTYTCLMTGSWDKTLKFWDTRSPNPMMTINLPERCYCADV
SQ  EYPMAVVGTANRGLIIYSLQNSPTEYKRQESPLKYQHRAISIFRDKKKEPTGCALGSIEGRVAIQYVNPGNPKDNFTFKC
SQ  HRTTGTSGYQDIYAVNDIAFHPVHGTLVTVGSDGTFSFWDKDARTKLKSSETMDQSITKCGFNANGQIFAYAVGYDWSKG
SQ  HEYFNPAKKPQIFLRSCYDELKPRIN
//
ID  Q9LE82;
PN  RAN GTPase-activating protein 1;
GN  RANGAP1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus envelope {ECO:0000269|PubMed:22270916}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=Localized in patchy areas at the nuclear envelope (NE) of interphase cells. Concentrates at the preprophase band (PPB) and remains associated with the cortical division site (CDS) during mitosis and cytokinesis. During mitosis, associates with mitotic spindles at the anaphase. Associated to the microtubular phragmoplast and the surface of the daughter nuclei at the telophase.
DR  UNIPROT: Q9LE82;
DR  Pfam: PF13516;
DR  Pfam: PF13943;
DE  Function: GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state. Plays a role in spatial signaling during cell division. {ECO:0000269|PubMed:12061901, ECO:0000269|PubMed:19011093}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1779358; Score: 0.74
DE  Interaction: Q8L7E5; IntAct: EBI-1796664; Score: 0.62
DE  Interaction: Q94AV5; IntAct: EBI-1779492; Score: 0.49
DE  Interaction: Q9FH18; IntAct: EBI-1779474; Score: 0.59
DE  Interaction: Q94BX2; IntAct: EBI-4518520; Score: 0.37
DE  Interaction: Q27IK7; IntAct: EBI-15740567; Score: 0.53
DE  Interaction: Q8LDQ4; IntAct: EBI-21138999; Score: 0.35
GO  GO:0032153;
GO  GO:0009504;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0009524;
GO  GO:0005819;
GO  GO:0005096;
GO  GO:0000911;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MDHSAKTTQNRVLSVKMWPPSKSTRLMLVERMTKNITTPSIFSRKYGLLSVEEAEQDAKRIEDLAFATANKHFQNEPDGD
SQ  GTSAVHVYAKESSKLMLDVIKRGPQEESEVEVSKDGDVFFDISGGSRAFIEEEEARDLLRPLADPRNSYTKIRFSNRSFG
SQ  SEAAKFAASVLSSIKDQLTEVDLSDFVAGRPEAEALEVMNMFSSALEGSKLRYLNLSDNALGEKGIRAFASLINSQHDLE
SQ  ELYLMNDGISEDAARAVRELLPSTDKIRVLQFHNNMTGDEGATAIAEIVRECPSLEDFRCSSTRIGSEGGVALAEALEHC
SQ  SHLKKLDLRDNMFGVEGGIALAKTLSVLTHLTEIYMSYLNLEDEGTEALSEALLKSAPSLEVLELAGNDITVKSTGNLAA
SQ  CIASKQSLAKLNLSENELKDEGTILIAKAVEGHDQLVEVDLSTNMIRRAGARALAQTVVKKNTFKLLNINGNFISEEGID
SQ  EVNDMFKDCLDKLVPLDDNDPEGEDFEDEDEEEEGEDGNELESKLGSLKIKQGEE
//
ID  Q9VIW3;
PN  Ran GTPase-activating protein;
GN  RanGAP;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17032737}. Nucleus membrane {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:31626769}; Peripheral membrane protein {ECO:0000269|PubMed:17032737}; Cytoplasmic side {ECO:0000269|PubMed:17032737}. Note=Association to cytoplasmic side of the nuclear pore complex is promoted by Nup214 (PubMed:17032737). Co-localizes with Nup358/RanBP2 to annulate lamellae (PubMed:31626769). {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:31626769}.
DR  UNIPROT: Q9VIW3;
DR  UNIPROT: Q9XZI5;
DR  Pfam: PF13516;
DE  Function: GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state (By similarity). Trans-acting factor necessary for meiotic distortion (PubMed:10073941). Distortion is only seen in individuals that carry the RanGAP tandem duplication and express a RanGAP truncated protein. Binding of truncated RanGAP product to the Responder(RSP) locus initiates events that lead to sperm dysfunction (PubMed:10073941). During oogenesis, plays a role in the biogenesis of annulate lamellae containing nuclear pore complex components (PubMed:31626769). {ECO:0000250|UniProtKB:Q684P5, ECO:0000269|PubMed:10073941, ECO:0000269|PubMed:31626769}.
DE  Reference Proteome: Yes;
DE  Interaction: O77237; IntAct: EBI-277125; Score: 0.00
DE  Interaction: Q9VL21; IntAct: EBI-278977; Score: 0.00
DE  Interaction: P51521; IntAct: EBI-281659; Score: 0.00
DE  Interaction: Q9V428; IntAct: EBI-285284; Score: 0.00
DE  Interaction: Q9UKK6; IntAct: EBI-302158; Score: 0.35
DE  Interaction: Q24570; IntAct: EBI-508117; Score: 0.00
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005096;
GO  GO:0003723;
GO  GO:0031267;
GO  GO:0090630;
GO  GO:0045132;
GO  GO:0006913;
GO  GO:0043547;
GO  GO:0006611;
GO  GO:0046822;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17032737};
SQ  MSTFNFASMAAQLGQEQGISFENKVLSWNTAADVQDVVDALNKQTTVHYLNLDGNTLGVEAAKAIGEGLKRHPEFRKALW
SQ  KNMFTGRLISEIPEALKHLGAALIVAGAKLTVLDLSDNALGPNGMRGLEELLRSPVCYSLQELLLCNCGLGPEGGSMLSR
SQ  ALIDLHANANKAGFPLQLRVFIGSRNRLEDAGATEMATAFQTLKTFEEIVLEQNSIYIEGVEALAESFKHNPHLRVLNMN
SQ  DNTLKSEGAEKIAEALPFLPLLREMSFGDCLIKTNGAYHFGEALERGNERLEVIDLGFNEINSDGGLVLVNAMGNKPKLR
SQ  ILNLDGNSFGEEGSEKIISEMSKLPTAAALQPFQHQEEEDLEDEYQADKQDADYEEEEEVHEHANDTTEEADEDSEGDED
SQ  DEEDEGDEEYSNVAEETAYVTTNAYTTKLFNDTTNSMASETFAVANKTISQKCTPEKFCLSQKPCSQEDFDSLDMDNKLE
SQ  ALQSIVNQFTGDNHLLLLVFTTLKCAHLSQSSKAALDLAVSLYQATFDYAIKTKQETRVLNYVLMQLRLLPCKEVFHSDY
SQ  DVKNCRFALREALKQPTFANDNIKNSFKTFLEGAES
//
ID  P46060;
PN  Ran GTPase-activating protein 1;
GN  RANGAP1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15037602, ECO:0000305|PubMed:8146159}. Nucleus, nucleoplasm {ECO:0000269|PubMed:8146159}. Nucleus envelope {ECO:0000269|PubMed:11854305, ECO:0000269|PubMed:15037602}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11854305}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11854305, ECO:0000269|PubMed:15037602}. Note=Cytoplasmic during interphase. Detected at the nuclear envelope during interphase (PubMed:11854305, PubMed:15037602). Targeted to the nuclear pores after sumoylation (PubMed:11854305). During mitosis, associates with mitotic spindles, but is essentially not detected at the spindle poles (PubMed:11854305, PubMed:15037602). Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase (PubMed:11854305). Mitotic location also requires sumoylation (PubMed:11854305). {ECO:0000269|PubMed:11854305, ECO:0000269|PubMed:15037602}.
DR  UNIPROT: P46060;
DR  UNIPROT: Q96JJ2;
DR  PDB: 1Z5S;
DR  PDB: 2GRN;
DR  PDB: 2GRO;
DR  PDB: 2GRP;
DR  PDB: 2GRQ;
DR  PDB: 2GRR;
DR  PDB: 2IO2;
DR  PDB: 2IO3;
DR  PDB: 2IY0;
DR  PDB: 3UIN;
DR  PDB: 3UIO;
DR  PDB: 3UIP;
DR  PDB: 5D2M;
DR  Pfam: PF13516;
DR  Pfam: PF07834;
DR  OMIM: 602362;
DR  DisGeNET: 5905;
DE  Function: GTPase activator for RAN (PubMed:8146159, PubMed:8896452, PubMed:16428860). Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export (PubMed:8896452, PubMed:27160050). Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (PubMed:27160050). {ECO:0000269|PubMed:16428860, ECO:0000269|PubMed:27160050, ECO:0000269|PubMed:8146159, ECO:0000269|PubMed:8896452}.
DE  Reference Proteome: Yes;
DE  Interaction: O14524; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: A0JLT2; IntAct: EBI-394580; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-7036111; Score: 0.95
DE  Interaction: P60520; IntAct: EBI-1064937; Score: 0.00
DE  Interaction: Q9HC24; IntAct: EBI-1065758; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1074789; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-1077160; Score: 0.00
DE  Interaction: Q9Y478; IntAct: EBI-1081606; Score: 0.00
DE  Interaction: P63165; IntAct: EBI-7036555; Score: 0.96
DE  Interaction: P55854; IntAct: EBI-1210650; Score: 0.00
DE  Interaction: P32121; IntAct: EBI-1642567; Score: 0.35
DE  Interaction: Q8IY92; IntAct: EBI-2371263; Score: 0.35
DE  Interaction: Q9NWV8; IntAct: EBI-2514464; Score: 0.40
DE  Interaction: Q9ERU9; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: Q9QWT9; IntAct: EBI-2558911; Score: 0.40
DE  Interaction: Q07832; IntAct: EBI-2560950; Score: 0.40
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: P08754; IntAct: EBI-3930105; Score: 0.37
DE  Interaction: P63096; IntAct: EBI-3930075; Score: 0.44
DE  Interaction: P13501; IntAct: EBI-3933514; Score: 0.37
DE  Interaction: Q9UBU9; IntAct: EBI-6262548; Score: 0.53
DE  Interaction: Q9UBE8; IntAct: EBI-6381385; Score: 0.35
DE  Interaction: Q9Y2T1; IntAct: EBI-8993980; Score: 0.37
DE  Interaction: Q96QB1; IntAct: EBI-8994097; Score: 0.37
DE  Interaction: Q15198; IntAct: EBI-8994216; Score: 0.37
DE  Interaction: Q13043; IntAct: EBI-10049645; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: Q99853; IntAct: EBI-11317404; Score: 0.35
DE  Interaction: O00358; IntAct: EBI-11317831; Score: 0.35
DE  Interaction: Q9UPW0; IntAct: EBI-11318497; Score: 0.35
DE  Interaction: Q12952; IntAct: EBI-11318689; Score: 0.35
DE  Interaction: Q9C009; IntAct: EBI-11319301; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11319716; Score: 0.46
DE  Interaction: Q06330; IntAct: EBI-11320091; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-11016929; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-11030093; Score: 0.35
DE  Interaction: P62627; IntAct: EBI-11032607; Score: 0.35
DE  Interaction: O75787; IntAct: EBI-11037152; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q8CBY8; IntAct: EBI-11074062; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q5EG47; IntAct: EBI-11114972; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-14035152; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: P18754; IntAct: EBI-21567271; Score: 0.35
DE  Interaction: P61769; IntAct: EBI-21675069; Score: 0.35
DE  Interaction: Q8N3R9; IntAct: EBI-21911830; Score: 0.35
DE  Interaction: Q9P0U3; IntAct: EBI-15611754; Score: 0.59
DE  Interaction: P61956; IntAct: EBI-15612001; Score: 0.75
DE  Interaction: Q9HC62; IntAct: EBI-15612044; Score: 0.59
DE  Interaction: Q921C5; IntAct: EBI-15847893; Score: 0.35
DE  Interaction: Q9BTM9; IntAct: EBI-15902832; Score: 0.35
DE  Interaction: Q08345; IntAct: EBI-22227061; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: Q96JN8; IntAct: EBI-16813376; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P03427; IntAct: EBI-25769583; Score: 0.37
DE  Interaction: Q96NK8; IntAct: EBI-20917522; Score: 0.40
DE  Interaction: Q92794; IntAct: EBI-20928992; Score: 0.40
DE  Interaction: Q15172; IntAct: EBI-20937820; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: Q9NQB0; IntAct: EBI-21265942; Score: 0.35
DE  Interaction: P49768; IntAct: EBI-21132675; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-21132926; Score: 0.67
DE  Interaction: P49792; IntAct: EBI-21928721; Score: 0.62
DE  Interaction: Q15052; IntAct: EBI-25409952; Score: 0.35
DE  Interaction: Q8WUY9; IntAct: EBI-25411615; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P22492; IntAct: EBI-25479342; Score: 0.35
DE  Interaction: Q9H3R0; IntAct: EBI-25479978; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574478; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610849; Score: 0.40
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: Q96QK1; IntAct: EBI-27081274; Score: 0.35
DE  Interaction: O75582; IntAct: EBI-28931316; Score: 0.35
DE  Interaction: P11274; IntAct: EBI-28931791; Score: 0.35
DE  Interaction: P53350; IntAct: EBI-28938281; Score: 0.35
DE  Interaction: Q96GD4; IntAct: EBI-28944360; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q05D32; IntAct: EBI-27113232; Score: 0.35
GO  GO:0016235;
GO  GO:1904115;
GO  GO:0005737;
GO  GO:1990723;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043231;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0106068;
GO  GO:0045296;
GO  GO:0005096;
GO  GO:0003723;
GO  GO:0031267;
GO  GO:0031625;
GO  GO:0090630;
GO  GO:1904117;
GO  GO:0046826;
GO  GO:0051168;
GO  GO:0006913;
GO  GO:0016925;
GO  GO:0048678;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASEDIAKLAETLAKTQVAGGQLSFKGKSLKLNTAEDAKDVIKEIEDFDSLEALRLEGNTVGVEAARVIAKALEKKSELK
SQ  RCHWSDMFTGRLRTEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVQGFEALLKSSACFTLQELKLNNCGMGIGGGK
SQ  ILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFRVIGTLEEVHMPQNGINHPGITALAQAFAVNPLLRV
SQ  INLNDNTFTEKGAVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAIRGGLPKLKELNLSFCEIKRDAALAVAEAMADK
SQ  AELEKLDLNGNTLGEEGCEQLQEVLEGFNMAKVLASLSDDEDEEEEEEGEEEEEEAEEEEEEDEEEEEEEEEEEEEEPQQ
SQ  RGQGEKSATPSRKILDPNTGEPAPVLSSPPPADVSTFLAFPSPEKLLRLGPKSSVLIAQQTDTSDPEKVVSAFLKVSSVF
SQ  KDEATVRMAVQDAVDALMQKAFNSSSFNSNTFLTRLLVHMGLLKSEDKVKAIANLYGPLMALNHMVQQDYFPKALAPLLL
SQ  AFVTKPNSALESCSFARHSLLQTLYKV
//
ID  P46061;
PN  Ran GTPase-activating protein 1;
GN  Rangap1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Nucleus, nucleoplasm {ECO:0000269|PubMed:26506250}. Nucleus envelope {ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P46060}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P46060}. Note=Cytoplasmic during interphase (PubMed:26506250). Detected at the nuclear envelope during interphase (PubMed:9442102, PubMed:9456312, PubMed:26506250). Shuttles between nucleus and cytoplasm (PubMed:26506250). Targeted to the nuclear pores after sumoylation. During mitosis, associates with mitotic spindles, but is essentially not detected at the spindle poles. Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase. Mitotic location also requires sumoylation (By similarity). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}.
DR  UNIPROT: P46061;
DR  UNIPROT: Q60801;
DR  UNIPROT: Q6NZB5;
DR  PDB: 1KPS;
DR  Pfam: PF13516;
DR  Pfam: PF07834;
DE  Function: GTPase activator for RAN. Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export (PubMed:18305100). Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (By similarity). Required for postimplantation embryonic development (PubMed:8314081). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:8314081}.
DE  Reference Proteome: Yes;
DE  Interaction: P35922; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-1033068; Score: 0.44
DE  Interaction: Q80Z64; IntAct: EBI-8820601; Score: 0.35
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: Q9EPK7; IntAct: EBI-17172030; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
GO  GO:0016235;
GO  GO:1904115;
GO  GO:0005737;
GO  GO:1990723;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0043231;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0106068;
GO  GO:0005096;
GO  GO:0003723;
GO  GO:0031267;
GO  GO:0031625;
GO  GO:0090630;
GO  GO:0071375;
GO  GO:1904117;
GO  GO:0046826;
GO  GO:0051168;
GO  GO:0006913;
GO  GO:0016925;
GO  GO:0048678;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASEDIAKLAETLAKTQVAGGQLSFKGKGLKLNTAEDAKDVIKEIEEFDGLEALRLEGNTVGVEAARVIAKALEKKSELK
SQ  RCHWSDMFTGRLRSEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVRGFEALLKSPACFTLQELKLNNCGMGIGGGK
SQ  ILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFGIIGTLEEVHMPQNGINHPGVTALAQAFAINPLLRV
SQ  INLNDNTFTEKGGVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAVRGGLPKLKELNLSFCEIKRDAALVVAEAVADK
SQ  AELEKLDLNGNALGEEGCEQLQEVMDSFNMAKVLASLSDDEGEDEDEEEEGEEDDEEEEDEEDEEDDDEEEEEQEEEEEP
SQ  PQRGSGEEPATPSRKILDPNSGEPAPVLSSPTPTDLSTFLSFPSPEKLLRLGPKVSVLIVQQTDTSDPEKVVSAFLKVAS
SQ  VFRDDASVKTAVLDAIDALMKKAFSCSSFNSNTFLTRLLIHMGLLKSEDKIKAIPSLHGPLMVLNHVVRQDYFPKALAPL
SQ  LLAFVTKPNGALETCSFARHNLLQTLYNI
//
ID  O13066;
PN  Ran GTPase-activating protein 1;
GN  rangap1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P46060}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P46060}. Nucleus envelope {ECO:0000250|UniProtKB:P46060}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P46060}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P46060}. Note=Cytoplasmic during interphase. Detected at the nuclear envelope during interphase. Targeted to the nuclear pores after sumoylation. During mitosis, associates with mitotic spindles, but is essentially not detected at the spindle poles. Mitotic location also requires sumoylation. {ECO:0000250|UniProtKB:P46060}.
DR  UNIPROT: O13066;
DR  Pfam: PF13516;
DR  Pfam: PF07834;
DE  Function: GTPase activator for RAN, converting it to the GDP-bound state (PubMed:9108047). Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is required for RAN-mediated nuclear import and export (By similarity). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:9108047}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005819;
GO  GO:0005096;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAEDIAQLADCLAKANVGDGELSFKGKTLKLNTAQDAEEVIREIEEYEGLQALRLEGNTVGVEAAKAIAEVLQRKPDLK
SQ  RCHWSDMFTGRLRPEIPTALRSLGDALITAGAQLTELDLSDNAFGPDGVRGFEALLKSPTCFTLQELKLNNCGMGIGGGK
SQ  ILAAALTECHKKSSAHGKPLALKVFIAGRNRLENDGATALSEAFRLIGTLEEVHMPQNGINHAGITALAESFKANSLLKV
SQ  INLNDNTFTEKGGVAMAEALKTLRQVEVINFGDCLVRSKGAQAIASALKEGLHKLKDLNLSYCEIKADAAVSLAESVEDK
SQ  SDLEKLDLNGNCLGEEGCEQVQEILESINMANILGSLSDDEDEDDDDDDEDDDDDEDDENDDEEVEEEEEEVEEEEGGDN
SQ  ENKEKSKEIPCLSGSAPASPPKLPVDASTFLSFPSPEKLVRMGPRRSAMIAQQVNVADTEKVVQAFIQVSSVYREDGEIK
SQ  AAVEETIDGLMKEAFENRGFQANVFITSLLVQMGLLKSEDKMKTIPHLNGPLLTLNHMVQQNYFPKSLASTLLAFISKPN
SQ  GVLENNASARHTLLCNLHNL
//
ID  Q9M651;
PN  RAN GTPase-activating protein 2;
GN  RANGAP2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=Localized in patchy areas at the nuclear envelope of interphase cells. During mitosis, associates with mitotic spindles at the anaphase. Associated to the microtubular phragmoplast and the surface of the daughter nuclei at the telophase.
DR  UNIPROT: Q9M651;
DR  Pfam: PF13516;
DR  Pfam: PF13943;
DE  Function: GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state. {ECO:0000269|PubMed:12061901}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1779572; Score: 0.37
DE  Interaction: Q8L7E5; IntAct: EBI-1796671; Score: 0.37
DE  Interaction: Q9FH18; IntAct: EBI-1779579; Score: 0.37
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0009524;
GO  GO:0000325;
GO  GO:0009536;
GO  GO:0005819;
GO  GO:0005096;
GO  GO:0006913;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MADILDSRPHAFSIKLWPPSLPTRKALIERITNNFSSKTIFTEKYGSLTKDQATENAKRIEDIAFSTANQQFEREPDGDG
SQ  GSAVQLYAKECSKLILEVLKKGPVAKVAARELISEDSVSPRETFFDISKGKRAFIEAEEAEELLKPLKEPGNAYTKICFS
SQ  NRSFGLGAARVAEPILASLKDQLKEVDLSDFVAGRPELEALEVMNIFSDALQGSILSSLNLSDNALGEKGVRAFGALLKS
SQ  LSSLEELYLMNDGISKEAAQAVSELIPSTENLRVLHFHNNMTGDEGALAIAEVVKRSPLLENFRCSSTRVGSKGGIALSE
SQ  ALEHCTHMEKLDLRDNMFGTEAGVSLSKTLSSFKHMTELYLSYLNLEDEGAIAIVNALKESASPIEVLEMAGNDITVEAA
SQ  SAIAACVAAKQDLNKLNLSENELKDEGCVQIANCIEEGHSKLQYIDMSTNYIRRAGARALAHVVVKKEAFKLLNIDGNII
SQ  SEEGIEELKEIFKKSPELLGALDENDPDGEEDDDDEEDEEDEENEGNGNGELESKLKNLEVNQED
//
ID  Q5U651;
PN  Ras-interacting protein 1;
GN  RASIP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15031288}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:15031288}. Note=Associated with perinuclear vesicles. Is recruited to Golgi stacks by activated HRAS.
DR  UNIPROT: Q5U651;
DR  UNIPROT: Q6U676;
DR  PDB: 5KHO;
DR  PDB: 5KHQ;
DR  Pfam: PF01843;
DR  Pfam: PF00788;
DR  PROSITE: PS51126;
DR  PROSITE: PS50200;
DR  OMIM: 609623;
DR  DisGeNET: 54922;
DE  Function: Required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. Acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Regulates the activity of Rho GTPases in part by recruiting ARHGAP29 and suppressing RhoA signaling and dampening ROCK and MYH9 activities in endothelial cells (By similarity). May act as effector for Golgi-bound HRAS and other Ras- like proteins. May promote HRAS-mediated transformation. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000250, ECO:0000269|PubMed:15031288, ECO:0000269|PubMed:22354037}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5NI89; IntAct: EBI-2797128; Score: 0.00
DE  Interaction: A0A0H2W4P6; IntAct: EBI-2856635; Score: 0.00
DE  Interaction: Q8N6T3; IntAct: EBI-3924759; Score: 0.37
DE  Interaction: P60953; IntAct: EBI-11002356; Score: 0.35
DE  Interaction: Q9H0H5; IntAct: EBI-11003256; Score: 0.35
DE  Interaction: O95229; IntAct: EBI-11007376; Score: 0.35
DE  Interaction: Q9H4P4; IntAct: EBI-11011881; Score: 0.35
DE  Interaction: Q7TSY8; IntAct: EBI-11024934; Score: 0.35
DE  Interaction: Q9DC28; IntAct: EBI-11075774; Score: 0.35
DE  Interaction: Q9JLB0; IntAct: EBI-11079122; Score: 0.35
DE  Interaction: Q9NVK5; IntAct: EBI-11131799; Score: 0.35
DE  Interaction: Q9BRV8; IntAct: EBI-11132072; Score: 0.35
DE  Interaction: O95817; IntAct: EBI-11135110; Score: 0.35
DE  Interaction: Q99PU7; IntAct: EBI-11138635; Score: 0.35
DE  Interaction: Q14103; IntAct: EBI-11152836; Score: 0.35
DE  Interaction: O43684; IntAct: EBI-11163266; Score: 0.35
DE  Interaction: Q6NYC8; IntAct: EBI-21774730; Score: 0.35
DE  Interaction: O43679; IntAct: EBI-15690604; Score: 0.37
DE  Interaction: P23528; IntAct: EBI-20904352; Score: 0.40
GO  GO:0005911;
GO  GO:0005795;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0051020;
GO  GO:0042803;
GO  GO:0001525;
GO  GO:0048754;
GO  GO:0010507;
GO  GO:1905709;
GO  GO:0035024;
GO  GO:2000299;
GO  GO:0033625;
GO  GO:0043087;
GO  GO:0007165;
GO  GO:0001570;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLSGERKEGGSPRFGKLHLPVGLWINSPRKQLAKLGRRWPSAASVKSSSSDTGSRSSEPLPPPPPHVELRRVGAVKAAGG
SQ  ASGSRAKRISQLFRGSGTGTTGSSGAGGPGTPGGAQRWASEKKLPELAAGVAPEPPLATRATAPPGVLKIFGAGLASGAN
SQ  YKSVLATARSTARELVAEALERYGLAGSPGGGPGESSCVDAFALCDALGRPAAAGVGSGEWRAEHLRVLGDSERPLLVQE
SQ  LWRARPGWARRFELRGREEARRLEQEAFGAADSEGTGAPSWRPQKNRSRAASGGAALASPGPGTGSGAPAGSGGKERSEN
SQ  LSLRRSVSELSLQGRRRRQQERRQQALSMAPGAADAQIGTADPGDFDQLTQCLIQAPSNRPYFLLLQGYQDAQDFVVYVM
SQ  TREQHVFGRGGNSSGRGGSPAPYVDTFLNAPDILPRHCTVRAGPEHPAMVRPSRGAPVTHNGCLLLREAELHPGDLLGLG
SQ  EHFLFMYKDPRTGGSGPARPPWLPARPGATPPGPGWAFSCRLCGRGLQERGEALAAYLDGREPVLRFRPREEEALLGEIV
SQ  RAAAAGSGDLPPLGPATLLALCVQHSARELELGHLPRLLGRLARLIKEAVWEKIKEIGDRQPENHPEGVPEVPLTPEAVS
SQ  VELRPLMLWMANTTELLSFVQEKVLEMEKEADQEDPQLCNDLELCDEAMALLDEVIMCTFQQSVYYLTKTLYSTLPALLD
SQ  SNPFTAGAELPGPGAELGAMPPGLRPTLGVFQAALELTSQCELHPDLVSQTFGYLFFFSNASLLNSLMERGQGRPFYQWS
SQ  RAVQIRTNLDLVLDWLQGAGLGDIATEFFRKLSMAVNLLCVPRTSLLKASWSSLRTDHPTLTPAQLHHLLSHYQLGPGRG
SQ  PPAAWDPPPAEREAVDTGDIFESFSSHPPLILPLGSSRLRLTGPVTDDALHRELRRLRRLLWDLEQQELPANYRHGPPVA
SQ  TSP
//
ID  Q3U0S6;
PN  Ras-interacting protein 1;
GN  Rasip1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Note=Associated with perinuclear vesicles. Is recruited to Golgi stacks by activated HRAS (By similarity). {ECO:0000250}.
DR  UNIPROT: Q3U0S6;
DR  UNIPROT: E9QLI7;
DR  UNIPROT: Q6GQW4;
DR  Pfam: PF01843;
DR  Pfam: PF00788;
DR  PROSITE: PS51126;
DR  PROSITE: PS50200;
DE  Function: Required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. Acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Regulates the activity of Rho GTPases in part by recruiting ARHGAP29 and suppressing RhoA signaling and dampening ROCK and MYH9 activities in endothelial cells. May act as effector for Golgi-bound HRAS and other Ras-like proteins. May promote HRAS-mediated transformation. Negative regulator of amino acid starvation-induced autophagy (By similarity). {ECO:0000250, ECO:0000269|PubMed:19272373, ECO:0000269|PubMed:21396893}.
DE  Reference Proteome: Yes;
GO  GO:0005911;
GO  GO:0005794;
GO  GO:0005795;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0051020;
GO  GO:0042803;
GO  GO:0031267;
GO  GO:0001525;
GO  GO:0048754;
GO  GO:0010507;
GO  GO:1905709;
GO  GO:0035024;
GO  GO:2000299;
GO  GO:0008284;
GO  GO:0033625;
GO  GO:0043087;
GO  GO:0007165;
GO  GO:0001570;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLSGERKEGGSPRFGKLHLPVGLWINSPRKQLAKLGRRWPSAASVKSSSSDTGSRSSEPLPPPPPPPHVELRRVGAVKAA
SQ  GGASGSRAKRISQLFRGSGAGGAGGPGTPGGAQRWASEKKLPELAAGVAPEPPLPTRAAVPPGVLKIFASGLASGANYKS
SQ  VLATERSTARELVAEALERYGLTGGRGAGDSGCVDAYALCDALGRPAVGVGGGEWRAEHLRVLADAERPLLVQDLWRARP
SQ  GWARRFELRGREEARRLEQEAFGAADADGTNAPSWRTQKNRSRAASGGAALASPGPGSGSGTPTGSGGKERSENLSLRRS
SQ  VSELSLQGRRRRQQERRQQALSMAPGAADAQMVPTDPGDFDQLTQCLIQAPSNRPYFLLLQGYQDAQDFVVYVMTREQHV
SQ  FGRGGPSSSRGGSPAPYVDTFLNAPDILPRHCTVRAGPEPPAMVRPSRGAPVTHNGCLLLREAELHPGDLLGLGEHFLFM
SQ  YKDPRSGGSGPARPSWLPARPGAAPPGPGWAFSCRLCGRGLQERGEALAAYLDGREPVLRFRPREEEALLGEIVRAAASG
SQ  AGDLPPLGPATLLALCVQHSARELELGHLPRLLGRLARLIKEAVWEKIKEIGDRQPENHPEGVPEVPLTPEAVSVELRPL
SQ  ILWMANTTELLSFVQEKVLEMEKEADQEGLSSDPQLCNDLELCDEALALLDEVIMCTFQQSVYYLTKTLYSTLPALLDSN
SQ  PFTAGAELPGPGAELEAMPPGLRPTLGVFQAALELTSQCELHPDLVSQTFGYLFFFSNASLLNSLMERGQGRPFYQWSRA
SQ  VQIRTNLDLVLDWLQGAGLGDIATEFFRKLSIAVNLLCVPRTSLLKASWSSLRTDYPTLTPAQLHHLLSHYQLGPGRGPP
SQ  PAWDPPPAERDAVDTGDIFESFSSHPPLILPLGSSRLRLTGPVTDDALHRELRRLRRLLWDLEQQELPANHRHGPPVAST
SQ  P
//
ID  P41917;
PN  GTP-binding nuclear protein Ran-2;
GN  RAN2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:17530257}. Nucleus envelope {ECO:0000269|PubMed:17530257}. Note=Localized in the perinuclear region with the highest concentration at the nuclear envelope at the interphase.
DR  UNIPROT: P41917;
DR  UNIPROT: Q0WVD9;
DR  UNIPROT: Q94K33;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8RWG8; IntAct: EBI-2325944; Score: 0.37
DE  Interaction: Q9LMK7; IntAct: EBI-2325973; Score: 0.37
DE  Interaction: Q9SHQ6; IntAct: EBI-12596165; Score: 0.40
DE  Interaction: F4K567; IntAct: EBI-12596177; Score: 0.40
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0009536;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0003729;
GO  GO:0006606;
GO  GO:0000054;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALPNQQTVDYPSFKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGVEVHPLDFFTNCGKIRFYCWDTAGQEKFGGLRD
SQ  GYYIHGQCAIIMFDVTARLTYKNVPTWHRDLCRVCENIPIVLCGNKVDVKNRQVKAKQVTFHRKKNLQYYEISAKSNYNF
SQ  EKPFLYLARKLAGDQNLHFVESPALAPPEVHLDIAAQQQNEADLAAAAAQPLPDDDDDAFE
//
ID  F4HYD7;
PN  Ran-binding protein M homolog;
GN  RANBPM;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:22676313}. Nucleus {ECO:0000269|PubMed:22676313}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22676313}. Note=Associates predominantly in the form of large cytoplasmic complexes. {ECO:0000269|PubMed:22676313}.
DR  UNIPROT: F4HYD7;
DR  UNIPROT: Q8VYQ8;
DR  UNIPROT: Q9C8P9;
DR  Pfam: PF10607;
DR  Pfam: PF00622;
DR  PROSITE: PS50188;
DR  PROSITE: PS50897;
DR  PROSITE: PS50896;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0007166;
GO  GO:0007010;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNSSPPPANSANGDTTNNGENGQDLNLNFLDKIRLSAKRDAKEDEGEELPTELNTINSAGGFLVVSPDKLSVKYTNTNLH
SQ  GHDVGVVQANKPAPIKCLTYYFEIFVKDSGIKGQIAIGFTKESFKMRRQPGWEVNSCGYHGDDGYLYRGQGKGEPFGPKF
SQ  TKDDAVGGGINYASQEFFFTKNGTIVGKIPKDIRGHLFPTVAVHSQNEEVLVNFGKKKFAFDIKGYEASERNKQQLAIEK
SQ  ISIPPNIGYGLVKTYLLHYGYEETLDAFNLATKNTVPPIHIDQENAIDEDDSSYALKQRKNLRQLVRNGEIDTALAELQK
SQ  LYPQIVQDDKSVVCFLLHCQKFIELVRVGKLEEGVNYGRLELAKFVGLTGFQDIVEDCFALLAYEKPEESSVWYFLEDSQ
SQ  RELVADAVNAAILSTNPNKKDVQRSCHLQSHLEKLLRQLTVCCLERRSLNGDQGETFRLRHVLNNNR
//
ID  Q3T054;
PN  GTP-binding nuclear protein Ran;
GN  RAN;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Melanosome {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: Q3T054;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0042470;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0055037;
GO  GO:0042565;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0070883;
GO  GO:0046982;
GO  GO:0030036;
GO  GO:0051301;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0032092;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:1902570;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0000054;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYY
SQ  IQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
//
ID  P62825;
PN  GTP-binding nuclear protein Ran;
GN  RAN;
OS  9615;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Melanosome {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: P62825;
DR  UNIPROT: P17080;
DR  UNIPROT: P28746;
DR  UNIPROT: P28747;
DR  UNIPROT: Q9CSP3;
DR  UNIPROT: Q9CWI7;
DR  UNIPROT: Q9CZA2;
DR  UNIPROT: Q9UDJ5;
DR  UNIPROT: Q9UEU9;
DR  PDB: 1A2K;
DR  PDB: 1BYU;
DR  PDB: 1QG2;
DR  PDB: 1QG4;
DR  PDB: 1WA5;
DR  PDB: 2BKU;
DR  PDB: 3A6P;
DR  PDB: 3RAN;
DR  PDB: 3W3Z;
DR  PDB: 5BXQ;
DR  PDB: 5YU6;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
DE  Interaction: P61972; IntAct: EBI-1026859; Score: 0.44
DE  Interaction: P33307; IntAct: EBI-1041382; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0042470;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0016442;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0005049;
GO  GO:0070883;
GO  GO:1905172;
GO  GO:0051301;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0046827;
GO  GO:0035281;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0000054;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYY
SQ  IQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
//
ID  Q7ZZX9;
PN  GTP-binding nuclear protein Ran;
GN  ran;
OS  7957;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: Q7ZZX9;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0006606;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAENEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKYNVWDTAGQEKFGGLRDGYYI
SQ  QAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPF
SQ  LWLARKLIGDPNLEFVEMSALAPPEIAMDPSLAAQYEHDLKVASETALPDEDDDL
//
ID  P42558;
PN  GTP-binding nuclear protein Ran;
GN  RAN;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: P42558;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0055037;
GO  GO:0042565;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0070883;
GO  GO:0046982;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0032092;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:1902570;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0000054;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYY
SQ  IQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEQDLQIAQTTALPDEDDDL
//
ID  P79735;
PN  GTP-binding nuclear protein Ran;
GN  ran;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: P79735;
DR  UNIPROT: Q7ZU75;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0003407;
GO  GO:0006606;
GO  GO:0060041;
GO  GO:0000054;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAENEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGAIKYNVWDTAGQEKFGGLRDGYYI
SQ  QAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPF
SQ  LWLARKLIGDPNLEFVEMPALAPPEIAMDPTLAAQYEHDLKVASETALPDEDDDL
//
ID  Q9VZ23;
PN  GTP-binding nuclear protein Ran;
GN  Ran;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:12121620}. Nucleus envelope {ECO:0000269|PubMed:12121620}. Cytoplasm {ECO:0000269|PubMed:12121620, ECO:0000305|PubMed:12653959}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12121620}. Note=Localizes around the microtubule spindle during mitosis. {ECO:0000269|PubMed:12121620}.
DR  UNIPROT: Q9VZ23;
DR  UNIPROT: Q9NH14;
DR  UNIPROT: Q9NHN9;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis (By similarity). GTP-bound Ran modulates both spindle and nuclear envelope assembly, supporting a role during mitosis (PubMed:12121620). During oogenesis, modulates formation of Nup358- containing granules and biogenesis of the nuclear pore complex probably by mediating the transport of their components along microtubules (PubMed:31626769). {ECO:0000250|UniProtKB:P62826, ECO:0000269|PubMed:12121620, ECO:0000269|PubMed:31626769}.
DE  Reference Proteome: Yes;
DE  Interaction: P07182; IntAct: EBI-234142; Score: 0.00
DE  Interaction: O62619; IntAct: EBI-234147; Score: 0.00
DE  Interaction: Q9W1A4; IntAct: EBI-464026; Score: 0.40
DE  Interaction: M9NFI9; IntAct: EBI-9933573; Score: 0.46
DE  Interaction: P31409; IntAct: EBI-9968286; Score: 0.35
DE  Interaction: Q9VS59; IntAct: EBI-10130282; Score: 0.37
DE  Interaction: Q9W3Z4; IntAct: EBI-15167671; Score: 0.49
DE  Interaction: Q0IGU0; IntAct: EBI-15167651; Score: 0.49
DE  Interaction: Q7K4C7; IntAct: EBI-26695047; Score: 0.49
DE  Interaction: Q9VWA6; IntAct: EBI-26695057; Score: 0.49
DE  Interaction: A8JNG7; IntAct: EBI-26695077; Score: 0.49
GO  GO:0005938;
GO  GO:0005737;
GO  GO:1990498;
GO  GO:0042564;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0046872;
GO  GO:0051301;
GO  GO:0000132;
GO  GO:0006886;
GO  GO:0000212;
GO  GO:0051168;
GO  GO:0051292;
GO  GO:0043243;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0007346;
GO  GO:0032880;
GO  GO:0000054;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQEGQDIPTFKCVLVGDGGTGKTTFVKRHMTGEFEKKYVATLGVEVHPLIFHTNRGAIRFNVWDTAGQEKFGGLRDGYY
SQ  IQGQCAVIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLVGDPNLEFVAMPALLPPEVKMDKDWQAQIERDLQEAQATALPDEDEEL
//
ID  P62826;
PN  GTP-binding nuclear protein Ran;
GN  RAN;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:1961752, ECO:0000269|PubMed:19753112, ECO:0000269|PubMed:31075303, ECO:0000269|PubMed:8421051, ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9351834, ECO:0000269|PubMed:9822603}. Nucleus envelope {ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9822603}. Cytoplasm, cytosol {ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:8276887}. Cytoplasm {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:9822603}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Predominantly nuclear during interphase (PubMed:8421051, PubMed:12194828, PubMed:10679025). Becomes dispersed throughout the cytoplasm during mitosis (PubMed:8421051, PubMed:12194828). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:8421051}.
DR  UNIPROT: P62826;
DR  UNIPROT: A8K3Z8;
DR  UNIPROT: P17080;
DR  UNIPROT: P28746;
DR  UNIPROT: P28747;
DR  UNIPROT: Q6IPB2;
DR  UNIPROT: Q86V08;
DR  UNIPROT: Q8NI90;
DR  UNIPROT: Q9CSP3;
DR  UNIPROT: Q9CWI7;
DR  UNIPROT: Q9CZA2;
DR  UNIPROT: Q9UDJ5;
DR  UNIPROT: Q9UEU9;
DR  PDB: 1I2M;
DR  PDB: 1IBR;
DR  PDB: 1K5D;
DR  PDB: 1K5G;
DR  PDB: 1QBK;
DR  PDB: 1RRP;
DR  PDB: 2MMC;
DR  PDB: 2MMG;
DR  PDB: 2N1B;
DR  PDB: 3CH5;
DR  PDB: 3EA5;
DR  PDB: 3GJ0;
DR  PDB: 3GJ3;
DR  PDB: 3GJ4;
DR  PDB: 3GJ5;
DR  PDB: 3GJ6;
DR  PDB: 3GJ7;
DR  PDB: 3GJ8;
DR  PDB: 3GJX;
DR  PDB: 3NBY;
DR  PDB: 3NBZ;
DR  PDB: 3NC0;
DR  PDB: 3NC1;
DR  PDB: 3ZJY;
DR  PDB: 4C0Q;
DR  PDB: 4GMX;
DR  PDB: 4GPT;
DR  PDB: 4HAT;
DR  PDB: 4HAU;
DR  PDB: 4HAV;
DR  PDB: 4HAW;
DR  PDB: 4HAX;
DR  PDB: 4HAY;
DR  PDB: 4HAZ;
DR  PDB: 4HB0;
DR  PDB: 4HB2;
DR  PDB: 4HB3;
DR  PDB: 4HB4;
DR  PDB: 4OL0;
DR  PDB: 4WVF;
DR  PDB: 5CIQ;
DR  PDB: 5CIT;
DR  PDB: 5CIW;
DR  PDB: 5CJ2;
DR  PDB: 5CLL;
DR  PDB: 5CLQ;
DR  PDB: 5DH9;
DR  PDB: 5DHA;
DR  PDB: 5DHF;
DR  PDB: 5DI9;
DR  PDB: 5DIF;
DR  PDB: 5DIS;
DR  PDB: 5DLQ;
DR  PDB: 5FYQ;
DR  PDB: 5JLJ;
DR  PDB: 5UWH;
DR  PDB: 5UWI;
DR  PDB: 5UWJ;
DR  PDB: 5UWO;
DR  PDB: 5UWP;
DR  PDB: 5UWQ;
DR  PDB: 5UWR;
DR  PDB: 5UWS;
DR  PDB: 5UWT;
DR  PDB: 5UWU;
DR  PDB: 5UWW;
DR  PDB: 5YRO;
DR  PDB: 5YST;
DR  PDB: 5YSU;
DR  PDB: 5YTB;
DR  PDB: 5ZPU;
DR  PDB: 6A38;
DR  PDB: 6A3A;
DR  PDB: 6A3B;
DR  PDB: 6A3C;
DR  PDB: 6A3E;
DR  PDB: 6CIT;
DR  PDB: 6KFT;
DR  PDB: 6LQ9;
DR  PDB: 6M60;
DR  PDB: 6M6X;
DR  PDB: 6Q82;
DR  PDB: 6Q84;
DR  PDB: 6TVO;
DR  PDB: 6X2M;
DR  PDB: 6X2O;
DR  PDB: 6X2P;
DR  PDB: 6X2R;
DR  PDB: 6X2S;
DR  PDB: 6X2U;
DR  PDB: 6X2V;
DR  PDB: 6X2W;
DR  PDB: 6X2X;
DR  PDB: 6X2Y;
DR  PDB: 6XJP;
DR  PDB: 6XJR;
DR  PDB: 6XJS;
DR  PDB: 6XJT;
DR  PDB: 6XJU;
DR  PDB: 7B51;
DR  PDB: 7CND;
DR  PDB: 7DBG;
DR  PDB: 7L5E;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DR  OMIM: 601179;
DR  DisGeNET: 5901;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs (PubMed:10400640, PubMed:8276887, PubMed:8896452, PubMed:8636225, PubMed:8692944, PubMed:9351834, PubMed:9428644, PubMed:9822603, PubMed:17209048, PubMed:26272610, PubMed:27306458). Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis (PubMed:7819259, PubMed:8896452, PubMed:8636225, PubMed:8692944, PubMed:9351834, PubMed:9428644, PubMed:9822603, PubMed:29040603, PubMed:11336674, PubMed:26272610). Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport (PubMed:8896452, PubMed:9351834, PubMed:9428644). Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (PubMed:20485264). RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation (PubMed:10408446, PubMed:29040603). Required for normal progress through mitosis (PubMed:8421051, PubMed:12194828, PubMed:29040603). The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (PubMed:18591255). Acts as a negative regulator of the kinase activity of VRK1 and VRK2 (PubMed:18617507). Enhances AR- mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases (PubMed:10400640). {ECO:0000269|PubMed:10400640, ECO:0000269|PubMed:10408446, ECO:0000269|PubMed:11336674, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:20485264, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:27306458, ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:7819259, ECO:0000269|PubMed:8276887, ECO:0000269|PubMed:8421051, ECO:0000269|PubMed:8636225, ECO:0000269|PubMed:8692944, ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9351834, ECO:0000269|PubMed:9428644, ECO:0000269|PubMed:9822603, ECO:0000305|PubMed:26272610}.
DE  Reference Proteome: Yes;
DE  Interaction: A6NFY4; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: O14524; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: O60356; IntAct: EBI-15569882; Score: 0.37
DE  Interaction: O95271; IntAct: EBI-9692184; Score: 0.40
DE  Interaction: P35658; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: P41391; IntAct: EBI-1032926; Score: 0.40
DE  Interaction: P46060; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-9688194; Score: 0.64
DE  Interaction: P49791; IntAct: EBI-15714795; Score: 0.67
DE  Interaction: P49792; IntAct: EBI-3933494; Score: 0.76
DE  Interaction: P52297; IntAct: EBI-286729; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P61970; IntAct: EBI-9688194; Score: 0.81
DE  Interaction: O42480; IntAct: EBI-286729; Score: 0.35
DE  Interaction: Q6GMY9; IntAct: EBI-286729; Score: 0.35
DE  Interaction: P52292; IntAct: EBI-13942323; Score: 0.40
DE  Interaction: Q92973; IntAct: EBI-1027757; Score: 0.44
DE  Interaction: P60709; IntAct: EBI-353790; Score: 0.40
DE  Interaction: P46527; IntAct: EBI-591758; Score: 0.40
DE  Interaction: Q9P2H0; IntAct: EBI-733094; Score: 0.00
DE  Interaction: P07196; IntAct: EBI-737516; Score: 0.00
DE  Interaction: P03254; IntAct: EBI-8626155; Score: 0.59
DE  Interaction: P03129; IntAct: EBI-8626194; Score: 0.44
DE  Interaction: P43487; IntAct: EBI-8626224; Score: 0.61
DE  Interaction: P03070; IntAct: EBI-8626209; Score: 0.44
DE  Interaction: P03255; IntAct: EBI-8544308; Score: 0.40
DE  Interaction: Q9H6Z4; IntAct: EBI-992712; Score: 0.40
DE  Interaction: P18754; IntAct: EBI-1031180; Score: 0.88
DE  Interaction: Q00005; IntAct: EBI-2211497; Score: 0.35
DE  Interaction: Q99986; IntAct: EBI-1795237; Score: 0.60
DE  Interaction: Q86Y07; IntAct: EBI-1795483; Score: 0.40
DE  Interaction: Q8IV63; IntAct: EBI-1795543; Score: 0.40
DE  Interaction: O15264; IntAct: EBI-2255044; Score: 0.35
DE  Interaction: Q8IY92; IntAct: EBI-2371120; Score: 0.35
DE  Interaction: Q9BQ83; IntAct: EBI-2372444; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: Q9JMK2; IntAct: EBI-2558429; Score: 0.40
DE  Interaction: Q8CEC0; IntAct: EBI-2562665; Score: 0.40
DE  Interaction: Q8VD62; IntAct: EBI-2562857; Score: 0.40
DE  Interaction: Q6ZQH8; IntAct: EBI-2563113; Score: 0.40
DE  Interaction: Q60610; IntAct: EBI-7567120; Score: 0.44
DE  Interaction: Q6ZPF3; IntAct: EBI-7567337; Score: 0.44
DE  Interaction: P43354; IntAct: EBI-2681788; Score: 0.00
DE  Interaction: Q15796; IntAct: EBI-2684985; Score: 0.00
DE  Interaction: O76187; IntAct: EBI-2905901; Score: 0.40
DE  Interaction: P18124; IntAct: EBI-8297497; Score: 0.40
DE  Interaction: Q9HAV4; IntAct: EBI-2938145; Score: 0.40
DE  Interaction: O94829; IntAct: EBI-8534600; Score: 0.73
DE  Interaction: Q99666; IntAct: EBI-3940764; Score: 0.55
DE  Interaction: Q5TAQ9; IntAct: EBI-7817945; Score: 0.27
DE  Interaction: O95758; IntAct: EBI-7850130; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: P10209; IntAct: EBI-6509326; Score: 0.37
DE  Interaction: P47813; IntAct: EBI-9207355; Score: 0.59
DE  Interaction: O15392; IntAct: EBI-9548404; Score: 0.63
DE  Interaction: P42771; IntAct: EBI-9691810; Score: 0.46
DE  Interaction: Q13625; IntAct: EBI-9692277; Score: 0.64
DE  Interaction: Q8WUF5; IntAct: EBI-9692274; Score: 0.65
DE  Interaction: Q8WVL7; IntAct: EBI-9691643; Score: 0.40
DE  Interaction: Q91974; IntAct: EBI-9691221; Score: 0.40
DE  Interaction: O14974; IntAct: EBI-9692208; Score: 0.40
DE  Interaction: Q9HBA0; IntAct: EBI-9692161; Score: 0.40
DE  Interaction: Q06547; IntAct: EBI-25889543; Score: 0.56
DE  Interaction: Q96KQ4; IntAct: EBI-9692121; Score: 0.40
DE  Interaction: P25963; IntAct: EBI-9692133; Score: 0.40
DE  Interaction: O14920; IntAct: EBI-10103342; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-10103376; Score: 0.35
DE  Interaction: P29597; IntAct: EBI-10104620; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-11322719; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q96L14; IntAct: EBI-11022408; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: P34022; IntAct: EBI-11080066; Score: 0.35
DE  Interaction: Q8CAQ8; IntAct: EBI-11096643; Score: 0.35
DE  Interaction: Q9Y496; IntAct: EBI-11097996; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.53
DE  Interaction: P26367; IntAct: EBI-11107399; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.53
DE  Interaction: O43896; IntAct: EBI-11140183; Score: 0.35
DE  Interaction: Q3V6T2; IntAct: EBI-11141559; Score: 0.35
DE  Interaction: Q9UBX2; IntAct: EBI-11614356; Score: 0.35
DE  Interaction: O43592; IntAct: EBI-24355918; Score: 0.56
DE  Interaction: O14787; IntAct: EBI-24386976; Score: 0.56
DE  Interaction: Q9UIA9; IntAct: EBI-24411618; Score: 0.56
DE  Interaction: Q9HD47; IntAct: EBI-25889861; Score: 0.56
DE  Interaction: Q9H9L7; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: Q96P70; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: Q70UQ0; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: Q69YH5; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: P0DJD1; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: Q15398; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: O14715; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: O00629; IntAct: EBI-21557447; Score: 0.35
DE  Interaction: Q53H80; IntAct: EBI-21567350; Score: 0.35
DE  Interaction: P54645; IntAct: EBI-16361875; Score: 0.35
DE  Interaction: P80386; IntAct: EBI-16362252; Score: 0.35
DE  Interaction: P70168; IntAct: EBI-15732723; Score: 0.44
DE  Interaction: P61925; IntAct: EBI-15886863; Score: 0.52
DE  Interaction: Q6P5F9; IntAct: EBI-15887025; Score: 0.68
DE  Interaction: O95149; IntAct: EBI-16064299; Score: 0.40
DE  Interaction: Q01968; IntAct: EBI-16412116; Score: 0.35
DE  Interaction: Q9EPK7; IntAct: EBI-17168930; Score: 0.35
DE  Interaction: Q07960; IntAct: EBI-17172410; Score: 0.40
DE  Interaction: Q9D3W4; IntAct: EBI-17172527; Score: 0.40
DE  Interaction: Q9CWR2; IntAct: EBI-17172552; Score: 0.40
DE  Interaction: O35381; IntAct: EBI-17172576; Score: 0.40
DE  Interaction: Q61074; IntAct: EBI-17172591; Score: 0.40
DE  Interaction: Q9EQU5; IntAct: EBI-17172606; Score: 0.40
DE  Interaction: O09012; IntAct: EBI-17172621; Score: 0.40
DE  Interaction: Q8VE09; IntAct: EBI-17172636; Score: 0.40
DE  Interaction: Q8VCE2; IntAct: EBI-17172666; Score: 0.40
DE  Interaction: Q9Z0P7; IntAct: EBI-17172681; Score: 0.40
DE  Interaction: P97822; IntAct: EBI-17172705; Score: 0.40
DE  Interaction: Q9Z1K5; IntAct: EBI-17172733; Score: 0.40
DE  Interaction: P58043; IntAct: EBI-17172748; Score: 0.40
DE  Interaction: Q8BP48; IntAct: EBI-17172763; Score: 0.40
DE  Interaction: Q60737; IntAct: EBI-17172823; Score: 0.40
DE  Interaction: P15659; IntAct: EBI-25769098; Score: 0.37
DE  Interaction: P03430; IntAct: EBI-25769362; Score: 0.37
DE  Interaction: P03427; IntAct: EBI-25769803; Score: 0.37
DE  Interaction: Q92731; IntAct: EBI-20764883; Score: 0.35
DE  Interaction: O75391; IntAct: EBI-20907624; Score: 0.40
DE  Interaction: Q93073; IntAct: EBI-20910936; Score: 0.40
DE  Interaction: O75054; IntAct: EBI-20912478; Score: 0.40
DE  Interaction: Q9NRL2; IntAct: EBI-20921060; Score: 0.40
DE  Interaction: P16401; IntAct: EBI-20928448; Score: 0.40
DE  Interaction: Q93079; IntAct: EBI-20929824; Score: 0.40
DE  Interaction: Q16695; IntAct: EBI-20929816; Score: 0.40
DE  Interaction: Q9HAP2; IntAct: EBI-20933308; Score: 0.40
DE  Interaction: P62805; IntAct: EBI-20933064; Score: 0.40
DE  Interaction: Q9BXS9; IntAct: EBI-20936124; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.53
DE  Interaction: Q9UQC2; IntAct: EBI-25384304; Score: 0.35
DE  Interaction: P63000; IntAct: EBI-25387902; Score: 0.35
DE  Interaction: P06239; IntAct: EBI-25394571; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.35
DE  Interaction: Q92797; IntAct: EBI-25889687; Score: 0.56
DE  Interaction: O43829; IntAct: EBI-25889679; Score: 0.56
DE  Interaction: P49459; IntAct: EBI-25889671; Score: 0.56
DE  Interaction: Q12888; IntAct: EBI-25889663; Score: 0.56
DE  Interaction: P54274; IntAct: EBI-25889655; Score: 0.56
DE  Interaction: O60927; IntAct: EBI-25889647; Score: 0.56
DE  Interaction: P22307; IntAct: EBI-25889639; Score: 0.56
DE  Interaction: P62701; IntAct: EBI-25889631; Score: 0.56
DE  Interaction: Q15382; IntAct: EBI-25889623; Score: 0.56
DE  Interaction: P47804; IntAct: EBI-25889615; Score: 0.56
DE  Interaction: Q04206; IntAct: EBI-25889607; Score: 0.56
DE  Interaction: Q09028; IntAct: EBI-25889599; Score: 0.56
DE  Interaction: Q07869; IntAct: EBI-25889591; Score: 0.56
DE  Interaction: P36954; IntAct: EBI-25889583; Score: 0.56
DE  Interaction: O15534; IntAct: EBI-25889575; Score: 0.56
DE  Interaction: P36639; IntAct: EBI-25889567; Score: 0.56
DE  Interaction: P27338; IntAct: EBI-25889559; Score: 0.56
DE  Interaction: Q9NRZ9; IntAct: EBI-25889551; Score: 0.56
DE  Interaction: P06241; IntAct: EBI-25889535; Score: 0.56
DE  Interaction: P35222; IntAct: EBI-25889527; Score: 0.56
DE  Interaction: Q86WV5; IntAct: EBI-25889519; Score: 0.56
DE  Interaction: P20807; IntAct: EBI-25889511; Score: 0.56
DE  Interaction: P17655; IntAct: EBI-25889503; Score: 0.56
DE  Interaction: A0A384MDV8; IntAct: EBI-25889495; Score: 0.56
DE  Interaction: P06276; IntAct: EBI-25889487; Score: 0.56
DE  Interaction: Q14032; IntAct: EBI-25889479; Score: 0.56
DE  Interaction: P36406; IntAct: EBI-25889471; Score: 0.56
DE  Interaction: P09525; IntAct: EBI-25889463; Score: 0.56
DE  Interaction: Q9Y3D0; IntAct: EBI-25889937; Score: 0.56
DE  Interaction: Q7Z3B4; IntAct: EBI-25889945; Score: 0.56
DE  Interaction: Q66PJ3; IntAct: EBI-25889919; Score: 0.56
DE  Interaction: Q96IZ7; IntAct: EBI-25889911; Score: 0.56
DE  Interaction: Q9UK76; IntAct: EBI-25889903; Score: 0.56
DE  Interaction: P0DPB6; IntAct: EBI-25889895; Score: 0.56
DE  Interaction: Q49AJ0; IntAct: EBI-25889885; Score: 0.56
DE  Interaction: Q9Y303; IntAct: EBI-25889877; Score: 0.56
DE  Interaction: Q9NNX6; IntAct: EBI-25889869; Score: 0.56
DE  Interaction: Q9H0W9; IntAct: EBI-25889853; Score: 0.56
DE  Interaction: Q9UIK5; IntAct: EBI-25889845; Score: 0.56
DE  Interaction: Q14181; IntAct: EBI-25889837; Score: 0.56
DE  Interaction: Q86US8; IntAct: EBI-25889829; Score: 0.56
DE  Interaction: Q13573; IntAct: EBI-25889821; Score: 0.56
DE  Interaction: O00472; IntAct: EBI-25889813; Score: 0.56
DE  Interaction: Q96H20; IntAct: EBI-25889805; Score: 0.56
DE  Interaction: O95070; IntAct: EBI-25889797; Score: 0.56
DE  Interaction: Q9Y614; IntAct: EBI-25889789; Score: 0.56
DE  Interaction: O60506; IntAct: EBI-25889781; Score: 0.56
DE  Interaction: Q13901; IntAct: EBI-25889773; Score: 0.56
DE  Interaction: Q8N5U6; IntAct: EBI-25889765; Score: 0.56
DE  Interaction: Q96EY1; IntAct: EBI-25889755; Score: 0.56
DE  Interaction: Q86V28; IntAct: EBI-25889739; Score: 0.56
DE  Interaction: O95674; IntAct: EBI-25889731; Score: 0.56
DE  Interaction: P0C870; IntAct: EBI-25889723; Score: 0.56
DE  Interaction: O15273; IntAct: EBI-25889715; Score: 0.56
DE  Interaction: O00257; IntAct: EBI-25889707; Score: 0.56
DE  Interaction: Q92782; IntAct: EBI-25889697; Score: 0.56
DE  Interaction: Q9NTN9; IntAct: EBI-25890047; Score: 0.56
DE  Interaction: Q5W111; IntAct: EBI-25890039; Score: 0.56
DE  Interaction: Q05CR2; IntAct: EBI-25890031; Score: 0.56
DE  Interaction: Q6GQQ9; IntAct: EBI-25890021; Score: 0.56
DE  Interaction: Q9BPU6; IntAct: EBI-25890013; Score: 0.56
DE  Interaction: Q8IYM2; IntAct: EBI-25890005; Score: 0.56
DE  Interaction: Q9NX94; IntAct: EBI-25889997; Score: 0.56
DE  Interaction: Q8TBB5; IntAct: EBI-25889989; Score: 0.56
DE  Interaction: Q9UKG9; IntAct: EBI-25889981; Score: 0.56
DE  Interaction: Q9UGL9; IntAct: EBI-25889973; Score: 0.56
DE  Interaction: Q6UY14; IntAct: EBI-25889963; Score: 0.56
DE  Interaction: Q9NSI6; IntAct: EBI-25889955; Score: 0.56
DE  Interaction: Q9P1Q0; IntAct: EBI-25889929; Score: 0.56
DE  Interaction: Q53FD0; IntAct: EBI-25890107; Score: 0.56
DE  Interaction: Q6N063; IntAct: EBI-25890097; Score: 0.56
DE  Interaction: Q9BUL5; IntAct: EBI-25890089; Score: 0.56
DE  Interaction: Q9H2C1; IntAct: EBI-25890057; Score: 0.56
DE  Interaction: Q96BR5; IntAct: EBI-25890073; Score: 0.56
DE  Interaction: A0A0A0MR05; IntAct: EBI-25890065; Score: 0.56
DE  Interaction: Q9BQA1; IntAct: EBI-25890081; Score: 0.56
DE  Interaction: Q9H0Y0; IntAct: EBI-25890197; Score: 0.56
DE  Interaction: Q9C004; IntAct: EBI-25890181; Score: 0.56
DE  Interaction: Q8N5Z5; IntAct: EBI-25890115; Score: 0.56
DE  Interaction: Q96BD6; IntAct: EBI-25890157; Score: 0.56
DE  Interaction: Q3SXR2; IntAct: EBI-25890149; Score: 0.56
DE  Interaction: Q9H8K7; IntAct: EBI-25890141; Score: 0.56
DE  Interaction: B7Z3E8; IntAct: EBI-25890133; Score: 0.56
DE  Interaction: Q6IN84; IntAct: EBI-25890125; Score: 0.56
DE  Interaction: Q16609; IntAct: EBI-25890165; Score: 0.56
DE  Interaction: Q494V2; IntAct: EBI-25890475; Score: 0.56
DE  Interaction: Q8IWT0; IntAct: EBI-25890451; Score: 0.56
DE  Interaction: Q66K80; IntAct: EBI-25890443; Score: 0.56
DE  Interaction: Q3SX64; IntAct: EBI-25890435; Score: 0.56
DE  Interaction: Q8N0U6; IntAct: EBI-25890427; Score: 0.56
DE  Interaction: Q496A3; IntAct: EBI-25890419; Score: 0.56
DE  Interaction: Q96Q83; IntAct: EBI-25890411; Score: 0.56
DE  Interaction: Q658K8; IntAct: EBI-25890403; Score: 0.56
DE  Interaction: A6NJ78; IntAct: EBI-25890393; Score: 0.56
DE  Interaction: Q8IZU1; IntAct: EBI-25890385; Score: 0.56
DE  Interaction: Q9H2U1; IntAct: EBI-25890377; Score: 0.56
DE  Interaction: Q6PJW8; IntAct: EBI-25890369; Score: 0.56
DE  Interaction: Q6DHV7; IntAct: EBI-25890361; Score: 0.56
DE  Interaction: Q96MA6; IntAct: EBI-25890353; Score: 0.56
DE  Interaction: Q6ZNL6; IntAct: EBI-25890343; Score: 0.56
DE  Interaction: Q96LX8; IntAct: EBI-25890335; Score: 0.56
DE  Interaction: Q86WT6; IntAct: EBI-25890327; Score: 0.56
DE  Interaction: Q6ZMI0; IntAct: EBI-25890319; Score: 0.56
DE  Interaction: Q8N1A0; IntAct: EBI-25890311; Score: 0.56
DE  Interaction: Q6XD76; IntAct: EBI-25890303; Score: 0.56
DE  Interaction: Q96A09; IntAct: EBI-25890295; Score: 0.56
DE  Interaction: Q8IYG6; IntAct: EBI-25890285; Score: 0.56
DE  Interaction: Q96Q07; IntAct: EBI-25890277; Score: 0.56
DE  Interaction: Q53NU3; IntAct: EBI-25890269; Score: 0.56
DE  Interaction: Q9BT25; IntAct: EBI-25890261; Score: 0.56
DE  Interaction: Q8WUX9; IntAct: EBI-25890253; Score: 0.56
DE  Interaction: Q8WUD1; IntAct: EBI-25890237; Score: 0.56
DE  Interaction: Q49A26; IntAct: EBI-25890229; Score: 0.56
DE  Interaction: Q6NXT2; IntAct: EBI-25890517; Score: 0.56
DE  Interaction: Q8WW27; IntAct: EBI-25890509; Score: 0.56
DE  Interaction: Q3KNS6; IntAct: EBI-25890483; Score: 0.56
DE  Interaction: A2RUH7; IntAct: EBI-25890459; Score: 0.56
DE  Interaction: Q5JTY5; IntAct: EBI-25890525; Score: 0.56
DE  Interaction: P09936; IntAct: EBI-25894615; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25930873; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25952651; Score: 0.56
DE  Interaction: P37840; IntAct: EBI-25983264; Score: 0.56
DE  Interaction: Q09161; IntAct: EBI-26398700; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-26374389; Score: 0.27
DE  Interaction: Q99608; IntAct: EBI-26955247; Score: 0.27
DE  Interaction: P06401; IntAct: EBI-26871590; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
GO  GO:0005814;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0042470;
GO  GO:0016020;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0055037;
GO  GO:0042565;
GO  GO:0045296;
GO  GO:0003682;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0046982;
GO  GO:0003723;
GO  GO:0030036;
GO  GO:0051301;
GO  GO:0006259;
GO  GO:0046039;
GO  GO:0000278;
GO  GO:0000070;
GO  GO:0007052;
GO  GO:0032092;
GO  GO:0042307;
GO  GO:0035281;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:1902570;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0000054;
GO  GO:0061015;
GO  GO:0016032;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYY
SQ  IQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
//
ID  Q4R4M9;
PN  GTP-binding nuclear protein Ran;
GN  RAN;
OS  9541;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Melanosome {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: Q4R4M9;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0042470;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0051301;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYY
SQ  IQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
//
ID  P62827;
PN  GTP-binding nuclear protein Ran;
GN  Ran;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:25946333}. Nucleus envelope {ECO:0000269|PubMed:25946333}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000269|PubMed:18347012}. Melanosome {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: P62827;
DR  UNIPROT: P17080;
DR  UNIPROT: P28746;
DR  UNIPROT: P28747;
DR  UNIPROT: Q3U954;
DR  UNIPROT: Q811M2;
DR  UNIPROT: Q86V08;
DR  UNIPROT: Q9CSP3;
DR  UNIPROT: Q9CWI7;
DR  UNIPROT: Q9CZA2;
DR  UNIPROT: Q9UDJ5;
DR  UNIPROT: Q9UEU9;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
DE  Interaction: P35569; IntAct: EBI-529645; Score: 0.35
DE  Interaction: Q6AXH7; IntAct: EBI-6876709; Score: 0.35
DE  Interaction: Q6ZQE4; IntAct: EBI-12595973; Score: 0.60
DE  Interaction: Q9EP53; IntAct: EBI-16734894; Score: 0.35
DE  Interaction: Q9Z2V6; IntAct: EBI-26473798; Score: 0.35
DE  Interaction: P97493; IntAct: EBI-26499412; Score: 0.35
GO  GO:0005814;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0001673;
GO  GO:0002177;
GO  GO:0042470;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0055037;
GO  GO:0042565;
GO  GO:0036126;
GO  GO:0045505;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0061676;
GO  GO:0000287;
GO  GO:0070883;
GO  GO:0019904;
GO  GO:0046982;
GO  GO:0044877;
GO  GO:0030036;
GO  GO:0051301;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0032092;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0008104;
GO  GO:1902570;
GO  GO:0031503;
GO  GO:0043393;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0000054;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYY
SQ  IQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
//
ID  P38544;
PN  GTP-binding nuclear protein Ran;
GN  ran;
OS  6282;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: P38544;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0046872;
GO  GO:0006913;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATGDDIPTFKLVLVGDGGTGKTTFVKRHLTGDPEKKYVATLGVEVHPLIFHTNRGQIRFNVWDTAGQEKFGGLRDGYYI
SQ  QGQCAIIMFDVTARVTYKNVPNWHRDLARVCENIPIVLCGNFVDVKDRKVKAKTITFHRKKNLQYYDISAKSNYNFEKPS
SQ  LWLVRKLLGDPNLEFVAMPALAPPEVQMDPTMVAQYEQEIAAAANAELPDDDEDL
//
ID  Q5R556;
PN  GTP-binding nuclear protein Ran;
GN  RAN;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Melanosome {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: Q5R556;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0042470;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0051301;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYY
SQ  IQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
//
ID  P62828;
PN  GTP-binding nuclear protein Ran;
GN  Ran;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Melanosome {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: P62828;
DR  UNIPROT: P17080;
DR  UNIPROT: P28746;
DR  UNIPROT: P28747;
DR  UNIPROT: Q9CSP3;
DR  UNIPROT: Q9CWI7;
DR  UNIPROT: Q9CZA2;
DR  UNIPROT: Q9UDJ5;
DR  UNIPROT: Q9UEU9;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P19332; IntAct: EBI-26374040; Score: 0.46
GO  GO:0005814;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0001673;
GO  GO:0002177;
GO  GO:0042470;
GO  GO:0030496;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0055037;
GO  GO:0042565;
GO  GO:0036126;
GO  GO:0045505;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0061676;
GO  GO:0000287;
GO  GO:0019904;
GO  GO:0046982;
GO  GO:0044877;
GO  GO:0030036;
GO  GO:0051301;
GO  GO:0071389;
GO  GO:0046039;
GO  GO:0021766;
GO  GO:0000226;
GO  GO:0000070;
GO  GO:0006913;
GO  GO:0032092;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0008104;
GO  GO:1902570;
GO  GO:0031503;
GO  GO:0043393;
GO  GO:0014070;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0000054;
GO  GO:0061015;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYY
SQ  IQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
//
ID  Q9YGC0;
PN  GTP-binding nuclear protein Ran;
GN  ran;
OS  8030;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: Q9YGC0;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0006606;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGAIKYNVWDTAGQEKFGGLRDGYYI
SQ  QAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPF
SQ  LWLARKLIGDPNLEFVAMPALAPPEILMDPSLAAQYEHDLKVASETALPDEDDDL
//
ID  P52301;
PN  GTP-binding nuclear protein Ran;
GN  ran;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000269|PubMed:8413630}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: P52301;
DR  UNIPROT: Q7ZYT6;
DR  UNIPROT: Q9IBE8;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs (PubMed:8413630). Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (By similarity). RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation (PubMed:10408446). Required for normal progress through mitosis (By similarity). In concert with nemp1a/b, required for proper eye development (PubMed:25946333). {ECO:0000250|UniProtKB:P62826, ECO:0000269|PubMed:10408446, ECO:0000269|PubMed:25946333, ECO:0000305|PubMed:8413630}.
DE  Reference Proteome: Yes;
DE  Interaction: B9X187; IntAct: EBI-12596100; Score: 0.40
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0001654;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0006606;
GO  GO:0000055;
GO  GO:0000056;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYY
SQ  IQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEQDLQNAQATALPDEDDDL
//
ID  Q6GL85;
PN  GTP-binding nuclear protein Ran;
GN  ran;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:P62826}.
DR  UNIPROT: Q6GL85;
DR  Pfam: PF00071;
DR  PROSITE: PS51418;
DE  Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP- bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis. {ECO:0000250|UniProtKB:P62826}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0000287;
GO  GO:0046039;
GO  GO:0000070;
GO  GO:0006606;
GO  GO:0000054;
GO  GO:0061015;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYY
SQ  IQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKP
SQ  FLWLARKLIGDPNFEFVAMPALAPPEVVMDPALAAQYEQDLQHAQATALPDEDDDL
//
ID  P62833;
PN  Ras-related protein Rap-1A;
GN  RAP1A;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane; Lipid-anchor. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cell junction {ECO:0000250}. Early endosome {ECO:0000250}. Note=Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Localized with RAPGEF2 at cell-cell junctions. Colocalized with RAPGEF2 in the perinuclear region (By similarity). {ECO:0000250}.
DR  UNIPROT: P62833;
DR  UNIPROT: A4IFG1;
DR  UNIPROT: P10113;
DR  Pfam: PF00071;
DR  PROSITE: PS51421;
DE  Function: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)- induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005769;
GO  GO:0098978;
GO  GO:0032045;
GO  GO:0005770;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0097225;
GO  GO:0003925;
GO  GO:0005525;
GO  GO:0005085;
GO  GO:0044877;
GO  GO:0031267;
GO  GO:0071320;
GO  GO:1990090;
GO  GO:0061028;
GO  GO:2000301;
GO  GO:0038180;
GO  GO:0007399;
GO  GO:0070374;
GO  GO:0043547;
GO  GO:0010976;
GO  GO:0045860;
GO  GO:2001214;
GO  GO:0072659;
GO  GO:0032486;
GO  GO:1901888;
GO  GO:0098696;
GO  GO:0016079;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P62834};
SQ  MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFAL
SQ  VYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYD
SQ  LVRQINRKTPVEKKKPKKKSCLLL
//
ID  P62834;
PN  Ras-related protein Rap-1A;
GN  RAP1A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:11359771}; Lipid-anchor {ECO:0000269|PubMed:11359771}. Cytoplasm {ECO:0000269|PubMed:11359771}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11359771}. Cell junction {ECO:0000250}. Early endosome {ECO:0000250}. Note=Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Localized with RAPGEF2 at cell-cell junctions (By similarity). Colocalized with RAPGEF2 in the perinuclear region. {ECO:0000250}.
DR  UNIPROT: P62834;
DR  UNIPROT: P10113;
DR  PDB: 1C1Y;
DR  PDB: 1GUA;
DR  PDB: 3KUC;
DR  PDB: 4KVG;
DR  Pfam: PF00071;
DR  PROSITE: PS51421;
DR  OMIM: 179520;
DR  DisGeNET: 5906;
DE  Function: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)- induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions. {ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:21840392}.
DE  Reference Proteome: Yes;
DE  Interaction: P03246; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q9Z0S9; IntAct: EBI-491425; Score: 0.40
DE  Interaction: Q8WWW0; IntAct: EBI-960490; Score: 0.65
DE  Interaction: Q5EBH1; IntAct: EBI-961174; Score: 0.61
DE  Interaction: P04049; IntAct: EBI-1026035; Score: 0.62
DE  Interaction: Q9UET6; IntAct: EBI-1063157; Score: 0.00
DE  Interaction: P40337; IntAct: EBI-1074441; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-1083743; Score: 0.00
DE  Interaction: P48039; IntAct: EBI-1188258; Score: 0.53
DE  Interaction: P30153; IntAct: EBI-1266406; Score: 0.35
DE  Interaction: Q14697; IntAct: EBI-3917532; Score: 0.37
DE  Interaction: P25445; IntAct: EBI-6590523; Score: 0.27
DE  Interaction: Q8TDF6; IntAct: EBI-6590814; Score: 0.27
DE  Interaction: P63104; IntAct: EBI-8758913; Score: 0.44
DE  Interaction: Q9Y4G8; IntAct: EBI-8766309; Score: 0.44
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06461; IntAct: EBI-11723785; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: Q80X90; IntAct: EBI-11053320; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-11132927; Score: 0.35
DE  Interaction: Q99IB8; IntAct: EBI-11599534; Score: 0.35
DE  Interaction: Q12967; IntAct: EBI-11682848; Score: 0.37
DE  Interaction: Q9NRW4; IntAct: EBI-21542541; Score: 0.35
DE  Interaction: Q9BQ48; IntAct: EBI-21664135; Score: 0.35
DE  Interaction: Q8TAG9; IntAct: EBI-21673041; Score: 0.35
DE  Interaction: O14880; IntAct: EBI-21690017; Score: 0.35
DE  Interaction: Q92845; IntAct: EBI-21702814; Score: 0.35
DE  Interaction: Q6PUV4; IntAct: EBI-21722654; Score: 0.35
DE  Interaction: P52306; IntAct: EBI-21808615; Score: 0.35
DE  Interaction: Q969Z0; IntAct: EBI-21877137; Score: 0.35
DE  Interaction: Q13905; IntAct: EBI-15953082; Score: 0.44
DE  Interaction: P36957; IntAct: EBI-20305285; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: O14979; IntAct: EBI-20923226; Score: 0.40
DE  Interaction: Q14103; IntAct: EBI-20923218; Score: 0.40
DE  Interaction: O43924; IntAct: EBI-21019227; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q8N6Q3; IntAct: EBI-21402192; Score: 0.35
DE  Interaction: P51636; IntAct: EBI-25383812; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27049069; Score: 0.27
DE  Interaction: Q9H300; IntAct: EBI-27049982; Score: 0.27
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: P15056; IntAct: EBI-27094546; Score: 0.40
GO  GO:0070161;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0010008;
GO  GO:0070062;
GO  GO:0098978;
GO  GO:0032045;
GO  GO:0005770;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0035579;
GO  GO:0097225;
GO  GO:0003925;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0005085;
GO  GO:0044877;
GO  GO:0031267;
GO  GO:0071320;
GO  GO:1990090;
GO  GO:0061028;
GO  GO:2000301;
GO  GO:0038180;
GO  GO:0007399;
GO  GO:0070374;
GO  GO:0043547;
GO  GO:0010976;
GO  GO:0045860;
GO  GO:2001214;
GO  GO:0072659;
GO  GO:0032486;
GO  GO:1901888;
GO  GO:0098696;
GO  GO:0016079;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:1899909};
SQ  MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFAL
SQ  VYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYD
SQ  LVRQINRKTPVEKKKPKKKSCLLL
//
ID  P62835;
PN  Ras-related protein Rap-1A;
GN  Rap1a;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction {ECO:0000269|PubMed:19635461}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Early endosome {ECO:0000250}. Late endosome {ECO:0000250}. Note=Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Colocalized with RAPGEF2 in the perinuclear region (By similarity). Localized with RAPGEF2 at cell-cell junctions. {ECO:0000250}.
DR  UNIPROT: P62835;
DR  UNIPROT: P10113;
DR  Pfam: PF00071;
DR  PROSITE: PS51421;
DE  Function: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes (By similarity). Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions. {ECO:0000250, ECO:0000269|PubMed:19635461}.
DE  Reference Proteome: Yes;
DE  Interaction: Q08460; IntAct: EBI-2024267; Score: 0.35
DE  Interaction: O00522; IntAct: EBI-12734750; Score: 0.40
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16726570; Score: 0.35
GO  GO:0070161;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005769;
GO  GO:0098978;
GO  GO:0032045;
GO  GO:0005770;
GO  GO:0043209;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0045335;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0097225;
GO  GO:0003925;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0005085;
GO  GO:0044877;
GO  GO:0031267;
GO  GO:0071320;
GO  GO:1990090;
GO  GO:0071407;
GO  GO:0071466;
GO  GO:0061028;
GO  GO:0032966;
GO  GO:2000301;
GO  GO:0038180;
GO  GO:0007399;
GO  GO:0070374;
GO  GO:1905451;
GO  GO:0046326;
GO  GO:0043547;
GO  GO:0010976;
GO  GO:0045860;
GO  GO:2001214;
GO  GO:0072659;
GO  GO:0032486;
GO  GO:1901888;
GO  GO:0098696;
GO  GO:0097327;
GO  GO:0007264;
GO  GO:0016079;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P62834};
SQ  MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFAL
SQ  VYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYD
SQ  LVRQINRKTPVEKKKPKKKSCLLL
//
ID  P62836;
PN  Ras-related protein Rap-1A;
GN  Rap1a;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17724123}. Early endosome {ECO:0000269|PubMed:17724123}. Late endosome {ECO:0000269|PubMed:17724123}. Cytoplasm {ECO:0000250}. Cell junction {ECO:0000250}. Note=Localized with RAPGEF2 at cell-cell junctions. Colocalized with RAPGEF2 in the perinuclear region (By similarity). Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. {ECO:0000250}.
DR  UNIPROT: P62836;
DR  UNIPROT: P10113;
DR  Pfam: PF00071;
DR  PROSITE: PS51421;
DE  Function: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes (By similarity). Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions. {ECO:0000250, ECO:0000269|PubMed:17724123}.
DE  Reference Proteome: Yes;
DE  Interaction: P80386; IntAct: EBI-16400563; Score: 0.35
GO  GO:0070161;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0098978;
GO  GO:0032045;
GO  GO:0005770;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0045335;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0097225;
GO  GO:0003925;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0005085;
GO  GO:0044877;
GO  GO:0031267;
GO  GO:0071320;
GO  GO:1990090;
GO  GO:0071407;
GO  GO:0071466;
GO  GO:0061028;
GO  GO:0097421;
GO  GO:0032966;
GO  GO:2000301;
GO  GO:0038180;
GO  GO:0007399;
GO  GO:0070374;
GO  GO:1905451;
GO  GO:0046326;
GO  GO:0043547;
GO  GO:0010976;
GO  GO:0045860;
GO  GO:2001214;
GO  GO:0072659;
GO  GO:0032486;
GO  GO:1901888;
GO  GO:0098696;
GO  GO:0097327;
GO  GO:0009743;
GO  GO:0007264;
GO  GO:0016079;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P62834};
SQ  MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFAL
SQ  VYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYD
SQ  LVRQINRKTPVEKKKPKKKSCLLL
//
ID  Q15283;
PN  Ras GTPase-activating protein 2;
GN  RASA2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region.
DR  UNIPROT: Q15283;
DR  UNIPROT: A8K7K1;
DR  UNIPROT: G3V0F9;
DR  UNIPROT: O00695;
DR  UNIPROT: Q15284;
DR  UNIPROT: Q92594;
DR  UNIPROT: Q99577;
DR  UNIPROT: Q9UEQ2;
DR  Pfam: PF00779;
DR  Pfam: PF00168;
DR  Pfam: PF00169;
DR  Pfam: PF00616;
DR  PROSITE: PS50004;
DR  PROSITE: PS50003;
DR  PROSITE: PS00509;
DR  PROSITE: PS50018;
DR  PROSITE: PS51113;
DR  OMIM: 601589;
DR  DisGeNET: 5922;
DE  Function: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4).
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005096;
GO  GO:0046872;
GO  GO:0005543;
GO  GO:0035556;
GO  GO:0046580;
GO  GO:0043087;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAAPAAAAASSEAPAASATAEPEAGDQDSREVRVLQSLRGKICEAKNLLPYLGPHKMRDCFCTINLDQEEVYRTQVVE
SQ  KSLSPFFSEEFYFEIPRTFQYLSFYVYDKNVLQRDLRIGKVAIKKEDLCNHSGKETWFSLQPVDSNSEVQGKVHLELKLN
SQ  ELITENGTVCQQLVVHIKACHGLPLINGQSCDPYATVSLVGPSRNDQKKTKVKKKTSNPQFNEIFYFEVTRSSSYTRKSQ
SQ  FQVEEEDIEKLEIRIDLWNNGNLVQDVFLGEIKVPVNVLRTDSSHQAWYLLQPRDNGNKSSKTDDLGSLRLNICYTEDYV
SQ  LPSEYYGPLKTLLLKSPDVQPISASAAYILSEICRDKNDAVLPLVRLLLHHDKLVPFATAVAELDLKDTQDANTIFRGNS
SQ  LATRCLDEMMKIVGGHYLKVTLKPILDEICDSSKSCEIDPIKLKEGDNVENNKENLRYYVDKLFNTIVKSSMSCPTVMCD
SQ  IFYSLRQMATQRFPNDPHVQYSAVSSFVFLRFFAVAVVSPHTFHLRPHHPDAQTIRTLTLISKTIQTLGSWGSLSKSKSS
SQ  FKETFMCEFFKMFQEEGYIIAVKKFLDEISSTETKESSGTSEPVHLKEGEMYKRAQGRTRIGKKNFKKRWFCLTSRELTY
SQ  HKQPGSKDAIYTIPVKNILAVEKLEESSFNKKNMFQVIHTEKPLYVQANNCVEANEWIDVLCRVSRCNQNRLSFYHPSVY
SQ  LNGNWLCCQETGENTLGCKPCTAGVPADIQIDIDEDRETERIYSLFTLSLLKLQKMEEACGTIAVYQGPQKEPDDYSNFV
SQ  IEDSVTTFKTIQQIKSIIEKLDEPHEKYRKKRSSSAKYGSKENPIVGKAS
//
ID  Q9Y272;
PN  Dexamethasone-induced Ras-related protein 1;
GN  RASD1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.
DR  UNIPROT: Q9Y272;
DR  UNIPROT: B2R709;
DR  UNIPROT: B4DFF4;
DR  UNIPROT: Q9NYB4;
DR  Pfam: PF00071;
DR  PROSITE: PS51421;
DR  OMIM: 605550;
DR  DisGeNET: 51655;
DE  Function: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-752746; Score: 0.37
DE  Interaction: O94972; IntAct: EBI-10325762; Score: 0.56
DE  Interaction: P10588; IntAct: EBI-4320347; Score: 0.40
DE  Interaction: Q99PV5; IntAct: EBI-6146266; Score: 0.00
DE  Interaction: P43243; IntAct: EBI-10325772; Score: 0.72
DE  Interaction: P61978; IntAct: EBI-10325782; Score: 0.56
DE  Interaction: Q15415; IntAct: EBI-10325792; Score: 0.72
DE  Interaction: P06428; IntAct: EBI-11738005; Score: 0.37
DE  Interaction: P60411; IntAct: EBI-24275367; Score: 0.56
DE  Interaction: Q13064; IntAct: EBI-24303758; Score: 0.56
DE  Interaction: Q96B26; IntAct: EBI-24304269; Score: 0.56
DE  Interaction: Q86X02; IntAct: EBI-24306796; Score: 0.56
DE  Interaction: O43390; IntAct: EBI-24346887; Score: 0.56
DE  Interaction: P0DPK4; IntAct: EBI-24358097; Score: 0.56
DE  Interaction: Q8IUG1; IntAct: EBI-24360657; Score: 0.56
DE  Interaction: Q86YV0; IntAct: EBI-25246276; Score: 0.56
DE  Interaction: Q9NYB9; IntAct: EBI-25258493; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-25259175; Score: 0.56
DE  Interaction: Q2TAC2; IntAct: EBI-24365172; Score: 0.56
DE  Interaction: P0DJD3; IntAct: EBI-24491672; Score: 0.56
DE  Interaction: Q16825; IntAct: EBI-24501862; Score: 0.56
DE  Interaction: Q99750; IntAct: EBI-24401121; Score: 0.56
DE  Interaction: O00308; IntAct: EBI-24369877; Score: 0.56
DE  Interaction: P26371; IntAct: EBI-24396272; Score: 0.56
DE  Interaction: O75525; IntAct: EBI-24402473; Score: 0.56
DE  Interaction: Q5JR59; IntAct: EBI-24456980; Score: 0.56
DE  Interaction: O76011; IntAct: EBI-24457300; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-24473269; Score: 0.56
DE  Interaction: Q3LI66; IntAct: EBI-24576504; Score: 0.56
DE  Interaction: Q9NQX1; IntAct: EBI-24598415; Score: 0.56
DE  Interaction: Q6PEX3; IntAct: EBI-24638857; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25939746; Score: 0.56
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016529;
GO  GO:0031681;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0007186;
GO  GO:0045892;
GO  GO:0007263;
GO  GO:0007165;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTS
SQ  GNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLRQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVDQREI
SQ  EQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGGDPG
SQ  DAFGIVAPFARRPSVHSDLMYIREKASAGSQAKDKERCVIS
//
ID  O35626;
PN  Dexamethasone-induced Ras-related protein 1;
GN  Rasd1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.
DR  UNIPROT: O35626;
DR  Pfam: PF00071;
DR  PROSITE: PS51421;
DE  Function: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P43136; IntAct: EBI-4319978; Score: 0.64
DE  Interaction: P27790; IntAct: EBI-4325272; Score: 0.37
DE  Interaction: P62874; IntAct: EBI-4325276; Score: 0.37
DE  Interaction: Q9JJ00; IntAct: EBI-4325299; Score: 0.37
DE  Interaction: Q62420; IntAct: EBI-4325302; Score: 0.37
DE  Interaction: Q920B9; IntAct: EBI-4325306; Score: 0.37
DE  Interaction: Q8CG79; IntAct: EBI-4325310; Score: 0.37
DE  Interaction: P68510; IntAct: EBI-4325314; Score: 0.37
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016529;
GO  GO:0031681;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0045892;
GO  GO:0007263;
GO  GO:0007165;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTS
SQ  GNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLKQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVEQREI
SQ  EQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGDHGD
SQ  AFGILAPFARRPSVHSDLMYIREKTSVGSQAKDKERCVIS
//
ID  Q9JKF8;
PN  Dexamethasone-induced Ras-related protein 1;
GN  Rasd1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18922798}. Nucleus {ECO:0000269|PubMed:18922798}.
DR  UNIPROT: Q9JKF8;
DR  UNIPROT: Q4KLL2;
DR  Pfam: PF00071;
DR  PROSITE: PS51421;
DE  Function: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016529;
GO  GO:0031681;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0045892;
GO  GO:0007263;
GO  GO:0007165;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTS
SQ  GNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLKQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVEQREI
SQ  EQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGDHGD
SQ  AFGILAPFARRPSVHSDLMYIREKTSVSSQAKDKERCVIS
//
ID  Q619T5;
PN  Ras and EF-hand domain-containing protein homolog;
GN  rsef;
OS  6238;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IZ41}.
DR  UNIPROT: Q619T5;
DR  UNIPROT: A8XJC9;
DR  Pfam: PF13833;
DR  Pfam: PF00071;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51419;
DE  Function: Binds GTP and GDP. Plays a role in uterine seam cell development. {ECO:0000250|UniProtKB:Q22908, ECO:0000250|UniProtKB:Q8IZ41}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MANPDVENLFSLCDSESKGFLTMEDLKKVCPQLDDNDLRFIFNELDRDGSGKIEKMEFLQGFQETVQHGESRGLNGMQRR
SQ  ASVAFDDGGPVFRRDELVFESESDSSSRPAIRVYDEEHYHSESDTNINIDFSVPCQEEVLVLYEQLQSSGVPALLRKFER
SQ  VVGSFHKELSEKKHENERLQRIYASEREMYNRRMEEMESEVDQQLELIEMKARQEERERLTKEKEEMRERMSEEMSEMRT
SQ  NIERLQRMEKVLERENERLNHQKDLSDKLKVVNEENNDLRQNLAENHLELAMIKSELAQVRADFDQKQDELSARRDQASH
SQ  ATEESESVRKQLQLLFDANRKLHETNESLRDALDSRASVLRQFNLRTPSPGLINSNRNSVENFQTSTNMFKSVPLHAISD
SQ  EEPDPETSLILDDAHSLQGMDIAEGLVGLNDANGPAERTFRIVMCGDAAVGKSSFVMRVIRRQFTNQLPSTLGVDFHVKT
SQ  VNVDGRNVALQLWDTAGQERFRSLCKSYFRRADGAILVYDVCAEHSFLRVRDWIETIKESTERSIPIILVGNKVDMRLQT
SQ  PGAVAKTDGASMAAAMGVLFMETSALDGSNIDNAMLALTRELMAVEDVEIRSTGVVLNPAATKKGGCFSKCRGS
//
ID  Q22908;
PN  Ras and EF-hand domain-containing protein homolog;
GN  rsef;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IZ41}.
DR  UNIPROT: Q22908;
DR  UNIPROT: Q21466;
DR  UNIPROT: Q22906;
DR  Pfam: PF00071;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51419;
DE  Function: Binds GTP and GDP (By similarity). Plays a role in uterine seam cell development (PubMed:25281934). {ECO:0000250|UniProtKB:Q8IZ41, ECO:0000269|PubMed:25281934}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSKPEVENLFSLCDSESKGYLTMEDLRKVCPQLDDNDLRFIFTELDQDGSGKIEKLEFLRGFQDTVQHGESHGLNGMQRR
SQ  ASVAVEDPPMFLRDEQMFDSESDSTSSRPAIRVFDEEHYHSESDTNINIDFSVPCQEEVLVLYEQLQSSGVPALLRKFER
SQ  VVGSFHKELSEKKHENERLQRIYASEREMYNRRMEEMESEVDQQLELTEMKARQEERDRLTKEKEEMRQRMSDEMSEMRN
SQ  NIERLQKMEKALERENERLNHQKELSDKLKVVNEENNDLRQNLAENHLELAMIKSELAQVRCEFDQKQDELSARRDQASH
SQ  ATEESESVRKQLQLLFDANRKLHETNESLRDALDSRASVLRQFNLRTPSPGLLSSNRNSVENFQTSTNVFRSVPLHAIST
SQ  EEQVPETSLILDDAHSLQGLDTPGDLMGLNDANGPAERTFRIVMCGDAAVGKSSFVMRVIRRQFTNQLPSTLGVDFHVKT
SQ  VNVDGRNVALQLWDTAGQERFRSLCKSYFRRADGAILVYDVCAEQSFLRVRDWIETIKESTERSIPIILVGNKVDMRIST
SQ  PGSVAKTDGASMAAAMGVLFMETSALDGSNIDNAMLALTRELMAVEDVEIRSTGVVLNPAVAKKGGCFSKCRGS
//
ID  A5WW21;
PN  Ras and EF-hand domain-containing protein;
GN  rasef;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IZ41}.
DR  UNIPROT: A5WW21;
DR  UNIPROT: A4QP53;
DR  Pfam: PF13499;
DR  Pfam: PF00071;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51419;
DE  Function: Binds predominantly GDP, and also GTP. {ECO:0000250|UniProtKB:Q8IZ41}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0016192;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNHAELRRLFAACDGNQSGRVEYEDFTTVCRELNVPADDIRTLFNKFDLDGDGYINFNDFSSSFQEVSEALNLASLGNCL
SQ  HSQRRAWDEFENTLDGDVAFYLGRQWDALSELYEGIHSTSDELLLQQFEDLIRALVTEIREHRMESEQLETSLRRTEEVS
SQ  SSQLAEMEEDLQQQLIHTERRVREEEQKKLDESIAMLQIKHENELADLQTTIERLTKQYQEESKLNTPREDSVKLRAQIK
SQ  DLMEENEELRASLMKAQMNVSILQVELDKLKNAFTDQKRQHERESDDLKKMVMEFQSYSSHIEMLQEMNKSLYDSNDGLR
SQ  SALSQENASTKRQLSPRNEVLPRKMKPIRQSTMNQSSFTNEEDTLALVKCWAEKYLDSGVSVQSEMDAMSGIDYDSDDSH
SQ  HSVETVHHSYSCVPSELEVSEVKPEALRSVARSTVGSISSSLRRRLSAFPVKQNEEDLLDTQDLAPVYRLVLAGDAGSGK
SQ  SSFLLRLSLNEFRGDIQTTLGVDFQIKKMLVDGEKTNLQIWDTAGQERFRSIARSYFRKAHGVLLLYDVTSESSFLNVRE
SQ  WVEQIRESTDEDIPMCIIGNKVDLRAARPEGSCVSSIHGEKLAMNYNALFCEASAKEGTNVIEAVLHLAREVKKHVKLGR
SQ  RSESQVKLSLHKRRKTLSNCCGV
//
ID  Q8IZ41;
PN  Ras and EF-hand domain-containing protein;
GN  RASEF;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17448446}.
DR  UNIPROT: Q8IZ41;
DR  UNIPROT: A6NC29;
DR  UNIPROT: Q96N04;
DR  PDB: 2P5S;
DR  PDB: 2PMY;
DR  Pfam: PF13499;
DR  Pfam: PF00071;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS51419;
DR  OMIM: 611344;
DR  DisGeNET: 158158;
DE  Function: Binds predominantly GDP, and also GTP (PubMed:17448446). Acts as a dynein adapter protein that activates dynein-mediated transport and dynein-dynactin motility on microtubules (PubMed:30814157). {ECO:0000269|PubMed:17448446, ECO:0000269|PubMed:30814157}.
DE  Reference Proteome: Yes;
DE  Interaction: P31150; IntAct: EBI-21855891; Score: 0.35
DE  Interaction: Q9UNT1; IntAct: EBI-21895210; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-27128270; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEADGDGEELARLRSVFAACDANRSGRLEREEFRALCTELRVRPADAEAVFQRLDADRDGAITFQEFARGFLGSLRGGRR
SQ  RDWGPLDPAPAVSEAGPETHDSEEDEGDEDAAAALATSCGPASPGRAWQDFQARLGDEAKFIPREEQVSTLYQNINLVEP
SQ  RLIQPYEHVIKNFIREIRLQSTEMENLAIAVKRAQDKAAMQLSELEEEMDQRIQAAEHKTRKDEKRKAEEALSDLRRQYE
SQ  TEVGDLQVTIKKLRKLEEQSKRVSQKEDVAALKKQIYDLSMENQKVKKDLLEAQTNIAFLQSELDALKSDYADQSLNTER
SQ  DLEIIRAYTEDRNSLERQIEILQTANRKLHDSNDGLRSALENSYSKFNRSLHINNISPGNTISRSSPKFIGHSPQPLGYD
SQ  RSSRSSYVDEDCDSLALCDPLQRTNCEVDSLPESCFDSGLSTLRDPNEYDSEVEYKHQRGFQRSHGVQESFGGDASDTDV
SQ  PDIRDEETFGLEDVASVLDWKPQGSVSEGSIVSSSRKPISALSPQTDLVDDNAKSFSSQKAYKIVLAGDAAVGKSSFLMR
SQ  LCKNEFRENISATLGVDFQMKTLIVDGERTVLQLWDTAGQERFRSIAKSYFRKADGVLLLYDVTCEKSFLNIREWVDMIE
SQ  DAAHETVPIMLVGNKADIRDTAATEGQKCVPGHFGEKLAMTYGALFCETSAKDGSNIVEAVLHLAREVKKRTDKDDSRSI
SQ  TNLTGTNSKKSPQMKNCCNG
//
ID  Q5RI75;
PN  Ras and EF-hand domain-containing protein homolog;
GN  Rasef;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IZ41}.
DR  UNIPROT: Q5RI75;
DR  UNIPROT: B2RQ59;
DR  UNIPROT: Q5RI76;
DR  Pfam: PF00071;
DR  PROSITE: PS51419;
DE  Function: Binds predominantly GDP, and also GTP (By similarity). Acts as a dynein adapter protein that activates dynein-mediated transport and dynein-dynactin motility on microtubules (By similarity). {ECO:0000250|UniProtKB:Q8IZ41}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0042802;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQEVSSSVAFIHRLLYTALRGLLGDRLKRGLKKEQVSTLYQNITLVEPRLLQPYERVIRNFLREIKLQSTEMENLAIAV
SQ  KRAQDKAAIQLSELEEEMDQRIQAVENESRKDEKRKAEEALTDLRRQYETEVGDLQVTIKRLKKLEEQSRQISQKQDVTA
SQ  LKKQIHDLTMENQKLKKELLEAQTNVAFLQSELDALKSDYADQSLNSERDLEIIREYTEDRSSLERQIEILQTANRKLHD
SQ  SNDGLRSALENTYSKLNRSLRINNISPGNTISRSSPKFNHHSSQPLAYDRSFHSSYADEDCDSLALCDPLQKMNYEVDSL
SQ  PESCFDSGLSTLRDNECDSEVDYKHQGEFQTLHRTEESLGGDASDTDVPDIRDEEAFDSESVASVLHWQPQGSAGEGSTL
SQ  SSSRKPISALSLQTDMVDNTSKVTSQKAYKIVLAGDAAVGKSSFLMRLCKNEFQGNTSATLGVDFQMKTLIVDGEQTVLQ
SQ  LWDTAGQERFRSIAKSYFRKADGVLLLYDVTCEKSFLNVREWVDMVEDGTHRTIPIMLVGNKADLRDVDNAENQKCISAY
SQ  LGEKLAMTYGALFCETSAKDGSNVVEAVLHLAREVKKRTEDDDSRSITSLAGSTSKKSLQMKNCCNG
//
ID  Q08CX1;
PN  Ras and EF-hand domain-containing protein;
GN  rasef;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IZ41}.
DR  UNIPROT: Q08CX1;
DR  Pfam: PF13499;
DR  Pfam: PF00071;
DR  PROSITE: PS50222;
DR  PROSITE: PS51419;
DE  Function: Binds predominantly GDP, and also GTP. {ECO:0000250|UniProtKB:Q8IZ41}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005509;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDKDELSRLRALFHTFDSKSSGRLEKGQFSALCAELKVSPSEAEDIFARLDSDKDSCITFEDFAMGFRGARGLHMPEGK
SQ  KDVEQGEPPKSPSTPDKEEKPEETSSPAWEDFQRRLADEVNYIPRREQASILYQNINIVEPLLIQQYEHVIRNFVREIRL
SQ  QSTEMENLAIAVKRAQDKAAIQLSELEEEMDQRIQAVEKRVKKEEKRKSEEALNDLKRQHESEVAELQVTIKKLKKLEEQ
SQ  SKNINLKEDVAVLRRRLHDLTMENQKLRKDLLEAQTSISFLQSELDALKSDYADQSLSSERDMDIIRGFTDERENLARQI
SQ  EILQTANRKLHDSNDGLRSALENSLMKYNRSLRTINTSPGSTISRNSPKLTRCTSPYDRSPRSSYLDEDYDSLAVCDPMQ
SQ  RMNCEVDSLPESCIDSGLSTLRDSNEYDSEAEYRPPRIFHRSRFPHENYGGDASDTDVPEIRDEESYAPDNGGNLDWKPS
SQ  NPVSRSSSGASSSRKCISALSANVTSAETVDKVHKYTHAEKAYKIVLAGDAAVGKSSFLMRLCKNEFRGNTSATLGVDFQ
SQ  MKTLVVDGEPTILQLWDTAGQERFRSIAKSYFRRADGVLLLYDVTCEKSFLNVREWIDMIEDATSEAIPIMMVGNKADLR
SQ  QLMAEQGHICVSTNYGEKLSRTYGALFCETSAKEGSNIVEAVLHLAREVRKRCDNEDDRGSVTNLSAAISKKPAQMKNCC
SQ  NV
//
ID  P01112;
PN  GTPase HRas, N-terminally processed;
GN  HRAS;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Golgi apparatus membrane; Lipid-anchor. Note=The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form (By similarity). Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000250}. [Isoform 2]: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Colocalizes with RACK1 to the perinuclear region.
DR  UNIPROT: P01112;
DR  UNIPROT: B5BUA0;
DR  UNIPROT: Q14080;
DR  UNIPROT: Q6FHV9;
DR  UNIPROT: Q9BR65;
DR  UNIPROT: Q9UCE2;
DR  PDB: 121P;
DR  PDB: 1AA9;
DR  PDB: 1AGP;
DR  PDB: 1BKD;
DR  PDB: 1CLU;
DR  PDB: 1CRP;
DR  PDB: 1CRQ;
DR  PDB: 1CRR;
DR  PDB: 1CTQ;
DR  PDB: 1GNP;
DR  PDB: 1GNQ;
DR  PDB: 1GNR;
DR  PDB: 1HE8;
DR  PDB: 1IAQ;
DR  PDB: 1IOZ;
DR  PDB: 1JAH;
DR  PDB: 1JAI;
DR  PDB: 1K8R;
DR  PDB: 1LF0;
DR  PDB: 1LF5;
DR  PDB: 1LFD;
DR  PDB: 1NVU;
DR  PDB: 1NVV;
DR  PDB: 1NVW;
DR  PDB: 1NVX;
DR  PDB: 1P2S;
DR  PDB: 1P2T;
DR  PDB: 1P2U;
DR  PDB: 1P2V;
DR  PDB: 1PLJ;
DR  PDB: 1PLK;
DR  PDB: 1PLL;
DR  PDB: 1Q21;
DR  PDB: 1QRA;
DR  PDB: 1RVD;
DR  PDB: 1WQ1;
DR  PDB: 1XCM;
DR  PDB: 1XD2;
DR  PDB: 1XJ0;
DR  PDB: 1ZVQ;
DR  PDB: 1ZW6;
DR  PDB: 221P;
DR  PDB: 2C5L;
DR  PDB: 2CE2;
DR  PDB: 2CL0;
DR  PDB: 2CL6;
DR  PDB: 2CL7;
DR  PDB: 2CLC;
DR  PDB: 2CLD;
DR  PDB: 2EVW;
DR  PDB: 2LCF;
DR  PDB: 2LWI;
DR  PDB: 2N42;
DR  PDB: 2N46;
DR  PDB: 2Q21;
DR  PDB: 2QUZ;
DR  PDB: 2RGA;
DR  PDB: 2RGB;
DR  PDB: 2RGC;
DR  PDB: 2RGD;
DR  PDB: 2RGE;
DR  PDB: 2RGG;
DR  PDB: 2UZI;
DR  PDB: 2VH5;
DR  PDB: 2X1V;
DR  PDB: 3DDC;
DR  PDB: 3I3S;
DR  PDB: 3K8Y;
DR  PDB: 3K9L;
DR  PDB: 3K9N;
DR  PDB: 3KKM;
DR  PDB: 3KKN;
DR  PDB: 3KUD;
DR  PDB: 3L8Y;
DR  PDB: 3L8Z;
DR  PDB: 3LBH;
DR  PDB: 3LBI;
DR  PDB: 3LBN;
DR  PDB: 3LO5;
DR  PDB: 3OIU;
DR  PDB: 3OIV;
DR  PDB: 3OIW;
DR  PDB: 3RRY;
DR  PDB: 3RRZ;
DR  PDB: 3RS0;
DR  PDB: 3RS2;
DR  PDB: 3RS3;
DR  PDB: 3RS4;
DR  PDB: 3RS5;
DR  PDB: 3RS7;
DR  PDB: 3RSL;
DR  PDB: 3RSO;
DR  PDB: 3TGP;
DR  PDB: 421P;
DR  PDB: 4DLR;
DR  PDB: 4DLS;
DR  PDB: 4DLT;
DR  PDB: 4DLU;
DR  PDB: 4DLV;
DR  PDB: 4DLW;
DR  PDB: 4DLX;
DR  PDB: 4DLY;
DR  PDB: 4DLZ;
DR  PDB: 4DST;
DR  PDB: 4DSU;
DR  PDB: 4EFL;
DR  PDB: 4EFM;
DR  PDB: 4EFN;
DR  PDB: 4G0N;
DR  PDB: 4G3X;
DR  PDB: 4K81;
DR  PDB: 4L9S;
DR  PDB: 4L9W;
DR  PDB: 4NYI;
DR  PDB: 4NYJ;
DR  PDB: 4NYM;
DR  PDB: 4Q21;
DR  PDB: 4RSG;
DR  PDB: 4URU;
DR  PDB: 4URV;
DR  PDB: 4URW;
DR  PDB: 4URX;
DR  PDB: 4URY;
DR  PDB: 4URZ;
DR  PDB: 4US0;
DR  PDB: 4US1;
DR  PDB: 4US2;
DR  PDB: 4XVQ;
DR  PDB: 4XVR;
DR  PDB: 521P;
DR  PDB: 5B2Z;
DR  PDB: 5B30;
DR  PDB: 5E95;
DR  PDB: 5P21;
DR  PDB: 5VBE;
DR  PDB: 5VBZ;
DR  PDB: 5WDO;
DR  PDB: 5WDP;
DR  PDB: 5WDQ;
DR  PDB: 5WFO;
DR  PDB: 5WFP;
DR  PDB: 5WFQ;
DR  PDB: 5WFR;
DR  PDB: 5WPL;
DR  PDB: 5X9S;
DR  PDB: 5ZC6;
DR  PDB: 621P;
DR  PDB: 6AMB;
DR  PDB: 6AXG;
DR  PDB: 6BVI;
DR  PDB: 6BVJ;
DR  PDB: 6BVK;
DR  PDB: 6BVL;
DR  PDB: 6BVM;
DR  PDB: 6CUO;
DR  PDB: 6CUP;
DR  PDB: 6CUR;
DR  PDB: 6D55;
DR  PDB: 6D56;
DR  PDB: 6D59;
DR  PDB: 6D5E;
DR  PDB: 6D5G;
DR  PDB: 6D5H;
DR  PDB: 6D5J;
DR  PDB: 6D5L;
DR  PDB: 6D5M;
DR  PDB: 6D5V;
DR  PDB: 6D5W;
DR  PDB: 6DZH;
DR  PDB: 6E6C;
DR  PDB: 6E6P;
DR  PDB: 6MQT;
DR  PDB: 6NTC;
DR  PDB: 6NTD;
DR  PDB: 6Q21;
DR  PDB: 6V94;
DR  PDB: 6V9F;
DR  PDB: 6V9J;
DR  PDB: 6V9L;
DR  PDB: 6V9M;
DR  PDB: 6V9N;
DR  PDB: 6V9O;
DR  PDB: 6ZJ0;
DR  PDB: 6ZL3;
DR  PDB: 721P;
DR  PDB: 7DPH;
DR  PDB: 7DPJ;
DR  PDB: 7JHP;
DR  PDB: 7JIF;
DR  PDB: 7JIG;
DR  PDB: 7JIH;
DR  PDB: 7JII;
DR  PDB: 7L0F;
DR  PDB: 7L0G;
DR  PDB: 7OG9;
DR  PDB: 7OGA;
DR  PDB: 7OGB;
DR  PDB: 7OGC;
DR  PDB: 7OGD;
DR  PDB: 7OGE;
DR  PDB: 7OGF;
DR  PDB: 821P;
DR  Pfam: PF00071;
DR  PROSITE: PS51421;
DR  OMIM: 109800;
DR  OMIM: 163200;
DR  OMIM: 188470;
DR  OMIM: 190020;
DR  OMIM: 218040;
DR  DisGeNET: 3265;
DE  Function: Involved in the activation of Ras protein signal transduction (PubMed:22821884). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:12740440, PubMed:14500341, PubMed:9020151). {ECO:0000269|PubMed:12740440, ECO:0000269|PubMed:14500341, ECO:0000269|PubMed:22821884, ECO:0000269|PubMed:9020151}.
DE  Disease: Costello syndrome (CSTLO) [MIM:218040]: A rare condition characterized by prenatally increased growth, postnatal growth deficiency, intellectual disability, distinctive facial appearance, cardiovascular abnormalities (typically pulmonic stenosis, hypertrophic cardiomyopathy and/or atrial tachycardia), tumor predisposition, skin and musculoskeletal abnormalities. {ECO:0000269|PubMed:16170316, ECO:0000269|PubMed:16329078, ECO:0000269|PubMed:16443854, ECO:0000269|PubMed:17054105, ECO:0000269|PubMed:18039947, ECO:0000269|PubMed:18247425, ECO:0000269|PubMed:19995790}. Note=The disease is caused by variants affecting the gene represented in this entry. Congenital myopathy with excess of muscle spindles (CMEMS) [MIM:218040]: Variant of Costello syndrome. {ECO:0000269|PubMed:17412879}. Note=The disease is caused by variants affecting the gene represented in this entry. Thyroid cancer, non-medullary, 2 (NMTC2) [MIM:188470]: A form of non-medullary thyroid cancer (NMTC), a cancer characterized by tumors originating from the thyroid follicular cells. NMTCs represent approximately 95% of all cases of thyroid cancer and are classified into papillary, follicular, Hurthle cell, and anaplastic neoplasms. {ECO:0000269|PubMed:12727991}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Note=Mutations which change positions 12, 13 or 61 activate the potential of HRAS to transform cultured cells and are implicated in a variety of human tumors. {ECO:0000269|PubMed:3670300}. Bladder cancer (BLC) [MIM:109800]: A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. {ECO:0000269|PubMed:6298635, ECO:0000269|PubMed:6844927}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Schimmelpenning-Feuerstein-Mims syndrome (SFM) [MIM:163200]: A disease characterized by sebaceous nevi, often on the face, associated with variable ipsilateral abnormalities of the central nervous system, ocular anomalies, and skeletal defects. Many oral manifestations have been reported, not only including hypoplastic and malformed teeth, and mucosal papillomatosis, but also ankyloglossia, hemihyperplastic tongue, intraoral nevus, giant cell granuloma, ameloblastoma, bone cysts, follicular cysts, oligodontia, and odontodysplasia. Sebaceous nevi follow the lines of Blaschko and these can continue as linear intraoral lesions, as in mucosal papillomatosis. {ECO:0000269|PubMed:22683711}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O14681; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O15162; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O75694; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P00533; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P04049; IntAct: EBI-8653209; Score: 0.98
DE  Interaction: Q03135; IntAct: EBI-8675908; Score: 0.51
DE  Interaction: P48736; IntAct: EBI-1030404; Score: 0.44
DE  Interaction: P28829; IntAct: EBI-1032361; Score: 0.44
DE  Interaction: Q7Z569; IntAct: EBI-350144; Score: 0.52
DE  Interaction: P12931; IntAct: EBI-8633225; Score: 0.57
DE  Interaction: Q9Z0S9; IntAct: EBI-476976; Score: 0.51
DE  Interaction: P10398; IntAct: EBI-537048; Score: 0.74
DE  Interaction: Q04631; IntAct: EBI-602542; Score: 0.40
DE  Interaction: Q8WWW0; IntAct: EBI-960623; Score: 0.59
DE  Interaction: Q5EBH1; IntAct: EBI-968687; Score: 0.78
DE  Interaction: Q9NS23; IntAct: EBI-8558178; Score: 0.68
DE  Interaction: Q9UQ13; IntAct: EBI-994100; Score: 0.35
DE  Interaction: Q9EQZ6; IntAct: EBI-990765; Score: 0.56
DE  Interaction: P20936; IntAct: EBI-1026524; Score: 0.44
DE  Interaction: Q03386; IntAct: EBI-1026915; Score: 0.44
DE  Interaction: Q07889; IntAct: EBI-1026981; Score: 0.94
DE  Interaction: P42684; IntAct: EBI-1102844; Score: 0.46
DE  Interaction: Q13671; IntAct: EBI-1102856; Score: 0.83
DE  Interaction: Q03385; IntAct: EBI-1102933; Score: 0.37
DE  Interaction: P42337; IntAct: EBI-1265969; Score: 0.59
DE  Interaction: P11233; IntAct: EBI-8568544; Score: 0.57
DE  Interaction: Q46342; IntAct: EBI-7213140; Score: 0.44
DE  Interaction: Q12967; IntAct: EBI-6592219; Score: 0.68
DE  Interaction: O15211; IntAct: EBI-34580956; Score: 0.55
DE  Interaction: Q9NZL6; IntAct: EBI-16090985; Score: 0.67
DE  Interaction: P05783; IntAct: EBI-3930926; Score: 0.37
DE  Interaction: O00329; IntAct: EBI-6470805; Score: 0.40
DE  Interaction: P27986; IntAct: EBI-6593440; Score: 0.27
DE  Interaction: Q9Y4G8; IntAct: EBI-8766313; Score: 0.44
DE  Interaction: P27958; IntAct: EBI-8785468; Score: 0.35
DE  Interaction: P36894; IntAct: EBI-8995396; Score: 0.37
DE  Interaction: O43683; IntAct: EBI-8995877; Score: 0.37
DE  Interaction: P12830; IntAct: EBI-8996430; Score: 0.37
DE  Interaction: Q8N726; IntAct: EBI-8996651; Score: 0.37
DE  Interaction: P35221; IntAct: EBI-8996872; Score: 0.37
DE  Interaction: Q969H0; IntAct: EBI-8997977; Score: 0.37
DE  Interaction: Q9UHC1; IntAct: EBI-8999031; Score: 0.37
DE  Interaction: P43246; IntAct: EBI-8999382; Score: 0.37
DE  Interaction: P52701; IntAct: EBI-8999486; Score: 0.37
DE  Interaction: Q9UIF7; IntAct: EBI-8999590; Score: 0.37
DE  Interaction: Q15198; IntAct: EBI-9000084; Score: 0.37
DE  Interaction: P42336; IntAct: EBI-9000279; Score: 0.37
DE  Interaction: Q12913; IntAct: EBI-9000778; Score: 0.37
DE  Interaction: Q13485; IntAct: EBI-9001402; Score: 0.37
DE  Interaction: Q15831; IntAct: EBI-9001857; Score: 0.37
DE  Interaction: Q8IZY5; IntAct: EBI-9068408; Score: 0.37
DE  Interaction: P09341; IntAct: EBI-9068421; Score: 0.37
DE  Interaction: Q4ZG55; IntAct: EBI-9068434; Score: 0.37
DE  Interaction: Q13007; IntAct: EBI-9068447; Score: 0.37
DE  Interaction: Q9UI38; IntAct: EBI-9068460; Score: 0.37
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: P52306; IntAct: EBI-24522591; Score: 0.63
DE  Interaction: P08678; IntAct: EBI-12520313; Score: 0.44
DE  Interaction: Q13503; IntAct: EBI-21501670; Score: 0.35
DE  Interaction: P53611; IntAct: EBI-21522680; Score: 0.35
DE  Interaction: Q53EQ6; IntAct: EBI-21523123; Score: 0.35
DE  Interaction: P21453; IntAct: EBI-21539478; Score: 0.35
DE  Interaction: Q9NRW4; IntAct: EBI-21542541; Score: 0.35
DE  Interaction: P09067; IntAct: EBI-21543288; Score: 0.35
DE  Interaction: Q9NT62; IntAct: EBI-21549217; Score: 0.35
DE  Interaction: Q6PEY0; IntAct: EBI-21551307; Score: 0.35
DE  Interaction: P26842; IntAct: EBI-21555258; Score: 0.35
DE  Interaction: Q16288; IntAct: EBI-21583226; Score: 0.35
DE  Interaction: Q8N5S1; IntAct: EBI-21587332; Score: 0.35
DE  Interaction: Q96SQ9; IntAct: EBI-21623270; Score: 0.35
DE  Interaction: P18827; IntAct: EBI-21643544; Score: 0.35
DE  Interaction: O14880; IntAct: EBI-21690017; Score: 0.35
DE  Interaction: Q8NFB2; IntAct: EBI-21757603; Score: 0.35
DE  Interaction: Q8TBF2; IntAct: EBI-21761583; Score: 0.35
DE  Interaction: Q86Z23; IntAct: EBI-21814288; Score: 0.35
DE  Interaction: O00141; IntAct: EBI-21824552; Score: 0.35
DE  Interaction: O95620; IntAct: EBI-21824582; Score: 0.35
DE  Interaction: P13995; IntAct: EBI-21824619; Score: 0.53
DE  Interaction: P15056; IntAct: EBI-21824663; Score: 0.83
DE  Interaction: P54277; IntAct: EBI-21824766; Score: 0.35
DE  Interaction: Q0VAA5; IntAct: EBI-21824840; Score: 0.40
DE  Interaction: Q15392; IntAct: EBI-21824853; Score: 0.35
DE  Interaction: Q16850; IntAct: EBI-21824896; Score: 0.48
DE  Interaction: Q9H0R4; IntAct: EBI-21824921; Score: 0.35
DE  Interaction: Q9Y277; IntAct: EBI-21825091; Score: 0.35
DE  Interaction: Q8WTQ1; IntAct: EBI-21825173; Score: 0.35
DE  Interaction: Q9UN70; IntAct: EBI-21824946; Score: 0.35
DE  Interaction: P27671; IntAct: EBI-15700316; Score: 0.62
DE  Interaction: Q9Y613; IntAct: EBI-15727765; Score: 0.44
DE  Interaction: P32871; IntAct: EBI-15826481; Score: 0.44
DE  Interaction: P11762; IntAct: EBI-15826583; Score: 0.44
DE  Interaction: Q15036; IntAct: EBI-15922865; Score: 0.44
DE  Interaction: Q3UHD6; IntAct: EBI-15922897; Score: 0.44
DE  Interaction: Q6P8Y7; IntAct: EBI-15922948; Score: 0.44
DE  Interaction: Q9QZQ1; IntAct: EBI-16090964; Score: 0.44
DE  Interaction: Q8K4S1; IntAct: EBI-16091073; Score: 0.44
DE  Interaction: O43566; IntAct: EBI-16091115; Score: 0.44
DE  Interaction: Q9Y5Z9; IntAct: EBI-21006492; Score: 0.58
DE  Interaction: P04156; IntAct: EBI-21014654; Score: 0.35
DE  Interaction: P21359; IntAct: EBI-22017087; Score: 0.60
DE  Interaction: P15408; IntAct: EBI-25868789; Score: 0.56
DE  Interaction: O14641; IntAct: EBI-25868781; Score: 0.56
DE  Interaction: Q14117; IntAct: EBI-25868773; Score: 0.56
DE  Interaction: P24941; IntAct: EBI-25868765; Score: 0.56
DE  Interaction: P36406; IntAct: EBI-25868757; Score: 0.56
DE  Interaction: O94868; IntAct: EBI-25869031; Score: 0.56
DE  Interaction: Q86XR8; IntAct: EBI-25869023; Score: 0.56
DE  Interaction: Q99558; IntAct: EBI-25869015; Score: 0.56
DE  Interaction: Q86V28; IntAct: EBI-25869007; Score: 0.56
DE  Interaction: O95674; IntAct: EBI-25868999; Score: 0.56
DE  Interaction: Q96GN5; IntAct: EBI-25868991; Score: 0.56
DE  Interaction: Q9H2G9; IntAct: EBI-25868983; Score: 0.66
DE  Interaction: P15407; IntAct: EBI-25868975; Score: 0.56
DE  Interaction: Q92783; IntAct: EBI-25868967; Score: 0.56
DE  Interaction: O43829; IntAct: EBI-25868959; Score: 0.56
DE  Interaction: P19544; IntAct: EBI-25868951; Score: 0.56
DE  Interaction: P22415; IntAct: EBI-25868935; Score: 0.56
DE  Interaction: Q99598; IntAct: EBI-25868927; Score: 0.56
DE  Interaction: Q6PHZ7; IntAct: EBI-25868919; Score: 0.56
DE  Interaction: P54274; IntAct: EBI-25868911; Score: 0.56
DE  Interaction: Q13586; IntAct: EBI-25868903; Score: 0.66
DE  Interaction: P28290; IntAct: EBI-25868893; Score: 0.56
DE  Interaction: Q12824; IntAct: EBI-25868885; Score: 0.56
DE  Interaction: Q15435; IntAct: EBI-25868877; Score: 0.56
DE  Interaction: O15534; IntAct: EBI-25868869; Score: 0.56
DE  Interaction: Q9BR81; IntAct: EBI-25868861; Score: 0.56
DE  Interaction: P27338; IntAct: EBI-25868853; Score: 0.56
DE  Interaction: Q14847; IntAct: EBI-25868845; Score: 0.56
DE  Interaction: Q14525; IntAct: EBI-25868837; Score: 0.56
DE  Interaction: P08727; IntAct: EBI-25868829; Score: 0.56
DE  Interaction: Q9BVG8; IntAct: EBI-25868821; Score: 0.56
DE  Interaction: P10809; IntAct: EBI-25868813; Score: 0.56
DE  Interaction: O43248; IntAct: EBI-25868805; Score: 0.56
DE  Interaction: P52655; IntAct: EBI-25868797; Score: 0.56
DE  Interaction: O75886; IntAct: EBI-25869047; Score: 0.56
DE  Interaction: Q99996; IntAct: EBI-25869039; Score: 0.56
DE  Interaction: Q9UPR0; IntAct: EBI-25869125; Score: 0.56
DE  Interaction: Q13573; IntAct: EBI-25869117; Score: 0.56
DE  Interaction: O43482; IntAct: EBI-25869109; Score: 0.56
DE  Interaction: Q9Y6W6; IntAct: EBI-25869101; Score: 0.56
DE  Interaction: Q13435; IntAct: EBI-25869083; Score: 0.56
DE  Interaction: Q15311; IntAct: EBI-25869075; Score: 0.56
DE  Interaction: O75528; IntAct: EBI-25869065; Score: 0.56
DE  Interaction: Q96EZ8; IntAct: EBI-25869057; Score: 0.56
DE  Interaction: Q9H3R5; IntAct: EBI-25869321; Score: 0.56
DE  Interaction: Q49A88; IntAct: EBI-25869311; Score: 0.56
DE  Interaction: Q5JXC2; IntAct: EBI-25869303; Score: 0.56
DE  Interaction: Q9BXU0; IntAct: EBI-25869295; Score: 0.56
DE  Interaction: Q2M2Z5; IntAct: EBI-25869287; Score: 0.56
DE  Interaction: Q9H270; IntAct: EBI-25869277; Score: 0.56
DE  Interaction: Q9P2K3; IntAct: EBI-25869269; Score: 0.56
DE  Interaction: Q96LR2; IntAct: EBI-25869261; Score: 0.56
DE  Interaction: Q8NEH6; IntAct: EBI-25869253; Score: 0.56
DE  Interaction: Q9BZ95; IntAct: EBI-25869245; Score: 0.56
DE  Interaction: Q9NXL2; IntAct: EBI-25869237; Score: 0.56
DE  Interaction: Q8WVD3; IntAct: EBI-25869229; Score: 0.56
DE  Interaction: P57682; IntAct: EBI-25869221; Score: 0.56
DE  Interaction: Q53GQ0; IntAct: EBI-25869213; Score: 0.56
DE  Interaction: P53677; IntAct: EBI-25869205; Score: 0.56
DE  Interaction: Q9BY12; IntAct: EBI-25869195; Score: 0.56
DE  Interaction: Q9UGJ1; IntAct: EBI-25869187; Score: 0.56
DE  Interaction: Q9ULD4; IntAct: EBI-25869179; Score: 0.56
DE  Interaction: Q00994; IntAct: EBI-25869171; Score: 0.56
DE  Interaction: Q7Z637; IntAct: EBI-25869163; Score: 0.56
DE  Interaction: Q9UH77; IntAct: EBI-25869153; Score: 0.56
DE  Interaction: Q8N5V2; IntAct: EBI-25869145; Score: 0.56
DE  Interaction: Q13352; IntAct: EBI-25869135; Score: 0.56
DE  Interaction: Q9UII2; IntAct: EBI-25869471; Score: 0.56
DE  Interaction: Q9Y605; IntAct: EBI-25869463; Score: 0.56
DE  Interaction: Q9BT25; IntAct: EBI-25869455; Score: 0.56
DE  Interaction: Q8WUX9; IntAct: EBI-25869447; Score: 0.66
DE  Interaction: Q8IY31; IntAct: EBI-25869437; Score: 0.56
DE  Interaction: Q96HB5; IntAct: EBI-25869429; Score: 0.56
DE  Interaction: Q96I34; IntAct: EBI-25869421; Score: 0.56
DE  Interaction: Q5PSV4; IntAct: EBI-25869413; Score: 0.56
DE  Interaction: Q5T0J7; IntAct: EBI-25869389; Score: 0.56
DE  Interaction: Q8IUR5; IntAct: EBI-25869381; Score: 0.56
DE  Interaction: Q9GZM8; IntAct: EBI-25869373; Score: 0.56
DE  Interaction: Q9C0F3; IntAct: EBI-25869365; Score: 0.56
DE  Interaction: A0AVK6; IntAct: EBI-25869355; Score: 0.56
DE  Interaction: Q8NB25; IntAct: EBI-25869345; Score: 0.56
DE  Interaction: Q9BUL5; IntAct: EBI-25869337; Score: 0.56
DE  Interaction: Q9H7T9; IntAct: EBI-25869329; Score: 0.56
DE  Interaction: Q8N4C7; IntAct: EBI-25869657; Score: 0.56
DE  Interaction: Q494V2; IntAct: EBI-25869641; Score: 0.56
DE  Interaction: Q8IXN7; IntAct: EBI-25869633; Score: 0.56
DE  Interaction: Q8IV36; IntAct: EBI-25869625; Score: 0.56
DE  Interaction: Q9Y4F5; IntAct: EBI-25869617; Score: 0.56
DE  Interaction: Q86W54; IntAct: EBI-25869609; Score: 0.56
DE  Interaction: Q8IZU1; IntAct: EBI-25869601; Score: 0.56
DE  Interaction: Q8TBY0; IntAct: EBI-25869593; Score: 0.56
DE  Interaction: Q96LL4; IntAct: EBI-25869585; Score: 0.56
DE  Interaction: Q8TAC0; IntAct: EBI-25869577; Score: 0.56
DE  Interaction: Q8NA54; IntAct: EBI-25869569; Score: 0.56
DE  Interaction: Q6PF05; IntAct: EBI-25869561; Score: 0.56
DE  Interaction: Q6P597; IntAct: EBI-25869553; Score: 0.56
DE  Interaction: Q86WT6; IntAct: EBI-25869545; Score: 0.56
DE  Interaction: Q8NEZ2; IntAct: EBI-25869537; Score: 0.56
DE  Interaction: Q8NDH6; IntAct: EBI-25869529; Score: 0.56
DE  Interaction: Q495M9; IntAct: EBI-25869521; Score: 0.56
DE  Interaction: Q5T1C6; IntAct: EBI-25869505; Score: 0.56
DE  Interaction: A5D8V7; IntAct: EBI-25869495; Score: 0.56
DE  Interaction: Q96CS2; IntAct: EBI-25869487; Score: 0.56
DE  Interaction: Q96HT8; IntAct: EBI-25869479; Score: 0.56
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: Q3V6T2; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UPS8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O95297; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q13585; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UIW2; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8N8Z6; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q92738; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q12893; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O14683; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86T03; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P52799; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8N4V1; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O75695; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q14574; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q16625; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8IXS8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q99623; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P62330; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9BZF9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9C0B5; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O94854; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q06481; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NQ66; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8TCT9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q15768; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P35610; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P29320; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UEY8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P18085; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q53GL0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96GF1; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q02487; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NW97; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P36383; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UGH3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8WUY9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q13009; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NZ43; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q14118; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q99618; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O95379; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O14654; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86X27; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O95819; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NUE0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NRG9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P46531; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O43169; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P05067; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5T2T1; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8IZA0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y6A9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86UU1; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O14828; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P53350; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q15223; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P23229; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8WXF7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8TEY7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NX61; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P27797; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9HDC5; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P20340; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9ULF5; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8N0U8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P43307; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y394; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8IWE4; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O60488; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9BSJ8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5VU97; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9BY67; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P53794; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P35240; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5SQN1; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P51153; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9H8Y8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9H0X4; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P43003; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NRW7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O60716; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9H2J7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P47929; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9HC07; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y2J2; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P11717; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UHN6; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q658Y4; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q13433; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: A4D1S0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O00161; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O00213; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O15258; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P55196; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P27448; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8N5K1; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q13948; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O00303; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5VT25; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5HYI8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86X29; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P60468; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q6P9B6; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96C24; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96J84; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P23634; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UPY5; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O60308; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O75386; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O15020; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O75396; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q13873; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O60279; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UNK0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O43795; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O14653; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P30519; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q15907; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96FZ7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O00767; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9ULJ7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86Y82; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8NEW0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5VYK3; IntAct: EBI-27045317; Score: 0.48
DE  Interaction: Q15005; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P51572; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q6UWI4; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P49257; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O75410; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8TBZ3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96BY7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NW15; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q92597; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8N4C8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96A57; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9P2W9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O75955; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q02952; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P29317; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y5M8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O00400; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O60245; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q7KZI7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y3L5; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P29966; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P11802; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y287; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q99569; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y2U8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P49768; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8NE01; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9BRX8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8TAA9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P60953; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P04920; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q6NTF9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9ULC3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O00186; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5SWX8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8NBN3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O43399; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UQB8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O95208; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P20700; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8TBA6; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O60493; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8WV19; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q99755; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8N183; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O95070; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y6M4; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8NF37; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8N4S9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5W0Z9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8IV08; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5T3J3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P13591; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q6PL24; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q14156; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P15260; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q6YN16; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NX63; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9H3Q1; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: A0FGR8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P01116; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P51809; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O43752; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y5Y0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: A6NIZ1; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NS69; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O43303; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96S66; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NW68; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y6M5; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P08240; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q00587; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P63027; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96KC8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UL25; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y6Y8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86SQ0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96QD8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P17302; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8NFX7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P62937; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UHQ9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q14739; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96HY6; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8TEU7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8NFQ8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P07947; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O43402; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q07960; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O15400; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y624; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y679; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P05023; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P41091; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8N653; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96Q45; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P27824; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P78324; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P61026; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O95067; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9P1Q0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NNW5; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9C0E8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9HC56; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96A33; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q01650; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y6N7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q14789; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UGV2; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9BZF1; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q6IAA8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O15498; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9P0U3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O00124; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q13277; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9H792; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O15126; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q13308; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8N6T3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q15758; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86Y07; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P08195; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86W92; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8N9N7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P30405; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q00059; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P05556; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NQS3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O95249; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P49069; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P16435; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q07820; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P28288; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O95573; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O95159; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q14126; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9BYI3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q658P3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9H2H9; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P04439; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P53985; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O75915; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9ULH0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86YQ8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P07948; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P50402; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96AG4; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P41440; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P49006; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P78310; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q99808; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5ZPR3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y385; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P35613; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9BWH2; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9BXK5; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q7Z6K3; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q92575; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O00429; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P18031; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P98172; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9BX67; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q15738; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q07065; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9H1E5; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NPA0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5VV42; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q15643; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q13443; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P62820; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q15836; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86UP2; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P02786; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P62979; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P55011; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P43121; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NRY6; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P13804; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P51648; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q15043; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9H3N1; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P09543; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y6M7; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P30825; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q5JTV8; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NZ45; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O95292; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9Y295; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9UET6; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q92692; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P42167; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9P0L0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q8WTV0; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q96A49; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NRY5; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q6AI08; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q9HAV4; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q8N335; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q6IAN0; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q96T76; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: P50570; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q92538; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: P11172; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q9NVI1; IntAct: EBI-34580918; Score: 0.42
DE  Interaction: Q96GA7; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q9Y5L0; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q86Y56; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q9UIA9; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: P23919; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q9H845; IntAct: EBI-34580942; Score: 0.35
DE  Interaction: P49591; IntAct: EBI-34580942; Score: 0.35
DE  Interaction: Q29RF7; IntAct: EBI-34580942; Score: 0.35
DE  Interaction: P37268; IntAct: EBI-34580942; Score: 0.35
DE  Interaction: Q96AE4; IntAct: EBI-34580956; Score: 0.35
DE  Interaction: Q53EU6; IntAct: EBI-34580956; Score: 0.35
DE  Interaction: Q9HB71; IntAct: EBI-34580956; Score: 0.35
DE  Interaction: Q00341; IntAct: EBI-34580956; Score: 0.35
DE  Interaction: Q8WYP3; IntAct: EBI-34581538; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0098978;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:1905360;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003925;
GO  GO:0019003;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0008022;
GO  GO:0060612;
GO  GO:0009887;
GO  GO:0007166;
GO  GO:0071480;
GO  GO:0090398;
GO  GO:0006935;
GO  GO:0042832;
GO  GO:0006897;
GO  GO:0048144;
GO  GO:0097193;
GO  GO:0000165;
GO  GO:0008285;
GO  GO:0010629;
GO  GO:0034260;
GO  GO:0043524;
GO  GO:0051402;
GO  GO:2000251;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0050679;
GO  GO:0070374;
GO  GO:0048146;
GO  GO:0043547;
GO  GO:0032729;
GO  GO:0046330;
GO  GO:0043406;
GO  GO:0043410;
GO  GO:2000630;
GO  GO:0010863;
GO  GO:0001934;
GO  GO:0090314;
GO  GO:1900029;
GO  GO:0045944;
GO  GO:0090303;
GO  GO:0007265;
GO  GO:0051726;
GO  GO:0042127;
GO  GO:0048169;
GO  GO:0043405;
GO  GO:0098696;
GO  GO:0006357;
GO  GO:0007165;
GO  GO:0050852;
GO  GO:0042088;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8626715};
SQ  MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
SQ  VFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLV
SQ  REIRQHKLRKLNPPDESGPGCMSCKCVLS
//
ID  Q8NDT2;
PN  Putative RNA-binding protein 15B;
GN  RBM15B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:16129689}. Nucleus speckle {ECO:0000269|PubMed:19586903}. Nucleus envelope {ECO:0000269|PubMed:19586903}. Note=Colocalizes with BMLF1 in the nucleus. Localized in the nucleoplasm with a granular staining pattern and excluded from the nucleoli. {ECO:0000269|PubMed:16129689}.
DR  UNIPROT: Q8NDT2;
DR  UNIPROT: A4QPG7;
DR  UNIPROT: Q6QE19;
DR  UNIPROT: Q9BV96;
DR  Pfam: PF00076;
DR  Pfam: PF07744;
DR  PROSITE: PS50102;
DR  PROSITE: PS50917;
DR  OMIM: 612602;
DR  DisGeNET: 29890;
DE  Function: RNA-binding protein that acts as a key regulator of N6- methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:16129689, PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6- methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:27602518). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Functions in the regulation of alternative or illicit splicing, possibly by regulating m6A methylation (PubMed:16129689). Inhibits pre-mRNA splicing (PubMed:21044963). Also functions as a mRNA export factor by acting as a cofactor for the nuclear export receptor NXF1 (PubMed:19586903). {ECO:0000269|PubMed:19586903, ECO:0000269|PubMed:21044963, ECO:0000269|PubMed:27602518, ECO:0000305|PubMed:16129689}.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-25368403; Score: 0.37
DE  Interaction: P59595; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: O00487; IntAct: EBI-737465; Score: 0.00
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: P11161; IntAct: EBI-3916834; Score: 0.37
DE  Interaction: P63316; IntAct: EBI-3918552; Score: 0.37
DE  Interaction: Q8N8Y2; IntAct: EBI-3925656; Score: 0.37
DE  Interaction: Q8IVL1; IntAct: EBI-10269920; Score: 0.56
DE  Interaction: Q9UJX2; IntAct: EBI-10269936; Score: 0.56
DE  Interaction: Q15003; IntAct: EBI-11006706; Score: 0.35
DE  Interaction: Q96L14; IntAct: EBI-11022408; Score: 0.35
DE  Interaction: Q96FV9; IntAct: EBI-11034504; Score: 0.35
DE  Interaction: P43243; IntAct: EBI-11071398; Score: 0.35
DE  Interaction: Q86U44; IntAct: EBI-11136579; Score: 0.35
DE  Interaction: Q92997; IntAct: EBI-25257901; Score: 0.56
DE  Interaction: Q14627; IntAct: EBI-21561326; Score: 0.35
DE  Interaction: Q7Z4N8; IntAct: EBI-21583801; Score: 0.35
DE  Interaction: P36406; IntAct: EBI-21627506; Score: 0.35
DE  Interaction: Q9BWE0; IntAct: EBI-21627543; Score: 0.35
DE  Interaction: Q9BRX9; IntAct: EBI-21634215; Score: 0.35
DE  Interaction: Q9NZQ3; IntAct: EBI-21676174; Score: 0.35
DE  Interaction: Q86VM9; IntAct: EBI-21769401; Score: 0.35
DE  Interaction: Q96T37; IntAct: EBI-21889356; Score: 0.35
DE  Interaction: Q53GT1; IntAct: EBI-21889356; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21907689; Score: 0.35
DE  Interaction: P15659; IntAct: EBI-25768922; Score: 0.37
DE  Interaction: P03430; IntAct: EBI-25769351; Score: 0.37
DE  Interaction: P03427; IntAct: EBI-25769417; Score: 0.37
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9BYV2; IntAct: EBI-22027638; Score: 0.00
DE  Interaction: O60563; IntAct: EBI-25477219; Score: 0.35
DE  Interaction: O76071; IntAct: EBI-25477658; Score: 0.35
DE  Interaction: O76024; IntAct: EBI-25898596; Score: 0.56
DE  Interaction: P0DTC9; IntAct: EBI-27129711; Score: 0.35
DE  Interaction: P15130; IntAct: EBI-27131516; Score: 0.35
DE  Interaction: Q0ZME3; IntAct: EBI-27131755; Score: 0.35
DE  Interaction: Q6Q1R8; IntAct: EBI-27132003; Score: 0.35
DE  Interaction: K9N4V7; IntAct: EBI-27132270; Score: 0.35
DE  Interaction: P33469; IntAct: EBI-27132272; Score: 0.35
GO  GO:0005635;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0036396;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0009048;
GO  GO:0006406;
GO  GO:0006397;
GO  GO:0000381;
GO  GO:0001510;
GO  GO:0008380;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKRQSERDSSPSGRGSSSSAKRPREREREAEAGGRRAAHKASGGAKHPVPARARDKPRGSGSGGGGHRDGRGTGDANHRA
SQ  SSGRSSGSGAGGGGRGGKASGDPGASGMSPRASPLPPPPPPPGAEPACPGSSAAAPEYKTLLISSLSPALPAEHLEDRLF
SQ  HQFKRFGEISLRLSHTPELGRVAYVNFRHPQDAREARQHALARQLLLYDRPLKVEPVYLRGGGGSSRRSSSSSAAASTPP
SQ  PGPPAPADPLGYLPLHGGYQYKQRSLSPVAAPPLREPRARHAAAAFALDAAAAAAVGLSRERALDYYGLYDDRGRPYGYP
SQ  AVCEEDLMPEDDQRATRNLFIGNLDHSVSEVELRRAFEKYGIIEEVVIKRPARGQGGAYAFLKFQNLDMAHRAKVAMSGR
SQ  VIGRNPIKIGYGKANPTTRLWVGGLGPNTSLAALAREFDRFGSIRTIDHVKGDSFAYIQYESLDAAQAACAKMRGFPLGG
SQ  PDRRLRVDFAKAEETRYPQQYQPSPLPVHYELLTDGYTRHRNLDADLVRDRTPPHLLYSDRDRTFLEGDWTSPSKSSDRR
SQ  NSLEGYSRSVRSRSGERWGADGDRGLPKPWEERRKRRSLSSDRGRTTHSPYEERSRTKGSGQQSERGSDRTPERSRKENH
SQ  SSEGTKESSSNSLSNSRHGAEERGHHHHHHEAADSSHGKKARDSERNHRTTEAEPKPLEEPKHETKKLKNLSEYAQTLQL
SQ  GWNGLLVLKNSCFPTSMHILEGDQGVISSLLKDHTSGSKLTQLKIAQRLRLDQPKLDEVTRRIKQGSPNGYAVLLATQAT
SQ  PSGLGTEGMPTVEPGLQRRLLRNLVSYLKQKQAAGVISLPVGGSKGRDGTGMLYAFPPCDFSQQYLQSALRTLGKLEEEH
SQ  MVIVIVRDTA
//
ID  Q6PHZ5;
PN  Putative RNA-binding protein 15B;
GN  Rbm15b;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NDT2}. Nucleus speckle {ECO:0000250|UniProtKB:Q8NDT2}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NDT2}. Note=Colocalizes with BMLF1 in the nucleus. Localized in the nucleoplasm with a granular staining pattern and excluded from the nucleoli. {ECO:0000250|UniProtKB:Q8NDT2}.
DR  UNIPROT: Q6PHZ5;
DR  UNIPROT: Q8C6G2;
DR  PDB: 1WHY;
DR  Pfam: PF00076;
DR  Pfam: PF07744;
DR  PROSITE: PS50102;
DR  PROSITE: PS50917;
DE  Function: RNA-binding protein that acts as a key regulator of N6- methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA. Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex. Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist. Functions in the regulation of alternative or illicit splicing, possibly by regulating m6A methylation. Inhibits pre-mRNA splicing. Also functions as a mRNA export factor by acting as a cofactor for the nuclear export receptor NXF1. {ECO:0000250|UniProtKB:Q8NDT2}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0036396;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0009048;
GO  GO:0006406;
GO  GO:0006397;
GO  GO:0000381;
GO  GO:0001510;
GO  GO:0008380;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKRQSERDSSPSGRGSSSSAKRPREREREAEAGGRRAAHKASGGTKHPVPARARDKPRGSGGGGGHRDGRAAGDANHRAS
SQ  GGRSSGAPGGGGRTGKASGDPGAGGASPRASPLPPPPPPPGAEPAGPGSTAAPEYKTLLISSLSPALPAEHLEDRLFHQF
SQ  KRFGEISLRLSHTPELGRVAYVNFRHPQDAREARQHALARQLLLYDRPLKVEPVYLRGGGSSRRSSSSSAAASTPPPGPP
SQ  APADPLGYLPLHGGYQYKQRSLSPVAAPPLREPRARHAAAAFALDAAAAAAVGLSRERALDYYGLYDDRGRPYGYQAVCE
SQ  EDLMPEDDQRATRNLFIGNLDHSVSEVELRRAFEKYGIIEEVVIKRPARGQGGAYAFLKFQNLDMAHRAKVAMSGRVIGR
SQ  NPIKIGYGKANPTTRLWVGGLGPNTSLAALAREFDRFGSIRTIDHVKGDSFAYIQYESLDAAQAACAKMRGFPLGGPDRR
SQ  LRVDFAKAEETRYPQQYQPSPLPVHYELLTDGYTRHRNLDADLRVRDRTPPHLLYSDRDRTFLEGDWTSLSKSSDRRNSL
SQ  EGYSRSVRSRSGERWGGDGDRSIAKPWEERRKRRSLSSDRGRTTHSPYEERSRTKGGGQQSERGSDRTPERSRKENHSSE
SQ  GTKESGSNSLSNSRHGAEERSHHHHHHEAPDSSHGKKTRESERNHRTTEAEPKTLEEPKHETKKLKTLSEYAQTLQLGWN
SQ  GLLVLKNSCFPTSMHILEGDQGVISGLLKDHPSGSKLTQLKIAQRLRLDQPKLDEVTRRIKQGSPNGYAVLLAIQSTPSG
SQ  PGAEGMPVVEPGLQRRLLRNLVSYLKQKQAAGVISLPVGGSKGRDNTGMLYAFPPCDFSQQYLQSALRTLGKLEEEHMVI
SQ  VIVRDTA
//
ID  Q96T37;
PN  RNA-binding protein 15;
GN  RBM15;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus speckle {ECO:0000269|PubMed:19586903, ECO:0000269|PubMed:24100041}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17001072, ECO:0000269|PubMed:19786495, ECO:0000269|PubMed:24100041}. Nucleus envelope {ECO:0000269|PubMed:19586903}. Nucleus membrane {ECO:0000269|PubMed:19786495}; Peripheral membrane protein {ECO:0000269|PubMed:19786495}. Note=Colocalizes at the nuclear pore with DBP5 and NXF1. {ECO:0000269|PubMed:19786495}.
DR  UNIPROT: Q96T37;
DR  UNIPROT: A1A693;
DR  UNIPROT: Q3ZB86;
DR  UNIPROT: Q4V760;
DR  UNIPROT: Q5D058;
DR  UNIPROT: Q5T613;
DR  UNIPROT: Q86VW9;
DR  UNIPROT: Q96PE4;
DR  UNIPROT: Q96SC5;
DR  UNIPROT: Q96SC6;
DR  UNIPROT: Q96SC9;
DR  UNIPROT: Q96SD0;
DR  UNIPROT: Q96T38;
DR  UNIPROT: Q9BRA5;
DR  UNIPROT: Q9H6R8;
DR  UNIPROT: Q9H9Y0;
DR  Pfam: PF00076;
DR  Pfam: PF07744;
DR  PROSITE: PS50102;
DR  PROSITE: PS50917;
DR  OMIM: 606077;
DR  DisGeNET: 64783;
DE  Function: RNA-binding protein that acts as a key regulator of N6- methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (By similarity). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (By similarity). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (PubMed:26575292). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (By similarity). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (By similarity). May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (PubMed:17001072, PubMed:19786495). High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (PubMed:17001072, PubMed:19786495). May be implicated in HOX gene regulation (PubMed:11344311). {ECO:0000250|UniProtKB:Q0VBL3, ECO:0000269|PubMed:17001072, ECO:0000269|PubMed:19786495, ECO:0000269|PubMed:26575292, ECO:0000269|PubMed:27602518, ECO:0000305|PubMed:11344311}.
DE  Disease: Note=A chromosomal aberration involving RBM15 may be a cause of acute megakaryoblastic leukemia. Translocation t(1;22)(p13;q13) with MKL1. Although both reciprocal fusion transcripts are detected in acute megakaryoblastic leukemia (AMKL, FAB-M7), the RBM15-MKL1 chimeric protein has all the putative functional domains encoded by each gene and is the candidate oncogene. {ECO:0000269|PubMed:11344311, ECO:0000269|PubMed:11431691}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13137; IntAct: EBI-10293900; Score: 0.56
DE  Interaction: Q8NDT2; IntAct: EBI-21889356; Score: 0.35
DE  Interaction: Q8NFQ8; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: O60346; IntAct: EBI-2514920; Score: 0.54
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: P45983; IntAct: EBI-7235213; Score: 0.37
DE  Interaction: P78362; IntAct: EBI-6658735; Score: 0.44
DE  Interaction: Q7TSJ6; IntAct: EBI-8798662; Score: 0.27
DE  Interaction: Q8IVL1; IntAct: EBI-10293910; Score: 0.56
DE  Interaction: Q92841; IntAct: EBI-10293920; Score: 0.56
DE  Interaction: Q9BRK4; IntAct: EBI-10293942; Score: 0.56
DE  Interaction: Q9C0F1; IntAct: EBI-10293956; Score: 0.56
DE  Interaction: Q96L14; IntAct: EBI-11022408; Score: 0.35
DE  Interaction: O60825; IntAct: EBI-11070701; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-11105437; Score: 0.35
DE  Interaction: Q6PDM2; IntAct: EBI-11155641; Score: 0.35
DE  Interaction: Q68CZ1; IntAct: EBI-11368346; Score: 0.27
DE  Interaction: Q8N0Z3; IntAct: EBI-11392023; Score: 0.27
DE  Interaction: Q9UJV9; IntAct: EBI-11473486; Score: 0.35
DE  Interaction: Q9H2G4; IntAct: EBI-24501963; Score: 0.56
DE  Interaction: Q8IZP0; IntAct: EBI-24422299; Score: 0.56
DE  Interaction: I6T1Z2; IntAct: EBI-12581451; Score: 0.35
DE  Interaction: Q9NZQ3; IntAct: EBI-21676174; Score: 0.35
DE  Interaction: Q8N307; IntAct: EBI-21729950; Score: 0.35
DE  Interaction: Q86VM9; IntAct: EBI-21769401; Score: 0.35
DE  Interaction: P40967; IntAct: EBI-21773380; Score: 0.35
DE  Interaction: Q86U44; IntAct: EBI-20594935; Score: 0.35
DE  Interaction: Q15007; IntAct: EBI-20595349; Score: 0.35
DE  Interaction: Q12824; IntAct: EBI-20624550; Score: 0.27
DE  Interaction: Q09666; IntAct: EBI-20913094; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q9ULK4; IntAct: EBI-25472850; Score: 0.35
DE  Interaction: Q09161; IntAct: EBI-26396507; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-26396827; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574478; Score: 0.35
DE  Interaction: P07947; IntAct: EBI-30849745; Score: 0.44
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P35968; IntAct: EBI-32723270; Score: 0.27
DE  Interaction: Q12866; IntAct: EBI-32723870; Score: 0.27
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0036396;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0001569;
GO  GO:0009048;
GO  GO:0045638;
GO  GO:0060674;
GO  GO:0007221;
GO  GO:0000381;
GO  GO:0045652;
GO  GO:0001510;
GO  GO:0048536;
GO  GO:0038163;
GO  GO:0060412;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:19786495};
SQ  MRTAGRDPVPRRSPRWRRAVPLCETSAGRRVTQLRGDDLRRPATMKGKERSPVKAKRSRGGEDSTSRGERSKKLGGSGGS
SQ  NGSSSGKTDSGGGSRRSLHLDKSSSRGGSREYDTGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSA
SQ  PGGGDGAEYKTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVL
SQ  YDRPLKIEAVYVSRRRSRSPLDKDTYPPSASVVGASVGGHRHPPGGGGGQRSLSPGGAALGYRDYRLQQLALGRLPPPPP
SQ  PPLPRDLERERDYPFYERVRPAYSLEPRVGAGAGAAPFREVDEISPEDDQRANRTLFLGNLDITVTESDLRRAFDRFGVI
SQ  TEVDIKRPSRGQTSTYGFLKFENLDMSHRAKLAMSGKIIIRNPIKIGYGKATPTTRLWVGGLGPWVPLAALAREFDRFGT
SQ  IRTIDYRKGDSWAYIQYESLDAAHAAWTHMRGFPLGGPDRRLRVDFADTEHRYQQQYLQPLPLTHYELVTDAFGHRAPDP
SQ  LRGARDRTPPLLYRDRDRDLYPDSDWVPPPPPVRERSTRTAATSVPAYEPLDSLDRRRDGWSLDRDRGDRDLPSSRDQPR
SQ  KRRLPEESGGRHLDRSPESDRPRKRHCAPSPDRSPELSSSRDRYNSDNDRSSRLLLERPSPIRDRRGSLEKSQGDKRDRK
SQ  NSASAERDRKHRTTAPTEGKSPLKKEDRSDGSAPSTSTASSKLKSPSQKQDGGTAPVASASPKLCLAWQGMLLLKNSNFP
SQ  SNMHLLQGDLQVASSLLVEGSTGGKVAQLKITQRLRLDQPKLDEVTRRIKVAGPNGYAILLAVPGSSDSRSSSSSAASDT
SQ  ATSTQRPLRNLVSYLKQKQAAGVISLPVGGNKDKENTGVLHAFPPCEFSQQFLDSPAKALAKSEEDYLVMIIVRGFGFQI
SQ  GVRYENKKRENLALTLL
//
ID  Q0VBL3;
PN  RNA-binding protein 15;
GN  Rbm15;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus speckle {ECO:0000250|UniProtKB:Q96T37}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17283045}. Nucleus envelope {ECO:0000250|UniProtKB:Q96T37}. Nucleus membrane {ECO:0000250|UniProtKB:Q96T37}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96T37}. Note=Colocalizes at the nuclear pore with DBP5 and NXF1. {ECO:0000250|UniProtKB:Q96T37}.
DR  UNIPROT: Q0VBL3;
DR  UNIPROT: A0PJG5;
DR  UNIPROT: Q3THK4;
DR  UNIPROT: Q3TLX0;
DR  UNIPROT: Q571M7;
DR  UNIPROT: Q66JP8;
DR  UNIPROT: Q6PGG1;
DR  UNIPROT: Q7TT82;
DR  Pfam: PF00076;
DR  Pfam: PF07744;
DR  PROSITE: PS50102;
DR  PROSITE: PS50917;
DE  Function: RNA-binding protein that acts as a key regulator of N6- methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:29535189). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:29535189). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (By similarity). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (PubMed:17283045, PubMed:17376872, PubMed:18981216, PubMed:25468569). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (By similarity). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (PubMed:18981216). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (PubMed:25468569). May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (By similarity). High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing- mediated NXF1 deposition, resulting in export prior to splicing (By similarity). May be implicated in HOX gene regulation (By similarity). {ECO:0000250|UniProtKB:Q96T37, ECO:0000269|PubMed:17283045, ECO:0000269|PubMed:17376872, ECO:0000269|PubMed:18981216, ECO:0000269|PubMed:25468569, ECO:0000269|PubMed:29535189}.
DE  Reference Proteome: Yes;
DE  Interaction: P49452; IntAct: EBI-8573213; Score: 0.35
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: P70326; IntAct: EBI-16360068; Score: 0.35
DE  Interaction: Q3UL36; IntAct: EBI-26888124; Score: 0.35
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0036396;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0001569;
GO  GO:0009048;
GO  GO:0045638;
GO  GO:0000122;
GO  GO:0060674;
GO  GO:0007221;
GO  GO:0000381;
GO  GO:0045652;
GO  GO:0001510;
GO  GO:0048536;
GO  GO:0038163;
GO  GO:0060412;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q96T37};
SQ  MRSAGREPLPRRSPRWRRASPLCETSAGWRVSQLRRDDLRRPSTMKGKERSPVKPKRSRGGEDSSSRGERSKKLGGSGGS
SQ  NGSSSGKTDSGGSRRSLHLDKSSSRGGSREYETGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSAP
SQ  GGGDGVEYKTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVLY
SQ  DRPLKIEAVYVSRRRSRSPLDKDAYAPSSSVVGTSVGSHRHAPGGGGGQRSLSPGGAALGYRDYRLQQLALGRLPPPPPP
SQ  PLPRELERERDYPFYDRVRPAYSLEPRVGAGAGAAPFREVDEISPEDDQRANRTLFLGNLDITVTENDLRRAFDRFGVIT
SQ  EVDIKRPSRGQTSTYGFLKFENLDMSHRAKLAMSGKIIIRNPIKIGYGKATPTTRLWVGGLGPWVPLAALAREFDRFGTI
SQ  RTIDYRKGDSWAYIQYESLDAAHAAWTHMRGFPLGGPDRRLRVDFADTEHRYQQQYLQPLPLTHYELVTDTFGHRAPDPL
SQ  RSARDRTPPLLYRDRDRDLYTDSDWVPPPPPVRERSARAATSAVTAYEPLDSLDRRRDGWSLDRDRGDRDLPSSRDQPRK
SQ  RRLPEESGGRHLDRSPESERPRKQRHCTPSPDRSPELSSNRDRYNSDNDRSSRLLLLERSSPVRDRRGSLEKSQSDKRDR
SQ  KNSASAERDRKHRTAAPTEGKNPLKKEDRSDGNAPSASTSSSKQKPPSQKQDGGTAPVAASSPKLCLAWQGMLLLKNSNF
SQ  PSNMHLLQGDLQVASSLLVEGSTGGKVAQLKITQRLRLDQPKLDEVTRRIKVAGPNGYAILLAVPGSSDSRSSSSSATSD
SQ  TAASTQRPLRNLVSYLKQKQAAGVISLPVGGNKDKENTGVLHAFPPCEFSQQFLDSPAKALAKSEEDYLVMIIVRAKLVN
SQ  SG
//
ID  Q9H2T7;
PN  Ran-binding protein 17;
GN  RANBP17;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q9H2T7;
DR  UNIPROT: Q8IU74;
DR  Pfam: PF03810;
DR  OMIM: 606141;
DR  DisGeNET: 64901;
DE  Function: May function as a nuclear transport receptor. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P06028; IntAct: EBI-21557067; Score: 0.35
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005525;
GO  GO:0005049;
GO  GO:0031267;
GO  GO:0051028;
GO  GO:0006611;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALHFQSLAELEVLCTHLYIGTDLTQRIEAEKALLELIDSPECLSKCQLLLEQGTTSYAQLLAATCLSKLVSRVSPLPVE
SQ  QRMDIRNYILNYVASQPKLAPFVIQALIQVIAKITKLGWFEVQKDQFVFREIIADVKKFLQGTVEHCIIGVIILSELTQE
SQ  MNLVDYSRPSAKHRKIATSFRDTSLKDVLVLACSLLKEVFAKPLNLQDQCQQNLVMQVLKLVLNCLNFDFIGSSADESAD
SQ  DLCTVQIPTTWRTIFLEPETLDLFFNLYHSLPPLLSQLALSCLVQFASTRRSLFNSPERAKYLGNLIKGVKRILENPQGL
SQ  SDPGNYHEFCRFLARLKTNYQLGELVMVKEYPEVIRLIANFTITSLQHWEFAPNSVHYLLTLWQRMVASVPFVKSTEPHL
SQ  LDTYAPEITKAFITSRLDSVAIVVRDHLDDPLDDTATVFQQLEQLCTVSRCEYEKTCALLVQLFDQNAQNYQKLLHPYSG
SQ  VTVDITIQEGRLAWLVYLVGTVVGGRLTYTSTDEHDAMDGELSCRVFQLISLMDTGLPRCCNEKIELAILWFLDQFRKTY
SQ  VGDQLQRTSKVYARMSEVLGITDDNHVLETFMTKIVTNLKYWGRYEPVISRTLQFLNDLSVGYILLKKLVKIDAVKFMLK
SQ  NHTSEHFPFLGISDNHSLSDFRCRTTFYTALTRLLMVDLGEDEDEFENFMLPLTVAFETVLQIFNNNFKQEDVKRMLIGL
SQ  ARDLRGIAFALNTKTSYTMLFDWMYPTYLPLLQNAVERWYGEPTCTTPILKLMAELMQNRSQRLNFDVSSPNGILLFREA
SQ  SKMVCTYGNQILSLGSLSKDQIYPMKLKGISICYSALKSALCGNYVSFGVFKLYGDNHFDNVLQAFVKMLLSVSHSDLLQ
SQ  YRKLSQSYYPLLECLTQDHMSFIINLEPPVLMYVLTSISEGLTTLDTVVSSSCCTSLDYIVTYLFKHIAKEGKKPLRCRE
SQ  ATQAGQRLLHFMQQNPDVLQQMMSVLMNTIVFEDCRNQWSVSRPLLGLILLNEKYFSELRASLINSQPLPKQEVLAQCFR
SQ  NLMEGVEQNLSVKNRDRFTQNLSVFRRDVAEALRSDGNTEPCSLDMMS
//
ID  Q99NF8;
PN  Ran-binding protein 17;
GN  Ranbp17;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q99NF8;
DR  UNIPROT: Q9D4E3;
DR  Pfam: PF03810;
DE  Function: May function as a nuclear transport receptor. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005049;
GO  GO:0031267;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0006611;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MALHFQSLAELEVLCTHLYVGTDLTERIEAEKALLELIDSPECLSKCQLLLEQGTTSYAQLLAATCLSKLVTRINPLPIE
SQ  QRIDIRNYILNYVASQPKLAPFVIQALIQVIAKLTKLGWFEVQKDEFVFREIIADVKKFLQGTVEHCIIGVIILCELTQE
SQ  MNLVDYSRPSAKHRKIATSFRDTSLKDILVLACSLLKQVLAKPLNLQDQDQQSLVMQVLKLVLSCLNFDFLGSSADESAD
SQ  DLCTVQIPTTWRTIFLEPETLDLFFNLYHSLPPLLSQLALSCLVQFASTRRSLFSSPERAKYLGNLIKGVKRILENPQGL
SQ  SDPGNYHEFCRFLARLKTNYQLGELVLVKEYAEVIGLIANFTITSLQHWEFAPNSVHYLLTLWQRMVASVPFVKSAEPHL
SQ  LDTYAPEITKAFITSRLESVAIVVRDNLEDPLDDTATVFQQLEQLCTVSRCEYEKTCTLLVQLFDQNAQNYQKLLHAAPG
SQ  LAVDMAIQEGRLAWLIYLVGTVVGGRLTYTSTDEHDAMDGELSCRVFQLISLMDTRLPHCTNEKIELAVLWFLDQFRKTY
SQ  VGDQLQRTSKVYARMSEVLGITDDNHVLETFMTKIVTNLKYWGRCEPVISRTLQFLSDLSVGYILLKKLVKIDAVKFMLK
SQ  NHTSEHFPFLGISETYNVGDFRCRTTFYTALTRLLMVDLGEDEDEFENFMLPLTVSFETVLQIFNNNFKQEEVKRMLIGL
SQ  ARDLRGIAFALNTKTSYTMLFDWIYPAYLPVLQRAIERWYGEPACTTPILKLLAELMQNRSQRLNFDVSSPNGILLFREA
SQ  SKMICTYGNQILSLGSLSKDKIYPMKLKGISICYSALKSALCGNYVSFGVFKLYGDNHFDNVLQAFVKMLLSVSHSDLLQ
SQ  YRKLSQSYYPLLECLTQDHMSFITNLEPPVLLYVLTSLSEGLTTLDTVVSSSCCTSLDYMVTYLFKHIAKEGKKPLRSRE
SQ  AMQAGQRLLHFMQQNPDVLQQMMSVLMNTIVFEDCRNQWSVSRPLLGLILLNEKYFSELRASLINSQPLPKQEVLGQCFR
SQ  NLMEGVEQNLSVKNRDRFTQNLSVFRRDVAEALRSDGHTDLSSLDMMS
//
ID  Q9LMK7;
PN  Ran-binding protein 1 homolog a;
GN  RANBP1A;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q9LMK7;
DR  UNIPROT: O04149;
DR  UNIPROT: Q9XHS1;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P41917; IntAct: EBI-2325973; Score: 0.37
DE  Interaction: P41916; IntAct: EBI-2325839; Score: 0.37
DE  Interaction: Q8H156; IntAct: EBI-2326020; Score: 0.55
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005576;
GO  GO:0005643;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0050790;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATNEPEHEHRDEEEAGANEDEDTGAQVAPIVRLEEVAVTTGEEDEDAVLDLKSKLYRFDKDANQWKERGAGTVKFLKHK
SQ  NTGKIRLVMRQSKTLKICANHFVKSGMSVQEHVGNEKSCVWHARDFADGELKDELFCIRFASIENCKTFMQKFKEVAESE
SQ  EEKEESKDAADTAGLLEKLTVEETKTEEKTEAKAVETAKTEVKAEEKKESEAEKSGEAKKTEESGPST
//
ID  Q8RWG8;
PN  Ran-binding protein 1 homolog b;
GN  RANBP1B;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q8RWG8;
DR  UNIPROT: O04150;
DR  UNIPROT: O64739;
DR  UNIPROT: Q2HIH4;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P41917; IntAct: EBI-2325944; Score: 0.37
DE  Interaction: P41916; IntAct: EBI-2325884; Score: 0.37
DE  Interaction: Q8H156; IntAct: EBI-2325999; Score: 0.37
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005643;
GO  GO:0005777;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0015031;
GO  GO:0050790;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASISNEPERENRDEEETGANEDEDTGAQVAPIVRLEEVAVTTGEEDEDTILDLKSKLYRFDKDGSQWKERGAGTVKFLK
SQ  HRVSGKIRLVMRQSKTLKICANHLVGSGMSVQEHAGNDKSCVWHARDFSDGELKDELFCIRFASVENCKAFMQKFKEVAE
SQ  SEEEKEESKDASDTAGLLEKLTVEEKESEKKPVEKAEENKKSEAVEEKKTEESVPSA
//
ID  P92985;
PN  Ran-binding protein 1 homolog c;
GN  RANBP1C;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: P92985;
DR  UNIPROT: Q9LUZ8;
DR  Pfam: PF00638;
DR  PROSITE: PS50196;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005643;
GO  GO:0009536;
GO  GO:0051028;
GO  GO:0006606;
GO  GO:0050790;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASTEPERENREDETEVNEDEDTGAQVAPIVRLEEVAVTTGEEDEDAVLDLKSKMYRFDKEGNQWKERGAGTVKLLKHKE
SQ  TGKVRLVMRQSKTLKICANHLISSGMSVQEHSGNEKSCLWHATDFSDGELKDELFCIRFASIENCKTFMEKFTEIAESQQ
SQ  VGKESTQGDEAAGLIENLSVEENISEEKAKEAEEKEPAKEDKETKKEKVEEEKKTEAST
//
ID  P48820;
PN  E3 SUMO-protein ligase RanBP2;
GN  RANBP2;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P49792}. Nucleus membrane {ECO:0000250|UniProtKB:P49792}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49792}. Nucleus envelope {ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments. {ECO:0000250|UniProtKB:P49792}.
DR  UNIPROT: P48820;
DR  UNIPROT: Q28091;
DR  Pfam: PF12185;
DR  Pfam: PF00160;
DR  Pfam: PF00638;
DR  PROSITE: PS00170;
DR  PROSITE: PS50072;
DR  PROSITE: PS50196;
DE  Function: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single- stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin- 1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. {ECO:0000250|UniProtKB:P49792}.
DE  Reference Proteome: Yes;
GO  GO:0005642;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0003755;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0046907;
GO  GO:0051028;
GO  GO:0006457;
GO  GO:0000413;
GO  GO:0016925;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  KQKFEECQRLLLDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQTKVSDEESKDSRAGATTAADVSGAPNT
SQ  ETTGPTLEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPGKLNQSGASVGTDE
SQ  DSDVTQEEERDGQHFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDAGQWKERGIGDIKILQNYENKQVRIVMRRD
SQ  QVLKLCANHRITPDMTLQNMKGTERVWVWTACDFADGERKIEHLAVRFKLQDVADSFKKIFDEAKVAQEKDFLITPHVAR
SQ  SATPRESPCGKMAVAVLEETTRERTDLSQGDDAADTTSEVGGVSGTPEPTTKAVVSPPKFVFGSESVKSIFSSEKSKPFA
SQ  FGNSSATGSLFGFSFNTPLKNNSSEASSAAQSGSERKVEPGGRQESQNSDLKSASDGKVKNTSPAFLKEQFSTSHTFKTP
SQ  EKVEERKKPEDLPSDDDVLIVYELTPTPEQRALASRLQLPPTFFCYKNRPDYISEEEEDDEDFDTAVKKLNGKLYLDDSE
SQ  TCRLSEENVTDNEKECVIVWEKKPTVEELAKADTLKLPPTFFCGICSDTDEDNGNAEDFQSELQKVQEAQKSQDENIASS
SQ  ADGMCTDDTKVTVPFLCKSEEPEFTTKSVSSPSVSSGTVDKPVDLSTRKENDADSTSQVESKTVTFGFGSGPGLSFADLA
SQ  SSNSGDFAFGSKDKNFQWANTGAAVFGAQSTSKVGEDEDGSDEEVVHNEDIHFEPIVSLPEVEVKSGEEDEEILFKERAK
SQ  LYRWDREASQWKDRGVGDIKILWHTVKNYFRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWTASDYADGEAKVEQ
SQ  LAVRFKTKEMADCFKKKFEECQQNLLKPQKGQDSLTAEFSKETNPVVFFDICADDEPLGRITMELFSNIVPKTAENFRAL
SQ  CTGEKGFGFKSSIFHRVIPDFVCQGGDITKHDGTGGRSIYGDKFEDENFDVKHTGPGLLSMANRGQDTNNSQFFITLKKA
SQ  ERLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVSRRIIITECGQI
//
ID  A0A0B4K7J2;
PN  E3 SUMO-protein ligase RanBP2;
GN  Nup358;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49792}. Note=Localizes to annulate lamellae, stacked membrane sheets of the endoplasmic reticulum. Localizes to granules which travel from nurse cells into the ooplasm through ring canals connecting the cytoplasm of the two cell types. {ECO:0000269|PubMed:31626769}.
DR  UNIPROT: A0A0B4K7J2;
DR  UNIPROT: D3DMF2;
DR  UNIPROT: Q8SWV7;
DR  UNIPROT: Q9VBU7;
DR  Pfam: PF00638;
DR  Pfam: PF00641;
DR  PROSITE: PS50196;
DR  PROSITE: PS50293;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DE  Function: E3 SUMO-protein ligase (By similarity). Component of the nuclear pore complex (NPC), a complex required for trafficking across the nuclear envelope (PubMed:17682050). Required for nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner, but also for the nuclear import of specific proteins such as phosphorylated Mad or the sesquiterpenoid juvenile hormone receptor Met as part of the juvenile hormone signal transduction pathway (PubMed:27979731, PubMed:17682050, PubMed:17682050). Plays a role in nuclear mRNA export by recruiting the mRNA transport complex composed of Nxt1 and sbr/Nxf1 to the NPC (PubMed:14729961). Essential during germline development for transposon silencing and piRNA biogenesis probably by regulating piwi localization to the nucleus (PubMed:29735528). During oogenesis, required to form granules that modulate the biogenesis of annulate lamellae containing nuclear pore complex components (PubMed:31626769). {ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:27979731, ECO:0000269|PubMed:29735528, ECO:0000269|PubMed:31626769}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VU13; IntAct: EBI-218350; Score: 0.00
DE  Interaction: A1ZAC2; IntAct: EBI-218354; Score: 0.00
DE  Interaction: Q9XZC2; IntAct: EBI-507984; Score: 0.37
DE  Interaction: Q9VWE4; IntAct: EBI-510659; Score: 0.00
DE  Interaction: Q24090; IntAct: EBI-512941; Score: 0.37
DE  Interaction: P22469; IntAct: EBI-7377317; Score: 0.37
DE  Interaction: P34082; IntAct: EBI-9957277; Score: 0.53
GO  GO:0005642;
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0046872;
GO  GO:0019789;
GO  GO:0007281;
GO  GO:0035626;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0051292;
GO  GO:0034587;
GO  GO:0008284;
GO  GO:0010628;
GO  GO:1900182;
GO  GO:0046833;
GO  GO:0006606;
GO  GO:0050790;
GO  GO:0032880;
GO  GO:0010528;
GO  GO:0007419;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFTTRKEVDAHVHKMLGKLQPGRERDIKGLAVARLYMKVQEYPKAIEYLNGYLRVRDDAVGHNMIATCYSRLNPPDVTEA
SQ  LQHYQRSIQIDPRQSEVVIDACELLVKENNASITECARYWLDQANSLDLSGNKQVFNLRMRVNLADSNGERDDTSGGDGE
SQ  QNTLEILMYKELQARPQDVNIRIQLLRSYVEKMKIDQAFNYALKTELESKNCTSQSNEWYEQIWMVLFKIEMAKDVKKNW
SQ  RFWHFALHTLDRLVQLSLEGSGLADSSKQLFRLDQYLFKFSTSIERSGDAPQRDLHQACIDHFTGQLLLHAVTLIFKREV
SQ  LANKNKWMSTLRSALPLLLLGYQVRPIDDSSTNQWIKHCDAEQKQLIQMWRPQGAFRCAQLGRTLLGCLDRSQMEIKNDR
SQ  ENAEFDENKNSGNSMPGLFADSEELLASAHQQCLDKSWRSQIYQQLFTHAEHKLKDTSSHLVRNLRLQLPLFEWPNLAHI
SQ  ENYELQALVLPPHSLAQHVYLALGTDPNKLGDAPRVVFYEGFQRDVKQNLNYCGQDSISQVDVDLYLYATTIQTRRKLQI
SQ  QREVYDSSNLGNRNAAARPHMMPFANLVGQLGAPEQSNWWDLVVRLNSNQLITEGNRAEQRAQLQHGLEAVRGVNGPKAD
SQ  AIIIFQLGKILNSRSDRSSLEARIDTLYRQGFSILRHQHNQQMESYVRVFKYGSAGSTAAWQDLQSLAEEAVTYFSEKMF
SQ  RIGQYEQFLDEVRGLHLPMAYFLQSEACHHLEESSKLPRTSRDRYSERRRECLQKTQKLIKNDDKHPLIAAMHRHQQDRN
SQ  SRGIDNSFGSPDVHNNSSAYEDAEDDFYSHAAFSANRSRRQLEVTPVTPIVMAQPSQEMEQAVKQISKSLCVLKDDVSVG
SQ  MEAMRQDIKVLTEKFTGLEDLLKKIKISSRDTPTRDVDPAAALGLDDLFIIEDALAEHQQQQQHQQQQSHNQGAIHPVVP
SQ  NPYTSGFYNGMPNTPSAQERFLQGPYGSPMFNQNQMYNYYAAQAQAQAQAQFLRTPPAPGSIPPPNMFGPRNPNFGLPSM
SQ  FPPPTVPSVAPYIDAMGNFTQPPPSLIPPPAQPAAPPAPLNILESKPVVALPTPGFFNTTTPVFGASPIQVPQSKPLTVP
SQ  TVPIPSTAPAPPIAGTVNPPATTAVPPPVHIPQVAPSVPAQPPAPAPVSVPSMFNRALNNQPVEKEPPANVVITSSDPLP
SQ  KPTTASVQPTLSVTIPAQHIKPSLVQAPEQPAQSAQPAQPSVSGVGSLSFNFGSKSSESPFSFKTQVAKAAAEKQKEQEE
SQ  AEQNQSGATDPNKTLPQDTSADDYDPRPDFKPIIPLPDEVEVRTGEEGEDIKFTSRAKLFRYVDKEWKERGTGVIKILCD
SQ  KATGVSRVLMRRDQTHKVCANHTITADITINVANQDKDKKSLLWAANDFADEQVTLERFLVRFKTGELAEEFRVAFTKAS
SQ  EAAKSKETVKPTVNTAEKGSTATAPAAFKSFVTSTPAANSLINKPQEQTKTQPNPDPPATAAKSLFGTLSVSAAPATSAP
SQ  ASATPFASFSFTPNGSSGFGTSTASPFGNLSFGTASAVGSGNNTTLFTTALIKDNTVQGKTLQQESQLNKSNSSDAEEEY
SQ  VPTAQFVPVIALPDIVEVVTGEENEDVLFEHRAKLLRWDKEANEWKERGLGNMKLLRDRTDPNKVRLLMRREQVHKLCCN
SQ  QRLLPETKFTYATNCKAAVTWGAQDYSDEELTTALLAVRFKSQDICQQFLEAVQKAQQSIGNEPKKEEVPSAAGEKEKPI
SQ  KGFGDAFKPKAGSWNCQACYTNNGQDQLYCLACQEPKDATVPPKQSGLDQGNALNLTTSSSNKFSFGFASSATLPATGGF
SQ  SFGGATQPKEKPAVAVVTASASAPTSVQTAALGFGKSSMTSGFGDAFKPAVGSWSCSACYVNNPGESLYCSACDAPKNDT
SQ  VPQKEKSLGSGLNLPPTSKFSFGFGAAAAGDKDQAGDGATFNFAAMPAAVAPTTSIGSSSFTFSMTKPKPDQQQPNSTAA
SQ  KEDEDNDSQEVEEEENNTYFSPVIPLPDKIDVKTGEEDEELLYVHKAKLYRLNESDWKERGLGDVKILRHRQTKKLRVVM
SQ  RREQVFKICLNHVLNENVVYREKTETSWMFAVHDFSEGESVLERFTLRFKNKEVAQGFMEAIKNALNETAKPIEDSPVVG
SQ  SVSQSTEANKPSQKNDGAAKSRGGESEVLDVGKTSSVRPTTHEVIPPLPMTLPLLTLPQPLAKPNDYQTPATILFKGSSL
SQ  SRNNSSASEASKTPSSAFIFGSTDKSEPGKDAGPLANLQKLASGEGQGNVLGSIFRSGSSNENSSDGSVKFFFGGGNKAA
SQ  EQQKKDSSESVFGGNKADSQSPATQEAPKLAFGGIAAPVFGDANPFGGHKVNLQKSDGKEEPKSIIGGTPLLFGGSNAFG
SQ  IPKIETQSPAKDFVFGSAPAFGQMATFSFTAAKNEKEKDITSNNTTDLKAEGKEKKELVPETTSTFADLAKTGSTFADLA
SQ  SNPGGTFADLANKTGNDFANLSANSQGTTVGFNKSAGGGFYNLTHQNAFKNFESPQATEECDDDGDATTDDNYDPHYDAI
SQ  VELPDEIVVTTGEENETKLFGERAKLYRYDAESKQWKERGVGEIKVLEHPELQTFRLIMRQEQIHKLVLNMNISASLQMD
SQ  YMNAQMKSFLWAGYNYAVDAEGKVDTEGVLERLACRFAKEEIASEFLNTVNSCIKRAKALQGDEENKNDDAPEEQASS
//
ID  P49792;
PN  E3 SUMO-protein ligase RanBP2;
GN  RANBP2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:7775481}. Nucleus membrane {ECO:0000269|PubMed:11839768}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:23353830, ECO:0000269|PubMed:7603572}. Nucleus envelope {ECO:0000269|PubMed:20386726}. Note=Detected in diffuse and discrete intranuclear foci (PubMed:11839768). Cytoplasmic filaments (PubMed:7775481). {ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:7775481}.
DR  UNIPROT: P49792;
DR  UNIPROT: Q13074;
DR  UNIPROT: Q15280;
DR  UNIPROT: Q53TE2;
DR  UNIPROT: Q59FH7;
DR  PDB: 1RRP;
DR  PDB: 1XKE;
DR  PDB: 1Z5S;
DR  PDB: 2LAS;
DR  PDB: 3UIN;
DR  PDB: 3UIO;
DR  PDB: 3UIP;
DR  PDB: 4GA0;
DR  PDB: 4I9Y;
DR  PDB: 4L6E;
DR  PDB: 4LQW;
DR  PDB: 5CLL;
DR  PDB: 5CLQ;
DR  Pfam: PF12185;
DR  Pfam: PF00160;
DR  Pfam: PF00638;
DR  Pfam: PF00641;
DR  PROSITE: PS00170;
DR  PROSITE: PS50072;
DR  PROSITE: PS50196;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DR  OMIM: 601181;
DR  OMIM: 608033;
DR  DisGeNET: 5903;
DE  Function: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:22194619, PubMed:15931224). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22194619, ECO:0000269|PubMed:23353830, ECO:0000269|PubMed:7775481, ECO:0000303|PubMed:10078529}.
DE  Disease: Encephalopathy, acute, infection-induced, 3 (IIAE3) [MIM:608033]: A rapidly progressive encephalopathy manifesting in susceptible individuals with seizures and coma. It can occur within days in otherwise healthy children after common viral infections such as influenza and parainfluenza, without evidence of viral infection of the brain or inflammatory cell infiltration. Brain T2-weighted magnetic resonance imaging reveals characteristic symmetric lesions present in the thalami, pons and brainstem. {ECO:0000269|PubMed:19118815, ECO:0000269|PubMed:34400285}. Note=The disease is caused by variants affecting the gene represented in this entry. Mutations in the RANBP2 gene predispose to IIAE3, but by themselves are insufficient to make the phenotype fully penetrant; additional genetic and environmental factors are required (PubMed:19118815). {ECO:0000269|PubMed:19118815}. Note=A chromosomal aberration involving RANBP2 is a cause of chromosome 8p11 myeloproliferative syndrome. Translocation t(2;8)(q12;p11) with FGFR1. Chromosome 8p11 myeloproliferative syndrome is characterized by myeloid hyperplasia, eosinophilia and T-cell or B- cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. {ECO:0000269|PubMed:23041776}.
DE  Reference Proteome: Yes;
DE  Interaction: O14524; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-4373195; Score: 0.46
DE  Interaction: P46060; IntAct: EBI-21928721; Score: 0.62
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: O60260; IntAct: EBI-973169; Score: 0.64
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.75
DE  Interaction: P02768; IntAct: EBI-1224020; Score: 0.35
DE  Interaction: P01106; IntAct: EBI-1237540; Score: 0.35
DE  Interaction: P11388; IntAct: EBI-1773456; Score: 0.40
DE  Interaction: Q01320; IntAct: EBI-1775292; Score: 0.40
DE  Interaction: P03116; IntAct: EBI-7414341; Score: 0.40
DE  Interaction: P33176; IntAct: EBI-8602425; Score: 0.40
DE  Interaction: Q9Z0E3; IntAct: EBI-2549710; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: Q9QWT9; IntAct: EBI-2558911; Score: 0.40
DE  Interaction: Q07832; IntAct: EBI-2560950; Score: 0.40
DE  Interaction: Q5NET2; IntAct: EBI-2801802; Score: 0.00
DE  Interaction: Q81LI7; IntAct: EBI-2823809; Score: 0.00
DE  Interaction: A0A380PEL1; IntAct: EBI-2841285; Score: 0.00
DE  Interaction: Q0WCK7; IntAct: EBI-2842408; Score: 0.00
DE  Interaction: A0A380PDY1; IntAct: EBI-2856426; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q9GZQ8; IntAct: EBI-3045543; Score: 0.35
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-3437454; Score: 0.00
DE  Interaction: Q12802; IntAct: EBI-3449822; Score: 0.00
DE  Interaction: Q4LE39; IntAct: EBI-3449836; Score: 0.00
DE  Interaction: Q9Y613; IntAct: EBI-3449871; Score: 0.00
DE  Interaction: P30533; IntAct: EBI-3449926; Score: 0.00
DE  Interaction: P21675; IntAct: EBI-3450016; Score: 0.00
DE  Interaction: Q96RY7; IntAct: EBI-3450063; Score: 0.00
DE  Interaction: P49792; IntAct: EBI-3450084; Score: 0.00
DE  Interaction: P52292; IntAct: EBI-3931429; Score: 0.37
DE  Interaction: Q13616; IntAct: EBI-3933504; Score: 0.37
DE  Interaction: P62826; IntAct: EBI-3933494; Score: 0.76
DE  Interaction: Q14324; IntAct: EBI-5661299; Score: 0.00
DE  Interaction: Q53GG5; IntAct: EBI-5662564; Score: 0.00
DE  Interaction: O15169; IntAct: EBI-6169699; Score: 0.35
DE  Interaction: P05919; IntAct: EBI-6176256; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-6262548; Score: 0.53
DE  Interaction: Q9UBE8; IntAct: EBI-6381385; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6515052; Score: 0.53
DE  Interaction: Q8WYP5; IntAct: EBI-9050350; Score: 0.40
DE  Interaction: Q13043; IntAct: EBI-10049645; Score: 0.35
DE  Interaction: Q72497; IntAct: EBI-9943756; Score: 0.44
DE  Interaction: Q99853; IntAct: EBI-11317404; Score: 0.35
DE  Interaction: Q12952; IntAct: EBI-11318689; Score: 0.35
DE  Interaction: Q9C009; IntAct: EBI-11319301; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: P03220; IntAct: EBI-11722152; Score: 0.35
DE  Interaction: Q2MG95; IntAct: EBI-11733653; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q9Z1B5; IntAct: EBI-10996176; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q9BVL2; IntAct: EBI-11077390; Score: 0.35
DE  Interaction: E9Q3P4; IntAct: EBI-11086604; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: P18754; IntAct: EBI-21567271; Score: 0.35
DE  Interaction: P61769; IntAct: EBI-21675069; Score: 0.35
DE  Interaction: Q9BXS6; IntAct: EBI-21691494; Score: 0.35
DE  Interaction: Q9Y228; IntAct: EBI-21696444; Score: 0.35
DE  Interaction: Q8IYT4; IntAct: EBI-16421609; Score: 0.35
DE  Interaction: P70168; IntAct: EBI-15732742; Score: 0.36
DE  Interaction: Q921C5; IntAct: EBI-15847872; Score: 0.63
DE  Interaction: Q8TD16; IntAct: EBI-15847951; Score: 0.40
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: Q15628; IntAct: EBI-20737473; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-20901016; Score: 0.40
DE  Interaction: Q8N9W5; IntAct: EBI-20913366; Score: 0.40
DE  Interaction: Q92878; IntAct: EBI-20918244; Score: 0.40
DE  Interaction: Q6P4A8; IntAct: EBI-20931312; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q9Y275; IntAct: EBI-21266480; Score: 0.35
DE  Interaction: O00213; IntAct: EBI-21017901; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: O00499; IntAct: EBI-21385533; Score: 0.00
DE  Interaction: Q5NHH2; IntAct: EBI-22299104; Score: 0.37
DE  Interaction: P11234; IntAct: EBI-25376255; Score: 0.35
DE  Interaction: P83105; IntAct: EBI-25745135; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: Q9Y5P2; IntAct: EBI-26354638; Score: 0.35
DE  Interaction: P42685; IntAct: EBI-28935169; Score: 0.35
DE  Interaction: P53350; IntAct: EBI-28938281; Score: 0.35
DE  Interaction: Q86UX6; IntAct: EBI-28942129; Score: 0.35
DE  Interaction: Q96GD4; IntAct: EBI-28944360; Score: 0.35
DE  Interaction: Q9Y6S9; IntAct: EBI-28948011; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q05D32; IntAct: EBI-27113232; Score: 0.35
DE  Interaction: O15297; IntAct: EBI-27113880; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
DE  Interaction: Q07866; IntAct: EBI-30822114; Score: 0.44
DE  Interaction: P63165; IntAct: EBI-30826718; Score: 0.44
GO  GO:0005642;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0106068;
GO  GO:0046872;
GO  GO:0003723;
GO  GO:0031267;
GO  GO:0061665;
GO  GO:0019789;
GO  GO:0051642;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0051168;
GO  GO:0006913;
GO  GO:0033133;
GO  GO:0006457;
GO  GO:0000413;
GO  GO:0016925;
GO  GO:0006111;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRRSKADVERYIASVQGSTPSPRQKSMKGFYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAV
SQ  ECYRRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWLERAAKLFPGSPAIYKLKEQLLDCEGEDGWNKLFDLIQSELYV
SQ  RPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYA
SQ  NLMLLTLSTRDVQESRELLQSFDSALQSVKSLGGNDELSATFLEMKGHFYMHAGSLLLKMGQHSSNVQWRALSELAALCY
SQ  LIAFQVPRPKIKLIKGEAGQNLLEMMACDRLSQSGHMLLNLSRGKQDFLKEIVETFANKSGQSALYDALFSSQSPKDTSF
SQ  LGSDDIGNIDVREPELEDLTRYDVGAIRAHNGSLQHLTWLGLQWNSLPALPGIRKWLKQLFHHLPHETSRLETNAPESIC
SQ  ILDLEVFLLGVVYTSHLQLKEKCNSHHSSYQPLCLPLPVCKQLCTERQKSWWDAVCTLIHRKAVPGNVAKLRLLVQHEIN
SQ  TLRAQEKHGLQPALLVHWAECLQKTGSGLNSFYDQREYIGRSVHYWKKVLPLLKIIKKKNSIPEPIDPLFKHFHSVDIQA
SQ  SEIVEYEEDAHITFAILDAVNGNIEDAVTAFESIKSVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIK
SQ  IIDDSDSNLSVVKKLPVPLESVKEMLNSVMQELEDYSEGGPLYKNGSLRNADSEIKHSTPSPTRYSLSPSKSYKYSPKTP
SQ  PRWAEDQNSLLKMICQQVEAIKKEMQELKLNSSNSASPHRWPTENYGPDSVPDGYQGSQTFHGAPLTVATTGPSVYYSQS
SQ  PAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYPQQMHTPPVQSSSACMFSQEMYGPPALRFESPATGILSPRGDD
SQ  YFNYNVQQTSTNPPLPEPGYFTKPPIAAHASRSAESKTIEFGKTNFVQPMPGEGLRPSLPTQAHTTQPTPFKFNSNFKSN
SQ  DGDFTFSSPQVVTQPPPAAYSNSESLLGLLTSDKPLQGDGYSGAKPIPGGQTIGPRNTFNFGSKNVSGISFTENMGSSQQ
SQ  KNSGFRRSDDMFTFHGPGKSVFGTPTLETANKNHETDGGSAHGDDDDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAK
SQ  LFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQ
SQ  LAIRFKTPEEAALFKCKFEEAQSILKAPGTNVAMASNQAVRIVKEPTSHDNKDICKSDAGNLNFEFQVAKKEGSWWHCNS
SQ  CSLKNASTAKKCVSCQNLNPSNKELVGPPLAETVFTPKTSPENVQDRFALVTPKKEGHWDCSICLVRNEPTVSRCIACQN
SQ  TKSANKSGSSFVHQASFKFGQGDLPKPINSDFRSVFSTKEGQWDCSACLVQNEGSSTKCAACQNPRKQSLPATSIPTPAS
SQ  FKFGTSETSKTLKSGFEDMFAKKEGQWDCSSCLVRNEANATRCVACQNPDKPSPSTSVPAPASFKFGTSETSKAPKSGFE
SQ  GMFTKKEGQWDCSVCLVRNEASATKCIACQNPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEA
SQ  SATKCIACQNPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQCPSKQNQTTAIS
SQ  TPASSEISKAPKSGFEGMFIRKGQWDCSVCCVQNESSSLKCVACDASKPTHKPIAEAPSAFTLGSEMKLHDSSGSQVGTG
SQ  FKSNFSEKASKFGNTEQGFKFGHVDQENSPSFMFQGSSNTEFKSTKEGFSIPVSADGFKFGISEPGNQEKKSEKPLENGT
SQ  GFQAQDISGQKNGRGVIFGQTSSTFTFADLAKSTSGEGFQFGKKDPNFKGFSGAGEKLFSSQYGKMANKANTSGDFEKDD
SQ  DAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQV
SQ  LKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDT
SQ  GRAAKLIQRAEEMKSGLKDFKTFLTNDQTKVTEEENKGSGTGAAGASDTTIKPNPENTGPTLEWDNYDLREDALDDSVSS
SQ  SSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPAKLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLPDLV
SQ  EVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTER
SQ  VWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSRSSTPRESPCGKIAVAVLEETTRERT
SQ  DVIQGDDVADATSEVEVSSTSETTPKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNSSATGSLFGFSFNAPLKSNNSET
SQ  SSVAQSGSESKVEPKKCELSKNSDIEQSSDSKVKNLFASFPTEESSINYTFKTPEKAKEKKKPEDSPSDDDVLIVYELTP
SQ  TAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKLYLDGSEKCRPLEENTADNEKECIIVWEKKPTV
SQ  EEKAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELQKVQEAQKSQTEEITSTTDSVYTGGTEVMVPSFCKSEEPDSIT
SQ  KSISSPSVSSETMDKPVDLSTRKEIDTDSTSQGESKIVSFGFGSSTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVF
SQ  GTQSVGTQSAGKVGEDEDGSDEEVVHNEDIHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKI
SQ  LWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEEC
SQ  QQNLMKLQKGHVSLAAELSKETNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGFGFKNSIFHRVIPDF
SQ  VCQGGDITKHDGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVK
SQ  KIESFGSPKGSVCRRITITECGQI
//
ID  Q9ERU9;
PN  E3 SUMO-protein ligase RanBP2;
GN  Ranbp2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P49792}. Nucleus membrane {ECO:0000250|UniProtKB:P49792}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49792}. Nucleus envelope {ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments. {ECO:0000250|UniProtKB:P49792}.
DR  UNIPROT: Q9ERU9;
DR  UNIPROT: E9QM01;
DR  UNIPROT: Q61992;
DR  UNIPROT: Q8C9K9;
DR  Pfam: PF12185;
DR  Pfam: PF00160;
DR  Pfam: PF00638;
DR  Pfam: PF00641;
DR  PROSITE: PS00170;
DR  PROSITE: PS50072;
DR  PROSITE: PS50196;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DE  Function: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single- stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1 (By similarity). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. {ECO:0000250|UniProtKB:P49792}.
DE  Reference Proteome: Yes;
DE  Interaction: A8CG34; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: O14524; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: O15504; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: O43633; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: O75694; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P35658; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P35922; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: P37198; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P46060; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: P49790; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: P52948; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: P63165; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: P63279; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: P78406; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q12769; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: Q53GS7; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8NFH4; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8TD16; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: Q8WUM0; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9BTX1; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9BW27; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q62077; IntAct: EBI-651424; Score: 0.37
DE  Interaction: Q9DBC7; IntAct: EBI-654833; Score: 0.37
DE  Interaction: P63141; IntAct: EBI-651684; Score: 0.37
DE  Interaction: Q9WVS6; IntAct: EBI-973674; Score: 0.40
DE  Interaction: Q01320; IntAct: EBI-1773469; Score: 0.40
DE  Interaction: Q9Z0E3; IntAct: EBI-2549816; Score: 0.35
DE  Interaction: P18754; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: B4DQN6; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: O00505; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: O00629; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: Q9BW19; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: P43487; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: A8K394; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: Q9UBU9; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: P55854; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: P52292; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: Q9BXS6; IntAct: EBI-2555617; Score: 0.40
DE  Interaction: Q99666; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: Q80Z64; IntAct: EBI-8820601; Score: 0.35
DE  Interaction: Q923J1; IntAct: EBI-9661302; Score: 0.35
DE  Interaction: Q9HD42; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q6NUQ4; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q5T4S7; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9Y4R8; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P14373; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: O95373; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9HC62; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P98170; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9H568; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9NPJ8; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9P0U3; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q14527; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q96SK2; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q13751; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q96A33; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: O14715; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: O94905; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8WUM4; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q8TB61; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9HD47; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9UKK6; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9UKX7; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q69YH5; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q96KM6; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q7Z4Q2; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P36873; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9H9B4; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9UHQ1; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9UF83; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: A8K7Q2; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: P61956; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: O60678; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q9Y2D8; IntAct: EBI-11694681; Score: 0.35
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: Q9EPK7; IntAct: EBI-17172030; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885104; Score: 0.35
GO  GO:0005642;
GO  GO:0005737;
GO  GO:1990723;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0044614;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0106068;
GO  GO:0046872;
GO  GO:0003755;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0031267;
GO  GO:0061665;
GO  GO:0019789;
GO  GO:0051642;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0051168;
GO  GO:0006913;
GO  GO:0033133;
GO  GO:0006457;
GO  GO:0000413;
GO  GO:0016925;
GO  GO:0006111;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRRSKADVERYIASVQGSAPSPREKSMKGFYFAKLYYEAKEYDLAKKYISTYINVQERDPKAHRFLGLLYEVEENIDKAV
SQ  ECYKRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWVERAAKLFPGSPAIYKLKEQLLDCKGEDGWNKLFDLIQSELYA
SQ  RPDDIHVNIRLVELYRSNKRLKDAVAHCHEADRNTALRSSLEWNLCVVQTLKEYLESLQCLDSDKSTWRATNKDLLLAYA
SQ  NLMLLTLSTRDVQEGRELLESFDSALQSVKSSVGGNDELSATFLETKGHFYMHVGSLLLKMGQQSDIQWRALSELAALCY
SQ  LVAFQVPRPKVKLIKGEAGQNLLETMAHDRLSQSGHMLLNLSRGKQDFLKEVVESFANKSGQSALCDALFSSQSSKERSF
SQ  LGNDDIGNLDGQVPDPDDLARYDTGAVRAHNGSLQHLTWLGLQWNSLSTLPAIRKWLKQLFHHLPQETSRLETNAPESIC
SQ  ILDLEVFLLGVIYTSHLQLKEKCNSHHTSYQPLCLPLPVCRQLCTERQKTWWDAVCTLIHRKALPGTSAKLRLLVQREIN
SQ  SLRGQEKHGLQPALLVHWAQSLQKTGSSLNSFYDQREYIGRSVHYWRKVLPLLKMIRKKNSIPEPIDPLFKHFHSVDIQA
SQ  SEIGEYEEDAHITFAILDAVNGNIEDAMTAFESIKNVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIR
SQ  ILDDSDSNTSVVQKLPVPLESVKEMLNSVMQELEDYSEGGTLYKNGCWRSADSELKHSTPSPTKYSLSPSKSYKYSPKTP
SQ  PRWAEDQNSLLKMICQQVEAIKKEMQELKLNSNNSASPHRWPAEPYGQDPAPDGYQGSQTFHGAPLTVATTGPSVYYSQS
SQ  PAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYSQQMHTPPVQSSSACMFSQEMYGPPLRFESPATGILSPRGDDY
SQ  FNYNVQQTSTNPPLPEPGYFTKPPLVAHASRSAESKVIEFGKSNFVQPMQGEVIRPPLTTPAHTTQPTPFKFNSNFKSND
SQ  GDFTFSSPQVVAQPPSTAYSNSESLLGLLTSDKPLQGDGYSGLKPISGQASGSRNTFSFGSKNTLTENMGPNQQKNFGFH
SQ  RSDDMFAFHGPGKSVFTTAASELANKSHETDGGSAHGDEEDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDG
SQ  ESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFK
SQ  TPEEAALFKCKFEEAQNILKALGTNTSTAPNHTLRIVKESATQDNKDICKADGGNLNFEFQIVKKEGPYWNCNSCSFKNA
SQ  ATAKKCVSCQNTNPTSNKELLGPPLVENGFAPKTGLENAQDRFATMTANKEGHWDCSVCLVRNEPTVSRCIACQNTKSAS
SQ  SFVQTSFKFGQGDLPKSVDSDFRSVFSKKEGQWECSVCLVRNERSAKKCVACENPGKQFKEWHCSLCSVKNEAHAIKCVA
SQ  CNNPVTPSLSTAPPSFKFGTSEMSKPFRIGFEGMFAKKEGQWDCSLCFVRNEASATHCIACQYPNKQNQPTSCVSAPASS
SQ  ETSRSPKSGFEGLFPKKEGEWECAVCSVQNESSSLKCVACEASKPTHKPHEAPSAFTVGSKSQSNESAGSQVGTEFKSNF
SQ  PEKNFKVGISEQKFKFGHVDQEKTPSFAFQGGSNTEFKSIKDGFSFCIPVSADGFKFGIQEKGNQEKKSEKHLENDPSFQ
SQ  AHDTSGQKNGSGVVFGQTSSTFTFADLAKSTSREGFQFGKKDPNFKGFSGAGEKLFSSQSGKVAEKANTSSDLEKDDDAY
SQ  KTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEISQWKERGLGNLKILKNEVNGKLRMLMRREQVLKV
SQ  CANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDTGRA
SQ  AKLIQRAEEMKSGLKDFKTFLTNDQVKVTDEENASSGADAPSASDTTAKQNPDNTGPALEWDNYDLREDALDDSVSSSSV
SQ  HASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPAKLNQSGASVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVS
SQ  SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQTMKGTERVWV
SQ  WTACDFADGERKIEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSHLSTPRESPCGKIAIAVLEETTRERTDLT
SQ  QGDEVIDTTSEAGETSSTSETTPKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNSSATGSLFGFSFNAPLKNSNSEMTS
SQ  RVQSGSEGKVKPDKCELPQNSDIKQSSDGKVKNLSAFSKENSSTSYTFKTPEKAQEKSKPEDLPSDNDILIVYELTPTPE
SQ  QKALAEKLLLPSTFFCYKNRPGYVSEEEEDDEDYEMAVKKLNGKLYLDDSEKPLEENLADNDKECVIVWEKKPTVEERAK
SQ  ADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELRKVCEAQKSQNEKVTDRVGIEHIGETEVTNPVGCKSEEPDSDTKHSSS
SQ  SPVSGTMDKPVDLSTRKETDMEFPSKGENKPVLFGFGSGTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVFGTQTTS
SQ  KGGEDEDGSDEDVVHNEDIHFEPIVSLPEVEVKSGEEDEEVLFKERAKLYRWDRDVSQWKERGIGDIKILWHTMKKYYRI
SQ  LMRRDQVFKVCANHVITKAMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEMTESFKKKFEECQQNIIKLQNGH
SQ  TSLAAELSKDTNPVVFFDVCADGEPLGRIIMELFSNIVPQTAENFRALCTGEKGFGFKNSIFHRVVPDFICQGGDITKYN
SQ  GTGGQSIYGDKFDDENFDLKHTGPGLLSMANYGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESFGSPKGS
SQ  VSRRICITECGQL
//
ID  H2QII6;
PN  E3 SUMO-protein ligase RanBP2;
GN  RANBP2;
OS  9598;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:22959972}. Nucleus membrane {ECO:0000269|PubMed:22959972}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:22959972}. Nucleus envelope {ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments. {ECO:0000250|UniProtKB:P49792}.
DR  UNIPROT: H2QII6;
DR  PDB: 4GA1;
DR  PDB: 4GA2;
DR  Pfam: PF12185;
DR  Pfam: PF00160;
DR  Pfam: PF00638;
DR  Pfam: PF00641;
DR  PROSITE: PS00170;
DR  PROSITE: PS50072;
DR  PROSITE: PS50196;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DR  PROSITE: PS01358;
DR  PROSITE: PS50199;
DE  Function: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (By similarity). Binds single- stranded RNA (in vitro) (PubMed:22959972). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. {ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:22959972}.
DE  Reference Proteome: Yes;
GO  GO:0005642;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0046872;
GO  GO:0003755;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0051028;
GO  GO:0006607;
GO  GO:0006457;
GO  GO:0000413;
GO  GO:0016925;
GO  GO:0050790;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRRSKADVERYIASVQGSTPSPRQKSIKGFYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAV
SQ  ECYRRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWVERAAKLFPGSPAVYKLKEQLLDCEGEDGWNKLFDLIQSELYV
SQ  RPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYA
SQ  NLMLLTLSTRDVQESRELLESFDSALQSVKSLGGNDELSATFLEMKGHFYMHAGSLLLKMGQHSSNVQWRALSELAALCY
SQ  LIAFQVPRPKIKLIKGEAGQNLLEMMACDRLSQSGHMLLNLSRGKQDFLREIVETFANKSGQSALYDALFSSQSPKDTSF
SQ  LGSDDIGNIDVREPELEDLARYDVGAIRAHDGSLQHLTWLGLQWNSLPALPGIRKWLKQLFHHLPQETSRLETNAPESIC
SQ  ILDLEVFLLGVVYTSHLQLKEKCNSHHSSYQPLCLPLPVCKQLCTERQKSWWDAVCTLIHRKAVPGNAAKLRLLVQHEIN
SQ  TLRAQEKHGLQPALLVHWAKCLQKTGSGLNSFYDQREYIGRSVHYWKKVLPLLKIIKKKNSIPEPIDPLFKHFHSVDIQA
SQ  SEIVEYEEDAHITFAILDVVNGNIEDAMTAFESIQSVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIK
SQ  IIDDSDSNLSVVKKLPVPLESVKEMLKSVMQELEAYSEGGPLYTNGSLRNADSEIKHSTPSHTRYSLSPSKSYKYSPKTP
SQ  PRWAEDQNSLLKMICQQVEAIKKEMQELKLNSSNSASPHRWPTENYGPDSVPDGYQGSQTFHGAPLTVATTGPSVYYSQS
SQ  PAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYPQQMHTPPVQSSSACMFSQEMYGPPALRFESPATGILSPRGDD
SQ  YFNYNVQQTSTNPPLPEPGYFTKPPIAAHASRSAESKTIEFGKTNFVQPMPGEGLRPSLPTQAHTTQPTPFKFNSNFKSN
SQ  DGDFTFSSPQVVTQPPPAAYSNSESLLGLLTSDKPLQGDGYSGAKPIPGGQTIGPRNTFNFGSKNVSGISFTENMGSSQQ
SQ  KNSGFRRSDDMFTFHGPGKSVFGTPTLETANKNHETDGGSAHGDDDDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAK
SQ  LFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQ
SQ  LAIRFKTPEEAALFKCKFEEAQSILKAPGTNVATASNQAVRIVKEPTSHDNKDICKSDAGNLNFEFQFAKKEGSWWHCNS
SQ  CSLKNASTAKKCVSCQNLNPSNKELVGPPLAETVFTPKTSPENVQDRFALVTPKKEGHWDCSICLVRNEPTVSRCIACQN
SQ  TKSANKSGSSFVHQASFKFGQGDLPKPINSDFRSVFSTKEGQWDCSACLVQNEGSSTKCAACQNPRKQSLPATSIPTPAS
SQ  FKFGTSETSKTLKSGFEDMFAKKEGQWDCSSCLVRNEANATRCVACQNPDKPSPSTSVPAPASFKFGTSETSKAPKSGFE
SQ  GMFTKKEGQWDCSVCLVRNEASATKCVACQNPGKQNQTTSAVSTPASSETSRAPKSGFEGMFTKKEGQWDCSVCLVRNEA
SQ  SATKCIACQSPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQCPSKQNQTTAIS
SQ  TPASSEISKAPKSGFEGMFIRKGQWDCSVCCVQNESSSLKCVACDASKPTHKPIAEAPSAFTLGSEMKLHDSPGSQVGTG
SQ  FKSNFSEKASKFGNTEQGFKFGHVDQENSPSFMFQGSSNTEFKSTKEGFSIPVSADGFKFGISEPGNQEKKSEKPLENDT
SQ  GFQAQDISGQKNGSGVIFGQTSSTFTFADLAKSTSGEGFQFGKKDPNFKGFSGAGEKLFSSQYGKMANKANTSGDFEKDD
SQ  DAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQV
SQ  LKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDT
SQ  GRAAKLIQRAEEMKSGLKDFKTFLTNDQTKVTEEENKGSGTGAAGASDTTIKPNPENTGPTLEWDNYDLREDALDDSVSS
SQ  SSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPGKLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLPDLV
SQ  EVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTER
SQ  VWLWTAYDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSRSSTPRESPCGKIAVAVLEETTRERT
SQ  DVTQGDDVADAASEVEVSSTSETTTKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNTSATGSLFGFSFNAPLKSNNSET
SQ  SSVAQSGSESKVEPNKCELSKNSDIEQSSDSKVKNLSASFPTEESSINYTFKTPEKAKEKKKPEDSPSDDDVLIVYELTP
SQ  TAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKLYLEGSEKCRPLEENTADNEKECIIVWEKKPTV
SQ  EEKAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELQKVQEAQKSQTEEITSTTDSVYTGGTEVMVPSFCKSEEPDSIT
SQ  KSISSPSVSSETMDKPVDLSTRKEIDTDSTSQGESKIVSFGFGSSTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVF
SQ  GTQSVGTQSAGKVGEDEDGSDEEVVHNEDIHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKI
SQ  LWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEEC
SQ  QQNLMKLQKGHVSLAAELSKETNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGFGFKNSIFHRVIPDF
SQ  VCQGGDITKHDGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFFITLKKAELLDFKHVVFGFVKDGMDTVK
SQ  KIESFGSPKGSVCRRITITECGQI
//
ID  Q7Z3Z2;
PN  Protein RD3;
GN  RD3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q8BRE0}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q8BRE0}. Endosome {ECO:0000250|UniProtKB:Q8BRE0}. Nucleus {ECO:0000269|PubMed:26100624, ECO:0000269|PubMed:29030614}. Cytoplasm {ECO:0000269|PubMed:26100624, ECO:0000269|PubMed:29030614}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:29030614}. Note=Colocalizes with GUCY2E and GUCY2F in rods and cones photoreceptors. Colocalizes with GUK1 in photoreceptor inner segments and to a lesser extent in the outer plexiform layer (By similarity). Strong dot-like perinuclear staining in the epithelial cells (PubMed:29030614). {ECO:0000250|UniProtKB:Q8BRE0, ECO:0000269|PubMed:29030614}.
DR  UNIPROT: Q7Z3Z2;
DR  UNIPROT: A8K595;
DR  PDB: 6DRF;
DR  Pfam: PF14473;
DR  OMIM: 180040;
DR  OMIM: 610612;
DR  DisGeNET: 343035;
DE  Function: Plays a critical role in the regulation of enzymes involved in nucleotide cycle in photoreceptors (PubMed:29515371, PubMed:21928830, PubMed:21078983, PubMed:27471269, PubMed:30559291). Inhibits the basal catalytic activity and the GCAP-stimulated activity of GUCY2D and GUCY2F, two retinal guanylyl cyclases involved in the production of cGMP in photoreceptors (PubMed:21928830, PubMed:27471269, PubMed:29515371, PubMed:30559291). Involved in the transport of GUCY2D and GUCY2F to their target sites in the photoreceptor outer segment (PubMed:21078983). Up-regulates the activity of GUK1, a kinase that also plays an essential role for recycling GMP and indirectly, cGMP (PubMed:29515371). Plays an important role for the survival of rods and cones in the retina (By similarity). {ECO:0000250|UniProtKB:Q8BRE0, ECO:0000269|PubMed:21078983, ECO:0000269|PubMed:21928830, ECO:0000269|PubMed:27471269, ECO:0000269|PubMed:29515371, ECO:0000269|PubMed:30559291}.
DE  Disease: Leber congenital amaurosis 12 (LCA12) [MIM:610612]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:17186464}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: A2ABF9; IntAct: EBI-10257502; Score: 0.56
DE  Interaction: Q14232; IntAct: EBI-10257514; Score: 0.78
DE  Interaction: Q96HA8; IntAct: EBI-24753164; Score: 0.56
DE  Interaction: Q9NPB3; IntAct: EBI-24796266; Score: 0.56
DE  Interaction: Q96KQ7; IntAct: EBI-24461107; Score: 0.56
DE  Interaction: Q8NFP9; IntAct: EBI-21854615; Score: 0.35
DE  Interaction: Q7L592; IntAct: EBI-21854615; Score: 0.35
DE  Interaction: P50851; IntAct: EBI-21854615; Score: 0.35
DE  Interaction: P19086; IntAct: EBI-21854615; Score: 0.35
DE  Interaction: Q02846; IntAct: EBI-20719207; Score: 0.46
GO  GO:0120199;
GO  GO:0005737;
GO  GO:0005768;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0120200;
GO  GO:0031283;
GO  GO:0015031;
GO  GO:0050896;
GO  GO:0060041;
GO  GO:0007601;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLISWLRWNEAPSRLSTRSPAEMVLETLMMELTGQMREAERQQRERSNAVRKVCTGVDYSWLASTPRSTYDLSPIERLQ
SQ  LEDVCVKIHPSYCGPAILRFRQLLAEQEPEVQEVSQLFRSVLQEVLERMKQEEEAHKLTRQWSLRPRGSLATFKTRARIS
SQ  PFASDIRTISEDVERDTPPPLRSWSMPEFRAPKAD
//
ID  Q8BRE0;
PN  Protein RD3;
GN  Rd3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:21078983, ECO:0000269|PubMed:29515371}. Photoreceptor inner segment {ECO:0000269|PubMed:21078983, ECO:0000269|PubMed:29515371}. Endosome {ECO:0000269|PubMed:21078983}. Nucleus {ECO:0000269|PubMed:17186464}. Cytoplasm {ECO:0000250|UniProtKB:Q7Z3Z2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7Z3Z2}. Note=Colocalizes with GUCY2E and GUCY2F in rods and cones photoreceptors. Colocalizes with GUK1 in photoreceptor inner segments and to a lesser extent in the outer plexiform layer (PubMed:29515371). Strong dot-like perinuclear staining in the epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q7Z3Z2, ECO:0000269|PubMed:29515371}.
DR  UNIPROT: Q8BRE0;
DR  UNIPROT: Q3SYJ8;
DR  UNIPROT: Q9CRS3;
DR  UNIPROT: Q9JMF2;
DR  Pfam: PF14473;
DE  Function: Plays a critical role in the regulation of enzymes involved in nucleotide cycle in photoreceptors (PubMed:21078983, PubMed:27471269). Inhibits the basal catalytic activity and the GCAP- stimulated activity of GUCY2E and GUCY2F, two retinal guanylyl cyclases involved in the production of cGMP in photoreceptors (PubMed:27471269). Involved in the transport of GUCY2E and GUCY2F to their target sites in the photoreceptor outer segment (PubMed:21078983). Up-regulates the activity of GUK1, a kinase that also plays an essential role for recycling GMP and indirectly, cGMP (By similarity). Plays an important role for the survival of rods and cones in the retina (PubMed:8486383, PubMed:17186464). {ECO:0000250|UniProtKB:Q7Z3Z2, ECO:0000269|PubMed:17186464, ECO:0000269|PubMed:21078983, ECO:0000269|PubMed:27471269, ECO:0000269|PubMed:8486383}.
DE  Disease: Note=A spontaneous mutation leading to a frameshift and in an unstable truncated protein lacking the C-terminal 89 amino acids causes retinal degeneration. Homozygotes mice (called rd-3) display retinal degeneration, beginning at 3 weeks of age, characterized by complete loss of photoreceptor rod cells by 5 weeks, and cones by 8 weeks. {ECO:0000269|PubMed:17186464, ECO:0000269|PubMed:8486383}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8BMK4; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q07797; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P15409; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P38647; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q925I1; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q8CAQ8; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: O08553; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P10126; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: O35129; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P20152; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P62874; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P29974; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P15499; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P27546; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q9D6R2; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q01853; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q91VR2; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q61595; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P27664; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P16858; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q8CJ40; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P46460; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q7TPR4; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: O70318; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P15105; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P20029; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q8BH59; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P20612; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q8VDN2; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P51881; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P20443; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P17182; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q03265; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P46096; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q6PIC6; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P48962; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q5SDA5; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q68FD5; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P63017; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P56480; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P05213; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P16546; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P99024; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: Q62261; IntAct: EBI-20718973; Score: 0.35
DE  Interaction: P52785; IntAct: EBI-20718973; Score: 0.35
GO  GO:0120199;
GO  GO:0005737;
GO  GO:0005768;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0001750;
GO  GO:0120200;
GO  GO:0031283;
GO  GO:0015031;
GO  GO:0050896;
GO  GO:0060041;
GO  GO:0007601;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLIPWLRWNDTPPRLSARTPAEMVLETLMMELAGQMREVERQQRERRSAVRKICTGVDYSWLANTPRPTYDISPGERLQ
SQ  LEDVCAKIHPSYCGPAILRFRQLLAEREPEVQEVARLFRSVLQEALEKMKQEEEAHKLTRQWSLRPRGSLSSFKTRARIA
SQ  PFASDIRTISEDVERDAPPPPRTWSMPEFRAPQAD
//
ID  P90897;
PN  DEAD-box ATP-dependent RNA helicase rde-12;
GN  rde;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:24684931}. Cytoplasmic granule {ECO:0000269|PubMed:24684930, ECO:0000269|PubMed:24684931}. Cytoplasm {ECO:0000269|PubMed:24684931}. Cytoplasm, P-body {ECO:0000269|PubMed:24684930}. Note=Colocalizes with pgl-1 in perinuclear P granules. Colocalizes with rsd-6 in a subset of germline and embryonic foci. {ECO:0000269|PubMed:24684930}.
DR  UNIPROT: P90897;
DR  UNIPROT: G3MU56;
DR  UNIPROT: G3MU57;
DR  Pfam: PF00270;
DR  Pfam: PF00271;
DR  PROSITE: PS00039;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51195;
DE  Function: Probable ATP-dependent RNA helicase involved in RNAi-mediated gene silencing (PubMed:24684930, PubMed:24684931). Specifically required in the endogenous siRNA pathway for biogenesis of secondary endogenous small interfering RNA (siRNA) intermediates called 22G-RNAs (PubMed:24684930, PubMed:24684931). May associate with and recruit rde- 10 to primary siRNA-targeted mRNA for secondary siRNA synthesis (PubMed:24684930). May be recruited to target mRNAs by rde-1 and/or ergo-1 (PubMed:24684930, PubMed:24684931). {ECO:0000269|PubMed:24684930, ECO:0000269|PubMed:24684931}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0043186;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0031332;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0019899;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0030154;
GO  GO:0007276;
GO  GO:0006417;
GO  GO:0043330;
GO  GO:0030422;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSFGNNAGGGGREYHDDRSNRDHRHGNGGSDAGQRRREDHNSSYQSYRRPDGRQDSYGGGHQGNHGNSYGRREDDRSHS
SQ  RDNHGGSRYGERDDRGNNGRSADNRYSQSNYNYDSNRGGQHYQRDNHGSKDDRGPMNQYNDHGSNHNSNSRNDQYRQGSY
SQ  QGDGHSGYRRDDDRRRNDNDQARPYQSNRDSDRNSPRDHHNYNSQSSPRSHQGGQDRYSAPKEDNQRRYDNHQGGHDSYR
SQ  GQNSGGYSGNNSGEYRNDYRSQQDSRDHRSGGNNSSSGFKNDGGFGGNDNRGFGNNGGGSFGNPNNSYRGNSNNIGGFHR
SQ  SDGSNSEGVNAPVRAPRDWVPVTRDIDELVRETADRLADCDVGQDRAVEIRNAEKDVRLTSWTNSGLHPTILETLKRIKY
SQ  NNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEETRNKARQDDGPLALILAPTRELAAQIHEALRT
SQ  YCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQDMKKDPLGHLGAII
SQ  KDAGFMESAATRQTIMTSATFNASVMTVANELMKRLPGQDEMIKIVLANGRLSKRVNLEFFECKGLAEKNAKLREILKQN
SQ  VNGKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVINF
SQ  DLPDGDPDQGADTFIHRAGRTGRTGRKENGLCVSFVDPQSDRDSLLAPKLVELIISQNLPDLKVPDFLDAMAKSSRGKSG
SQ  TSGFGQRGGYGGRGGGFGGTGRGRGGGVFGGGGRGGDFGGSGNFGGSGGGGSFGGSGGGGGFGGVKPSGFGGSRNNAEPT
SQ  SSGGGFGAPKAPTGFPSDNNDASEDAPAAGGFGFSTKAAQDAKKAEESATLGSSTFGTANNADEEPTETGADGNDDDEW
//
ID  F1RCY6;
PN  Regulator of nonsense transcripts 1;
GN  upf1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9EPU0}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q92900}. Nucleus {ECO:0000250|UniProtKB:Q92900}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9EPU0}.
DR  UNIPROT: F1RCY6;
DR  UNIPROT: A0A0R4IY20;
DR  UNIPROT: Q7ZVZ4;
DR  Pfam: PF13086;
DR  Pfam: PF13087;
DR  Pfam: PF04851;
DR  Pfam: PF18141;
DR  Pfam: PF09416;
DR  PROSITE: PS51997;
DE  Function: RNA-dependent helicase and ATPase required for nonsense- mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. The formation of an upf1-upf2-upf3 surveillance complex is believed to activate NMD. {ECO:0000250|UniProtKB:Q92900}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0003677;
GO  GO:0016787;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0008270;
GO  GO:0043009;
GO  GO:0000956;
GO  GO:0000184;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTQGQTQSQLDNQVNGPDGVLPNGEDAVGKTSQLLA
SQ  ELNFEEDEEDTYYTKDLPVHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVL
SQ  ECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQ
SQ  INKLEELWKENPTATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKR
SQ  IAYFTLPKTDSGDMRLMQGDEICLRYKGDMAPLWKGIGHVIKVPDNYGDEIAIELRSSAGAPVEVPHNFQVDFVWKSTSF
SQ  DRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKTV
SQ  TSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQL
SQ  KDETGELSSSDEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVVLGAKQLILV
SQ  GDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRLKKGFDFQWP
SQ  QPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTRLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQE
SQ  VEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLNYYKEQKVLVE
SQ  GPLNNLRESLMQFSKPRKLVNTINPGARFMSTAMYDAREAMIPGSVYDRSSTGRPSNMYFQTHDQVGMIGTGPNPMGSLN
SQ  IPIPFNLVMPPMPPPGYLGQVNGPAAGRGAPKGKTGGRGGRQRNRGTGNHGSGQPNMPNSQASQDLVSQPFSQGPLTQGY
SQ  ITMSQPSQMSQPGLSQPELSQDSYLGDEFKSQMDVALSQDSTYQGERAYQHGGVTGLSQY
//
ID  Q92900;
PN  Regulator of nonsense transcripts 1;
GN  UPF1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:11163187}. Cytoplasm, P-body. Nucleus {ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:18362360}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9EPU0}. Note=Hyperphosphorylated form is targeted to the P-body, while unphosphorylated protein is distributed throughout the cytoplasm. Localized in the chromatoid bodies of round spermatids (By similarity). {ECO:0000250|UniProtKB:Q9EPU0}.
DR  UNIPROT: Q92900;
DR  UNIPROT: O00239;
DR  UNIPROT: O43343;
DR  UNIPROT: Q86Z25;
DR  UNIPROT: Q92842;
DR  PDB: 2GJK;
DR  PDB: 2GK6;
DR  PDB: 2GK7;
DR  PDB: 2IYK;
DR  PDB: 2WJV;
DR  PDB: 2WJY;
DR  PDB: 2XZO;
DR  PDB: 2XZP;
DR  PDB: 6EJ5;
DR  PDB: 6Z3R;
DR  Pfam: PF13086;
DR  Pfam: PF13087;
DR  Pfam: PF04851;
DR  Pfam: PF18141;
DR  Pfam: PF09416;
DR  PROSITE: PS51997;
DR  OMIM: 601430;
DR  DisGeNET: 5976;
DE  Function: RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs (PubMed:11163187, PubMed:16086026, PubMed:18172165, PubMed:21145460, PubMed:21419344, PubMed:24726324). Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD (PubMed:11544179, PubMed:25220460). Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (PubMed:19417104). In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD (PubMed:21419344). Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation and allowing the recycling of NMD factors (PubMed:12554878). UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways (PubMed:18447585). Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2 (PubMed:16086026, PubMed:18172165). For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed (PubMed:18447585, PubMed:25220460). The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD (PubMed:21145460). Together with UPF2 and dependent on TDRD6, mediates the degradation of mRNA harboring long 3'UTR by inducing the NMD machinery (By similarity). Also capable of unwinding double-stranded DNA and translocating on single-stranded DNA (PubMed:30218034). {ECO:0000250|UniProtKB:Q9EPU0, ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:11544179, ECO:0000269|PubMed:12554878, ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:18447585, ECO:0000269|PubMed:19417104, ECO:0000269|PubMed:21145460, ECO:0000269|PubMed:21419344, ECO:0000269|PubMed:24726324, ECO:0000269|PubMed:25220460, ECO:0000269|PubMed:30218034}.
DE  Reference Proteome: Yes;
DE  Interaction: O15234; IntAct: EBI-15784788; Score: 0.70
DE  Interaction: Q14203; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: O95777; IntAct: EBI-374478; Score: 0.00
DE  Interaction: O77932; IntAct: EBI-374506; Score: 0.00
DE  Interaction: P54198; IntAct: EBI-374148; Score: 0.00
DE  Interaction: Q9UI30; IntAct: EBI-374151; Score: 0.00
DE  Interaction: Q96CS7; IntAct: EBI-374154; Score: 0.00
DE  Interaction: Q6IA69; IntAct: EBI-374157; Score: 0.00
DE  Interaction: Q9NR19; IntAct: EBI-374160; Score: 0.00
DE  Interaction: O95870; IntAct: EBI-374163; Score: 0.00
DE  Interaction: Q9BQY4; IntAct: EBI-374166; Score: 0.00
DE  Interaction: Q5VT52; IntAct: EBI-374169; Score: 0.00
DE  Interaction: Q9UJJ9; IntAct: EBI-374172; Score: 0.00
DE  Interaction: O95793; IntAct: EBI-536589; Score: 0.71
DE  Interaction: Q9HAU5; IntAct: EBI-536644; Score: 0.95
DE  Interaction: Q9BZI7; IntAct: EBI-536644; Score: 0.85
DE  Interaction: Q9NPI6; IntAct: EBI-1006512; Score: 0.78
DE  Interaction: Q8IU60; IntAct: EBI-1006558; Score: 0.64
DE  Interaction: Q6P2E9; IntAct: EBI-1006676; Score: 0.35
DE  Interaction: Q96F86; IntAct: EBI-1006676; Score: 0.35
DE  Interaction: Q92900; IntAct: EBI-1013658; Score: 0.35
DE  Interaction: Q9H1J1; IntAct: EBI-1013658; Score: 0.56
DE  Interaction: Q08491; IntAct: EBI-1015023; Score: 0.40
DE  Interaction: P63104; IntAct: EBI-7196933; Score: 0.40
DE  Interaction: Q92597; IntAct: EBI-1191079; Score: 0.40
DE  Interaction: P02787; IntAct: EBI-1221355; Score: 0.35
DE  Interaction: Q9UL03; IntAct: EBI-7390665; Score: 0.40
DE  Interaction: Q9UL18; IntAct: EBI-7641372; Score: 0.35
DE  Interaction: Q9UKV8; IntAct: EBI-7641372; Score: 0.35
DE  Interaction: P62495; IntAct: EBI-7801134; Score: 0.35
DE  Interaction: P15170; IntAct: EBI-7801176; Score: 0.40
DE  Interaction: Q96Q15; IntAct: EBI-7801538; Score: 0.76
DE  Interaction: P38919; IntAct: EBI-1776452; Score: 0.73
DE  Interaction: Q13868; IntAct: EBI-1776452; Score: 0.35
DE  Interaction: Q8IZH2; IntAct: EBI-1776452; Score: 0.53
DE  Interaction: O00303; IntAct: EBI-1776488; Score: 0.35
DE  Interaction: Q14152; IntAct: EBI-1776488; Score: 0.62
DE  Interaction: Q9BY44; IntAct: EBI-1776650; Score: 0.35
DE  Interaction: P55884; IntAct: EBI-1776650; Score: 0.35
DE  Interaction: P20042; IntAct: EBI-1780552; Score: 0.35
DE  Interaction: Q7ARD3; IntAct: EBI-2856375; Score: 0.00
DE  Interaction: P03372; IntAct: EBI-2878124; Score: 0.35
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: P11940; IntAct: EBI-3903950; Score: 0.53
DE  Interaction: Q86US8; IntAct: EBI-3400857; Score: 0.50
DE  Interaction: Q92540; IntAct: EBI-3400857; Score: 0.53
DE  Interaction: Q9UPR3; IntAct: EBI-3400857; Score: 0.50
DE  Interaction: Q9Y5S9; IntAct: EBI-3867797; Score: 0.64
DE  Interaction: Q15287; IntAct: EBI-3867801; Score: 0.35
DE  Interaction: Q8IYB3; IntAct: EBI-3867832; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-3867844; Score: 0.35
DE  Interaction: Q86V81; IntAct: EBI-3867856; Score: 0.35
DE  Interaction: P35659; IntAct: EBI-3869271; Score: 0.40
DE  Interaction: Q8IYD1; IntAct: EBI-3869636; Score: 0.58
DE  Interaction: Q149F3; IntAct: EBI-3870213; Score: 0.40
DE  Interaction: Q12796; IntAct: EBI-3903305; Score: 0.37
DE  Interaction: Q9NPJ4; IntAct: EBI-3903302; Score: 0.62
DE  Interaction: P26196; IntAct: EBI-4302807; Score: 0.27
DE  Interaction: P62913; IntAct: EBI-3903945; Score: 0.35
DE  Interaction: P13639; IntAct: EBI-3903945; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-3903950; Score: 0.53
DE  Interaction: Q09161; IntAct: EBI-3903950; Score: 0.69
DE  Interaction: P62424; IntAct: EBI-3903973; Score: 0.35
DE  Interaction: P62753; IntAct: EBI-3903973; Score: 0.35
DE  Interaction: Q8ND04; IntAct: EBI-3903928; Score: 0.35
DE  Interaction: Q9H0W8; IntAct: EBI-3903928; Score: 0.35
DE  Interaction: P23396; IntAct: EBI-3903935; Score: 0.35
DE  Interaction: P67870; IntAct: EBI-7137830; Score: 0.37
DE  Interaction: O14746; IntAct: EBI-7068109; Score: 0.52
DE  Interaction: Q96AP0; IntAct: EBI-7068137; Score: 0.52
DE  Interaction: Q6QDQ4; IntAct: EBI-5276631; Score: 0.35
DE  Interaction: O95758; IntAct: EBI-7850130; Score: 0.35
DE  Interaction: P03496; IntAct: EBI-6154589; Score: 0.53
DE  Interaction: O56264; IntAct: EBI-6157161; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6189915; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q93034; IntAct: EBI-21331078; Score: 0.35
DE  Interaction: Q4VGL6; IntAct: EBI-8759371; Score: 0.35
DE  Interaction: P0C090; IntAct: EBI-8759987; Score: 0.35
DE  Interaction: O75164; IntAct: EBI-8793243; Score: 0.35
DE  Interaction: Q9UN81; IntAct: EBI-8874497; Score: 0.58
DE  Interaction: Q8TE30; IntAct: EBI-8875022; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-9393294; Score: 0.35
DE  Interaction: P67809; IntAct: EBI-9985228; Score: 0.35
DE  Interaction: Q16666; IntAct: EBI-9995438; Score: 0.35
DE  Interaction: O14862; IntAct: EBI-9995694; Score: 0.35
DE  Interaction: P41218; IntAct: EBI-9996028; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: P03211; IntAct: EBI-11722110; Score: 0.35
DE  Interaction: Q6VGS8; IntAct: EBI-11733617; Score: 0.35
DE  Interaction: Q9NZN8; IntAct: EBI-11026348; Score: 0.35
DE  Interaction: Q6ZQ29; IntAct: EBI-11075869; Score: 0.35
DE  Interaction: P70372; IntAct: EBI-11075952; Score: 0.35
DE  Interaction: P54368; IntAct: EBI-11123446; Score: 0.35
DE  Interaction: Q99523; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9Z172; IntAct: EBI-11157923; Score: 0.35
DE  Interaction: Q6SPF0; IntAct: EBI-11160311; Score: 0.35
DE  Interaction: P19712; IntAct: EBI-10901375; Score: 0.35
DE  Interaction: Q7Z7A1; IntAct: EBI-11371427; Score: 0.27
DE  Interaction: Q8N4C6; IntAct: EBI-11374469; Score: 0.27
DE  Interaction: Q96NL6; IntAct: EBI-11376636; Score: 0.27
DE  Interaction: O60308; IntAct: EBI-11380299; Score: 0.27
DE  Interaction: Q15468; IntAct: EBI-11383475; Score: 0.27
DE  Interaction: Q5SW79; IntAct: EBI-11385552; Score: 0.27
DE  Interaction: Q5TB80; IntAct: EBI-11385924; Score: 0.27
DE  Interaction: Q68CZ1; IntAct: EBI-11386978; Score: 0.27
DE  Interaction: Q96LK0; IntAct: EBI-11395817; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q13509; IntAct: EBI-11897134; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-11897791; Score: 0.35
DE  Interaction: P03466; IntAct: EBI-12577908; Score: 0.35
DE  Interaction: I6TAH8; IntAct: EBI-12580639; Score: 0.35
DE  Interaction: Q5EP28; IntAct: EBI-12582318; Score: 0.35
DE  Interaction: C5E522; IntAct: EBI-12583659; Score: 0.35
DE  Interaction: C5E524; IntAct: EBI-12584088; Score: 0.35
DE  Interaction: Q1K9H2; IntAct: EBI-12586510; Score: 0.35
DE  Interaction: P56945; IntAct: EBI-15099687; Score: 0.35
DE  Interaction: O95478; IntAct: EBI-21528968; Score: 0.35
DE  Interaction: Q9GZY0; IntAct: EBI-21528397; Score: 0.35
DE  Interaction: P16104; IntAct: EBI-21578956; Score: 0.35
DE  Interaction: P22492; IntAct: EBI-21580683; Score: 0.35
DE  Interaction: P47902; IntAct: EBI-21581572; Score: 0.35
DE  Interaction: P08621; IntAct: EBI-21606424; Score: 0.35
DE  Interaction: O60293; IntAct: EBI-21634559; Score: 0.35
DE  Interaction: P55075; IntAct: EBI-21635166; Score: 0.35
DE  Interaction: Q8IXZ2; IntAct: EBI-21635987; Score: 0.35
DE  Interaction: Q12905; IntAct: EBI-21665924; Score: 0.35
DE  Interaction: P10412; IntAct: EBI-21665473; Score: 0.35
DE  Interaction: Q12926; IntAct: EBI-21666158; Score: 0.35
DE  Interaction: Q96AK3; IntAct: EBI-21666867; Score: 0.35
DE  Interaction: Q9NQ55; IntAct: EBI-21667205; Score: 0.35
DE  Interaction: Q7Z2W4; IntAct: EBI-21679163; Score: 0.35
DE  Interaction: Q8WYQ5; IntAct: EBI-21679517; Score: 0.35
DE  Interaction: Q13595; IntAct: EBI-21690239; Score: 0.35
DE  Interaction: Q9NQX1; IntAct: EBI-21728580; Score: 0.35
DE  Interaction: Q96HE9; IntAct: EBI-21733724; Score: 0.35
DE  Interaction: B0UZZ8; IntAct: EBI-21740634; Score: 0.35
DE  Interaction: Q02539; IntAct: EBI-21742951; Score: 0.35
DE  Interaction: Q9BYG3; IntAct: EBI-21743958; Score: 0.35
DE  Interaction: Q9NZM5; IntAct: EBI-21744295; Score: 0.35
DE  Interaction: Q66K89; IntAct: EBI-21745571; Score: 0.35
DE  Interaction: P09651; IntAct: EBI-21752216; Score: 0.35
DE  Interaction: Q96SI9; IntAct: EBI-21752787; Score: 0.35
DE  Interaction: Q86VM9; IntAct: EBI-21769401; Score: 0.35
DE  Interaction: Q02878; IntAct: EBI-21778758; Score: 0.35
DE  Interaction: Q8TBF4; IntAct: EBI-21780331; Score: 0.35
DE  Interaction: Q9H9Y2; IntAct: EBI-21794281; Score: 0.35
DE  Interaction: Q9H609; IntAct: EBI-21821387; Score: 0.35
DE  Interaction: Q9Y316; IntAct: EBI-21887469; Score: 0.35
DE  Interaction: Q14493; IntAct: EBI-15555844; Score: 0.50
DE  Interaction: P61326; IntAct: EBI-15674190; Score: 0.35
DE  Interaction: P55265; IntAct: EBI-15694802; Score: 0.52
DE  Interaction: Q9BTM9; IntAct: EBI-15902685; Score: 0.35
DE  Interaction: P06730; IntAct: EBI-16057922; Score: 0.46
DE  Interaction: Q86U42; IntAct: EBI-16058014; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-16792282; Score: 0.42
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20799352; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9BZR8; IntAct: EBI-21258469; Score: 0.35
DE  Interaction: Q15646; IntAct: EBI-21262435; Score: 0.35
DE  Interaction: Q15139; IntAct: EBI-25395029; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-25490574; Score: 0.64
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-26396827; Score: 0.35
DE  Interaction: Q96LU5; IntAct: EBI-27050332; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: P05154; IntAct: EBI-27038496; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27111302; Score: 0.35
DE  Interaction: Q9HCE1; IntAct: EBI-27090881; Score: 0.35
DE  Interaction: K0BVN3; IntAct: EBI-27090881; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952324; Score: 0.27
DE  Interaction: Q8NCK7; IntAct: EBI-27105115; Score: 0.35
DE  Interaction: Q9BZB8; IntAct: EBI-29019560; Score: 0.42
DE  Interaction: O43474; IntAct: EBI-29020028; Score: 0.35
DE  Interaction: O60248; IntAct: EBI-29371942; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-29721059; Score: 0.27
GO  GO:0000785;
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0035145;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0044530;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003682;
GO  GO:0036121;
GO  GO:0004386;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0042162;
GO  GO:0008270;
GO  GO:0061158;
GO  GO:0044770;
GO  GO:0071347;
GO  GO:0071222;
GO  GO:0032508;
GO  GO:0006281;
GO  GO:0006260;
GO  GO:0071044;
GO  GO:0006406;
GO  GO:0000956;
GO  GO:0000294;
GO  GO:0000184;
GO  GO:0061014;
GO  GO:0032204;
GO  GO:0006449;
GO  GO:0032201;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTPPGGPGGPGGGGAGGPGGAGAGAAAGQLDAQVGP
SQ  EGILQNGAVDDSVAKTSQLLAELNFEEDEEDTYYTKDLPIHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHL
SQ  VRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLS
SQ  WLVKIPSEQEQLRARQITAQQINKLEELWKENPSATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKL
SQ  KESQTQDNITVRWDLGLNKKRIAYFTLPKTDSGNEDLVIIWLRDMRLMQGDEICLRYKGDLAPLWKGIGHVIKVPDNYGD
SQ  EIAIELRSSVGAPVEVTHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLP
SQ  DLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSR
SQ  EAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSADEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQ
SQ  FRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALS
SQ  AFPSNIFYEGSLQNGVTAADRVKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTKLLKAGAKPDQ
SQ  IGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYG
SQ  VIIVGNPKALSKQPLWNHLLNYYKEQKVLVEGPLNNLRESLMQFSKPRKLVNTINPGARFMTTAMYDAREAIIPGSVYDR
SQ  SSQGRPSSMYFQTHDQIGMISAGPSHVAAMNIPIPFNLVMPPMPPPGYFGQANGPAAGRGTPKGKTGRGGRQKNRFGLPG
SQ  PSQTNLPNSQASQDVASQPFSQGALTQGYISMSQPSQMSQPGLSQPELSQDSYLGDEFKSQIDVALSQDSTYQGERAYQH
SQ  GGVTGLSQY
//
ID  Q9EPU0;
PN  Regulator of nonsense transcripts 1;
GN  Upf1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:27149095}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q92900}. Nucleus {ECO:0000250|UniProtKB:Q92900}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27149095}. Note=Hyperphosphorylated form is targeted to the P-body, while unphosphorylated protein is distributed throughout the cytoplasm (By similarity). Localized in the chromatoid bodies of round spermatids (PubMed:27149095). {ECO:0000250|UniProtKB:Q92900, ECO:0000269|PubMed:27149095}.
DR  UNIPROT: Q9EPU0;
DR  UNIPROT: Q3UG00;
DR  UNIPROT: Q6GYP5;
DR  UNIPROT: Q6PHQ5;
DR  UNIPROT: Q8K0N4;
DR  UNIPROT: Q99PR4;
DR  Pfam: PF13086;
DR  Pfam: PF13087;
DR  Pfam: PF04851;
DR  Pfam: PF18141;
DR  Pfam: PF09416;
DR  PROSITE: PS51997;
DE  Function: RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs (By similarity). Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD (By similarity). Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (By similarity). In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD (By similarity). Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation and allowing the recycling of NMD factors (By similarity). UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways (By similarity). Plays a role in replication- dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2 (By similarity). For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed (By similarity). The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD (By similarity). Together with UPF2 and dependent on TDRD6, mediates the degradation of mRNA harboring long 3'UTR by inducing the NMD machinery (PubMed:27149095). Also capable of unwinding double-stranded DNA and translocating on single-stranded DNA (By similarity). {ECO:0000250|UniProtKB:Q92900, ECO:0000269|PubMed:27149095}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3TBT3; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6AXH7; IntAct: EBI-6876709; Score: 0.35
DE  Interaction: Q8CJG0; IntAct: EBI-9030750; Score: 0.35
DE  Interaction: A0A0F6AZL3; IntAct: EBI-13950507; Score: 0.35
DE  Interaction: Q7TMF2; IntAct: EBI-16026264; Score: 0.50
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: Q4U2R1; IntAct: EBI-16730475; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
DE  Interaction: Q9CQE6; IntAct: EBI-26472808; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26472902; Score: 0.35
DE  Interaction: O95793; IntAct: EBI-26900398; Score: 0.35
GO  GO:0000785;
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0035145;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0044530;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003682;
GO  GO:0036121;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0042162;
GO  GO:0008270;
GO  GO:0061158;
GO  GO:0044770;
GO  GO:0071347;
GO  GO:0071222;
GO  GO:0032508;
GO  GO:0006281;
GO  GO:0006260;
GO  GO:0071044;
GO  GO:0000956;
GO  GO:0000294;
GO  GO:0000184;
GO  GO:0061014;
GO  GO:0032204;
GO  GO:0006449;
GO  GO:0032201;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTPPGGPGGAGGPGGAGAGGAAGQLDAQVGPEGILQ
SQ  NGAVDDSVAKTSQLLAELNFEEDEEDTYYTKDLPVHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKC
SQ  KEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKI
SQ  PSEQEQLRARQITAQQINKLEELWKENPSATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQT
SQ  QDNITVRWDLGLNKKRIAFFTLPKTDSGNEDLVIIWLRDMRLMQGDEICLRYKGDLAPLWKGIGHVIKVPDNYGDEIAIE
SQ  LRSSVGAPVEVTHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVVIKCQLPKRFTAQGLPDLNHS
SQ  QVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDS
SQ  PVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSADEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSIL
SQ  IDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSN
SQ  IFYEGSLQNGVTAADRVKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTKLLKAGAKPDQIGIIT
SQ  PYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVG
SQ  NPKALSKQPLWNHLLSYYKEQKALVEGPLNNLRESLMQFSKPRKLVNTVNPGARFMTTAMYDAREAIIPGSVYDRSSQGR
SQ  PSNMYFQTHDQISMISAGPSHVAAMNIPIPFNLVMPPMPPPGYFGQANGPAAGRGTPKTKTGRGGRQKNRFGLPGPSQTT
SQ  LPNSQASQDVASQPFSQGALTQGYVSMSQPSQMSQPGLSQPELSQDSYLGDEFKSQIDVALSQDSTYQGERAYQHGGVTG
SQ  LSQY
//
ID  F4IUX6;
PN  Regulator of nonsense transcripts UPF2;
GN  UPF2;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus, nucleolus {ECO:0000269|PubMed:19602621}. Cytoplasm {ECO:0000269|PubMed:19602621}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: F4IUX6;
DR  UNIPROT: O80955;
DR  Pfam: PF02854;
DR  Pfam: PF04050;
DE  Function: Recruited by UPF3 associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3 stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA (By similarity). Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Required for plant development and adaptation to environmental stresses, including plant defense and response to wounding. {ECO:0000250, ECO:0000269|PubMed:22353561}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0035145;
GO  GO:0005730;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0003729;
GO  GO:0042742;
GO  GO:0009867;
GO  GO:0048571;
GO  GO:0000184;
GO  GO:0009611;
GO  GO:0009863;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDHPEDESHSEKQDDEEALARLEEIKKSIEAKLTLRQNNLNPERPDSAYLRTLDSSIKRNTAVIKKLKQINEEQREGLMD
SQ  DLRGVNLSKFVSEAVTAICEAKLKSSDIQAAVQICSLLHQRYKEFSASLTQGLLKVFFPGKSAEDLEADKNSKAMKKRST
SQ  LKLLLELYYVGVIEDSNIFINIIKDLTSVEQLKDRDTTQTNLTLLTSFARQGRIFLGLPISGQDEDFFKGLDVTADQKKS
SQ  FKKAFNTYYDALADLLQSEHKLLLQMEKENAKLVNAKGELSEDSASSYEKLRKSYDHLYRNISSLAEALDMQPPVMPEDG
SQ  TTRLTAGDEASPSGTVKDTSVPEPIWDDEDTKTFYECLPDLRAFVPAVLLGEAEPKSNEQSAKAKEKLSESSSEVVENQQ
SQ  TTEDTTEVSADSASMDDRSNAEQPKEKEEVEKEKAKDTKKEKGKEKDSEKKMEHEKEKGKSLDVANFERLLQRLPGCVSR
SQ  DLIDQLTVEYCYLNSKTNRKKLVKALFNVPRTSLELLAYYSRMVATLASCMKDIPSMLVQMLEDEFNSLVHKKDQMNIET
SQ  KIRNIRFIGELCKFKIVPAGLVFSCLKACLDEFTHHNIDVACNLLETCGRFLYRSPETTLRMTNMLDILMRLKNVKNLDP
SQ  RQSTLVENAYYLCKPPERSARISKVRPPLHQYVRKLLFSDLDKDSIANVLKQLRKLPWSECEQYILKCFMKVHKGKYGQI
SQ  HLIASLTSGLSRHHDEFVVAVVDEVLEEIRVGLELNEYGAQQKRLAHMRFLGELYNYEHVDSSVIFETLYLTLLYGHDTS
SQ  EQEVLDPPEDFFRVRMVIILLETCGHYFDRGSSKKRLDQFLIHFQRYILSKGHLPLDIEFDLQDLFANLRPNMTRYSTID
SQ  EVNAAILQLEEREHASSGDKVSIERHSDTKPSNKSSSDVISSNGKSTAKDIRENGEAHGEESDSDSGSGSVVRDGQNEEL
SQ  DDGNHERGSESGDGDDYDDGDGPGSDDDKFRVRQKVVTVDLEEQADFDQELKALLQESMEQRKLELRGRPALNMTIPMSV
SQ  FEGSGKDHHHFGRVVGENGEEVLDEENGEQREVQVKVLVKRGNKQQTRQMLIPSDCALVQSTKQKEAAELEEKQDIKRLV
SQ  LEYNERDEEEANGLGTQILNWTSGGSRGSTRTGEGSGKSGGSRHRFYYHQGGGGSYHARRK
//
ID  Q9HAU5;
PN  Regulator of nonsense transcripts 2;
GN  UPF2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11073994, ECO:0000269|PubMed:11113196, ECO:0000269|PubMed:11163187}. Cytoplasm {ECO:0000250|UniProtKB:A2AT37}.
DR  UNIPROT: Q9HAU5;
DR  UNIPROT: A6NLJ5;
DR  UNIPROT: D3DRS0;
DR  UNIPROT: Q14BM1;
DR  UNIPROT: Q5W0J4;
DR  UNIPROT: Q8N8U1;
DR  UNIPROT: Q9H1J2;
DR  UNIPROT: Q9NWL1;
DR  UNIPROT: Q9P2D9;
DR  UNIPROT: Q9Y4M9;
DR  PDB: 1UW4;
DR  PDB: 2WJV;
DR  PDB: 4CEK;
DR  PDB: 4CEM;
DR  Pfam: PF02854;
DR  Pfam: PF04050;
DR  OMIM: 605529;
DR  DisGeNET: 26019;
DE  Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA. {ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:18066079}.
DE  Reference Proteome: Yes;
DE  Interaction: O15234; IntAct: EBI-15855293; Score: 0.70
DE  Interaction: Q92900; IntAct: EBI-536644; Score: 0.95
DE  Interaction: Q9BZI7; IntAct: EBI-8638371; Score: 0.90
DE  Interaction: Q96B26; IntAct: EBI-374509; Score: 0.00
DE  Interaction: P26651; IntAct: EBI-374512; Score: 0.00
DE  Interaction: Q8IZD4; IntAct: EBI-374515; Score: 0.00
DE  Interaction: Q9Y3B2; IntAct: EBI-374518; Score: 0.00
DE  Interaction: P42285; IntAct: EBI-374521; Score: 0.00
DE  Interaction: Q9HAU5; IntAct: EBI-374524; Score: 0.00
DE  Interaction: Q9H0D6; IntAct: EBI-374530; Score: 0.00
DE  Interaction: Q8IU60; IntAct: EBI-374527; Score: 0.00
DE  Interaction: Q01780; IntAct: EBI-374533; Score: 0.00
DE  Interaction: Q9H9D4; IntAct: EBI-374536; Score: 0.00
DE  Interaction: O15116; IntAct: EBI-374539; Score: 0.00
DE  Interaction: P62841; IntAct: EBI-374175; Score: 0.00
DE  Interaction: P46777; IntAct: EBI-374178; Score: 0.00
DE  Interaction: Q99623; IntAct: EBI-374181; Score: 0.00
DE  Interaction: Q9GZQ8; IntAct: EBI-374184; Score: 0.00
DE  Interaction: P62851; IntAct: EBI-374187; Score: 0.00
DE  Interaction: Q9ULX3; IntAct: EBI-374190; Score: 0.00
DE  Interaction: Q04637; IntAct: EBI-464801; Score: 0.35
DE  Interaction: Q08491; IntAct: EBI-1015741; Score: 0.40
DE  Interaction: Q9UL03; IntAct: EBI-7390697; Score: 0.40
DE  Interaction: P55884; IntAct: EBI-7390800; Score: 0.40
DE  Interaction: Q96Q15; IntAct: EBI-7801538; Score: 0.80
DE  Interaction: Q9H3D4; IntAct: EBI-2564044; Score: 0.35
DE  Interaction: P0DPB3; IntAct: EBI-2685984; Score: 0.00
DE  Interaction: P10242; IntAct: EBI-2692642; Score: 0.00
DE  Interaction: P58526; IntAct: EBI-2856368; Score: 0.00
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q9H1J1; IntAct: EBI-3864585; Score: 0.77
DE  Interaction: Q15287; IntAct: EBI-3867801; Score: 0.53
DE  Interaction: Q8IYB3; IntAct: EBI-3867832; Score: 0.35
DE  Interaction: Q9Y5S9; IntAct: EBI-3870117; Score: 0.64
DE  Interaction: Q9H8T0; IntAct: EBI-5653160; Score: 0.00
DE  Interaction: O95758; IntAct: EBI-7850130; Score: 0.35
DE  Interaction: Q9UHX1; IntAct: EBI-10310020; Score: 0.56
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q9NS87; IntAct: EBI-11078400; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: O00233; IntAct: EBI-16630268; Score: 0.44
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27105115; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-30830161; Score: 0.44
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0005829;
GO  GO:0035145;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0060090;
GO  GO:0003723;
GO  GO:0042162;
GO  GO:0031100;
GO  GO:0001889;
GO  GO:0006406;
GO  GO:0000184;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPAERKKPASMEEKDSLPNNKEKDCSERRTVSSKERPKDDIKLTAKKEVSKAPEDKKKRLEDDKRKKEDKERKKKDEEKV
SQ  KAEEESKKKEEEEKKKHQEEERKKQEEQAKRQQEEEAAAQMKEKEESIQLHQEAWERHHLRKELRSKNQNAPDSRPEENF
SQ  FSRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKISDVNCAVHLCSLFHQRYADFAPSL
SQ  LQVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKNIINADRESHTHVSVVISFCRHCGDDIA
SQ  GLVPRKVKSAAEKFNLSFPPSEIISPEKQQPFQNLLKEYFTSLTKHLKRDHRELQNTERQNRRILHSKGELSEDRHKQYE
SQ  EFAMSYQKLLANSQSLADLLDENMPDLPQDKPTPEEHGPGIDIFTPGKPGEYDLEGGIWEDEDARNFYENLIDLKAFVPA
SQ  ILFKDNEKSCQNKESNKDDTKEAKESKENKEVSSPDDLELELENLEINDDTLELEGGDEAEDLTKKLLDEQEQEDEEAST
SQ  GSHLKLIVDAFLQQLPNCVNRDLIDKAAMDFCMNMNTKANRKKLVRALFIVPRQRLDLLPFYARLVATLHPCMSDVAEDL
SQ  CSMLRGDFRFHVRKKDQINIETKNKTVRFIGELTKFKMFTKNDTLHCLKMLLSDFSHHHIEMACTLLETCGRFLFRSPES
SQ  HLRTSVLLEQMMRKKQAMHLDARYVTMVENAYYYCNPPPAEKTVKKKRPPLQEYVRKLLYKDLSKVTTEKVLRQMRKLPW
SQ  QDQEVKDYVICCMINIWNVKYNSIHCVANLLAGLVLYQEDVGIHVVDGVLEDIRLGMEVNQPKFNQRRISSAKFLGELYN
SQ  YRMVESAVIFRTLYSFTSFGVNPDGSPSSLDPPEHLFRIRLVCTILDTCGQYFDRGSSKRKLDCFLVYFQRYVWWKKSLE
SQ  VWTKDHPFPIDIDYMISDTLELLRPKIKLCNSLEESIRQVQDLEREFLIKLGLVNDKDSKDSMTEGENLEEDEEEEEGGA
SQ  ETEEQSGNESEVNEPEEEEGSDNDDDEGEEEEEENTDYLTDSNKENETDEENTEVMIKGGGLKHVPCVEDEDFIQALDKM
SQ  MLENLQQRSGESVKVHQLDVAIPLHLKSQLRKGPPLGGGEGEAESADTMPFVMLTRKGNKQQFKILNVPMSSQLAANHWN
SQ  QQQAEQEERMRMKKLTLDINERQEQEDYQEMLQSLAQRPAPANTNRERRPRYQHPKGAPNADLIFKTGGRRR
//
ID  A2AT37;
PN  Regulator of nonsense transcripts 2;
GN  Upf2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HAU5}. Cytoplasm {ECO:0000269|PubMed:27149095}.
DR  UNIPROT: A2AT37;
DR  Pfam: PF02854;
DR  Pfam: PF04050;
DE  Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA. {ECO:0000250|UniProtKB:Q9HAU5}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3TBT3; IntAct: EBI-10729637; Score: 0.35
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0005829;
GO  GO:0035145;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0003723;
GO  GO:0042162;
GO  GO:0031100;
GO  GO:0001889;
GO  GO:0000184;
GO  GO:0006986;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPAERKKSASMEEKESLLNNKEKDCSERRPVSSKEKPRDDLKVTAKKEVSKVPEDKKKRLEEDKRKKEDKERKKKEEEKV
SQ  KAEEELKKKEEEEKKKQEEEERKKQEEQAKRQQEEAAAQLKEKEESLQLHQEAWERHQLRKELRSKNQNAPDNRPEENFF
SQ  SRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKLSDVNCAAHLCSLFHQRYSDFAPSLL
SQ  QVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKSIINADRESHTHVSVVISFCRHCGDDIAG
SQ  LVPRKVKSAAEKFNLSFPPSEIISPEKQQPFQNLLKEYFTSLTKHLKRDHRELQNTERQNRRILHSKGELSEDRHKQYEE
SQ  FAMSYQKLLANSQSLADLLDENMPDLPQDKPTPEEHGPGIDIFTPGKPGEYDLEGGIWEDEDARNFYENLIDLKAFVPAI
SQ  LFKDNEKSQNKDSNKDDSKEAKEPKDNKEASSPDDLELELENLEINDDTLELEGADEAEDLTKKLLDEQEQEDEEASTGS
SQ  HLKLIVDAFLQQLPNCVNRDLIDKAAMDFCMNMNTKANRKKLVRALFIVPRQRLDLLPFYARLVATLHPCMSDVAEDLCS
SQ  MLRGDFRFHVRKKDQINIETKNKTVRFIGELTKFKMFTKNDTLHCLKMLLSDFSHHHIEMACTLLETCGRFLFRSPESHL
SQ  RTSVLLEQMMRKKQAMHLDARYVTMVENAYYYCNPPPAEKTVRKKRPPLQEYVRKLLYKDLSKVTTEKVLRQMRKLPWQD
SQ  QEVKDYVICCMINIWNVKYNSIHCVANLLAGLVLYQEDVGIHVVDGVLEDIRLGMEVNQPKFNQRRISSAKFLGELYNYR
SQ  MVESAVIFRTLYSFTSFGVNPDGSPSSLDPPEHLFRIRLVCTILDTCGQYFDRGSSKRKLDCFLVYFQRYVWWKKSLEVW
SQ  TKDHPFPIDIDYMISDTLELLRPKIKLCNSLEESIRQVQDLEREFLIKLGLVNDKESKDSMTEGENLEEDEEEEEGGAET
SQ  EEQSGNESEVNEPEEEEGSEEEEEGEEEEEENTDYLTDSNKENETDEENAEVMIKGGGLKHVPCVEDEDFIQALDKMMLE
SQ  NLQQRSGESVKVHQLDVAIPLHLKSQLRKGPPLGGGEGETESADTMPFVMLTRKGNKQQFKILNVPMSSQLAANHWNQQQ
SQ  AEQEERMRMKKLTLDINERQEQEDYQEMLQSLAQRPAPANTNRERRPRYQHPKGAPNADLIFKTGGRRR
//
ID  O23523;
PN  RGG repeats nuclear RNA binding protein A;
GN  RGGA;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:25783413}. Nucleus {ECO:0000250|UniProtKB:Q9SQ56, ECO:0000255|PROSITE-ProRule:PRU00768}.
DR  UNIPROT: O23523;
DR  UNIPROT: A8MQG3;
DR  UNIPROT: A8MQJ5;
DR  Pfam: PF04774;
DR  Pfam: PF09598;
DE  Function: Binds RNA. Regulates responses to abscisic acid (ABA). Promotes stomata closure in drought conditions. Involved in resistance to salt and drought stresses via the accumulation of Pro. {ECO:0000269|PubMed:25783413}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0009738;
GO  GO:0071470;
GO  GO:0071472;
GO  GO:0009787;
GO  GO:0009737;
GO  GO:0006970;
GO  GO:0009651;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATLNPFDLLDDDAEDPSQLAVAIEKIDKSKKSGQVSSLPAKSAPKLPSKPLPPAQAVREARSDAPRGGGGRGGFNRGRG
SQ  GYNRDDGNNGYSGGYTKPSGEGDVSKSSYERRGGGGAPRGSFRGEGGGPGGGRRGGFSNEGGDGERPRRAFERRSGTGRG
SQ  SDFKRDGSGRGNWGTPGEEIAAETEAVAGVETEKDVGEKPAVDDVAADANKEDTVVEEKEPEDKEMTLDEYEKILEEKKK
SQ  ALQSLTTSERKVDTKVFESMQQLSNKKSNDEIFIKLGSDKDKRKDDKEEKAKKAVSINEFLKPAEGGNYYRGGRGGRGRG
SQ  GRGRGGVSSGESGGYRNEAAPAIGDAAQFPSLGGK
//
ID  Q9SQ56;
PN  RGG repeats nuclear RNA binding protein A;
GN  RggA;
OS  4097;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:11905967}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O23523}.
DR  UNIPROT: Q9SQ56;
DR  Pfam: PF04774;
DE  Function: Binds RNA. {ECO:0000269|PubMed:11905967}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0009416;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  RGGGRGGPRGGGRGRGPGRGRGFNQESADDENAFGSNNGFSGRYRVQEDGESGKLSERRGGYGGPRGGFHGGRRGGFNNG
SQ  DAAEGEGERPRRVFDRRSGTGRGNEYIKREGSGRGNWGTPADDIAQETEVPVNDGEKIVEAEKEAGQEEAEDTNKDSTAA
SQ  EPEEKEPEEKEMTLEEYEKLMEEKRKALLALKPEERKVNLDKELESMQLLSNKKNDDEIFIKLGSEKEKRKEAVEKARKT
SQ  QSINEFLKPAEGENYSRRGGRGRGPGRGRGGFGGGVGGNKSFSAPSIEDVGQFPSLVAK
//
ID  O23593;
PN  RGG repeats nuclear RNA binding protein B;
GN  RGGB;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9SQ56}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O23523}.
DR  UNIPROT: O23593;
DR  UNIPROT: Q8LB56;
DR  Pfam: PF04774;
DR  Pfam: PF09598;
DE  Function: Binds RNA. {ECO:0000250|UniProtKB:Q9SQ56}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0003729;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASVNPFDLLDDDAEDPSQIVASKPLKVVAPVQTAKSGKMPTKPPPPSQAVREARNAPGGGRGAGRGGSYGRGGRGGNNR
SQ  DSRNNDGPANENGYGGGYRRSEEGDGARRGGPVGGYRGDRRGSYSNGGDSGDSERPRKNYDRHSRTAYGNEDKRDGAGRA
SQ  NWGTTQDDITPVTEESTAVVDKNLTVEKQDGEGEATDAKNETPAEKAEEKPEDKEMTLEEYEKVLEEKKKALQATKVEER
SQ  KVDTKAFEAMQQLSSKKSNNDEVFIKLGTEKDKRITEREEKTRKSLSINEFLKPADGKSYYRPRGGYQGGREGRGPREGN
SQ  QRDGGRNLREGGRNQRDGGAAAQAPTPAIGDSAQFPTLGK
//
ID  Q9LVT8;
PN  RGG repeats nuclear RNA binding protein C;
GN  RGGC;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9SQ56}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O23523}.
DR  UNIPROT: Q9LVT8;
DR  UNIPROT: A8MQD7;
DR  UNIPROT: A8MRX4;
DR  UNIPROT: Q8LDQ7;
DR  Pfam: PF04774;
DR  Pfam: PF09598;
DE  Function: Binds RNA. {ECO:0000250|UniProtKB:Q9SQ56}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0009536;
GO  GO:0003729;
GO  GO:0003723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASLNPFDLLGDDAEDPSQLAVALSQKVEKAAAAVQPPKAAKFPTKPAPPSQAVRESRNAPQGGRGGTGGRGGFSRGRGN
SQ  GGYNRDNRNNDAPGNENGFSGGYRRPSEDADGASRGGSVGGYRVGGGREGPRRGGVANGESGDVERPPRNYDRHSRTGHG
SQ  TGMKRNGGGRGNWGTTEDDIPPTSEEPTTEVEKSPVAEKQGGEDETPEAKKELTAEEKAQKEAEEAEAREMTLEEYEKIL
SQ  EEKKKALQATKVEERKVDTKVFESMQQLSNKKNTDEEIFIKLGSDKEKRKDATEKAKKSLSINEFLKPADGKRYNGRGGG
SQ  SRGRGGRGGRGEGGNQRYAKEAAAPAIGDTAQFPSLG
//
ID  Q08DP6;
PN  Rho GTPase-activating protein 10;
GN  ARHGAP10;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Association to cell membrane is dependent on PH domain. {ECO:0000250}.
DR  UNIPROT: Q08DP6;
DR  Pfam: PF00169;
DR  Pfam: PF00620;
DR  Pfam: PF14604;
DR  PROSITE: PS50003;
DR  PROSITE: PS50238;
DR  PROSITE: PS50002;
DE  Function: GTPase activator for the small GTPases RhoA and Cdc42 by converting them to an inactive GDP-bound state. Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005096;
GO  GO:0007010;
GO  GO:0043066;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGLQPLEFSDCYLDSPWFRERIRAHEAELERTNKFIKELIKDGKNLIAATKTLSAAQRKFAHSLRDFKFEFIGDAETDDE
SQ  RCIDASLREFSNFLKNLEEQREIMALSVTETLIKPLEKFRKEQLGAVKEEKKKFDKETERNYSLIDKHLNLSAKKKDSHL
SQ  QEADIQVEQNRQHFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMFTFYHQGHELAKDFNHYKMELQINIQNTRNRFE
SQ  GTRSEVEELMNKIRQNPKDHKRASQFTAEGYLYVQEKRPPPFGSSWVKHYCMYRKAAKKFTMIPFEHRSGGKLGDGEVFF
SQ  LKECIRRHTDSIDRRFCFDVEAADRPGISLTMQAFSEEERKQWLEVLGGKEALFPSFNRAIIPRPEGSAQLDKMGFTILR
SQ  KCIRAVETRGINDQGLYRVVGVSSKVQRLLSMLMDVKTCNEVDLENSVDWEVKTITSALKQYLRSLPEPLMTYELHGDFI
SQ  VPAKSGSPESRVNAIHFLVHKLPEKNKEMLDILVKHLTNVSNHSKQNLMTVANLGVVFGPTLMRPQEETVAAIMDLKFQN
SQ  IVVEILIENHEKIFRTPPDATLPEPGPLSAPPNAPPRQSKRQGQRTKRPVAVYNLCLELEDGDRPSLPKEDTPPSSLDSL
SQ  SSPSPTTATALGHPGPDRNHLLTDGGSFGDWAPTAPSQARSSAVQWLNPQSPTTPSCSPAVTPPSPKLPPVPLSLPATVA
SQ  DKPPESIISRKARAVYPCEAEHSSELSFEIGAIFEDVQTSREPGWLEGTLNGKRGLIPQNYVKLL
//
ID  A1A4S6;
PN  Rho GTPase-activating protein 10;
GN  ARHGAP10;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Association to cell membrane is dependent on PH domain. {ECO:0000250}.
DR  UNIPROT: A1A4S6;
DR  UNIPROT: A1L0S5;
DR  UNIPROT: Q2VPC4;
DR  UNIPROT: Q2VPC5;
DR  UNIPROT: Q96EV3;
DR  UNIPROT: Q96S75;
DR  PDB: 2MIO;
DR  Pfam: PF00169;
DR  Pfam: PF00620;
DR  Pfam: PF14604;
DR  PROSITE: PS50003;
DR  PROSITE: PS50238;
DR  PROSITE: PS50002;
DR  OMIM: 609746;
DR  DisGeNET: 79658;
DE  Function: GTPase activator for the small GTPases RhoA and Cdc42 by converting them to an inactive GDP-bound state. Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death (By similarity). {ECO:0000250, ECO:0000269|PubMed:11432776}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6P5Z2; IntAct: EBI-1390955; Score: 0.68
DE  Interaction: P78314; IntAct: EBI-10692719; Score: 0.49
DE  Interaction: Q92625; IntAct: EBI-10697254; Score: 0.37
DE  Interaction: Q9C009; IntAct: EBI-11321694; Score: 0.35
DE  Interaction: Q9UNA1; IntAct: EBI-11898726; Score: 0.00
DE  Interaction: Q9ULB1; IntAct: EBI-11898717; Score: 0.00
DE  Interaction: Q9Y426; IntAct: EBI-21517999; Score: 0.35
DE  Interaction: C9J6V4; IntAct: EBI-21517948; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: Q02539; IntAct: EBI-20937220; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-21302175; Score: 0.35
DE  Interaction: Q14289; IntAct: EBI-28941112; Score: 0.35
DE  Interaction: Q05209; IntAct: EBI-27116319; Score: 0.27
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005096;
GO  GO:0007010;
GO  GO:0043066;
GO  GO:0051056;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGLQPLEFSDCYLDSPWFRERIRAHEAELERTNKFIKELIKDGKNLIAATKSLSVAQRKFAHSLRDFKFEFIGDAVTDDE
SQ  RCIDASLREFSNFLKNLEEQREIMALSVTETLIKPLEKFRKEQLGAVKEEKKKFDKETEKNYSLIDKHLNLSAKKKDSHL
SQ  QEADIQVEQNRQHFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMFTFYHQGHELAKDFNHYKMELQINIQNTRNRFE
SQ  GTRSEVEELMNKIRQNPKDHKRASQFTAEGYLYVQEKRPAPFGSSWVKHYCMYRKAAKKFNMIPFEHRSGGKLGDGEVFF
SQ  LKECTKRHTDSIDRRFCFDIEAADRPGVSLTMQAFSEEERKQWLEALGGKEALSHSFNTAIIPRPEGNAQLDKMGFTIIR
SQ  KCISAVETRGINDQGLYRVVGVSSKVQRLLSMLMDVKTCNEVDLENSADWEVKTITSALKQYLRSLPEPLMTYELHGDFI
SQ  VPAKSGSPESRVNAIHFLVHKLPEKNKEMLDILVKHLTNVSNHSKQNLMTVANLGVVFGPTLMRPQEETVAALMDLKFQN
SQ  IVVEILIENHEKIFRTPPDTTFPEPTCLSASPPNAPPRQSKRQGQRTKRPVAVYNLCLELEDGDNPYPSKEDTPTSSLDS
SQ  LSSPSPVTTAVPGPPGPDKNHLLADGGSFGDWASTIPGQTRSSMVQWLNPQSPTTTSSNSAVTPLSPGSSPFPFSPPATV
SQ  ADKPPESIRSRKARAVYPCEAEHSSELSFEIGAIFEDVQTSREPGWLEGTLNGKRGLIPQNYVKLL
//
ID  Q6Y5D8;
PN  Rho GTPase-activating protein 10;
GN  Arhgap10;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cell membrane. Note=Association to cell membrane is dependent on PH domain.
DR  UNIPROT: Q6Y5D8;
DR  UNIPROT: Q6Y5D6;
DR  UNIPROT: Q6Y5D7;
DR  UNIPROT: Q99MT3;
DR  UNIPROT: Q99MT4;
DR  Pfam: PF00169;
DR  Pfam: PF00620;
DR  Pfam: PF14604;
DR  PROSITE: PS50003;
DR  PROSITE: PS50238;
DR  PROSITE: PS50002;
DE  Function: GTPase activator for the small GTPases RhoA and Cdc42 by converting them to an inactive GDP-bound state. Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death. {ECO:0000269|PubMed:11238453, ECO:0000269|PubMed:15471851}.
DE  Reference Proteome: Yes;
DE  Interaction: Q29502; IntAct: EBI-4396533; Score: 0.53
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005096;
GO  GO:0007010;
GO  GO:0043066;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGLQPLEFSDCYLDSPWFRERIRAHEAELERTNKFIKELIKDGKNLISATKSLSAAQRKFAHSLRDFKFEFIGDAETDDE
SQ  RCIDASLREFSNFLKNLEEQREIMALSVTETLIKPLEKFRKEQLGAVKEEKKKFDKETEKNYSLIDKHLTLSARKKDSHL
SQ  QEADLQVEQNRQHFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMFTFYHQGHELSKDFNHYKMELQINIQNTRNRFE
SQ  GTRSEVEELMNKIRQNPKDQKRASQFTAEGYLYVQEKRPAPFGSSWVKHYCMYRKTAKKFNMIPFEHRSGGKLGDGEAFF
SQ  LKECTKRHMDSTDRRFCFDIEAADRPGVPLTVQAFSEEERKQWLEALGGKEALFHTFNRAIVPRPEGGAQLDKMGFTILR
SQ  KCISAVETRGINDQGLYRVVGVSSKVQRLLSMLMDVKMCNELDLENSADWEVKTVTSALKQYLRSLPEPLMTYELHRDFI
SQ  VPAKSGSPESRVNAIHFLVHKLPEKNKEMLDILVKHLTNVSSHSKQNLMTVANLGVVFGPTLMRPQEETVAAIMDLKFQN
SQ  IVVEILIENHEKIFRTSPDTTFAEPTCLSASPPNAPPRQSKRQGQRTKRPVAVYNLCLELEEGDSPSPLKEDPPSSSQDS
SQ  LSTPSPTTSAAHGPPGLDGNHLAADGGSCGDATATTPSQTRPSMVQWLNMQSPTTPSSNPAGTPPSPRMSPFPLSPAASI
SQ  VDKLPECVINRKARAVYPCEAEHSSELSFEIGAIFEDVQTSREPGWLEGTLNGKRGLIPQNYVKLL
//
ID  Q6DJJ6;
PN  Rhophilin-2-A;
GN  rhpn2;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q6DJJ6;
DR  Pfam: PF03097;
DR  Pfam: PF02185;
DR  Pfam: PF17820;
DR  PROSITE: PS51180;
DR  PROSITE: PS50106;
DR  PROSITE: PS51860;
DE  Function: Binds specifically to GTP-Rho. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTDALLPGSLNGKRLSEQNYFRKGKSIAQTGRSKLQNQRASLNQQILKAMRMRVGAENLLRATSNNKIREQVLLELSFVN
SQ  SNLQRLKEELERLNISVEVYQHTEQDSNIPLIPLGLKETKDVDFTTAFKDFISEHYSEDASEYENELADLMDLRQACRTP
SQ  SRDEAGVELLVSYFQQLGYLENRFFPPSRNLGILFTWYDSFTGVPVSQPNISLEKASILFNIAALYTQIGTRCNRQTKIG
SQ  LEEAVTAFQKATGVLNYLKETFTHTPSYDMSPAMLGVLIKMLLAEAHECYFEKMILSGIQNEFCTLLKAAQEAAKVGEVH
SQ  MQVYTLMNQAPIKENVPYSWSVMVQVKAEHYKALANYFVAIILIDYQLSLSDDEDKQEKAISQLYDSMPEGLTAQTILKD
SQ  QQQRTLLGKAHLSKAIRSHEEAIRFSTLCSTLRQIDVLQKILSAFHQRSQLKFSQHQKPDDFLDLLSAPDIVSKTEYQAK
SQ  TISPQLSKDKVTDIFQRLGPLSVFSVKQRWSAPRKICITKEDGDFGFVLRGDCPVQVISLDPLCPAATEGLKEGDYIVSV
SQ  AGKDCKWCSTSQVMDMLQATGKQSIEIQVISIQDQTYSMPTKSATYYAGMQKTYSLVCLTMDNVKHTKTQKATKKLSFLS
SQ  WGFRNRQKAASTLCLPSEVKGKPKTDNLFSFPDNSLCSESVLY
//
ID  Q63ZR5;
PN  Rhophilin-2-B;
GN  rhpn2;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q63ZR5;
DR  Pfam: PF03097;
DR  Pfam: PF02185;
DR  Pfam: PF17820;
DR  PROSITE: PS51180;
DR  PROSITE: PS50106;
DR  PROSITE: PS51860;
DE  Function: Binds specifically to GTP-Rho. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTDALLPANLNAKRLSEQNYFRKGKSIAQTGRSKLQNQRAILNQQILKAMRMRAGAENLLRATANNKIREQVLLELSFVN
SQ  SNLQRLKEELERLNISVEVYQHTEQASNIPLIPLGLKETKDVDFTTAFKDFILEHYSEDASEYENELADLMDLRQACRTP
SQ  SRDEAGVELLVSYFQQLGYLENRFFPPSRNIGILFTWYDSFTGVPVSQPNISLEKASILFNIAALYSQIGTRCNRQTKIG
SQ  LEEAVTTFQKAAGVLNYLKETFTHTPSYDMSPAMLGALIKMLLAEAHECYFEKMILSGIQNEFCTLLKAAQEAAKVSEVH
SQ  MQVYTLMNQAPIKENVPYSWSVMVQVKAEHYKALANYFVAITLIDYQLNLSDDEDKQEKAISQLYDSMPEGLTAQTILKD
SQ  QQQRTLLGKAHLSKAIRSHEEAIRFSTLCSTLRQIDVLQLILSAFHQRSLLKFSQHQKPDDFLDLLSAPDIVSKTEYQAE
SQ  TIPPQLSKDKVTDIFQRLGPLSIFSVKQRWSAPRKMCITKEDGDFGFVLKGDCPVQVISLDPLCPAATEGLKEGDYIVSV
SQ  AGKDCKWCSTSQVMDMLQETGQDSIEIQVISIQDQTNSLANKSATYYAGMQKTYSLVCLTMDNDKNTKTQKATKKLSFLS
SQ  WGFKNRQKAASTICLPSEVKGKPKTDMVFSFPDNSLSTESALY
//
ID  A4FUC9;
PN  Rhophilin-2;
GN  RHPN2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: A4FUC9;
DR  Pfam: PF03097;
DR  Pfam: PF02185;
DR  PROSITE: PS51180;
DR  PROSITE: PS50106;
DR  PROSITE: PS51860;
DE  Function: Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003094;
GO  GO:0051497;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTDTLLPAAPQPLEKEGNCYFRKGCNPLAQTGRSKLQNQRAALNQQILKAMRMRTGAENLLKAATNQKVREQVRLELSFL
SQ  NSDLQMLKEELEGLNISVGVYQNTEEAFTIPLIPLGLKETKDVDFSVALKDFILEHYSEDSYLYEDEIADLMDLRQACRT
SQ  PSRNEAGVELLMSYFMQLGFVESRFFPPTRQMGILFTWYDSLTGVPVSQQNLLLEKASILFNIGALYTQIGTRCNRQTEA
SQ  GLESTVDAFQRAAGVLNYLKETFTHTPSYDMSPAMLSVLVKMMLAQAQESTFEKVCLPGLQNEFFLLVKVAQEAAKVGEV
SQ  YRQLHTAMNQEPVKENIPYSWASLACVKAHHYEALAHYFTATLLIDHQLKPGEDEDHQEKCLSQLYSHMPEGLTPLATLK
SQ  NVHQRQLLGKSHLCQAVTHHEESMREASLCKKLRNIDVLQEVLSAAHDRSQLKYTQLREDDDLLNLTDAPDIVSKTEREV
SQ  EIIVPQFSKVTVTDFFQKLGPLSVFSANKRWTAPRSIHFTAEEGDLGFTLRGNSPVQVHFLDPYCSAAAAGTKEGDYIVS
SQ  IQDVDCKWLTLSEVMKMLKSFGQDDIEMKVVSLLDATSTMHSKCATYSVGMQKTYSMICLGIDVDDKTDKTKKVSKKLSF
SQ  LSWGTNKNRQKSASTLCLPSVGVTMPPVKKKLSSPFSLLNTDSSLY
//
ID  Q8HXG3;
PN  Rhophilin-2;
GN  RHPN2;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q8HXG3;
DR  Pfam: PF03097;
DR  Pfam: PF02185;
DR  PROSITE: PS51180;
DR  PROSITE: PS50106;
DR  PROSITE: PS51860;
DE  Function: Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0051497;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTDALLPAAPQPLEKESDGYFRKGCNPLAQTGRSKLQNQRAALNQQILKAVRMRTGAENLLKVATNHKVREQVRLELSFV
SQ  NSDLQMLKEELEGLNISVGVYQSTEEAFTVPLIPLGLKETKDIDFSVVLKDFILEHYSEDSYLYEDEIADLMDLRQACRT
SQ  PSRDEAGVELLMSYFIQLGFVESRFFPPTRQMGILFTWYDSLTGVPVSQQNLLLEKASILFNIGALYTQIGTRCNRRTQA
SQ  GLDGAVDAFQRAAGVLHHLKETFTHTPSYDMSPAMLSVLVKMMLAQAQENVFEKICLPGIRNEFFVLVKVAQEAAKVGEV
SQ  YRQLHTAMSQAPVKENIPYSWASLVCVKAHHYAALAHYFAATLLIDHQLKPGADEDHQEKCLSQLYDHMPEGLTPLATLK
SQ  SGHQRRQLGKSHLRRAVAHHEESVREASLCKKLRNIEVLQDVLSVAHERSRLKYAQHQDDDDLLNLIDAPDIISKTEQEV
SQ  EIILPQFSKVTATDFFQKLGPLSVFSANKRWTPPRSIHFTAEEGDLGFTLRGNSPVQVHFLDPHCSAALAGAKEGDYIVS
SQ  IQDVDCKWLTVSEVMKLLKACGRDGVEMKVVSLLDFTSSMHNKCATYSVGMQKTYSMICLAIDDDDKTDKTKKISKKLSF
SQ  LSWGTDKNRVKSASTLCLPSVGVARPQVKKKLPSPFSLLNSDSSLY
//
ID  Q8IUC4;
PN  Rhophilin-2;
GN  RHPN2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12473120}.
DR  UNIPROT: Q8IUC4;
DR  UNIPROT: B2RCG8;
DR  UNIPROT: B3KUY8;
DR  UNIPROT: B4DUS7;
DR  UNIPROT: Q8N3T7;
DR  UNIPROT: Q8N9D6;
DR  UNIPROT: Q8NE33;
DR  UNIPROT: Q96RU1;
DR  PDB: 2VSV;
DR  Pfam: PF03097;
DR  Pfam: PF02185;
DR  PROSITE: PS51180;
DR  PROSITE: PS51860;
DR  OMIM: 617932;
DR  DisGeNET: 85415;
DE  Function: Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity. {ECO:0000269|PubMed:12221077}.
DE  Reference Proteome: Yes;
DE  Interaction: P40337; IntAct: EBI-1059874; Score: 0.00
DE  Interaction: Q9UBN6; IntAct: EBI-1062633; Score: 0.00
DE  Interaction: P10321; IntAct: EBI-1064255; Score: 0.00
DE  Interaction: P20823; IntAct: EBI-1073373; Score: 0.00
DE  Interaction: Q9UET6; IntAct: EBI-1074557; Score: 0.00
DE  Interaction: Q9H1Y0; IntAct: EBI-1074608; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-1081405; Score: 0.00
DE  Interaction: P31947; IntAct: EBI-7543847; Score: 0.40
DE  Interaction: P13631; IntAct: EBI-3921027; Score: 0.37
DE  Interaction: O43521; IntAct: EBI-21803818; Score: 0.35
DE  Interaction: Q9BU70; IntAct: EBI-21872745; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21907689; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25773054; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-26974147; Score: 0.40
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003094;
GO  GO:0051497;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTDALLPAAPQPLEKENDGYFRKGCNPLAQTGRSKLQNQRAALNQQILKAVRMRTGAENLLKVATNSKVREQVRLELSFV
SQ  NSDLQMLKEELEGLNISVGVYQNTEEAFTIPLIPLGLKETKDVDFAVVLKDFILEHYSEDGYLYEDEIADLMDLRQACRT
SQ  PSRDEAGVELLMTYFIQLGFVESRFFPPTRQMGLLFTWYDSLTGVPVSQQNLLLEKASVLFNTGALYTQIGTRCDRQTQA
SQ  GLESAIDAFQRAAGVLNYLKDTFTHTPSYDMSPAMLSVLVKMMLAQAQESVFEKISLPGIRNEFFMLVKVAQEAAKVGEV
SQ  YQQLHAAMSQAPVKENIPYSWASLACVKAHHYAALAHYFTAILLIDHQVKPGTDLDHQEKCLSQLYDHMPEGLTPLATLK
SQ  NDQQRRQLGKSHLRRAMAHHEESVREASLCKKLRSIEVLQKVLCAAQERSRLTYAQHQEEDDLLNLIDAPSVVAKTEQEV
SQ  DIILPQFSKLTVTDFFQKLGPLSVFSANKRWTPPRSIRFTAEEGDLGFTLRGNAPVQVHFLDPYCSASVAGAREGDYIVS
SQ  IQLVDCKWLTLSEVMKLLKSFGEDEIEMKVVSLLDSTSSMHNKSATYSVGMQKTYSMICLAIDDDDKTDKTKKISKKLSF
SQ  LSWGTNKNRQKSASTLCLPSVGAARPQVKKKLPSPFSLLNSDSSWY
//
ID  Q8BWR8;
PN  Rhophilin-2;
GN  Rhpn2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q8BWR8;
DR  UNIPROT: Q9DBN2;
DR  PDB: 1VAE;
DR  Pfam: PF03097;
DR  Pfam: PF02185;
DR  PROSITE: PS51180;
DR  PROSITE: PS50106;
DR  PROSITE: PS51860;
DE  Function: Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003094;
GO  GO:0051497;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTDTLLPAAPQPLEKEGDDYFRKGCNPLAQTGRSKLQNQRAALNQQILKAVRMRTGAENLLKVATNQKVREQVRLELSFV
SQ  NSDLQMLKEELEGLNISVGVYQGTEEAFTIPLIPLGLKETKEVDFSIVFKDFILEHYSEDSYLYEDDIADLMDLRQACRT
SQ  PSRDEAGVELLMSYFIQLGFVESRFFPPTRHMGLLFTWYDSFTGVPVSQQTLLLEKASVLFNIGALYTQIGTRCNRQTQA
SQ  GLESAVDAFQRAAGVLNYLKETFTHTPSYDMSPAMLSVLVKMMLAQAQESVFEKVCLPGIQNEFFVLVKVAQEAAKVAEA
SQ  YRQLHAAMSQEPVKENIPYSWASVAYVKAYHYGALAHYFAATLLIDHQLKPGADEDHQEKCLSQLYDRMPEGMTPLATLK
SQ  NAGQRVLLGKGHLHRAIGFHEESLREANLCKKLRDIQVLRDVLSAAHQRTQLKHTQHREDDDLLNLIDAPDVLPKTEREV
SQ  KITFPDFSKVTVTDFFQKLGPLSVFSASKRWSPPRGIHFTVEEGDLGFTLRGNTPVQVHFLDPHCSASLAGAKEGDYIVS
SQ  IQGVDCKWLTVSEVMKLLKSFGGEEVEMKVVSLLDSTSSMHNKCATYSVGMQKTYSMICLSMDDDDKADKTKKISKKLSF
SQ  LSWGTSKNRQKSASTLCLPEVGLARSQNKKKLPTPFSLLNSDSSLY
//
ID  Q9LVD0;
PN  18S rRNA (guanine-N(7))-methyltransferase RID2;
GN  RID2;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:21401745}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O43709}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43709}. Cytoplasm {ECO:0000250|UniProtKB:P25627}. Nucleus, nucleolus {ECO:0000269|PubMed:21401745}.
DR  UNIPROT: Q9LVD0;
DR  Pfam: PF08241;
DR  Pfam: PF12589;
DE  Function: Essential protein (PubMed:21401745). S-adenosyl-L-methionine- dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity (By similarity). Involved in the pre-rRNA processing steps in the nucleolus leading to small- subunit rRNA production independently of its RNA-modifying catalytic activity. Supports cell proliferation (PubMed:21401745). Required for the initiation of lateral root primordia formation and for the root apical meristem (RAM) organization as well as for leaves development (PubMed:14522871). During callus formation from hypocotyl and root explants, required for the initial stage of reactivation of cell proliferation in the hypocotyl stele (PubMed:21401745). Involved in leaf polarity establishment by functioning cooperatively with AS2 to repress abaxial genes ARF3, ARF4, KAN1, KAN2, YAB1 and YAB5, and the knox homeobox genes KNAT1, KNAT2, KNAT6, and STM to promote adaxial development in leaf primordia at shoot apical meristems at high temperatures (PubMed:27334696). {ECO:0000250|UniProtKB:P25627, ECO:0000269|PubMed:14522871, ECO:0000269|PubMed:21401745, ECO:0000269|PubMed:27334696}.
DE  Reference Proteome: Yes;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016435;
GO  GO:1990110;
GO  GO:0048527;
GO  GO:0010078;
GO  GO:0048364;
GO  GO:0070476;
GO  GO:0006364;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNRPELLAPPEIFYDDTEARKYTSSSRIVEIQAKLSERALELLALPEDGVPRFLLDIGCGSGLSGETLSEDGHHWIGLD
SQ  ISASMLHVAVEREVEGDLLLGDMGQGLGLRSGVIDGAISISAVQWLCNADKSSHEPRLRLKAFFGSLYRCLSRGARAVFQ
SQ  VYPENIAQRELILRQALQAGFGGGLVVDYPHSTKKRKEFLVLTCGTVQTSIQTSKNEYDESCSEDDNSDDEESEEVGVSD
SQ  RNRPRKRQRTNTKVKGREWVLRKKEQSRRKGKNVPADSKFTSRKRRTRF
//
ID  Q29RU0;
PN  E3 ubiquitin-protein ligase RNF128;
GN  RNF128;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partially colocalized with the endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and with the late endosomal GTPase RAB7A. {ECO:0000250}.
DR  UNIPROT: Q29RU0;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down- regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals. {ECO:0000250|UniProtKB:Q8TEB7}.
DE  Reference Proteome: Yes;
GO  GO:0005856;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0016740;
GO  GO:0016567;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGQLPGAGVFCRGGCGFSRLLAWCFLLVLSPQTPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPV
SQ  AGVLVPPDGPGALNACNPHTNFTVPTVPGDWGSSVQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIP
SQ  MSHPGAGDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNA
SQ  RAQSRKQRQLKADAKKAIGRLQLRTQKQGDKEIGPDGDSCAVCIELYKPNDLVRILTCNHVFHKTCVDPWLLEHRTCPMC
SQ  KCDILKALGIEVDVEDGSVSLQVPVSNETSSNASPHEEDNRSETASSGYASVQGADEPPLEEHAHSANENLQLVNHEANS
SQ  MAVDVVPHVDNPTFEEDESPDQETTVREIKS
//
ID  Q8TEB7;
PN  E3 ubiquitin-protein ligase RNF128;
GN  RNF128;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12705856, ECO:0000269|PubMed:22016387}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partially colocalized with the endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and with the late endosomal GTPase RAB7A (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8TEB7;
DR  UNIPROT: A0PJI4;
DR  UNIPROT: Q6PH80;
DR  UNIPROT: Q6ZTJ8;
DR  UNIPROT: Q96RF3;
DR  UNIPROT: Q9H5E4;
DR  PDB: 3ICU;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DR  OMIM: 300439;
DR  DisGeNET: 79589;
DE  Function: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down- regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals. {ECO:0000269|PubMed:12705856, ECO:0000269|PubMed:22016387}.
DE  Reference Proteome: Yes;
DE  Interaction: P0C6X7; IntAct: EBI-25488783; Score: 0.37
DE  Interaction: P63279; IntAct: EBI-2341627; Score: 0.37
DE  Interaction: Q9NPD8; IntAct: EBI-2341840; Score: 0.37
DE  Interaction: Q92624; IntAct: EBI-10275130; Score: 0.56
DE  Interaction: Q8TAP6; IntAct: EBI-10275120; Score: 0.72
DE  Interaction: Q9UHD9; IntAct: EBI-24442817; Score: 0.56
DE  Interaction: Q15036; IntAct: EBI-24588332; Score: 0.56
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005770;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0001818;
GO  GO:1904352;
GO  GO:0061462;
GO  GO:0031647;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGPPPGAGVSCRGGCGFSRLLAWCFLLALSPQAPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPV
SQ  AGVLVPPDGPGALNACNPHTNFTVPTVWGSTVQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIPMSH
SQ  PGAVDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNARAQ
SQ  SRKQRQLKADAKKAIGRLQLRTLKQGDKEIGPDGDSCAVCIELYKPNDLVRILTCNHIFHKTCVDPWLLEHRTCPMCKCD
SQ  ILKALGIEVDVEDGSVSLQVPVSNEISNSASSHEEDNRSETASSGYASVQGTDEPPLEEHVQSTNESLQLVNHEANSVAV
SQ  DVIPHVDNPTFEEDETPNQETAVREIKS
//
ID  Q9D304;
PN  E3 ubiquitin-protein ligase RNF128;
GN  Rnf128;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partially colocalized with the endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and with the late endosomal GTPase RAB7A. {ECO:0000250}.
DR  UNIPROT: Q9D304;
DR  UNIPROT: Q3UJY0;
DR  UNIPROT: Q9CVG1;
DR  UNIPROT: Q9DBN3;
DR  UNIPROT: Q9JJF8;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down- regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals (By similarity). {ECO:0000250, ECO:0000269|PubMed:12435366, ECO:0000269|PubMed:12705856}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005770;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0001818;
GO  GO:0031647;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGPPPGIGVYCRGGCGAARLLAWCFLLALSPHAPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPV
SQ  SGVLVPPDGPGALNACNPHTNFTVPTVWGSTVQVSWLALIQRGGGCTFADKIHLASERGASGAVIFNFPGTRNEVIPMSH
SQ  PGAGDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNARAQ
SQ  SRKQRQLKADAKKAIGKLQLRTLKQGDKEIGPDGDSCAVCIELYKPNDLVRILTCNHIFHKTCVDPWLLEHRTCPMCKCD
SQ  ILKALGIEVDVEDGSVSLQVPVSNEASNTASPHEEDSRSETASSGYASVQGADEPPLEEHAQSANENLQLVNHEANSVAV
SQ  DVVPHVDNPTFEEDETPDQEAAVREIKS
//
ID  Q5RF74;
PN  E3 ubiquitin-protein ligase RNF128;
GN  RNF128;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partially colocalized with the endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and with the late endosomal GTPase RAB7A. {ECO:0000250}.
DR  UNIPROT: Q5RF74;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down- regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals. {ECO:0000250|UniProtKB:Q8TEB7}.
DE  Reference Proteome: Yes;
GO  GO:0005856;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0005770;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0001818;
GO  GO:0031647;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGPPLGAGVSCRGGCGSSRLLAWCFLLALSPQAPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPV
SQ  AGVLVPPDGPGALNACNPHTNFTVPTVWGSTVQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIPMSH
SQ  PGAGDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNARAQ
SQ  SRKQRQLKADAKKAIGRLQLRTLKQGDREIGPDGDSCAVCIELYKPNDLVRILTCNHIFHKTCVDPWLLEHRTCPMCKCD
SQ  ILKALGIEVDVEDGSVSLQVPVSNEISNSASSHEEDNRSETASSGYASVQGADEPPLEEHVQSTNENLQLVNHEANSVAV
SQ  DVIPHVDNPTFEEDETPHQETAVREIKS
//
ID  Q8AWW4;
PN  E3 ubiquitin-protein ligase RNF128;
GN  rnf128;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q8AWW4;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that catalyzes polyubiquitin chains (By similarity). Converts epidermis into cement gland and neural tissue in whole embryos. {ECO:0000250, ECO:0000269|PubMed:12435366}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0016740;
GO  GO:0016567;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGALKMRCQCFPLPYLSLLALLLLNLSLTRAETLWTANVNYSYVYDNKTYGEEGEIGVFGQDSPIERAAGLVVLPKSEKL
SQ  YTACKDNVNFSVPSGWTGPWIALIQRGGGCTFTEKINRAAERGARAVVVYNNGIDNEVFEMSHPGTKDTVAIMIGNLKGN
SQ  EIVDLIKGGMQVTMVIEVGRKHGSWINHYSIFFVSVSFFIVTAATVGYFIFYSARRWRLTRAQNKKQKRLKAEAKKAIGK
SQ  LQLRTIKQGDKVLGPDGDSCAVCIEPYKPSDVVRILTCNHFFHKNCIDPWLLEHRTCPMCKCDILKSLGIAEDEEEGTSV
SQ  AIPSVSSELQRSTVQITEEENHSETASSGYASVRGGDEQVDEGQHIYENTELVHEASATSIEVLPHMDNPGFESEDVHVH
SQ  EMKS
//
ID  Q86T96;
PN  E3 ubiquitin-protein ligase RNF180;
GN  RNF180;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus envelope {ECO:0000250|UniProtKB:Q3U827}.
DR  UNIPROT: Q86T96;
DR  UNIPROT: Q0JSU3;
DR  UNIPROT: Q495A8;
DR  UNIPROT: Q8NBD1;
DR  Pfam: PF19332;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DR  OMIM: 616015;
DR  DisGeNET: 285671;
DE  Function: E3 ubiquitin-protein ligase which promotes polyubiquitination and degradation by the proteasome pathway of ZIC2. {ECO:0000250|UniProtKB:Q3U827}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031227;
GO  GO:0005635;
GO  GO:0046872;
GO  GO:0031624;
GO  GO:0061630;
GO  GO:0030534;
GO  GO:0042415;
GO  GO:0032436;
GO  GO:0031398;
GO  GO:0000209;
GO  GO:0050790;
GO  GO:0042428;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRSKELITKNHSQEETSILRCWKCRKCIASSGCFMEYLENQVIKDKDDSVDAQNICHVWHMNVEALPEWISCLIQKAQW
SQ  TVGKLNCPFCGARLGGFNFVSTPKCSCGQLAAVHLSKSRTDYQPTQAGRLMRPSVKYLSHPRVQSGCDKEALLTGGGSEN
SQ  RNHRLLNMARNNNDPGRLTEALCLEVRPTYFEMKNEKLLSKASEPKYQLFVPQLVTGRCATRAFHRKSHSLDLNISEKLT
SQ  LLPTLYEIHSKTTAYSRLNETQPIDLSGLPLQSSKNSYSFQNPSSFDPSMLLQRFSVAPHETQTQRGGEFQCGLEAASVY
SQ  SDHTNTNNLTFLMDLPSAGRSMPEASDQEEHLSPLDFLHSANFSLGSINQRLNKRERSKLKNLRRKQRRRERWLQKQGKY
SQ  SGVGLLDHMTLNNEMSTDEDNEYAEEKDSYICAVCLDVYFNPYMCYPCHHIFCEPCLRTLAKDNPSSTPCPLCRTIISRV
SQ  FFQTELNNATKTFFTKEYLKIKQSFQKSNSAKWPLPSCRKAFHLFGGFRRHAAPVTRRQFPHGAHRMDYLHFEDDSRGWW
SQ  FDMDMVIIYIYSVNWVIGFIVFCFLCYFFFPF
//
ID  Q3U827;
PN  E3 ubiquitin-protein ligase RNF180;
GN  Rnf180;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18363970}; Single-pass membrane protein {ECO:0000269|PubMed:18363970}. Nucleus envelope {ECO:0000269|PubMed:18363970}.
DR  UNIPROT: Q3U827;
DR  UNIPROT: Q3UW39;
DR  UNIPROT: Q80ZX1;
DR  UNIPROT: Q8CCR1;
DR  UNIPROT: Q9CXV6;
DR  Pfam: PF19332;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase which promotes polyubiquitination and degradation by the proteasome pathway of ZIC2. {ECO:0000269|PubMed:18363970}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031227;
GO  GO:0005635;
GO  GO:0046872;
GO  GO:0031624;
GO  GO:0061630;
GO  GO:0030534;
GO  GO:0042415;
GO  GO:1901360;
GO  GO:0032436;
GO  GO:0031398;
GO  GO:0000209;
GO  GO:0050790;
GO  GO:0042428;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRSEESTSTQSPEEQTGTLHCWRCRKCIASSGCFMTPLETQVVEQDRHESVDAQNTCHLWHMNVDALPEWISCLLQKAQ
SQ  WTVGKLNCPFCGARLGGFNFVSTPKCSCGQLAAVHLCKSRTDHQAAQGGRLMRPALKHLPHPGVPSGCDKETLLTGGGSK
SQ  TRNHWLLSMARNSNGLGRLTEALCLEVRATYFEMKNEKLLFKASDPKCQPFVPQPDTGRCPSRASHRKSHSLDLNISEKL
SQ  ILLPTLYEIHRKPTAYPRLNETGPIDLSGLALPCSNSSCSFQSPPSFDPNMLLHRLSVAPHETQAQRGRECQCGLEASSV
SQ  YSDHANANSLPFLMDLPSAGRSVLEASDQEEHLSQLDFLRSASFPLGTINHRLNNRERSKLRTLRRQQRRERWLQKQGKY
SQ  SGVGLLDHMTVSNEMSTDEETEFPEEKDSYMCAVCLDVYFNPYMCYPCHHIFCEPCLRTLAKDNPASTPCPLCRTIISRV
SQ  FLQTELNNATKTFFTKEYLKIKQSFQKSSSAKWPLPSCRKGFHLFGGFHRRAAPVTRRQFPHGAHRMDYLHFEDDSRGWW
SQ  FDMDMVIIYIYSVNWVIGFVVFCFLCYFFFPF
//
ID  Q5RAK3;
PN  E3 ubiquitin-protein ligase RNF180;
GN  RNF180;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus envelope {ECO:0000250|UniProtKB:Q3U827}.
DR  UNIPROT: Q5RAK3;
DR  Pfam: PF19332;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase which promotes polyubiquitination and degradation by the proteasome pathway of ZIC2. {ECO:0000250|UniProtKB:Q3U827}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031227;
GO  GO:0005635;
GO  GO:0046872;
GO  GO:0031624;
GO  GO:0061630;
GO  GO:0030534;
GO  GO:0042415;
GO  GO:0032436;
GO  GO:0031398;
GO  GO:0000209;
GO  GO:0050790;
GO  GO:0042428;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRSKELITKNHSQEETSILRCWKCRKCIASSGCFMEYFENQVIKDKDDSVDAQNICHVWHMNIESLPEWISCLIQKAQW
SQ  TVGKLNCPFCGARLGGFNFVSTPKCSCGQLAAVHLSKSRTDYQPTQAGRLMRPSVKYLSHPRVQSGCDKEVLLTGGGSKN
SQ  RNHRLLNMARNNNDPGRLTEALCLEVRPTYFEMKNEKLLSKASEPKYQLFVPQLVTGRCTTRAFHRKSHSLDLNISEKLT
SQ  LLPTLYEIRGKTTAYSRLNETQPIDLSGLPLQSSKNSCSFQNPSSFDPGMLLQRFSVAPHETQTQRGGEFQCGLEAASVY
SQ  SDHTNTNNLTFLMDLPSAGRSMPEASDQEEHLSPLDFLHSANFSLGSINQRLNKRERSKLKNLRRKQRRRERWLQKQGKY
SQ  SGVGFLDHMTLNNEMSTDEDNEYAEEKDSYICAVCLDVYFNPYMCYPCRHIFCEPCLRTLAKDNPSSTPCPLCRTIISRV
SQ  FFQTELNNATKTFFTKEYLKIKQSFQKSNSAKWPLPSCRKAFHLFGGFHRHAAPVTRRQFPHGAHRMDYLHFEDDSRGWW
SQ  FDMDMVIIYIYSVNWVIGFIVFCFLCYFFFPF
//
ID  P41391;
PN  Ran GTPase-activating protein 1;
GN  rna1;
OS  284812;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region {ECO:0000305}. Note=Possibly enriched in the nuclear periphery.
DR  UNIPROT: P41391;
DR  PDB: 1K5D;
DR  PDB: 1K5G;
DR  PDB: 1YRG;
DR  PDB: 2CA6;
DE  Function: GTPase activator for the nuclear Ras-related regulatory protein spi1 (Ran), converting it to the putatively inactive GDP-bound state.
DE  Reference Proteome: Yes;
DE  Interaction: P62826; IntAct: EBI-1032926; Score: 0.40
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005096;
GO  GO:0031267;
GO  GO:0090630;
GO  GO:0006913;
GO  GO:0046827;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRFSIEGKSLKLDAITTEDEKSVFAVLLEDDSVKEIVLSGNTIGTEAARWLSENIASKKDLEIAEFSDIFTGRVKDEIP
SQ  EALRLLLQALLKCPKLHTVRLSDNAFGPTAQEPLIDFLSKHTPLEHLYLHNNGLGPQAGAKIARALQELAVNKKAKNAPP
SQ  LRSIICGRNRLENGSMKEWAKTFQSHRLLHTVKMVQNGIRPEGIEHLLLEGLAYCQELKVLDLQDNTFTHLGSSALAIAL
SQ  KSWPNLRELGLNDCLLSARGAAAVVDAFSKLENIGLQTLRLQYNEIELDAVRTLKTVIDEKMPDLLFLELNGNRFSEEDD
SQ  VVDEIREVFSTRGRGELDELDDMEELTDEEEEDEEEEAESQSPEPETSEEEKEDKELADELSKAHI
//
ID  Q0VD51;
PN  E3 ubiquitin-protein ligase RNF13;
GN  RNF13;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:O54965}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:O54965}; Single-pass type I membrane protein {ECO:0000255}. Note=Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane. {ECO:0000250|UniProtKB:O54965}.
DR  UNIPROT: Q0VD51;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that regulates cell proliferation. Involved in apoptosis regulation. Mediates ER stress- induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA. Also involved in protein trafficking and localization. {ECO:0000250|UniProtKB:O43567}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0008432;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0051640;
GO  GO:0070304;
GO  GO:0051865;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPI
SQ  VPPPVRDNSSGTFIVLIRRLDCNFDEKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKD
SQ  EFTYEKGGHIILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVC
SQ  AICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVSEHTPLLRPLASAST
SQ  QSFGALSESRSHQNMTESSDYEEDDNDTDSSDAENEINEHSVVVQLQPNGERDYNIANTV
//
ID  Q90972;
PN  E3 ubiquitin-protein ligase RNF13;
GN  RNF13;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:O54965}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000305|PubMed:8610176}; Single-pass type I membrane protein {ECO:0000255}. Note=Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane. {ECO:0000250|UniProtKB:O54965}.
DR  UNIPROT: Q90972;
DR  UNIPROT: Q533M4;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that regulates cell proliferation (PubMed:20015074). Involved in apoptosis regulation. Mediates ER stress-induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA (By similarity). {ECO:0000250|UniProtKB:O43567, ECO:0000269|PubMed:20015074}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0005654;
GO  GO:0008432;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0051640;
GO  GO:0070304;
GO  GO:0051865;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLSIGMLMLSATQIYTIVTVQLFAFLNLLPVEADILAYNFENGTQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPI
SQ  APPPLRDNSSTAFIVLIRRLECNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEILKKIDIPSVFIGEASANSLKE
SQ  EFTYEKGGHVVLIPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVC
SQ  AICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSETDSSQEENEVSENTPLLRPLASVST
SQ  QSFGALSESHSHQNMTESSEYEEDDNDNIDSSDAESGVNEESVVVQLQPNDERDYRVTNTV
//
ID  O43567;
PN  E3 ubiquitin-protein ligase RNF13;
GN  RNF13;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18794910, ECO:0000269|PubMed:23378536, ECO:0000269|PubMed:24387786}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000305|PubMed:24387786}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:O54965}; Single-pass type I membrane protein {ECO:0000255}. Note=Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane. {ECO:0000250|UniProtKB:O54965}.
DR  UNIPROT: O43567;
DR  UNIPROT: A6NC87;
DR  UNIPROT: B3KR12;
DR  UNIPROT: Q05D66;
DR  UNIPROT: Q6IBJ9;
DR  PDB: 5ZBU;
DR  PDB: 5ZC4;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DR  OMIM: 609247;
DR  OMIM: 618379;
DR  DisGeNET: 11342;
DE  Function: E3 ubiquitin-protein ligase that regulates cell proliferation (PubMed:18794910, PubMed:23378536, PubMed:30595371). Involved in apoptosis regulation (PubMed:23378536, PubMed:30595371). Mediates ER stress-induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA (PubMed:23378536, PubMed:30595371). Also involved in protein trafficking and localization (PubMed:24387786). {ECO:0000269|PubMed:18794910, ECO:0000269|PubMed:23378536, ECO:0000269|PubMed:24387786, ECO:0000269|PubMed:30595371}.
DE  Disease: Developmental and epileptic encephalopathy 73 (DEE73) [MIM:618379]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE73 is an autosomal dominant form with onset at birth. {ECO:0000269|PubMed:30595371}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P51668; IntAct: EBI-2129187; Score: 0.37
DE  Interaction: P62837; IntAct: EBI-2129341; Score: 0.37
DE  Interaction: P61077; IntAct: EBI-2129485; Score: 0.37
DE  Interaction: Q9Y2X8; IntAct: EBI-2129621; Score: 0.37
DE  Interaction: P51965; IntAct: EBI-2129713; Score: 0.37
DE  Interaction: Q969T4; IntAct: EBI-2129801; Score: 0.37
DE  Interaction: P61088; IntAct: EBI-2130077; Score: 0.59
DE  Interaction: Q13404; IntAct: EBI-9970220; Score: 0.00
DE  Interaction: P22314; IntAct: EBI-9970220; Score: 0.00
DE  Interaction: P42229; IntAct: EBI-11034384; Score: 0.35
DE  Interaction: P48681; IntAct: EBI-11119785; Score: 0.35
DE  Interaction: O00214; IntAct: EBI-21518344; Score: 0.35
DE  Interaction: Q86Y82; IntAct: EBI-21524609; Score: 0.35
DE  Interaction: Q9UEU0; IntAct: EBI-21525256; Score: 0.35
DE  Interaction: Q9Y240; IntAct: EBI-21531678; Score: 0.35
DE  Interaction: Q9H8J5; IntAct: EBI-21537025; Score: 0.35
DE  Interaction: O43291; IntAct: EBI-21587968; Score: 0.35
DE  Interaction: O00182; IntAct: EBI-21597945; Score: 0.35
DE  Interaction: P32241; IntAct: EBI-21613594; Score: 0.35
DE  Interaction: Q9Y3E1; IntAct: EBI-21693236; Score: 0.35
DE  Interaction: Q9H6Y7; IntAct: EBI-21693236; Score: 0.35
DE  Interaction: Q92572; IntAct: EBI-21693236; Score: 0.35
DE  Interaction: P59780; IntAct: EBI-21693236; Score: 0.35
DE  Interaction: P56377; IntAct: EBI-21693236; Score: 0.35
DE  Interaction: P51798; IntAct: EBI-21693236; Score: 0.35
DE  Interaction: P29597; IntAct: EBI-21693236; Score: 0.35
DE  Interaction: P24468; IntAct: EBI-21693236; Score: 0.35
DE  Interaction: O60637; IntAct: EBI-21693236; Score: 0.35
DE  Interaction: O43602; IntAct: EBI-21693236; Score: 0.35
DE  Interaction: O14617; IntAct: EBI-21693236; Score: 0.35
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0008432;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0051640;
GO  GO:0070304;
GO  GO:0051865;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPI
SQ  VPPPVKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKD
SQ  EFTYEKGGHLILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVC
SQ  AICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVTEHTPLLRPLASVSA
SQ  QSFGALSESRSHQNMTESSDYEEDDNEDTDSSDAENEINEHDVVVQLQPNGERDYNIANTV
//
ID  O54965;
PN  E3 ubiquitin-protein ligase RNF13;
GN  Rnf13;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:19292867}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19292867}; Single-pass type I membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:20230530}; Single-pass type I membrane protein {ECO:0000255}. Note=The mature protein is subjected to extensive proteolysis that leads to the shedding of the ectodomain into the lumen of vesicles and the release of the C-terminal fragment into the cytosol (PubMed:20230530). Not detected in early endosomes (PubMed:20230530). Treatment of the cells with either PMA or ionomycin stabilizes the full-length protein which relocalizes to recycling endosomes and to the inner nuclear membrane (PubMed:20230530). {ECO:0000269|PubMed:20230530}.
DR  UNIPROT: O54965;
DR  UNIPROT: O54966;
DR  UNIPROT: Q6PEA8;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that regulates cell proliferation (PubMed:19292867). Involved in apoptosis regulation (By similarity). Mediates ER stress-induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA (By similarity). Also involved in protein trafficking and localization (By similarity). {ECO:0000250|UniProtKB:O43567, ECO:0000269|PubMed:19292867}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0008432;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0051640;
GO  GO:0070304;
GO  GO:0051865;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFEDLPARFGYRLPAEGLKGFLINSKPENACEPI
SQ  VPPPLKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIDTLKKIDIPSVFIGESSANSLKD
SQ  EFTYEKGGHIILVPELSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRNRRNRLRKDQLKKLPVHKFKKGDEYDVC
SQ  AICLEEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENQVSEHTPLLPPSASART
SQ  QSFGSLSESHSHHNMTESSDYEDDDNEETDSSDADNEITDHSVVVQLQPNGEQDYNIANTV
//
ID  Q5RCV8;
PN  E3 ubiquitin-protein ligase RNF13;
GN  RNF13;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:O54965}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:O54965}; Single-pass type I membrane protein {ECO:0000255}. Note=Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane. {ECO:0000250|UniProtKB:O54965}.
DR  UNIPROT: Q5RCV8;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that regulates cell proliferation. Involved in apoptosis regulation. Mediates ER stress- induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA. Also involved in protein trafficking and localization. {ECO:0000250|UniProtKB:O43567}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0008432;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0051640;
GO  GO:0070304;
GO  GO:0051865;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPI
SQ  VPPPVKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKD
SQ  EFTYEKGGHLILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVC
SQ  AICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVTEHTPLLRPLASVSA
SQ  QSFGALSESRSHQNMTESSDYEEDDNEDTDSSDAENEINEHDVVVQLQPNGERDYNIANTV
//
ID  Q66HG0;
PN  E3 ubiquitin-protein ligase RNF13;
GN  Rnf13;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:O54965}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:O54965}; Single-pass type I membrane protein {ECO:0000255}. Note=Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane. {ECO:0000250|UniProtKB:O54965}.
DR  UNIPROT: Q66HG0;
DR  Pfam: PF02225;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that regulates cell proliferation. Involved in apoptosis regulation. Mediates ER stress- induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA. Also involved in protein trafficking and localization. {ECO:0000250|UniProtKB:O43567}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0031902;
GO  GO:0005765;
GO  GO:0005637;
GO  GO:0005654;
GO  GO:0008432;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0051640;
GO  GO:0070304;
GO  GO:0051865;
GO  GO:0016567;
GO  GO:0006511;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFEDLPARFGYRLPAEGLKGFLINSKPENACEPI
SQ  VPPPLKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIDILKKIDIPSVFIGESSANSLKD
SQ  EFTYEKGGHVILVPELSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRNRRNRLRKDQLKKLPVHKFKKGDEYDVC
SQ  AICLEEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENQVSEHTPLLPPSASART
SQ  QSFGSLSESHSHHMTESSDYEDDDNEETDSSDADNEITDHSVVVQLQPNGEPDYNIANTV
//
ID  Q68DV7;
PN  E3 ubiquitin-protein ligase RNF43;
GN  RNF43;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Nucleus envelope. Note=According to a report, may be secreted. {ECO:0000269|PubMed:15492824}.
DR  UNIPROT: Q68DV7;
DR  UNIPROT: A8K4R2;
DR  UNIPROT: B7Z443;
DR  UNIPROT: B7Z5D5;
DR  UNIPROT: B7Z5J5;
DR  UNIPROT: Q65ZA4;
DR  UNIPROT: Q6AI04;
DR  UNIPROT: Q9NXD0;
DR  PDB: 4KNG;
DR  Pfam: PF13639;
DR  Pfam: PF18212;
DR  PROSITE: PS50089;
DR  OMIM: 612482;
DR  OMIM: 617108;
DR  DisGeNET: 54894;
DE  Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway (PubMed:18313049, PubMed:22575959, PubMed:22895187). Along with RSPO2 and ZNRF3, constitutes a master switch that governs limb specification (By similarity). {ECO:0000250|UniProtKB:P0DPR2, ECO:0000269|PubMed:18313049, ECO:0000269|PubMed:22575959, ECO:0000269|PubMed:22895187}.
DE  Disease: Sessile serrated polyposis cancer syndrome (SSPCS) [MIM:617108]: A rare disease characterized by multiple and/or large serrated polyps developing in the colon, and an increased personal and familial risk of colorectal cancer. A patient is diagnosed with SSPCS if at least one of the following criteria is met: the presence of at least five sessile serrated polyps proximal to the sigmoid colon, two of which are greater than 10 mm in diameter; the presence of any number of serrated polyps occurring proximal to the sigmoid colon in an individual who has a first-degree relative with serrated polyposis; the presence of more than 20 serrated polyps of any size distributed throughout the colon. Sessile serrated polyps are also known as sessile serrated adenomas (SSA) and are estimated to be responsible for 20 to 35% of all colon cancers. Individuals with SSPCS may have a strong personal or family history of extracolonic cancers. {ECO:0000269|PubMed:24512911, ECO:0000269|PubMed:27081527}. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9ULX6; IntAct: EBI-1647059; Score: 0.51
DE  Interaction: P0CG47; IntAct: EBI-1647301; Score: 0.40
DE  Interaction: Q68DV7; IntAct: EBI-1647320; Score: 0.44
DE  Interaction: P62837; IntAct: EBI-1647320; Score: 0.59
DE  Interaction: Q29504; IntAct: EBI-1647320; Score: 0.44
DE  Interaction: P61077; IntAct: EBI-1647344; Score: 0.59
DE  Interaction: P51668; IntAct: EBI-2129226; Score: 0.37
DE  Interaction: Q9Y2X8; IntAct: EBI-2129645; Score: 0.37
DE  Interaction: P51965; IntAct: EBI-2129745; Score: 0.37
DE  Interaction: Q969T4; IntAct: EBI-2129825; Score: 0.37
DE  Interaction: P61088; IntAct: EBI-2130105; Score: 0.37
DE  Interaction: Q15233; IntAct: EBI-2296169; Score: 0.56
DE  Interaction: P23246; IntAct: EBI-2296169; Score: 0.56
DE  Interaction: Q96S97; IntAct: EBI-21871496; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-21871496; Score: 0.35
DE  Interaction: P49674; IntAct: EBI-21871496; Score: 0.35
GO  GO:0005789;
GO  GO:0005887;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0005109;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0030178;
GO  GO:0016567;
GO  GO:0072089;
GO  GO:0006511;
GO  GO:0038018;
GO  GO:0016055;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGGHQLQLAALWPWLLMATLQAGFGRTGLVLAAAVESERSAEQKAIIRVIPLKMDPTGKLNLTLEGVFAGVAEITPAEG
SQ  KLMQSHPLYLCNASDDDNLEPGFISIVKLESPRRAPRPCLSLASKARMAGERGASAVLFDITEDRAAAEQLQQPLGLTWP
SQ  VVLIWGNDAEKLMEFVYKNQKAHVRIELKEPPAWPDYDVWILMTVVGTIFVIILASVLRIRCRPRHSRPDPLQQRTAWAI
SQ  SQLATRRYQASCRQARGEWPDSGSSCSSAPVCAICLEEFSEGQELRVISCLHEFHRNCVDPWLHQHRTCPLCMFNITEGD
SQ  SFSQSLGPSRSYQEPGRRLHLIRQHPGHAHYHLPAAYLLGPSRSAVARPPRPGPFLPSQEPGMGPRHHRFPRAAHPRAPG
SQ  EQQRLAGAQHPYAQGWGLSHLQSTSQHPAACPVPLRRARPPDSSGSGESYCTERSGYLADGPASDSSSGPCHGSSSDSVV
SQ  NCTDISLQGVHGSSSTFCSSLSSDFDPLVYCSPKGDPQRVDMQPSVTSRPRSLDSVVPTGETQVSSHVHYHRHRHHHYKK
SQ  RFQWHGRKPGPETGVPQSRPPIPRTQPQPEPPSPDQQVTRSNSAAPSGRLSNPQCPRALPEPAPGPVDASSICPSTSSLF
SQ  NLQKSSLSARHPQRKRRGGPSEPTPGSRPQDATVHPACQIFPHYTPSVAYPWSPEAHPLICGPPGLDKRLLPETPGPCYS
SQ  NSQPVWLCLTPRQPLEPHPPGEGPSEWSSDTAEGRPCPYPHCQVLSAQPGSEEELEELCEQAV
//
ID  Q5NCP0;
PN  E3 ubiquitin-protein ligase RNF43;
GN  Rnf43;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}. Note=May be secreted. {ECO:0000250}.
DR  UNIPROT: Q5NCP0;
DR  UNIPROT: B2KGH3;
DR  UNIPROT: Q6DI76;
DR  UNIPROT: Q8BME0;
DR  UNIPROT: Q8C191;
DR  UNIPROT: Q8K0X4;
DR  Pfam: PF13639;
DR  Pfam: PF18212;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway (PubMed:22895187). Along with RSPO2 and ZNRF3, constitutes a master switch that governs limb specification (By similarity). {ECO:0000250|UniProtKB:P0DPR2, ECO:0000269|PubMed:22895187}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9EQD0; IntAct: EBI-16007021; Score: 0.40
GO  GO:0005789;
GO  GO:0005887;
GO  GO:0005635;
GO  GO:0005109;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0030178;
GO  GO:0016567;
GO  GO:0072089;
GO  GO:0006511;
GO  GO:0038018;
GO  GO:0016055;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGGHQLQLAVLWPWLLMATLHAGFGHTGRVLAAAVESERSAEQKAVIRVIPLKMDPTGKLNLTLEGVFAGVAEVTPAEG
SQ  KLMQSHPLYLCNASDDDNLEPGFISIVKLESPRRAPRPCLSLASKARMAGERGANAVLFDITEDRSAAEQLQQPLGLTKP
SQ  VVLIWGSDAAKLMEFVYKNRKAYVWIELKEPPAGANYDVWILLTVVGTVFVIILASVLRIRCRPHHSRPDPLQQRTARAI
SQ  SQLATRRYQAGCRRARAEWPDSGSSCSSTPVCAICLEEFSEGQELRVISCLHEFHRTCVDPWLYQHRTCPLCMFNIVEGD
SQ  SFSQAPAASPSYQEPGRRLHLIRQHPGHAHYHLPSAYLLGPSRTSVARTPRPRPFLPSQEPSMGSRHQRLPRTSHLRAPE
SQ  EQQHLAVSPHPYAQGWGLNRLRCTSQHPAACPVALRRARPHESSGSGESYCTERSGYLADGPASDSSSGPCHGSSSDSVV
SQ  NCTDVSLQGIHGSSSTFRSSLSSDFDPLVYCSPEGDLQGKGIQPSVTSRPRSLDSVVPRGETQVSSHIHYHRHRHHHYKR
SQ  QFQWHGRKPGPETGIPQSMPAASHTQLEPSLPDQQLITPNPTASSMLPNPQRPRALTEPAPGLAEASSPSPSPKPNPSGL
SQ  LNLQKSSLTVRHPHRKRRGGPSEPLPTSLPPDLTVHTACPVFPHYSPRLAYPWPPEVHPLMFRPPGPDRRLLHEVPGPCY
SQ  SSSQPVWLYLNPCQPLGPCLPGEGHSKWTFDSPEGRRCPYSHCQVLPAQPGSEEELEELCEQAV
//
ID  P0DPR2;
PN  E3 ubiquitin-protein ligase RNF43;
GN  rnf43;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q68DV7}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q68DV7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q68DV7}; Single- pass type I membrane protein {ECO:0000250|UniProtKB:Q68DV7}. Nucleus envelope {ECO:0000250|UniProtKB:Q68DV7}.
DR  UNIPROT: P0DPR2;
DR  Pfam: PF13639;
DR  Pfam: PF18212;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway (By similarity). Along with RSPO2 and ZNRF3, constitutes a master switch that governs limb specification (PubMed:29769720). {ECO:0000250|UniProtKB:Q68DV7, ECO:0000269|PubMed:29769720}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0005887;
GO  GO:0005635;
GO  GO:0005109;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0006511;
GO  GO:0038018;
GO  GO:0016055;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNRARLQLASLWLLLTVTLQAVASAMGTTEREMDVKALIRVTPLQAEESGGVGQGNLTLEGLFARVAEISPAEGRLLQFH
SQ  PLSLCNTSEDDQTKPGFISIVKLETPDRDTQPCLSLANKARLAGERGAHAVLFDITNDRGALQQLQQPAGINQPVVLIWG
SQ  PDAEKLMDVVNKNKEALVKIEVQEQPKWLHHDIWILLTVAGTVMFFVLYAVARLLCRQPPPQDSIQQQTLLAISRLGTRR
SQ  YQQRMLKDQRASGGWVETASTSSSVPVCAICLEEFTDGQELRILPCCHEYHLGCVDPWLRQNHTCPLCMYDILDSGTPPR
SQ  PLAHRAPSQTQLWGRYPGSARLMSHLPPHGTPMVFPTPNNSLFLPRAPYYLDHTHHWQMPEQMAMQMRTHRRGAEGTREL
SQ  GISPGCQDSSGYLPDDPGSDSSSGPCHGSSSENCTDISLHCLHGTSSSSVHSSQSNQEDSSPPALASYLLPQGELPALNP
SQ  LLSTQASYASHVHFHQHRHHHYRRNQPSMSHSHPHRSKRRTKVSRADPSYYREHRHTTGANGELRSLMVRREPRPSCSRT
SQ  CFDPRTNREHPRHQQSMPQAASVVQGSSEPDVATSLRGSRTDPPSRTYRKKKSSAPSHLPLLYSPRHCHPANSVQMSESS
SQ  HPRWAEEVRLLHSRVNSHRENTAMMHLYHPPHHNQGATEEIEAVCEHAV
//
ID  O14188;
PN  Ras GTPase-activating-like protein rng2;
GN  rng2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm, cytoskeleton. Nucleus envelope. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localized to the F-actin ring and spindle pole body during interphase and mitosis. Also found in septum.
DR  UNIPROT: O14188;
DR  UNIPROT: Q9USG0;
DR  PDB: 1P2X;
DR  PDB: 1P5S;
DR  Pfam: PF00307;
DR  Pfam: PF00612;
DR  Pfam: PF00616;
DR  Pfam: PF03836;
DR  PROSITE: PS50021;
DR  PROSITE: PS50096;
DR  PROSITE: PS50018;
DE  Function: Required for cytokinesis. Component of the contractile F- actin ring; required for its construction following assembly of F-actin at the division site. {ECO:0000269|PubMed:9635188}.
DE  Reference Proteome: Yes;
DE  Interaction: P05933; IntAct: EBI-1152509; Score: 0.52
DE  Interaction: P10989; IntAct: EBI-7190604; Score: 0.49
GO  GO:0005737;
GO  GO:0071341;
GO  GO:0110085;
GO  GO:0120104;
GO  GO:0044732;
GO  GO:0005635;
GO  GO:0005816;
GO  GO:0051015;
GO  GO:0005516;
GO  GO:0008093;
GO  GO:0005096;
GO  GO:1903478;
GO  GO:0000917;
GO  GO:1903486;
GO  GO:1903475;
GO  GO:1903479;
GO  GO:1902404;
GO  GO:1902406;
GO  GO:0032956;
GO  GO:0043087;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDVNVGLSRLQSQAGAPVGTKGSNTRLAAKQRETLQAYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQ
SQ  KFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPPLIKSD
SQ  ENLSFTDEDVSIIVRRLRQSNVILPNFKALSADFMLRASPVSSRTPSPTRFPKHARFQTLNSSDSASIYSSPYTSPTLEF
SQ  SKKDASARSDILKMHRRTKSATPSLEQFNEPYKQTLPSHSIEFEDSFFQPPSQKGHMQRSFLTTFSAPTRRREALFSTTS
SQ  GLSQRSPVDEKIVNAIQACGRGVLVRLRLVDMLQSLVEQSSSVVLLQAVIRGYISRNTYRIRKKAYDELVNWVTSIQSIS
SQ  RAYLIRAQYRKVVLQEEATKSIQTLQSIIRGGFYRRKYHSLIERLDLFTPSFVLIQSSALGFLTRHAIVNMLDNLYNYIP
SQ  LFNRMQSILRANMFRNEWSNFLDSVQSFPVSFHSICKGRLIRDSINRLNGSLLGELDNFIKLQNLSRGFMIRRAFKEKLE
SQ  KLKASTSSFIALQAIVRAFLLRKNLESIYDSFQKSHLSVIKAQSLYRGFITRTKIDYCNDYLLKRLPDIVFMQSAVRAIL
SQ  LRDDVNYTEVQLDSFIPEIVLLQSLIRGYLSRNKFSRKLQNFHKNMENPIVAKSIFRGRQEGLAYRELATAKNPPVMTVK
SQ  NFVHLLDDTNFDFEEEVLLEKMRKEIVQQVRDNEEIEVHINELDVKIALLVKNKISLDDVLKHHNKYKFGKQSTEYLKIN
SQ  TLSMKSLNNSSRKFLELYQCFFYVLQTNEMYLANYFQALKTEGTSSVKIRHAVYLVLQIFGHGSNRREEVLLLRFISQVI
SQ  KLEAALVNSSQDLLSDDCVWKLLFTGYRGDVREVKLWKTILGRIHKVLVADNHLDFEINPLTLFKSFNPEVASQTDSPKL
SQ  TLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYV
SQ  APVLVSPDNFKLVDGSITALQRKNLYTLSSILSEIFSIESCDSKQLGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYF
SQ  EFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPPDVNDPLRAVVNSLGPVSEQDNDFVQDETDVKLELNPKFCT
SQ  IENPVAQERTLIVQTKRYILFIIRIQNGLNLLEILVKPVTDSDEAAWQNLLAEESEKNARNYDLFDDSIFSMSFAELKYT
SQ  ALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYIEQAMETL
SQ  QSKKGKKKLIPFSKQYFHMRDLRKSGRVPRFGSFKYPALKLYDRGVLVSISHMPQKEKLYITISADEVGKFILEATSPTV
SQ  KVSSPRCELHLDDLLSAQYNKVLTLDVLDGRLKLNTNMFLHLIFSKFYS
//
ID  Q148F6;
PN  Protein rogdi homolog;
GN  ROGDI;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Presynapse {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, axon {ECO:0000250|UniProtKB:Q4V7D2}. Perikaryon {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q4V7D2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4V7D2}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000250|UniProtKB:Q4V7D2}.
DR  UNIPROT: Q148F6;
DR  Pfam: PF10259;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0043204;
GO  GO:0043291;
GO  GO:0008021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATVMAATAAERAVLEEEFRWLLHDEVHAVLRQLQDILKEASLRFTLPGSGTEGPTKQENFILGSCGTDQVKGVLTLQGD
SQ  ALSQADVNLKMPRNNQLLHFAFREDKQWKLQQIQDARNHVSQAIYLLANRDESYQFRTGAEVLKLMDAVMLQLTRARNRL
SQ  TTPATLTLPEIAASGLTRMFAPTLPSDLLVNVYINLNKLCLTVYQLHTLQPNSTKNFRPAGGAVLHSPGAMFEWGTQRLE
SQ  VSHVHKVESVIPWLNDALVFFTVSLQLCQQLKDKISVFSSYWSCRPF
//
ID  O17213;
PN  Protein rogdi homolog;
GN  H14A12;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}.
DR  UNIPROT: O17213;
DR  Pfam: PF10259;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0043291;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEVQSLTITTNYPPKPASPNPQDIRDTIRSNKTNENLWIQRKDVDTTLRSALEHLKACCIVLNLSAKCDERLNVAVSHGT
SQ  TEKYQLMSRTGSSDNLKAAVTLLDDNVIQAEVTVKYPKAGGGYYRAVAQPDVQWKLQQLQDLGNHISRVTITLCDLQHEV
SQ  NLLKGDGERDAFTLATGARILEELKLTMNEISLARNSIMLPRKRSLLELCYFPPTRKFVPPLPQDQLISFYISCCRLVCA
SQ  SYQMVPKTVHPQGLSVFMAESQLPHLDDVIKHLNTVMAILQKLINYLSATMS
//
ID  Q7ZVT5;
PN  Protein rogdi homolog;
GN  rogdi;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Presynapse {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, axon {ECO:0000250|UniProtKB:Q4V7D2}. Perikaryon {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q4V7D2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4V7D2}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000250|UniProtKB:Q4V7D2}.
DR  UNIPROT: Q7ZVT5;
DR  Pfam: PF10259;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0043204;
GO  GO:0043291;
GO  GO:0008021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTAASQAERTVLEEEFNWLLKEEVHAVLKQLQDILKEASRRLSMPSPGLEGQLKQENFILGSSTMDQVKGVLTLQGEALT
SQ  QADINIKVAKSSQVMHFAFRDDKQWKLQQIQDARNHVNQALQLLSSRDDSYHFKTGAEVNKLMDAIMLQLTRARNRLTTP
SQ  ASMTLPELAASGLMKMFTPPMPGDVMVNFYINLSKLCLTVYQLHVLQPNTTKNFKPAGSSVLHNPGAMFEHNNTKFEVSH
SQ  VHKVECVVPWLNDTLVFFTISLQLCQQLKDKISVFSSFWNYRPF
//
ID  Q9VVE2;
PN  Protein rogdi;
GN  rogdi;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Presynapse {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, axon {ECO:0000250|UniProtKB:Q4V7D2}. Perikaryon {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q4V7D2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4V7D2}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000250|UniProtKB:Q4V7D2}.
DR  UNIPROT: Q9VVE2;
DR  UNIPROT: Q32KF2;
DR  UNIPROT: Q8IQP4;
DR  UNIPROT: Q95T16;
DR  Pfam: PF10259;
DE  Function: Plays a role in promoting sleep by enhancing metabotropic transmission of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) in GABAergic neurons upstream of a wake-inducing dopaminergic pathway. {ECO:0000269|PubMed:28900300}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VCH1; IntAct: EBI-199512; Score: 0.00
DE  Interaction: Q9VY61; IntAct: EBI-216289; Score: 0.00
DE  Interaction: Q0E8K5; IntAct: EBI-220799; Score: 0.00
DE  Interaction: Q9VVC2; IntAct: EBI-226383; Score: 0.00
DE  Interaction: P11929; IntAct: EBI-234009; Score: 0.00
DE  Interaction: Q9VU23; IntAct: EBI-234639; Score: 0.00
DE  Interaction: Q9VYV9; IntAct: EBI-258534; Score: 0.00
DE  Interaction: P10734; IntAct: EBI-274719; Score: 0.00
DE  Interaction: Q7K4Z4; IntAct: EBI-278444; Score: 0.00
DE  Interaction: P62152; IntAct: EBI-283358; Score: 0.00
DE  Interaction: P42287; IntAct: EBI-509567; Score: 0.37
DE  Interaction: P18431; IntAct: EBI-9925534; Score: 0.60
DE  Interaction: Q9VJQ6; IntAct: EBI-26734859; Score: 0.49
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0043204;
GO  GO:0043291;
GO  GO:0008021;
GO  GO:0048149;
GO  GO:0061534;
GO  GO:0030431;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKMLADTEREEALNLQIEFEWVLRQEVHAILKQLRSILVECAHRFPVPLYENEGKKTEKFILTVSPDQLKAVLTLTGDAI
SQ  TQADISFKLCKAPSQTQRTSITHDSPWKLQQVQDAANHLQTAINHIDDVDDSYHFKTSDEVLHVIGNILDALQRGRNSLL
SQ  VPKKKPIDELIKGRNMKSLVPNLPEDLAVSFYLQSHKLIIAVYQLLNNQGTMRFDSRQAEASVQWLNDVLLLLMNGQKLC
SQ  QQLKDKISVFSVYKDFTVGSRSPSALSY
//
ID  Q9GZN7;
PN  Protein rogdi homolog;
GN  ROGDI;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:22482807}. Presynapse {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, axon {ECO:0000250|UniProtKB:Q4V7D2}. Perikaryon {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q4V7D2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4V7D2}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000250|UniProtKB:Q4V7D2}.
DR  UNIPROT: Q9GZN7;
DR  UNIPROT: Q6IA00;
DR  PDB: 5XQH;
DR  PDB: 5XQI;
DR  Pfam: PF10259;
DR  OMIM: 226750;
DR  OMIM: 614574;
DR  DisGeNET: 79641;
DE  Function: 
DE  Disease: Kohlschuetter-Toenz syndrome (KTZS) [MIM:226750]: An autosomal recessive disorder characterized by severe global developmental delay, early-onset intractable seizures, spasticity, and amelogenesis imperfecta affecting both primary and secondary teeth and causing yellow or brown discoloration of the teeth. Although the phenotype is consistent, there is variability. Intellectual disability is related to the severity of seizures, and the disorder can thus be considered an epileptic encephalopathy. Some infants show normal development until seizure onset, whereas others are delayed from birth. The most severely affected individuals have profound intellectual disability, never acquire speech, and become bedridden early in life. {ECO:0000269|PubMed:22424600, ECO:0000269|PubMed:22482807, ECO:0000269|PubMed:25565929, ECO:0000269|PubMed:29153277}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q7L5N1; IntAct: EBI-730002; Score: 0.00
DE  Interaction: Q9P2H0; IntAct: EBI-730005; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-1105806; Score: 0.00
DE  Interaction: Q8CLN2; IntAct: EBI-2855911; Score: 0.00
DE  Interaction: Q9WMX2; IntAct: EBI-9081929; Score: 0.37
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q96MT8; IntAct: EBI-24506344; Score: 0.56
DE  Interaction: Q9Y4E6; IntAct: EBI-21716390; Score: 0.35
DE  Interaction: Q9Y485; IntAct: EBI-21716390; Score: 0.35
DE  Interaction: Q8TDJ6; IntAct: EBI-21716390; Score: 0.35
DE  Interaction: P50993; IntAct: EBI-21716390; Score: 0.35
DE  Interaction: P13535; IntAct: EBI-21716390; Score: 0.35
DE  Interaction: P12883; IntAct: EBI-21716390; Score: 0.35
DE  Interaction: O14983; IntAct: EBI-21716390; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-27127141; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0043204;
GO  GO:0043291;
GO  GO:0008021;
GO  GO:0007420;
GO  GO:0030097;
GO  GO:0022008;
GO  GO:0042475;
GO  GO:0008284;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATVMAATAAERAVLEEEFRWLLHDEVHAVLKQLQDILKEASLRFTLPGSGTEGPAKQENFILGSCGTDQVKGVLTLQGD
SQ  ALSQADVNLKMPRNNQLLHFAFREDKQWKLQQIQDARNHVSQAIYLLTSRDQSYQFKTGAEVLKLMDAVMLQLTRARNRL
SQ  TTPATLTLPEIAASGLTRMFAPALPSDLLVNVYINLNKLCLTVYQLHALQPNSTKNFRPAGGAVLHSPGAMFEWGSQRLE
SQ  VSHVHKVECVIPWLNDALVYFTVSLQLCQQLKDKISVFSSYWSYRPF
//
ID  Q3TDK6;
PN  Protein rogdi homolog;
GN  Rogdi;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Presynapse {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, axon {ECO:0000250|UniProtKB:Q4V7D2}. Perikaryon {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q4V7D2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4V7D2}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000250|UniProtKB:Q4V7D2}.
DR  UNIPROT: Q3TDK6;
DR  UNIPROT: Q8BL37;
DR  UNIPROT: Q922N4;
DR  UNIPROT: Q923H8;
DR  Pfam: PF10259;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P62158; IntAct: EBI-911456; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-6271507; Score: 0.35
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0043204;
GO  GO:0098793;
GO  GO:0043291;
GO  GO:0008021;
GO  GO:0007420;
GO  GO:0030097;
GO  GO:0022008;
GO  GO:0042475;
GO  GO:0008284;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATAMAASAAERAVLEEEFRWLLHAEVHAVLRQLQDILKEASLRFTLPGPSTEGPAKQENFILGSCGTDQVKGTLTLQGD
SQ  ALSQADVNLKMPRNNQLLHLAFREDKQWKLQQIQDARNHVSQAIYLLANRDESYQFKTGAEVLKLMDAVMLQLTRARSRL
SQ  TTPATLTLPEIAASGLTRMFAPTLPSDLLVNVYINLNKLCLTVYQLHALQPTSTKNFRPAGGAVLHSPGAMFEWGSQRLE
SQ  VSHVHKVECVIPWLNDALVYFTVSLQLCQQLKDKIAVFSSYWSSRPF
//
ID  Q5R7X1;
PN  Protein rogdi homolog;
GN  ROGDI;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Presynapse {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, axon {ECO:0000250|UniProtKB:Q4V7D2}. Perikaryon {ECO:0000250|UniProtKB:Q4V7D2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q4V7D2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q4V7D2}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000250|UniProtKB:Q4V7D2}.
DR  UNIPROT: Q5R7X1;
DR  Pfam: PF10259;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0043204;
GO  GO:0008021;
GO  GO:0007420;
GO  GO:0030097;
GO  GO:0022008;
GO  GO:0042475;
GO  GO:0008284;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATVMAATAAERAVLEEEFRWLLHDEVHAVLKQLQDILKEASLRFTLPGSGTEGPAKQENFILGSCGTDQVKGVLTLQGD
SQ  ALSQADVNLKMPRNNQLLHFTFREDKQWKLQQIQDARNHVSQAIYLLISRDESYQFKTGAEVLKLMDAVMLQLTRARNRL
SQ  TTPATLTLPEIAASGLTRMFAPALPSDLLVNVYINLNKLCLTVYQLHALQPNSTKNFRPAGGAVLHSPGAMFEWGSQRLE
SQ  VSHVHKVECVIPWLNDALVYFTVSLQLCQQLKDKISVFSSYWSYRPF
//
ID  Q4V7D2;
PN  Protein rogdi homolog;
GN  Rogdi;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q9GZN7}. Presynapse {ECO:0000269|PubMed:29150638}. Cell projection, axon {ECO:0000269|PubMed:29150638}. Perikaryon {ECO:0000269|PubMed:29150638}. Cell projection, dendrite {ECO:0000269|PubMed:29150638}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:29150638}. Note=Detected primarily at presynaptic sites on axons, and to a lesser degree in soma and dendrites. Not detected at post-synaptic sites. {ECO:0000269|PubMed:29150638}.
DR  UNIPROT: Q4V7D2;
DR  Pfam: PF10259;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0030425;
GO  GO:0005635;
GO  GO:0043204;
GO  GO:0098793;
GO  GO:0043291;
GO  GO:0008021;
GO  GO:0007420;
GO  GO:0030097;
GO  GO:0022008;
GO  GO:0042475;
GO  GO:0008284;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATAMAASAAERAVLEEEFRWLLHAEVHAVLRQLQDILKEASLRFTLPGPSTEGPAKQENFILGSCGTDQVKGVLTLQGD
SQ  ALSQADVNLKMPRNNQLLHFAFREDKQWKLQQIQDARNHVSQAIYLLANRDESYQFKTGAEVLKLMDAVMLQLTRARNRL
SQ  TTPATLTLPEIAASGLTRMFAPTLPSDLLVNVYINLNKLCLTVYQLHTLQPTSTKNFRPAGGAVLHSPGAMFEWGSQRLE
SQ  VSHVHKVECVIPWLNDALVYFTVSLQLCQQLKDKISVFSSYWSSRPF
//
ID  F1MSG6;
PN  Rap guanine nucleotide exchange factor 2;
GN  RAPGEF2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Late endosome {ECO:0000250}. Cell junction {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane. Colocalized with CTNNB1 at cell-cell contacts (By similarity). {ECO:0000250}.
DR  UNIPROT: F1MSG6;
DR  Pfam: PF00595;
DR  Pfam: PF00788;
DR  Pfam: PF00617;
DR  Pfam: PF00618;
DR  PROSITE: PS50042;
DR  PROSITE: PS50106;
DR  PROSITE: PS50200;
DR  PROSITE: PS50009;
DR  PROSITE: PS50212;
DE  Function: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B- Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions (By similarity). Binds to cAMP. {ECO:0000250, ECO:0000269|PubMed:23800469}.
DE  Reference Proteome: Yes;
DE  Interaction: Q02248; IntAct: EBI-6927091; Score: 0.50
DE  Interaction: Q0VCX4; IntAct: EBI-6927177; Score: 0.40
GO  GO:0016324;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0030139;
GO  GO:0005770;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0045202;
GO  GO:0031697;
GO  GO:0030552;
GO  GO:0005096;
GO  GO:0005085;
GO  GO:0030165;
GO  GO:0050699;
GO  GO:0071880;
GO  GO:0001568;
GO  GO:0031547;
GO  GO:0019933;
GO  GO:0071320;
GO  GO:0071321;
GO  GO:1990090;
GO  GO:0061028;
GO  GO:0021884;
GO  GO:0007186;
GO  GO:0008285;
GO  GO:0050774;
GO  GO:0048022;
GO  GO:0038180;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0007218;
GO  GO:2000481;
GO  GO:0043950;
GO  GO:2000670;
GO  GO:0070374;
GO  GO:0043547;
GO  GO:2001224;
GO  GO:0010976;
GO  GO:0032092;
GO  GO:0045860;
GO  GO:2001214;
GO  GO:0032486;
GO  GO:0007265;
GO  GO:1901888;
GO  GO:0021591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPE
SQ  TAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAG
SQ  TIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
SQ  NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLCSPMEVGKKLLEWF
SQ  NDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPAREAPLPFI
SQ  LLGGSEKGFGIFVDSVDSASKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
SQ  KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQD
SQ  DSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFSATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVVQAIRE
SQ  FAVTATPDQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
SQ  VATQLSMRNFELFRNIEPTEYIDDLFKLKSKTSCANLKTFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRE
SQ  CKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFL
SQ  HEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSS
SQ  FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPTDKKPVKSETSPVAPRAGLQPKAQPQPQP
SQ  PQPPHKLNQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHRRPAEDTISNTSSQLSSPPTSPQS
SQ  SPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSFDSLPVSLPDERRQRPSVSIVETSLASGRLERRPAVEPDQYSLG
SQ  SCAPLSESRGLYAAATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDYPG
SQ  DAAGLWASSSHMDQIMFPDHSAKYSRQSQSRESLDQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSLDADSSSMTA
SQ  VTAEEAKPAAMAAHIAVTPSAAKGLIARKEGRYREPPPTPPGYVGIPITDFPEAHPHPARKPPDYTVALQRSRMLARPAE
SQ  PPAPGSARPAPRPQWHRPGDGDPRAGPCAPPGLTAEEDEDEQVSAV
//
ID  F1PBJ0;
PN  Rap guanine nucleotide exchange factor 2;
GN  RAPGEF2;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction {ECO:0000269|PubMed:10873669}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Late endosome {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane (By similarity). Colocalized with CTNNB1 and TJP1 at cell-cell contacts. {ECO:0000250}.
DR  UNIPROT: F1PBJ0;
DR  Pfam: PF00595;
DR  Pfam: PF00788;
DR  Pfam: PF00617;
DR  Pfam: PF00618;
DR  PROSITE: PS50042;
DR  PROSITE: PS50106;
DR  PROSITE: PS50200;
DR  PROSITE: PS50009;
DR  PROSITE: PS50212;
DE  Function: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B- Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions.
DE  Reference Proteome: Yes;
DE  Interaction: B6V8E6; IntAct: EBI-6927144; Score: 0.46
GO  GO:0016324;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0030139;
GO  GO:0005770;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0045202;
GO  GO:0031697;
GO  GO:0030552;
GO  GO:0005096;
GO  GO:0005085;
GO  GO:0030165;
GO  GO:0050699;
GO  GO:0071880;
GO  GO:0001568;
GO  GO:0031547;
GO  GO:0019933;
GO  GO:0071320;
GO  GO:0071321;
GO  GO:1990090;
GO  GO:0061028;
GO  GO:0021884;
GO  GO:0007186;
GO  GO:0008285;
GO  GO:0050774;
GO  GO:0048022;
GO  GO:0038180;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0007218;
GO  GO:2000481;
GO  GO:0043950;
GO  GO:2000670;
GO  GO:0070374;
GO  GO:0043547;
GO  GO:2001224;
GO  GO:0010976;
GO  GO:0032092;
GO  GO:0045860;
GO  GO:2001214;
GO  GO:0032486;
GO  GO:0007265;
GO  GO:1901888;
GO  GO:0021591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPE
SQ  TAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAG
SQ  TIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
SQ  NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWF
SQ  NDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFI
SQ  LLGGSEKGFGIFVDSVDSGSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
SQ  KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQD
SQ  DSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFSTTPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIRE
SQ  FAVTATPDQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
SQ  VATQLSMRNFELFRNIEPTEYIDDLFKLKSKTSCANLKKFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRE
SQ  CKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFL
SQ  HEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSS
SQ  FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSETSPVAPRAGSQQKAQAQPPP
SQ  PQPQPQHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTSP
SQ  QSSPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHEERRQRHSVSIVETNLGVGRMERRTMMEPDQYS
SQ  LGSYAPMAESRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDY
SQ  SGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSV
SQ  TSVTTEETKPVPMPAHVAVTSSTAKGLIVRKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVARP
SQ  TDTAAPSPIQQPHGHPASGRPVNKPQWHKPNECDPRLAPYQSQGFSTEEDEDEQVSAV
//
ID  Q9Y4G8;
PN  Rap guanine nucleotide exchange factor 2;
GN  RAPGEF2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cell membrane. Late endosome. Cell junction {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Colocalizes with ADRB1 at the plasma membrane. Synaptosome. Enriched in synaptic plasma membrane and neuronal cell body. Colocalized with CTNNB1 at cell-cell contacts (By similarity). Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane. {ECO:0000250}.
DR  UNIPROT: Q9Y4G8;
DR  UNIPROT: D3DP27;
DR  PDB: 6QDT;
DR  Pfam: PF00595;
DR  Pfam: PF00788;
DR  Pfam: PF00617;
DR  Pfam: PF00618;
DR  PROSITE: PS50042;
DR  PROSITE: PS50106;
DR  PROSITE: PS50200;
DR  PROSITE: PS50009;
DR  PROSITE: PS50212;
DR  OMIM: 609530;
DR  OMIM: 618075;
DR  DisGeNET: 9693;
DE  Function: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP (PubMed:23800469, PubMed:10801446) or not (PubMed:10608844, PubMed:10548487, PubMed:11359771). Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP- independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269|PubMed:10548487, ECO:0000269|PubMed:10608844, ECO:0000269|PubMed:10608883, ECO:0000269|PubMed:10801446, ECO:0000269|PubMed:10934204, ECO:0000269|PubMed:11359771, ECO:0000269|PubMed:12391161, ECO:0000269|PubMed:16272156, ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:21840392, ECO:0000269|PubMed:23800469}.
DE  Disease: Epilepsy, familial adult myoclonic, 7 (FAME7) [MIM:618075]: A form of familial myoclonic epilepsy, a neurologic disorder characterized by cortical hand tremors, myoclonic jerks and occasional generalized or focal seizures with a non-progressive or very slowly progressive disease course. Usually, myoclonic tremor is the presenting symptom, characterized by tremulous finger movements and myoclonic jerks of the limbs increased by action and posture. In a minority of patients, seizures are the presenting symptom. Some patients exhibit mild cognitive impairment. FAME7 inheritance is autosomal dominant. {ECO:0000269|PubMed:29507423}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-8766313; Score: 0.44
DE  Interaction: P62834; IntAct: EBI-8766309; Score: 0.44
DE  Interaction: Q12840; IntAct: EBI-3450200; Score: 0.00
DE  Interaction: Q9Y3A3; IntAct: EBI-3450242; Score: 0.00
DE  Interaction: P41743; IntAct: EBI-2434129; Score: 0.35
DE  Interaction: Q86UL8; IntAct: EBI-7129086; Score: 0.52
DE  Interaction: Q99623; IntAct: EBI-1084965; Score: 0.00
DE  Interaction: P63104; IntAct: EBI-7195964; Score: 0.40
DE  Interaction: P03928; IntAct: EBI-3450122; Score: 0.00
DE  Interaction: P08107; IntAct: EBI-3450193; Score: 0.00
DE  Interaction: P33176; IntAct: EBI-3450207; Score: 0.00
DE  Interaction: P31016; IntAct: EBI-7958027; Score: 0.44
DE  Interaction: P46934; IntAct: EBI-7026879; Score: 0.44
DE  Interaction: Q62940; IntAct: EBI-7026897; Score: 0.44
DE  Interaction: Q96PU5; IntAct: EBI-7026931; Score: 0.44
DE  Interaction: B1AYL1; IntAct: EBI-8068510; Score: 0.44
DE  Interaction: P46937; IntAct: EBI-6912563; Score: 0.53
DE  Interaction: Q96QZ7; IntAct: EBI-8769602; Score: 0.52
DE  Interaction: Q9H0H5; IntAct: EBI-11003256; Score: 0.35
DE  Interaction: P26041; IntAct: EBI-11010611; Score: 0.35
DE  Interaction: Q9UJA5; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q14696; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q6BDS2; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q96L50; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q96KM6; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q8N9Q2; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: A6H8Y1; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: C9J1X0; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q9BYT9; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q99442; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q96IX5; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: O43414; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: P20674; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: P98170; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: G5E9A6; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q9H930; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q14558; IntAct: EBI-11041084; Score: 0.35
DE  Interaction: Q96JG6; IntAct: EBI-11134088; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q16695; IntAct: EBI-20921180; Score: 0.40
DE  Interaction: P16401; IntAct: EBI-20925170; Score: 0.40
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030139;
GO  GO:0005887;
GO  GO:0005770;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0045202;
GO  GO:0031697;
GO  GO:0005509;
GO  GO:0030552;
GO  GO:0019992;
GO  GO:0005096;
GO  GO:0005085;
GO  GO:0030165;
GO  GO:0070300;
GO  GO:0050699;
GO  GO:0071880;
GO  GO:0001568;
GO  GO:0031547;
GO  GO:0019933;
GO  GO:0071320;
GO  GO:0071321;
GO  GO:1990090;
GO  GO:0061028;
GO  GO:0090557;
GO  GO:0021884;
GO  GO:0007186;
GO  GO:0035556;
GO  GO:0000165;
GO  GO:0030033;
GO  GO:0008285;
GO  GO:0050774;
GO  GO:0048022;
GO  GO:0038180;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0007218;
GO  GO:2000481;
GO  GO:0043950;
GO  GO:2000670;
GO  GO:0070374;
GO  GO:0043547;
GO  GO:2001224;
GO  GO:0010976;
GO  GO:0032092;
GO  GO:0045860;
GO  GO:2001214;
GO  GO:0072659;
GO  GO:0032486;
GO  GO:0007265;
GO  GO:1901888;
GO  GO:0048167;
GO  GO:0007264;
GO  GO:0021591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPE
SQ  TAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAG
SQ  TIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
SQ  NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWF
SQ  NDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFI
SQ  LLGGSEKGFGIFVDSVDSGSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
SQ  KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQD
SQ  DSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFSATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIRE
SQ  FAVTATPDQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
SQ  VATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRE
SQ  CKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFL
SQ  HEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSS
SQ  FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSETSPVAPRAGSQQKAQSLPQP
SQ  QQQPPPAHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTS
SQ  PQSSPRKGYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVETNLGMGRMERRTMIEPDQY
SQ  SLGSYAPMSEGRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFD
SQ  YSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSS
SQ  LTSVTTEETKPVPMPAHIAVASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVAR
SQ  SSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDEDEQVSAV
//
ID  Q8CHG7;
PN  Rap guanine nucleotide exchange factor 2;
GN  Rapgef2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Late endosome {ECO:0000250}. Cell junction {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane. Colocalized with CTNNB1 at cell-cell contacts (By similarity). {ECO:0000250}.
DR  UNIPROT: Q8CHG7;
DR  UNIPROT: E9QMD0;
DR  Pfam: PF00595;
DR  Pfam: PF00788;
DR  Pfam: PF00617;
DR  Pfam: PF00618;
DR  PROSITE: PS50042;
DR  PROSITE: PS50106;
DR  PROSITE: PS50200;
DR  PROSITE: PS50009;
DR  PROSITE: PS50212;
DE  Function: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B- Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269|PubMed:16272156, ECO:0000269|PubMed:17826737, ECO:0000269|PubMed:19453629, ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:21864586, ECO:0000269|PubMed:23800469}.
DE  Reference Proteome: Yes;
DE  Interaction: P35922; IntAct: EBI-16728828; Score: 0.35
DE  Interaction: Q7TMB8; IntAct: EBI-16727444; Score: 0.35
DE  Interaction: P46934; IntAct: EBI-7027504; Score: 0.44
DE  Interaction: Q02248; IntAct: EBI-6927528; Score: 0.40
DE  Interaction: Q4ACU6; IntAct: EBI-16726570; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16736255; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26472137; Score: 0.35
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030139;
GO  GO:0005770;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0045202;
GO  GO:0031697;
GO  GO:0030552;
GO  GO:0005096;
GO  GO:0005085;
GO  GO:0030165;
GO  GO:0070300;
GO  GO:0019901;
GO  GO:0050699;
GO  GO:0071880;
GO  GO:0001568;
GO  GO:0031547;
GO  GO:0019933;
GO  GO:0071320;
GO  GO:0071321;
GO  GO:1990090;
GO  GO:0061028;
GO  GO:0090557;
GO  GO:0021884;
GO  GO:0007186;
GO  GO:0030033;
GO  GO:0008285;
GO  GO:0050774;
GO  GO:0048022;
GO  GO:0038180;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0007218;
GO  GO:2000481;
GO  GO:0043950;
GO  GO:2000670;
GO  GO:0070374;
GO  GO:0043547;
GO  GO:2001224;
GO  GO:0010976;
GO  GO:0032092;
GO  GO:0045860;
GO  GO:2001214;
GO  GO:0072659;
GO  GO:0032486;
GO  GO:0007265;
GO  GO:1901888;
GO  GO:0048167;
GO  GO:0021591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPLAAPANHGVLGQQEKQSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPE
SQ  TAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAG
SQ  TIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
SQ  NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWF
SQ  NDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFI
SQ  LLGGSEKGFGIFVDSVDSCSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
SQ  KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQD
SQ  DSIVGLRQTKHIPAALPVSGTLSSSNPDLLQSHHRILDFSTTPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIRE
SQ  FAVTATPEQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
SQ  VATQLSMRNFELFRNIEPTEYIDDLFKLKSKTSCANLKKFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRE
SQ  CKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLSGQNLQPPVIPLFPVIKKDLTFL
SQ  HEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSANATVLDVAQTGGHKKRVRRSS
SQ  FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATSTLPKNPGDKKPVKSETSPVAPRAGPQQKVQPQQPL
SQ  AQPQPPHKVSQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHRKQAEDTISNASSQLSSPPTSP
SQ  QSSPRKGYALALSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVESNLGVGRMERRTLMEPDQYS
SQ  LGSYAPVSESRGLYAAATVISSPSTEELSHDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDY
SQ  SGDAASIWASGGHMDQMMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSAEAESSSM
SQ  VPVTTEEAKPVPMPAHIAVTPSTTKGLIARKEGRYREPPPTPPGYVGIPIADFPEGPCHPARKPPDYNVALQRSRMVARP
SQ  TEAPAPGQTPPAAAASRPGSKPQWHKPSDADPRLAPFQPQGFAGAEEDEDEQVSAV
//
ID  F1M386;
PN  Rap guanine nucleotide exchange factor 2;
GN  Rapgef2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:10548487, ECO:0000269|PubMed:10801446, ECO:0000269|PubMed:12391161, ECO:0000269|PubMed:17724123}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Late endosome {ECO:0000250}. Cell junction {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane. Colocalized with CTNNB1 at cell-cell contacts (By similarity). Colocalizes with ADRB1 at the plasma membrane. Synaptosome. Enriched in synaptic plasma membrane and neuronal cell body. {ECO:0000250}.
DR  UNIPROT: F1M386;
DR  UNIPROT: D3ZD17;
DR  Pfam: PF00595;
DR  Pfam: PF00788;
DR  Pfam: PF00617;
DR  Pfam: PF00618;
DR  PROSITE: PS50042;
DR  PROSITE: PS50106;
DR  PROSITE: PS50200;
DR  PROSITE: PS50009;
DR  PROSITE: PS50212;
DE  Function: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B- Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269|PubMed:17724123}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5XIE8; IntAct: EBI-26439741; Score: 0.35
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0005911;
GO  GO:0005737;
GO  GO:0030139;
GO  GO:0005770;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0045202;
GO  GO:0031697;
GO  GO:0030552;
GO  GO:0005096;
GO  GO:0005085;
GO  GO:0030165;
GO  GO:0070300;
GO  GO:0019901;
GO  GO:0050699;
GO  GO:0071880;
GO  GO:0001568;
GO  GO:0031547;
GO  GO:0019933;
GO  GO:0071320;
GO  GO:0071321;
GO  GO:1990090;
GO  GO:0061028;
GO  GO:0090557;
GO  GO:0021884;
GO  GO:0007186;
GO  GO:0030033;
GO  GO:0008285;
GO  GO:0050774;
GO  GO:0048022;
GO  GO:0038180;
GO  GO:0001764;
GO  GO:0031175;
GO  GO:0007218;
GO  GO:2000481;
GO  GO:0043950;
GO  GO:2000670;
GO  GO:0070374;
GO  GO:0043547;
GO  GO:2001224;
GO  GO:0010976;
GO  GO:0032092;
GO  GO:0045860;
GO  GO:2001214;
GO  GO:0072659;
GO  GO:0032486;
GO  GO:0007265;
GO  GO:1901888;
GO  GO:0048167;
GO  GO:0021591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKPLAAPANHGVLGQQEKQSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPE
SQ  TAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAG
SQ  TIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
SQ  NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWF
SQ  NDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRSMTLTKPSREAPLPFI
SQ  LLGGSEKGFGIFVDSVDSSSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
SQ  KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQD
SQ  DSIVGLRQTKHIPAALPVSGTLSSSNPDLLQSHHRILDFSTTPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIRE
SQ  FAVTATPEQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
SQ  VATQLSMRNFELFRNIEPTEYIDDLFKLKSKTSCANLKKFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRE
SQ  CKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLSGQNLQPPVIPLFPVIKKDLTFL
SQ  HEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSANATVLDVAQTGGHKKRVRRSS
SQ  FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATSTLPKNPADRKPVKSETSPVAPRAGPQQKAQPQQPL
SQ  APPQPSHKVSQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHRKQAEDTISNASSQLSSPPTSP
SQ  QSSPRKGYALALSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVESNLGVGRMERRTLMEPDQYS
SQ  LGSYAPVSESRGLYAAATVISSPSTEELSHDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDY
SQ  SGDATGIWASGGHMDQIMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSTEAESSSM
SQ  VPVTTEEAKPVPMPAHIAVTPSTTKGLIARKEGRYREPPPTPPGYVGIPIADFPEGPCHPARKPPDYNVALQRSRMVARP
SQ  TEAPAPGQTPPAATASRPGSKPQWHKPSDADPRLAPFQPQGFAGAEEDEDEQVSAV
//
ID  Q684P5;
PN  Rap1 GTPase-activating protein 2;
GN  RAP1GAP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15632203}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15632203}.
DR  UNIPROT: Q684P5;
DR  UNIPROT: B2RTY5;
DR  UNIPROT: Q684P4;
DR  UNIPROT: Q6AI00;
DR  UNIPROT: Q6ZVF0;
DR  UNIPROT: Q9UPW2;
DR  Pfam: PF02145;
DR  PROSITE: PS50085;
DR  OMIM: 618714;
DR  DisGeNET: 23108;
DE  Function: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP- bound state. {ECO:0000269|PubMed:15632203}.
DE  Reference Proteome: Yes;
DE  Interaction: P62258; IntAct: EBI-3452989; Score: 0.00
DE  Interaction: Q9H4A3; IntAct: EBI-3454034; Score: 0.00
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q6FHY5; IntAct: EBI-24366985; Score: 0.56
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005096;
GO  GO:0090630;
GO  GO:0002250;
GO  GO:0008361;
GO  GO:0051056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGRKRSVSFGGFGWIDKTMLASLKVKKQELANSSDATLPDRPLSPPLTAPPTMKSSEFFEMLEKMQGIKLEEQKPGPQK
SQ  NKDDYIPYPSIDEVVEKGGPYPQVILPQFGGYWIEDPENVGTPTSLGSSICEEEEEDNLSPNTFGYKLECKGEARAYRRH
SQ  FLGKDHLNFYCTGSSLGNLILSVKCEEAEGIEYLRVILRSKLKTVHERIPLAGLSKLPSVPQIAKAFCDDAVGLRFNPVL
SQ  YPKASQMIVSYDEHEVNNTFKFGVIYQKARQTLEEELFGNNEESPAFKEFLDLLGDTITLQDFKGFRGGLDVTHGQTGVE
SQ  SVYTTFRDREIMFHVSTKLPFTDGDAQQLQRKRHIGNDIVAIIFQEENTPFVPDMIASNFLHAYIVVQVETPGTETPSYK
SQ  VSVTAREDVPTFGPPLPSPPVFQKGPEFREFLLTKLTNAENACCKSDKFAKLEDRTRAALLDNLHDELHAHTQAMLGLGP
SQ  EEDKFENGGHGGFLESFKRAIRVRSHSMETMVGGQKKSHSGGIPGSLSGGISHNSMEVTKTTFSPPVVAATVKNQSRSPI
SQ  KRRSGLFPRLHTGSEGQGDSRARCDSTSSTPKTPDGGHSSQEIKSETSSNPSSPEICPNKEKPFMKLKENGRAISRSSSS
SQ  TSSVSSTAGEGEAMEEGDSGGSQPSTTSPFKQEVFVYSPSPSSESPSLGAAATPIIMSRSPTDAKSRNSPRSNLKFRFDK
SQ  LSHASSGAGH
//
ID  P19811;
PN  Non-structural protein 12;
GN  rep;
OS  299386;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp1 papain-like cysteine proteinase]: Host nucleus. Host cytoplasm. [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}.
DR  UNIPROT: P19811;
DR  UNIPROT: Q88625;
DR  UNIPROT: Q8QZQ5;
DR  UNIPROT: Q91DM2;
DR  PDB: 1MBM;
DR  PDB: 2L8K;
DR  PDB: 4IUM;
DR  PDB: 4N0N;
DR  PDB: 4N0O;
DR  PDB: 5F17;
DR  PDB: 5HBZ;
DR  PDB: 5HC1;
DR  Pfam: PF16749;
DR  Pfam: PF19215;
DR  Pfam: PF12581;
DR  Pfam: PF14754;
DR  Pfam: PF14755;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF17873;
DR  Pfam: PF01443;
DR  Pfam: PF17977;
DR  PROSITE: PS51538;
DR  PROSITE: PS51961;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000269|PubMed:18078692}. Nsp1 is essential for viral subgenomic mRNA synthesis. {ECO:0000269|PubMed:11172046}. Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity. {ECO:0000269|PubMed:18078692}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000269|PubMed:18078692}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000269|PubMed:11000230, ECO:0000269|PubMed:24369429}. [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (PubMed:19297500). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:19297500}.
DE  Reference Proteome: Yes;
DE  Interaction: P19811; IntAct: EBI-27070292; Score: 0.56
GO  GO:0033644;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0070008;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039579;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATFSATGFGGSFVRDWSLDLPDACEHGAGLCCEVDGSTLCAECFRGCEGMEQCPGLFMGLLKLASPVPVGHKFLIGWYR
SQ  AAKVTGRYNFLELLQHPAFAQLRVVDARLAIEEASVFISTDHASAKRFPGARFALTPVYANAWVVSPAANSLIVTTDQEQ
SQ  DGFCWLKLLPPDRREAGLRLYYNHYREQRTGWLSKTGLRLWLGDLGLGINASSGGLKFHIMRGSPQRAWHITTRSCKLKS
SQ  YYVCDISEADWSCLPAGNYGGYNPPGDGACGYRCLAFMNGATVVSAGCSSDLWCDDELAYRVFQLSPTFTVTIPGGRVCP
SQ  NAKYAMICDKQHWRVKRAKGVGLCLDESCFRGICNCQRMSGPPPAPVSAAVLDHILEAATFGNVRVVTPEGQPRPVPAPR
SQ  VRPSANSSGDVKDPAPVPPVPKPRTKLATPNPTQAPIPAPRTRLQGASTQEPLASAGVASDSAPKWRVAKTVYSSAERFR
SQ  TELVQRARSVGDVLVQALPLKTPAVQRYTMTLKMMRSRFSWHCDVWYPLAVIACLLPIWPSLALLLSFAIGLIPSVGNNV
SQ  VLTALLVSSANYVASMDHQCEGAACLALLEEEHYYRAVRWRPITGALSLVLNLLGQVGYVARSTFDAAYVPCTVFDLCSF
SQ  AILYLCRNRCWRCFGRCVRVGPATHVLGSTGQRVSKLALIDLCDHFSKPTIDVVGMATGWSGCYTGTAAMERQCASTVDP
SQ  HSFDQKKAGATVYLTPPVNSGSALQCLNVMWKRPIGSTVLGEQTGAVVTAVKSISFSPPCCVSTTLPTRPGVTVVDHALY
SQ  NRLTASGVDPALLRVGQGDFLKLNPGFRLIGGWIYGICYFVLVVVSTFTCLPIKCGIGTRDPFCRRVFSVPVTKTQEHCH
SQ  AGMCASAEGISLDSLGLTQLQSYWIAAVTSGLVILLVCHRLAISALDLLTLASPLVLLVFPWASVGLLLACSLAGAAVKI
SQ  QLLATLFVNLFFPQATLVTMGYWACVAALAVYSLMGLRVKVNVPMCVTPAHFLLLARSAGQSREQMLRVSAAAPTNSLLG
SQ  VARDCYVTGTTRLYIPKEGGMVFEGLFRSPKARGNVGFVAGSSYGTGSVWTRNNEVVVLTASHVVGRANMATLKIGDAML
SQ  TLTFKKNGDFAEAVTTQSELPGNWPQLHFAQPTTGPASWCTATGDEEGLLSGEVCLAWTTSGDSGSAVVQGDAVVGVHTG
SQ  SNTSGVAYVTTPSGKLLGADTVTLSSLSKHFTGPLTSIPKDIPDNIIADVDAVPRSLAMLIDGLSNRESSLSGPQLLLIA
SQ  CFMWSYLNQPAYLPYVLGFFAANFFLPKSVGRPVVTGLLWLCCLFTPLSMRLCLFHLVCATVTGNVISLWFYITAAGTSY
SQ  LSEMWFGGYPTMLFVPRFLVYQFPGWAIGTVLAVCSITMLAAALGHTLLLDVFSASGRFDRTFMMKYFLEGGVKESVTAS
SQ  VTRAYGKPITQESLTATLAALTDDDFQFLSDVLDCRAVRSAMNLRAALTSFQVAQYRNILNASLQVDRDAARSRRLMAKL
SQ  ADFAVEQEVTAGDRVVVIDGLDRMAHFKDDLVLVPLTTKVVGGSRCTICDVVKEEANDTPVKPMPSRRRRKGLPKGAQLE
SQ  WDRHQEEKRNAGDDDFAVSNDYVKRVPKYWDPSDTRGTTVKIAGTTYQKVVDYSGNVHYVEHQEDLLDYVLGKGSYEGLD
SQ  QDKVLDLTNMLKVDPTELSSKDKAKARQLAHLLLDLANPVEAVNQLNLRAPHIFPGDVGRRTFADSKDKGFVALHSRTMF
SQ  LAARDFLFNIKFVCDEEFTKTPKDTLLGYVRACPGYWFIFRRTHRSLIDAYWDSMECVYALPTISDFDVSPGDVAVTGER
SQ  WDFESPGGGRAKRLTADLVHAFQGFHGASYSYDDKVAAAVSGDPYRSDGVLYNTRWGNIPYSVPTNALEATACYRAGCEA
SQ  VTDGTNVIATIGPFPEQQPIPDIPKSVLDNCADISCDAFIAPAAETALCGDLEKYNLSTQGFVLPSVFSMVRAYLKEEIG
SQ  DAPPLYLPSTVPSKNSQAGINGAEFPTKSLQSYCLIDDMVSQSMKSNLQTATMATCKRQYCSKYKIRSILGTNNYIGLGL
SQ  RACLSGVTAAFQKAGKDGSPIYLGKSKFDPIPAPDKYCLETDLESCDRSTPALVRWFATNLIFELAGQPELVHSYVLNCC
SQ  HDLVVAGSVAFTKRGGLSSGDPITSISNTIYSLVLYTQHMLLCGLEGYFPEIAEKYLDGSLELRDMFKYVRVYIYSDDVV
SQ  LTTPNQHYAASFDRWVPHLQALLGFKVDPKKTVNTSSPSFLGCRFKQVDGKCYLASLQDRVTRSLLYHIGAKNPSEYYEA
SQ  AVSIFKDSIICCDEDWWTDLHRRISGAARTDGVEFPTIEMLTSFRTKQYESAVCTVCGAAPVAKSACGGWFCGNCVPYHA
SQ  GHCHTTSLFANCGHDIMYRSTYCTMCEGSPKQMVPKVPHPILDHLLCHIDYGSKEELTLVVADGRTTSPPGRYKVGHKVV
SQ  AVVADVGGNIVFGCGPGSHIAVPLQDTLKGVVVNKALKNAAASEYVEGPPGSGKTFHLVKDVLAVVGSATLVVPTHASML
SQ  DCINKLKQAGADPYFVVPKYTVLDFPRPGSGNITVRLPQVGTSEGETFVDEVAYFSPVDLARILTQGRVKGYGDLNQLGC
SQ  VGPASVPRNLWLRHFVSLEPLRVCHRFGAAVCDLIKGIYPYYEPAPHTTKVVFVPNPDFEKGVVITAYHKDRGLGHRTID
SQ  SIQGCTFPVVTLRLPTPQSLTRPRAVVAVTRASQELYIYDPFDQLSGLLKFTKEAEAQDLIHGPPTACHLGQEIDLWSNE
SQ  GLEYYKEVNLLYTHVPIKDGVIHSYPNCGPACGWEKQSNKISCLPRVAQNLGYHYSPDLPGFCPIPKELAEHWPVVSNDR
SQ  YPNCLQITLQQVCELSKPCSAGYMVGQSVFVQTPGVTSYWLTEWVDGKARALPDSLFSSGRFETNSRAFLDEAEEKFAAA
SQ  HPHACLGEINKSTVGGSHFIFSQYLPPLLPADAVALVGASLAGKAAKAACSVVDVYAPSFEPYLHPETLSRVYKIMIDFK
SQ  PCRLMVWRNATFYVQEGVDAVTSALAAVSKLIKVPANEPVSFHVASGYRTNALVAPQAKISIGAYAAEWALSTEPPPAGY
SQ  AIVRRYIVKRLLSSTEVFLCRRGVVSSTSVQTICALEGCKPLFNFLQIGSVIGPV
//
ID  Q06502;
PN  Non-structural protein 12;
GN  rep;
OS  300015;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}.
DR  UNIPROT: Q06502;
DR  UNIPROT: Q06503;
DR  Pfam: PF16749;
DR  Pfam: PF12581;
DR  Pfam: PF05410;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51961;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The Nsp1 chain is essential for viral subgenomic mRNA synthesis. {ECO:0000250}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000250}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250}. [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P19811}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0070008;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQSGFDRCLCTPNARVFWERGQVYCTRCLAARPLLPLSQQHPRLGALGLFYRPASPLSWEAPVTYPTKECRPGGMCWLSS
SQ  IYPIARMTSGNHNFQARLNFIASVVYRDGKLTSKHLEEDFEVYSRGCRWYPITGPVPGIALYANAVHVSDESFPGATHVL
SQ  SNLPLPQQPLRKGLCPFADARANVWRYKGNTVFVSPQGYLWTTGSNDSVPEPWGEDRRLCEKIISSLPADHLVKINFSNY
SQ  PFDYSFTGGDGAGFVVFPCKERDTKFSKCWEKIFEDHSGWMAACEEADLADRMGYRTPAGVAGPYLARRLQVRGLRAVVK
SQ  PENNDYIVWALGVPESYIRHVSRAGEPVEEFFVKVGEFSIVSNCVVTPHPKFRFQTRKYYGYSPPGDGACGLHCISAMLN
SQ  DIFGDSFTTRLGKCSRDSSEWLSDQDLYQLVMTANLPATIGHCPSAIYKLDCVNQHWTVTKRKGDRAVGRLAPDCLRGVC
SQ  GECEMGIHIGADTDLSPIVELQLAQDVSPRPGALLWFLELHELCVVDDDFAHAIARAGEEYRRAMGIPRDDWVILAELMT
SQ  ENCRTRHQVLEKLQRGLQLQASSRPSSPASVSPASSVDLSAAGLLLSGTESDKEAVVAVNDGCYTVLGFDKNEATKSEQD
SQ  LATDLFCDLVKPMETSTTKLESRKILEAAAKALESCKPKRKRSRKKKTRTPSPTCSVDAAVAEPTSVNSLGNQDTRETCA
SQ  SEKKAEKCPTPTPPPRPKRAALKNSNSGCVLKDIIWNQTGPGVKCLTIVEDVRAFLKGITPPGGVLSTRSRITKHIVDHF
SQ  HSICEQTPELVLAHAEHQAKNLHELLASETAKLILGIGEDPLKKLVGSQRSLPRRLGFGAWLGGQQKTSGGCGEREFKDV
SQ  GRKSGAERTPSKRDLGVSLGDQLSQDGARRLSSSTACEIKESVPPIIDSGGGLSQKFMAWLNHQVFVLSSHLLAVWSFIF
SQ  GSRQVLGVFDYVYTLFCLCCVLLCFYLPAIGFMTLVGCVFGSPWRVRLSVFSVWLCVAVVVFQEVLPEPGAVCTSASAER
SQ  AAALERYTSNGVHRPVNHLSVGLVGTVAGFVARSVGGPRRYWFYFLRLMVLLDLGLVFLAVALRGSCKKCFCKCVRTASH
SQ  EVQLRVFPSTKVARTTLEAICDMYSAPRVDPIFIATGVRGCWTGSVSPHQVTEKPVSYSNLDDKKISNKTVVPPPTDPQQ
SQ  AVRCLKVLQCGGSIQDVSVPEVKKVTKVPFKAPFFPNVTIDPECYIVVDPVTYSAAMRGGYGVSHLIVGLGDFAEVNGLR
SQ  FVSGGQIADFVCLGLYVLLNFLLSAWLSSPVSCGRGTNDPWCRNPFSYPVVGQGVMCNSHLCVAEDGLTSPMTLSYSLID
SQ  WALMVAIMATVAIFFAKISLLVDVVCVFCCLLMYAFPSLSIAAFGFPFVLCKVSLHPITLVWVQFFLLAVNVWAGVASVV
SQ  VLISSWFLARATSSLGLITPYDVHMITATPRGASSLASAPEGTYLAAVRRSALTGRCCMFVPTNFGSVLEGSLRTRGCAK
SQ  NVVSVFGSASGSGGVFTINGNPVVVTASHLLSDGKARVSCVGFSQCLDFKCAGDYAFARVANWKGDAPKAELSHRRGRAY
SQ  CSPLVGLSLDLLGKNSAFCFTKCGDSGSPVVDEDGNLLGIHTGSNKRGSGMVTTHGGKTLGMANVKLSEMCPHYSGPGVP
SQ  VSTVKLPKHLVVDVETVSSDLVAVVESLPALEGALSSMQLLCVFFFLWRLIHVPDVPVIRIAFFFLNEILPVMLARLMFS
SQ  FALSLFFCVHWLFCSSVAVAFGDCCSKSVTGYSVQVLLLRLVIAALNRPCGPFGFSLLGQLSQCCLMLCLLDIELQLLGC
SQ  LYLGQLLMWPPKEIFFHPTGQFMFLPLFLSLFKRNALADMLVGNGCFDAAFFLKYFAEGNLRDGVSDSCNMTPEGLTAAL
SQ  AITLSDDDLEFLQRHSEFKCFVSASNMRNGAKEFIESAYARALRAQLAATDKIKASKSILAKLESFAGGVVTQVEPGDVV
SQ  VVLGKKVIGDLVEVVINDAKHVIRVIETRTMAGTQFSVGTICGDLENACEDPSGLVKTSKKQARRQKRTGLGTEVVGTVV
SQ  IDGVSYNKVWHIATGDVTYEGCLVTENPQLRPLGMTTIGRFQEFIRKHGEKVKTSVEKYPVGKKKSVEFNITTYLLDGEE
SQ  YDVPDHEPLEWTITIGESDLEAERLTVDQALRHMGHDSLLTAKEKEKLARIIESLNGLQQASALNCLATSGLDRCTRGGL
SQ  TVSGDAVKLVRYHSRTFSIGDVNLKVMGREEYGRTVGKQGHCLVANLVDGVVVMRKHEPSLVDVLLTGEDADLISPTHGP
SQ  GNTGVHGFTWDFEAPPTDLELELSEQIITACSIRRGDAPSLDLPYKLHPVRGNPYRDRGVLYNTRFGDIKYLTPQKTKEP
SQ  LHAAACFNPKGVPVSDSETLVATTLPHGFELYVPTIPQSVLEYLDSRPMHRKCCVRAVVRGLAECDLQKFDLSRQGFVLP
SQ  GVLYMVRRYLCRLVGIRRRLFLPSTYPAKNSMAGINGNRFPTHVVQSHPDIDALCERACKEHWQTVTPCTLKKQYCSKAK
SQ  TRTILGTNNFVALGLRSALSGVTQGFMRKGIGSPICLGKNKFTPLPTKVSGRCLEADLASCDRSTPAIIRWFTTNLLFEL
SQ  AGPEEWIPSYVLNCCHDAVSTMSGCFDKRGGLSSGDPVTSVSNTVYSLVIYAQHMVLSAFRCGHKVGGLFLRDSLEMEQL
SQ  FELQPLLVYSDDVVLYDESSELPNYHFFVDHLDLMLGFKTDRSKTVITSDPQFPGCRIAAGRVLVPQRDRILAALAYHMK
SQ  ASCVSDYFASAAAILMDACACCDYDEDWYFDLVCGIADCARKEGFRFPGPSFYVDMWKRLSVEEKKKCRTCAHCGAPSTL
SQ  VSSCGLNLCDYHGHGHPHCPVVLPCGHAVGSGVCDGCSSPVMSLNTELDKLLACVPYHPPKVELLSVNDGVSSLPPGRYQ
SQ  ARGGVVSVRRDILGNVVDLPDGDYQVMKVAQTCADICMVSINSHILRSQFITGAPGTGKTTYLLSVVRDDDVIYTPTHRT
SQ  MLDVVKALGTCRFDPPKDTPLEFPVPSRTGPCVRLIRAGFIPGRVSYLDEAAYCNPLDVLKILSKTPLVCVGDLNQLPPV
SQ  DFIGPCYAFALMLGRQLIEVFRFGPSIVNPIKKFYREELVSRGPDTGVKFLKSYQPYGQVLTPYHRDRVDGAITIDSSQG
SQ  CTYDVITVYLPTPKSLNSARALVAITRARFYVFVYDPHNQLEQYLNMSEHEPAGAVAFWCGEQPMMISEGRVQRLSGPAQ
SQ  TTDPKLQQLMGLEGTASPLPQVAHNLGFYYSPDLVQFARIPSELCKHWPVVTAQNRTDWPDRLVCSMSKIDKCSRAIFCA
SQ  GYHVGPSVFLGVPGVVSYYLTKFLKGKPVPLPDSLMSTGRIALNVREYLDEKEMEFSSRCPHAFIGEVKGSNVGGCHHVT
SQ  SRYLPPVLVPGSVVKIGVSCPGKAAKELCTVTDVYLPELDPYLNPPTKSMDYKLLVDFQPVKLMVWKDATAYFHEGIRPM
SQ  ESMSRFLKVPQEEGVFFDLDEFVTNAKVSKLPCKYSVSANQFLTDVVLSMTHPSLAPPDYELLFARAYCVPGLDVGTLNA
SQ  YIYRRGPSTYTTSNIARLVKDICCPVGCKGSGYMFPK
//
ID  Q83017;
PN  Non-structural protein 12;
GN  rep;
OS  300016;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}.
DR  UNIPROT: Q83017;
DR  UNIPROT: Q83018;
DR  UNIPROT: Q83024;
DR  UNIPROT: Q83025;
DR  UNIPROT: Q86716;
DR  Pfam: PF16749;
DR  Pfam: PF12581;
DR  Pfam: PF05410;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51961;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The Nsp1 chain is essential for viral subgenomic mRNA synthesis. {ECO:0000250}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000250}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250}. [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P19811}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0016829;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0070008;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQSGFDRCLCTPNARVFWEHGQVYCTRCLAARPLLPLSQQNPRLGALGLFYRPATPLTWEAPITYPTKECRPGGLCWLSG
SQ  IYPIARMTSGNHNFQARLNFVASVVYRDGKLTSKHLEEEFEVYSRGCRWYPITGPVPGIALYANAVHVSDEPFPGCTHVL
SQ  SNLPLPQQPLRKGLCPFSDARAEVWRYKGNTIFVSEQGYLWTTGSNDSVPEPWGEARRLCEKIIASLPADHLVKIEFSNY
SQ  PFDYSFTGGDGAGYVLFPCKKNDTKFSKCWEKVFEDHSSWKVACEEADLADRMGYRTPAGVAGPYLARRLQYRGLRAVVK
SQ  PEQNDYVVWALGVPESYIRHISRAGEPVENFFVRVGEFSIVSNCVATPYPKFRFQTRKYYGYSPPGDGACGLHCISAIIN
SQ  DIFGDALCTKLTNCSRDSSEWLSDQDMYQLVMTARLPATLGHCPSATYKLDCVNQHWTVTKRKGDRALGGLSPECVRGVC
SQ  GGECKFVPTYPREINLELAAKSPISALAFSLGVEPYCDCWNFTNSVLVNDSLAVETARAGEAYRSAMGIPKDDWVLLAEL
SQ  MTENCLTRREVLDKLQRGLRLHATSKPGSPASVSPASSIDFSAAGLLLDGTESDKEAVVAVNNDCYTVLGFDKNSATKSE
SQ  QELATGLFSELVEPMETSTSKHESRKILEAASRALKSAKPKRKRNKKKKTSSPTPTPPETPTREVPGAIEVVSGDEEAGA
SQ  CESATIVPDKAQARPPPRPKRQALKKAEQGFILKDIIWNPTESGVKCLTIVEDVRAFLKSITPPGGALGTRARITAHIVE
SQ  QFHVIRESTPELVLAHAEHQAKNMHELLLSEKAKLILGIGEDTLKKLVSSQRSLPRSIGFGAWLSDQQKTADSCGEREFV
SQ  EVPLKSGAEPTPSKRDLGVSLGDQLSQDGAPRLSSSTACEIKERVPPIKDSGGGLGQKFMAWLNHQVFLLSSHLLAMWSV
SQ  VLGSRQKLNWADYVYTLFCLCCVLLCFHFPAIGFIPLAGCVFGSPWRVRLSVFSVWLCVAVVVFQEVLPEPGSVCSSASA
SQ  ECAAALERYSGNGVHRPVNHIGVGLVGTVAGFVARVVGGPRHYWFYFLRLMVVLDLGLVFLAVALRGRCKKCFCKCVRVA
SQ  PHEVHLRVFPLTKVARPTLEAVCDMYSAPRVDPILVATGIKGCWQGKVSPHQVTDKPVSYSNLEEKKISNKTVVPPPTDP
SQ  QQAVKCLKVLQCGGSIQDVGVPEVKKVSKVPYKAPFFPNVSIDPECYIVVDPVTYSAAMRGGYGVSHLIVGTGDFAEVNG
SQ  LRFVSGGHVADFVCLGLYVMLNFLISAWLSSPVSCGRGTNDPWCKNPFSYPVVGQGVMCNSHLCISEDGLTSPMVLSYSL
SQ  IDWALMIAVIATVAIFIAKVSLLVDVICVFLCLLMYVFPPLSVIAFAFPFALCKVHLHPVTLVWVQFFLLAVNFWAGVAV
SQ  AVILISSWFLARATSSTGLVTPYDVHLVTSTPRGASSLASAPEGTYLAAVRRSALTGRCCMFVPTNFGSVLEGSLRTRGC
SQ  AKNVVSVFGSASGSGGVFTIHGNPVVVTATHLLSDGKARVSCVGFSQCLTFKSVGDYAFARVAEWKGDAPKVELSDRRGR
SQ  AYCSPQVEWSLVLLGPNTAFCFTKCGDSGSPVVDEDGNLIGVHTGSNKRGSGMITTHNGKTLGMSNVKLSEMCQHYGGSG
SQ  VPVSTVRLPKHLIVDVEAVASDLVAVVESLPTPEGALSSVQLLCVFFFLWRLIHVPFVPVIAVAFFFLNEILPVVLARLM
SQ  FSFALSLFSVFTGFSVQVLLLRLVIAALNRSAVSFGSFLLGQLFHCCLMPSHLETLGPVPGYFYPSTTEVASKEIFVTLL
SQ  AIHVLALLLSLFKRPMLADVLVGNGSFDAAFFLKYFAEGNLRDGVSDSCNMTPEGLTAALAITLSDDDLEFLQRHSEFKC
SQ  FVSASNMRNGAKEFIESAYARALRAQLAATDKIKASKSILAKLESFAGGVVTKVEPGDVVVVLGKKIVGDLVEITINDVK
SQ  HVIRVIETRVMAGTQFSVGTICGDLENACEDPSGLVKTSKKQRRRQKRTGLGTEVVGTVEIDGVSYNKVWHKATGDVTYE
SQ  GFLVSENSRLRTLGTSAIGRFQEFIRKHGSKVKTSVEKYPVGKNKHIEFAVTTYNLDGEEFDVPDHEPLEWTITIGDSDL
SQ  EAERLTVDQALRHMGHDSLLTPKEKEKLARIIESLNGLQQSSALNCLTTSGLERCSRGGVTVSKDAVKIVKYHSRTFSIG
SQ  DVNLKVMSFDEYRRTMGKPGHLLVAKLTDGVVVMRKHEPSLVDVILTGEDAEFFPRTHGPGNTGIHRFVWDFESPPVDLE
SQ  LELSEQIITACSMRRGDAPALDLPYKLHPVRGDPYRHRGVLFNTRFGDITYLIPEKTKEPLHAAACYNKGVPVSDSETLV
SQ  ATTLPHGFELYVPTLPPSVLEYLDSRPDTPRMLTKHGCASAAEKDLQKFDLSRQGFVLPGVLYMVRRYLSRLIGVRRRLF
SQ  MPSTYPAKNSMAGINGGRFPLTWLQSHPDIDALCKRACEEHWQTVTPCTLKKQYCSKSKTRTILGTNNFVALGLRSALSG
SQ  VTQGFMRKGIGTPICLGKNKFTPLPVRIGGRCLEADLASCDRSTPAIIRWFTTNLLFELAGAEEWIPSYVLNCCHDVVST
SQ  MSGCFDKRGGLSSGDPVTSISNTVYSLIIYAQHMVLSAFRCGHKIGGLFLQDSLEMEQLFELQPLLVYSDDVVFYNESDE
SQ  LPNYHFFVDHLDLMLGFKTDRSKTVITSEPKLPGCRISGGRVLVPQRDRIVAALAYQMKASCVGEYFASAAAILMDACAC
SQ  CDHDESWYFDLVCGIAECAGSPWFRFPGPSFFLDMWNRLSAEEKKKCRTCAHCGAPATLVSSCGLNLCDYHGHGHPHCPV
SQ  VLPCGHAVGSGVCEQCSSSAMNLNTELDILLMCVPYHPPKVELLSVNDKVSSLPPGAYQARGGVVSVRRDILGNVVDLPD
SQ  GDYQVMKVAQTCADISMVSVNSNILRSQFVTGAPGTGKTTYLLSVVRDDDVIYTPTHRTMLDVVKALKVCRFDPPKDTPL
SQ  EFPVPGRTGPTVRLIGAGFVPGRVSYLDEAAYCNPLDVLKVLSKTPLVCVGDLNQLPPVGFNGPCFAFSLMPGRQLIEVF
SQ  RFGPAVVNSIKKFYKEELVPRGPDTGVKFLKQYQPYGQVLTPYHRDRVDGAITIDSSQGCTYDVVTVYLPTPKSLNSARA
SQ  LVALTRARHYVFIYDPYDQLQQYLQVFEHEPADAWAFWCGDQPKMIVGGVVKQLAGHSRTTDLKLQQLMGLEGTASPLPQ
SQ  VGHNLGFYYSPDLIQFAKIPPELCKHWPVVTAQNRTEWPDRLVCGMNKMDKNSRAVFCAGYYVGPSIFLGVPGVVSYYLT
SQ  KYLKGESVPLPDSIMSTGRIRLNVREYLDENEIEFAKKCPQPFIGEVKGSNVGGCHHVTSRFLPPVLVPGSVVKVGVSCP
SQ  GKAAKGLCTVTDVYLPELDSYLHPPSKSMDYKLLVDFQPVKLMVWKDATAYFHEGIRPMEAMSRFLKVPEGEGVFFDLDE
SQ  FVTNAKVSKLPCKYSVSAHQFLTEVVLSMTPTSEAPPDYELLFARAYCVPGLDVGTLNAYIYKRGPSTYTTSNFARLVKD
SQ  TAVPVGCKGSGYMFPK
//
ID  Q9YN02;
PN  Non-structural protein 12;
GN  rep;
OS  300561;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp1]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. [Nsp1-beta papain-like cysteine proteinase]: Host cytoplasm {ECO:0000250}. [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}.
DR  UNIPROT: Q9YN02;
DR  UNIPROT: Q9YN01;
DR  PDB: 5EYI;
DR  PDB: 5YLX;
DR  Pfam: PF16749;
DR  Pfam: PF19215;
DR  Pfam: PF14757;
DR  Pfam: PF14756;
DR  Pfam: PF05410;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51961;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. Nsp1 is essential for viral subgenomic mRNA synthesis. {ECO:0000250}. Nsp1-alpha inhibits IFN-beta production. Counteracts the action of NF-kappaB by decreasing the phosphorylation of IkappaB-alpha, such that the degradation of IkappaB-alpha is suppressed. This leads to the blockage of NF-kappaB nuclear translocation and thus interference of NF-kappaB activation. Also seems to inhibit IRF3-dependent pathways (By similarity). {ECO:0000250}. Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity. Deubiquitinates host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation (By similarity). {ECO:0000250}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000250}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250}. [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P19811}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039579;
GO  GO:0039563;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGILDRCTCTPNARVFVAEGQVYCTRCLSARSLLPLNLQVSELGVLGLFYRPEEPLRWTLPRAFPTVECSPAGACWLSA
SQ  IFPIARMTSGNLNFQQRMVRVAAEIYRAGQLTPAVLKALQVYERGCRWYPIVGPVPGVAVFANSLHVSDKPFPGATHVLT
SQ  NLPLPQRPKPEDFCPFECAMATVYDIGHDAVMYVAEGKISWAPRGGDEVKFEAVPGELKLIANRLRTSFPPHHAVDMSKF
SQ  AFTAPGCGVSMRVERQHGCLPADTVPEGNCWWSLFDLLPLEVQDKEIRHANQFGYQTKHGVSGKYLQRRLQVNGLRAVTD
SQ  SNGPIVVQYFSVKESWIRHLKLAGEPSYSGFEDLLRIRVEPNTSPLANTEGKIFRFGSHKWYGAGKRARKARSCATATVA
SQ  GRALSVRETRQAKEHEVAGADKAEHLKHYSPPAEGNCGWHCISAIANRMVNSIFETTLPERVRPPDDWATDDDLANAIQI
SQ  LRLPAALDRNGACTSAKYVLKLEGEHWTVTVTPGMSPSLLPLECVQGCCEHKGGLGSPDAIEVSGFDPACLDWLAEVMHL
SQ  PSSAIPAALAEMSGDSDRSASPVTTVWTVSQFFARHSGGNHPDQVRLGKIISLCQVIEDCCCSQNKTNRVTPEEVAAKID
SQ  LYLRGATNLEECLARLEKARPPRVIDTSFDWDVVLPGVEAATQTNKLPQVNQCRALVPVVTQKSLDNNSVPLTAFSLANY
SQ  YYRAQGDEVRHRERLTAVLSKLEEVVREEYGLMPTEPGPRPTLPRGLDELKDQMEEDLLRLANAQATSDMMAWAVEQVDL
SQ  KTWVKNYPRWTPPPPPPKVQPRKTKPVKSLPERKPVPAPRRKVGPDCGSPVSLGGDVPNSWEDLAVSSPLDLPTPPEPAT
SQ  LSSELVIVSSPQCIFRPATPLSEPAPIPAPRGTVSRPVTPLSEPIPVPAPRRKFQQVKRLSSAAAVPLHQNEPLDLSASS
SQ  QTEYEASPSAPPQSGGVLGVEGHEAEETLSEISDMSGNIKPASVSSSSSLSSVEITRPKYSAQAIIDSGGPCSGHLQGVK
SQ  ETCLSVMREACDATKLDDPATQEWLSRMWDRVDMLTWRNTSVCQAIRTLDGRLKFLPKMILETPPPYPCEFVMMPHTPAP
SQ  SVGAESDLTIGSVATEDVPRILEKIENVGEMANQEPSAFSEDKPVDDQLVNDPRISSRRPDESTAAPSAGTGGAGSFTDL
SQ  PSSDGADADGGGPFRTAKRKAERLFDQLSRQVFDLVSHLPVFFSRLFHPGGGYSTGDWGFAAFTLLCLFLCYSYPAFGIA
SQ  PLLGVFSGTSRRVRMGVFGCWLAFAVGLFKPVSDPVGAACEFDSPECRNILLSFELLKPWDPVRSLVVGPVGLGLAILGR
SQ  LLGGARCIWHFLLRLGIVADCILAGAYVLSQGRCKKCWGSCIRTAPNEVAFNVFPFTRATRSSLIDLCDRFCAPKGMDPI
SQ  FLATGWRGCWAGRSPIEQPSEKPIAFAQLDEKKITARTVVAQPYDPNQAVKCLRVLQAGGAMVAEAVPKVVKVSAVPFRA
SQ  PFFPTGVKVDPDCRVVVDPDTFTAALRSGYSTTNLVLGVGDFAQLNGLKIRQISKPSGGGPHLMAALHVACSMALHMLTG
SQ  IYVTAVGSCGTGTNDPWCANPFAVPGYGPGSLCTSRLCISQHGLTLPLTALVAGFGIQEIALVVLIFVSIGGMAHRLSCK
SQ  ADMLCILLAIASYVWVPLTWLLCVFPCWLRCFSLHPLTILWLVFFLISVNMPSGILAMVLLVSLWLLGRYTNVAGLVTPY
SQ  DIHHYTSGPRGVAALATAPDGTYLAAVRRAALTGRTMLFTPSQLGSLLEGAFRTRKPSLNTVNVIGSSMGSGGVFTIDGK
SQ  VKCVTAAHVLTGNSARVSGVGFNQMLDFDVKGDFAIADCPNWQGAAPKAQFCADGWTGRAYWLTSSGVEPGVIGKGFAFC
SQ  FTACGDSGSPVITEAGELVGVHTGSNKQGGGIVTRPSGQFCNVAPIKLSELSEFFAGPKVPLGDVKVGSHIIKDISEVPS
SQ  DLCALLAAKPELEGGLSTVQLLCVFFLLWRMMGHAWTPLVAVSFFILNEVLPAVLVRSVFSFGMFVLSWLTPWSAQILMI
SQ  RLLTAALNRNRWSLAFFSLGAVTGFVADLAATQGHPLQAVMNLSTYAFLPRMMVVTSPVPVITCGVVHLLAIILYLFKYR
SQ  GLHQILVGDGVFSAAFFLRYFAEGKLREGVSQSCGMNHESLTGALAMRLNDEDLDFLMKWTDFKCFVSASNMRNAAGQFI
SQ  EAAYAKALRVELAQLVQVDKVRGVLAKLEAFADTVAPQLSPGDIVVALGHTPVGSIFDLKVGSTKHTLQAIETRVLAGSK
SQ  MTVARVVDPTPTPPPAPVPIPLPPKVLENGPNAWGDEDRLNKKKRRRMEALGIYVMGGKKYQKFWDKNSGDVFYEEVHNN
SQ  TDEWECLRVGDPADFDPEKGTLCGHVTIENKAYHVYISPSGKKFLVPVNPENGRVQWEAAKLSMEQALGMMNVDGELTAK
SQ  ELEKLKRIIDKLQGLTKEQCLNCLLAASGLTRCGRGGLVVTETAVKIVKFHNRTFTLGPVNLKVASEVELKDAVEHNQHP
SQ  VARPIDGGVVLLRSAVPSLIDVLISGADASPKLLAHHGPGNTGIDGTLWDFESEATKEEVALSAQIIQACDIRRGDAPKI
SQ  GLPYKLYPVRGNPERVKGVLQNTRFGDIPYKTPSDTGSPVHAAACLTPNATPVTDGRSVLATTMPPGFELYVPTIPASVL
SQ  DYLDSRPDCPKQLTEHGCEDAALKDLSKYDLSTQGFVLPGVLRLVRKYLFAHVGKCPPVHRPSTYPAKNSMAGINGNRFP
SQ  TKDIQSVPEIDVLCAQAVRENWQTVTPCTLKKQYCGKKKTRTILGTNNFIALAHRAALSGVTQGFMKKAFNSPIALGKNK
SQ  FKELQTSVLGRCLEADLASCDRSTPAIVRWFAANLLYELACAEEHLPSYVLNCCHDLLVTQSGAVTKRGGLSSGDPITSV
SQ  SNTIYSLVIYAQHMVLSYFKSGHPHGLLFLQDQLKFEDMLKVQPLIVYSDDLVLYAESPTMPNYHWWVEHLNLMLGFQTD
SQ  PKKTAITDSPSFLGCRIINGRQLVPNRDRILAALAYHMKASNVSEYYASAAAILMDSCACLEYDPEWFEELVVGIAQCAR
SQ  KDGYSFPGTPFFMSMWEKLRSNYEGKKSRVCGYCGAPAPYATACGLDVCIYHTHFHQHCPVTIWCGHPAGSGSCSECKSP
SQ  VGKGTSPLDEVLEQVPYKPPRTVIMHVEQGLTPLDPGRYQTRRGLVSVRRGIRGNEVELPDGDYASTALLPTCKEINMVA
SQ  VASNVLRSRFIIGPPGAGKTYWLLQQVQDGDVIYTPTHQTMLDMIRALGTCRFNVPAGTTLQFPVPSRTGPWVRILAGGW
SQ  CPGKNSFLDEAAYCNHLDVLRLLSKTTLTCLGDFKQLHPVGFDSHCYVFDIMPQTQLKTIWRFGQNICDAIQPDYRDKLM
SQ  SMVNTTRVTYVEKPVRYGQVLTPYHRDREDDAITIDSSQGATFDVVTLHLPTKDSLNRQRALVAITRARHAIFVYDPHRQ
SQ  LQGLFDLPAKGTPVNLAVHRDGQLIVLDRNNKECTVAQALGNGDKFRATDKRVVDSLRAICADLEGSSSPLPKVAHNLGF
SQ  YFSPDLTQFAKLPVELAPHWPVVTTQNNEKWPDRLVASLRPIHKYSRACIGAGYMVGPSVFLGTPGVVSYYLTKFVKGEA
SQ  QLLPETVFSTGRIEVDCREYLDDREREVAASLPHAFIGDVKGTTVGGCHHVTSRYLPRVLPKESVAVVGVSSPGKAAKAL
SQ  CTLTDVYLPDLEAYLHPETQSKCWKMMLDFKEVRLMVWRDKTAYFQLEGRYFTWYQLASYASYIRVPVNSTVYLDPCMGP
SQ  ALCNRRVVGSTHWGADLAVTPYDYGAKIILSSAYHGEMPPGYKILACAEFSLDDPVRYKHTWGFESDTAYLYEFTGNGED
SQ  WEDYNDAFRARQEGKIYKATATSLKFHFPPGPVIEPTLGLN
//
ID  Q8B912;
PN  Non-structural protein 12;
GN  rep;
OS  300563;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp1]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. [Nsp1-beta papain-like cysteine proteinase]: Host cytoplasm {ECO:0000250}. [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}.
DR  UNIPROT: Q8B912;
DR  UNIPROT: Q8B911;
DR  Pfam: PF16749;
DR  Pfam: PF19215;
DR  Pfam: PF14757;
DR  Pfam: PF14756;
DR  Pfam: PF05410;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51961;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. Nsp1 is essential for viral subgenomic mRNA synthesis. {ECO:0000250}. Nsp1-alpha inhibits IFN-beta production. Counteracts the action of NF-kappaB by decreasing the phosphorylation of IkappaB-alpha, such that the degradation of IkappaB-alpha is suppressed. This leads to the blockage of NF-kappaB nuclear translocation and thus interference of NF-kappaB activation. Also seems to inhibit IRF3-dependent pathways (By similarity). {ECO:0000250}. Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity. Deubiquitinates host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation (By similarity). {ECO:0000250}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000250}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250}. [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P19811}.
DE  Reference Proteome: No;
GO  GO:0033644;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039579;
GO  GO:0039563;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGILDRCTCTPNARVFVAEGQVYCTRCLSARSLLPLNLQVPELGVLGLFYRPEEPLRWTLPRAFPTVECSPTGACWLSA
SQ  IFPIARMTSGNLNFQQRMVRVAGEIYRAGQLTPTVLKTIQVYERGCRWYPIVGPVPGVGVYANSLHVSDKPFPGATHVLT
SQ  NLPLPQRPKPEDFCPFECAMADVYDIGRGAVMYVAGGKVSWAPRGGDEVKFEPVPKELKLVANRLHTSFPPHHVVDMSKF
SQ  TFMTPGSGVSMRVEYQYGCLPADTVPEGNCWWRLFDLLPPEVQNKEIRHANQFGYQTKHGVPGKYLQRRLQVNGLRAVTD
SQ  THGPIVIQYFSVKESWIRHLKPVEEPSLPGFEDLLRIRVEPNTSPLAGKNEKIFRFGSHKWYGAGKRARKARSGATTMVA
SQ  HRASSAHETRQATKHEGAGANKAEHLKLYSPPAEGNCGWHCISAIVNRMVNSNFETTLPERVRPPDDWATDEDLVNTIQI
SQ  LRLPAALDRNGACGGAKYVLKLEGEHWTVSVNPGMSPSLLPLECVQGCCEHKGGLGSPDAVEVSGFDPACLDRLLQVMHL
SQ  PSSTIPAALAELSDDSNRPVSPAAATWTVSQSYARHRGGNHHDQVCLGKIISLCQVIEDCCCHQNKTNRATPEEVAAKID
SQ  QYLRGATSLEECLAKLERVSPPGAADTSFDWNVVLPGVEAAHQTTEQLHVNPCRTLVPPVTQEPLGKDSVPLTAFSLSNC
SQ  YYPAQGNEVRHRERLNSVLSKLEEVVLEEYGLMSTGLGPRPVLPSGLDELKDQMEEDLLKLANTQATSEMMAWAAEQVDL
SQ  KAWVKSYPRWTPPPPPPRVQPRKTKSVKSLPEDKPVPAPRRKVRSGCGSPVLMGDNVPNGSEDLTVGGPLNFPTPSEPMT
SQ  PMSEPVLTPALQRVPKLMTPLDGSAPVPAPRRTVSRPMTPLSEPIFLSAPRHKFQQVEEANPATTTLTHQNEPLDLSASS
SQ  QTEYEASPLASSQNMSILEAGGQEAEEVLSEISDILNDTSPAPVSSSSSLSSVKITRPKYSAQAIIDSGGPCSGHLQKEK
SQ  EACLSIMREACDASKLSDPATQEWLSRMWDRVDMLTWRNTSAYQAFRTLNGRFEFLPKMILETPPPHPCGFVMLPHTPAP
SQ  SVSAESDLTIGSVATEDVPRILGKIGDTGELLNQGPSAPFKGGPVCDQPAKNSRMSPRESDESIIAPPADTGGAGSFTDL
SQ  PSSDSVDANGGGPLRTVKTKAGRLLDQLSCQVFSLVSHLPVFFSHLFKSDSGYSPGDWGFAAFTLFCLFLCYSYPFFGFA
SQ  PLLGVFSGSSRRVRMGVFGCWLAFAVGLFKPVSDPVGTACEFDSPECRNVLHSFELLKPWDPVRSLVVGPVGLGLAILGR
SQ  LLGGARYVWHFLLRFGIVADCILAGAYVLSQGRCKKCWGSCVRTAPNEIAFNVFPFTRATRSSLIDLCDRFCAPKGMDPI
SQ  FLATVWRGCWTGRSPIEQPSEKPIAFAQLDEKRITARTVVAQPYDPNQAVKCLRVLQAGGAMVAEAVPKVVKVSAIPFRA
SQ  PFFPAGVKVDPECRIVVDPDTFTTALRSGYSTTNLVLGMGDFAQLNGLKIRQISKPSGGGSHLVAALHVACSMALHMLAG
SQ  VYVTAVGSCGTGTNDPWCTNPFAAPGYGPGSLCTSRLCISQHGLTLPLTALVAGFGLQEIALVVLIFVSMGGMAHRLSCK
SQ  ADMLCILLAIASYVWVPLTWLLCVFPCWLRWFSLHPLTILWLVFFLISVNIPSGILAVVLLVSLWLLGRYTNIAGLVTPY
SQ  DIHHYTSGPRGVAALATAPDGTYLAAVRRAALTGRTMLFTPSQLGSLLEGAFRTQKPSLNTVNVVGSSMGSGGVFTIDGK
SQ  IKCVTAAHVLTGNSARVSGVGFNQMLDFDVKGDFAIADCPNWQGAAPKAQFCEDGWTGRAYWLTSSGVEPGVIGNGFAFC
SQ  FTACGDSGSPVITEAGELVGVHTGSNKQGGGIVTRPSGQFCNVTPIKLSELSEFFAGPKVPLGDVKIGSHIIKDTCEVPS
SQ  DLCALLAAKPELEGGLSTVQLLCVFFLLWRMMGHAWTPLVAVGFFILNEILPAVLVRSVFSFGMFVLSWLTPWSAQVLMI
SQ  RLLTAALNRNRLSLGFYSLGAVTSFVADLAVTQGHPLQVVMNLSTYAFLPRMMVVTSPVPVIACGVVHLLAIILYLFKYR
SQ  CLHYVLVGDGVFSSAFFLRYFAEGKLREGVSQSCGMSHESLTGALAMRLTDEDLDFLTKWTDFKCFVSASNMRNAAGQFI
SQ  EAAYAKALRIELAQLVQVDKVRGTLAKLEAFADTVAPQLSPGDIVVALGHTPVGSIFDLKVGSTKHTLQAIETRVLAGSK
SQ  MTVARVVDPTPAPPPVPVPIPLPPKVLENGPNAWGDEDRLNKKKRRRMEAVGIFVMDGKKYQKFWDKNSGDVFYEEVHNS
SQ  TDEWECLRAGDPADFDPETGVQCGHITIEDRVYNVFTSPSGRKFLVPANPENRRAQWEAAKLSVEQALGMMNVDGELTAK
SQ  ELEKLKGIIDKLQGLTKEQCLNCLLAASGLTRCGRGGLVVTETAVKIVKFHNRTFTLGPVNLKVASEVELKDAVEHNQHP
SQ  VARPVDGGVVLLRSAVPSLIDVLISGADASPKLLARHGPGNTGIDGTLWDFEAEATKEEVALSAQIIQACDIRRGDAPEI
SQ  GLPYKLYPVRGNPERVKGVLQNTRFGDIPYKTPSDTGSPVHAAACLTPNATPVTDGRSVLATTMPSGFELYVPTIPASVL
SQ  DYLDSRPDCPKQLTEHGCEDAALRDLSKYDLVTQGFVLPGVLRLVRKYLFAHVGKCPPVHRPSTYPAKNSMAGINGNRFP
SQ  TKDIQSVPEIDVLCAQAVRENWQTVTPCTLKKQYCGKKKTRTILGTNNFIALAHRAALSGVTQGFMKKAFNSPIALGKNK
SQ  FKELQTPVLGRCLEADLASCDRSTPAIVRWFAANLLYELACAEEHLPSYVLNCCHDLLVTQSGAVTKRGGLSSGDPITSV
SQ  SNTIYSLVIYAQHMVLSYFKSGHPHGLLFLQDQLKFEDMLKVQPLIVYSDDLVLYAESPSMPNYHWWVEHLNLMLGFQTD
SQ  PKKTAITDSPTFLGCRIINGRQLVPNRDRILAALAYHMKASNVSEYYASAAAILMDSCACLEYDPEWFEELVVGIAQCAR
SQ  KDGYSFPGPPFFLSMWEKLRSNHEGKKSRMCGYCMAPAPYATACGLDVCVYHTHFHQHCPVIIWCGHPAGSGSCGECEPP
SQ  LGKGTSPLDEVLEQVPYKPPRTVIMHVEQGLTPLDPGRYQTRRGLVSVRRGIRGNEVDLPDGDYASTALLPTCKEINMVA
SQ  VAPNVLRSRFIIGPPGAGKTHWLLQQVQDGDVIYTPTHQTMLDMIRALGTCRFNVPAGTTLQFPAPSRTGPWVRILAGGW
SQ  CPGKNSFLDEAAYCNHLDVLRLLSKTTLTCLGDFKQLHPVGFDSHCYVFDIMPQTQLKTIWRFGQNICDAIQPDYRDKLV
SQ  SMVNTTRVTYVEKPVRYGQVLTPYHRDREDGAITIDSSQGATFDVVTLHLPTKDSLNRQRALVAITRARHAIFVYDPHRQ
SQ  LQSMFDLPAKGTPVNLAVHRDEQLIVLDRNNKEITVAQALGNGDKFRATDKRVVDSLRAICADLEGSSSPLPKVAHNLGF
SQ  YFSPDLTQFAKLPAELAPHWPVVTTQNNERWPDRLVASLRPIHKYSRACIGAGYMVGPSVFLGTPGVVSYYLTKFVRGEA
SQ  QVLPETVFSTGRIEVDCREYLDDREREVAESLPHAFIGDVKGTTVGGCHHVTSKYLPRFLPKESVAVVGVSSPGEAAKAF
SQ  CTLTDVYLPDLEAYLHPETQSKCWKVMLDFKEVRLMVWKGKTAYFQLEGRHFTWYQLASYTSYIRVPVNSTVYLDPCMGP
SQ  ALCNRRVVGSTHWGADLAVTPYDYGAKIILSSAYHGEMPPGYKILACAEFSLDDPVRYKHTWGFESDTAYLYEFTGNGED
SQ  WEDYNGAFRARQKGKIYKATATSMKFHFPPGPVIEPTLGLN
//
ID  Q04561;
PN  Non-structural protein 12;
GN  rep;
OS  11049;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp1]: Host nucleus {ECO:0000269|PubMed:23287061}. Host cytoplasm {ECO:0000269|PubMed:23287061}. [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:28235682}. Host cytoplasm {ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:28235682}. [Nsp1-beta papain-like cysteine proteinase]: Host nucleus {ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:28235682}. [Nsp2 cysteine proteinase]: Host cytoplasm {ECO:0000269|PubMed:28648849}. Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host endoplasmic reticulum {ECO:0000269|PubMed:21799305}. Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Serine protease nsp4]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000269|PubMed:25449571}. Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase nsp10]: Host cytoplasm {ECO:0000269|PubMed:28648849}. Host cytoplasm, host perinuclear region {ECO:0000305}. [Uridylate-specific endoribonuclease nsp11]: Host cytoplasm {ECO:0000269|PubMed:29444948}. Host nucleus {ECO:0000269|PubMed:29444948}. [Non-structural protein 12]: Host cytoplasm {ECO:0000269|PubMed:29920289}.
DR  UNIPROT: Q04561;
DR  Pfam: PF16749;
DR  Pfam: PF14757;
DR  Pfam: PF14758;
DR  Pfam: PF05410;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51961;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: [Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. [Nsp1-alpha papain-like cysteine proteinase]: Inhibits host IFN-beta production. Plays a role in the degradation of the host transcriptional activator CREBBP protein. The degradation of host CREBBP which is a key component of the IFN enhanceosome is likely responsible for the inhibition of interferon mediated by Nsp1-alpha. Participates also in the inhibition of host NF-kappa-B activation by counteracting LUBAC-dependent induction of NF-kappa-B. Reduces host NEMO ubiquitination by blocking the interaction between the two LUBAC complex components RNF31 and SHARPIN. {ECO:0000250|UniProtKB:Q9WJB2, ECO:0000269|PubMed:23287061, ECO:0000269|PubMed:27881655}. [Nsp1-beta papain-like cysteine proteinase]: Plays a role in blocking host mRNA nuclear export to the cytoplasm and subversion of host protein synthesis (PubMed:28235682). Additionally, inhibits the interferon-activated JAK/STAT signal transduction by mediating the ubiquitination and subsequent proteasomal degradation of host KPNA1. {ECO:0000250|UniProtKB:Q9WJB2, ECO:0000269|PubMed:28235682}. [Nsp2 cysteine proteinase]: Multifunctional protein that acts as a viral protease and as a viral antagonist of host immune response. Cleaves the nsp2/nsp3 site in the viral polyprotein. Displays deubiquitinating activity that cleaves both ubiquitinated and ISGylated products and therefore inhibits ubiquitin and ISG15-dependent host innate immunity. Deubiquitinates also host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation. {ECO:0000250|UniProtKB:A0MD28}. [Non-structural protein 3]: Plays a role in the inhibition of the immune response by interacting with host IFITM1. This interaction leads to the proteasomal degradation of the IFN-induced antiviral protein IFITM1. {ECO:0000269|PubMed:25102331}. [Serine protease nsp4]: Cleaves the majority of cleavage sites present in the C-terminus of the polyprotein. Triggers host apoptosis through caspase-3, -8, and -9 activations. Subverts host innate immune responses through its protease activity. Targets the NF- kappa-B essential modulator NEMO and mediates its cleavage (PubMed:25008936). Blocks host interferon beta induction and downstream signaling by cleaving mitochondrial MAVS, dislodging it from the mitochondria (PubMed:27329948). Impairs host defense by cleaving host mRNA-decapping enzyme DCP1A to attenuate its antiviral activity (PubMed:30158128). {ECO:0000269|PubMed:19646449, ECO:0000269|PubMed:23936003, ECO:0000269|PubMed:25008936, ECO:0000269|PubMed:27329948, ECO:0000269|PubMed:30158128}. [Non-structural protein 5-6-7]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. {ECO:0000269|PubMed:21799305}. [Non-structural protein 5]: Plays a role in the inhibition of host STAT3 signaling pathway by inducing the degradation of STAT3. {ECO:0000269|PubMed:27881658}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000269|PubMed:25449571}. [Helicase nsp10]: Displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000269|PubMed:12127789}. [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, PKR (By similarity) and NLRP3 inflammasome (PubMed:26398903). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). Also plays a role in the inhibition of host type I interferon production by recruiting host OTULIN to promote removal of linear ubiquitination targeting host NEMO (PubMed:29444948). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P19811, ECO:0000269|PubMed:26398903, ECO:0000269|PubMed:29444948}.
DE  Reference Proteome: Yes;
DE  Interaction: A5D9M6; IntAct: EBI-11702011; Score: 0.40
DE  Interaction: A0A068CA64; IntAct: EBI-11702092; Score: 0.40
GO  GO:0030430;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0004521;
GO  GO:0016829;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039520;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039579;
GO  GO:0039514;
GO  GO:0039563;
GO  GO:0039522;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0039545;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGTFSRCMCTPAARVFWNAGQVFCTRCLSARSLLSPELQDTDLGAVGLFYKPRDKLHWKVPIGIPQVECTPSGCCWLSA
SQ  VFPLARMTSGNHNFLQRLVKVADVLYRDGCLAPRHLRELQVYERGCNWYPITGPVPGMGLFANSMHVSDQPFPGATHVLT
SQ  NSPLPQQACRQPFCPFEEAHSSVYRWKKFVVFTDSSLNGRSRMMWTPESDDSAALEVLPPELERQVEILIRSFPAHHPVD
SQ  LADWELTESPENGFSFNTSHSCGHLVQNPDVFDGKCWLSCFLGQSVEVRCHEEHLADAFGYQTKWGVHGKYLQRRLQVRG
SQ  IRAVVDPDGPIHVEALSCPQSWIRHLTLDDDVTPGFVRLTSLRIVPNTEPTTSRIFRFGAHKWYGAAGKRARAKRAAKSE
SQ  KDSAPTPKVALPVPTCGITTYSPPTDGSCGWHVLAAIMNRMINGDFTSPLTQYNRPEDDWASDYDLVQAIQCLRLPATVV
SQ  RNRACPNAKYLIKLNGVHWEVEVRSGMAPRSLSRECVVGVCSEGCVAPPYPADGLPKRALEALASAYRLPSDCVSSGIAD
SQ  FLANPPPQEFWTLDKMLTSPSPERSGFSSLYKLLLEVVPQKCGATEGAFIYAVERMLKDCPSSKQAMALLAKIKVPSSKA
SQ  PSVSLDECFPTDVLADFEPASQERPQSSGAAVVLCSPDAKEFEEAAPEEVQESGHKAVHSALLAEGPNNEQVQVVAGEQL
SQ  KLGGCGLAVGNAHEGALVSAGLINLVGGNLSPSDPMKENMLNSREDEPLDLSQPAPASTTTLVREQTPDNPGSDAGALPV
SQ  TVREFVPTGPILCHVEHCGTESGDSSSPLDLSDAQTLDQPLNLSLAAWPVRATASDPGWVHGRREPVFVKPRNAFSDGDS
SQ  ALQFGELSESSSVIEFDRTKDAPVVDAPVDLTTSNEALSVVDPFEFAELKRPRFSAQALIDRGGPLADVHAKIKNRVYEQ
SQ  CLQACEPGSRATPATREWLDKMWDRVDMKTWRCTSQFQAGRILASLKFLPDMIQDTPPPVPRKNRASDNAGLKQLVAQWD
SQ  RKLSVTPPPKPVGPVLDQIVPPPTDIQQEDVTPSDGPPHAPDFPSRVSTGGSWKGLMLSGTRLAGSISQRLMTWVFEVFS
SQ  HLPAFMLTLFSPRGSMAPGDWLFAGVVLLALLLCRSYPILGCLPLLGVFSGSLRRVRLGVFGSWMAFAVFLFSTPSNPVG
SQ  SSCDHDSPECHAELLALEQRQLWEPVRGLVVGPSGLLCVILGKLLGGSRYLWHVLLRLCMLADLALSLVYVVSQGRCHKC
SQ  WGKCIRTAPAEVALNVFPFSRATRVSLVSLCDRFQTPKGVDPVHLATGWRGCWRGESPIHQPHQKPIAYANLDEKKMSAQ
SQ  TVVAVPYDPSQAIKCLKVLQAGGAIVDQPTPEVVRVSEIPFSAPFFPKVPVNPDCRVVVDSDTFVAAVRCGYSTAQLVLG
SQ  RGNFAKLNQTPPRNSISTKTTGGASYTLAVAQVSAWTLVHFILGLWFTSPQVCGRGTADPWCSNPFSYPTYGPGVVCSSR
SQ  LCVSADGVTLPLFSAVAQLSGREVGIFILVLVSLTALAHRMALKADMLVVFSAFCAYAWPMSSWLICFFPILLKWVTLHP
SQ  LTMLWVHSFLVFCLPAAGILSLGITGLLWAIGRFTQVAGIITPYDIHQYTSGPRGAAAVATAPEGTYMAAVRRAALTGRT
SQ  LIFTPSAVGSLLEGAFRTHKPCLNTVNVVGSSLGSGGVFTIDGRRTVVTAAHVLNGDTARVTGDSYNRMHTFKTNGDYAW
SQ  SHADDWQGVAPVVKVAKGYRGRAYWQTSTGVEPGIIGEGFAFCFTNCGDSGSPVISESGDLIGIHTGSNKLGSGLVTTPE
SQ  GETCTIKETKLSDLSRHFAGPSVPLGDIKLSPAIIPDVTSIPSDLASLLASVPVVEGGLSTVQLLCVFFLLWRMMGHAWT
SQ  PIVAVGFFLLNEILPAVLVRAVFSFALFVLAWATPWSAQVLMIRLLTASLNRNKLSLAFYALGGVVGLAAEIGTFAGRLS
SQ  ELSQALSTYCFLPRVLAMTSCVPTIIIGGLHTLGVILWLFKYRCLHNMLVGDGSFSSAFFLRYFAEGNLRKGVSQSCGMN
SQ  NESLTAALACKLSQADLDFLSSLTNFKCFVSASNMKNAAGQYIEAAYAKALRQELASLVQIDKMKGVLSKLEAFAETATP
SQ  SLDIGDVIVLLGQHPHGSILDINVGTERKTVSVQETRSLGGSKFSVCTVVSNTPVDALTGIPLQTPTPLFENGPRHRSEE
SQ  DDLKVERMKKHCVSLGFHNINGKVYCKIWDKSTGDTFYTDDSRYTQDHAFQDRSADYRDRDYEGVQTTPQQGFDPKSETP
SQ  VGTVVIGGITYNRYLIKGKEVLVPKPDNCLEAAKLSLEQALAGMGQTCDLTAAEVEKLKRIISQLQGLTTEQALNCLLAA
SQ  SGLTRCGRGGLVVTETAVKIIKYHSRTFTLGPLDLKVTSEVEVKKSTEQGHAVVANLCSGVILMRPHPPSLVDVLLKPGL
SQ  DTIPGIQPGHGAGNMGVDGSIWDFETAPTKAELELSKQIIQACEVRRGDAPNLQLPYKLYPVRGDPERHKGRLINTRFGD
SQ  LPYKTPQDTKSAIHAACCLHPNGAPVSDGKSTLGTTLQHGFELYVPTVPYSVMEYLDSRPDTPFMCTKHGTSKAAAEDLQ
SQ  KYDLSTQGFVLPGVLRLVRRFIFGHIGKAPPLFLPSTYPAKNSMAGINGQRFPTKDVQSIPEIDEMCARAVKENWQTVTP
SQ  CTLKKQYCSKPKTRTILGTNNFIALAHRSALSGVTQAFMKKAWKSPIALGKNKFKELHCTVAGRCLEADLASCDRSTPAI
SQ  VRWFVANLLYELAGCEEYLPSYVLNCCHDLVATQDGAFTKRGGLSSGDPVTSVSNTVYSLVIYAQHMVLSALKMGHEIGL
SQ  KFLEEQLKFEDLLEIQPMLVYSDDLVLYAERPTFPNYHWWVEHLDLMLGFRTDPKKTVITDKPSFLGCRIEAGRQLVPNR
SQ  DRILAALAYHMKAQNASEYYASAAAILMDSCACIDHDPEWYEDLICGIARCARQDGYSFPGPAFFMSMWEKLRSHNEGKK
SQ  FRHCGICDAKADYASACGLDLCLFHSHFHQHCPVTLSCGHHAGSKECSQCQSPVGAGRSPLDAVLKQIPYKPPRTVIMKV
SQ  GNKTTALDPGRYQSRRGLVAVKRGIAGNEVDLSDGDYQVVPLLPTCKDINMVKVACNVLLSKFIVGPPGSGKTTWLLSQV
SQ  QDDDVIYTPTHQTMFDIVSALKVCRYSIPGASGLPFPPPARSGPWVRLIASGHVPGRVSYLDEAGYCNHLDILRLLSKTP
SQ  LVCLGDLQQLHPVGFDSYCYVFDQMPQKQLTTIYRFGPNICAAIQPCYREKLESKARNTRVVFTTRPVAFGQVLTPYHKD
SQ  RIGSAITIDSSQGATFDIVTLHLPSPKSLNKSRALVAITRARHGLFIYDPHNQLQEFFNLTPERTDCNLVFSRGDELVVL
SQ  NADNAVTTVAKALETGPSRFRVSDPRCKSLLAACSASLEGSCMPLPQVAHNLGFYFSPDSPTFAPLPKELAPHWPVVTHQ
SQ  NNRAWPDRLVASMRPIDARYSKPMVGAGYVVGPSTFLGTPGVVSYYLTLYIRGEPQALPETLVSTGRIATDCREYLDAAE
SQ  EEAAKELPHAFIGDVKGTTVGGCHHITSKYLPRSLPKDSVAVVGVSSPGRAAKAVCTLTDVYLPELRPYLQPETASKCWK
SQ  LKLDFRDVRLMVWKGATAYFQLEGLTWSALPDYARFIQLPKDAVVYIDPCIGPATANRKVVRTTDWRADLAVTPYDYGAQ
SQ  NILTTAWFEDLGPQWKILGLQPFRRAFGFENTEDWAILARRMNDGKDYTDYNWNCVRERPHAIYGRARDHTYHFAPGTEL
SQ  QVELGKPRLPPGQVP
//
ID  Q9WJB2;
PN  Non-structural protein 12;
GN  rep;
OS  300559;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp1]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000269|PubMed:20850164}. Host cytoplasm {ECO:0000269|PubMed:20850164}. [Nsp1-beta papain-like cysteine proteinase]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. [Nsp2 cysteine proteinase]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host membrane {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04561}. [Non-structural protein 3]: Host membrane {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04561}. [Non-structural protein 5-6-7]: Host endoplasmic reticulum {ECO:0000250|UniProtKB:Q04561}. Host membrane {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04561}. [Serine protease nsp4]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q04561}. [Helicase nsp10]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q04561}. [Uridylate-specific endoribonuclease nsp11]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host nucleus {ECO:0000250|UniProtKB:Q04561}. [Non-structural protein 12]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}.
DR  UNIPROT: Q9WJB2;
DR  UNIPROT: Q80KX0;
DR  UNIPROT: Q80KX1;
DR  UNIPROT: Q9WJB3;
DR  Pfam: PF16749;
DR  Pfam: PF19215;
DR  Pfam: PF14757;
DR  Pfam: PF14756;
DR  Pfam: PF05410;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51961;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: [Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:Q04561}. [Nsp1-alpha papain-like cysteine proteinase]: Inhibits host IFN-beta production. Plays a role in the degradation of the host transcriptional activator CREBBP protein. The degradation of host CREBBP which is a key component of the IFN enhanceosome is likely responsible for the inhibition of interferon mediated by Nsp1-alpha. Participates also in the inhibition of host NF-kappa-B activation by counteracting LUBAC-dependent induction of NF-kappa-B. Reduces host NEMO ubiquitination by blocking the interaction between the two LUBAC complex components RNF31 and SHARPIN. {ECO:0000250|UniProtKB:Q04561, ECO:0000269|PubMed:20006994, ECO:0000269|PubMed:20850164, ECO:0000269|PubMed:21438756}. [Nsp1-beta papain-like cysteine proteinase]: Plays a role in blocking host mRNA nuclear export to the cytoplasm and subversion of host protein synthesis. Additionally, inhibits the interferon-activated JAK/STAT signal transduction by mediating the ubiquitination and subsequent proteasomal degradation of host KPNA1. {ECO:0000250|UniProtKB:Q04561, ECO:0000269|PubMed:20006994, ECO:0000269|PubMed:23449802}. [Nsp2 cysteine proteinase]: Multifunctional protein that acts as a viral protease and as a viral antagonist of host immune response. Cleaves the nsp2/nsp3 site in the viral polyprotein. Displays deubiquitinating activity that cleaves both ubiquitinated and ISGylated products and therefore inhibits ubiquitin and ISG15-dependent host innate immunity. Deubiquitinates also host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation. {ECO:0000250|UniProtKB:A0MD28, ECO:0000269|PubMed:18078692}. [Non-structural protein 3]: Plays a role in the inhibition of the immune response by interacting with host IFITM1. This interaction leads to the proteasomal degradation of the IFN-induced antiviral protein IFITM1. {ECO:0000250|UniProtKB:Q04561}. [Serine protease nsp4]: Cleaves the majority of cleavage sites present in the C-terminus of the polyprotein. Triggers host apoptosis through caspase-3, -8, and -9 activations. Subverts host innate immune responses through its protease activity. Targets the NF- kappa-B essential modulator NEMO and mediates its cleavage. Blocks host interferon beta induction and downstream signaling by cleaving mitochondrial MAVS, dislodging it from the mitochondria. Impairs host defense by cleaving host mRNA-decapping enzyme DCP1A to attenuate its antiviral activity. {ECO:0000250|UniProtKB:Q04561}. [Non-structural protein 5-6-7]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. {ECO:0000250|UniProtKB:Q04561}. [Non-structural protein 5]: Plays a role in the inhibition of host STAT3 signaling pathway by inducing the degradation of STAT3. {ECO:0000250|UniProtKB:Q04561}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:Q04561}. [Helicase nsp10]: Displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250|UniProtKB:Q04561}. [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P19811}.
DE  Reference Proteome: No;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039579;
GO  GO:0039563;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGILDRCTCTPNARVFMAEGQVYCTRCLSARSLLPLNLQVSELGVLGLFYRPEEPLRWTLPRAFPTVECSPAGACWLSA
SQ  IFPIARMTSGNLNFQQRMVRVAAELYRAGQLTPAVLKALQVYERGCRWYPIVGPVPGVAVFANSLHVSDKPFPGATHVLT
SQ  NLPLPQRPKPEDFCPFECAMATVYDIGHDAVMYVAERKVSWAPRGGDEVKFEAVPGELKLIANRLRTSFPPHHTVDMSKF
SQ  AFTAPGCGVSMRVERQHGCLPADTVPEGNCWWSLFDLLPLEVQNKEIRHANQFGYQTKHGVSGKYLQRRLQVNGLRAVTD
SQ  LNGPIVVQYFSVKESWIRHLKLAGEPSYSGFEDLLRIRVEPNTSPLADKEEKIFRFGSHKWYGAGKRARKARSCATATVA
SQ  GRALSVRETRQAKEHEVAGANKAEHLKHYSPPAEGNCGWHCISAIANRMVNSKFETTLPERVRPPDDWATDEDLVNAIQI
SQ  LRLPAALDRNGACTSAKYVLKLEGEHWTVTVTPGMSPSLLPLECVQGCCGHKGGLGSPDAVEVSGFDPACLDRLAEVMHL
SQ  PSSAIPAALAEMSGDSDRSASPVTTVWTVSQFFARHSGGNHPDQVRLGKIISLCQVIEDCCCSQNKTNRVTPEEVAAKID
SQ  LYLRGATNLEECLARLEKARPPRVIDTSFDWDVVLPGVEAATQTIKLPQVNQCRALVPVVTQKSLDNNSVPLTAFSLANY
SQ  YYRAQGDEVRHRERLTAVLSKLEKVVREEYGLMPTEPGPRPTLPRGLDELKDQMEEDLLKLANAQTTSDMMAWAVEQVDL
SQ  KTWVKNYPRWTPPPPPPKVQPRKTKPVKSLPERKPVPAPRRKVGSDCGSPVSLGGDVPNSWEDLAVSSPFDLPTPPEPAT
SQ  PSSELVIVSSPQCIFRPATPLSEPAPIPAPRGTVSRPVTPLSEPIPVPAPRRKFQQVKRLSSAAAIPPYQDEPLDLSASS
SQ  QTEYEASPPAPPQSGGVLGVEGHEAEETLSEISDMSGNIKPASVSSSSSLSSVRITRPKYSAQAIIDSGGPCSGHLQEVK
SQ  ETCLSVMREACDATKLDDPATQEWLSRMWDRVDMLTWRNTSVYQAICTLDGRLKFLPKMILETPPPYPCEFVMMPHTPAP
SQ  SVGAESDLTIGSVATEDVPRILEKIENVGEMANQGPLAFSEDKPVDDQLVNDPRISSRRPDESTSAPSAGTGGAGSFTDL
SQ  PPSDGADADGGGPFRTVKRKAERLFDQLSRQVFDLVSHLPVFFSRLFYPGGGYSPGDWGFAAFTLLCLFLCYSYPAFGIA
SQ  PLLGVFSGSSRRVRMGVFGCWLAFAVGLFKPVSDPVGAACEFDSPECRNILHSFELLKPWDPVRSLVVGPVGLGLAILGR
SQ  LLGGARCIWHFLLRLGIVADCILAGAYVLSQGRCKKCWGSCIRTAPNEVAFNVFPFTRATRSSLIDLCDRFCAPKGMDPI
SQ  FLATGWRGCWAGRSPIEQPSEKPIAFAQLDEKKITARTVVAQPYDPNQAVKCLRVLQSGGAMVAKAVPKVVKVSAVPFRA
SQ  PFFPTGVKVDPDCRVVVDPDTFTAALRSGYSTTNLVLGVGDFAQLNGLKIRQISKPSGGGPHLMAALHVACSMALHMLAG
SQ  IYVTAVGSCGTGTNDPWCANPFAVPGYGPGSLCTSRLCISQHGLTLPLTALVAGFGIQEIALVVLIFVSIGGMAHRLSCK
SQ  ADMLCVLLAIASYVWVPLTWLLCVFPCWLRCFSLHPLTILWLVFFLISVNMPSGILAMVLLVSLWLLGRYTNVAGLVTPY
SQ  DIHHYTSGPRGVAALATAPDGTYLAAVRRAALTGRTMLFTPSQLGSLLEGAFRTRKPSLNTVNVIGSSMGSGGVFTIDGK
SQ  VKCVTAAHVLTGNSARVSGVGFNQMLDFDVKGDFAIADCPNWQGAAPKTQFCTDGWTGRAYWLTSSGVEPGVIGKGFAFC
SQ  FTACGDSGSPVITEAGELVGVHTGSNKQGGGIVTRPSGQFCNVAPIKLSELSEFFAGPKVPLGDVKVGSHIIKDISEVPS
SQ  DLCALLAAKPELEGGLSTVQLLCVFFLLWRMMGHAWTPLVAVSFFILNEVLPAVLVRSVFSFGMFVLSWLTPWSAQVLMI
SQ  RLLTAALNRNRWSLAFFSLGAVTGFVADLAATQGHPLQAVMNLSTYAFLPRMMVVTSPVPVITCGVVHLLAIILYLFKYR
SQ  GPHHILVGDGVFSAAFFLRYFAEGKLREGVSQSCGMNHESLTGALAMRLNDEDLDFLMKWTDFKCFVSASNMRNAAGQFI
SQ  EAAYAKALRVELAQLVQVDKVRGTLAKLEAFADTVAPQLSPGDIVVALGHTPVGSIFDLKVGSTKHTLQAIETRVLAGSK
SQ  MTVARVVDPTPTPPPAPVPIPLPPKVLENGPNAWGDEDRLNKKKRRRMEALGIYVMGGKKYQKFWDKNSGDVFYEEVHNN
SQ  TDEWECLRVGDPADFDPEKGTLCGHVTIENKAYHVYTSPSGKKFLVPVNPENGRVQWEAAKLSVEQALGMMNVDGELTAK
SQ  ELEKLKRIIDKLQGLTKEQCLNCLAASDLTRCGRGGLVVTETAVKIVKFHNRTFTLGPVNLKVASEVELKDAVEHNQHPV
SQ  ARPIDGGVVLLRSAVPSLIDVLISGADASPKLLAHHGPGNTGIDGTLWDFESEATKEEVALSAQIIQACDIRRGDAPEIG
SQ  LPYKLYPVRGNPERVKGVLQNTRFGDIPYKTPSDTGSPVHAAACLTPNATPVTDGRSVLATTMPPGFELYVPTIPASVLD
SQ  YLDSRPDCPKQLTEHGCEDAALKDLSKYDLSTQGFVLPGVLRLVRKYLFAHVGKCPPVHRPSTYPAKNSMAGINGNRFPT
SQ  KDIQSVPEIDVLCAQAVRENWQTVTPCTLKKQYCGKKKTRTILGTNNFIALAHRAVLSGVTQGFMKKAFNSPIALGKNKF
SQ  KELQTPVLGRCLEADLASCDRSTPAIVRWFAANLLYELACAEEHLPSYVLNCCHDLLVTQSGAVTKRGGLSSGDPITSVS
SQ  NTIYSLVIYAQHMVLSYFKSGHPHGLLFLQDQLKFEDMLKVQPLIVYSDDLVLYAESPTMPNYHWWVEHLNLMLGFQTDP
SQ  KKTAITDSPSFLGCRIINGRQLVPNRDRILAALAYHMKASNVSEYYASAAAILMDSCACLEYDPEWFEELVVGIAQCARK
SQ  DGYSFPGTPFFMSMWEKLRSNYEGKKSRVCGYCGAPAPYATACGLDVCIYHTHFHQHCPVTIWCGHPAGSGSCSECKSPV
SQ  GKGTSPLDEVLEQVPYKPPRTVIMHVEQGLTPLDPGRYQTRRGLVSVRRGIRGNEVGLPDGDYASTALLPTCKEINMVAV
SQ  ASNVLRSRFIIGPPGAGKTYWLLQQVQDGDVIYTPTHQTMLDMIRALGTCRFNVPAGTTLQFPVPSRTGPWVRILAGGWC
SQ  PGKNSFLDEAAYCNHLDVLRLLSKTTLTCLGDFKQLHPVGFDSHCYVFDIMPQTQLKTIWRFGQNICDAIQPDYRDKLMS
SQ  MVNTTRVTYVEKPVRYGQVLTPYHRDREDDAITIDSSQGATFDVVTLHLPTKDSLNRQRALVAITRARHAIFVYDPHRQL
SQ  QGLFDLPAKGTPVNLAVHCDGQLIVLDRNNKECTVAQALGNGDKFRATDKRVVDSLRAICADLEGSSSPLPKVAHNLGFY
SQ  FSPDLTQFAKLPVELAPHWPVVSTQNNEKWPDRLVASLRPIHKYSRACIGAGYMVGPSVFLGTPGVVSYYLTKFVKGGAQ
SQ  VLPETVFSTGRIEVDCREYLDDREREVAASLPHGFIGDVKGTTVGGCHHVTSRYLPRVLPKESVAVVGVSSPGKAAKALC
SQ  TLTDVYLPDLEAYLHPETQSKCWKMMLDFKEVRLMVWKDKTAYFQLEGRYFTWYQLASYASYIRVPVNSTVYLDPCMGPA
SQ  LCNRRVVGSTHWGADLAVTPYDYGAKIILSSAYHGEMPPGYKILACAEFSLDDPVKYKHTWGFESDTAYLYEFTGNGEDW
SQ  EDYNDAFRARQEGKIYKATATSLKFYFPPGPVIEPTLGLN
//
ID  A0MD28;
PN  Non-structural protein 12;
GN  RPOA;
OS  857306;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp1]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. [Nsp1-beta papain-like cysteine proteinase]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. [Nsp2 cysteine proteinase]: Host cytoplasm {ECO:0000269|PubMed:23043113}. Host membrane {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04561}. [Non-structural protein 3]: Host membrane {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04561}. [Non-structural protein 5-6-7]: Host endoplasmic reticulum {ECO:0000250|UniProtKB:Q04561}. Host membrane {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04561}. [Serine protease nsp4]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. [RNA-directed RNA polymerase]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q04561}. [Helicase nsp10]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q04561}. [Uridylate-specific endoribonuclease nsp11]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host nucleus {ECO:0000250|UniProtKB:Q04561}. [Non-structural protein 12]: Host cytoplasm {ECO:0000250|UniProtKB:Q04561}.
DR  UNIPROT: A0MD28;
DR  UNIPROT: A0MD29;
DR  UNIPROT: Q6U9W7;
DR  UNIPROT: Q6U9W8;
DR  Pfam: PF16749;
DR  Pfam: PF14757;
DR  Pfam: PF14758;
DR  Pfam: PF05410;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51961;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: [Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {ECO:0000250|UniProtKB:Q04561}. [Nsp1-alpha papain-like cysteine proteinase]: Inhibits host IFN-beta production. Plays a role in the degradation of the host transcriptional activator CREBBP protein. The degradation of host CREBBP which is a key component of the IFN enhanceosome is likely responsible for the inhibition of interferon mediated by Nsp1-alpha. Participates also in the inhibition of host NF-kappa-B activation by counteracting LUBAC-dependent induction of NF-kappa-B. Reduces host NEMO ubiquitination by blocking the interaction between the two LUBAC complex components RNF31 and SHARPIN. {ECO:0000250|UniProtKB:Q04561}. [Nsp1-beta papain-like cysteine proteinase]: Plays a role in blocking host mRNA nuclear export to the cytoplasm and subversion of host protein synthesis. Additionally, inhibits the interferon-activated JAK/STAT signal transduction by mediating the ubiquitination and subsequent proteasomal degradation of host KPNA1. {ECO:0000250|UniProtKB:Q04561}. [Nsp2 cysteine proteinase]: Multifunctional protein that acts as a viral protease and as a viral antagonist of host immune response. Cleaves the nsp2/nsp3 site in the viral polyprotein. Displays deubiquitinating activity that cleaves both ubiquitinated and ISGylated products and therefore inhibits ubiquitin and ISG15-dependent host innate immunity. Deubiquitinates also host NFKBIA, thereby interfering with NFKBIA degradation and impairing subsequent NF-kappa-B activation. {ECO:0000269|PubMed:20504922, ECO:0000269|PubMed:22258253}. [Non-structural protein 3]: Plays a role in the inhibition of the immune response by interacting with host IFITM1. This interaction leads to the proteasomal degradation of the IFN-induced antiviral protein IFITM1. {ECO:0000250|UniProtKB:Q04561}. [Serine protease nsp4]: Cleaves the majority of cleavage sites present in the C-terminus of the polyprotein. Triggers host apoptosis through caspase-3, -8, and -9 activations. Subverts host innate immune responses through its protease activity. Targets the NF- kappa-B essential modulator NEMO and mediates its cleavage. Blocks host interferon beta induction and downstream signaling by cleaving mitochondrial MAVS, dislodging it from the mitochondria. Impairs host defense by cleaving host mRNA-decapping enzyme DCP1A to attenuate its antiviral activity. {ECO:0000250|UniProtKB:Q04561}. [Non-structural protein 5-6-7]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. {ECO:0000250|UniProtKB:Q04561}. [Non-structural protein 5]: Plays a role in the inhibition of host STAT3 signaling pathway by inducing the degradation of STAT3. {ECO:0000250|UniProtKB:Q04561}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:Q04561}. [Helicase nsp10]: Displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250|UniProtKB:Q04561}. [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P19811}.
DE  Reference Proteome: No;
GO  GO:0044165;
GO  GO:0033644;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0039648;
GO  GO:0006508;
GO  GO:0039579;
GO  GO:0039563;
GO  GO:0039644;
GO  GO:0039502;
GO  GO:0019082;
GO  GO:0039694;
GO  GO:0075523;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGTFSRCMCTPAARVFWNAGQVFCTRCLSARPLLSPELQDTDLGVVGLFYKPKDKIHWKVPIGIPQVECTPSGCCWLSA
SQ  VFPLARMTSGNHNFLQRLVKVADVLYRDGCLAPRHLRELQVYERGCSWYPITGPVPGMGLFANSMHVSDQPFPGATHVLT
SQ  NSPLPQRACRQPFCPFEEAHSDVYRWKKFVIFTDSSPNGRFRMMWTPESDDSAALEVLPPELERQVEILTRSFPAHHPIN
SQ  LADWELTESPENGFSFGTSHSCGHIVQNPNVFDGKCWLTCFLGQSAEVCYHEEHLANALGYQTKWGVHGKYLQRRLQVRG
SQ  MRAVVDPDGPIHVEALSCSQSWVRHLTLNNDVTPGFVRLTSIRIVSNTEPTAFRIFRFGAHKWYGAAGKRARAKRATKSG
SQ  KDSALAPKIAPPVPTCGITTYSPPTDGSCGWHVLAAIVNRMINGDFTSPLPQYNRPEDDWASDYDLAQAIQCLQLPATVV
SQ  RNRACPNAKYLIKLNGVHWEVEVRSGMAPRSLSRECVVGVCSEGCVAPPYPADGLPKRALEALASAYRLPSDCVSSGIAD
SQ  FLADPPPQEFWTLDKMLTSPSPERSGFSSLYKLLLEVVPQKCGATEGAFVYAVERMLKDCPSPEQAMALLAKIKVPSSKA
SQ  PSVSLDECFPAGVPADFEPAFQERPRSPGAAVALCSPDAKGFEGTASEEAQESGHKAVHAVPLAEGPNNEQVQVVAGEQL
SQ  ELGGCGLAIGSAQSSSDSKRENMHNSREDEPLDLSHPAPAATTTLVGEQTPDNPGSDASALPIAVRGFVPTGPILRHVEH
SQ  CGTESGDSSSPLDLSFAQTLDQPLDLSLAAWPVKATASDPGWVRGRCEPVFLKPRKAFSDGDSALQFGELSESSSVIEFD
SQ  QTKDTLVADAPVDLTTSNEALSAVDPSEFVELRRPRHSAQALIDRGGPLADVHAKIKNRVYEQCLQACEPGSRATPATRE
SQ  WLDKMWDRVDMKTWRCTSQFQAGRILASLKFLPDMIQDTPPPVPRKNRASDNAGLKQLVARWDKKLSVTPPPKSAGLVLD
SQ  QTVPPPTDIQQEDATPSDGLSHASDFSSRVSTSWSWKGLMLSGTRLAGSAGQRLMTWVFEVYSHLPAFILTLFSPRGSMA
SQ  PGDWLFAGVVLLALLLCRSYPILGCLPLLGVFSGSLRRVRLGVFGSWMAFAVFLFSTPSNPVGSSCDHDSPECHAELLAL
SQ  EQRQLWEPVRGLVVGPSGLLCVILGKLLGGSRHLWHVILRLCMLTDLALSLVYVVSQGRCHKCWGKCIRTAPAEVALNVF
SQ  PFSRATRNSLTSLCDRFQTPKGVDPVHLATGWRGCWRGESPIHQPHQKPIAYANLDEKKISAQTVVAVPYDPSQAIKCLK
SQ  VLQAGGAIVDQPTPEVVRVSEIPFSAPFFPKVPVNPDCRIVVDSDTFVAAVRCGYSTAQLVLGRGNFAKLNQTPLRDSAS
SQ  TKTTGGASYTLAVAQVSVWTLVHFILGLWFTSPQVCGRGTADPWCSNPFSYPAYGPGVVCSSRLCVSADGVTLPLFSAVA
SQ  QLSGREVGIFILVLVSLTALAHRLALKADMLVVFSAFCAYAWPMSSWLICFFPILLKWVTLHPLTMLWVHSFLVFCMPAA
SQ  GILSLGITGLLWAVGRFTQVAGIITPYDIHQYTSGPRGAAAVATAPEGTYMAAVRRAALTGRTLIFTPSAVGSLLEGAFR
SQ  THKPCLNTVNVVGSSLGSGGVFTIDGRKTVVTAAHVLNGDTARVTGDSYNRMHTFKTSGDYAWSHADDWQGVAPVVKVAK
SQ  GYRGRAYWQTSTGVEPGVIGEGFAFCFTNCGDSGSPVISESGDLIGIHTGSNKLGSGLVTTPEGETCAIKETKLSDLSRH
SQ  FAGPSVPLGDIKLSPAIVPDVTSIPSDLASLLASVPVMEGGLSTVQLLCVFFLLWRMMGHAWTPIVAVGFFLLNEILPAV
SQ  LVRAVFSFALFILAWATPWSAQVLMIRLLTASLNRNKLSLAFYALGGVVGLAAEIGAFAGRLPELSQALSTYCFLPRVLA
SQ  MASYVPIIIIGGLHALGVILWLFKYRCLHNMLVGDGSFSSAFFLRYFAEGNLRKGVSQSCGMSNESLTAALACKLSQADL
SQ  DFLSSLTNFKCFVSASNMKNAAGQYIEAAYAKALRQELASLVQVDKMKGILSKLEAFAETATPSLDAGDVVVLLGQHPHG
SQ  SILDINVGTERKTVSVQETRSLGGSKFSVCTVVSNTPVDALTGIPLQTPTPLFENGPRHRGEEDDLRVERMKKHCVSLGF
SQ  HNINGKVYCKIWDKSTGDTFYTDDSRYTQDLAFQDRSADYRDRDYEGVQTAPQQGFDPKSETPIGTVVIGGITYNRYLIK
SQ  GKEVLVPKPDNCLEAAKLSLEQALAGMGQTCDLTAAEVEKLRRIISQLQGLTTEQALNCLLAASGLTRCGRGGLVVTETA
SQ  VKIVKYHSRTFTLGPLDLKVTSEAEVKKSTEQGHAVVANLCSGVILMRPHPPSLVDVLLKPGLDTKPGIQPGHGAGNMGV
SQ  DGSTWDFETAPTKAELELSKQIIQACEVRRGDAPNLQLPYKLYPVRGDPERHGGRLINTRFGDLSYKTPQDTKSAIHAAC
SQ  CLHPNGAPVSDGKSTLGTTLQHGFELYVPTVPYSVMEYLDSRPDTPFMCTKHGTSKAAAEDLQKYDLSTQGFVLPGVLRL
SQ  VRRFIFGHIGKAPPLFLPSTYPAKNSMAGINGQRFPTKDVQSIPEIDEMCARAVKENWQTVTPCTLKKQYCSKPKTRTIL
SQ  GTNNFIALAHRSALSGVTQAFMKKAWKSPIALGKNKFKELHCTVAGRCLEADLASCDRSTPAIVRWFVANLLYELAGCEE
SQ  YLPSYVLNCCHDLVATQDGAFTKRGGLSSGDPVTSVSNTVYSLIIYAQHMVLSALKMGHEIGLKFLEEQLKFEDLLEIQP
SQ  MLVYSDDLVLYAERPTFPNYHWWVEHLDLMLGFRTDPKKTVITDKPSFLGCRIEAGRQLVPNRDRILAALAYHMKAQNAS
SQ  EYYASAAAILMDSCACIDHDPEWYEDLICGIARCARQDGYSFPGPAFFMSMWEKLRSHNEGKKFRHCGICDAKADHASAC
SQ  GLDLCLFHSHFHQHCPVTLSCGHHAGSRECSQCQSPVGAGRSPLDAVLKQIPYKPPRTVIMKVGNKTTALDPGRYQSRRG
SQ  LVAVKRGIAGNEVDLPDGDYQVVPLLPTCKDINMVKVACNVLLSKFIVGPPGSGKTTWLLSQVQDDDVIYTPTHQTMFDI
SQ  VSALKVCRYSIPGASGLPFPPPARSGPWVRLVASGHVPGRTSYLDEAGYCNHLDILRLLSKTPLVCLGDLQQLHPVGFDS
SQ  YCYVFDQMPQKQLTTIYRFGPNICAAIQPCYREKLESKARNTRVVFTTWPVAFGQVLTPYHKDRIGSAITIDSSQGATFD
SQ  IVTLHLPSPKSLNKSRALVAITRARHGLFIYDPHNQLQEFFNLIPERTDCNLVFSRGDDLVVLSADNAVTTVAKALGTGP
SQ  SRFRVSDPRCKSLLAACSASLEGSCMPLPQVAHNLGFYFSPDSPAFAPLPKELAPHWPVVTHQNNRAWPDRLVASMRPID
SQ  ARYSKPMVGAGYVVGPSTFLGTPGVVSYYLTLYIRGEPQALPETLVSTGRIATDCREYLDAAEEEAAKELPHAFIGDVKG
SQ  TTVGGCHHITSKYLPRTLPKDSVAVVGVSSPGRAAKAMCTLTDVYLPELRPYLQPETASKCWKLKLDFRDVRLMVWKGAT
SQ  AYFQLEGLTWSALPDYARFIQLPKDAVVYIDPCIGPATANRKVVRTTDWRADLAVTPYDYGAQNILTTAWFEDLGPQWKI
SQ  LGLQPFRRAFGFENTEDWAILARRMSDGKDYTDYNWDCVRERPHAIYGRARDHTYHFAPGTELQVELGKPRLPPGREP
//
ID  Q68772;
PN  Non-structural protein 12;
GN  rep;
OS  38143;
SL  Nucleus Position: SL-0382;
SL  Comments: [Nsp2 cysteine proteinase]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [Non-structural protein 5-6-7]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. [3C-like serine proteinase]: Host cytoplasm {ECO:0000305}. [RNA-directed RNA polymerase]: Host cytoplasm, host perinuclear region {ECO:0000305}. [Helicase]: Host cytoplasm, host perinuclear region {ECO:0000305}.
DR  UNIPROT: Q68772;
DR  UNIPROT: P89132;
DR  UNIPROT: Q87077;
DR  Pfam: PF16749;
DR  Pfam: PF19215;
DR  Pfam: PF05411;
DR  Pfam: PF05412;
DR  Pfam: PF05579;
DR  Pfam: PF00680;
DR  Pfam: PF01443;
DR  PROSITE: PS51538;
DR  PROSITE: PS51961;
DR  PROSITE: PS51493;
DR  PROSITE: PS51539;
DR  PROSITE: PS51540;
DR  PROSITE: PS51652;
DR  PROSITE: PS51958;
DR  PROSITE: PS51947;
DR  PROSITE: PS51657;
DR  PROSITE: PS50507;
DE  Function: The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. The Nsp1 chain is essential for viral subgenomic mRNA synthesis. {ECO:0000250}. The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. {ECO:0000250}. [Uridylate-specific endoribonuclease nsp11]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'- cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P19811}. The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0033644;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0004197;
GO  GO:0003678;
GO  GO:0004519;
GO  GO:0016829;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0003968;
GO  GO:0004252;
GO  GO:0008270;
GO  GO:0006351;
GO  GO:0006508;
GO  GO:0019082;
GO  GO:0039694;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFCECPRSNLVVMCSGAFCCVLCGHRRRPRPASESDRAKYGPIVQYVEARVAHVYSGLEGRYCALEMIPITYGNKFPYCK
SQ  PLPVSFVIKTLAGVQGDLTRLEETPLPGGYGVIPCWGPHLAAVGYLSPAHVGRDWFEGATHAIVHIGSYGGHERPTTIPF
SQ  NTTGGDVYQLGTCTIVETIDHVEWHAGVKPGTAICPLDRIDFAQKVITAFPEGFLANKAWLGDKRGTLKVEADPETAALS
SQ  FEHGRCWLKLFPDPACELTTASTFGYQLNCGVQGKYIARRLQTNGLKLVQNQEGKFIAYTFHRGSWLGHIGHADESVPPD
SQ  CQIIARFDVLPYNEWSPLPLLKLPGKTYFGGNASSVSWPEWKYDEQLLYADSLTAGFCWLQLFPPLSRKSEAQRAILAQQ
SQ  VNNYGVTGTYLEYRLRQYGIVLAECDYGEHYIYAAASDSSIRHISPVPIHDRHHVFVTRLTARFGAFDEGFDLGFGTRYG
SQ  RRRGGGKKSGQSSGVRAPGRTTPDLAGDWGKAVDDQEKTASKVTTDKAMSTSEPAVVQVGCETKPVADAAAVPASVNSTG
SQ  CALLPVQADPCCTAGVAAKESEPKAVAAPSIPITFGAPAGETLPVAASPLVVKKDKRCISVKLTAKKALPKETFIPPPDG
SQ  GCGVHAFAAIQYHINTGHWPEQKPVVNWAYEAWTTNEDIGHMICSTETPAALEPCLHARYVVRLDSDHWVVDHYPNRPMC
SQ  FVEACAHGWCSSLLSEPTGEEGEHLVDCSALYDCLGKFRNGTEFADTVLGLSKTAHCCNKRVPTPRKQAIMSLLNRPNCV
SQ  PCIAPPSQVRTVDPSQPAAPLPPVPRPRKRKAAAQQVSKVPSEQDPSLAHDPPEKPDSVRPPKLGYLDRAWNNMLARTHK
SQ  LHNLQQRVFGLYPQLLSMLLPSGARPSTPRLLGCYFSMAVAMFFLFLGSPLFILCAVLAGVIAPSARYPKILCCCLVVVY
SQ  ICTLFADAISSVCDNDDADCRAFLSDLGDRYSTNQPVYITPGPATFFLAVSRNFFVVSVALFPLHLLLLMVDVLLVIGVL
SQ  CMDGYCFRCFSRCVRKAPEEVSLLTIPQSRVSRRFLLDICDFYSAPPVDIIRLATGLNGCFRGDYSPIGSSTSVITADKI
SQ  DVKKVSCRTVCSFPSCPSEAVKVLHVLSVRGQMCAHNEQKVEKVDALPCKNPLFPYDLSSKKIVPVDSGTYEILSSIGCD
SQ  MSHLVIGDGDFFKVMGVPRPSPFTVMRLRACRVVGGGRIFRTALAAAWVLFFVCAGYWVQMSTPCGIGTNDPFCKSSFGV
SQ  PTYVNQGVCHGQYCASSKGVSRATSILTVRNPAVAPYIVLAACLVYLASVYVPGIIEVSLLVLNALLPAGPAISALRTLV
SQ  MIIAAPHLSMKYIAFFCCTTAFVDFTSVVVVLTALLVGWILARYTGIGGFVTPYDIHDVVKSQRDGVAVANAPPNTYLGA
SQ  VRRAALTGKPAFFVANNTGIVLEGLLREKTRASNSVSVYGVTCGSGGLFSDGNNTVCLTATHVCGNNKAVVDYQGTRYEA
SQ  VFTTKGDYASAVVPIPGAFPPLKFAPQSYTGRAYWYANTGVETGFVGTTGCLVFSGPGDSGSPIITPDGLIVGVHTGSDS
SQ  KGSGAYTTPNGLTVSGPLSLKEMGAHYEGPIVDVPTRLPRNVHNDTKSVPQPLARLLESSINLEGGLGTIQLIIVAVVLW
SQ  KYAVDPLSIPFVVAFFLLNEILPKCLIRCFYNYSLFCLAAFSPLASRIFFIRLLTAALNRNPTALICHACFAGIAVLNDF
SQ  IILGDIRLALRFTSFYVVGVNHDAIAIAVIGALVCVAACCLELFGLPQMASVIGCHGSFDPTFLSRYVHEGIRQGVSSGF
SQ  GTESLSTALACALSEDELNFLAQAVDHKAIVSAIHVHKTLQDYILSKNAKILRASLASVHANHNASKALASLDKFLQGTS
SQ  TQLKPGDPVILLGSTSAELVSVFSGDSEYIAEPIRSHPVAGTICTLCVVQAKCEGGLVTQVNGKFSPAKYLAVAGKVLAD
SQ  HPDYKLENDGRFPRTREDRVKDSVQVDTVDIGSHTFKKMWNKTTGDVWYDIIMPESAANPLAVHDLDSAVAAIGMSKEIP
SQ  EKDMNRLRAIISKLQGLVSSEALNLLTAAGCTSADRSGLVITLDYAKIITHHARTRAFSSIDFKVVSPDEAMRTARLSPS
SQ  PQPIIASFSDDKFLLLRRHPPSLLDVLTKGLDATCREPLHSPGDQGIDGYLWDFEAPHSKEAIWLSNQIISACAARRGDA
SQ  PGCYPYKLHPVRGDPYRVGNVLKNTRFGDVTYTAVSDSDSPWLKVASINSGGCPVVTDRVLGSTIPVGSEIYLPTLPESV
SQ  LDYLDSRPDCPTYYTQHGCEAAALQDLKKFNLSTQGFILPEVLNIVRNYLLGTIGYRPAIYKPSTVPSNDSHAGINGLSF
SQ  STKTLQALPDIDELCEKAIAEVWQTVTPVTLKKQFCSKAKTRTILGTNAMASLALRALLSGVTQGFQLAGKNSPICLGKS
SQ  KFDPCTFEVKGRCLETDLASCDRSTPAIVRHFATKLLFEMACAERALPLYVVNCCHDLIVTQTSAATKRGGLSSGDPVTS
SQ  IANTIYSLVLYVQHMVLTLLENGHPLSLKFLSGKLNFQDLYKLQAFIVYSDDLILLNESDDLPNFERWVPHLELALGFKV
SQ  DPKKTVITSNPGFLGCEYRHGWLVPQKQRVLAALAYHVNAKDVHTYYINATAILNDASALSAFEPDWFDDLVIGLADCAR
SQ  KDGYSFPGPAAFREFFSRVSGYQFEGKEVQVCSICCSTARTTSLCGMALCDFCAHRHYHPGCHVLSSFCKHVIGSNTCKM
SQ  CSIPILKDRTKFAELLASDQYRSVCTVEVTVVDGYTDAAPGRYSYQKKQYMLRKERRGCPLDLPDGKYSMKLLPNSCSGI
SQ  CVPKAQENATLSNFVVGPPGSGKTTFISNLLDDDAVVYCPTHVSLIAYSKSLPAARFSVPRGQDPAEYGTPALSGPTLQL
SQ  LSAGYVPGAKHYLDEACYANPFDVFKLLSKTPITAIGDPAQLTPVGFDTPLYVFELMKKNALHAIYRFGQNICNAIQPCY
SQ  STKLVSQRQGDTEVIFQTKFAPRGKVLTPYHRDRVGAAVTIDSSQGSTYDVVTLYLPTKGSLTLARGLVGITRARERLYV
SQ  YDPHHQLAKYFNLQPSSTTIRPHAVVIDGKARVMLSDKCYAAPEDFPGMLCTARPATAADRKILEETCLKLDFLESGSLS
SQ  PLPRVCYNLGFYYSPDITKLLPIPSELAKHWPVATNRNNPEWPNRLVVSATRLSPLSHPAVCAGYYVGDSLFVGTPNVTS
SQ  YWLTKFLDGRAVPMEDSVYSTGRFEMDIRDYLDSAERDFAAKHPHAFIGDTKGTTVGGCHHITSQYLPHVLPADSVVKVG
SQ  VSKPGVAHKALCTVTDIYLPMLGSYTSPPTQSKVYKVNVDHKACKLMVWRDQTMYFQEGFDYHTLVDALRFVRLSSDGVY
SQ  RVAPELTPMIGNRRLDLGAKPLRPVDLAITPWDDPKCEFLVTHASPFDMSDEFLLVNAFDFIKEDLLGKSVTPVYFYKRL
SQ  SEPLHFDQNLPPHVGAILSKAPRFISLAKVFNFCFTPTACHCKVSVKTATGDHMCKCSLSSDEFLSRFNPTVGTP
//
ID  Q5ZKD5;
PN  RRP12-like protein;
GN  RRP12;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleolus {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q5ZKD5;
DR  Pfam: PF08161;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0006364;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARCGRLRAGTAAKLRRWRKGHSSDCNPETRRHRLAARSRFYSRPTEKSNLTVDAVKLHNELQSGSLRVERPSGSSQLPM
SQ  EEGDAGEAATERSSGTFLSGLSDCTNVTFSRVQRFWESNSAAHKEICAVLAAVTDVIRSQGGKETETEYFAALMTTLEAV
SQ  DSPESVAAVAYLLNLVLKRVPSPVLIKKFSDASKAFMNIISSQACSGSTSALRWVLSCLATLLRKQDLAAWSYPVTLQVY
SQ  HGLLSFCVHTKPKVRKAAQHGVCSVLRGSEFMFGDEAPEHHPAAPSSAKFCVQEIEKAGGTKEATTTLHVLALLRDLLPC
SQ  FPAAVLKTCCETLLRVMTLSHVLVTACAMQAFHSLFSAQPRTSCLPAELNAQIITALYDYVPSANDLQPLLTWLTTMERA
SQ  HVNLGRLQKDLCWAHLPRLFSATMNCFLSPHLQVVAAAAQTLETLLNECIAPHMDELGNVSASTPAPGSYLCKMFRSVEE
SQ  GLTYRFHAAWDGVLQVLEVFFEVCGKQCHPIMRKCLQSLCDLRLSPHFPYTTEVDQAVGAAVGAMGPEVLLEAVPLQIDG
SQ  KEETLDFPRSWLLPVLRDYVQGARLGFFTSYFLPLAATLKSRALEFAQAGKSLESKIYDTLQWQVWTLLPGFCTRPTDVV
SQ  EAFKGLARTLGMAISERPDLRPTVCQALRTLIHHGCGTDAERAEVGRFAKNFLPILFNVYSQPEEDGGSSSQRRSVLDTV
SQ  RAYLTITDPQLGCGFLQKASEKLTSPESSEFARLSILDLVVAMSPYANEQALGSLYRTIQPSLQSKDHSMQKKAYRVLEE
SQ  VCAAPHAPCQAFVHSHLEELQAVLLDSLKSAASPAKRPRLKCLFHIMKQLSAEHEPFVTALVPEVILCTKEVSVGARKNA
SQ  FMLLVEMGHAFIRFGPTPQEAMERFLLLVYAGLTGSVTMISCTVLALTRLFFEFRDHMELNVVEQLLQNICLLLGSRTRD
SQ  VVKAALGFIKVVLLLVDTTLLAKHVQTMLEAVGSLSDDMRRHFRMKLRNLFTKFIRKFGFELVQGLLPAEFHKVLVNIRK
SQ  AEARSRKQRALRQAAAEAEEEEAPAQPKGDSMEEILADSEEEEEEEEERRRGKVRKKQARQKGQAWLKEGEEDEPLNFLD
SQ  PNVSQRVLATEPSLKKSRGVKHDFQVSEDGRLIIHDEEEEVDNDEAKGVEEEVADVLQEVGLRSKKSQKRRFREEPDDDE
SQ  PETGTYSQYRAGGSGIHRPLDKKPAFGAEYRSKKGKGDVKKKGQLDPYAYIPLNRAKLNKRKQAKMQGQFKGLMKGAQRG
SQ  AKAGRKNRLKDRRP
//
ID  Q5JTH9;
PN  RRP12-like protein;
GN  RRP12;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q5JTH9;
DR  UNIPROT: B4DK00;
DR  UNIPROT: E9PCK7;
DR  UNIPROT: Q5JTH8;
DR  UNIPROT: Q69YK4;
DR  UNIPROT: Q96E87;
DR  UNIPROT: Q9BUH3;
DR  UNIPROT: Q9Y4C7;
DR  Pfam: PF08161;
DR  OMIM: 617723;
DR  DisGeNET: 23223;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O95271; IntAct: EBI-30838215; Score: 0.44
DE  Interaction: Q96CW1; IntAct: EBI-311571; Score: 0.37
DE  Interaction: Q99558; IntAct: EBI-363073; Score: 0.00
DE  Interaction: Q9NY93; IntAct: EBI-1075899; Score: 0.00
DE  Interaction: Q9JMK2; IntAct: EBI-2558429; Score: 0.40
DE  Interaction: P62960; IntAct: EBI-2560211; Score: 0.40
DE  Interaction: P01100; IntAct: EBI-2688688; Score: 0.00
DE  Interaction: P03372; IntAct: EBI-2877710; Score: 0.60
DE  Interaction: Q92731; IntAct: EBI-2880211; Score: 0.46
DE  Interaction: P68400; IntAct: EBI-5294760; Score: 0.44
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-21328549; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: Q16666; IntAct: EBI-9995438; Score: 0.35
DE  Interaction: P41218; IntAct: EBI-9996028; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: Q99661; IntAct: EBI-11004229; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: F8VQC1; IntAct: EBI-11054725; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-11069711; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-11088773; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104527; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-11145880; Score: 0.35
DE  Interaction: Q9QZD9; IntAct: EBI-11149349; Score: 0.35
DE  Interaction: P56180; IntAct: EBI-14025693; Score: 0.42
DE  Interaction: Q96KR7; IntAct: EBI-14027299; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-14035664; Score: 0.35
DE  Interaction: P11487; IntAct: EBI-21532550; Score: 0.35
DE  Interaction: Q6AW86; IntAct: EBI-21553112; Score: 0.35
DE  Interaction: P22492; IntAct: EBI-21580683; Score: 0.35
DE  Interaction: O43159; IntAct: EBI-21627620; Score: 0.35
DE  Interaction: P55075; IntAct: EBI-21635166; Score: 0.35
DE  Interaction: P10412; IntAct: EBI-21665473; Score: 0.35
DE  Interaction: Q8WYQ3; IntAct: EBI-21674595; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-21677299; Score: 0.35
DE  Interaction: Q15020; IntAct: EBI-21678189; Score: 0.35
DE  Interaction: Q5T3I0; IntAct: EBI-21681508; Score: 0.35
DE  Interaction: Q8N0W7; IntAct: EBI-21682168; Score: 0.35
DE  Interaction: O14836; IntAct: EBI-21700334; Score: 0.35
DE  Interaction: P19438; IntAct: EBI-21717945; Score: 0.35
DE  Interaction: Q96HE9; IntAct: EBI-21733724; Score: 0.35
DE  Interaction: Q9NY72; IntAct: EBI-21735451; Score: 0.35
DE  Interaction: P62263; IntAct: EBI-21741976; Score: 0.35
DE  Interaction: Q02539; IntAct: EBI-21742951; Score: 0.35
DE  Interaction: Q9BYG3; IntAct: EBI-21743958; Score: 0.35
DE  Interaction: P18124; IntAct: EBI-21745402; Score: 0.35
DE  Interaction: P01127; IntAct: EBI-21779861; Score: 0.35
DE  Interaction: Q13895; IntAct: EBI-21815267; Score: 0.35
DE  Interaction: Q2NL82; IntAct: EBI-21815364; Score: 0.35
DE  Interaction: Q86VZ2; IntAct: EBI-21853663; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-16786806; Score: 0.27
DE  Interaction: Q96GD4; IntAct: EBI-16787973; Score: 0.27
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P22087; IntAct: EBI-16792282; Score: 0.42
DE  Interaction: P68431; IntAct: EBI-16793336; Score: 0.42
DE  Interaction: P62491; IntAct: EBI-16797971; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: P62753; IntAct: EBI-16798663; Score: 0.42
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: P27824; IntAct: EBI-16789004; Score: 0.42
DE  Interaction: Q15075; IntAct: EBI-16791787; Score: 0.27
DE  Interaction: Q08379; IntAct: EBI-16793089; Score: 0.27
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-21255178; Score: 0.37
DE  Interaction: Q9ULX6; IntAct: EBI-26451653; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: P11274; IntAct: EBI-28931791; Score: 0.35
DE  Interaction: P11801; IntAct: EBI-28931861; Score: 0.35
DE  Interaction: P43405; IntAct: EBI-28935283; Score: 0.35
DE  Interaction: P78362; IntAct: EBI-28948274; Score: 0.35
DE  Interaction: Q9Y2H9; IntAct: EBI-28948459; Score: 0.35
DE  Interaction: Q9H5K3; IntAct: EBI-28948637; Score: 0.35
DE  Interaction: O60729; IntAct: EBI-27115568; Score: 0.27
DE  Interaction: Q9UIH9; IntAct: EBI-29019642; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.42
DE  Interaction: O43474; IntAct: EBI-29020028; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
DE  Interaction: P31314; IntAct: EBI-29607649; Score: 0.35
DE  Interaction: P50458; IntAct: EBI-29019155; Score: 0.27
DE  Interaction: P01106; IntAct: EBI-29661630; Score: 0.27
DE  Interaction: P48431; IntAct: EBI-29721059; Score: 0.27
DE  Interaction: O43763; IntAct: EBI-29786140; Score: 0.27
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P21709; IntAct: EBI-32720516; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005886;
GO  GO:0003723;
GO  GO:0006364;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGRSGKLPSGVSAKLKRWKKGHSSDSNPAICRHRQAARSRFFSRPSGRSDLTVDAVKLHNELQSGSLRLGKSEAPETPME
SQ  EEAELVLTEKSSGTFLSGLSDCTNVTFSKVQRFWESNSAAHKEICAVLAAVTEVIRSQGGKETETEYFAALMTTMEAVES
SQ  PESLAAVAYLLNLVLKRVPSPVLIKKFSDTSKAFMDIMSAQASSGSTSVLRWVLSCLATLLRKQDLEAWGYPVTLQVYHG
SQ  LLSFTVHPKPKIRKAAQHGVCSVLKGSEFMFEKAPAHHPAAISTAKFCIQEIEKSGGSKEATTTLHMLTLLKDLLPCFPE
SQ  GLVKSCSETLLRVMTLSHVLVTACAMQAFHSLFHARPGLSTLSAELNAQIITALYDYVPSENDLQPLLAWLKVMEKAHIN
SQ  LVRLQWDLGLGHLPRFFGTAVTCLLSPHSQVLTAATQSLKEILKECVAPHMADIGSVTSSASGPAQSVAKMFRAVEEGLT
SQ  YKFHAAWSSVLQLLCVFFEACGRQAHPVMRKCLQSLCDLRLSPHFPHTAALDQAVGAAVTSMGPEVVLQAVPLEIDGSEE
SQ  TLDFPRSWLLPVIRDHVQETRLGFFTTYFLPLANTLKSKAMDLAQAGSTVESKIYDTLQWQMWTLLPGFCTRPTDVAISF
SQ  KGLARTLGMAISERPDLRVTVCQALRTLITKGCQAEADRAEVSRFAKNFLPILFNLYGQPVAAGDTPAPRRAVLETIRTY
SQ  LTITDTQLVNSLLEKASEKVLDPASSDFTRLSVLDLVVALAPCADEAAISKLYSTIRPYLESKAHGVQKKAYRVLEEVCA
SQ  SPQGPGALFVQSHLEDLKKTLLDSLRSTSSPAKRPRLKCLLHIVRKLSAEHKEFITALIPEVILCTKEVSVGARKNAFAL
SQ  LVEMGHAFLRFGSNQEEALQCYLVLIYPGLVGAVTMVSCSILALTHLLFEFKGLMGTSTVEQLLENVCLLLASRTRDVVK
SQ  SALGFIKVAVTVMDVAHLAKHVQLVMEAIGKLSDDMRRHFRMKLRNLFTKFIRKFGFELVKRLLPEEYHRVLVNIRKAEA
SQ  RAKRHRALSQAAVEEEEEEEEEEEPAQGKGDSIEEILADSEDEEDNEEEERSRGKEQRKLARQRSRAWLKEGGGDEPLNF
SQ  LDPKVAQRVLATQPGPGRGRKKDHGFKVSADGRLIIREEADGNKMEEEEGAKGEDEEMADPMEDVIIRNKKHQKLKHQKE
SQ  AEEEELEIPPQYQAGGSGIHRPVAKKAMPGAEYKAKKAKGDVKKKGRPDPYAYIPLNRSKLNRRKKMKLQGQFKGLVKAA
SQ  RRGSQVGHKNRRKDRRP
//
ID  Q6P5B0;
PN  RRP12-like protein;
GN  Rrp12;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleolus {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q6P5B0;
DR  UNIPROT: Q7TMI5;
DR  UNIPROT: Q80TU2;
DR  Pfam: PF08161;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q3TBT3; IntAct: EBI-10729637; Score: 0.35
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005886;
GO  GO:0006364;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGRSGKLPSGVSAKLKRWKKGHSSDSNPATCRHRQAARSRFFSRPSGKSDLTVDAVKLHNELQSGTLSLGKSQAPETTMD
SQ  QDPEVAFTEKSSGTFLSGLSDCTNVTFSKVQRFWESNSAAHKEICAVLAAVTEVIRSQGGKETETEYFAALMTTMEAVES
SQ  PESLAAVAYLLNLVLKRVPSPVLMKKFSDTSKAFMDIMSAQASSGSTSALRWVLSCLAILLRKQDLEAWGYPITLQVYHG
SQ  LLSFTVHAKPKIRKAAQHGVCSVLKGSDFMFGEKAPAHHPAAVSTAKFCIQEIEKSGGSKEATTTLHMLTLLKDMLPCFP
SQ  EGLVKSCSETLLRVMTLNHVLVTACAMQAFHNLFHAKPSPSTLSAELNAQIVTALYDYVPSENDLQPLLAWLKVMEKAHI
SQ  NLVRLQRDLGLGHLARFFGTAVTCLLSPHSQVAAAATQTLKEILKECVAPHIADIGSVTSSASGPPQYITKMFRAVEEGL
SQ  TYKFHAAWSSVLQLLGVFFEACGKQAHPVMKKCLQSLCDLRLSPHFPHTAALDQAVGAAVTSMGPEVVLQAVPLEIDGSE
SQ  ETLDFPRSWLLPVIRDHVRETRLGFFTTYFLPLATTLKRKAMDLAQAGSTVESKIYDTLQWQIWTLLPGFCTRPTDVAAS
SQ  FKGLARTLGTAINERPDLRVTVCQALRTLITKGCEAEADRAEVSRFAKNFLPILFNLYGQPVAAGEAAAPRRAVLETIKT
SQ  YLTITEAQLVNSFLEKATEKVLDPASSDFTRLSVLDLVVALAPYSDEAAISKLYSTIRPYLESKVHGVQKKAYRVLEEVC
SQ  ASSQGPAARFVQSHLDDLKKTLLDSLRTTSSPAKRPRLKCLIHIVKTLSAEHEEFIAALIPEVILCTKEVSVGARKSAFT
SQ  LLVEMGHAFLRFGSNQEDALQRYLVLIYPGLLGAVTTVSCSILALTHLLFEFKGLMGTSTVEQLLENVCLLLASRTRDVV
SQ  KSALGFIKVAVVVMDVVHLAKHVQLVMEAIGKLSDDMRRHFRMKLRNLFIKFTRKFGFELVKGLLPAEYHKVLINIRKAE
SQ  TRAKKHRALSQAAVEEEEEEEEEEEPVQSKGDSIEEILADSEDEDEEEERGRGKEQRKLARQRSRAWLKEGGGDEPLNFL
SQ  DPKVAHRVLATQPGPGRGKKRDHGFKLSADGRLIIREEEDGNKVEEEDGTKGEDEDMTDAMEDASVRSKKKLKRQREDEE
SQ  DELEIPPRYQAGGSGIHRPVAKKAAPGAEYKAKKAKGDVKKKGRLDPYAYVPLNRSKLNRRKKVKLQGQFKGLVKATQRG
SQ  SQAGHKLRRKDRRRP
//
ID  P53694;
PN  Reticulon-like protein 1;
GN  rtn1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein {ECO:0000269|PubMed:20434336}. Nucleus membrane {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein {ECO:0000269|PubMed:20434336}. Note=Enriched at the cell equator during mitosis.
DR  UNIPROT: P53694;
DR  Pfam: PF02453;
DR  PROSITE: PS50845;
DE  Function: Required for the correct positioning of the cellular division plane by delimiting the actomyosin ring assembly at the cell equator. Overexpression causes cell lysis. {ECO:0000269|PubMed:20434336}.
DE  Reference Proteome: Yes;
GO  GO:0032153;
GO  GO:0032541;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:1990809;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSEQHSLNPFESGSVTASDVAAAKSGAEDLVNTLTAHTVHPSTELPSATSFPSALPNSENPVIQNISSSSSEPHHTSQST
SQ  PGETSSPVCPVSGAHGGADKKCPALEAGCPFTNTTKQNVDPEISNALWSVLTWKNTSCSFSTLMSILALVYVPSWINLPR
SQ  LFFRTFRYVFLITSIIEFGGLFASNGKRGVLSHFRSSYITCDSKALDRIVNSIVDIFNVMLIQFQRILFAESPILTFTAS
SQ  VAAFIEFFLSGFLSYKSLFVWNVLFAFILPRLYVCNERSIKHLVASLERSGDKLKKQATETINTTVNK
//
ID  Q7ZUH1;
PN  RNA transcription, translation and transport factor protein;
GN  rtraf;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y224}. Note=Shuttles between the cytosol and the nucleus. {ECO:0000250|UniProtKB:Q9Y224}.
DR  UNIPROT: Q7ZUH1;
DR  Pfam: PF10036;
DE  Function: RNA-binding protein involved in modulation of mRNA transcription by Polymerase II. Component of the tRNA-splicing ligase complex. {ECO:0000250|UniProtKB:Q9Y224}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0072669;
GO  GO:0003723;
GO  GO:0000993;
GO  GO:0006469;
GO  GO:0045944;
GO  GO:0006388;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRRKLTALEYHNPTGFDCKDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIPSSDWPKYFEKYLQDVNCPFSVQERQETV
SQ  DWLLGLAVRFEYGDNVEKYRNCKPVTETNDVQKSADPLINLDSNNPDFKAGVLALANLLKIQRHDDYLVMLKAIKILVQE
SQ  RLTPDAIAKASQAKEGLPVTLDKHILGFDTGDATLNEAAQVLRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLGKV
SQ  GR
//
ID  Q9Y224;
PN  RNA transcription, translation and transport factor protein;
GN  RTRAF;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:15147888, ECO:0000269|PubMed:24608264}. Cytoplasm, cytosol {ECO:0000269|PubMed:15147888, ECO:0000269|PubMed:24608264}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15147888}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15147888}. Note=May localize at the centrosome during mitosis (PubMed:15147888). Shuttles between the cytosol and the nucleus: enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low (PubMed:24608264). {ECO:0000269|PubMed:15147888, ECO:0000269|PubMed:24608264}. Nucleus {ECO:0000269|PubMed:26864902}. Cytoplasm {ECO:0000269|PubMed:26864902}. Note=(Microbial infection) Following influenza A virus (IAV) infection, included in influenza A virions via its association with packaged viral ribonucleoproteins (vRNP) in the nucleus and cytoplasm (PubMed:21900157, PubMed:26864902). {ECO:0000269|PubMed:21900157, ECO:0000269|PubMed:26864902}.
DR  UNIPROT: Q9Y224;
DR  PDB: 7P3A;
DR  Pfam: PF10036;
DR  OMIM: 610858;
DR  DisGeNET: 51637;
DE  Function: RNA-binding protein involved in modulation of mRNA transcription by Polymerase II (PubMed:16950395). Component of the tRNA-splicing ligase complex and is required for tRNA ligation (PubMed:24870230). May be required for RNA transport (PubMed:24608264). {ECO:0000269|PubMed:16950395, ECO:0000269|PubMed:24608264, ECO:0000269|PubMed:24870230}. (Microbial infection) In case of infection by influenza virus A (IVA), is involved in viral replication (PubMed:21900157). {ECO:0000269|PubMed:21900157}.
DE  Reference Proteome: Yes;
DE  Interaction: O75190; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: P59595; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-7195640; Score: 0.40
DE  Interaction: Q9NRI5; IntAct: EBI-1105474; Score: 0.00
DE  Interaction: Q8N4C6; IntAct: EBI-1164109; Score: 0.56
DE  Interaction: Q9Y224; IntAct: EBI-1164152; Score: 0.73
DE  Interaction: A0A2B6C7W6; IntAct: EBI-2811250; Score: 0.00
DE  Interaction: A0A3Q0PRD7; IntAct: EBI-2817447; Score: 0.00
DE  Interaction: Q81VT8; IntAct: EBI-2817440; Score: 0.00
DE  Interaction: A0A6L8P1C8; IntAct: EBI-2836006; Score: 0.00
DE  Interaction: P60520; IntAct: EBI-3046676; Score: 0.35
DE  Interaction: P31343; IntAct: EBI-5452624; Score: 0.58
DE  Interaction: P24928; IntAct: EBI-6050476; Score: 0.40
DE  Interaction: Q1K9H5; IntAct: EBI-6050645; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-6050645; Score: 0.43
DE  Interaction: Q1I2B2; IntAct: EBI-6050645; Score: 0.35
DE  Interaction: P98078; IntAct: EBI-6100356; Score: 0.35
DE  Interaction: O56264; IntAct: EBI-6157161; Score: 0.35
DE  Interaction: P12792; IntAct: EBI-6159029; Score: 0.35
DE  Interaction: D1LN35; IntAct: EBI-6159328; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21323857; Score: 0.35
DE  Interaction: Q96GG9; IntAct: EBI-21325177; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-21327757; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q93034; IntAct: EBI-21331078; Score: 0.35
DE  Interaction: Q8NCA5; IntAct: EBI-10269246; Score: 0.81
DE  Interaction: O60307; IntAct: EBI-10103761; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: Q96FV9; IntAct: EBI-11034504; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: Q8R050; IntAct: EBI-11056816; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: O00567; IntAct: EBI-11069711; Score: 0.35
DE  Interaction: P43243; IntAct: EBI-11071398; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-11088773; Score: 0.35
DE  Interaction: P25206; IntAct: EBI-11097548; Score: 0.35
DE  Interaction: Q8CCJ3; IntAct: EBI-11104920; Score: 0.35
DE  Interaction: Q67020; IntAct: EBI-11514481; Score: 0.57
DE  Interaction: P03433; IntAct: EBI-11514611; Score: 0.37
DE  Interaction: Q9UIG4; IntAct: EBI-24776957; Score: 0.56
DE  Interaction: Q194T2; IntAct: EBI-12587457; Score: 0.35
DE  Interaction: P46531; IntAct: EBI-13915571; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.35
DE  Interaction: Q7KZN9; IntAct: EBI-20304305; Score: 0.35
DE  Interaction: P09622; IntAct: EBI-20304669; Score: 0.35
DE  Interaction: O00429; IntAct: EBI-20305770; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: Q9Y2H1; IntAct: EBI-20624829; Score: 0.27
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: Q9BVC5; IntAct: EBI-20916280; Score: 0.40
DE  Interaction: Q52LJ0; IntAct: EBI-20924042; Score: 0.56
DE  Interaction: Q92499; IntAct: EBI-20924034; Score: 0.64
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: O96013; IntAct: EBI-26962273; Score: 0.35
DE  Interaction: Q9Y586; IntAct: EBI-21261050; Score: 0.35
DE  Interaction: Q9Y3I0; IntAct: EBI-21264222; Score: 0.68
DE  Interaction: P35637; IntAct: EBI-21208916; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: A0A024R136; IntAct: EBI-25411916; Score: 0.35
DE  Interaction: A0A0H3L6J6; IntAct: EBI-25401190; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P15884; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: Q9BWW4; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: Q9NQ29; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: Q9H1R3; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: P28288; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: Q92804; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: P51572; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: Q9NVH1; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: Q08378; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: Q17RN3; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: P62979; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: Q9H0W5; IntAct: EBI-26615064; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-26994159; Score: 0.53
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27111302; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: Q9BVS4; IntAct: EBI-28944998; Score: 0.35
DE  Interaction: P15130; IntAct: EBI-27131516; Score: 0.35
DE  Interaction: Q0ZME3; IntAct: EBI-27131755; Score: 0.35
DE  Interaction: Q6Q1R8; IntAct: EBI-27132003; Score: 0.35
DE  Interaction: K9N4V7; IntAct: EBI-27132270; Score: 0.35
DE  Interaction: P33469; IntAct: EBI-27132272; Score: 0.35
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0072669;
GO  GO:0042802;
GO  GO:0003723;
GO  GO:0000993;
GO  GO:0006469;
GO  GO:0045944;
GO  GO:0050658;
GO  GO:0006388;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRRKLTALDYHNPAGFNCKDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIHSSDWPKFFEKYLRDVNCPFKIQDRQEAI
SQ  DWLLGLAVRLEYGDNAEKYKDLVPDNSKTADNATKNAEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLVMLKAIRILV
SQ  QERLTQDAVAKANQTKEGLPVALDKHILGFDTGDAVLNEAAQILRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLG
SQ  KVGR
//
ID  Q9CQE8;
PN  RNA transcription, translation and transport factor protein;
GN  RTRAF;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y224}. Note=May localize at the centrosome during mitosis. Shuttles between the cytosol and the nucleus: enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9CQE8;
DR  Pfam: PF10036;
DE  Function: RNA-binding protein involved in modulation of mRNA transcription by Polymerase II. Component of the tRNA-splicing ligase complex and is required for tRNA ligation. May be required for RNA transport. {ECO:0000250|UniProtKB:Q9Y224}.
DE  Reference Proteome: Yes;
DE  Interaction: P62158; IntAct: EBI-911456; Score: 0.35
DE  Interaction: Q923J1; IntAct: EBI-9661302; Score: 0.35
DE  Interaction: P14094; IntAct: EBI-20566937; Score: 0.35
DE  Interaction: P07602; IntAct: EBI-21347829; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26472137; Score: 0.35
DE  Interaction: Q8VI24; IntAct: EBI-26885060; Score: 0.35
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0072669;
GO  GO:0042802;
GO  GO:0003723;
GO  GO:0000993;
GO  GO:0006469;
GO  GO:0045944;
GO  GO:0006388;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRRKLTALDYHNPSGFNCKDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIHSSDWPKFFEKYLKDVNCPFKIQDRQEAI
SQ  DWLLGLAVRLEYGDNAEKYKDLVPDNRKNTDNAAKNAEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLVMLKAIRILV
SQ  QERLTQDAVAKANQTKEGLPVALEKHILGFDTGDAVLNEAAQILRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLG
SQ  KVGR
//
ID  Q5R8I2;
PN  RNA transcription, translation and transport factor protein;
GN  RTRAF;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y224}. Note=May localize at the centrosome during mitosis. Shuttles between the cytosol and the nucleus: enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low. {ECO:0000250|UniProtKB:Q9Y224}.
DR  UNIPROT: Q5R8I2;
DR  Pfam: PF10036;
DE  Function: RNA-binding protein involved in modulation of mRNA transcription by Polymerase II. Component of the tRNA-splicing ligase complex and is required for tRNA ligation. May be required for RNA transport. {ECO:0000250|UniProtKB:Q9Y224}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0072669;
GO  GO:0042802;
GO  GO:0003723;
GO  GO:0000993;
GO  GO:0006469;
GO  GO:0045944;
GO  GO:0006388;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRRKLTALDYHNPAGFNCKDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIHSSDWPKFFEKYLRDVNCPFKIQDRQEAI
SQ  DWLLGLAVRLEYGDNAEKYKDLVPDNSKTADNATKNAEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLVMLKAIRILV
SQ  QERLTQDAVAKANQTKEGLPVALDKHILGFDTGDAVLNEAAQILRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLG
SQ  KVGR
//
ID  Q63ZS0;
PN  RNA transcription, translation and transport factor protein;
GN  rtraf;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y224}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y224}. Note=Shuttles between the cytosol and the nucleus. {ECO:0000250|UniProtKB:Q9Y224}.
DR  UNIPROT: Q63ZS0;
DR  Pfam: PF10036;
DE  Function: RNA-binding protein involved in modulation of mRNA transcription by Polymerase II. Component of the tRNA-splicing ligase complex. {ECO:0000250|UniProtKB:Q9Y224}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6P5F9; IntAct: EBI-11606853; Score: 0.35
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0072686;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0072669;
GO  GO:0003723;
GO  GO:0000993;
GO  GO:0006469;
GO  GO:0045944;
GO  GO:0006388;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRRKLQALDYHNPAGFNFKDETEFRNFLVWLEDQKIRHYKIEERGNLRNIHSSEWPAQYEKYLNDVNCPFKVQERQESI
SQ  DWLLGLAVRLEYGDNAAKYQNAKPYNSDVSKSAEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLMMLKAIRILVQERL
SQ  SQEAVAKSNSAKEGLPVALDKHILGFDTGDAVLNDAARILRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLGKVGR
//
ID  P60123;
PN  RuvB-like 1;
GN  Ruvbl1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9Y265}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y265}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y265}. Membrane {ECO:0000250|UniProtKB:Q9Y265}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y265}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q9DE26}. Note=Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol, although it is also present in the cytoplasm and associated with the cell membranes. In prophase and prometaphase it is located at the centrosome and the branching microtubule spindles. After mitotic nuclear membrane disintigration it accumulates at the centrosome and sites of tubulin polymerization. As cells pass through metaphase and into telophase it is located close to the centrosome at the early phase of tubulin polymerization. In anaphase it accumulates at the zone of tubule interdigitation. In telophase it is found at polar tubule overlap, and it reappears at the site of chromosomal decondensation in the daughter cells. {ECO:0000250|UniProtKB:Q9Y265}.
DR  UNIPROT: P60123;
DR  UNIPROT: O35753;
DR  Pfam: PF06068;
DR  Pfam: PF17856;
DE  Function: Possesses single-stranded DNA-stimulated ATPase and ATP- dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring- like structure contribute to the ATPase activity (By similarity). Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (By similarity). This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription (By similarity). This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (By similarity). The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400 (By similarity). NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage (By similarity). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (By similarity). Proposed core component of the chromatin remodeling INO80 complex which exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP- dependent nucleosome sliding (By similarity). Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex (By similarity). Essential for cell proliferation (By similarity). May be able to bind plasminogen at cell surface and enhance plasminogen activation (By similarity). {ECO:0000250|UniProtKB:Q9Y265}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P21708; IntAct: EBI-7624936; Score: 0.35
DE  Interaction: Q01728; IntAct: EBI-16423604; Score: 0.46
GO  GO:0101031;
GO  GO:0120293;
GO  GO:0031011;
GO  GO:0005815;
GO  GO:0071339;
GO  GO:0035267;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0000786;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0097255;
GO  GO:1990904;
GO  GO:1990062;
GO  GO:0000812;
GO  GO:0043138;
GO  GO:0043531;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0051117;
GO  GO:0003678;
GO  GO:0017025;
GO  GO:0001094;
GO  GO:0003713;
GO  GO:0000492;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0006338;
GO  GO:0006310;
GO  GO:0006281;
GO  GO:0016573;
GO  GO:0043968;
GO  GO:0043967;
GO  GO:0090263;
GO  GO:0045739;
GO  GO:0045893;
GO  GO:1905168;
GO  GO:0010756;
GO  GO:1904507;
GO  GO:0051726;
GO  GO:0033044;
GO  GO:0006282;
GO  GO:0006275;
GO  GO:0060382;
GO  GO:0045995;
GO  GO:2000269;
GO  GO:0006357;
GO  GO:0000723;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKIEEVKSTTKTQRIASHSHVKGLGLDESGLAKQAASGLVGQENAREACGVIVELIKSKKMAGRAVLLAGPPGTGKTALA
SQ  LAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFRRAIGLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIG
SQ  LKTAKGTKQLKLDPSIFESLQKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHKKKEIIQDVTL
SQ  HDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGVAELVPGVLFVDEVHMLDIECFTYLHRALE
SQ  SSIAPIVIFASNRGNCVIRGTEDITSPHGIPLDLLDRVMIIRTMLYTPQEMKQIIKIRAQTEGINISEEALNHLGEIGTK
SQ  TTLRYSVQLLTPANLLAKINGKDSIEKEHVEEISELFYDAKSSAKILADQQDKYMK
//
ID  O77691;
PN  Protein S100-A6;
GN  S100A6;
OS  9796;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
DR  UNIPROT: O77691;
DR  Pfam: PF01023;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS00303;
DE  Function: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001726;
GO  GO:0005509;
GO  GO:0048306;
GO  GO:0042803;
GO  GO:0044548;
GO  GO:0005523;
GO  GO:0008270;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MACPLDQAISLLVAIFHKYSSREGDKNTLSKGELKELIQKELTIGAELEDSEIAKLLDDLDQNKDQVVNFQEYVTFLGAL
SQ  AMIYNEVLKACS
//
ID  P06703;
PN  Protein S100-A6;
GN  S100A6;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
DR  UNIPROT: P06703;
DR  UNIPROT: D3DV39;
DR  UNIPROT: Q5RHS4;
DR  PDB: 1K8U;
DR  PDB: 1K96;
DR  PDB: 1K9K;
DR  PDB: 1K9P;
DR  PDB: 2M1K;
DR  PDB: 4YBH;
DR  Pfam: PF01023;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS00303;
DR  OMIM: 114110;
DR  DisGeNET: 6277;
DE  Function: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative. {ECO:0000269|PubMed:22399290}.
DE  Reference Proteome: Yes;
DE  Interaction: P03246; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P62993; IntAct: EBI-350217; Score: 0.35
DE  Interaction: P04271; IntAct: EBI-945511; Score: 0.65
DE  Interaction: P06703; IntAct: EBI-945542; Score: 0.37
DE  Interaction: P63104; IntAct: EBI-7198215; Score: 0.40
DE  Interaction: P26882; IntAct: EBI-7835180; Score: 0.59
DE  Interaction: Q02790; IntAct: EBI-7835253; Score: 0.59
DE  Interaction: Q00987; IntAct: EBI-8045742; Score: 0.56
DE  Interaction: P04637; IntAct: EBI-8045854; Score: 0.68
DE  Interaction: P52292; IntAct: EBI-8468931; Score: 0.61
DE  Interaction: Q3SYU7; IntAct: EBI-8469041; Score: 0.40
DE  Interaction: P52293; IntAct: EBI-8469341; Score: 0.40
DE  Interaction: P50542; IntAct: EBI-10194898; Score: 0.56
DE  Interaction: P0CK49; IntAct: EBI-11725356; Score: 0.35
DE  Interaction: Q2MG95; IntAct: EBI-11733653; Score: 0.35
DE  Interaction: P33215; IntAct: EBI-10993316; Score: 0.35
DE  Interaction: Q92544; IntAct: EBI-11126692; Score: 0.35
DE  Interaction: P26447; IntAct: EBI-11158347; Score: 0.35
DE  Interaction: O95619; IntAct: EBI-11158562; Score: 0.35
DE  Interaction: B3EWG5; IntAct: EBI-24644742; Score: 0.56
DE  Interaction: P61960; IntAct: EBI-21833372; Score: 0.40
DE  Interaction: Q9BUK0; IntAct: EBI-21833385; Score: 0.40
DE  Interaction: Q9NQG1; IntAct: EBI-21833398; Score: 0.35
DE  Interaction: Q9UPU7; IntAct: EBI-21833417; Score: 0.40
DE  Interaction: P27824; IntAct: EBI-16789225; Score: 0.27
DE  Interaction: P68431; IntAct: EBI-16793802; Score: 0.27
DE  Interaction: Q9BWW4; IntAct: EBI-21265722; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: Q99963; IntAct: EBI-25376320; Score: 0.35
DE  Interaction: P29353; IntAct: EBI-25380474; Score: 0.35
DE  Interaction: P30086; IntAct: EBI-25381702; Score: 0.35
DE  Interaction: P15531; IntAct: EBI-25393623; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-25400636; Score: 0.54
DE  Interaction: P32418; IntAct: EBI-25402569; Score: 0.44
DE  Interaction: Q9HB71; IntAct: EBI-25403594; Score: 0.54
DE  Interaction: Q96NB1; IntAct: EBI-25403823; Score: 0.40
DE  Interaction: Q8TD43; IntAct: EBI-25404225; Score: 0.54
DE  Interaction: Q15418; IntAct: EBI-25404661; Score: 0.44
DE  Interaction: Q9BUB5; IntAct: EBI-25404957; Score: 0.40
DE  Interaction: O95684; IntAct: EBI-25405095; Score: 0.54
DE  Interaction: P0DOF2; IntAct: EBI-25607852; Score: 0.35
DE  Interaction: P83105; IntAct: EBI-25745135; Score: 0.46
DE  Interaction: P60033; IntAct: EBI-25645944; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005576;
GO  GO:0031234;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001726;
GO  GO:0005509;
GO  GO:0048306;
GO  GO:0015075;
GO  GO:0042803;
GO  GO:0044548;
GO  GO:0005523;
GO  GO:0008270;
GO  GO:0007409;
GO  GO:0048146;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MACPLDQAIGLLVAIFHKYSGREGDKHTLSKKELKELIQKELTIGSKLQDAEIARLMEDLDRNKDQEVNFQEYVTFLGAL
SQ  ALIYNEALKG
//
ID  P14069;
PN  Protein S100-A6;
GN  S100a6;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
DR  UNIPROT: P14069;
DR  PDB: 4P2Y;
DR  Pfam: PF01023;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS00303;
DE  Function: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P30416; IntAct: EBI-7835551; Score: 0.35
DE  Interaction: Q08752; IntAct: EBI-7835551; Score: 0.35
DE  Interaction: Q9CXW3; IntAct: EBI-6478783; Score: 0.65
DE  Interaction: A0A0F6B423; IntAct: EBI-13953902; Score: 0.35
GO  GO:0062023;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001726;
GO  GO:0005509;
GO  GO:0048306;
GO  GO:0015075;
GO  GO:0042803;
GO  GO:0044548;
GO  GO:0005523;
GO  GO:0008270;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MACPLDQAIGLLVAIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIARLMDDLDRNKDQEVNFQEYVAFLGAL
SQ  ALIYNEALK
//
ID  Q2EN75;
PN  Protein S100-A6;
GN  S100A6;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
DR  UNIPROT: Q2EN75;
DR  Pfam: PF01023;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS00303;
DE  Function: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005509;
GO  GO:0098586;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MACPLDQAIGLLVAIFHKYSGQEGDKNTLSKSELKELIQKELTIGAKLQDAEIAKLMDDLDRNKDQVVNFQEYVTFLGAL
SQ  AMIYNDVLRG
//
ID  P30801;
PN  Protein S100-A6;
GN  S100A6;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
DR  UNIPROT: P30801;
DR  PDB: 1A03;
DR  PDB: 1CNP;
DR  PDB: 1JWD;
DR  PDB: 2CNP;
DR  PDB: 2JTT;
DR  Pfam: PF01023;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS00303;
DE  Function: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0005635;
GO  GO:0005509;
GO  GO:0047485;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGAL
SQ  AMIYNEALKG
//
ID  P05964;
PN  Protein S100-A6;
GN  S100a6;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
DR  UNIPROT: P05964;
DR  UNIPROT: Q9R2B7;
DR  Pfam: PF01023;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DR  PROSITE: PS00303;
DE  Function: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P61980; IntAct: EBI-931365; Score: 0.35
DE  Interaction: Q9BQB4; IntAct: EBI-5746499; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001726;
GO  GO:0005509;
GO  GO:0048306;
GO  GO:0015075;
GO  GO:0042803;
GO  GO:0044548;
GO  GO:0005523;
GO  GO:0008270;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MACPLDQAIGLLVAIFHKYSGKEGDKHTLSKKELKELIQKELTIGAKLQDAEIARLMDDLDRNKDQEVNFQEYVAFLGAL
SQ  ALIYNEALK
//
ID  Q14542;
PN  Equilibrative nucleoside transporter 2;
GN  SLC29A2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Basolateral cell membrane {ECO:0000269|PubMed:12527552}; Multi-pass membrane protein {ECO:0000269|PubMed:12527552}. Nucleus membrane {ECO:0000269|PubMed:12527552}; Multi-pass membrane protein {ECO:0000269|PubMed:12527552}. Note=Localized at the basolateral cell membrane in polarized MDCK cells.
DR  UNIPROT: Q14542;
DR  UNIPROT: B3KPY7;
DR  UNIPROT: O43530;
DR  UNIPROT: Q52M84;
DR  UNIPROT: Q96R00;
DR  UNIPROT: Q9UPE0;
DR  Pfam: PF01733;
DR  OMIM: 602110;
DR  DisGeNET: 3177;
DE  Function: Mediates equilibrative transport of purine, pyrimidine nucleosides and the purine base hypoxanthine. Very less sensitive than SLC29A1 to inhibition by nitrobenzylthioinosine (NBMPR), dipyridamole, dilazep and draflazine. {ECO:0000269|PubMed:9396714}.
DE  Reference Proteome: Yes;
DE  Interaction: O43889; IntAct: EBI-8649617; Score: 0.37
DE  Interaction: P60033; IntAct: EBI-25645944; Score: 0.35
GO  GO:0016323;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0005326;
GO  GO:0005337;
GO  GO:0015211;
GO  GO:0015213;
GO  GO:0015853;
GO  GO:0032238;
GO  GO:0032869;
GO  GO:0015854;
GO  GO:0035344;
GO  GO:0007595;
GO  GO:0098810;
GO  GO:0006836;
GO  GO:0001504;
GO  GO:1901642;
GO  GO:0015858;
GO  GO:0015860;
GO  GO:0072531;
GO  GO:0035364;
GO  GO:0150104;
GO  GO:0015862;
GO  GO:0006855;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARGDAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQARLAGAGNSTARILSTNHTGPEDAFNFNNWVTLLSQLPLL
SQ  LFTLLNSFLYQCVPETVRILGSLLAILLLFALTAALVKVDMSPGPFFSITMASVCFINSFSAVLQGSLFGQLGTMPSTYS
SQ  TLFLSGQGLAGIFAALAMLLSMASGVDAETSALGYFITPCVGILMSIVCYLSLPHLKFARYYLANKSSQAQAQELETKAE
SQ  LLQSDENGIPSSPQKVALTLDLDLEKEPESEPDEPQKPGKPSVFTVFQKIWLTALCLVLVFTVTLSVFPAITAMVTSSTS
SQ  PGKWSQFFNPICCFLLFNIMDWLGRSLTSYFLWPDEDSRLLPLLVCLRFLFVPLFMLCHVPQRSRLPILFPQDAYFITFM
SQ  LLFAVSNGYLVSLTMCLAPRQVLPHEREVAGALMTFFLALGLSCGASLSFLFKALL
//
ID  Q61672;
PN  Equilibrative nucleoside transporter 2;
GN  Slc29a2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Multi-pass membrane protein. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q61672;
DR  UNIPROT: Q9JIT8;
DR  Pfam: PF01733;
DE  Function: Mediates equilibrative transport of purine and pyrimidine nucleosides, and the purine base hypoxanthine.
DE  Reference Proteome: Yes;
GO  GO:0016323;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0005326;
GO  GO:0005337;
GO  GO:0015211;
GO  GO:0015213;
GO  GO:0015853;
GO  GO:0032238;
GO  GO:0032869;
GO  GO:0015854;
GO  GO:0035344;
GO  GO:0007595;
GO  GO:0098810;
GO  GO:0006836;
GO  GO:0001504;
GO  GO:1901642;
GO  GO:0015858;
GO  GO:0015860;
GO  GO:0072531;
GO  GO:0035364;
GO  GO:0015862;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARGNAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQGRLAGTNSSAETMGTNHTSPTDTFNFNNWVTLLSQLPLLL
SQ  FTLLNSFLYQCIPESVRILGSLLAILLLFALTAALVKVDLSPGLFFSVTMASVWFINSFCAVLQGSLFGQLGTMPSTYST
SQ  LFLSGQGLAGIFAALAMLMSLASGVDAQTSALGYFITPCVGILLSIVCYLSLPHLKFARYYLTEKLSQAPTQELETKAEL
SQ  LQADEKNGVPISPQQASPTLDLDPEKEPEPEEPQKPGKPSVFVVFRKIWLTALCLVLVFTVTLSVFPAITAMVTTSSNSP
SQ  GKWGLFFNPICCFLLFNVMDWLGRSLTSYFLWPDEDSQQLLPLLVCLRFLFVPLFMLCHVPQHARLPIIFRQDAYFITFM
SQ  LLFAVSNGYLVSLTMCLAPRQVLPHEREVAGALMTFFLALGLSCGASLSFLFKALL
//
ID  Q9NQ40;
PN  Solute carrier family 52, riboflavin transporter, member 3;
GN  SLC52A3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Apical cell membrane {ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:21512156, ECO:0000269|PubMed:24264046}; Multi-pass membrane protein {ECO:0000269|PubMed:20463145}. Cell membrane {ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:27702554}. [Isoform 1]: Cell membrane {ECO:0000269|PubMed:29428966}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:29428966}; Multi- pass membrane protein. Cytoplasm {ECO:0000269|PubMed:29428966}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:29428966}.
DR  UNIPROT: Q9NQ40;
DR  UNIPROT: A0A2I6BQ49;
DR  UNIPROT: A8K6P1;
DR  UNIPROT: K0A6P4;
DR  UNIPROT: Q5W1A0;
DR  UNIPROT: Q5W1A1;
DR  UNIPROT: Q8NCL7;
DR  UNIPROT: Q96GD5;
DR  Pfam: PF06237;
DR  OMIM: 211500;
DR  OMIM: 211530;
DR  OMIM: 613350;
DR  DisGeNET: 113278;
DE  Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism (PubMed:20463145, PubMed:22273710, PubMed:24264046, PubMed:27702554). Humans are unable to synthesize vitamin B2/riboflavin and must obtain it via intestinal absorption (PubMed:20463145). {ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:24264046, ECO:0000269|PubMed:27702554, ECO:0000303|PubMed:20463145}.
DE  Disease: Brown-Vialetto-Van Laere syndrome 1 (BVVLS1) [MIM:211530]: A rare neurologic disorder characterized by sensorineural hearing loss and a variety of cranial nerve palsies, which develop over a relatively short period of time in a previously healthy individual. Sensorineural hearing loss may precede the neurological signs. The course is invariably progressive, but the rate of decline is variable within and between families. With disease evolution, long tract signs, lower motor neuron signs, cerebellar ataxia and lower cranial nerve (III-VI) palsies develop, giving rise to a complex picture resembling amyotrophic lateral sclerosis. Diaphragmatic weakness and respiratory compromise are some of the most distressing features, leading to recurrent chest infections and respiratory failure, which are often the cause of patients' demise. {ECO:0000269|PubMed:20206331, ECO:0000269|PubMed:20920669, ECO:0000269|PubMed:21110228, ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:22633641, ECO:0000269|PubMed:22718020, ECO:0000269|PubMed:22824638, ECO:0000269|PubMed:27702554}. Note=The disease is caused by variants affecting the gene represented in this entry. Fazio-Londe disease (FALOND) [MIM:211500]: A rare neurological disease characterized by progressive weakness of the muscles innervated by cranial nerves of the lower brain stem. It may present in childhood with severe neurological deterioration with hypotonia, respiratory insufficiency leading to premature death, or later in life with bulbar weakness which progresses to involve motor neurons throughout the neuroaxis. Clinical manifestations include dysarthria, dysphagia, facial weakness, tongue weakness, and fasciculations of the tongue and facial muscles. {ECO:0000269|PubMed:21110228}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O14656; IntAct: EBI-25847442; Score: 0.56
DE  Interaction: P50570; IntAct: EBI-25845313; Score: 0.56
DE  Interaction: P54252; IntAct: EBI-25974800; Score: 0.56
GO  GO:0016324;
GO  GO:0005737;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0032217;
GO  GO:0034605;
GO  GO:0006771;
GO  GO:0032218;
GO  GO:0007605;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAFLMHLLVCVFGMGSWVTINGLWVELPLLVMELPEGWYLPSYLTVVIQLANIGPLLVTLLHHFRPSCLSEVPIIFTLLG
SQ  VGTVTCIIFAFLWNMTSWVLDGHHSIAFLVLTFFLALVDCTSSVTFLPFMSRLPTYYLTTFFVGEGLSGLLPALVALAQG
SQ  SGLTTCVNVTEISDSVPSPVPTRETDIAQGVPRALVSALPGMEAPLSHLESRYLPAHFSPLVFFLLLSIMMACCLVAFFV
SQ  LQRQPRCWEASVEDLLNDQVTLHSIRPREENDLGPAGTVDSSQGQGYLEEKAAPCCPAHLAFIYTLVAFVNALTNGMLPS
SQ  VQTYSCLSYGPVAYHLAATLSIVANPLASLVSMFLPNRSLLFLGVLSVLGTCFGGYNMAMAVMSPCPLLQGHWGGEVLIV
SQ  ASWVLFSGCLSYVKVMLGVVLRDLSRSALLWCGAAVQLGSLLGALLMFPLVNVLRLFSSADFCNLHCPA
//
ID  O74889;
PN  SAC3 family protein 1;
GN  SPCC576;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O74889;
DR  Pfam: PF03399;
DR  PROSITE: PS50250;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0006406;
GO  GO:0006611;
GO  GO:0042274;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEKRNETGNNRLKRSNNRGKSKKDWKDASVETTPRETSVDEDNTSVFEDVEAQDSRQKRFSSTLEGNRFEELRSLREKER
SQ  EVAIQNGLIDDPTKPRQLDEAVTFVGTCPDMCPEYEREQREYQNNLERWEINPETGRVDKNLAVKAFHRPAAGNEQALPS
SQ  DVRPPPVLKKSLDYLVDKIVCGPDPLENTHFFVRDRTRSIRQDFTLQNCRDLDAVACHERIARYHILCIHQLCEKKQFSA
SQ  QQEVEQLRKGILQSLCEFYDDLRKVKIRCPNEPEFRSYAIITHLRDPDVVRQSQILPIEIFDDQRVQLALRLSALAQKNN
SQ  ERVGHILPRNTEACPNLYTRFFKLVQSPAVTYLMACLLESHFMSIRKGALKAMRKAFMSAHANFPCGDLKRILHFDTVEQ
SQ  AASFSRYYGLEVSDDNGELSINLNKTAFFNDSKPDFRQLFSQTLVESKLQNRSFADIINGSRYNIDRVSPNTAFSTNIPL
SQ  SLPFANKEPQPIAGFKKNTPETSVVSKNLSTFNGKFNVNAPVFTPRSFPTKPFSATDISSVQPTNLPNGSTNGTETFIPP
SQ  VQNSITSNKEAVKPIKNKPKPISFESLSAVGNLIISDSLSRIVRQILQNLYTEWVHEKTNLVFATMFRTIFREVLLDGIA
SQ  SEVYLKSLKKHAISQISVRAHHSWVKKQEKMMLEMREKNRQEKYFSVLNSVVKAESSNITRLPIKRTFYGDTRNLDKASE
SQ  KLRAEHDRTRRLWKPVLMDSLFSNLQKFPVYEDWHLLIFNASTSSMMKTWLCAKFSLKETNKTSFWHSSYNLFNRQYHVD
SQ  MPDNVSDLPQTRLCYGACVYNVGLLDEEKRKDLANSDLNSSPKLIQGNDSRSAHESSANKLFSFVHDISRLTITKLPLLL
SQ  IFWSDSNLDMQGITQKYRFLELITSTWSAISSIHVLTITNDRDMDLEHSLKVLLDNVTVEKSPFAQLEELEVVRKKREAE
SQ  IEASSKTVKRLASNNKFLTDSNVEGLLEAPTSLENSLVEDDKWASLRQKIKAARDLLKKVETFY
//
ID  P46674;
PN  Nuclear mRNA export protein SAC3;
GN  SAC3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:14562095}. Note=Localizes to the nuclear pores.
DR  UNIPROT: P46674;
DR  UNIPROT: D6VSD9;
DR  PDB: 3FWB;
DR  PDB: 3FWC;
DR  PDB: 3T5V;
DR  PDB: 4C31;
DR  PDB: 4MBE;
DR  PDB: 4TRQ;
DR  PDB: 5G5P;
DR  PDB: 5L3T;
DR  Pfam: PF12209;
DR  Pfam: PF03399;
DR  PROSITE: PS50250;
DE  Function: Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. {ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:12702719}.
DE  Reference Proteome: Yes;
DE  Interaction: P06704; IntAct: EBI-7945717; Score: 0.77
DE  Interaction: P20676; IntAct: EBI-2124372; Score: 0.40
DE  Interaction: P25491; IntAct: EBI-3766328; Score: 0.35
DE  Interaction: P40073; IntAct: EBI-601163; Score: 0.37
DE  Interaction: Q08231; IntAct: EBI-797734; Score: 0.88
DE  Interaction: P50101; IntAct: EBI-7110957; Score: 0.40
DE  Interaction: P13517; IntAct: EBI-7228158; Score: 0.40
DE  Interaction: Q04062; IntAct: EBI-7650434; Score: 0.40
DE  Interaction: P39010; IntAct: EBI-7897739; Score: 0.44
DE  Interaction: Q6WNK7; IntAct: EBI-1370393; Score: 0.82
DE  Interaction: Q99257; IntAct: EBI-2124319; Score: 0.50
DE  Interaction: P34232; IntAct: EBI-2124319; Score: 0.40
DE  Interaction: Q07478; IntAct: EBI-2124381; Score: 0.40
DE  Interaction: P38811; IntAct: EBI-2213151; Score: 0.40
DE  Interaction: P35177; IntAct: EBI-2213151; Score: 0.40
DE  Interaction: Q06410; IntAct: EBI-2345986; Score: 0.37
DE  Interaction: Q06677; IntAct: EBI-3758909; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3773334; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3783327; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3788346; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3791492; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3801253; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3807444; Score: 0.35
DE  Interaction: P47079; IntAct: EBI-3824057; Score: 0.35
DE  Interaction: P38129; IntAct: EBI-4389629; Score: 0.35
DE  Interaction: Q05027; IntAct: EBI-4391019; Score: 0.35
DE  Interaction: O94742; IntAct: EBI-15970376; Score: 0.61
GO  GO:0005737;
GO  GO:0044614;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0060090;
GO  GO:0030029;
GO  GO:0000278;
GO  GO:0031124;
GO  GO:0006406;
GO  GO:0071028;
GO  GO:0045944;
GO  GO:0000973;
GO  GO:0006611;
GO  GO:0042274;
GO  GO:0006283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNTSFGSVVPSTNFNFFKGHGNNDNTSANSTVNNSNFFLNSNETKPSKNVFMVHSTSQKKSQQPLQNLSHSPSYTENKPD
SQ  KKKKYMINDAKTIQLVGPLISSPDNLGFQKRSHKARELPRFLINQEPQLEKRAFVQDPWDKANQEKMISLEESIDDLNEL
SQ  YETLKKMRNTERSIMEEKGLVDKADSAKDLYDAIVFQGTCLDMCPTFERSRRNVEYTVYSYEKNQPNDKKASRTKALKVF
SQ  ARPAAAAAPPLPSDVRPPHILVKTLDYIVDNLLTTLPESEGFLWDRMRSIRQDFTYQNYSGPEAVDCNERIVRIHLLILH
SQ  IMVKSNVEFSLQQELEQLHKSLITLSEIYDDVRSSGGTCPNEAEFRAYALLSKIRDPQYDENIQRLPKHIFQDKLVQMAL
SQ  CFRRVISNSAYTERGFVKTENCLNFYARFFQLMQSPSLPLLMGFFLQMHLTDIRFYALRALSHTLNKKHKPIPFIYLENM
SQ  LLFNNRQEIIEFCNYYSIEIINGDAADLKTLQHYSHKLSETQPLKKTYLTCLERRLQKTTYKGLINGGEDNLASSVYVKD
SQ  PKKDRIPSIADQSFLMENFQNNYNEKLNQNSSVKPQINTSPKRVATRPNHFPFSQESKQLPQISQSHTLSTNPLLTPQVH
SQ  GDLSEQKQQQIKTVTDGGSPFVFDQSAQNSTVEASKAHMISTTSNGAYDEKLSSEQEEMRKKEEQRIEEEKTQLKKKQEN
SQ  ADKQVITEQIANDLVKEVVNSSVISIVKREFSEANYRKDFIDTMTRELYDAFLHERLYLIYMDSRAELKRNSTLKKKFFE
SQ  KWQASYSQAKKNRILEEKKREEIKLVSHQLGVPGFKKSTCLFRTPYKGNVNSSFMLSSSDKNLIFSPVNDEFNKFATHLT
SQ  KISKLWRPLEMQSIYYDNLTKKFPSNSLTPANLFIYAKDWTSLSNRWILSKFNLQTAQDSKKFSNNIISSRIICIDDEYE
SQ  PSDFSDLQLLIFNTGVTNPDIFDLEMKLKDDGEELIKLITGISLNTNICFSLLIIYWESAENTLSESTIKHLLKLNRISK
SQ  NYSSVIERIDLMNLTEESPHKCLEDKLSEISHSYVYKLTERGKYDKTLRQKRSLAGIHSRSTQLQTTKDIDQKMKKMLEK
SQ  EKNKYQQQIGERNTYAHLESHIDASPRSKKRKLPILLSTSHSSQFKTPLASRLNTSGSSTSPPLPSHLAMKFRKNSRVTS
SQ  LHTVLPVSTPSHSNNIPAASFSGNNTTDIQSQQLIENQKSTSVYLNNVSERILGNQEICQTPINPVTPVLDGADQGKEDI
SQ  PDSILELKILIDSVKKKVNND
//
ID  Q09825;
PN  Spindle pole body-associated protein sad1;
GN  sad1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus membrane; Single-pass membrane protein.
DR  UNIPROT: Q09825;
DR  UNIPROT: Q9UU40;
DR  PDB: 6A6W;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Associates with the spindle pole body and maintains a functional interface between the nuclear membrane and the microtubule motor proteins. Involved in chromosome segregation during meiosis where it associates with the telomeres. {ECO:0000269|PubMed:16615890}.
DE  Reference Proteome: Yes;
DE  Interaction: O13712; IntAct: EBI-1557581; Score: 0.55
DE  Interaction: O74446; IntAct: EBI-1557543; Score: 0.37
DE  Interaction: Q92358; IntAct: EBI-929742; Score: 0.46
DE  Interaction: Q9US52; IntAct: EBI-929836; Score: 0.32
DE  Interaction: Q9UU83; IntAct: EBI-1542573; Score: 0.37
DE  Interaction: P87245; IntAct: EBI-1557414; Score: 0.55
DE  Interaction: O13802; IntAct: EBI-1557451; Score: 0.37
DE  Interaction: Q9USK8; IntAct: EBI-1557455; Score: 0.37
DE  Interaction: O13779; IntAct: EBI-1557461; Score: 0.37
DE  Interaction: O74388; IntAct: EBI-1557470; Score: 0.37
DE  Interaction: O60187; IntAct: EBI-1557475; Score: 0.37
DE  Interaction: O42914; IntAct: EBI-1557484; Score: 0.37
DE  Interaction: O94531; IntAct: EBI-1557488; Score: 0.37
DE  Interaction: O43087; IntAct: EBI-1557492; Score: 0.37
DE  Interaction: O59678; IntAct: EBI-1557498; Score: 0.37
DE  Interaction: Q9HFE5; IntAct: EBI-1557503; Score: 0.37
DE  Interaction: Q9USM3; IntAct: EBI-1557507; Score: 0.37
DE  Interaction: Q09874; IntAct: EBI-1557511; Score: 0.37
DE  Interaction: Q09877; IntAct: EBI-1557515; Score: 0.37
DE  Interaction: O94486; IntAct: EBI-1557520; Score: 0.37
DE  Interaction: P87128; IntAct: EBI-1557524; Score: 0.37
DE  Interaction: O74843; IntAct: EBI-1557528; Score: 0.37
DE  Interaction: P87074; IntAct: EBI-1557547; Score: 0.37
DE  Interaction: P78820; IntAct: EBI-1557554; Score: 0.37
DE  Interaction: Q9P6M1; IntAct: EBI-1557559; Score: 0.37
DE  Interaction: Q9UTE0; IntAct: EBI-1557577; Score: 0.37
DE  Interaction: O74338; IntAct: EBI-1557585; Score: 0.37
DE  Interaction: Q09825; IntAct: EBI-1542715; Score: 0.55
DE  Interaction: O42667; IntAct: EBI-1556648; Score: 0.27
DE  Interaction: Q10336; IntAct: EBI-1562137; Score: 0.27
DE  Interaction: P50528; IntAct: EBI-8529503; Score: 0.27
DE  Interaction: O13787; IntAct: EBI-21242797; Score: 0.37
DE  Interaction: Q10322; IntAct: EBI-21242908; Score: 0.37
DE  Interaction: P10815; IntAct: EBI-21245606; Score: 0.37
GO  GO:0005737;
GO  GO:0061497;
GO  GO:0005639;
GO  GO:0031021;
GO  GO:0034993;
GO  GO:0090619;
GO  GO:0035974;
GO  GO:0005874;
GO  GO:0044732;
GO  GO:0071958;
GO  GO:0005635;
GO  GO:0071957;
GO  GO:1990612;
GO  GO:0035861;
GO  GO:0043495;
GO  GO:0106166;
GO  GO:0051301;
GO  GO:0072766;
GO  GO:0032121;
GO  GO:0140480;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFTNTPVGGKRERQNGAHPAWSTLGANSAQIHQNTADLASKMHKLRYTKIRSPPTRVSIESITPKQRFPAPNFEQAYHSN
SQ  IRYEQEESDNEEFENVVKNGHEASTNVFYESDGDDEEFVNEEYENSIDEESDDEGYSLNEDTTATNASFRYPMNQRSTRK
SQ  SQFYSSKFKPLLWFGITLFSTLLIITLLHKGQEFYSRSFSSDNSQPSNSPVPNIPPASNDTKTSLKPDIIKDFTDSPSKV
SQ  GGNEEFDYSTGDLITKKEFDKILQQKVEQLKQSLKEEMSNYKSSVPFEVELNDDWKFFIESTVRKYLTDPVSMPNFALLS
SQ  TGAEVLPALTSKRYVRRPSAFIPRFTSYFFDSLVVRGHEPSIALTPNNAVAMCWSFQGSEGQLGISLSRPVYVTNVTIEH
SQ  VQHKIAHDLSSAPKDFELWVQGMSSKMFVLLGKARYSLTEDSIQTFSFESSNYIVAEPIQNVILKIKSNWGNPNYTCLYQ
SQ  VRVHGTVPNADEQPIPSLGEKAESTAENTGQDSS
//
ID  Q6FNV4;
PN  Protein transport protein SEC13-1;
GN  SEC131;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q6FNV4;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVEIANAHNDLIHDAVLDYYGKKLATCSSDKTIKIFEVEGESHKLVDTLVGHEGPVWRVDWAHPKFGTILASCSYDGKVI
SQ  IWKEENDRWSQIAVHAVHTASVNSVQWAPHEYGALLLAASSDGKVSVVEFKENGTATPLIFDAHAIGVNAASWAPATVEG
SQ  GNNPGEAPKEVRRFVTGGADNLVKIWRYNPETQSYLVEDTLEGHSDWVRDVAWSPSVLLRSYIASVSQDRTCNIWTQEDN
SQ  TGPWVKTQLTPEEFPDVLWRASWSLSGNILAISGGDNKVTLWKENLNGKWESAGEVNQ
//
ID  Q6FQU6;
PN  Protein transport protein SEC13-2;
GN  SEC132;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q6FQU6;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVKIENAHEGVIHHAALNYYGTRLATCSSDKTVKIFEINDVNNSSSLLETLVGHEGPVWYADWCHPSLGENLLATCGYDG
SQ  KVLIWKESGHGGKMQIIGKHAVHSASVNCVKWAPHEYGLILLCGSADGKISVVELKDGQIASTKILDNAHKFGVNSISWA
SQ  PLMKTDSSDDGDETTAVKQFISGGNDNLVKIWKFDDDQETYVVADTLEGHKDAVTAVDWSPTTLLQSYVASVSNDKQCLV
SQ  WTQDHSSKKNDWKKISVNEGKFEQKLGSVSWSLSGNLLAVSDDDKNVTIWKESGDGKWEEVVN
//
ID  O64740;
PN  Protein transport protein SEC13 homolog B;
GN  SEC13B;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Golgi apparatus {ECO:0000305|PubMed:24280388}. Endoplasmic reticulum {ECO:0000269|PubMed:21189294, ECO:0000305|PubMed:24280388}. Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
DR  UNIPROT: O64740;
DR  UNIPROT: Q8LAX1;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Required for protein transport from the endoplasmic reticulum to the Golgi apparatus. {ECO:0000305|PubMed:24280388}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9C9L2; IntAct: EBI-4484912; Score: 0.37
DE  Interaction: Q8LAZ7; IntAct: EBI-4484896; Score: 0.37
DE  Interaction: O48847; IntAct: EBI-4484904; Score: 0.37
DE  Interaction: Q9LT89; IntAct: EBI-4484920; Score: 0.37
GO  GO:0030127;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005730;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPGQKIETGHEDIVHDVQMDYYGKRIATASSDCTIKITGVSNNGGSQQLATLTGHRGPVWEVAWAHPKYGSILASCSYDG
SQ  QVILWKEGNQNQWTQDHVFTDHKSSVNSIAWAPHDIGLSLACGSSDGNISVFTARADGGWDTSRIDQAHPVGVTSVSWAP
SQ  ATAPGALVSSGLLDPVYKLASGGCDNTVKVWKLANGSWKMDCFPALQKHTDWVRDVAWAPNLGLPKSTIASGSQDGKVII
SQ  WTVGKEGEQWEGKVLKDFMTPVWRVSWSLTGNLLAVSDGNNNVTVWKEAVDGEWEQVTAVEP
//
ID  P06105;
PN  Protein SCP160;
GN  SCP160;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Attached to the cytoplasmic surface of the ER-nuclear envelope membranes.
DR  UNIPROT: P06105;
DR  UNIPROT: D6VWA3;
DR  Pfam: PF00013;
DR  PROSITE: PS50084;
DE  Function: Involved in the control of mitotic chromosome transmission. Required during cell division for faithful partitioning of the ER- nuclear envelope membranes which, in S.cerevisiae, enclose the duplicated chromosomes.
DE  Reference Proteome: Yes;
DE  Interaction: P08539; IntAct: EBI-393279; Score: 0.37
DE  Interaction: P36041; IntAct: EBI-443624; Score: 0.40
DE  Interaction: P38788; IntAct: EBI-785576; Score: 0.53
DE  Interaction: P38934; IntAct: EBI-801975; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P36008; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-804060; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-804060; Score: 0.53
DE  Interaction: P26783; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P05753; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P32905; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P05317; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P26321; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P14120; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P38706; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P0C2I0; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P41805; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P16861; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P32501; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P15790; IntAct: EBI-804060; Score: 0.35
DE  Interaction: P38011; IntAct: EBI-804060; Score: 0.44
DE  Interaction: P34160; IntAct: EBI-806268; Score: 0.35
DE  Interaction: P32527; IntAct: EBI-810703; Score: 0.53
DE  Interaction: P32357; IntAct: EBI-812457; Score: 0.27
DE  Interaction: P38285; IntAct: EBI-813567; Score: 0.27
DE  Interaction: Q12476; IntAct: EBI-814722; Score: 0.27
DE  Interaction: P23293; IntAct: EBI-816529; Score: 0.27
DE  Interaction: P15646; IntAct: EBI-816864; Score: 0.27
DE  Interaction: P39960; IntAct: EBI-818184; Score: 0.27
DE  Interaction: P06101; IntAct: EBI-819385; Score: 0.27
DE  Interaction: Q08109; IntAct: EBI-7343245; Score: 0.40
DE  Interaction: Q12250; IntAct: EBI-7646948; Score: 0.40
DE  Interaction: P40517; IntAct: EBI-7888793; Score: 0.40
DE  Interaction: P40545; IntAct: EBI-8051257; Score: 0.40
DE  Interaction: Q07821; IntAct: EBI-8083656; Score: 0.40
DE  Interaction: P08566; IntAct: EBI-8223739; Score: 0.22
DE  Interaction: P29295; IntAct: EBI-1558981; Score: 0.35
DE  Interaction: P39073; IntAct: EBI-2613846; Score: 0.35
DE  Interaction: Q01477; IntAct: EBI-7992250; Score: 0.35
DE  Interaction: P53741; IntAct: EBI-7994013; Score: 0.35
DE  Interaction: P46997; IntAct: EBI-3658160; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-3661947; Score: 0.35
DE  Interaction: P25491; IntAct: EBI-3664276; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3676746; Score: 0.53
DE  Interaction: P15108; IntAct: EBI-3735115; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3736611; Score: 0.35
DE  Interaction: P53863; IntAct: EBI-3769501; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3801349; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3807476; Score: 0.35
DE  Interaction: P31539; IntAct: EBI-3827800; Score: 0.35
DE  Interaction: P19735; IntAct: EBI-16276714; Score: 0.35
DE  Interaction: Q04675; IntAct: EBI-16281991; Score: 0.35
DE  Interaction: P53243; IntAct: EBI-16289027; Score: 0.35
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000329;
GO  GO:0031965;
GO  GO:0042175;
GO  GO:0005634;
GO  GO:0005844;
GO  GO:0001965;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0043577;
GO  GO:0007059;
GO  GO:0045141;
GO  GO:0000280;
GO  GO:0000750;
GO  GO:0030466;
GO  GO:0031509;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MSEEQTAIDSPPSTVEGSVETVTTIDSPSTTASTIAATAEEHPQLEKKPTPLPSLKDLPSLGSNAAFANVKVSWGPNMKP
SQ  AVSNSPSPSPSAPSLTTGLGAKRMRSKNIQEAFTLDLQSQLSITKPELSRIVQSVKKNHDVSVESTLSKNARTFLVSGVA
SQ  ANVHEAKRELVKKLTKPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSNVSLFGDFE
SQ  SVNLAKAKILAIVKEETKNATIKLVVEDEKYLPYIDVSEFASDEGDEEVKVQFYKKSGDIVILGPREKAKATKTSIQDYL
SQ  KKLASNLDEEKVKIPSKFQFLIDAEELKEKYNVIVTFPSTPDDELVSFVGLRDKVGEAITYARSSSKSYVVESLDISKAH
SQ  SKNLTHAKNLIMYFTKYSVLKGLEESHPNVKISLPSIQSLPTAETVTIHISAKSDEANDIKAVRKELISFVNNIPPSETL
SQ  VITDLDYELFGGSIKHCLLASESSVAFVQFGDYYPNDNSILLVALTEDEDFKPSIEEIQASLNKANESLNSLRTKQNNME
SQ  TKTYEFSEEVQDSLFKPSSATWKLIMEDISEQEGHLQIKLHTPEENQLTVRGDEKAAKAANKIFESILNSPSSKSKMTVN
SQ  IPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKDKTVEVTLTGLEYNLTHAKKYLAAEAKKWADIITKELIVP
SQ  VKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNEIVTIRGPSRGVNKAHEELKALLDFEMENGHKMVINVPAEHVPRIIGK
SQ  NGDNINDIRAEYGVEMDFLQKSTDPKAQETGEVELEITGSRQNIKDAAKRVESIVAEASDFVTEVLKIDHKYHKSIVGSG
SQ  GHILREIISKAGGEEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIVKDAENSVTKTIDIPAERKGALIGPGGI
SQ  VRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILNEIIRENFDREVDVPASIYEYVSERGAFIQKLRMDLSV
SQ  NVRFGNTSKKANKLARAPIEIPLEKVCGSTEGENAEKTKFTIEEVGAPTSSEEGDITMRLTYEPIDLSSILSDGEEKEVT
SQ  KDTSNDSAKKEEALDTAVKLIKERIAKAPSATYAGYVWGADTRRFNMIVGPGGSNIKKIREAADVIINVPRKSDKVNDVV
SQ  YIRGTKAGVEKAGEMVLKSLRR
//
ID  O15027;
PN  Protein transport protein Sec16A;
GN  SEC16A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17005010, ECO:0000269|PubMed:29300766}; Peripheral membrane protein {ECO:0000269|PubMed:17005010}. Golgi apparatus membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:E9QAT4}. Cytoplasm, cytosol {ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:21768384}. Microsome membrane {ECO:0000269|PubMed:17428803}. Note=SAR1A activity is required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation (PubMed:17192411). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). MIA3 and LRRK2 are required for its proper localization to ERES (PubMed:25201882, PubMed:28442536, PubMed:19638414, PubMed:17428803, PubMed:22355596). Recruited to microsomal membrane in SAR1-dependent manner (PubMed:17428803). {ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:19638414, ECO:0000269|PubMed:22355596, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:28442536}.
DR  UNIPROT: O15027;
DR  UNIPROT: A1YCA4;
DR  UNIPROT: J3KNL6;
DR  UNIPROT: Q4G0D7;
DR  UNIPROT: Q5SXP0;
DR  UNIPROT: Q5SXP1;
DR  UNIPROT: Q8N347;
DR  UNIPROT: Q96HP1;
DR  Pfam: PF12932;
DR  Pfam: PF12931;
DR  OMIM: 612854;
DR  DisGeNET: 9919;
DE  Function: Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17192411, PubMed:17005010, PubMed:17428803, PubMed:21768384, PubMed:22355596). Mediates the recruitment of MIA3/TANGO to ERES (PubMed:28442536). Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (PubMed:28067262). Positively regulates the protein stability of E3 ubiquitin-protein ligases RNF152 and RNF183 and the ER localization of RNF183 (PubMed:29300766). Acts as a RAB10 effector in the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter- enriched vesicles delivery to the cell membrane in adipocytes (By similarity). {ECO:0000250|UniProtKB:E9QAT4, ECO:0000269|PubMed:17005010, ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:21768384, ECO:0000269|PubMed:22355596, ECO:0000269|PubMed:28067262, ECO:0000269|PubMed:28442536, ECO:0000269|PubMed:29300766}.
DE  Reference Proteome: Yes;
DE  Interaction: O14976; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q99759; IntAct: EBI-362439; Score: 0.00
DE  Interaction: D3DR86; IntAct: EBI-365389; Score: 0.00
DE  Interaction: Q8AZK7; IntAct: EBI-9632715; Score: 0.35
DE  Interaction: P29353; IntAct: EBI-2615019; Score: 0.35
DE  Interaction: P01375; IntAct: EBI-2691312; Score: 0.00
DE  Interaction: Q15051; IntAct: EBI-4286917; Score: 0.35
DE  Interaction: O95758; IntAct: EBI-7850130; Score: 0.35
DE  Interaction: P48729; IntAct: EBI-6255977; Score: 0.64
DE  Interaction: P49674; IntAct: EBI-6256083; Score: 0.53
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q9UBN7; IntAct: EBI-6597993; Score: 0.35
DE  Interaction: Q9BY41; IntAct: EBI-6598094; Score: 0.35
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: Q9H4B6; IntAct: EBI-8798025; Score: 0.57
DE  Interaction: O15084; IntAct: EBI-8798340; Score: 0.27
DE  Interaction: O95835; IntAct: EBI-8798552; Score: 0.27
DE  Interaction: Q7TSJ6; IntAct: EBI-8800022; Score: 0.27
DE  Interaction: Q9H6Z9; IntAct: EBI-12503146; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-10045643; Score: 0.65
DE  Interaction: P55735; IntAct: EBI-10045785; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-9996267; Score: 0.35
DE  Interaction: Q92731; IntAct: EBI-9996422; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-10103481; Score: 0.53
DE  Interaction: P03179; IntAct: EBI-11721697; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: Q2MG96; IntAct: EBI-11733890; Score: 0.35
DE  Interaction: Q69117; IntAct: EBI-11733954; Score: 0.35
DE  Interaction: E9QKK1; IntAct: EBI-10995761; Score: 0.35
DE  Interaction: Q91X51; IntAct: EBI-11015786; Score: 0.35
DE  Interaction: Q8VC57; IntAct: EBI-11027413; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-11030093; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q9DBR0; IntAct: EBI-11047776; Score: 0.35
DE  Interaction: Q9D7I8; IntAct: EBI-11048266; Score: 0.35
DE  Interaction: Q9ERG0; IntAct: EBI-11054044; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062262; Score: 0.35
DE  Interaction: Q9Z2X1; IntAct: EBI-11066678; Score: 0.35
DE  Interaction: Q8K389; IntAct: EBI-11068831; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079358; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: P09497; IntAct: EBI-11081190; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: Q13492; IntAct: EBI-11082344; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: P50548; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P61978; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: E9PC66; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9NX05; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P31942; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P52272; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q8N0X7; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9ULX6; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q92540; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: O95817; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: O95782; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P27708; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P13861; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9BWF3; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P53675; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q15437; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q96I24; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q8TD26; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q8N684; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q32P28; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P18206; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q1KMD3; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q14677; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9HAU0; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q08379; IntAct: EBI-11083608; Score: 0.48
DE  Interaction: Q9NZB2; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P15924; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q5JSZ5; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9UHV9; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: O95487; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P09651; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P05783; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: F5H365; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q6ZRV2; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q14134; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P42694; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: O15460; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: O95486; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q6UN15; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q8N163; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P09496; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q8WUF5; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: C9JE98; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q99959; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q8IWZ3; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q96MX6; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9UHF7; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9NRA8; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9NWS0; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q14244; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q86UY5; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q14498; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P12268; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P53992; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q13470; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q63ZY3; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: O15379; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9Y2F9; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q5T0W9; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q5T5P2; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9Y446; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q14671; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: H0YH87; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: O00443; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q96PK6; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9NSY1; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q14203; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P20839; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9C0J8; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q9H4H8; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: O60763; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: P04003; IntAct: EBI-11083608; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: Q15691; IntAct: EBI-11091481; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-11092730; Score: 0.35
DE  Interaction: Q9WTI7; IntAct: EBI-11093786; Score: 0.35
DE  Interaction: Q8CAF4; IntAct: EBI-11096313; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11098811; Score: 0.35
DE  Interaction: Q6ZPU9; IntAct: EBI-11102340; Score: 0.35
DE  Interaction: Q6PJG2; IntAct: EBI-11106137; Score: 0.35
DE  Interaction: P24941; IntAct: EBI-11106375; Score: 0.35
DE  Interaction: Q96QS3; IntAct: EBI-11107478; Score: 0.35
DE  Interaction: Q9Z1Z0; IntAct: EBI-11110688; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: Q96HQ2; IntAct: EBI-11125466; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-11132927; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-11142496; Score: 0.35
DE  Interaction: P31323; IntAct: EBI-11146630; Score: 0.35
DE  Interaction: Q9HC77; IntAct: EBI-11397411; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9NZN9; IntAct: EBI-12448890; Score: 0.51
DE  Interaction: Q9NQH7; IntAct: EBI-12452910; Score: 0.51
DE  Interaction: P03431; IntAct: EBI-12579142; Score: 0.35
DE  Interaction: P03428; IntAct: EBI-12579909; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581941; Score: 0.35
DE  Interaction: Q5EP37; IntAct: EBI-12582596; Score: 0.35
DE  Interaction: C5E526; IntAct: EBI-12584472; Score: 0.35
DE  Interaction: C5E527; IntAct: EBI-12585279; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12588098; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12588729; Score: 0.35
DE  Interaction: O14829; IntAct: EBI-14024386; Score: 0.35
DE  Interaction: Q9BY84; IntAct: EBI-14027455; Score: 0.35
DE  Interaction: P07196; IntAct: EBI-21716934; Score: 0.35
DE  Interaction: Q9BVA0; IntAct: EBI-16421856; Score: 0.35
DE  Interaction: Q01968; IntAct: EBI-16412116; Score: 0.35
DE  Interaction: Q96RS6; IntAct: EBI-20723339; Score: 0.35
DE  Interaction: Q6ZNJ1; IntAct: EBI-16749633; Score: 0.64
DE  Interaction: Q96N67; IntAct: EBI-16749780; Score: 0.50
DE  Interaction: Q08AM6; IntAct: EBI-16749791; Score: 0.35
DE  Interaction: Q9NWT8; IntAct: EBI-16786806; Score: 0.27
DE  Interaction: Q96GD4; IntAct: EBI-16787973; Score: 0.57
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.42
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: P49841; IntAct: EBI-16793176; Score: 0.42
DE  Interaction: P19367; IntAct: EBI-16794773; Score: 0.27
DE  Interaction: O14880; IntAct: EBI-16796348; Score: 0.27
DE  Interaction: P25786; IntAct: EBI-16797556; Score: 0.42
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: P62491; IntAct: EBI-16797971; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: O75880; IntAct: EBI-16799233; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.42
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: O95831; IntAct: EBI-16786589; Score: 0.42
DE  Interaction: P50613; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: P49336; IntAct: EBI-16790691; Score: 0.35
DE  Interaction: Q15075; IntAct: EBI-16791749; Score: 0.35
DE  Interaction: P15311; IntAct: EBI-16792111; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-16792571; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P20339; IntAct: EBI-16798290; Score: 0.35
DE  Interaction: Q71U36; IntAct: EBI-16799786; Score: 0.35
DE  Interaction: P23258; IntAct: EBI-16800136; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-16795491; Score: 0.27
DE  Interaction: O75521; IntAct: EBI-16811476; Score: 0.35
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: Q12824; IntAct: EBI-20623811; Score: 0.42
DE  Interaction: Q9Y2H1; IntAct: EBI-20624096; Score: 0.42
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: A2A935; IntAct: EBI-21024514; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q9ULK4; IntAct: EBI-25472850; Score: 0.35
DE  Interaction: Q9UQM7; IntAct: EBI-25380388; Score: 0.35
DE  Interaction: P28482; IntAct: EBI-25381527; Score: 0.35
DE  Interaction: Q8N4T4; IntAct: EBI-25408280; Score: 0.35
DE  Interaction: Q7Z5H3; IntAct: EBI-25409874; Score: 0.35
DE  Interaction: Q8IZD9; IntAct: EBI-25411696; Score: 0.35
DE  Interaction: P0DTC7; IntAct: EBI-25510184; Score: 0.35
DE  Interaction: P0DTC8; IntAct: EBI-25510273; Score: 0.35
DE  Interaction: A0A663DJA2; IntAct: EBI-25510410; Score: 0.35
DE  Interaction: Q13627; IntAct: EBI-26367331; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574571; Score: 0.35
DE  Interaction: Q96LU5; IntAct: EBI-27050332; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-27084109; Score: 0.35
DE  Interaction: O14733; IntAct: EBI-28930089; Score: 0.35
DE  Interaction: P11274; IntAct: EBI-28931791; Score: 0.35
DE  Interaction: P42680; IntAct: EBI-28935138; Score: 0.35
DE  Interaction: P48730; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P53671; IntAct: EBI-28938453; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-28939366; Score: 0.35
DE  Interaction: Q14012; IntAct: EBI-28939656; Score: 0.35
DE  Interaction: Q15208; IntAct: EBI-28941263; Score: 0.35
DE  Interaction: Q16654; IntAct: EBI-28941523; Score: 0.35
DE  Interaction: Q6P3W7; IntAct: EBI-28941741; Score: 0.35
DE  Interaction: Q6P5Z2; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q76MJ5; IntAct: EBI-28941934; Score: 0.35
DE  Interaction: Q8TAS1; IntAct: EBI-28943630; Score: 0.35
DE  Interaction: Q8TDX7; IntAct: EBI-28943744; Score: 0.35
DE  Interaction: Q9BUB5; IntAct: EBI-28944975; Score: 0.35
DE  Interaction: Q9BYP7; IntAct: EBI-28946054; Score: 0.35
DE  Interaction: Q9NRM7; IntAct: EBI-28946455; Score: 0.35
DE  Interaction: Q9NSY0; IntAct: EBI-28946547; Score: 0.35
DE  Interaction: Q9UJY1; IntAct: EBI-28946841; Score: 0.35
DE  Interaction: Q9Y6S9; IntAct: EBI-28948011; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: O00167; IntAct: EBI-27116032; Score: 0.27
DE  Interaction: Q15326; IntAct: EBI-30824425; Score: 0.44
DE  Interaction: Q13363; IntAct: EBI-28997163; Score: 0.27
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
DE  Interaction: P43268; IntAct: EBI-29015385; Score: 0.27
DE  Interaction: P41212; IntAct: EBI-29015445; Score: 0.27
DE  Interaction: Q9UIH9; IntAct: EBI-29018016; Score: 0.27
DE  Interaction: Q13887; IntAct: EBI-29018613; Score: 0.27
DE  Interaction: Q99612; IntAct: EBI-29018743; Score: 0.27
DE  Interaction: Q13886; IntAct: EBI-29018980; Score: 0.27
DE  Interaction: Q14934; IntAct: EBI-29668679; Score: 0.27
DE  Interaction: Q06945; IntAct: EBI-29725484; Score: 0.27
DE  Interaction: Q14765; IntAct: EBI-29763222; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: Q96ED9; IntAct: EBI-34575530; Score: 0.27
GO  GO:0005829;
GO  GO:0070971;
GO  GO:0005789;
GO  GO:0012507;
GO  GO:0000139;
GO  GO:0031090;
GO  GO:0048471;
GO  GO:0006914;
GO  GO:0048208;
GO  GO:0007029;
GO  GO:0006888;
GO  GO:0007030;
GO  GO:0043000;
GO  GO:0032527;
GO  GO:0070973;
GO  GO:0072659;
GO  GO:0050821;
GO  GO:0034976;
GO  GO:0021762;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MQPPPQTVPSGMAGPPPAGNPRSVFWASSPYRRRANNNAAVAPTTCPLQPVTDPFAFSRQALQSTPLGSSSKSSPPVLQG
SQ  PAPAGFSQHPGLLVPHTHARDSSQGPCEPLPGPLTQPRAHASPFSGALTPSAPPGPEMNRSAEVGPSSEPEVQTLPYLPH
SQ  YIPGVDPETSHGGHPHGNMPGLDRPLSRQNPHDGVVTPAASPSLPQPGLQMPGQWGPVQGGPQPSGQHRSPCPEGPVPSG
SQ  VPCATSVPHFPTPSILHQGPGHEQHSPLVAPPAALPSDGRDEVSHLQSGSHLANNSDPESTFRQNPRIVNHWASPELRQN
SQ  PGVKNEHRPASALVNPLARGDSPENRTHHPLGAGAGSGCAPLEADSGASGALAMFFQGGETENEENLSSEKAGLSGQADF
SQ  DDFCSSPGLGRPPAPTHVGAGSLCQALLPGPSNEAAGDVWGDTASTGVPDASGSQYENVENLEFVQNQEVLPSEPLNLDP
SQ  SSPSDQFRYGPLPGPAVPRHGAVCHTGAPDATLHTVHPDSVSSSYSSRSHGRLSGSARPQELVGTFIQQEVGKPEDEASG
SQ  SFFKQIDSSPVGGETDETTVSQNYRGSVSQPSTPSPPKPTGIFQTSANSSFEPVKSHLVGVKPFEADRANVVGEVRETCV
SQ  RQKQCRPAAALPDASPGNLEQPPDNMETLCAPQVCPLPLNSTTEAVHMLPHAGAPPLDTVYPAPEKRPSARTQGPVKCES
SQ  PATTLWAQSELPDFGGNVLLAPAAPALYVCAKPQPPVVQPPEEAMSGQQSRNPSSAAPVQSRGGIGASENLENPPKMGEE
SQ  EALQSQASSGYASLLSSPPTESLQNPPVLIAQPDHSYNLAQPINFSVSLSNSHEKNQSWREALVGDRPAVSSWALGGDSG
SQ  ENTSLSGIPTSSVLSLSLPSSVAQSNFPQGSGASEMVSNQPANLLVQPPSQPVPENLVPESQKDRKAGSALPGFANSPAG
SQ  STSVVLVPPAHGTLVPDGNKANHSSHQEDTYGALDFTLSRTLENPVNVYNPSHSDSLASQQSVASHPRQSGPGAPNLDRF
SQ  YQQVTKDAQGQPGLERAQQELVPPQQQASPPQLPKAMFSELSNPESLPAQGQAQNSAQSPASLVLVDAGQQLPPRPPQSS
SQ  SVSLVSSGSGQAAVPSEQPWPQPVPALAPGPPPQDLAAYYYYRPLYDAYQPQYSLPYPPEPGAASLYYQDVYSLYEPRYR
SQ  PYDGAASAYAQNYRYPEPERPSSRASHSSERPPPRQGYPEGYYSSKSGWSSQSDYYASYYSSQYDYGDPGHWDRYHYSAR
SQ  VRDPRTYDRRYWCDAEYDAYRREHSAFGDRPEKRDNNWRYDPRFTGSFDDDPDPHRDPYGEEVDRRSVHSEHSARSLHSA
SQ  HSLASRRSSLSSHSHQSQIYRSHNVAAGSYEAPLPPGSFHGDFAYGTYRSNFSSGPGFPEYGYPADTVWPAMEQVSSRPT
SQ  SPEKFSVPHVCARFGPGGQLIKVIPNLPSEGQPALVEVHSMEALLQHTSEQEEMRAFPGPLAKDDTHKVDVINFAQNKAM
SQ  KCLQNENLIDKESASLLWNFIVLLCRQNGTVVGTDIAELLLRDHRTVWLPGKSPNEANLIDFTNEAVEQVEEEESGEAQL
SQ  SFLTGGPAAAASSLERETERFRELLLYGRKKDALESAMKNGLWGHALLLASKMDSRTHARVMTRFANSLPINDPLQTVYQ
SQ  LMSGRMPAASTCCGDEKWGDWRPHLAMVLSNLNNNMDVESRTMATMGDTLASRGLLDAAHFCYLMAQAGFGVYTKKTTKL
SQ  VLIGSNHSLPFLKFATNEAIQRTEAYEYAQSLGAETCPLPSFQVFKFIYSCRLAEMGLATQAFHYCEAIAKSILTQPHLY
SQ  SPVLISQLVQMASQLRLFDPQLKEKPEEESLAAPTWLVHLQQVERQIKEGAGVWHQDGALPQQCPGTPSSEMEQLDRPGL
SQ  SQPGALGIANPLLAVPAPSPEHSSPSVRLLPSAPQTLPDGPLASPARVPMFPVPLPPGPLEPGPGCVTPGPALGFLEPSG
SQ  PGLPPGVPPLQERRHLLQEARSPDPGIVPQEAPVGNSLSELSEENFDGKFANLTPSRTVPDSEAPPGWDRADSGPTQPPL
SQ  SLSPAPETKRPGQAAKKETKEPKKGESWFFRWLPGKKKTEAYLPDDKNKSIVWDEKKNQWVNLNEPEEEKKAPPPPPTSM
SQ  PKTVQAAPPALPGPPGAPVNMYSRRAAGTRARYVDVLNPSGTQRSEPALAPADFVAPLAPLPIPSNLFVPTPDAEEPQLP
SQ  DGTGREGPAAARGLANPEPAPEPKVLSSAASLPGSELPSSRPEGSQGGELSRCSSMSSLSREVSQHFNQAPGDLPAAGGP
SQ  PSGAMPFYNPAQLAQACATSGSSRLGRIGQRKHLVLN
//
ID  E9QAT4;
PN  Protein transport protein Sec16A;
GN  Sec16a;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein. Golgi apparatus membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15027}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27354378}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15027}. Microsome membrane {ECO:0000250|UniProtKB:O15027}. Note=SAR1A activity is required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation (By similarity). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). MIA3 and LRRK2 are required for its proper localization to ERES (PubMed:25201882). Recruited to microsomal membrane in SAR1-dependent manner (By similarity). {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:25201882}.
DR  UNIPROT: E9QAT4;
DR  UNIPROT: A2AIX1;
DR  UNIPROT: Q80U43;
DR  UNIPROT: Q811L5;
DR  Pfam: PF12932;
DR  Pfam: PF12931;
DE  Function: Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17428803). Mediates the recruitment of MIA3/TANGO to ERES. Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (By similarity). Acts as a RAB10 effector in the regulation of insulin- induced SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in adipocytes (PubMed:27354378). {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:27354378}.
DE  Reference Proteome: Yes;
DE  Interaction: P39428; IntAct: EBI-658728; Score: 0.37
DE  Interaction: P49452; IntAct: EBI-8573213; Score: 0.35
DE  Interaction: Q80Z64; IntAct: EBI-8820601; Score: 0.35
DE  Interaction: Q5S006; IntAct: EBI-10045676; Score: 0.46
DE  Interaction: Q5S007; IntAct: EBI-10046253; Score: 0.27
DE  Interaction: Q8BPI1; IntAct: EBI-15744736; Score: 0.35
DE  Interaction: Q61584; IntAct: EBI-16729686; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0005829;
GO  GO:0070971;
GO  GO:0005789;
GO  GO:0012507;
GO  GO:0000139;
GO  GO:0031090;
GO  GO:0048471;
GO  GO:0006914;
GO  GO:0048208;
GO  GO:0007029;
GO  GO:0006888;
GO  GO:0007030;
GO  GO:0043000;
GO  GO:0032527;
GO  GO:0070973;
GO  GO:0072659;
GO  GO:0050821;
GO  GO:0034976;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O15027};
SQ  MQPPPQAVPSGVAGPPPAGNPRSMFWANSPYRKPANNAPVAPITRPLQPVTDPFAFNRQTLQNTPVGSSSKSSLPNLPGP
SQ  ALSVFSQWPGLPVTPTNAGDSSTGLHEPLSGTLSQPRADASLFPPASTPSSLPGLEVSRNAEADPSSGHEVQMLPHSAHY
SQ  IPGVGPEQPLGGQMNDSGSGPDQPMNRHAPHDGAVTHAASPFLPQPQMPGQWGPAQGGPQPSYQHHSPYLEGPVQNMGLQ
SQ  AASLPHFPPPSSLHQGPGHESHAPQTFTPASLASGEGNEIVHQQSKNHPLSSFPPKHTFEQNSRIGNMWASPELKQNPGV
SQ  NKEHLLDPAHVNPFTQGNSPENQAHHPPVAATNHALQEAASGALSMFFQGEETENEENLSSEKAGLDKRLNLDSFSSTSR
SQ  LGHPPPPGASGVYQAFPRGPSSEAAQEGDAQPYFSQSVGVRLDKQSTVPPANDAWGDVPGTGTRCASGPQCENVENLEFV
SQ  QNQEVLPRETLSVDPFPLSDQIRYGPLPGPAASRPATVGLTRGGGLNLEAPDTPLHPTRPDSVSSSYSSHSHRSPPGSAR
SQ  PQELVGTFIQQEVGKLEDDTSGSFFKQIDSSPVGGETDEVTGSQNCCSSLSQPSTPSPPKPTGVFQTSANSSFEPVKSHL
SQ  VGVKPVEADRANMVVEVRGTQYCPKKRRAAVAPPDATSGNLEQPPDNMETPCAPQACPLPLSTTGEAGQLVSNTAGTPLD
SQ  TVRPVPDKRPSARAQGPVKCESPATTLWAQNELPDFGGNVLLAPAAPALYVPVKPKPSEVVHHPEKGMSGQKAWKQGSVP
SQ  PLQNQDPPGASENLENPPKVGEEEALPVQASSGYASLLSSPPTESLHNQPVLIAQPDQSYNLAQPINFSVSLLNPNEKNQ
SQ  SWGDAVVGERSIVSNNWALGGDPEERAALSGVPASAVTGASLPSSIPQNCAPQGSGSSEMIASQSASWLVQQLSPQTPQS
SQ  PHPNAEKGPSEFVSSPAGNTSVMLVPPASSTLVPNSNKAKHSSNQEEAVGALDFTLNRTLENPVRMYSPSPSDGPASQQP
SQ  LPNHPRQSGPGLHNQDHFYQQVTKDAQDQHRLERAQPELVPPRPQNSPQVPQASCPEPSNPESPPTQGQSESLAQPPASP
SQ  ASVNTGQLLPQPPQASSASVTSTNSSQAAVRSEQLWLHPPPPNTFGPAPQDLASYYYYRPLYDAYQSQYPSPYPSDPGTA
SQ  SLYYQDMYGLYEPRYRPYDSSASAYAENHRYSEPERPSSRASHYSDQLAPRQGYPEGYYNSKSGWSSHSDYYANYYSGQY
SQ  DYGDPSRWDRYYGSRLRDPRTWDRRYWYDSEHDPYRKDHYAYSDRPEKCDDHWRYDPRFTGSFDDDAEIHRDPYGEEADR
SQ  RSIHSEHSARSLRSTHSLPSRRSSLSSHSHQSQIYRSHHVTGGSFEAPHAPGSFHGDYAYGTYASNFSGAHGFPEYSYPA
SQ  DTSWPAVEQVPSRPTSPEKFTVPHVCARFGPGGQLLKVIPNLPSEGQPALVEIHSLETLLQHTPEQEEMRSFPGPLGKDD
SQ  THKVDVINFAQNKATKCLQNESLIDKESASLLWKFIILLCRQNGTVVGTDIAELLLRDHRTVWLPGKSPNEANLIDFTNE
SQ  AVEQVEEEESGEAQLSFLTDSQTVTTSVLEKETERFRELLLYGRKKDALESAMKNGLWGHALLLASKMDSRTHARVMTRF
SQ  ANSLPINDPLQTVYQLMSGRMPAASTCCGDEKWGDWRPHLAMVLSNLNNNMDVESRTMATMGDTLASKGLLDAAHFCYLM
SQ  AQVGFGVYTKKTTKLVLIGSNHSLPFLKFATNEAIQRTEAYEYAQSLGAHTCSLPNFQVFKFIYLCRLAEMGLATQAFHY
SQ  CEVIAKSVLTQPGAYSPVLISQLTQMASQLRLFDPQLKEKPEEESFVEPAWLVQLQHVERQIQEGTVLWSQDGTEPQQCR
SQ  ITSGSEVEQSDGPGLNQQAGPQADNPLLMPSTEPLMHGVQLLPTAPQTLPDGQPAHLSRVPMFPVPMSRGPLELSPAYGP
SQ  PGSALGFPESSRSDPAVLHPGQALPPTTLSLQESGLPPQEAKSPDPEMVPRGSPVRHSPPELSQEEFGESFADPGSSRTA
SQ  QDLETSPVWDLGSSSLTRAPSLTSDSEGKKPAQAVKKEPKEPKKTESWFSRWLPGKKRTEAYLPDDKNKSIVWDEKKNQW
SQ  VNLNEPEEEKKAPPPPPTSFPRVPQVAPTGPAGPPTASVNVFSRKAGGSRARYVDVLNPSGTQRSEPALAPADFFAPLAP
SQ  LPIPSNLFVPNPDAEEPQPADGTGCRGQAPAGTQSKAESTLEPKVGSSTVSAPGPELLPSKPDGSQGGEAPGDHCPTGAP
SQ  HGGSVPFYNPAQLVQASVTSGNSRPGRIGQRKYAALN
//
ID  Q14524;
PN  Sodium channel protein type 5 subunit alpha;
GN  SCN5A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:1309946, ECO:0000269|PubMed:19074138, ECO:0000269|PubMed:21447824, ECO:0000269|PubMed:23085483, ECO:0000269|PubMed:23420830, ECO:0000269|PubMed:25370050, ECO:0000269|PubMed:26279430}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21447824}. Cell membrane, sarcolemma, T- tubule {ECO:0000250|UniProtKB:P15389}. Note=RANGRF promotes trafficking to the cell membrane. {ECO:0000269|PubMed:21447824, ECO:0000269|PubMed:23420830}.
DR  UNIPROT: Q14524;
DR  UNIPROT: A5H1P8;
DR  UNIPROT: A6N922;
DR  UNIPROT: A6N923;
DR  UNIPROT: B2RTU0;
DR  UNIPROT: E7ET19;
DR  UNIPROT: E9PEF3;
DR  UNIPROT: E9PEK2;
DR  UNIPROT: E9PFW7;
DR  UNIPROT: Q59H93;
DR  UNIPROT: Q75RX9;
DR  UNIPROT: Q75RY0;
DR  UNIPROT: Q86UR3;
DR  UNIPROT: Q8IZC9;
DR  UNIPROT: Q96J69;
DR  PDB: 2KBI;
DR  PDB: 2L53;
DR  PDB: 4DCK;
DR  PDB: 4DJC;
DR  PDB: 4JQ0;
DR  PDB: 4OVN;
DR  PDB: 5DBR;
DR  PDB: 6LQA;
DR  PDB: 6MUD;
DR  PDB: 7DTC;
DR  PDB: 7L83;
DR  Pfam: PF00520;
DR  Pfam: PF06512;
DR  Pfam: PF11933;
DR  OMIM: 108770;
DR  OMIM: 113900;
DR  OMIM: 272120;
DR  OMIM: 600163;
DR  OMIM: 601144;
DR  OMIM: 601154;
DR  OMIM: 603829;
DR  OMIM: 603830;
DR  OMIM: 608567;
DR  OMIM: 614022;
DR  DisGeNET: 6331;
DE  Function: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (PubMed:1309946, PubMed:21447824, PubMed:25370050, PubMed:23420830, PubMed:23085483, PubMed:26279430, PubMed:26392562, PubMed:26776555). It is a tetrodotoxin-resistant Na(+) channel isoform (PubMed:1309946). This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels (PubMed:19074138). {ECO:0000269|PubMed:1309946, ECO:0000269|PubMed:19074138, ECO:0000269|PubMed:21447824, ECO:0000269|PubMed:23085483, ECO:0000269|PubMed:23420830, ECO:0000269|PubMed:24167619, ECO:0000269|PubMed:25370050, ECO:0000269|PubMed:26279430, ECO:0000269|PubMed:26392562, ECO:0000269|PubMed:26776555}.
DE  Disease: Progressive familial heart block 1A (PFHB1A) [MIM:113900]: A cardiac bundle branch disorder characterized by progressive alteration of cardiac conduction through the His-Purkinje system, with a pattern of a right bundle-branch block and/or left anterior hemiblock occurring individually or together. It leads to complete atrio-ventricular block causing syncope and sudden death. {ECO:0000269|PubMed:11234013, ECO:0000269|PubMed:11804990, ECO:0000269|PubMed:12569159, ECO:0000269|PubMed:12574143, ECO:0000269|PubMed:19251209, ECO:0000269|PubMed:23420830}. Note=The disease is caused by variants affecting the gene represented in this entry. Long QT syndrome 3 (LQT3) [MIM:603830]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. {ECO:0000269|PubMed:10377081, ECO:0000269|PubMed:10508990, ECO:0000269|PubMed:10590249, ECO:0000269|PubMed:10627139, ECO:0000269|PubMed:10911008, ECO:0000269|PubMed:10973849, ECO:0000269|PubMed:11304498, ECO:0000269|PubMed:11410597, ECO:0000269|PubMed:11710892, ECO:0000269|PubMed:11889015, ECO:0000269|PubMed:11997281, ECO:0000269|PubMed:12209021, ECO:0000269|PubMed:12454206, ECO:0000269|PubMed:12673799, ECO:0000269|PubMed:15840476, ECO:0000269|PubMed:16414944, ECO:0000269|PubMed:16922724, ECO:0000269|PubMed:18060054, ECO:0000269|PubMed:18451998, ECO:0000269|PubMed:18708744, ECO:0000269|PubMed:18848812, ECO:0000269|PubMed:18929331, ECO:0000269|PubMed:19716085, ECO:0000269|PubMed:26392562, ECO:0000269|PubMed:7651517, ECO:0000269|PubMed:7889574, ECO:0000269|PubMed:8541846, ECO:0000269|PubMed:9506831, ECO:0000269|PubMed:9686753, ECO:0000269|Ref.35}. Note=The disease is caused by variants affecting the gene represented in this entry. Brugada syndrome 1 (BRGDA1) [MIM:601144]: A tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:10532948, ECO:0000269|PubMed:10618304, ECO:0000269|PubMed:10690282, ECO:0000269|PubMed:11410597, ECO:0000269|PubMed:11748104, ECO:0000269|PubMed:11823453, ECO:0000269|PubMed:11901046, ECO:0000269|PubMed:12051963, ECO:0000269|PubMed:12106943, ECO:0000269|PubMed:15023552, ECO:0000269|PubMed:15338453, ECO:0000269|PubMed:15579534, ECO:0000269|PubMed:15851320, ECO:0000269|PubMed:16266370, ECO:0000269|PubMed:16325048, ECO:0000269|PubMed:16616735, ECO:0000269|PubMed:17075016, ECO:0000269|PubMed:17081365, ECO:0000269|PubMed:17198989, ECO:0000269|PubMed:18252757, ECO:0000269|PubMed:18341814, ECO:0000269|PubMed:18451998, ECO:0000269|PubMed:18456723, ECO:0000269|PubMed:18616619, ECO:0000269|PubMed:19251209, ECO:0000269|PubMed:19272188, ECO:0000269|PubMed:20129283, ECO:0000269|PubMed:23085483, ECO:0000269|PubMed:23420830, ECO:0000269|PubMed:24167619, ECO:0000269|PubMed:26279430, ECO:0000269|PubMed:26776555, ECO:0000269|PubMed:32850980, ECO:0000269|PubMed:9521325}. Note=The disease is caused by variants affecting the gene represented in this entry. Sick sinus syndrome 1 (SSS1) [MIM:608567]: The term 'sick sinus syndrome' encompasses a variety of conditions caused by sinus node dysfunction. The most common clinical manifestations are syncope, presyncope, dizziness, and fatigue. Electrocardiogram typically shows sinus bradycardia, sinus arrest, and/or sinoatrial block. Episodes of atrial tachycardias coexisting with sinus bradycardia ('tachycardia- bradycardia syndrome') are also common in this disorder. SSS occurs most often in the elderly associated with underlying heart disease or previous cardiac surgery, but can also occur in the fetus, infant, or child without heart disease or other contributing factors. SSS1 onset is in utero, infancy, or early childhood. {ECO:0000269|PubMed:11748104, ECO:0000269|PubMed:14523039, ECO:0000269|PubMed:22795782}. Note=The disease is caused by variants affecting the gene represented in this entry. Familial paroxysmal ventricular fibrillation 1 (VF1) [MIM:603829]: A cardiac arrhythmia marked by fibrillary contractions of the ventricular muscle due to rapid repetitive excitation of myocardial fibers without coordinated contraction of the ventricle and by absence of atrial activity. {ECO:0000269|PubMed:10940383}. Note=The disease is caused by variants affecting the gene represented in this entry. Sudden infant death syndrome (SIDS) [MIM:272120]: SIDS is the sudden death of an infant younger than 1 year that remains unexplained after a thorough case investigation, including performance of a complete autopsy, examination of the death scene, and review of clinical history. Pathophysiologic mechanisms for SIDS may include respiratory dysfunction, cardiac dysrhythmias, cardiorespiratory instability, and inborn errors of metabolism, but definitive pathogenic mechanisms precipitating an infant sudden death remain elusive. {ECO:0000269|PubMed:18596570, ECO:0000269|PubMed:19302788}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Atrial standstill 1 (ATRST1) [MIM:108770]: A rare arrhythmia characterized by the absence of electrical and mechanical activity in the atria. Electrocardiographically, it is characterized by bradycardia, the absence of P waves, and a junctional narrow complex escape rhythm. {ECO:0000269|PubMed:12522116, ECO:0000269|PubMed:23420830}. Note=The disease may be caused by variants affecting distinct genetic loci, including the gene represented in this entry. A mutation in SCN5A has been detected in combination with a rare GJA5 genotype in a large family with atrial standstill. Cardiomyopathy, dilated 1E (CMD1E) [MIM:601154]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:15466643, ECO:0000269|PubMed:23420830}. Note=The disease is caused by variants affecting the gene represented in this entry. Atrial fibrillation, familial, 10 (ATFB10) [MIM:614022]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:18088563, ECO:0000269|PubMed:18378609}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NY99; IntAct: EBI-8556892; Score: 0.51
DE  Interaction: Q61234; IntAct: EBI-8669491; Score: 0.40
DE  Interaction: P41220; IntAct: EBI-737552; Score: 0.00
DE  Interaction: P02768; IntAct: EBI-1222961; Score: 0.35
DE  Interaction: P62158; IntAct: EBI-2930225; Score: 0.93
DE  Interaction: P26045; IntAct: EBI-8620386; Score: 0.53
DE  Interaction: Q99873; IntAct: EBI-8673374; Score: 0.47
DE  Interaction: O60678; IntAct: EBI-8673437; Score: 0.47
DE  Interaction: O14744; IntAct: EBI-8673420; Score: 0.27
DE  Interaction: Q13557; IntAct: EBI-9637464; Score: 0.61
DE  Interaction: P11275; IntAct: EBI-9674620; Score: 0.44
DE  Interaction: Q12959; IntAct: EBI-11793004; Score: 0.40
DE  Interaction: Q9Y3B6; IntAct: EBI-24496050; Score: 0.56
DE  Interaction: Q8N9N5; IntAct: EBI-24609814; Score: 0.56
DE  Interaction: Q8WW24; IntAct: EBI-24627863; Score: 0.56
DE  Interaction: Q96E35; IntAct: EBI-24558772; Score: 0.60
DE  Interaction: Q49AR9; IntAct: EBI-24601634; Score: 0.56
DE  Interaction: Q8N335; IntAct: EBI-13644311; Score: 0.40
DE  Interaction: Q13424; IntAct: EBI-15712197; Score: 0.35
DE  Interaction: P29476; IntAct: EBI-15712197; Score: 0.35
DE  Interaction: Q6Q477; IntAct: EBI-15712197; Score: 0.35
DE  Interaction: Q12955; IntAct: EBI-15807622; Score: 0.44
DE  Interaction: Q92913; IntAct: EBI-15987728; Score: 0.35
DE  Interaction: P61328; IntAct: EBI-15987771; Score: 0.54
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P46934; IntAct: EBI-30832580; Score: 0.44
GO  GO:0005901;
GO  GO:0009986;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0014704;
GO  GO:0016328;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0042383;
GO  GO:0030315;
GO  GO:0001518;
GO  GO:0030018;
GO  GO:0030506;
GO  GO:0005516;
GO  GO:0019899;
GO  GO:0017134;
GO  GO:0050998;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0097110;
GO  GO:0044325;
GO  GO:0031625;
GO  GO:0005244;
GO  GO:0005248;
GO  GO:0086060;
GO  GO:0086061;
GO  GO:0086006;
GO  GO:0086062;
GO  GO:0086063;
GO  GO:0086014;
GO  GO:0086016;
GO  GO:0086067;
GO  GO:0003360;
GO  GO:0086043;
GO  GO:0003161;
GO  GO:0086002;
GO  GO:0060048;
GO  GO:0003231;
GO  GO:0071277;
GO  GO:0021549;
GO  GO:0051899;
GO  GO:0086010;
GO  GO:0098912;
GO  GO:0086045;
GO  GO:0086048;
GO  GO:0086012;
GO  GO:0086047;
GO  GO:0086046;
GO  GO:0019228;
GO  GO:0042475;
GO  GO:0045760;
GO  GO:0050679;
GO  GO:0010765;
GO  GO:0060371;
GO  GO:0060372;
GO  GO:0086004;
GO  GO:0002027;
GO  GO:0086091;
GO  GO:1902305;
GO  GO:0060373;
GO  GO:0060307;
GO  GO:0014894;
GO  GO:0086015;
GO  GO:0035725;
GO  GO:0006814;
GO  GO:0021537;
GO  GO:0086005;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:D0E0C2};
SQ  MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIGEPL
SQ  EDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLIMCTILTNCVFMAQHDPPPWTKYV
SQ  EYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIV
SQ  GALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLKNGT
SQ  SDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLG
SQ  SFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRK
SQ  RMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSEADFADDENSTAGESESHHTS
SQ  LLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGVVSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGP
SQ  QMLTSQAPCVDGFEEPGARQRALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTD
SQ  LTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSR
SQ  MSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWH
SQ  MMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQ
SQ  LALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVPPTRKETRFEEGEQPGQGTPG
SQ  DPEPVCVPIAVAESDTDDQEEDEENSLGTEEESSKQQESQPVSGGPEAPPDSRTWSQVSATASSEAEASASQADWRQQWK
SQ  AEPQAPGCGETPEDSCSEGSTADMTNTAELLEQIPDLGQDVKDPEDCFTEGCVRRCPCCAVDTTQAPGKVWWRLRKTCYH
SQ  IVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVD
SQ  VSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKF
SQ  GRCINQTEGDLPLNYTIVNNKSQCESLNLTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQW
SQ  EYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGF
SQ  IFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKINILAKINLLFVAIFTGECIVKLAALRHYYFTNSWNIFDFVVVI
SQ  LSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFA
SQ  YVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPTLPNSNGSRGDCGSPAVGILFFTTYIIISF
SQ  LIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYSVLSDFADALSEPLRIAKPNQISLINMDL
SQ  PMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSAMVIQRAFRRHLLQRS
SQ  LKHASFLFRQQAGSGLSEEDAPEREGLIAYVMSENFSRPLGPPSSSSISSTSFPPSYDSVTRATSDNLQVRGSDYSHSED
SQ  LADFPPSPDRDRESIV
//
ID  Q9JJV9;
PN  Sodium channel protein type 5 subunit alpha;
GN  Scn5a;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:11834499, ECO:0000269|PubMed:23420830}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14524}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:P15389}. Note=RANGRF promotes trafficking to the cell membrane. {ECO:0000269|PubMed:23420830}.
DR  UNIPROT: Q9JJV9;
DR  UNIPROT: E9Q1D2;
DR  UNIPROT: Q3UH91;
DR  Pfam: PF00520;
DR  Pfam: PF06512;
DR  Pfam: PF11933;
DE  Function: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (PubMed:11834499, PubMed:23420830). It is a tetrodotoxin-resistant Na(+) channel isoform. This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels (By similarity). {ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:11834499, ECO:0000269|PubMed:23420830}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Z0J4; IntAct: EBI-15712165; Score: 0.35
DE  Interaction: Q6Q477; IntAct: EBI-15712165; Score: 0.35
DE  Interaction: Q61234; IntAct: EBI-15712165; Score: 0.35
DE  Interaction: Q4U4S6; IntAct: EBI-26520955; Score: 0.40
GO  GO:0005901;
GO  GO:0009986;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0014704;
GO  GO:0016328;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0042383;
GO  GO:0034706;
GO  GO:0030315;
GO  GO:0001518;
GO  GO:0030018;
GO  GO:0030506;
GO  GO:0005516;
GO  GO:0019899;
GO  GO:0017134;
GO  GO:0050998;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0097110;
GO  GO:0044325;
GO  GO:0031625;
GO  GO:0005244;
GO  GO:0005248;
GO  GO:0086060;
GO  GO:0086061;
GO  GO:0086006;
GO  GO:0086062;
GO  GO:0086063;
GO  GO:0086014;
GO  GO:0086016;
GO  GO:0086067;
GO  GO:0086043;
GO  GO:0086002;
GO  GO:0060048;
GO  GO:0003231;
GO  GO:0071277;
GO  GO:0051899;
GO  GO:0086010;
GO  GO:0098912;
GO  GO:0086045;
GO  GO:0086048;
GO  GO:0086012;
GO  GO:0086047;
GO  GO:0086046;
GO  GO:0019228;
GO  GO:0045760;
GO  GO:0050679;
GO  GO:0010460;
GO  GO:0010765;
GO  GO:0060371;
GO  GO:0060372;
GO  GO:0086004;
GO  GO:0002027;
GO  GO:0086091;
GO  GO:1902305;
GO  GO:0060373;
GO  GO:0060307;
GO  GO:0014894;
GO  GO:0014070;
GO  GO:0086015;
GO  GO:0098719;
GO  GO:0035725;
GO  GO:0006814;
GO  GO:0086005;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:D0E0C2};
SQ  MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSATSQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPRELIGEPL
SQ  EDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPVRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKYV
SQ  EYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIV
SQ  GALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGIVWNSLDVYLNDPANYLLKNGT
SQ  TDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLG
SQ  SFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVTNHERRSKRRK
SQ  RLSSGTEDGGDDRLPKSDSEDGPRALNQLSLTHGLSRTSMRPRSSRGSIFTFRRRDQGSEADFADDENSTAGESESHRTS
SQ  LLVPWPLRRPSTQGQPGFGTSAPGHVLNGKRNSTVDCNGVVSLLGAGDAEATSPGSHLLRPIVLDRPPDTTTPSEEPGGP
SQ  QMLTPQAPCADGFEEPGARQRALSAVSVLTSALEELEESHRKCPPCWNRFAQHYLIWECCPLWMSIKQKVKFVVMDPFAD
SQ  LTITMCIVLNTLFMALEHYNMTAEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSR
SQ  MGNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRHRISDSGLLPR
SQ  WHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDGEMNN
SQ  LQLALARIQRGLRFVKRTTWDFCCGLLRRRPKKPAALATHSQLPSCIAAPRSPPPPEVEKAPPARKETRFEEDKRPGQGT
SQ  PGDTEPVCVPIAVAESDTDDQEEDEENSLGTEEEESSKQESQVVSGGHEPPQEPRAWSQVSETTSSEAEASTSQADWQQE
SQ  REAEPRAPGCGETPEDSYSEGSTADMTNTADLLEQIPDLGEDVKDPEDCFTEGCVRRCPCCMVDTTQAPGKVWWRLRKTC
SQ  YRIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLI
SQ  VDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAG
SQ  KFGRCINQTEGDLPLNYTIVNNKSECESFNVTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQP
SQ  QWEDNLYMYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQ
SQ  GFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKVNILAKINLLFVAIFTGECIVKMAALRHYYFTNSWNIFDFVV
SQ  VILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMAN
SQ  FAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYIII
SQ  SFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYLALSDFADALSEPLRIAKPNQISLINM
SQ  DLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSATVIQRAFRRHLLQ
SQ  RSVKHASFLFRQQAGSSGLSDEDAPEREGLIAYMMNENFSRRSGPLSSSSISSTSFPPSYDSVTRATSDNLPVRASDYSR
SQ  SEDLADFPPSPDRDRESIV
//
ID  P15389;
PN  Sodium channel protein type 5 subunit alpha;
GN  Scn5a;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q14524}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14524}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:15579534}. Note=RANGRF promotes trafficking to the cell membrane. {ECO:0000250|UniProtKB:Q14524}.
DR  UNIPROT: P15389;
DR  UNIPROT: Q925G6;
DR  PDB: 6UZ0;
DR  PDB: 6UZ3;
DR  PDB: 7FBS;
DR  PDB: 7K18;
DR  Pfam: PF00520;
DR  Pfam: PF06512;
DR  Pfam: PF11933;
DE  Function: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant Na(+) channel isoform. This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels. {ECO:0000250|UniProtKB:Q14524, ECO:0000250|UniProtKB:Q9JJV9}.
DE  Reference Proteome: Yes;
DE  Interaction: Q64273; IntAct: EBI-15981683; Score: 0.35
DE  Interaction: Q62696; IntAct: EBI-15981701; Score: 0.35
GO  GO:0005901;
GO  GO:0009986;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0014704;
GO  GO:0016328;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0042383;
GO  GO:0034706;
GO  GO:0030315;
GO  GO:0001518;
GO  GO:0030018;
GO  GO:0030506;
GO  GO:0005516;
GO  GO:0019899;
GO  GO:0017134;
GO  GO:0050998;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0097110;
GO  GO:0044325;
GO  GO:0031625;
GO  GO:0005244;
GO  GO:0005248;
GO  GO:0086060;
GO  GO:0086061;
GO  GO:0086006;
GO  GO:0086062;
GO  GO:0086063;
GO  GO:0086014;
GO  GO:0086016;
GO  GO:0086067;
GO  GO:0003360;
GO  GO:0086043;
GO  GO:0086002;
GO  GO:0060048;
GO  GO:0003231;
GO  GO:0071277;
GO  GO:0021549;
GO  GO:0051899;
GO  GO:0086010;
GO  GO:0098912;
GO  GO:0086045;
GO  GO:0086048;
GO  GO:0086012;
GO  GO:0086047;
GO  GO:0086046;
GO  GO:0019228;
GO  GO:0042475;
GO  GO:0045760;
GO  GO:0050679;
GO  GO:0010460;
GO  GO:0010765;
GO  GO:0060371;
GO  GO:0060372;
GO  GO:0086004;
GO  GO:0002027;
GO  GO:0086091;
GO  GO:1902305;
GO  GO:0060373;
GO  GO:0060307;
GO  GO:0014894;
GO  GO:0014070;
GO  GO:0086015;
GO  GO:0098719;
GO  GO:0035725;
GO  GO:0006814;
GO  GO:0021537;
GO  GO:0086005;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:D0E0C2};
SQ  MANLLLPRGTSSFRRFTRESLAAIEKRMAEKQARGGSATSQESREGLQEEEAPRPQLDLQASKKLPDLYGNPPRELIGEP
SQ  LEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPVRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKY
SQ  VEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTI
SQ  VGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGLVWNSLDVYLNDPANYLLKNG
SQ  TTDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFL
SQ  GSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVTNHERKSKRR
SQ  KRLSSGTEDGGDDRLPKSDSEDGPRALNQLSLTHGLSRTSMRPRSSRGSIFTFRRRDQGSEADFADDENSTAGESESHRT
SQ  SLLVPWPLRHPSAQGQPGPGASAPGYVLNGKRNSTVDCNGVVSLLGAGDAEATSPGSYLLRPMVLDRPPDTTTPSEEPGG
SQ  PQMLTPQAPCADGFEEPGARQRALSAVSVLTSALEELEESHRKCPPCWNRFAQHYLIWECCPLWMSIKQKVKFVVMDPFA
SQ  DLTITMCIVLNTLFMALEHYNMTAEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLS
SQ  RMGNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRHRISDSGLLP
SQ  RWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDGEMN
SQ  NLQLALARIQRGLRFVKRTTWDFCCGILRRRPKKPAALATHSQLPSCITAPRSPPPPEVEKVPPARKETRFEEDKRPGQG
SQ  TPGDSEPVCVPIAVAESDTEDQEEDEENSLGTEEESSKQESQVVSGGHEPYQEPRAWSQVSETTSSEAGASTSQADWQQE
SQ  QKTEPQAPGCGETPEDSYSEGSTADMTNTADLLEQIPDLGEDVKDPEDCFTEGCVRRCPCCMVDTTQSPGKVWWRLRKTC
SQ  YRIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLI
SQ  VDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAG
SQ  KFGRCINQTEGDLPLNYTIVNNKSECESFNVTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQP
SQ  QWEDNLYMYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQ
SQ  GFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKVNILAKINLLFVAIFTGECIVKMAALRHYYFTNSWNIFDFVV
SQ  VILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMAN
SQ  FAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYIII
SQ  SFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYLALSDFADALSEPLRIAKPNQISLINM
SQ  DLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSATVIQRAFRRHLLQ
SQ  RSVKHASFLFRQQAGGSGLSDEDAPEREGLIAYMMNGNFSRRSAPLSSSSISSTSFPPSYDSVTRATSDNLPVRASDYSR
SQ  SEDLADFPPSPDRDRESIV
//
ID  P40075;
PN  Vesicle-associated membrane protein-associated protein SCS2;
GN  SCS2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Nucleus membrane; Single-pass type IV membrane protein.
DR  UNIPROT: P40075;
DR  UNIPROT: D3DM26;
DR  PDB: 6LP4;
DR  Pfam: PF00635;
DR  PROSITE: PS50202;
DE  Function: Targets proteins containing a FFAT motif to endoplasmic reticulum membranes. Regulates phospholipid biosynthesis by modulating the subcellular localization of the transcriptional repressor OPI1. {ECO:0000269|PubMed:12727870, ECO:0000269|PubMed:15668246}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P35845; IntAct: EBI-803541; Score: 0.55
DE  Interaction: P40069; IntAct: EBI-7043141; Score: 0.35
DE  Interaction: P53968; IntAct: EBI-393147; Score: 0.37
DE  Interaction: P17064; IntAct: EBI-7774593; Score: 0.37
DE  Interaction: P21957; IntAct: EBI-788157; Score: 0.59
DE  Interaction: P16140; IntAct: EBI-803541; Score: 0.53
DE  Interaction: P37297; IntAct: EBI-803541; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-803541; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-803541; Score: 0.53
DE  Interaction: P10591; IntAct: EBI-803541; Score: 0.53
DE  Interaction: P38886; IntAct: EBI-803541; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-803541; Score: 0.35
DE  Interaction: P53252; IntAct: EBI-803541; Score: 0.53
DE  Interaction: Q12451; IntAct: EBI-803541; Score: 0.55
DE  Interaction: Q00402; IntAct: EBI-803541; Score: 0.69
DE  Interaction: P38631; IntAct: EBI-803541; Score: 0.35
DE  Interaction: P12385; IntAct: EBI-813651; Score: 0.27
DE  Interaction: P47088; IntAct: EBI-856798; Score: 0.00
DE  Interaction: P40509; IntAct: EBI-7677816; Score: 0.40
DE  Interaction: P53622; IntAct: EBI-8225904; Score: 0.22
DE  Interaction: Q03656; IntAct: EBI-2613750; Score: 0.35
DE  Interaction: P38713; IntAct: EBI-3843675; Score: 0.57
DE  Interaction: P39523; IntAct: EBI-9977109; Score: 0.62
DE  Interaction: Q07657; IntAct: EBI-9977134; Score: 0.63
DE  Interaction: P34216; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P25694; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P34760; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P32610; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P00358; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: Q12230; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: Q06385; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P19882; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: Q12377; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P00925; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P60010; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P21672; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: Q08229; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P07149; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P18759; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P22137; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P38616; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P00950; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: Q03661; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P19097; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P28834; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P47079; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P41277; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P28241; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: P22203; IntAct: EBI-9975925; Score: 0.35
DE  Interaction: O15209; IntAct: EBI-11530372; Score: 0.56
DE  Interaction: Q08984; IntAct: EBI-12425154; Score: 0.37
DE  Interaction: Q04660; IntAct: EBI-16268743; Score: 0.35
DE  Interaction: P38882; IntAct: EBI-16289509; Score: 0.35
GO  GO:0005935;
GO  GO:0005934;
GO  GO:0000781;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0071561;
GO  GO:0005886;
GO  GO:0033149;
GO  GO:0035091;
GO  GO:0048309;
GO  GO:0090158;
GO  GO:0061163;
GO  GO:0061817;
GO  GO:0042308;
GO  GO:0008654;
GO  GO:0032377;
GO  GO:0060304;
GO  GO:0031509;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAVEISPDVLVYKSPLTEQSTEYASISNNSDQTIAFKVKTTAPKFYCVRPNAAVVAPGETIQVQVIFLGLTEEPAADFK
SQ  CRDKFLVITLPSPYDLNGKAVADVWSDLEAEFKQQAISKKIKVKYLISPDVHPAQNQNIQENKETVEPVVQDSEPKEVPA
SQ  VVNEKEVPAEPETQPPVQVKKEEVPPVVQKTVPHENEKQTSNSTPAPQNQIKEAATVPAENESSSMGIFILVALLILVLG
SQ  WFYR
//
ID  Q75BS2;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  284811;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q75BS2;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTITNAHTELIHDAVLDYYGKRLATCSSDKTIQIFEVDGDSHKLVDSLHGHEGPVWQVDWAHPKFGVILASCSYDGKVL
SQ  IWKEENGRWSQIAAYEVHSASVNSVKWAPHEYGPLLLCSSSDGKFSVVEFKENGTTSPIIIDAHAIGVNAACWAPATIED
SQ  DGQQSQHLRRIATGGADNLVKIWKYNPEANTYLLEDTLAAHADWVRDVAWSPSVLPRAYLATVSQDRTCIIWTQENNQGP
SQ  WTKTLLKEDKFPDVLWRASWSLSGNILALSGGDNKVTLWKENLEGKWESAAEIEQ
//
ID  A1CGS0;
PN  Protein transport protein sec13;
GN  sec13;
OS  344612;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: A1CGS0;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Sec13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MIHDAGLDYYGRRLATCSSDKTIKIFEIEGETHRLAETLKGHEGAVWCVAWAHPKFGTILASSSYDGKVLIWREQHQSPT
SQ  SPAAGSAWTKVFDFSLHTASVNMVSWAPHESGCLLACASSDGHVSVLEFRDNSWTHQIFHAHGMGVNSISWAPAAAPGSL
SQ  ISSNPGPGQQRRFVTGGSDNLLKIWDYNPESKTYNITQTLEGHSDWVRDVAWSPSILSKSYIASASQDKTVRIWTSDASN
SQ  PGQWTSQQLEFDTVLWRVSWSPSGNILAVSGGDNKVSLWKENLKGQWEKVKDIEE
//
ID  Q4WNK7;
PN  Protein transport protein sec13;
GN  sec13;
OS  330879;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q4WNK7;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Sec13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTRGTNLVGPFLQHDAGLDYYGRRLATCSSDKTIKIFEIEGETHRLIETLKGHEGAVWCVAWAHPKFGTILASSSYDGKV
SQ  LIWREQHQNATSPVAGSTWTKVFDFSLHTASVNMVSWAPHESGCLLACASSDGHVSVLEFRDNSWTHQIFHAHGMGVNSI
SQ  SWAPAASPGSLISSNPGPGQQRRFVTGGSDNLLKIWDYNPESKTYNLSQTLEGHSDWVRDVAWSPSILSKSYIASASQDK
SQ  TVRIWTSDASNPGQWTSQQLEFDTVLWRVSWSPSGNILAVSGGDNKVSLWKENLKGQWEKVKDIEE
//
ID  A2QHM1;
PN  Protein transport protein sec13;
GN  sec13;
OS  425011;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: A2QHM1;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Sec13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAAQVISNSGHDEMIHDAGLDYYGRRLATCSSDKTIKIFEIEGETHRLIETLKGHEGAVWCVAWAHPKFGTILASSSYDG
SQ  KVLIWREQHQNATSPVAGGAWTKVFDFSLHTASVNMVSWAPHESGCLLACASSDGHVSVLEFRDNSWTHQIFHAHGMGVN
SQ  SISWAPAAAPGSLISSNPGPGQQRRFVTGGSDNLLKIWDYNPETKTYNNTQTLEGHSDWVRDVAWSPSVLSKSYIASASQ
SQ  DKTVRIWTSDASNPGQWTSQQLEFDTVLWRVSWSPSGNILAVSGGDNKVSLWKENLKGQWEKVKDIEE
//
ID  Q2UG43;
PN  Protein transport protein sec13;
GN  sec13;
OS  510516;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q2UG43;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Sec13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MHDAGLDYYGRRLATCSSDKTIKIFEIEGETHRLVETLKGHEGAVWCIAWAHPKFGTILASSSYDGKVLIWREQHQNTTS
SQ  PVAVNTWTKVFDFSLHTASVNMVSWAPHESGCLLACASSDGHVSVLEFQDNSWTHQIFHAHGMGVNSISWAPAASPGSLI
SQ  SANPGPGQQRRFVTGGSDNLLKIWDYNSETKSYNLSQTLEGHSDWVRDVAWSPSILSKSYIASASQDKTVRIWTSDVSNP
SQ  GQWASQQLEFDTVLWRVSWSPSGNILAVSGGDNKVSLWKENLKGQWEKVKDIEE
//
ID  Q0CHM0;
PN  Protein transport protein sec13;
GN  sec13;
OS  341663;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q0CHM0;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Sec13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAAAQVISNSGHEDMIHDAGLDYYGRRLATCSSDKTIKVFEIEGEAHRLVETLKGHEGAVWCVAWAHPKFGTILASSSYD
SQ  GKVLIWREQHQNTTSPAAGSAWTKVFDFSLHTASVNMVSWAPHESGCLLGCASSDGHVSVLEFQDNSWTHQIFHAHGMGV
SQ  NSISWAPAAAPGSLISANPGPGQQRRFVTGGSDNLLKIWDYNPETKTYNLSQTLEGHSDWVRDVAWSPSILSKSYIASAS
SQ  QDKTVRIWTSDASNPGQWTSQQLEFDSVLWRVSWSPSGNILAVSGGDNKVSLWKENLKGQWEKVKDIEE
//
ID  Q3ZCC9;
PN  Protein SEC13 homolog;
GN  SEC13;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P55735}. Lysosome membrane {ECO:0000250|UniProtKB:P55735}. Note=In interphase, localizes at both sides of the NPC. {ECO:0000250|UniProtKB:P55735}.
DR  UNIPROT: Q3ZCC9;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles. Required for the exit of adipsin (CFD/ADN), an adipocyte-secreted protein from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P55735, ECO:0000250|UniProtKB:Q9D1M0}. As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. {ECO:0000250|UniProtKB:P55735}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0042802;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0090110;
GO  GO:0051028;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0072659;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P55735};
SQ  MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILVADLRGHEGPVWQVAWAHPMYGNILASCSYD
SQ  RKVIIWKEENGTWEKTHEHTGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGLGQWEVKKINNAHTIGCNAVSWAP
SQ  AVVPGSLIDQPSGQKPNYIKKFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRV
SQ  FVWTCDDASGNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGPVSTSVTEGQQN
SQ  DQ
//
ID  A8XJ40;
PN  Protein SEC13 homolog;
GN  npp;
OS  6238;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P55735}. Lysosome membrane {ECO:0000250|UniProtKB:P55735}.
DR  UNIPROT: A8XJ40;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. {ECO:0000250|UniProtKB:P55735}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:P55735}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005765;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0010973;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P55735};
SQ  MTTIRQRIDTQHRDAIHDAQLNIYGNRLATCGSDRLVKIFEVRPNGQSYPLIELSGHNGPVWKVSWAHPKYGGLLASASY
SQ  DKKVIIWQEVNGRWQKTYEWETHEASVTSVAFAPHQFGLMLASSSADGTIGILRFDAQTQQWQSSRIQNCHDQGVNSVSW
SQ  APGTADPAGKKRFVSAGNDKLVKIWLLNEELNEWTCEKAIHCHKDFVREAAWCPVTNKGQHSIVSCGLDGNLVLYRIADI
SQ  ETAEWKSKLLEQAPCALYHASFSPCGSFLSVSGDDNMITLWRENLQGQWIKIPRENKEREGMGQQR
//
ID  Q9N4A7;
PN  Protein SEC13 homolog;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21478858}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:21478858}. Lysosome membrane {ECO:0000250|UniProtKB:P55735}. Note=Localizes close to endoplasmic reticulum exit sites (ERES) and the nuclear envelopes of proliferating germ nuclei. {ECO:0000269|PubMed:21478858}.
DR  UNIPROT: Q9N4A7;
DR  UNIPROT: Q9N4A6;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat (By similarity). Required for the nuclear import of hcp-4 during mitotic prophase, this step is essential for centrosome assembly and resolution (PubMed:28122936). {ECO:0000250|UniProtKB:P55735, ECO:0000269|PubMed:28122936}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:P55735}.
DE  Reference Proteome: Yes;
DE  Interaction: O01870; IntAct: EBI-335258; Score: 0.00
DE  Interaction: H2KZQ8; IntAct: EBI-2416122; Score: 0.49
DE  Interaction: P34643; IntAct: EBI-2421514; Score: 0.49
DE  Interaction: Q9XWR1; IntAct: EBI-6456137; Score: 0.37
DE  Interaction: Q1ZXS5; IntAct: EBI-6457496; Score: 0.37
DE  Interaction: P91001; IntAct: EBI-6460971; Score: 0.37
DE  Interaction: Q03563; IntAct: EBI-6462989; Score: 0.37
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005765;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0051301;
GO  GO:0090114;
GO  GO:0009792;
GO  GO:1990893;
GO  GO:0051028;
GO  GO:0051169;
GO  GO:0006997;
GO  GO:0010973;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P55735};
SQ  MTTVRQRIDTQHRDAIHDAQLNIYGSRLATCGSDRLVKIFEVRPNGQSYPMAELVGHSGPVWKVSWAHPKYGGLLASASY
SQ  DKKVIIWNEQQGRWQKAYEWAAHEASTTCVAFAPHQYGLMLASASADGDIGILRYDNSSNEWISSKIQKCHEQGVNSVCW
SQ  APGSADPAAKKRLVSAGNDKNVKIWAFDDATNEWILEKTLAGHTDFVREAAWCPVTNNGQHTIVSCGMEGNLVLFRTSNI
SQ  ETEEWKAKLLETAPCALYHSSFSPCGSFLSVAGDDNVITIWRENLQGQWIKVPRDNKEREGMSQAVGAPGAQR
//
ID  Q5AEF2;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  237561;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q5AEF2;
DR  UNIPROT: A0A1D8PJN9;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTIGNAHDDLIHDAVLDYYGKRLATCSSDKTIKIFDLDGTDNYKLITTLTGHEGPVWQVSWAHPKFGSILASCSYDGKA
SQ  LIWKEQPETQQWSIIAEHTVHQASVNSVSWAPHELGAVLLCTSSDGKVSVVDFNDDGTTSHVIFDAHAIGANSATWAPVS
SQ  TSSKDSAALKQQRRIVSCGSDNLAKIWKYDAANNTYVEEAKLEGHTDWVRDVAWSPSNLIRSYIATASQDRTVLIWTQDR
SQ  DGKWQKQLLTEEKFPDVCWRCSWSLSGNILAVSGGDNKVSLWKENLQGKWESAGEVDQ
//
ID  Q2GSM6;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  306901;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q2GSM6;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MIHDAVLDYYGRRLATCSSDRTIKIFEIEGETQRLTETLKGHDGAVWCVSWAHPKYGNILASAGYDGKVLIWREQNGAWQ
SQ  RIYDFSLHKASVNVVSWSPHEAGCVLACASSDGNVSVLEFKDNNSWEHSIFHAHGLGVNSVSWAPATNPGSIVSSKPSPK
SQ  STGNRRFVTGGSDNALKIWAFDAATGAYKLEREPLTGHTDWVRDVAWSPTVLQKSYIASASEDRTVRIWTSDPANPQQWN
SQ  CKVLGFDAAVWRVSWSLSGNVLAASGGDNKVTLWKENLKGEWECVKSIEE
//
ID  G0SA60;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: G0SA60;
DR  UNIPROT: G0ZGU9;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
DE  Interaction: G0S2G1; IntAct: EBI-16069540; Score: 0.49
DE  Interaction: G0SAK3; IntAct: EBI-16069606; Score: 0.44
DE  Interaction: G0SDQ4; IntAct: EBI-16069846; Score: 0.35
GO  GO:0030127;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQQASGAQVITNSGHDDMIHDAVLDYYGRRLATCSSDRTIKIFEIDGDSQRLTETLKGHDGAVWCVSWAHPKYGNILAS
SQ  AGYDGKVFIWRELNGAWSRIYDFALHKASVNVVSWAPHEAGCLLACASSDGSVSVLEFKDNSTWDYVIFPAHGLGVNSVS
SQ  WAPATSPGSIVSSKPGPKATGNRRFVTGGSDNTLKIWAYDPATNTYKMEREPLTGHTDWVRDVAWSPTVLQKSYIASASQ
SQ  DGTVRIWTSDPANPLAWNCKVLHFDSALWRVSWSLSGNVLAVSGSDNKVTLWKENLKGEWECVKTIEE
//
ID  Q1DZQ0;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  246410;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q1DZQ0;
DR  UNIPROT: J3KDG8;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAQVITNSGHDDMIHDAGMDYYGRRLATCSSDKTIKIFELEGDSHRLIETLKGHEGAVWCVAWAHPKFGTILASSSYDGK
SQ  VLIWREQSSAASTGSSWSRVFDFSLHTASVNMVSWAPHELGCVLACASSDGHVSVLEFRDNSWTHQIFHAHGMGVNSVSW
SQ  APAAAPGSVISATPSTGQIRRFVTGGSDNLVKIWDYNPETKTYATSHVLEGHTGWVRDVSWSPSILSRSYIASASQDKTV
SQ  RIWTSDPSNPNEWTSHQLEFDAVVWRVSWSLSGNILAVSGGDNKVSLWKENLKGQWEKVKDIEE
//
ID  P0CS51;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  283643;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: P0CS51;
DR  UNIPROT: Q55MW6;
DR  UNIPROT: Q5KB95;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: No;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MCLWPLIQSAQASKPVPVETQHEDMIHDAQLDYYGKRLATCSSDRTIRIFNVIKGEAKGEPVILKGHTAAVWQVSWAHPS
SQ  FGSILASCSYDGRVFIWKEVGQGQGKGSGGELQDGWERIKEHTLHTASVNSIAWAPYDLGPILACASSDGKVSVLSFQND
SQ  GSIEVNIFPAHGTGANAISWAPSVLSTVSGVSRSQQPSNSLAPQKRFVTAGSDNLIRIWGFDEEQKKWTEEETIKGHEDW
SQ  VRDVAWAPNIGLPGMYIASASQDRTVLIHSRPSPSSSWTSAPLLPSLPQSQDPHFPDAVWRVSWSLAGNVLAVSCGDGKV
SQ  SLWKEGVGKGWECVSDFSS
//
ID  P0CS50;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  214684;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: P0CS50;
DR  UNIPROT: Q55MW6;
DR  UNIPROT: Q5KB95;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MCLWPLIQSAQASKPVPVETQHEDMIHDAQLDYYGKRLATCSSDRTIRIFNVIKGEAKGEPVILKGHTAAVWQVSWAHPS
SQ  FGSILASCSYDGRVFIWKEVGQGQGKGSGGELQDGWERIKEHTLHTASVNSIAWAPYDLGPILACASSDGKVSVLSFQND
SQ  GSIEVNIFPAHGTGANAISWAPSVLSTVSGVSRSQQPSNSLAPQKRFVTAGSDNLIRIWGFDEEQKKWTEEETIKGHEDW
SQ  VRDVAWAPNIGLPGMYIASASQDRTVLIHSRPSPSSSWTSAPLLPSLPQSQDPHFPDAVWRVSWSLAGNVLAVSCGDGKV
SQ  SLWKEGVGKGWECVSDFSS
//
ID  Q6BIR1;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  284592;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q6BIR1;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTIGNAHDDLIHDAVLDYYGKRLATCSSDKTIKLFEVEGTENYKLVETLIGHEGPVWQVAWAHPKFGSILASCSYDGKA
SQ  LIWKEQPETQQWSIIAEHTVHQASVNSVSWAPHELGAILLCTSSDGKVSVVDFNDDGTTSHIIFDAHAIGVNSASWAPLS
SQ  NNNTKGKDTNSIRRFVTCGSDNLAKIWKFDSSKNAYIEEAVLEGHTDWVRDVCWSPSILIRSYIATASQDRTVLIWSQDN
SQ  NGKWQKQLLTEEMFPDVCWRCSWSLSGNILAVSGGDNKVSLWKENLQGKWESAGEVE
//
ID  Q54DS8;
PN  Protein SEC13 homolog;
GN  sec13;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P55735}. Lysosome membrane {ECO:0000250|UniProtKB:P55735}.
DR  UNIPROT: Q54DS8;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. {ECO:0000250|UniProtKB:P55735}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005765;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0006888;
GO  GO:0051028;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P55735};
SQ  MATQNVDSGHEDMVHDAQFDYYGKFLATCSSDKMIKIFDVGGENPQHLVDLRGHEGPVWQVAWAHPKFGKILASASYDRK
SQ  VIVWKEVGNNSWSIIHQYAGHELSVNSISWAPHEFGLSLACASSDGSVTIHNYNNNVWEAPQKIQVSQIGVNSVSWSPAA
SQ  IPTSLVNSANTIIPAPIKRIVTGSCDNLIKIFKNVEDKWILDKQLEDHKDWVRDVAWAPNIGLPYSKIASCSQDRSVIVW
SQ  TQDENGVWSGKPLPKFDDIVWRVSWSVIGNILAVSCGDNQVTLWKEGVDSEWKLISHVENN
//
ID  Q9V3J4;
PN  Protein SEC13 homolog;
GN  Sec13;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:20144761}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20144761}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20144761}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:20144761}. Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Lysosome membrane {ECO:0000305|PubMed:27166823}. Note=Localizes to chromatin, specifically to areas undergoing transcriptional activation. Chromatin localization is independent of the nuclear pore complex (PubMed:20144761).
DR  UNIPROT: Q9V3J4;
DR  UNIPROT: Q7KLW8;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat (By similarity). At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles (By similarity). Recruited to transcriptionally active chromatin at the time of transcription initiation by RNA polymerase II (PubMed:20144761). Required for proper expression of ecdysone-responsive genes such as Eip74EF and Eip75B during larval development (PubMed:20144761). Required for reactivation of transcription after heat shock (PubMed:20144761). Required for nuclear import of phosphorylated Mad via importin msk (PubMed:20547758). Has no role in classical nuclear localization signal (cNLS)-dependent nuclear import via importin-beta (PubMed:20547758). {ECO:0000250|UniProtKB:P55735, ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:20547758}. A component of the GATOR subcomplex GATOR2 which functions as an activator of the amino acid-sensing branch of the TORC1 signaling pathway (PubMed:27166823). The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the TORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation (PubMed:27166823). GATOR2 activates the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex, controlling the switch to cell proliferation and growth under nutrient replete conditions and during female oocyte development (PubMed:27166823). {ECO:0000269|PubMed:27166823}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VM98; IntAct: EBI-213755; Score: 0.00
DE  Interaction: Q9VPR6; IntAct: EBI-231935; Score: 0.00
DE  Interaction: A1Z7J7; IntAct: EBI-281518; Score: 0.00
DE  Interaction: Q24323; IntAct: EBI-9935156; Score: 0.35
DE  Interaction: Q7KN04; IntAct: EBI-9936955; Score: 0.35
DE  Interaction: Q8SYH8; IntAct: EBI-26738085; Score: 0.49
DE  Interaction: Q9W2K8; IntAct: EBI-26738075; Score: 0.49
DE  Interaction: Q8MRL2; IntAct: EBI-26738065; Score: 0.49
DE  Interaction: P56672; IntAct: EBI-26738055; Score: 0.49
DE  Interaction: Q7K049; IntAct: EBI-26738045; Score: 0.49
GO  GO:0000785;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0005765;
GO  GO:0005815;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0005703;
GO  GO:0035859;
GO  GO:0003682;
GO  GO:0005198;
GO  GO:0034605;
GO  GO:0035293;
GO  GO:0090114;
GO  GO:0035077;
GO  GO:0008363;
GO  GO:0051028;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0045944;
GO  GO:0060261;
GO  GO:0032527;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MVSLLQEIDTEHEDMVHHAALDFYGLLLATCSSDGSVRIFHSRKNNKALAELKGHQGPVWQVAWAHPKFGNILASCSYDR
SQ  KVIVWKSTTPRDWTKLYEYSNHDSSVNSVDFAPSEYGLVLACASSDGSVSVLTCNTEYGVWDAKKIPNAHTIGVNAISWC
SQ  PAQAPDPAFDQRVTSRSAAVKRLVSGGCDNLVKIWREDNDRWVEEHRLEAHSDWVRDVAWAPSIGLPRSQIATASQDRHV
SQ  IVWSSNADLSEWTSTVLHTFDDAVWSISWSTTGNILAVTGGDNNVTLWKENTEGQWIRINYESGTAIQSKQPSHLPHSHS
SQ  QQQQALQQHQQQAPSHPGPSSDSEHSSNLSNSQLSN
//
ID  Q5B563;
PN  Protein transport protein sec13;
GN  sec13;
OS  227321;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q5B563;
DR  UNIPROT: C8V976;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Sec13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAAAQVISNSGHDDMIHDAGLDYYGRRLATCSSDKTIKIFEIEGDTHKLVETLKGHEGPVWCVEWAHPKFGTILASSSYD
SQ  GKVLIWREQHQSSTAPIGSGAWTKVFDFSLHTASVNMISWAPHETGCLLACASSDGHVSVLEFRDNSWTHQIFHAHGMGV
SQ  NSISWAPAASPGSLVSSNPGIGQQRRFVTGGSDNLLKIWDYNPETKTYNATQTLEGHSDWVRDVAWSPSILSKSYIASAS
SQ  QDKTVRVWTADASNPGQWTSQVLEFDNVLWRVSWSPSGNILAVSGGDNKVSLWKENLRGQWEKVKDIEE
//
ID  P55735;
PN  Protein SEC13 homolog;
GN  SEC13;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:8972206}; Peripheral membrane protein {ECO:0000269|PubMed:8972206}; Cytoplasmic side {ECO:0000269|PubMed:8972206}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:8972206}; Peripheral membrane protein {ECO:0000269|PubMed:8972206}; Cytoplasmic side {ECO:0000269|PubMed:8972206}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:14517296, ECO:0000269|PubMed:18160040}. Lysosome membrane {ECO:0000269|PubMed:28199306}. Note=In interphase, localizes at both sides of the NPC. {ECO:0000269|PubMed:14517296}.
DR  UNIPROT: P55735;
DR  UNIPROT: A8MV37;
DR  UNIPROT: B4DXJ1;
DR  UNIPROT: Q5BJF0;
DR  UNIPROT: Q9BRM6;
DR  UNIPROT: Q9BUG7;
DR  PDB: 3BG0;
DR  PDB: 3BG1;
DR  PDB: 5A9Q;
DR  PDB: 7PEQ;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 600152;
DR  DisGeNET: 6396;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles (PubMed:8972206). Required for the exit of adipsin (CFD/ADN), an adipocyte-secreted protein from the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q9D1M0, ECO:0000269|PubMed:8972206}. As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex (PubMed:23723238). It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1 (PubMed:25457612, PubMed:27487210). {ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:27487210}.
DE  Reference Proteome: Yes;
DE  Interaction: O14976; IntAct: EBI-11150908; Score: 0.35
DE  Interaction: O15027; IntAct: EBI-10045785; Score: 0.35
DE  Interaction: O15504; IntAct: EBI-11888324; Score: 0.37
DE  Interaction: P00533; IntAct: EBI-1188138; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: P35729; IntAct: EBI-11888124; Score: 0.40
DE  Interaction: P37198; IntAct: EBI-11889192; Score: 0.49
DE  Interaction: P48730; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: P49687; IntAct: EBI-1580653; Score: 0.70
DE  Interaction: P52948; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: Q9NYJ8; IntAct: EBI-364084; Score: 0.00
DE  Interaction: Q96JE7; IntAct: EBI-10215087; Score: 0.67
DE  Interaction: P23508; IntAct: EBI-1064832; Score: 0.00
DE  Interaction: P62330; IntAct: EBI-1065067; Score: 0.00
DE  Interaction: P56537; IntAct: EBI-1065835; Score: 0.00
DE  Interaction: P78396; IntAct: EBI-1065995; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1085427; Score: 0.00
DE  Interaction: P38968; IntAct: EBI-1371500; Score: 0.37
DE  Interaction: P55735; IntAct: EBI-1580729; Score: 0.63
DE  Interaction: Q8AZK7; IntAct: EBI-9632715; Score: 0.35
DE  Interaction: O94979; IntAct: EBI-15564415; Score: 0.78
DE  Interaction: Q15436; IntAct: EBI-1811868; Score: 0.51
DE  Interaction: Q8BH74; IntAct: EBI-2563157; Score: 0.56
DE  Interaction: Q6PFD9; IntAct: EBI-2563676; Score: 0.56
DE  Interaction: A0A6L7HN52; IntAct: EBI-2814709; Score: 0.00
DE  Interaction: A0A0H2W3Z6; IntAct: EBI-2841273; Score: 0.00
DE  Interaction: P43351; IntAct: EBI-3646827; Score: 0.35
DE  Interaction: P56749; IntAct: EBI-3913268; Score: 0.37
DE  Interaction: P48729; IntAct: EBI-6255977; Score: 0.53
DE  Interaction: P49674; IntAct: EBI-6256083; Score: 0.53
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-6873172; Score: 0.37
DE  Interaction: Q8WYP5; IntAct: EBI-9050503; Score: 0.32
DE  Interaction: Q9BW27; IntAct: EBI-9032422; Score: 0.56
DE  Interaction: O00463; IntAct: EBI-10215073; Score: 0.56
DE  Interaction: Q92731; IntAct: EBI-9996422; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q91X51; IntAct: EBI-11015786; Score: 0.35
DE  Interaction: Q9CWZ3; IntAct: EBI-11033143; Score: 0.35
DE  Interaction: P56377; IntAct: EBI-11037753; Score: 0.35
DE  Interaction: P21333; IntAct: EBI-11038784; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: G3X972; IntAct: EBI-11079358; Score: 0.35
DE  Interaction: P09497; IntAct: EBI-11081190; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: Q13492; IntAct: EBI-11082344; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.62
DE  Interaction: P58043; IntAct: EBI-11102804; Score: 0.35
DE  Interaction: Q9Z1Z0; IntAct: EBI-11110688; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.53
DE  Interaction: Q9BPU9; IntAct: EBI-11377507; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q8NFH4; IntAct: EBI-11888954; Score: 0.66
DE  Interaction: Q96HA1; IntAct: EBI-11889618; Score: 0.37
DE  Interaction: E9PK14; IntAct: EBI-24352333; Score: 0.56
DE  Interaction: B4DHB6; IntAct: EBI-25247831; Score: 0.56
DE  Interaction: Q96D03; IntAct: EBI-22745968; Score: 0.56
DE  Interaction: Q9GZV7; IntAct: EBI-24623649; Score: 0.56
DE  Interaction: Q8IZF2; IntAct: EBI-25168512; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q9NXC5; IntAct: EBI-21716983; Score: 0.64
DE  Interaction: Q9BW85; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: Q96S15; IntAct: EBI-21716983; Score: 0.53
DE  Interaction: Q96EA4; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: Q96CP2; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: Q96BP3; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: Q8NAV1; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: Q12769; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: Q03154; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: P58004; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: P11274; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: O15400; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: O15062; IntAct: EBI-21716983; Score: 0.35
DE  Interaction: Q6PJI9; IntAct: EBI-21755234; Score: 0.53
DE  Interaction: Q92734; IntAct: EBI-21779377; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-21865034; Score: 0.53
DE  Interaction: Q01968; IntAct: EBI-16412116; Score: 0.35
DE  Interaction: Q96RS6; IntAct: EBI-20723623; Score: 0.35
DE  Interaction: Q5T011; IntAct: EBI-16752607; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-16788578; Score: 0.35
DE  Interaction: P49336; IntAct: EBI-16790691; Score: 0.35
DE  Interaction: Q15075; IntAct: EBI-16791749; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800982; Score: 0.35
DE  Interaction: Q12824; IntAct: EBI-20623811; Score: 0.42
DE  Interaction: Q9Y2H1; IntAct: EBI-20624096; Score: 0.42
DE  Interaction: Q9NPC1; IntAct: EBI-20809540; Score: 0.37
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q5T7N2; IntAct: EBI-20993270; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-25943752; Score: 0.56
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q8IZD9; IntAct: EBI-25411696; Score: 0.35
DE  Interaction: A0A0H3LAS2; IntAct: EBI-25400946; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-27084109; Score: 0.35
DE  Interaction: P42680; IntAct: EBI-28935138; Score: 0.35
DE  Interaction: Q96GD4; IntAct: EBI-28944360; Score: 0.35
DE  Interaction: Q96KG9; IntAct: EBI-28944481; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q99607; IntAct: EBI-29000285; Score: 0.35
DE  Interaction: P43694; IntAct: EBI-29011567; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
DE  Interaction: P35711; IntAct: EBI-29375677; Score: 0.35
DE  Interaction: P41212; IntAct: EBI-29015445; Score: 0.27
DE  Interaction: Q13619; IntAct: EBI-30863570; Score: 0.35
DE  Interaction: Q9Y4G2; IntAct: EBI-32711159; Score: 0.35
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
GO  GO:0030127;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0012507;
GO  GO:0070062;
GO  GO:0061700;
GO  GO:0043231;
GO  GO:0005765;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0042802;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0090110;
GO  GO:0006886;
GO  GO:0051028;
GO  GO:1904262;
GO  GO:0006913;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:8972206};
SQ  MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYD
SQ  RKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAP
SQ  AVVPGSLIDHPSGQKPNYIKRFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRV
SQ  FIWTCDDASSNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASVTEGQQN
SQ  EQ
//
ID  Q6CSZ5;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  284590;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q6CSZ5;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTINNAHSELIHDAVLDYYGKRLATCSSDHTVKIFEVEGETHKLVDTLQGHEGPVWQVDWAHPKFGVILASCSYDGKVL
SQ  IWKEVNGRWSQIAAHEVHSASVNSIQWAPHEYGPLLLAASSDGKVSVVEFKENGTTSPIIIDAHSIGANTACWAPATLQQ
SQ  QSNQGTSGSASPQQVRRFVTGGADNLVKIWKYNSDAATYLLEHTLEGHSDWVRDVAWSPTVLSRSYLASVSQDRTCIIWT
SQ  QDSKEDTWKKTLLKEDKFPDVLWRASWSLSGNILALSCGDNTVTLWKENLEGKWEPAGQVTE
//
ID  P53024;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  644223;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: P53024;
DR  UNIPROT: C4QV39;
DR  PDB: 4L9O;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
DE  Interaction: Q0PVE0; IntAct: EBI-6960543; Score: 0.27
DE  Interaction: Q0PVD7; IntAct: EBI-6960629; Score: 0.27
DE  Interaction: Q0PVD9; IntAct: EBI-6960595; Score: 0.27
DE  Interaction: Q9P4C6; IntAct: EBI-6960710; Score: 0.27
DE  Interaction: Q0PVD8; IntAct: EBI-6960663; Score: 0.27
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTIGNAHDDLIHDAVLDYYGRRLATCSSDKTIKIFEIDGENQRLVETLIGHEGPVWQVAWAHPKFGVILASCSYDGKVL
SQ  IWKEDNGVWNKVAEHSVHQASVNSVSWAPHEYGPVLLCASSDGKISIVEFKDGGALEPIVIQGHAIGVNAASWAPISLPD
SQ  NTRRFVSGGCDNLVKIWRYDDAAKTFIEEEAFQGHSDWVRDVAWSPSRLSKSYIATASQDRTVLIWTKDGKSNKWEKQPL
SQ  TKEKFPDVCWRASWSLSGNVLAISGGDNKVTLWKENIQGKWESAGEVDQ
//
ID  A5DXE2;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  379508;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: A5DXE2;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTIGNAHEDLIHDAVLDYYGKRLATCSSDKTIKIYDIEGTENYKLTATLTGHEGPIWQVAWAHPKFGSILASCSYDGKV
SQ  LIWKEQQDTQQWSIIAEHTIHQASVNSVSWAPHELGAVLLCTSSDGKVSVVDFNDDGTTSHVIFDAHAIGVNSASWAPFT
SQ  AASSTSSKDANTLKQHRRFVTCGSDNLVKIWKYDTALETYAEEAKLEGHTDWVRDVAWSPSNLVRPYIATASQDCTVLIW
SQ  TQDKDGKWQSQPLTEEKFPDVCWRCSWSLSGNILAVSGGDNKVTLWKENLQGKWESAGEVELIK
//
ID  A4REK3;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  242507;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: A4REK3;
DR  UNIPROT: G4NB29;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MIHDAVLDYYGRRLATCSSDRTIKIFEVEGETHRLTETLKGHEGAVWCVAWAHPKYGNILASSGYDGKVFIWREQGGAWQ
SQ  KIFDFALHKASVNIVSWSPHESGCLLACASSDGHVSVLEFKDNSFDHQTFLAHGQGVNSVSWAPSTAPGSIISTNATPAA
SQ  QRRFVTGGSDNTLKIWSWDAASAQYRCEEGGVLSGHTDWVLDVDWSPTVLQKSYIASASQDRTVRIWTSDSSNPGVWQSR
SQ  VLKEFDTTVWRVSWSLSGNVLAVSSGDNKVTLWKENLKGEWACVNSLED
//
ID  Q9D1M0;
PN  Protein SEC13 homolog;
GN  Sec13;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P55735}. Lysosome membrane {ECO:0000250|UniProtKB:P55735}. Note=In interphase, localizes at both sides of the NPC. {ECO:0000250|UniProtKB:P55735}.
DR  UNIPROT: Q9D1M0;
DR  UNIPROT: Q99M12;
DR  UNIPROT: Q9D712;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles (By similarity). Required for the exit of adipsin (CFD/ADN), an adipocyte-secreted protein from the endoplasmic reticulum (PubMed:27354378). {ECO:0000250|UniProtKB:P55735, ECO:0000269|PubMed:27354378}. As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. {ECO:0000250|UniProtKB:P55735}.
DE  Reference Proteome: Yes;
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: Q8CG73; IntAct: EBI-4284701; Score: 0.35
DE  Interaction: Q80Z64; IntAct: EBI-8820601; Score: 0.35
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26471064; Score: 0.35
GO  GO:0030127;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0043231;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005654;
GO  GO:0032991;
GO  GO:0042802;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0090110;
GO  GO:0006888;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0072659;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P55735};
SQ  MVSVMNTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYD
SQ  RKVIIWKEENGTWEKTHEHSGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAP
SQ  AVVPGSLIDQPSGQKPNYIKKFASGGCDNLIKLWREEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRV
SQ  FIWTCDDASGNMWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASITEGQQN
SQ  EQ
//
ID  Q7RZF5;
PN  Protein transport protein sec13;
GN  nup;
OS  367110;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
DR  UNIPROT: Q7RZF5;
DR  Pfam: PF12894;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Nup-20/sec13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTAGAQVIANSGHDDMIHDAVLDYYGRRLATCSSDRTIKIFEIEGESQRLVETLKGHDGAVWSVAWAHPKYGNILASAGY
SQ  DGKVLIWREQAGSWQRIFDFALHKASVNIVSWSPHEAGCLLACASSDGNVSVLEFKDNSWEHNIFHAHGLGVNSVSWAPA
SQ  TTPGSIVSSNPGPGSTGNRRFVTGGSDNLLKIWTFDPATNGYKLEREPLAGHTDWVRDVAWSPTVLQKSYIASASQDKTV
SQ  RIWTSDAANPGEWKCKVLNFDAAVWRVSWSLSGNVLAASSDNNKVTLWKENLKGEWENVKTIEE
//
ID  Q0UNA9;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  321614;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q0UNA9;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MADNGQNVDLLSIEANEVQHDAVLDYYGRRLATCSSDKTIKIFEVEGDKHTLVETLRGHEGPVWCVAWAHPKYGNILASS
SQ  SYDGKVIIWREQSSTWQKIYEVALHTASVNIVAWAPHEVGCLLACASSDGNVSVLEFKDNAWSHVIFQACGSGVNSVSWA
SQ  PAVAPGQVVSASGNQAGAARRFVTGGSDCQVKLWDFSAETGSWQSTQILTGHTDWVRDVAWSPTVLSKSYIASASQDKTV
SQ  RIWTSSDLRDWKSTVLNVDAVAWRVSWSLSGNVLAVSTGDNRVSLWKERLSGGWECVKTIEE
//
ID  A5DHD9;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  294746;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: A5DHD9;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTIANAHDELIHDAVLDYYGKRLATCSSDKTIKIFEVEGTENYQLTETLVGHEGPVWQVAWAHPKFGSILASCSYDGKV
SQ  LVWKESPDRSWSIISEHKVHQASVNSVSWAPHELGAVLLCTSSDGRVSVVDFNDDGTSTHIIFEAHKIGVNSASWAPVDT
SQ  KSPVRRFVTGGSDNLAKVWSLDASKSTYVEEAKLEGHTDWVRDVCWSPSALVRSYIATASQDRTVLIWHQDGEGKWQKQK
SQ  LTEELFPDVCWRCSWSFSGNILAVSGGDNKVSLWKENLQGKWESAGEVDQ
//
ID  A3LNW3;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  322104;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: A3LNW3;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTIGNAHNDLIHDAVLDYYGKRLATCSSDKSINIFDIDGTESYKLVSTLTGHDGPVWQVSWAHPKFGSILASCSFDGKA
SQ  LIWKEQPETQQWSIIAEHSVHQASVNSVSWAPHELGAVLLCASSDGKVSVVDFNDDGTTSHVVFDAHAIGANSASWAPLS
SQ  STPSPNQKDAASLKQQRRFVTCGSDNLAKIWKYDAANNTYVEEARLEGHTDWVRDVAWSPSMLVRTYIATASQDRTVLIW
SQ  TQDKAGKWQKQLLTEDKFPDVCWRCSWSLSGNILAVSGGDNKVSLWKENLQGKWESAGEVVQ
//
ID  Q5XFW8;
PN  Protein SEC13 homolog;
GN  Sec13;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P55735}. Lysosome membrane {ECO:0000250|UniProtKB:P55735}. Note=In interphase, localizes at both sides of the NPC. {ECO:0000250|UniProtKB:P55735}.
DR  UNIPROT: Q5XFW8;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles. Required for the exit of adipsin (CFD/ADN), an adipocyte-secreted protein from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P55735, ECO:0000250|UniProtKB:Q9D1M0}. As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. {ECO:0000250|UniProtKB:P55735}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0005765;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0032991;
GO  GO:0042802;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0090110;
GO  GO:0006888;
GO  GO:0051028;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:0072659;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P55735};
SQ  MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYD
SQ  RKVIIWKEENGTWEKTHEHSGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAP
SQ  AVVPGSLIDQPSGQKPNYIKKFASGGCDNLIKLWREEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRV
SQ  FIWTCDDASGNMWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASITEGQQN
SQ  EQ
//
ID  O94319;
PN  Protein transport protein sec13;
GN  sec13;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: O94319;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). Involved in septum formation. {ECO:0000250|UniProtKB:Q04491, ECO:0000269|PubMed:11821054}.
DE  Reference Proteome: Yes;
DE  Interaction: O13637; IntAct: EBI-21245983; Score: 0.37
GO  GO:0030127;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005634;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTTVDTQHDDMIHDAILDYYGKRLATCSSDQTIKVFSIENNQQTLLETLRGHSGPVWQLGWAHPKFGTILASASYDGHVI
SQ  VWRETGGVWSELMDHTAHQASVNAVSWAPHEYGALLACASSDGKVSVLEFKDDGSCDTRIFTAHEPGCNAVCWSPPSLSG
SQ  SVVGQSPAAGPKKLATAGCDNLVKIWAFDAGVNNWILEDTLAGHVDWTRDVAWAPSVGLTKTYLASASQDKNVFIWTKEG
SQ  DGPWQKTPLTEEKFPDIAWRVSWSLSGNILAVSCGDNKVYLFKESQNKWQLLNELSN
//
ID  Q4PCB8;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  237631;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q4PCB8;
DR  UNIPROT: A0A0D1E5R0;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTTVTSSSAGLSLSAERPKNIETQHEDMVHDAQLDFYGKRLATCSSDRTVKVFDIVNGTPSTTAETLHGHQGPVWQVAWA
SQ  HPTFGDILASCSYDGKVVIWKDNGAGASIGASAPYGSQSAYGAPTSSAGGWTKIKEHTLHTASVNSISWAPHELGSILAC
SQ  ASSDGNVSVLTFNNDGTWAVDLVAAHPVGCNAVSWAPAVVPGSLISAQSVGANAGAASNGEAKLVKRFASAGCDNTVKIW
SQ  EFSQEANRFVEVEALQGHSDWVRDVAFAPNVGLPRSYLATASQDRTVLIWTQDSPTAAWSKTALNPISASAAAGAGSNKF
SQ  PDTVWRVSWSVSGNVLAVSCGDGKITLWKENLKGAWECVSEMDS
//
ID  Q6BZX5;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  284591;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q04491}.
DR  UNIPROT: Q6BZX5;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). {ECO:0000250|UniProtKB:Q04491}.
DE  Reference Proteome: Yes;
GO  GO:0030127;
GO  GO:0005789;
GO  GO:0061700;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MVTIGNTHDDLIHDAVLDYYGKRLATCSSDKTIKIFEIDGDNHKLVETLRGHEGPVWQVSWAHPKFGSIIASASYDGKVF
SQ  IWREENGRWTNIAQHQHNASVNSVVWAPQEYGPLLLCASSDGNVSVVEFKEGGNCEATTFAAHDVGANSASWAPPAVSGS
SQ  LIQPINGKASNNIRIVTGGCDNLVKIWKYDPSSKTYVIEETLSGHKDWVRDVAWSSSVLSKSYIASASQDKTVIVWTQEG
SQ  NQPWKKKLLQDIPFPDVVWKVSWSLSGNVLAVSGGDNKVTLWKENLTGEWESAGVVEE
//
ID  Q04491;
PN  Protein transport protein SEC13;
GN  SEC13;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Vacuole membrane; Peripheral membrane protein.
DR  UNIPROT: Q04491;
DR  UNIPROT: D6VYK9;
DR  PDB: 2PM6;
DR  PDB: 2PM7;
DR  PDB: 2PM9;
DR  PDB: 3IKO;
DR  PDB: 3JRO;
DR  PDB: 3JRP;
DR  PDB: 3MZK;
DR  PDB: 3MZL;
DR  PDB: 4BZJ;
DR  PDB: 4BZK;
DR  PDB: 4XMM;
DR  PDB: 4XMN;
DR  PDB: 6ZG5;
DR  PDB: 6ZG6;
DR  PDB: 6ZL0;
DR  PDB: 7N84;
DR  PDB: 7N9F;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double-membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral ER membrane protein SEC12, exchanges GDP for GTP and recruits the heterodimer SEC23/24, which in turn recruits the heterotetramer SEC13-SEC31. The polymerization of COPII coat complexes then causes physically the deformation (budding) of the membrane, leading to the creation of a transport vesicle. The COPII complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23 functions as the SAR1 GTPase activating protein, whose activity is stimulated in the presence of SEC13/31. SEC13 is directly or indirectly required for normal ER membrane and nuclear envelope morphology. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10720463, ECO:0000269|PubMed:10747086, ECO:0000269|PubMed:11535824, ECO:0000269|PubMed:11717432, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12215173, ECO:0000269|PubMed:12475940, ECO:0000269|PubMed:14627716, ECO:0000269|PubMed:21454883, ECO:0000269|PubMed:2188733, ECO:0000269|PubMed:6996832, ECO:0000269|PubMed:7026045, ECO:0000269|PubMed:8548805, ECO:0000269|PubMed:8565072, ECO:0000269|PubMed:8909535, ECO:0000269|PubMed:9023343, ECO:0000269|PubMed:9199164, ECO:0000269|PubMed:9409822, ECO:0000269|PubMed:9427388}.
DE  Reference Proteome: Yes;
DE  Interaction: P35729; IntAct: EBI-812133; Score: 0.88
DE  Interaction: P36161; IntAct: EBI-16281671; Score: 0.35
DE  Interaction: P40318; IntAct: EBI-939365; Score: 0.44
DE  Interaction: P46673; IntAct: EBI-812133; Score: 0.53
DE  Interaction: P49687; IntAct: EBI-797641; Score: 0.97
DE  Interaction: P52891; IntAct: EBI-800196; Score: 0.53
DE  Interaction: P53011; IntAct: EBI-812133; Score: 0.53
DE  Interaction: Q03897; IntAct: EBI-392049; Score: 0.55
DE  Interaction: P48415; IntAct: EBI-784627; Score: 0.35
DE  Interaction: P41543; IntAct: EBI-785977; Score: 0.35
DE  Interaction: Q06102; IntAct: EBI-786567; Score: 0.35
DE  Interaction: P38968; IntAct: EBI-788839; Score: 0.84
DE  Interaction: P40482; IntAct: EBI-790183; Score: 0.35
DE  Interaction: P15303; IntAct: EBI-796945; Score: 0.35
DE  Interaction: P32639; IntAct: EBI-798593; Score: 0.35
DE  Interaction: Q03103; IntAct: EBI-811197; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-812133; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-812133; Score: 0.35
DE  Interaction: P32582; IntAct: EBI-815440; Score: 0.27
DE  Interaction: P16474; IntAct: EBI-819047; Score: 0.27
DE  Interaction: P30619; IntAct: EBI-7004382; Score: 0.44
DE  Interaction: Q04491; IntAct: EBI-1580735; Score: 0.40
DE  Interaction: Q04359; IntAct: EBI-2344074; Score: 0.37
DE  Interaction: P21965; IntAct: EBI-2617565; Score: 0.35
DE  Interaction: Q01477; IntAct: EBI-7992250; Score: 0.35
DE  Interaction: P53741; IntAct: EBI-7994013; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3676810; Score: 0.53
DE  Interaction: P33416; IntAct: EBI-3747075; Score: 0.35
DE  Interaction: P47170; IntAct: EBI-9821605; Score: 0.58
DE  Interaction: P39923; IntAct: EBI-9819823; Score: 0.35
DE  Interaction: Q08281; IntAct: EBI-9819987; Score: 0.35
DE  Interaction: P38164; IntAct: EBI-9820321; Score: 0.35
DE  Interaction: P38732; IntAct: EBI-16281671; Score: 0.35
DE  Interaction: P15992; IntAct: EBI-16281671; Score: 0.35
DE  Interaction: P05150; IntAct: EBI-16281671; Score: 0.35
GO  GO:0071944;
GO  GO:0030127;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005774;
GO  GO:0005198;
GO  GO:0090114;
GO  GO:0051028;
GO  GO:0051664;
GO  GO:0006913;
GO  GO:0045893;
GO  GO:1902953;
GO  GO:0043547;
GO  GO:0070863;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0032527;
GO  GO:0006606;
GO  GO:1903432;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MVVIANAHNELIHDAVLDYYGKRLATCSSDKTIKIFEVEGETHKLIDTLTGHEGPVWRVDWAHPKFGTILASCSYDGKVL
SQ  IWKEENGRWSQIAVHAVHSASVNSVQWAPHEYGPLLLVASSDGKVSVVEFKENGTTSPIIIDAHAIGVNSASWAPATIEE
SQ  DGEHNGTKESRKFVTGGADNLVKIWKYNSDAQTYVLESTLEGHSDWVRDVAWSPTVLLRSYLASVSQDRTCIIWTQDNEQ
SQ  GPWKKTLLKEEKFPDVLWRASWSLSGNVLALSGGDNKVTLWKENLEGKWEPAGEVHQ
//
ID  Q9HGN7;
PN  Translocation protein sec63;
GN  sec63;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9HGN7;
DR  Pfam: PF00226;
DR  Pfam: PF02889;
DR  PROSITE: PS50076;
DE  Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from sec61 may govern the activity of the translocon. sec63 may affect sec61-polypeptide interactions by increasing the affinity of targeting pathways for sec61 and/or by modifying sec61 to allow more efficient polypeptide interaction. May also be involved in SRP-dependent cotranslational translocation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031207;
GO  GO:0030544;
GO  GO:0008320;
GO  GO:0006620;
GO  GO:0031204;
GO  GO:0006614;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSEYKYDEQGIFFPVFLLVGTSCCVLPLTYSTILGPSASKEKKNVRDPFQKYRPKDLKVQRKSIFRLRYIFLILGWLAI
SQ  GFLSYKIANSRLKLNIWDPYEILGIAKGTSVDDVRRHYKRLSIKFHPDKVRNMVNTTREEVEKHYIEITNAYRALTDDKT
SQ  RENYALYGTPDVPQHISVGIALPKWISESENSIYILGFYGLVFGIVLPYAVGKWWYGSRTYTRDHVHVDTVDEWFPKMET
SQ  SLTLDELLSLFASSKELTSLVPNEKNPKEYILKLLFDHLNRKKTNNFNTHQILSQSDVVLNALLSVATAFGFANPVDNVL
SQ  KLWQHIVQAIPLDAPFPLLQLPHLLMEDVKNLSIRNISSIPQFLSLSEEQTKDYLPNYSKNQLKEMREIANGIPRISVVA
SQ  AKVLVDDDEYITVGAIANLILDLKCSYGTEVVPEVSTDGTETATKKDEEDAEKYHQSKDVVLGDVETLPYAWAPYFTQHH
SQ  KTAWWIYVVDPRQNRVIVPPFSITDIPKTLRTFRIPFQVPPVAGTFSFQLHIMSNSYVGEDVISNLTMIVKDTSVLQEQL
SQ  QEEAVSDLEDNSDIDESANAGKDFSDDENIGSDEEDESEYDPMDTDTSDGE
//
ID  P14906;
PN  Protein translocation protein SEC63;
GN  SEC63;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. Nucleus inner membrane; Multi-pass membrane protein.
DR  UNIPROT: P14906;
DR  UNIPROT: D6W2V5;
DR  UNIPROT: Q08690;
DR  PDB: 6N3Q;
DR  PDB: 6ND1;
DR  PDB: 7AFT;
DR  PDB: 7KAH;
DR  PDB: 7KAI;
DR  PDB: 7KAJ;
DR  PDB: 7KAO;
DR  PDB: 7KAP;
DR  PDB: 7KAQ;
DR  PDB: 7KAR;
DR  PDB: 7KAS;
DR  PDB: 7KAT;
DR  PDB: 7KAU;
DR  PDB: 7KB5;
DR  Pfam: PF00226;
DR  PROSITE: PS00636;
DR  PROSITE: PS50076;
DE  Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC63 may affect SEC1-polypeptide interactions by increasing the affinity of targeting pathways for SEC61 and/or by modifying SEC61 to allow more efficient polypeptide interaction. May also be involved in SRP-dependent cotranslational translocation. Is essential for cell growth and for germination. {ECO:0000269|PubMed:11226176}.
DE  Reference Proteome: Yes;
DE  Interaction: P30605; IntAct: EBI-7743571; Score: 0.37
DE  Interaction: P39742; IntAct: EBI-7750338; Score: 0.83
DE  Interaction: P04817; IntAct: EBI-7750372; Score: 0.37
DE  Interaction: P33754; IntAct: EBI-7750388; Score: 0.83
DE  Interaction: P40073; IntAct: EBI-7757792; Score: 0.37
DE  Interaction: P33767; IntAct: EBI-7757893; Score: 0.37
DE  Interaction: P16151; IntAct: EBI-7758032; Score: 0.37
DE  Interaction: P25621; IntAct: EBI-7758150; Score: 0.37
DE  Interaction: P38353; IntAct: EBI-7758268; Score: 0.37
DE  Interaction: P38298; IntAct: EBI-7758389; Score: 0.37
DE  Interaction: P38079; IntAct: EBI-7758511; Score: 0.37
DE  Interaction: P16140; IntAct: EBI-797191; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-797191; Score: 0.35
DE  Interaction: P21825; IntAct: EBI-797191; Score: 0.75
DE  Interaction: P32629; IntAct: EBI-819187; Score: 0.27
DE  Interaction: Q02159; IntAct: EBI-860869; Score: 0.00
DE  Interaction: P47026; IntAct: EBI-853504; Score: 0.35
DE  Interaction: P40217; IntAct: EBI-7678715; Score: 0.56
DE  Interaction: P16474; IntAct: EBI-966961; Score: 0.40
DE  Interaction: P32447; IntAct: EBI-3665462; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-3665470; Score: 0.35
DE  Interaction: P14922; IntAct: EBI-3665478; Score: 0.35
DE  Interaction: P39704; IntAct: EBI-3665486; Score: 0.35
DE  Interaction: P21268; IntAct: EBI-3665494; Score: 0.35
DE  Interaction: P00927; IntAct: EBI-3665502; Score: 0.35
DE  Interaction: P50946; IntAct: EBI-3665510; Score: 0.35
DE  Interaction: Q12524; IntAct: EBI-3665518; Score: 0.35
DE  Interaction: P54885; IntAct: EBI-3665526; Score: 0.35
DE  Interaction: P06103; IntAct: EBI-3665534; Score: 0.35
DE  Interaction: P40016; IntAct: EBI-3665542; Score: 0.35
DE  Interaction: Q12250; IntAct: EBI-3665550; Score: 0.35
DE  Interaction: Q05543; IntAct: EBI-3665558; Score: 0.35
DE  Interaction: O94742; IntAct: EBI-3665566; Score: 0.35
DE  Interaction: P31376; IntAct: EBI-3665574; Score: 0.35
DE  Interaction: P38326; IntAct: EBI-3665582; Score: 0.35
DE  Interaction: P38123; IntAct: EBI-3665590; Score: 0.35
DE  Interaction: Q05471; IntAct: EBI-3665598; Score: 0.35
DE  Interaction: Q04067; IntAct: EBI-3665606; Score: 0.35
DE  Interaction: Q05946; IntAct: EBI-3665614; Score: 0.35
DE  Interaction: P34110; IntAct: EBI-3665622; Score: 0.35
DE  Interaction: P16521; IntAct: EBI-3665630; Score: 0.35
DE  Interaction: P53719; IntAct: EBI-3665638; Score: 0.35
DE  Interaction: P53740; IntAct: EBI-3665646; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3665654; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3665662; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3701587; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3733411; Score: 0.35
DE  Interaction: P39079; IntAct: EBI-3740483; Score: 0.35
DE  Interaction: P37898; IntAct: EBI-3769653; Score: 0.35
DE  Interaction: Q12168; IntAct: EBI-3769661; Score: 0.35
DE  Interaction: P60010; IntAct: EBI-3769669; Score: 0.35
DE  Interaction: P22108; IntAct: EBI-3769677; Score: 0.35
DE  Interaction: P08566; IntAct: EBI-3769687; Score: 0.35
DE  Interaction: Q06834; IntAct: EBI-3769695; Score: 0.35
DE  Interaction: Q08347; IntAct: EBI-3769703; Score: 0.35
DE  Interaction: Q07457; IntAct: EBI-3769711; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-3769719; Score: 0.35
DE  Interaction: Q12018; IntAct: EBI-3769727; Score: 0.35
DE  Interaction: Q06697; IntAct: EBI-3769735; Score: 0.35
DE  Interaction: P53197; IntAct: EBI-3769743; Score: 0.35
DE  Interaction: P40094; IntAct: EBI-3769751; Score: 0.35
DE  Interaction: Q01454; IntAct: EBI-3769759; Score: 0.35
DE  Interaction: P38865; IntAct: EBI-3769767; Score: 0.35
DE  Interaction: P31373; IntAct: EBI-3769775; Score: 0.35
DE  Interaction: P32582; IntAct: EBI-3769783; Score: 0.35
DE  Interaction: Q08496; IntAct: EBI-3769791; Score: 0.35
DE  Interaction: P53759; IntAct: EBI-3769799; Score: 0.35
DE  Interaction: Q06053; IntAct: EBI-3769807; Score: 0.35
DE  Interaction: P38737; IntAct: EBI-3769815; Score: 0.35
DE  Interaction: P36053; IntAct: EBI-3769823; Score: 0.35
DE  Interaction: P00924; IntAct: EBI-3769831; Score: 0.35
DE  Interaction: P00925; IntAct: EBI-3769839; Score: 0.35
DE  Interaction: P45976; IntAct: EBI-3769847; Score: 0.35
DE  Interaction: P15442; IntAct: EBI-3769855; Score: 0.35
DE  Interaction: Q12680; IntAct: EBI-3769863; Score: 0.35
DE  Interaction: P32347; IntAct: EBI-3769871; Score: 0.35
DE  Interaction: P28241; IntAct: EBI-3769879; Score: 0.35
DE  Interaction: P53982; IntAct: EBI-3769887; Score: 0.35
DE  Interaction: P47170; IntAct: EBI-3769895; Score: 0.35
DE  Interaction: P32361; IntAct: EBI-3769903; Score: 0.35
DE  Interaction: P48526; IntAct: EBI-3769911; Score: 0.35
DE  Interaction: P38144; IntAct: EBI-3769919; Score: 0.35
DE  Interaction: Q12494; IntAct: EBI-3769927; Score: 0.35
DE  Interaction: P38853; IntAct: EBI-3769935; Score: 0.35
DE  Interaction: Q02574; IntAct: EBI-3769943; Score: 0.35
DE  Interaction: P00958; IntAct: EBI-3769951; Score: 0.35
DE  Interaction: Q07980; IntAct: EBI-3769959; Score: 0.35
DE  Interaction: Q02455; IntAct: EBI-3769967; Score: 0.35
DE  Interaction: P40457; IntAct: EBI-3769975; Score: 0.35
DE  Interaction: P48563; IntAct: EBI-3769983; Score: 0.35
DE  Interaction: P30775; IntAct: EBI-3769991; Score: 0.35
DE  Interaction: P53166; IntAct: EBI-3769999; Score: 0.35
DE  Interaction: Q02950; IntAct: EBI-3770007; Score: 0.35
DE  Interaction: P47047; IntAct: EBI-3770015; Score: 0.35
DE  Interaction: P19524; IntAct: EBI-3770023; Score: 0.35
DE  Interaction: P33420; IntAct: EBI-3770031; Score: 0.35
DE  Interaction: Q01560; IntAct: EBI-3770039; Score: 0.35
DE  Interaction: P38271; IntAct: EBI-3770047; Score: 0.35
DE  Interaction: Q12451; IntAct: EBI-3770055; Score: 0.35
DE  Interaction: P40960; IntAct: EBI-3770063; Score: 0.35
DE  Interaction: P17558; IntAct: EBI-3770071; Score: 0.35
DE  Interaction: P40433; IntAct: EBI-3770079; Score: 0.35
DE  Interaction: P00560; IntAct: EBI-3770087; Score: 0.35
DE  Interaction: P36093; IntAct: EBI-3770095; Score: 0.35
DE  Interaction: P07271; IntAct: EBI-3770103; Score: 0.35
DE  Interaction: P33334; IntAct: EBI-3770111; Score: 0.35
DE  Interaction: P52489; IntAct: EBI-3770119; Score: 0.35
DE  Interaction: P38344; IntAct: EBI-3770127; Score: 0.35
DE  Interaction: P29539; IntAct: EBI-3770135; Score: 0.35
DE  Interaction: P53552; IntAct: EBI-3770143; Score: 0.35
DE  Interaction: P05748; IntAct: EBI-3770151; Score: 0.35
DE  Interaction: P54780; IntAct: EBI-3770159; Score: 0.35
DE  Interaction: P05749; IntAct: EBI-3770167; Score: 0.35
DE  Interaction: Q12149; IntAct: EBI-3770175; Score: 0.35
DE  Interaction: Q02206; IntAct: EBI-3770183; Score: 0.35
DE  Interaction: P40482; IntAct: EBI-3770191; Score: 0.35
DE  Interaction: P11075; IntAct: EBI-3770207; Score: 0.35
DE  Interaction: P34223; IntAct: EBI-3770223; Score: 0.35
DE  Interaction: Q06315; IntAct: EBI-3770231; Score: 0.35
DE  Interaction: P39928; IntAct: EBI-3770239; Score: 0.35
DE  Interaction: P32908; IntAct: EBI-3770247; Score: 0.35
DE  Interaction: P25357; IntAct: EBI-3770255; Score: 0.35
DE  Interaction: P36126; IntAct: EBI-3770263; Score: 0.35
DE  Interaction: P25567; IntAct: EBI-3770271; Score: 0.35
DE  Interaction: P36085; IntAct: EBI-3770280; Score: 0.35
DE  Interaction: P08153; IntAct: EBI-3770288; Score: 0.35
DE  Interaction: Q06510; IntAct: EBI-3770296; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-3770304; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-3770312; Score: 0.35
DE  Interaction: P32367; IntAct: EBI-3770320; Score: 0.35
DE  Interaction: P35169; IntAct: EBI-3770336; Score: 0.35
DE  Interaction: P40061; IntAct: EBI-3770344; Score: 0.35
DE  Interaction: P53874; IntAct: EBI-3770352; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-3770360; Score: 0.35
DE  Interaction: P34241; IntAct: EBI-3770368; Score: 0.35
DE  Interaction: Q12339; IntAct: EBI-3770376; Score: 0.35
DE  Interaction: Q06685; IntAct: EBI-3770384; Score: 0.35
DE  Interaction: P22203; IntAct: EBI-3770392; Score: 0.35
DE  Interaction: O13584; IntAct: EBI-3770400; Score: 0.35
DE  Interaction: P33301; IntAct: EBI-3770408; Score: 0.35
DE  Interaction: P19880; IntAct: EBI-3770416; Score: 0.35
DE  Interaction: O13527; IntAct: EBI-3770424; Score: 0.35
DE  Interaction: P87264; IntAct: EBI-3770435; Score: 0.35
DE  Interaction: P39991; IntAct: EBI-3770443; Score: 0.35
DE  Interaction: P38854; IntAct: EBI-3770451; Score: 0.35
DE  Interaction: P34246; IntAct: EBI-3770459; Score: 0.35
DE  Interaction: Q05948; IntAct: EBI-3770467; Score: 0.35
DE  Interaction: Q06567; IntAct: EBI-3770475; Score: 0.35
DE  Interaction: Q03153; IntAct: EBI-3770483; Score: 0.35
DE  Interaction: Q12751; IntAct: EBI-3770491; Score: 0.35
DE  Interaction: P42842; IntAct: EBI-3770499; Score: 0.35
DE  Interaction: Q12697; IntAct: EBI-3770513; Score: 0.35
DE  Interaction: Q08748; IntAct: EBI-3770521; Score: 0.35
DE  Interaction: Q06813; IntAct: EBI-3770529; Score: 0.35
DE  Interaction: P36019; IntAct: EBI-3770537; Score: 0.35
DE  Interaction: P31111; IntAct: EBI-3770545; Score: 0.35
DE  Interaction: P32915; IntAct: EBI-9352295; Score: 0.79
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005739;
GO  GO:0005637;
GO  GO:0030867;
GO  GO:0031207;
GO  GO:0071256;
GO  GO:0008320;
GO  GO:0046967;
GO  GO:0006620;
GO  GO:0031204;
GO  GO:0006614;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPTNYEYDEASETWPSFILTGLLMVVGPMTLLQIYQIFFGANAEDGNSGKSKEFNEEVFKNLNEEYTSDEIKQFRRKFDK
SQ  NSNKKSKIWSRRNIIIIVGWILVAILLQRINSNDAIKDAATKLFDPYEILGISTSASDRDIKSAYRKLSVKFHPDKLAKG
SQ  LTPDEKSVMEETYVQITKAYESLTDELVRQNYLKYGHPDGPQSTSHGIALPRFLVDGSASPLLVVCYVALLGLILPYFVS
SQ  RWWARTQSYTKKGIHNVTASNFVSNLVNYKPSEIVTTDLILHWLSFAHEFKQFFPDLQPTDFEKLLQDHINRRDSGKLNN
SQ  AKFRIVAKCHSLLHGLLDIACGFRNLDIALGAINTFKCIVQAVPLTPNCQILQLPNVDKEHFITKTGDIHTLGKLFTLED
SQ  AKIGEVLGIKDQAKLNETLRVASHIPNLKIIKADFLVPGENQVTPSSTPYISLKVLVRSAKQPLIPTSLIPEENLTEPQD
SQ  FESQRDPFAMMSKQPLVPYSFAPFFPTKRRGSWCCLVSSQKDGKILQTPIIIEKLSYKNLNDDKDFFDKRIKMDLTKHEK
SQ  FDINDWEIGTIKIPLGQPAPETVGDFFFRVIVKSTDYFTTDLDITMNMKVRDSPAVEQVEVYSEEDDEYSTDDDETESDD
SQ  ESDASDYTDIDTDTEAEDDESPE
//
ID  Q4FZW5;
PN  Nucleoporin SEH1-A;
GN  seh1l;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: Q4FZW5;
DR  PDB: 6LK8;
DR  PDB: 7VCI;
DR  PDB: 7VOP;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000250|UniProtKB:Q96EE3}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:Q96EE3}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSENGNWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFD
SQ  RTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGVVRIYEAPDVMNLSQWSLQHEIS
SQ  CKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNIMGKVQIYEYNENTRKYAKAETLMSVSDPVHDIAFAPNLGRSFHILAV
SQ  ATKDVRIFTMKPLRKELSSSGGVTKFEIHTVAQFDNHNSQVWRVSWNITGTVLASSGDDGTVRLWKANYMDNWKCIGVLK
SQ  GDGNPVGNSYQGFFGSSVGSAGQSLQNSVNGTPSSGRKHS
//
ID  Q6GNF1;
PN  Nucleoporin SEH1-B;
GN  seh1l;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: Q6GNF1;
DR  PDB: 7WB4;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000250|UniProtKB:Q96EE3}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:Q96EE3}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSENVNWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFD
SQ  RTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGVVRIYEAPDVMNLSQWSLQHEIS
SQ  CKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNIMGKVQIYEYNENTRKYAKAETLMSVSDPVHDIAFAPNLGRSFHILAV
SQ  ATKDVRIFTMKPLRKELSSSGGVTKFENHTVAQFDNHNSQVWRVSWNITGTVLASSGDDGTVRLWKANYMDNWKCIGVLK
SQ  GDGNPVGNSFQGIFGSSIGSASHGLQNSVNGTSTSGRKHS
//
ID  Q93VR9;
PN  Protein SEH1;
GN  SEH1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21189294, ECO:0000269|PubMed:22902705}. Nucleus {ECO:0000269|PubMed:22288649, ECO:0000269|PubMed:22902705}. Cytoplasm {ECO:0000269|PubMed:22288649, ECO:0000269|PubMed:22902705}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}. Note=Part of the cellular SEH1 pool is not permanently associated with the Nup107-160 complex. {ECO:0000305|PubMed:22902705}.
DR  UNIPROT: Q93VR9;
DR  UNIPROT: Q8LB12;
DR  UNIPROT: Q9C5X7;
DR  UNIPROT: Q9C7V9;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Required for proper export of mRNAs from the nucleus to the cytoplasm. {ECO:0000269|PubMed:22288649}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0034198;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAKSMATLDSGTTCSSWNQSGDRLAAGSLNGKLSIYESSTSSSSTFSCTSKVRVSESSIVKIVWLPSEYGDAVACVCEDG
SQ  SLSIWEELSEDAHGLEWKLCKSMKNKSSQVLDVQFGVSRKSLKMVAAYSDGYLRVFELLNPLELKNWQLQAEFQNVIDSL
SQ  STLGKPSSLSASVSWNPMKGEEQEPSFVLAFNSDSPHLNSSKIWEFDEAHNRWLAVAELALPEDKGDPVYALSWAPNIGR
SQ  PYEVVAVATHKGIGIWHVGLAPDLEGRLPVKKVSSLSGHQGEVWQMEWDMSGMTLASTGSDGMVKLWQSNLNGEWHEQAT
SQ  LEPVPS
//
ID  A7YY75;
PN  Nucleoporin SEH1;
GN  SEH1L;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: A7YY75;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000250|UniProtKB:Q96EE3}. As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. {ECO:0000250|UniProtKB:Q96EE3}.
DE  Reference Proteome: Yes;
GO  GO:0061700;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0034198;
GO  GO:0050830;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0031503;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSESGEWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFD
SQ  RTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGIVRIYEAPDVMNLSQWSLQHEIS
SQ  CKLSCSCISWNPSSSRAHAPMIAVGSDDSSPNAMAKVQIFEYNENTRKYAKAETLLTVTDPVHDIAFAPNLGRSFHILAI
SQ  ATKDVRIFTLKPVRKELTSSGGPTKFEIHIVAQFDNHNSQVWRVSWNITGTVLASSGDDGCVRLWKANYMDNWKCTGILK
SQ  GNGSPVNGSSQQGNSNPSVGSNIPSLQNSLNGSSAGRKHS
//
ID  A8WVD2;
PN  Nucleoporin SEH1;
GN  npp;
OS  6238;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: A8WVD2;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Probable component of the nuclear pore complex (NPC) which is involved in the trafficking of macromolecules between the cytoplasm and nucleus. {ECO:0000250|UniProtKB:O45933}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:P55735}.
DE  Reference Proteome: Yes;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0034198;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSADKSPYQIEPYKTVGAHRDLIHCVSFDPHGRRMATCASDMTMAIWDRQPDGNWRRSAHWKCHGGAVWRVIWAHPEFGQ
SQ  IVASCSYDRTIVIWEEQIVRTEKDLKCKESQWIRRTIISDNRSDVTDICFSPRHLGLSLASCNVLGAVRIYEAPDVVDAS
SQ  RWNLIHELQAFHTRCGCVTWSLSRMHRPLIAVGSDEKKAGGKERVVIYENIDGLRKWQRIHSLVFDMPCPITDLKFSPIS
SQ  MVDSHQLAIASGDVHVFNIKVPRTAILEEDGVDNPIHLADYSFQRVALLGDQRKAWRIRYNLIGSVITSTSLDGTLRSWK
SQ  SLFVNQWVKLSEMNVDDYVPTADEVHKIVEAKTTERLPSQLDKVYF
//
ID  O45933;
PN  Nucleoporin SEH1;
GN  npp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: O45933;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Probable component of the nuclear pore complex (NPC) which is involved in the trafficking of macromolecules between the cytoplasm and nucleus. {ECO:0000269|PubMed:12937276}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:P55735}.
DE  Reference Proteome: Yes;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0034198;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MQEDDSVKPFQTVGAHRDLIHCVSFDPHGRRMATCASDMTMAIWDRKPDGNWRRSAHWKCHGGAVWRVIWAHPEFGQIVA
SQ  TCSYDRTIVIWEEQIVRSEKDLKQKESQWIRRTIISDNRSDVTDICFSPRHLGLMMASCNVLGTVRIYEAPDIVDASRWN
SQ  LIHELQAFHTRCGCVTWSLSRMHRPLIAVGSDEKKAENKKRVVIYENIDGLRKWQRINSLVFDLPCPITDLKFSPISMVD
SQ  SHQLAVASGDVHVYNIKVARSAILEEDGVENPIQLADYNLIKVALLGDHRKAWRLRYNLMGSVISSTSLDGTLRSWKSLF
SQ  VNQWVKLSEMNVDDYVPSPEEVRAFISSKTTERLPSQLEKTYF
//
ID  G0S450;
PN  Nucleoporin SEH1;
GN  SEH1;
OS  759272;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P53011}. Nucleus membrane {ECO:0000250|UniProtKB:P53011}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53011}; Cytoplasmic side {ECO:0000250|UniProtKB:P53011}. Nucleus membrane {ECO:0000250|UniProtKB:P53011}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53011}; Nucleoplasmic side {ECO:0000250|UniProtKB:P53011}. Note=Symmetric distribution. {ECO:0000250|UniProtKB:P53011}.
DR  UNIPROT: G0S450;
DR  UNIPROT: G0ZGV0;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Involved in nuclear poly(A)+ RNA export and NPC biogenesis. {ECO:0000250|UniProtKB:P53011}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005198;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P53011};
SQ  MSKAAAFLTDPPLVDDRPSFETILKHGHQDLVQAVAFNGHGDRCATGSVDGKIRVFNRLKEGIWRLCDNWTAHAGEILEL
SQ  QWLPTTVYPNLLASLGIEGRFKLWAEDPSAAPGRRFAESTRNGPLITIPSPRLSSHPSHLTHSQHPQQQPHHHHAPESIL
SQ  PSNPPPTSNPPQATGSTTAGSGAKPAFETRNPRSPYRSFSIKHIDDTRTTYLALLSADGGLTVYENDRVENLAAFSLMDE
SQ  FNVLDPTAATGPGQASTAPRGQETSFRVRFDPNPDVCYTALRDGVLSDALGLVVAVQDTVKVYRTRDAVRASLGLAAATK
SQ  EFYLAAEVVAGVHRGLVRDVAWAPGNIRGYDIIATACQDGFVRVFRLDTLSPSTSDTTKFAREPSSIDLTQGGELDDEKR
SQ  AQESAPESRWSSSRVRRHATRRQGPSQDALTITTSGLRASLDSHNHQQTPSRELDAADRRSRRAWTNQPGQVRHTLTEIS
SQ  RLDNHRTPVWRVAFDDDGQILGSVGDEGKLLCYRQKPDGTWAKSSEMSVVKVKMAAPQ
//
ID  Q6TGU2;
PN  Nucleoporin SEH1;
GN  seh1l;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: Q6TGU2;
DR  UNIPROT: Q1LXR9;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000250|UniProtKB:Q96EE3}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:Q96EE3}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0034198;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFVAKSIAADHKDLIHDVSYDFHGRRMATCSSDQSVKVWDKGDDGEWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFD
SQ  RTAAVWEEIVGESNDKQRGQSHWIKRTTLVDSRTSVTDVKFAPKHMGLMLTTCSADGVVRIYEAPDVMNLSQWSLQHEIS
SQ  CKLACSCISWNPSSSRAHPPMIAVGGDDSNGAYSGKVQIHEYNENTRKYAKAETLMTVTDPVHDIAFAPNLGRSFHVLAI
SQ  ATKDVRIFKLLPLRRESANSSGPTKFEVQVMAQFDSHNSQVWRVSWNITSTLLASSGDDGCVRLWKANYMDNWKCTGILR
SQ  GDGSPVNGSSGPSAALSAVGVPGAAQMIVGAATAGRKKAQLMPG
//
ID  Q7K2X8;
PN  Nucleoporin seh1;
GN  Nup44A;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:21521741}. Lysosome {ECO:0000269|PubMed:25512509}. Note=Enriched on the nuclear envelope of nurse cells, oocytes and syncytial embryos (PubMed:21521741). In egg chambers detected in lysosomes and autolysosomes of both fed and starved females (PubMed:25512509). {ECO:0000269|PubMed:21521741, ECO:0000269|PubMed:25512509}.
DR  UNIPROT: Q7K2X8;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Probable component of the nuclear pore complex (NPC) (By similarity). Involved in maintaining the localization of another nucleoporin Mtor to the nuclear envelope of early meiotic female germline cells (PubMed:21521741). It is not involved in recruiting the nucleoporins Mtor, Nup107, Nup153 and FG-containing nucleoporins to the NPC (PubMed:21521741). {ECO:0000250|UniProtKB:Q96EE3, ECO:0000269|PubMed:21521741}. An essential component of the GATOR subcomplex GATOR2 which functions as an activator of the amino acid-sensing branch of the TORC1 signaling pathway (PubMed:27166823, PubMed:23723238). The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the TORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation (PubMed:27166823, PubMed:23723238, PubMed:25512509). GATOR2 activates the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex, controlling the switch to cell proliferation growth under nutrient replete conditions and growth during female oocyte development (PubMed:21521741, PubMed:25512509, PubMed:23723238, PubMed:27166823). This component is required for activating TORC1 specifically in germline cells to promote cell growth and maintain the oocyte fate, probably influences the organization and/or function of microtubules within ovarian cysts, and promotes accumulation of another GATOR2 complex member mio in germline and somatic tissues (PubMed:27166823, PubMed:23723238, PubMed:25512509, PubMed:21521741). GATOR1 and GATOR2 act at different stages of oogenesis to regulate TORC1 in order to control meiotic entry and promote oocyte growth and development (PubMed:25512509). After exactly four mitotic cyst divisions, the GATOR1 complex members (Iml1, Nprl2 and Nprl3) down-regulate TORC1 to slow cellular metabolism and promote the mitotic/meiotic transition (PubMed:25512509). At later stages of oogenesis, the mio and Nup44A components of the GATOR2 complex inhibit GATOR1 and thus activate TORC1 to promote meiotic progression, and drive oocyte growth and development (PubMed:21521741, PubMed:25512509). In addition to its role in the regulation of the TORC1 complex, functions independently of TORC1 to prevent the inappropriate accumulation of autolysosomes in germline tissues (PubMed:27166823). {ECO:0000269|PubMed:21521741, ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25512509, ECO:0000269|PubMed:27166823}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VH77; IntAct: EBI-284688; Score: 0.00
GO  GO:0044754;
GO  GO:0061700;
GO  GO:0005764;
GO  GO:0005635;
GO  GO:0031080;
GO  GO:0032991;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0051301;
GO  GO:0034198;
GO  GO:0007293;
GO  GO:0051321;
GO  GO:0010507;
GO  GO:0048477;
GO  GO:0010508;
GO  GO:0045793;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0051445;
GO  GO:0007346;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFDVEPIIADHKDVIHDVVFDYYGRRMATCSSDQTVKIWDEDGQGKWNVTSSWKAHSGSIWRVSWAHPEFGQVVATCSFD
SQ  RTASVWEEVIGEKVSSTNTPTRRWVRRTTLVDSRTSVTDVEFAPKYLGLLLATASADGIIRIYEAPDIMNLSQWPVQHEI
SQ  SNKLPLSCLSWNTSTYMVTQLLAAGSDEAATPTGKVFLFAYSENSRKCVKIDTVNDITDPVTDVAFAPNAGRTFHMLAVA
SQ  SKDLYIVNLRGVTDATDISKLDIQTIKFSEHNCPVWRVCWNMLATMLISTGDDGCVRLWRMNYNRQWRCAAVLKAEGSGP
SQ  TYEPAPPTPTLATTASATAKFYKKGTIGNQVPWH
//
ID  Q96EE3;
PN  Nucleoporin SEH1;
GN  SEH1L;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:17363900}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:17363900}. Lysosome membrane {ECO:0000269|PubMed:28199306}.
DR  UNIPROT: Q96EE3;
DR  UNIPROT: A8K5B1;
DR  UNIPROT: Q8NFU6;
DR  UNIPROT: Q96MH3;
DR  UNIPROT: Q9C069;
DR  PDB: 5A9Q;
DR  PDB: 7PEQ;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 609263;
DR  DisGeNET: 81929;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:17363900}. As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex (PubMed:23723238). It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1 (PubMed:25457612, PubMed:27487210). {ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:27487210}.
DE  Reference Proteome: Yes;
DE  Interaction: A8CG34; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P35658; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P46060; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P55735; IntAct: EBI-11086798; Score: 0.62
DE  Interaction: P57740; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P63165; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P63279; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q12769; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: Q53GS7; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q5SRE5; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-2563676; Score: 0.40
DE  Interaction: Q80U93; IntAct: EBI-11014856; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-2563157; Score: 0.40
DE  Interaction: Q8N1F7; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-11086798; Score: 0.67
DE  Interaction: Q8NFH4; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q8TEM1; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-9050503; Score: 0.49
DE  Interaction: Q92621; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q1EHW4; IntAct: EBI-922367; Score: 0.35
DE  Interaction: Q8IY92; IntAct: EBI-2371120; Score: 0.35
DE  Interaction: P24386; IntAct: EBI-2515120; Score: 0.40
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q14457; IntAct: EBI-3622591; Score: 0.35
DE  Interaction: Q93050; IntAct: EBI-3912272; Score: 0.37
DE  Interaction: P04578; IntAct: EBI-6176529; Score: 0.46
DE  Interaction: Q9BW27; IntAct: EBI-9032422; Score: 0.70
DE  Interaction: Q9H6Z9; IntAct: EBI-12503146; Score: 0.35
DE  Interaction: P19838; IntAct: EBI-11322417; Score: 0.35
DE  Interaction: E9QKK1; IntAct: EBI-10995761; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: E9PUA5; IntAct: EBI-10999661; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: O75864; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: E9PF10; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q99567; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q6NUQ4; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q9BTX1; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q6PJI9; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q96SK2; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q96S15; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q9NXC5; IntAct: EBI-11086798; Score: 0.53
DE  Interaction: O43683; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: P58043; IntAct: EBI-11102804; Score: 0.35
DE  Interaction: E5LBS6; IntAct: EBI-14062727; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q68D86; IntAct: EBI-21526180; Score: 0.35
DE  Interaction: P02511; IntAct: EBI-21564160; Score: 0.35
DE  Interaction: Q8IYS4; IntAct: EBI-21565697; Score: 0.35
DE  Interaction: Q99435; IntAct: EBI-21661256; Score: 0.35
DE  Interaction: Q9GZP0; IntAct: EBI-21663347; Score: 0.35
DE  Interaction: O15496; IntAct: EBI-21699277; Score: 0.35
DE  Interaction: Q86XD5; IntAct: EBI-21711466; Score: 0.35
DE  Interaction: Q96RS6; IntAct: EBI-20723623; Score: 0.35
DE  Interaction: Q5T011; IntAct: EBI-16752607; Score: 0.35
DE  Interaction: O95714; IntAct: EBI-16811721; Score: 0.35
DE  Interaction: Q83A11; IntAct: EBI-21286703; Score: 0.37
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: O14929; IntAct: EBI-25478994; Score: 0.35
DE  Interaction: P0DTC2; IntAct: EBI-27088073; Score: 0.35
DE  Interaction: Q9NSY0; IntAct: EBI-28946547; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: Q93009; IntAct: EBI-30843837; Score: 0.44
DE  Interaction: Q9Y4G2; IntAct: EBI-32711159; Score: 0.35
GO  GO:0005829;
GO  GO:0061700;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0034198;
GO  GO:0050830;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:1904262;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0031503;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSESGDWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFD
SQ  RTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGIVRIYEAPDVMNLSQWSLQHEIS
SQ  CKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNAMAKVQIFEYNENTRKYAKAETLMTVTDPVHDIAFAPNLGRSFHILAI
SQ  ATKDVRIFTLKPVRKELTSSGGPTKFEIHIVAQFDNHNSQVWRVSWNITGTVLASSGDDGCVRLWKANYMDNWKCTGILK
SQ  GNGSPVNGSSQQGTSNPSLGSTIPSLQNSLNGSSAGRKHS
//
ID  Q8R2U0;
PN  Nucleoporin SEH1;
GN  Seh1l;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: Q8R2U0;
DR  UNIPROT: Q3TLC9;
DR  UNIPROT: Q3UP79;
DR  UNIPROT: Q9D0K7;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000250|UniProtKB:Q96EE3}. As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. {ECO:0000250|UniProtKB:Q96EE3}.
DE  Reference Proteome: Yes;
GO  GO:0061700;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0034198;
GO  GO:0050830;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0032008;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:0031503;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSESGDWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFD
SQ  RTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGIVRVYEAPDVMNLSQWSLQHEVS
SQ  CKLCCSCISWNPSSSRAHPPMIAVGSDDSSPNSMAKVQIFEYNENTRKYAKAETLMTVTDPVHDIAFAPNLGRSFHILAV
SQ  ATKDVRIFTLKPLRKELTSSGGPTKFEIHIVAQFDNHNSQVWRVSWNITGTVLASSGDDGCVRLWKANYMDNWKCTGILK
SQ  GNGSPVNGSSQLGNSNPSLSSNIPNLQNSLNGTSASRKHS
//
ID  C1BK83;
PN  Nucleoporin SEH1;
GN  seh1l;
OS  8014;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: C1BK83;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000250|UniProtKB:Q96EE3}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:Q96EE3}.
DE  Reference Proteome: No;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFVARSIAADHKDLIHDVSYDFHGRRMATCSSDQSVKVWDKSDNGEWNCTASWKTHSGSVWRVTWAHPEFGQVLASCSFD
SQ  RTAAVWEEIVGESNDKQRGLSHWIKRTTLVDSRTSVTDVKFAPKHMGLMLTTCSADGVVRIYEAPDVMNLSQWSLQHEIS
SQ  CKLSCSCISWNPSSSRAHSPMIAVGSDDSNTAYSGKVQIYEYVENTRKYAKVETLMTVTDPVHDIAFAPNLGRSFHVLAI
SQ  ATKDVRIFKLIPMRKESSSSGPTKLEVQLQAQFDGHNSQVWRVSWNITSTLLASSGDDGCVRLWKANYMDNWKCTGILRG
SQ  DGSPVNGAAGQAGTPGAAGTPGGPASQNALQAVAGRKKAQLMPG
//
ID  Q5RAN6;
PN  Nucleoporin SEH1;
GN  SEH1L;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: Q5RAN6;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000250|UniProtKB:Q96EE3}. As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1. {ECO:0000250|UniProtKB:Q96EE3}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0005198;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSESGDWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFD
SQ  RTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGIVRIYEAPDVMNLSQWSLQHEIS
SQ  CKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNAMAKVQIFEYNENTRKYAKAETLMTVTDPVHDIAFAPNLGRSFHILAI
SQ  ATKDVRIFTLKPVRKELTSSGGPTKFEIHIVAHFDNHNSQVWRVSWNITGTVLASSGDDGCVRLWKANYMDNWKCTGILK
SQ  GNGSPVNGSSQQGTSNPSLGSNIPSLQNSLNGSSAGRKHS
//
ID  Q10099;
PN  Nucleoporin seh1;
GN  seh1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm. Nucleus, nuclear pore complex.
DR  UNIPROT: Q10099;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. {ECO:0000269|PubMed:15116432}.
DE  Reference Proteome: Yes;
DE  Interaction: O43044; IntAct: EBI-1563770; Score: 0.40
DE  Interaction: Q9UUE5; IntAct: EBI-1563788; Score: 0.35
DE  Interaction: Q9UTK4; IntAct: EBI-1563788; Score: 0.35
GO  GO:0005829;
GO  GO:0061700;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0005634;
GO  GO:0035859;
GO  GO:0005774;
GO  GO:0005198;
GO  GO:0034198;
GO  GO:0051028;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDDISATTIQTNHQDLVNDVTYDFYGRRMVSCSADQRVKVYDFNDDTETWAITSEWRAGDASLMRVAWAHPSFGQVLAVC
SQ  SLDRGVRIYEEQKKNFESKTWVEVAKLMDARSAVLDISFCPFQHGCKLAAVSADATLRIYEAMEPGNLTYWTLMNEIALM
SQ  PSPPSRNEQPAFCVNWCPSRWREQYIAVGCMNDAYIYKQNSHGKWKKVAELPGHTDLIRDICWAPSMGSSYYLIATACKD
SQ  GNVRIFKVETLCEEVFQEEEDAGNSMTEDSNFNLNSLKVELIGEYDNHKCQVWRCRFNVTGTILSSSGDDGCVRLWKASY
SQ  ANLFKCISVVSLEKKPEKL
//
ID  Q5U4Y8;
PN  Nucleoporin SEH1;
GN  seh1l;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane {ECO:0000250|UniProtKB:Q96EE3}.
DR  UNIPROT: Q5U4Y8;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. {ECO:0000250|UniProtKB:Q96EE3}. As a component of the GATOR complex may function in the amino acid-sensing branch of the TORC1 signaling pathway. {ECO:0000250|UniProtKB:Q96EE3}.
DE  Reference Proteome: Yes;
GO  GO:0000776;
GO  GO:0005765;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005198;
GO  GO:0051315;
GO  GO:0051301;
GO  GO:0034198;
GO  GO:0007080;
GO  GO:0051028;
GO  GO:0006999;
GO  GO:1904263;
GO  GO:0015031;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSENGDWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFD
SQ  RTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGVVRIYEAPDVMNLSQWSLQHEIS
SQ  CKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNIMGKVQIYEYNENTRKYAKAETLMSVSDPVHDIAFAPNLGRSFHILAV
SQ  ATKDVRIFTMKPLRKELSSSGGVTKFEIHTVAQFDNHNSQVWRVSWNITGTVLASSGDDGTVRLWKANYMDNWKCIGVLK
SQ  GDGNPVGNSCQGIFGSSVGSAIQSLQNSVNGTSSSGRKHS
//
ID  P53011;
PN  Nucleoporin SEH1;
GN  SEH1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane {ECO:0000269|PubMed:10684247}; Peripheral membrane protein {ECO:0000269|PubMed:10684247}; Cytoplasmic side {ECO:0000269|PubMed:10684247}. Vacuole membrane {ECO:0000269|PubMed:21454883}; Peripheral membrane protein {ECO:0000269|PubMed:21454883}. Nucleus membrane {ECO:0000269|PubMed:10684247}; Peripheral membrane protein {ECO:0000269|PubMed:10684247}; Nucleoplasmic side {ECO:0000269|PubMed:10684247}. Note=Symmetric distribution. {ECO:0000269|PubMed:10684247}.
DR  UNIPROT: P53011;
DR  UNIPROT: D6VU45;
DR  PDB: 3EWE;
DR  PDB: 3F3F;
DR  PDB: 3F3G;
DR  PDB: 3F3P;
DR  PDB: 4XMM;
DR  PDB: 6X08;
DR  PDB: 7N84;
DR  PDB: 7N9F;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Involved in nuclear poly(A)+ RNA export and NPC biogenesis. It is also required for normal nuclear morphology. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12206772, ECO:0000269|PubMed:21454883, ECO:0000269|PubMed:8565072}.
DE  Reference Proteome: Yes;
DE  Interaction: P35729; IntAct: EBI-800487; Score: 0.91
DE  Interaction: P46673; IntAct: EBI-1580856; Score: 0.92
DE  Interaction: P49687; IntAct: EBI-797641; Score: 0.81
DE  Interaction: P52891; IntAct: EBI-800196; Score: 0.64
DE  Interaction: P38305; IntAct: EBI-761900; Score: 0.40
DE  Interaction: Q12315; IntAct: EBI-849734; Score: 0.32
DE  Interaction: P40018; IntAct: EBI-784510; Score: 0.35
DE  Interaction: P09440; IntAct: EBI-785631; Score: 0.35
DE  Interaction: P41543; IntAct: EBI-785977; Score: 0.35
DE  Interaction: P41811; IntAct: EBI-786711; Score: 0.35
DE  Interaction: P18888; IntAct: EBI-793082; Score: 0.35
DE  Interaction: P32639; IntAct: EBI-798593; Score: 0.35
DE  Interaction: Q04491; IntAct: EBI-812133; Score: 0.53
DE  Interaction: P32357; IntAct: EBI-814258; Score: 0.27
DE  Interaction: P32582; IntAct: EBI-815440; Score: 0.27
DE  Interaction: P53919; IntAct: EBI-858574; Score: 0.00
DE  Interaction: Q99257; IntAct: EBI-8220602; Score: 0.47
DE  Interaction: Q02630; IntAct: EBI-1269890; Score: 0.00
DE  Interaction: P34232; IntAct: EBI-7700687; Score: 0.35
DE  Interaction: P13186; IntAct: EBI-2612251; Score: 0.35
DE  Interaction: P21965; IntAct: EBI-2612461; Score: 0.35
DE  Interaction: P32472; IntAct: EBI-2883301; Score: 0.00
DE  Interaction: Q06677; IntAct: EBI-3758933; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3791596; Score: 0.35
DE  Interaction: P39078; IntAct: EBI-3822714; Score: 0.35
DE  Interaction: P31539; IntAct: EBI-3827816; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-4385804; Score: 0.35
DE  Interaction: P47170; IntAct: EBI-9821605; Score: 0.58
DE  Interaction: P39923; IntAct: EBI-9819823; Score: 0.35
DE  Interaction: P38742; IntAct: EBI-9819915; Score: 0.35
DE  Interaction: Q08281; IntAct: EBI-9819987; Score: 0.35
DE  Interaction: Q03897; IntAct: EBI-9820072; Score: 0.53
DE  Interaction: P38164; IntAct: EBI-9820321; Score: 0.50
DE  Interaction: Q8WUM0; IntAct: EBI-11890201; Score: 0.40
DE  Interaction: Q08496; IntAct: EBI-16268078; Score: 0.35
DE  Interaction: P09734; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P37291; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P39954; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P41277; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P05694; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P00817; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P07342; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P04806; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P38720; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P07262; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P04397; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P00924; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P29311; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P53090; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P37302; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: Q05911; IntAct: EBI-16281928; Score: 0.35
DE  Interaction: P19414; IntAct: EBI-16281928; Score: 0.35
GO  GO:0097042;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0031080;
GO  GO:0035859;
GO  GO:0005774;
GO  GO:0017056;
GO  GO:0034198;
GO  GO:0051028;
GO  GO:0006913;
GO  GO:1904263;
GO  GO:0015031;
GO  GO:1903432;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10684247};
SQ  MQPFDSGHDDLVHDVVYDFYGRHVATCSSDQHIKVFKLDKDTSNWELSDSWRAHDSSIVAIDWASPEYGRIIASASYDKT
SQ  VKLWEEDPDQEECSGRRWNKLCTLNDSKGSLYSVKFAPAHLGLKLACLGNDGILRLYDALEPSDLRSWTLTSEMKVLSIP
SQ  PANHLQSDFCLSWCPSRFSPEKLAVSALEQAIIYQRGKDGKLHVAAKLPGHKSLIRSISWAPSIGRWYQLIATGCKDGRI
SQ  RIFKITEKLSPLASEESLTNSNMFDNSADVDMDAQGRSDSNTEEKAELQSNLQVELLSEHDDHNGEVWSVSWNLTGTILS
SQ  SAGDDGKVRLWKATYSNEFKCMSVITAQQ
//
ID  Q9H4I8;
PN  Serine hydrolase-like protein 2;
GN  SERHL2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Peroxisome {ECO:0000250}. Note=Concentrated in perinuclear vesicles. May be located in peroxisomes. {ECO:0000250}.
DR  UNIPROT: Q9H4I8;
DR  UNIPROT: B1AHE9;
DR  UNIPROT: B1AHF0;
DR  UNIPROT: Q0VDJ1;
DR  UNIPROT: Q5H973;
DR  UNIPROT: Q9BR29;
DR  UNIPROT: Q9BR30;
DR  UNIPROT: Q9Y3I9;
DR  Pfam: PF00561;
DR  OMIM: 619045;
DR  DisGeNET: 253190;
DE  Function: Probable serine hydrolase. May be related to cell muscle hypertrophy.
DE  Reference Proteome: Yes;
DE  Interaction: Q8TDZ2; IntAct: EBI-21881296; Score: 0.35
DE  Interaction: Q9Y6M4; IntAct: EBI-21881296; Score: 0.35
DE  Interaction: Q9Y4D1; IntAct: EBI-21881296; Score: 0.35
DE  Interaction: Q9NWQ8; IntAct: EBI-21881296; Score: 0.35
DE  Interaction: Q9HAV0; IntAct: EBI-21881296; Score: 0.35
DE  Interaction: Q05086; IntAct: EBI-21881296; Score: 0.35
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0016787;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSENAAPGLISELKLAVPWGHIAAKAWGSLQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVP
SQ  YYLQTFVSEIRRVVAALKWNRFSILGHSFGGVVGGMFFCTFPEMVDKLILLDTPLFLLESDEMENLLTYKRRAIEHVLQV
SQ  EASQEPSHVFSLKQLLQRLLKSNSHLSEECGELLLQRGTTKVATGLVLNRDQRLAWAENSIDFISRELCAHSIRKLQAHV
SQ  LLIKAVHGYFDSRQNYSEKESLSFMIDTMKSTLKEQFQFVEVPGNHCVHMSEPQHVASIISSFLQCTHMLPAQL
//
ID  Q8WWX9;
PN  Selenoprotein M;
GN  SELENOM;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11839807}. Endoplasmic reticulum {ECO:0000305|PubMed:11839807}. Golgi apparatus {ECO:0000305|PubMed:11839807}. Note=Localized to perinuclear structures corresponding to Golgi and endoplasmic reticulum.
DR  UNIPROT: Q8WWX9;
DR  UNIPROT: A8MPZ2;
DR  Pfam: PF08806;
DR  OMIM: 610918;
DR  DisGeNET: 140606;
DE  Function: May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5JR59; IntAct: EBI-10277692; Score: 0.56
DE  Interaction: Q7Z3S9; IntAct: EBI-10277702; Score: 0.56
DE  Interaction: Q99750; IntAct: EBI-24297485; Score: 0.56
DE  Interaction: Q8IUG1; IntAct: EBI-24318815; Score: 0.56
DE  Interaction: Q96EQ0; IntAct: EBI-24323331; Score: 0.56
DE  Interaction: P61604; IntAct: EBI-24339388; Score: 0.56
DE  Interaction: Q7RTP0; IntAct: EBI-25278643; Score: 0.56
DE  Interaction: P60328; IntAct: EBI-24452632; Score: 0.56
DE  Interaction: Q9H6H4; IntAct: EBI-24641382; Score: 0.56
DE  Interaction: Q9BY50; IntAct: EBI-24657753; Score: 0.56
DE  Interaction: Q9UMX5; IntAct: EBI-21862585; Score: 0.35
DE  Interaction: P83105; IntAct: EBI-25745135; Score: 0.35
GO  GO:0005788;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0016491;
GO  GO:0060612;
GO  GO:0035934;
GO  GO:0042445;
GO  GO:0035264;
GO  GO:0010269;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLLLPPLALLLLLAALVAPATAATAYRPDWNRLSGLTRARVETCGGUQLNRLKEVKAFVTQDIPFYHNLVMKHLPGADP
SQ  ELVLLGRRYEELERIPLSEMTREEINALVQELGFYRKAAPDAQVPPEYVWAPAKPPEETSDHADL
//
ID  Q8VHC3;
PN  Selenoprotein M;
GN  Selenom;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11839807}. Endoplasmic reticulum {ECO:0000305|PubMed:11839807}. Golgi apparatus {ECO:0000305|PubMed:11839807}. Note=Localized to perinuclear structures corresponding to Golgi and endoplasmic reticulum.
DR  UNIPROT: Q8VHC3;
DR  UNIPROT: B2RVS9;
DR  UNIPROT: Q3V374;
DR  UNIPROT: Q8CBT7;
DR  UNIPROT: Q8VCJ0;
DR  PDB: 2A2P;
DR  Pfam: PF08806;
DE  Function: May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0016491;
GO  GO:0060612;
GO  GO:0035934;
GO  GO:0042445;
GO  GO:0035264;
GO  GO:0010269;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSILLSPPSLLLLLAALVAPATSTTNYRPDWNRLRGLARGRVETCGGUQLNRLKEVKAFVTEDIQLYHNLVMKHLPGADP
SQ  ELVLLSRNYQELERIPLSQMTRDEINALVQELGFYRKSAPEAQVPPEYLWAPAKPPEEASEHDDL
//
ID  Q9HC62;
PN  Sentrin-specific protease 2;
GN  SENP2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12192048}. Nucleus membrane {ECO:0000269|PubMed:12192048}; Peripheral membrane protein {ECO:0000269|PubMed:12192048}; Nucleoplasmic side {ECO:0000269|PubMed:12192048}. Cytoplasm {ECO:0000269|PubMed:16738331}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000269|PubMed:16738331}.
DR  UNIPROT: Q9HC62;
DR  UNIPROT: B4DQ42;
DR  UNIPROT: Q8IW97;
DR  UNIPROT: Q96SR2;
DR  UNIPROT: Q9P2L5;
DR  PDB: 1TGZ;
DR  PDB: 1TH0;
DR  PDB: 2IO0;
DR  PDB: 2IO1;
DR  PDB: 2IO2;
DR  PDB: 2IO3;
DR  PDB: 3ZO5;
DR  PDB: 5AEK;
DR  Pfam: PF02902;
DR  PROSITE: PS50600;
DR  OMIM: 608261;
DR  DisGeNET: 59343;
DE  Function: Protease that catalyzes two essential functions in the SUMO pathway (PubMed:11896061, PubMed:12192048, PubMed:20194620, PubMed:21965678, PubMed:15296745). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin- like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins (PubMed:15296745). The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein (PubMed:20194620, PubMed:21965678, PubMed:15296745). May down- regulate CTNNB1 levels and thereby modulate the Wnt pathway (By similarity). Deconjugates SUMO2 from MTA1 (PubMed:21965678). Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (PubMed:20194620). Acts as a regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1 during the late phase of viral infection (By similarity). {ECO:0000250|UniProtKB:Q91ZX6, ECO:0000269|PubMed:11896061, ECO:0000269|PubMed:12192048, ECO:0000269|PubMed:15296745, ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:21965678}.
DE  Reference Proteome: Yes;
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P46060; IntAct: EBI-15612044; Score: 0.59
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P63165; IntAct: EBI-1039804; Score: 0.62
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8N205; IntAct: EBI-10310600; Score: 0.56
DE  Interaction: Q8N6L0; IntAct: EBI-10310610; Score: 0.72
DE  Interaction: Q9ERU9; IntAct: EBI-10999306; Score: 0.35
DE  Interaction: Q96SN8; IntAct: EBI-731539; Score: 0.00
DE  Interaction: Q15796; IntAct: EBI-2688488; Score: 0.00
DE  Interaction: Q96FF9; IntAct: EBI-3925171; Score: 0.37
DE  Interaction: P55327; IntAct: EBI-3940774; Score: 0.37
DE  Interaction: Q9Y6K9; IntAct: EBI-5778245; Score: 0.58
DE  Interaction: P61978; IntAct: EBI-8103058; Score: 0.40
DE  Interaction: P55854; IntAct: EBI-10310548; Score: 0.74
DE  Interaction: Q6RW13; IntAct: EBI-10310580; Score: 0.56
DE  Interaction: P61956; IntAct: EBI-10310558; Score: 0.72
DE  Interaction: Q15041; IntAct: EBI-10310570; Score: 0.56
DE  Interaction: Q8IVP5; IntAct: EBI-10310590; Score: 0.56
DE  Interaction: Q8WW34; IntAct: EBI-10310620; Score: 0.56
DE  Interaction: P03070; IntAct: EBI-11738381; Score: 0.37
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q8BH65; IntAct: EBI-11109889; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11398030; Score: 0.27
DE  Interaction: Q86VR2; IntAct: EBI-24510629; Score: 0.56
DE  Interaction: P55056; IntAct: EBI-24682547; Score: 0.56
DE  Interaction: Q9NS64; IntAct: EBI-24591855; Score: 0.56
DE  Interaction: P53701; IntAct: EBI-24635455; Score: 0.56
DE  Interaction: Q96CM8; IntAct: EBI-24774886; Score: 0.56
DE  Interaction: Q5T9G4; IntAct: EBI-25212470; Score: 0.56
DE  Interaction: Q8N3Y7; IntAct: EBI-24803428; Score: 0.56
DE  Interaction: Q9UBN6; IntAct: EBI-25274349; Score: 0.56
DE  Interaction: P03427; IntAct: EBI-14404759; Score: 0.35
DE  Interaction: Q96RU2; IntAct: EBI-21834668; Score: 0.35
DE  Interaction: P07205; IntAct: EBI-21834668; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: P40227; IntAct: EBI-20905992; Score: 0.40
DE  Interaction: O60563; IntAct: EBI-25477219; Score: 0.35
DE  Interaction: O76071; IntAct: EBI-25477658; Score: 0.35
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016929;
GO  GO:0070139;
GO  GO:0045444;
GO  GO:0051028;
GO  GO:0031397;
GO  GO:0031398;
GO  GO:0031648;
GO  GO:0016926;
GO  GO:0015031;
GO  GO:0030111;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:12192048};
SQ  MYRWLVRILGTIFRFCDRSVPPARALLKRRRSDSTLFSTVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTKP
SQ  MVTSACNGTRNVAPSGEVFSNSSSCELTGSGSWNNMLKLGNKSPNGISDYPKIRVTVTRDQPRRVLPSFGFTLNSEGCNR
SQ  RPGGRRHSKGNPESSLMWKPQEQAVTEMISEESGKGLRRPHCTVEEGVQKEEREKYRKLLERLKESGHGNSVCPVTSNYH
SQ  SSQRSQMDTLKTKGWGEEQNHGVKTTQFVPKQYRLVETRGPLCSLRSEKRCSKGKITDTETMVGIRFENESRRGYQLEPD
SQ  LSEEVSARLRLGSGSNGLLRRKVSIIETKEKNCSGKERDRRTDDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRG
SQ  DIQTLKNYHWLNDEVINFYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKVHWS
SQ  LVVIDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNSDLNLLEWTHHSMKPHEIPQQLNGSDCGMFTCKYADYIS
SQ  RDKPITFTQHQMPLFRKKMVWEILHQQLL
//
ID  Q91ZX6;
PN  Sentrin-specific protease 2;
GN  Senp2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: [Isoform 1]: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9HC62}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HC62}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HC62}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9HC62}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9HC62}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:11489887}. Cytoplasmic vesicle {ECO:0000269|PubMed:11489887}. Note=Found in the cytoplasm and in cytoplasmic vesicles, together with axin. {ECO:0000269|PubMed:11489887}. [Isoform 3]: Nucleus, PML body {ECO:0000269|PubMed:12419228}.
DR  UNIPROT: Q91ZX6;
DR  UNIPROT: Q544T8;
DR  UNIPROT: Q811R3;
DR  UNIPROT: Q9D4Z0;
DR  Pfam: PF02902;
DR  PROSITE: PS50600;
DE  Function: Protease that catalyzes two essential functions in the SUMO pathway (PubMed:11489887, PubMed:20194620). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins (By similarity). The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein (PubMed:11489887, PubMed:20194620, PubMed:27637147). May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway (PubMed:11489887). Deconjugates SUMO2 from MTA1 (By similarity). Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (PubMed:20194620). Acts as a regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1 during the late phase of viral infection (PubMed:27637147). {ECO:0000250|UniProtKB:Q9HC62, ECO:0000269|PubMed:11489887, ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:27637147}. [Isoform 3]: Activates transcription. {ECO:0000269|PubMed:12419228}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0016605;
GO  GO:0016929;
GO  GO:0019904;
GO  GO:0070139;
GO  GO:0009950;
GO  GO:0045444;
GO  GO:0007507;
GO  GO:0060711;
GO  GO:0051028;
GO  GO:0035562;
GO  GO:0032091;
GO  GO:0031397;
GO  GO:0001934;
GO  GO:0031398;
GO  GO:0045944;
GO  GO:0031648;
GO  GO:0016926;
GO  GO:0015031;
GO  GO:0032875;
GO  GO:2000045;
GO  GO:0051246;
GO  GO:0060712;
GO  GO:0060707;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9HC62};
SQ  MYRWLAKVLGTILRLCERPAPGARALLKRRRSSSTLFSTAVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTK
SQ  PMVSSACNGTRNVAPSGEVFSNSSSCELMSSGSCSSMLKLGNKSPNGISDYPKIRVTVTRDQPRRVLPSFGFTLKSEGYN
SQ  RRPSGRRHSKSNPESSLTWKPQEQGVTEMISEEGGKGVRRPHCTVEEGVQKDEREKYRKLLERLKEGAHGSTFPPTVSHH
SQ  SSQRIQMDTLKTKGWVEEQNHGVRTTHFVPKQYRVVETRGPLCSMRSEKRYSKGKADTEKVVGLRFEKEGTRGHQMEPDL
SQ  SEEVSARLRLGSGSNGLLRRKISVLEIKEKNFPSKEKDRRTEDLFEFTEDMEKEISNALGHGPPDEILSSAFKLRITRGD
SQ  IQTLKNYHWLNDEVINFYMNLLVERSKKQGYPALHAFSTFFYPKLKSGGYQAVKRWTKGVNLFEQELVLVPIHRKVHWSL
SQ  VVMDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNTDLNLLEWTHYSMKPHEIPQQLNGSDCGMFTCKYADYISR
SQ  DKPITFTQHQMPLFRKKMVWEILHQQLL
//
ID  Q5R7K7;
PN  Sentrin-specific protease 2;
GN  SENP2;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9HC62}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HC62}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HC62}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9HC62}. Cytoplasm {ECO:0000250|UniProtKB:Q9HC62}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9HC62}.
DR  UNIPROT: Q5R7K7;
DR  UNIPROT: Q5RDS3;
DR  Pfam: PF02902;
DR  PROSITE: PS50600;
DE  Function: Protease that catalyzes two essential functions in the SUMO pathway. The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein (By similarity). May down- regulate CTNNB1 levels and thereby modulate the Wnt pathway (By similarity). Deconjugates SUMO2 from MTA1. Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (By similarity). Acts as a regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1 during the late phase of viral infection (By similarity). {ECO:0000250|UniProtKB:Q91ZX6, ECO:0000250|UniProtKB:Q9HC62}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0016929;
GO  GO:0045444;
GO  GO:0051028;
GO  GO:0016926;
GO  GO:0015031;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9HC62};
SQ  MYRWLVRILGTIFRFCDRSVPPARALLKRRRSDSTLFSTVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTKP
SQ  MVTSACNGTRNVAPSGEVFSNPSSCELTGSGSWNNMLKLGNKSPNGISDYPKIRVTVTRDQPRRVLPSFGFTLNSEGYNR
SQ  RPGGRRHSKGNPESSLMWKPQEQAVTEMISEESGKGLRRPHRTVEEGVQKEEREKYRKLLERLKESGHGNSVCPVTSNYH
SQ  SSQRSQMDTLKTKGWGEEQNHGVKTTQFVPKQYRLVETRGPLCSLRSEKRCSKGKITDTEKMVGIRFENESRRGYQLEPD
SQ  LSEEVSARLRLGSGSNGLLRRKVSIIETKEKNCSGKERDRRTDDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRG
SQ  DIQTLKNYHWLNDEVINFYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKVHWS
SQ  LVVIDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNIDLNLLEWTHYSMKPHEIPQQLNGSDCGMFTCKYADYIS
SQ  RDKPITFTQHQMPLFRKKMVWEILHQQLL
//
ID  Q9EQE1;
PN  Sentrin-specific protease 2;
GN  Senp2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9HC62}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HC62}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HC62}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9HC62}. Cytoplasm {ECO:0000250|UniProtKB:Q9HC62}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9HC62}.
DR  UNIPROT: Q9EQE1;
DR  Pfam: PF02902;
DR  PROSITE: PS50600;
DE  Function: Protease that catalyzes two essential functions in the SUMO pathway (By similarity). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins (By similarity). The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon- linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein (By similarity). May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway (PubMed:10944533, PubMed:11997515). Deconjugates SUMO2 from MTA1 (By similarity). Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (By similarity). Acts as a regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1 during the late phase of viral infection (By similarity). {ECO:0000250|UniProtKB:Q91ZX6, ECO:0000250|UniProtKB:Q9HC62, ECO:0000269|PubMed:10944533, ECO:0000269|PubMed:11997515}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0016605;
GO  GO:0016929;
GO  GO:0019904;
GO  GO:0070139;
GO  GO:0009950;
GO  GO:0045444;
GO  GO:0007507;
GO  GO:0060711;
GO  GO:0051028;
GO  GO:0035562;
GO  GO:0032091;
GO  GO:0031397;
GO  GO:0001934;
GO  GO:0031398;
GO  GO:0045944;
GO  GO:0031648;
GO  GO:0016926;
GO  GO:0015031;
GO  GO:0032875;
GO  GO:2000045;
GO  GO:0051246;
GO  GO:0060712;
GO  GO:0060707;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9HC62};
SQ  MYRWLTKVLGTILRLCERPAPGARALLKRRRSSSSLFSTAVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTK
SQ  PMVSSACNGTRNVAPSGEVFSNSPSCELTTSGSCSSMLKLGNKSPNGISDYPKIRVTVARDQPRRVLPSFGFTLKSEGYN
SQ  RRPSGRRHSKSNPESSLPWKPQEQGVTEMISEEGGKGARRPHCTVEEGVQKDEREKYLKLLERLKEGAHGSTFPPAVSHH
SQ  SSQRTQMDTLKTKGWMEEQNHGVRTTHLVPKQYRVVETRGPLCSVRSEKRYSKGKADTEKVVGLRFEKDGTRGHQLEPDL
SQ  SEEVSARLRLGSGSNGLLRRKISVLEAKEKNFPSKEKDRRTEDLFELTEDMEKEISNALGHGPPDEILSSAFKLRITRGD
SQ  IQTLKNYHWLNDEVINFYMNLLVERSKKQGYPALHALSTFFYPKLKSGGYQAVKRWTKGVNLFDQELVLVPIHRKVHWSL
SQ  VVMDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNTDLNLLEWTHYSMKPHEIPQQLNGSDCGMFTCKYADYISR
SQ  DKPITFTQHQMPLFRKKMVWEILHQQLL
//
ID  Q09353;
PN  Sentrin-specific protease;
GN  ulp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:25475837}.
DR  UNIPROT: Q09353;
DR  UNIPROT: Q8IU18;
DR  Pfam: PF02902;
DR  PROSITE: PS50600;
DE  Function: Protease that deconjugates smo-1 from targeted proteins and may catalyze the processing of smo-1 to its mature form. {ECO:0000269|PubMed:15107848, ECO:0000269|PubMed:25475837}.
DE  Reference Proteome: Yes;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0016929;
GO  GO:0009792;
GO  GO:1904333;
GO  GO:0016926;
GO  GO:0032880;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRRSDLSDKDSQSRKRHWLTDQAVTNEEKEQSPTKRTRKTKSQGLGGLFNTFFGMFVSSNSGEKEKTEVSGEVQVQEDD
SQ  EIIVEGTTRRVAENKKYMIFLNEDAPVRANAGSEENEVIIEKHVQKNVEIRNDEEKQEVQGDLVLTLSSSPKSPKNLEKS
SQ  FEVQQDDEEPDVLFEKVVKTPNKQLQEARRFQNELIFLNDNPDTPDDVSVISDSRSKEFISPTPDDSVSRPITPSLSSLS
SQ  NYTSNNVRDYWRRNSAKKPEVLRRVPVRHQFKHSTSVRKMNTIIDLKKIKNHLSSRDRLLQGVVASGQYEAKAISGIVEK
SQ  KPKKMQRTSSTDILARAKNKIAELGGSRSNTPSLLSREPSIIIDSEESTSSSYRQHARSNSSESDSYRKLNDILSQINSL
SQ  GIGSAYRGPQRYQNSYQLSKQKEDKLLEEARIREGHRSQTRGDRLEDVRKRLELQGIAIRPKVEKKKVDDFMALPDAADA
SQ  LVERAWSGGNPNEQFVDAFSIQICKKDLATLSGLHWLNDEIINFYLQLICDRSNGDSKYPKIYAFNTFFYSNIVSKGYAS
SQ  VKRWTRKVDIFAFDIVLVPVHLGMHWCMAVIDMGEKKIEFYDSLYDGNTAVLPALRGYLEAESLDKKKTAMNFSGWTIQQ
SQ  MTDIPRQQNGSDCGVFSCQFGEWASRRTTPRFTQKNMPYYRKRMVYEIVSKKLLATI
//
ID  A6QQL3;
PN  Septin-14;
GN  SEPTIN14;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q6ZU15}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6ZU15}. Cell projection, axon {ECO:0000250|UniProtKB:Q9DA97}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9DA97}. Perikaryon {ECO:0000250|UniProtKB:Q9DA97}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9DA97}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q6ZU15}. Note=Colocalizes with actin stress fibers (By similarity). Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:Q6ZU15, ECO:0000250|UniProtKB:Q9DA97}.
DR  UNIPROT: A6QQL3;
DR  Pfam: PF00735;
DR  PROSITE: PS51719;
DE  Function: Filament-forming cytoskeletal GTPase (Probable). Involved in the migration of cortical neurons and the formation of neuron leading processes during embryonic development (By similarity). Plays a role in sperm head formation during spermiogenesis, potentially via facilitating localization of ACTN4 to cell filaments (By similarity). {ECO:0000250|UniProtKB:Q6ZU15, ECO:0000250|UniProtKB:Q9DA97, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0001669;
GO  GO:0030424;
GO  GO:0032153;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0030425;
GO  GO:0015630;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0031105;
GO  GO:0005940;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0060090;
GO  GO:0061640;
GO  GO:0001764;
GO  GO:0008104;
GO  GO:1905719;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEKPMCPSTQIPDDEDTQKEDNIRCLNMLGHFGFDCLAHQLVDKSVQQGFFFNILCVGETGIGKSTLIDTLFNTSLKDK
SQ  KSSHFYASVGLKIQTYELQENNVQLKLTVVKTVGYGDQINKEASYQPIVDYLDAQFESYLQEELKIKRSLGNYRDSRVHV
SQ  CLYFISPTGHSLKSLDILTMKNIDSKVNIIPVIAKADAISKSDLQTFKCAIMNELISNGIQMYQFPTDNETSTHMNSSMN
SQ  GLLPFAVVGSTEEVKVGKRTVRGRQYPWGILQVENENHCDFVKLRDMLLCTNREDLKEQTHTRHYERYRRNRLHMMGFTD
SQ  MGPNNQPVSFQEIYEAKRQELLEQCQREEEELKHKFMQRVKEKETAFKEAEKELQDKFEHLKKVQQEETMRLEEERRQLE
SQ  EEILELCKMKASSGTLQSQVCTSVKKDKERKK
//
ID  Q6ZU15;
PN  Septin-14;
GN  SEPTIN14;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:17922164}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17922164, ECO:0000269|PubMed:31450874}. Cell projection, axon {ECO:0000250|UniProtKB:Q9DA97}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9DA97}. Perikaryon {ECO:0000250|UniProtKB:Q9DA97}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9DA97}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:32249155}. Note=Colocalizes with actin stress fibers (PubMed:17922164). Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:Q9DA97, ECO:0000269|PubMed:17922164}.
DR  UNIPROT: Q6ZU15;
DR  UNIPROT: A6NCC2;
DR  UNIPROT: B4DXD6;
DR  Pfam: PF00735;
DR  PROSITE: PS51719;
DR  OMIM: 612140;
DR  DisGeNET: 346288;
DE  Function: Filament-forming cytoskeletal GTPase (Probable). Involved in the migration of cortical neurons and the formation of neuron leading processes during embryonic development (By similarity). Plays a role in sperm head formation during spermiogenesis, potentially via facilitating localization of ACTN4 to cell filaments (PubMed:33228246). {ECO:0000250|UniProtKB:Q9DA97, ECO:0000269|PubMed:33228246, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UHD8; IntAct: EBI-2009321; Score: 0.54
DE  Interaction: Q8WYJ6; IntAct: EBI-2009333; Score: 0.37
DE  Interaction: Q15019; IntAct: EBI-2009337; Score: 0.37
DE  Interaction: Q9WU34; IntAct: EBI-2009364; Score: 0.37
DE  Interaction: O43236; IntAct: EBI-2009368; Score: 0.37
DE  Interaction: Q16181; IntAct: EBI-2009400; Score: 0.37
DE  Interaction: B3GNI6; IntAct: EBI-2009411; Score: 0.37
DE  Interaction: Q4V8G5; IntAct: EBI-2009423; Score: 0.37
DE  Interaction: Q96HA8; IntAct: EBI-24521085; Score: 0.56
DE  Interaction: Q9H8Y8; IntAct: EBI-23727439; Score: 0.56
DE  Interaction: Q9BRG1; IntAct: EBI-24554656; Score: 0.56
DE  Interaction: Q9H6L4; IntAct: EBI-24557731; Score: 0.56
DE  Interaction: Q9H5Z6; IntAct: EBI-24588389; Score: 0.56
DE  Interaction: Q14141; IntAct: EBI-21746554; Score: 0.35
DE  Interaction: Q9H3Q1; IntAct: EBI-21746903; Score: 0.35
DE  Interaction: Q9P0V9; IntAct: EBI-21746988; Score: 0.35
DE  Interaction: Q9UH03; IntAct: EBI-21747031; Score: 0.35
GO  GO:0001669;
GO  GO:0030424;
GO  GO:0032153;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0030425;
GO  GO:0015630;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0031105;
GO  GO:0005940;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0060090;
GO  GO:0061640;
GO  GO:0001764;
GO  GO:0008104;
GO  GO:1905719;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAERTMAMPTQIPADGDTQKENNIRCLTTIGHFGFECLPNQLVSRSIRQGFTFNILCVGETGIGKSTLIDTLFNTNLKDN
SQ  KSSHFYSNVGLQIQTYELQESNVQLKLTVVETVGYGDQIDKEASYQPIVDYIDAQFEAYLQEELKIKRSLFEYHDSRVHV
SQ  CLYFISPTGHSLKSLDLLTMKNLDSKVNIIPLIAKADTISKNDLQTFKNKIMSELISNGIQIYQLPTDEETAAQANSSVS
SQ  GLLPFAVVGSTDEVKVGKRMVRGRHYPWGVLQVENENHCDFVKLRDMLLCTNMENLKEKTHTQHYECYRYQKLQKMGFTD
SQ  VGPNNQPVSFQEIFEAKRQEFYDQCQREEEELKQRFMQRVKEKEATFKEAEKELQDKFEHLKMIQQEEIRKLEEEKKQLE
SQ  GEIIDFYKMKAASEALQTQLSTDTKKDKHRKK
//
ID  Q9DA97;
PN  Septin-14;
GN  Septin14;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:20181826}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33228246}. Cell projection, axon {ECO:0000269|PubMed:20181826}. Cell projection, dendrite {ECO:0000269|PubMed:20181826}. Perikaryon {ECO:0000269|PubMed:20181826}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:33228246}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q6ZU15}. Note=Colocalizes with actin stress fibers (By similarity). Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (PubMed:33228246). {ECO:0000250|UniProtKB:Q6ZU15, ECO:0000269|PubMed:33228246}.
DR  UNIPROT: Q9DA97;
DR  UNIPROT: E9QMM2;
DR  Pfam: PF00735;
DR  PROSITE: PS51719;
DE  Function: Filament-forming cytoskeletal GTPase (Probable). Involved in the migration of cortical neurons and the formation of neuron leading processes during embryonic development (PubMed:20181826). Plays a role in sperm head formation during spermiogenesis, potentially via facilitating localization of ACTN4 to cell filaments (By similarity). {ECO:0000250|UniProtKB:Q6ZU15, ECO:0000269|PubMed:20181826, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0001669;
GO  GO:0030424;
GO  GO:0032153;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0030425;
GO  GO:0015630;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0031105;
GO  GO:0005940;
GO  GO:0005525;
GO  GO:0003924;
GO  GO:0060090;
GO  GO:0061640;
GO  GO:0001764;
GO  GO:0008104;
GO  GO:1905719;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEKPTNTSVPIPGSEDPQKENIRCLSTLGHFGFECLPTQLVNKSIQKGFSFNILCVGETGIGKTTLINTLFNTNLKETK
SQ  SSHFYSKVGLTVKTYELLERNIPLRLTVVKTVGYGDQINKEASYQPVVDYLDAQFEAYLQEELKIKRSLADYHDSRIHVC
SQ  LYFITPTGHSLKSLDLLTMKSIDRRVNIIPLIAKADSLSKNDLQRFKNNIMSELNSNGIQIYQFQVDDEASAQVNSSGLL
SQ  PFAVVGSMEEVKVGKRMVRGRHYPWGVLQEVENENHCDFVKLRDLLLSTNMEDLKDQTHTQHYECYRSNRLQKLGFSDTG
SQ  PDNRPVSFQEMYEAKRREFHNQCQKEEEELKQTFMQRVKEKELTFKDAEKELQDKFEHLKRIQQEEILKLEEERRKLEEQ
SQ  IIDFYKMKAASESAQAQVCTNIKKDKDRKK
//
ID  Q13530;
PN  Serine incorporator 3;
GN  SERINC3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q86VE9}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9QZI9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9QZI9}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:26416734}. Note=(Microbial infection) Upon HIV-1 infection, it is redirected to perinuclear region following interaction with HIV-1 Nef, excluding it from virions particles, thereby preventing subsequent antiviral defense activity (Probable). {ECO:0000305|PubMed:26416734}.
DR  UNIPROT: Q13530;
DR  UNIPROT: B4DUE9;
DR  UNIPROT: O43717;
DR  UNIPROT: Q9BR33;
DR  Pfam: PF03348;
DR  OMIM: 607165;
DR  DisGeNET: 10955;
DE  Function: Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm (PubMed:26416733, PubMed:26416734). {ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}.
DE  Reference Proteome: Yes;
DE  Interaction: O15260; IntAct: EBI-1059797; Score: 0.00
DE  Interaction: P24390; IntAct: EBI-1059822; Score: 0.00
DE  Interaction: Q99623; IntAct: EBI-1061397; Score: 0.00
DE  Interaction: Q9P035; IntAct: EBI-1078346; Score: 0.00
DE  Interaction: P53985; IntAct: EBI-1081007; Score: 0.00
DE  Interaction: Q9Y277; IntAct: EBI-1082606; Score: 0.00
DE  Interaction: P33947; IntAct: EBI-1083230; Score: 0.00
DE  Interaction: Q9HAV4; IntAct: EBI-1085165; Score: 0.00
DE  Interaction: P45880; IntAct: EBI-1086232; Score: 0.00
DE  Interaction: P62841; IntAct: EBI-3915396; Score: 0.37
DE  Interaction: O95393; IntAct: EBI-3922519; Score: 0.37
DE  Interaction: A0A286YCX6; IntAct: EBI-11119288; Score: 0.35
DE  Interaction: P30556; IntAct: EBI-20802983; Score: 0.37
DE  Interaction: P14416; IntAct: EBI-20805908; Score: 0.37
DE  Interaction: Q13263; IntAct: EBI-20929800; Score: 0.40
DE  Interaction: P28799; IntAct: EBI-25860965; Score: 0.56
DE  Interaction: O43933; IntAct: EBI-25881831; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25898215; Score: 0.56
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0015194;
GO  GO:0051607;
GO  GO:0009597;
GO  GO:0045087;
GO  GO:0006564;
GO  GO:0006658;
GO  GO:1902237;
GO  GO:0006665;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGAVLGVFSLASWVPCLCSGASCLLCSCCPNSKNSTVTRLIYAFILLLSTVVSYIMQRKEMETYLKKIPGFCEGGFKIHE
SQ  ADINADKDCDVLVGYKAVYRISFAMAIFFFVFSLLMFKVKTSKDLRAAVHNGFWFFKIAALIGIMVGSFYIPGGYFSSVW
SQ  FVVGMIGAALFILIQLVLLVDFAHSWNESWVNRMEEGNPRLWYAALLSFTSAFYILSIICVGLLYTYYTKPDGCTENKFF
SQ  ISINLILCVVASIISIHPKIQEHQPRSGLLQSSLITLYTMYLTWSAMSNEPDRSCNPNLMSFITRITAPTLAPGNSTAVV
SQ  PTPTPPSKSGSLLDSDNFIGLFVFVLCLLYSSIRTSTNSQVDKLTLSGSDSVILGDTTTSGASDEEDGQPRRAVDNEKEG
SQ  VQYSYSLFHLMLCLASLYIMMTLTSWYSPDAKFQSMTSKWPAVWVKISSSWVCLLLYVWTLVAPLVLTSRDFS
//
ID  Q86VE9;
PN  Serine incorporator 5;
GN  SERINC5;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26416734, ECO:0000305|PubMed:26416733}. Note=(Microbial infection) Upon HIV-1 infection, it is redirected to perinuclear region following interaction with HIV-1 Nef, excluding it from virions particles, thereby preventing subsequent antiviral defense activity (PubMed:26416733, PubMed:26416734). Localizes to the cell membrane, where it is efficiently incorporated into budding virions and impairs subsequent virion entry into target cells (PubMed:26416733, PubMed:26416734). {ECO:0000269|PubMed:26416734, ECO:0000305|PubMed:26416733}.
DR  UNIPROT: Q86VE9;
DR  UNIPROT: B4DMH7;
DR  UNIPROT: Q495A4;
DR  UNIPROT: Q495A6;
DR  Pfam: PF03348;
DR  OMIM: 614551;
DR  DisGeNET: 256987;
DE  Function: Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm (PubMed:26416733, PubMed:26416734). Enhances the incorporation of serine into phosphatidylserine and sphingolipids. May play a role in providing serine molecules for the formation of myelin glycosphingolipids in oligodendrocytes (By similarity). {ECO:0000250|UniProtKB:Q63175, ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}.
DE  Reference Proteome: Yes;
DE  Interaction: P88995; IntAct: EBI-9641349; Score: 0.37
DE  Interaction: P25105; IntAct: EBI-20811174; Score: 0.37
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0043209;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0015194;
GO  GO:0051607;
GO  GO:0009597;
GO  GO:0045087;
GO  GO:0006564;
GO  GO:0042552;
GO  GO:0006658;
GO  GO:0008654;
GO  GO:1904219;
GO  GO:1904222;
GO  GO:0006665;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAQCCAGQLACCCGSAGCSLCCDCCPRIRQSLSTRFMYALYFILVVVLCCIMMSTTVAHKMKEHIPFFEDMCKGIKAGD
SQ  TCEKLVGYSAVYRVCFGMACFFFIFCLLTLKINNSKSCRAHIHNGFWFFKLLLLGAMCSGAFFIPDQDTFLNAWRYVGAV
SQ  GGFLFIGIQLLLLVEFAHKWNKNWTAGTASNKLWYASLALVTLIMYSIATGGLVLMAVFYTQKDSCMENKILLGVNGGLC
SQ  LLISLVAISPWVQNRQPHSGLLQSGVISCYVTYLTFSALSSKPAEVVLDEHGKNVTICVPDFGQDLYRDENLVTILGTSL
SQ  LIGCILYSCLTSTTRSSSDALQGRYAAPELEIARCCFCFSPGGEDTEEQQPGKEGPRVIYDEKKGTVYIYSYFHFVFFLA
SQ  SLYVMMTVTNWFNHVRSAFHLLP
//
ID  Q9EPB5;
PN  Serine hydrolase-like protein;
GN  Serhl;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Peroxisome. Note=Concentrated in perinuclear vesicles. May be located in peroxisomes.
DR  UNIPROT: Q9EPB5;
DR  UNIPROT: Q9DCZ8;
DR  Pfam: PF00561;
DE  Function: Probable serine hydrolase. May be related to cell muscle hypertrophy.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005739;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0016787;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGLHSELKLAVPWGHIALKVWGSQKNPPVLCLHGWLDNANSFDRLIPLLPQDFCYMAMDFGGHGLSSHYNPGLPYYQQNF
SQ  VSEVRRVATAFKWNQFTLLGHSFGGCVGGTFACMFPEMVDKLILLDSTPFFLDSNEMENILTYRRRNIEHTLQVEASQKK
SQ  SLRAVSPEEMLQGFLNNNSHLDKDCGELILQRGTTKVDAGLVLNRDRRISWPENSFDFVSKEMFVHSAKSLQASVLMIKA
SQ  LQGYYDVRRANDADKAPMHFMVDTLRSTLKERFQFVEVPGNHYIHMNKPQVVAGVVGPFLQGLQRMTSARL
//
ID  G5EEU2;
PN  Histone-lysine N-methyltransferase set-25;
GN  set;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus {ECO:0000269|PubMed:22939621}. Chromosome {ECO:0000269|PubMed:22939621}. Nucleus lamina {ECO:0000269|PubMed:22939621}. Note=Colocalizes with its own product and hpl-1 in foci in the peripheral region of the nucleus, in a manner dependent on H3K9me3. {ECO:0000269|PubMed:22939621}.
DR  UNIPROT: G5EEU2;
DR  Pfam: PF00856;
DR  PROSITE: PS50280;
DE  Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using mono- and dimethylated H3 'Lys-9' as substrate (PubMed:22939621). Acts redundantly with the methyltransferase met-2 to position chromosome arms at the nuclear lamina (PubMed:22939621). Required for small-RNA-induced H3K9 methylation (PubMed:26365259). Together with met-2, protects and stabilizes repeat-rich genomic regions by suppressing transcription- induced replication stress through methylation of H3K9 (PubMed:27668659). {ECO:0000269|PubMed:22939621, ECO:0000269|PubMed:26365259, ECO:0000269|PubMed:27668659}.
DE  Reference Proteome: Yes;
GO  GO:0000792;
GO  GO:0005652;
GO  GO:0003690;
GO  GO:0042054;
GO  GO:0046872;
GO  GO:0016571;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLPAWGTSTEATASHAGWDGDDEGDIRAAYTEDEKKENIPPISLTSVSTNGAYPGQKRRRSESVRTLKPECPPEETQRLR
SQ  QRRRISATDATQSSRTMNVIEDRKPRVNRARKSQDAPSTSTCGFETPVGTKRKSKAADSQKPPKQSKLRKIDEASTSKAV
SQ  DNSSKDGKKTTKPAVTQSNRRRSGLSLRPVPIETIFSESSGRESSTEDEADVSHQQRVEKIAKNPIMVVVLPLGPGNYPN
SQ  NERITVVSTYKSRVNKNCNEARRAQRHGSWSRKGIAFPGIPTKKFTKSDLAKYGAHASNWPAQAAFRSEEGKILIYYEGW
SQ  TCLTLHRLSVEECARTAPTILEEMSIRDKFIETVKSAAAEEAKLVVEKNQENGIELTLDEALKQIFIEPVPQSSPENVFW
SQ  IYQDLSYFHTMDNRDLGLAPVFYISSYTQSVRPPCYAYTAINIVDVDAYKRCLESRANMSFADLTGQKIWMPTRSKACEN
SQ  GTKCKCDARFMFLYDPHDVTNLECTPDGKVDFTDFKIDNARIVMECSDACGCSLDCPRRSLQRGQQHPLAVYYEGPEKGF
SQ  GVRAAANIKAGELVCEYTGDVTLLPTSDPVASSSTKTDDGEEQENPEAPERVDSSYDAAFNAMDTKIIISAKKTGNISRF
SQ  INHSCDPSSVFVEVYSRRFEEDPLIPRVAVYAIKDIALGEEITIAYYEPGIEWKRSSVKCRCKSTKCMGTLPAF
//
ID  Q9UST7;
PN  Transcription factor tau subunit sfc3;
GN  sfc3;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9UST7;
DR  Pfam: PF04182;
DE  Function: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. Cooperates with sfc6 in DNA binding. Localizes to chromatin insulator sequence without recruiting RNA polymerase III and plays a role in nuclear organization. {ECO:0000250|UniProtKB:P34111, ECO:0000269|PubMed:10906331, ECO:0000269|PubMed:16751097}.
DE  Reference Proteome: Yes;
DE  Interaction: O14229; IntAct: EBI-1564366; Score: 0.35
DE  Interaction: O74458; IntAct: EBI-1564366; Score: 0.35
DE  Interaction: O60174; IntAct: EBI-1564366; Score: 0.35
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0000127;
GO  GO:0003677;
GO  GO:0000995;
GO  GO:0042791;
GO  GO:0006384;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDSLIRHCSEEIALDGSSGCSIDRLWEFAANFFFRQGIVQNLDDNYKTFVWPLILKEDGIEVWIEDEDATGLRSKMQEIP
SQ  WNYQDITIELRARIRLFASEDRQWLTLTYKTKTDSKIQPLAFELLSCISRYRQEGVDRIQLCKETKQEPRSVYGRIQALE
SQ  DASLISKVAINRSRAQTALLVLKRFESENSTINETVAQVSGKQIYNTEKIRSNICDAVQSSRNGICRHVDARAMVNLNHS
SQ  RWERRYYARQVTYLHNNGYLRKCLTFVPNSPERCIRCLQFIKPYISSLDATEDDVDFTEVDDIPEDDELEEEEPLLPSKE
SQ  EFDASFLQPLADVGPTLPQWSRFRPLEFQCFVLIRNAGFHGVITLQILSGLTGIRFNKPLFKLLGSLVEHRSSVPNHLSH
SQ  MSITRFEDKTKKSRQYRYFTLQSQLNRLIRDGIPAETISKLLPHVHSLAGEFSPIDSSLFLNSLHHKGNMESNAEVSPDG
SQ  MTLLPRKRGRPRKSANISVTSSPIRPSKNENNLPSLAISPVSEGFIQNATISTPSTSSNLSIAGSLTPSKTSRIYRGLAP
SQ  LKNPEFNEDHVKKAEHLEPLLNVSSSVPSKNFTVSSPDHLKYGNTSSLQVSDSQSSIDLDSSFHYPVSVDSQLSHSTGSL
SQ  MANFSSPTKKRRLESVDFIFLQRKGLILSYLVEQNGAFEISRKMFEDLADLKVRRNPETSRTVMDRRTFQQTLEKLMQEK
SQ  KVRKLVIATNNGLGKLVRKDIVVQYDMKPDSPRFQQLRAQITTPEIEKQSTPEILKDVDVDFLKRNTSLSRRKSMPAEIK
SQ  RHKESSETKPVDKEEVKKNEKEKDDPMRLAQQLLESLAPDFALHENTQQKSPVEKPKKLRKDRYASVEEFDYFSSTEHAS
SQ  KRSVKRFKNDFTSDEDETLIRAVVITQIYYGGTNRLIKWEAVQKCFPNRDIYALTRRYLSIRQHTKFKGLQQFLSENWQQ
SQ  MYKDAVSRKDLMPYPDSVDDFDPTPYVKASCRPYMISSSNLATTRLPRDLVDVYETYNIEVVKQETNFREMIFDPSLSVA
SQ  SKMNAYCDMPFTMPLSLNDKQNNEGDENCEKGQLFDAKSTIKSIVAIPDATYDARFSQERLMQYPEDILIAAHQELLDKR
SQ  IITRVNSENSRLQPGRNFQFTEKFASSLKSPLPPFLLSQAKRFNKFLLEGFQNHKNHLFEETSNSGTLACILDLLSQGKL
SQ  QISIVGSKFNEYGLSEGYRTRLLEHDNINVTLVLSGKESESKKNYGVTEKLATPPSHEPRLWLNGKCELIEMIWMNIEQS
SQ  IVYQLLRKPGILRSQLTNLLFPGLEPREFNEVLDYFIAAGAAIEKDGLYLNHNYLFKLT
//
ID  Q58DH7;
PN  Sigma non-opioid intracellular receptor 1;
GN  SIGMAR1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000250|UniProtKB:O55242}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis. Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (By similarity). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DR  UNIPROT: Q58DH7;
DR  Pfam: PF04622;
DE  Function: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (By similarity). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0014069;
GO  GO:0098839;
GO  GO:0036474;
GO  GO:0006869;
GO  GO:0043523;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MCWAVGRRWAWAALLLAVAAVLAQVVWLWLGTQSFVFQHEEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEDLQ
SQ  WVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSSGHSGRYWAEISDTIISGTFHQWREGTTKSEVFYPGETVVHGPGEAT
SQ  AVEWGPNTWMVEYGRGVIPSTLGFALADTVFSTQDFLTLFYTLRAYARGLRLELTTYLFGQDA
//
ID  Q60492;
PN  Sigma non-opioid intracellular receptor 1;
GN  SIGMAR1;
OS  10141;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000250|UniProtKB:O55242}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis. Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (By similarity). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DR  UNIPROT: Q60492;
DR  Pfam: PF04622;
DE  Function: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (By similarity). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0014069;
GO  GO:0098839;
GO  GO:0036474;
GO  GO:0006869;
GO  GO:0043523;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MQWAVGRRWLWVALFLAAVAVLTQIVWLWLGTQNFVFQREEIAQLARQYAGLDHELAFSKLIVELRRLHPVHVLPDEELQ
SQ  WVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSPRHSGRYWAEISDTIISGTFHQWREGTTKSEVFYPGETVVHGPGEAT
SQ  AVEWGPNTWMVEYGRGVIPSTLGFALADTVFSTQDFLTLFYTLRVYARALQLELTTYLFGQDP
//
ID  Q5ZL84;
PN  Sigma non-opioid intracellular receptor 1;
GN  SIGMAR1;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DR  UNIPROT: Q5ZL84;
DR  Pfam: PF04622;
DE  Function: May function in lipid transport from the endoplasmic reticulum and be involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. May regulate calcium efflux at the endoplasmic reticulum (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0006869;
GO  GO:0043523;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MGVAGPWVLRVGLGLGAFALLLQGLRGWLACKRYEFQPAEIAELARHHAGLDHELAFSKIIVELRKKHPGHILPDEDLQW
SQ  VFVNAGGWMGSMCLLHASLTEYVLLFGTAIDTGGHSGRYWAEIYDTIISGTFRQWKEGTTRSEIYYPGDTIVHQAGEATS
SQ  VQWSAGTWMVEYGRGFVPSTLAFALADTLFSTQDFITLFYTLRAYTKGLLLEASAFFSTLGC
//
ID  Q7ZWG9;
PN  Sigma non-opioid intracellular receptor 1;
GN  sigmar1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DR  UNIPROT: Q7ZWG9;
DR  Pfam: PF04622;
DE  Function: May function in lipid transport from the endoplasmic reticulum and be involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. May regulate calcium efflux at the endoplasmic reticulum (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0006869;
GO  GO:0009611;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MSLIRTILKLVVVVGFLSLTVQFIRHWMANKQYVFTKEEVAKLAKQYAGQDHEQAFSKVVVELRRRYPGHILPDEDLQWV
SQ  FVNAGGWMGSMCLLHASLTEYVLLFGTAVDTGGHSGRYWAEISDTIISGTFRQWKEGTTKSETYYPGDTIVHSAGEATSV
SQ  QWSSGTWMVEYGRGFIPSTLGFALADTMFSTQDFLTLFYTARVYVKGMILEASTFLTESGVL
//
ID  Q99720;
PN  Sigma non-opioid intracellular receptor 1;
GN  SIGMAR1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:10406945}. Nucleus outer membrane {ECO:0000269|PubMed:10406945}. Nucleus envelope {ECO:0000269|PubMed:11476895, ECO:0000269|PubMed:9341151}. Cytoplasmic vesicle {ECO:0000269|PubMed:10406945}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10406945}. Membrane {ECO:0000269|PubMed:11476895, ECO:0000269|PubMed:27042935, ECO:0000269|PubMed:9341151}; Single-pass membrane protein {ECO:0000269|PubMed:27042935}. Lipid droplet {ECO:0000250|UniProtKB:O55242}. Cell junction. Cell membrane {ECO:0000269|PubMed:23314020}. Cell projection, growth cone. Postsynaptic density membrane {ECO:0000269|PubMed:23314020}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (PubMed:10406945). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum. Accumulation at the endoplasmic reticulum is prominent in alpha-motor neurons of patients with amyotrophic lateral sclerosis (PubMed:23314020). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand- binding. In motor neurons it is enriched at cholinergic postsynaptic densities (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000269|PubMed:10406945, ECO:0000269|PubMed:23314020}.
DR  UNIPROT: Q99720;
DR  UNIPROT: D3DRM7;
DR  UNIPROT: O00673;
DR  UNIPROT: O00725;
DR  UNIPROT: Q0Z9W6;
DR  UNIPROT: Q153Z1;
DR  UNIPROT: Q2TSD1;
DR  UNIPROT: Q53GN2;
DR  UNIPROT: Q7Z653;
DR  UNIPROT: Q8N7H3;
DR  UNIPROT: Q9NYX0;
DR  PDB: 5HK1;
DR  PDB: 5HK2;
DR  PDB: 6DJZ;
DR  PDB: 6DK0;
DR  PDB: 6DK1;
DR  Pfam: PF04622;
DR  OMIM: 601978;
DR  OMIM: 605726;
DR  OMIM: 614373;
DR  DisGeNET: 10280;
DE  Function: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:16472803, PubMed:9341151). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000269|PubMed:16472803, ECO:0000269|PubMed:9341151}.
DE  Disease: Amyotrophic lateral sclerosis 16, juvenile (ALS16) [MIM:614373]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:21842496}. Note=The disease is caused by variants affecting the gene represented in this entry. Distal spinal muscular atrophy, autosomal recessive, 2 (DSMA2) [MIM:605726]: An autosomal recessive neuromuscular disorder characterized by onset of distal muscle weakness and wasting affecting the lower and upper limbs in the first decade. There is no sensory involvement. {ECO:0000269|PubMed:26078401, ECO:0000269|PubMed:27629094}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P0C6X7; IntAct: EBI-26377180; Score: 0.40
DE  Interaction: P0DTD1; IntAct: EBI-25490993; Score: 0.73
DE  Interaction: Q13286; IntAct: EBI-3248480; Score: 0.35
DE  Interaction: Q5EBL8; IntAct: EBI-3922105; Score: 0.37
DE  Interaction: Q6NUS6; IntAct: EBI-11387310; Score: 0.27
DE  Interaction: P27105; IntAct: EBI-12452286; Score: 0.51
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q16799; IntAct: EBI-21515832; Score: 0.35
DE  Interaction: Q8IZF4; IntAct: EBI-21536448; Score: 0.35
DE  Interaction: Q99720; IntAct: EBI-16203486; Score: 0.74
DE  Interaction: P05067; IntAct: EBI-21132574; Score: 0.46
DE  Interaction: P14416; IntAct: EBI-21455412; Score: 0.52
DE  Interaction: Q92847; IntAct: EBI-21459169; Score: 0.50
DE  Interaction: Q9UGJ1; IntAct: EBI-25486484; Score: 0.35
DE  Interaction: P0DTC5; IntAct: EBI-26495256; Score: 0.35
DE  Interaction: O00213; IntAct: EBI-25831044; Score: 0.56
DE  Interaction: P50454; IntAct: EBI-25836526; Score: 0.56
DE  Interaction: P17612; IntAct: EBI-25884713; Score: 0.56
DE  Interaction: P37173; IntAct: EBI-25892804; Score: 0.56
DE  Interaction: P30626; IntAct: EBI-26610305; Score: 0.35
DE  Interaction: P34972; IntAct: EBI-26880846; Score: 0.35
DE  Interaction: Q9H5K3; IntAct: EBI-28948637; Score: 0.35
DE  Interaction: Q05DH4; IntAct: EBI-34574576; Score: 0.27
GO  GO:0070161;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0014069;
GO  GO:0098839;
GO  GO:0004985;
GO  GO:0042802;
GO  GO:0036474;
GO  GO:0006869;
GO  GO:0007399;
GO  GO:0070207;
GO  GO:0043523;
TP  Membrane Topology: Transmembrane; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:27042935};
SQ  MQWAVGRRWAWAALLLAVAAVLTQVVWLWLGTQSFVFQREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQ
SQ  WVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSRGHSGRYWAEISDTIISGTFHQWREGTTKSEVFYPGETVVHGPGEAT
SQ  AVEWGPNTWMVEYGRGVIPSTLAFALADTVFSTQDFLTLFYTLRSYARGLRLELTTYLFGQDP
//
ID  O55242;
PN  Sigma non-opioid intracellular receptor 1;
GN  Sigmar1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000269|PubMed:12730355}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12730355}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000269|PubMed:12730355}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000269|PubMed:20167253}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (PubMed:12730355). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (PubMed:20167253). {ECO:0000250|UniProtKB:Q99720, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:20167253}.
DR  UNIPROT: O55242;
DR  UNIPROT: Q9JKU9;
DR  Pfam: PF04622;
DE  Function: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane (PubMed:12730355). Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:11149946, PubMed:14622179, PubMed:15571673, PubMed:15777781, PubMed:23332758, PubMed:9425306, PubMed:9603192). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (PubMed:25678561). Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (PubMed:26792191). {ECO:0000269|PubMed:11149946, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:14622179, ECO:0000269|PubMed:15571673, ECO:0000269|PubMed:15777781, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:25678561, ECO:0000269|PubMed:26792191, ECO:0000269|PubMed:9425306, ECO:0000269|PubMed:9603192}.
DE  Reference Proteome: Yes;
DE  Interaction: G3I8R9; IntAct: EBI-1557718; Score: 0.59
DE  Interaction: P63141; IntAct: EBI-6692884; Score: 0.56
DE  Interaction: P61168; IntAct: EBI-21455660; Score: 0.47
GO  GO:0070161;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0014069;
GO  GO:0098839;
GO  GO:0004985;
GO  GO:0042802;
GO  GO:0038023;
GO  GO:0036474;
GO  GO:0006869;
GO  GO:0007399;
GO  GO:0070207;
GO  GO:0043523;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MPWAAGRRWAWITLILTIIAVLIQAAWLWLGTQNFVFSREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQ
SQ  WVFVNAGGWMGAMCILHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWKEGTTKSEVFYPGETVVHGPGEAT
SQ  ALEWGPNTWMVEYGRGVIPSTLFFALADTFFSTQDYLTLFYTLRAYARGLRLELTTYLFGQDS
//
ID  Q5PXE3;
PN  Sigma non-opioid intracellular receptor 1;
GN  SIGMAR1;
OS  36723;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000250|UniProtKB:O55242}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis. Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (By similarity). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DR  UNIPROT: Q5PXE3;
DR  Pfam: PF04622;
DE  Function: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (By similarity). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DE  Reference Proteome: No;
GO  GO:0070161;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0014069;
GO  GO:0098839;
GO  GO:0036474;
GO  GO:0006869;
GO  GO:0043523;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MQWALGRRWVWAALLLAAAAVLTQVVWLWLGTQSFVFQHEEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQ
SQ  WVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSRGHSGRYWAEISDTIISGTFHQWREGTTKSEVFYPGETVVHGPGEAT
SQ  AVEWGPNTWMVEYGRGVIPSTLAFALADTIFSTQDFLTLFYTLRAYARGLRLEFTTYLFGQDS
//
ID  Q9R0C9;
PN  Sigma non-opioid intracellular receptor 1;
GN  Sigmar1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15466698}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000269|PubMed:15466698}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (PubMed:15466698). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720, ECO:0000269|PubMed:15466698}.
DR  UNIPROT: Q9R0C9;
DR  UNIPROT: Q9R1J7;
DR  UNIPROT: Q9Z2W2;
DR  Pfam: PF04622;
DE  Function: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration. Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000269|PubMed:11861817, ECO:0000269|PubMed:11988171, ECO:0000269|PubMed:15170821, ECO:0000269|PubMed:15466698, ECO:0000269|PubMed:16522641, ECO:0000269|PubMed:9489711}.
DE  Reference Proteome: Yes;
DE  Interaction: P06761; IntAct: EBI-1557847; Score: 0.40
DE  Interaction: G3I8R9; IntAct: EBI-1557888; Score: 0.40
DE  Interaction: P63141; IntAct: EBI-6692782; Score: 0.52
DE  Interaction: Q9QYH7; IntAct: EBI-21459552; Score: 0.27
GO  GO:0070161;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0014069;
GO  GO:0098839;
GO  GO:0004985;
GO  GO:0031852;
GO  GO:0038023;
GO  GO:0036474;
GO  GO:0006869;
GO  GO:0007399;
GO  GO:0070207;
GO  GO:0043523;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MPWAVGRRWAWITLFLTIVAVLIQAVWLWLGTQSFVFQREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQ
SQ  WVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWREGTTKSEVYYPGETVVHGPGEAT
SQ  AVEWGPNTWMVEYGRGVIPSTLAFALSDTIFSTQDFLTLFYTLRAYARGLRLELTTYLFGQDP
//
ID  Q645J3;
PN  Sigma non-opioid intracellular receptor 1;
GN  SIGMAR1;
OS  8321;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DR  UNIPROT: Q645J3;
DR  Pfam: PF04622;
DE  Function: May function in lipid transport from the endoplasmic reticulum and be involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. May regulate calcium efflux at the endoplasmic reticulum (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0006869;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MAVLSSRAMRAALGLAVLAVVIQLLRTWLSSKSYLFNQKDIAELAKQHAGMDFEVAFSKIIVELRKKHPGHILPDEDLQW
SQ  IFVNAGGWMGSMCLLHASLTEYILLFGTAIDTGGHSGRYWADISDTVITGTFRQWKEGTTKSEVFYPGDTIVHVAGEATS
SQ  VHWSGGTWMVEYGRGFIPSTMGFALADTIFSTQDFCTLFYTFRIYARCLLLETHTYLSELGLS
//
ID  Q5PXE2;
PN  Sigma non-opioid intracellular receptor 1;
GN  SIGMAR1;
OS  9337;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000250|UniProtKB:O55242}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis. Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (By similarity). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DR  UNIPROT: Q5PXE2;
DR  Pfam: PF04622;
DE  Function: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (By similarity). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DE  Reference Proteome: No;
GO  GO:0070161;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0030426;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0014069;
GO  GO:0098839;
GO  GO:0036474;
GO  GO:0006869;
GO  GO:0043523;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MQWAAGRRWAWITLFLTIVAVLIQAVWLWLGTQSFVFQREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQ
SQ  WVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWREGTTKSEVYYPGETVVHGPGEAT
SQ  AVEWGPNTWMVEYGRGVIPSTLAFALSDTIFSTQDFLTLFYTLRAYARGLRLELTTYLFGQDS
//
ID  Q6DCU6;
PN  Sigma non-opioid intracellular receptor 1;
GN  sigmar1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DR  UNIPROT: Q6DCU6;
DR  PDB: 7W2B;
DR  PDB: 7W2C;
DR  PDB: 7W2D;
DR  PDB: 7W2E;
DR  PDB: 7W2F;
DR  PDB: 7W2G;
DR  PDB: 7W2H;
DR  Pfam: PF04622;
DE  Function: May function in lipid transport from the endoplasmic reticulum and be involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. May regulate calcium efflux at the endoplasmic reticulum (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0006869;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MALWLGLRAVLVVAGLAVLLQLIRGWLSSKSYVFNREEIARLAKEHSGLDYEVAFSKIIVELRKKHPGHILQDEDLQWVF
SQ  VNAGGWMGSMCLLHASLTEYVLLFGTAVDTGGHSGRYWAEISDTILSGTFRQWKEGTTKSEIFYPGDTIVHEVGEATSVQ
SQ  WSSGTWMVEYGRGFIPSTLAFALADTIFSTQDFLTLFYTVKVYSKALLLEASTHLSQLGFF
//
ID  Q66IM1;
PN  Sigma non-opioid intracellular receptor 1;
GN  sigmar1;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99720}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720}.
DR  UNIPROT: Q66IM1;
DR  Pfam: PF04622;
DE  Function: May function in lipid transport from the endoplasmic reticulum and be involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. May regulate calcium efflux at the endoplasmic reticulum (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0006869;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q99720};
SQ  MALWRGLRAVLAVAGLAVAVQLLRGWLGSKSYVFNREEIARLAKEHSGLDYEVAFSKIITELRKKHPGRILPDEDLQWVF
SQ  VNAGGWMGSMCLLHASLTEYVLLFGTAVDTSGHSGRYWAEISDTILSGTFRQWKEGSTKSEIFYPGDTIVHEVGEATSVQ
SQ  WSAGTWMVEYGRGFIPSTLGFALADTIFSTQDFLTLFYTVKVYGKALLLETSTHLSELGFF
//
ID  Q3MHW7;
PN  Sigma intracellular receptor 2;
GN  TMEM97;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated. {ECO:0000250|UniProtKB:Q5BJF2}.
DR  UNIPROT: Q3MHW7;
DR  UNIPROT: A1L510;
DR  PDB: 7M93;
DR  PDB: 7M94;
DR  PDB: 7M95;
DR  PDB: 7M96;
DR  PDB: 7MFI;
DR  PROSITE: PS51751;
DE  Function: Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins. {ECO:0000269|PubMed:28559337}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005791;
GO  GO:0030867;
GO  GO:0042632;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGTLGARRGLEWFLGFYFLSHIPITLLMDLQGVLPRDLYPVELRNLQQWYIEEFKDPLLQTPPAWFKSFLFCELVFQLPF
SQ  FPIAAYAFFKGGCKWIRTPAIIYSVHTMTTLIPILSTLLLDDFSKASHFRGQGPKTFQERLFLISVYIPYFLIPLILLLF
SQ  MVRNPYYKSEEKRKKK
//
ID  Q5BJF2;
PN  Sigma intracellular receptor 2;
GN  TMEM97;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:19583955}; Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum membrane {ECO:0000269|PubMed:19583955}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated. {ECO:0000269|PubMed:19583955}.
DR  UNIPROT: Q5BJF2;
DR  UNIPROT: B4DS02;
DR  UNIPROT: Q07823;
DR  PROSITE: PS51751;
DR  OMIM: 612912;
DR  DisGeNET: 27346;
DE  Function: Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cancer cells (PubMed:28559337). Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation (PubMed:23922215, PubMed:25620095). Under investigation for its potential diagnostic and therapeutic uses (PubMed:23922215, PubMed:25620095). May play a role as a regulator of cellular cholesterol homeostasis (PubMed:19583955). May function as sterol isomerase (PubMed:25566323). May alter the activity of some cytochrome P450 proteins (PubMed:22292588). {ECO:0000269|PubMed:19583955, ECO:0000269|PubMed:28559337, ECO:0000303|PubMed:22292588, ECO:0000303|PubMed:23922215, ECO:0000303|PubMed:25620095, ECO:0000305|PubMed:25566323}.
DE  Reference Proteome: Yes;
DE  Interaction: O14524; IntAct: EBI-24702243; Score: 0.56
DE  Interaction: Q15125; IntAct: EBI-24740501; Score: 0.56
DE  Interaction: Q9GZY8; IntAct: EBI-24506673; Score: 0.56
DE  Interaction: Q13323; IntAct: EBI-24613171; Score: 0.56
DE  Interaction: O60883; IntAct: EBI-24662803; Score: 0.56
DE  Interaction: A6NM10; IntAct: EBI-24668368; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-24673216; Score: 0.56
DE  Interaction: Q8TAF8; IntAct: EBI-23694570; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-23716233; Score: 0.56
DE  Interaction: Q13336; IntAct: EBI-24687434; Score: 0.56
DE  Interaction: Q6IN84; IntAct: EBI-23725656; Score: 0.56
DE  Interaction: Q9Y375; IntAct: EBI-24692888; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24707719; Score: 0.56
DE  Interaction: P43628; IntAct: EBI-24715119; Score: 0.56
DE  Interaction: Q96K19; IntAct: EBI-24716686; Score: 0.56
DE  Interaction: Q13113; IntAct: EBI-24720124; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-24720080; Score: 0.56
DE  Interaction: O15552; IntAct: EBI-24721232; Score: 0.56
DE  Interaction: Q9NR31; IntAct: EBI-24722305; Score: 0.56
DE  Interaction: O95470; IntAct: EBI-23777879; Score: 0.56
DE  Interaction: Q7Z5P4; IntAct: EBI-23790301; Score: 0.56
DE  Interaction: P41181; IntAct: EBI-24750677; Score: 0.56
DE  Interaction: Q7Z7G2; IntAct: EBI-24754691; Score: 0.56
DE  Interaction: P19397; IntAct: EBI-24755339; Score: 0.56
DE  Interaction: Q9H400; IntAct: EBI-24767380; Score: 0.56
DE  Interaction: O75712; IntAct: EBI-24767724; Score: 0.56
DE  Interaction: P15941; IntAct: EBI-24768397; Score: 0.56
DE  Interaction: Q9Y680; IntAct: EBI-24770454; Score: 0.56
DE  Interaction: Q99675; IntAct: EBI-23863356; Score: 0.56
DE  Interaction: O95377; IntAct: EBI-24782498; Score: 0.56
DE  Interaction: Q9H2K0; IntAct: EBI-24797742; Score: 0.56
DE  Interaction: Q14802; IntAct: EBI-23909400; Score: 0.56
DE  Interaction: O75787; IntAct: EBI-25276925; Score: 0.56
DE  Interaction: P38484; IntAct: EBI-25288358; Score: 0.56
DE  Interaction: Q9H902; IntAct: EBI-25288571; Score: 0.56
DE  Interaction: Q96B21; IntAct: EBI-25288527; Score: 0.56
DE  Interaction: Q9BSE2; IntAct: EBI-24449108; Score: 0.56
DE  Interaction: Q8WWH4; IntAct: EBI-24547189; Score: 0.56
DE  Interaction: Q9BVX2; IntAct: EBI-24551340; Score: 0.56
DE  Interaction: P04233; IntAct: EBI-24558651; Score: 0.56
DE  Interaction: Q96AG4; IntAct: EBI-24560640; Score: 0.56
DE  Interaction: A2A2Y4; IntAct: EBI-24581809; Score: 0.56
DE  Interaction: Q9BXK5; IntAct: EBI-24604201; Score: 0.56
DE  Interaction: Q15849; IntAct: EBI-24636787; Score: 0.60
DE  Interaction: Q9BQ51; IntAct: EBI-24646794; Score: 0.56
DE  Interaction: O95471; IntAct: EBI-24650808; Score: 0.56
DE  Interaction: Q9Y282; IntAct: EBI-24653486; Score: 0.56
DE  Interaction: Q8TED1; IntAct: EBI-24654027; Score: 0.56
DE  Interaction: Q9H7M9; IntAct: EBI-24659004; Score: 0.56
DE  Interaction: Q5JX71; IntAct: EBI-24745243; Score: 0.56
DE  Interaction: Q3SXY8; IntAct: EBI-24747218; Score: 0.56
DE  Interaction: Q4KMG9; IntAct: EBI-24761990; Score: 0.56
DE  Interaction: O43278; IntAct: EBI-24774612; Score: 0.56
DE  Interaction: P60201; IntAct: EBI-24802605; Score: 0.56
DE  Interaction: Q8WWF3; IntAct: EBI-24805465; Score: 0.56
DE  Interaction: A8MZ59; IntAct: EBI-24807328; Score: 0.56
DE  Interaction: Q8N183; IntAct: EBI-24808896; Score: 0.56
DE  Interaction: Q9BQT9; IntAct: EBI-25265926; Score: 0.56
DE  Interaction: Q9UBD6; IntAct: EBI-25275092; Score: 0.56
DE  Interaction: Q9P296; IntAct: EBI-21519943; Score: 0.35
DE  Interaction: Q13477; IntAct: EBI-21555701; Score: 0.35
DE  Interaction: P32241; IntAct: EBI-21613594; Score: 0.35
DE  Interaction: Q16774; IntAct: EBI-21649631; Score: 0.35
DE  Interaction: O00186; IntAct: EBI-21649631; Score: 0.35
DE  Interaction: P01903; IntAct: EBI-21827013; Score: 0.35
DE  Interaction: Q9BX73; IntAct: EBI-21890043; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21132574; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTD3; IntAct: EBI-25491532; Score: 0.53
DE  Interaction: P60033; IntAct: EBI-25645944; Score: 0.35
DE  Interaction: H9EJ66; IntAct: EBI-25685143; Score: 0.35
DE  Interaction: P19739; IntAct: EBI-25685423; Score: 0.35
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005791;
GO  GO:0030867;
GO  GO:0042632;
GO  GO:0001558;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGAPATRRCVEWLLGLYFLSHIPITLFMDLQAVLPRELYPVEFRNLLKWYAKEFKDPLLQEPPAWFKSFLFCELVFQLPF
SQ  FPIATYAFLKGSCKWIRTPAIIYSVHTMTTLIPILSTFLFEDFSKASGFKGQRPETLHERLTLVSVYAPYLLIPFILLIF
SQ  MLRSPYYKYEEKRKKK
//
ID  Q4R8A8;
PN  Sigma intracellular receptor 2;
GN  Tmem97;
OS  9541;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated. {ECO:0000250|UniProtKB:Q5BJF2}.
DR  UNIPROT: Q4R8A8;
DR  PROSITE: PS51751;
DE  Function: Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins. {ECO:0000250|UniProtKB:Q5BJF2}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005791;
GO  GO:0030867;
GO  GO:0042632;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGVPATRRCVEWLLGIYFLSHIPITLFMDLQAVLPRELYPVEFRNLLKWYAKEFKDPLLQEPPAWFKSFLFCELVFQLPF
SQ  FPIATYAFLKGSCKWIRTPAIIYSVHTMTTLIPILSTFLFEDFSKASGFKGQRPETLHERLTLISVYAPYLLIPFILLIF
SQ  MLRSPYYKYEEKRKKK
//
ID  Q8VD00;
PN  Sigma intracellular receptor 2;
GN  Tmem97;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated. {ECO:0000250|UniProtKB:Q5BJF2}.
DR  UNIPROT: Q8VD00;
DR  PROSITE: PS51751;
DE  Function: Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins. {ECO:0000250|UniProtKB:Q5BJF2}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005791;
GO  GO:0030867;
GO  GO:0042632;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGALAARRCVEWLLGLYFVSHIPITLFIDLQAVLPPELYPQEFSNLLRWYSKEFKDPLMQEPPVWFKSFLLCELVFQLPF
SQ  FPIAAYAFFKGSCRWIRIPAIIYAAHTITTLIPILYTLLFEDFSKAVAFKGQRPESFRERLTLVGVYAPYLIIPLILLLF
SQ  MLRNPYYKYEEKRKKK
//
ID  Q5U3Y7;
PN  Sigma intracellular receptor 2;
GN  Tmem97;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated. {ECO:0000250|UniProtKB:Q5BJF2}.
DR  UNIPROT: Q5U3Y7;
DR  PROSITE: PS51751;
DE  Function: Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins. {ECO:0000250|UniProtKB:Q5BJF2}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005791;
GO  GO:0030867;
GO  GO:0042632;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGAVTARRCVEWLLGLYFVSHIPITMFIDLQALLPPELYPQEFSNLLRWYSKEFKDPLMQEPPVWFKSFLFCELVFQLPF
SQ  FPIAAYAFFKGSCRWIRIPAIIYAVHTITTLIPILYTILFEDFSKAIAFKGQRPENFRERLTLVGVYAPYLIIPLILLLF
SQ  MLRNPYYKFEEKRKKK
//
ID  Q6DFQ5;
PN  Sigma intracellular receptor 2;
GN  tmem97;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5BJF2}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated. {ECO:0000250|UniProtKB:Q5BJF2}.
DR  UNIPROT: Q6DFQ5;
DR  PROSITE: PS51751;
DE  Function: Intracellular orphan receptor that binds numerous drugs and which is highly expressed in various proliferating cells. Corresponds to the sigma-2 receptor, which is thought to play important role in regulating cell survival, morphology and differentiation. May play a role as a regulator of cellular cholesterol homeostasis. May function as sterol isomerase. May alter the activity of some cytochrome P450 proteins. {ECO:0000250|UniProtKB:Q5BJF2}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005764;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005791;
GO  GO:0030867;
GO  GO:0042632;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAVCARLLEWIFFFYFFSHIPITLLVDLQAVLPPSLYPQELLDLMKWYTVAFKDHLMANPPPWFKSFVYCEAILQLPFFP
SQ  VAAYAFFKGGCKWIRIPAIVYSAHVATTVIAIIGHILFGEFPKSDVIAPLTQKDRLTLVSIYAPYLLVPVLLLLTMLFSP
SQ  RYRQEEKRKRK
//
ID  Q9LDX1;
PN  Protein SUPPRESSOR OF GENE SILENCING 3;
GN  SGS3;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:18165314}. Cytoplasmic granule {ECO:0000269|PubMed:30778176}. Note=Accumulates in inclusion bodies in the cell periphery (PubMed:18165314). May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). Co-localizes with SGIP1 in cytoplasmic granules (PubMed:30778176). {ECO:0000250, ECO:0000269|PubMed:18165314, ECO:0000269|PubMed:30778176}.
DR  UNIPROT: Q9LDX1;
DR  Pfam: PF03468;
DR  Pfam: PF03470;
DE  Function: Required for post-transcriptional gene silencing and natural virus resistance. May bind nucleic acids and is essential for the biogenesis of trans-acting siRNAs but is not required for silencing induced by IR-PTGS. Involved in the juvenile-to-adult transition regulation. In case of begomoviruses infection, it is targeted by the viral protein V2 leading to suppression of post-transcriptional gene silencing. Involved in the mechanisms necessary for quick response to heat and subsequent heritable transgenerational memory of heat acclimation (global warming) such as early flowering and attenuated immunity; this process includes epigenetic regulation as well as post- transcriptional gene silencing (PTGS) (PubMed:30778176). In response to heat, HSFA2 is activated and promotes the expression of REF6 which in turn derepresses HSFA2, thus establishing an heritable feedback loop able to trigger SGIP1 and subsequent SGIP1-mediated SGS3 degradation; this prevents the biosynthesis of trans-acting siRNA (tasiRNA) and leads to the release of HTT5, which drives early flowering but attenuates immunity (PubMed:30778176). {ECO:0000269|PubMed:15165191, ECO:0000269|PubMed:15466488, ECO:0000269|PubMed:30778176}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9SG02; IntAct: EBI-6951771; Score: 0.44
DE  Interaction: Q764F6; IntAct: EBI-15678084; Score: 0.44
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0031625;
GO  GO:0042742;
GO  GO:0051607;
GO  GO:0010286;
GO  GO:0050688;
GO  GO:2000028;
GO  GO:0070921;
GO  GO:0009408;
GO  GO:0009616;
GO  GO:0030422;
GO  GO:0010267;
GO  GO:0010050;
GO  GO:0010025;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSRAGPMSKEKNVQGGYRPEVEQLVQGLAGTRLASSQDDGGEWEVISKKNKNKPGNTSGKTWVSQNSNPPRAWGGQQQG
SQ  RGSNVSGRGNNVSGRGNGNGRGIQANISGRGRALSRKYDNNFVAPPPVSRPPLEGGWNWQARGGSAQHTAVQEFPDVEDD
SQ  VDNASEEENDSDALDDSDDDLASDDYDSDVSQKSHGSRKQNKWFKKFFGSLDSLSIEQINEPQRQWHCPACQNGPGAIDW
SQ  YNLHPLLAHARTKGARRVKLHRELAEVLEKDLQMRGASVIPCGEIYGQWKGLGEDEKDYEIVWPPMVIIMNTRLDKDDND
SQ  KWLGMGNQELLEYFDKYEALRARHSYGPQGHRGMSVLMFESSATGYLEAERLHRELAEMGLDRIAWGQKRSMFSGGVRQL
SQ  YGFLATKQDLDIFNQHSQGKTRLKFELKSYQEMVVKELRQISEDNQQLNYFKNKLSKQNKHAKVLEESLEIMSEKLRRTA
SQ  EDNRIVRQRTKMQHEQNREEMDAHDRFFMDSIKQIHERRDAKEENFEMLQQQERAKVVGQQQQNINPSSNDDCRKRAEEV
SQ  SSFIEFQEKEMEEFVEEREMLIKDQEKKMEDMKKRHHEEIFDLEKEFDEALEQLMYKHGLHNEDD
//
ID  A5YVF1;
PN  Protein SUPPRESSOR OF GENE SILENCING 3;
GN  SGS3;
OS  4081;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:18165314}. Note=Accumulates in inclusion bodies in the cell periphery. May interact with the ER network from the perinuclear region out to the cell periphery (By similarity). {ECO:0000250}.
DR  UNIPROT: A5YVF1;
DR  Pfam: PF03468;
DR  Pfam: PF03470;
DE  Function: Required for post-transcriptional gene silencing and natural virus resistance.
DE  Reference Proteome: Yes;
DE  Interaction: Q764F6; IntAct: EBI-15678029; Score: 0.54
GO  GO:0048471;
GO  GO:0051607;
GO  GO:0031047;
GO  GO:0050688;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSFSKWGGKPSNSSEKQKASSTPTVEEINRGVGDIGLNSEQNEGWEVYARKPKNKGGSSAGKQWAPQNPSPKAWGNQNTK
SQ  AWGHPDVGKKSGTRNNAGSGRGSGNNWSTPSDPQKLARPHLYDGGFPSSAPVPPALKNGWDWSSRVASAHPKDNSQVAAA
SQ  ADDDKASEHDAEDNELDFLDESDDDLHSDDFDSDVGEMSYETRKKNPWFNQLFHSLDSLTVTEINEPERQWHCPACKGGP
SQ  GAIEWFTGLQSLMTHAKTKGLRVKIHRELAELLEEDLRQRGTSVVPPGEVYGRWGGMEFKDKEIVWPPMVIIMNTRLDKD
SQ  ENDKWIGMGNQELLEYFSSYAAVKARHSYGPQGHRGMSLLIFEASAVGYIEADRLSEHFSENGRNRDAWERRSARFYPGG
SQ  KRLLYGYMADKKDIDNFNQHSAGKSKLKFEMRSYKEAVWNPAKQMREDNQQLIWFKNKAAKHQMQAKALEESLSLVSEKH
SQ  RQTLEENKIVRLKTKMHHEQIKEEMEFQEQFFKDQIKIIHDARTAREDNFEKTQQEQREMVKQSNANTASVEDHRVRAEK
SQ  VAKFIKLQDKEMEEFVEERENLMRTHDDRIAALRRKYWEEEVELERKFDLELSKLMEKYSPKQSDEVNSSGTM
//
ID  A5D7F8;
PN  E3 ubiquitin-protein ligase SH3RF1;
GN  SH3RF1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. Note=Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
DR  UNIPROT: A5D7F8;
DR  Pfam: PF07653;
DR  Pfam: PF14604;
DR  PROSITE: PS50002;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin- dependent and clathrin-independent endocytosis. Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005078;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:2001237;
GO  GO:0001764;
GO  GO:0046330;
GO  GO:0032436;
GO  GO:0051865;
GO  GO:0016567;
GO  GO:0043370;
GO  GO:2000564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEQLPSNILLVRLLDGIKQRP
SQ  WKPGPVGGSGTNGTSALRAQSSAVVTCSPKDGPSSQGGPQPRAQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDI
SQ  IVLRRQVDENWYHGEVGGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEG
SQ  MLADKIGIFPISYVEFNSAAKQLIEWDQPPGPGVAAGEGALATTPSSTTTKQPDGKKNTKKRHSFTSLSMASKASQAAQQ
SQ  RHSMEISPPVLISSSNPAAAARIGELAGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPAEAPYPAALATLNPPLP
SQ  PPPLQAATPTGTAVAAAAGMGPRPTAGPTDQTTHPRPQPRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGT
SQ  SMHTSKIGVFPGNYVAPVTRAVTSASQGKVPMLTTGPASRGGVLANPPSTGGPAQKPPGNGVAGGPGVPTAVVSAAHVQT
SQ  SPQAKVLLHASGQMTVNQARSAARTVSAHSQERPTAAVTPIQVQSTPGQSHHPLVSPQPPAPLGPPAHAAASGLGRVGGP
SQ  LACATAPASIPAASLEPEPSSRPATLLPGTPTSPDSGSAARPDKDGKKEKKGLLKLLSGASTKRKPRGSPPASPTLDAEL
SQ  GAELSCGPPGPPCACPGPCDGDTMAPGPQRRASSLDSAPVAPPPRQPCSSLGPAASEVRPAVCERHRVVVSYPPQSEAEL
SQ  ELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI
//
ID  A5D8S5;
PN  E3 ubiquitin-protein ligase SH3RF1;
GN  sh3rf1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}.
DR  UNIPROT: A5D8S5;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  Pfam: PF13445;
DR  PROSITE: PS50002;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Acts as a scaffold protein that contributes to the effective activation of the JNK signaling pathway. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005078;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0043066;
GO  GO:0001764;
GO  GO:0046330;
GO  GO:0032436;
GO  GO:0051865;
GO  GO:0016567;
GO  GO:0043370;
GO  GO:2000564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDESALLDLLECPVCLERLDATAKVLPCQHTFCRRCLLGIVGSRGELRCPECRTLVESGVDELPSNILLVRLLDGIKQRP
SQ  RRTGSVHGTCANGSAVAGVRAQGAGGSQRDPGPTGGQSQRVQAKSTPVRGVPQLPCAKALYNYDGKEPGDLKFSKGDIII
SQ  LRRQVDENWYHGEMGGVHGFFPTNFVQVIKPLPQPPPQCKALYDFELKDKEADKDCLPFSKDDILTVIRRVDENWAEGML
SQ  GDKIGIFPISYVEFNSAARQLIELDKPSEGGGDSSEGPSSSSSGPQANGSQKAPGEKKNSKKRHSFTSLTMSHKPCLAPP
SQ  PQRHSMEISGPVLISSSNPTAAARIGELSGGLSSSAPSQVHICTTGLIVTPPPSSPVTTATVFTFPPETSYASIPVDALP
SQ  PPPPPPPQSQSSVVGAAALNAGQRPSPAAGDQSGRQRPTVYVAMFPYSPRKEDELELRKGEMFLVLERCQDGWFKGTSMH
SQ  TGKIGVFPGNYMSPVSRTVSGSSQPKVPLTLCSQAGRGVTIVSPSSALGSMDLSKPLPVCPNATPSCSLPAAVVTAAHLP
SQ  TGQHPKVLMHVTSQMTVNQARNAVRTAVSHSQDRPTAAVTPIQSHNPVAYLPSTAVVLQASPVLNSSSGCSSARVGVALG
SQ  CAAASLTPPNVSAASLDTDAMRPVPMVALPVNAGSTKPLGAASNHGVACRLDKDCKREKKGLLKLLSNKKKLRPSPPSSP
SQ  TLEAEQSVSMELPQGAVGPEMALSGSAGHNGRIGACPMDSELSMSSSSSNTDAVTHRSSPQDNTAPIAPPPRQPCSSLLS
SQ  MQHDGRPIVCERYRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGRTGLFPGSFVDSI
//
ID  Q7Z6J0;
PN  E3 ubiquitin-protein ligase SH3RF1;
GN  SH3RF1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:15659549, ECO:0000269|PubMed:17420289}. Note=Colocalizes, with AKT2, in lamellipodia (By similarity). Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000269|PubMed:17420289}.
DR  UNIPROT: Q7Z6J0;
DR  UNIPROT: Q05BT2;
DR  UNIPROT: Q8IW46;
DR  UNIPROT: Q9HAM2;
DR  UNIPROT: Q9P234;
DR  PDB: 7NZC;
DR  PDB: 7NZD;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  PROSITE: PS50002;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DR  OMIM: 618642;
DR  DisGeNET: 57630;
DE  Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination (PubMed:15659549, PubMed:20696164). Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin- independent endocytosis (PubMed:19710010). Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (By similarity). {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000269|PubMed:15659549, ECO:0000269|PubMed:19710010, ECO:0000269|PubMed:20696164}. (Microbial infection) Plays an essential role in the targeting of HIV-1 Gag to the plasma membrane, this function is dependent on it's RING domain, and hence it's E3 ligase activity. {ECO:0000269|PubMed:15659549}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: Q13177; IntAct: EBI-7976274; Score: 0.40
DE  Interaction: Q9H2E6; IntAct: EBI-311719; Score: 0.37
DE  Interaction: Q13444; IntAct: EBI-7977073; Score: 0.40
DE  Interaction: P31749; IntAct: EBI-1374066; Score: 0.44
DE  Interaction: P31751; IntAct: EBI-1374415; Score: 0.44
DE  Interaction: P0CG48; IntAct: EBI-8143255; Score: 0.40
DE  Interaction: P63000; IntAct: EBI-8143779; Score: 0.59
DE  Interaction: Q8IVH8; IntAct: EBI-3443365; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-3962281; Score: 0.35
DE  Interaction: O43255; IntAct: EBI-4371961; Score: 0.63
DE  Interaction: P31946; IntAct: EBI-8796749; Score: 0.35
DE  Interaction: Q9Y2I6; IntAct: EBI-11399685; Score: 0.27
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: Q5NFP9; IntAct: EBI-22299321; Score: 0.37
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005078;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:2001237;
GO  GO:0001764;
GO  GO:0046330;
GO  GO:0032436;
GO  GO:0051865;
GO  GO:0016567;
GO  GO:0043370;
GO  GO:2000564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEELPSNILLVRLLDGIKQRP
SQ  WKPGPGGGSGTNCTNALRSQSSTVANCSSKDLQSSQGGQQPRVQSWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDI
SQ  IILRRQVDENWYHGEVNGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEG
SQ  MLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDAGECSSAAAQSSTAPKHSDTKKNTKKRHSFTSLTMANKSSQASQN
SQ  RHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPSDVPYQAALGTLNPPLP
SQ  PPPLLAATVLASTPPGATAAAAAAGMGPRPMAGSTDQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQD
SQ  GWFKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQTSRGVTMVSPSTAGGPAQKLQGNGVAGSPSVVPAAVV
SQ  SAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQERPTAAVTPIQVQNAAGLSPASVGLSHHSLASPQPAPLMPGS
SQ  ATHTAAISISRASAPLACAAAAPLTSPSITSASLEAEPSGRIVTVLPGLPTSPDSASSACGNSSATKPDKDSKKEKKGLL
SQ  KLLSGASTKRKPRVSPPASPTLEVELGSAELPLQGAVGPELPPGGGHGRAGSCPVDGDGPVTTAVAGAALAQDAFHRKAS
SQ  SLDSAVPIAPPPRQACSSLGPVLNESRPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLF
SQ  PGSFVENI
//
ID  Q69ZI1;
PN  E3 ubiquitin-protein ligase SH3RF1;
GN  Sh3rf1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000269|PubMed:14504284, ECO:0000269|PubMed:22959435}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:14504284}. Note=Colocalizes, with AKT2 in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network (By similarity). {ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:14504284}.
DR  UNIPROT: Q69ZI1;
DR  UNIPROT: O70254;
DR  UNIPROT: Q3UG42;
DR  UNIPROT: Q6P9M8;
DR  UNIPROT: Q8BR66;
DR  UNIPROT: Q8C2T5;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  PROSITE: PS50002;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing its dynamin- dependent and clathrin-independent endocytosis (By similarity). Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells (PubMed:23963642, PubMed:27084103, PubMed:9482736). Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (PubMed:22959435). {ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:22959435, ECO:0000269|PubMed:23963642, ECO:0000269|PubMed:27084103, ECO:0000269|PubMed:9482736}.
DE  Reference Proteome: Yes;
DE  Interaction: P61092; IntAct: EBI-957393; Score: 0.37
DE  Interaction: Q06985; IntAct: EBI-957397; Score: 0.37
DE  Interaction: Q06986; IntAct: EBI-957425; Score: 0.37
DE  Interaction: Q8IUQ4; IntAct: EBI-957438; Score: 0.54
DE  Interaction: Q9Z2F7; IntAct: EBI-1774643; Score: 0.58
DE  Interaction: P60953; IntAct: EBI-16881205; Score: 0.37
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005078;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:2001237;
GO  GO:0001764;
GO  GO:0046330;
GO  GO:0032436;
GO  GO:0051865;
GO  GO:0016567;
GO  GO:0043370;
GO  GO:2000564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVDELPSNILLVRLLDGIKQRP
SQ  WKPGPGGGGGTTCTNTLRAQGSTVVNCGSKDLQSSQCGQQPRVQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDI
SQ  IILRRQVDENWYHGEVSGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEG
SQ  MLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDTAECPSATAQSTSASKHPDTKKNTRKRHSFTSLTMANKSSQGSQN
SQ  RHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPAFTFPSDVPYQAALGSMNPPLP
SQ  PPPLLAATVLASTPSGATAAVAAAAAAAAAAGMGPRPVMGSSEQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFL
SQ  VFERCQDGWYKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVSMSTAGQASRGVTMVSPSTAGGPTQKPQGNGVAGNPS
SQ  VVPTAVVSAAHIQTSPQAKVLLHMSGQMTVNQARNAVRTVAAHSQERPTAAVTPIQVQNAACLGPASVGLPHHSLASQPL
SQ  PPMAGPAAHGAAVSISRTNAPMACAAGASLASPNMTSAMLETEPSGRTVTILPGLPTSPESAASACGNSSAGKPDKDSKK
SQ  EKKGLLKLLSGASTKRKPRVSPPASPTLDVELGAGEAPLQGAVGPELPLGGSHGRVGSCPTDGDGPVAAGTAALAQDAFH
SQ  RKTSSLDSAVPIAPPPRQACSSLGPVMNEARPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGK
SQ  TGLFPGSFVENI
//
ID  Q5RBR0;
PN  E3 ubiquitin-protein ligase SH3RF1;
GN  SH3RF1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. Note=Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
DR  UNIPROT: Q5RBR0;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  PROSITE: PS50002;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin- dependent and clathrin-independent endocytosis. Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F- actin assembly. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005078;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0001764;
GO  GO:0046330;
GO  GO:0051865;
GO  GO:0043370;
GO  GO:2000564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEELPSNILLVRLLDGIKQRP
SQ  WKPGPGGGSGTNCTNALRSQSSTVANCSSKDLQSSQGGQQPRVQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDI
SQ  IILRRQVDENWYHGEVNGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEG
SQ  MLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDAGECSSAAAQSSTAPKHSDTKKNTKKRHSFTSLTMANKSSQASQN
SQ  RHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPSDVPYQATLGTLNPPLL
SQ  PPPLLAATVLASTPPGAAAAAAAAGMGPRPMAGSTDQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQD
SQ  GWFKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQTSRGVTMVSPSTAGGPAQKLQGNGVAGSPSVVPTAVV
SQ  SAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQERPTAAVTPIQVQNAAGLSPASVGLPHHSLASPQPAPLMPGS
SQ  ATHTAAISISRASAPLACAAAAPLTSSSITSASLEAEPSGRIVTVLPGLPTSPDSASLACGNSSATKPDKDSKKEKKGLL
SQ  KLLSGASTKRKPRVSPPASPTLEVELGSAELPLHGAVGPELPPGGGHGRAGSCPVDGDGPVTTAVAGAALAQDAFHRKAS
SQ  SLDSAVPIAPPPRQACSSLGPVLNESRPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLF
SQ  PGSFVENI
//
ID  Q71F54;
PN  E3 ubiquitin-protein ligase SH3RF1;
GN  Sh3rf1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16571722}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. Note=Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
DR  UNIPROT: Q71F54;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  PROSITE: PS50002;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin- dependent and clathrin-independent endocytosis (By similarity). Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway (PubMed:12514131). Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (By similarity). {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:12514131}.
DE  Reference Proteome: Yes;
DE  Interaction: Q920M9; IntAct: EBI-957537; Score: 0.40
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005078;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:2001237;
GO  GO:0001764;
GO  GO:0046330;
GO  GO:0032436;
GO  GO:0051865;
GO  GO:0016567;
GO  GO:0043370;
GO  GO:2000564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVDELPSNILLVRLLDGIKQRP
SQ  WKPGPGGGGSTTCTNVLRAQGSTVVNCGSKDLQSPQCGQQPRVQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDI
SQ  IILRRQVDENWYHGEVNGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEG
SQ  MLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDTAECPSATAAQSSSASKHSDTKKNTRKRHSFTSLTMANKSSQASQ
SQ  NRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPTDVPYQAALGTMNPPL
SQ  PPPPLLATTVLASTPSGATAAAVAAAAAAVAAGVGPRPAVGSTEQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMF
SQ  LVFERCQDGWYKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQASRGVTMVSPSTAGGPAQKPQGNGVAGNP
SQ  SVVPTAVVSAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQERPTAAVTPIQVQNAACIGPASVGLPHHSLASQP
SQ  LPPMVGPAAHIAAVNINRTSVPLACAAGASSLASPNMTTAALETEPSGRTVTILPGLPTSPESAASACGNSSAVKPDKDS
SQ  KKEKKGLLKLLSGASTKRKPRVSPPASPTLDVELGSGEVPLQGAVGPELPLGGVHGRVGSCPTDGDGPVAAGTAALAQDA
SQ  FHRKTSSLDSAVPIAPPPRQACSSLGPVMNEARPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRN
SQ  GKTGLFPGSFVENI
//
ID  Q6NRD3;
PN  E3 ubiquitin-protein ligase SH3RF1;
GN  sh3rf1;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}.
DR  UNIPROT: Q6NRD3;
DR  UNIPROT: Q3L1I1;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  Pfam: PF00097;
DR  PROSITE: PS50002;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Acts as a scaffold protein that contributes to the effective activation of the JNK signaling pathway (By similarity). Plays an essential role in the anterior neural development. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:16125690}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8QHK8; IntAct: EBI-7734026; Score: 0.40
DE  Interaction: O14964; IntAct: EBI-7734085; Score: 0.40
GO  GO:0005794;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005078;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0001764;
GO  GO:0046330;
GO  GO:0051865;
GO  GO:0043370;
GO  GO:2000564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVSSRKELRCPECRTLVECGVDELPSNILLVRLLDGIRQRP
SQ  RKAGDGGSAGNSTNALRAQGSVTTNGGLNDAQNTQSGQQRIQARSPPVRGVPQLPCAKALYNYEGKEPGDLKFNKGDIIV
SQ  LRRQVDENWYHGEINGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFLKDDILTVIRRVDENWAEGML
SQ  GDKIGIFPISYVEFNSAAKQLIELDKPSGADTGEGSSGTSHSGNSQKQADAKKNTKKRHSFTSLTMSNKSSQSVQNRHSM
SQ  EISPPVLISSSNPTAAARISELTGLSCSAPSQDMNPPLLPPPPMATPVITSASSGAAAVAQRNIIGPVEQVPHLRTSARP
SQ  SVFIAIYPYIPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAPVTRALTTATPAKVAMATATTSNVV
SQ  NLVTPTPPGAPCQKLPVSGVEFAKTSSTNGVSPAGVPGCHIQTSPQSKVLLHMSGQMTVNQARNAVRTAAAHSQDRPTAA
SQ  VTPIQAQTPAASALPQQAAASQQVPPPLSAPAAYINAAMNISRPSVPAASAASSALPTAAFEAESSWKSSSGLSGCSFSE
SQ  NVSAPLNSAANKQDKDSKKEKKGLLKLLSGASTKRKPRSSPPHSPTQEVEQTNSEAAAALEGAVGPDIVPVIVNGRAAPC
SQ  TVDCDSVSASTPAQDNRKPASLDNNIPIAPPPRQPCSSLGSVLNDSRPCERYRVMVSYPPQSEAELELKEGDIVFVHKKR
SQ  EDGWFKGTLQRNGKTGLFPGSFVENI
//
ID  Q28E95;
PN  E3 ubiquitin-protein ligase SH3RF1;
GN  sh3rf1;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}.
DR  UNIPROT: Q28E95;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  Pfam: PF00097;
DR  PROSITE: PS50002;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Acts as a scaffold protein that contributes to the effective activation of the JNK signaling pathway. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q6NRD3, ECO:0000250|UniProtKB:Q7Z6J0}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0030027;
GO  GO:0048471;
GO  GO:0005078;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0043066;
GO  GO:0001764;
GO  GO:0046330;
GO  GO:0032436;
GO  GO:0051865;
GO  GO:0016567;
GO  GO:0043370;
GO  GO:2000564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVSSRNELRCPECRTLVECGVDELPSNILLVRLLDGIKQRP
SQ  RKAGVGGSAGNSTNVLRAQGSLTTNCGLNDAQNIHGGQQRIQARSPPVRGVPQLPCAKALYNYEGKEPGDLKFNKGDIIV
SQ  LRRQVDENWYHGEINGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFLKDDILTVIRRVDENWAEGML
SQ  GDKIGIFPISYVEFNSAAKQLIELDKPSGVDTGEGSSGTTHSSNSQKQADAKKNTKKRHSFTSLTMSNKSSQSVQNRHSM
SQ  EISPPVLISSSNPTAAARISELTGLSCSAPSQVHISTTGLIVTPPPSSPVVSGPAFTFPPEVTYQAALGDLNPPLLPPPP
SQ  LATPVITSTSSGAAAAVQRSISGPAEQVTHLRTSTRPSVFVAIYPYIPRKEDELELRKGEMFLVFERCQDGWFKGTSMHT
SQ  SKIGVFPGNYVAPVTRALTTATPAKVAMATASSSNVVNLVTPTPPGAPCQKLQGNGAEFAKTVSTNGVPPAGIPGSHIQS
SQ  SPQAKVLLHMSGQMTVNQARNAVRTAAAHSQDRPTAAVTPIQAQIPSASVLPQQAATSQQMPPPLSGPAAYINAAMNISR
SQ  PSVPVASAASSSVSSAAFETECNWKSGSGLAACSFPENVSAPLNSAANKQDKDSKKEKKGLLKLLSGASTKRKPRSSPPH
SQ  SPTQELEQTNSEAALEGAVGPDILPVNGNGRVASCTVDCDLVSASALVQDNRKPASLDTNVPIAPPPRQPCSSLGTVLND
SQ  SRPCERYRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI
//
ID  Q3T0A9;
PN  Protein shisa-5;
GN  SHISA5;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}.
DR  UNIPROT: Q3T0A9;
DR  Pfam: PF13908;
DE  Function: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0042771;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAPAPAPRILVLLLLLLPAPEGAQSELCMISHGRKVDPWVCPDFCCGNCNDQYCCSDVLKQVMWIEEDCHAPEASILTD
SQ  DFDSGFDSDPVARFGTVIAIGVTLFVIAVVTVIVCCTCSCCCLYKMCRRPQPVVTTTMATTVTHTPYLQPPSYPGPTYQG
SQ  YHSVVPQPGMPTAPYPTQPTGPPAYHETMAGGAALPYPASQPPYNPAYMEPPKAVP
//
ID  Q5ZIS9;
PN  Protein shisa-5;
GN  Shisa5;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}.
DR  UNIPROT: Q5ZIS9;
DR  Pfam: PF13908;
DE  Function: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006915;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGFGTLVAIGVIVFAVVVITIILCLTCSCCCLYKACRRPQPVVTTTTATTVVHAPYPQQQGVPPSYPAAPYQGYQPVAIQ
SQ  PQPGMPVAPYPAQYPPPYPMQPPDPPAYHETVAAGAGAPYPISQPPYNPAYMDPQKPTY
//
ID  Q8N114;
PN  Protein shisa-5;
GN  SHISA5;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12135983}; Single-pass type I membrane protein {ECO:0000269|PubMed:12135983}. Nucleus membrane {ECO:0000269|PubMed:12135983}.
DR  UNIPROT: Q8N114;
DR  UNIPROT: B3KW99;
DR  UNIPROT: F8W9N8;
DR  UNIPROT: Q69YY9;
DR  UNIPROT: Q7Z433;
DR  UNIPROT: Q8NHL9;
DR  UNIPROT: Q96MW8;
DR  UNIPROT: Q9BV58;
DR  Pfam: PF13908;
DR  OMIM: 607290;
DR  DisGeNET: 51246;
DE  Function: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000269|PubMed:12135983}.
DE  Reference Proteome: Yes;
DE  Interaction: Q92905; IntAct: EBI-2115585; Score: 0.00
DE  Interaction: Q9NZC7; IntAct: EBI-6366380; Score: 0.52
DE  Interaction: P12815; IntAct: EBI-6693554; Score: 0.60
DE  Interaction: Q92754; IntAct: EBI-9681881; Score: 0.37
DE  Interaction: O43765; IntAct: EBI-23679796; Score: 0.56
DE  Interaction: Q6ICB0; IntAct: EBI-23689591; Score: 0.56
DE  Interaction: Q15041; IntAct: EBI-24754432; Score: 0.56
DE  Interaction: Q9NYZ1; IntAct: EBI-23908959; Score: 0.56
DE  Interaction: P57086; IntAct: EBI-24575497; Score: 0.56
DE  Interaction: Q96EQ0; IntAct: EBI-25180907; Score: 0.56
DE  Interaction: Q99816; IntAct: EBI-30839933; Score: 0.44
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0050699;
GO  GO:0042771;
GO  GO:0043123;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTAPVPAPRILLPLLLLLLLTPPPGARGEVCMASRGLSLFPESCPDFCCGTCDDQYCCSDVLKKFVWSEERCAVPEASVP
SQ  ASVEPVEQLGSALRFRPGYNDPMSGFGATLAVGLTIFVLSVVTIIICFTCSCCCLYKTCRRPRPVVTTTTSTTVVHAPYP
SQ  QPPSVPPSYPGPSYQGYHTMPPQPGMPAAPYPMQYPPPYPAQPMGPPAYHETLAGGAAAPYPASQPPYNPAYMDAPKAAL
//
ID  Q9D7I0;
PN  Protein shisa-5;
GN  Shisa5;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12135983}; Single-pass type I membrane protein {ECO:0000269|PubMed:12135983}. Nucleus membrane {ECO:0000269|PubMed:12135983}.
DR  UNIPROT: Q9D7I0;
DR  UNIPROT: Q8BJ86;
DR  UNIPROT: Q8BJ87;
DR  UNIPROT: Q8BLE9;
DR  UNIPROT: Q8K4W3;
DR  UNIPROT: Q91Z37;
DR  UNIPROT: Q9CQP5;
DR  Pfam: PF13908;
DE  Function: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000269|PubMed:12135983}.
DE  Reference Proteome: Yes;
DE  Interaction: P12815; IntAct: EBI-6857545; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0050699;
GO  GO:0072332;
GO  GO:0042771;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAPAPSLWTLLLLLLLLPPPPGAHGELCRPFGEDNSIPVFCPDFCCGSCSNQYCCSDVLRKIQWNEEMCPEPESRFSTP
SQ  AEETPEHLGSALKFRSSFDSDPMSGFGATVAIGVTIFVVFIATIIICFTCSCCCLYKMCCPQRPVVTNTTTTTVVHAPYP
SQ  QPQPQPVAPSYPGPTYQGYHPMPPQPGMPAAPYPTQYPPPYLAQPTGPPPYHESLAGASQPPYNPTYMDSLKTIP
//
ID  Q5RDV6;
PN  Protein shisa-5;
GN  SHISA5;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}.
DR  UNIPROT: Q5RDV6;
DR  Pfam: PF13908;
DE  Function: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0006915;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGFGATLAVGLTIFVLSVVTIIICFTCSCCCLYKTCRRPRPVVTTTTSTTVVHAPYPQPPSVPPSYPGPSYQGYHTMPPQ
SQ  PGMPAAPYPMQYPPPYPAQPMGPPAYHETLAGGAAAPYPASQPPYNPAYMDAPKAAL
//
ID  Q5XIH2;
PN  Protein shisa-5;
GN  Shisa5;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}.
DR  UNIPROT: Q5XIH2;
DR  Pfam: PF13908;
DE  Function: Can induce apoptosis in a caspase-dependent manner and plays a role in p53/TP53-dependent apoptosis. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0072332;
GO  GO:0042771;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGFGATVAIGLTVFVVFIATIIVCFTCSCCCLYKMCCRPRPVVSNTTTTTVVHTAYPQPQPVAPSYPGPTYQGYHPMPPQ
SQ  PGMPAAPYPTQYPPPYLAQSTGPPAYHETLAGASQPPYNPAYMDPPKAVP
//
ID  F4I3V6;
PN  Protein SHORT HYPOCOTYL IN WHITE LIGHT 1;
GN  SHW1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00768, ECO:0000269|PubMed:18375596, ECO:0000269|PubMed:26474641}; Multi-pass membrane protein {ECO:0000255}. Note=Constitutively localized in the nucleus of hypocotyl cells. {ECO:0000269|PubMed:18375596}.
DR  UNIPROT: F4I3V6;
DR  UNIPROT: Q0WTQ6;
DR  UNIPROT: Q8LGA9;
DE  Function: Negative regulator of photomorphogenesis modulating both light and abscisic acid (ABA) signaling pathways (PubMed:19704523, PubMed:18375596, PubMed:26474641). Regulates negatively the light- mediated inhibition of hypocotyl elongation, probably in a PHYB- mediated signaling pathway, but promotes flowering time (especially in long days) and lateral root formation (PubMed:18375596, PubMed:19704523). Enhances light-regulated gene expression (PubMed:18375596). Promotes COP1-mediated degradation of HY5 during seedling development (e.g. hypocotyl growth) through enhanced ubiquitination in the darkness. Also involved in root gravitropism (PubMed:26474641, PubMed:18375596). {ECO:0000269|PubMed:18375596, ECO:0000269|PubMed:19704523, ECO:0000269|PubMed:26474641}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0009738;
GO  GO:0009908;
GO  GO:0010100;
GO  GO:0009958;
GO  GO:1901333;
GO  GO:0048578;
GO  GO:0009787;
GO  GO:0031540;
GO  GO:0010380;
GO  GO:0090227;
GO  GO:0009642;
GO  GO:0009416;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAATTTLSSSSSSPSLTLINASHRFVSVTPFSSNSIFLRRRFRRLNRSLASSSSHSRRRYESDDRFFGGGDNYDVVPDD
SQ  DGFSDDDDEEDERESSVDLLIRFLRSMFKKVSKRTKKASRRILPAAMSPRLVSFAVDGILLLGSLSITRAFLEVICNLGG
SQ  TVFTVILLIRLFWAAASFFQTYGNSFGPNPVN
//
ID  Q5ZSQ2;
PN  Adenosine monophosphate-protein hydrolase SidD;
GN  sidD;
OS  272624;
SL  Nucleus Position: SL-0382;
SL  Comments: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:21680813}.
DR  UNIPROT: Q5ZSQ2;
DR  PDB: 4IIK;
DR  PDB: 4IIP;
DR  PDB: 6RP4;
DR  PDB: 6RRE;
DE  Function: Virulence effector that plays a role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as an adenosine monophosphate-protein hydrolase (de-AMPylase) by mediating the hydrolysis of adenosine 5'-monophosphate (AMP) to 'Tyr-77' of host RAB1B, thereby releasing RAB1B from bacterial phagosomes and rendering RAB1B accessible for inactivation by LepB. De- AMPylation of RAB1B cannot take place when LidA is bound to RAB1B. {ECO:0000269|PubMed:21680813, ECO:0000269|PubMed:21734656, ECO:0000269|PubMed:22228731}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0046872;
GO  GO:0044603;
GO  GO:0031267;
GO  GO:0018117;
GO  GO:0044602;
GO  GO:0043087;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVYYEIIKDIVFTYNLQFTHLIHNDRISEVNLGGVTMRSIITQICNGVLHGQSYQSGSNDLDKGNSEIFASSLFVHLNEQ
SQ  GKEIIKHKDSDDKIVIGYTKDGMAFQIVVDGFYGCERQAVFSFIDNYVLPLIDNFSLDLTRYPDSKKVTESLIHTIYSLR
SQ  SKHAPLAEFTMSLCVTYQKDEQLFCAGFGIGDTGIAIKRNEGTIEQLVCHTEVDGFKDAFDNYSSANIDLVIERNSVFNT
SQ  KVMPGDELVGYTYVPPMLEMTEKEFEVETVDGKKINKRIVRHLNLDPGNFDDKDPLFSQLLQVVKSKQKQLVEQAKETGQ
SQ  IQRFGDDFTVGRLVIPDQLLINQLRIHALSIGVSDGLLSYIKNENENKGFLGIYGFFTGADKNIEKATLYKNLIAKYQNN
SQ  HFISLIILSALVSDSKTPLMTQYLVGYLDFPSKALLANKITELLLKELENPDMREILGSRLATDVIEELETKIIRYIHNP
SQ  AGSDIHSTLNLWTADKIKAATNSSLTI
//
ID  O74446;
PN  Sad1-interacting factor 2;
GN  sif2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Localized primarily along the nuclear envelope in a punctate pattern. {ECO:0000269|PubMed:14655046}.
DR  UNIPROT: O74446;
DR  UNIPROT: Q1MTQ4;
DR  Pfam: PF02582;
DE  Function: Required for sporulation where it is believed to have a role in meiotic nuclear division. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q09825; IntAct: EBI-1557543; Score: 0.37
GO  GO:0016021;
GO  GO:0005759;
GO  GO:0031965;
GO  GO:0051321;
GO  GO:0140053;
GO  GO:0030435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNRIGPQRSTKTAAKLRLLPSTEEFDDFRRQDTGREVYSQIPQIEGSTAKRDAEHLGKRHREFLPRVTAYCTCDTFRVD
SQ  LLFKFFQSRRSSHKTRPKQFDECIYSPYSYNNEETTDLLPDTLESSRGTLNRESSQESLQSIFEESGLDRNQPLFREVFC
SQ  FTYGVVVLWGYTIDEEHRFLRELGRFEIEKLKIEDMEVEEFNYYITTLYQPRIFNDFIALRDASNYMIRLSISHAIAQSV
SQ  KISLFEELVNETIDATKDTPQMIAETGRVNLKREEIMMAVGQLFILRININLQGSVLDSPELMWTEPQLEPIYTAARSYL
SQ  EINQRVALLNQRVEVIGDLLSMLKEQITHTHDESLEWIVVILMGLLVLIALFSIVVDWKLFQ
//
ID  Q09877;
PN  Sad1-interacting factor 3;
GN  sif3;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q09877;
DR  UNIPROT: O94555;
DR  Pfam: PF02582;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q09825; IntAct: EBI-1557515; Score: 0.37
GO  GO:0016021;
GO  GO:0005759;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0140053;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSTKDKLNLPPKRTINTRLSTPVHIPPPINSESTRITPQHGSPPRFGDHRISAAQGLFQRRRNARKIDHPLGWFLKNRHA
SQ  AAHIPQRTTKTSQKLVLLPENHAVNSFNEEESNYEDLLTPSDAYNLIKLENLPRDKREELGFPRATAYCVCEAFQLPKVK
SQ  HFLKHYHKVRAKKYDEVLYAVYHLPLVYGRSESCRVSSGPAPDDMPSSASNHNQKHLDSDKPDNENFDSHIISQLYRISE
SQ  IFVFSYGVVVFWNFSLSQEKDILADLTFGGDNSLMVKPLAEEECEIEDLHFHYAPNTKRPRIYNDMIHIPSADNKMKLAM
SQ  SHALAQSVKLSRFELRTDVTMNSALFYPKKLALYGHLGLSRVEVVRMSGHLFQLRVDVNLISNILDTPDFLWDSEPLLLP
SQ  LYTAFREYLEIGPRTNVLNRRCKVIFDMLDIFGKSSADRKMNSITWIIIILISLFVIIFTLEVILRLRWAHR
//
ID  O01477;
PN  Protein simr-1;
GN  simr;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:32338603}. Note=Localizes to perinuclear foci in germ cells, called SIMR foci, which are distinct from Mutator foci, P granules and Z granules (PubMed:32338603). SIMR foci are stacked, with znfx-1 localizing between simr-1 and pgl-1 (PubMed:32338603). Its localization at SIMR foci is adjacent to the mutator complex protein mut-16 (PubMed:32338603). Perinuclear localization is not dependent on mut-16 (PubMed:32338603). {ECO:0000269|PubMed:32338603}.
DR  UNIPROT: O01477;
DE  Function: Acts downstream of piRNA production to promote mediator complex-dependent endogenous siRNA biogenesis from piRNA-target mRNAs in the RNA interference pathway in germ cells (PubMed:32338603). Not required to identify target mRNA by the piRNA pathway (PubMed:32338603). Plays a role in both spermatogenesis and oogenesis and in maintaining fertility over multiple generations, probably by directing mutator-dependent silencing to piRNA-targeted genes (PubMed:32338603). {ECO:0000269|PubMed:32338603}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0090727;
GO  GO:1905881;
GO  GO:0030422;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNEKQQWDDAYCLAEEMHDAGRPFKREELNIADQFICSRFSTIFEYDPYKDTYGFRNQELTHAIPVKSKCRHISDVDIL
SQ  ELKKNTANADIRFPSYLNICPVYAMHPFTVLAFDLSKPVPMGMNASMENAAPNMKSPTEAEITPGTIYIFKHRDNKCYRC
SQ  VILFEDGDNNVSDADRKYMVAFLDTPQVVSVKLKTLFHLGKFTIESYPCALYCCRAVGILEIRKDFGADLNGQINEFYKD
SQ  KVKRKSGVHALIYKKDDRGDKLIFDCPSILGTSMTMALEIKDVIGHRSVAENDPTALSYDELVSKQLPTVDIDDHNSSVV
SQ  LDLEESVIAQELGSTNGADCPCNNDNIDDFMQSQRQNPLDNNRDNWDRINESRSSMQSFAINQSQAITANPTPQPTFDES
SQ  SGEVQTIPESINNLALNGRYLEDGRGTEEIREERSVESRQIGNQVVSQASCNYLEARQNSTQTANAESVCAIISESHAAL
SQ  PTDIQVIPSQHVLNENNHTVLPSVAPIIRNATGHSHIFGRQIPSPAFRRESLSSGNSIQVATFAATTGPCGSNTSRPTAQ
SQ  NTANSSINQDMSISNSSTNARLITIAQDNLNDTENWPNSEREQSATEMESGAEATTNSAVDEFAQVSDDMKGLADSMINF
SQ  LRLTANSNNQDAFKANIFAMELISTKIPNQLTKRFFTLKIAEAKSLAEGFN
//
ID  Q5XVI1;
PN  Protein SINE1;
GN  SINE1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:24891605}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q5XVI1;
DR  UNIPROT: Q1KS90;
DR  UNIPROT: Q9SLJ5;
DE  Function: Plays a role in nucleus positioning in guard cells. {ECO:0000269|PubMed:24891605}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0032797;
GO  GO:0003779;
GO  GO:0007097;
GO  GO:0000387;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGLNLNPILRQELANLDKDTESRKSAMKALKSYVKDLDSKAIPGFLAQVFETKETNSLSGEYTISLYEILARVHGPNIVP
SQ  QIDTIMSTIVKTLASSAGSFPLQQACSKVIPAIARYGIDPTTTEDKKRVIIHSLCKPLTDSLLASQESLTSGAALCLKAL
SQ  VDSDNWRFASDEMVNRVCQNVVVALDSNSNQTHLQMGLVMSLAKHNPLIVEAYARLLIHTGLRILGFGVSEGNSQKRLSA
SQ  VQMLNFLMKCLDPRSIYSEVELIIKEMERCQSDQMAYVRGAAYEAMMTSKRIAAELESKMEKGCRSVTGSNFSRRNCSSI
SQ  VPDYSLSPESQTLGSFSGYDSPVESSPISHTSCNSEFDRRSVNRKLWRRDENGGVVDISLKDGLFSRVTKGSTTVSDSPL
SQ  VPYDTCENGDEFEGFLMESLRNTTPSPQRQRSRRINAEDFNIFSTPRKLISSLQYPDDVDLDHSDIQSPILRGEREKTIG
SQ  SRKNPKLRKQFPTMVETMSSTITVSEDTAQTQMITGKKKKKKMSYAKLVIAISFVVVALFATVILMVNQDDDVGYYTVPT
//
ID  Q9SQR5;
PN  Protein SINE2;
GN  SINE2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:24891605}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9SQR5;
DE  Function: Plays a role in innate immunity against the oomycete pathogen A.arabidopsidis (Hpa). {ECO:0000269|PubMed:24891605}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0032797;
GO  GO:0061760;
GO  GO:0000387;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGRNLGSAFRQELANLDKDPDSHKTAMSNLRSIVKDLDAKVVHVFVAQLSDVKEIGLESGGYTVSLFEDLARAHGVKIAP
SQ  HIDIIMPAIIRTLSSSEGSLRVQQACSRAVAAMARYGIDPTTPEDKKTNVIHSLCKPLSDSLIDSQHQQHLALGSALCLK
SQ  SLVDCDNWRSASSEMVNNVCQSLAVALEATSSEAKSHMALVMALSKHNPFTVEAYARLFVKSGLRILDLGVVEGDSQKRL
SQ  LAIQMLNFLMKNLNPKSISSELELIYQEMEKYQKDQHYVKMAAHETMRQAERLICEADPMFDAENCKPRNSLSGSVKSTS
SQ  SLREHDGSVYSRQDRSYVNDQDEYDVLFSGVASGRTLVSGSPLVTFGDNNQETGFVIESPRIGDQIQCSGVENGNIESVW
SQ  FHQRNRSSEFNESVCSRTNRSRSSRRNTKKRQSGDICSKHHRHGFAQDPFTELLDNRQQLLQYSETSSSSSIYDTSGTTT
SQ  PTNTTEDICEKPKTDLDSEAKLKTVETELDPRLGRSKGVLKLGLSVFSIAVAGFASFMWMYLQDDMMPPHLVPT
//
ID  Q9C900;
PN  Protein SINE3;
GN  SINE3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:24891605}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9C900;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9ZW05; IntAct: EBI-16997601; Score: 0.37
DE  Interaction: Q9M8T0; IntAct: EBI-17007042; Score: 0.37
DE  Interaction: O82390; IntAct: EBI-17012685; Score: 0.37
DE  Interaction: Q9C7S5; IntAct: EBI-17015616; Score: 0.37
DE  Interaction: Q67ZM7; IntAct: EBI-17032980; Score: 0.37
DE  Interaction: Q6NKQ9; IntAct: EBI-17086424; Score: 0.37
DE  Interaction: Q7XA70; IntAct: EBI-17090060; Score: 0.37
DE  Interaction: F4I1K2; IntAct: EBI-17093504; Score: 0.37
DE  Interaction: F4KIB2; IntAct: EBI-17093156; Score: 0.37
DE  Interaction: Q9SV74; IntAct: EBI-17094929; Score: 0.37
DE  Interaction: Q8RXK1; IntAct: EBI-17101958; Score: 0.37
DE  Interaction: Q9FE70; IntAct: EBI-17116307; Score: 0.37
DE  Interaction: Q9LRT1; IntAct: EBI-17131403; Score: 0.37
DE  Interaction: Q9SY89; IntAct: EBI-17131367; Score: 0.37
DE  Interaction: Q9FZB1; IntAct: EBI-17131336; Score: 0.37
DE  Interaction: Q9SNA0; IntAct: EBI-17131816; Score: 0.37
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKEIQIPRKSFARSSELGAKRLKDPEMKNRKVTTEKRQIATFSDVSFESTKDPMDFSPISQISGAISDSEAESVIQGSSL
SQ  DLMSTPEICLPADDSPVSTITSVEARIDTSSTDRIQSIVDLPASVQSLRGEINELKKLICSVDNSAEINWVDRVVTVKFR
SQ  IVLLSFILWAILAAIVVFFSSGEERAYRGPLPT
//
ID  Q9SW31;
PN  Protein SINE4;
GN  SINE4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:24891605}; Single-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9SW31;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEEREESSSHEHLKEKLRELEEEWTAMKTGKNSSAVSWITVEDALEYVENSPRNLMLSLQHKPKAEMIQEISPLRRKLFH
SQ  DSDDDDQTKKTTLLSHSSCWSSNVTSSSDTTKAKKKTTIRRFVSVTMVLLLSWVLVVLMNHFDHLSMNTQIITLVPT
//
ID  Q96FS4;
PN  Signal-induced proliferation-associated protein 1;
GN  SIPA1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:9346962}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9346962}. Endomembrane system; Peripheral membrane protein {ECO:0000269|PubMed:9346962}. Note=Mostly localized in the perinuclear membraneous region. {ECO:0000269|PubMed:9346962}.
DR  UNIPROT: Q96FS4;
DR  UNIPROT: O14518;
DR  UNIPROT: O60484;
DR  UNIPROT: O60618;
DR  UNIPROT: Q2YD83;
DR  Pfam: PF00595;
DR  Pfam: PF02145;
DR  PROSITE: PS50106;
DR  PROSITE: PS50085;
DR  OMIM: 602180;
DR  DisGeNET: 6494;
DE  Function: GTPase activator for the nuclear Ras-related regulatory proteins Rap1 and Rap2 in vitro, converting them to the putatively inactive GDP-bound state (PubMed:9346962). Affects cell cycle progression (By similarity). {ECO:0000250|UniProtKB:P46062, ECO:0000269|PubMed:9346962}.
DE  Reference Proteome: Yes;
DE  Interaction: P38936; IntAct: EBI-3927642; Score: 0.51
DE  Interaction: O14640; IntAct: EBI-3928857; Score: 0.37
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q8R034; IntAct: EBI-11003686; Score: 0.35
DE  Interaction: Q9NQW6; IntAct: EBI-11009421; Score: 0.35
DE  Interaction: O00159; IntAct: EBI-11030803; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062262; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-11092730; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11098811; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-11132927; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-11142496; Score: 0.35
DE  Interaction: P56945; IntAct: EBI-15099687; Score: 0.35
DE  Interaction: P27348; IntAct: EBI-21902679; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-21903886; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21907689; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-21909838; Score: 0.35
DE  Interaction: O68690; IntAct: EBI-20817631; Score: 0.37
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: Q9BYB0; IntAct: EBI-26514894; Score: 0.37
DE  Interaction: P61964; IntAct: EBI-30845695; Score: 0.44
DE  Interaction: P03372; IntAct: EBI-34581889; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0030133;
GO  GO:0005096;
GO  GO:0008022;
GO  GO:0090630;
GO  GO:0002250;
GO  GO:0042631;
GO  GO:0007010;
GO  GO:0035556;
GO  GO:0007162;
GO  GO:0045786;
GO  GO:0030308;
GO  GO:0051056;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:9346962};
SQ  MPMWAGGVGSPRRGMAPASTDDLFARKLRQPARPPLTPHTFEPRPVRGPLLRSGSDAGEARPPTPASPRARAHSHEEASR
SQ  PAATSTRLFTDPLALLGLPAEEPEPAFPPVLEPRWFAHYDVQSLLFDWAPRSQGMGSHSEASSGTLASAEDQAASSDLLH
SQ  GAPGFVCELGGEGELGLGGPASPPVPPALPNAAVSILEEPQNRTSAYSLEHADLGAGYYRKYFYGKEHQNFFGMDESLGP
SQ  VAVSLRREEKEGSGGGTLHSYRVIVRTTQLRTLRGTISEDALPPGPPRGLSPRKLLEHVAPQLSPSCLRLGSASPKVPRT
SQ  LLTLDEQVLSFQRKVGILYCRAGQGSEEEMYNNQEAGPAFMQFLTLLGDVVRLKGFESYRAQLDTKTDSTGTHSLYTTYQ
SQ  DHEIMFHVSTMLPYTPNNQQQLLRKRHIGNDIVTIVFQEPGSKPFCPTTIRSHFQHVFLVVRAHTPCTPHTTYRVAVSRT
SQ  QDTPAFGPALPAGGGPFAANADFRAFLLAKALNGEQAAGHARQFHAMATRTRQQYLQDLATNEVTTTSLDSASRFGLPSL
SQ  GGRRRAAPRGPGAELQAAGSLVWGVRAAPGARVAAGAQASGPEGIEVPCLLGISAEALVLVAPRDGRVVFNCACRDVLAW
SQ  TFSEQQLDLYHGRGEAITLRFDGSPGQAVGEVVARLQLVSRGCETRELALPRDGQGRLGFEVDAEGFVTHVERFTFAETA
SQ  GLRPGARLLRVCGQTLPSLRPEAAAQLLRSAPKVCVTVLPPDESGRPRRSFSELYTLSLQEPSRRGAPDPVQDEVQGVTL
SQ  LPTTKQLLHLCLQDGGSPPGPGDLAEERTEFLHSQNSLSPRSSLSDEAPVLPNTTPDLLLATTAKPSVPSADSETPLTQD
SQ  RPGSPSGSEDKGNPAPELRASFLPRTLSLRNSISRIMSEAGSGTLEDEWQAISEIASTCNTILESLSREGQPIPESGDPK
SQ  GTPKSDAEPEPGNLSEKVSHLESMLRKLQEDLQKEKADRAALEEEVRSLRHNNRRLQAESESAATRLLLASKQLGSPTAD
SQ  LA
//
ID  P46062;
PN  Signal-induced proliferation-associated protein 1;
GN  Sipa1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:7799964}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96FS4}. Endomembrane system; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96FS4}. Note=Mostly localized in the perinuclear membraneous region. {ECO:0000250|UniProtKB:Q96FS4}.
DR  UNIPROT: P46062;
DR  UNIPROT: P70204;
DR  Pfam: PF00595;
DR  Pfam: PF02145;
DR  PROSITE: PS50106;
DR  PROSITE: PS50085;
DE  Function: GTPase activator for the nuclear Ras-related regulatory proteins Rap1, Rsr1 and Ran in vitro, converting them to the putatively inactive GDP-bound state. Affects cell cycle progression. {ECO:0000269|PubMed:7799964}.
DE  Reference Proteome: Yes;
DE  Interaction: Q4U2R1; IntAct: EBI-16730475; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0030133;
GO  GO:0005096;
GO  GO:0008022;
GO  GO:0090630;
GO  GO:0042631;
GO  GO:0051726;
GO  GO:0051056;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q96FS4};
SQ  MWAGGVGSPRRGMAPAPTDDLFARKLRQPARPPLTPNTFEPRPARGPLLRSGSDAGEVRPPTPASPRARAHSHEDASRPA
SQ  ATPTRLFTDPLALLGLPAEEPEPTFPPVLEPRWFAHYDVQSLLFDWAPRPRGTGSHTEANSGTLAEGQTTTSDLLLGAPG
SQ  FVSELGGEGELGLGGPISPPVPPALPNAAVSVLEEPQTRTTTYSLEHADLGAGYYRKYFYGKEHQNFFGLDEALGPVAVS
SQ  LRREEKEGSGGGTLHSYRVIVRTTQLRTLRGTISEDALPPGPPSVSPRKLLEHVAPRLSPTCLRLGSASPKVPRQLLTLD
SQ  EQVLSFQRKGGILYCRAGQGSEEEMYNNQEAGAAFMQFLTLLGDVVRLKGFESYRAQLDTKTDSTGTHSLYTTYQDHEIM
SQ  FHVSTMLPYTPNNQQQLLRKRHIGNDIVTIVFQEPGSKPFCPTTIRSHFQHVFLVVRAHAPCTPHTSYRVAVSRTQDTPA
SQ  FGPALPEGGGPFAANADFRAFLLAKALNGEQAAGHARQFHAMATRTRQQYLQDLATNEVTTTSLDSASRFGLPSLGGRRR
SQ  ATPRSPGADVQAAGALMWGVRAAPGARVAAGAETSGPDDAEVPCLLGISAETLVLVAPRDGRVVFNCACRDVLAWTFSEH
SQ  QLDLYHGRGEAITLRLDGAPGQAVGEVVARLQLVSRGCETRELALPRDGQGRLGFEVDAEGFITHVERFTFAETTGLRPG
SQ  ARLLRVCGQTLPKLGPETAAQMLRSAPKVCVTVLPPDESGRPRRSFSELYMLSLKEPSRRGGPEPVQDETGKLVILPPTK
SQ  QLLHFCLKDSSSPPGPGDLTEERTEFLRTHNSLSSGSSLSDEAPVLPNTTPDLLLVTTANPSAPGTDRETPPSQDQSGSP
SQ  SSHEDTSDSGPELRASILPRTLSLRNSISKIMSEAGSETLEDEWQSISEIASTCNTILESLSREGQPISESGDPKEALKC
SQ  DSEPEPGSLSEKVSHLESMLWKLQEDLQREKADRAALEEEVRSLRHNNQRLLAESESAATRLLLASKHLGAPTTDLA
//
ID  Q8IXJ6;
PN  NAD-dependent protein deacetylase sirtuin-2;
GN  SIRT2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:12697818, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16648462, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:20543840, ECO:0000269|PubMed:23908241, ECO:0000269|PubMed:24177535}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8VDQ8}. Cytoplasm {ECO:0000269|PubMed:12697818, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16648462, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:20543840, ECO:0000269|PubMed:23908241, ECO:0000269|PubMed:24681946}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12620231}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17726514}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:17726514}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17488717}. Midbody {ECO:0000269|PubMed:17726514}. Chromosome {ECO:0000269|PubMed:16648462, ECO:0000269|PubMed:23468428}. Perikaryon {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8VDQ8}. Myelin membrane {ECO:0000250|UniProtKB:Q8VDQ8}. Note=Localizes in the cytoplasm during most of the cell cycle except in the G2/M transition and during mitosis, where it is localized in association with chromatin and induces deacetylation of histone at 'Lys-16' (H4K16ac) (PubMed:17726514, PubMed:23468428). Colocalizes with KMT5A at mitotic foci (PubMed:23468428). Colocalizes with CDK1 at centrosome during prophase and splindle fibers during metaphase (PubMed:17488717). Colocalizes with Aurora kinase AURKA at centrosome during early prophase and in the centrioles and growing mitotic spindle throughout metaphase (PubMed:17488717). Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody (PubMed:17488717). Colocalizes with microtubules (PubMed:12620231). Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity). Shuttles between the cytoplasm and the nucleus through the CRM1 export pathway (PubMed:17726514). Colocalizes with EP300 in the nucleus (PubMed:24177535). Translocates to the nucleus and chromatin upon bacterium Listeria monocytogenes infection in interphase cells (PubMed:23908241). Deacetylates FOXO3 in the cytoplasm (By similarity). Colocalizes with PLP1 in internodal regions, at paranodal axoglial junction and Schmidt-Lanterman incisures of myelin sheat (By similarity). Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons (By similarity). Colocalizes with alpha-tubulin in neuronal growth cone (By similarity). Localizes in the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes (By similarity). Colocalizes with alpha-tubulin on the meiotic spindle as the oocytes enter into metaphase, and also during meiotic anaphase and telophase, especially with the midbody (By similarity). Colocalizes with PARD3 in internodal region of axons (By similarity). Colocalizes with acetylated alpha-tubulin in cell projection processes during primary oligodendrocyte precursor (OLP) differentiation (By similarity). {ECO:0000250|UniProtKB:Q8VDQ8, ECO:0000269|PubMed:12620231, ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:23468428, ECO:0000269|PubMed:23908241, ECO:0000269|PubMed:24177535}. [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:24177535}. Nucleus {ECO:0000269|PubMed:24177535}. Note=Predominantly localized in the cytoplasmic. {ECO:0000269|PubMed:24177535}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:24177535}. Nucleus {ECO:0000269|PubMed:24177535}. Note=Predominantly localized in the cytoplasmic. {ECO:0000269|PubMed:24177535}. [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:24177535}. Nucleus {ECO:0000269|PubMed:24177535}. Note=Predominantly localized in the nucleus. {ECO:0000269|PubMed:24177535}.
DR  UNIPROT: Q8IXJ6;
DR  UNIPROT: A8K3V1;
DR  UNIPROT: B2RB45;
DR  UNIPROT: O95889;
DR  UNIPROT: Q924Y7;
DR  UNIPROT: Q9P0G8;
DR  UNIPROT: Q9UNT0;
DR  UNIPROT: Q9Y6E9;
DR  UNIPROT: U5TP13;
DR  PDB: 1J8F;
DR  PDB: 3ZGO;
DR  PDB: 3ZGV;
DR  PDB: 4L3O;
DR  PDB: 4R8M;
DR  PDB: 4RMG;
DR  PDB: 4RMH;
DR  PDB: 4RMI;
DR  PDB: 4RMJ;
DR  PDB: 4X3O;
DR  PDB: 4X3P;
DR  PDB: 4Y6L;
DR  PDB: 4Y6O;
DR  PDB: 4Y6Q;
DR  PDB: 5D7O;
DR  PDB: 5D7P;
DR  PDB: 5D7Q;
DR  PDB: 5DY4;
DR  PDB: 5DY5;
DR  PDB: 5FYQ;
DR  PDB: 5G4C;
DR  PDB: 5MAR;
DR  PDB: 5MAT;
DR  PDB: 5Y0Z;
DR  PDB: 5Y5N;
DR  PDB: 5YQL;
DR  PDB: 5YQM;
DR  PDB: 5YQN;
DR  PDB: 5YQO;
DR  PDB: 6L65;
DR  PDB: 6L66;
DR  PDB: 6L71;
DR  PDB: 6L72;
DR  PDB: 6NR0;
DR  PDB: 6QCN;
DR  PDB: 7BOS;
DR  PDB: 7BOT;
DR  Pfam: PF02146;
DR  PROSITE: PS50305;
DR  OMIM: 604480;
DR  DisGeNET: 22933;
DE  Function: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors (PubMed:24177535, PubMed:12620231, PubMed:16648462, PubMed:18249187, PubMed:18332217, PubMed:18995842, PubMed:20587414, PubMed:21081649, PubMed:20543840, PubMed:22014574, PubMed:21726808, PubMed:21949390, PubMed:22771473, PubMed:23468428, PubMed:23908241, PubMed:24940000, PubMed:24769394, PubMed:24681946). Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy (PubMed:24177535, PubMed:12620231, PubMed:16648462, PubMed:18249187, PubMed:18332217, PubMed:18995842, PubMed:20587414, PubMed:21081649, PubMed:20543840, PubMed:22014574, PubMed:21726808, PubMed:21949390, PubMed:22771473, PubMed:23468428, PubMed:23908241, PubMed:24940000, PubMed:24769394, PubMed:24681946). Plays a major role in the control of cell cycle progression and genomic stability (PubMed:12697818, PubMed:17488717, PubMed:16909107, PubMed:17726514, PubMed:19282667, PubMed:23468428). Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes (PubMed:12697818, PubMed:17488717, PubMed:16909107, PubMed:17726514, PubMed:19282667, PubMed:23468428). Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis (PubMed:22014574). Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes (PubMed:23468428). Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis (PubMed:23468428). Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression (PubMed:23468428). Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response (PubMed:23468428). Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition (PubMed:20587414). Upon bacterium Listeria monocytogenes infection, deacetylates 'Lys-18' of histone H3 in a receptor tyrosine kinase MET- and PI3K/Akt-dependent manner, thereby inhibiting transcriptional activity and promoting late stages of listeria infection (PubMed:23908241). During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function (PubMed:24940000). Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis (PubMed:24940000). Deacetylates alpha- tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells (PubMed:18332217, PubMed:18995842). Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2- mediated alpha-tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation (PubMed:17488717). Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination (PubMed:21949390). Involved in several cellular metabolic pathways (PubMed:20543840, PubMed:21726808, PubMed:24769394). Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability (PubMed:21726808). Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage (PubMed:24769394). Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis (PubMed:20543840). Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity (PubMed:20543840). Plays a role in the regulation of lysosome- mediated degradation of protein aggregates by autophagy in neuronal cells (PubMed:20543840). Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1- mediated autophagy (PubMed:20543840). Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation (By similarity). Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia (PubMed:24681946). Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation (PubMed:21081649). Inhibits transcriptional activation by deacetylating p53/TP53 and EP300 (PubMed:18249187, PubMed:18995842). Deacetylates also EIF5A (PubMed:22771473). Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions (PubMed:24769394). Plays a role as tumor suppressor (PubMed:22014574). In addition to protein deacetylase activity, also has activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as ARF6 and KRAS, thereby regulating their association with membranes (PubMed:25704306, PubMed:29239724, PubMed:32103017). {ECO:0000250|UniProtKB:Q8VDQ8, ECO:0000269|PubMed:12620231, ECO:0000269|PubMed:12697818, ECO:0000269|PubMed:16648462, ECO:0000269|PubMed:16909107, ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:17574768, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:18249187, ECO:0000269|PubMed:18332217, ECO:0000269|PubMed:18640115, ECO:0000269|PubMed:18722353, ECO:0000269|PubMed:18995842, ECO:0000269|PubMed:19282667, ECO:0000269|PubMed:20543840, ECO:0000269|PubMed:20587414, ECO:0000269|PubMed:21081649, ECO:0000269|PubMed:21726808, ECO:0000269|PubMed:21949390, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:22771473, ECO:0000269|PubMed:22819792, ECO:0000269|PubMed:23468428, ECO:0000269|PubMed:23908241, ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:24177535, ECO:0000269|PubMed:24681946, ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:24940000, ECO:0000269|PubMed:25704306, ECO:0000269|PubMed:29239724, ECO:0000269|PubMed:32103017}. [Isoform 1]: Deacetylates EP300, alpha-tubulin and histone H3 and H4. {ECO:0000269|PubMed:24177535}. [Isoform 2]: Deacetylates EP300, alpha-tubulin and histone H3 and H4. {ECO:0000269|PubMed:24177535}. [Isoform 5]: Lacks deacetylation activity, at least toward known SIRT2 targets. {ECO:0000269|PubMed:24177535}.
DE  Reference Proteome: Yes;
DE  Interaction: Q06609; IntAct: EBI-9064676; Score: 0.37
DE  Interaction: Q86UE4; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: Q92831; IntAct: EBI-477370; Score: 0.58
DE  Interaction: Q92830; IntAct: EBI-477646; Score: 0.40
DE  Interaction: P15172; IntAct: EBI-488593; Score: 0.46
DE  Interaction: Q9UBN7; IntAct: EBI-489322; Score: 0.46
DE  Interaction: P49591; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-1064145; Score: 0.00
DE  Interaction: P13807; IntAct: EBI-1068114; Score: 0.00
DE  Interaction: Q8N1N4; IntAct: EBI-1069878; Score: 0.00
DE  Interaction: Q9NQC3; IntAct: EBI-1071311; Score: 0.00
DE  Interaction: O43791; IntAct: EBI-1074765; Score: 0.00
DE  Interaction: O60729; IntAct: EBI-8634723; Score: 0.52
DE  Interaction: Q9UM11; IntAct: EBI-5239678; Score: 0.54
DE  Interaction: Q12834; IntAct: EBI-5239674; Score: 0.54
DE  Interaction: P30260; IntAct: EBI-5238684; Score: 0.40
DE  Interaction: P01106; IntAct: EBI-6556138; Score: 0.40
DE  Interaction: P11413; IntAct: EBI-9831107; Score: 0.52
DE  Interaction: O60566; IntAct: EBI-9995104; Score: 0.58
DE  Interaction: Q04206; IntAct: EBI-9997616; Score: 0.54
DE  Interaction: P62805; IntAct: EBI-9997912; Score: 0.27
DE  Interaction: Q8VC57; IntAct: EBI-11009211; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-11142496; Score: 0.35
DE  Interaction: Q8N157; IntAct: EBI-11374392; Score: 0.27
DE  Interaction: Q8TES7; IntAct: EBI-11374846; Score: 0.27
DE  Interaction: Q96ST8; IntAct: EBI-11377220; Score: 0.27
DE  Interaction: Q5BJF6; IntAct: EBI-11384576; Score: 0.27
DE  Interaction: Q68CZ1; IntAct: EBI-11386978; Score: 0.27
DE  Interaction: Q96NL6; IntAct: EBI-11396361; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q9BQG2; IntAct: EBI-21530973; Score: 0.35
DE  Interaction: Q9H8J5; IntAct: EBI-21537025; Score: 0.35
DE  Interaction: Q9HCL2; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: Q9H2M9; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: Q8WU76; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: Q15042; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: Q13416; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: P51809; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: O60427; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: O15121; IntAct: EBI-21722691; Score: 0.35
DE  Interaction: P30711; IntAct: EBI-21731095; Score: 0.35
DE  Interaction: P11532; IntAct: EBI-21781853; Score: 0.35
DE  Interaction: Q6ICG6; IntAct: EBI-21806899; Score: 0.35
DE  Interaction: O95863; IntAct: EBI-21847611; Score: 0.35
DE  Interaction: A1A5C7; IntAct: EBI-21849167; Score: 0.35
DE  Interaction: Q96BY2; IntAct: EBI-21884195; Score: 0.35
DE  Interaction: P0CG30; IntAct: EBI-21894956; Score: 0.35
DE  Interaction: Q99NH2; IntAct: EBI-15946059; Score: 0.40
DE  Interaction: P15311; IntAct: EBI-16791848; Score: 0.27
DE  Interaction: P30559; IntAct: EBI-20811054; Score: 0.37
DE  Interaction: P10636; IntAct: EBI-20749487; Score: 0.35
DE  Interaction: P22102; IntAct: EBI-25484744; Score: 0.40
DE  Interaction: Q9BYB0; IntAct: EBI-26508685; Score: 0.51
DE  Interaction: Q96T52; IntAct: EBI-27049069; Score: 0.27
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0005677;
GO  GO:0005694;
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0097386;
GO  GO:0030426;
GO  GO:0000792;
GO  GO:0044224;
GO  GO:0043219;
GO  GO:0072687;
GO  GO:0005874;
GO  GO:0030496;
GO  GO:0005739;
GO  GO:0072686;
GO  GO:0043209;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0033010;
GO  GO:0033270;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0043220;
GO  GO:0005819;
GO  GO:0003682;
GO  GO:0140297;
GO  GO:0035035;
GO  GO:0004407;
GO  GO:0042826;
GO  GO:0003950;
GO  GO:0070403;
GO  GO:0017136;
GO  GO:0046970;
GO  GO:0034979;
GO  GO:0140773;
GO  GO:0140774;
GO  GO:0033558;
GO  GO:0042903;
GO  GO:0043130;
GO  GO:0008270;
GO  GO:0006914;
GO  GO:0051301;
GO  GO:0044242;
GO  GO:0061433;
GO  GO:0071872;
GO  GO:0035729;
GO  GO:0071456;
GO  GO:0071219;
GO  GO:0034599;
GO  GO:0048012;
GO  GO:0031507;
GO  GO:0016575;
GO  GO:0070932;
GO  GO:0070933;
GO  GO:0045087;
GO  GO:0051321;
GO  GO:0007084;
GO  GO:0022011;
GO  GO:0010507;
GO  GO:0008285;
GO  GO:1900425;
GO  GO:0045892;
GO  GO:0045599;
GO  GO:1900226;
GO  GO:0070446;
GO  GO:0010801;
GO  GO:0042177;
GO  GO:2000378;
GO  GO:0045843;
GO  GO:0000122;
GO  GO:0061428;
GO  GO:0044546;
GO  GO:0034983;
GO  GO:0014065;
GO  GO:0051987;
GO  GO:0051781;
GO  GO:0043388;
GO  GO:1900119;
GO  GO:0045836;
GO  GO:1900195;
GO  GO:0032436;
GO  GO:2000777;
GO  GO:0045944;
GO  GO:0043161;
GO  GO:0006471;
GO  GO:0006476;
GO  GO:0043491;
GO  GO:0000183;
GO  GO:0051726;
GO  GO:0007096;
GO  GO:0031641;
GO  GO:0042325;
GO  GO:0051775;
GO  GO:0021762;
GO  GO:0031509;
GO  GO:0090042;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVI
SQ  CLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGL
SQ  LLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLP
SQ  ARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAW
SQ  LGECDQGCLALAELLGWKKELEDLVRREHASIDAQSGAGVPNPSTSASPKKSPPPAKDEARTTEREKPQ
//
ID  Q4R834;
PN  NAD-dependent protein deacetylase sirtuin-2;
GN  SIRT2;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8VDQ8}. Cytoplasm {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8IXJ6}. Midbody {ECO:0000250|UniProtKB:Q8IXJ6}. Chromosome {ECO:0000250|UniProtKB:Q8IXJ6}. Perikaryon {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8VDQ8}. Myelin membrane {ECO:0000250|UniProtKB:Q8VDQ8}. Note=Localizes in the cytoplasm during most of the cell cycle except in the G2/M transition and during mitosis, where it is localized in association with chromatin and induces deacetylation of histone at 'Lys-16' (H4K16ac). Colocalizes with KMT5A at mitotic foci. Colocalizes with CDK1 at centrosome during prophase and splindle fibers during metaphase. Colocalizes with Aurora kinase AURKA at centrosome during early prophase and in the centrioles and growing mitotic spindle throughout metaphase. Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody. Colocalizes with microtubules (By similarity). Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity). Shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. Colocalizes with EP300 in the nucleus. Translocates to the nucleus and chromatin upon bacterium Listeria monocytogenes infection in interphase cells (By similarity). Deacetylates FOXO3 in the cytoplasm. Colocalizes with PLP1 in internodal regions, at paranodal axoglial junction and Schmidt- Lanterman incisures of myelin sheat. Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons. Colocalizes with alpha-tubulin in neuronal growth cone. Localizes in the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes. Colocalizes with alpha-tubulin on the meiotic spindle as the oocytes enter into metaphase, and also during meiotic anaphase and telophase, especially with the midbody. Colocalizes with PARD3 in internodal region of axons (By similarity). Colocalizes with acetylated alpha- tubulin in cell projection processes during primary oligodendrocyte precursor (OLP) differentiation (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8}.
DR  UNIPROT: Q4R834;
DR  Pfam: PF02146;
DR  PROSITE: PS50305;
DE  Function: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors. Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis. Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response. Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition. During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis. Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha- tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity. Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells. Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy (By similarity). Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation (By similarity). Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative regulator on oxidative stress-tolerance in response to anoxia- reoxygenation conditions. Plays a role as tumor suppressor (By similarity). In addition to protein deacetylase activity, also has activity toward long-chain fatty acyl groups and mediates protein- lysine demyristoylation and depalmitoylation of target proteins, such as ARF6 and KRAS, thereby regulating their association with membranes (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0097386;
GO  GO:0030426;
GO  GO:0000792;
GO  GO:0044224;
GO  GO:0043219;
GO  GO:0072687;
GO  GO:0005874;
GO  GO:0030496;
GO  GO:0072686;
GO  GO:0043209;
GO  GO:0005634;
GO  GO:0033010;
GO  GO:0033270;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0043220;
GO  GO:0005819;
GO  GO:0003682;
GO  GO:0004407;
GO  GO:0046872;
GO  GO:0070403;
GO  GO:0046970;
GO  GO:0034979;
GO  GO:0140773;
GO  GO:0140774;
GO  GO:0033558;
GO  GO:0042903;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0044242;
GO  GO:0061433;
GO  GO:0071872;
GO  GO:0035729;
GO  GO:0071456;
GO  GO:0071219;
GO  GO:0034599;
GO  GO:0048012;
GO  GO:0070932;
GO  GO:0070933;
GO  GO:0022011;
GO  GO:0010507;
GO  GO:0008285;
GO  GO:1900425;
GO  GO:0045599;
GO  GO:0070446;
GO  GO:0010801;
GO  GO:0042177;
GO  GO:2000378;
GO  GO:0000122;
GO  GO:0061428;
GO  GO:0034983;
GO  GO:0014065;
GO  GO:0051987;
GO  GO:0051781;
GO  GO:0043388;
GO  GO:1900119;
GO  GO:0045836;
GO  GO:1900195;
GO  GO:0032436;
GO  GO:2000777;
GO  GO:0045944;
GO  GO:0043161;
GO  GO:0006476;
GO  GO:0043491;
GO  GO:0051726;
GO  GO:0031641;
GO  GO:0090042;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVI
SQ  CLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGL
SQ  LLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLP
SQ  ARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMILGLGGGMDFDSKKAYRDVAW
SQ  LGDCDQGCLALAELLGWKKELEDLVRREHASIDAQSGAEAPNPSTSASPRKSPPPAQDEARTTEREKPQ
//
ID  Q8VDQ8;
PN  NAD-dependent protein deacetylase sirtuin-2;
GN  Sirt2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:19037106, ECO:0000269|PubMed:24334550, ECO:0000269|PubMed:24460154}. Cytoplasm {ECO:0000269|PubMed:11056054, ECO:0000269|PubMed:17521387, ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:19037106, ECO:0000269|PubMed:24334550, ECO:0000269|PubMed:24460154}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16933150}. Perikaryon {ECO:0000269|PubMed:16933150}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8IXJ6}. Cell projection {ECO:0000269|PubMed:16933150}. Cell projection, growth cone {ECO:0000269|PubMed:18332217}. Myelin membrane {ECO:0000269|PubMed:16933150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:24334550}. Chromosome {ECO:0000250|UniProtKB:Q8IXJ6}. Midbody {ECO:0000269|PubMed:24334550}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IXJ6}. Note=Localizes in the cytoplasm during most of the cell cycle except in the G2/M transition and during mitosis, where it is localized in association with chromatin and induces deacetylation of histone at 'Lys-16' (H4K16ac). Colocalizes with KMT5A at mitotic foci. Colocalizes with CDK1 at centrosome during prophase and splindle fibers during metaphase. Colocalizes with Aurora kinase AURKA at centrosome during early prophase and in the centrioles and growing mitotic spindle throughout metaphase. Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody. Colocalizes with microtubules (By similarity). Deacetylates FOXO3 in the cytoplasm (PubMed:17521387). Colocalizes with PLP1 in internodal regions of myelin sheat, at paranodal axoglial junction and Schmidt-Lanterman incisures (PubMed:16933150). Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons (PubMed:16933150). Colocalizes with alpha-tubulin in neuronal growth cone (PubMed:18332217). Localizes in the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes (PubMed:24334550). Colocalizes with alpha- tubulin on the meiotic spindle as the oocytes enter into metaphase, and also during meiotic anaphase and telophase, especially with the midbody (PubMed:24334550). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000269|PubMed:16933150, ECO:0000269|PubMed:17521387, ECO:0000269|PubMed:18332217, ECO:0000269|PubMed:24334550}.
DR  UNIPROT: Q8VDQ8;
DR  UNIPROT: E9PXF5;
DR  UNIPROT: Q9CXS5;
DR  UNIPROT: Q9EQ18;
DR  UNIPROT: Q9ERJ9;
DR  UNIPROT: U5TP50;
DR  Pfam: PF02146;
DR  PROSITE: PS50305;
DE  Function: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors (PubMed:17521387, PubMed:17681146, PubMed:17574768, PubMed:19037106, PubMed:22014574, PubMed:21791548, PubMed:21841822, PubMed:24334550). Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis. Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response. Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition. During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis. Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells (PubMed:17574768, PubMed:21791548). Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha-tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6- phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity (PubMed:17681146, PubMed:19037106). Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells (PubMed:17681146, PubMed:19037106). Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy (PubMed:17681146, PubMed:19037106). Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation (PubMed:17521387, PubMed:21841822). Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions. Plays a role as tumor suppressor (PubMed:22014574, PubMed:23468428). In addition to protein deacetylase activity, also has activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as ARF6 and KRAS, thereby regulating their association with membranes (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000269|PubMed:17521387, ECO:0000269|PubMed:17574768, ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:19037106, ECO:0000269|PubMed:21791548, ECO:0000269|PubMed:21841822, ECO:0000269|PubMed:21949390, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:23468428, ECO:0000269|PubMed:24334550}. [Isoform 1]: Deacetylates alpha-tubulin. {ECO:0000269|PubMed:21791548}. [Isoform 2]: Deacetylates alpha-tubulin. {ECO:0000269|PubMed:21791548}. [Isoform 4]: Deacetylates alpha-tubulin. {ECO:0000269|PubMed:21791548}.
DE  Reference Proteome: Yes;
DE  Interaction: P62158; IntAct: EBI-911456; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-2307988; Score: 0.35
DE  Interaction: Q9H1A4; IntAct: EBI-5238431; Score: 0.35
DE  Interaction: P30260; IntAct: EBI-5238431; Score: 0.35
DE  Interaction: Q13042; IntAct: EBI-5238431; Score: 0.35
DE  Interaction: Q9UJX5; IntAct: EBI-5238431; Score: 0.35
DE  Interaction: Q9UJX2; IntAct: EBI-5238431; Score: 0.35
DE  Interaction: O14965; IntAct: EBI-5238431; Score: 0.60
DE  Interaction: Q9UM11; IntAct: EBI-5238451; Score: 0.50
DE  Interaction: Q12834; IntAct: EBI-5238451; Score: 0.50
DE  Interaction: Q9R1K5; IntAct: EBI-5238551; Score: 0.40
DE  Interaction: Q9JJ66; IntAct: EBI-5238595; Score: 0.40
DE  Interaction: Q05BA5; IntAct: EBI-26680480; Score: 0.37
DE  Interaction: Q61545; IntAct: EBI-26680472; Score: 0.37
DE  Interaction: Q9JL10; IntAct: EBI-26680504; Score: 0.37
DE  Interaction: O55144; IntAct: EBI-26680496; Score: 0.37
DE  Interaction: Q07279; IntAct: EBI-26680488; Score: 0.37
DE  Interaction: Q9D032; IntAct: EBI-26682471; Score: 0.37
DE  Interaction: Q91X45; IntAct: EBI-26682848; Score: 0.37
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0097386;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0000792;
GO  GO:0044224;
GO  GO:0043219;
GO  GO:0072687;
GO  GO:0005874;
GO  GO:0030496;
GO  GO:0005739;
GO  GO:0072686;
GO  GO:0043209;
GO  GO:0035748;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0033010;
GO  GO:0033270;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0043220;
GO  GO:0005819;
GO  GO:0097456;
GO  GO:0003682;
GO  GO:0140297;
GO  GO:0035035;
GO  GO:0004407;
GO  GO:0042826;
GO  GO:0003950;
GO  GO:0070403;
GO  GO:0017136;
GO  GO:0046970;
GO  GO:0034979;
GO  GO:0140773;
GO  GO:0140774;
GO  GO:0033558;
GO  GO:0042903;
GO  GO:0043130;
GO  GO:0008270;
GO  GO:0006914;
GO  GO:0051301;
GO  GO:0044242;
GO  GO:0061433;
GO  GO:0071872;
GO  GO:0035729;
GO  GO:0071456;
GO  GO:0071219;
GO  GO:0034599;
GO  GO:0048012;
GO  GO:0016575;
GO  GO:0070932;
GO  GO:0070933;
GO  GO:0051321;
GO  GO:0022011;
GO  GO:0043066;
GO  GO:0010507;
GO  GO:0008285;
GO  GO:1900425;
GO  GO:0045892;
GO  GO:0045599;
GO  GO:1900226;
GO  GO:0048715;
GO  GO:0070446;
GO  GO:0010801;
GO  GO:0042177;
GO  GO:2000378;
GO  GO:0045843;
GO  GO:0000122;
GO  GO:0061428;
GO  GO:0044546;
GO  GO:0034983;
GO  GO:0014065;
GO  GO:0051987;
GO  GO:0051781;
GO  GO:0043388;
GO  GO:1900119;
GO  GO:0045836;
GO  GO:1900195;
GO  GO:0032436;
GO  GO:2000777;
GO  GO:0045944;
GO  GO:0043161;
GO  GO:0006471;
GO  GO:0006476;
GO  GO:0043491;
GO  GO:0051726;
GO  GO:0045598;
GO  GO:0031641;
GO  GO:0099149;
GO  GO:0090042;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEPDPSDPLETQAGKVQEAQDSDSDTEGGATGGEAEMDFLRNLFTQTLGLGSQKERLLDELTLEGVTRYMQSERCRKVI
SQ  CLVGAGISTSAGIPDFRSPSTGLYANLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFIRLLKEKGL
SQ  LLRCYTQNIDTLERVAGLEPQDLVEAHGTFYTSHCVNTSCRKEYTMGWMKEKIFSEATPRCEQCQSVVKPDIVFFGENLP
SQ  SRFFSCMQSDFSKVDLLIIMGTSLQVQPFASLISKAPLATPRLLINKEKTGQTDPFLGMMMGLGGGMDFDSKKAYRDVAW
SQ  LGDCDQGCLALADLLGWKKELEDLVRREHANIDAQSGSQAPNPSTTISPGKSPPPAKEAARTKEKEEQQ
//
ID  Q5RBF1;
PN  NAD-dependent protein deacetylase sirtuin-2;
GN  SIRT2;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8VDQ8}. Cytoplasm {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8IXJ6}. Midbody {ECO:0000250|UniProtKB:Q8IXJ6}. Chromosome {ECO:0000250|UniProtKB:Q8IXJ6}. Perikaryon {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8VDQ8}. Myelin membrane {ECO:0000250|UniProtKB:Q8VDQ8}. Note=Localizes in the cytoplasm during most of the cell cycle except in the G2/M transition and during mitosis, where it is localized in association with chromatin and induces deacetylation of histone at 'Lys-16' (H4K16ac). Colocalizes with KMT5A at mitotic foci. Colocalizes with CDK1 at centrosome during prophase and splindle fibers during metaphase. Colocalizes with Aurora kinase AURKA at centrosome during early prophase and in the centrioles and growing mitotic spindle throughout metaphase. Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody. Colocalizes with microtubules (By similarity). Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity). Shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. Colocalizes with EP300 in the nucleus. Translocates to the nucleus and chromatin upon bacterium Listeria monocytogenes infection in interphase cells (By similarity). Deacetylates FOXO3 in the cytoplasm. Colocalizes with PLP1 in internodal regions, at paranodal axoglial junction and Schmidt- Lanterman incisures of myelin sheat. Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons. Colocalizes with alpha-tubulin in neuronal growth cone. Localizes in the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes. Colocalizes with alpha-tubulin on the meiotic spindle as the oocytes enter into metaphase, and also during meiotic anaphase and telophase, especially with the midbody. Colocalizes with PARD3 in internodal region of axons (By similarity). Colocalizes with acetylated alpha- tubulin in cell projection processes during primary oligodendrocyte precursor (OLP) differentiation (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8}.
DR  UNIPROT: Q5RBF1;
DR  Pfam: PF02146;
DR  PROSITE: PS50305;
DE  Function: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors. Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis. Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response. Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition. During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis. Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha- tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity. Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells. Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy (By similarity). Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation (By similarity). Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative regulator on oxidative stress-tolerance in response to anoxia- reoxygenation conditions. Plays a role as tumor suppressor (By similarity). In addition to protein deacetylase activity, also has activity toward long-chain fatty acyl groups and mediates protein- lysine demyristoylation and depalmitoylation of target proteins, such as ARF6 and KRAS, thereby regulating their association with membranes (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8}.
DE  Reference Proteome: Yes;
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0097386;
GO  GO:0030426;
GO  GO:0000792;
GO  GO:0044224;
GO  GO:0043219;
GO  GO:0072687;
GO  GO:0005874;
GO  GO:0030496;
GO  GO:0072686;
GO  GO:0043209;
GO  GO:0005634;
GO  GO:0033010;
GO  GO:0033270;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0043220;
GO  GO:0005819;
GO  GO:0003682;
GO  GO:0004407;
GO  GO:0046872;
GO  GO:0070403;
GO  GO:0046970;
GO  GO:0034979;
GO  GO:0140773;
GO  GO:0140774;
GO  GO:0033558;
GO  GO:0042903;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:0044242;
GO  GO:0061433;
GO  GO:0071872;
GO  GO:0035729;
GO  GO:0071456;
GO  GO:0071219;
GO  GO:0034599;
GO  GO:0048012;
GO  GO:0070932;
GO  GO:0070933;
GO  GO:0022011;
GO  GO:0010507;
GO  GO:0008285;
GO  GO:1900425;
GO  GO:0045599;
GO  GO:0070446;
GO  GO:0010801;
GO  GO:0042177;
GO  GO:2000378;
GO  GO:0000122;
GO  GO:0061428;
GO  GO:0034983;
GO  GO:0014065;
GO  GO:0051987;
GO  GO:0051781;
GO  GO:0043388;
GO  GO:1900119;
GO  GO:0045836;
GO  GO:1900195;
GO  GO:0032436;
GO  GO:2000777;
GO  GO:0045944;
GO  GO:0043161;
GO  GO:0006476;
GO  GO:0043491;
GO  GO:0051726;
GO  GO:0031641;
GO  GO:0090042;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEA
SQ  IFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVS
SQ  ASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAP
SQ  LSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQSG
SQ  AGVPNPSTSASPKKSPPPAKDEARTTEREKPQ
//
ID  Q5RJQ4;
PN  NAD-dependent protein deacetylase sirtuin-2;
GN  Sirt2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8VDQ8}. Cytoplasm {ECO:0000269|PubMed:17344398}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IXJ6}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8IXJ6}. Midbody {ECO:0000250|UniProtKB:Q8IXJ6}. Chromosome {ECO:0000250|UniProtKB:Q8IXJ6}. Perikaryon {ECO:0000269|PubMed:17344398}. Cell projection {ECO:0000250|UniProtKB:Q8VDQ8}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8VDQ8}. Myelin membrane {ECO:0000269|PubMed:17344398}. Note=Localizes in the cytoplasm during most of the cell cycle except in the G2/M transition and during mitosis, where it is localized in association with chromatin and induces deacetylation of histone at 'Lys-16' (H4K16ac). Colocalizes with KMT5A at mitotic foci. Colocalizes with CDK1 at centrosome during prophase and splindle fibers during metaphase. Colocalizes with Aurora kinase AURKA at centrosome during early prophase and in the centrioles and growing mitotic spindle throughout metaphase. Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody. Colocalizes with microtubules (By similarity). Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity). Shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. Colocalizes with EP300 in the nucleus. Translocates to the nucleus and chromatin upon bacterium Listeria monocytogenes infection in interphase cells (By similarity). Deacetylates FOXO3 in the cytoplasm. Colocalizes with PLP1 in internodal regions, at paranodal axoglial junction and Schmidt- Lanterman incisures of myelin sheat. Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons. Colocalizes with alpha-tubulin in neuronal growth cone. Localizes in the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes. Colocalizes with alpha-tubulin on the meiotic spindle as the oocytes enter into metaphase, and also during meiotic anaphase and telophase, especially with the midbody. Colocalizes with PARD3 in internodal region of axons (By similarity). Colocalizes with acetylated alpha- tubulin in cell projection processes during primary oligodendrocyte precursor (OLP) differentiation (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8}.
DR  UNIPROT: Q5RJQ4;
DR  Pfam: PF02146;
DR  PROSITE: PS50305;
DE  Function: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors (PubMed:17344398). Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis. Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response. Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition. During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis. Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha- tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity. Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells. Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy (By similarity). Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation (By similarity). Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative regulator on oxidative stress-tolerance in response to anoxia- reoxygenation conditions. Plays a role as tumor suppressor (PubMed:22943040). In addition to protein deacetylase activity, also has activity toward long-chain fatty acyl groups and mediates protein- lysine demyristoylation and depalmitoylation of target proteins, such as ARF6 and KRAS, thereby regulating their association with membranes (By similarity). {ECO:0000250|UniProtKB:Q8IXJ6, ECO:0000250|UniProtKB:Q8VDQ8, ECO:0000269|PubMed:17344398, ECO:0000269|PubMed:21949390, ECO:0000269|PubMed:22943040}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5XIE8; IntAct: EBI-26438079; Score: 0.35
GO  GO:0005814;
GO  GO:0005813;
GO  GO:0005694;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0097386;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0000792;
GO  GO:0044224;
GO  GO:0043219;
GO  GO:0072687;
GO  GO:0005874;
GO  GO:0030496;
GO  GO:0005739;
GO  GO:0072686;
GO  GO:0043209;
GO  GO:0035748;
GO  GO:0005634;
GO  GO:0033010;
GO  GO:0033270;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0043220;
GO  GO:0005819;
GO  GO:0097456;
GO  GO:0048487;
GO  GO:0003682;
GO  GO:0140297;
GO  GO:0035035;
GO  GO:0004407;
GO  GO:0042826;
GO  GO:0003950;
GO  GO:0070403;
GO  GO:0017136;
GO  GO:0046970;
GO  GO:0034979;
GO  GO:0140773;
GO  GO:0140774;
GO  GO:0033558;
GO  GO:0042903;
GO  GO:0043130;
GO  GO:0008270;
GO  GO:0006914;
GO  GO:0051301;
GO  GO:0044242;
GO  GO:0061433;
GO  GO:0071872;
GO  GO:0035729;
GO  GO:0071456;
GO  GO:0071219;
GO  GO:0034599;
GO  GO:0007417;
GO  GO:0048012;
GO  GO:0016575;
GO  GO:0070932;
GO  GO:0070933;
GO  GO:0051321;
GO  GO:0022011;
GO  GO:0043066;
GO  GO:0010507;
GO  GO:0008285;
GO  GO:1900425;
GO  GO:0045892;
GO  GO:0045599;
GO  GO:1900226;
GO  GO:0048715;
GO  GO:0070446;
GO  GO:0010801;
GO  GO:0042177;
GO  GO:2000378;
GO  GO:0045843;
GO  GO:0000122;
GO  GO:0061428;
GO  GO:0044546;
GO  GO:0034983;
GO  GO:0014065;
GO  GO:0051987;
GO  GO:0051781;
GO  GO:0043388;
GO  GO:1900119;
GO  GO:0045836;
GO  GO:1900195;
GO  GO:0032436;
GO  GO:2000777;
GO  GO:0045944;
GO  GO:0043161;
GO  GO:0006471;
GO  GO:0006476;
GO  GO:0043491;
GO  GO:0051726;
GO  GO:0045598;
GO  GO:0031641;
GO  GO:0099149;
GO  GO:0090042;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDFLRNLFTQTLGLGSQKERLLDELTLEGVTRYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYANLEKYHLPYPEA
SQ  IFEISYFKKHPEPFFALAKELYPGQFKPTICHYFIRLLKEKGLLLRCYTQNIDTLERVAGLEPQDLVEAHGTFYTSHCVN
SQ  TSCGKEYTMSWMKEKIFSEATPKCEKCQNVVKPDIVFFGENLPPRFFSCMQSDFSKVDLLIIMGTSLQVQPFASLISKAP
SQ  LATPRLLINKEKTGQTDPFLGMMMGLGGGMDFDSKKAYRDVAWLGDCDQGCLALADLLGWKELEDLVRREHANIDAQSGS
SQ  QASNPSATVSPRKSPPPAKEAARTKEKEEH
//
ID  O57686;
PN  Small ubiquitin-related modifier 1-A;
GN  sumo1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}.
DR  UNIPROT: O57686;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer (PubMed:9427648). Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric sumo1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:9427648}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0008134;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0016925;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSSEDLGDKKDGGDYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYRQRQGVPMNSLRFLFEGQRISDHQTPKE
SQ  LGMEEEDVIEVYQEQTGGHSTF
//
ID  Q5EAX4;
PN  Small ubiquitin-related modifier 1-B;
GN  sumo1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}.
DR  UNIPROT: Q5EAX4;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer (By similarity). Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric sumo1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (By similarity). {ECO:0000250|UniProtKB:O57686, ECO:0000250|UniProtKB:P63165}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0008134;
GO  GO:0016925;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSSEDLGDKKEGGDYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRISDHQTPKE
SQ  LGMEEEDVIEVYQEQTGGHSTI
//
ID  O95295;
PN  SNARE-associated protein Snapin;
GN  SNAPIN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q9Z266}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z266}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:19168546, ECO:0000269|PubMed:21102408}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z266}. Lysosome membrane {ECO:0000305|PubMed:25898167}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:21102408}. Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells. {ECO:0000269|PubMed:19168546}.
DR  UNIPROT: O95295;
DR  UNIPROT: D3DV56;
DR  UNIPROT: Q5SXU8;
DR  Pfam: PF14712;
DR  OMIM: 607007;
DR  DisGeNET: 23557;
DE  Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE- mediated membrane fusion in non-neuronal cells (PubMed:17182842, PubMed:18167355). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (PubMed:25898167). {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:25898167}.
DE  Reference Proteome: Yes;
DE  Interaction: A1L4K1; IntAct: EBI-24500672; Score: 0.56
DE  Interaction: Q9Y561; IntAct: EBI-296734; Score: 0.37
DE  Interaction: Q9NUP1; IntAct: EBI-465885; Score: 0.37
DE  Interaction: Q6QNY1; IntAct: EBI-465893; Score: 0.83
DE  Interaction: Q96EV8; IntAct: EBI-465897; Score: 0.82
DE  Interaction: P78537; IntAct: EBI-465910; Score: 0.76
DE  Interaction: Q9UL45; IntAct: EBI-466025; Score: 0.53
DE  Interaction: Q6QNY0; IntAct: EBI-466164; Score: 0.35
DE  Interaction: Q15796; IntAct: EBI-7225073; Score: 0.37
DE  Interaction: Q08345; IntAct: EBI-728871; Score: 0.00
DE  Interaction: O95163; IntAct: EBI-729336; Score: 0.00
DE  Interaction: P26641; IntAct: EBI-730846; Score: 0.00
DE  Interaction: P54257; IntAct: EBI-730849; Score: 0.00
DE  Interaction: Q92993; IntAct: EBI-730852; Score: 0.00
DE  Interaction: Q16891; IntAct: EBI-730855; Score: 0.00
DE  Interaction: O95251; IntAct: EBI-730858; Score: 0.00
DE  Interaction: Q96AW1; IntAct: EBI-733337; Score: 0.00
DE  Interaction: O60282; IntAct: EBI-733340; Score: 0.00
DE  Interaction: Q96R06; IntAct: EBI-733343; Score: 0.00
DE  Interaction: P11047; IntAct: EBI-735808; Score: 0.00
DE  Interaction: Q15849; IntAct: EBI-1573308; Score: 0.60
DE  Interaction: Q62668; IntAct: EBI-1573609; Score: 0.62
DE  Interaction: Q08850; IntAct: EBI-1573773; Score: 0.35
DE  Interaction: O70377; IntAct: EBI-1573773; Score: 0.35
DE  Interaction: Q16539; IntAct: EBI-2116941; Score: 0.00
DE  Interaction: Q96L14; IntAct: EBI-2554834; Score: 0.56
DE  Interaction: Q9D0F1; IntAct: EBI-2558810; Score: 0.40
DE  Interaction: Q6A065; IntAct: EBI-2563315; Score: 0.40
DE  Interaction: Q8CZZ7; IntAct: EBI-2855566; Score: 0.00
DE  Interaction: Q7Z465; IntAct: EBI-3943766; Score: 0.37
DE  Interaction: O75923; IntAct: EBI-5357023; Score: 0.50
DE  Interaction: Q9BZ29; IntAct: EBI-5656556; Score: 0.00
DE  Interaction: P13929; IntAct: EBI-5658499; Score: 0.00
DE  Interaction: P35609; IntAct: EBI-5664140; Score: 0.00
DE  Interaction: P05023; IntAct: EBI-5664157; Score: 0.00
DE  Interaction: O00499; IntAct: EBI-5664176; Score: 0.00
DE  Interaction: Q5VT25; IntAct: EBI-5664210; Score: 0.00
DE  Interaction: Q5SW79; IntAct: EBI-21644990; Score: 0.55
DE  Interaction: Q8N3K9; IntAct: EBI-5664244; Score: 0.00
DE  Interaction: P17661; IntAct: EBI-5664261; Score: 0.00
DE  Interaction: P50570; IntAct: EBI-5664279; Score: 0.00
DE  Interaction: Q03001; IntAct: EBI-5664296; Score: 0.00
DE  Interaction: Q9NV70; IntAct: EBI-21673234; Score: 0.35
DE  Interaction: Q8IWE2; IntAct: EBI-5664349; Score: 0.00
DE  Interaction: Q9H6L5; IntAct: EBI-5664367; Score: 0.00
DE  Interaction: Q14974; IntAct: EBI-5664409; Score: 0.00
DE  Interaction: Q04695; IntAct: EBI-5664449; Score: 0.00
DE  Interaction: P24043; IntAct: EBI-5664487; Score: 0.00
DE  Interaction: Q9UPN3; IntAct: EBI-5664521; Score: 0.00
DE  Interaction: Q7Z406; IntAct: EBI-5664555; Score: 0.00
DE  Interaction: P11055; IntAct: EBI-5664573; Score: 0.00
DE  Interaction: P12883; IntAct: EBI-5664609; Score: 0.00
DE  Interaction: Q14511; IntAct: EBI-5664643; Score: 0.00
DE  Interaction: Q15149; IntAct: EBI-5664660; Score: 0.00
DE  Interaction: Q15276; IntAct: EBI-5664677; Score: 0.00
DE  Interaction: Q9UJ41; IntAct: EBI-24270079; Score: 0.56
DE  Interaction: Q96Q15; IntAct: EBI-5664713; Score: 0.00
DE  Interaction: P11277; IntAct: EBI-5664730; Score: 0.00
DE  Interaction: Q01082; IntAct: EBI-5664785; Score: 0.00
DE  Interaction: O94826; IntAct: EBI-5664802; Score: 0.00
DE  Interaction: P09493; IntAct: EBI-5664819; Score: 0.00
DE  Interaction: P07951; IntAct: EBI-24798942; Score: 0.56
DE  Interaction: Q969Q1; IntAct: EBI-5664873; Score: 0.00
DE  Interaction: P62258; IntAct: EBI-5664890; Score: 0.00
DE  Interaction: P63104; IntAct: EBI-5664907; Score: 0.00
DE  Interaction: Q5S007; IntAct: EBI-8752670; Score: 0.66
DE  Interaction: P60881; IntAct: EBI-8753069; Score: 0.40
DE  Interaction: H7BX26; IntAct: EBI-11021989; Score: 0.35
DE  Interaction: Q96NL6; IntAct: EBI-11396361; Score: 0.27
DE  Interaction: P48039; IntAct: EBI-11576732; Score: 0.00
DE  Interaction: P08779; IntAct: EBI-24330490; Score: 0.56
DE  Interaction: Q9UBB9; IntAct: EBI-24341172; Score: 0.56
DE  Interaction: Q7Z3Y8; IntAct: EBI-24484835; Score: 0.56
DE  Interaction: P19012; IntAct: EBI-24486820; Score: 0.56
DE  Interaction: P08727; IntAct: EBI-24509579; Score: 0.56
DE  Interaction: Q7Z3Y9; IntAct: EBI-22754657; Score: 0.56
DE  Interaction: P51946; IntAct: EBI-22754942; Score: 0.56
DE  Interaction: Q63ZY3; IntAct: EBI-24665653; Score: 0.56
DE  Interaction: Q12934; IntAct: EBI-24669400; Score: 0.56
DE  Interaction: Q9Y3C0; IntAct: EBI-24672862; Score: 0.56
DE  Interaction: Q9H1M0; IntAct: EBI-24680175; Score: 0.56
DE  Interaction: Q7Z6G3; IntAct: EBI-24691932; Score: 0.56
DE  Interaction: P49585; IntAct: EBI-24694444; Score: 0.56
DE  Interaction: Q8N9N5; IntAct: EBI-23767493; Score: 0.56
DE  Interaction: P20700; IntAct: EBI-24720012; Score: 0.56
DE  Interaction: Q8IV53; IntAct: EBI-23774805; Score: 0.56
DE  Interaction: P06753; IntAct: EBI-23779263; Score: 0.56
DE  Interaction: P67936; IntAct: EBI-24766526; Score: 0.56
DE  Interaction: Q70UQ0; IntAct: EBI-24768892; Score: 0.67
DE  Interaction: Q13515; IntAct: EBI-24778153; Score: 0.56
DE  Interaction: Q68D86; IntAct: EBI-24778626; Score: 0.56
DE  Interaction: P35900; IntAct: EBI-24793035; Score: 0.56
DE  Interaction: Q5JTB6; IntAct: EBI-25276210; Score: 0.56
DE  Interaction: Q9NYB9; IntAct: EBI-24602317; Score: 0.56
DE  Interaction: Q99816; IntAct: EBI-23929943; Score: 0.56
DE  Interaction: Q9UPT5; IntAct: EBI-25288795; Score: 0.56
DE  Interaction: Q2M2I5; IntAct: EBI-24455909; Score: 0.60
DE  Interaction: Q2T9L4; IntAct: EBI-24558210; Score: 0.56
DE  Interaction: Q96BD8; IntAct: EBI-24594639; Score: 0.56
DE  Interaction: Q8IYW4; IntAct: EBI-25161488; Score: 0.56
DE  Interaction: Q9Y5B8; IntAct: EBI-24760105; Score: 0.56
DE  Interaction: A1L168; IntAct: EBI-24806766; Score: 0.56
DE  Interaction: Q86WT6; IntAct: EBI-21541317; Score: 0.35
DE  Interaction: Q8TDR4; IntAct: EBI-21617027; Score: 0.35
DE  Interaction: Q9Y2V7; IntAct: EBI-21673529; Score: 0.35
DE  Interaction: Q9UJT2; IntAct: EBI-21696311; Score: 0.35
DE  Interaction: Q9NX95; IntAct: EBI-21720503; Score: 0.35
DE  Interaction: O60296; IntAct: EBI-21729552; Score: 0.35
DE  Interaction: Q8WVE6; IntAct: EBI-21754350; Score: 0.35
DE  Interaction: Q9UIL1; IntAct: EBI-21762105; Score: 0.35
DE  Interaction: Q07866; IntAct: EBI-21768919; Score: 0.35
DE  Interaction: A5D8V7; IntAct: EBI-21779481; Score: 0.35
DE  Interaction: Q8N7C3; IntAct: EBI-21782264; Score: 0.35
DE  Interaction: Q96GS4; IntAct: EBI-21795617; Score: 0.35
DE  Interaction: Q5T0J7; IntAct: EBI-21813461; Score: 0.35
DE  Interaction: Q8TDM0; IntAct: EBI-21813727; Score: 0.35
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q19QW5; IntAct: EBI-25649498; Score: 0.37
DE  Interaction: Q7TLC7; IntAct: EBI-26377368; Score: 0.35
DE  Interaction: P26583; IntAct: EBI-26436206; Score: 0.37
GO  GO:0001669;
GO  GO:0070161;
GO  GO:1904115;
GO  GO:0031083;
GO  GO:0099078;
GO  GO:0098574;
GO  GO:0005829;
GO  GO:0000139;
GO  GO:0002177;
GO  GO:0048471;
GO  GO:0030141;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0030672;
GO  GO:0000149;
GO  GO:0008089;
GO  GO:0048490;
GO  GO:0097352;
GO  GO:0008333;
GO  GO:0006886;
GO  GO:1902774;
GO  GO:0007042;
GO  GO:0032418;
GO  GO:0007040;
GO  GO:0032438;
GO  GO:0010977;
GO  GO:0070050;
GO  GO:0031175;
GO  GO:0007269;
GO  GO:0072384;
GO  GO:1902824;
GO  GO:0051604;
GO  GO:0031503;
GO  GO:0051036;
GO  GO:0062196;
GO  GO:0043393;
GO  GO:2000300;
GO  GO:0008090;
GO  GO:0016079;
GO  GO:0031629;
GO  GO:0016188;
GO  GO:0048489;
GO  GO:0072553;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9Z266};
SQ  MAGAGSAAVSGAGTPVAGPTGRDLFAEGLLEFLRPAVQQLDSHVHAVRESQVELREQIDNLATELCRINEDQKVALDLDP
SQ  YVKKLLNARRRVVLVNNILQNAQERLRRLNHSVAKETARRRAMLDSGIYPPGSPGK
//
ID  Q9Z266;
PN  SNARE-associated protein Snapin;
GN  Snapin;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000269|PubMed:12877659}; Peripheral membrane protein {ECO:0000269|PubMed:12877659}; Cytoplasmic side {ECO:0000269|PubMed:12877659}. Cytoplasm, cytosol {ECO:0000269|PubMed:12877659}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12877659}. Golgi apparatus membrane {ECO:0000269|PubMed:17101137}. Lysosome membrane {ECO:0000250|UniProtKB:O95295}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11283605}. Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells. {ECO:0000250|UniProtKB:O95295}.
DR  UNIPROT: Q9Z266;
DR  UNIPROT: Q3U8V4;
DR  UNIPROT: Q922V7;
DR  Pfam: PF14712;
DE  Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE- mediated membrane fusion in non-neuronal cells (PubMed:16760431, PubMed:19546860, PubMed:21998198). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity). {ECO:0000250|UniProtKB:O95295, ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}.
DE  Reference Proteome: Yes;
DE  Interaction: P60879; IntAct: EBI-8753132; Score: 0.40
DE  Interaction: Q06486; IntAct: EBI-7088881; Score: 0.51
DE  Interaction: P97633; IntAct: EBI-7089078; Score: 0.37
DE  Interaction: Q9JJ76; IntAct: EBI-7089008; Score: 0.37
DE  Interaction: Q03343; IntAct: EBI-8760866; Score: 0.35
GO  GO:0001669;
GO  GO:0070161;
GO  GO:1904115;
GO  GO:0031083;
GO  GO:0099078;
GO  GO:0098574;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0000139;
GO  GO:0002177;
GO  GO:0048471;
GO  GO:0030141;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0030672;
GO  GO:0000149;
GO  GO:0008089;
GO  GO:0048490;
GO  GO:0097352;
GO  GO:0017156;
GO  GO:0007268;
GO  GO:0008333;
GO  GO:0051650;
GO  GO:0006886;
GO  GO:1902774;
GO  GO:0007042;
GO  GO:0032418;
GO  GO:0007040;
GO  GO:0032438;
GO  GO:0010977;
GO  GO:0070050;
GO  GO:0031175;
GO  GO:0072384;
GO  GO:0051604;
GO  GO:0031503;
GO  GO:0051036;
GO  GO:0062196;
GO  GO:0043393;
GO  GO:2000300;
GO  GO:0008090;
GO  GO:0016079;
GO  GO:0031629;
GO  GO:0016188;
GO  GO:0048489;
GO  GO:0072553;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:12877659};
SQ  MAAAGSAAVSGAGTPVAGPTGRDLFAEGLLEFLRPAVQQLDSHVHAVRESQVELREQIDNLATELCRINEDQKVALDLDP
SQ  YVKKLLNARRRVVLVNNILQNAQERLRRLNHSVAKETARRRAMLDSGVYPPGSPSK
//
ID  P60192;
PN  SNARE-associated protein Snapin;
GN  Snapin;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000250|UniProtKB:Q9Z266}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z266}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Z266}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z266}. Lysosome membrane {ECO:0000250|UniProtKB:O95295}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:18167355}. Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells. {ECO:0000250|UniProtKB:O95295}.
DR  UNIPROT: P60192;
DR  Pfam: PF14712;
DE  Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE- mediated membrane fusion in non-neuronal cells (PubMed:10195194, PubMed:11283605). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity). {ECO:0000250|UniProtKB:O95295, ECO:0000269|PubMed:10195194, ECO:0000269|PubMed:11283605}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: P21139; IntAct: EBI-7089219; Score: 0.27
DE  Interaction: Q06486; IntAct: EBI-7089182; Score: 0.27
DE  Interaction: Q68FS2; IntAct: EBI-8514670; Score: 0.35
DE  Interaction: D3ZCV0; IntAct: EBI-5351457; Score: 0.40
DE  Interaction: O35433; IntAct: EBI-26900768; Score: 0.40
DE  Interaction: Q9WUD2; IntAct: EBI-26900776; Score: 0.40
GO  GO:0001669;
GO  GO:0070161;
GO  GO:1904115;
GO  GO:0031083;
GO  GO:0099078;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0000139;
GO  GO:0005765;
GO  GO:0002177;
GO  GO:0048471;
GO  GO:0030141;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0030672;
GO  GO:0000149;
GO  GO:0008089;
GO  GO:0048490;
GO  GO:0097352;
GO  GO:0007268;
GO  GO:0008333;
GO  GO:0051650;
GO  GO:0006886;
GO  GO:1902774;
GO  GO:0007042;
GO  GO:0032418;
GO  GO:0007040;
GO  GO:0010977;
GO  GO:0070050;
GO  GO:0031175;
GO  GO:0051604;
GO  GO:0031503;
GO  GO:0043393;
GO  GO:2000300;
GO  GO:0008090;
GO  GO:0016079;
GO  GO:0031629;
GO  GO:0016188;
GO  GO:0048489;
GO  GO:0072553;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9Z266};
SQ  MAAAGSAAVSGAGTPVAGPTGRDLFAEGLLEFLRPAVQQLDSHVHAVRESQVELREQIDNLATELCRINEDQKVALDLDP
SQ  YVKKLLNARRRVVLVNNILQNAQERLRRLNHSVAKETARRRAMLDSGVYPPGSPSK
//
ID  P52497;
PN  Carbon catabolite-derepressing protein kinase;
GN  SNF1;
OS  5476;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
DR  UNIPROT: P52497;
DR  UNIPROT: Q00309;
DR  Pfam: PF16579;
DR  Pfam: PF00069;
DR  Pfam: PF08587;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8 (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0005975;
GO  GO:0006468;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSEQAQPQASADQQQHQHNHHHHHHHHHHNENQSQQQVPIDPAANPANRIGRYQILKTLGEGSFGKVKLAQHLGTGQKVA
SQ  LKIINRKTLAKSDMQGRVEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEFAGKELFDYIVQRGKMPEDEARRFFQQII
SQ  AAVEYCHRHKIVHRDLKPENLLLDDQLNVKIADFGLSNIMTDGNFLKTSCGSPNYMPAPEVISGKLYAGPEVDVWSAGVI
SQ  LYVMLCGRLPFDDEFIPALFKKISNGVYTLPNYLSAGAKHLLTRMLVVNPLNRITIHEIMEDDWFKQDMPDYLLPPDLSK
SQ  NKNSKIDVDEDVIRALSVTMGYDRDCKIVNVIEKANKQVAAGNSSSQQSKSSNEILDAYLLMKENHALVKDLKKSKSENI
SQ  ESFLSQSPPPSPFPNRGSTSSAPGVQQSLTYQTLATVPDLSTLPNSTIAILPTSLPSIHRAYMAETKQNGDPSQQHAPPP
SQ  TKKSKTRWHFGIRSRSYPLDVMGEIYRALKNLGAEWAKPTEEELWTIRVRWKYDTSAQFECGSAPNLMKMQIQLFQLEPN
SQ  NYLVSFKFSGWESAHGNAGTDSPQSHRQQDLDEVGSFSAYPFLHLATRLIMELAVNSQSG
//
ID  Q00372;
PN  Carbon catabolite-derepressing protein kinase;
GN  SNF1;
OS  284593;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
DR  UNIPROT: Q00372;
DR  UNIPROT: Q6FJ61;
DR  Pfam: PF16579;
DR  Pfam: PF00069;
DR  Pfam: PF08587;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8 (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000144;
GO  GO:0005641;
GO  GO:0031965;
GO  GO:0031588;
GO  GO:0005774;
GO  GO:0004679;
GO  GO:0005524;
GO  GO:0005085;
GO  GO:0042802;
GO  GO:0106310;
GO  GO:0007155;
GO  GO:0006995;
GO  GO:0000132;
GO  GO:0071940;
GO  GO:0001403;
GO  GO:0017148;
GO  GO:1900436;
GO  GO:0045722;
GO  GO:0016239;
GO  GO:2000222;
GO  GO:0006468;
GO  GO:2000217;
GO  GO:0034976;
GO  GO:0006986;
GO  GO:0090606;
GO  GO:0005993;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MENKEHHHHHHHHHHHHSNGSYVSNKVSSLADGSRVGNYQIVKTLGEGSFGKVKLAYHVTTGQKVALKIINKKVLAKSDM
SQ  QGRIEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEYAGNELFDYIVQRNKMSEQEARRFFQQIISAVEYCHRHKIVHR
SQ  DLKPENLLLDEHLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYVMLCRRLPFDDES
SQ  IPVLFKNISNGVYTLPKFLSPGASDLIKRMLIVNPLNRISIHEIMQDEWFKVDLAEYLVPQDLKQQEQFNKKSGNEENVE
SQ  EIDDEMVVTLSKTMGYDKDEIYEALESSEDTPAYNEIRNAYILIKDNKSLIKDMKQDNNVTQELDTFLSQSPPTFQQNGD
SQ  GMKASEDQKKKHSGRRLASSVTQQRTFHQPPFMDQSKEEDSTISILPTSLPQIHRANMLAQGLPAASKISPLVTKKSKTR
SQ  WHFGIRSRSYPLDVMGEIYIALKNLGAEWAKPSEEDLWTIRVRWKYDSDESRLIEDGVKKIPNLMKIVIQLFQIETNNYL
SQ  VDFKFDGWESTYGDSTISTNMSEDEMSTFSAYPFLHLTTKLIMELAVNSQGN
//
ID  O94168;
PN  Carbon catabolite-derepressing protein kinase;
GN  SNF1;
OS  5482;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
DR  UNIPROT: O94168;
DR  Pfam: PF16579;
DR  Pfam: PF00069;
DR  Pfam: PF08587;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8 (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0005975;
GO  GO:0006468;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MSEQNQGQPDQQHSGDHQHHHHHHHHHHHSQQPAQPIPIDPNVNPANRIGRYQIIKTLGEGSFGKVKLAQHVGTGQKVAL
SQ  KIINRKTLAKSDMQGRVEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEFAGKELFDYIVQRGKMPEDEARRFFQQIIA
SQ  AVEYCHRHKIVHRDLKPENLLLDDQLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSSGVILY
SQ  VMLCGRLPFDDEFIPALFKKISNGVYTLPNYLSPGAKHLLTRMLVVNPLNRITIHEIMEDEWFKQDMPDYLLPPDLSKIK
SQ  TSKIDIDEDVISALSVTMGYDRDEIISVIEKANREAAAGGATPTNQSKSTNEVLDAYLLMKENHTLVKDLKKSKSENIES
SQ  FLSLSPPPSSSFPNPGSTSSAPGVQQSLTYQTLATVPDLSTLPNSTIAILPTSLPSIHRAYMMETKVNDPQQQIPAPQPT
SQ  KKLKTRWHFGIRSRSYPLDVMGEIYRALKNLGAEWAKPTEEELWTIRVRWKYDSTPQLRVWQRTNLMKMQIQLFQLEPNN
SQ  YLVDFKFDGWEQTSDESKNDASLDYKQQDLDEVGSFSAYPFLHLATRLIMELAVNSQSG
//
ID  P06782;
PN  Carbon catabolite-derepressing protein kinase;
GN  SNF1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:25869125}. Nucleus {ECO:0000269|PubMed:25869125}. Nucleus membrane {ECO:0000269|PubMed:17237508}; Peripheral membrane protein {ECO:0000269|PubMed:17237508}. Note=Nuclear translocation occurs under nitrogen and glucose starvation conditions (PubMed:25869125). {ECO:0000269|PubMed:25869125}.
DR  UNIPROT: P06782;
DR  UNIPROT: D6VTA0;
DR  PDB: 2FH9;
DR  PDB: 2QLV;
DR  PDB: 3DAE;
DR  PDB: 3HYH;
DR  PDB: 3MN3;
DR  PDB: 3T4N;
DR  PDB: 3TDH;
DR  PDB: 3TE5;
DR  Pfam: PF16579;
DR  Pfam: PF00069;
DR  Pfam: PF08587;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine protein kinase essential for release from glucose repression (PubMed:3526554, PubMed:6366512, PubMed:3049551, PubMed:1944227, PubMed:8289797, PubMed:8628258, PubMed:25869125). Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes (PubMed:8289797, PubMed:26667037). The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters (PubMed:15719021). The complex also negatively regulates the HOG1 MAPK pathway in ER stress response including unfolded protein response (UPR) (PubMed:25730376, PubMed:26394309). Under nutrient/energy depletion, the complex phosphorylates and activates PAS kinase PSK1 which in turn activates PBS1, leading to the inhibition of the TORC1 signaling pathway (PubMed:25428989). SNF1 also interacts and phosphorylates adenylate cyclase CYR1 and negatively regulates the protein kinase A signaling pathway (PubMed:26309257). Also phosphorylates and regulates the transcriptional activator CAT8 (PubMed:15121831). {ECO:0000269|PubMed:15121831, ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:1944227, ECO:0000269|PubMed:25428989, ECO:0000269|PubMed:25730376, ECO:0000269|PubMed:25869125, ECO:0000269|PubMed:26309257, ECO:0000269|PubMed:26394309, ECO:0000269|PubMed:26667037, ECO:0000269|PubMed:3049551, ECO:0000269|PubMed:3526554, ECO:0000269|PubMed:6366512, ECO:0000269|PubMed:8289797, ECO:0000269|PubMed:8628258}.
DE  Reference Proteome: Yes;
DE  Interaction: Q04739; IntAct: EBI-391371; Score: 0.86
DE  Interaction: P34164; IntAct: EBI-391374; Score: 0.91
DE  Interaction: P40151; IntAct: EBI-391377; Score: 0.37
DE  Interaction: Q03957; IntAct: EBI-7822865; Score: 0.51
DE  Interaction: P12904; IntAct: EBI-6956627; Score: 0.97
DE  Interaction: P11484; IntAct: EBI-804120; Score: 0.53
DE  Interaction: P32578; IntAct: EBI-804120; Score: 0.67
DE  Interaction: Q00816; IntAct: EBI-804120; Score: 0.72
DE  Interaction: P38990; IntAct: EBI-804120; Score: 0.56
DE  Interaction: P22204; IntAct: EBI-821767; Score: 0.35
DE  Interaction: P32598; IntAct: EBI-821800; Score: 0.35
DE  Interaction: P07270; IntAct: EBI-821981; Score: 0.35
DE  Interaction: P36047; IntAct: EBI-822217; Score: 0.35
DE  Interaction: P14693; IntAct: EBI-855112; Score: 0.00
DE  Interaction: P0CG63; IntAct: EBI-7480635; Score: 0.44
DE  Interaction: Q04049; IntAct: EBI-7569766; Score: 0.40
DE  Interaction: P40433; IntAct: EBI-7452404; Score: 0.35
DE  Interaction: Q84VQ1; IntAct: EBI-2042520; Score: 0.37
DE  Interaction: Q9SCY5; IntAct: EBI-2042539; Score: 0.37
DE  Interaction: Q42384; IntAct: EBI-2107111; Score: 0.37
DE  Interaction: P32562; IntAct: EBI-2112894; Score: 0.35
DE  Interaction: Q08732; IntAct: EBI-2610513; Score: 0.35
DE  Interaction: P22211; IntAct: EBI-2612723; Score: 0.50
DE  Interaction: P47035; IntAct: EBI-2613798; Score: 0.35
DE  Interaction: Q00684; IntAct: EBI-2613798; Score: 0.50
DE  Interaction: P80667; IntAct: EBI-7469935; Score: 0.37
DE  Interaction: P10591; IntAct: EBI-3677386; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3729858; Score: 0.35
DE  Interaction: P25491; IntAct: EBI-3766560; Score: 0.35
DE  Interaction: P09435; IntAct: EBI-3775934; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3788442; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3814316; Score: 0.35
DE  Interaction: P31539; IntAct: EBI-3827904; Score: 0.35
DE  Interaction: P11792; IntAct: EBI-4567519; Score: 0.44
DE  Interaction: P50222; IntAct: EBI-11522962; Score: 0.56
DE  Interaction: Q9UKT9; IntAct: EBI-11523031; Score: 0.56
DE  Interaction: Q9BQ66; IntAct: EBI-11523022; Score: 0.56
DE  Interaction: Q99750; IntAct: EBI-11523013; Score: 0.56
DE  Interaction: Q8N5R6; IntAct: EBI-11522974; Score: 0.56
DE  Interaction: P14373; IntAct: EBI-11522995; Score: 0.56
DE  Interaction: O43597; IntAct: EBI-11522986; Score: 0.56
DE  Interaction: P54619; IntAct: EBI-11523004; Score: 0.56
DE  Interaction: P30822; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P06782; IntAct: EBI-15573379; Score: 0.74
DE  Interaction: Q06213; IntAct: EBI-15978232; Score: 0.37
DE  Interaction: P38782; IntAct: EBI-15978215; Score: 0.37
DE  Interaction: P32570; IntAct: EBI-15978331; Score: 0.37
DE  Interaction: P47821; IntAct: EBI-15978390; Score: 0.37
DE  Interaction: Q00776; IntAct: EBI-16263794; Score: 0.35
DE  Interaction: Q99186; IntAct: EBI-16263964; Score: 0.35
DE  Interaction: P07260; IntAct: EBI-16265957; Score: 0.35
DE  Interaction: P24719; IntAct: EBI-16273423; Score: 0.35
DE  Interaction: P38622; IntAct: EBI-16279033; Score: 0.35
DE  Interaction: Q04279; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P04838; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P25567; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P11075; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P10659; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P09232; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P04806; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: Q04233; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P04385; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P07149; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P25694; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P29311; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P11076; IntAct: EBI-16283487; Score: 0.35
DE  Interaction: P38915; IntAct: EBI-16284064; Score: 0.40
DE  Interaction: Q03897; IntAct: EBI-16287729; Score: 0.35
DE  Interaction: P18961; IntAct: EBI-16292335; Score: 0.35
DE  Interaction: P38232; IntAct: EBI-16397973; Score: 0.51
GO  GO:0000144;
GO  GO:0005737;
GO  GO:0005739;
GO  GO:0005641;
GO  GO:0031965;
GO  GO:0031588;
GO  GO:0005634;
GO  GO:0005774;
GO  GO:0004679;
GO  GO:0005524;
GO  GO:0005085;
GO  GO:0042802;
GO  GO:0140677;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0005975;
GO  GO:0007155;
GO  GO:0006995;
GO  GO:0000132;
GO  GO:0030447;
GO  GO:0071940;
GO  GO:0035556;
GO  GO:0001403;
GO  GO:0017148;
GO  GO:1900436;
GO  GO:0045722;
GO  GO:0016239;
GO  GO:2000222;
GO  GO:0006468;
GO  GO:1904547;
GO  GO:2000217;
GO  GO:0034976;
GO  GO:0006986;
GO  GO:0090606;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:17237508};
SQ  MSSNNNTNTAPANANSSHHHHHHHHHHHHHGHGGSNSTLNNPKSSLADGAHIGNYQIVKTLGEGSFGKVKLAYHTTTGQK
SQ  VALKIINKKVLAKSDMQGRIEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEYAGNELFDYIVQRDKMSEQEARRFFQQ
SQ  IISAVEYCHRHKIVHRDLKPENLLLDEHLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGV
SQ  ILYVMLCRRLPFDDESIPVLFKNISNGVYTLPKFLSPGAAGLIKRMLIVNPLNRISIHEIMQDDWFKVDLPEYLLPPDLK
SQ  PHPEEENENNDSKKDGSSPDNDEIDDNLVNILSSTMGYEKDEIYESLESSEDTPAFNEIRDAYMLIKENKSLIKDMKANK
SQ  SVSDELDTFLSQSPPTFQQQSKSHQKSQVDHETAKQHARRMASAITQQRTYHQSPFMDQYKEEDSTVSILPTSLPQIHRA
SQ  NMLAQGSPAASKISPLVTKKSKTRWHFGIRSRSYPLDVMGEIYIALKNLGAEWAKPSEEDLWTIKLRWKYDIGNKTNTNE
SQ  KIPDLMKMVIQLFQIETNNYLVDFKFDGWESSYGDDTTVSNISEDEMSTFSAYPFLHLTTKLIMELAVNSQSN
//
ID  P39929;
PN  Vacuolar-sorting protein SNF7;
GN  SNF7;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:12194857}. Endosome membrane {ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:24139821}; Peripheral membrane protein {ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:24139821}. Nucleus envelope {ECO:0000269|PubMed:25303532}.
DR  UNIPROT: P39929;
DR  UNIPROT: D6VY27;
DR  UNIPROT: E9P8V6;
DR  PDB: 5FD7;
DR  PDB: 5FD9;
DR  PDB: 5T8L;
DR  PDB: 5T8N;
DR  Pfam: PF03357;
DE  Function: Acts a component of the ESCRT-III complex required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB) (PubMed:11559748, PubMed:12194857). The sequential action of ESCRT-0, -I, and -II together with the ordered assembly of ESCRT-III links membrane invagination to cargo sorting (PubMed:12194857). Membrane scission in the neck of the growing vesicle releases mature, cargo-laden ILVs into the lumen (PubMed:24139821, PubMed:24711499). ESCRT-III is critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery (PubMed:24139821, PubMed:24711499). SNF7 is the most abundant ESCRT-III subunit which forms membrane- sculpting filaments with 30 Angstrom periodicity and a exposed cationic membrane-binding surface (PubMed:26670543). Its activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces (PubMed:26670543). SNF7 filaments then form spirals that could function as spiral springs (PubMed:26522593). The elastic expansion of compressed SNF7 spirals generates an area difference between the two sides of the membrane and thus curvature which could be the origin of membrane deformation leading eventually to fission (PubMed:26522593). SNF7 recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles (PubMed:11029042, PubMed:15935782). ESCRT-III is also recruited to the nuclear envelope (NE) by integral INM proteins to surveil and clear defective nuclear pore complex (NPC) assembly intermediates to ensure the fidelity of NPC assembly (PubMed:25303532). {ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:15935782, ECO:0000269|PubMed:24139821, ECO:0000269|PubMed:24711499, ECO:0000269|PubMed:25303532, ECO:0000269|PubMed:26522593, ECO:0000269|PubMed:3062374}.
DE  Reference Proteome: Yes;
DE  Interaction: P38181; IntAct: EBI-10052681; Score: 0.44
DE  Interaction: P52917; IntAct: EBI-391794; Score: 0.68
DE  Interaction: P53272; IntAct: EBI-392178; Score: 0.37
DE  Interaction: P80667; IntAct: EBI-600779; Score: 0.37
DE  Interaction: P48582; IntAct: EBI-819215; Score: 0.64
DE  Interaction: Q08817; IntAct: EBI-861610; Score: 0.00
DE  Interaction: P36095; IntAct: EBI-7823281; Score: 0.60
DE  Interaction: P08539; IntAct: EBI-974019; Score: 0.27
DE  Interaction: P36108; IntAct: EBI-6399231; Score: 0.53
DE  Interaction: P39929; IntAct: EBI-2213976; Score: 0.83
DE  Interaction: P69771; IntAct: EBI-6331250; Score: 0.00
DE  Interaction: Q03390; IntAct: EBI-6331261; Score: 0.00
DE  Interaction: Q06263; IntAct: EBI-15578482; Score: 0.57
DE  Interaction: Q04272; IntAct: EBI-2213958; Score: 0.76
DE  Interaction: P38111; IntAct: EBI-2612535; Score: 0.35
DE  Interaction: P38110; IntAct: EBI-2613994; Score: 0.35
DE  Interaction: P32447; IntAct: EBI-2881693; Score: 0.00
DE  Interaction: Q12495; IntAct: EBI-2882508; Score: 0.00
DE  Interaction: Q02796; IntAct: EBI-2885698; Score: 0.00
DE  Interaction: Q07979; IntAct: EBI-2886754; Score: 0.00
DE  Interaction: P40340; IntAct: EBI-2889086; Score: 0.00
DE  Interaction: P10591; IntAct: EBI-3677426; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3695875; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3715530; Score: 0.35
DE  Interaction: Q05931; IntAct: EBI-3720038; Score: 0.35
DE  Interaction: Q12483; IntAct: EBI-6530347; Score: 0.62
DE  Interaction: P47142; IntAct: EBI-6530347; Score: 0.55
DE  Interaction: Q06696; IntAct: EBI-6530347; Score: 0.55
DE  Interaction: Q03281; IntAct: EBI-10052667; Score: 0.58
DE  Interaction: Q03707; IntAct: EBI-10052658; Score: 0.37
DE  Interaction: Q03049; IntAct: EBI-16298512; Score: 0.00
GO  GO:0005737;
GO  GO:0009898;
GO  GO:0000815;
GO  GO:0005771;
GO  GO:0005635;
GO  GO:0005886;
GO  GO:0042802;
GO  GO:1904669;
GO  GO:0071454;
GO  GO:1904902;
GO  GO:0070676;
GO  GO:0045324;
GO  GO:0032511;
GO  GO:0015031;
GO  GO:0061709;
GO  GO:0043162;
GO  GO:0006900;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MWSSLFGWTSSNAKNKESPTKAIVRLREHINLLSKKQSHLRTQITNQENEARIFLTKGNKVMAKNALKKKKTIEQLLSKV
SQ  EGTMESMEQQLFSIESANLNLETMRAMQEGAKAMKTIHSGLDIDKVDETMDEIREQVELGDEISDAISRPLITGANEVDE
SQ  DELDEELDMLAQENANQETSKIVNNNVNAAPISENKVSLPSVPSNKIKQSENSVKDGEEEEDEEDEDEKALRELQAEMGL
//
ID  P40548;
PN  HSP70 co-chaperone SNL1;
GN  SNL1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9450961}; Single-pass type II membrane protein {ECO:0000269|PubMed:9450961}. Nucleus membrane {ECO:0000269|PubMed:9450961}; Single-pass type II membrane protein {ECO:0000269|PubMed:9450961}.
DR  UNIPROT: P40548;
DR  UNIPROT: D6VVR3;
DR  Pfam: PF02179;
DR  PROSITE: PS51035;
DE  Function: Stimulator of ATPase activity of molecular chaperones of the HSP70 family (principally of the SSA class). Stimulation is important for HSP70-substrate complex dissociation after folding of newly synthesized or refolded proteins. SNL1 is probably involved in nuclear pore biogenesis and in particular the folding or refolding of misfolded NUP116, GLE2 and NIC96. {ECO:0000269|PubMed:12105220, ECO:0000269|PubMed:9450961}.
DE  Reference Proteome: Yes;
DE  Interaction: P39547; IntAct: EBI-7744731; Score: 0.37
DE  Interaction: P43542; IntAct: EBI-7744291; Score: 0.37
DE  Interaction: P04817; IntAct: EBI-7744327; Score: 0.37
DE  Interaction: P33767; IntAct: EBI-7744363; Score: 0.37
DE  Interaction: P49018; IntAct: EBI-7744397; Score: 0.37
DE  Interaction: P38992; IntAct: EBI-7744433; Score: 0.37
DE  Interaction: P25376; IntAct: EBI-7744479; Score: 0.37
DE  Interaction: P38356; IntAct: EBI-7744544; Score: 0.37
DE  Interaction: P38353; IntAct: EBI-7744633; Score: 0.37
DE  Interaction: P38298; IntAct: EBI-7744699; Score: 0.37
DE  Interaction: P35206; IntAct: EBI-7744715; Score: 0.37
DE  Interaction: Q06247; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P00359; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P11075; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P05754; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P02365; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P05753; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P0CX31; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P23248; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P14127; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P06367; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P05756; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P05317; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P29453; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P05739; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P39741; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P14120; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P05736; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P38706; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P0C2I0; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P38754; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P40212; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P50108; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P38631; IntAct: EBI-803442; Score: 0.35
DE  Interaction: P50105; IntAct: EBI-7775425; Score: 0.40
DE  Interaction: Q02336; IntAct: EBI-8228340; Score: 0.22
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0051087;
GO  GO:0043022;
GO  GO:0006999;
GO  GO:0006457;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSHNAMEHWKSKLSKTSTSTYVLLAVIAVVFLVTIRRPNGSKGKSSKKRASKKNKKGKNQFEKAPVPLTLEEQIDNVSLR
SQ  YGNELEGRSKDLINRFDVEDEKDIYERNYCNEMLLKLLIELDSIDLINVDESLRRPLKEKRKGVIKEIQAMLKSLDSLK
//
ID  Q17QQ3;
PN  Synaptosomal-associated protein 25;
GN  SNAP25;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60879}. Cell membrane {ECO:0000250|UniProtKB:P60881}; Lipid-anchor {ECO:0000250|UniProtKB:P60879}. Synapse, synaptosome {ECO:0000250|UniProtKB:P60879}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60879, ECO:0000250|UniProtKB:P60881}.
DR  UNIPROT: Q17QQ3;
DR  Pfam: PF00835;
DR  PROSITE: PS50192;
DE  Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P60881}.
DE  Reference Proteome: Yes;
DE  Interaction: P61763; IntAct: EBI-7336122; Score: 0.52
DE  Interaction: P32850; IntAct: EBI-7336175; Score: 0.40
DE  Interaction: P48018; IntAct: EBI-7336187; Score: 0.40
GO  GO:0070161;
GO  GO:0031083;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0031234;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0042734;
GO  GO:0097470;
GO  GO:0031201;
GO  GO:0036477;
GO  GO:0008021;
GO  GO:0070032;
GO  GO:0005802;
GO  GO:0005484;
GO  GO:0019905;
GO  GO:0017075;
GO  GO:0005249;
GO  GO:0008306;
GO  GO:0098967;
GO  GO:0006887;
GO  GO:0007626;
GO  GO:0060291;
GO  GO:0099590;
GO  GO:0070201;
GO  GO:0010975;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P60879};
SQ  MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTD
SQ  LGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNL
SQ  RHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
//
ID  P60880;
PN  Synaptosomal-associated protein 25;
GN  SNAP25;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60879}. Cell membrane {ECO:0000250|UniProtKB:P60881}; Lipid-anchor {ECO:0000250|UniProtKB:P60879}. Synapse, synaptosome {ECO:0000250|UniProtKB:P60879}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60879, ECO:0000250|UniProtKB:P60881}.
DR  UNIPROT: P60880;
DR  UNIPROT: B2RAU4;
DR  UNIPROT: D3DW16;
DR  UNIPROT: D3DW17;
DR  UNIPROT: P13795;
DR  UNIPROT: P36974;
DR  UNIPROT: P70557;
DR  UNIPROT: P70558;
DR  UNIPROT: Q53EM2;
DR  UNIPROT: Q5U0B5;
DR  UNIPROT: Q8IXK3;
DR  UNIPROT: Q96FM2;
DR  UNIPROT: Q9BR45;
DR  PDB: 1KIL;
DR  PDB: 1XTG;
DR  PDB: 2N1T;
DR  PDB: 3DDA;
DR  PDB: 3DDB;
DR  PDB: 3RK2;
DR  PDB: 3RK3;
DR  PDB: 3RL0;
DR  PDB: 3ZUR;
DR  PDB: 5W7I;
DR  PDB: 5W7J;
DR  PDB: 6JLH;
DR  Pfam: PF00835;
DR  PROSITE: PS50192;
DR  OMIM: 600322;
DR  OMIM: 616330;
DR  DisGeNET: 6616;
DE  Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells. {ECO:0000250|UniProtKB:P60881}.
DE  Disease: Myasthenic syndrome, congenital, 18 (CMS18) [MIM:616330]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre- synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early- onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS18 is an autosomal dominant presynaptic disorder clinically characterized by early-onset muscle weakness and easy fatigability associated with delayed psychomotor development and ataxia. {ECO:0000269|PubMed:25381298}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-4397510; Score: 0.55
DE  Interaction: P04406; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-26952878; Score: 0.56
DE  Interaction: Q8IUH5; IntAct: EBI-524783; Score: 0.49
DE  Interaction: Q16623; IntAct: EBI-26578093; Score: 0.55
DE  Interaction: O75558; IntAct: EBI-24362633; Score: 0.56
DE  Interaction: Q7Z6L0; IntAct: EBI-735805; Score: 0.00
DE  Interaction: Q15811; IntAct: EBI-8589666; Score: 0.35
DE  Interaction: P63041; IntAct: EBI-1032873; Score: 0.40
DE  Interaction: Q62668; IntAct: EBI-1633551; Score: 0.35
DE  Interaction: A0A8I3MJW7; IntAct: EBI-1633551; Score: 0.35
DE  Interaction: Q9Y3C0; IntAct: EBI-2350431; Score: 0.49
DE  Interaction: P42858; IntAct: EBI-25947049; Score: 0.56
DE  Interaction: Q13360; IntAct: EBI-24670770; Score: 0.56
DE  Interaction: Q9BRT2; IntAct: EBI-24783513; Score: 0.56
DE  Interaction: Q8N4C7; IntAct: EBI-25157949; Score: 0.56
DE  Interaction: Q9UHK0; IntAct: EBI-21549449; Score: 0.35
DE  Interaction: Q16854; IntAct: EBI-21603108; Score: 0.35
DE  Interaction: Q9NVR5; IntAct: EBI-21603625; Score: 0.35
DE  Interaction: Q00496; IntAct: EBI-15556226; Score: 0.44
DE  Interaction: P32851; IntAct: EBI-15937576; Score: 0.74
DE  Interaction: P61765; IntAct: EBI-15623390; Score: 0.40
DE  Interaction: P63045; IntAct: EBI-15623390; Score: 0.40
DE  Interaction: O14810; IntAct: EBI-15937521; Score: 0.73
DE  Interaction: P60880; IntAct: EBI-15937576; Score: 0.66
DE  Interaction: P63027; IntAct: EBI-15937576; Score: 0.76
DE  Interaction: P37840; IntAct: EBI-21013481; Score: 0.50
DE  Interaction: O95183; IntAct: EBI-21267749; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25686340; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
DE  Interaction: P61278; IntAct: EBI-26494704; Score: 0.35
DE  Interaction: Q9NRW1; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: Q13642; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: Q9UL88; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: Q9NP29; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P05026; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P06576; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: Q59EP4; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P46821; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P25705; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P62820; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P60601; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P84077; IntAct: EBI-26578093; Score: 0.51
DE  Interaction: P11142; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P61421; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: Q15904; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: Q9H313; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P36542; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P20336; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P55072; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P17600; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: O95721; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P61764; IntAct: EBI-26578093; Score: 0.53
DE  Interaction: P46459; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P23763; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: Q6PUV4; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: Q86Y82; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: O15400; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P21579; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: P61266; IntAct: EBI-26578093; Score: 0.35
DE  Interaction: Q99719; IntAct: EBI-26578142; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0031234;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0042734;
GO  GO:0097470;
GO  GO:0031201;
GO  GO:0036477;
GO  GO:0035579;
GO  GO:0008021;
GO  GO:0070032;
GO  GO:0070821;
GO  GO:0005802;
GO  GO:0048306;
GO  GO:0008289;
GO  GO:0060090;
GO  GO:0005484;
GO  GO:0019905;
GO  GO:0017075;
GO  GO:0005249;
GO  GO:0008306;
GO  GO:0007268;
GO  GO:0098967;
GO  GO:0006887;
GO  GO:0051179;
GO  GO:0007626;
GO  GO:0060291;
GO  GO:0099590;
GO  GO:0001504;
GO  GO:0050796;
GO  GO:0010975;
GO  GO:0016081;
GO  GO:0016079;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P60879};
SQ  MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTD
SQ  LGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNL
SQ  RHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
//
ID  P60877;
PN  Synaptosomal-associated protein 25;
GN  SNAP25;
OS  9544;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60879}. Cell membrane {ECO:0000250|UniProtKB:P60881}; Lipid-anchor {ECO:0000250|UniProtKB:P60879}. Synapse, synaptosome {ECO:0000250|UniProtKB:P60879}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60879, ECO:0000250|UniProtKB:P60881}.
DR  UNIPROT: P60877;
DR  UNIPROT: P13795;
DR  UNIPROT: P36974;
DR  UNIPROT: P70557;
DR  UNIPROT: P70558;
DR  UNIPROT: Q8IXK3;
DR  UNIPROT: Q96FM2;
DR  UNIPROT: Q9BR45;
DR  Pfam: PF00835;
DR  PROSITE: PS50192;
DE  Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells. {ECO:0000250|UniProtKB:P60881}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0031083;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0031234;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0042734;
GO  GO:0097470;
GO  GO:0031201;
GO  GO:0036477;
GO  GO:0008021;
GO  GO:0070032;
GO  GO:0005802;
GO  GO:0005484;
GO  GO:0019905;
GO  GO:0017075;
GO  GO:0005249;
GO  GO:0008306;
GO  GO:0098967;
GO  GO:0006887;
GO  GO:0007626;
GO  GO:0060291;
GO  GO:0099590;
GO  GO:0070201;
GO  GO:0010975;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P60879};
SQ  MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTD
SQ  LGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNL
SQ  RHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
//
ID  P60879;
PN  Synaptosomal-associated protein 25;
GN  Snap25;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16672379}. Cell membrane {ECO:0000269|PubMed:10413679, ECO:0000269|PubMed:9349529}; Lipid-anchor {ECO:0000269|PubMed:9349529}. Synapse, synaptosome {ECO:0000269|PubMed:2592413}. Photoreceptor inner segment {ECO:0000269|PubMed:26406599}. Note=Membrane association requires palmitoylation (PubMed:9349529). Expressed throughout cytoplasm, concentrating at the perinuclear region (PubMed:16672379). Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60881, ECO:0000269|PubMed:16672379, ECO:0000269|PubMed:9349529}.
DR  UNIPROT: P60879;
DR  UNIPROT: A2AIC2;
DR  UNIPROT: A2AIC3;
DR  UNIPROT: P13795;
DR  UNIPROT: P36974;
DR  UNIPROT: P70557;
DR  UNIPROT: P70558;
DR  UNIPROT: Q8IXK3;
DR  UNIPROT: Q96FM2;
DR  UNIPROT: Q9BR45;
DR  Pfam: PF00835;
DR  PROSITE: PS50192;
DE  Function: t-SNARE involved in the molecular regulation of neurotransmitter release (PubMed:8243676, PubMed:8103915). May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF (PubMed:16672379). Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells (By similarity). {ECO:0000250|UniProtKB:P60881, ECO:0000269|PubMed:16672379, ECO:0000305|PubMed:8103915, ECO:0000305|PubMed:8243676}.
DE  Reference Proteome: Yes;
DE  Interaction: P46097; IntAct: EBI-8499647; Score: 0.40
DE  Interaction: Q9QXY2; IntAct: EBI-1394107; Score: 0.37
DE  Interaction: Q155P7; IntAct: EBI-2211246; Score: 0.74
DE  Interaction: Q68FD5; IntAct: EBI-2216050; Score: 0.35
DE  Interaction: P63101; IntAct: EBI-2255635; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-2307988; Score: 0.35
DE  Interaction: P32851; IntAct: EBI-2462697; Score: 0.79
DE  Interaction: P21707; IntAct: EBI-2462753; Score: 0.59
DE  Interaction: P63044; IntAct: EBI-2462849; Score: 0.94
DE  Interaction: O35526; IntAct: EBI-7780109; Score: 0.69
DE  Interaction: Q9DBG3; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: Q05793; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: P68369; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: P17426; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: Q62277; IntAct: EBI-7780147; Score: 0.53
DE  Interaction: Q7TMM9; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: Q8VDN2; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: Q7TSJ2; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: Q61329; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: P28738; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: P16858; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: Q8K212; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: Q61768; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: P28660; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: P68368; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: P99024; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: P51863; IntAct: EBI-7780147; Score: 0.35
DE  Interaction: Q9EPL2; IntAct: EBI-3869454; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6666752; Score: 0.35
DE  Interaction: Q13561; IntAct: EBI-6857116; Score: 0.35
DE  Interaction: Q9Z266; IntAct: EBI-8753132; Score: 0.40
DE  Interaction: Q03343; IntAct: EBI-8760866; Score: 0.35
DE  Interaction: P42859; IntAct: EBI-9071558; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-9072041; Score: 0.35
DE  Interaction: P48039; IntAct: EBI-11566110; Score: 0.43
DE  Interaction: P49286; IntAct: EBI-11572298; Score: 0.27
DE  Interaction: Q99LI8; IntAct: EBI-15579089; Score: 0.44
DE  Interaction: Q8IPM8; IntAct: EBI-15591677; Score: 0.40
DE  Interaction: Q62717; IntAct: EBI-15804405; Score: 0.50
DE  Interaction: P37840; IntAct: EBI-21013458; Score: 0.35
DE  Interaction: P60904; IntAct: EBI-21013458; Score: 0.35
DE  Interaction: O55042; IntAct: EBI-21013465; Score: 0.35
GO  GO:0015629;
GO  GO:0099026;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0044295;
GO  GO:0031083;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0031234;
GO  GO:0030175;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0043229;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0043209;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0048787;
GO  GO:0042734;
GO  GO:0097470;
GO  GO:0031201;
GO  GO:0036477;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0070044;
GO  GO:0070032;
GO  GO:0070033;
GO  GO:0005802;
GO  GO:0031982;
GO  GO:0008076;
GO  GO:0048306;
GO  GO:0017022;
GO  GO:0019904;
GO  GO:0047485;
GO  GO:0005484;
GO  GO:0000149;
GO  GO:0019905;
GO  GO:0017075;
GO  GO:0044325;
GO  GO:0005249;
GO  GO:0008306;
GO  GO:0048791;
GO  GO:0016197;
GO  GO:0098967;
GO  GO:0006887;
GO  GO:0007626;
GO  GO:0007616;
GO  GO:0060291;
GO  GO:0099590;
GO  GO:0007269;
GO  GO:0046887;
GO  GO:0070201;
GO  GO:0010975;
GO  GO:0030431;
GO  GO:0035493;
GO  GO:0016079;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:9349529};
SQ  MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTD
SQ  LGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNL
SQ  RHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
//
ID  Q5R1X1;
PN  Synaptosomal-associated protein 25;
GN  SNAP25;
OS  9598;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60879}. Cell membrane {ECO:0000250|UniProtKB:P60881}; Lipid-anchor {ECO:0000250|UniProtKB:P60879}. Synapse, synaptosome {ECO:0000250|UniProtKB:P60879}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60879, ECO:0000250|UniProtKB:P60881}.
DR  UNIPROT: Q5R1X1;
DR  Pfam: PF00835;
DR  PROSITE: PS50192;
DE  Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells. {ECO:0000250, ECO:0000250|UniProtKB:P60881}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0031083;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0031234;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0042734;
GO  GO:0097470;
GO  GO:0031201;
GO  GO:0036477;
GO  GO:0008021;
GO  GO:0070032;
GO  GO:0005802;
GO  GO:0005484;
GO  GO:0019905;
GO  GO:0017075;
GO  GO:0005249;
GO  GO:0008306;
GO  GO:0098967;
GO  GO:0006887;
GO  GO:0007626;
GO  GO:0060291;
GO  GO:0099590;
GO  GO:0070201;
GO  GO:0010975;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P60879};
SQ  MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTD
SQ  LGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNL
SQ  RHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
//
ID  Q5NVG5;
PN  Synaptosomal-associated protein 25;
GN  SNAP25;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60879}. Cell membrane {ECO:0000250|UniProtKB:P60881}; Lipid-anchor {ECO:0000250|UniProtKB:P60879}. Synapse, synaptosome {ECO:0000250|UniProtKB:P60879}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60879, ECO:0000250|UniProtKB:P60881}.
DR  UNIPROT: Q5NVG5;
DR  UNIPROT: Q5NVK3;
DR  UNIPROT: Q5R505;
DR  UNIPROT: Q5R690;
DR  UNIPROT: Q5R6U7;
DR  Pfam: PF00835;
DR  PROSITE: PS50192;
DE  Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells. {ECO:0000250, ECO:0000250|UniProtKB:P60881}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0031201;
GO  GO:0045202;
GO  GO:0017075;
GO  GO:0005249;
GO  GO:0006887;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P60879};
SQ  MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNSTD
SQ  LGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNL
SQ  RHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
//
ID  P55820;
PN  Synaptosomal-associated protein 25;
GN  SNAP25;
OS  9986;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60879}. Cell membrane {ECO:0000250|UniProtKB:P60881}; Lipid-anchor {ECO:0000250|UniProtKB:P60879}. Synapse, synaptosome {ECO:0000250|UniProtKB:P60879}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60879, ECO:0000250|UniProtKB:P60881}.
DR  UNIPROT: P55820;
DE  Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells. {ECO:0000250|UniProtKB:P60881}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0031201;
GO  GO:0045202;
GO  GO:0017075;
GO  GO:0005249;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P60879};
SQ  MLQLVEESSKDAGIRXLVMLDEQGEQLERVVDEREQMAISGGFIRIMEKMLGSG
//
ID  P60881;
PN  Synaptosomal-associated protein 25;
GN  Snap25;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60879}. Cell membrane {ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:23341457}; Lipid- anchor {ECO:0000250|UniProtKB:P60879}. Synapse, synaptosome {ECO:0000269|PubMed:1281490}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires palmitoylation (By similarity). Expressed throughout cytoplasm, concentrating at the perinuclear region (By similarity). Colocalizes with KCNB1 at the cell membrane (PubMed:12403834). Colocalizes with PLCL1 at the cell membrane (PubMed:23341457). {ECO:0000250|UniProtKB:P60879, ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:1281490, ECO:0000269|PubMed:23341457}.
DR  UNIPROT: P60881;
DR  UNIPROT: P13795;
DR  UNIPROT: P36974;
DR  UNIPROT: P70557;
DR  UNIPROT: P70558;
DR  UNIPROT: Q8IXK3;
DR  UNIPROT: Q96FM2;
DR  UNIPROT: Q9BR45;
DR  PDB: 1JTH;
DR  PDB: 1N7S;
DR  PDB: 1SFC;
DR  PDB: 1URQ;
DR  PDB: 3HD7;
DR  PDB: 3IPD;
DR  PDB: 3J96;
DR  PDB: 3J97;
DR  PDB: 3J98;
DR  PDB: 3J99;
DR  PDB: 5CCG;
DR  PDB: 5CCH;
DR  PDB: 5CCI;
DR  PDB: 5KJ7;
DR  PDB: 5KJ8;
DR  PDB: 5LOB;
DR  PDB: 5LOW;
DR  PDB: 5W5C;
DR  PDB: 5W5D;
DR  PDB: 6IP1;
DR  PDB: 6MDM;
DR  PDB: 6MDN;
DR  PDB: 6MDO;
DR  PDB: 6MDP;
DR  PDB: 6MTI;
DR  PDB: 6WVW;
DR  Pfam: PF00835;
DR  PROSITE: PS50192;
DE  Function: t-SNARE involved in the molecular regulation of neurotransmitter release (PubMed:8243676, PubMed:8103915). May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells (PubMed:12403834). {ECO:0000269|PubMed:12403834, ECO:0000305|PubMed:8103915, ECO:0000305|PubMed:8243676}.
DE  Reference Proteome: Yes;
DE  Interaction: O95295; IntAct: EBI-8753069; Score: 0.40
DE  Interaction: Q9JJ50; IntAct: EBI-7287330; Score: 0.53
DE  Interaction: Q9WVE9; IntAct: EBI-7031678; Score: 0.60
DE  Interaction: P32851; IntAct: EBI-7031830; Score: 0.97
DE  Interaction: P21575; IntAct: EBI-7031910; Score: 0.40
DE  Interaction: P47709; IntAct: EBI-8545674; Score: 0.52
DE  Interaction: P60881; IntAct: EBI-1027245; Score: 0.81
DE  Interaction: P63045; IntAct: EBI-1027245; Score: 0.95
DE  Interaction: Q9WU70; IntAct: EBI-1039933; Score: 0.40
DE  Interaction: Q9QXY2; IntAct: EBI-1394117; Score: 0.54
DE  Interaction: Q63666; IntAct: EBI-7573643; Score: 0.46
DE  Interaction: Q63635; IntAct: EBI-7573728; Score: 0.40
DE  Interaction: G3V7P1; IntAct: EBI-7573698; Score: 0.40
DE  Interaction: Q9WUF4; IntAct: EBI-7573895; Score: 0.35
DE  Interaction: Q4KMA2; IntAct: EBI-2640427; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6665350; Score: 0.35
DE  Interaction: Q08850; IntAct: EBI-9822143; Score: 0.40
DE  Interaction: Q9BV40; IntAct: EBI-9822143; Score: 0.40
DE  Interaction: Q15836; IntAct: EBI-9822137; Score: 0.40
DE  Interaction: P63027; IntAct: EBI-9822200; Score: 0.40
DE  Interaction: A0A142I9X8; IntAct: EBI-11701393; Score: 0.35
DE  Interaction: Q08849; IntAct: EBI-15578272; Score: 0.61
DE  Interaction: O16000; IntAct: EBI-15595291; Score: 0.40
DE  Interaction: P63041; IntAct: EBI-15657265; Score: 0.35
DE  Interaction: P84087; IntAct: EBI-15743043; Score: 0.35
DE  Interaction: P21707; IntAct: EBI-15837855; Score: 0.44
DE  Interaction: Q9JHW5; IntAct: EBI-16138941; Score: 0.50
DE  Interaction: P18708; IntAct: EBI-16139061; Score: 0.49
DE  Interaction: P54921; IntAct: EBI-16139110; Score: 0.40
DE  Interaction: P19332; IntAct: EBI-26374040; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26438079; Score: 0.35
GO  GO:0015629;
GO  GO:0099026;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0044295;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0031234;
GO  GO:0030175;
GO  GO:0098978;
GO  GO:0030426;
GO  GO:0043229;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0001917;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0048787;
GO  GO:0042734;
GO  GO:0097470;
GO  GO:0031201;
GO  GO:0036477;
GO  GO:0045202;
GO  GO:0008021;
GO  GO:0070044;
GO  GO:0070032;
GO  GO:0070033;
GO  GO:0043195;
GO  GO:0005802;
GO  GO:0008076;
GO  GO:0048306;
GO  GO:0017022;
GO  GO:0019904;
GO  GO:0047485;
GO  GO:0005484;
GO  GO:0000149;
GO  GO:0019905;
GO  GO:0017075;
GO  GO:0044325;
GO  GO:0005249;
GO  GO:0008306;
GO  GO:0007409;
GO  GO:0048791;
GO  GO:0016197;
GO  GO:0098967;
GO  GO:0006887;
GO  GO:0030252;
GO  GO:0007626;
GO  GO:0007616;
GO  GO:0060291;
GO  GO:0030182;
GO  GO:0099590;
GO  GO:0007269;
GO  GO:0046887;
GO  GO:0032024;
GO  GO:0070201;
GO  GO:0010975;
GO  GO:0051963;
GO  GO:0030431;
GO  GO:0035493;
GO  GO:0016079;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P60879};
SQ  MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTD
SQ  LGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNL
SQ  RHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
//
ID  A6QP11;
PN  Synaptosomal-associated protein 47;
GN  SNAP47;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Appears to be exclusively membrane-bound. {ECO:0000250}.
DR  UNIPROT: A6QP11;
DR  PROSITE: PS50192;
DE  Function: May play a role in intracellular membrane fusion. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016020;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGDTCVQTWPCSYYLELEKRWVPGRLSLTSLSLKFMTDKTRETLVSFPLSSIIEIKKEASHFIFSSITILERDHSKHWF
SQ  SSLQPSRNAVFSVIEHFWRELLLSESGAAAEAASSSMTKGKELTCLMACTQKRLEDTARVLHHQGEQLDGISRGLDKMES
SQ  DLDVADRLLTELESPSWWPFSSKLWKTPSETKPKWDASMADSKAFGKEGIVIQVPAVISQRTESHVKPGRLTVLVSGLEI
SQ  YNSDSLLMHRFEREDVDDIKVHTPYEISICQRFIGKPDISYRLISAKMPEVIPILEVQFSKKIELLEVAMMLGSTRTSSL
SQ  AEKGYSVWHAASGLMDQATHCEPSSGSQEGRPLQLQTSEPVISEEDTQELGQILRKLKGLALDTETELERQDEALDGITE
SQ  AVDRATLTIDKHNRRMKKLT
//
ID  Q5SQN1;
PN  Synaptosomal-associated protein 47;
GN  SNAP47;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Appears to be exclusively membrane-bound. {ECO:0000250}.
DR  UNIPROT: Q5SQN1;
DR  UNIPROT: B6EDE0;
DR  UNIPROT: Q5HYB5;
DR  UNIPROT: Q5TBZ3;
DR  UNIPROT: Q8N558;
DR  UNIPROT: Q8TB31;
DR  UNIPROT: Q8TCW8;
DR  UNIPROT: Q8WV46;
DR  UNIPROT: Q96CQ3;
DR  UNIPROT: Q96FE1;
DR  UNIPROT: Q96I66;
DR  UNIPROT: Q96NU3;
DR  UNIPROT: Q9BT10;
DR  UNIPROT: Q9BVB2;
DR  PROSITE: PS50192;
DR  OMIM: 619659;
DR  DisGeNET: 116841;
DE  Function: Plays a role in intracellular membrane fusion. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P0C6X7; IntAct: EBI-25488935; Score: 0.51
DE  Interaction: P51809; IntAct: EBI-11293774; Score: 0.52
DE  Interaction: Q9BV40; IntAct: EBI-11293795; Score: 0.40
DE  Interaction: O75379; IntAct: EBI-11293806; Score: 0.40
DE  Interaction: Q15836; IntAct: EBI-11293962; Score: 0.40
DE  Interaction: Q9Y6D6; IntAct: EBI-11294278; Score: 0.37
DE  Interaction: Q92845; IntAct: EBI-11294286; Score: 0.37
DE  Interaction: Q9UPN3; IntAct: EBI-11294304; Score: 0.37
DE  Interaction: Q13190; IntAct: EBI-11302354; Score: 0.40
DE  Interaction: Q86Y82; IntAct: EBI-11302363; Score: 0.56
DE  Interaction: P32851; IntAct: EBI-11302387; Score: 0.56
DE  Interaction: P43360; IntAct: EBI-10244846; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-10244873; Score: 0.56
DE  Interaction: Q12846; IntAct: EBI-10244885; Score: 0.56
DE  Interaction: Q6P597; IntAct: EBI-10244895; Score: 0.56
DE  Interaction: Q8IYX8; IntAct: EBI-10244905; Score: 0.56
DE  Interaction: Q8IZU0; IntAct: EBI-10244917; Score: 0.56
DE  Interaction: Q969F0; IntAct: EBI-10244927; Score: 0.56
DE  Interaction: Q96R06; IntAct: EBI-10244937; Score: 0.56
DE  Interaction: Q9UJV3; IntAct: EBI-10244947; Score: 0.56
DE  Interaction: P28574; IntAct: EBI-11108899; Score: 0.35
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q8N137; IntAct: EBI-11392655; Score: 0.27
DE  Interaction: P61266; IntAct: EBI-24295375; Score: 0.56
DE  Interaction: Q16623; IntAct: EBI-24355819; Score: 0.56
DE  Interaction: Q8IWR1; IntAct: EBI-25264418; Score: 0.56
DE  Interaction: Q9HCJ2; IntAct: EBI-23745786; Score: 0.56
DE  Interaction: Q96K19; IntAct: EBI-23761080; Score: 0.56
DE  Interaction: Q9NR31; IntAct: EBI-24713075; Score: 0.56
DE  Interaction: Q9Y624; IntAct: EBI-24795529; Score: 0.56
DE  Interaction: Q8N6L0; IntAct: EBI-24469364; Score: 0.56
DE  Interaction: P15151; IntAct: EBI-24658033; Score: 0.56
DE  Interaction: P41181; IntAct: EBI-24774511; Score: 0.56
DE  Interaction: Q9H400; IntAct: EBI-24798784; Score: 0.56
DE  Interaction: O14880; IntAct: EBI-24809743; Score: 0.56
DE  Interaction: P55056; IntAct: EBI-25232479; Score: 0.56
DE  Interaction: Q9UJY5; IntAct: EBI-11916394; Score: 0.00
DE  Interaction: Q9NTX5; IntAct: EBI-11916385; Score: 0.00
DE  Interaction: O75396; IntAct: EBI-21524354; Score: 0.35
DE  Interaction: Q9P2W9; IntAct: EBI-21525162; Score: 0.35
DE  Interaction: O15400; IntAct: EBI-21528726; Score: 0.35
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: O95183; IntAct: EBI-21267749; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568044; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: Q5W0V3; IntAct: EBI-34574999; Score: 0.27
GO  GO:0012505;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0098793;
GO  GO:0031201;
GO  GO:0005484;
GO  GO:0019905;
GO  GO:0006887;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRAARRGLHCAGAERPRRRGRLWDSSGVPQRQKRPGPWRTQTQEQMSRDVCIHTWPCTYYLEPKRRWVTGQLSLTSLSLR
SQ  FMTDSTGEILVSFPLSSIVEIKKEASHFIFSSITILEKGHAKHWFSSLRPSRNVVFSIIEHFWRELLLSQPGAVADASVP
SQ  RTRGEELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTELESPAWWPFSSKLWKTPPETKPRED
SQ  VSMTSCEPFGKEGILIKIPAVISHRTESHVKPGRLTVLVSGLEIHDSSSLLMHRFEREDVDDIKVHSPYEISIRQRFIGK
SQ  PDMAYRLISAKMPEVIPILEVQFSKKMELLEDALVLRSARTSSPAEKSCSVWHAASGLMGRTLHREPPAGDQEGTALHLQ
SQ  TSLPALSEADTQELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKRLT
//
ID  Q8R570;
PN  Synaptosomal-associated protein 47;
GN  Snap47;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000269|PubMed:16621800}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16621800}. Note=Appears to be exclusively membrane- bound. In primary neurons, widely distributed in both cell bodies and neuronal processes.
DR  UNIPROT: Q8R570;
DR  UNIPROT: Q3UNK4;
DR  UNIPROT: Q8BK87;
DR  PROSITE: PS50192;
DE  Function: May play a role in intracellular membrane fusion. {ECO:0000269|PubMed:16621800}.
DE  Reference Proteome: Yes;
DE  Interaction: P48039; IntAct: EBI-11576452; Score: 0.35
GO  GO:0032279;
GO  GO:0031083;
GO  GO:0030425;
GO  GO:0098978;
GO  GO:0098686;
GO  GO:0016020;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0031201;
GO  GO:0030672;
GO  GO:0005484;
GO  GO:0019905;
GO  GO:0098967;
GO  GO:0006887;
GO  GO:0060291;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
GO  GO:0099003;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSDMRVHSWSCSYYLDLEKQWVSGKLTLTPHSLKFIVEKTEEVLVGLPLSSIIEIRKESSLFIFGAITVLEKGQTKHWF
SQ  SSLQPSRNVVFNVIEHFWRELLLSQPGTAANIPSHVTRGQELIGLMANSQKRMEDTAKDLQQQSEQLDSVLKGLEKMESD
SQ  LDVADRLLTELETPSWWPFGSKFWKMPAEENLKEGVSSTCEPFGKEGVVITVPAIISERAESHSKLGKLTVLVSALEIYD
SQ  SCSLLLHRFEKEDVDDIKVHSPYEVSIRQRFIGKPDVAYQLISAKMPEVIPILEVQFSSKIELLEDALVLRNKVFASSAE
SQ  RHAASRPKGCTPHRELPTGGQEGEQLQLQKNLPLFSEGEAQELTQILSKMKGLALDTEAELERQDAALDGITVAVDRATL
SQ  NVDKQNRRMRKLM
//
ID  Q6P6S0;
PN  Synaptosomal-associated protein 47;
GN  Snap47;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Endomembrane system {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Appears to be exclusively membrane-bound. {ECO:0000250}.
DR  UNIPROT: Q6P6S0;
DR  PROSITE: PS50192;
DE  Function: May play a role in intracellular membrane fusion. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0032279;
GO  GO:0030425;
GO  GO:0098978;
GO  GO:0098686;
GO  GO:0016020;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0031201;
GO  GO:0030672;
GO  GO:0005484;
GO  GO:0019905;
GO  GO:0098967;
GO  GO:0006887;
GO  GO:0060291;
GO  GO:0031629;
GO  GO:0016082;
GO  GO:0006906;
GO  GO:0099003;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSDVRVHTWPCSYYLDLEKQWLPGKLTLTPRSLKFSVDKAEEVLVGLPLSSITEIRKETSLFIFSAITVLEKGQAKHWF
SQ  SSLRPSRNVVFNIIEHFWRELLLSQPGTAANPTSPMTRGQELMGLMASSQRRMEDTAKVLHHQGEQLDSVMRGLEKMESD
SQ  LDVADRLLTELETPSWWPFSAKFWKTPVEAKPRDSVSVAPCEPFGKEGVVIRVPAVVSQRTESHSKPGKLTVLVSGLEIH
SQ  DSSSLLLHRFEKEDVDDIKVHSPYEVSIRQRFIGKPDVAYRLISAKMPEVIPILEVQFSKKIELLEDALVLRSRGRASPA
SQ  EGGCSIRHAASRLMGCTTHQELPTGGQEGQQSQLQKDWPLLSEGEAQELTQILSKLKGLALDTEAELERQDAALDGITVA
SQ  VDRATLTVDKHNRRMRKLL
//
ID  Q6NUT7;
PN  Sortilin;
GN  sort1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Endosome membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Nucleus membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Cell membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}; Extracellular side {ECO:0000250|UniProtKB:Q99523}. Lysosome membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}.
DR  UNIPROT: Q6NUT7;
DR  Pfam: PF15902;
DR  Pfam: PF15901;
DE  Function: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal proteins bind specifically to the receptor in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. Also required for protein transport from the Golgi apparatus to the endosomes. May also mediate transport from the endoplasmic reticulum to the Golgi. {ECO:0000250|UniProtKB:Q99523}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0032580;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0006897;
GO  GO:0006895;
GO  GO:0006892;
GO  GO:0016050;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSTVLCCVLVLLISVALCMDFEERPSSSWRSEQTMFLKSHKSRNLLSLRDLQQPDHGKMKRSEESAQNQCESLHGYQSTL
SQ  QNDTHTHNFNDLSGSVSLAWVGDGTGVLLVLTTFQVPLFIMRFGQSKLYRSEDYGKTFQDITDLINNTFIQTEFGIAIGP
SQ  DNSGKVILTGDLAEGKVTKIFRSVDFGKSFVTSELPFHPLMQITYNPKDSNILMVYSINYDLWLSKDFGANWKKIHESVC
SQ  LVKWGIDDTIFLTTNPNGSCSDRGTLELRKSLDYGKTFKTIGNRIYSFGLGGRFVFASIMTDSGSTRMIHVSVDQGETWD
SQ  MAQLPTVGHEQFYSILAANNDMVFMHVDEPGDSGIGTIYISDDRGIVFSKSLERHLYTTTGGDTDFTNITSLRGVYITSV
SQ  LAEDGSVQTVITFNQGGEWRPLMKPWNGVCDSTAKHPSECSLHIHASYSISMKLNVPMQPLSETNAVGLVLAHGSVGGAV
SQ  SVLSPDVYVSDDGGYTWFQALKGPHHYAILDSGGLLVAVEHNPTHPISQIKFSTDEGQCWHAHNFTDDPIYFTGLASEPG
SQ  ARSMNVSLWGYRDTILNQYWVSVTVDFRQLLSRDCQENDYIQWLAHSSDINSPTDGCVLGYKERFLRLRRDSVCWNGRDY
SQ  KVTKEPTTCPCTLTDFHDFGFYHEENSSVCVEQPDLIGHSLEFCLHGRKEQLQTSGYRKIPGDHCEEGITPERKEIDLSK
SQ  KCVSNLLRTEQLTKEHSFNSAPIIAVVIIVLLISAVAGVIFIKKYVCGGRFLVHRYSVLQQHAEANGIDGLDDLDTLEGG
SQ  KTHYHDDSDEDLLE
//
ID  Q99523;
PN  Sortilin;
GN  SORT1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:16787399, ECO:0000269|PubMed:18817523}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:18817523}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single- pass type I membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane; Single-pass type I membrane protein; Extracellular side. Lysosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. May also be found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes may be enhanced by insulin.
DR  UNIPROT: Q99523;
DR  UNIPROT: B4DWI3;
DR  UNIPROT: C0JYZ0;
DR  UNIPROT: Q8IZ49;
DR  PDB: 3F6K;
DR  PDB: 3G2U;
DR  PDB: 3G2V;
DR  PDB: 4MSL;
DR  PDB: 4N7E;
DR  PDB: 4PO7;
DR  PDB: 5MRH;
DR  PDB: 5MRI;
DR  PDB: 6EHO;
DR  PDB: 6X3L;
DR  PDB: 6X48;
DR  PDB: 6X4H;
DR  Pfam: PF15902;
DR  Pfam: PF15901;
DR  OMIM: 602458;
DR  OMIM: 613589;
DR  DisGeNET: 6272;
DE  Function: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal proteins bind specifically to the receptor in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex (PubMed:16787399). The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi. {ECO:0000269|PubMed:10085125, ECO:0000269|PubMed:11331584, ECO:0000269|PubMed:11390366, ECO:0000269|PubMed:12209882, ECO:0000269|PubMed:12598608, ECO:0000269|PubMed:14657016, ECO:0000269|PubMed:14985763, ECO:0000269|PubMed:15313463, ECO:0000269|PubMed:15930396, ECO:0000269|PubMed:15987945, ECO:0000269|PubMed:16787399, ECO:0000269|PubMed:18817523}.
DE  Disease: Note=A common polymorphism located in a non-coding region between CELSR2 and PSRC1 alters a CEBP transcription factor binding site and is responsible for changes in hepatic expression of SORT1. Altered SORT1 expression in liver affects low density lipoprotein cholesterol levels in plasma and is associated with susceptibility to myocardial infarction. {ECO:0000269|PubMed:20686566}.
DE  Reference Proteome: Yes;
DE  Interaction: P03246; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: Q16620; IntAct: EBI-9828457; Score: 0.44
DE  Interaction: Q63604; IntAct: EBI-9663445; Score: 0.43
DE  Interaction: Q6PIV2; IntAct: EBI-11321774; Score: 0.35
DE  Interaction: Q86WG5; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8NC56; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q92900; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9UJY4; IntAct: EBI-7835669; Score: 0.70
DE  Interaction: Q9UJY5; IntAct: EBI-7866420; Score: 0.67
DE  Interaction: P24941; IntAct: EBI-11154667; Score: 0.56
DE  Interaction: P28799; IntAct: EBI-8759908; Score: 0.61
DE  Interaction: P11151; IntAct: EBI-8794584; Score: 0.66
DE  Interaction: P30533; IntAct: EBI-8794629; Score: 0.81
DE  Interaction: P06858; IntAct: EBI-8795527; Score: 0.44
DE  Interaction: P01138; IntAct: EBI-9253924; Score: 0.68
DE  Interaction: P30990; IntAct: EBI-25298265; Score: 0.70
DE  Interaction: P08138; IntAct: EBI-9346945; Score: 0.40
DE  Interaction: Q8IVD9; IntAct: EBI-9395191; Score: 0.35
DE  Interaction: P54256; IntAct: EBI-9663445; Score: 0.43
DE  Interaction: Q16288; IntAct: EBI-9827681; Score: 0.54
DE  Interaction: P04629; IntAct: EBI-9827696; Score: 0.46
DE  Interaction: Q14653; IntAct: EBI-11321946; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: Q2MG95; IntAct: EBI-11733653; Score: 0.35
DE  Interaction: Q8IXK0; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q7Z7F7; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: O43543; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8IZY2; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q6KCM7; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8N8A6; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: O95678; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q6PKC3; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: J3KP15; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8IXQ6; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q86YS7; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9H6R4; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: G5E9A6; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9P0T7; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: O43504; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: H3BS42; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q96AY2; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: O43674; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9UHR4; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9H2D6; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9BXF6; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: H3BNT4; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P78368; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q6T4R5; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9Y2H6; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8IWU2; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q86WP2; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9Y6X9; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9BZF9; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q7Z7K6; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P12882; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8N8R5; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: G5E9S8; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P98170; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: O94782; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9H792; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q92934; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P06493; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9NYU1; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: E9PRI1; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: O00308; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9NP74; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q16222; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9NW13; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: O15020; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8WW22; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q15646; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8TED0; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q6PCT2; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q13867; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: G3V5I9; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P00738; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P46087; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9Y2L1; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8TDN6; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: O60287; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: H0YAJ5; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q96MF7; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P67809; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9Y4E8; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P53621; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: A7KAX9; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q96A35; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9NXA8; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8IY21; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: G4U4J3; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P42680; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q08378; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8NCE0; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P07949; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q6IN84; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q13428; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P51659; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: C9J6P4; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q659A1; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q6L8Q7; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q14146; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q14232; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P00966; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: J3KNB8; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: A1X283; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9Y2U9; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P51153; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q53SF7; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q96CS3; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q01970; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9UPY3; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q92733; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8IYD8; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P13533; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q6UVK1; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9UHL9; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P42356; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q5JRA6; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q71F56; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P54577; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8TE77; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8ND56; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q8NFA0; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9Y490; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9UMF0; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q96P70; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q7Z2E3; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9NQY0; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q9NUQ7; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q13488; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q96A73; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: P43307; IntAct: EBI-11154667; Score: 0.35
DE  Interaction: Q92520; IntAct: EBI-22754816; Score: 0.56
DE  Interaction: O95183; IntAct: EBI-22756180; Score: 0.56
DE  Interaction: Q6PL45; IntAct: EBI-25279435; Score: 0.56
DE  Interaction: Q8TBE1; IntAct: EBI-24650011; Score: 0.56
DE  Interaction: P02787; IntAct: EBI-24758574; Score: 0.56
DE  Interaction: P23560; IntAct: EBI-24760183; Score: 0.56
DE  Interaction: Q96K78; IntAct: EBI-25271609; Score: 0.56
DE  Interaction: Q20MH8; IntAct: EBI-12586258; Score: 0.35
DE  Interaction: Q99523; IntAct: EBI-25396647; Score: 0.68
DE  Interaction: Q15077; IntAct: EBI-21272198; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21183114; Score: 0.54
DE  Interaction: P26441; IntAct: EBI-25298162; Score: 0.57
DE  Interaction: Q9UBD9; IntAct: EBI-25298249; Score: 0.40
DE  Interaction: O75462; IntAct: EBI-25298249; Score: 0.40
DE  Interaction: P83714; IntAct: EBI-25298290; Score: 0.54
DE  Interaction: Q16619; IntAct: EBI-25298330; Score: 0.44
DE  Interaction: P15018; IntAct: EBI-25298341; Score: 0.44
DE  Interaction: P13725; IntAct: EBI-25298353; Score: 0.44
DE  Interaction: P42702; IntAct: EBI-25298362; Score: 0.51
DE  Interaction: P05231; IntAct: EBI-25396627; Score: 0.57
DE  Interaction: P01580; IntAct: EBI-25396634; Score: 0.44
DE  Interaction: Q9JLC4; IntAct: EBI-25300430; Score: 0.54
DE  Interaction: Q8WY21; IntAct: EBI-25300575; Score: 0.54
DE  Interaction: P06280; IntAct: EBI-25396912; Score: 0.59
DE  Interaction: P01266; IntAct: EBI-25406637; Score: 0.54
DE  Interaction: P06882; IntAct: EBI-25406672; Score: 0.54
DE  Interaction: P20068; IntAct: EBI-25406716; Score: 0.40
DE  Interaction: P01267; IntAct: EBI-25408014; Score: 0.40
DE  Interaction: O96028; IntAct: EBI-25486814; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25687199; Score: 0.35
DE  Interaction: Q7TFA1; IntAct: EBI-25688644; Score: 0.35
DE  Interaction: Q9UBQ0; IntAct: EBI-25890950; Score: 0.56
DE  Interaction: Q13363; IntAct: EBI-27045766; Score: 0.35
DE  Interaction: Q8IV63; IntAct: EBI-28942353; Score: 0.35
DE  Interaction: Q96KG9; IntAct: EBI-28944481; Score: 0.35
DE  Interaction: Q92932; IntAct: EBI-27115082; Score: 0.35
GO  GO:0009986;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005769;
GO  GO:0005789;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0032580;
GO  GO:0016021;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030140;
GO  GO:0019899;
GO  GO:0048406;
GO  GO:0010465;
GO  GO:0030379;
GO  GO:1905394;
GO  GO:0006897;
GO  GO:0008333;
GO  GO:0032509;
GO  GO:0008625;
GO  GO:0007186;
GO  GO:0046323;
GO  GO:0006895;
GO  GO:0090160;
GO  GO:0014902;
GO  GO:0045599;
GO  GO:0051005;
GO  GO:0007218;
GO  GO:0048011;
GO  GO:0001503;
GO  GO:0048227;
GO  GO:0006892;
GO  GO:0006622;
GO  GO:0010468;
GO  GO:0032868;
GO  GO:0016050;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MERPWGAADGLSRWPHGLGLLLLLQLLPPSTLSQDRLDAPPPPAAPLPRWSGPIGVSWGLRAAAAGGAFPRGGRWRRSAP
SQ  GEDEECGRVRDFVAKLANNTHQHVFDDLRGSVSLSWVGDSTGVILVLTTFHVPLVIMTFGQSKLYRSEDYGKNFKDITDL
SQ  INNTFIRTEFGMAIGPENSGKVVLTAEVSGGSRGGRIFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLW
SQ  VSKNFGGKWEEIHKAVCLAKWGSDNTIFFTTYANGSCKADLGALELWRTSDLGKSFKTIGVKIYSFGLGGRFLFASVMAD
SQ  KDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGG
SQ  ETDFTNVTSLRGVYITSVLSEDNSIQTMITFDQGGRWTHLRKPENSECDATAKNKNECSLHIHASYSISQKLNVPMAPLS
SQ  EPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWTKMLEGPHYYTILDSGGIIVAIEHSSRPINVIKFSTDEGQCWQTY
SQ  TFTRDPIYFTGLASEPGARSMNISIWGFTESFLTSQWVSYTIDFKDILERNCEEKDYTIWLAHSTDPEDYEDGCILGYKE
SQ  QFLRLRKSSVCQNGRDYVVTKQPSICLCSLEDFLCDFGYYRPENDSKCVEQPELKGHDLEFCLYGREEHLTTNGYRKIPG
SQ  DKCQGGVNPVREVKDLKKKCTSNFLSPEKQNSKSNSVPIILAIVGLMLVTVVAGVLIVKKYVCGGRFLVHRYSVLQQHAE
SQ  ANGVDGVDALDTASHTNKSGYHDDSDEDLLE
//
ID  Q6PHU5;
PN  Sortilin;
GN  Sort1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Endosome membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Nucleus membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Cell membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}; Extracellular side {ECO:0000250|UniProtKB:Q99523}. Lysosome membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Note=Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. May also be found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes may be enhanced by insulin. {ECO:0000250|UniProtKB:Q99523}.
DR  UNIPROT: Q6PHU5;
DR  UNIPROT: A2AEE8;
DR  UNIPROT: Q3UHE2;
DR  UNIPROT: Q8K043;
DR  UNIPROT: Q9QXW6;
DR  PDB: 5NMR;
DR  PDB: 5NMT;
DR  PDB: 5NNI;
DR  PDB: 5NNJ;
DR  PDB: 5ZNN;
DR  Pfam: PF15902;
DR  Pfam: PF15901;
DE  Function: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal proteins bind specifically to the receptor in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi. {ECO:0000269|PubMed:10594043, ECO:0000269|PubMed:15236332, ECO:0000269|PubMed:15236333, ECO:0000269|PubMed:15372498, ECO:0000269|PubMed:15992544, ECO:0000269|PubMed:19407813, ECO:0000269|PubMed:21102451}.
DE  Reference Proteome: Yes;
DE  Interaction: P15209; IntAct: EBI-9663469; Score: 0.64
DE  Interaction: Q9Z0W1; IntAct: EBI-6985714; Score: 0.58
DE  Interaction: Q8CJ26; IntAct: EBI-6985761; Score: 0.54
DE  Interaction: P11152; IntAct: EBI-8801159; Score: 0.40
DE  Interaction: O35668; IntAct: EBI-9663576; Score: 0.27
DE  Interaction: Q8C0E2; IntAct: EBI-9827151; Score: 0.35
DE  Interaction: P01139; IntAct: EBI-9827151; Score: 0.35
DE  Interaction: Q9EQH3; IntAct: EBI-9827151; Score: 0.56
DE  Interaction: Q3UFB7; IntAct: EBI-9828117; Score: 0.27
DE  Interaction: P97438; IntAct: EBI-15850443; Score: 0.40
DE  Interaction: P12023; IntAct: EBI-21183104; Score: 0.52
DE  Interaction: O08710; IntAct: EBI-25408041; Score: 0.40
GO  GO:0009986;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005769;
GO  GO:0005789;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0032580;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0043025;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030140;
GO  GO:0019899;
GO  GO:0048406;
GO  GO:0010465;
GO  GO:0030379;
GO  GO:1905394;
GO  GO:0006897;
GO  GO:0008333;
GO  GO:0032509;
GO  GO:0008625;
GO  GO:0007186;
GO  GO:0046323;
GO  GO:0006895;
GO  GO:0090160;
GO  GO:0014902;
GO  GO:0045599;
GO  GO:0051005;
GO  GO:0007218;
GO  GO:0048011;
GO  GO:0001503;
GO  GO:0048227;
GO  GO:1904037;
GO  GO:0006892;
GO  GO:0006622;
GO  GO:0010468;
GO  GO:0032868;
GO  GO:0016050;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MERPRGAADGLLRWPLGLLLLLQLLPPAAVGQDRLDAPPPPAPPLLRWAGPVGVSWGLRAAAPGGPVPRAGRWRRGAPAE
SQ  DQDCGRLPDFIAKLTNNTHQHVFDDLSGSVSLSWVGDSTGVILVLTTFQVPLVIVSFGQSKLYRSEDYGKNFKDITNLIN
SQ  NTFIRTEFGMAIGPENSGKVILTAEVSGGSRGGRVFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLWVS
SQ  KNFGEKWEEIHKAVCLAKWGPNNIIFFTTHVNGSCKADLGALELWRTSDLGKTFKTIGVKIYSFGLGGRFLFASVMADKD
SQ  TTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANEDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGET
SQ  DFTNVTSLRGVYITSTLSEDNSIQSMITFDQGGRWEHLRKPENSKCDATAKNKNECSLHIHASYSISQKLNVPMAPLSEP
SQ  NAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWAKMLEGPHYYTILDSGGIIVAIEHSNRPINVIKFSTDEGQCWQSYVF
SQ  TQEPIYFTGLASEPGARSMNISIWGFTESFITRQWVSYTVDFKDILERNCEEDDYTTWLAHSTDPGDYKDGCILGYKEQF
SQ  LRLRKSSVCQNGRDYVVAKQPSVCPCSLEDFLCDFGYFRPENASECVEQPELKGHELEFCLYGKEEHLTTNGYRKIPGDK
SQ  CQGGMNPAREVKDLKKKCTSNFLNPTKQNSKSNSVPIILAIVGLMLVTVVAGVLIVKKYVCGGRFLVHRYSVLQQHAEAD
SQ  GVEALDSTSHAKSGYHDDSDEDLLE
//
ID  O54861;
PN  Sortilin;
GN  Sort1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Endosome membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Nucleus membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Cell membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}; Extracellular side {ECO:0000250|UniProtKB:Q99523}. Lysosome membrane {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99523}. Note=Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. May also be found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes may be enhanced by insulin. {ECO:0000250|UniProtKB:Q99523}.
DR  UNIPROT: O54861;
DR  UNIPROT: O35389;
DR  Pfam: PF15902;
DR  Pfam: PF15901;
DE  Function: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal proteins bind specifically to the receptor in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin (By similarity). May also mediate transport from the endoplasmic reticulum to the Golgi (PubMed:12771154). {ECO:0000250|UniProtKB:Q99523, ECO:0000269|PubMed:12771154}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q8K5A9; IntAct: EBI-6985580; Score: 0.35
DE  Interaction: P07174; IntAct: EBI-6985580; Score: 0.35
DE  Interaction: P01266; IntAct: EBI-25408099; Score: 0.37
GO  GO:0009986;
GO  GO:0005905;
GO  GO:0030136;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0005769;
GO  GO:0005789;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0032580;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005765;
GO  GO:0005764;
GO  GO:0043025;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030140;
GO  GO:0019899;
GO  GO:0016492;
GO  GO:0048406;
GO  GO:0010465;
GO  GO:0030379;
GO  GO:1905394;
GO  GO:0006897;
GO  GO:0008333;
GO  GO:0032509;
GO  GO:0008625;
GO  GO:0007186;
GO  GO:0046323;
GO  GO:0006895;
GO  GO:0090160;
GO  GO:0006886;
GO  GO:0014902;
GO  GO:0045599;
GO  GO:0051005;
GO  GO:0007218;
GO  GO:0048011;
GO  GO:0001503;
GO  GO:0048227;
GO  GO:1904037;
GO  GO:0006892;
GO  GO:0006622;
GO  GO:0010468;
GO  GO:0032868;
GO  GO:0016050;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MERPRGAADGLLRWPLGLLLLLQLLPPAAVGQDRLDAPPPPAPPLLRWAGPVGVSWGLRAAAPGGPVPRAGRWRRGAPAE
SQ  DQDCGRLPDFIAKLTNNTHQHVFDDLSGSVSLSWVGDSTGVILVLTTFQVPLVIVSFGQSKLYRSEDYGKNFKDITNLIN
SQ  NTFIRTEFGMAIGPENSGKVILTAEVSGGSRGGRVFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLWVS
SQ  KNFGEKWEEIHKAVCLAKWGPNNIIFFTTHVNGSCKADLGALELWRTSDLGKTFKTIGVKIYSFGLGGRFLFASVMADKD
SQ  TTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGET
SQ  DFTNVTSLRGVYITSTLSEDNSIQSMITFDQGGRWEHLQKPENSKCDATAKNKNECSLHIHASYSISQKLNVPMAPLSEP
SQ  NAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWAKMLEGPHYYTILDSGGIIVAIEHSNRPINVIKFSTDEGQCWQSYVF
SQ  SQEPVYFTGLASEPGARSMNISIWGFTESFLTRQWVSYTIDFKDILERNCEENDYTTWLAHSTDPGDYKDGCILGYKEQF
SQ  LRLRKSSVCQNGRDYVVAKQPSICPCSLEDFLCDFGYFRPENASECVEQPELKGHELEFCLYGKEEHLTTNGYRKIPGDR
SQ  CQGGMNPAREVKDLKKKCTSNFLNPKKQNSKSSSVPIILAIVGLMLVTVVAGVLIVKKYVCGGRFLVHRYSVLQQHAEAD
SQ  GVEALDTASHAKSGYHDDSDEDLLE
//
ID  P53148;
PN  Spindle pole body component SPC105;
GN  SPC105;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Chromosome, centromere, kinetochore. Note=Localizes to the nuclear side of the spindle pole body.
DR  UNIPROT: P53148;
DR  UNIPROT: D6VU52;
DR  PDB: 4BL0;
DR  Pfam: PF18210;
DR  Pfam: PF08317;
DE  Function: Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint. {ECO:0000269|PubMed:19893618}.
DE  Reference Proteome: Yes;
DE  Interaction: P47149; IntAct: EBI-599281; Score: 0.37
DE  Interaction: P14693; IntAct: EBI-855274; Score: 0.00
DE  Interaction: Q04431; IntAct: EBI-7384815; Score: 0.66
DE  Interaction: Q04477; IntAct: EBI-1002308; Score: 0.64
DE  Interaction: P40568; IntAct: EBI-1543715; Score: 0.35
DE  Interaction: Q12143; IntAct: EBI-1543729; Score: 0.35
DE  Interaction: P39731; IntAct: EBI-1543771; Score: 0.35
DE  Interaction: P40460; IntAct: EBI-1543811; Score: 0.50
DE  Interaction: P33895; IntAct: EBI-1543811; Score: 0.35
DE  Interaction: P54199; IntAct: EBI-2612619; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3695987; Score: 0.35
DE  Interaction: P36016; IntAct: EBI-3707979; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3722158; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3729986; Score: 0.35
DE  Interaction: Q06677; IntAct: EBI-3759021; Score: 0.35
GO  GO:0000776;
GO  GO:0005739;
GO  GO:0031617;
GO  GO:0031965;
GO  GO:0005816;
GO  GO:0008017;
GO  GO:0051382;
GO  GO:1990758;
GO  GO:0007094;
GO  GO:0034501;
GO  GO:0031134;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MNVDERSRIGGREKDAGPGKGILKQNQSSQMTSSFLENPGVRIPTRIITKKEVLDGSNTTSRINTSNLQSMVKRRVSFAP
SQ  DVTLHSFTFVPEQNNEIKEPRRRKTSTNSPTKISSQEEPLVTSTQIDDARTEEKTAAEEDPDTSGMELTEPIVATPDSNK
SQ  ASQHDPTSMEMTEVFPRSIRQKNPDVEGESIESSQQIDDVEAVREETMELTAIHNVHDYDSISKDTVEGEPIDLTEYESK
SQ  PYVPNSVSRSTGKSSDYSVERSNDKSDLSKSENKTNSSQPMEITDIFHADPQNPMSLHSDNNINNDGNEMELTQIQTNFD
SQ  RDNHHIDESPSEKHAFSSNKRRKLDTVSDYAASVTTPVKEAKDTSGEDNDGDLEMMEKMSPITFSDVDNKIGTRSNDVFT
SQ  IEPGTEDTGMQTATDDEEDGENVDDNGNKIVEKTRLPEIDKEGQSGIALPTQDYTLREFINEVGVGFLDTKLIDDLDKKV
SQ  NFPLNSFNFVENQRIDNVFSAFYIDIPILEVEAFRCKELWRSINESKDKFKDFEAQIDKSHPPLLLQEYFSSDEKMKQLM
SQ  RDQLQLVKGYSKLEAAMEWYEWRKKQLNGLELILAENLNTLKREYEKLNEEVEKVNSIRGKIRKLNEAIKEEIRSLKNLP
SQ  SDSYKPTLMNRIKIEAFKQELMEHSISLSSSNDFTQEMRSLKLAIAKKSNDILTLRSEVASIDKKIEKRKLFTRFDLPKL
SQ  RDTLKILESLTGVRFLKFSKATLSIAFLQLDDLRVDINLANFKNNPLSSMKVMNDSNNDDMSYHLFTMLLKNVEAEHQDS
SQ  MLSNLFFAMKKWRPLLKYIKLLKLLFPVKITQTEEEEALLQFKDYDRRNKTAFFYVISLVSFAQGVFSENGQIPMKVHIS
SQ  TQQDYSPSREVLSDRITHKISGVLPSFTKSRIHLEFT
//
ID  Q9NPE6;
PN  Sperm-associated antigen 4 protein;
GN  SPAG4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O55034}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:O55034}. Nucleus envelope {ECO:0000250|UniProtKB:Q9JJF2}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9JJF2}. Note=In spermatids, it is localized in the transient manchette and in the axoneme of elongating spermatids and epididymal sperm (By similarity). Colocalized with SEPT12 at the nuclear periphery in round spermatids, at sperm neck in elongated spermatids and at midpiece regions in ejaculated spermatozoa (PubMed:25775403). {ECO:0000250|UniProtKB:O55034, ECO:0000269|PubMed:25775403}.
DR  UNIPROT: Q9NPE6;
DR  UNIPROT: O43648;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DR  OMIM: 603038;
DR  DisGeNET: 6676;
DE  Function: Involved in spermatogenesis. Required for sperm head formation but not required to establish and maintain general polarity of the sperm head. Required for anchoring and organization of the manchette. Required for targeting of SUN3 and probably SYNE1 through a probable SUN1:SYNE3 LINC complex to the nuclear envelope and involved in accurate posterior sperm head localization of the complex. May anchor SUN3 the nuclear envelope. Involved in maintenance of the nuclear envelope integrity. May assist the organization and assembly of outer dense fibers (ODFs), a specific structure of the sperm tail. {ECO:0000250|UniProtKB:O55034, ECO:0000250|UniProtKB:Q9JJF2}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8IXM6; IntAct: EBI-24640159; Score: 0.56
DE  Interaction: Q8TC36; IntAct: EBI-24639374; Score: 0.56
DE  Interaction: Q9BXJ8; IntAct: EBI-22744045; Score: 0.56
DE  Interaction: Q9H2S6; IntAct: EBI-24572530; Score: 0.56
DE  Interaction: Q8IYM1; IntAct: EBI-10819487; Score: 0.61
DE  Interaction: O95870; IntAct: EBI-24265964; Score: 0.56
DE  Interaction: Q9H2L4; IntAct: EBI-24266054; Score: 0.56
DE  Interaction: Q6UX98; IntAct: EBI-22746269; Score: 0.56
DE  Interaction: Q8IWU4; IntAct: EBI-22747198; Score: 0.56
DE  Interaction: P0DJD7; IntAct: EBI-24267883; Score: 0.56
DE  Interaction: P78329; IntAct: EBI-22747716; Score: 0.56
DE  Interaction: O14653; IntAct: EBI-24510927; Score: 0.56
DE  Interaction: P07306; IntAct: EBI-24514111; Score: 0.56
DE  Interaction: P24593; IntAct: EBI-24520110; Score: 0.56
DE  Interaction: Q5TGU0; IntAct: EBI-24524123; Score: 0.56
DE  Interaction: Q5J8X5; IntAct: EBI-24529588; Score: 0.56
DE  Interaction: Q96GQ5; IntAct: EBI-24610016; Score: 0.56
DE  Interaction: O00767; IntAct: EBI-24626536; Score: 0.56
DE  Interaction: Q14656; IntAct: EBI-24535767; Score: 0.56
DE  Interaction: P43378; IntAct: EBI-24536184; Score: 0.56
DE  Interaction: Q96IW7; IntAct: EBI-24547117; Score: 0.56
DE  Interaction: O95393; IntAct: EBI-24551734; Score: 0.56
DE  Interaction: Q969E2; IntAct: EBI-24579620; Score: 0.56
DE  Interaction: Q8TDX6; IntAct: EBI-24580321; Score: 0.56
DE  Interaction: Q7Z2K6; IntAct: EBI-24591721; Score: 0.56
DE  Interaction: P26678; IntAct: EBI-24597706; Score: 0.56
DE  Interaction: A5PKU2; IntAct: EBI-24637775; Score: 0.56
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0031514;
GO  GO:0005635;
GO  GO:0043495;
GO  GO:0005198;
GO  GO:0030154;
GO  GO:0006998;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRSSRPGSASSSRKHTPNFFSENSSMSITSEDSKGLRSAEPGPGEPEGRRARGPSCGEPALSAGVPGGTTWAGSSQQKP
SQ  APRSHNWQTACGAATVRGGASEPTGSPVVSEEPLDLLPTLDLRQEMPPPRVFKSFLSLLFQGLSVLLSLAGDVLVSMYRE
SQ  VCSIRFLFTAVSLLSLFLSAFWLGLLYLVSPLENEPKEMLTLSEYHERVRSQGQQLQQLQAELDKLHKEVSTVRAANSER
SQ  VAKLVFQRLNEDFVRKPDYALSSVGASIDLQKTSHDYADRNTAYFWNRFSFWNYARPPTVILEPHVFPGNCWAFEGDQGQ
SQ  VVIQLPGRVQLSDITLQHPPPSVEHTGGANSAPRDFAVFGLQVYDETEVSLGKFTFDVEKSEIQTFHLQNDPPAAFPKVK
SQ  IQILSNWGHPRFTCLYRVRAHGVRTSEGAEGSAQGPH
//
ID  Q9JJF2;
PN  Sperm-associated antigen 4 protein;
GN  Spag4;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000250}. [Isoform 1]: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O55034}. Nucleus envelope {ECO:0000269|PubMed:26621829}. Nucleus inner membrane {ECO:0000305}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:O55034}. Note=In spermatids, isoform 1 is localized in the transient manchette and in the axoneme of elongating spermatids and epididymal sperm (By similarity). Conflictingly is not found in axoneme but only associated with the manchette where cytoplasmic microtubules contact the nuclear envelope. Localizes at the posterior lateral side of round and elongating spermatids (PubMed:26621829). {ECO:0000250|UniProtKB:O55034, ECO:0000269|PubMed:26621829}.
DR  UNIPROT: Q9JJF2;
DR  UNIPROT: A3KGK4;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Involved in spermatogenesis. Required for sperm head formation but not required to establish and maintain general polarity of the sperm head. Required for anchoring and organization of the manchette. Required for targeting of SUN3 and probably SYNE1 through a probable SUN1:SYNE3 LINC complex to the nuclear envelope and involved in accurate posterior sperm head localization of the complex. May anchor SUN3 the nuclear envelope. Involved in maintenance of the nuclear envelope integrity. May assist the organization and assembly of outer dense fibers (ODFs), a specific structure of the sperm tail. {ECO:0000269|PubMed:26621829}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5SS91; IntAct: EBI-12557506; Score: 0.51
DE  Interaction: Q6ZWR6; IntAct: EBI-12557523; Score: 0.46
DE  Interaction: Q9JJF2; IntAct: EBI-12557600; Score: 0.46
GO  GO:0005737;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005874;
GO  GO:0031514;
GO  GO:0005635;
GO  GO:0042802;
GO  GO:0043495;
GO  GO:0030154;
GO  GO:0006998;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRSPRSGSAASSHNHTPNFYSENSNSSHSATSGDSNGRRSAGPELGEPEGRRARGSSCGEPALSPGMPGGDTWAGSSRP
SQ  KLAPRSHNGQTACGAATVRGGASEPSGSSVVLEEQLNLLPILDLRQEMPTPRVSKSFLSLLFQVLSMVLSLAVDGLVCVC
SQ  REICSIRFLFTAVSLLSIFLAALWWGLLYLIPPLENEPTEMLTLSQYHHRVHSQGQQLQQLQAELNKLHKEVSSVRAAHS
SQ  ERVAKLVFQRLNEDFVRKPDYALSSVGASIDLEKTSSDYEDQNTAYFWNRLSFWNYARPPSVILEPDVFPGNCWAFEGDK
SQ  GQVVIRLPGHVQLSDITLQHPPPTVAHTGGASSAPRDFAVYGLQADDETEVFLGKFIFDVQKSEIQTFHLQNDPPSAFPK
SQ  VKIQILSNWGHPRFTCLYRVRAHGVRTSEWADDNATGVTGGPH
//
ID  O55034;
PN  Sperm-associated antigen 4 protein;
GN  Spag4;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10373309}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:10373309}. Nucleus envelope {ECO:0000250|UniProtKB:Q9JJF2}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9JJF2}. Note=In spermatids, it is localized in the transient manchette and in the axoneme of elongating spermatids and epididymal sperm. {ECO:0000269|PubMed:10373309}.
DR  UNIPROT: O55034;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Involved in spermatogenesis. Required for sperm head formation but not required to establish and maintain general polarity of the sperm head. Required for anchoring and organization of the manchette. Required for targeting of SUN3 and probably SYNE1 through a probable SUN1:SYNE3 LINC complex to the nuclear envelope and involved in accurate posterior sperm head localization of the complex. May anchor SUN3 the nuclear envelope. Involved in maintenance of the nuclear envelope integrity (By similarity). May assist the organization and assembly of outer dense fibers (ODFs), a specific structure of the sperm tail (PubMed:10373309). {ECO:0000250|UniProtKB:Q9JJF2, ECO:0000305|PubMed:10373309}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005874;
GO  GO:0031514;
GO  GO:0005635;
GO  GO:0042802;
GO  GO:0043495;
GO  GO:0030154;
GO  GO:0006998;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRRNPRPGSAASSHNHTPNFYSENSNSSHSATSGDSNGRRSAGPELGEPDGRMARGSSCGEPALSSGVPGGDTWAGSSRP
SQ  KLAPRSHNGQTACGAATVRGGASEPSGSPAVLEEQLNLLPILDLRQEMPPPPVSKSFLSLFFQVLSVFLSLVADGLVCVY
SQ  REICSIRFLFTAVSLLSIFLAALWWGLLYLIPPLENEPKEMLTLSQYHHRVHSQGQQLQQLQAELSKLHKEVTSVRAAHS
SQ  ERVAKLVFQRLNEDFVRKPDYALSSVGASIDLEKTSSDYEDRNTAYFWNRLSFWNYARPPSVILEPDVFPGNCWAFEGEQ
SQ  GQVVIRLPGHVQLSDITLQHPPPTVAHTGGASSAPRDFAVFGLQADDDETEVFLGKFIFEVQKSEIQTFHLQNDPPSAFP
SQ  KVKIQILSNWGHPRFTCLYRVRAHGVRISESAEDNAMGVTGGPH
//
ID  A2VDN5;
PN  Spastin;
GN  SPAST;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP- Rule:MF_03021}. Cell projection, axon {ECO:0000250|UniProtKB:Q9UBP0}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Localizes to endoplasmic reticulum tubular network. Mainly nuclear in interphase cells and becomes associated with the centrosomes, spindle microtubules, midzone and finally the midbody during cell division (By similarity). {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP- Rule:MF_03021}.
DR  UNIPROT: A2VDN5;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing. Probably plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP- Rule:MF_03021}.
DE  Disease: Note=Defects in SPAST are the cause of bovine spinal dysmyelination (BSD), a neurodegenerative disorder characterized by pathological changes of the myelin sheaths in the spinal cord. Defects appear immediately at birth and include lateral recumbency with slight to moderate opisthotonos, body tremor, and spastic extension of the limbs. General muscle atrophy due to denervation occurs to variable degrees and is most obvious in the hind limbs. BSD is a longstanding problem in the American Brown Swiss (ABS) breed and in several European cattle breeds upgraded with ABS. The morphological cause of the phenotype is bilateral symmetrical hypo- and demyelination of axons in the cervical and thoracic segments of the spinal cord. The disease is caused by variants affecting the gene represented in this entry. {ECO:0000269|PubMed:19714378}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0030496;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000922;
GO  GO:0043014;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048487;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0008089;
GO  GO:0019896;
GO  GO:0007409;
GO  GO:0032506;
GO  GO:0006888;
GO  GO:0010458;
GO  GO:0090148;
GO  GO:0008152;
GO  GO:0001578;
GO  GO:0051013;
GO  GO:0000281;
GO  GO:0051228;
GO  GO:0031468;
GO  GO:0032467;
GO  GO:0031117;
GO  GO:0034214;
GO  GO:0051260;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03021};
SQ  MNSPGGRGKKKGSGGPSSPVPPRPPPPCQARSRPAPKPAPPPQSPHKRNLYYFSYPLFLGFALLRLVAFHLGLLFVWLCQ
SQ  RFSRALMAAKRSSGAAPASASPPAPVPGGEAERVRAFHKQAFEYISVALRIDEDEKVGQKDQAVEWYKKGIEELEKGIAV
SQ  VVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKLQPSLQFSKSQTDVYNDSTNLTCRNGHLQSESGAVPKRKDPLTHA
SQ  SNSLPRSKTVMKTGPTGLSGHHRAPSCSGLSMVSGVRQGPGSAAATHKSTPKTNRTNKPSTPTTAARKKKDLKNFRNVDS
SQ  NLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNAT
SQ  FFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLV
SQ  MGATNRPQELDEAVLRRFTKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTNGYSGSDLTALAKDAALGPIR
SQ  ELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
//
ID  A8QFF6;
PN  Probable spastin homolog Bm1_53365;
GN  Bm1_53365;
OS  6279;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: A8QFF6;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  PROSITE: PS00674;
DE  Function: Severs microtubules, probably in an ATP-dependent fashion. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0016853;
GO  GO:0008568;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLHPQKLEQQNYETFNKAYLKSKQLVTEGVSIDEISSNNDEQRKRIAMEKYRMGIEYFEKALKISPDKVYPEKRSEVITH
SQ  REAMKRNLEATKGRLSDLEKMFPSKGNRNLQHRPVQFVSPSISKPQTAQLSSRPISSEKKNINYSNARTRSNLLKGVDDK
SQ  FGGPLLNEILNQDDVKMSDIIGAETAKRALEETVILPTVNPSLFSGLRQPAQGILLFGPPGNGKTLLARAVAGECGSTMF
SQ  LNVSAASLTSKWVGDAEKIVRALFQIARNGQPTIIFIDEIDSILCERNEKETEVSRRMKTEFLIQMDGMLSSKDDRLLVI
SQ  GATNRPEELDSAILRRFPKRILIDVPNAAARLKLIMSLLEKTKTSFDLGLTQRQILAEWTHGYSNSDLVALCREAAMVPI
SQ  RDLSRKDIKNLVSTELRPITLRDFEIAMKAIKPSTNERMLQKLRKYAATAGQSD
//
ID  A8XV40;
PN  Probable spastin homolog spas-1;
GN  spas;
OS  6238;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localized to the perinuclear region of the cytoplasm in early embryos. Present in the cytoskeletal fraction. {ECO:0000250}.
DR  UNIPROT: A8XV40;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  PROSITE: PS00674;
DE  Function: Severs microtubules, probably in an ATP-dependent fashion. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0016853;
GO  GO:0008568;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFAFSKAPAGCSTYERVTQKFQDGSNKLRAAIEMDELTKQNGTINEKLQTAELYKQARQMLKEANEFNIMDIPESKRSEV
SQ  REKREKTLNLEKSAQDRLIKICNEVDPNMKRASTAADPCRAARITPRNTRATVPGDKKVSKVKQTEKAPHVCSRGDRCGA
SQ  HQPPPEKKSTPLKPVNQIRTRVKENKNPIGVQQQVFSFILSCCMRRNCRRPHYLFPCMISLKMNYFKFQATLPNQLNTVN
SQ  RSNLLKGVDKAIGERLLDEILDSTGVRMDDVAGCHSAKATLEEAVILPALNPNLFSGLRQPVKGILLFGPPGNGKTLLAK
SQ  AVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIARNGQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGAT
SQ  SSPDDRILVIGATNRPYELDDAVLRRFPKRIMLNLPDTEARKELITNTLKKHDMMDGLSSSDIRYIASNTSGFSNSDLVA
SQ  LCKEAAMVPVREIHRSKLSVTDGDKIRKIRASDFDTALRTIRPSTSDRILSKLSDFSRNFGC
//
ID  Q8MNV0;
PN  Spastin homolog;
GN  spas;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UBP0}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17531954}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17531954}. Note=Forms an intramembrane hairpin-like structure in the membrane (By similarity). Localizes to the cytoskeleton, perinuclear region and cytoplasm in early embryos (PubMed:17531954). {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000269|PubMed:17531954}.
DR  UNIPROT: Q8MNV0;
DR  UNIPROT: G5EEF8;
DR  UNIPROT: Q7M3K5;
DR  UNIPROT: Q8MNU9;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules (PubMed:17531954, PubMed:19619244, PubMed:22561316, PubMed:18202664). Probably by regulating microtubule remodeling, plays a role in new synapse formation in GABAergic DD (Dorsal D type) neurons (PubMed:26051896). {ECO:0000269|PubMed:17531954, ECO:0000269|PubMed:18202664, ECO:0000269|PubMed:19619244, ECO:0000269|PubMed:22561316, ECO:0000269|PubMed:26051896}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8MNV0; IntAct: EBI-15680282; Score: 0.62
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0016020;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0042802;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0001578;
GO  GO:0007019;
GO  GO:0051013;
GO  GO:0007399;
GO  GO:0051647;
GO  GO:0048477;
GO  GO:0031117;
GO  GO:0040025;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9UBP0};
SQ  MFAFSKGPAGSSTYDRVAQKFQDGYEKMRAAIEMDELTKHAGSIQEKLRTAELYKEARSLLKEANEFNIMDIPETRRSEI
SQ  RDKRQNMMKLEKSAQDRLIAICNEVDPNVKQSRSATVGPSRPASAARVTPRPTRATAPEKKNAAKAKENDENRHVCSRGD
SQ  RCGAHHQPVTKKSDTVHPEPPVQASNRKMETVKRVKVDKASLPMHQNPVNRAALLNGVDKVIGERLLDEVLDNTGVRMDD
SQ  VAGCHSAKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTI
SQ  RGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSADDRILVIGATNRPHELDDAVLRRFPKR
SQ  IMLNLPDEEARKELITKTLKKHNMMDGLISSDIRYIASNTSGFSNSDLVALCKEAAMVPIREIDRSKLSMTDGEKIRKIR
SQ  ASDFDTALRTIRPSTSQKIMSKLSDFSRSFGC
//
ID  Q5ZK92;
PN  Spastin;
GN  SPAST;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP- Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. {ECO:0000255|HAMAP-Rule:MF_03021}.
DR  UNIPROT: Q5ZK92;
DR  UNIPROT: B5AH49;
DR  UNIPROT: B5AH50;
DR  UNIPROT: E1C6S3;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. Also plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP-Rule:MF_03021}.
DE  Reference Proteome: Yes;
GO  GO:1904115;
GO  GO:0005813;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0030496;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000922;
GO  GO:0043014;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048487;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0008089;
GO  GO:0019896;
GO  GO:0007409;
GO  GO:0032506;
GO  GO:0006888;
GO  GO:0010458;
GO  GO:0090148;
GO  GO:0001578;
GO  GO:0051013;
GO  GO:0000281;
GO  GO:0051228;
GO  GO:0031468;
GO  GO:0032467;
GO  GO:0031117;
GO  GO:0034214;
GO  GO:0051260;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03021};
SQ  MNSPGGRGKKKGSAGSSSAPPAAGASPSAPSGPAPPAPPAGAAAAAAASPHKRNLYYFSYPLFAAFALLRFVAFQLGLLV
SQ  AWLCERLSRGALMAAKSSRAGDAPEPGGAAERVRACHKRAFECISMALRIDEDERAGQKEQAVEWYKKGIEELERGIAVL
SQ  VVGQGDQCERARRLQSKMMTNLAMAKDRLQLLEKLQADLQISKPQMEVYNDSTNLACRNGHLQSESGAVPKKKDPLTHTS
SQ  NSLPRSKTVAKTGSTGLSGHHRTPSYSGISTASVSRPAANPATSTHKAAPKNSRTNKPSTPTPAARKKKDTKVFRNVDSN
SQ  LANLILNEIVDSGPAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATF
SQ  FNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSSGEDRILVM
SQ  GATNRPQELDDAVLRRFTKRVYVSLPNEETRLILLKNLLSKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRE
SQ  LKPEQVKNMSASEMRNIKLSDFTESLKKIKRSLSPQTLEAYIRWNKDFGDTTV
//
ID  Q6NW58;
PN  Spastin;
GN  spast;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP- Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. {ECO:0000255|HAMAP-Rule:MF_03021}.
DR  UNIPROT: Q6NW58;
DR  UNIPROT: Q6JUU0;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. Also plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP-Rule:MF_03021}.
DE  Reference Proteome: Yes;
GO  GO:1904115;
GO  GO:0005813;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0030496;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0043014;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048487;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0008089;
GO  GO:0048675;
GO  GO:0007411;
GO  GO:0019896;
GO  GO:0007409;
GO  GO:0021955;
GO  GO:0032506;
GO  GO:0031122;
GO  GO:0006888;
GO  GO:0007032;
GO  GO:0010458;
GO  GO:0090148;
GO  GO:0001578;
GO  GO:0000226;
GO  GO:0051013;
GO  GO:0000281;
GO  GO:0051228;
GO  GO:0043066;
GO  GO:0031468;
GO  GO:0045773;
GO  GO:0031117;
GO  GO:0034214;
GO  GO:0051260;
GO  GO:0072593;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03021};
SQ  MNSGHKARLRGGRACGPVSDGSARGNRLLFYTRSLSRVPEWLLRVLLLLLRWLFQPIRRAMAARAKECGPDGSEETGERI
SQ  RNYHKQAFEFISVALQIDEDEKGDKQKAVQWYRKGIAELEKGIQIQVTGAGEKADRARKLQDKMITNLSMAEDRLKLLGN
SQ  LLSQSPAESSSDDSFYSFSNGNLRPAPASGAVSKKKDTLTITNQTSLRPKNPPKSTPNASGLNCTPSAAQSSRTGPQNNQ
SQ  KGPTVKGKNNVKASTTATASPQRKRDMKNFKNVDSKLASLILNEIVDSGSVVRFDDIAGQDLAKQALQEIVILPALRPEL
SQ  FTGLRAPARGLLLFGPPGNGKTMLAKAVAMESNATFFNISAATLTSKYVGEGEKLVRALFAVARELQPSIIFIDEIDSLL
SQ  CERREGEHDASRRLKTEFLIEFDGVQSGGDERVLVMGATNRPQELDEAVLRRFAKRIYVALPTEETRLKLLKNLLSKHRN
SQ  PLSQKELSQLARLTDGYSGSDLTSLAKDAALGPIRELKPEQVRNMSAHEMRDIRISDFLESLKRIKRSVSPQTLDQYVRW
SQ  NREYGDTTGV
//
ID  Q9UBP0;
PN  Spastin;
GN  SPAST;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:19000169}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000305|PubMed:20200447}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:16602018}. Midbody {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18997780, ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:25390646}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:15269182, ECO:0000269|PubMed:15891913, ECO:0000269|PubMed:25390646}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:15716377, ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:18410514, ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:20200447}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:11809724, ECO:0000269|PubMed:15147984, ECO:0000269|PubMed:15269182, ECO:0000269|PubMed:15537668}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:15147984, ECO:0000269|PubMed:15269182, ECO:0000269|PubMed:16026783}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:15269182}. Cytoplasm {ECO:0000255|HAMAP- Rule:MF_03021, ECO:0000269|PubMed:16026783, ECO:0000269|PubMed:20200447}. Cell projection, axon {ECO:0000269|PubMed:15269182}. Note=Forms an intramembrane hairpin-like structure in the membrane (PubMed:20200447). Localization to the centrosome is independent of microtubules (PubMed:15891913). Localizes to the midbody of dividing cells, and this requires CHMP1B (PubMed:18997780). Enriched in the distal axons and branches of postmitotic neurons (PubMed:15269182). Mainly nuclear in interphase cells and becomes associated with the centrosomes, spindle microtubules, midzone and finally the midbody during cell division (PubMed:15269182). {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:15269182, ECO:0000269|PubMed:15891913, ECO:0000269|PubMed:18997780, ECO:0000305|PubMed:20200447}. [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:23969831}; Peripheral membrane protein {ECO:0000305|PubMed:20200447}. Nucleus membrane {ECO:0000269|PubMed:26040712}. Lipid droplet {ECO:0000269|PubMed:25875445}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:20200447}. Endosome {ECO:0000269|PubMed:23897888}. Note=Forms an intramembrane hairpin-like structure in the membrane (PubMed:20200447). Recruited to nuclear membrane by IST1 during late anaphase (PubMed:26040712). Localizes to endoplasmic reticulum tubular network (PubMed:23969831). {ECO:0000269|PubMed:23969831, ECO:0000269|PubMed:26040712, ECO:0000305|PubMed:20200447}. [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:20200447, ECO:0000269|PubMed:23969831}. Endosome {ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:23897888}. Nucleus membrane {ECO:0000269|PubMed:16026783, ECO:0000269|PubMed:26040712}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25390646}. Note=Constitutes the main endosomal form (PubMed:19000169). Recruited to nuclear membrane by IST1 during late anaphase (PubMed:26040712). {ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:26040712}.
DR  UNIPROT: Q9UBP0;
DR  UNIPROT: A7E2A7;
DR  UNIPROT: Q9UPR9;
DR  PDB: 3EAB;
DR  PDB: 3VFD;
DR  PDB: 5Z6Q;
DR  PDB: 5Z6R;
DR  PDB: 6PEK;
DR  PDB: 6PEN;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DR  OMIM: 182601;
DR  OMIM: 604277;
DR  DisGeNET: 6683;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated (PubMed:11809724, PubMed:15716377, PubMed:16219033, PubMed:17389232, PubMed:20530212, PubMed:22637577, PubMed:26875866). Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866). Severing activity is not dependent on tubulin acetylation or detyrosination (PubMed:26875866). Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex (PubMed:19000169, PubMed:21310966, PubMed:26040712). Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex (PubMed:21310966). Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling (PubMed:23897888). Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (PubMed:23897888). Probably plays a role in axon growth and the formation of axonal branches (PubMed:15716377). {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:11809724, ECO:0000269|PubMed:15716377, ECO:0000269|PubMed:16219033, ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:20530212, ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:22637577, ECO:0000269|PubMed:23897888, ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:26875866}. [Isoform 1]: Involved in lipid metabolism by regulating the size and distribution of lipid droplets. {ECO:0000269|PubMed:25875445}.
DE  Disease: Spastic paraplegia 4, autosomal dominant (SPG4) [MIM:182601]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:10610178, ECO:0000269|PubMed:10699187, ECO:0000269|PubMed:11015453, ECO:0000269|PubMed:11039577, ECO:0000269|PubMed:11087788, ECO:0000269|PubMed:11309678, ECO:0000269|PubMed:11809724, ECO:0000269|PubMed:11843700, ECO:0000269|PubMed:11985387, ECO:0000269|PubMed:12124993, ECO:0000269|PubMed:12161613, ECO:0000269|PubMed:12163196, ECO:0000269|PubMed:12202986, ECO:0000269|PubMed:12460147, ECO:0000269|PubMed:12552568, ECO:0000269|PubMed:12939659, ECO:0000269|PubMed:14732620, ECO:0000269|PubMed:15159500, ECO:0000269|PubMed:15210521, ECO:0000269|PubMed:15248095, ECO:0000269|PubMed:15326248, ECO:0000269|PubMed:15482961, ECO:0000269|PubMed:15667412, ECO:0000269|PubMed:15716377, ECO:0000269|PubMed:15891913, ECO:0000269|PubMed:16339213, ECO:0000269|PubMed:16682546, ECO:0000269|PubMed:16684598, ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:17594340, ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:20214791, ECO:0000269|PubMed:20550563, ECO:0000269|PubMed:20562464, ECO:0000269|PubMed:20718791, ECO:0000269|PubMed:20932283, ECO:0000269|PubMed:21546041, ECO:0000269|PubMed:22960362, ECO:0000269|PubMed:23279441, ECO:0000269|PubMed:24824479, ECO:0000269|PubMed:25045380, ECO:0000269|PubMed:25421405, ECO:0000269|PubMed:28572275}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O43633; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: P52948; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: P53990; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q8NFH3; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q8WUM0; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q9BW27; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-11151252; Score: 0.35
DE  Interaction: P02768; IntAct: EBI-1222961; Score: 0.35
DE  Interaction: A0A0H2W6D4; IntAct: EBI-2854381; Score: 0.00
DE  Interaction: Q86XJ1; IntAct: EBI-9248304; Score: 0.27
DE  Interaction: Q96GD4; IntAct: EBI-9248289; Score: 0.27
DE  Interaction: P05214; IntAct: EBI-10992821; Score: 0.35
DE  Interaction: P06240; IntAct: EBI-10997111; Score: 0.35
DE  Interaction: E9QLB2; IntAct: EBI-11017420; Score: 0.35
DE  Interaction: Q6PB44; IntAct: EBI-11097749; Score: 0.35
DE  Interaction: P46467; IntAct: EBI-11115954; Score: 0.35
DE  Interaction: Q923W1; IntAct: EBI-11136374; Score: 0.35
DE  Interaction: Q96P20; IntAct: EBI-11141914; Score: 0.35
DE  Interaction: P15408; IntAct: EBI-11145265; Score: 0.35
DE  Interaction: Q9Y484; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q9NP79; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q8IUE6; IntAct: EBI-21757061; Score: 0.35
DE  Interaction: Q6ZNA4; IntAct: EBI-21806464; Score: 0.35
DE  Interaction: Q8WXF7; IntAct: EBI-15590258; Score: 0.59
DE  Interaction: P83105; IntAct: EBI-25745135; Score: 0.35
DE  Interaction: Q5T4F4; IntAct: EBI-25506678; Score: 0.46
DE  Interaction: Q00765; IntAct: EBI-25683908; Score: 0.27
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0071782;
GO  GO:0005768;
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005874;
GO  GO:0030496;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000922;
GO  GO:0043014;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048487;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0044877;
GO  GO:0008089;
GO  GO:0019896;
GO  GO:0007409;
GO  GO:0032506;
GO  GO:0061640;
GO  GO:0006888;
GO  GO:0010458;
GO  GO:0090148;
GO  GO:0008152;
GO  GO:0001578;
GO  GO:0051013;
GO  GO:0000281;
GO  GO:0007084;
GO  GO:0051228;
GO  GO:0031468;
GO  GO:0032467;
GO  GO:0031117;
GO  GO:0034214;
GO  GO:0051260;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305|PubMed:20200447};
SQ  MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQ
SQ  RFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGI
SQ  AVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKMQPVLPFSKSQTDVYNDSTNLACRNGHLQSESGAVPKRKDPLT
SQ  HTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNV
SQ  DSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESN
SQ  ATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRV
SQ  LVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGP
SQ  IRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
//
ID  Q9QYY8;
PN  Spastin;
GN  Spast;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP- Rule:MF_03021}. Cell projection, axon {ECO:0000250|UniProtKB:Q9UBP0}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B (By similarity). Enriched in the distal axons and branches of postmitotic neurons (By similarity). Evenly distributed along early axons and concentrates in the growth cone of the axons of late stage 3 neurons (PubMed:18234839). Mainly nuclear in interphase cells and becomes associated with the centrosomes, spindle microtubules, midzone and finally the midbody during cell division (By similarity). {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18234839}. [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UBP0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UBP0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9UBP0}. Lipid droplet {ECO:0000250|UniProtKB:Q9UBP0}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UBP0}. Endosome {ECO:0000250|UniProtKB:Q9UBP0}. Note=Forms an intramembrane hairpin- like structure in the membrane. Recruited to nuclear membrane by IST1 during late anaphase. Localizes to endoplasmic reticulum tubular network. {ECO:0000250|UniProtKB:Q9UBP0}. [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q9UBP0}. Endosome {ECO:0000250|UniProtKB:Q9UBP0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9UBP0}. Note=Constitutes the main endosomal form. Recruited to nuclear membrane by IST1 during late anaphase. {ECO:0000250|UniProtKB:Q9UBP0}.
DR  UNIPROT: Q9QYY8;
DR  UNIPROT: Q6ZPY6;
DR  UNIPROT: Q80VE0;
DR  UNIPROT: Q9CVK0;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated (PubMed:19141076 PubMed:20530212). Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). Severing activity is not dependent on tubulin acetylation or detyrosination (By similarity). Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation (By similarity). It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia (By similarity). SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex (By similarity). Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex (By similarity). Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase (By similarity). Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling (By similarity). Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (By similarity). Probably plays a role in axon growth and the formation of axonal branches (PubMed:18234839). {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18234839, ECO:0000269|PubMed:19141076, ECO:0000269|PubMed:20530212}. [Isoform 1]: Involved in lipid metabolism by regulating the size and distribution of lipid droplets. {ECO:0000250|UniProtKB:Q9UBP0}.
DE  Reference Proteome: Yes;
DE  Interaction: O43633; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: P49454; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: P53990; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q9H444; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q9Y3E7; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q9Y2B5; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: O75340; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q9UQN3; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q96N66; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q8WUM4; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q96BY9; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q15904; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: P09496; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: O75348; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q03135; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q9HD42; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q96NT0; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: B4E2V5; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: O75477; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: P21281; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q99816; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q8WV92; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q9ULH0; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q13425; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: E9PSI1; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q9NZZ3; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: F5H4Q5; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q9Y6W3; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q14254; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: F5H4F1; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q8IVT2; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q9Y5K6; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: O75955; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: P38606; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q93050; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q96EY5; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: Q9NQS3; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: P14384; IntAct: EBI-11090422; Score: 0.35
DE  Interaction: P61421; IntAct: EBI-11090422; Score: 0.35
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0071782;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0030496;
GO  GO:0031965;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000922;
GO  GO:0043014;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048487;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0008089;
GO  GO:0019896;
GO  GO:0007409;
GO  GO:0032506;
GO  GO:0006888;
GO  GO:0010458;
GO  GO:0090148;
GO  GO:0008152;
GO  GO:0001578;
GO  GO:0051013;
GO  GO:0000281;
GO  GO:0051228;
GO  GO:0031468;
GO  GO:0032467;
GO  GO:0031117;
GO  GO:0034214;
GO  GO:0051260;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9UBP0};
SQ  MSSPAGRRKKKGSGGASPAPARPPPPAAVPAPAAGPAPAAGSPPKRNPSSFSSPLVVGFALLRLLACHLGLLFAWLCQRF
SQ  SRALMAAKRSSGTAPAPASPSPPEPGPGGEAESVRVFHKQAFEYISIALRIDEEEKAGQKEQAVEWYKKGIEELEKGIAV
SQ  IVTGQGEQYERARRLQAKMMTNLVMAKDRLQLLEKLQPVLQFSKSQTDVYNESTNLTCRNGHLQSESGAVPKRKDPLTHA
SQ  SNSLPRSKTVLKSGSAGLSGHHRAPSCSGLSMVSGARPGPGPAATTHKGTPKPNRTNKPSTPTTAVRKKKDLKNFRNVDS
SQ  NLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNAT
SQ  FFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLV
SQ  MGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIR
SQ  ELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
//
ID  Q719N1;
PN  Spastin;
GN  SPAST;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP- Rule:MF_03021}. Cell projection, axon {ECO:0000250|UniProtKB:Q9UBP0}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Localizes to endoplasmic reticulum tubular network. Mainly nuclear in interphase cells and becomes associated with the centrosomes, spindle microtubules, midzone and finally the midbody during cell division (By similarity). {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP- Rule:MF_03021}.
DR  UNIPROT: Q719N1;
DR  UNIPROT: F1S3Z2;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing. Probably plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP- Rule:MF_03021}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005813;
GO  GO:0005783;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0030496;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000922;
GO  GO:0043014;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048487;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0008089;
GO  GO:0019896;
GO  GO:0007409;
GO  GO:0032506;
GO  GO:0006888;
GO  GO:0010458;
GO  GO:0090148;
GO  GO:0008152;
GO  GO:0001578;
GO  GO:0051013;
GO  GO:0000281;
GO  GO:0051228;
GO  GO:0031468;
GO  GO:0031117;
GO  GO:0034214;
GO  GO:0051260;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03021};
SQ  MNSPGGRGKKKGSGGPSSPVPPRPPPPCLASSRPAPRPAPPPQSPHKRNLYYFSYPLFLGFALLRLVAFHLGLLFVWLCQ
SQ  RFSRALMAAKRSSRAAPAPASASPPAPVPGGEVERVRAFHKQAFEYISVALRIDEDEKVGQKEQAVEWYKKGIEELEKGI
SQ  AVVVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKLQPVLQFSKSQMDVYNDSTNLTCRNGHLQSESGAVPKRKDPLT
SQ  HPSNSLPRSKAIMKTGSTGLSGHHRAPSCSGLSIVSGMRQGPGPTTATHKSTPKTNRTNKPSTPTTAPRKKKDLKNFRNV
SQ  DSNLANFIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESN
SQ  ATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLRERREGEHDASRRLKTEFLIEFDGVQSAGDDRV
SQ  LVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARLTDGYSGSDLTALAKDAALGP
SQ  IRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
//
ID  B2RYN7;
PN  Spastin;
GN  Spast;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP- Rule:MF_03021}. Cell projection, axon {ECO:0000250|UniProtKB:Q9UBP0}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Localizes to endoplasmic reticulum tubular network. Mainly nuclear in interphase cells and becomes associated with the centrosomes, spindle microtubules, midzone and finally the midbody during cell division (By similarity). {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP- Rule:MF_03021}.
DR  UNIPROT: B2RYN7;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (By similarity). Probably plays a role in axon growth and the formation of axonal branches (PubMed:18234839). {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18234839}.
DE  Reference Proteome: Yes;
DE  Interaction: P15127; IntAct: EBI-21297848; Score: 0.35
GO  GO:0030424;
GO  GO:1904115;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0030496;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000922;
GO  GO:0043014;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048487;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0008089;
GO  GO:0019896;
GO  GO:0007409;
GO  GO:0032506;
GO  GO:0006888;
GO  GO:0010458;
GO  GO:0090148;
GO  GO:0008152;
GO  GO:0001578;
GO  GO:0051013;
GO  GO:0000281;
GO  GO:0051228;
GO  GO:0031468;
GO  GO:0032467;
GO  GO:0031117;
GO  GO:0034214;
GO  GO:0051260;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03021};
SQ  MSSPAGRRKKKGSGGASPAPARPPPPAAVPAPAAGPAPAPGSPHKRNLYYFSYPLVVGFALLRLLACHLGLLFVWLCQRF
SQ  SRALMAAKRSSGTAPAPASPSTPAPGPGGEAESVRVFHKQAFEYISIALRIDEEEKGQKEQAVEWYKKGIEELEKGIAVI
SQ  VTGQGEQYERARRLQAKMMTNLVMAKDRLQLLESGAVPKKKDPLTHASNSLPRSKTVMKSGSTGLSGHHRAPSCSGLSMV
SQ  SGARPGSGPAATTHKGTSKPNRTNKPSTPTTAVRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQ
SQ  EIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQP
SQ  SIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRL
SQ  LLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRS
SQ  VSPQTLEAYIRWNKDFGDTTV
//
ID  Q6AZT2;
PN  Spastin;
GN  spast;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP- Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. {ECO:0000255|HAMAP-Rule:MF_03021}.
DR  UNIPROT: Q6AZT2;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. Also plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP-Rule:MF_03021}.
DE  Reference Proteome: Yes;
GO  GO:1904115;
GO  GO:0005813;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0030496;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0043014;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048487;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0008089;
GO  GO:0019896;
GO  GO:0007409;
GO  GO:0032506;
GO  GO:0006888;
GO  GO:0010458;
GO  GO:0090148;
GO  GO:0001578;
GO  GO:0051013;
GO  GO:0000281;
GO  GO:0051228;
GO  GO:0031468;
GO  GO:0031117;
GO  GO:0034214;
GO  GO:0051260;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03021};
SQ  MNSPGGRNDKKKPVTPAAETGPGSPTTPPSTETQVVLAPPSPHKRNLHLFSYPLLAVFSLLRFLAFQLGLLFVWCCELLS
SQ  RSVMADKGRTVASTAAAQDRPQEPEVVRSYHQQAFQYISLALRVDEEEKDQKEQAVQWYKKGIEELEKGIAVPISGKGEQ
SQ  YDRARRLQAKMSTNLIMAKDRLQLLAKLQADIQGPHSQMEVCSDNTNLPCRNGLLKPEKGAVPKKKDPPPITSNSYSRTK
SQ  APPKSGSLGNRIPNCTSVPTSARQAGAHTPSNRGATGKNNTRTNKPATPTTAVRKKDMKNLRNVDSNLANLILNEIVDSG
SQ  PSVKFADIAGQDLAKQALQEIVILPSIRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYV
SQ  GEGEKLVRALFSVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSGGDDRVLVMGATNRPQELDDAV
SQ  LRRFTKRVYVALPNEETRLVLLKNLLSKQGNPLSEKELTQLSRLTEGYSGSDITALAKDAALGPIRELKPEQVKNMAASE
SQ  MRNMKYSDFLGSLKKIKCSVSHSTLESYIRWNQDFGDTTV
//
ID  Q05AS3;
PN  Spastin;
GN  spast;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP- Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. {ECO:0000255|HAMAP-Rule:MF_03021}.
DR  UNIPROT: Q05AS3;
DR  UNIPROT: Q28H96;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. Also plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP-Rule:MF_03021}.
DE  Reference Proteome: Yes;
GO  GO:1904115;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005874;
GO  GO:0015630;
GO  GO:0030496;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:0043014;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0048487;
GO  GO:0016853;
GO  GO:0008017;
GO  GO:0008568;
GO  GO:0008089;
GO  GO:0019896;
GO  GO:0007409;
GO  GO:0032506;
GO  GO:0006888;
GO  GO:0010458;
GO  GO:0090148;
GO  GO:0001578;
GO  GO:0051013;
GO  GO:0000281;
GO  GO:0051228;
GO  GO:0031468;
GO  GO:0031117;
GO  GO:0034214;
GO  GO:0051260;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_03021};
SQ  MNSPGGRNNKKKPVTPAAETGPGPPTPPPPPAETQVLLAPPSLHKRNLYLFSYPLLAAFSLLRFLAFQLGLLFVWFCERL
SQ  SRRVMADKGSTAARTAAAPAQDRPQEPEVVRSYHQQAFQYISMALRIDEEEKDQKEQAIQWYKKGIEELEKGIAVTITGK
SQ  GEQYDRARRLQAKMSTNLLMAKDRLQLLAKLKADIQGQHSQMEVCSDNTNLPCRNGLLKPEKGAVPKKKDPPSISSNSYS
SQ  RVKAAPKSGSLGNRIPNCTGVSSSARQAGPNAPSNRGAAGKNNTRTNKPTTPTTAVRKKDMKNLRNVDSNLANLILNEIV
SQ  DSGPTVKFADIAGQDLAKQALQEIVILPSIRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS
SQ  KYVGEGEKLVRALFSVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSGGDDRVLVMGATNRPQELD
SQ  DAVLRRFTKRVYVSLPNEETRLLLLKNLLSKQGNPLNEKELTQLSRLTEGYSGSDITALAKDAALGPIRELKPEQVKNMA
SQ  ASEMRNIKYSDFLSSLKKIKCSVSPSTLESYIRWNKEFGDTTV
//
ID  P54217;
PN  Spermatocyte protein spe-11;
GN  spe;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:8565851}. Note=Localized to the perinuclear region of sperm.
DR  UNIPROT: P54217;
DE  Function: Paternally sperm-supplied factor required for embryogenesis (PubMed:8565851, PubMed:20971008). Plays a role in preventing polyspermy possibly by promoting the formation of a continuous and cohesive eggshell chitin layer (PubMed:20971008). {ECO:0000269|PubMed:20971008, ECO:0000269|PubMed:8565851}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030703;
GO  GO:0060468;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDEEIDISTALNNKTTPKKKSLKRNSNSQEGYESPEEREIVYPSVFGAIGTPMAKSDNAKEWDEWKEKERKKDKAEWKR
SQ  YLRSKWDMTQGHLPLVSDSEFLKGRKEHKEYNSKARMDILDGLDEVNEGFFNCGKGAAMNIRYNDKNVSKKGAKKFVATV
SQ  ETAMKKAGNPTMEQMMTDDLDEDEARAEAEWERQREQRKLASRAYDAAMDEREDDAKYVPWDEYCQEMEELGKELKIGEK
SQ  HYKKWLEKKMDENKVTHKFNAYQLDLKCLDEDAFSNKKSLKSVVRNVQKFYRKMREPKK
//
ID  Q1LYM3;
PN  Protein spire homolog 1;
GN  spire1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q52KF3}. Cleavage furrow {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q08AE8}. Cell membrane {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q52KF3}.
DR  UNIPROT: Q1LYM3;
DR  UNIPROT: Q08BK5;
DR  Pfam: PF16474;
DR  PROSITE: PS51377;
DE  Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis. Also acts in the nucleus: together with FMN2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. In addition, promotes innate immune signaling downstream of dsRNA sensing. Mechanistically, contributes to IRF3 phosphorylation and activation downstream of MAVS and upstream of TBK1. {ECO:0000250|UniProtKB:Q08AE8}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0032154;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0051639;
GO  GO:0030041;
GO  GO:0045010;
GO  GO:0036089;
GO  GO:0051295;
GO  GO:0070649;
GO  GO:0048193;
GO  GO:0046907;
GO  GO:0040038;
GO  GO:2000781;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q52KF3};
SQ  MTDGGMLISPSALQDPGDGARPEDIAMDCTDGEEELCLEEILTLYSQPINEEQAWAVCYQCCRWLTQKHRRKETGVSPPG
SQ  RIAGPGDVRIRKDGNVKLYQPSNPDKHTPPSSSIEIIESLGIMIYKALDYGLKEHEERELSPPLEQLIDLMTNMADTETD
SQ  CPDEGYEATEEEDEGEEENAEVSNVRGYRDIISLCLSHLPSPSDAPNHYQAVCRALYAETKELRTFLEKIKSAKENLRKM
SQ  EGETEEPVRDLNELQNADWARFWVQVMRDLRHGVKLKKVQERQYNPLAIEYQLTPYEMLMDDIRSKRYKLRKVMVNGDIP
SQ  PRLKKSAHEIILEFIRSRPPLNPVSARKLKPHAPQPPTLHERILEEIRSERKLRPVSPDMIRRSRLGAGKSISTPQDLFR
SQ  SSDIPDGPRKLAISTLSLANGTSPARSPVNGVAGGHSLSQRKRLLKAPTLAELDSSDSEEEQSTRKSDSSSSISTSLVED
SQ  TSPESVMGKKPPPQFLPISSTPQPDKRIAPQRRHSIEKEAPTNIRHFLPPSRQNSKSLAHALGSGHAEEFCFPVECLTLT
SQ  VEEVMHIRQVLVKAELEKFQQYKDIYNALKKGKLCFSCRSKKFSLFTWSYTCQFCKRPVCSQCCKKMKLPSKPHASLPIS
SQ  SLGPSILPKKEPGASSAPTDKTSSTSSHKKNSLQRSLSRSSKHGDRSSSKDELELPEQFTEDWSTMEVCVDCKKFINDII
SQ  SNSRRNLSTKRARLHRRTHSVYSSSTSSSNYKPTERTIKEV
//
ID  Q08AE8;
PN  Protein spire homolog 1;
GN  SPIRE1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11747823}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11747823}. Cell membrane {ECO:0000269|PubMed:11747823}; Peripheral membrane protein {ECO:0000269|PubMed:11747823}; Cytoplasmic side {ECO:0000269|PubMed:11747823}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q52KF3}. Note=Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (By similarity). Punctate spots in perinuclear region and cytoplasm, colocalized with Rab11 (By similarity). {ECO:0000250|UniProtKB:Q52KF3}.
DR  UNIPROT: Q08AE8;
DR  UNIPROT: A8K2B5;
DR  UNIPROT: J3KQ50;
DR  UNIPROT: J3KQR5;
DR  UNIPROT: Q1RMD4;
DR  UNIPROT: Q8NDP1;
DR  UNIPROT: Q9NQ71;
DR  UNIPROT: Q9ULT4;
DR  PDB: 2YLE;
DR  PDB: 2YLF;
DR  PDB: 3R7G;
DR  PDB: 3RBW;
DR  Pfam: PF16474;
DR  PROSITE: PS51377;
DR  OMIM: 609216;
DR  DisGeNET: 56907;
DE  Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament (PubMed:11747823, PubMed:21620703). Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (PubMed:11747823). Required for asymmetric spindle positioning and asymmetric cell division during meiosis (PubMed:21620703). Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis (PubMed:21620703). Also acts in the nucleus: together with FMN2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage (PubMed:26287480). In addition, promotes innate immune signaling downstream of dsRNA sensing (PubMed:35148361). Mechanistically, contributes to IRF3 phosphorylation and activation downstream of MAVS and upstream of TBK1 (PubMed:35148361). {ECO:0000269|PubMed:11747823, ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:26287480, ECO:0000269|PubMed:35148361}.
DE  Reference Proteome: Yes;
DE  Interaction: P27348; IntAct: EBI-21902679; Score: 0.56
DE  Interaction: P31947; IntAct: EBI-7544015; Score: 0.40
DE  Interaction: P68466; IntAct: EBI-6158939; Score: 0.35
DE  Interaction: O75161; IntAct: EBI-11783022; Score: 0.40
DE  Interaction: Q96RK4; IntAct: EBI-24711859; Score: 0.56
DE  Interaction: Q9Y3M2; IntAct: EBI-11911975; Score: 0.00
DE  Interaction: P56945; IntAct: EBI-15099538; Score: 0.35
DE  Interaction: Q4VC05; IntAct: EBI-21637103; Score: 0.35
DE  Interaction: Q8WUZ0; IntAct: EBI-21637520; Score: 0.35
DE  Interaction: Q9NYL9; IntAct: EBI-21701240; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-21903886; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21905461; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21907689; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-21909838; Score: 0.35
DE  Interaction: P68135; IntAct: EBI-16095106; Score: 0.44
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P13637; IntAct: EBI-25832773; Score: 0.56
DE  Interaction: P16284; IntAct: EBI-25881511; Score: 0.56
DE  Interaction: Q13393; IntAct: EBI-25882505; Score: 0.56
GO  GO:0005938;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0031307;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003779;
GO  GO:0030036;
GO  GO:0051639;
GO  GO:0030041;
GO  GO:0045010;
GO  GO:0036089;
GO  GO:0051295;
GO  GO:0070649;
GO  GO:0048193;
GO  GO:0046907;
GO  GO:0040038;
GO  GO:2000781;
GO  GO:0090141;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q52KF3};
SQ  MAQAAGPAGGGEPRTEAVGGEGPREPGAAGGAAGGSRDALSLEEILRLYNQPINEEQAWAVCYQCCGSLRAAARRRQPRH
SQ  RVRSAAQIRVWRDGAVTLAPAADDAGEPPPVAGKLGYSQCMETEVIESLGIIIYKALDYGLKENEERELSPPLEQLIDHM
SQ  ANTVEADGSNDEGYEAAEEGLGDEDEKRKISAIRSYRDVMKLCAAHLPTESDAPNHYQAVCRALFAETMELHTFLTKIKS
SQ  AKENLKKIQEMEKSDESSTDLEELKNADWARFWVQVMRDLRNGVKLKKVQERQYNPLPIEYQLTPYEMLMDDIRCKRYTL
SQ  RKVMVNGDIPPRLKKSAHEIILDFIRSRPPLNPVSARKLKPTPPRPRSLHERILEEIKAERKLRPVSPEEIRRSRLAMRP
SQ  LSMSYSFDLSDVTTPESTKNLVESSMVNGGLTSQTKENGLSTSQQVPAQRKKLLRAPTLAELDSSESEEETLHKSTSSSS
SQ  VSPSFPEEPVLEAVSTRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPPSRQSSRSLEEFCYPVECLALTV
SQ  EEVMHIRQVLVKAELEKYQQYKDIYTALKKGKLCFCCRTRRFSFFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFS
SQ  LGPSALQRGESSMRSEKPSTAHHRPLRSIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSL
SQ  VLANKRARLKRKTQSFYMSSPGPSEYCPSERTISEI
//
ID  Q4R707;
PN  Protein spire homolog 1;
GN  SPIRE1;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q52KF3}. Cleavage furrow {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q08AE8}. Cell membrane {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q52KF3}. Note=Punctate spots in perinuclear region and cytoplasm, co-localized with Rab11. Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion. {ECO:0000250|UniProtKB:Q52KF3}.
DR  UNIPROT: Q4R707;
DR  Pfam: PF16474;
DR  PROSITE: PS51377;
DE  Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis. Also acts in the nucleus: together with FMN2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. In addition, promotes innate immune signaling downstream of dsRNA sensing. Mechanistically, contributes to IRF3 phosphorylation and activation downstream of MAVS and upstream of TBK1. {ECO:0000250|UniProtKB:Q08AE8}.
DE  Reference Proteome: Yes;
GO  GO:0005938;
GO  GO:0032154;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0030036;
GO  GO:0045010;
GO  GO:0036089;
GO  GO:0051295;
GO  GO:0070649;
GO  GO:0046907;
GO  GO:0040038;
GO  GO:2000781;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q52KF3};
SQ  MANTVEADGSNDEGYEAAEEGPEDEEDEKREISAIRSYRDVMKLCAAHLPTESDAPNHYQAVCRALFAETMELHTFLAKV
SQ  KSAKENLKKIQEMEKSDESSTDLEELKNADWARFWVQVMRDLRNGVKLKKVQERQYNPLPIEYQLTPYEMLMDDIRCKRY
SQ  TLRKVMVNGDIPPRLKKSAHEIILDFIRSRPPLNPVSARKLKPTPPRPRSLHERILEEIKAERKLRPVSPEEIRRSRLDV
SQ  TTPESTKNLMESSMVNGGLTSQTKENGLSSAEQVPAQRKKLLKAPTLAELDSSESEEETLHKSTSSSSVSPSFPEEPVLE
SQ  AVSTRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPPSRQSSRSLEEFCYPVECLALTVEEVMHIRQVLVK
SQ  AELEKYQQYKDIYTALKKGKLCFCCRTRRFSFFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGPSALQRGESS
SQ  MRSEKPSTAHHRPLRSIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSLVLANKRARLKRK
SQ  TQSFYMSPPGPSEYCPSERTISEI
//
ID  Q52KF3;
PN  Protein spire homolog 1;
GN  Spire1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21983562}. Cytoplasm, cytosol {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}. Cleavage furrow {ECO:0000269|PubMed:21620703}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q08AE8}. Cell membrane {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}; Peripheral membrane protein {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}; Cytoplasmic side {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21983562}; Peripheral membrane protein {ECO:0000269|PubMed:21983562}; Cytoplasmic side {ECO:0000269|PubMed:21983562}. Note=Punctate spots in perinuclear region and cytoplasm, co-localized with Rab11 (PubMed:21983562). Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (PubMed:21620703). {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}.
DR  UNIPROT: Q52KF3;
DR  UNIPROT: Q6PDJ5;
DR  UNIPROT: Q80V45;
DR  Pfam: PF16474;
DR  PROSITE: PS51377;
DE  Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (PubMed:21983562). Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis (PubMed:21620703). Also acts in the nucleus: together with FMN2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. In addition, promotes innate immune signaling downstream of dsRNA sensing. Mechanistically, contributes to IRF3 phosphorylation and activation downstream of MAVS and upstream of TBK1. {ECO:0000250|UniProtKB:Q08AE8, ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0005938;
GO  GO:0032154;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0031307;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0030036;
GO  GO:0051639;
GO  GO:0030041;
GO  GO:0045010;
GO  GO:0001662;
GO  GO:0036089;
GO  GO:0060996;
GO  GO:0051295;
GO  GO:0070649;
GO  GO:0048193;
GO  GO:0046907;
GO  GO:0040038;
GO  GO:2000781;
GO  GO:0090141;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:21983562};
SQ  MANTVEADGSKDEGYEAADEGPEDEDGEKRSISAIRSYQDVMKICAAHLPTESEAPNHYQAVCRALFAETMELHTFLTKI
SQ  KSAKENLKKIQEMEKGDESSTDLEDLKNADWARFWVQVMRDLRNGVKLKKVQQRQYNPLPIEYQLTPYEMLMDDIRCKRY
SQ  TLRKVMVNGDVPPRLKKSAHEVILDFIRSRPPLNPVSARKLKPTPPRPRSLHERILEEIKAERKLRPVSPEEIRRSRLVR
SQ  PLSMSHSFDLSDVTTPESPKNVGESSMVNGGLTSQTKENGLSAAQQGSAQRKRLLKAPTLAELDSSDSEEEKSLHKSTSS
SQ  SSASPSLYEDPVLEAMCSRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPPSRQSSRSLEEFCYPVECLAL
SQ  TVEEVMHIRQVLVKAELEKYQQYKDVYTALKKGKLCFCCRTRRFSFFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPI
SQ  FSLGPSALQRGESCSRSEKPSTSHHRPLRSIARFSTKSRSVDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRR
SQ  SLVLANKRARLKRKTQSFYMSSAGPSEYCPSERTINEI
//
ID  Q9U1K1;
PN  Protein spire;
GN  spir;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10744979}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10744979}. Cell membrane {ECO:0000269|PubMed:21730168}; Peripheral membrane protein {ECO:0000269|PubMed:21730168}; Cytoplasmic side {ECO:0000269|PubMed:21730168}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21730168}; Peripheral membrane protein {ECO:0000269|PubMed:21730168}; Cytoplasmic side {ECO:0000269|PubMed:21730168}. Note=Punctate spots in perinuclear region and cytoplasm. {ECO:0000269|PubMed:10744979}.
DR  UNIPROT: Q9U1K1;
DR  UNIPROT: Q5U0Z8;
DR  UNIPROT: Q8INV3;
DR  UNIPROT: Q8INV4;
DR  UNIPROT: Q8INV5;
DR  UNIPROT: Q8SXP3;
DR  UNIPROT: Q8T8P8;
DR  UNIPROT: Q9U4F0;
DR  UNIPROT: Q9U4F1;
DR  UNIPROT: Q9VIN3;
DR  UNIPROT: Q9VIN4;
DR  PDB: 3MMV;
DR  PDB: 3MN5;
DR  PDB: 3MN6;
DR  PDB: 3MN7;
DR  PDB: 3MN9;
DR  PDB: 3UE5;
DR  PDB: 4EFH;
DR  Pfam: PF16474;
DR  PROSITE: PS51377;
DR  PROSITE: PS51082;
DE  Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton. {ECO:0000269|PubMed:10556052, ECO:0000269|PubMed:10744979, ECO:0000269|PubMed:15674283, ECO:0000269|PubMed:20538977, ECO:0000269|PubMed:21730168}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VRF5; IntAct: EBI-197814; Score: 0.00
DE  Interaction: Q7K159; IntAct: EBI-197818; Score: 0.00
DE  Interaction: Q7JQ36; IntAct: EBI-197822; Score: 0.00
DE  Interaction: Q9VBN2; IntAct: EBI-197831; Score: 0.00
DE  Interaction: P92208; IntAct: EBI-871706; Score: 0.50
DE  Interaction: P08736; IntAct: EBI-197839; Score: 0.00
DE  Interaction: Q9VHS2; IntAct: EBI-197843; Score: 0.00
DE  Interaction: Q9VFP2; IntAct: EBI-197847; Score: 0.00
DE  Interaction: Q9XYZ4; IntAct: EBI-509448; Score: 0.00
DE  Interaction: P10987; IntAct: EBI-15859640; Score: 0.76
DE  Interaction: P40793; IntAct: EBI-871870; Score: 0.27
DE  Interaction: P40792; IntAct: EBI-874148; Score: 0.27
DE  Interaction: P48148; IntAct: EBI-874192; Score: 0.27
DE  Interaction: Q95RI5; IntAct: EBI-9941865; Score: 0.50
DE  Interaction: Q99323; IntAct: EBI-9942589; Score: 0.35
DE  Interaction: Q9W542; IntAct: EBI-9942822; Score: 0.35
DE  Interaction: Q9VSW1; IntAct: EBI-9943131; Score: 0.35
DE  Interaction: Q9VH81; IntAct: EBI-9948351; Score: 0.35
DE  Interaction: Q8INK3; IntAct: EBI-9964589; Score: 0.35
DE  Interaction: Q9VHP0; IntAct: EBI-9966138; Score: 0.35
DE  Interaction: Q9VZP5; IntAct: EBI-9967416; Score: 0.35
DE  Interaction: P68135; IntAct: EBI-15859700; Score: 0.81
GO  GO:0005938;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003779;
GO  GO:0008017;
GO  GO:0030036;
GO  GO:0051639;
GO  GO:0007015;
GO  GO:0030041;
GO  GO:0030029;
GO  GO:0045010;
GO  GO:0007304;
GO  GO:0036089;
GO  GO:0051295;
GO  GO:0048193;
GO  GO:0046907;
GO  GO:0030717;
GO  GO:0048477;
GO  GO:0040038;
GO  GO:0007315;
GO  GO:0045451;
GO  GO:0007316;
GO  GO:0015031;
GO  GO:0051493;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:21730168};
SQ  MTEHQAEEQADTPPTKVKATPTPTPSGKFKDAKEDAFLSTSPDSANGDAQHKLPADQLAMSSSAHPQQAGQARPLILQAF
SQ  HRCSSPEQCVTLHDILDSFKAPLSEDQAWALIHQFAGLYHQVAVQAHTCAADYEAALPTGFELHFHRDGSVHFSGPDQLT
SQ  PKEQLQQEQIPLPPQHDVIVDQPDHSASSSGDSSVINRAFDNSNHHHHHQHHHPPLVVSHRKIISELAEIVYTALDYNLP
SQ  EDEECQVSQELENLFNFMTADETDDDCIDEGIDEGDKRWDDESEEERNDTKELEHIIETCRNHIKTTLPENHYRAVCRAL
SQ  VTETIELRVFLQQVLNNEAGAEKLIKASESSATTQQELAKLGFNDWARFWVQVIDELRRGVRLKKSNHERTPIEYELTPY
SQ  EILMGDIRAKKYQLRKVMVNGDIPPRVKKDAHAMILEFIRSRPPLKKASDRQLGPPRMCEPSPREQLMESIRKGKELKQI
SQ  TPPEAPTLRERVLPSANSTLSRSRQRLIKVDFSKFQDDDLFYDENSISSSHSTAATHQHHPHFAEMHRCSQPKMPPYPFG
SQ  GYMVPSQARQDCRETASLMRPRRTMEPAKQVPPPEEPSFTKDEYHKFYDTALESYDLATQCESRRASLRRHTIVGCQSNL
SQ  DETHSMPPTRPESRQSDDVSKETPKRSPAEQTHPSDEGSSTSSLGPWNKSFMDKQTWMERGDDRLSVTLAEIVHIRSVMT
SQ  KAELEGLPMDVRVKEDVEKRRVCFLCLRTRFSFFGPWGIQCKLCQRTVCAKCYTKMRIPSEHFRNVPLVLISPSLLSSPA
SQ  SSSTPSPSHHAQQAHSSSTGNIMDDQFPKSLIERLLRSESDRKTRSTVGSAPSSPKHQRSNMSTPGISVGPGASSSSAAA
SQ  TGQAVEALHDQATMSSSYSAAMRPSGVHQQQKQHYNNAMSRSMEGPRSLPVHSPAYRPLSNNSTLERKSRFSRGFNLFSS
SQ  GSHLAQTQEQKENLRGEQVTVCNDCQGLVNEITSSVKQKRSSARNRTIQNLTLDLTPVWK
//
ID  Q29KT5;
PN  Protein spire;
GN  spir;
OS  46245;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Punctate spots in perinuclear region and cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q29KT5;
DR  Pfam: PF16474;
DR  PROSITE: PS51377;
DR  PROSITE: PS51082;
DE  Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0003779;
GO  GO:0045010;
GO  GO:0022607;
GO  GO:0015031;
GO  GO:0016192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MTEHHMDVQADATQSASESKAMAAPKGKFSEAEEGFLSTSPDSANGDAQQAHTHTHIISHTHSKGAAKTQTQTQNGNGTL
SQ  GMGLGAPMLPGGSRQLLRQAFYQCSCPEQCVTLNNILDSFKAPLSEDQAWALIYQFGSLYYKVAAQAHKSGGDYEADLPS
SQ  RFELHFHRDGNVHFSGAERLPELVESQEQEASQQEQQQKQPQMDDSATSSVDSNAALDRAFDNNNHEHHHHHHHQHHHPV
SQ  DSNAALDRAHHTPLVVSHRKIISEMAEIVYTALDYNLPEDEECQMSQELENLFNFMTADETDEDCIDEGIDEGDKRWDDE
SQ  AEEERNDTKELEHIIETCRNHLQKPALADNHYKAVCRALATETIELRVFLQQVLNNGAEKLIKAAESSPTTQKELAKLGF
SQ  NDWARFWVQVIDELRRGVRLKKSNFERTPIEYELTPYEILMGDIRAKKYQLRKVMVNGDIPPRVKKDAHAMILEFIRSRP
SQ  PLKKASERQLGPPRMCTPTPREQLMESIRQGKELKQITPPEAPPLRQRMLPSANSTLSRSRQRLIKVDFSQLQDDELFFD
SQ  DSSMSSSHSTAATHQHHQQHQPHHAHLAELHRCSQPKMPPYPFGGYMVPSQARQECQATATQLRPRRTMDTSAPRQTLPQ
SQ  PQAQARPPPPAEPSFTEDEYHRFFDNALESYDLATQCESRRASLRRHTIVGCQSNLEETHSMPPTRPESRQSDDAGSQSQ
SQ  SGASSEAPGIRKSPLMEGDHSQTTDGPPRLDEAHSTSSLGPWNKSFMDKQTWMERGDDRLSVTLAEIVHIRSVMTKAELE
SQ  GLPMDVRVKEDVEKRRVCFLCLRTRFSFFGPWGIQCKLCQRTVCAKCYTKMRIPSEHFRNVPLVLISPSLLSSPASSSTP
SQ  SPSHHAHQAHSSSTGNIMDDQFPKSLIERLLRSESDRKTRSTVGSAPSSPKHQRSNMSTPGISVGPGAGASTSAAPGHAV
SQ  EALHDQAAMSASYSSAMRPSGVMQHHQKHHYNNAMSRSMEGPRSLPVHSPAYRPLSNSSTLERKSRFSRGFALFSSGSHL
SQ  AQTQDQKENLRGEQVPVCNDCQGLVNEITSSVKQKRSSARNRTIQNLTLDLTPVWK
//
ID  P53541;
PN  Putative meiotic phospholipase SPO1;
GN  SPO1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.
DR  UNIPROT: P53541;
DR  UNIPROT: D6W1G5;
DR  Pfam: PF01735;
DR  PROSITE: PS51210;
DE  Function: Regulates spindle pole duplication in meiosis I, but not in mitosis. Required for meiosis I, meiosis II chromosome segregation and spore formation. Binds phosphatidylinositol (4)P mono- and polyphosphates. {ECO:0000269|PubMed:10855497, ECO:0000269|PubMed:17179081}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-16283760; Score: 0.35
DE  Interaction: P33757; IntAct: EBI-391428; Score: 0.37
DE  Interaction: P89113; IntAct: EBI-394074; Score: 0.37
DE  Interaction: P53267; IntAct: EBI-517229; Score: 0.37
DE  Interaction: Q07732; IntAct: EBI-8060892; Score: 0.27
DE  Interaction: P11484; IntAct: EBI-3696035; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3730034; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3795751; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-16283760; Score: 0.35
DE  Interaction: P23641; IntAct: EBI-16283760; Score: 0.35
DE  Interaction: P16474; IntAct: EBI-16283760; Score: 0.35
DE  Interaction: P25694; IntAct: EBI-16283760; Score: 0.35
DE  Interaction: P29311; IntAct: EBI-16283760; Score: 0.35
DE  Interaction: P15703; IntAct: EBI-16283760; Score: 0.35
DE  Interaction: P07251; IntAct: EBI-16283760; Score: 0.35
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005576;
GO  GO:0000324;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0005628;
GO  GO:0004623;
GO  GO:0004620;
GO  GO:0032120;
GO  GO:0046475;
GO  GO:0030474;
GO  GO:0070583;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQKLLFVFSVLLTVVLATAPFQVQCPSSPLIREAKHELCPEETLYLKKKKIKTKNKLIQFLKSLTEAKFSSKFYKRVLKD
SQ  PPKIGIAISGGGYRSMLVGTGFISQMNDYGLFEYSDYIAGLSGGSWILMDLVVQNFEVKSLLQEWDLEEDLLLGIPEFDI
SQ  SEEEIVTNAKKEYNDNDLKMKKRQGGSLITSSSNFYEQIEEIMNSIEEIPEDYMITKRNLNPLARLKKIFFPNNTFTGTD
SQ  AKIETFKKVLDFYKSLHLKIKPKKMEGFQISFTDYWGKAIVQRLKKNFDDDPNHSFSFSKLVNSSKKFKECSVPIPIFVA
SQ  NCKNGLLSNVIFEFTPFEFGSWENILRLFVKLPYLGSKIVSGKAEKCINNFDDLGFITATSSSIFNNVLIFIWNLASQSS
SQ  REAMKALNMVMGIFGLGKEEIFSISKDSSRLETDYAVYQPNPFYLYPEKDNVLTNKNHLYLVDGGEDGENIPLRTLVIPE
SQ  RELDVIFVLDSSSDIDNYPNGSKLKRIFEKLDEENVHYQFPNNVKTFTHPIVIGCNATKRTGHDSFLPIIIYHANANHGN
SQ  ASNTSTFKITYNQSEVSSMLPTGRGVFSNDYDLYYKNCLGCILTKRTMDRLPRKKKFSPFCLQCFKDYCYS
//
ID  Q9USQ0;
PN  Sporulation-specific protein spo7;
GN  spo7;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Multi- pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9USQ0;
DR  Pfam: PF03907;
DE  Function: Probable regulatory component of the nem1-spo7 complex which acts as a phosphatase and may be required for proper nuclear membrane morphology. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0019888;
GO  GO:0071072;
GO  GO:0006998;
GO  GO:0023052;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSYVPNTLSVYHNLLILEASFRKTYLQLQVRRQKYMAFYVSLLVWNFYFGYRVFYRISKYSLIDLTYKLCLLCGIVTLL
SQ  LFYFSGLYRTTIVYPSRYVQQVNKAMRFFNIRLVITPVPWFQVRKPLDCGVHLILSSKRFDILVIEGWEAFRSSYFASIH
SQ  RKNNSIQSNESSESPSSKQN
//
ID  P18410;
PN  Sporulation-specific protein SPO7;
GN  SPO7;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9822591}; Multi-pass membrane protein {ECO:0000269|PubMed:9822591}. Nucleus membrane {ECO:0000269|PubMed:9822591}; Multi-pass membrane protein {ECO:0000269|PubMed:9822591}.
DR  UNIPROT: P18410;
DR  UNIPROT: D6VPK9;
DR  Pfam: PF03907;
DE  Function: Regulatory component of the NEM1-SPO7 complex which acts as a phosphatase and dephosphorylates the phosphatidic acid phosphohydrolase PAH1 (PubMed:15889145). Essential for the formation of a spherical nucleus and meiotic division (PubMed:9822591). The NEM1-SPOo7 protein phosphatase is required for efficient mitophagy under prolonged respiration, as well as for reticulophagy and pexophagy (PubMed:29305265). {ECO:0000269|PubMed:15889145, ECO:0000269|PubMed:29305265, ECO:0000269|PubMed:9822591}.
DE  Reference Proteome: Yes;
DE  Interaction: P10664; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P32591; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P05753; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P02407; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P05737; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P05739; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P38757; IntAct: EBI-787710; Score: 0.56
DE  Interaction: P12945; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P32501; IntAct: EBI-787710; Score: 0.35
DE  Interaction: P38631; IntAct: EBI-787710; Score: 0.35
DE  Interaction: Q02772; IntAct: EBI-6317771; Score: 0.00
DE  Interaction: P04821; IntAct: EBI-7299668; Score: 0.44
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0071595;
GO  GO:0031965;
GO  GO:0019888;
GO  GO:0006629;
GO  GO:0071072;
GO  GO:0006998;
GO  GO:1903740;
GO  GO:0071071;
GO  GO:0061709;
GO  GO:0030435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEPESIGDVGNHAQDDSASIVSGPRRRSTSKTSSAKNIRNSSNISPASMIFRNLLILEDDLRRQAHEQKILKWQFTLFLA
SQ  SMAGVGAFTFYELYFTSDYVKGLHRVILQFTLSFISITVVLFHISGQYRRTIVIPRRFFTSTNKGIRQFNVKLVKVQSTW
SQ  DEKYTDSVRFVSRTIAYCNIYCLKKFLWLKDDNAIVKFWKSVTIQSQPRIGAVDVKLVLNPRAFSAEIREGWEIYRDEFW
SQ  AREGARRRKQAHELRPKSE
//
ID  Q0VC82;
PN  Selenide, water dikinase 1;
GN  SEPHS1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: Q0VC82;
DR  Pfam: PF00586;
DR  Pfam: PF02769;
DE  Function: Synthesizes selenophosphate from selenide and ATP. {ECO:0000250|UniProtKB:P49903}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0004756;
GO  GO:0016310;
GO  GO:0016260;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSARESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGL
SQ  SLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVT
SQ  GGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
SQ  MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPET
SQ  SGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS
//
ID  Q7ZW38;
PN  Selenide, water dikinase 1;
GN  sephs1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: Q7ZW38;
DR  UNIPROT: Q1LXT8;
DR  Pfam: PF00586;
DR  Pfam: PF02769;
DE  Function: Synthesizes selenophosphate from selenide and ATP. {ECO:0000250|UniProtKB:P49903}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0004756;
GO  GO:0016310;
GO  GO:0016260;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSVRESFNPESYELDKNFRLTRFTELKGTGCKVPQDVLQKLLESLQENHYQEDEQFLGAVMPRLGIGMDTCVIPLRHGGL
SQ  SLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKLTEKERDKVMPLVIQGFKDASEEAGTSVT
SQ  GGQTVINPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
SQ  MLNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLARQQRTEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPET
SQ  SGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNTTPGATS
//
ID  P49903;
PN  Selenide, water dikinase 1;
GN  SEPHS1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:20471958}; Peripheral membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:20471958}; Peripheral membrane protein {ECO:0000305}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:20471958}. [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:20471958}. [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:20471958}.
DR  UNIPROT: P49903;
DR  UNIPROT: B4DWK0;
DR  UNIPROT: D3DRS9;
DR  UNIPROT: D6PSQ9;
DR  UNIPROT: Q5T5U8;
DR  UNIPROT: Q5T5U9;
DR  UNIPROT: Q9BVT4;
DR  PDB: 3FD5;
DR  PDB: 3FD6;
DR  Pfam: PF00586;
DR  Pfam: PF02769;
DR  OMIM: 600902;
DR  DisGeNET: 22929;
DE  Function: Synthesizes selenophosphate from selenide and ATP. {ECO:0000269|PubMed:7665581}.
DE  Reference Proteome: Yes;
DE  Interaction: P0C6X7; IntAct: EBI-25688150; Score: 0.35
DE  Interaction: P32456; IntAct: EBI-735757; Score: 0.00
DE  Interaction: Q9UKR5; IntAct: EBI-730777; Score: 0.00
DE  Interaction: Q14194; IntAct: EBI-730780; Score: 0.00
DE  Interaction: P21673; IntAct: EBI-733262; Score: 0.00
DE  Interaction: Q8N357; IntAct: EBI-733283; Score: 0.00
DE  Interaction: Q96ID5; IntAct: EBI-733286; Score: 0.00
DE  Interaction: Q13432; IntAct: EBI-733289; Score: 0.00
DE  Interaction: Q96E40; IntAct: EBI-735754; Score: 0.00
DE  Interaction: P49903; IntAct: EBI-758899; Score: 0.80
DE  Interaction: Q9UBN6; IntAct: EBI-1064933; Score: 0.00
DE  Interaction: O60739; IntAct: EBI-1069012; Score: 0.00
DE  Interaction: Q9BXL8; IntAct: EBI-8638900; Score: 0.37
DE  Interaction: P24278; IntAct: EBI-8653789; Score: 0.78
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: Q2TAL8; IntAct: EBI-10211705; Score: 0.72
DE  Interaction: O95125; IntAct: EBI-24494526; Score: 0.56
DE  Interaction: Q9UPG8; IntAct: EBI-24621127; Score: 0.56
DE  Interaction: Q8N554; IntAct: EBI-24667690; Score: 0.56
DE  Interaction: Q8TF50; IntAct: EBI-24391494; Score: 0.56
DE  Interaction: Q6S9Z5; IntAct: EBI-24791955; Score: 0.56
DE  Interaction: Q6GPH4; IntAct: EBI-25266597; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q14774; IntAct: EBI-21809008; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21374426; Score: 0.00
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0005525;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0004756;
GO  GO:0016310;
GO  GO:0036211;
GO  GO:0016260;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSTRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGL
SQ  SLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVT
SQ  GGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
SQ  MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPET
SQ  SGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS
//
ID  Q8BH69;
PN  Selenide, water dikinase 1;
GN  Sephs1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: Q8BH69;
DR  Pfam: PF00586;
DR  Pfam: PF02769;
DE  Function: Synthesizes selenophosphate from selenide and ATP. {ECO:0000250|UniProtKB:P49903}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3U1F9; IntAct: EBI-12603117; Score: 0.40
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0004756;
GO  GO:0016310;
GO  GO:0016260;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSTRESFNPETYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGL
SQ  SLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVIPLIIQGFKDAAEEAGTSVT
SQ  GGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
SQ  MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPET
SQ  SGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS
//
ID  Q5RF87;
PN  Selenide, water dikinase 1;
GN  SEPHS1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: Q5RF87;
DR  Pfam: PF00586;
DR  Pfam: PF02769;
DE  Function: Synthesizes selenophosphate from selenide and ATP. {ECO:0000250|UniProtKB:P49903}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0004756;
GO  GO:0016310;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSTRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGL
SQ  SLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVT
SQ  GGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
SQ  MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPET
SQ  SGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS
//
ID  Q6PF47;
PN  Selenide, water dikinase 1;
GN  sephs1;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: Q6PF47;
DR  Pfam: PF00586;
DR  Pfam: PF02769;
DE  Function: Synthesizes selenophosphate from selenide and ATP. {ECO:0000250|UniProtKB:P49903}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0004756;
GO  GO:0016310;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSVRESFNPESYELDKSFRLTRFAELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGL
SQ  SLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKLTDRERDKVMPLIIQGFKDAAEEAGTSVT
SQ  GGQTVLNPWVVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
SQ  MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGSCPET
SQ  SGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQIATQNVNPTPGATS
//
ID  Q6GL12;
PN  Selenide, water dikinase 1;
GN  sephs1;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:P49903}; Peripheral membrane protein {ECO:0000305}.
DR  UNIPROT: Q6GL12;
DR  Pfam: PF00586;
DR  Pfam: PF02769;
DE  Function: Synthesizes selenophosphate from selenide and ATP. {ECO:0000250|UniProtKB:P49903}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0004756;
GO  GO:0016310;
GO  GO:0016260;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSVRESFNPESYELDKSFRLTRFAELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGL
SQ  SLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKLTDRERDKVMPLIIQGFKDAAEEAGTSVT
SQ  GGQTVLNPWVVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
SQ  MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGSCPET
SQ  SGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVASQNVNPTPGATS
//
ID  Q2YDE2;
PN  Spermatogenesis-associated protein 46;
GN  SPATA46;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q4FZF2}. Note=Located throughout the subacrosomal area. {ECO:0000250|UniProtKB:Q4FZF2}.
DR  UNIPROT: Q2YDE2;
DR  Pfam: PF17734;
DE  Function: Plays a role in spermiogenesis and fertilization. {ECO:0000250|UniProtKB:Q4FZF2}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0030154;
GO  GO:0009566;
GO  GO:0007342;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENFSLLSISGTRISSSALSTLPDIMSSRATSLPDIAKPVLPTEVPSPVQALPPQCPGGVLRHGVHNIVISPDCILGDAP
SQ  NGEQLRWNCTIYRPWFSPYSYFLCKDKESHLETYSFSEVQRDEGQRDSCLPEDTADSVCSSSPSPENTCPREATKKSRPG
SQ  PDTTDSITFQDILMASKWHPAQQNGYKCASCCRLYPTLHSLKSHIKRGFKEGFSCKVYYHKLKTLWYKEQKARPGDRLSL
SQ  GSGQAFR
//
ID  Q5T0L3;
PN  Spermatogenesis-associated protein 46;
GN  SPATA46;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q4FZF2}. Note=Located throughout the subacrosomal area. {ECO:0000250|UniProtKB:Q4FZF2}.
DR  UNIPROT: Q5T0L3;
DR  UNIPROT: Q6X961;
DR  UNIPROT: Q8NEC3;
DR  Pfam: PF17734;
DR  OMIM: 617257;
DR  DisGeNET: 284680;
DE  Function: Plays a role in spermiogenesis and fertilization. {ECO:0000250|UniProtKB:Q4FZF2}.
DE  Reference Proteome: Yes;
DE  Interaction: Q15834; IntAct: EBI-757936; Score: 0.37
DE  Interaction: Q93062; IntAct: EBI-10245259; Score: 0.56
DE  Interaction: Q13077; IntAct: EBI-24285622; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-24509568; Score: 0.56
DE  Interaction: Q9H0I2; IntAct: EBI-22747893; Score: 0.56
DE  Interaction: O43711; IntAct: EBI-24743792; Score: 0.56
DE  Interaction: O76011; IntAct: EBI-24425889; Score: 0.56
DE  Interaction: P50747; IntAct: EBI-24746309; Score: 0.67
DE  Interaction: Q9Y343; IntAct: EBI-21529086; Score: 0.35
DE  Interaction: Q99685; IntAct: EBI-21529086; Score: 0.35
DE  Interaction: Q14C86; IntAct: EBI-21529086; Score: 0.35
DE  Interaction: P48729; IntAct: EBI-21529086; Score: 0.35
DE  Interaction: O15151; IntAct: EBI-21529086; Score: 0.35
DE  Interaction: A2RUC4; IntAct: EBI-21529086; Score: 0.35
DE  Interaction: P02489; IntAct: EBI-25839698; Score: 0.56
DE  Interaction: Q14204; IntAct: EBI-25844382; Score: 0.56
DE  Interaction: Q86V38; IntAct: EBI-25847033; Score: 0.56
DE  Interaction: P31942; IntAct: EBI-25868701; Score: 0.56
DE  Interaction: Q92876; IntAct: EBI-25888311; Score: 0.56
GO  GO:0031965;
GO  GO:0030154;
GO  GO:0009566;
GO  GO:0007342;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENFSLLSISGPPISSSALSAFPDIMFSRATSLPDIAKTAVPTEASSPAQALPPQYQSIIVRQGIQNTALSPDCSLGDTQ
SQ  HGEKLRRNCTIYRPWFSPYSYFVCADKESQLEAYDFPEVQQDEGKWDNCLSEDMAENICSSSSSPENTCPREATKKSRHG
SQ  LDSITSQDILMASRWHPAQQNGYKCVACCRMYPTLDFLKSHIKRGFREGFSCKVYYRKLKALWSKEQKARLGDRLSSGSC
SQ  QAFNSPAEHLRQIGGEAYLCL
//
ID  Q4R7L6;
PN  Spermatogenesis-associated protein 46;
GN  SPATA46;
OS  9541;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q4FZF2}. Note=Located throughout the subacrosomal area. {ECO:0000250|UniProtKB:Q4FZF2}.
DR  UNIPROT: Q4R7L6;
DR  Pfam: PF17734;
DE  Function: Plays a role in spermiogenesis and fertilization. {ECO:0000250|UniProtKB:Q4FZF2}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0030154;
GO  GO:0007342;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENFSLLSISGPPISSSALSAFPDIMFSRATSLPDIAKTAVPTEASSPAQALPPQYQSITVRQGIQNTALSPDCSLGDTQ
SQ  HGEKLRRNCTIYRPWFSPYSYFVCADKESHPEAYDFPEVQQDEGKWDNCLSEDMAESICSSSSSAENTCPREATKKSRHG
SQ  LDSITSQDILMASRWHPAQQNGYKCAACCRMYPTLDFLKSHIKRGFREGFSCKVYYRKLKALWSKEPKAWLGDRLSSGSC
SQ  QAFNSPAEHLR
//
ID  Q4FZF2;
PN  Spermatogenesis-associated protein 46;
GN  Spata46;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:27488028}. Note=Located throughout the subacrosomal area (PubMed:27488028). {ECO:0000269|PubMed:27488028}.
DR  UNIPROT: Q4FZF2;
DR  Pfam: PF17734;
DE  Function: Plays a role in spermiogenesis and fertilization. {ECO:0000269|PubMed:27488028}.
DE  Reference Proteome: Yes;
GO  GO:0031965;
GO  GO:0030154;
GO  GO:0009566;
GO  GO:0007342;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDNYSLLSTPRPRISSSALSAFPDIMSSLATSLPDLGDTQNGEQLRRNCTIYRPWFSPYSYFVCTDKESHLEAYGFPEVD
SQ  REEGRGDNCLLEDVAESVCSSSSSQENTYPREANRKSKHGLDSITSQDILMASKWHPAQQNGYKCASCCRMYPTLHSLKS
SQ  HIKGGFKEGFSCKVYYRKLKTLWGKEQKARTGDRISLGSCQAFK
//
ID  O94875;
PN  Sorbin and SH3 domain-containing protein 2;
GN  SORBS2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16125169, ECO:0000269|PubMed:9211900}. Apical cell membrane {ECO:0000269|PubMed:18559503}. Cell junction, focal adhesion {ECO:0000269|PubMed:18559503}. Cell projection, lamellipodium {ECO:0000269|PubMed:18559503}. Note=Found at the Z-disk sarcomeres, stress fibers, dense bodies and focal adhesion. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells. {ECO:0000269|PubMed:18559503}.
DR  UNIPROT: O94875;
DR  UNIPROT: A6NEK9;
DR  UNIPROT: B3KPQ7;
DR  UNIPROT: B7Z1G5;
DR  UNIPROT: B7Z3X6;
DR  UNIPROT: C9JKV9;
DR  UNIPROT: D3DP62;
DR  UNIPROT: D3DP63;
DR  UNIPROT: E9PAS5;
DR  UNIPROT: E9PAW4;
DR  UNIPROT: G3XAI0;
DR  UNIPROT: H7BXR4;
DR  UNIPROT: J3KNZ5;
DR  UNIPROT: O60592;
DR  UNIPROT: O60593;
DR  UNIPROT: Q96EX0;
DR  PDB: 5VEI;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  Pfam: PF02208;
DR  PROSITE: PS50002;
DR  PROSITE: PS50831;
DR  OMIM: 616349;
DR  DisGeNET: 8470;
DE  Function: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000269|PubMed:12475393, ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:9211900}.
DE  Reference Proteome: Yes;
DE  Interaction: O43426; IntAct: EBI-7818742; Score: 0.56
DE  Interaction: O43707; IntAct: EBI-12689671; Score: 0.60
DE  Interaction: Q9H2E6; IntAct: EBI-311707; Score: 0.37
DE  Interaction: P62258; IntAct: EBI-755740; Score: 0.37
DE  Interaction: Q13177; IntAct: EBI-7976043; Score: 0.52
DE  Interaction: Q13444; IntAct: EBI-7976983; Score: 0.40
DE  Interaction: P63104; IntAct: EBI-7192223; Score: 0.57
DE  Interaction: P31947; IntAct: EBI-7544702; Score: 0.40
DE  Interaction: Q8WX93; IntAct: EBI-7800139; Score: 0.51
DE  Interaction: P00520; IntAct: EBI-8065572; Score: 0.40
DE  Interaction: Q5NGV7; IntAct: EBI-2804174; Score: 0.00
DE  Interaction: A0A5P8YH58; IntAct: EBI-2862289; Score: 0.00
DE  Interaction: P31751; IntAct: EBI-3926549; Score: 0.37
DE  Interaction: Q00987; IntAct: EBI-3932143; Score: 0.37
DE  Interaction: P00533; IntAct: EBI-4397010; Score: 0.55
DE  Interaction: P55055; IntAct: EBI-7261984; Score: 0.37
DE  Interaction: Q92558; IntAct: EBI-6173706; Score: 0.37
DE  Interaction: P31946; IntAct: EBI-8796749; Score: 0.35
DE  Interaction: Q9WMX2; IntAct: EBI-9082089; Score: 0.51
DE  Interaction: O41958; IntAct: EBI-9640881; Score: 0.37
DE  Interaction: A5D8V6; IntAct: EBI-10173612; Score: 0.56
DE  Interaction: O43639; IntAct: EBI-10184809; Score: 0.56
DE  Interaction: O43281; IntAct: EBI-10190873; Score: 0.56
DE  Interaction: V9HW98; IntAct: EBI-10190887; Score: 0.56
DE  Interaction: P42768; IntAct: EBI-10208750; Score: 0.56
DE  Interaction: Q8N5M1; IntAct: EBI-10266530; Score: 0.56
DE  Interaction: Q9H788; IntAct: EBI-10308135; Score: 0.56
DE  Interaction: O94875; IntAct: EBI-24296200; Score: 0.56
DE  Interaction: P62141; IntAct: EBI-10994001; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11004631; Score: 0.35
DE  Interaction: Q9NQW6; IntAct: EBI-11009421; Score: 0.35
DE  Interaction: Q92614; IntAct: EBI-11030093; Score: 0.35
DE  Interaction: O00159; IntAct: EBI-11030803; Score: 0.35
DE  Interaction: P21333; IntAct: EBI-11038784; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q80X90; IntAct: EBI-11053320; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: Q9D6P8; IntAct: EBI-11062262; Score: 0.35
DE  Interaction: Q9JHJ0; IntAct: EBI-11063313; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: Q16643; IntAct: EBI-11080402; Score: 0.35
DE  Interaction: Q00610; IntAct: EBI-11082478; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: Q15691; IntAct: EBI-11091481; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-11092730; Score: 0.35
DE  Interaction: Q9WTI7; IntAct: EBI-11093786; Score: 0.35
DE  Interaction: Q61879; IntAct: EBI-11099615; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-11132927; Score: 0.35
DE  Interaction: P62140; IntAct: EBI-11142496; Score: 0.35
DE  Interaction: Q13191; IntAct: EBI-24291967; Score: 0.56
DE  Interaction: Q9Y2H0; IntAct: EBI-24309435; Score: 0.56
DE  Interaction: O00401; IntAct: EBI-25248174; Score: 0.56
DE  Interaction: Q96N21; IntAct: EBI-23738002; Score: 0.56
DE  Interaction: Q8IZP0; IntAct: EBI-24392341; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-24456579; Score: 0.56
DE  Interaction: O14512; IntAct: EBI-24541810; Score: 0.56
DE  Interaction: O15372; IntAct: EBI-24567139; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q01968; IntAct: EBI-16412116; Score: 0.35
DE  Interaction: E7ELX2; IntAct: EBI-20625922; Score: 0.35
DE  Interaction: O14874; IntAct: EBI-20901264; Score: 0.40
DE  Interaction: P61981; IntAct: EBI-26966879; Score: 0.35
DE  Interaction: Q13443; IntAct: EBI-21225890; Score: 0.44
DE  Interaction: Q9BYB0; IntAct: EBI-26514930; Score: 0.37
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-30828287; Score: 0.44
GO  GO:0015629;
GO  GO:0016324;
GO  GO:0030425;
GO  GO:0005925;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0030018;
GO  GO:0008093;
GO  GO:0042802;
GO  GO:0003723;
GO  GO:0005200;
GO  GO:0008307;
GO  GO:0007015;
GO  GO:0061049;
GO  GO:0007219;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSYYQRPFSPSAYSLPASLNSSIVMQHGTSLDSTDTYPQHAQSLDGTTSSSIPLYRSSEEEKRVTVIKAPHYPGIGPVDE
SQ  SGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDDDTDMYNTPYTYNAGLYNPPYSAQSHPAAKTQTYRPLSKSHSDNSPNA
SQ  FKDASSPVPPPHVPPPVPPLRPRDRSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQHERPASLYQSSIDRSL
SQ  ERPMSSASMASDFRKRRKSEPAVGPPRGLGDQSASRTSPGRVDLPGSSTTLTKSFTSSSPSSPSRAKGGDDSKICPSLCS
SQ  YSGLNGNPSSELDYCSTYRQHLDVPRDSPRAISFKNGWQMARQNAEIWSSTEETVSPKIKSRSCDDLLNDDCDSFPDPKV
SQ  KSESMGSLLCEEDSKESCPMAWGSPYVPEVRSNGRSRIRHRSARNAPGFLKMYKKMHRINRKDLMNSEVICSVKSRILQY
SQ  ESEQQHKDLLRAWSQCSTEEVPRDMVPTRISEFEKLIQKSKSMPNLGDDMLSPVTLEPPQNGLCPKRRFSIEYLLEEENQ
SQ  SGPPARGRRGCQSNALVPIHIEVTSDEQPRAHVEFSDSDQDGVVSDHSDYIHLEGSSFCSESDFDHFSFTSSESFYGSSH
SQ  HHHHHHHHHHRHLISSCKGRCPASYTRFTTMLKHERARHENTEEPRRQEMDPGLSKLAFLVSPVPFRRKKNSAPKKQTEK
SQ  AKCKASVFEALDSALKDICDQIKAEKKRGSLPDNSILHRLISELLPDVPERNSSLRALRRSPLHQPLHPLPPDGAIHCPP
SQ  YQNDCGRMPRSASFQDVDTANSSCHHQDRGGALQDRESPRSYSSTLTDMGRSAPRERRGTPEKEKLPAKAVYDFKAQTSK
SQ  ELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKLTPPEKAQPARPPPPAQPGEIGEAIAKYNFNADTNVELSLR
SQ  KGDRVILLKRVDQNWYEGKIPGTNRQGIFPVSYVEVVKKNTKGAEDYPDPPIPHSYSSDRIHSLSSNKPQRPVFTHENIQ
SQ  GGGEPFQALYNYTPRNEDELELRESDVIDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
//
ID  Q3UTJ2;
PN  Sorbin and SH3 domain-containing protein 2;
GN  Sorbs2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Apical cell membrane {ECO:0000250|UniProtKB:O94875}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O94875}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O94875}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Found at the Z line sarcomeres, stress fibers, dense bodies and focal adhesion. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells. {ECO:0000250, ECO:0000250|UniProtKB:O94875}.
DR  UNIPROT: Q3UTJ2;
DR  UNIPROT: Q3USC6;
DR  UNIPROT: Q80TS1;
DR  UNIPROT: Q8BJL6;
DR  UNIPROT: Q8BJU3;
DR  UNIPROT: Q8BLW9;
DR  UNIPROT: Q8BX47;
DR  UNIPROT: Q8CHU0;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  Pfam: PF02208;
DR  PROSITE: PS50002;
DR  PROSITE: PS50831;
DE  Function: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 (By similarity). May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O94875}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
DE  Interaction: Q80YT7; IntAct: EBI-16732484; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16736255; Score: 0.35
DE  Interaction: P51637; IntAct: EBI-20565496; Score: 0.35
DE  Interaction: A2AKD7; IntAct: EBI-20566393; Score: 0.35
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
DE  Interaction: P16056; IntAct: EBI-27118288; Score: 0.35
GO  GO:0016324;
GO  GO:0005856;
GO  GO:0030425;
GO  GO:0005925;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045202;
GO  GO:0030018;
GO  GO:0042802;
GO  GO:0019904;
GO  GO:0095500;
GO  GO:0007015;
GO  GO:0061049;
GO  GO:0007219;
GO  GO:1904393;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNTDSGGCARKRAAMSVTLTSVKRVQSSPNLLAAGRESQSPDSAWRSYNDRNPETLNGDATYSSLAAKGFRSVRPNLQDK
SQ  RSPTQSQITINGNSGGAVSPVSYYQRPFSPSAYSLPASLNSSIIMQHGRSLDSAETYSQHAQSLDGTMGSSIPLYRSSEE
SQ  EKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPGLYNSPYSAQSHPAAKTQTYRPLSKSHSD
SQ  NGTDAFKEVPSPVPPPHVPPRPRDQSSTLKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQHERPVSIYQSSIDRSL
SQ  ERPSSSASMAGDFRKRRKSEPAVGPLRGLGDQSSSRTSPGRADLPGSSSTFTKSFISSSPSSPSRAQGGDDSKMCPPLCS
SQ  YSGLNGTPSGELECCNAYRQHLDVPGDSQRAITFKNGWQMARQNAEIWSSTEETVSPKIKSRSCDDLLNDDCDSFPDPKT
SQ  KSESMGSLLCEEDSKESCPMTWASPYIQEVCGNSRSRLKHRSAHNAPGFLKMYKKMHRINRKDLMNSEVICSVKSRILQY
SQ  EKEQQHRGLLHGWSQSSTEEVPRDVVPTRISEFEKLIQKSKSMPNLGDEMLSPITLEPPQNGLCPKRRFSIESLLEEETQ
SQ  VRHPSQGQRSCKSNTLVPIHIEVTSDEQPRTHMEFSDSDQDGVVSDHSDYVHVEGSSFCSESDFDHFSFTSSESFYGSSH
SQ  HHHHHHHHHRHLISSCKGRCPASYTRFTTMLKHERAKHENMDRPRRQEMDPGLSKLAFLVSPVPFRRKKILTPQKQTEKA
SQ  KCKASVVEALDSALKDICDQIKAEKRRGSLPDNSILHRLISELLPQIPERNSSLHALKRSPMHQPFHPLPPDGASHCPLY
SQ  QNDCGRMPHSASFPDVDTTSNYHAQDYGSALSLQDHESPRSYSSTLTDLGRSASRERRGTPEKEKLPAKAVYDFKAQTSK
SQ  ELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKLTPPEKAQPARPPPPVQPGEIGEAIAKYNFNADTNVELSLR
SQ  KGDRIILLKRVDQNWYEGKIPGTNRQGIFPVSYVEVVKRNAKGAEDYPDPPLPHSYSSDRIYTLSSNKPQRPGFSHENIQ
SQ  GGGEPFQALYNYTPRNEDELELRESDVVDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
//
ID  P28220;
PN  Sorbin;
GN  SORBS2;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O94875}. Apical cell membrane {ECO:0000250|UniProtKB:O94875}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O94875}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O94875}. Note=Detected in the stress fibers, synaptosomal cytosol, postsynaptic density fraction, Z-disks and intercalated. The CBL/PTK2B/ARGBP2 complex is recruited to lipid rafts following growth factor stimulation. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells. {ECO:0000250|UniProtKB:O94875}.
DR  UNIPROT: P28220;
DR  UNIPROT: Q95ME6;
DR  Pfam: PF02208;
DR  PROSITE: PS50831;
DE  Function: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 or with AKT1 and PAK1, thus mediating AKT1-mediated activation of PAK1 (By similarity). May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12. Increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000250|UniProtKB:O35413, ECO:0000250|UniProtKB:O94875}.
DE  Reference Proteome: Yes;
GO  GO:0016324;
GO  GO:0030425;
GO  GO:0005925;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0045202;
GO  GO:0007015;
GO  GO:0007219;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRAATPLQTVDRPKDWYKTMFKQIHMVHKPDDDTDMYNTPYTYNAGLYNSPYSAQSHPAAKTQTYRPLSKSHSDNGTDAF
SQ  KDASSPVPPPHVPPPVPPLRPRDRSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQHERPVTKPQAGRRKV
//
ID  O35413;
PN  Sorbin and SH3 domain-containing protein 2;
GN  Sorbs2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10521485, ECO:0000269|PubMed:15128873, ECO:0000269|PubMed:15659545, ECO:0000269|PubMed:16125169}. Apical cell membrane {ECO:0000250|UniProtKB:O94875}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O94875}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O94875}. Note=Detected in the stress fibers, synaptosomal cytosol, postsynaptic density fraction, Z-disks and intercalated. The CBL/PTK2B/ARGBP2 complex is recruited to lipid rafts following growth factor stimulation. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells. {ECO:0000250|UniProtKB:O94875}.
DR  UNIPROT: O35413;
DR  UNIPROT: Q923T8;
DR  Pfam: PF00018;
DR  Pfam: PF14604;
DR  Pfam: PF02208;
DR  PROSITE: PS50002;
DR  PROSITE: PS50831;
DE  Function: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 (By similarity). May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (By similarity). Isoform 2 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000250, ECO:0000250|UniProtKB:O94875, ECO:0000269|PubMed:10521485}.
DE  Reference Proteome: Yes;
DE  Interaction: Q62910; IntAct: EBI-7458056; Score: 0.40
DE  Interaction: P16086; IntAct: EBI-7458130; Score: 0.40
DE  Interaction: P21575; IntAct: EBI-7458357; Score: 0.59
DE  Interaction: P39052; IntAct: EBI-7458445; Score: 0.40
DE  Interaction: Q9WVJ4; IntAct: EBI-7458481; Score: 0.40
DE  Interaction: Q5FWU0; IntAct: EBI-7458532; Score: 0.40
DE  Interaction: P49286; IntAct: EBI-11578506; Score: 0.00
DE  Interaction: Q5XIE8; IntAct: EBI-26439741; Score: 0.35
GO  GO:0016324;
GO  GO:0030425;
GO  GO:0005925;
GO  GO:0030027;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0014069;
GO  GO:0045202;
GO  GO:0019904;
GO  GO:0095500;
GO  GO:0007015;
GO  GO:0061049;
GO  GO:0007219;
GO  GO:1904393;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNTDSGGCARKRAAMSVTLTSVKRVQSSPNLLAAGRESHSPDSAWRSYNGRNPETLNGDATYSSLAAKGFRSVRPNLQDK
SQ  KSPTQSHITINGNSGGAVSPVSYYQRPFSPSAYSLPASLNSSIIMPHGRSLDSAETYSQHAQSLDGTMGSSIPLYRSSEE
SQ  EKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDEDTDMYNTPYTYNAGLYNSPYSAQSHPA
SQ  AKTQTYRPLSKSHSDNGTDAFKEATSPVPPPHVPPRPRDQSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQH
SQ  ERPVSVYQSSIDRSLERPSSSASMAGDFRKRRKSEPAVGPPRGLGDHSSSRTSPGRADLPGSSSTFTTSFISSSPSSPSR
SQ  AQGGDDSKMCPPLCSYSGLNGSPSSELECCGAYRRHLDVPQDSQRAITFKNGWQMARQNAEIWSSTEEAVSPKIKSRSCD
SQ  DLLNDDCGSFPDPKTKSESMGSLLCDEGSKESDPMTWTSPYIPEVCGNSRSRLKHRSAHNAPGFLKMYKKMHRINRKDLM
SQ  NSEVICSVKSRILQYEKEQQHRGLLHGWSQSSTEEVPRDVVPTRISEFEKLIQKSKSMPNLGDEMLSPVTLEPPQNGLCP
SQ  KRRFSIESLLEEETQVRHPSQGQRSCKSNTLVPIHIEVTSDEQPRTHMEFSDSDQDGVVSDHSDNVHVERSSFCSESDFD
SQ  HFSFTSSESFYGSSHHHHHHHHHHGHFISSCKGRCPASYTRFTTMLKHERAKHENIDRPRRQDMDPGLSKLAFLVSPVPF
SQ  RRKKVLTPQKQTEQAKCKASVVEALDSALKDICDQIKAEKRRGSLPDNSILHRLISELLPQIPKRNSSLNALKRSPMHQP
SQ  FHPLPQDGAIHCPLYQNDCGRMPHSASFPDVDTTSSYHAQDYGSVLSLQDHESPRSYSSTLTDLGRSVSRERRGTPEKEV
SQ  KLPAKAVYDFKAQTSKELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKLTPPEKAQPARPPPPVQPGEIGEAI
SQ  AKYNFNADTNVELSLRKGDRIILLKRVDQNWYEGKIPGTNRQGIFPVSYVEVVKRNTKGSEDYPDPPLPHSYSSDRIYSL
SQ  SSNKPQRPVFSHENIQGGGEPFQALYNYTPRNEDELELRESDVVDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
//
ID  Q03707;
PN  Inner nuclear membrane protein SRC1;
GN  SRC1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16929305}; Multi-pass membrane protein {ECO:0000269|PubMed:16929305}. Note=Targeting to the inner nuclear membrane requires the SRP1 and KAP95 karyopherins and the Ran cycle.
DR  UNIPROT: Q03707;
DR  UNIPROT: D6VZE1;
DR  UNIPROT: Q03712;
DR  PDB: 4XZR;
DR  Pfam: PF12949;
DR  Pfam: PF09402;
DE  Function: Plays a role in sister chromatid separation. {ECO:0000269|PubMed:11754482}.
DE  Reference Proteome: Yes;
DE  Interaction: P25491; IntAct: EBI-3766672; Score: 0.35
DE  Interaction: P38181; IntAct: EBI-10052689; Score: 0.37
DE  Interaction: P39929; IntAct: EBI-10052658; Score: 0.37
DE  Interaction: Q02821; IntAct: EBI-16159762; Score: 0.68
DE  Interaction: P48510; IntAct: EBI-394272; Score: 0.37
DE  Interaction: Q03406; IntAct: EBI-394275; Score: 0.37
DE  Interaction: Q12159; IntAct: EBI-795996; Score: 0.35
DE  Interaction: Q12066; IntAct: EBI-795996; Score: 0.35
DE  Interaction: Q12213; IntAct: EBI-795996; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-795996; Score: 0.35
DE  Interaction: P53141; IntAct: EBI-7762064; Score: 0.40
DE  Interaction: Q06485; IntAct: EBI-8221070; Score: 0.22
DE  Interaction: Q04087; IntAct: EBI-2212766; Score: 0.40
DE  Interaction: P25651; IntAct: EBI-2212775; Score: 0.40
DE  Interaction: P80667; IntAct: EBI-7340507; Score: 0.31
DE  Interaction: P10591; IntAct: EBI-3773694; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3784072; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3791828; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3795791; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3801877; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3807844; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3826087; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3829680; Score: 0.35
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0034399;
GO  GO:0003682;
GO  GO:0034087;
GO  GO:0043007;
GO  GO:0000070;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSDLEYLEDGFDPNSMKVATLRRILVENNVDFPSNARKNALVGLFDEKVKPQIPQLRKMYLNVRPSDEGIVKMDRPSSS
SQ  PSIASPRRSRRARREKSASPMAKQFKKNRILDDVSNDDDDDDDDDDDNDKKDDPLIVPSGTDTDEVDDEEDDVITSSSNK
SQ  SDTNDFQQNSDTRKKRKDPDSDDWSESNSKENKIDNKHLNLLSSDSEIEQDYQKAKKRKTSDLNQEHGNGSAILGKLSVK
SQ  TPIKNTNRKPVSMDNFNDSLTSSGTENDPFVPNIRHNPKELGTANGTGHSTPLSKLKVSASFADKLPQKEVPSTILVPEV
SQ  EQQEPSQSERTPSLFSSEGSGSESEAPLLPEITTPGPHQPMGNTSNNVVEMIDTDSSNLVSDEDEVLVPTRIETPQLPTE
SQ  KDVEKCEARVQELQEEVNEQLEHENGSEFDVKQGSGKVGNRHKFKRALKFLSKSLLALFLFCIFIVIPLLFGLWYREQRL
SQ  LIGYCGHEVPSHRVSGNSFEFIQKLDNLLQDYRPKCIPCPPNGICYPYLKLKCKPDYKLAPSRLDFLEIIPAQGKCVKDD
SQ  KKQQLVSEVVEKSLEFLRAKNAQISCGDGKDDIESGMTEDALYQIFNEARAPWIRDDEFEDLWIQVIKDLTEEPEILWRQ
SQ  LSPTDNNIGGNSNNIIKTNDVPRQKRHLPEKFISKTRNFRSTSKKYIGMKCRFEREIYQTYKKFQRPIWLMFLLIVISKV
SQ  IEIKLKNYYRKKARIEELVTQTMEKLKFQKIKSMSDPKENAYLSIVQLRDIFLSDIVDLKYKNQLWSEVVKYLEHNNSNI
SQ  KSNLTEIRGEIMKCWEWIGPMELNEPKDSAENKI
//
ID  P00523;
PN  Proto-oncogene tyrosine-protein kinase Src;
GN  SRC;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:1378446, ECO:0000269|PubMed:8325872}; Lipid-anchor {ECO:0000250|UniProtKB:P05480}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05480}. Endosome membrane {ECO:0000269|PubMed:1378446}; Peripheral membrane protein {ECO:0000269|PubMed:1378446}. Nucleus {ECO:0000269|PubMed:8550628}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8325872}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P05480}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P12931}. Note=Localizes to focal adhesion sites following integrin engagement (By similarity). Localization to focal adhesion sites requires myristoylation and the SH3 domain. {ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:P12931}.
DR  UNIPROT: P00523;
DR  UNIPROT: Q90992;
DR  UNIPROT: Q90993;
DR  UNIPROT: Q91343;
DR  UNIPROT: Q91345;
DR  UNIPROT: Q92013;
DR  UNIPROT: Q98915;
DR  PDB: 1F1W;
DR  PDB: 1F2F;
DR  PDB: 1NLO;
DR  PDB: 1NLP;
DR  PDB: 1P13;
DR  PDB: 1PRL;
DR  PDB: 1PRM;
DR  PDB: 1RLP;
DR  PDB: 1RLQ;
DR  PDB: 1SRL;
DR  PDB: 1SRM;
DR  PDB: 2HWO;
DR  PDB: 2HWP;
DR  PDB: 2OIQ;
DR  PDB: 2PTK;
DR  PDB: 2QI8;
DR  PDB: 2QLQ;
DR  PDB: 2QQ7;
DR  PDB: 3D7T;
DR  PDB: 3D7U;
DR  PDB: 3DQW;
DR  PDB: 3DQX;
DR  PDB: 3EL7;
DR  PDB: 3EL8;
DR  PDB: 3EN4;
DR  PDB: 3EN5;
DR  PDB: 3EN6;
DR  PDB: 3EN7;
DR  PDB: 3F3T;
DR  PDB: 3F3U;
DR  PDB: 3F3V;
DR  PDB: 3F3W;
DR  PDB: 3F6X;
DR  PDB: 3FJ5;
DR  PDB: 3G5D;
DR  PDB: 3G6G;
DR  PDB: 3G6H;
DR  PDB: 3GEQ;
DR  PDB: 3LOK;
DR  PDB: 3OEZ;
DR  PDB: 3OF0;
DR  PDB: 3QLF;
DR  PDB: 3QLG;
DR  PDB: 3SVV;
DR  PDB: 3TZ7;
DR  PDB: 3TZ8;
DR  PDB: 3TZ9;
DR  PDB: 3U4W;
DR  PDB: 3U51;
DR  PDB: 3UQF;
DR  PDB: 3UQG;
DR  PDB: 4AGW;
DR  PDB: 4DGG;
DR  PDB: 4FIC;
DR  PDB: 4HVU;
DR  PDB: 4HVV;
DR  PDB: 4HVW;
DR  PDB: 4JZ3;
DR  PDB: 4JZ4;
DR  PDB: 4LE9;
DR  PDB: 4LGG;
DR  PDB: 4LGH;
DR  PDB: 4MCV;
DR  PDB: 4O2P;
DR  PDB: 4OML;
DR  PDB: 4OMM;
DR  PDB: 4OMN;
DR  PDB: 4OMO;
DR  PDB: 4OMP;
DR  PDB: 4OMQ;
DR  PDB: 4QT7;
DR  PDB: 4RTU;
DR  PDB: 4RTV;
DR  PDB: 4RTW;
DR  PDB: 4RTX;
DR  PDB: 4RTY;
DR  PDB: 4RTZ;
DR  PDB: 4U5J;
DR  PDB: 4YBJ;
DR  PDB: 4YBK;
DR  PDB: 5BMM;
DR  PDB: 5D10;
DR  PDB: 5D11;
DR  PDB: 5D12;
DR  PDB: 5EC7;
DR  PDB: 5ECA;
DR  PDB: 5I11;
DR  PDB: 5J5S;
DR  PDB: 5K9I;
DR  PDB: 5OAV;
DR  PDB: 5OB0;
DR  PDB: 5OB1;
DR  PDB: 5OB2;
DR  PDB: 5SWH;
DR  PDB: 5SYS;
DR  PDB: 5T0P;
DR  PDB: 5TEH;
DR  PDB: 5XP5;
DR  PDB: 5XP7;
DR  PDB: 6HVE;
DR  PDB: 6HVF;
DR  PDB: 6L8L;
DR  PDB: 6WIW;
DR  PDB: 6XVM;
DR  PDB: 6XVN;
DR  PDB: 6XVO;
DR  PDB: 6XX2;
DR  PDB: 6XX3;
DR  PDB: 6XX4;
DR  PDB: 6XX5;
DR  PDB: 7A30;
DR  PDB: 7A31;
DR  PDB: 7A32;
DR  PDB: 7A33;
DR  PDB: 7A34;
DR  PDB: 7A35;
DR  PDB: 7A36;
DR  PDB: 7A37;
DR  PDB: 7A38;
DR  PDB: 7A39;
DR  PDB: 7A3A;
DR  PDB: 7A3B;
DR  PDB: 7A3C;
DR  PDB: 7A3D;
DR  PDB: 7A3E;
DR  PDB: 7AH3;
DR  PDB: 7D57;
DR  PDB: 7D5O;
DR  PDB: 7NER;
DR  PDB: 7NES;
DR  PDB: 7NET;
DR  PDB: 7WF5;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DE  Function: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (PubMed:1717492, PubMed:8550628). Involved in anchorage-independent cell growth (PubMed:19307596). {ECO:0000250|UniProtKB:P12931, ECO:0000269|PubMed:1717492, ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:8550628, ECO:0000305|PubMed:11964124, ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}.
DE  Reference Proteome: Yes;
DE  Interaction: Q07666; IntAct: EBI-8561516; Score: 0.44
DE  Interaction: P29353; IntAct: EBI-8561584; Score: 0.44
DE  Interaction: P61980; IntAct: EBI-8561566; Score: 0.54
DE  Interaction: Q9QWY8; IntAct: EBI-848034; Score: 0.58
DE  Interaction: O97902; IntAct: EBI-848183; Score: 0.44
DE  Interaction: Q9QWI6; IntAct: EBI-2658391; Score: 0.40
DE  Interaction: P41240; IntAct: EBI-1800285; Score: 0.72
DE  Interaction: Q9NZA1; IntAct: EBI-8566694; Score: 0.40
DE  Interaction: O88703; IntAct: EBI-7729832; Score: 0.58
DE  Interaction: Q13094; IntAct: EBI-7643746; Score: 0.40
DE  Interaction: Q8IZP0; IntAct: EBI-8050329; Score: 0.44
DE  Interaction: P18052; IntAct: EBI-6956234; Score: 0.52
DE  Interaction: P18433; IntAct: EBI-7205200; Score: 0.59
DE  Interaction: P03372; IntAct: EBI-7411101; Score: 0.56
DE  Interaction: P15311; IntAct: EBI-7453484; Score: 0.35
DE  Interaction: Q90738; IntAct: EBI-8690413; Score: 0.56
DE  Interaction: Q07954; IntAct: EBI-7457866; Score: 0.44
DE  Interaction: O75051; IntAct: EBI-6510192; Score: 0.35
DE  Interaction: P49615; IntAct: EBI-6510183; Score: 0.40
DE  Interaction: Q9Y4D1; IntAct: EBI-6550665; Score: 0.56
DE  Interaction: Q00944; IntAct: EBI-6861774; Score: 0.59
DE  Interaction: Q16543; IntAct: EBI-9362141; Score: 0.40
GO  GO:0030054;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0016020;
GO  GO:0005743;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0005524;
GO  GO:0071253;
GO  GO:0070851;
GO  GO:0020037;
GO  GO:0004715;
GO  GO:0019903;
GO  GO:0004713;
GO  GO:0005102;
GO  GO:0045453;
GO  GO:0007155;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0007173;
GO  GO:0045087;
GO  GO:2001237;
GO  GO:2001243;
GO  GO:0036035;
GO  GO:0050847;
GO  GO:0051726;
GO  GO:0007169;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALA
SQ  GGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESER
SQ  LLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHR
SQ  LTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE
SQ  KLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVC
SQ  KVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYR
SQ  MPCPPECPESLHDLMCQCWRKDPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
//
ID  Q1JPZ3;
PN  Proto-oncogene tyrosine-protein kinase Src;
GN  src;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P00523}; Lipid-anchor {ECO:0000250|UniProtKB:P05480}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05480}. Nucleus {ECO:0000250|UniProtKB:P00523}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P00523}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P05480}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P12931}. Note=Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain. {ECO:0000250|UniProtKB:P12931}.
DR  UNIPROT: Q1JPZ3;
DR  UNIPROT: Q6EWH0;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DE  Function: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each src kinase is very difficult. Src appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of src to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including ptk2/fak1 and paxillin (pxn) (By similarity). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Involved in anchorage-independent cell growth (By similarity). {ECO:0000250|UniProtKB:P12931, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0030054;
GO  GO:0005856;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0005743;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0070851;
GO  GO:0004715;
GO  GO:0004713;
GO  GO:0005102;
GO  GO:0045453;
GO  GO:0007155;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0007173;
GO  GO:0045087;
GO  GO:2001237;
GO  GO:2001243;
GO  GO:0036035;
GO  GO:0050847;
GO  GO:0043114;
GO  GO:0001878;
GO  GO:0007169;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGGVKSKPKELGQRSRSLDDGTGGHHHHTPNPTSFTPNRSPPVEGSRRGTQPNIINAEQALFGGVNSTTNSITSPNRIGI
SQ  LGGVTTFVALYDYESRTASDLSFRKGERLQIVNNTEGDWWLARSLTTGESGYIPSNYVAPSDSIQAEEWYFGKITRRDSE
SQ  RLLLNLENRRGTFLVRESETTKGAYCLSVLDYDNVKGLNVKHYKIRKLDSGGFYITSRTQFSTLQQLVNHYRQHADGLCH
SQ  SLTDVCPVLKPPTQGLARDAWEIPRDSLRLDVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRH
SQ  EKLVQLYAVVSEEPIYIVTEYMGQGSLLDFLKGDMGKMLRLPQLVDMASQIASGMAYVERMNYVHRDLRAANILVGDNLV
SQ  CKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGY
SQ  RMPCPAECPDSLHELMLTCWRKEPEERPTFEYLQGFLEDYFTSTEPQYQPGENL
//
ID  P12931;
PN  Proto-oncogene tyrosine-protein kinase Src;
GN  SRC;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:7525268}; Lipid-anchor {ECO:0000269|PubMed:22801373}. Mitochondrion inner membrane {ECO:0000269|PubMed:12615910}. Nucleus {ECO:0000269|PubMed:7853507}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7525268}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19307596}. Cell junction, focal adhesion {ECO:0000269|PubMed:22801373}. Note=Localizes to focal adhesion sites following integrin engagement (PubMed:22801373). Localization to focal adhesion sites requires myristoylation and the SH3 domain (PubMed:7525268). Colocalizes with PDLIM4 at the perinuclear region, but not at focal adhesions (PubMed:19307596). {ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:22801373, ECO:0000269|PubMed:7525268}.
DR  UNIPROT: P12931;
DR  UNIPROT: E1P5V4;
DR  UNIPROT: Q76P87;
DR  UNIPROT: Q86VB9;
DR  UNIPROT: Q9H5A8;
DR  PDB: 1A07;
DR  PDB: 1A08;
DR  PDB: 1A09;
DR  PDB: 1A1A;
DR  PDB: 1A1B;
DR  PDB: 1A1C;
DR  PDB: 1A1E;
DR  PDB: 1FMK;
DR  PDB: 1HCS;
DR  PDB: 1HCT;
DR  PDB: 1KSW;
DR  PDB: 1O41;
DR  PDB: 1O42;
DR  PDB: 1O43;
DR  PDB: 1O44;
DR  PDB: 1O45;
DR  PDB: 1O46;
DR  PDB: 1O47;
DR  PDB: 1O48;
DR  PDB: 1O49;
DR  PDB: 1O4A;
DR  PDB: 1O4B;
DR  PDB: 1O4C;
DR  PDB: 1O4D;
DR  PDB: 1O4E;
DR  PDB: 1O4F;
DR  PDB: 1O4G;
DR  PDB: 1O4H;
DR  PDB: 1O4I;
DR  PDB: 1O4J;
DR  PDB: 1O4K;
DR  PDB: 1O4L;
DR  PDB: 1O4M;
DR  PDB: 1O4N;
DR  PDB: 1O4O;
DR  PDB: 1O4P;
DR  PDB: 1O4Q;
DR  PDB: 1O4R;
DR  PDB: 1SHD;
DR  PDB: 1Y57;
DR  PDB: 1YI6;
DR  PDB: 1YOJ;
DR  PDB: 1YOL;
DR  PDB: 1YOM;
DR  PDB: 2BDF;
DR  PDB: 2BDJ;
DR  PDB: 2H8H;
DR  PDB: 2SRC;
DR  PDB: 3VRO;
DR  PDB: 3ZMP;
DR  PDB: 3ZMQ;
DR  PDB: 4F59;
DR  PDB: 4F5A;
DR  PDB: 4F5B;
DR  PDB: 4HXJ;
DR  PDB: 4K11;
DR  PDB: 4MXO;
DR  PDB: 4MXX;
DR  PDB: 4MXY;
DR  PDB: 4MXZ;
DR  PDB: 6ATE;
DR  PDB: 6C4S;
DR  PDB: 6E6E;
DR  PDB: 6EHJ;
DR  PDB: 7NG7;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DR  OMIM: 190090;
DR  OMIM: 616937;
DR  DisGeNET: 6714;
DE  Function: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (PubMed:21411625). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell- cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1 (PubMed:11389730). Plays a role in EGF-mediated calcium- activated chloride channel activation (PubMed:18586953). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr- 1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta- arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (PubMed:7853507). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC- PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:8755529, PubMed:14585963). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750). Enhances DDX58/RIG-I-elicited antiviral signaling (PubMed:19419966). Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates BCAR1 at 'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity (PubMed:20525694). Phosphorylates synaptic vesicle protein synaptophysin (SYP) (By similarity). Involved in anchorage-independent cell growth (PubMed:19307596). Required for podosome formation (By similarity). Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration (PubMed:25731159). {ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:Q9WUD9, ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:18586953, ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:21309750, ECO:0000269|PubMed:21411625, ECO:0000269|PubMed:22710723, ECO:0000269|PubMed:25731159, ECO:0000269|PubMed:7853507, ECO:0000269|PubMed:8755529, ECO:0000269|PubMed:8759729, ECO:0000305|PubMed:11964124, ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}. [Isoform 1]: Non-receptor protein tyrosine kinase which phosphorylates synaptophysin with high affinity. {ECO:0000250|UniProtKB:Q9WUD9}. [Isoform 2]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr- 419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in L1CAM-mediated neurite elongation, possibly by acting downstream of L1CAM to drive cytoskeletal rearrangements involved in neurite outgrowth (By similarity). {ECO:0000250|UniProtKB:Q9WUD9}. [Isoform 3]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr- 419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in neurite elongation (By similarity). {ECO:0000250|UniProtKB:Q9WUD9}.
DE  Disease: Note=SRC kinase activity has been shown to be increased in several tumor tissues and tumor cell lines such as colon carcinoma cells. {ECO:0000269|PubMed:2498394, ECO:0000269|PubMed:3093483}. Thrombocytopenia 6 (THC6) [MIM:616937]: A form of thrombocytopenia, a hematologic disorder defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. THC6 is an autosomal dominant form. Affected individuals may also have bone abnormalities and an increased risk for myelofibrosis. {ECO:0000269|PubMed:26936507}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O43707; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P00519; IntAct: EBI-7286298; Score: 0.59
DE  Interaction: P00533; IntAct: EBI-7248693; Score: 0.90
DE  Interaction: P01112; IntAct: EBI-8633225; Score: 0.57
DE  Interaction: P04626; IntAct: EBI-8289901; Score: 0.71
DE  Interaction: P07948; IntAct: EBI-11359552; Score: 0.67
DE  Interaction: P0DTD1; IntAct: EBI-27092586; Score: 0.44
DE  Interaction: P25962; IntAct: EBI-7406154; Score: 0.54
DE  Interaction: P15941; IntAct: EBI-7913825; Score: 0.75
DE  Interaction: P17302; IntAct: EBI-7413469; Score: 0.35
DE  Interaction: Q16832; IntAct: EBI-8168082; Score: 0.40
DE  Interaction: Q03135; IntAct: EBI-8675931; Score: 0.32
DE  Interaction: Q02248; IntAct: EBI-8624542; Score: 0.44
DE  Interaction: Q8R5G7; IntAct: EBI-621510; Score: 0.56
DE  Interaction: Q9H5V8; IntAct: EBI-7606952; Score: 0.79
DE  Interaction: Q05655; IntAct: EBI-7607017; Score: 0.40
DE  Interaction: Q05193; IntAct: EBI-7591679; Score: 0.44
DE  Interaction: P50570; IntAct: EBI-7591812; Score: 0.44
DE  Interaction: Q60749; IntAct: EBI-697861; Score: 0.44
DE  Interaction: Q9Y6K9; IntAct: EBI-697929; Score: 0.50
DE  Interaction: O15111; IntAct: EBI-697951; Score: 0.35
DE  Interaction: O14920; IntAct: EBI-697951; Score: 0.35
DE  Interaction: Q07666; IntAct: EBI-2437436; Score: 0.57
DE  Interaction: Q8WUM4; IntAct: EBI-7397413; Score: 0.65
DE  Interaction: P03407; IntAct: EBI-7355101; Score: 0.40
DE  Interaction: Q9QPN3; IntAct: EBI-7355187; Score: 0.40
DE  Interaction: P04604; IntAct: EBI-7355423; Score: 0.40
DE  Interaction: P21860; IntAct: EBI-7885161; Score: 0.44
DE  Interaction: P52800; IntAct: EBI-8107779; Score: 0.40
DE  Interaction: P12814; IntAct: EBI-968854; Score: 0.52
DE  Interaction: Q05397; IntAct: EBI-968957; Score: 0.92
DE  Interaction: Q90VU7; IntAct: EBI-7975353; Score: 0.40
DE  Interaction: Q13177; IntAct: EBI-7975714; Score: 0.52
DE  Interaction: Q13444; IntAct: EBI-7976357; Score: 0.75
DE  Interaction: O15455; IntAct: EBI-8580898; Score: 0.46
DE  Interaction: P09848; IntAct: EBI-7047891; Score: 0.44
DE  Interaction: P06241; IntAct: EBI-6967679; Score: 0.56
DE  Interaction: P42227; IntAct: EBI-1163828; Score: 0.44
DE  Interaction: Q63767; IntAct: EBI-1176840; Score: 0.44
DE  Interaction: P22681; IntAct: EBI-7146896; Score: 0.84
DE  Interaction: P07550; IntAct: EBI-7173594; Score: 0.61
DE  Interaction: P12931; IntAct: EBI-7173747; Score: 0.44
DE  Interaction: P46527; IntAct: EBI-1200966; Score: 0.44
DE  Interaction: Q9H204; IntAct: EBI-1206815; Score: 0.66
DE  Interaction: P55196; IntAct: EBI-7407779; Score: 0.65
DE  Interaction: Q9C0H9; IntAct: EBI-2658373; Score: 0.40
DE  Interaction: P41240; IntAct: EBI-2658427; Score: 0.40
DE  Interaction: Q9QWI6; IntAct: EBI-2658513; Score: 0.40
DE  Interaction: Q9ULH1; IntAct: EBI-1960274; Score: 0.61
DE  Interaction: Q92988; IntAct: EBI-1960262; Score: 0.40
DE  Interaction: Q8IZD9; IntAct: EBI-1960286; Score: 0.40
DE  Interaction: O15360; IntAct: EBI-1960310; Score: 0.40
DE  Interaction: P43699; IntAct: EBI-1960322; Score: 0.40
DE  Interaction: O75167; IntAct: EBI-1960334; Score: 0.40
DE  Interaction: Q9P1A6; IntAct: EBI-1960358; Score: 0.40
DE  Interaction: Q15036; IntAct: EBI-1960382; Score: 0.40
DE  Interaction: Q9Y2H0; IntAct: EBI-1960370; Score: 0.40
DE  Interaction: O43918; IntAct: EBI-1960394; Score: 0.40
DE  Interaction: O95886; IntAct: EBI-1960406; Score: 0.40
DE  Interaction: Q9NQC3; IntAct: EBI-1960418; Score: 0.40
DE  Interaction: O43150; IntAct: EBI-1960430; Score: 0.40
DE  Interaction: Q9NQ76; IntAct: EBI-1960442; Score: 0.40
DE  Interaction: Q9Y2J2; IntAct: EBI-1960454; Score: 0.40
DE  Interaction: P20810; IntAct: EBI-1960466; Score: 0.40
DE  Interaction: Q9NZM4; IntAct: EBI-1960478; Score: 0.40
DE  Interaction: Q9H1R2; IntAct: EBI-1960490; Score: 0.40
DE  Interaction: P15586; IntAct: EBI-1960502; Score: 0.40
DE  Interaction: P31995; IntAct: EBI-1960538; Score: 0.40
DE  Interaction: P31994; IntAct: EBI-1960526; Score: 0.40
DE  Interaction: P31273; IntAct: EBI-1960514; Score: 0.40
DE  Interaction: O43909; IntAct: EBI-1960562; Score: 0.40
DE  Interaction: P23759; IntAct: EBI-1960550; Score: 0.40
DE  Interaction: P26373; IntAct: EBI-1960574; Score: 0.40
DE  Interaction: Q9NRJ4; IntAct: EBI-1960586; Score: 0.40
DE  Interaction: O14490; IntAct: EBI-1960598; Score: 0.40
DE  Interaction: Q96Q35; IntAct: EBI-1960610; Score: 0.40
DE  Interaction: O95157; IntAct: EBI-1960622; Score: 0.40
DE  Interaction: Q13905; IntAct: EBI-1960634; Score: 0.40
DE  Interaction: Q9UPX8; IntAct: EBI-1960646; Score: 0.40
DE  Interaction: Q13796; IntAct: EBI-1960658; Score: 0.40
DE  Interaction: P49916; IntAct: EBI-1960670; Score: 0.40
DE  Interaction: O15371; IntAct: EBI-1960682; Score: 0.40
DE  Interaction: Q8TB24; IntAct: EBI-1960694; Score: 0.40
DE  Interaction: O43281; IntAct: EBI-1960706; Score: 0.40
DE  Interaction: P42684; IntAct: EBI-1960730; Score: 0.40
DE  Interaction: Q9UL51; IntAct: EBI-1960718; Score: 0.40
DE  Interaction: Q9NZV5; IntAct: EBI-1960742; Score: 0.40
DE  Interaction: Q9BYB0; IntAct: EBI-1960754; Score: 0.40
DE  Interaction: Q9H9L3; IntAct: EBI-1960766; Score: 0.40
DE  Interaction: Q9BWW9; IntAct: EBI-1960778; Score: 0.40
DE  Interaction: Q14008; IntAct: EBI-1960802; Score: 0.40
DE  Interaction: Q07890; IntAct: EBI-1960790; Score: 0.40
DE  Interaction: Q92918; IntAct: EBI-1960814; Score: 0.40
DE  Interaction: O00254; IntAct: EBI-1960826; Score: 0.40
DE  Interaction: Q13087; IntAct: EBI-1960838; Score: 0.40
DE  Interaction: P78345; IntAct: EBI-1960850; Score: 0.40
DE  Interaction: Q8IWT3; IntAct: EBI-1960862; Score: 0.40
DE  Interaction: P08047; IntAct: EBI-1960874; Score: 0.40
DE  Interaction: Q14185; IntAct: EBI-1960886; Score: 0.40
DE  Interaction: Q86X10; IntAct: EBI-1960898; Score: 0.40
DE  Interaction: Q9HCU4; IntAct: EBI-1960922; Score: 0.40
DE  Interaction: Q13023; IntAct: EBI-1960946; Score: 0.40
DE  Interaction: P23760; IntAct: EBI-1960958; Score: 0.40
DE  Interaction: Q07889; IntAct: EBI-1960934; Score: 0.40
DE  Interaction: Q05996; IntAct: EBI-1960970; Score: 0.40
DE  Interaction: P28340; IntAct: EBI-1960982; Score: 0.40
DE  Interaction: Q14118; IntAct: EBI-1960994; Score: 0.40
DE  Interaction: O60493; IntAct: EBI-1961006; Score: 0.40
DE  Interaction: Q96NS5; IntAct: EBI-1961030; Score: 0.40
DE  Interaction: P20774; IntAct: EBI-1961018; Score: 0.40
DE  Interaction: P46013; IntAct: EBI-1961042; Score: 0.40
DE  Interaction: P48960; IntAct: EBI-1961054; Score: 0.40
DE  Interaction: P78329; IntAct: EBI-1961078; Score: 0.40
DE  Interaction: Q15027; IntAct: EBI-1961090; Score: 0.40
DE  Interaction: P47928; IntAct: EBI-1961114; Score: 0.40
DE  Interaction: O43900; IntAct: EBI-1961102; Score: 0.40
DE  Interaction: P10301; IntAct: EBI-1961138; Score: 0.40
DE  Interaction: Q9Y2D5; IntAct: EBI-1961126; Score: 0.40
DE  Interaction: P49023; IntAct: EBI-7066367; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-7248693; Score: 0.85
DE  Interaction: P25445; IntAct: EBI-1648094; Score: 0.40
DE  Interaction: Q8TBB1; IntAct: EBI-7649813; Score: 0.56
DE  Interaction: P0CG48; IntAct: EBI-7650187; Score: 0.40
DE  Interaction: O70263; IntAct: EBI-7650384; Score: 0.40
DE  Interaction: P16284; IntAct: EBI-1766207; Score: 0.59
DE  Interaction: P18031; IntAct: EBI-8688791; Score: 0.94
DE  Interaction: P34152; IntAct: EBI-7921275; Score: 0.56
DE  Interaction: Q62884; IntAct: EBI-7505047; Score: 0.60
DE  Interaction: P61978; IntAct: EBI-7185667; Score: 0.59
DE  Interaction: Q13191; IntAct: EBI-7081394; Score: 0.40
DE  Interaction: P56945; IntAct: EBI-7040544; Score: 0.69
DE  Interaction: P27635; IntAct: EBI-8537576; Score: 0.59
DE  Interaction: P10636; IntAct: EBI-7796404; Score: 0.44
DE  Interaction: P04370; IntAct: EBI-7728029; Score: 0.40
DE  Interaction: P27986; IntAct: EBI-7585571; Score: 0.78
DE  Interaction: P60709; IntAct: EBI-7585640; Score: 0.27
DE  Interaction: Q80YS6; IntAct: EBI-7295737; Score: 0.40
DE  Interaction: P13645; IntAct: EBI-7609832; Score: 0.40
DE  Interaction: Q9NQI0; IntAct: EBI-7609853; Score: 0.40
DE  Interaction: Q4V348; IntAct: EBI-7609909; Score: 0.40
DE  Interaction: P35326; IntAct: EBI-7743289; Score: 0.60
DE  Interaction: P48023; IntAct: EBI-2481635; Score: 0.40
DE  Interaction: Q13094; IntAct: EBI-7643766; Score: 0.40
DE  Interaction: P18052; IntAct: EBI-7811172; Score: 0.40
DE  Interaction: Q68CZ2; IntAct: EBI-2607034; Score: 0.59
DE  Interaction: Q8IZP0; IntAct: EBI-8050301; Score: 0.44
DE  Interaction: P97288; IntAct: EBI-7149469; Score: 0.54
DE  Interaction: P35968; IntAct: EBI-2899201; Score: 0.77
DE  Interaction: P08581; IntAct: EBI-2927759; Score: 0.70
DE  Interaction: P18433; IntAct: EBI-7205168; Score: 0.66
DE  Interaction: P23743; IntAct: EBI-7559520; Score: 0.46
DE  Interaction: P35918; IntAct: EBI-8425905; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-8606171; Score: 0.35
DE  Interaction: P33151; IntAct: EBI-8609007; Score: 0.35
DE  Interaction: Q14289; IntAct: EBI-7095687; Score: 0.64
DE  Interaction: Q9NWQ8; IntAct: EBI-11358847; Score: 0.35
DE  Interaction: P40763; IntAct: EBI-11359552; Score: 0.53
DE  Interaction: O60674; IntAct: EBI-3133061; Score: 0.35
DE  Interaction: P68400; IntAct: EBI-3133113; Score: 0.56
DE  Interaction: P21333; IntAct: EBI-3451163; Score: 0.00
DE  Interaction: Q8WX93; IntAct: EBI-7432098; Score: 0.40
DE  Interaction: Q9WNA9; IntAct: EBI-7555504; Score: 0.44
DE  Interaction: Q7Z7K6; IntAct: EBI-7613065; Score: 0.40
DE  Interaction: P05023; IntAct: EBI-4303332; Score: 0.35
DE  Interaction: Q16825; IntAct: EBI-7186498; Score: 0.40
DE  Interaction: O08715; IntAct: EBI-7186509; Score: 0.40
DE  Interaction: Q14194; IntAct: EBI-7392387; Score: 0.37
DE  Interaction: Q06124; IntAct: EBI-7870944; Score: 0.44
DE  Interaction: P70424; IntAct: EBI-5451946; Score: 0.40
DE  Interaction: P08962; IntAct: EBI-7784524; Score: 0.40
DE  Interaction: Q03348; IntAct: EBI-7784512; Score: 0.40
DE  Interaction: Q9H3S7; IntAct: EBI-8423677; Score: 0.50
DE  Interaction: P12830; IntAct: EBI-5922639; Score: 0.50
DE  Interaction: Q75N03; IntAct: EBI-5922652; Score: 0.35
DE  Interaction: Q01973; IntAct: EBI-6082870; Score: 0.68
DE  Interaction: Q00993; IntAct: EBI-7694934; Score: 0.40
DE  Interaction: P30530; IntAct: EBI-7695010; Score: 0.40
DE  Interaction: P21145; IntAct: EBI-6253688; Score: 0.43
DE  Interaction: O00459; IntAct: EBI-6256917; Score: 0.35
DE  Interaction: Q92569; IntAct: EBI-6256917; Score: 0.62
DE  Interaction: Q8NF50; IntAct: EBI-6390168; Score: 0.40
DE  Interaction: P31749; IntAct: EBI-6590127; Score: 0.27
DE  Interaction: P46108; IntAct: EBI-6600082; Score: 0.27
DE  Interaction: Q8NFZ0; IntAct: EBI-6914350; Score: 0.40
DE  Interaction: P05062; IntAct: EBI-9001545; Score: 0.37
DE  Interaction: Q14032; IntAct: EBI-9001558; Score: 0.37
DE  Interaction: Q9BU70; IntAct: EBI-9001571; Score: 0.37
DE  Interaction: O60911; IntAct: EBI-9001584; Score: 0.37
DE  Interaction: Q00597; IntAct: EBI-9001597; Score: 0.37
DE  Interaction: O00757; IntAct: EBI-9001610; Score: 0.37
DE  Interaction: Q8IXK2; IntAct: EBI-9001623; Score: 0.37
DE  Interaction: Q9BXL5; IntAct: EBI-9001636; Score: 0.37
DE  Interaction: Q9P1Z9; IntAct: EBI-9001649; Score: 0.37
DE  Interaction: Q02750; IntAct: EBI-9001662; Score: 0.37
DE  Interaction: Q16644; IntAct: EBI-9001675; Score: 0.37
DE  Interaction: Q9NR45; IntAct: EBI-9001688; Score: 0.37
DE  Interaction: P62714; IntAct: EBI-9001701; Score: 0.37
DE  Interaction: P56962; IntAct: EBI-9001714; Score: 0.37
DE  Interaction: P23025; IntAct: EBI-9001727; Score: 0.37
DE  Interaction: O75820; IntAct: EBI-9001740; Score: 0.37
DE  Interaction: P10275; IntAct: EBI-9451123; Score: 0.44
DE  Interaction: Q13480; IntAct: EBI-9456279; Score: 0.44
DE  Interaction: P10721; IntAct: EBI-9464893; Score: 0.44
DE  Interaction: P14921; IntAct: EBI-9698851; Score: 0.44
DE  Interaction: Q9H3M7; IntAct: EBI-11686298; Score: 0.44
DE  Interaction: P06401; IntAct: EBI-12590606; Score: 0.44
DE  Interaction: P19367; IntAct: EBI-14988411; Score: 0.52
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q96QD9; IntAct: EBI-21501187; Score: 0.35
DE  Interaction: Q13503; IntAct: EBI-21501670; Score: 0.35
DE  Interaction: P21453; IntAct: EBI-21539478; Score: 0.35
DE  Interaction: P42677; IntAct: EBI-21539860; Score: 0.35
DE  Interaction: P09067; IntAct: EBI-21543288; Score: 0.35
DE  Interaction: O95136; IntAct: EBI-21551126; Score: 0.35
DE  Interaction: Q8N5S1; IntAct: EBI-21587332; Score: 0.35
DE  Interaction: O75626; IntAct: EBI-21603026; Score: 0.35
DE  Interaction: P21580; IntAct: EBI-21620094; Score: 0.35
DE  Interaction: Q96SQ9; IntAct: EBI-21623270; Score: 0.35
DE  Interaction: P25963; IntAct: EBI-21664926; Score: 0.35
DE  Interaction: Q6QAJ8; IntAct: EBI-21691086; Score: 0.35
DE  Interaction: Q9BTV5; IntAct: EBI-21692187; Score: 0.35
DE  Interaction: Q92845; IntAct: EBI-21702814; Score: 0.35
DE  Interaction: Q96S94; IntAct: EBI-21750627; Score: 0.35
DE  Interaction: Q8NFB2; IntAct: EBI-21757603; Score: 0.35
DE  Interaction: P49326; IntAct: EBI-21774649; Score: 0.35
DE  Interaction: Q86Z23; IntAct: EBI-21814288; Score: 0.35
DE  Interaction: Q9Y277; IntAct: EBI-21825091; Score: 0.35
DE  Interaction: Q9UN70; IntAct: EBI-21824946; Score: 0.35
DE  Interaction: Q6P158; IntAct: EBI-21831097; Score: 0.35
DE  Interaction: Q8N6N7; IntAct: EBI-21832308; Score: 0.35
DE  Interaction: Q8WUY3; IntAct: EBI-21832277; Score: 0.35
DE  Interaction: Q8N165; IntAct: EBI-21836274; Score: 0.35
DE  Interaction: Q92542; IntAct: EBI-21836991; Score: 0.35
DE  Interaction: Q3KPI0; IntAct: EBI-21837817; Score: 0.35
DE  Interaction: Q9UBH0; IntAct: EBI-21842113; Score: 0.35
DE  Interaction: Q9BYJ1; IntAct: EBI-21843741; Score: 0.35
DE  Interaction: P15260; IntAct: EBI-21848322; Score: 0.35
DE  Interaction: O76003; IntAct: EBI-21849210; Score: 0.35
DE  Interaction: Q99808; IntAct: EBI-21849345; Score: 0.35
DE  Interaction: Q96AZ6; IntAct: EBI-21849278; Score: 0.35
DE  Interaction: P14854; IntAct: EBI-21849241; Score: 0.35
DE  Interaction: P49407; IntAct: EBI-15565377; Score: 0.62
DE  Interaction: P35408; IntAct: EBI-15565467; Score: 0.40
DE  Interaction: P78536; IntAct: EBI-15581054; Score: 0.40
DE  Interaction: P07900; IntAct: EBI-15591551; Score: 0.67
DE  Interaction: Q96AQ6; IntAct: EBI-15606312; Score: 0.35
DE  Interaction: Q60598; IntAct: EBI-15645629; Score: 0.44
DE  Interaction: O00560; IntAct: EBI-15731494; Score: 0.40
DE  Interaction: P32121; IntAct: EBI-15749890; Score: 0.56
DE  Interaction: P25101; IntAct: EBI-15756430; Score: 0.40
DE  Interaction: P29066; IntAct: EBI-15756483; Score: 0.40
DE  Interaction: P21980; IntAct: EBI-15828007; Score: 0.40
DE  Interaction: P35222; IntAct: EBI-15951997; Score: 0.54
DE  Interaction: P29353; IntAct: EBI-16183922; Score: 0.44
DE  Interaction: Q01968; IntAct: EBI-16412116; Score: 0.35
DE  Interaction: Q08345; IntAct: EBI-22053903; Score: 0.35
DE  Interaction: Q6NYC1; IntAct: EBI-16745030; Score: 0.35
DE  Interaction: Q9BR61; IntAct: EBI-21225038; Score: 0.56
DE  Interaction: O60551; IntAct: EBI-21226608; Score: 0.44
DE  Interaction: Q01974; IntAct: EBI-20982927; Score: 0.37
DE  Interaction: O14672; IntAct: EBI-21223655; Score: 0.54
DE  Interaction: P78325; IntAct: EBI-21225676; Score: 0.44
DE  Interaction: O43184; IntAct: EBI-21225905; Score: 0.56
DE  Interaction: Q9H013; IntAct: EBI-21226684; Score: 0.44
DE  Interaction: Q62985; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: Q9WUD9; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: Q9Z2F5; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: Q68FX8; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: Q9QZC5; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: P10634; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: A0A0G2K064; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: B2GV53; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: Q6AYR1; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: Q5XI60; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: P62744; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q68FS2; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: P61621; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: F1M062; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: F1M5N4; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: D3ZIL6; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q10758; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: A0A0G2K261; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q5BK57; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: P54001; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: P21816; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q5M8C3; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: P11466; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q6AYC9; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: A0A8I6AI13; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: P62902; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: D3ZLE6; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: D4A3Q2; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: F1LQH2; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: F1LM66; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: A0A096MJZ8; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: D3ZKR8; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q63279; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: B5DEH4; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: F1M951; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: F1LM93; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: D3ZYG0; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q06884; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: B2GUV7; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q8K4V4; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: P25030; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q5RKG9; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: D3ZQ63; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: F1M0R1; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: B2RYD7; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: D3ZDP2; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: F1LNL3; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q66HR0; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: P00176; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q63186; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q499Q3; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q5PQL2; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: A0A0A0MY43; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q4QQT3; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: G3V781; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q5RKH0; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: M0R671; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: D3ZMS1; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: O08662; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: D3ZJ01; IntAct: EBI-22261657; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-22297428; Score: 0.62
DE  Interaction: O60783; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P07437; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-25384369; Score: 0.53
DE  Interaction: P11021; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P11940; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q9H361; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P40939; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P67936; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P06753; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P82650; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P82914; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q00325; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q00341; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q13310; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q15366; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P57721; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q71RC2; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q96AG4; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q99700; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q9Y291; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q9Y2R9; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: O60306; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P07910; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P09651; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q32P51; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P11142; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P12236; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P27708; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P33993; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P34932; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P38646; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P63313; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P68363; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P68366; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q8NEV1; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q01081; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q02952; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q13151; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q13263; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q14839; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q15370; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q8N163; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q92598; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: Q93009; IntAct: EBI-25384369; Score: 0.35
DE  Interaction: P05387; IntAct: EBI-25394988; Score: 0.35
DE  Interaction: Q12904; IntAct: EBI-25394988; Score: 0.35
DE  Interaction: Q15046; IntAct: EBI-25394988; Score: 0.35
DE  Interaction: O60264; IntAct: EBI-25394988; Score: 0.35
DE  Interaction: P28370; IntAct: EBI-25394988; Score: 0.35
DE  Interaction: Q6XD76; IntAct: EBI-25892220; Score: 0.56
DE  Interaction: O14796; IntAct: EBI-25892212; Score: 0.56
DE  Interaction: Q9UIH9; IntAct: EBI-25892204; Score: 0.56
DE  Interaction: Q14693; IntAct: EBI-25892196; Score: 0.56
DE  Interaction: Q15907; IntAct: EBI-25892188; Score: 0.56
DE  Interaction: Q14457; IntAct: EBI-25892180; Score: 0.56
DE  Interaction: Q9UNY5; IntAct: EBI-25892172; Score: 0.56
DE  Interaction: Q13829; IntAct: EBI-25892164; Score: 0.56
DE  Interaction: O60880; IntAct: EBI-25892148; Score: 0.56
DE  Interaction: Q13322; IntAct: EBI-25892138; Score: 0.56
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P63252; IntAct: EBI-28956128; Score: 0.27
DE  Interaction: P13569; IntAct: EBI-27084109; Score: 0.35
DE  Interaction: Q99592; IntAct: EBI-27093179; Score: 0.35
DE  Interaction: P07947; IntAct: EBI-28931668; Score: 0.35
DE  Interaction: P08631; IntAct: EBI-28931703; Score: 0.35
DE  Interaction: Q8TEL6; IntAct: EBI-28931938; Score: 0.35
DE  Interaction: Q05513; IntAct: EBI-28931938; Score: 0.35
DE  Interaction: P09769; IntAct: EBI-28931938; Score: 0.35
DE  Interaction: P06239; IntAct: EBI-28931938; Score: 0.35
DE  Interaction: P05090; IntAct: EBI-28931938; Score: 0.35
DE  Interaction: O00170; IntAct: EBI-28931938; Score: 0.35
DE  Interaction: Q86V86; IntAct: EBI-28942203; Score: 0.35
DE  Interaction: Q8TEA7; IntAct: EBI-28943849; Score: 0.35
DE  Interaction: P42566; IntAct: EBI-30822769; Score: 0.44
GO  GO:0005884;
GO  GO:0005901;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:1902737;
GO  GO:0044294;
GO  GO:0070062;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0098978;
GO  GO:0005770;
GO  GO:0005764;
GO  GO:0045121;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0002102;
GO  GO:0014069;
GO  GO:0099091;
GO  GO:0032587;
GO  GO:0097060;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0070700;
GO  GO:0045296;
GO  GO:0071253;
GO  GO:0019899;
GO  GO:0046875;
GO  GO:0070851;
GO  GO:0020037;
GO  GO:0005158;
GO  GO:0005178;
GO  GO:0008289;
GO  GO:0004715;
GO  GO:0030331;
GO  GO:0016004;
GO  GO:0043274;
GO  GO:0051219;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0005080;
GO  GO:0004713;
GO  GO:0097110;
GO  GO:0042169;
GO  GO:0005102;
GO  GO:0044325;
GO  GO:0032148;
GO  GO:0034332;
GO  GO:0086098;
GO  GO:0045453;
GO  GO:0060444;
GO  GO:0007155;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0098609;
GO  GO:0071398;
GO  GO:0071498;
GO  GO:0070301;
GO  GO:0071456;
GO  GO:0032869;
GO  GO:0071222;
GO  GO:0071375;
GO  GO:0036120;
GO  GO:0071393;
GO  GO:1990646;
GO  GO:0071897;
GO  GO:0035635;
GO  GO:0048013;
GO  GO:0007173;
GO  GO:0038128;
GO  GO:0038096;
GO  GO:0048041;
GO  GO:0030900;
GO  GO:0045087;
GO  GO:0007229;
GO  GO:0070102;
GO  GO:0060576;
GO  GO:0035556;
GO  GO:0007611;
GO  GO:0050900;
GO  GO:0016236;
GO  GO:0051450;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:0045892;
GO  GO:2001237;
GO  GO:0051895;
GO  GO:0002862;
GO  GO:2001243;
GO  GO:0051902;
GO  GO:0031333;
GO  GO:0051974;
GO  GO:0032211;
GO  GO:0048011;
GO  GO:0042476;
GO  GO:0048477;
GO  GO:0036035;
GO  GO:0018105;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0030168;
GO  GO:0043065;
GO  GO:0045780;
GO  GO:0090263;
GO  GO:0045737;
GO  GO:0001819;
GO  GO:0035306;
GO  GO:2000573;
GO  GO:0045893;
GO  GO:0010634;
GO  GO:0070374;
GO  GO:0010907;
GO  GO:0035332;
GO  GO:0046628;
GO  GO:0033625;
GO  GO:2000394;
GO  GO:2000256;
GO  GO:0043406;
GO  GO:1903997;
GO  GO:0045747;
GO  GO:2000386;
GO  GO:0050731;
GO  GO:0043552;
GO  GO:0014068;
GO  GO:2000588;
GO  GO:0071803;
GO  GO:0031954;
GO  GO:0051897;
GO  GO:1900182;
GO  GO:0010954;
GO  GO:0071902;
GO  GO:0051222;
GO  GO:0046579;
GO  GO:0051057;
GO  GO:0014911;
GO  GO:1904707;
GO  GO:0001545;
GO  GO:0050847;
GO  GO:0046777;
GO  GO:0031648;
GO  GO:0045124;
GO  GO:2001286;
GO  GO:0060491;
GO  GO:0022407;
GO  GO:2000641;
GO  GO:0010632;
GO  GO:0033146;
GO  GO:0098962;
GO  GO:0043393;
GO  GO:0043114;
GO  GO:0010447;
GO  GO:0051602;
GO  GO:0070555;
GO  GO:0009612;
GO  GO:0051385;
GO  GO:0031667;
GO  GO:0009615;
GO  GO:0009410;
GO  GO:0007172;
GO  GO:0007165;
GO  GO:0014856;
GO  GO:0007283;
GO  GO:0002223;
GO  GO:0043149;
GO  GO:0034446;
GO  GO:0031295;
GO  GO:0045056;
GO  GO:0007179;
GO  GO:0007169;
GO  GO:0060065;
GO  GO:0048010;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:7525268};
SQ  MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAG
SQ  PLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRE
SQ  SERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGL
SQ  CHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKL
SQ  RHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGEN
SQ  LVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVER
SQ  GYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
//
ID  P05480;
PN  Proto-oncogene tyrosine-protein kinase Src;
GN  Src;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:21525037}; Lipid-anchor {ECO:0000269|PubMed:22801373}. Mitochondrion inner membrane {ECO:0000269|PubMed:12615910}. Nucleus {ECO:0000269|PubMed:12615910}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12615910}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P12931}. Cell junction, focal adhesion {ECO:0000269|PubMed:22801373}. Note=Localizes to focal adhesion sites following integrin engagement (PubMed:22801373). Localization to focal adhesion sites requires myristoylation and the SH3 domain. Colocalizes with PDLIM4 at the perinuclear region, but not at focal adhesions. {ECO:0000250|UniProtKB:P12931, ECO:0000269|PubMed:22801373}.
DR  UNIPROT: P05480;
DR  UNIPROT: F8WI90;
DR  UNIPROT: Q2M4I4;
DR  PDB: 6F3F;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DE  Function: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta- catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (PubMed:9344858). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation (By similarity). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta- arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (By similarity). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-738'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-226'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Phosphorylates synaptic vesicle protein synaptophysin (SYP) (By similarity). Involved in anchorage- independent cell growth (By similarity). Required for podosome formation (PubMed:21525037). Mediates IL6 signaling by activating YAP1- NOTCH pathway to induce inflammation-induced epithelial regeneration (PubMed:25731159). {ECO:0000250|UniProtKB:P12931, ECO:0000250|UniProtKB:Q9WUD9, ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:21525037, ECO:0000269|PubMed:25731159, ECO:0000269|PubMed:8641341, ECO:0000269|PubMed:9344858, ECO:0000305|PubMed:11964124, ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}. [Isoform 1]: Non-receptor protein tyrosine kinase which phosphorylates synaptophysin with high affinity. {ECO:0000250|UniProtKB:Q9WUD9}. [Isoform 2]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr- 418 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in L1CAM-mediated neurite elongation, possibly by acting downstream of L1CAM to drive cytoskeletal rearrangements involved in neurite outgrowth (By similarity). {ECO:0000250|UniProtKB:Q9WUD9}.
DE  Reference Proteome: Yes;
DE  Interaction: P16054; IntAct: EBI-298523; Score: 0.35
DE  Interaction: P34152; IntAct: EBI-7361479; Score: 0.59
DE  Interaction: P35438; IntAct: EBI-396959; Score: 0.46
DE  Interaction: O70469; IntAct: EBI-7588669; Score: 0.52
DE  Interaction: Q9WU78; IntAct: EBI-7397819; Score: 0.40
DE  Interaction: P07141; IntAct: EBI-777167; Score: 0.52
DE  Interaction: P54763; IntAct: EBI-983237; Score: 0.46
DE  Interaction: P31016; IntAct: EBI-6988922; Score: 0.65
DE  Interaction: Q00960; IntAct: EBI-6989312; Score: 0.40
DE  Interaction: Q8T4F7; IntAct: EBI-1556974; Score: 0.40
DE  Interaction: O13016; IntAct: EBI-8162501; Score: 0.40
DE  Interaction: Q05397; IntAct: EBI-7976544; Score: 0.68
DE  Interaction: Q9QWI6; IntAct: EBI-2658867; Score: 0.35
DE  Interaction: P97288; IntAct: EBI-7149929; Score: 0.40
DE  Interaction: P70315; IntAct: EBI-2898940; Score: 0.52
DE  Interaction: P18052; IntAct: EBI-8563541; Score: 0.44
DE  Interaction: P07333; IntAct: EBI-8611641; Score: 0.35
DE  Interaction: P08050; IntAct: EBI-8615639; Score: 0.35
DE  Interaction: Q00959; IntAct: EBI-8554030; Score: 0.56
DE  Interaction: Q01973; IntAct: EBI-6082586; Score: 0.54
DE  Interaction: P05106; IntAct: EBI-6119848; Score: 0.60
DE  Interaction: P35546; IntAct: EBI-7942053; Score: 0.46
DE  Interaction: Q9CQV6; IntAct: EBI-7942092; Score: 0.53
DE  Interaction: P49023; IntAct: EBI-6471299; Score: 0.27
DE  Interaction: Q63767; IntAct: EBI-6471866; Score: 0.47
DE  Interaction: Q8VI36; IntAct: EBI-6471318; Score: 0.40
DE  Interaction: Q8C180; IntAct: EBI-9210301; Score: 0.44
DE  Interaction: P19367; IntAct: EBI-14988387; Score: 0.64
DE  Interaction: P52789; IntAct: EBI-15099842; Score: 0.60
DE  Interaction: Q61056; IntAct: EBI-15563522; Score: 0.44
DE  Interaction: Q13507; IntAct: EBI-15563553; Score: 0.60
DE  Interaction: Q61143; IntAct: EBI-15563631; Score: 0.44
DE  Interaction: Q9QX29; IntAct: EBI-15563679; Score: 0.44
DE  Interaction: Q9R244; IntAct: EBI-15563736; Score: 0.44
DE  Interaction: Q9QUQ5; IntAct: EBI-15563789; Score: 0.44
DE  Interaction: P09581; IntAct: EBI-15732483; Score: 0.40
DE  Interaction: O54890; IntAct: EBI-15732500; Score: 0.40
DE  Interaction: P31750; IntAct: EBI-15749817; Score: 0.50
DE  Interaction: P15208; IntAct: EBI-15749928; Score: 0.35
DE  Interaction: P23242; IntAct: EBI-15909386; Score: 0.50
DE  Interaction: P22682; IntAct: EBI-15956028; Score: 0.40
DE  Interaction: Q4ACU6; IntAct: EBI-16726570; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16736255; Score: 0.35
GO  GO:0005884;
GO  GO:0005901;
GO  GO:0030054;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:1902737;
GO  GO:0044294;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0098978;
GO  GO:0005770;
GO  GO:0005764;
GO  GO:0016020;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0002102;
GO  GO:0014069;
GO  GO:0099091;
GO  GO:0032587;
GO  GO:0097060;
GO  GO:0005524;
GO  GO:0070700;
GO  GO:0050839;
GO  GO:0071253;
GO  GO:0019899;
GO  GO:0046875;
GO  GO:0070851;
GO  GO:0020037;
GO  GO:0005158;
GO  GO:0005178;
GO  GO:0016301;
GO  GO:0004715;
GO  GO:0030331;
GO  GO:0016004;
GO  GO:0043274;
GO  GO:0051219;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0005080;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0097110;
GO  GO:0042169;
GO  GO:0005102;
GO  GO:0044325;
GO  GO:0032148;
GO  GO:0034332;
GO  GO:0086098;
GO  GO:0045453;
GO  GO:0060444;
GO  GO:0007155;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0016477;
GO  GO:0008283;
GO  GO:0098609;
GO  GO:0071398;
GO  GO:0071498;
GO  GO:0070301;
GO  GO:0071456;
GO  GO:0032869;
GO  GO:0071222;
GO  GO:0071375;
GO  GO:0036120;
GO  GO:0071393;
GO  GO:1990646;
GO  GO:0034614;
GO  GO:0071560;
GO  GO:0071897;
GO  GO:0007173;
GO  GO:0048041;
GO  GO:0030900;
GO  GO:0045087;
GO  GO:0007229;
GO  GO:0070102;
GO  GO:0060576;
GO  GO:0035556;
GO  GO:0007611;
GO  GO:0051450;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:0045892;
GO  GO:2001237;
GO  GO:0051895;
GO  GO:2001243;
GO  GO:0051902;
GO  GO:0031333;
GO  GO:0051974;
GO  GO:0032211;
GO  GO:0048011;
GO  GO:0042476;
GO  GO:0048477;
GO  GO:0036035;
GO  GO:0018105;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0016310;
GO  GO:0043065;
GO  GO:0045780;
GO  GO:0090263;
GO  GO:0045785;
GO  GO:0045737;
GO  GO:0001819;
GO  GO:0035306;
GO  GO:2000573;
GO  GO:0045893;
GO  GO:0010634;
GO  GO:0070374;
GO  GO:0010628;
GO  GO:0010907;
GO  GO:0035332;
GO  GO:0046628;
GO  GO:1902533;
GO  GO:2000394;
GO  GO:2000256;
GO  GO:0043406;
GO  GO:0045747;
GO  GO:2000386;
GO  GO:0050731;
GO  GO:0043552;
GO  GO:2000588;
GO  GO:0071803;
GO  GO:0031954;
GO  GO:0051897;
GO  GO:1900182;
GO  GO:0010954;
GO  GO:0071902;
GO  GO:0051222;
GO  GO:0046579;
GO  GO:0051057;
GO  GO:0014911;
GO  GO:1904707;
GO  GO:0001545;
GO  GO:0050847;
GO  GO:0046777;
GO  GO:0031648;
GO  GO:0006468;
GO  GO:2001286;
GO  GO:0060491;
GO  GO:0022407;
GO  GO:2000641;
GO  GO:0010632;
GO  GO:0033146;
GO  GO:0098962;
GO  GO:0043393;
GO  GO:0010447;
GO  GO:0051602;
GO  GO:0070555;
GO  GO:0009612;
GO  GO:0051385;
GO  GO:0031667;
GO  GO:0009615;
GO  GO:0009410;
GO  GO:0014856;
GO  GO:0007283;
GO  GO:0043149;
GO  GO:0034446;
GO  GO:0045056;
GO  GO:0007179;
GO  GO:0007169;
GO  GO:0060065;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGSNKSKPKDASQRRRSLEPSENVHGAGGAFPASQTPSKPASADGHRGPSAAFVPPAAEPKLFGGFNSSDTVTSPQRAGP
SQ  LAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRES
SQ  ERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLC
SQ  HRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLR
SQ  HEKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKGETGKYLRLPQLVDMSAQIASGMAYVERMNYVHRDLRAANILVGENL
SQ  VCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERG
SQ  YRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
//
ID  Q9WUD9;
PN  Proto-oncogene tyrosine-protein kinase Src;
GN  Src;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P05480}; Lipid-anchor {ECO:0000250|UniProtKB:P05480}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05480}. Nucleus {ECO:0000250|UniProtKB:P05480}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P05480}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P12931}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P05480}. Note=Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain (By similarity). Colocalizes with PDLIM4 at the perinuclear region, but not at focal adhesions. {ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:P12931}.
DR  UNIPROT: Q9WUD9;
DR  UNIPROT: G3V776;
DR  UNIPROT: Q45QJ2;
DR  UNIPROT: Q9JJ10;
DR  Pfam: PF07714;
DR  Pfam: PF00017;
DR  Pfam: PF00018;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  PROSITE: PS50001;
DR  PROSITE: PS50002;
DE  Function: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta- catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation (By similarity). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta- arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (By similarity). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-738'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr- 9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-226'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Phosphorylates synaptic vesicle protein synaptophysin (SYP) (PubMed:26026271). Involved in anchorage- independent cell growth (By similarity). Required for podosome formation (By similarity). Mediates IL6 signaling by activating YAP1- NOTCH pathway to induce inflammation-induced epithelial regeneration (By similarity). {ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:P12931, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:26026271, ECO:0000305}. [Isoform 1]: Non-receptor protein tyrosine kinase which phosphorylates synaptophysin with high affinity. {ECO:0000269|PubMed:26026271}. [Isoform 2]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr- 419 and subsequent activation (PubMed:26026271). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (PubMed:26026271). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (PubMed:26026271). Plays a role in L1CAM-mediated neurite elongation, possibly by acting downstream of L1CAM to drive cytoskeletal rearrangements involved in neurite outgrowth (PubMed:28220894). {ECO:0000269|PubMed:26026271, ECO:0000269|PubMed:28220894}. [Isoform 3]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr- 419 and subsequent activation (PubMed:26026271). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (PubMed:26026271). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (PubMed:26026271). Plays a role in neurite elongation (PubMed:28220894). {ECO:0000269|PubMed:26026271, ECO:0000269|PubMed:28220894}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-22179950; Score: 0.35
DE  Interaction: P12931; IntAct: EBI-22249049; Score: 0.35
DE  Interaction: P70600; IntAct: EBI-16803792; Score: 0.40
DE  Interaction: Q9NQC7; IntAct: EBI-22254510; Score: 0.35
DE  Interaction: P20171; IntAct: EBI-8633311; Score: 0.40
DE  Interaction: Q63767; IntAct: EBI-7856282; Score: 0.56
DE  Interaction: P18031; IntAct: EBI-8423787; Score: 0.56
DE  Interaction: P18545; IntAct: EBI-7942964; Score: 0.37
DE  Interaction: P22002; IntAct: EBI-7937536; Score: 0.59
DE  Interaction: P06211; IntAct: EBI-7983739; Score: 0.35
DE  Interaction: Q56B11; IntAct: EBI-7983770; Score: 0.35
DE  Interaction: P28648; IntAct: EBI-7784672; Score: 0.40
DE  Interaction: Q03348; IntAct: EBI-7784537; Score: 0.40
DE  Interaction: O08617; IntAct: EBI-8584407; Score: 0.54
DE  Interaction: B4F7E7; IntAct: EBI-15715474; Score: 0.40
DE  Interaction: P08050; IntAct: EBI-15786947; Score: 0.40
DE  Interaction: Q9H223; IntAct: EBI-22238397; Score: 0.35
DE  Interaction: P36871; IntAct: EBI-22239685; Score: 0.35
DE  Interaction: Q13523; IntAct: EBI-22240189; Score: 0.35
DE  Interaction: P08575; IntAct: EBI-22240438; Score: 0.35
DE  Interaction: Q06124; IntAct: EBI-22240309; Score: 0.35
DE  Interaction: P16234; IntAct: EBI-22246750; Score: 0.35
DE  Interaction: P09619; IntAct: EBI-22247388; Score: 0.35
DE  Interaction: P35590; IntAct: EBI-22249141; Score: 0.35
DE  Interaction: P35968; IntAct: EBI-22252773; Score: 0.35
DE  Interaction: P11274; IntAct: EBI-22253111; Score: 0.35
DE  Interaction: Q13191; IntAct: EBI-22253483; Score: 0.35
DE  Interaction: Q7L591; IntAct: EBI-22253842; Score: 0.35
DE  Interaction: Q13094; IntAct: EBI-22254633; Score: 0.35
DE  Interaction: Q9UQC2; IntAct: EBI-22254457; Score: 0.35
DE  Interaction: Q92569; IntAct: EBI-22254928; Score: 0.35
DE  Interaction: P18433; IntAct: EBI-22255840; Score: 0.35
DE  Interaction: O14543; IntAct: EBI-22256732; Score: 0.35
DE  Interaction: P15498; IntAct: EBI-22257448; Score: 0.35
DE  Interaction: Q6PKG0; IntAct: EBI-22258441; Score: 0.35
GO  GO:0005884;
GO  GO:0005901;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:1902737;
GO  GO:0044294;
GO  GO:0031234;
GO  GO:0005925;
GO  GO:0098978;
GO  GO:0005770;
GO  GO:0005764;
GO  GO:0016020;
GO  GO:0005743;
GO  GO:0005739;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0002102;
GO  GO:0014069;
GO  GO:0099091;
GO  GO:0032587;
GO  GO:0097060;
GO  GO:0005524;
GO  GO:0070700;
GO  GO:0050839;
GO  GO:0071253;
GO  GO:0019899;
GO  GO:0046875;
GO  GO:0070851;
GO  GO:0020037;
GO  GO:0005158;
GO  GO:0005178;
GO  GO:0016301;
GO  GO:0019900;
GO  GO:0004715;
GO  GO:0030331;
GO  GO:0016004;
GO  GO:0043274;
GO  GO:0051219;
GO  GO:0008022;
GO  GO:0019904;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0005080;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0097110;
GO  GO:0042169;
GO  GO:0005102;
GO  GO:0044325;
GO  GO:0032148;
GO  GO:0034332;
GO  GO:0086098;
GO  GO:0045453;
GO  GO:0007420;
GO  GO:0060444;
GO  GO:0007155;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0016477;
GO  GO:0008283;
GO  GO:0098609;
GO  GO:1904385;
GO  GO:0071398;
GO  GO:0071498;
GO  GO:0070301;
GO  GO:0071456;
GO  GO:0032869;
GO  GO:0071222;
GO  GO:0071375;
GO  GO:0036120;
GO  GO:0071393;
GO  GO:1990646;
GO  GO:0034614;
GO  GO:0071560;
GO  GO:0071897;
GO  GO:0007173;
GO  GO:0048041;
GO  GO:0030900;
GO  GO:0045087;
GO  GO:0007229;
GO  GO:0070102;
GO  GO:0060576;
GO  GO:0035556;
GO  GO:0007611;
GO  GO:0051450;
GO  GO:2000811;
GO  GO:0043066;
GO  GO:0043154;
GO  GO:0045892;
GO  GO:2001237;
GO  GO:0051895;
GO  GO:2001243;
GO  GO:0051902;
GO  GO:0031333;
GO  GO:0051974;
GO  GO:0032211;
GO  GO:0048011;
GO  GO:0042476;
GO  GO:0048477;
GO  GO:0036035;
GO  GO:0018105;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0016310;
GO  GO:0043065;
GO  GO:0045780;
GO  GO:0090263;
GO  GO:0045785;
GO  GO:0045737;
GO  GO:0001819;
GO  GO:0035306;
GO  GO:2000573;
GO  GO:0045893;
GO  GO:0010634;
GO  GO:0070374;
GO  GO:0010628;
GO  GO:0010907;
GO  GO:0035332;
GO  GO:0046628;
GO  GO:1902533;
GO  GO:2000394;
GO  GO:2000256;
GO  GO:0043406;
GO  GO:0045747;
GO  GO:2000386;
GO  GO:0050731;
GO  GO:0043552;
GO  GO:0010641;
GO  GO:2000588;
GO  GO:0071803;
GO  GO:0031954;
GO  GO:0051897;
GO  GO:1900182;
GO  GO:0010954;
GO  GO:0071902;
GO  GO:0051222;
GO  GO:0046579;
GO  GO:0051057;
GO  GO:0014911;
GO  GO:1904707;
GO  GO:0001545;
GO  GO:0050847;
GO  GO:0046777;
GO  GO:0031648;
GO  GO:0006468;
GO  GO:2001286;
GO  GO:0060491;
GO  GO:0022407;
GO  GO:2000641;
GO  GO:0010632;
GO  GO:0033146;
GO  GO:0098962;
GO  GO:0043393;
GO  GO:0010447;
GO  GO:0051602;
GO  GO:0070542;
GO  GO:0042542;
GO  GO:0070555;
GO  GO:0009612;
GO  GO:0051385;
GO  GO:0031667;
GO  GO:0009615;
GO  GO:0009410;
GO  GO:0014856;
GO  GO:0007283;
GO  GO:0043149;
GO  GO:0034446;
GO  GO:0045056;
GO  GO:0007179;
GO  GO:0007169;
GO  GO:0060065;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGSNKSKPKDASQRRRSLEPAENVHGAGGAFPASQTPSKPASADGHRGPNAAFVPPAAAEPKLFGGFNSSDTVTSPQRAG
SQ  PLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRE
SQ  SERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGL
SQ  CHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKL
SQ  RHEKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKGETGKYLRLPQLVDMSAQIASGMAYVERMNYVHRDLRAANILVGEN
SQ  LVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVER
SQ  GYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
//
ID  Q05B65;
PN  Serum response factor-binding protein 1;
GN  SRFBP1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}.
DR  UNIPROT: Q05B65;
DR  Pfam: PF09073;
DE  Function: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). {ECO:0000250|UniProtKB:Q9CZ91}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEPETLNLNNEVVKMRKEVKRIRVLVIRKLVRSVGRLKSKKGREDALLKNQRRAQRLLEEIRAMKELKPDVVTKSALGE
SQ  DINFEKICKKPDSTAAERAIARLAVHPLLKKKIDVLKAAVKSFKDARQNVVEVKSSNSASEENHSKDTLCSNDDASKLQH
SQ  EGTIIREQKEKEAKILAKKPINNSKEKIAKMDHGPKAMDVPNSLSKPSGKDSPASSASQKTPSDPKMKALSKTKKMKESS
SQ  SSLDVDSDGEELYEEEKEYFDDSTEERFYKQSSMSEDSDSGDDFFIGKVKRARKKESSCRFSDKEQNPPKNLLLEEGILE
SQ  THQNLQNDKNKPRTEARRFESVFFQSLSGSKSLERNHREQVPRSKTMDFQHIEPQNKNQFNKKAQRGFENTKQKSQLPLH
SQ  PSWEASRRRKEQQSKIAVFQGKKITFDD
//
ID  Q8NEF9;
PN  Serum response factor-binding protein 1;
GN  SRFBP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}.
DR  UNIPROT: Q8NEF9;
DR  UNIPROT: Q5QFI2;
DR  UNIPROT: Q96AH4;
DR  UNIPROT: Q96DK2;
DR  Pfam: PF09073;
DR  OMIM: 610479;
DR  DisGeNET: 153443;
DE  Function: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). {ECO:0000250|UniProtKB:Q9CZ91}.
DE  Reference Proteome: Yes;
DE  Interaction: P29991; IntAct: EBI-8827650; Score: 0.37
DE  Interaction: P59595; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: A0A6L8PTK5; IntAct: EBI-2824678; Score: 0.00
DE  Interaction: A0A6L8P1Q0; IntAct: EBI-2824697; Score: 0.00
DE  Interaction: Q99IB8; IntAct: EBI-6928142; Score: 0.37
DE  Interaction: P60033; IntAct: EBI-10766934; Score: 0.43
DE  Interaction: Q96JN0; IntAct: EBI-11124931; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-21512315; Score: 0.48
DE  Interaction: Q13895; IntAct: EBI-21815267; Score: 0.35
DE  Interaction: Q969U6; IntAct: EBI-21883583; Score: 0.35
DE  Interaction: Q13206; IntAct: EBI-21883583; Score: 0.35
DE  Interaction: P68431; IntAct: EBI-16794028; Score: 0.27
DE  Interaction: P05067; IntAct: EBI-20821761; Score: 0.35
DE  Interaction: Q9NXE4; IntAct: EBI-20919780; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: A6H8W8; IntAct: EBI-25408765; Score: 0.35
DE  Interaction: Q8IW93; IntAct: EBI-25410221; Score: 0.35
DE  Interaction: Q9P227; IntAct: EBI-25410568; Score: 0.35
DE  Interaction: Q9NWB6; IntAct: EBI-26886979; Score: 0.27
DE  Interaction: O60729; IntAct: EBI-27115568; Score: 0.27
DE  Interaction: P0DTC9; IntAct: EBI-27127583; Score: 0.35
DE  Interaction: P15130; IntAct: EBI-27131516; Score: 0.35
DE  Interaction: Q0ZME3; IntAct: EBI-27131755; Score: 0.35
DE  Interaction: Q6Q1R8; IntAct: EBI-27132003; Score: 0.35
DE  Interaction: K9N4V7; IntAct: EBI-27132270; Score: 0.35
DE  Interaction: P33469; IntAct: EBI-27132272; Score: 0.35
GO  GO:0030686;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0003723;
GO  GO:0030490;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQPGTLNLNNEVVKMRKEVKRIRVLVIRKLVRSVGRLKSKKGTEDALLKNQRRAQRLLEEIHAMKELKPDIVTKSALGD
SQ  DINFEKIFKKPDSTATERAIARLAVHPLLKKKIDVLKAAVQAFKEARQNVAEVESSKNASEDNHSENTLYSNDNGSNLQR
SQ  EATVISEQKVKETKILAKKPIHNSKEKIAKMEHGPKAVTIANSPSKPSEKDSVVSLESQKTPADPKLKTLSQTKKNKGSD
SQ  SSLSGNSDGGEEFCEEEKEYFDDSTEERFYKQSSMSEDSDSGDDFFIGKVRRTRKKESSCHSSVKEQKPLEKVFLKEDTG
SQ  ETHGDTRNDKIKPSTETRKLESVFFHSLSGSKSSRRNFKEQAPKTRSLDFPQNEPQIKNQFNKKLSGRLENTKQQLQLPL
SQ  HPSWEASRRRKEQQSNIAVFQGKKITFDD
//
ID  Q9CZ91;
PN  Serum response factor-binding protein 1;
GN  Srfbp1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16647043}.
DR  UNIPROT: Q9CZ91;
DR  UNIPROT: Q3UGY0;
DR  UNIPROT: Q3UMK2;
DR  UNIPROT: Q3UR20;
DR  UNIPROT: Q8R3W6;
DR  UNIPROT: Q9CRL0;
DR  Pfam: PF09073;
DE  Function: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells. {ECO:0000269|PubMed:15492011, ECO:0000269|PubMed:16647043}.
DE  Reference Proteome: Yes;
GO  GO:0030686;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030490;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAADPLPPSAMVQPGTLNLNNEVVKMRKEVKRIRVLVIRKLVRSVGRLKSKKGTEDALLKNQRRAQRLLEEIHAMKELKP
SQ  DVVTKSALSDDINFEKTCKKPDSTATDRAVARLAGHPLLKKKIDVLKDAVQAFKDARQSAPAAESSESTSGEGRCKDIAR
SQ  SKDDARESQHPERTVVREQKAKDTNTAAKNAASGSKEKLAKTEQAPRAGTTPGSQGRPSGKGAGVNSEHQGAPAPGDSNQ
SQ  GKASTKTPEDSVCEPANNGVSEEEESEGEKEYFDDSTEERFYKQSSASEDSDSGDDFFIGKVRRTRKKESGVHSSAKELK
SQ  PLPKVPSKTSTLETPWDVRNDKHRPIPEARKFESVFFHSLAGPKSSRRDPREQAPKNKAPDFPENEPPVKKQFTKSAYRG
SQ  FESVKQTMQAPLHPSWEASRRRKEQQSKIAVFQGKKITFDD
//
ID  Q5NVE2;
PN  Serum response factor-binding protein 1;
GN  SRFBP1;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}.
DR  UNIPROT: Q5NVE2;
DR  Pfam: PF09073;
DE  Function: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). {ECO:0000250|UniProtKB:Q9CZ91}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAQPGTLNLNNEVVKMRKEVKRIRVLVIRKLVRSVGRLKSKKGTEDALLKNQRRAQRLLEEIHAMKELKPDMVTKSALGD
SQ  DINFEKICKKPDSTATERAIARLAVHPLLKKKIDVLKAAVQAFKEARQNVTEVESSKNASEDNHSKNTLYSNDNGSNLQR
SQ  EGTVISEQEVKETKILAKKPIHNSKEKIAKMEHGPKAVTIANSPSKPSEKDSVISLESQKTPADPKLKTLSQTKKNKESD
SQ  SSLSGNSDGGEELCEEEKEYFDDSTEERFYKQSSMSEDSDSGDDFFIGKVRRTRKKESSCHSSVKEQKRLEKVFLKEDTG
SQ  ETHGDTRNDKTKPSTETRKLESVFFHSLSGSKSSRRNFKEQAPKTRSLDFPQNEPQFKNQFNKKLSRRLENTKQQLQLPL
SQ  HPSWEASRRRKEQQSNIAVFQGKKITFDD
//
ID  Q66H19;
PN  Serum response factor-binding protein 1;
GN  Srfbp1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}.
DR  UNIPROT: Q66H19;
DR  Pfam: PF09073;
DE  Function: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). {ECO:0000250|UniProtKB:Q9CZ91}.
DE  Reference Proteome: Yes;
GO  GO:0030686;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030490;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAADPSPPSAMAQPRPLNLNNEVVKMRKEVKRIRVLVIRKLVRSVSRLKSKKGSEDALLKNQRRAQRLLQEIHAMKELKP
SQ  DVITKSALNDDINFEKTCKKPDSTATERAIARLAVHPLLKRKVDALKAAIQAFKDARQNAPEAESSKSASKESQCEDIPR
SQ  SQAEASESQHPERTVVGEQKGKDKDPTTAKKAGSGSKEKLAKGKQGPKAVATPHSPGKPSEKGAGINSERQGAPTPGNHS
SQ  QGKASTRTTEDSVCEPDDNSISKEEVSEEEKEYFDDSTEERFYKQSSASEDSDSGDDFFIGKVRRTRKKECAVPSSAKEQ
SQ  KPLPKVSSKTNTLETHWDIRNDKHKLIPEARKLESVFFHSLSGPKSSRRDPREQAPKNKAPDIPENEPPIQNKFTKSARR
SQ  GFESAKQPSYAPLHPSWEASRRRKEQQSKIAVFQGKKITFDD
//
ID  Q5XGC9;
PN  Serum response factor-binding protein 1;
GN  srfbp1;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}.
DR  UNIPROT: Q5XGC9;
DR  UNIPROT: Q28EI0;
DR  Pfam: PF09073;
DE  Function: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). {ECO:0000250|UniProtKB:Q9CZ91}.
DE  Reference Proteome: Yes;
GO  GO:0030686;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030490;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEPVLNLNNEVVKLRKDVKKVKVLIIRKLTRHIAKLKSKKGTEELILKNQRRAQRLLEEIHSVKELKPDDVTKTALRKEI
SQ  SFEKVCKKPNSTAEERALARLATHPLLKQKITAIKEAIKAFKDARKTAAEGEREREKDEPEQVTKIKETKKPVQAKLNKN
SQ  TEEIKSAKEHVKEEKCKNLLEDSDKGTEKALELPYVQENLPEQTAENKEQPKAQDVERPAVERPAVERPAVERPAVERPA
SQ  VERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPAVERPA
SQ  VERPVVESPAVERPPVESPPKKKACLEQELGCELSDIEDSDKEKEYFDDSTEERFYKHSSSFEDSDSGSDNDFFIGKIRR
SQ  TKKKKSDKDGSKQKEEKVPPTKEKAQTSEVQKEIPTAKSMKLKSVFCKSLSQTKPKPSFTKRETNFRQERNKRPVMPQAS
SQ  PLAKKPLQSKATSVRQPGRKLEAQPLHPSWEASRKRKEQQAQITKFQGKKIVFDD
//
ID  F4JS25;
PN  Suppressor of RPS4-RLD 1;
GN  SRFR1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:18774967, ECO:0000269|PubMed:21079790}. Cytoplasm {ECO:0000269|PubMed:18774967}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18774967}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Microsome {ECO:0000269|PubMed:21079790}. Note=Found in microsomes when interacting with SNC1 and RPS4. {ECO:0000269|PubMed:21079790}.
DR  UNIPROT: F4JS25;
DR  UNIPROT: Q8GYX1;
DR  UNIPROT: Q9SZU6;
DR  Pfam: PF13181;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Negative regulator of effector-triggered immunity associated with the EDS1 resistance pathway (PubMed:15469494, PubMed:18774967, PubMed:19649196, PubMed:19525323, PubMed:20862316, PubMed:21079790). May localize its interactors to a microsomal membrane (PubMed:22158819). May therefore negatively regulate RPS4 and SNC1 translocation to the nucleus (PubMed:21079790). Contributes to the regulation of RPS2 and RPS4 protein levels and negatively regulates SNC1 stability (PubMed:20862316). {ECO:0000269|PubMed:15469494, ECO:0000269|PubMed:18774967, ECO:0000269|PubMed:19525323, ECO:0000269|PubMed:19649196, ECO:0000269|PubMed:20862316, ECO:0000269|PubMed:21079790, ECO:0000269|PubMed:22158819}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9FPR2; IntAct: EBI-4481445; Score: 0.44
DE  Interaction: Q9SUR9; IntAct: EBI-4498032; Score: 0.37
DE  Interaction: Q9SUT5; IntAct: EBI-4498040; Score: 0.37
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0043231;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0060090;
GO  GO:0042742;
GO  GO:0031348;
GO  GO:0045892;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MATATATSERFELAKHCSSRNWSKAIRVLDSLLAKESSILDICNRAFCYNQLELHKHVIKDCDKALLLEPFAIQAFILKG
SQ  RALLALGRKQEAVLVLEQGYKSALQQTADVKQLLELEELLKDARREIDGILKSHATESPQETPAYHSEKSDEKSDKLDNH
SQ  ESGASSNGNSHESSSELGEQSKIVSFSKVASKASKQSDGNSDLCNGSVYKEKENGKCGSQINGYYESCKPCNGSDLHDNL
SQ  AESSDRFGELSINGNKISIKSSKMSHKAEARCGISDESRKNKKYTIARISGTHSISVDFRLSRGIAQVNEGNYTKAISIF
SQ  DKVLKEEPTYPEALIGRGTAYAFQRELESAIADFTKAIQSNPAASEAWKRRGQARAALGEYVEAVEDLTKALVFEPNSPD
SQ  VLHERGIVNFKSKDFTAAVKDLSICLKQEKDNKSAYTYLGLAFASLGEYKKAEEAHLKSIQLDSNYLEAWLHLAQFYQEL
SQ  ADHCKALECIEQVLQVDNRVWKAYHLRGLVFHGLGEHRKAIQELSIGLSIENTIECLYLRGSCYHAVGEYRDAVKDYDAT
SQ  VDVELDAVEKFVLQCLAFYQKELALYTASKVSSEFLCFDIDGDIDPMFKEYWCKRLHPKNVCEKVYRQPPLRESLKKGKL
SQ  KKQDLAITKQKANILRFADLIGKRIQYDCPGFLPNKRQHRMAGLAVIEIAQKVSKAWRIEWRNSTKGTTKNGKKNRRRER
SQ  TNILSQNRGGAGCSSSSFSETSTGYASLEDRSSGRSILSWQDVYSPAVRWRQISEPCDPVVWVNKLSEEFNSGFGSHTPM
SQ  VLGQAKVVRYFPNYERTLTLAKSIIKDKLSVRSKKDKVIDLSKDEKIEKIMRAETCDELHNIVGEDFWVATWCDSTGSEG
SQ  KRLEGTRITCIQKPGRLGYDFSIRTPCTPARWSDFDEEMTSAWEALCTAYCGENYGSTELDALETVRDAILRMTYYWYNF
SQ  MPLARGTAVTGFVVLLGLLLAANMEFTETIPKGLQIDWEAILNVEPGSFVDSVKSWLYPSLKINTSWRDHTEISSAFSTT
SQ  GAVVAALSTYND
//
ID  Q2KI99;
PN  Stimulator of interferon genes protein;
GN  STING1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86WV6, ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: Q2KI99;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol. Upon binding of c-di-GMP or cGAMP, STING oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state. In addition to promote the production of type I interferons, plays a direct role in autophagy. Following cGAMP- binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome. The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (By similarity). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'-cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP. The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free-ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (By similarity). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0000139;
GO  GO:0030176;
GO  GO:1990701;
GO  GO:0005741;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:1990231;
GO  GO:0061507;
GO  GO:0035438;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0061629;
GO  GO:0031625;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0071360;
GO  GO:0035458;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0002230;
GO  GO:0051091;
GO  GO:0032728;
GO  GO:0016239;
GO  GO:0032092;
GO  GO:0045944;
GO  GO:0032481;
GO  GO:0060340;
GO  GO:0051259;
GO  GO:0050727;
GO  GO:0061709;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q86WV6};
SQ  MPHSSLHPSIPQPRGLRAQKAALVLLSACLVALWGLGEPPDYTLKWLVLHLASQQMGLLIKGICSLAEELCHVHSRYHGS
SQ  YWRAVRACLCSSMRCGALLLLSCYFYCSLPNMADLPFTWMLALLGLSQALNILLGLQGLAPAEVSAICEKRNFNVAHGLA
SQ  WSYYIGYLRLILPGLPARIQIYNQFHNNTLQGAGSHRLHILFPLDCGVPDDLNVADPNIRFLHELPQQSADRAGIKGRVY
SQ  TNSIYELLENGQRAGVCVLEYATPLQTLFAMSQDGRAGFSREDRLEQAKLFCRTLEDILANAPESQNNCRLIVYQEPAEG
SQ  SSFSLSQEILQHLRQEEREVTMGSTETSVMPGSSVLSQEPELLISGLEKPLPLRSDVF
//
ID  E1C7U0;
PN  Stimulator of interferon genes protein;
GN  STING1;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: E1C7U0;
DR  UNIPROT: A0A1D5P7Q9;
DR  PDB: 6NT6;
DR  PDB: 6NT7;
DR  PDB: 6NT8;
DR  PDB: 6NT9;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (By similarity). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (PubMed:30842659). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes and is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state (PubMed:30842659). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Exhibits 2',3' phosphodiester linkage- specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:30842659}.
DE  Reference Proteome: Yes;
DE  Interaction: E1C7U0; IntAct: EBI-25397709; Score: 0.36
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0061507;
GO  GO:0035438;
GO  GO:0042803;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0032728;
GO  GO:0016239;
GO  GO:0032481;
GO  GO:0051259;
GO  GO:0061709;
TP  Membrane Topology: Transmembrane; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:30842659};
SQ  MPQDPSTRSSPARLLIPEPRAGRARHAACVLLAVCFVVLFLSGEPLAPIIRSVCTQLAALQLGVLLKGCCCLAEEIFHLH
SQ  SRHHGSLWQVLCSCFPPRWYLALLLVGGSAYLDPPEDNGHSPRLALTLSCLCQLLVLALGLQKLSAVEVSELTESSKKNV
SQ  AHGLAWSYYIGYLKVVLPRLKECMEELSRTNPMLRAHRDTWKLHILVPLGCDIWDDLEKADSNIQYLADLPETILTRAGI
SQ  KRRVYKHSLYVIRDKDNKLRPCVLEFASPLQTLCAMSQDDCAAFSREQRLEQARLFYRSLRDILGSSKECAGLYRLIAYE
SQ  EPAEPESHFLSGLILWHLQQQQREEYMVQEELPLGTSSVELSLQVSSSDLPQPLRSDCP
//
ID  E7F4N7;
PN  Stimulator of interferon genes protein;
GN  sting1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23091644}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase tbk1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: E7F4N7;
DR  UNIPROT: K4Q6R6;
DR  PDB: 6MYD;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:23091644). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (PubMed:23091644). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes and is able to activate both NF-kappa-B and irf3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state (PubMed:30842662). In addition to promote the production of type I interferons, plays a direct role in autophagy (PubMed:30842662). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). The ERGIC serves as the membrane source for LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome. The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation. Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:23091644, ECO:0000269|PubMed:30842662}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0061507;
GO  GO:0035438;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0039528;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0038061;
GO  GO:0002230;
GO  GO:0016239;
GO  GO:0032481;
GO  GO:0010506;
GO  GO:0009615;
GO  GO:0061709;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSVMGEDALVPRARSRLPVMCAAGLGFLTLAVAWLLDSDKFSERAGIIAFGLMLERFIYCICLLAEELLFHSRQRYHGRM
SQ  SEIFRACFRGSGILGMCAIFLMLMLGGVSFSVKQWSHFNLMCAGYMLLNSLGVLGPAPVEISEICEAKKMNVAHGLAWSF
SQ  YIGYLKFLLPALEVNVREYSRRERLSSPRLHILLPLNARVPSKPEEEDTNVVFHENLPDLKLDRAGVRKRSYTNSVYKIT
SQ  HNNETFSCILEYATPLLTLYQMSQESSAGFGERERKQQVLLFYRTLSQILDNSLECRNRYRLILLNDEHTGDPHYLSREL
SQ  FQNLKQQDGEIFMDPTNEVHPVPEEGPVGNCNGALQATFHEEPMSDEPTLMFSRPQSLRSEPVETTDYFNPSSAMKQN
//
ID  A0A291NUI5;
PN  Stimulator of interferon genes protein;
GN  STING1;
OS  77214;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: A0A291NUI5;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting that the cGAS-STING pathway promotes a limited inflammatory response (PubMed:29478775). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:29478775}.
DE  Reference Proteome: No;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0035438;
GO  GO:0002218;
GO  GO:0045087;
GO  GO:0032481;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSHSSLHPSIPWPRGHKAKVAAFVLLIVCLAALWKLGEPSDHLLQWLVLHLASLHLRLLFKRVCCLAEELCHIHPRYQGN
SQ  YSRAVRACLGCPIRYGAVLLLSCYFYVSLPNTVDLPLTWMLAHLGLSEALNILLGLQSLTPAEISTICEQRNFNVAHGLA
SQ  WSYYIGYLQLILPGLRARIHTYNQLHSNTLQGVGSHRLYILFPLDCGVLDDLSAADPNIRFLHELPRQSADRAGIKGRVY
SQ  TNSVYELLEKGKPVGTCVLEYATPLQTLFAMSQDGRAGFSQEDRLEQAKLFCRTLEDILADAPESQKNCRLIVYQEPTEE
SQ  SDFSLSQEILKHLRQEEREEVTMGTAGTFVAPGSSTLHQEPELLISGMDQPLPLRTDIF
//
ID  Q86WV6;
PN  Stimulator of interferon genes protein;
GN  STING1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:19285439, ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740, ECO:0000269|PubMed:25254379, ECO:0000269|PubMed:29694889, ECO:0000269|PubMed:30842653, ECO:0000269|PubMed:30842659, ECO:0000269|PubMed:32690950}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:30842659, ECO:0000269|PubMed:32690950}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:29694889, ECO:0000269|PubMed:30842653}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:30842662, ECO:0000269|PubMed:32690950}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:32690950}. Golgi apparatus membrane {ECO:0000269|PubMed:30842653}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:30842662}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:19285439, ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited (PubMed:19433799, PubMed:30842659, PubMed:30842653, PubMed:29694889). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (PubMed:30842662). {ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:29694889, ECO:0000269|PubMed:30842653, ECO:0000269|PubMed:30842659, ECO:0000269|PubMed:30842662, ECO:0000269|PubMed:32690950}.
DR  UNIPROT: Q86WV6;
DR  UNIPROT: A8K3P6;
DR  UNIPROT: B6EB35;
DR  UNIPROT: D6RBX0;
DR  UNIPROT: D6RE01;
DR  UNIPROT: D6RID9;
DR  PDB: 4EF4;
DR  PDB: 4EF5;
DR  PDB: 4EMT;
DR  PDB: 4EMU;
DR  PDB: 4F5D;
DR  PDB: 4F5E;
DR  PDB: 4F5W;
DR  PDB: 4F5Y;
DR  PDB: 4F9E;
DR  PDB: 4F9G;
DR  PDB: 4KSY;
DR  PDB: 4LOH;
DR  PDB: 4LOI;
DR  PDB: 4QXO;
DR  PDB: 4QXP;
DR  PDB: 4QXQ;
DR  PDB: 4QXR;
DR  PDB: 5BQX;
DR  PDB: 5JEJ;
DR  PDB: 6CFF;
DR  PDB: 6CY7;
DR  PDB: 6DNK;
DR  PDB: 6DXG;
DR  PDB: 6DXL;
DR  PDB: 6MX0;
DR  PDB: 6MX3;
DR  PDB: 6MXE;
DR  PDB: 6NT5;
DR  PDB: 6O8B;
DR  PDB: 6O8C;
DR  PDB: 6RM0;
DR  PDB: 6S26;
DR  PDB: 6S27;
DR  PDB: 6S86;
DR  PDB: 6UKM;
DR  PDB: 6UKU;
DR  PDB: 6UKV;
DR  PDB: 6UKW;
DR  PDB: 6UKX;
DR  PDB: 6UKY;
DR  PDB: 6UKZ;
DR  PDB: 6UL0;
DR  PDB: 6XF3;
DR  PDB: 6XF4;
DR  PDB: 6XNP;
DR  PDB: 6Y99;
DR  PDB: 6YWA;
DR  PDB: 7KVX;
DR  PDB: 7KW1;
DR  Pfam: PF15009;
DR  OMIM: 612374;
DR  OMIM: 615934;
DR  DisGeNET: 340061;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:18724357, PubMed:18818105, PubMed:19433799, PubMed:19776740, PubMed:23027953, PubMed:23910378, PubMed:23747010, PubMed:29973723, PubMed:30842659, PubMed:35045565). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (PubMed:26300263). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (PubMed:21947006, PubMed:23258412, PubMed:23707065, PubMed:23722158, PubMed:26229117, PubMed:23910378, PubMed:23747010, PubMed:30842659). Upon binding of c- di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (PubMed:22394562, PubMed:25636800, PubMed:29973723, PubMed:30842653, PubMed:35045565). In addition to promote the production of type I interferons, plays a direct role in autophagy (PubMed:30568238, PubMed:30842662). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (PubMed:30842662). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (PubMed:30842662). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (PubMed:30568238, PubMed:30842662). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (By similarity). Exhibits 2',3' phosphodiester linkage- specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'- cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:26300263, PubMed:23910378, PubMed:23747010). The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free- ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation (PubMed:26150511). May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (PubMed:18724357). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740, ECO:0000269|PubMed:21947006, ECO:0000269|PubMed:22394562, ECO:0000269|PubMed:23027953, ECO:0000269|PubMed:23258412, ECO:0000269|PubMed:23707065, ECO:0000269|PubMed:23722158, ECO:0000269|PubMed:23747010, ECO:0000269|PubMed:23910378, ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:26150511, ECO:0000269|PubMed:26229117, ECO:0000269|PubMed:26300263, ECO:0000269|PubMed:29973723, ECO:0000269|PubMed:30568238, ECO:0000269|PubMed:30842653, ECO:0000269|PubMed:30842659, ECO:0000269|PubMed:30842662, ECO:0000269|PubMed:35045565}. (Microbial infection) Antiviral activity is antagonized by oncoproteins, such as papillomavirus (HPV) protein E7 and adenovirus early E1A protein (PubMed:26405230). Such oncoproteins prevent the ability to sense cytosolic DNA (PubMed:26405230). {ECO:0000269|PubMed:26405230}.
DE  Disease: STING-associated vasculopathy, infantile-onset (SAVI) [MIM:615934]: An autoinflammatory disease characterized by early-onset systemic inflammation and cutaneous vasculopathy, resulting in severe skin lesions. Violaceous, scaling lesions of fingers, toes, nose, cheeks and ears progress to acral necrosis in most of the patients. Some patients have severe interstitial lung disease. {ECO:0000269|PubMed:25029335, ECO:0000269|PubMed:25401470, ECO:0000269|PubMed:30842659}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P0C6X5; IntAct: EBI-25622122; Score: 0.46
DE  Interaction: P0C6X7; IntAct: EBI-25751009; Score: 0.40
DE  Interaction: P12270; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: P27958; IntAct: EBI-8790013; Score: 0.54
DE  Interaction: Q5NEU6; IntAct: EBI-2800350; Score: 0.00
DE  Interaction: Q16666; IntAct: EBI-3862073; Score: 0.52
DE  Interaction: P42226; IntAct: EBI-5237739; Score: 0.63
DE  Interaction: Q7Z434; IntAct: EBI-5237922; Score: 0.84
DE  Interaction: Q969M3; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: O15118; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: Q8TCT9; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-6116464; Score: 0.50
DE  Interaction: P33527; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: O95573; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: P46977; IntAct: EBI-6116464; Score: 0.50
DE  Interaction: Q8TCJ2; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: P39656; IntAct: EBI-6116464; Score: 0.50
DE  Interaction: Q8NE01; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-6116464; Score: 0.90
DE  Interaction: Q96KA5; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: Q92990; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: Q4ZIN3; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: O15260; IntAct: EBI-6116464; Score: 0.62
DE  Interaction: Q15043; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: O95470; IntAct: EBI-6116464; Score: 0.50
DE  Interaction: Q96A33; IntAct: EBI-6116464; Score: 0.50
DE  Interaction: O94822; IntAct: EBI-6116464; Score: 0.50
DE  Interaction: Q96N66; IntAct: EBI-6116464; Score: 0.50
DE  Interaction: P61619; IntAct: EBI-6116464; Score: 0.35
DE  Interaction: P17020; IntAct: EBI-6509669; Score: 0.37
DE  Interaction: Q99IB8; IntAct: EBI-8786474; Score: 0.46
DE  Interaction: Q86WV6; IntAct: EBI-8803392; Score: 0.96
DE  Interaction: O60488; IntAct: EBI-8789904; Score: 0.27
DE  Interaction: Q96DZ9; IntAct: EBI-23747110; Score: 0.56
DE  Interaction: Q9Y342; IntAct: EBI-24736301; Score: 0.56
DE  Interaction: Q9NZ01; IntAct: EBI-23834338; Score: 0.56
DE  Interaction: Q96HR9; IntAct: EBI-24767652; Score: 0.56
DE  Interaction: Q9NV29; IntAct: EBI-23859114; Score: 0.56
DE  Interaction: Q9BWQ6; IntAct: EBI-23922496; Score: 0.56
DE  Interaction: B2RUZ4; IntAct: EBI-25148720; Score: 0.56
DE  Interaction: Q13190; IntAct: EBI-24659319; Score: 0.56
DE  Interaction: O95214; IntAct: EBI-24800678; Score: 0.56
DE  Interaction: Q96NY8; IntAct: EBI-21898607; Score: 0.40
DE  Interaction: P43308; IntAct: EBI-15725012; Score: 0.48
DE  Interaction: O95786; IntAct: EBI-15725052; Score: 0.52
DE  Interaction: P60468; IntAct: EBI-15725077; Score: 0.35
DE  Interaction: P09913; IntAct: EBI-15778414; Score: 0.56
DE  Interaction: P09914; IntAct: EBI-15778491; Score: 0.56
DE  Interaction: Q14164; IntAct: EBI-15780301; Score: 0.40
DE  Interaction: P06788; IntAct: EBI-16178391; Score: 0.40
DE  Interaction: P03255; IntAct: EBI-16178410; Score: 0.40
DE  Interaction: Q9UM54; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q9UBE0; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q9NVH2; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q9NQT4; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q9BZL6; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q96HW7; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q8WV92; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q8TDD1; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q8N201; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q8IUH3; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q70E73; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q4V328; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: P49770; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: P43307; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: P26358; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: P18031; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: O15120; IntAct: EBI-20201138; Score: 0.35
DE  Interaction: Q92733; IntAct: EBI-20201323; Score: 0.35
DE  Interaction: Q08AM6; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: Q9H0H0; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: Q9Y6R6; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: Q9Y679; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: P40763; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: P04196; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: P01584; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: O60669; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: A7E2V4; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: Q14653; IntAct: EBI-25751145; Score: 0.40
DE  Interaction: P0CG47; IntAct: EBI-25751339; Score: 0.40
DE  Interaction: P0DTD2; IntAct: EBI-25819292; Score: 0.46
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0000139;
GO  GO:0030176;
GO  GO:1990701;
GO  GO:0005741;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:0030667;
GO  GO:1902554;
GO  GO:1990231;
GO  GO:0061507;
GO  GO:0035438;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0061629;
GO  GO:0031625;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0071360;
GO  GO:0035458;
GO  GO:0071407;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0002230;
GO  GO:0051091;
GO  GO:0032728;
GO  GO:0016239;
GO  GO:0032092;
GO  GO:0045944;
GO  GO:0032481;
GO  GO:0060340;
GO  GO:0051259;
GO  GO:0050727;
GO  GO:0061709;
TP  Membrane Topology: Transmembrane; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:30842659};
SQ  MPHSSLHPSIPCPRGHGAQKAALVLLSACLVTLWGLGEPPEHTLRYLVLHLASLQLGLLLNGVCSLAEELRHIHSRYRGS
SQ  YWRTVRACLGCPLRRGALLLLSIYFYYSLPNAVGPPFTWMLALLGLSQALNILLGLKGLAPAEISAVCEKGNFNVAHGLA
SQ  WSYYIGYLRLILPELQARIRTYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLSMADPNIRFLDKLPQQTGDHAGIKDRVY
SQ  SNSIYELLENGQRAGTCVLEYATPLQTLFAMSQYSQAGFSREDRLEQAKLFCRTLEDILADAPESQNNCRLIAYQEPADD
SQ  SSFSLSQEVLRHLRQEEKEEVTVGSLKTSAVPSTSTMSQEPELLISGMEKPLPLRTDFS
//
ID  Q3TBT3;
PN  Stimulator of interferon genes protein;
GN  Sting1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19776740, ECO:0000269|PubMed:27324217}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:28930687}; Multi- pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:27324217, ECO:0000269|PubMed:29973723}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:29056340, ECO:0000269|PubMed:29496741}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:18559423}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:18559423}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: Q3TBT3;
DR  UNIPROT: A7YGY9;
DR  UNIPROT: Q3TAV5;
DR  UNIPROT: Q3TYP5;
DR  UNIPROT: Q3TZY8;
DR  UNIPROT: Q3UJW3;
DR  UNIPROT: Q8C227;
DR  UNIPROT: Q8C5Q3;
DR  UNIPROT: Q8K393;
DR  UNIPROT: Q9CZY7;
DR  PDB: 4JC5;
DR  PDB: 4KBY;
DR  PDB: 4KC0;
DR  PDB: 4LOJ;
DR  PDB: 4LOK;
DR  PDB: 4LOL;
DR  PDB: 4YP1;
DR  PDB: 6XNN;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:18818105, PubMed:19433799, PubMed:19776740, PubMed:26229117, PubMed:26669264, PubMed:27324217, PubMed:28529930, PubMed:29973723). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (PubMed:18818105, PubMed:19433799, PubMed:19776740, PubMed:26229117, PubMed:26669264). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (PubMed:21947006, PubMed:23722158, PubMed:23258412, PubMed:23519410, PubMed:23910378). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (PubMed:25636800, PubMed:27324217, PubMed:29973723). In addition to promote the production of type I interferons, plays a direct role in autophagy (PubMed:30568238). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (PubMed:29056340). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'-cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:26300263). The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free- ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation (By similarity). May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (By similarity). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (PubMed:18559423). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:18559423, ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740, ECO:0000269|PubMed:21947006, ECO:0000269|PubMed:23258412, ECO:0000269|PubMed:23519410, ECO:0000269|PubMed:23722158, ECO:0000269|PubMed:23910378, ECO:0000269|PubMed:25636800, ECO:0000269|PubMed:26229117, ECO:0000269|PubMed:26300263, ECO:0000269|PubMed:26669264, ECO:0000269|PubMed:27324217, ECO:0000269|PubMed:28529930, ECO:0000269|PubMed:29056340, ECO:0000269|PubMed:29973723, ECO:0000269|PubMed:30568238}.
DE  Reference Proteome: Yes;
DE  Interaction: A2AT37; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q16666; IntAct: EBI-3862096; Score: 0.40
DE  Interaction: P52633; IntAct: EBI-5237821; Score: 0.35
DE  Interaction: Q9WUN2; IntAct: EBI-5237821; Score: 0.56
DE  Interaction: Q91VN6; IntAct: EBI-5323837; Score: 0.66
DE  Interaction: Q69ZN7; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9CWP6; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P23249; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P27046; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P46978; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6NZJ6; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q2EMV9; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q3TNL8; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6P4T2; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6PD26; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q3UPH7; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8BFZ9; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: A8C756; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: D4AFX7; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q3UJB9; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6ZQ08; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q7TQH0; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9EPL8; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6PIC6; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8BWZ3; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: E9PVA8; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8C7X2; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q569Z6; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q3UU96; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: E9QKZ2; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9CY50; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8CGC7; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q5SWU9; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: E9QAE3; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6P5B0; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q80U72; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q91YQ5; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8BH79; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: E9Q7G0; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: A2ANY6; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q99MR6; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9EP69; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8CAS9; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: E9PZJ8; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: L7N451; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6P5D8; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6ZQ58; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q924C1; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9D071; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8K1R3; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: B9EJ54; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8BKC5; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9D8C4; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: B2RQC6; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q3ULL6; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: G5E829; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9CR67; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q922J9; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q68FD5; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9EPK7; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: O35309; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: G5E8N7; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: O89079; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9ESJ0; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9JLI8; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P61620; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9Z1D1; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q922D4; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9CQM9; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9JKF1; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q60931; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q60930; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9Z1Q9; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q62351; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q01320; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q64310; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9Z315; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P07091; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q9EPU0; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P55096; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P12382; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P27546; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P97310; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q80ZH7; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6P9P6; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q61699; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q31125; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P13864; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: O54734; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: O35129; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: O55143; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P14094; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8VDN2; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: P14869; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q921K2; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q61102; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q99PV0; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6PDQ2; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8BWY9; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q8BX17; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q3UIR3; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: Q6NZL1; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: O54957; IntAct: EBI-12602258; Score: 0.35
DE  Interaction: Q3U1F9; IntAct: EBI-12603102; Score: 0.35
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0030176;
GO  GO:1990701;
GO  GO:0005741;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:1990231;
GO  GO:0061507;
GO  GO:0035438;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0061629;
GO  GO:0031625;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0071360;
GO  GO:0035458;
GO  GO:0071407;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0002230;
GO  GO:0051091;
GO  GO:0032728;
GO  GO:0016239;
GO  GO:0032092;
GO  GO:0045944;
GO  GO:0032481;
GO  GO:0060340;
GO  GO:0051259;
GO  GO:0010468;
GO  GO:0050727;
GO  GO:0061709;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q86WV6};
SQ  MPYSNLHPAIPRPRGHRSKYVALIFLVASLMILWVAKDPPNHTLKYLALHLASHELGLLLKNLCCLAEELCHVQSRYQGS
SQ  YWKAVRACLGCPIHCMAMILLSSYFYFLQNTADIYLSWMFGLLVLYKSLSMLLGLQSLTPAEVSAVCEEKKLNVAHGLAW
SQ  SYYIGYLRLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDNLSVVDPNIRFRDMLPQQNIDRAGIKNRVYS
SQ  NSVYEILENGQPAGVCILEYATPLQTLFAMSQDAKAGFSREDRLEQAKLFCRTLEEILEDVPESRNNCRLIVYQEPTDGN
SQ  SFSLSQEVLRHIRQEEKEEVTMNAPMTSVAPPPSVLSQEPRLLISGMDQPLPLRTDLI
//
ID  B8XX90;
PN  Stimulator of interferon genes protein;
GN  STING1;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20346968}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86WV6, ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:20346968}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: B8XX90;
DR  PDB: 6A03;
DR  PDB: 6A04;
DR  PDB: 6A05;
DR  PDB: 6A06;
DR  PDB: 6IYF;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol. Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state. In addition to promote the production of type I interferons, plays a direct role in autophagy. Following cGAMP- binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome. The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (By similarity). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'-cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP. The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free-ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (By similarity). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}.
DE  Reference Proteome: Yes;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0061507;
GO  GO:0035438;
GO  GO:0042803;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0032728;
GO  GO:0016239;
GO  GO:0032481;
GO  GO:0061709;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q86WV6};
SQ  MPYSSLHPSIPQPRGLRAQVAALVLLGACLVALWGLGELPEYTLRWLVLHLASQQIGLLVKGLCSLAEELCHVHSRYQSS
SQ  YWRAARACLGCPIRCGALLLLSCYFYFSIRDKAGLPLPWMLALLGLSQALNILLGLQHLAPAEVSAICEKRNFNVAHGLA
SQ  WSYYIGYLRLILPGLRARIQAYNQRHKNVLGGIGNHRLHILFPLDCGVPDDLSVADPNIRFLHELPQQSADRAGIKGRVY
SQ  TNSIYELLENGQPAGVCVLGYATPLQTLFAMSQDGRAGFSREDRLEQAKLFCRTLEDILADAPEAQNNCRLIVYQEPTEG
SQ  GSFSLSQEILRHLRQEEREVTMGSAETSVVPTSSTLSQEPELLISGMEQPLPLRSDIF
//
ID  A0A291NUG3;
PN  Stimulator of interferon genes protein;
GN  STING1;
OS  59476;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: A0A291NUG3;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting that the cGAS-STING pathway promotes a limited inflammatory response (PubMed:29478775). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:29478775}.
DE  Reference Proteome: No;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0035438;
GO  GO:0002218;
GO  GO:0045087;
GO  GO:0032481;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLHSSLHPSIPQPRGRRAKKAAFVLLSVCLVVLWDLGERPEHILQWLMLHLASLQLGLLFKGVCSLVEELRHVHSRYQGS
SQ  YWKAVRACLGCPIRCGTLLLLSCYFYTPFPNTTHLPFTWTLALLGLSQALSILLDLQDLAPAEVSAVCERRNLNVAQGMA
SQ  WSFYIGYLRLILPGLPARIHSYNQHHNNLLRGAGSHRLYILFPLDCGVPDDLSMVDPNIRFLHELPLQKADRAGIKSRVY
SQ  TNSVYELLENGRPVGACVLEYATPLQTLFAMSQDSRAGFSREDRLEQAKLFCKTLEDILADAPECQNNCRLVVYQEPAEG
SQ  GNFSLSQEILRHLKQEEKEEVTVDSARTSVMPDPSMLPQGPELLISSMDQPLPLRTDVF
//
ID  F1M391;
PN  Stimulator of interferon genes protein;
GN  Sting1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86WV6, ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: F1M391;
DR  PDB: 5GRM;
DR  PDB: 5GS5;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:26669264). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (PubMed:26669264). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (By similarity). Exhibits 2',3' phosphodiester linkage- specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'- cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:26669264). The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free-ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation (By similarity). May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (By similarity). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:26669264}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0030176;
GO  GO:1990701;
GO  GO:0005741;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0005886;
GO  GO:1990231;
GO  GO:0061507;
GO  GO:0035438;
GO  GO:0042802;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0061629;
GO  GO:0031625;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0071360;
GO  GO:0035458;
GO  GO:0071407;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0002230;
GO  GO:0051091;
GO  GO:0032728;
GO  GO:0016239;
GO  GO:0032092;
GO  GO:0045944;
GO  GO:0032481;
GO  GO:0060340;
GO  GO:0051259;
GO  GO:0010468;
GO  GO:0050727;
GO  GO:0061709;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q86WV6};
SQ  MPYSNLHPSIPRPRSYRFKLAAFVLLVGSLMSLWMTGEPPSHTLHYLALHVASQQLGLLLKKLCCLAEELCHVQSRYQGS
SQ  YWKAVRACVGSPICFMALILLSFYFYCSLENTSDLRLAWHLGILVLSKSLSMTLDLQSLAPAEVSAVCEEKNFNVAHGLA
SQ  WSYYIGYLKLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDDLSVADPNIRFRDMLPQQNTDRAGVKNRAY
SQ  SNSVYELLENGQPAGACILEYATPLQTLFAMSQDGKAGFSREDRLEQAKLFCRTLEEILADVPESRNHCRLIVYQESEEG
SQ  NSFSLSQEVLRHIRQEEKEEVTMSGPPTSVAPRPSLLSQEPRLLISGMEQPLPLRTDLI
//
ID  A0A291NUI4;
PN  Stimulator of interferon genes protein;
GN  STING1;
OS  59479;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). {ECO:0000250|UniProtKB:Q86WV6}.
DR  UNIPROT: A0A291NUI4;
DR  Pfam: PF15009;
DE  Function: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting that the cGAS-STING pathway promotes a limited inflammatory response (PubMed:29478775). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:29478775}.
DE  Reference Proteome: Yes;
GO  GO:0000421;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0035438;
GO  GO:0002218;
GO  GO:0045087;
GO  GO:0032481;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPHSSLHPSIPRPRGHRAKKAAFVLLSTCLAALWELGEPADHILRWLVLHLASEQLGLLFKGLCSLAEEIRHVHSRYQGS
SQ  YWRAFRACLGCPIRCGVLLLLSCYCYTFLPNTAGLPFAWIVALLGLSQALNILLDLQGLAPAVVSTVCEQGNFNVAHGLA
SQ  WSYYIGYLRLILPGLQARIHTYNQRHNNTVRGTGVHKLYILLPLDCGVPDDLSVADPNIRFLHELPKQSADRAGIKGRVY
SQ  TNSIYEILENGKPVGTCVLEYATPLQTLFAMSQDSRAGFSREERLEQAKLFCQTLGDILADVPESQYCRLIVYLDAAEGS
SQ  SFSLSQEILKHLKQEEKEEVTVGTMGSSGVLESSTLDKEPQLLISGMDQPLPLRTDVF
//
ID  A8E5V9;
PN  Stimulator of interferon genes protein;
GN  sting1;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30842662}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase tbk1 is recruited (PubMed:30842662). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:30842662}.
DR  UNIPROT: A8E5V9;
DR  Pfam: PF15009;
DE  Function: Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy. Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol (PubMed:26300263, PubMed:30842662). Following cGAMP-binding, promotes the formation of autophagosomes, leading to target cytosolic DNA for degradation by the lysosome (PubMed:30842662). Exhibits guanine base- specific ligand recognition. Binds 3'-3'linked cGAMP, 2'-3' linked cGAMP and 3'-3' linked c-di-GMP with much greater affinity as compared to 3'-3' linked c-di-AMP (PubMed:26300263). Lacks the C-terminal tail (CTT) found in other vertebrate orthologs which is essential for interferon signaling (PubMed:26300263). {ECO:0000269|PubMed:26300263, ECO:0000269|PubMed:30842662}.
DE  Reference Proteome: Yes;
GO  GO:0005776;
GO  GO:0000421;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0061507;
GO  GO:0035438;
GO  GO:0042803;
GO  GO:0002218;
GO  GO:0000045;
GO  GO:0051607;
GO  GO:0045087;
GO  GO:0032728;
GO  GO:0016239;
GO  GO:0032481;
GO  GO:0061709;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MACVLAIGSILFVWILGKGKYSGAQLIYRMATNFAISQGCCLVTCACELTEEIKHLHTRYNGHYWRALKASFNLSCAAFV
SQ  TAILCYVFYEPKLMASLPLTIDITLTLLSWLFCWILGIQGPTPATISEITEIKQLNVAHGLAWSYYVGYLQFVLPALKES
SQ  IQKFNEENHNLLKFPETCRLHILIPLSCRLYGDLKDVDENITFLKEIPPLYIDRAGIKGRVFKNNVYRILDEDGRPYNCI
SQ  VEYATPLASLLKMTDIPSAAFSADDRLQQTKLFYRTLKDILENAHELQNTYRLIVYEDFPETKDHSRHLLSQEILKHIRQ
SQ  QHSEEYSML
//
ID  O75716;
PN  Serine/threonine-protein kinase 16;
GN  STK16;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles. {ECO:0000250}.
DR  UNIPROT: O75716;
DR  UNIPROT: A8K9H9;
DR  UNIPROT: Q5U0F8;
DR  UNIPROT: Q96KI2;
DR  UNIPROT: Q9BUH4;
DR  UNIPROT: Q9UEN3;
DR  UNIPROT: Q9UP78;
DR  PDB: 2BUJ;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 604719;
DR  DisGeNET: 8576;
DE  Function: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. {ECO:0000269|PubMed:10364453}.
DE  Reference Proteome: Yes;
DE  Interaction: O15162; IntAct: EBI-10189073; Score: 0.56
DE  Interaction: P49247; IntAct: EBI-757201; Score: 0.67
DE  Interaction: Q8N5Z5; IntAct: EBI-757423; Score: 0.78
DE  Interaction: Q6UY14; IntAct: EBI-757837; Score: 0.62
DE  Interaction: Q15583; IntAct: EBI-1060072; Score: 0.00
DE  Interaction: Q05084; IntAct: EBI-1061392; Score: 0.00
DE  Interaction: Q9NRH2; IntAct: EBI-1063140; Score: 0.00
DE  Interaction: O75116; IntAct: EBI-1066240; Score: 0.00
DE  Interaction: P26441; IntAct: EBI-1066319; Score: 0.00
DE  Interaction: Q96RG2; IntAct: EBI-1067304; Score: 0.00
DE  Interaction: P63162; IntAct: EBI-1070450; Score: 0.00
DE  Interaction: Q93063; IntAct: EBI-1070470; Score: 0.00
DE  Interaction: P41235; IntAct: EBI-1071104; Score: 0.00
DE  Interaction: P40337; IntAct: EBI-1074035; Score: 0.00
DE  Interaction: Q9HB66; IntAct: EBI-1075221; Score: 0.00
DE  Interaction: Q14680; IntAct: EBI-1078077; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1078621; Score: 0.00
DE  Interaction: Q6P2I7; IntAct: EBI-1084989; Score: 0.00
DE  Interaction: Q8N5R6; IntAct: EBI-8639058; Score: 0.37
DE  Interaction: P67870; IntAct: EBI-7136780; Score: 0.37
DE  Interaction: Q8IWZ5; IntAct: EBI-10189041; Score: 0.72
DE  Interaction: P50222; IntAct: EBI-10189051; Score: 0.56
DE  Interaction: Q8IYX7; IntAct: EBI-10189061; Score: 0.72
DE  Interaction: O43186; IntAct: EBI-10189085; Score: 0.56
DE  Interaction: O43597; IntAct: EBI-10189095; Score: 0.56
DE  Interaction: O43734; IntAct: EBI-10189107; Score: 0.56
DE  Interaction: O95967; IntAct: EBI-10189117; Score: 0.72
DE  Interaction: P12757; IntAct: EBI-10189127; Score: 0.56
DE  Interaction: P14373; IntAct: EBI-10189139; Score: 0.56
DE  Interaction: P15884; IntAct: EBI-10189151; Score: 0.56
DE  Interaction: P60370; IntAct: EBI-10189177; Score: 0.56
DE  Interaction: P60409; IntAct: EBI-10189187; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-10189197; Score: 0.72
DE  Interaction: P60411; IntAct: EBI-10189209; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-10189221; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-10189231; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-10189241; Score: 0.72
DE  Interaction: Q13137; IntAct: EBI-10189253; Score: 0.56
DE  Interaction: Q13829; IntAct: EBI-10189263; Score: 0.56
DE  Interaction: Q15654; IntAct: EBI-10189275; Score: 0.56
DE  Interaction: Q5JR59; IntAct: EBI-10189289; Score: 0.56
DE  Interaction: Q5JST6; IntAct: EBI-10189301; Score: 0.56
DE  Interaction: Q5JXC2; IntAct: EBI-10189313; Score: 0.67
DE  Interaction: Q6PEX3; IntAct: EBI-10189325; Score: 0.56
DE  Interaction: Q7Z3S9; IntAct: EBI-10189344; Score: 0.56
DE  Interaction: Q8HWS3; IntAct: EBI-10189356; Score: 0.56
DE  Interaction: Q92824; IntAct: EBI-10189400; Score: 0.56
DE  Interaction: Q96EY1; IntAct: EBI-10189410; Score: 0.56
DE  Interaction: Q96Q35; IntAct: EBI-10189422; Score: 0.56
DE  Interaction: Q99081; IntAct: EBI-10189434; Score: 0.56
DE  Interaction: Q9BQ13; IntAct: EBI-10189446; Score: 0.67
DE  Interaction: Q9GZT8; IntAct: EBI-10189463; Score: 0.56
DE  Interaction: Q9NRY6; IntAct: EBI-10189475; Score: 0.72
DE  Interaction: Q9UKT9; IntAct: EBI-10189487; Score: 0.56
DE  Interaction: Q9Y295; IntAct: EBI-10325852; Score: 0.56
DE  Interaction: Q8XC86; IntAct: EBI-10038684; Score: 0.37
DE  Interaction: Q7DB77; IntAct: EBI-10039518; Score: 0.51
DE  Interaction: B7UM99; IntAct: EBI-10040304; Score: 0.37
DE  Interaction: Q13185; IntAct: EBI-24281792; Score: 0.56
DE  Interaction: A8MQ03; IntAct: EBI-24308246; Score: 0.56
DE  Interaction: P0DPK4; IntAct: EBI-24330984; Score: 0.56
DE  Interaction: Q7Z3K6; IntAct: EBI-24336466; Score: 0.56
DE  Interaction: Q70EL1; IntAct: EBI-24353346; Score: 0.56
DE  Interaction: Q9NQX0; IntAct: EBI-24363537; Score: 0.56
DE  Interaction: Q8IUG1; IntAct: EBI-25258808; Score: 0.56
DE  Interaction: Q96KN3; IntAct: EBI-25259197; Score: 0.56
DE  Interaction: Q9Y3S2; IntAct: EBI-24486018; Score: 0.56
DE  Interaction: P51114; IntAct: EBI-24486544; Score: 0.56
DE  Interaction: P31321; IntAct: EBI-24491334; Score: 0.56
DE  Interaction: O95994; IntAct: EBI-24509792; Score: 0.56
DE  Interaction: Q2I0M5; IntAct: EBI-24516412; Score: 0.56
DE  Interaction: O15496; IntAct: EBI-24522989; Score: 0.56
DE  Interaction: Q96D03; IntAct: EBI-24524948; Score: 0.56
DE  Interaction: Q9HBZ2; IntAct: EBI-24529669; Score: 0.56
DE  Interaction: A8MUP2; IntAct: EBI-24619225; Score: 0.56
DE  Interaction: Q03431; IntAct: EBI-24625735; Score: 0.56
DE  Interaction: Q8IUC1; IntAct: EBI-24630962; Score: 0.56
DE  Interaction: Q93015; IntAct: EBI-24640795; Score: 0.56
DE  Interaction: Q06546; IntAct: EBI-24716574; Score: 0.56
DE  Interaction: Q6NX45; IntAct: EBI-25275432; Score: 0.56
DE  Interaction: O14508; IntAct: EBI-23924597; Score: 0.56
DE  Interaction: Q52LG2; IntAct: EBI-24408520; Score: 0.56
DE  Interaction: Q07627; IntAct: EBI-24428974; Score: 0.56
DE  Interaction: Q15323; IntAct: EBI-24437382; Score: 0.56
DE  Interaction: Q5T749; IntAct: EBI-24469802; Score: 0.56
DE  Interaction: P27918; IntAct: EBI-24556586; Score: 0.56
DE  Interaction: Q9Y6H3; IntAct: EBI-24559916; Score: 0.56
DE  Interaction: O43559; IntAct: EBI-24586436; Score: 0.56
DE  Interaction: Q7RTU4; IntAct: EBI-24593098; Score: 0.56
DE  Interaction: Q6P1L6; IntAct: EBI-24603190; Score: 0.56
DE  Interaction: Q9BS75; IntAct: EBI-24604089; Score: 0.56
DE  Interaction: Q9Y4P1; IntAct: EBI-21856478; Score: 0.35
DE  Interaction: Q96GV9; IntAct: EBI-21856478; Score: 0.35
DE  Interaction: Q8WVV4; IntAct: EBI-21856478; Score: 0.35
DE  Interaction: Q6ZVX7; IntAct: EBI-21856478; Score: 0.35
DE  Interaction: Q6BDS2; IntAct: EBI-21856478; Score: 0.35
DE  Interaction: Q5QP82; IntAct: EBI-21856478; Score: 0.35
DE  Interaction: Q3ZCM7; IntAct: EBI-21856478; Score: 0.35
DE  Interaction: Q13509; IntAct: EBI-21856478; Score: 0.35
DE  Interaction: P20930; IntAct: EBI-21856478; Score: 0.35
DE  Interaction: P32233; IntAct: EBI-15679531; Score: 0.64
DE  Interaction: Q9Y2A7; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: Q92896; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: Q8IWX8; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: Q14566; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: Q13405; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: Q12888; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: Q06418; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: P61081; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: P41240; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: P33993; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: P31350; IntAct: EBI-28931389; Score: 0.35
DE  Interaction: P09497; IntAct: EBI-28931389; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005798;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0004715;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0000978;
GO  GO:0071560;
GO  GO:0045944;
GO  GO:0046777;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Curator Inference {ECO:0000305|PubMed:10364453};
SQ  MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRL
SQ  VAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEG
SQ  QPVLMDLGSMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQ
SQ  KGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQHTTQI
//
ID  O88697;
PN  Serine/threonine-protein kinase 16;
GN  Stk16;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9712705}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles.
DR  UNIPROT: O88697;
DR  UNIPROT: Q3UEG5;
DR  UNIPROT: Q9JMJ0;
DR  UNIPROT: Q9JMJ1;
DR  UNIPROT: Q9QX00;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates (By similarity). May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. {ECO:0000250, ECO:0000269|PubMed:9878782}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005798;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0004715;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0000978;
GO  GO:0071560;
GO  GO:0045944;
GO  GO:0046777;
GO  GO:0006468;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGHALCVCSRGTVIIDNKRYLFVQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDQEEAQREAEMHRLFQHPNILRL
SQ  MAYSLKERGAKHEAWLLLPFFKKGTLWNEIERLKDQGSFLTEDQILPLLLGISRGLEAIHAKGYAHRDLKPTNILLGDEG
SQ  QPVLMDLGSMNQACIQVEGSRQALALQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQ
SQ  KGDSVALAVQNELSIPQSPRHSSALRQLLSSMMTVDPQQRPHIPVLLSQLEALQPPAPGQHTTQI
//
ID  P57760;
PN  Serine/threonine-protein kinase 16;
GN  Stk16;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles. {ECO:0000250}.
DR  UNIPROT: P57760;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates (By similarity). May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005798;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005524;
GO  GO:0004715;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0000978;
GO  GO:0071560;
GO  GO:0045944;
GO  GO:0046777;
GO  GO:0006468;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGHALCVCSRGTVIIDNKRYLFVQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDQEEAQREADMHRLFQHPNILRL
SQ  MAYSLKERGAKHEAWLLLPFFKRGTLWNEIERLKDQGNFLTEDQILPLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEG
SQ  QPVLMDLGSMNQACIQVEGSRQALALQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQ
SQ  KGDSVALAVQNDLSIPQSPRHSSALRQLLASMMTVDPQQRPHIPVLLSQLEALQPPAPGQHTTQI
//
ID  Q0VD22;
PN  Serine/threonine-protein kinase 33;
GN  STK33;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q0VD22;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0044773;
GO  GO:0006468;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADSSCGKKSTKCPHCSSASQKNALCICSCKTKLSPMSVVEMSQTSSTGSSEFIVSPEKRKEKGASKDVTSGKDSPSKSS
SQ  NIERKPSQQQWGRGNFTEGKVPHIRMDNGAALQEIYTFGRILGQGSFGMVIEAIDKERETKWAIKKVNKEKAGSSAVKLL
SQ  EREVDILKSVKHEHIIHLEQVFETPKKMYLVMELCEDGELKEILERKGHFSENETRWIIQSLASAIAYLHNKDIVHRDLK
SQ  LENIMVKSSFIDANNEMNLNIKVTDFGLAVKKHGRSEVMLQTTCGTPIYMAPEVINAHDYSQQCDIWSIGVIMYILLCGK
SQ  APFMASSEEKLFELIKKGELHFKNSIWNSISDCAKSVLKQLMKVDPAHRITAKELLDNQWLTGNTVSSARPTNVLEMMKE
SQ  WKNNPESDEESTTDQRDSRSGQEESKVYQPSRNVPDVSNSSDEEEGKQVGRTNKTCRKNNCFISPNCEIPSQHLEHFCNS
SQ  FFVVGL
//
ID  Q9BYT3;
PN  Serine/threonine-protein kinase 33;
GN  STK33;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}.
DR  UNIPROT: Q9BYT3;
DR  UNIPROT: Q658S6;
DR  UNIPROT: Q8NEF5;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 607670;
DR  DisGeNET: 65975;
DE  Function: Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME (By similarity). Not essential for the survival of KRAS-dependent AML cell lines. {ECO:0000250, ECO:0000269|PubMed:21742770}.
DE  Reference Proteome: Yes;
DE  Interaction: P29692; IntAct: EBI-2687046; Score: 0.00
DE  Interaction: Q8IVS8; IntAct: EBI-3925286; Score: 0.37
DE  Interaction: P14618; IntAct: EBI-9353489; Score: 0.44
DE  Interaction: Q5S007; IntAct: EBI-9660321; Score: 0.44
DE  Interaction: O43852; IntAct: EBI-20903056; Score: 0.40
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q9HCN8; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: Q96TA2; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: Q8WVX9; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: Q13451; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: P35613; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: P27708; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: P09543; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: P08631; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: P00367; IntAct: EBI-28946086; Score: 0.35
DE  Interaction: O43819; IntAct: EBI-28946086; Score: 0.35
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0044773;
GO  GO:0046777;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADSGLDKKSTKCPDCSSASQKDVLCVCSSKTRVPPVLVVEMSQTSSIGSAESLISLERKKEKNINRDITSRKDLPSRTS
SQ  NVERKASQQQWGRGNFTEGKVPHIRIENGAAIEEIYTFGRILGKGSFGIVIEATDKETETKWAIKKVNKEKAGSSAVKLL
SQ  EREVNILKSVKHEHIIHLEQVFETPKKMYLVMELCEDGELKEILDRKGHFSENETRWIIQSLASAIAYLHNNDIVHRDLK
SQ  LENIMVKSSLIDDNNEINLNIKVTDFGLAVKKQSRSEAMLQATCGTPIYMAPEVISAHDYSQQCDIWSIGVVMYMLLRGE
SQ  PPFLASSEEKLFELIRKGELHFENAVWNSISDCAKSVLKQLMKVDPAHRITAKELLDNQWLTGNKLSSVRPTNVLEMMKE
SQ  WKNNPESVEENTTEEKNKPSTEEKLKSYQPWGNVPDANYTSDEEEEKQSTAYEKQFPATSKDNFDMCSSSFTSSKLLPAE
SQ  IKGEMEKTPVTPSQGTATKYPAKSGALSRTKKKL
//
ID  Q924X7;
PN  Serine/threonine-protein kinase 33;
GN  Stk33;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16176263}.
DR  UNIPROT: Q924X7;
DR  UNIPROT: Q4A1D4;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME. {ECO:0000269|PubMed:18811945}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0044773;
GO  GO:0046777;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADPSLNDNPTACPHCASSQAGLLCVCPAGKSPVLVVEMSQTSSIGSTEFFASQERKKERNTSRESSLKDLSIRTSNVER
SQ  KPQAQWSRSNVTVGKIPHIRMDDGAGIEEFYTFGRILGQGSFGMVFEAIDKETGAKWAIKKVNKEKAGSSAMKLLEREVS
SQ  ILKTVNHQHIIHLEQVFESPQKMYLVMELCEDGELKAVMDQRGHFSENETRLIIQSLASAIAYLHNKDIVHRDLKLENIM
SQ  VKSSFIDDNNEMNLNIKVTDFGLSVQKHGSRSEGMMQTTCGTPIYMAPEVINAHDYSQQCDIWSIGVIMFILLCGEPPFL
SQ  ANSEEKLYELIKKGELRFENPVWESVSDSAKNTLKQLMKVDPAHRITAKELLDNQWLTGNTLSSARPTNVLEMMKEWKNN
SQ  PESDEETNTDEETEQSAVYSPSANTAKQPTNAAKKPAAESVGMTSSNSSSSKLLSAESKAEPEKSSETVGHASVAKTTLK
SQ  STTLFRGKKRL
//
ID  P39015;
PN  Suppressor protein STM1;
GN  STM1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Nucleus. Cytoplasm, perinuclear region. Note=Concentrated in the perinuclear region.
DR  UNIPROT: P39015;
DR  UNIPROT: D6VYE5;
DR  PDB: 4U3M;
DR  PDB: 4U3N;
DR  PDB: 4U3U;
DR  PDB: 4U4N;
DR  PDB: 4U4O;
DR  PDB: 4U4Q;
DR  PDB: 4U4R;
DR  PDB: 4U4U;
DR  PDB: 4U4Y;
DR  PDB: 4U4Z;
DR  PDB: 4U50;
DR  PDB: 4U51;
DR  PDB: 4U52;
DR  PDB: 4U53;
DR  PDB: 4U55;
DR  PDB: 4U56;
DR  PDB: 4U6F;
DR  PDB: 4V88;
DR  PDB: 4V8Y;
DR  PDB: 4V8Z;
DR  PDB: 5DAT;
DR  PDB: 5DC3;
DR  PDB: 5DGE;
DR  PDB: 5FCI;
DR  PDB: 5FCJ;
DR  PDB: 5I4L;
DR  PDB: 5LYB;
DR  PDB: 5NDG;
DR  PDB: 5NDV;
DR  PDB: 5NDW;
DR  PDB: 5OBM;
DR  PDB: 5TGA;
DR  PDB: 5TGM;
DR  PDB: 6HHQ;
DR  Pfam: PF09598;
DE  Function: Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs. Acts with CDC13 to control telomere length homeostasis. Involved in the control of the apoptosis-like cell death. {ECO:0000269|PubMed:15044472}.
DE  Reference Proteome: Yes;
DE  Interaction: P06704; IntAct: EBI-7945762; Score: 0.40
DE  Interaction: P22147; IntAct: EBI-7383874; Score: 0.40
DE  Interaction: P30822; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39015; IntAct: EBI-7102530; Score: 0.40
DE  Interaction: P40968; IntAct: EBI-7102563; Score: 0.40
DE  Interaction: P10863; IntAct: EBI-7109009; Score: 0.40
DE  Interaction: Q12114; IntAct: EBI-784698; Score: 0.35
DE  Interaction: P38968; IntAct: EBI-788839; Score: 0.35
DE  Interaction: P38199; IntAct: EBI-796822; Score: 0.35
DE  Interaction: P07280; IntAct: EBI-801098; Score: 0.35
DE  Interaction: P32790; IntAct: EBI-802790; Score: 0.35
DE  Interaction: Q08687; IntAct: EBI-807945; Score: 0.35
DE  Interaction: P11632; IntAct: EBI-808830; Score: 0.35
DE  Interaction: P38700; IntAct: EBI-813960; Score: 0.27
DE  Interaction: P38822; IntAct: EBI-815028; Score: 0.27
DE  Interaction: P32357; IntAct: EBI-817406; Score: 0.27
DE  Interaction: P38285; IntAct: EBI-818288; Score: 0.27
DE  Interaction: P40522; IntAct: EBI-819618; Score: 0.27
DE  Interaction: Q12389; IntAct: EBI-819624; Score: 0.27
DE  Interaction: P00330; IntAct: EBI-819848; Score: 0.27
DE  Interaction: Q02486; IntAct: EBI-820332; Score: 0.27
DE  Interaction: P02293; IntAct: EBI-820511; Score: 0.27
DE  Interaction: P07270; IntAct: EBI-821981; Score: 0.35
DE  Interaction: P22082; IntAct: EBI-822228; Score: 0.35
DE  Interaction: P39940; IntAct: EBI-937964; Score: 0.44
DE  Interaction: P43582; IntAct: EBI-938833; Score: 0.44
DE  Interaction: P40318; IntAct: EBI-939185; Score: 0.44
DE  Interaction: P46995; IntAct: EBI-939475; Score: 0.44
DE  Interaction: P22696; IntAct: EBI-939677; Score: 0.44
DE  Interaction: P33203; IntAct: EBI-940012; Score: 0.44
DE  Interaction: Q06525; IntAct: EBI-940637; Score: 0.44
DE  Interaction: P38633; IntAct: EBI-7030235; Score: 0.40
DE  Interaction: P32558; IntAct: EBI-7033179; Score: 0.40
DE  Interaction: P42945; IntAct: EBI-7118959; Score: 0.40
DE  Interaction: Q06188; IntAct: EBI-7172803; Score: 0.40
DE  Interaction: Q06109; IntAct: EBI-7201165; Score: 0.40
DE  Interaction: P53741; IntAct: EBI-7226242; Score: 0.56
DE  Interaction: P40023; IntAct: EBI-7284277; Score: 0.40
DE  Interaction: P20448; IntAct: EBI-7328235; Score: 0.40
DE  Interaction: P48570; IntAct: EBI-7405961; Score: 0.40
DE  Interaction: P32505; IntAct: EBI-7425228; Score: 0.40
DE  Interaction: P38205; IntAct: EBI-7427415; Score: 0.40
DE  Interaction: P39744; IntAct: EBI-7430572; Score: 0.40
DE  Interaction: P53742; IntAct: EBI-7433745; Score: 0.40
DE  Interaction: P21951; IntAct: EBI-7459287; Score: 0.40
DE  Interaction: Q07350; IntAct: EBI-7554433; Score: 0.40
DE  Interaction: P53131; IntAct: EBI-7558289; Score: 0.40
DE  Interaction: P31374; IntAct: EBI-7560747; Score: 0.40
DE  Interaction: Q04373; IntAct: EBI-7563094; Score: 0.40
DE  Interaction: P38251; IntAct: EBI-7577892; Score: 0.40
DE  Interaction: Q03195; IntAct: EBI-7580304; Score: 0.40
DE  Interaction: P25046; IntAct: EBI-7583439; Score: 0.40
DE  Interaction: P0C0T4; IntAct: EBI-7651776; Score: 0.40
DE  Interaction: P47050; IntAct: EBI-7664713; Score: 0.40
DE  Interaction: P32368; IntAct: EBI-7668370; Score: 0.40
DE  Interaction: P40509; IntAct: EBI-7677023; Score: 0.40
DE  Interaction: P23293; IntAct: EBI-7692513; Score: 0.40
DE  Interaction: P22579; IntAct: EBI-7697200; Score: 0.40
DE  Interaction: P35207; IntAct: EBI-7700401; Score: 0.40
DE  Interaction: Q02793; IntAct: EBI-7701654; Score: 0.40
DE  Interaction: P40072; IntAct: EBI-7703803; Score: 0.40
DE  Interaction: P46965; IntAct: EBI-7734821; Score: 0.40
DE  Interaction: P38123; IntAct: EBI-7768968; Score: 0.40
DE  Interaction: P36100; IntAct: EBI-7777929; Score: 0.40
DE  Interaction: Q07381; IntAct: EBI-7786590; Score: 0.40
DE  Interaction: Q06672; IntAct: EBI-7787631; Score: 0.40
DE  Interaction: P53874; IntAct: EBI-7789499; Score: 0.40
DE  Interaction: Q01477; IntAct: EBI-7792626; Score: 0.56
DE  Interaction: P53254; IntAct: EBI-7813272; Score: 0.40
DE  Interaction: Q08831; IntAct: EBI-7831006; Score: 0.40
DE  Interaction: P38197; IntAct: EBI-7834574; Score: 0.40
DE  Interaction: P40487; IntAct: EBI-7858467; Score: 0.40
DE  Interaction: P40462; IntAct: EBI-7859020; Score: 0.40
DE  Interaction: Q07953; IntAct: EBI-7861598; Score: 0.40
DE  Interaction: Q3E747; IntAct: EBI-7862695; Score: 0.40
DE  Interaction: P38806; IntAct: EBI-7869465; Score: 0.40
DE  Interaction: P53911; IntAct: EBI-7870828; Score: 0.40
DE  Interaction: Q12080; IntAct: EBI-7884725; Score: 0.40
DE  Interaction: Q12152; IntAct: EBI-7884942; Score: 0.40
DE  Interaction: Q12179; IntAct: EBI-7885829; Score: 0.40
DE  Interaction: P50275; IntAct: EBI-7913090; Score: 0.44
DE  Interaction: Q04199; IntAct: EBI-7937753; Score: 0.40
DE  Interaction: P38626; IntAct: EBI-7943352; Score: 0.40
DE  Interaction: Q06697; IntAct: EBI-7949322; Score: 0.40
DE  Interaction: P47130; IntAct: EBI-7983878; Score: 0.40
DE  Interaction: Q02554; IntAct: EBI-7987846; Score: 0.40
DE  Interaction: P18899; IntAct: EBI-7998863; Score: 0.40
DE  Interaction: P24482; IntAct: EBI-8000629; Score: 0.40
DE  Interaction: P32803; IntAct: EBI-8005417; Score: 0.40
DE  Interaction: P39704; IntAct: EBI-8008355; Score: 0.40
DE  Interaction: P15442; IntAct: EBI-8014597; Score: 0.40
DE  Interaction: Q04233; IntAct: EBI-8017049; Score: 0.40
DE  Interaction: P41911; IntAct: EBI-8019433; Score: 0.40
DE  Interaction: P32806; IntAct: EBI-8020973; Score: 0.40
DE  Interaction: Q12341; IntAct: EBI-8021985; Score: 0.40
DE  Interaction: P53685; IntAct: EBI-8059242; Score: 0.40
DE  Interaction: P38304; IntAct: EBI-8434332; Score: 0.40
DE  Interaction: Q06164; IntAct: EBI-8437245; Score: 0.40
DE  Interaction: P38694; IntAct: EBI-8443741; Score: 0.40
DE  Interaction: P32495; IntAct: EBI-8449766; Score: 0.40
DE  Interaction: Q07896; IntAct: EBI-8452527; Score: 0.40
DE  Interaction: P53927; IntAct: EBI-8453525; Score: 0.40
DE  Interaction: P42841; IntAct: EBI-8486372; Score: 0.40
DE  Interaction: P33775; IntAct: EBI-8494631; Score: 0.40
DE  Interaction: P40454; IntAct: EBI-2886504; Score: 0.00
DE  Interaction: P25294; IntAct: EBI-3662273; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3678076; Score: 0.53
DE  Interaction: P11484; IntAct: EBI-3784224; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3791884; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3801989; Score: 0.35
DE  Interaction: P22943; IntAct: EBI-3831611; Score: 0.35
DE  Interaction: P36160; IntAct: EBI-7433031; Score: 0.35
DE  Interaction: Q00416; IntAct: EBI-16421063; Score: 0.35
DE  Interaction: P39109; IntAct: EBI-20816574; Score: 0.37
DE  Interaction: P38011; IntAct: EBI-26974569; Score: 0.78
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005844;
GO  GO:0003677;
GO  GO:0043022;
GO  GO:0042162;
GO  GO:0045142;
GO  GO:0043066;
GO  GO:0043558;
GO  GO:0000723;
GO  GO:0031929;
GO  GO:0006414;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNPFDLLGNDVEDADVVVLPPKEIVKSNTSSKKADVPPPSADPSKARKNRPRPSGNEGAIRDKTAGRRNNRSKDVTDSA
SQ  TTKKSNTRRATDRHSRTGKTDTKKKVNQGWGDDKKELSAEKEAQADAAAEIAEDAAEAEDAGKPKTAQLSLQDYLNQQAN
SQ  NQFNKVPEAKKVELDAERIETAEKEAYVPATKVKNVKSKQLKTKEYLEFDATFVESNTRKNFGDRNNNSRNNFNNRRGGR
SQ  GARKGNNTANATNSANTVQKNRNIDVSNLPSLA
//
ID  Q90987;
PN  Stathmin-2;
GN  STMN2;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, axon {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Associated with punctate structures in the perinuclear cytoplasm, axons, and growth cones of developing neurons. SCG10 exists in both soluble and membrane- bound forms (By similarity). {ECO:0000250}.
DR  UNIPROT: Q90987;
DR  Pfam: PF00836;
DR  PROSITE: PS00563;
DR  PROSITE: PS01041;
DR  PROSITE: PS51663;
DE  Function: Is a key regulator of neurite extension through regulation of microtubule instabilily. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0048306;
GO  GO:0015631;
GO  GO:1990090;
GO  GO:0007019;
GO  GO:0007026;
GO  GO:0031115;
GO  GO:0010977;
GO  GO:0031175;
GO  GO:0031117;
GO  GO:0010976;
GO  GO:0031110;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MAKTAMAYKEKMKELSMLSLICSCFYPEPRNMNIYKYDDMEVKQINKRASGQAFELILKPPSPVSEAPRTLASPKKKELS
SQ  LEEIQKKLEAAEERRKSQEAQVLKHLAEKREHEREVLQKALEENNNFSKMAEEKLILKMEQIKENREANLAALIERLQEK
SQ  ERHAAEVRRNKELQVELSG
//
ID  Q93045;
PN  Stathmin-2;
GN  STMN2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, axon. Golgi apparatus. Endosome {ECO:0000250}. Cell projection, lamellipodium. Note=Associated with punctate structures in the perinuclear cytoplasm, axons, and growth cones of developing neurons. SCG10 exists in both soluble and membrane- bound forms. Colocalized with CIB1 in neurites of developing hippocampal primary neurons (By similarity). Colocalized with CIB1 in the cell body, neuritis and growth cones of neurons. Colocalized with CIB1 to the leading edge of lamellipodia. {ECO:0000250}.
DR  UNIPROT: Q93045;
DR  UNIPROT: A8K9M2;
DR  UNIPROT: G3V110;
DR  UNIPROT: O14952;
DR  UNIPROT: Q6PK68;
DR  Pfam: PF00836;
DR  PROSITE: PS00563;
DR  PROSITE: PS01041;
DR  PROSITE: PS51663;
DR  OMIM: 600621;
DR  DisGeNET: 11075;
DE  Function: Regulator of microtubule stability. When phosphorylated by MAPK8, stabilizes microtubules and consequently controls neurite length in cortical neurons. In the developing brain, negatively regulates the rate of exit from multipolar stage and retards radial migration from the ventricular zone (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-25368535; Score: 0.37
DE  Interaction: P68104; IntAct: EBI-730906; Score: 0.00
DE  Interaction: Q96AW1; IntAct: EBI-733397; Score: 0.00
DE  Interaction: Q8IYF3; IntAct: EBI-760875; Score: 0.70
DE  Interaction: Q96PX6; IntAct: EBI-7393213; Score: 0.37
DE  Interaction: Q8NHQ1; IntAct: EBI-7393233; Score: 0.37
DE  Interaction: Q96D09; IntAct: EBI-7393253; Score: 0.37
DE  Interaction: P08138; IntAct: EBI-7393289; Score: 0.37
DE  Interaction: Q02742; IntAct: EBI-8773630; Score: 0.37
DE  Interaction: P40222; IntAct: EBI-10280152; Score: 0.67
DE  Interaction: Q12800; IntAct: EBI-10280162; Score: 0.56
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: Q86VW0; IntAct: EBI-24499442; Score: 0.56
DE  Interaction: O95983; IntAct: EBI-24672647; Score: 0.56
DE  Interaction: P20618; IntAct: EBI-24719788; Score: 0.56
DE  Interaction: Q96HA8; IntAct: EBI-24747979; Score: 0.56
DE  Interaction: Q86YD7; IntAct: EBI-24783132; Score: 0.56
DE  Interaction: Q8TD31; IntAct: EBI-24642780; Score: 0.56
DE  Interaction: Q9UI47; IntAct: EBI-24800038; Score: 0.56
DE  Interaction: Q83DF6; IntAct: EBI-21285366; Score: 0.37
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: Q13268; IntAct: EBI-20910208; Score: 0.40
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0048306;
GO  GO:0015631;
GO  GO:1990090;
GO  GO:0007019;
GO  GO:0007026;
GO  GO:0031115;
GO  GO:0010977;
GO  GO:0031175;
GO  GO:0031117;
GO  GO:0010976;
GO  GO:0031110;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:21471001};
SQ  MAKTAMAYKEKMKELSMLSLICSCFYPEPRNINIYTYDDMEVKQINKRASGQAFELILKPPSPISEAPRTLASPKKKDLS
SQ  LEEIQKKLEAAEERRKSQEAQVLKQLAEKREHEREVLQKALEENNNFSKMAEEKLILKMEQIKENREANLAAIIERLQEK
SQ  ERHAAEVRRNKELQVELSG
//
ID  P55821;
PN  Stathmin-2;
GN  Stmn2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16618812}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16618812}. Cell projection, growth cone {ECO:0000269|PubMed:16618812}. Cell projection, axon {ECO:0000269|PubMed:16618812}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endosome {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Colocalized with CIB1 in neurites of developing hippocampal primary neurons. Colocalized with CIB1 in the cell body, neuritis, growth cones of neurons and in neurites of developing hippocampal primary neurons. Colocalized with CIB1 to the leading edge of lamellipodia (By similarity). Associated with punctate structures in the perinuclear cytoplasm, axons, and growth cones of developing neurons. Exists in both soluble and membrane-bound forms. In the developing brain, mostly cytosolic. {ECO:0000250}.
DR  UNIPROT: P55821;
DR  Pfam: PF00836;
DR  PROSITE: PS00563;
DR  PROSITE: PS01041;
DR  PROSITE: PS51663;
DE  Function: Regulator of microtubule stability. When phosphorylated by MAPK8, stabilizes microtubules and consequently controls neurite length in cortical neurons. In the developing brain, negatively regulates the rate of exit from multipolar stage and retards radial migration from the ventricular zone. {ECO:0000269|PubMed:21297631}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7TQF1; IntAct: EBI-7412883; Score: 0.54
DE  Interaction: Q9EPL2; IntAct: EBI-3869454; Score: 0.35
GO  GO:0005737;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0031982;
GO  GO:0048306;
GO  GO:0015631;
GO  GO:1990090;
GO  GO:0007019;
GO  GO:0007026;
GO  GO:0031115;
GO  GO:0010977;
GO  GO:0031175;
GO  GO:0031117;
GO  GO:0010976;
GO  GO:0031110;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAKTAMAYKEKMKELSMLSLICSCFYPEPRNINIYTYDDMEVKQINKRASGQAFELILKPPSPISEAPRTLASPKKKDLS
SQ  LEEIQKKLEAAEERRKSQEAQVLKQLAEKREHEREVLQKALEENNNFSKMAEEKLILKMEQIKENREANLAAIIERLQEK
SQ  ERHAAEVRRNKELQVELSG
//
ID  P21818;
PN  Stathmin-2;
GN  Stmn2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cell projection, growth cone. Cell projection, axon. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus. Endosome. Cell projection, lamellipodium {ECO:0000250}. Note=Colocalized with CIB1 in the cell body, neuritis and growth cones of neurons. Colocalized with CIB1 to the leading edge of lamellipodia (By similarity). Associated with punctate structures in the perinuclear cytoplasm, axons, and growth cones of developing neurons. Exists in both soluble and membrane-bound forms. Colocalized with CIB1 in neurites of developing hippocampal primary neurons. {ECO:0000250}.
DR  UNIPROT: P21818;
DR  UNIPROT: Q9ERH2;
DR  Pfam: PF00836;
DR  PROSITE: PS00563;
DR  PROSITE: PS01041;
DR  PROSITE: PS51663;
DE  Function: Regulator of microtubule stability. When phosphorylated by MAPK8, stabilizes microtubules and consequently controls neurite length in cortical neurons. In the developing brain, negatively regulates the rate of exit from multipolar stage and retards radial migration from the ventricular zone. {ECO:0000269|PubMed:16618812, ECO:0000269|PubMed:21297631, ECO:0000269|PubMed:9012855}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005768;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0031982;
GO  GO:0048306;
GO  GO:0015631;
GO  GO:1990090;
GO  GO:0007019;
GO  GO:0007026;
GO  GO:0031115;
GO  GO:0010977;
GO  GO:0031175;
GO  GO:0031117;
GO  GO:0010976;
GO  GO:0031110;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MAKTAMAYKEKMKELSMLSLICSCFYPEPRNINIYTYDDMEVKQINKRASGQAFELILKPPSPISEAPRTLASPKKKDLS
SQ  LEEIQKKLEAAEGRRKSQEAQVLKQLAEKREHEREVLQKALEENNNFSKMAEEKLILKMEQIKENREANLAAIIERLQEK
SQ  ERHAAEVRRNKELQVELSG
//
ID  Q5E9D1;
PN  Small ubiquitin-related modifier 1;
GN  SUMO1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DR  UNIPROT: Q5E9D1;
DR  UNIPROT: Q3ZC68;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3. {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0015459;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0045759;
GO  GO:1902260;
GO  GO:0016925;
GO  GO:0060021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKEL
SQ  GMEEEDVIEVYQEQTGGHSTV
//
ID  Q9MZD5;
PN  Small ubiquitin-related modifier 1;
GN  SUMO1;
OS  9863;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DR  UNIPROT: Q9MZD5;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3. {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0015459;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0045759;
GO  GO:1902260;
GO  GO:0016925;
GO  GO:0060021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKEL
SQ  GMEEEDVIEVYHEQTGGHSTV
//
ID  Q8QGH2;
PN  Small ubiquitin-related modifier 1;
GN  SUMO1;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}.
DR  UNIPROT: Q8QGH2;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. {ECO:0000250|UniProtKB:P63165}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0031386;
GO  GO:0008134;
GO  GO:0044389;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0016925;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSAEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRITDNHTPKEL
SQ  GMEEEDVIEVYQEQTGGHSTV
//
ID  Q7SZR5;
PN  Small ubiquitin-related modifier 1;
GN  sumo1;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}.
DR  UNIPROT: Q7SZR5;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric sumo1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. {ECO:0000250|UniProtKB:P63165}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0031386;
GO  GO:0044389;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0043009;
GO  GO:0060216;
GO  GO:0016925;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDTETKPSSDGGEKKDGEYIKLKVIGQDNSEIHFKVKMTTHLKKLKESYSQRQGVPVNSLRFLFEGQRITDNLTPKELG
SQ  MEDEDVIEVYQEQTGGCRND
//
ID  P63165;
PN  Small ubiquitin-related modifier 1;
GN  SUMO1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:10574707, ECO:0000269|PubMed:12383504}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000269|PubMed:12383504, ECO:0000269|PubMed:9162015}. Nucleus, PML body {ECO:0000269|PubMed:10574707, ECO:0000269|PubMed:12383504, ECO:0000269|PubMed:22406621}. Cell membrane {ECO:0000269|PubMed:19223394}. Nucleus {ECO:0000269|PubMed:24651376, ECO:0000269|PubMed:9162015}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (PubMed:24651376). {ECO:0000250|UniProtKB:P63166, ECO:0000269|PubMed:24651376}.
DR  UNIPROT: P63165;
DR  UNIPROT: A8MUS8;
DR  UNIPROT: B2R4I5;
DR  UNIPROT: P55856;
DR  UNIPROT: Q6FGG0;
DR  UNIPROT: Q6NZ62;
DR  UNIPROT: Q93068;
DR  PDB: 1A5R;
DR  PDB: 1TGZ;
DR  PDB: 1WYW;
DR  PDB: 1Y8R;
DR  PDB: 1Z5S;
DR  PDB: 2ASQ;
DR  PDB: 2BF8;
DR  PDB: 2G4D;
DR  PDB: 2IO2;
DR  PDB: 2IY0;
DR  PDB: 2IY1;
DR  PDB: 2KQS;
DR  PDB: 2LAS;
DR  PDB: 2MW5;
DR  PDB: 2N1A;
DR  PDB: 2N1V;
DR  PDB: 2PE6;
DR  PDB: 2UYZ;
DR  PDB: 2VRR;
DR  PDB: 3KYC;
DR  PDB: 3KYD;
DR  PDB: 3RZW;
DR  PDB: 3UIP;
DR  PDB: 4WJN;
DR  PDB: 4WJO;
DR  PDB: 4WJP;
DR  PDB: 4WJQ;
DR  PDB: 5AEK;
DR  PDB: 5B7A;
DR  PDB: 5ELJ;
DR  PDB: 5GHD;
DR  PDB: 6EOP;
DR  PDB: 6EOT;
DR  PDB: 6J4I;
DR  PDB: 6JXU;
DR  PDB: 6JXV;
DR  PDB: 6K5T;
DR  PDB: 6TRW;
DR  PDB: 6UYO;
DR  PDB: 6UYP;
DR  PDB: 6UYQ;
DR  PDB: 6UYR;
DR  PDB: 6UYS;
DR  PDB: 6UYT;
DR  PDB: 6UYU;
DR  PDB: 6UYV;
DR  PDB: 6UYX;
DR  PDB: 6UYY;
DR  PDB: 6UYZ;
DR  PDB: 6V7P;
DR  PDB: 6V7Q;
DR  PDB: 6V7R;
DR  PDB: 6V7S;
DR  PDB: 6WW3;
DR  PDB: 6XOG;
DR  PDB: 6XOH;
DR  PDB: 6XOI;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DR  OMIM: 601912;
DR  OMIM: 613705;
DR  DisGeNET: 7341;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (PubMed:24651376). {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:19223394, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24651376, ECO:0000269|PubMed:9019411, ECO:0000269|PubMed:9162015}.
DE  Disease: Non-syndromic orofacial cleft 10 (OFC10) [MIM:613705]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. {ECO:0000269|PubMed:16990542}. Note=The disease is caused by variants affecting the gene represented in this entry. A chromosomal aberration involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays.
DE  Reference Proteome: Yes;
DE  Interaction: P46060; IntAct: EBI-7036555; Score: 0.96
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-30826718; Score: 0.44
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: P59595; IntAct: EBI-7602710; Score: 0.54
DE  Interaction: Q9UBC3; IntAct: EBI-80165; Score: 0.70
DE  Interaction: Q9UER7; IntAct: EBI-367065; Score: 0.78
DE  Interaction: P29590; IntAct: EBI-367073; Score: 0.83
DE  Interaction: Q9H2X6; IntAct: EBI-7631580; Score: 0.54
DE  Interaction: Q9P0U3; IntAct: EBI-7631805; Score: 0.87
DE  Interaction: Q96GM8; IntAct: EBI-736070; Score: 0.00
DE  Interaction: Q8NCR3; IntAct: EBI-754177; Score: 0.37
DE  Interaction: P23497; IntAct: EBI-759019; Score: 0.76
DE  Interaction: P03116; IntAct: EBI-7316595; Score: 0.40
DE  Interaction: P56693; IntAct: EBI-8087462; Score: 0.44
DE  Interaction: Q13569; IntAct: EBI-8543687; Score: 0.67
DE  Interaction: Q9UBE0; IntAct: EBI-1037073; Score: 0.66
DE  Interaction: Q9HC62; IntAct: EBI-1039804; Score: 0.62
DE  Interaction: P63279; IntAct: EBI-7406754; Score: 0.95
DE  Interaction: P19419; IntAct: EBI-7035798; Score: 0.66
DE  Interaction: Q02078; IntAct: EBI-15799620; Score: 0.54
DE  Interaction: P21359; IntAct: EBI-7036435; Score: 0.40
DE  Interaction: Q96ST3; IntAct: EBI-7036520; Score: 0.40
DE  Interaction: Q9UIS9; IntAct: EBI-7060348; Score: 0.52
DE  Interaction: Q8N1G0; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q9C0J8; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: O15294; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q96QC0; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q5VWQ0; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: P54886; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q15697; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q96JM2; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: O14874; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q92610; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q7Z7K6; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q9NYW8; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: O14647; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q01082; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q5T0B9; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q9NX05; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: O43309; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q96PQ6; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q9H0J9; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q92766; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q9H5H4; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q9NS39; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q5BJG6; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q14865; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q9C086; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q5T5X7; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q16778; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: O43290; IntAct: EBI-1211852; Score: 0.50
DE  Interaction: Q7L2E3; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: P05187; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: P27105; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q9H2Y7; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q9HCK8; IntAct: EBI-1210299; Score: 0.00
DE  Interaction: Q9Y3V2; IntAct: EBI-1549907; Score: 0.44
DE  Interaction: P63165; IntAct: EBI-1559403; Score: 0.37
DE  Interaction: P25445; IntAct: EBI-1559446; Score: 0.37
DE  Interaction: Q92786; IntAct: EBI-8463533; Score: 0.40
DE  Interaction: Q00653; IntAct: EBI-8017134; Score: 0.40
DE  Interaction: P18146; IntAct: EBI-8513652; Score: 0.40
DE  Interaction: Q969V5; IntAct: EBI-6987810; Score: 0.35
DE  Interaction: Q99856; IntAct: EBI-8566246; Score: 0.35
DE  Interaction: Q9ERU9; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: Q07832; IntAct: EBI-2560950; Score: 0.40
DE  Interaction: P06730; IntAct: EBI-7852202; Score: 0.40
DE  Interaction: Q81KT8; IntAct: EBI-2821603; Score: 0.00
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: P09874; IntAct: EBI-7258849; Score: 0.40
DE  Interaction: Q16665; IntAct: EBI-2940265; Score: 0.69
DE  Interaction: Q99814; IntAct: EBI-2941366; Score: 0.40
DE  Interaction: Q9H160; IntAct: EBI-3400801; Score: 0.40
DE  Interaction: P10242; IntAct: EBI-3505387; Score: 0.54
DE  Interaction: P01104; IntAct: EBI-3505439; Score: 0.40
DE  Interaction: O88846; IntAct: EBI-8568973; Score: 0.40
DE  Interaction: Q8NCN4; IntAct: EBI-8569133; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-8557085; Score: 0.35
DE  Interaction: Q14164; IntAct: EBI-8557104; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-8557104; Score: 0.35
DE  Interaction: Q9Y6K9; IntAct: EBI-8557226; Score: 0.56
DE  Interaction: Q60953; IntAct: EBI-4408663; Score: 0.40
DE  Interaction: P10275; IntAct: EBI-3904089; Score: 0.60
DE  Interaction: Q13489; IntAct: EBI-3926841; Score: 0.37
DE  Interaction: O75928; IntAct: EBI-3934352; Score: 0.78
DE  Interaction: Q60636; IntAct: EBI-7000799; Score: 0.40
DE  Interaction: Q01826; IntAct: EBI-4391866; Score: 0.51
DE  Interaction: Q9H6Y7; IntAct: EBI-5663462; Score: 0.00
DE  Interaction: Q8BID6; IntAct: EBI-7769112; Score: 0.40
DE  Interaction: O88898; IntAct: EBI-7769233; Score: 0.40
DE  Interaction: O75475; IntAct: EBI-7946621; Score: 0.43
DE  Interaction: O75626; IntAct: EBI-7839462; Score: 0.40
DE  Interaction: Q5W0Q7; IntAct: EBI-8017558; Score: 0.61
DE  Interaction: Q6DRC5; IntAct: EBI-8018170; Score: 0.44
DE  Interaction: P61978; IntAct: EBI-8102993; Score: 0.40
DE  Interaction: Q8UN00; IntAct: EBI-6693059; Score: 0.40
DE  Interaction: Q92793; IntAct: EBI-9208489; Score: 0.40
DE  Interaction: P17655; IntAct: EBI-9212484; Score: 0.40
DE  Interaction: P45481; IntAct: EBI-9210386; Score: 0.40
DE  Interaction: P15884; IntAct: EBI-9210401; Score: 0.40
DE  Interaction: P10276; IntAct: EBI-9520823; Score: 0.56
DE  Interaction: P0C206; IntAct: EBI-9675643; Score: 0.49
DE  Interaction: O14964; IntAct: EBI-10181926; Score: 0.56
DE  Interaction: O95073; IntAct: EBI-10191069; Score: 0.56
DE  Interaction: P07910; IntAct: EBI-10195362; Score: 0.72
DE  Interaction: P15336; IntAct: EBI-10198728; Score: 0.72
DE  Interaction: P48431; IntAct: EBI-10210270; Score: 0.67
DE  Interaction: G2XKQ0; IntAct: EBI-10220500; Score: 0.56
DE  Interaction: Q12800; IntAct: EBI-10220534; Score: 0.56
DE  Interaction: Q7KZS0; IntAct: EBI-10220546; Score: 0.72
DE  Interaction: Q8WWZ3; IntAct: EBI-10220556; Score: 0.56
DE  Interaction: Q9HCK0; IntAct: EBI-10220566; Score: 0.72
DE  Interaction: Q05D60; IntAct: EBI-10223856; Score: 0.56
DE  Interaction: Q15916; IntAct: EBI-10237252; Score: 0.56
DE  Interaction: Q53SE7; IntAct: EBI-10242759; Score: 0.56
DE  Interaction: Q59GP6; IntAct: EBI-10243451; Score: 0.56
DE  Interaction: Q96B23; IntAct: EBI-10243503; Score: 0.79
DE  Interaction: Q6PEW1; IntAct: EBI-10253312; Score: 0.72
DE  Interaction: Q86UW9; IntAct: EBI-10259108; Score: 0.56
DE  Interaction: Q8NDC0; IntAct: EBI-10269510; Score: 0.56
DE  Interaction: Q8TES7; IntAct: EBI-10275280; Score: 0.56
DE  Interaction: Q9BPY3; IntAct: EBI-10295861; Score: 0.56
DE  Interaction: Q9BQY4; IntAct: EBI-10296568; Score: 0.56
DE  Interaction: Q9BUZ4; IntAct: EBI-10299128; Score: 0.56
DE  Interaction: Q9H257; IntAct: EBI-10305541; Score: 0.56
DE  Interaction: Q9UBT2; IntAct: EBI-10319390; Score: 0.85
DE  Interaction: Q9UJ78; IntAct: EBI-10322298; Score: 0.68
DE  Interaction: Q9Y4B4; IntAct: EBI-10328076; Score: 0.72
DE  Interaction: Q7Z333; IntAct: EBI-10093988; Score: 0.37
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q99P88; IntAct: EBI-10997466; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P63280; IntAct: EBI-11044140; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11086798; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11115566; Score: 0.35
DE  Interaction: A0A0S2Z4M1; IntAct: EBI-16430011; Score: 0.56
DE  Interaction: A0A0S2Z3N6; IntAct: EBI-16434661; Score: 0.56
DE  Interaction: O15169; IntAct: EBI-16434639; Score: 0.56
DE  Interaction: Q9QXY6; IntAct: EBI-11685546; Score: 0.44
DE  Interaction: Q8N680; IntAct: EBI-24293200; Score: 0.56
DE  Interaction: Q9Y2F9; IntAct: EBI-25246984; Score: 0.56
DE  Interaction: O75360; IntAct: EBI-25255095; Score: 0.56
DE  Interaction: O00463; IntAct: EBI-24610292; Score: 0.56
DE  Interaction: Q8N3Z6; IntAct: EBI-24712488; Score: 0.56
DE  Interaction: Q96MM3; IntAct: EBI-24434806; Score: 0.56
DE  Interaction: P78317; IntAct: EBI-24572385; Score: 0.68
DE  Interaction: Q12933; IntAct: EBI-24596054; Score: 0.56
DE  Interaction: P04637; IntAct: EBI-15584314; Score: 0.72
DE  Interaction: P22460; IntAct: EBI-15620361; Score: 0.40
DE  Interaction: P03243; IntAct: EBI-15631628; Score: 0.40
DE  Interaction: P06748; IntAct: EBI-15640342; Score: 0.52
DE  Interaction: P10914; IntAct: EBI-15666674; Score: 0.54
DE  Interaction: Q00613; IntAct: EBI-15799774; Score: 0.44
DE  Interaction: Q06609; IntAct: EBI-15819689; Score: 0.44
DE  Interaction: P38398; IntAct: EBI-15822830; Score: 0.60
DE  Interaction: Q12888; IntAct: EBI-15823042; Score: 0.54
DE  Interaction: O00180; IntAct: EBI-15855964; Score: 0.51
DE  Interaction: P26367; IntAct: EBI-15892992; Score: 0.44
DE  Interaction: Q12873; IntAct: EBI-15930412; Score: 0.44
DE  Interaction: Q13263; IntAct: EBI-15930462; Score: 0.40
DE  Interaction: O75030; IntAct: EBI-15949109; Score: 0.40
DE  Interaction: Q61686; IntAct: EBI-15972508; Score: 0.40
DE  Interaction: P11474; IntAct: EBI-20303027; Score: 0.44
DE  Interaction: P62508; IntAct: EBI-20303735; Score: 0.44
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: P41597; IntAct: EBI-20804248; Score: 0.37
DE  Interaction: Q8WWM9; IntAct: EBI-21174846; Score: 0.35
DE  Interaction: P17676; IntAct: EBI-21288928; Score: 0.60
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: O00257; IntAct: EBI-21306927; Score: 0.46
DE  Interaction: Q06787; IntAct: EBI-21388180; Score: 0.00
DE  Interaction: P42858; IntAct: EBI-25952752; Score: 0.56
DE  Interaction: Q9BYX4; IntAct: EBI-26884401; Score: 0.40
DE  Interaction: P53350; IntAct: EBI-28938281; Score: 0.35
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: O15083; IntAct: EBI-30826674; Score: 0.44
DE  Interaction: O75925; IntAct: EBI-30826685; Score: 0.44
DE  Interaction: Q08379; IntAct: EBI-30826740; Score: 0.44
DE  Interaction: P16220; IntAct: EBI-30826696; Score: 0.44
DE  Interaction: P18846; IntAct: EBI-30826707; Score: 0.44
DE  Interaction: Q6N043; IntAct: EBI-30826751; Score: 0.44
DE  Interaction: Q6ZNA4; IntAct: EBI-30826762; Score: 0.44
DE  Interaction: Q9H4L7; IntAct: EBI-30826828; Score: 0.44
DE  Interaction: Q96QT4; IntAct: EBI-30826806; Score: 0.44
DE  Interaction: Q9BWV3; IntAct: EBI-30826817; Score: 0.44
DE  Interaction: Q8IV16; IntAct: EBI-30826773; Score: 0.44
DE  Interaction: Q8N2W9; IntAct: EBI-30826784; Score: 0.44
DE  Interaction: Q9NPG4; IntAct: EBI-30826839; Score: 0.44
DE  Interaction: Q9UNY4; IntAct: EBI-30826872; Score: 0.44
DE  Interaction: Q9Y6X2; IntAct: EBI-30826883; Score: 0.44
DE  Interaction: P10070; IntAct: EBI-29016408; Score: 0.27
DE  Interaction: Q5W0V3; IntAct: EBI-34574999; Score: 0.27
GO  GO:0005829;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0001741;
GO  GO:0019899;
GO  GO:0015459;
GO  GO:0031386;
GO  GO:0003723;
GO  GO:0044388;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0044389;
GO  GO:1990381;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0006281;
GO  GO:0045759;
GO  GO:1902260;
GO  GO:0043392;
GO  GO:0043433;
GO  GO:0045892;
GO  GO:0042308;
GO  GO:0010621;
GO  GO:0030578;
GO  GO:1901896;
GO  GO:0032436;
GO  GO:0031334;
GO  GO:0090204;
GO  GO:0050821;
GO  GO:0016925;
GO  GO:0086004;
GO  GO:0032880;
GO  GO:0060021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKEL
SQ  GMEEEDVIEVYQEQTGGHSTV
//
ID  Q2EF74;
PN  Small ubiquitin-related modifier 1;
GN  SUMO1;
OS  43179;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000269|PubMed:16955077}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000269|PubMed:16955077}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DR  UNIPROT: Q2EF74;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (By similarity). May be involved in modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3. {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166, ECO:0000269|PubMed:16955077}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0015459;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0045759;
GO  GO:1902260;
GO  GO:0016925;
GO  GO:0060021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKEL
SQ  GMEEEDVIEVYQEQTGGHSNV
//
ID  P63166;
PN  Small ubiquitin-related modifier 1;
GN  Sumo1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000269|PubMed:18681895}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (PubMed:18681895). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:18681895}.
DR  UNIPROT: P63166;
DR  UNIPROT: P55856;
DR  UNIPROT: Q3TX92;
DR  UNIPROT: Q93068;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:16990542}.
DE  Reference Proteome: Yes;
DE  Interaction: O15350; IntAct: EBI-7375055; Score: 0.37
DE  Interaction: P21605; IntAct: EBI-7468354; Score: 0.37
DE  Interaction: P55098; IntAct: EBI-310273; Score: 0.37
DE  Interaction: Q9WUF3; IntAct: EBI-310423; Score: 0.37
DE  Interaction: Q61221; IntAct: EBI-466248; Score: 0.46
DE  Interaction: Q03267; IntAct: EBI-908619; Score: 0.51
DE  Interaction: O08900; IntAct: EBI-908661; Score: 0.37
DE  Interaction: P18031; IntAct: EBI-1267439; Score: 0.40
DE  Interaction: Q9WTN3; IntAct: EBI-10764236; Score: 0.47
DE  Interaction: P07356; IntAct: EBI-10765559; Score: 0.40
DE  Interaction: Q505F1; IntAct: EBI-15617100; Score: 0.64
DE  Interaction: P23804; IntAct: EBI-15747487; Score: 0.40
DE  Interaction: P63015; IntAct: EBI-15892975; Score: 0.40
DE  Interaction: P26367; IntAct: EBI-15892953; Score: 0.40
DE  Interaction: Q9EPK7; IntAct: EBI-17172030; Score: 0.35
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0001650;
GO  GO:0000792;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0045202;
GO  GO:0008076;
GO  GO:0001741;
GO  GO:0019899;
GO  GO:0015459;
GO  GO:0031386;
GO  GO:0044388;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0044389;
GO  GO:1990381;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0045759;
GO  GO:1902260;
GO  GO:0043392;
GO  GO:0043433;
GO  GO:0045892;
GO  GO:0042308;
GO  GO:0010621;
GO  GO:0030578;
GO  GO:1901896;
GO  GO:0032436;
GO  GO:0031334;
GO  GO:0090204;
GO  GO:0050821;
GO  GO:0016925;
GO  GO:1903169;
GO  GO:0086004;
GO  GO:0006355;
GO  GO:0031647;
GO  GO:0060021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKEL
SQ  GMEEEDVIEVYQEQTGGHSTV
//
ID  Q9PT08;
PN  Small ubiquitin-related modifier 1;
GN  sumo1;
OS  8022;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}.
DR  UNIPROT: Q9PT08;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric sumo1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. {ECO:0000250|UniProtKB:P63165}.
DE  Reference Proteome: No;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0008134;
GO  GO:0016925;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDTDTKPSGQDGGDQKDGEYIKLKVIGQDNSEIHFKVKMTTHLKKLKESYSQRQGVHMSTLRFLFEGQRISDNHTPKEL
SQ  GMEDEDVIEVYQEQTGGLRNN
//
ID  A7WLH8;
PN  Small ubiquitin-related modifier 1;
GN  SUMO1;
OS  9823;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DR  UNIPROT: A7WLH8;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3. {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DE  Reference Proteome: Yes;
DE  Interaction: P21530; IntAct: EBI-12589850; Score: 0.37
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0015459;
GO  GO:0031386;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0044389;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0045759;
GO  GO:1902260;
GO  GO:0016925;
GO  GO:0060021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKEL
SQ  GMEEEDVIEVYQEQTGGHSTV
//
ID  Q5R6J4;
PN  Small ubiquitin-related modifier 1;
GN  SUMO1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DR  UNIPROT: Q5R6J4;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3. {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0015459;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0045759;
GO  GO:1902260;
GO  GO:0016925;
GO  GO:0060021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKEL
SQ  GMEEEDVIEVYQEQTGGHSTV
//
ID  Q5I0H3;
PN  Small ubiquitin-related modifier 1;
GN  Sumo1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DR  UNIPROT: Q5I0H3;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3. {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8VIB2; IntAct: EBI-7253147; Score: 0.27
DE  Interaction: P10361; IntAct: EBI-7284307; Score: 0.40
DE  Interaction: P20272; IntAct: EBI-7284318; Score: 0.46
DE  Interaction: P42260; IntAct: EBI-7809876; Score: 0.70
DE  Interaction: Q66H32; IntAct: EBI-15636110; Score: 0.40
DE  Interaction: P38656; IntAct: EBI-15649195; Score: 0.52
DE  Interaction: P05455; IntAct: EBI-15649312; Score: 0.40
GO  GO:0005737;
GO  GO:0030425;
GO  GO:0001650;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0045202;
GO  GO:0001741;
GO  GO:0019899;
GO  GO:0015459;
GO  GO:0031386;
GO  GO:0044388;
GO  GO:0008134;
GO  GO:0031625;
GO  GO:0044389;
GO  GO:1990381;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0071456;
GO  GO:0045759;
GO  GO:1902260;
GO  GO:0043392;
GO  GO:0043433;
GO  GO:0045892;
GO  GO:0042308;
GO  GO:0010621;
GO  GO:0030578;
GO  GO:1901896;
GO  GO:0032436;
GO  GO:0031334;
GO  GO:0090204;
GO  GO:0050821;
GO  GO:0016925;
GO  GO:1903169;
GO  GO:0086004;
GO  GO:0006355;
GO  GO:0031647;
GO  GO:0060021;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKEL
SQ  GMEEEDVIEVYQEQTGGHSTV
//
ID  Q6DEP7;
PN  Small ubiquitin-related modifier 1;
GN  sumo1;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}.
DR  UNIPROT: Q6DEP7;
DR  Pfam: PF11976;
DR  PROSITE: PS50053;
DE  Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer (By similarity). Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric sumo1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (By similarity). {ECO:0000250|UniProtKB:O57686, ECO:0000250|UniProtKB:P63165}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0097165;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0031386;
GO  GO:0008134;
GO  GO:0044389;
GO  GO:0071276;
GO  GO:0034605;
GO  GO:0016925;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSDQEAKPSSEDLGDKKEGGDYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRISDHQTPKE
SQ  LGMEEEDVIEVYQEQTGGHSTI
//
ID  Q9FF75;
PN  SUN domain-containing protein 1;
GN  SUN1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:19807882, ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:25412930}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:21294795}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21294795}; Single-pass type II membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:22270916}. Note=Dynamic localization during mitosis and meosis, tightly coupled with nuclear envelope (NE) dynamics. Localized with the nuclear envelope during meiotic prophase I. NE re-formation during metaphase is temporally and spatially coordinated with plant-specific microtubule structures such as phragmoplasts. During anaphase, after NE breakdown (NEBD), predominantly localized with the endoplasmic reticulum, in the outside of the segregated chromosomes and not in between segregated chromosomes. {ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:25412930}.
DR  UNIPROT: Q9FF75;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (PubMed:24667841, PubMed:25759303). Required for the maintenance and/or formation of polarized nuclear shape in root hairs (PubMed:21294795, PubMed:25759303). Modulates the anchoring and mobility of WIP proteins and RANGAP1 in the nuclear envelope (NE) (PubMed:22270916). In association with SUN2, may be involved in telomere attachment to nuclear envelope in the prophase of meiosis (PubMed:25412930). As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:22270916, ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:25412930, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8RWU6; IntAct: EBI-4502264; Score: 0.37
DE  Interaction: Q9FG89; IntAct: EBI-4514232; Score: 0.37
DE  Interaction: Q9SG79; IntAct: EBI-11657653; Score: 0.37
DE  Interaction: Q9FH18; IntAct: EBI-11657658; Score: 0.37
GO  GO:0005856;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0009524;
GO  GO:0043621;
GO  GO:0043495;
GO  GO:0070197;
GO  GO:0006998;
GO  GO:0006997;
GO  GO:0051291;
GO  GO:0051260;
GO  GO:0090435;
GO  GO:2000769;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSASTVSITANTAAATRRTPILAGEKKSNFDYPQSESLANGGVGEAGGTSRDLSRGEATLDRSQGQDLGPVTRRSVSAAT
SQ  GTNTTATQRRTRKVATPKSEKARWKTVVRIFAKQLGALLIIVGLIQLTRKMILKASSPSSPISSYETEMAFSGLESRIAE
SQ  VDGLVKATTNSMQVQVELLDKKMEREAKVLRQEIERKASAFQSELKKIESRTESLEKSVDEVNAKPWVTKDELERIYEEL
SQ  KKGNVDDSAFSEISIDELRAYARDIMEKEIEKHAADGLGRVDYALASGGAFVMEHSDPYLVGKGSSWFATTMRRAHTNAV
SQ  KMLSPSFGEPGQCFPLKGSEGYVQIRLRGPIIPEAFTLEHVAKSVAYDRSSAPKDCRVSGSLQGPESSAETENMQLLTEF
SQ  TYDLDRSNAQTFNILESSSSGLIDTVRLDFTSNHGSDSHTCIYRFRVHGRAPDPVPVVGTNLDQDSSPESE
//
ID  Q20924;
PN  Sun domain-containing protein 1;
GN  sun;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305|PubMed:14697201}; Single-pass membrane protein {ECO:0000305|PubMed:14697201}. Nucleus envelope {ECO:0000269|PubMed:24297748}.
DR  UNIPROT: Q20924;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Involved in centrosome attachment to the nucleus. Required for zyg-12 localization to the nuclear envelope. Together with pot-1, it is required to anchor telomeres to the nuclear envelope in embryos (PubMed:24297748). {ECO:0000269|PubMed:14697201, ECO:0000269|PubMed:24297748}.
DE  Reference Proteome: Yes;
DE  Interaction: P30429; IntAct: EBI-15599089; Score: 0.56
DE  Interaction: Q21443; IntAct: EBI-15599068; Score: 0.44
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0043495;
GO  GO:0051642;
GO  GO:0009792;
GO  GO:0006998;
GO  GO:0008104;
GO  GO:0010824;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALRHTISPQFSNRHSPPVTRSVSRTGVHQPLDTSTPVTRRDSQPGTITGTIQRFHESADDSEIDLNSSKFIYKEHFSYK
SQ  EITSMKKEMWYDWLEYRIRMVRRRFVPTWAQFKRTLMAVVLFAMLYKYARDCLFDGTHHNSEGSYADKDANWASEKQKFH
SQ  QTISNLRAEFSAHDKQLDFKTDHLEKLLENVLEHSKGWKESAIEELKQIKLWQAEISDALQQMKKEIDDAKSTKIIHSTP
SQ  EKAPETAPTASLPPSSQLQPMHITRRALLGVNVANSLIGASIDHSCSSRPVSAKDGFFYDFMSYFGTFQEGYALLDRDVL
SQ  SPGEAWCTYDKRATLTVKLARFVIPKSVSYQHVRWSGIVPNHAPKLYDVVACTDSCCTKWQPLVANCEYKERDGSYDEQE
SQ  QFCSVPTIQNHSPINHVQFRFRENHGDMPKTCAYLIRVYGEPVDPPKETQPMTDNGTESKLESAIVNSVSETA
//
ID  Q558Z2;
PN  Sun domain-containing protein 1;
GN  sun1;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:18266910, ECO:0000269|PubMed:19632001}; Single-pass membrane protein {ECO:0000269|PubMed:18266910, ECO:0000269|PubMed:19632001}; Nucleoplasmic side {ECO:0000269|PubMed:18266910, ECO:0000269|PubMed:19632001}.
DR  UNIPROT: Q558Z2;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: May have an important role in defining the spacing of the nuclear envelope lumen. Essential for centrosome attachment to the nucleus, maintenance of correct ploidy, proper mitosis, association of the centromere cluster with the centrosome and the maintenance of genome stability. Requires direct chromatin binding for inner nuclear membrane targeting. {ECO:0000269|PubMed:18266910, ECO:0000269|PubMed:19632001}.
DE  Reference Proteome: Yes;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0003682;
GO  GO:0003677;
GO  GO:0042802;
GO  GO:0043495;
GO  GO:0051301;
GO  GO:0034508;
GO  GO:0007098;
GO  GO:0051642;
GO  GO:0000070;
GO  GO:0006998;
GO  GO:0006997;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGDYKPNYQSSPSRKRLPLQSKDQASIYKYQTPSTLNLYNNTVNNNSSNNSNNHLLHNSNPNSSYLYDSSKQYSNQINI
SQ  RNNSNSNSNTNNITSKKASSSYSINNKVDHNSHNNNDDDDIEDDVDINYSTNNASSNILHNRFSNSNKDDSYIDYSTDEN
SQ  PKILKQPQPLYNHLNNQIQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQRNNNNNSNSSNNNNTSTTIKRNNQQID
SQ  NNSNKNIISKFIGDPWKNFYYGSNKSLWPFERNNNSNNSSNNNNKVNFKQAIWIFIFSVLFIGCLLGLFSTNFYGIHIYF
SQ  PSFSTTKTNSPFNSTNNNIQFSNLITKEQLYPIIDEYFKKNEILKSYNKLFEKIENDIKYLSEREQYKDIINEIKEELKL
SQ  VKLSNMDEDRVNQLISKMINHYNNNENNKQELKELLSKSIEELTKLKSDSKEQLIQISTESMNQLGQLKSESINQLGQVK
SQ  SESIDKFQSTLKSLSKEEQSKIEREFNHQFNQLNKDADQLLSQHSLKIEKLREEINENQQSSLLKLTQEYKQLEERLKEF
SQ  SSKLQQSISSSSMDQFESWKLVFIKDIEERINKESSKLTNQYIQLTQQFTKIQSFIKDNPSIDSLTNTIESLEGIKLLIE
SQ  DILEVYSADKIAKVDYALGLAGASIEYNALHYRVSETYPPIKGSGSGSGSGGANGNSLGLYYYNLATNWIFPQPKPNPPE
SQ  TILDPMVNTGSCWGFYTGNGTIVIRLAKKIAITEVTMEHISSNISHHIDSAPKEFQVFGLINSSDIGQSLGVFTYDTTIN
SQ  RHLQTFKVNKIQSTTTTTTNQDQNDDDNIQEFSHVALRILSNHGYRYTCIYRFRVHGYQIPHPEQEQIQIIQEEQSFKQE
SQ  EINQQQIEQIEQIEQIEKQQQSDEL
//
ID  O94901;
PN  SUN domain-containing protein 1;
GN  SUN1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19933576}. Note=At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. {ECO:0000250|UniProtKB:Q9D666}.
DR  UNIPROT: O94901;
DR  UNIPROT: A5PL20;
DR  UNIPROT: B3KMV7;
DR  UNIPROT: B4DZF7;
DR  UNIPROT: B7WNY4;
DR  UNIPROT: B7WP53;
DR  UNIPROT: E9PDU4;
DR  UNIPROT: E9PF23;
DR  UNIPROT: F8WD13;
DR  UNIPROT: Q96CZ7;
DR  UNIPROT: Q9HA14;
DR  UNIPROT: Q9UH98;
DR  PDB: 6R15;
DR  PDB: 6R16;
DR  PDB: 6R2I;
DR  PDB: 7E34;
DR  Pfam: PF18580;
DR  Pfam: PF09387;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DR  OMIM: 607723;
DR  DisGeNET: 23353;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (PubMed:18039933, PubMed:18396275). The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration (By similarity). Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly (By similarity). Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis (By similarity). Helps to define the distribution of nuclear pore complexes (NPCs) (By similarity). Required for efficient localization of SYNE4 in the nuclear envelope (By similarity). May be involved in nuclear remodeling during sperm head formation in spermatogenesis (By similarity). May play a role in DNA repair by suppressing non- homologous end joining repair to facilitate the repair of DNA cross- links (PubMed:24375709). {ECO:0000250|UniProtKB:Q9D666, ECO:0000269|PubMed:18039933, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:24375709}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5NFR9; IntAct: EBI-2796914; Score: 0.00
DE  Interaction: Q8NF91; IntAct: EBI-6163229; Score: 0.52
DE  Interaction: Q8WXH0; IntAct: EBI-6163348; Score: 0.52
DE  Interaction: O94901; IntAct: EBI-6171008; Score: 0.40
DE  Interaction: P04578; IntAct: EBI-6174316; Score: 0.46
DE  Interaction: P06461; IntAct: EBI-11723785; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11398030; Score: 0.27
DE  Interaction: Q80VJ8; IntAct: EBI-11685143; Score: 0.27
DE  Interaction: Q9Y6Q1; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: Q86UE6; IntAct: EBI-21507777; Score: 0.35
DE  Interaction: P16444; IntAct: EBI-21514808; Score: 0.35
DE  Interaction: Q8TCN5; IntAct: EBI-21528943; Score: 0.35
DE  Interaction: Q15654; IntAct: EBI-21528943; Score: 0.35
DE  Interaction: A2RUC4; IntAct: EBI-21528943; Score: 0.35
DE  Interaction: Q8WWF5; IntAct: EBI-21589535; Score: 0.35
DE  Interaction: Q9BQ31; IntAct: EBI-21590203; Score: 0.35
DE  Interaction: Q8N6G5; IntAct: EBI-21622328; Score: 0.35
DE  Interaction: Q9NVF7; IntAct: EBI-21671334; Score: 0.35
DE  Interaction: Q53F39; IntAct: EBI-21694305; Score: 0.35
DE  Interaction: Q6AZY7; IntAct: EBI-21722497; Score: 0.35
DE  Interaction: Q401N2; IntAct: EBI-21749859; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-20908648; Score: 0.40
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-22057164; Score: 0.46
DE  Interaction: P02545; IntAct: EBI-22057187; Score: 0.40
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
GO  GO:0005737;
GO  GO:0005639;
GO  GO:0043231;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0140444;
GO  GO:0005521;
GO  GO:0043495;
GO  GO:0051642;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0006998;
GO  GO:0090292;
GO  GO:0021817;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MDFSRLHMYSPPQCVPENTGYTYALSSSYSSDALDFETEHKLDPVFDSPRMSRRSLRLATTACTLGDGEAVGADSGTSSA
SQ  VSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGVSHGGTVSLQDAVTRRPPVLDESWIREQTTVDHFWGLDDDGDLKG
SQ  GNKAAIQGNGDVGAAAATAHNGFSCSNCSMLSERKDVLTAHPAAPGPVSRVYSRDRNQKCYFLLQILRRIGAVGQAVSRT
SQ  AWSALWLAVVAPGKAASGVFWWLGIGWYQFVTLISWLNVFLLTRCLRNICKFLVLLIPLFLLLAGLSLRGQGNFFSFLPV
SQ  LNWASMHRTQRVDDPQDVFKPTTSRLKQPLQGDSEAFPWHWMSGVEQQVASLSGQCHHHGENLRELTTLLQKLQARVDQM
SQ  EGGAAGPSASVRDAVGQPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQLLPTVEHLQL
SQ  ELDQLKSELSSWRHVKTGCETVDAVQERVDVQVREMVKLLFSEDQQGGSLEQLLQRFSSQFVSKGDLQTMLRDLQLQILR
SQ  NVTHHVSVTKQLPTSEAVVSAVSEAGASGITEAQARAIVNSALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTAL
SQ  MSLFGIPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTLEHIPKTLSPTGNISSAPKDFAVYGLEN
SQ  EYQEEGQLLGQFTYDQDGESLQMFQALKRPDDTAFQIVELRIFSNWGHPEYTCLYRFRVHGEPVK
//
ID  Q9D666;
PN  SUN domain-containing protein 1;
GN  Sun1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:11593002, ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:17724119, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19841137, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:23348741}; Single-pass type II membrane protein {ECO:0000269|PubMed:11593002, ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:17724119, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19841137, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:23348741}. Note=At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. In round spermatids mainly localizes to the posterior pole of the nucleus. This localization is gradually disappearing during spermiogenesis. In elongated spermatids localizes to anterior regions outside the nucleus indicative for isoform 5. {ECO:0000269|PubMed:20711465, ECO:0000269|PubMed:26842404}. [Isoform 5]: Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane {ECO:0000305|PubMed:20711465}. Note=Localized to the anterior pole of spermatids. {ECO:0000305|PubMed:20711465}.
DR  UNIPROT: Q9D666;
DR  UNIPROT: D3Z0V9;
DR  UNIPROT: Q3TIW3;
DR  UNIPROT: Q3TV96;
DR  UNIPROT: Q6B4H0;
DR  UNIPROT: Q80SU8;
DR  UNIPROT: Q8BZ99;
DR  UNIPROT: Q99P23;
DR  PDB: 5YWZ;
DR  Pfam: PF18580;
DR  Pfam: PF09387;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (PubMed:20711465, PubMed:16380439, PubMed:24062341, PubMed:25892231, PubMed:26842404). The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (PubMed:19874786). Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration (PubMed:19874786). Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly (PubMed:17543860, PubMed:19211677, PubMed:19509342, PubMed:24062341, PubMed:25892231, PubMed:26842404). Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis (PubMed:17543860). Helps to define the distribution of nuclear pore complexes (NPCs) (PubMed:17724119). Required for efficient localization of SYNE4 in the nuclear envelope (PubMed:23348741). May be involved in nuclear remodeling during sperm head formation in spermatogenesis (PubMed:20711465). May play a role in DNA repair by suppressing non-homologous end joining repair to facilitate the repair of DNA cross-links (By similarity). {ECO:0000250|UniProtKB:O94901, ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:17543860, ECO:0000269|PubMed:17724119, ECO:0000269|PubMed:19211677, ECO:0000269|PubMed:19509342, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20711465, ECO:0000269|PubMed:23348741, ECO:0000269|PubMed:24062341, ECO:0000269|PubMed:25892231, ECO:0000269|PubMed:26842404}. Isoform 5 may be involved in nuclear remodeling during sperm head formation in spermatogenesis. A probable SUN1 isoform 5:SYNE3 LINC complex may tether spermatid nuclei to anterior cytoskeletal structures such as actin filaments present at membraneous junctions of spermatids and Sertoli cells. {ECO:0000305|PubMed:20711465}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-8034322; Score: 0.53
DE  Interaction: P50402; IntAct: EBI-6752609; Score: 0.52
DE  Interaction: Q4FZC9; IntAct: EBI-12557085; Score: 0.57
DE  Interaction: Q80VJ8; IntAct: EBI-11666366; Score: 0.59
DE  Interaction: Q8C0V1; IntAct: EBI-16089819; Score: 0.50
DE  Interaction: Q8WXH0; IntAct: EBI-6838672; Score: 0.40
DE  Interaction: Q8CAM5; IntAct: EBI-11568900; Score: 0.35
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005639;
GO  GO:0043231;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0002081;
GO  GO:0140444;
GO  GO:0005521;
GO  GO:0043495;
GO  GO:0051642;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0006998;
GO  GO:0090292;
GO  GO:0021817;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MDFSRLHTYTPPQCVPENTGYTYALSSSYSSDALDFETEHKLEPVFDSPRMSRRSLRLVTTASYSSGDSQAIDSHISTSR
SQ  ATPAKGRETRTVKQRRSASKPAFSINHLSGKGLSSSTSHDSSCSLRSATVLRHPVLDESLIREQTKVDHFWGLDDDGDLK
SQ  GGNKAATQGNGELAAEVASSNGYTCRDCRMLSARTDALTAHSAIHGTTSRVYSRDRTLKPRGVSFYLDRTLWLAKSTSSS
SQ  FASFIVQLFQVVLMKLNFETYKLKGYESRAYESQSYETKSHESEAHLGHCGRMTAGELSRVDGESLCDDCKGKKHLEIHT
SQ  ATHSQLPQPHRVAGAMGRLCIYTGDLLVQALRRTRAAGWSVAEAVWSVLWLAVSAPGKAASGTFWWLGSGWYQFVTLISW
SQ  LNVFLLTRCLRNICKVFVLLLPLLLLLGAGVSLWGQGNFFSLLPVLNWTAMQPTQRVDDSKGMHRPGPLPPSPPPKVDHK
SQ  ASQWPQESDMGQKVASLSAQCHNHDERLAELTVLLQKLQIRVDQVDDGREGLSLWVKNVVGQHLQEMGTIEPPDAKTDFM
SQ  TFHHDHEVRLSNLEDVLRKLTEKSEAIQKELEETKLKAGSRDEEQPLLDRVQHLELELNLLKSQLSDWQHLKTSCEQAGA
SQ  RIQETVQLMFSEDQQGGSLEWLLEKLSSRFVSKDELQVLLHDLELKLLQNITHHITVTGQAPTSEAIVSAVNQAGISGIT
SQ  EAQAHIIVNNALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALLSLFGVPLWYFSQSPRVVIQPDIYPGNCWAF
SQ  KGSQGYLVVRLSMKIYPTTFTMEHIPKTLSPTGNISSAPKDFAVYGLETEYQEEGQPLGRFTYDQEGDSLQMFHTLERPD
SQ  QAFQIVELRVLSNWGHPEYTCLYRFRVHGEPIQ
//
ID  Q9SG79;
PN  SUN domain-containing protein 2;
GN  SUN2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:19807882, ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:25412930}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:21294795}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21294795}; Single-pass type II membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:22270916}. Note=Dynamic localization during mitosis and meiosis, tightly coupled with nuclear envelope (NE) dynamics. Localized with the nuclear envelope during meiotic prophase I. NE re-formation during metaphase is temporally and spatially coordinated with plant-specific microtubule structures such as phragmoplasts. During anaphase, after NE breakdown (NEBD), predominantly localized with the endoplasmic reticulum, in the outside of the segregated chromosomes and not in between segregated chromosomes. {ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:25412930}.
DR  UNIPROT: Q9SG79;
DR  UNIPROT: Q8L9I5;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (PubMed:24667841). Required for the maintenance and/or formation of polarized nuclear shape in root hairs (PubMed:21294795). Modulates the anchoring and mobility of WIP proteins in the nuclear envelope (NE) (PubMed:22270916). In association with SUN1, may be involved in telomere attachment to nuclear envelope in the prophase of meiosis (PubMed:25412930). As component of the SUN-WIP- WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:22270916, ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:25412930, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9FF75; IntAct: EBI-11657653; Score: 0.37
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0009524;
GO  GO:0005819;
GO  GO:0043621;
GO  GO:0043495;
GO  GO:0070197;
GO  GO:0006998;
GO  GO:0006997;
GO  GO:0051291;
GO  GO:0051260;
GO  GO:0090435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSASTVSITASPRTIRRTPVLSGEKKSNFDFPPSESHANAAIGESSAGTNKDLIRAEAAGERSNTYDVGPVTRKSGSTAT
SQ  GTNTTTTQRRTRKSQGNKIDRGKWKTVVRVFAKQFGALLLLVGLIQLIRKLTLKDSSLSSSNFPIETEMVLSELESRISA
SQ  VDGLVKTTTKMMQVQVEFLDKKMDSESRALRQTIDSTSSVLHSELKKVESKTERLQVSVDELNAKPLVSREELERVYEEL
SQ  KKGKVGDSDVNIDKLRAYARDIVEKEIGKHVADGLGRVDYALASGGAFVMGHSDPFLVGNGRNWFGTSRRRVHSKAVKML
SQ  TPSFGEPGQCFPLKGSNGYVLVRLRAPIIPEAVTLEHVSKAVAYDRSSAPKDCRVSGWLGDIDMETETMPLLTEFSYDLD
SQ  RSNAQTFDIADSAHSGLVNTVRLDFNSNHGSSSHTCIYRFRVHGRELDSVSVAHA
//
ID  Q54MI3;
PN  SUN domain-containing protein 2;
GN  sun2;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q54MI3;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005773;
GO  GO:0031154;
GO  GO:0000281;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIINKKYILFILLLLFITSCTIVFSQQQQQQTEQSEQTEQAINNDVNNSINDIFENDSSKQLRQPQQQHTIVDDGNNNNN
SQ  NNNNNNNNNNNNNNNNNNNNNNNNNNNNNNPIDNKDILGLKKLALLKQFEEQKSKSENDINNDIVILNLENDNPNQIIET
SQ  TTTTLNNSNDNKNNIIDDNQDEKLNENIKEDKNEIKNEIKNENQEKDKGIIDVEKDENQPNIEEKGKEKQNLLEKGIENE
SQ  NQNENQIQIEKEKEIEIEIEKEKEKENKELIEESKTEKDNQQKENKENTNEINVTVVEEPEQPQPQQQNQQEQQEQQQQE
SQ  HKEEQQQQEQQQQEQQTQQEQQTHQQQQEHQETQKNSSEETKTQSPIQVNTTDVNNEIELKNEGDNNSQLNDSSIPITSP
SQ  LTNDNDTLKTTKEDSNNNNKNEVINNQTPLIDEKNHQHNYEGNNRNGDDVSIISNIPKTNKAPETQQQQQQQQQQQQQQQ
SQ  QQQQQQQQQQQQQQQQQQQQQQQQQQQHVVLTPNDLPDKFNYASSECGANVLQTNKEAWEVSSILASSRDRYLLNECNKS
SQ  QWFVVELCEEIGVQIIELANFEFFSSMFKDFIVLGSNRYPAQSWHYLGQFTAENSRKQQYFVLKEKAWYKYLKVKILSHY
SQ  GDQLYCPISSFKVYGSTMVDDLKNQVDINISELEKFQRDLSSIPYPMEIGSDTSYSTTTSTTSSSSTSSSYPSSKTKSSN
SQ  SEYPSWERIQSFSEKLRKNVEQQLIQPPSVLNTNDNNNNNNNNNNNNNNNNNNNNNNNNNEEQFIYYETNGNGGPPSTST
SQ  STSSSSSQNHQARTPQSVFKTLADKIKAIEFNQSIGNKFMEKLERYYSEEIKNLKFDVSEFLNDIIKLGNSLDEKLKDHR
SQ  KYDDNKFKETSKEIKILKEKIEKLEEQKSADRNFYLVVTLVSLLIGLLLKPLFTSSSSSSNKSYPNSMPNSPTYLNSGSN
SQ  NYNNNGIINSSGGSGGGGGNLQNSSFIGINGQLNFSDDNISAFLNSSCSNFGLNNNNNNNNGINNNNNNSNSNSNNNSIN
SQ  NGSININSNNSLQQRIHHNKYIHQRRNSSPLVGVQLESFFSPNAIPPTIPIVPQDDNNINYNYNNNNNTNNINNNYNYNN
SQ  NNNNNNNNNNNNNNNNNNNSDNYNNNNNSNNNVNSPSSPTPSSIILSPKFITSIPKNINYYNNGGSGSHLKNRFSRQASE
SQ  SVLSQNHYQINHQNHSLNGVTTNINNNNSNSNGNSNGNSNNMTNGLPPVSMPSSSSHDNLLLHRGNNQSKKYKRRSHL
//
ID  Q9UH99;
PN  SUN domain-containing protein 2;
GN  SUN2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:15082709}; Single-pass type II membrane protein {ECO:0000269|PubMed:15082709}. Nucleus envelope {ECO:0000269|PubMed:15082709, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:17724119}. Endosome membrane {ECO:0000269|PubMed:10818110}; Single-pass type II membrane protein {ECO:0000305}.
DR  UNIPROT: Q9UH99;
DR  UNIPROT: B0QY62;
DR  UNIPROT: O75156;
DR  UNIPROT: Q2NKN8;
DR  UNIPROT: Q2T9F7;
DR  UNIPROT: Q504T5;
DR  UNIPROT: Q6B4H1;
DR  UNIPROT: Q7Z3E3;
DR  PDB: 3UNP;
DR  PDB: 4DXR;
DR  PDB: 4DXS;
DR  PDB: 4DXT;
DR  PDB: 4FI9;
DR  PDB: 6WMD;
DR  PDB: 6WME;
DR  PDB: 6WMF;
DR  PDB: 6WMG;
DR  Pfam: PF18580;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DR  OMIM: 613569;
DR  DisGeNET: 25777;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome- nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5. {ECO:0000250|UniProtKB:Q8BJS4, ECO:0000269|PubMed:18396275, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: O43707; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-6838684; Score: 0.64
DE  Interaction: P50402; IntAct: EBI-6753091; Score: 0.64
DE  Interaction: Q14974; IntAct: EBI-8021405; Score: 0.40
DE  Interaction: Q8IXM6; IntAct: EBI-10262580; Score: 0.56
DE  Interaction: Q8NF91; IntAct: EBI-6163101; Score: 0.59
DE  Interaction: Q8WXH0; IntAct: EBI-6163111; Score: 0.77
DE  Interaction: Q9BTV4; IntAct: EBI-22085077; Score: 0.43
DE  Interaction: Q9GZS1; IntAct: EBI-1062028; Score: 0.00
DE  Interaction: Q9HC24; IntAct: EBI-1065806; Score: 0.00
DE  Interaction: P51148; IntAct: EBI-11124397; Score: 0.67
DE  Interaction: O15519; IntAct: EBI-1081176; Score: 0.00
DE  Interaction: O94817; IntAct: EBI-1081793; Score: 0.00
DE  Interaction: Q9H9G7; IntAct: EBI-2267899; Score: 0.35
DE  Interaction: Q9Y2K6; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q9Y297; IntAct: EBI-2514141; Score: 0.56
DE  Interaction: Q9UKB1; IntAct: EBI-2514231; Score: 0.40
DE  Interaction: A0A6L7HC63; IntAct: EBI-2811375; Score: 0.00
DE  Interaction: Q8ZAR3; IntAct: EBI-2850887; Score: 0.00
DE  Interaction: P02866; IntAct: EBI-2906001; Score: 0.35
DE  Interaction: P52292; IntAct: EBI-8021334; Score: 0.50
DE  Interaction: P53618; IntAct: EBI-8021495; Score: 0.56
DE  Interaction: P20339; IntAct: EBI-3938247; Score: 0.74
DE  Interaction: P61020; IntAct: EBI-3938257; Score: 0.37
DE  Interaction: P60866; IntAct: EBI-3938267; Score: 0.37
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: Q9UH99; IntAct: EBI-6163189; Score: 0.56
DE  Interaction: P45983; IntAct: EBI-10103723; Score: 0.35
DE  Interaction: Q13131; IntAct: EBI-10103860; Score: 0.35
DE  Interaction: P31943; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: Q9Y678; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: P22314; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: O00159; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: P68032; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: Q9ULV4; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: P12814; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: Q8N9N8; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: P60842; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: O00571; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: Q9NVE4; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: P13639; IntAct: EBI-10761374; Score: 0.35
DE  Interaction: Q8WZ42; IntAct: EBI-10761431; Score: 0.35
DE  Interaction: P68104; IntAct: EBI-10761431; Score: 0.35
DE  Interaction: P35278; IntAct: EBI-11002326; Score: 0.35
DE  Interaction: Q5SRY7; IntAct: EBI-11073514; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: A5A5U1; IntAct: EBI-12582509; Score: 0.35
DE  Interaction: I6T1Z2; IntAct: EBI-12581312; Score: 0.35
DE  Interaction: C5E526; IntAct: EBI-12584472; Score: 0.35
DE  Interaction: C5E527; IntAct: EBI-12585279; Score: 0.35
DE  Interaction: Q1K9H5; IntAct: EBI-12587743; Score: 0.35
DE  Interaction: B4URF7; IntAct: EBI-12589250; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: P56539; IntAct: EBI-21503437; Score: 0.35
DE  Interaction: Q9NWM8; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: Q9BTZ2; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: Q96FZ7; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: Q8TBX8; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: Q16851; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: Q07157; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: P78356; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: P50579; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: P48426; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: P42336; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: P16219; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: A5A3E0; IntAct: EBI-21542862; Score: 0.35
DE  Interaction: Q8WWF5; IntAct: EBI-21589535; Score: 0.35
DE  Interaction: Q8N6G5; IntAct: EBI-21622328; Score: 0.35
DE  Interaction: Q9Y5E2; IntAct: EBI-21688054; Score: 0.35
DE  Interaction: Q53F39; IntAct: EBI-21694305; Score: 0.35
DE  Interaction: Q6AZY7; IntAct: EBI-21722497; Score: 0.35
DE  Interaction: Q9H9Q2; IntAct: EBI-21739689; Score: 0.35
DE  Interaction: Q9NZM5; IntAct: EBI-21744295; Score: 0.35
DE  Interaction: Q9UKA2; IntAct: EBI-21810867; Score: 0.35
DE  Interaction: Q2TAP0; IntAct: EBI-21848389; Score: 0.35
DE  Interaction: Q53F19; IntAct: EBI-20623276; Score: 0.35
DE  Interaction: P52298; IntAct: EBI-20623424; Score: 0.35
DE  Interaction: Q15084; IntAct: EBI-20910128; Score: 0.40
DE  Interaction: P05204; IntAct: EBI-20922938; Score: 0.40
DE  Interaction: Q9Y251; IntAct: EBI-21260107; Score: 0.35
DE  Interaction: Q9UET6; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: Q9NNW5; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: Q96Q15; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: Q96PK6; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: Q6P5S8; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: Q6NZY4; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: Q13616; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: Q04446; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: P63208; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: P31946; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: P30049; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: O95470; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: J3KTF8; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: B4DH70; IntAct: EBI-21265800; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q99963; IntAct: EBI-25388104; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25491278; Score: 0.53
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.35
DE  Interaction: D0ZIB5; IntAct: EBI-27034209; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27111302; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
GO  GO:0010008;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0140444;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0008017;
GO  GO:0043495;
GO  GO:0051642;
GO  GO:0051321;
GO  GO:0007052;
GO  GO:0006998;
GO  GO:0090292;
GO  GO:0007097;
GO  GO:0031022;
GO  GO:0030335;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis;
SQ  MSRRSQRLTRYSQGDDDGSSSSGGSSVAGSQSTLFKDSPLRTLKRKSSNMKRLSPAPQLGPSSDAHTSYYSESLVHESWF
SQ  PPRSSLEELHGDANWGEDLRVRRRRGTGGSESSRASGLVGRKATEDFLGSSSGYSSEDDYVGYSDVDQQSSSSRLRSAVS
SQ  RAGSLLWMVATSPGRLFRLLYWWAGTTWYRLTTAASLLDVFVLTRRFSSLKTFLWFLLPLLLLTCLTYGAWYFYPYGLQT
SQ  FHPALVSWWAAKDSRRPDEGWEARDSSPHFQAEQRVMSRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGG
SQ  GGLSHEDTLALLEGLVSRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQ
SQ  ESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREE
SQ  MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESGGASVIS
SQ  TRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALSPNSTIS
SQ  SAPKDFAIFGFDEDLQQEGTLLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH
//
ID  Q8BJS4;
PN  SUN domain-containing protein 2;
GN  Sun2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UH99}. Nucleus envelope {ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:19933576}. Endosome membrane {ECO:0000250|UniProtKB:Q9UH99}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9UH99}. Note=Colocalizes with KASH5 at sites of telomere attachment in meiocytes. {ECO:0000269|PubMed:24586178}.
DR  UNIPROT: Q8BJS4;
DR  UNIPROT: Q3TBU0;
DR  UNIPROT: Q3U160;
DR  UNIPROT: Q6B4H2;
DR  PDB: 5ED8;
DR  PDB: 5ED9;
DR  Pfam: PF18580;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome- nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for Rab5-GDP and participate in the activation of Rab5. {ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:19509342, ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:21177258, ECO:0000269|PubMed:23071752, ECO:0000269|PubMed:24586178, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: A2A8U2; IntAct: EBI-12591483; Score: 0.54
DE  Interaction: P48678; IntAct: EBI-12591503; Score: 0.35
DE  Interaction: Q6ZWQ0; IntAct: EBI-16189259; Score: 0.53
DE  Interaction: Q80VJ8; IntAct: EBI-11666392; Score: 0.37
DE  Interaction: P39428; IntAct: EBI-657584; Score: 0.37
DE  Interaction: Q3U1F9; IntAct: EBI-12603117; Score: 0.40
DE  Interaction: Q8BJS4; IntAct: EBI-16189288; Score: 0.65
DE  Interaction: P07602; IntAct: EBI-21347829; Score: 0.35
GO  GO:0000781;
GO  GO:0000794;
GO  GO:0010008;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0140444;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0043495;
GO  GO:0051642;
GO  GO:0051321;
GO  GO:0006998;
GO  GO:0090292;
GO  GO:0031022;
GO  GO:0021817;
GO  GO:0030335;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSRRSQRLTRYSQDDNDGGSSSSGASSVAGSQGTVFKDSPLRTLKRKSSNMKHLSPAPQLGPSSDSHTSYYSESVVRESY
SQ  IGSPRAVSLARSALLDDHLHSEPYWSGDLRGRRRRGTGGSESSKANGLTAESKASEDFFGSSSGYSSEDDLAGYTDSDQH
SQ  SSGSRLRSAASRAGSFVWTLVTFPGRLFGLLYWWIGTTWYRLTTAASLLDVFVLTRSRHFSLNLKSFLWFLLLLLLLTGL
SQ  TYGAWHFYPLGLQTLQPAVVSWWAAKESRKQPEVWESRDASQHFQAEQRVLSRVHSLERRLEALAADFSSNWQKEAIRLE
SQ  RLELRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLKEDLRRDTVAHIQEELATLRAEHHQDSEDLFKKIVQASQESEA
SQ  RVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESQFPDWIRQFLL
SQ  GDRGARSGLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQRYSEDRIGM
SQ  VDYALESGGASVISTRCSETYETKTALLSLFGIPLWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTL
SQ  EHVPKALSPNSTISSAPKDFAIFGFDEDLQQEGTLLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCI
SQ  YRFRVHGEPAH
//
ID  F4I316;
PN  SUN domain-containing protein 3;
GN  SUN3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: F4I316;
DR  UNIPROT: O23133;
DR  UNIPROT: Q8GX04;
DR  UNIPROT: Q8H7G6;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Encodes a member of the mid-SUN subfamily of SUN-domain proteins that is localized to both the nuclear envelope and the ER. It is involved in early seed development and nuclear morphology. [TAIR].
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0043621;
GO  GO:0042742;
GO  GO:0009409;
GO  GO:0009651;
GO  GO:0009414;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQRSCRTRRRVSVNKFNGRNSFYKVSLSLVFLLWVLLFFSTLLISHGDGAKDEPLNDSMGMADPDDGQSDEKVVPFDGPL
SQ  SLASASVDVTSDLSRNDDVNLSEESEDKEQEAEISSTVSGNDIESKDTYLLKQSEINKKDTGIDAGSKYDDFPKKSEINN
SQ  TGTWNDTEGKDDNNFLKQSQLNKTGTGNDTESSDNEFLEQNQMNKTVLGNGTEINVSKVDQPSRAVPLGLDEFKSRASNS
SQ  RNKSLSDQVSGVIHRMEPGGKEYNYASASKGAKVLSSNKEAKGAASILSRDNDKYLRNPCSTEGKFVVVELSEETLVNTI
SQ  KIANFEHYSSNLKEFELQGTLVYPTDTWVHMGNFTASNVKHEQNFTLLEPKWVRYLKLNFISHYGSEFYCTLSLIEVYGV
SQ  DAVERMLEDLISVQDNKNAYKPREGDSEHKEKPMQQIESLEGDDGADKSTHREKEKEAPPENMLAKTEASMAKSSNKLSE
SQ  PVEEMRHHQPGSRMPGDTVLKILMQKLRSLDLNLSILERYLEELNLRYGNIFKEMDREAGVREKAIVALRLDLEGMKERQ
SQ  EGMVSEAEEMKEWRKRVEAEMEKAEKEKENIRQSLEQVSKRLEWMEKKCLTVFTVCLGFGIIAVIAVVIGMGTGLAEKTG
SQ  SGAWLLLLISSTFIMFVLSL
//
ID  Q0II64;
PN  SUN domain-containing protein 3;
GN  SUN3;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q5SS91}. Nucleus inner membrane {ECO:0000305}.
DR  UNIPROT: Q0II64;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: As a probable component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nuclear remodeling during sperm head formation in spermatogenesis. A probable SUN3:SYNE1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250|UniProtKB:Q5SS91}.
DE  Reference Proteome: Yes;
GO  GO:0005639;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRPNSRGSSRLFRAPSEDASSGSSGSAVLPQEENPNASGLTRSWKAVMGMVFILTLLLLGFINHMKLKEKAFPQKSRQ
SQ  IYAVIAEYGSRLYNYQARLRMPKEQLELLKKESQTLENNFREILFLIEQIDVLKALLRDMQDGLHNYSWNADIDPAEGWN
SQ  HTEVIDEEMSNLVNYILKKLREDQVQMADYALKSAGASVVEAGTSESYKNNKAKLYWHGIGFLNYEMPPDIILQPDVHPG
SQ  KCWAFPGSQGHALIKLARKIIPTAVTMEHISEKVSPSGNISSAPKEFSVYGVLKQCEGEEIFLGQFVYNKTGTTVQTFAL
SQ  QHEVPEFLLCVKLKILSNWGHPNYTCLYRFRVHGTPKDDS
//
ID  Q8TAQ9;
PN  SUN domain-containing protein 3;
GN  SUN3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q5SS91}. Nucleus inner membrane {ECO:0000305}.
DR  UNIPROT: Q8TAQ9;
DR  UNIPROT: A4D2F3;
DR  UNIPROT: B4DXK1;
DR  UNIPROT: D3DVM3;
DR  UNIPROT: E7EWC8;
DR  UNIPROT: Q4F965;
DR  UNIPROT: Q7Z4U8;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DR  OMIM: 618984;
DR  DisGeNET: 256979;
DE  Function: As a probable component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nuclear remodeling during sperm head formation in spermatogenesis. A probable SUN3:SYNE1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250|UniProtKB:Q5SS91}.
DE  Reference Proteome: Yes;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0043495;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGKTKARRAAMFFRRCSEDASGSASGNALLSEDENPDANGVTRSWKIILSTMLTLTFLLVGLLNHQWLKETDVPQKSRQ
SQ  LYAIIAEYGSRLYKYQARLRMPKEQLELLKKESQNLENNFRQILFLIEQIDVLKALLRDMKDGMDNNHNWNTHGDPVEDP
SQ  DHTEEVSNLVNYVLKKLREDQVEMADYALKSAGASIIEAGTSESYKNNKAKLYWHGIGFLNHEMPPDIILQPDVYPGKCW
SQ  AFPGSQGHTLIKLATKIIPTAVTMEHISEKVSPSGNISSAPKEFSVYGITKKCEGEEIFLGQFIYNKTGTTVQTFELQHA
SQ  VSEYLLCVKLNIFSNWGHPKYTCLYRFRVHGTPGKHI
//
ID  Q95LV7;
PN  SUN domain-containing protein 3;
GN  SUN3;
OS  9541;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q5SS91}. Nucleus inner membrane {ECO:0000305}.
DR  UNIPROT: Q95LV7;
DR  UNIPROT: G7P1S8;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: As a probable component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nuclear remodeling during sperm head formation in spermatogenesis. A probable SUN3:SYNE1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250|UniProtKB:Q5SS91}.
DE  Reference Proteome: Yes;
GO  GO:0005639;
GO  GO:0034993;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGKAKARRAAMFFRGCSEDASGSTSGSTLLSEDENPDTNGVTRSWKIILSTMFTLTFLLVGLLSHQWLKETEVPQKSRQ
SQ  LYAIIAEYGSRLYKYQARLRMPKEQLELLKKESQTLENNFHKILLLIEQIDVLKALLRDMKDGTDNNHSWNTHGDPVEDP
SQ  DHTEVLDEEMSNLVNYVLKKLREDQVQMADYALKSAGASIIEAGTSESYKNNKAKLYWHGISFLNHEMPPDIILQPDVYP
SQ  GNCWAFPGSQGHTLIKLATKIIPTAVTMEHISEKVSPSGNISSAPKEFSVYGITKKCEGEEIFLGQFIYNKTGTTVQTFE
SQ  LQHAVSEYLLCVKLNIFSNWGHPKYTCLYRFRVHGTPGKHI
//
ID  Q5SS91;
PN  SUN domain-containing protein 3;
GN  Sun3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:20711465}. Nucleus inner membrane {ECO:0000305}. Note=Localized to spermatid nucleus posterior pole lateral regions excluding the implantation fossa during entire sperm head elongation. {ECO:0000269|PubMed:20711465}.
DR  UNIPROT: Q5SS91;
DR  UNIPROT: Q8BHY0;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: As a probable component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nuclear remodeling during sperm head formation in spermatogenesis. A probable SUN3:SYNE1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000305|PubMed:20711465}.
DE  Reference Proteome: Yes;
DE  Interaction: Q4FZC9; IntAct: EBI-12557132; Score: 0.40
DE  Interaction: Q6ZWR6; IntAct: EBI-12557121; Score: 0.46
DE  Interaction: Q9JJF2; IntAct: EBI-12557506; Score: 0.51
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0043495;
GO  GO:0006998;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLTRSWKIILSTVFISTFLLVGLLNHQWLKETEFPQKPRQLYTVIAEYGSRLYNYQARLRMPKEQQELLKKESQTLENNF
SQ  REILFLIEQIDVLKALLKDMKDGVHNHSLPVHRDAVQDQATTDVLDEEMSNLVHYVLKKFRGDQIQLADYALKSAGASVI
SQ  EAGTSESYKNNKAKLYWHGIGFLNYEMPPDMILQPDVHPGKCWAFPGSQGHILIKLARKIIPTAVTMEHISEKVSPSGNI
SQ  SSAPKEFSVYGVMKKCEGEEIFLGQFIYNKMEATIQTFELQNEASESLLCVKLQILSNWGHPKYTCLYRFRVHGIPSDYT
//
ID  F4I8I0;
PN  SUN domain-containing protein 4;
GN  SUN4;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: F4I8I0;
DR  UNIPROT: Q0WQI7;
DR  UNIPROT: Q9C9H3;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Encodes a member of the mid-SUN subfamily of SUN-domain proteins that is localized to both the nuclear envelope and the ER. It is involved in early seed development and nuclear morphology. [TAIR].
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0043621;
GO  GO:0006997;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQRSRRALLVRRRVSETTSNGRNRFYKVSLSLVFLIWGLVFLSTLWISHVDGDKGRSLVDSVEKGEPDDERADETAESVD
SQ  ATSLESTSVHSNPGLSSDVDIAAAGESKGSETILKQLEVDNTIVIVGNVTESKDNVPMKQSEINNNTVPGNDTETTGSKL
SQ  DQLSRAVPLGLDEFKSRASNSRDKSLSGQVTGVIHRMEPGGKEYNYAAASKGAKVLSSNKEAKGASSIICRDKDKYLRNP
SQ  CSTEGKFVVIELSEETLVNTIKIANFEHYSSNLKDFEILGTLVYPTDTWVHLGNFTALNMKHEQNFTFADPKWVRYLKLN
SQ  LLSHYGSEFYCTLSLLEVYGVDAVERMLEDLISIQDKNILKLQEGDTEQKEKKTMQAKESFESDEDKSKQKEKEQEASPE
SQ  NAVVKDEVSLEKRKLPDPVEEIKHQPGSRMPGDTVLKILMQKIRSLDVSLSVLESYLEERSLKYGMIFKEMDLEASKREK
SQ  EVETMRLEVEGMKEREENTKKEAMEMRKWRMRVETELEKAENEKEKVKERLEQVLERLEWMEKKGVVVFTICVGFGTIAV
SQ  VAVVFGMGIVRAEKQGGLAWLLLLISSTFVMFILSL
//
ID  Q8TC36;
PN  SUN domain-containing protein 5;
GN  SUN5;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000305|PubMed:27640305}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9DA32}. Golgi apparatus {ECO:0000250|UniProtKB:Q9DA32}. Note=During spermiogenesis, traffics through the Golgi apparatus before reaching the round spermatid inner membrane of the nuclear envelope and later migrates to the coupling apparatus of the sperm during sperm head elongation and differentiation. In mature spermatozoa, is localized to the coupling apparatus of the sperm head and tail in the implementation fossa. {ECO:0000305|PubMed:27640305}.
DR  UNIPROT: Q8TC36;
DR  UNIPROT: A6NJ82;
DR  UNIPROT: Q5T9R0;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DR  OMIM: 613942;
DR  OMIM: 617187;
DR  DisGeNET: 140732;
DE  Function: Plays an essential role in anchoring sperm head to the tail. Is responsible for the attachment of the coupling apparatus to the sperm nuclear envelope. {ECO:0000305|PubMed:28541472, ECO:0000305|PubMed:28945193}.
DE  Disease: Spermatogenic failure 16 (SPGF16) [MIM:617187]: An infertility disorder caused by spermatogenesis defects and characterized by abnormally shaped spermatozoa in the semen of affected individuals. Most spermatozoa are made up of headless tails, while a small proportion has an abnormal head-tail junction. A few spermatozoa are made up of tailless heads. {ECO:0000269|PubMed:27640305, ECO:0000269|PubMed:28541472, ECO:0000269|PubMed:28945193, ECO:0000269|PubMed:29298896}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NPE6; IntAct: EBI-24639374; Score: 0.56
GO  GO:0005794;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0097224;
GO  GO:0043495;
GO  GO:0006998;
GO  GO:0007286;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPRSSRSPGDPGALLEDVAHNPRPRRIAQRGRNTSRMAEDTSPNMNDNILLPVRNNDQALGLTQCMLGCVSWFTCFACSL
SQ  RTQAQQVLFNTCRCKLLCQKLMEKTGILLLCAFGFWMFSIHLPSKMKVWQDDSINGPLQSLRLYQEKVRHHSGEIQDLRG
SQ  SMNQLIAKLQEMEAMSDEQKMAQKIMKMIHGDYIEKPDFALKSIGASIDFEHTSVTYNHEKAHSYWNWIQLWNYAQPPDV
SQ  ILEPNVTPGNCWAFEGDRGQVTIQLAQKVYLSNLTLQHIPKTISLSGSLDTAPKDFVIYGMEGSPKEEVFLGAFQFQPEN
SQ  IIQMFPLQNQPARAFSAVKVKISSNWGNPGFTCLYRVRVHGSVAPPREQPHQNPYPKRD
//
ID  Q9DA32;
PN  SUN domain-containing protein 5;
GN  Sun5;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:21159740, ECO:0000269|PubMed:25775128, ECO:0000269|PubMed:28945193, ECO:0000269|PubMed:29298896}; Single-pass membrane protein {ECO:0000269|PubMed:21159740}. Golgi apparatus {ECO:0000269|PubMed:25775128}. Note=During spermiogenesis, traffics through the Golgi apparatus before reaching the round spermatid inner membrane of the nuclear envelope and later migrates to the coupling apparatus of the sperm during sperm head elongation and differentiation. In mature spermatozoa, is localized to the coupling apparatus of the sperm head and tail in the implementation fossa. {ECO:0000269|PubMed:21159740, ECO:0000269|PubMed:25775128, ECO:0000269|PubMed:28945193}.
DR  UNIPROT: Q9DA32;
DR  UNIPROT: D2DR64;
DR  UNIPROT: Q5DT38;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Plays an essential role in anchoring sperm head to the tail. Is responsible for the attachment of the coupling apparatus to the sperm nuclear envelope. {ECO:0000269|PubMed:28945193, ECO:0000305|PubMed:21711156}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0097224;
GO  GO:0043495;
GO  GO:0006998;
GO  GO:0007286;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPRTRNIGALCTLPEDTTHSGRPRRGVQRSYISRMAEPAPANMNDPLLLPLRMNTPGLSLVQILLGYMSWLTYLACFLRT
SQ  QTQQVFLNTCRCKLFCQKVMEKMGLLVLCVFGFWMFSMHLPSKVEVWQDDSINGPLQSLRMYQEKVRHHTGEIQDLRGSM
SQ  NQLIAKLQKMEAISDEQKMAQKIMKMIQGDYIEKPDFALKSIGASIDFEHTSATYNHDKARSYWNWIRLWNYAQPPDVIL
SQ  EPNVTPGNCWAFASDRGQVTIRLAQKVYLSNITLQHIPKTISLSGSPDTAPKDIVIYGLESLPREEVFLGAFQFQPENVI
SQ  QMFQLQNLPPRSFAAVKVKISSNWGNPRFTCMYRVRVHGSVTPPKDSHLEPLS
//
ID  Q2NL30;
PN  Histone-lysine N-methyltransferase SUV39H1;
GN  SUV39H1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus {ECO:0000250}. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Associates with centromeric constitutive heterochromatin. {ECO:0000250}.
DR  UNIPROT: Q2NL30;
DR  Pfam: PF00385;
DR  Pfam: PF05033;
DR  Pfam: PF00856;
DR  PROSITE: PS00598;
DR  PROSITE: PS50013;
DR  PROSITE: PS50868;
DR  PROSITE: PS50867;
DR  PROSITE: PS51579;
DR  PROSITE: PS50280;
DE  Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000775;
GO  GO:0000792;
GO  GO:0005652;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0046974;
GO  GO:0000976;
GO  GO:0008270;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0006325;
GO  GO:0036123;
GO  GO:0036124;
GO  GO:0042754;
GO  GO:0045892;
GO  GO:0048511;
GO  GO:0006364;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAESLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNL
SQ  KCVRILKQFHKDLERELLRRHHRSKPPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAF
SQ  VYINEYRVGEGITLNQVAVGCECQDCLWAPAGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKG
SQ  IRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISH
SQ  FVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIEC
SQ  KCGTESCRKYLF
//
ID  O43463;
PN  Histone-lysine N-methyltransferase SUV39H1;
GN  SUV39H1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus. Nucleus lamina. Nucleus, nucleoplasm. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin.
DR  UNIPROT: O43463;
DR  UNIPROT: B2R6E8;
DR  UNIPROT: B4DST0;
DR  UNIPROT: Q53G60;
DR  UNIPROT: Q6FHK6;
DR  PDB: 3MTS;
DR  Pfam: PF00385;
DR  Pfam: PF05033;
DR  Pfam: PF00856;
DR  PROSITE: PS00598;
DR  PROSITE: PS50013;
DR  PROSITE: PS50868;
DR  PROSITE: PS50867;
DR  PROSITE: PS51579;
DR  PROSITE: PS50280;
DR  OMIM: 300254;
DR  DisGeNET: 6839;
DE  Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. {ECO:0000269|PubMed:14765126, ECO:0000269|PubMed:16449642, ECO:0000269|PubMed:16818776, ECO:0000269|PubMed:16858404, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:18485871}.
DE  Reference Proteome: Yes;
DE  Interaction: P68432; IntAct: EBI-350122; Score: 0.44
DE  Interaction: P68431; IntAct: EBI-360204; Score: 0.40
DE  Interaction: P45973; IntAct: EBI-760225; Score: 0.95
DE  Interaction: Q15156; IntAct: EBI-869185; Score: 0.52
DE  Interaction: P29590; IntAct: EBI-870893; Score: 0.40
DE  Interaction: Q9UIS9; IntAct: EBI-994581; Score: 0.56
DE  Interaction: Q13547; IntAct: EBI-994733; Score: 0.52
DE  Interaction: Q92769; IntAct: EBI-994747; Score: 0.52
DE  Interaction: Q9C0K0; IntAct: EBI-7212308; Score: 0.56
DE  Interaction: O43159; IntAct: EBI-2008823; Score: 0.52
DE  Interaction: Q96ED9; IntAct: EBI-8647977; Score: 0.67
DE  Interaction: O00257; IntAct: EBI-5277008; Score: 0.44
DE  Interaction: O95260; IntAct: EBI-8464506; Score: 0.51
DE  Interaction: P15313; IntAct: EBI-8464546; Score: 0.37
DE  Interaction: P18847; IntAct: EBI-8464526; Score: 0.37
DE  Interaction: Q8TBE0; IntAct: EBI-8464603; Score: 0.37
DE  Interaction: Q9NWQ4; IntAct: EBI-8465349; Score: 0.51
DE  Interaction: Q86X59; IntAct: EBI-8465546; Score: 0.37
DE  Interaction: Q5T0J7; IntAct: EBI-8465745; Score: 0.37
DE  Interaction: Q53FE4; IntAct: EBI-8465880; Score: 0.37
DE  Interaction: Q6P047; IntAct: EBI-8466103; Score: 0.51
DE  Interaction: Q96H12; IntAct: EBI-8466221; Score: 0.37
DE  Interaction: A5D8V7; IntAct: EBI-8466476; Score: 0.51
DE  Interaction: Q494V2; IntAct: EBI-8466606; Score: 0.37
DE  Interaction: Q9UJX2; IntAct: EBI-8466789; Score: 0.37
DE  Interaction: Q9BXL8; IntAct: EBI-8466866; Score: 0.51
DE  Interaction: Q96GN5; IntAct: EBI-8467032; Score: 0.37
DE  Interaction: P49761; IntAct: EBI-8467270; Score: 0.51
DE  Interaction: Q96SW2; IntAct: EBI-8467328; Score: 0.37
DE  Interaction: Q6UXH1; IntAct: EBI-8467387; Score: 0.37
DE  Interaction: Q8NFT6; IntAct: EBI-8467523; Score: 0.37
DE  Interaction: P60002; IntAct: EBI-8467848; Score: 0.37
DE  Interaction: Q15910; IntAct: EBI-8468009; Score: 0.51
DE  Interaction: Q6ZNL6; IntAct: EBI-8468327; Score: 0.51
DE  Interaction: Q6PJQ5; IntAct: EBI-8468537; Score: 0.37
DE  Interaction: Q96NE9; IntAct: EBI-8468582; Score: 0.37
DE  Interaction: P35637; IntAct: EBI-8468619; Score: 0.37
DE  Interaction: P06241; IntAct: EBI-8468767; Score: 0.37
DE  Interaction: Q6P1K8; IntAct: EBI-8469749; Score: 0.37
DE  Interaction: Q9BX10; IntAct: EBI-8469814; Score: 0.51
DE  Interaction: Q6NXT2; IntAct: EBI-8469928; Score: 0.37
DE  Interaction: P49639; IntAct: EBI-8470602; Score: 0.51
DE  Interaction: P09017; IntAct: EBI-8470785; Score: 0.51
DE  Interaction: P41134; IntAct: EBI-8470899; Score: 0.37
DE  Interaction: Q02363; IntAct: EBI-8470956; Score: 0.37
DE  Interaction: P22692; IntAct: EBI-8471165; Score: 0.37
DE  Interaction: Q14005; IntAct: EBI-8471351; Score: 0.37
DE  Interaction: Q9UNL4; IntAct: EBI-8471427; Score: 0.37
DE  Interaction: Q9H0H0; IntAct: EBI-8471498; Score: 0.37
DE  Interaction: Q9UIH9; IntAct: EBI-8472230; Score: 0.37
DE  Interaction: Q8TBB5; IntAct: EBI-8472509; Score: 0.51
DE  Interaction: Q9Y2M5; IntAct: EBI-8472700; Score: 0.37
DE  Interaction: Q9BYZ2; IntAct: EBI-8473716; Score: 0.37
DE  Interaction: Q96PV6; IntAct: EBI-8473810; Score: 0.37
DE  Interaction: Q68G74; IntAct: EBI-8474100; Score: 0.37
DE  Interaction: Q8TBB1; IntAct: EBI-8474341; Score: 0.37
DE  Interaction: Q96JB6; IntAct: EBI-8474426; Score: 0.37
DE  Interaction: Q9UDY8; IntAct: EBI-8474830; Score: 0.37
DE  Interaction: O95243; IntAct: EBI-8474998; Score: 0.37
DE  Interaction: Q96EZ8; IntAct: EBI-8475092; Score: 0.37
DE  Interaction: Q9Y483; IntAct: EBI-8476026; Score: 0.37
DE  Interaction: Q9Y2Z2; IntAct: EBI-8476214; Score: 0.37
DE  Interaction: P55055; IntAct: EBI-8477342; Score: 0.37
DE  Interaction: Q13133; IntAct: EBI-8477418; Score: 0.51
DE  Interaction: Q9H6K4; IntAct: EBI-8477926; Score: 0.37
DE  Interaction: Q5T6S3; IntAct: EBI-8478603; Score: 0.51
DE  Interaction: Q96T60; IntAct: EBI-8478792; Score: 0.37
DE  Interaction: P49643; IntAct: EBI-8479094; Score: 0.37
DE  Interaction: P62191; IntAct: EBI-8479522; Score: 0.51
DE  Interaction: Q9NS23; IntAct: EBI-8480267; Score: 0.51
DE  Interaction: P50749; IntAct: EBI-8480360; Score: 0.51
DE  Interaction: Q6UXX9; IntAct: EBI-8481068; Score: 0.37
DE  Interaction: Q8IYM2; IntAct: EBI-8481728; Score: 0.37
DE  Interaction: Q86W54; IntAct: EBI-8483275; Score: 0.37
DE  Interaction: Q7Z699; IntAct: EBI-8483411; Score: 0.37
DE  Interaction: Q96BD6; IntAct: EBI-8483512; Score: 0.51
DE  Interaction: O43295; IntAct: EBI-8483786; Score: 0.37
DE  Interaction: O75558; IntAct: EBI-8484895; Score: 0.37
DE  Interaction: Q8N4C7; IntAct: EBI-8485007; Score: 0.51
DE  Interaction: O60341; IntAct: EBI-8485081; Score: 0.37
DE  Interaction: Q96LA8; IntAct: EBI-8485135; Score: 0.37
DE  Interaction: P17152; IntAct: EBI-8485829; Score: 0.37
DE  Interaction: Q13829; IntAct: EBI-8485866; Score: 0.37
DE  Interaction: Q01081; IntAct: EBI-8487076; Score: 0.51
DE  Interaction: Q8IZQ1; IntAct: EBI-8487862; Score: 0.37
DE  Interaction: Q5TAQ9; IntAct: EBI-8488086; Score: 0.51
DE  Interaction: O95785; IntAct: EBI-8488561; Score: 0.37
DE  Interaction: O43167; IntAct: EBI-8488636; Score: 0.37
DE  Interaction: Q9NP64; IntAct: EBI-8488764; Score: 0.37
DE  Interaction: Q9Y2L8; IntAct: EBI-8488958; Score: 0.51
DE  Interaction: P49910; IntAct: EBI-8489049; Score: 0.37
DE  Interaction: O15535; IntAct: EBI-8489086; Score: 0.37
DE  Interaction: Q9C0F3; IntAct: EBI-8489696; Score: 0.51
DE  Interaction: Q9Y4E5; IntAct: EBI-8490124; Score: 0.37
DE  Interaction: Q68EA5; IntAct: EBI-8490810; Score: 0.37
DE  Interaction: Q9BS31; IntAct: EBI-8491151; Score: 0.51
DE  Interaction: Q9BS34; IntAct: EBI-8491255; Score: 0.51
DE  Interaction: Q3KNS6; IntAct: EBI-8491346; Score: 0.37
DE  Interaction: Q13185; IntAct: EBI-8831531; Score: 0.74
DE  Interaction: P17987; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: Q99832; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: P48643; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: P78371; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: P50991; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: P83916; IntAct: EBI-8836034; Score: 0.67
DE  Interaction: P01106; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: O75556; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: Q8IWI9; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: Q14839; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: O60281; IntAct: EBI-8836034; Score: 0.35
DE  Interaction: Q63HR2; IntAct: EBI-10697145; Score: 0.37
DE  Interaction: Q8TB24; IntAct: EBI-10700383; Score: 0.37
DE  Interaction: P60409; IntAct: EBI-10183935; Score: 0.72
DE  Interaction: Q8NHQ1; IntAct: EBI-10183945; Score: 0.56
DE  Interaction: Q9BRK4; IntAct: EBI-10183965; Score: 0.72
DE  Interaction: V9HWG0; IntAct: EBI-10183975; Score: 0.56
DE  Interaction: P52732; IntAct: EBI-11007621; Score: 0.35
DE  Interaction: P83917; IntAct: EBI-11012671; Score: 0.35
DE  Interaction: P24588; IntAct: EBI-11022813; Score: 0.35
DE  Interaction: Q9UER7; IntAct: EBI-11088574; Score: 0.35
DE  Interaction: P26447; IntAct: EBI-11158347; Score: 0.35
DE  Interaction: Q92997; IntAct: EBI-24357699; Score: 0.56
DE  Interaction: Q6TGC4; IntAct: EBI-24512010; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-24401717; Score: 0.56
DE  Interaction: Q9UGI0; IntAct: EBI-24411282; Score: 0.56
DE  Interaction: Q8WV44; IntAct: EBI-24426170; Score: 0.56
DE  Interaction: Q96I34; IntAct: EBI-24430731; Score: 0.56
DE  Interaction: Q8N680; IntAct: EBI-24438043; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-24471464; Score: 0.56
DE  Interaction: Q8WW24; IntAct: EBI-24557231; Score: 0.56
DE  Interaction: Q8TAU3; IntAct: EBI-24563312; Score: 0.56
DE  Interaction: Q7Z4V0; IntAct: EBI-24811250; Score: 0.56
DE  Interaction: Q13371; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q9UPU5; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q9NPA3; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q9H582; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q9H0I2; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q9BTE3; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q96KQ7; IntAct: EBI-15916314; Score: 0.46
DE  Interaction: Q93008; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q70CQ2; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q6VMQ6; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q5TDH0; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q15047; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q15018; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: O60732; IntAct: EBI-21777725; Score: 0.35
DE  Interaction: Q96EB6; IntAct: EBI-15671006; Score: 0.54
DE  Interaction: Q9H9B1; IntAct: EBI-15916287; Score: 0.46
DE  Interaction: Q14191; IntAct: EBI-16155310; Score: 0.35
DE  Interaction: Q969R5; IntAct: EBI-25485605; Score: 0.35
DE  Interaction: Q9BYN8; IntAct: EBI-25485605; Score: 0.35
DE  Interaction: Q8N136; IntAct: EBI-25485605; Score: 0.35
DE  Interaction: P50454; IntAct: EBI-25836502; Score: 0.56
DE  Interaction: Q86V38; IntAct: EBI-25846409; Score: 0.56
DE  Interaction: Q92876; IntAct: EBI-25887383; Score: 0.56
DE  Interaction: P54725; IntAct: EBI-25889399; Score: 0.56
DE  Interaction: P37173; IntAct: EBI-25892730; Score: 0.56
GO  GO:0005677;
GO  GO:0000775;
GO  GO:0000794;
GO  GO:0061773;
GO  GO:0000792;
GO  GO:0005652;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0033553;
GO  GO:0003682;
GO  GO:0042054;
GO  GO:0046974;
GO  GO:0018024;
GO  GO:0047485;
GO  GO:0008757;
GO  GO:0000976;
GO  GO:0008270;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0006974;
GO  GO:0042149;
GO  GO:0071456;
GO  GO:0006325;
GO  GO:0097009;
GO  GO:0036123;
GO  GO:0036124;
GO  GO:0034968;
GO  GO:0045786;
GO  GO:0042754;
GO  GO:0045892;
GO  GO:0000122;
GO  GO:0031065;
GO  GO:0031062;
GO  GO:0000183;
GO  GO:0046015;
GO  GO:0048511;
GO  GO:0006364;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNL
SQ  KCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAF
SQ  VYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKG
SQ  IRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISH
SQ  FVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIEC
SQ  KCGTESCRKYLF
//
ID  O54864;
PN  Histone-lysine N-methyltransferase SUV39H1;
GN  Suv39h1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin.
DR  UNIPROT: O54864;
DR  UNIPROT: Q3TEW2;
DR  UNIPROT: Q3UT51;
DR  UNIPROT: Q8C2L3;
DR  UNIPROT: Q9JLC7;
DR  UNIPROT: Q9JLP8;
DR  Pfam: PF00385;
DR  Pfam: PF05033;
DR  Pfam: PF00856;
DR  PROSITE: PS00598;
DR  PROSITE: PS50013;
DR  PROSITE: PS50868;
DR  PROSITE: PS50867;
DR  PROSITE: PS51579;
DR  PROSITE: PS50280;
DE  Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin- like repressive state through H3 'Lys-9' trimethylation. {ECO:0000269|PubMed:11701123, ECO:0000269|PubMed:12867029, ECO:0000269|PubMed:14690609, ECO:0000269|PubMed:14690610, ECO:0000269|PubMed:14702045, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:24413057}.
DE  Reference Proteome: Yes;
DE  Interaction: O88895; IntAct: EBI-302283; Score: 0.35
DE  Interaction: P70288; IntAct: EBI-302283; Score: 0.46
DE  Interaction: O09106; IntAct: EBI-302283; Score: 0.46
DE  Interaction: Q60973; IntAct: EBI-302308; Score: 0.35
DE  Interaction: Q60972; IntAct: EBI-302308; Score: 0.35
DE  Interaction: P68432; IntAct: EBI-354640; Score: 0.44
DE  Interaction: P68431; IntAct: EBI-354701; Score: 0.44
DE  Interaction: O70237; IntAct: EBI-8517394; Score: 0.40
DE  Interaction: P10085; IntAct: EBI-8578067; Score: 0.58
DE  Interaction: Q15047; IntAct: EBI-15916263; Score: 0.35
DE  Interaction: P23198; IntAct: EBI-16089648; Score: 0.35
DE  Interaction: O54943; IntAct: EBI-16089648; Score: 0.35
GO  GO:0005677;
GO  GO:0000775;
GO  GO:0061773;
GO  GO:0000792;
GO  GO:0005652;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0033553;
GO  GO:0042054;
GO  GO:0046974;
GO  GO:0018024;
GO  GO:0008168;
GO  GO:0008276;
GO  GO:0047485;
GO  GO:0000977;
GO  GO:0008757;
GO  GO:0000976;
GO  GO:0008270;
GO  GO:0001835;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0006974;
GO  GO:0042149;
GO  GO:0071456;
GO  GO:0051276;
GO  GO:0008340;
GO  GO:0097009;
GO  GO:0031507;
GO  GO:0036123;
GO  GO:0051567;
GO  GO:0036124;
GO  GO:0034968;
GO  GO:0045786;
GO  GO:0042754;
GO  GO:0045892;
GO  GO:0000122;
GO  GO:0031065;
GO  GO:1900114;
GO  GO:0031062;
GO  GO:0000183;
GO  GO:0030500;
GO  GO:2000772;
GO  GO:0006282;
GO  GO:0040014;
GO  GO:0046015;
GO  GO:0048511;
GO  GO:0006364;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNL
SQ  KCIRVLKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSF
SQ  VYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKG
SQ  IRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISH
SQ  FVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIEC
SQ  KCGTTACRKYLF
//
ID  Q5RB81;
PN  Histone-lysine N-methyltransferase SUV39H1;
GN  SUV39H1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Comments: Nucleus {ECO:0000250}. Nucleus lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Associates with centromeric constitutive heterochromatin. {ECO:0000250}.
DR  UNIPROT: Q5RB81;
DR  UNIPROT: Q5RAM0;
DR  Pfam: PF00385;
DR  Pfam: PF05033;
DR  Pfam: PF00856;
DR  PROSITE: PS00598;
DR  PROSITE: PS50013;
DR  PROSITE: PS50868;
DR  PROSITE: PS50867;
DR  PROSITE: PS51579;
DR  PROSITE: PS50280;
DE  Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0000775;
GO  GO:0000792;
GO  GO:0005652;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0046974;
GO  GO:0000976;
GO  GO:0008270;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0006325;
GO  GO:0036123;
GO  GO:0036124;
GO  GO:0042754;
GO  GO:0045892;
GO  GO:0048511;
GO  GO:0006364;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNL
SQ  KCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAF
SQ  VYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKG
SQ  IRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISH
SQ  FVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIEC
SQ  KCGTESCRKYLF
//
ID  O02101;
PN  SWI/SNF chromatin-remodeling accessory subunit 2;
GN  swsn;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:26739451}. Chromosome {ECO:0000269|PubMed:26739451}. Nucleus envelope {ECO:0000269|PubMed:26739451}. Note=Localizes to mitotic chromosomes in the early embryo. {ECO:0000269|PubMed:26739451}.
DR  UNIPROT: O02101;
DR  Pfam: PF02201;
DE  Function: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (By similarity). Probably regulates vulva development through the let-60/Ras pathway (PubMed:26739451). Involved in nuclear reassembly after mitosis and recruitment of nuclear envelope protein, mel-28, to the nuclear periphery in the early embryo and in the adult germline (PubMed:26739451). Involved in gonadogenesis (PubMed:26739451, PubMed:24402584). {ECO:0000250|UniProtKB:Q96GM5, ECO:0000269|PubMed:24402584, ECO:0000269|PubMed:26739451}.
DE  Reference Proteome: Yes;
DE  Interaction: G5EFL0; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: H8ESF3; IntAct: EBI-6734418; Score: 0.00
DE  Interaction: C1P633; IntAct: EBI-11469543; Score: 0.37
DE  Interaction: P34255; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q09441; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: X5M8S5; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: P46499; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: V6CLP5; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: V6CLP9; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9NAA7; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5ECX4; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: S6F5A3; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: L8E833; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EFE3; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q95Y48; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EG14; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: I2HA96; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: H9G2Y6; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9BL39; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O45148; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9TXL4; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q19126; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: H2L296; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EEH6; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: A4F336; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9N4L9; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q10021; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q09579; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9N4N4; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O61834; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O61853; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q09302; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q22935; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q86B36; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9N384; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O44674; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O17406; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EGT7; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: H2KYR1; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q23059; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q86NI2; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O44454; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9GZH5; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: D3YT47; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: C6KRN1; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9XW62; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: A6ZJ59; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O02224; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EBK8; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q1ZXT0; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EF26; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q8STE5; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q21253; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q19749; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O44451; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O17953; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O17732; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EFK8; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5ED29; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q20624; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9XVR8; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q69Z12; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q18508; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q21088; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q21201; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9U332; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: P90747; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O17679; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O01757; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q10129; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9U1W1; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EF87; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q21018; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EBX5; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O44952; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O62415; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q22832; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O45784; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5ECZ0; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q22078; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q21831; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O62270; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q21021; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O62228; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q9XV68; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O45378; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EF53; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: G5EBX3; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: O45279; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q17817; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q17763; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q17629; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q10941; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q09449; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q22799; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: P52899; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q10002; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: Q09665; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: P34328; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: P34339; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: P18334; IntAct: EBI-25615276; Score: 0.35
DE  Interaction: P16356; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q6BER6; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: P45966; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9N337; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q95Q17; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q93442; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9NEL2; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: P91019; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: G5EGU9; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: P34475; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q09422; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q10573; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q21193; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: O45244; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: P90916; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9N5A1; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: O02042; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q965S8; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q09242; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: P30632; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9N350; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q17795; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q8WQ97; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9GZI6; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q20563; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q21172; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: P91453; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: A9D0C6; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q8MXR6; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q23026; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: O01505; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: A6ZJ71; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: D5SGZ9; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q5H9M9; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: H2KZN0; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9N5S7; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q93315; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q20937; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: P10771; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: O61793; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q23523; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q23679; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9N4F2; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q966M5; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q10661; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: P90866; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9BKQ7; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q20010; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q8I4M5; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9NA98; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q17740; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9XZI6; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q17963; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9BI74; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q03570; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q94046; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q2A949; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: G5EEY5; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: H9G301; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9N363; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: O61707; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: A5JYT2; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9XUS2; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q22944; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9U1W2; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: G5EGI1; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: P34428; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q20497; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9NAL4; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9XW73; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q2XN10; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q9N4G4; IntAct: EBI-25616084; Score: 0.35
DE  Interaction: Q09477; IntAct: EBI-25616084; Score: 0.35
GO  GO:0000793;
GO  GO:0005635;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016514;
GO  GO:0061629;
GO  GO:0003712;
GO  GO:0006338;
GO  GO:2000781;
GO  GO:2000045;
GO  GO:0030071;
GO  GO:2000819;
GO  GO:0006357;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MHSQQRPNPQMNRHPYGTPGSAPQMRRPGGFAGQPPQMHGPRMVAPPAAPLPKKKKYADKCIHPKIRELEPDAENYMALL
SQ  ASEQKLDSTLSRKKLDIQEALKRPSKVKKRLRIYISHTFIEEKQPEKDTDEASLPMWELRVEGRLLDEQPPAPAIPGQRP
SQ  VPKRKFSSFFKSLVIELDKEMYGPDQHLVEWHRTPQTNETDGFQVKRAGDRPVKCRILLLLDNHPAKFKLHPRLAKVLGI
SQ  ATETRPKIIEALWQYIKTHGLQDPQERDIINCDTFLSQCFGVNRMRFMEVPNKLHQLLQQTDPLEFNHIIQRPKEGQEQV
SQ  STCYDIDVEMEDPVKQFMHTFVHSPGLANDIQTLDQKCYDIIEQINELKTRRDFYARFYTEPAEFIKSWVMSQNSDLKTM
SQ  NELSGDLEAERFAESYVRPETEEGVQRYMFQKVNQKRHELEQSLGVRSN
//
ID  Q04175;
PN  Importin beta SMX1;
GN  SXM1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm. Nucleus, nuclear pore complex.
DR  UNIPROT: Q04175;
DR  UNIPROT: D6VT29;
DR  Pfam: PF08506;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Nuclear transport factor (karyopherin) involved in protein transport between the cytoplasm and nucleoplasm. Required for the nuclear import of ribosomal proteins (RPL11, RPL16, RPL25, RPL31A), the poly(A)-binding protein PAB1, the HO endonuclease or the tRNA and snRNA chaperone LHP1. Indirectly involved in nuclear mRNA export through its PAB1 nuclear import activity. {ECO:0000269|PubMed:12684370, ECO:0000269|PubMed:15004228, ECO:0000269|PubMed:15769879, ECO:0000269|PubMed:16507575, ECO:0000269|PubMed:9238021, ECO:0000269|PubMed:9412461, ECO:0000269|PubMed:9817748}.
DE  Reference Proteome: Yes;
DE  Interaction: P14907; IntAct: EBI-1173446; Score: 0.40
DE  Interaction: P20676; IntAct: EBI-1173466; Score: 0.40
DE  Interaction: P25491; IntAct: EBI-3664452; Score: 0.35
DE  Interaction: P40477; IntAct: EBI-1173457; Score: 0.40
DE  Interaction: Q03900; IntAct: EBI-391536; Score: 0.37
DE  Interaction: Q08229; IntAct: EBI-391539; Score: 0.37
DE  Interaction: P16140; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P36144; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-792680; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P46654; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P26785; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P0C0W9; IntAct: EBI-792680; Score: 0.56
DE  Interaction: P41940; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P33399; IntAct: EBI-792680; Score: 0.70
DE  Interaction: P33892; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P00549; IntAct: EBI-792680; Score: 0.35
DE  Interaction: P39715; IntAct: EBI-807214; Score: 0.53
DE  Interaction: P32357; IntAct: EBI-814816; Score: 0.27
DE  Interaction: P38697; IntAct: EBI-818076; Score: 0.27
DE  Interaction: P07702; IntAct: EBI-818099; Score: 0.27
DE  Interaction: P36000; IntAct: EBI-818671; Score: 0.27
DE  Interaction: Q03862; IntAct: EBI-820134; Score: 0.27
DE  Interaction: P53230; IntAct: EBI-854989; Score: 0.00
DE  Interaction: Q3E757; IntAct: EBI-1173432; Score: 0.40
DE  Interaction: P04456; IntAct: EBI-1173432; Score: 0.40
DE  Interaction: P87262; IntAct: EBI-1173432; Score: 0.40
DE  Interaction: P40525; IntAct: EBI-1173432; Score: 0.40
DE  Interaction: P22696; IntAct: EBI-2883245; Score: 0.00
DE  Interaction: Q03833; IntAct: EBI-2883650; Score: 0.00
DE  Interaction: P53688; IntAct: EBI-2884674; Score: 0.00
DE  Interaction: P40564; IntAct: EBI-3657084; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3678289; Score: 0.35
DE  Interaction: P39987; IntAct: EBI-3703411; Score: 0.35
DE  Interaction: P52919; IntAct: EBI-7043004; Score: 0.35
DE  Interaction: P53131; IntAct: EBI-10903607; Score: 0.35
DE  Interaction: Q12531; IntAct: EBI-16292501; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0031267;
GO  GO:0006406;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVQEQAILSCIEQTMVADAKIIKEAEQQLFEFQKQPGFTSFLLNIVSDDNFALNVRLSSAIYLKNKIHRSWDTKREDGIK
SQ  ADEKLSIKERLIETLVKNCENNHIRPILTETINGILVGQEDWDLAPIIKNLLSSGDASYIYPGLLLLFQLCKAHRWDMVG
SQ  SRDYIDSVIEELFPIVEGIASNIGSQTDYRSNEILYLILKSFKYACLNNLPQYFSQPERIMSWVQLHLYLCSKPLPVEVM
SQ  ELDPADRSLDKRVKVNKWGFGNLNRFLQRYNKITKAITKEFIDYIFNTIVPIILREFFKDIEAWGNNSLWLSDSSLYFLI
SQ  SFLEKCVTIDQLYPLIEPHLQIIFENVIFPCLCANEQSIELLEDDQEEYTRRYFDINREGSTPDAASADFIFLIGSKRPE
SQ  KLNNILPFINDIFTRFDANSSDINMAFKEEGALRTLSNLFSFIDEPSVLENIFGHFIVPLLSQDKYMFLVARSLETIALY
SQ  SEEFKDMNILSQLFELTYTNFLNSNVLPVQIEAADAIKCLIVSNPQIHPAVSAHVPGMMEKLLKLSKIFEIDILSEVMEA
SQ  LVERFSDELSPFAKDLASNLVEQFLRIAQALVENPSETYSASDQEQEIQASGLLQTMTTMVMSMNKVPLIESLAPVVKFV
SQ  VLHAQISFITEAVDLLDALTISSHLLYNQIAPPIWELLHDILDSFQTYAMDYFEAYSIFFETIVMTGFPQDQTYVQPLLE
SQ  ILSAKLESEVDYDIEHVMQILMYFALSMRDIPLFSKAIKVSTNDELGLDSKCIVKLGLANLFAKPIETLQIMENEGFTIN
SQ  FFTNWFNEKFYSVFAIKLQVLVILTLLKMPEVPNSVSPLLNNLTNKLVELTLSLPKAIRNRDAVTEGKSLEGDLTPEEEE
SQ  EYFIECDDDMKETVLDQINVFQEVHTFFKNLQNEDAGKYEKIINYLDESKRDSLQVILEFVSQH
//
ID  Q96A49;
PN  Synapse-associated protein 1;
GN  SYAP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9D5V6}. Golgi apparatus {ECO:0000250|UniProtKB:Q9D5V6}. Perikaryon {ECO:0000250|UniProtKB:Q9D5V6}. Cell projection, axon {ECO:0000250|UniProtKB:Q9D5V6}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9D5V6}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9D5V6}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q9D5V6}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9D5V6}. Membrane {ECO:0000269|PubMed:23300339}. Note=Localizes to cholinergic neuromuscular junctions and in actin-rich growth cone regions (By similarity). Membrane-associated in a epidermal growth factor (EGF)-dependent manner (PubMed:23300339). {ECO:0000250|UniProtKB:Q9D5V6, ECO:0000269|PubMed:23300339}.
DR  UNIPROT: Q96A49;
DR  UNIPROT: Q68CP1;
DR  UNIPROT: Q96C60;
DR  UNIPROT: Q96JQ6;
DR  UNIPROT: Q96T20;
DR  PDB: 1X3A;
DR  Pfam: PF03909;
DR  PROSITE: PS50858;
DE  Function: Plays a role in adipocyte differentiation by promoting mTORC2-mediated phosphorylation of AKT1 at 'Ser-473' after growth factor stimulation (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q6ZMQ8; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q16659; IntAct: EBI-12502733; Score: 0.35
DE  Interaction: Q96FW1; IntAct: EBI-10770198; Score: 0.35
DE  Interaction: Q9CS74; IntAct: EBI-11150651; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-11398030; Score: 0.27
DE  Interaction: Q9NUX5; IntAct: EBI-11304963; Score: 0.51
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: P10827; IntAct: EBI-24380444; Score: 0.56
DE  Interaction: O14798; IntAct: EBI-24707651; Score: 0.56
DE  Interaction: P30301; IntAct: EBI-24712218; Score: 0.56
DE  Interaction: O95159; IntAct: EBI-24729358; Score: 0.56
DE  Interaction: Q15848; IntAct: EBI-24739002; Score: 0.56
DE  Interaction: Q8WVK2; IntAct: EBI-21500567; Score: 0.35
DE  Interaction: P02675; IntAct: EBI-21646531; Score: 0.35
DE  Interaction: P05120; IntAct: EBI-21713063; Score: 0.35
DE  Interaction: P59536; IntAct: EBI-21736177; Score: 0.35
DE  Interaction: Q96K76; IntAct: EBI-21756437; Score: 0.35
DE  Interaction: Q9NY26; IntAct: EBI-21772441; Score: 0.35
DE  Interaction: P04798; IntAct: EBI-21774067; Score: 0.35
DE  Interaction: Q13526; IntAct: EBI-21884604; Score: 0.40
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: P15311; IntAct: EBI-16791848; Score: 0.27
DE  Interaction: O14880; IntAct: EBI-16796348; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797429; Score: 0.27
DE  Interaction: O75880; IntAct: EBI-16799233; Score: 0.27
DE  Interaction: Q9H9B4; IntAct: EBI-16799442; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: Q99608; IntAct: EBI-26955093; Score: 0.47
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: Q06124; IntAct: EBI-32723738; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0070062;
GO  GO:0031234;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0045211;
GO  GO:0042734;
GO  GO:0045202;
GO  GO:0030154;
GO  GO:0071364;
GO  GO:0032869;
GO  GO:1990314;
GO  GO:0036120;
GO  GO:0045600;
GO  GO:0071902;
GO  GO:0048172;
GO  GO:0038203;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFRGLSSWLGLQQPVAGGGQPNGDAPPEQPSETVAESAEEELQQAGDQELLHQAKDFGNYLFNFASAATKKITESVAETA
SQ  QTIKKSVEEGKIDGIIDKTIIGDFQKEQKKFVEEQHTKKSEAAVPPWVDTNDEETIQQQILALSADKRNFLRDPPAGVQF
SQ  NFDFDQMYPVALVMLQEDELLSKMRFALVPKLVKEEVFWRNYFYRVSLIKQSAQLTALAAQQQAAGKEEKSNGREQDLPL
SQ  AEAVRPKTPPVVIKSQLKTQEDEEEISTSPGVSEFVSDAFDACNLNQEDLRKEMEQLVLDKKQEETAVLEEDSADWEKEL
SQ  QQELQEYEVVTESEKRDENWDKEIEKMLQEEN
//
ID  Q9D5V6;
PN  Synapse-associated protein 1;
GN  Syap1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:27344443}. Golgi apparatus {ECO:0000269|PubMed:27344443}. Perikaryon {ECO:0000269|PubMed:27344443}. Cell projection, axon {ECO:0000269|PubMed:27344443}. Cell projection, dendrite {ECO:0000269|PubMed:27344443}. Cell projection, growth cone {ECO:0000269|PubMed:27344443}. Presynaptic cell membrane {ECO:0000269|PubMed:27344443}. Postsynaptic cell membrane {ECO:0000269|PubMed:27344443}. Membrane {ECO:0000250|UniProtKB:Q96A49}. Note=Localizes to cholinergic neuromuscular junctions and in actin-rich growth cone regions (PubMed:27344443). Membrane-associated in a epidermal growth factor (EGF)-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q96A49, ECO:0000269|PubMed:27344443}.
DR  UNIPROT: Q9D5V6;
DR  UNIPROT: Q3UI67;
DR  UNIPROT: Q9D870;
DR  Pfam: PF03909;
DR  PROSITE: PS50858;
DE  Function: Plays a role in adipocyte differentiation by promoting mTORC2-mediated phosphorylation of AKT1 at 'Ser-473' after growth factor stimulation (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
DE  Reference Proteome: Yes;
DE  Interaction: P97493; IntAct: EBI-26499997; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0031234;
GO  GO:0005794;
GO  GO:0030426;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0045211;
GO  GO:0042734;
GO  GO:0045202;
GO  GO:0030154;
GO  GO:0071364;
GO  GO:0032869;
GO  GO:1990314;
GO  GO:0036120;
GO  GO:0045600;
GO  GO:0071902;
GO  GO:0048172;
GO  GO:0038203;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFGGLSSWLGLKPPEGAAAEGEEPPSRDGDKLSAGAAPSEESPERPVEPTEEQQQQPPTEDPQFLHQAKGLGNYLYNFAS
SQ  AATKKITESVTETAQTIKKSVEEGKIDDILDKTILGDFQKEQKKFVEEQNTKKSEAAVPPWVESHDEETIQQQILALSAD
SQ  KRNFLRDPPAGVQFNFDFDQMYPVALVMLQEDELLSKMRFALVPKLVKEEVFWRNYFYRISLIKQSAQLTALAAQQQASG
SQ  KEEKSSNRDDNLPLTEAVRPKTPPVVIKSQLKSQEDEEEISTSPGVSEFVSDAFDTCSLNQEDLRKEMEQLVLDKKQEEA
SQ  TALEEDSTDWEKELQQELQEYEVVAESEKRDENWDKEIEKMLQES
//
ID  Q3T0C9;
PN  Synaptojanin-2-binding protein;
GN  SYNJ2BP;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9D6K5, ECO:0000250|UniProtKB:Q9WVJ4}; Single- pass type IV membrane protein {ECO:0000250|UniProtKB:Q9D6K5, ECO:0000250|UniProtKB:Q9WVJ4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9D6K5, ECO:0000250|UniProtKB:Q9WVJ4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9D6K5, ECO:0000250|UniProtKB:Q9WVJ4}.
DR  UNIPROT: Q3T0C9;
DR  Pfam: PF00595;
DR  PROSITE: PS50106;
DE  Function: Regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. {ECO:0000250|UniProtKB:Q9D6K5}.
DE  Reference Proteome: Yes;
GO  GO:0016323;
GO  GO:0030054;
GO  GO:0016021;
GO  GO:0005741;
GO  GO:0031594;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0098839;
GO  GO:0098609;
GO  GO:0007268;
GO  GO:0006897;
GO  GO:0045197;
GO  GO:0016525;
GO  GO:0010596;
GO  GO:0001937;
GO  GO:0070373;
GO  GO:1903671;
GO  GO:0043113;
GO  GO:0097120;
GO  GO:0008593;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNGRVDYLVTEEEINLTRGPSGLGFNIVGGTDQQYVSNDSGIFVSRIKENGAAALDGRLQEGDKILSVNGQDLKNLLHQD
SQ  AVDLFRNAGYAVSLRVQHRLQVQNGPIGPQGEGEPSGIPIAMVLVPVFALTMVAAWAFMRYRQRL
//
ID  Q9D6K5;
PN  Synaptojanin-2-binding protein;
GN  Synj2bp;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9WVJ4}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9WVJ4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9WVJ4}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11882656}.
DR  UNIPROT: Q9D6K5;
DR  UNIPROT: Q2TTN6;
DR  UNIPROT: Q6YNE6;
DR  UNIPROT: Q78HT9;
DR  UNIPROT: Q8K4F3;
DR  UNIPROT: Q9D8G4;
DR  Pfam: PF00595;
DR  PROSITE: PS50106;
DE  Function: Isoform 1 regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Isoform 2 and isoform 3 show a stimulatory affect on activin-induced signal transduction and enhance activin type 2 expression at the cell surface. {ECO:0000269|PubMed:11882656, ECO:0000269|PubMed:16648306}.
DE  Reference Proteome: Yes;
DE  Interaction: A2ARV4; IntAct: EBI-300919; Score: 0.51
DE  Interaction: Q91ZX7; IntAct: EBI-301424; Score: 0.40
DE  Interaction: Q61483; IntAct: EBI-11699888; Score: 0.37
DE  Interaction: Q9JI71; IntAct: EBI-11699894; Score: 0.44
GO  GO:0016323;
GO  GO:0030054;
GO  GO:0009986;
GO  GO:0031307;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0031594;
GO  GO:0043005;
GO  GO:0048471;
GO  GO:0098839;
GO  GO:0008022;
GO  GO:0070699;
GO  GO:0098609;
GO  GO:0007268;
GO  GO:0007028;
GO  GO:0006897;
GO  GO:0045197;
GO  GO:0048312;
GO  GO:0032926;
GO  GO:0016525;
GO  GO:0010596;
GO  GO:0001937;
GO  GO:0070373;
GO  GO:1903671;
GO  GO:0032927;
GO  GO:2000010;
GO  GO:0002092;
GO  GO:0006605;
GO  GO:0043113;
GO  GO:0097120;
GO  GO:0030100;
GO  GO:0008593;
GO  GO:0007266;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNGRVDYLVTEEEINLTRGPSGLGFNIVGGTDQQYVSNDSGIYVSRIKEDGAAAQDGRLQEGDKILSVNGQDLKNLLHQD
SQ  AVDLFRNAGCAVSLRVQHRLPVQNGPIVHRGEGEPSGVPVAMVLLPVFALTMVAVWAFVRYRKQL
//
ID  Q4VY51;
PN  Probable ion channel SYM8;
GN  SYM8;
OS  3888;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q4VY51;
DR  UNIPROT: A9Q1K1;
DR  UNIPROT: A9Q1K2;
DR  UNIPROT: A9Q1K4;
DR  UNIPROT: A9Q1K5;
DR  Pfam: PF06241;
DE  Function: Required for both rhizobial and mycorrhizal symbiosis. Involved in Nod-factor-induced calcium spiking. May induce a change in membrane polarization that activates the opening of a calcium channel required for calcium spiking. Might be calcium gated. {ECO:0000269|PubMed:11078515, ECO:0000269|PubMed:17918620}.
DE  Reference Proteome: No;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0042802;
GO  GO:0034220;
GO  GO:0009877;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKSNEEPNSNLNTNKPPLKRTKTLAQQPSLNLRVSIAAADNGIGNSSSSSTKTDFEQQQRNYPSFLGIGSTSRKRRPPP
SQ  PPKPSNITPNVKPPASDFQTKPHSEPKTSPSSSSPPSLPIAITKQQQQQHSISSPIFYLFVITCVIFVPYSAFLQYKLAK
SQ  LKDMKLQLCCQIDFCSGNGKTSLQKDVVDDGSFSYYILNADSRTISLYIVLFTLVLPFILYKYIDYLPQMINFSRRTNSN
SQ  KEDVPLKKRVAYMVDVFFSIYPYAKLLALLFATLFLIAFGGLALYAVTGGSMAEALWHSWTYVADAGNHAETEGMGQRIV
SQ  SVSISAGGMLIFAMMLGLVSDAISEKVDSLRKGKSEVIERNHVLILGWSDKLGSLLKQLAIANKSVGGGVIVVLAEKEKE
SQ  EMEMDIAKLEFDFMGTSVICRSGSPLILADLKKVSVSKARAIIVLASDENADQSDARALRVVLSLTGVKEALRGHVVVEM
SQ  SDLDNEPLVKLVGGELIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIKRWPELDGLLFKDILISFPDAIPC
SQ  GVKVSADGGKIVINPDDNYVLRDGDEVLVIAEDDDTYAPGPLPEVRKGYFPRIRDPPKYPEKILFCGWRRDIDDMIMVLE
SQ  AFLAPGSELWMFNEVPEKQRERKLAAGELDVFGLENIKLVHREGNAVIRRHLESLPLETFDSILILADESVEDSVAHSDS
SQ  RSLATLLLIRDIQSRRLPYRDTKSTSLRLSGFSHNSWIREMQQASDKSIIISEILDSRTRNLVSVSRISDYVLSNELVSM
SQ  ALAMVAEDKQINRVLEELFAEEGNEMCIKPAEFYLFDQEELCFYDIMIRGRTRKEIVIGYRLASQERALINPSEKSMTRK
SQ  WSLDDVFVVIASGE
//
ID  Q9H7C4;
PN  Syncoilin;
GN  SYNC;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9EPM5}. Note=In skeletal muscle, colocalizes with DES and DTNA, and is localized at the myotendinous and neuromuscular junctions, sarcolemma and Z-lines. In myotubes, detected in a punctate cytoplasmic pattern (By similarity). {ECO:0000250|UniProtKB:Q9EPM5}.
DR  UNIPROT: Q9H7C4;
DR  UNIPROT: B4DNK8;
DR  UNIPROT: B4DY58;
DR  UNIPROT: C9IY41;
DR  Pfam: PF00038;
DR  PROSITE: PS51842;
DR  OMIM: 611750;
DR  DisGeNET: 81493;
DE  Function: Atypical type III intermediate filament (IF) protein that may play a supportive role in the efficient coupling of mechanical stress between the myofibril and fiber exterior. May facilitate lateral force transmission during skeletal muscle contraction. Does not form homofilaments nor heterofilaments with other IF proteins. {ECO:0000250|UniProtKB:Q9EPM5}.
DE  Reference Proteome: Yes;
DE  Interaction: Q13137; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q13393; IntAct: EBI-25882515; Score: 0.56
DE  Interaction: Q9BV73; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: P08670; IntAct: EBI-25896426; Score: 0.56
DE  Interaction: Q8TEQ6; IntAct: EBI-11086338; Score: 0.35
DE  Interaction: P20152; IntAct: EBI-11150248; Score: 0.35
DE  Interaction: O15061; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q9Y6K9; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q9Y2X7; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q9P2K6; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q9NS87; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q9H2U2; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q9H2C0; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q9BZF9; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q96T51; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q96JN2; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q96EK4; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q96A19; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q8TBA6; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q8IWJ2; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q6P4E1; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q5JTD0; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q53EZ4; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q16352; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q15750; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q15276; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q15052; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q15025; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q14BN4; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q14161; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q14155; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: Q08378; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: P48681; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: P41219; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: P23508; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: P17661; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: P14136; IntAct: EBI-25858572; Score: 0.56
DE  Interaction: P07197; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: P07196; IntAct: EBI-25877887; Score: 0.56
DE  Interaction: O43318; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: O14777; IntAct: EBI-21702482; Score: 0.35
DE  Interaction: P61604; IntAct: EBI-20900543; Score: 0.40
DE  Interaction: Q8TDR0; IntAct: EBI-21389780; Score: 0.00
DE  Interaction: P68133; IntAct: EBI-25830425; Score: 0.56
DE  Interaction: P13637; IntAct: EBI-25832791; Score: 0.56
DE  Interaction: P16284; IntAct: EBI-25881579; Score: 0.56
DE  Interaction: P20339; IntAct: EBI-25889147; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25899416; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25916238; Score: 0.56
GO  GO:0005829;
GO  GO:0005882;
GO  GO:0031594;
GO  GO:0048471;
GO  GO:0042383;
GO  GO:0030018;
GO  GO:0045103;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASPEPRRGGDGAAQAARKTRVEANSPLPKNSGSLNEAEALNPEVTLSSEGSLNLEDILYLEDTGDLDETLYVQETEKAE
SQ  EALYIEEAMQPDEALHVEEPGNPEETVCVEETTEPDRIQFVEGPVEPGKPTSPEHVVYEGETVTRAEKSNPEESLRAEQS
SQ  PSMEENLSIEDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQDILAAYKLHAQAELERDGLREEIR
SQ  LVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQE
SQ  SRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVR
SQ  QKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLLPKSLEQADAPTSQAGGMETQSQG
SQ  AV
//
ID  Q9EPM5;
PN  Syncoilin;
GN  Sync;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11053421, ECO:0000269|PubMed:11694502, ECO:0000269|PubMed:17629480}. Note=In skeletal muscle, colocalizes with DES and DTNA, and is localized at the myotendinous and neuromuscular junctions, sarcolemma and Z-lines. In myotubes, detected in a punctate cytoplasmic pattern. {ECO:0000269|PubMed:11053421, ECO:0000269|PubMed:11694502, ECO:0000269|PubMed:17629480}.
DR  UNIPROT: Q9EPM5;
DR  UNIPROT: Q3KP79;
DR  UNIPROT: Q3TKN1;
DR  UNIPROT: Q3TUH9;
DR  UNIPROT: Q8C4J4;
DR  UNIPROT: Q9CT88;
DR  Pfam: PF00038;
DR  PROSITE: PS51842;
DE  Function: Atypical type III intermediate filament (IF) protein that may play a supportive role in the efficient coupling of mechanical stress between the myofibril and fiber exterior. May facilitate lateral force transmission during skeletal muscle contraction. Does not form homofilaments nor heterofilaments with other IF proteins. {ECO:0000269|PubMed:11694502, ECO:0000269|PubMed:18367591}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y4J8; IntAct: EBI-7424047; Score: 0.54
DE  Interaction: P31001; IntAct: EBI-8031285; Score: 0.46
DE  Interaction: P15331; IntAct: EBI-27023883; Score: 0.46
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005882;
GO  GO:0031594;
GO  GO:0048471;
GO  GO:0042383;
GO  GO:0030018;
GO  GO:0045103;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASPEPLRGGDGARASREPHTEASFPLQESESPKEAKTFNPEATLSLEGTVNLEDILYLGASGDFEESFYEEEYEKPALT
SQ  LFIDESRQPDEALGLEEPVRPEEMLSVEESVTPDEVQISEQPVEPAKSPTACEGEMVATEGSLPAQPIPNTEEDPLSVED
SQ  LERLEARFQQCVQAVSQLEEERDQLIHELVLLREPALQEVQQVHQDILAAYKLHAQAELERDGLREEIRTVKQKLFKVTK
SQ  ECVAYQYQLECRQQDVAQFADCREALTTRAAQLSEELTQLRDACQKQKEQLQQQLEAPPTQSDGHFLQESRRLSTQFENL
SQ  MAESRQGLEEEYEPQLLRLLERKEAGTKALQDTQAEIQEMREALRPLEAEARQLQLQNRNLEDQITLVRQKRDEEVQQYR
SQ  EQLEEMEERQRQLRSGVQVQQQKNKEMERLRMSLAEELSTYKAMLPKSLEQADAPTSQAGGVEAQSPGTV
//
ID  Q8NF91;
PN  Nesprin-1;
GN  SYNE1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus. Nucleus envelope. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. In skeletal and smooth muscles, a significant amount is found in the sarcomeres. In myoblasts, relocalized from the nuclear envelope to the nucleus and cytoplasm during cell differentiation. [Isoform GSRP-56]: Golgi apparatus {ECO:0000269|PubMed:16875688}.
DR  UNIPROT: Q8NF91;
DR  UNIPROT: B3W695;
DR  UNIPROT: E7EQI5;
DR  UNIPROT: H0Y4C0;
DR  UNIPROT: O94890;
DR  UNIPROT: Q3ZCV0;
DR  UNIPROT: Q5JV19;
DR  UNIPROT: Q5JV22;
DR  UNIPROT: Q8N9P7;
DR  UNIPROT: Q8TCP1;
DR  UNIPROT: Q8WWW6;
DR  UNIPROT: Q8WWW7;
DR  UNIPROT: Q8WXF6;
DR  UNIPROT: Q96N17;
DR  UNIPROT: Q9C0A7;
DR  UNIPROT: Q9H525;
DR  UNIPROT: Q9H526;
DR  UNIPROT: Q9NS36;
DR  UNIPROT: Q9NU50;
DR  UNIPROT: Q9UJ06;
DR  UNIPROT: Q9UJ07;
DR  UNIPROT: Q9ULF8;
DR  PDB: 4DXR;
DR  PDB: 6R15;
DR  PDB: 6XF2;
DR  Pfam: PF00307;
DR  Pfam: PF10541;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS51049;
DR  OMIM: 608441;
DR  OMIM: 610743;
DR  OMIM: 612998;
DR  OMIM: 618484;
DR  DisGeNET: 23345;
DE  Function: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nucleus- centrosome attachment and nuclear migration in neural progenitors implicating LINC complex association with SUN1/2 and probably association with cytoplasmic dynein-dynactin motor complexes; SYNE1 and SYNE2 may act redundantly. Required for centrosome migration to the apical cell surface during early ciliogenesis. May be involved in nuclear remodeling during sperm head formation in spermatogenesis; a probable SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:11792814, ECO:0000269|PubMed:18396275}.
DE  Disease: Spinocerebellar ataxia, autosomal recessive, 8 (SCAR8) [MIM:610743]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR8 is an autosomal recessive form. {ECO:0000269|PubMed:17159980}. Note=The disease is caused by variants affecting the gene represented in this entry. Emery-Dreifuss muscular dystrophy 4, autosomal dominant (EDMD4) [MIM:612998]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:17761684}. Note=The disease is caused by variants affecting the gene represented in this entry. Arthrogryposis multiplex congenita 3, myogenic type (AMC3) [MIM:618484]: A form of arthrogryposis multiplex congenita, a heterogeneous group of disorders characterized by multiple joint contractures resulting, in some cases, from reduced or absent fetal movements. AMC3 is an autosomal recessive form characterized by decreased fetal movements, muscular hypotonia, delayed motor development, loss of ambulation, variable skeletal defects, and persistent contractures of interphalangeal joints. {ECO:0000269|PubMed:19542096, ECO:0000269|PubMed:24319099, ECO:0000269|PubMed:27782104}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O08579; IntAct: EBI-10760599; Score: 0.27
DE  Interaction: O94901; IntAct: EBI-6163229; Score: 0.52
DE  Interaction: P02545; IntAct: EBI-10759435; Score: 0.40
DE  Interaction: P29991; IntAct: EBI-8829342; Score: 0.37
DE  Interaction: P50402; IntAct: EBI-10759458; Score: 0.52
DE  Interaction: Q9NRI5; IntAct: EBI-928988; Score: 0.63
DE  Interaction: Q9UL18; IntAct: EBI-7641969; Score: 0.35
DE  Interaction: Q9UKV8; IntAct: EBI-7642586; Score: 0.35
DE  Interaction: Q9CZA6; IntAct: EBI-2558595; Score: 0.40
DE  Interaction: A0A6L8PXW6; IntAct: EBI-2821558; Score: 0.00
DE  Interaction: A0A0H2W6E9; IntAct: EBI-2853434; Score: 0.00
DE  Interaction: P25054; IntAct: EBI-3437601; Score: 0.00
DE  Interaction: P60953; IntAct: EBI-3438787; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-3962281; Score: 0.35
DE  Interaction: P52179; IntAct: EBI-5661704; Score: 0.00
DE  Interaction: Q96S44; IntAct: EBI-5665321; Score: 0.00
DE  Interaction: P04413; IntAct: EBI-6155452; Score: 0.35
DE  Interaction: P09992; IntAct: EBI-6156280; Score: 0.35
DE  Interaction: Q9UH99; IntAct: EBI-6163101; Score: 0.59
DE  Interaction: Q9WMX2; IntAct: EBI-9081937; Score: 0.37
DE  Interaction: Q8NF91; IntAct: EBI-10758911; Score: 0.51
DE  Interaction: O14829; IntAct: EBI-14023711; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-14035332; Score: 0.35
DE  Interaction: Q9NWB7; IntAct: EBI-21499109; Score: 0.35
DE  Interaction: P30411; IntAct: EBI-20803507; Score: 0.37
DE  Interaction: P05204; IntAct: EBI-20914784; Score: 0.40
DE  Interaction: Q5T1B0; IntAct: EBI-20930480; Score: 0.40
DE  Interaction: P16401; IntAct: EBI-20931392; Score: 0.40
DE  Interaction: Q9BUQ8; IntAct: EBI-20937852; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9GZM8; IntAct: EBI-21375847; Score: 0.00
DE  Interaction: Q96MT8; IntAct: EBI-21375834; Score: 0.00
DE  Interaction: Q9NV70; IntAct: EBI-21375821; Score: 0.00
DE  Interaction: Q8TDR0; IntAct: EBI-21375794; Score: 0.00
DE  Interaction: O60239; IntAct: EBI-21375860; Score: 0.00
DE  Interaction: Q9UKE5; IntAct: EBI-21375779; Score: 0.00
DE  Interaction: Q99459; IntAct: EBI-21375873; Score: 0.00
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055586; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27111302; Score: 0.35
DE  Interaction: Q13283; IntAct: EBI-28955349; Score: 0.35
DE  Interaction: P21709; IntAct: EBI-32720516; Score: 0.27
DE  Interaction: Q04912; IntAct: EBI-32725158; Score: 0.27
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0045211;
GO  GO:0030017;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0140444;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0042803;
GO  GO:0003723;
GO  GO:0007030;
GO  GO:0042692;
GO  GO:0090292;
GO  GO:0006997;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MATSRGASRCPRDIANVMQRLQDEQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGVKLLALLEVLSGQKLPCEQG
SQ  RRMKRIHAVANIGTALKFLEGRKIKLVNINSTDIADGRPSIVLGLMWTIILYFQIEELTSNLPQLQSLSSSASSVDSIVS
SQ  SETPSPPSKRKVTTKIQGNAKKALLKWVQYTAGKQTGIEVKDFGKSWRSGVAFHSVIHAIRPELVDLETVKGRSNRENLE
SQ  DAFTIAETELGIPRLLDPEDVDVDKPDEKSIMTYVAQFLKHYPDIHNASTDGQEDDEILPGFPSFANSVQNFKREDRVIF
SQ  KEMKVWIEQFERDLTRAQMVESNLQDKYQSFKHFRVQYEMKRKQIEHLIQPLHRDGKLSLDQALVKQSWDRVTSRLFDWH
SQ  IQLDKSLPAPLGTIGAWLYRAEVALREEITVQQVHEETANTIQRKLEQHKDLLQNTDAHKRAFHEIYRTRSVNGIPVPPD
SQ  QLEDMAERFHFVSSTSELHLMKMEFLELKYRLLSLLVLAESKLKSWIIKYGRRESVEQLLQNYVSFIENSKFFEQYEVTY
SQ  QILKQTAEMYVKADGSVEEAENVMKFMNETTAQWRNLSVEVRSVRSMLEEVISNWDRYGNTVASLQAWLEDAEKMLNQSE
SQ  NAKKDFFRNLPHWIQQHTAMNDAGNFLIETCDEMVSRDLKQQLLLLNGRWRELFMEVKQYAQADEMDRMKKEYTDCVVTL
SQ  SAFATEAHKKLSEPLEVSFMNVKLLIQDLEDIEQRVPVMDAQYKIITKTAHLITKESPQEEGKEMFATMSKLKEQLTKVK
SQ  ECYSPLLYESQQLLIPLEELEKQMTSFYDSLGKINEIITVLEREAQSSALFKQKHQELLACQENCKKTLTLIEKGSQSVQ
SQ  KFVTLSNVLKHFDQTRLQRQIADIHVAFQSMVKKTGDWKKHVETNSRLMKKFEESRAELEKVLRIAQEGLEEKGDPEELL
SQ  RRHTEFFSQLDQRVLNAFLKACDELTDILPEQEQQGLQEAVRKLHKQWKDLQGEAPYHLLHLKIDVEKNRFLASVEECRT
SQ  ELDRETKLMPQEGSEKIIKEHRVFFSDKGPHHLCEKRLQLIEELCVKLPVRDPVRDTPGTCHVTLKELRAAIDSTYRKLM
SQ  EDPDKWKDYTSRFSEFSSWISTNETQLKGIKGEAIDTANHGEVKRAVEEIRNGVTKRGETLSWLKSRLKVLTEVSSENEA
SQ  QKQGDELAKLSSSFKALVTLLSEVEKMLSNFGDCVQYKEIVKNSLEELISGSKEVQEQAEKILDTENLFEAQQLLLHHQQ
SQ  KTKRISAKKRDVQQQIAQAQQGEGGLPDRGHEELRKLESTLDGLERSRERQERRIQVTLRKWERFETNKETVVRYLFQTG
SQ  SSHERFLSFSSLESLSSELEQTKEFSKRTESIAVQAENLVKEASEIPLGPQNKQLLQQQAKSIKEQVKKLEDTLEEDIKT
SQ  MEMVKTKWDHFGSNFETLSVWITEKEKELNALETSSSAMDMQISQIKVTIQEIESKLSSIVGLEEEAQSFAQFVTTGESA
SQ  RIKAKLTQIRRYGEELREHAQCLEGTILGHLSQQQKFEENLRKIQQSVSEFEDKLAVPIKICSSATETYKVLQEHMDLCQ
SQ  ALESLSSAITAFSASARKVVNRDSCVQEAAALQQQYEDILRRAKERQTALENLLAHWQRLEKELSSFLTWLERGEAKASS
SQ  PEMDISADRVKVEGELQLIQALQNEVVSQASFYSKLLQLKESLFSVASKDDVKMMKLHLEQLDERWRDLPQIINKRINFL
SQ  QSVVAEHQQFDELLLSFSVWIKLFLSELQTTSEISIMDHQVALTRHKDHAAEVESKKGELQSLQGHLAKLGSLGRAEDLH
SQ  LLQGKAEDCFQLFEEASQVVERRQLALSHLAEFLQSHASLSGILRQLRQTVEATNSMNKNESDLIEKDLNDALQNAKALE
SQ  SAAVSLDGILSKAQYHLKIGSSEQRTSCRATADQLCGEVERIQNLLGTKQSEADALAVLKKAFQDQKEELLKSIEDIEER
SQ  TDKERLKEPTRQALQQRLRVFNQLEDELNSHEHELCWLKDKAKQIAQKDVAFAPEVDREINRLEVTWDDTKRLIHENQGQ
SQ  CCGLIDLMREYQNLKSAVSKVLENASSVIVTRTTIKDQEDLKWAFSKHETAKNKMNYKQKDLDNFTSKGKHLLSELKKIH
SQ  SSDFSLVKTDMESTVDKWLDVSEKLEENMDRLRVSLSIWDDVLSTRDEIEGWSNNCVPQMAENISNLDNHLRAEELLKEF
SQ  ESEVKNKALRLEELHSKVNDLKELTKNLETPPDLQFIEADLMQKLEHAKEITEVAKGTLKDFTAQSTQVEKFINDITTWF
SQ  TKVEESLMNCAQNETCEALKKVKDIQKELQSQQSNISSTQENLNSLCRKYHSAELESLGRAMTGLIKKHEAVSQLCSKTQ
SQ  ASLQESLEKHFSESMQEFQEWFLGAKAAAKESSDRTGDSKVLEAKLHDLQNILDSVSDGQSKLDAVTQEGQTLYAHLSKQ
SQ  IVSSIQEQITKANEEFQAFLKQCLKDKQALQDCASELGSFEDQHRKLNLWIHEMEERFNTENLGESKQHIPEKKNEVHKV
SQ  EMFLGELLAARESLDKLSQRGQLLSEEGHGAGQEGRLCSQLLTSHQNLLRMTKEKLRSCQVALQEHEALEEALQSMWFWV
SQ  KAIQDRLACAESTLGSKDTLEKRLSQIQDILLMKGEGEVKLNMAIGKGEQALRSSNKEGQRVIQTQLETLKEVWADIMSS
SQ  SVHAQSTLESVISQWNDYVERKNQLEQWMESVDQKIEHPLQPQPGLKEKFVLLDHLQSILSEAEDHTRALHRLIAKSREL
SQ  YEKTEDESFKDTAQEELKTQFNDIMTVAKEKMRKVEEIVKDHLMYLDAVHEFTDWLHSAKEELHRWSDMSGDSSATQKKL
SQ  SKIKELIDSREIGASRLSRVESLAPEVKQNTTASGCELMHTEMQALRADWKQWEDSVFQTQSCLENLVSQMALSEQEFSG
SQ  QVAQLEQALEQFSALLKTWAQQLTLLEGKNTDEEIVECWHKGQEILDALQKAEPRTEDLKSQLNELCRFSRDLSTYSGKV
SQ  SGLIKEYNCLCLQASKGCQNKEQILQQRFRKAFRDFQQWLVNAKITTAKCFDIPQNISEVSTSLQKIQEFLSESENGQHK
SQ  LNMMLSKGELLSTLLTKEKAKGIQAKVTAAKEDWKNFHSNLHQKESALENLKIQMKDFEVSAEPIQDWLSKTEKMVHESS
SQ  NRLYDLPAKRREQQKLQSVLEEIHCYEPQLNRLKEKAQQLWEGQAASKSFRHRVSQLSSQYLALSNLTKEKVSRLDRIVA
SQ  EHNQFSLGIKELQDWMTDAIHMLDSYCHPTSDKSVLDSRTLKLEALLSVKQEKEIQMKMIVTRGESVLQNTSPEGIPTIQ
SQ  QQLQSVKDMWASLLSAGIRCKSQLEGALSKWTSYQDGVRQFSGWMDSMEANLNESERQHAELRDKTTMLGKAKLLNEEVL
SQ  SYSSLLETIEVKGAGMTEHYVTQLELQDLQERYRAIQERAKEAVTKSEKLVRLHQEYQRDLKAFEVWLGQEQEKLDQYSV
SQ  LEGDAHTHETTLRDLQELQVHCAEGQALLNSVLHTREDVIPSGIPQAEDRALESLRQDWQAYQHRLSETRTQFNNVVNKL
SQ  RLMEQKFQQVDEWLKTAEEKVSPRTRRQSNRATKEIQLHQMKKWHEEVTAYRDEVEEVGARAQEILDESHVNSRMGCQAT
SQ  QLTSRYQALLLQVLEQIKFLEEEIQSLEESESSLSSYSDWYGSTHKNFKNVATKIDKVDTVMMGKKLKTLEVLLKDMEKG
SQ  HSLLKSAREKGERAVKYLEEGEAERLRKEIHDHMEQLKELTSTVRKEHMTLEKGLHLAKEFSDKCKALTQWIAEYQEILH
SQ  VPEEPKMELYEKKAQLSKYKSLQQTVLSHEPSVKSVREKGEALLELVQDVTLKDKIDQLQSDYQDLCSIGKEHVFSLEAK
SQ  VKDHEDYNSELQEVEKWLLQMSGRLVAPDLLETSSLETITQQLAHHKAMMEEIAGFEDRLNNLQMKGDTLIGQCADHLQA
SQ  KLKQNVHAHLQGTKDSYSAICSTAQRMYQSLEHELQKHVSRQDTLQQCQAWLSAVQPDLEPSPQPPLSRAEAIKQVKHFR
SQ  ALQEQARTYLDLLCSMCDLSNASVKTTAKDIQQTEQTIEQKLVQAQNLTQGWEEIKHLKSELWIYLQDADQQLQNMKRRH
SQ  SELELNIAQNMVSQVKDFVKKLQSKQASVNTIIEKVNKLTKKEESPEHKEINHLNDQWLDLCRQSNNLCLQREEDLQRTR
SQ  DYHDCMNVVEVFLEKFTTEWDNLARSDAESTAVHLEALKKLALALQERKYAIEDLKDQKQKMIEHLNLDDKELVKEQTSH
SQ  LEQRWFQLEDLIKRKIQVSVTNLEELNVVQSRFQELMEWAEEQQPNIAEALKQSPPPDMAQNLLMDHLAICSELEAKQML
SQ  LKSLIKDADRVMADLGLNERQVIQKALSDAQSHVNCLSDLVGQRRKYLNKALSEKTQFLMAVFQATSQIQQHERKIMFRE
SQ  HICLLPDDVSKQVKTCKSAQASLKTYQNEVTGLWAQGRELMKEVTEQEKSEVLGKLQELQSVYDSVLQKCSHRLQELEKN
SQ  LVSRKHFKEDFDKACHWLKQADIVTFPEINLMNESSELHTQLAKYQNILEQSPEYENLLLTLQRTGQTILPSLNEVDHSY
SQ  LSEKLNALPRQFNVIVALAKDKFYKVQEAILARKEYASLIELTTQSLSELEAQFLRMSKVPTDLAVEEALSLQDGCRAIL
SQ  DEVAGLGEAVDELNQKKEGFRSTGQPWQPDKMLHLVTLYHRLKRQTEQRVSLLEDTTSAYQEHEKMCQQLERQLKSVKEE
SQ  QSKVNEETLPAEEKLKMYHSLAGSLQDSGIVLKRVTIHLEDLAPHLDPLAYEKARHQIQSWQGELKLLTSAIGETVTECE
SQ  SRMVQSIDFQTEMSRSLDWLRRVKAELSGPVYLDLNLQDIQEEIRKIQIHQEEVQSSLRIMNALSHKEKEKFTKAKELIS
SQ  ADLEHSLAELSELDGDIQEALRTRQATLTEIYSQCQRYYQVFQAANDWLEDAQELLQLAGNGLDVESAEENLKSHMEFFS
SQ  TEDQFHSNLEELHSLVATLDPLIKPTGKEDLEQKVASLELRSQRMSRDSGAQVDLLQRCTAQWHDYQKAREEVIELMNDT
SQ  EKKLSEFSLLKTSSSHEAEEKLSEHKALVSVVNSFHEKIVALEEKASQLEKTGNDASKATLSRSMTTVWQRWTRLRAVAQ
SQ  DQEKILEDAVDEWTGFNNKVKKATEMIDQLQDKLPGSSAEKASKAELLTLLEYHDTFVLELEQQQSALGMLRQQTLSMLQ
SQ  DGAAPTPGEEPPLMQEITAMQDRCLNMQEKVKTNGKLVKQELKDREMVETQINSVKCWVQETKEYLGNPTIEIDAQLEEL
SQ  QILLTEATNHRQNIEKMAEEQKEKYLGLYTILPSELSLQLAEVALDLKIRDQIQDKIKEVEQSKATSQELSRQIQKLAKD
SQ  LTTILTKLKAKTDNVVQAKTDQKVLGEELDGCNSKLMELDAAVQKFLEQNGQLGKPLAKKIGKLTELHQQTIRQAENRLS
SQ  KLNQAASHLEEYNEMLELILKWIEKAKVLAHGTIAWNSASQLREQYILHQTLLEESKEIDSELEAMTEKLQYLTSVYCTE
SQ  KMSQQVAELGRETEELRQMIKIRLQNLQDAAKDMKKFEAELKKLQAALEQAQATLTSPEVGRLSLKEQLSHRQHLLSEME
SQ  SLKPKVQAVQLCQSALRIPEDVVASLPLCHAALRLQEEASRLQHTAIQQCNIMQEAVVQYEQYEQEMKHLQQLIEGAHRE
SQ  IEDKPVATSNIQELQAQISRHEELAQKIKGYQEQIASLNSKCKMLTMKAKHATMLLTVTEVEGLAEGTEDLDGELLPTPS
SQ  AHPSVVMMTAGRCHTLLSPVTEESGEEGTNSEISSPPACRSPSPVANTDASVNQDIAYYQALSAERLQTDAAKIHPSTSA
SQ  SQEFYEPGLEPSATAKLGDLQRSWETLKNVISEKQRTLYEALERQQKYQDSLQSISTKMEAIELKLSESPEPGRSPESQM
SQ  AEHQALMDEILMLQDEINELQSSLAEELVSESCEADPAEQLALQSTLTVLAERMSTIRMKASGKRQLLEEKLNDQLEEQR
SQ  QEQALQRYRCEADELDSWLLSTKATLDTALSPPKEPMDMEAQLMDCQNMLVEIEQKVVALSELSVHNENLLLEGKAHTKD
SQ  EAEQLAGKLRRLKGSLLELQRALHDKQLNMQGTAQEKEESDVDLTATQSPGVQEWLAQARTTWTQQRQSSLQQQKELEQE
SQ  LAEQKSLLRSVASRGEEILIQHSAAETSGDAGEKPDVLSQELGMEGEKSSAEDQMRMKWESLHQEFSTKQKLLQNVLEQE
SQ  QEQVLYSRPNRLLSGVPLYKGDVPTQDKSAVTSLLDGLNQAFEEVSSQSGGAKRQSIHLEQKLYDGVSATSTWLDDVEER
SQ  LFVATALLPEETETCLFNQEILAKDIKEMSEEMDKNKNLFSQAFPENGDNRDVIEDTLGCLLGRLSLLDSVVNQRCHQMK
SQ  ERLQQILNFQNDLKVLFTSLADNKYIILQKLANVFEQPVAEQIEAIQQAEDGLKEFDAGIIELKRRGDKLQVEQPSMQEL
SQ  SKLQDMYDELMMIIGSRRSGLNQNLTLKSQYERALQDLADLLETGQEKMAGDQKIIVSSKEEIQQLLDKHKEYFQGLESH
SQ  MILTETLFRKIISFAVQKETQFHTELMAQASAVLKRAHKRGVELEYILETWSHLDEDQQELSRQLEVVESSIPSVGLVEE
SQ  NEDRLIDRITLYQHLKSSLNEYQPKLYQVLDDGKRLLISISCSDLESQLNQLGECWLSNTNKMSKELHRLETILKHWTRY
SQ  QSESADLIHWLQSAKDRLEFWTQQSVTVPQELEMVRDHLNAFLEFSKEVDAQSSLKSSVLSTGNQLLRLKKVDTATLRSE
SQ  LSRIDSQWTDLLTNIPAVQEKLHQLQMDKLPSRHAISEVMSWISLMENVIQKDEDNIKNSIGYKAIHEYLQKYKGFKIDI
SQ  NCKQLTVDFVNQSVLQISSQDVESKRSDKTDFAEQLGAMNKSWQILQGLVTEKIQLLEGLLESWSEYENNVQCLKTWFET
SQ  QEKRLKQQHRIGDQASVQNALKDCQDLEDLIKAKEKEVEKIEQNGLALIQNKKEDVSSIVMSTLRELGQTWANLDHMVGQ
SQ  LKILLKSVLDQWSSHKVAFDKINSYLMEARYSLSRFRLLTGSLEAVQVQVDNLQNLQDDLEKQERSLQKFGSITNQLLKE
SQ  CHPPVTETLTNTLKEVNMRWNNLLEEIAEQLQSSKALLQLWQRYKDYSKQCASTVQQQEDRTNELLKAATNKDIADDEVA
SQ  TWIQDCNDLLKGLGTVKDSLFFLHELGEQLKQQVDASAASAIQSDQLSLSQHLCALEQALCKQQTSLQAGVLDYETFAKS
SQ  LEALEAWIVEAEEILQGQDPSHSSDLSTIQERMEELKGQMLKFSSMAPDLDRLNELGYRLPLNDKEIKRMQNLNRHWSLI
SQ  SSQTTERFSKLQSFLLQHQTFLEKCETWMEFLVQTEQKLAVEISGNYQHLLEQQRAHELFQAEMFSRQQILHSIIIDGQR
SQ  LLEQGQVDDRDEFNLKLTLLSNQWQGVIRRAQQRRGIIDSQIRQWQRYREMAEKLRKWLVEVSYLPMSGLGSVPIPLQQA
SQ  RTLFDEVQFKEKVFLRQQGSYILTVEAGKQLLLSADSGAEAALQAELAEIQEKWKSASMRLEEQKKKLAFLLKDWEKCEK
SQ  GIADSLEKLRTFKKKLSQSLPDHHEELHAEQMRCKELENAVGSWTDDLTQLSLLKDTLSAYISADDISILNERVELLQRQ
SQ  WEELCHQLSLRRQQIGERLNEWAVFSEKNKELCEWLTQMESKVSQNGDILIEEMIEKLKKDYQEEIAIAQENKIQLQQMG
SQ  ERLAKASHESKASEIEYKLGKVNDRWQHLLDLIAARVKKLKETLVAVQQLDKNMSSLRTWLAHIESELAKPIVYDSCNSE
SQ  EIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACATDAECDSIQQATRNLDRRWRNICAMSMERRLKIEETWRL
SQ  WQKFLDDYSRFEDWLKSSERTAAFPSSSGVIYTVAKEELKKFEAFQRQVHECLTQLELINKQYRRLARENRTDSACSLKQ
SQ  MVHEGNQRWDNLQKRVTSILRRLKHFIGQREEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEISLNH
SQ  NKIEQIIAQGEQLIEKSEPLDAAIIEEELDELRRYCQEVFGRVERYHKKLIRLPLPDDEHDLSDRELELEDSAALSDLHW
SQ  HDRSADSLLSPQPSSNLSLSLAQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESAMSRALPSEDEEGQDDKDFYLRG
SQ  AVGLSGDHSALESQIRQLGKALDDSRFQIQQTENIIRSKTPTGPELDTSYKGYMKLLGECSSSIDSVKRLEHKLKEEEES
SQ  LPGFVNLHSTETQTAGVIDRWELLQAQALSKELRMKQNLQKWQQFNSDLNSIWAWLGDTEEELEQLQRLELSTDIQTIEL
SQ  QIKKLKELQKAVDHRKAIILSINLCSPEFTQADSKESRDLQDRLSQMNGRWDRVCSLLEEWRGLLQDALMQCQGFHEMSH
SQ  GLLLMLENIDRRKNEIVPIDSNLDAEILQDHHKQLMQIKHELLESQLRVASLQDMSCQLLVNAEGTDCLEAKEKVHVIGN
SQ  RLKLLLKEVSRHIKELEKLLDVSSSQQDLSSWSSADELDTSGSVSPTSGRSTPNRQKTPRGKCSLSQPGPSVSSPHSRST
SQ  KGGSDSSLSEPGPGRSGRGFLFRVLRAALPLQLLLLLLIGLACLVPMSEEDYSCALSNNFARSFHPMLRYTNGPPPL
//
ID  Q6ZWR6;
PN  Nesprin-1;
GN  Syne1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus. Nucleus envelope. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere {ECO:0000250}. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. In skeletal and smooth muscles, a significant amount is found in the sarcomeres (By similarity). {ECO:0000250}.
DR  UNIPROT: Q6ZWR6;
DR  UNIPROT: Q8K3T7;
DR  UNIPROT: Q9ERT7;
DR  UNIPROT: Q9ERT8;
DR  Pfam: PF00307;
DR  Pfam: PF10541;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS51049;
DE  Function: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nucleus- centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probably association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 seem to act redundantly in cerebellum, midbrain, brain stem, and other brain regions except cerebral cortex and hippocampus. Required for centrosome migration to the apical cell surface during early ciliogenesis. May be involved in nuclear remodeling during sperm head formation in spermatogenesis; a probable SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette. {ECO:0000250|UniProtKB:Q8NF91, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19874786}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5SS91; IntAct: EBI-12557121; Score: 0.46
DE  Interaction: Q6ZMZ3; IntAct: EBI-10760858; Score: 0.51
DE  Interaction: Q6ZWR6; IntAct: EBI-10760752; Score: 0.40
DE  Interaction: Q9JJF2; IntAct: EBI-12557523; Score: 0.46
DE  Interaction: Q99ME6; IntAct: EBI-15644511; Score: 0.37
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: Q9D415; IntAct: EBI-16725590; Score: 0.35
DE  Interaction: Q3UHD9; IntAct: EBI-16736255; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
DE  Interaction: Q9QWI6; IntAct: EBI-27100778; Score: 0.35
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005794;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0000932;
GO  GO:0045211;
GO  GO:0030017;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0140444;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0042803;
GO  GO:0051642;
GO  GO:0007030;
GO  GO:0042692;
GO  GO:0090292;
GO  GO:0007097;
GO  GO:1902017;
GO  GO:0007283;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MATSRASSRSHRDITNVMQRLQDEQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQG
SQ  HRVKRIHAVANIGTALKFLEGRKIKLVNINATDIADGRPSIVLGLMWTIILYFQIEELTSNLPQLQSLSSSASSVDSMVS
SQ  TETASPPSKRKVAAKIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLE
SQ  DAFTIAETQLGIPRLLDPEDVDVDKPDEKSIMTYVAQFLTQYPDIHGAGCDGQEDDVVFVGFTNNIALLLGFQRDDRLIL
SQ  KETKVWIEQFERDFTRAQMTESSLQDKYQAFKHFRVQYEMKRKQVEHIIQPLQRDGKLTLDQALVKQCWERVSSRLFDWH
SQ  IQLDKSLPAPLGTIGAWLYRAEVALREEITIQQVHEETANTIQRKLEQHKDLLQNTDAHKRAFHEIYQTRSVNGIPMPPD
SQ  QLEDMAERFHFVSSTSELHLMKMEFLELKYRLLSLLVLAESKLKSWIIKYGRRESVELLLQSYISFIENSKFFEQYEVTY
SQ  QILKQTADIYVKAEGSVEEAENVMKFMSEATAQWRNLSVEVRSVRSMLEEVISNWDRYGDTVASLQAWLEDAEKMLSQSE
SQ  HAKKDFFRNLPHWIQQHTAMNDAGNFLIETCDEIVSRDLKQQLLLLNGRWRELFMEVKQYARADEMDRMKKEYIDVTTTL
SQ  FGFATEAHRKLSEPLEVSFINVKLLIQDLEDLEKRVPVMDAQYKMIAKKAHLFAKESPQEEANEMLTTMSKLKEQLSKVK
SQ  ECCSPLLYEAQQLTVPLEELETQITSFYDSLGKINEILSVLEQEAQSSTLFKQKHQELLASQENCKKSLTLIEKGSQSVQ
SQ  KLVTSSQARKPWDHTKLQKQIADVHHAFQSMIKKTGDWKKHVEANSRLMKKFEESRAELEKVLRVAQEGLEEKGDPEELL
SQ  RRHTEFFSQLDQRVLNAFLKACDELTDILPEQEQQGLQEAVRKLHKQWKDLQGEAPYHLLHLKIAVEKDRFSAAVEECRA
SQ  ELEQETKLAPQEGSEKIIKEHRVFFSDKGPHHLCEKRLQLIEELCGKLPVQDPVRDTCGACHTALKELKASIDNTYTMLV
SQ  DDPDKWKDYTSRFSEFSSWVSAKKACLKKIKDEPIDTGNHDEVKHMVDEIRNDITKKGESLSWLKSRLKYLIDISSENEA
SQ  QKRGDELAELSSSFKALVALLSEVEKLLSNFGECVQYKEIVKSSLEGLISGPQESKEEAEMILDSKNLLEAQQLLLHHQQ
SQ  KTKMISAKKRDLQEQMEQAQQGGQAGPGQEELRKLESTLTGLEQSRERQERRIQVSLRKWERFETNKETVVRYLFQTGSS
SQ  HERFLSFSSLESLSSELEQTKEFSKRTESIATQAENLVKEAAELPLGPRNKRVLQRQAKSIKEQVTTLEDTLEEDIKTME
SQ  MVKSKWDHFGSNFETLSIWILEKENELSSLEASASAADVQISQIKVTIQEIESKIDSIVGLEEEAQSFAQFVTTGESARI
SQ  KAKLTQIRRYWEELQEHARGLEGTILGHLSQQQKFEENLRKIRQSVSEFAERLADPIKICSSAAETYKVLQEHMDLCQAV
SQ  ESLSSTVTMFSASAQKAVNRESCTQEAAALQQQYEEILHKAKEMQTALEDLLARWQRLEKGLSPFLTWLERCEAIASSPE
SQ  KDISADRGKVESELQLIQALQNEVVSQASLYSNLLQLKEALFSVASKEDVAVMKLQLEQLDERWGDLPQIISKRMHFLQS
SQ  VLAEHKQFDELLFSFSVWIKQFLGELQRTSEINLRDHQVALTRHKDHAAEIEKKRGEITHLQGHLSQLRSLGRAQDLHPL
SQ  QSKVDDCFQLFEEASQVVERRKLALAQLAEFLQSHACMSTLLYQLRQTVEATKSMSKKQSDSLKTDLHSAIQDVKTLESS
SQ  AISLDGTLTKAQCHLKSASPEERTSCRATTDQLSLEVERIQNLLGTKQSEADALVALKEAFREQKEELLRSIEDIEERMD
SQ  RERLKVPTRQALQHRLRVFNQLEDELNSHEHELCWLKDKAKQIAQKDVAFAPEVDREINGLEATWDDTRRQIHENQGQCC
SQ  GLIDLVREYQSLKSTVCNVLEDASNVVVMRATIKDQGDLKWAFSKHETSRNEMNSKQKELDSFTSKGKHLLSELKKIHSG
SQ  DFSLVKTDMESTLDKWLDVSERIEENMDMLRVSLSIWDDVLSRKDEIEGWSNSSLPKLAENISNLNNSLRAEELLKELES
SQ  EVKIKALKLEDLHSKINNLKELTKNPETPTELQFIEADLRQKLEHAKEITEEARGTLKDFTAQRTQVERFVKDITAWLIN
SQ  VEESLTRCAQTETCEGLKKAKDIRKELQSQQNSITSTQEELNSLCRKHHSVELESLGRAMTGLIKKHEATSQLCSQTQAR
SQ  IQDSLEKHFSGSMKEFQEWFLGAKAAARESSNLTGDSQILEARLHNLQGVLDSLSDGQSKLDVVTQEGQTLYAHLPKQIV
SQ  SSIQEQITKANEEFQAFLKQCLKEKQALQDCVSELGSFEDQHRKLNLWIHEMEERLKTENLGESKHHISEKKNEVRKVEM
SQ  FLGELLAARESLDKLSQRGQLLSEESHSAGKGGCRSTQLLTSYQSLLRVTKEKLRSCQLALKEHEALEEATQSMWARVKD
SQ  VQDRLACAESTLGNKETLEGRLSQIQDILLMKGEGEVKLNLAIGKGDQALRSSNKEGQQAIQDQLEMLKKAWAEAMNSAV
SQ  HAQSTLESVIDQWNDYLEKKSQLEQWMESVDQRLEHPLQLQPGLKEKFSLLDHFQSIVSEAEDHTGALQQLAAKSRELYQ
SQ  KTQDESFKEAGQEELRTQFQDIMTVAKEKMRTVEDLVKDHLMYLDAVQEFADWLHSAKEELHRWSDTSGDPSATQKKLLK
SQ  IKELIDSREIGAGRLSRVESLAPAVKQNTAASGCELLNSEMQALRADWRQWEDCLFQTQSSLESLVSEMALSEQEFFGQV
SQ  TQLEQALEQFCTLLKTWAQQLTLLEGKNSDEEILECWHKGREILDALQKAEPMTEDLKSQLNELCRFSRDLSPYSEKVSG
SQ  LIKEYNCLCLQASKGCQNKEQILQERFQKASRGFQQWLVNAKITTAKCFDLPQNLSEVSSSLQKIQEFLSESENGQHKLN
SQ  TMLFKGELLSSLLTEEKAQAVQAKVLTAKEEWKSFHANLHQKESALENLKIQMKDFEVSAELVQNWLSKTERLVQESSNR
SQ  LYDLPAKRREQQKLQSVLEEIQCYEPQLHRLKEKARQLWEGQAASKSFVHRVSQLSSQYLALSNVTKEKVSRLDRIIAEH
SQ  NRFSQGVKELQDWMSDAVHMLDSYCLPTSDKSVLDSRMLKLEALLSVRQEKEIQMKMVVTRGEYVLQSTSLEGSAAVQQQ
SQ  LQAVKDMWESLLSAAIRCKSQLEGALSKWTSYQDDVRQFSSWMDSVEVSLTESEKQHTELREKITALGKAKLLNEEVLSH
SQ  SSLLETIEVKRAAMTEHYVTQLELQDLQERHQALKEKAKEAVTKLEKLVRLHQEYQRDLKAFESWLEQEQEKLDRCSVHE
SQ  GDTNAHETMLRDLQELQVRCAEGQALLNSVLHTREDVIPSGLPQAEDRVLESLRQDWQVYQHRLAEARMQLNNVVNKLRL
SQ  MEQKFQQADEWLKRMEEKINFRSECQSSRSDKEIQLLQLKKWHEDLSAHRDEVEEVGTRAQGILDETHISSRMGCQATQL
SQ  TSRYQALLLQVLEQIKFFEEELQCLEETESSLSSYSDWYGSTHKNFKNVATKIDKVDESMMGKKLKTLEVLLKDMEKGHS
SQ  LLKSAREKGERAMKFLAEHEAEALRKEIHTYMEQLKNLTSTVRKECMSLEKGLHLAKEFSDKYKVLAQWMAEYQEILCTP
SQ  EEPKMELYEKKAQLSKYKSLQQMVLSHEPSVTSVQEKSEALLELVQDQSLKDKIQKLQSDFQDLCSRAKERVFSLEAKVK
SQ  DHEDYNTELQEVEKWLLQMSGRLVAPDLLEMSSLETITQQLAHHKAMMEEIAGFEDRLDNLKAKGDTLIGQCPEHLQAKQ
SQ  KQTVQAHLQGTKDSYSAICSTAQRVYRSLEYELQKHVSSQDTLQQCQAWISAVQPDLKPSPQPPLSRAEAVKQVKHFRAL
SQ  QEQARTYLDLLCSMCDLSNSSVKNTAKDIQQTEQLIEQRLVQAQNLTQGWEEIKSLKAELWIYLQDADQQLQNMKRRHTE
SQ  LEINIAQNMVMQVKDFIKQLQCKQVSVSTIVEKVDKLTKNQESPEHKEITHLNDQWQDLCLQSDKLCAQREQDLQRTSSY
SQ  HDHMRVVEAFLEKFTTEWDSLARSNAESTAIHLEALKKLALALQEEMYAIDDLKDCKQKLIEQLGLDDRELVREQTSHLE
SQ  QRWFQLQDLVKRKIQVSVTNLEELNVIQSRFQELMEWAEEQQPNIVEALKQSPPPGMAQHLLMDHLAICSELEAKQVLLK
SQ  SLMKDADRVMADLGLNERKVIQKALSEAQKHVSCLSDLVGQRRKYLNKALSEKTQFLMAVFQATSQIQQHERKIVFREYI
SQ  CLLPDDVSKQVKTCKTAQASLKTYQNEVTGLCAQGRELMKGITKQEQEEVLGKLQELQTVYDTVLQKCSHRLQELEKSLV
SQ  SRKHFKEDFDKACHWLKQADIVTFPEINLMNEKTELHAQLDKYQSILEQSPEYENLLLTLQTTGQAMLPSLNEVDHSYLS
SQ  EKLSALPQQFNVIVALAKDKFYKTQEAILARKEYTSLIELTTQSLGDLEDQFLKMRKMPSDLIVEESVSLQQSCSALLGE
SQ  VVALGEAVNELNQKKESFRSTGQPWQPEKMLQLATLYHRLKRQAEQRVSFLEDTTSVYKEHAQMCRQLESQLEVVKREQA
SQ  KVNEETLPAEEKLKVYHSLAGSLQDSGILLKRVATHLEDLSPHLDPTAYEKAKSQVQSWQEELKQMTSDVGELVTECESR
SQ  MVQSIDFQTEMSRSLDWLRRVKAELSGPVCLDLSLQDIQEEIRKIQIHQEEVLSSLRIMSALSHKEQEKFTKAKELISAD
SQ  LEHTLAELQELDGDVQEALRTRQATLTEIYSRCQRYYQVFQAANDWLDDAQEMLQLAGNGLDVESAEENLRSHMEFFKTE
SQ  GQFHSNMEELRGLVARLDPLIKATGKEELAQKMASLEKRSQGIIQESHTQRDLLQRCMVQWQEYQKAREGVIELMNDAEK
SQ  KLSEFAVLKTSSIHEAEEKLSKHKALVSVVDSFHEKIVALEEKASQLEQTGNDTSKATLSRSMTTVWQRWTRLRAVAQDQ
SQ  EKILEDAVDEWKRLSAKVKETTEVINQLQGRLPGSSTEKASKAELMTLLESHDTYLMDLESQQLTLGVLQQRALSMLQDR
SQ  AFPGTEEEVPILRAITALQDQCLNMQEKVKNHGKLVKQELQEREAVETRINSVKSWVQETKDYLGNPTIEIDTQLEELKR
SQ  LLAEATSHQESIEKIAEEQKNKYLGLYTVLPSEISLQLAEVALDLKIHDQIQEKVQEIEEGKAMSQEFSCKIQKVTKDLT
SQ  TILTKLKAKTDDLVHAKAEHKMLGEELDGCNSKLMELDAAIQTFSERHSQLGQPLAKKIGKLTELHQQTIRQAENRLSKL
SQ  NQALSHMEEYNEMLETVRKWIEKAKVLVHGNIAWNSASQLQEQYILHQTLLEESGEIDSDLEAMAEKVQHLANVYCTGKL
SQ  SQQVTQFGREMEELRQAIRVRLRNLQDAAKDMKKFEGELRNLQVALEQAQTILTSPEVGRRSLKEQLCHRQHLLSEMESL
SQ  KPKMQAVQLCQSALRIPEDVVASLPLCHAALRLQEEASQLQHTAIQQCNIMQAKKHSLIFPPKEAVVQYEQYKQEMKHLQ
SQ  QLIEEAHREIEDKPVATSNIQELQAQISLHEELAQKIKGYQEQIDSLNSKCKMLTMKAKHATMLLTVTEVEGLAEGTEDL
SQ  DRELHPTPSAHPSVVMMTAGRCHTLLSPVTEESGEEGTNSEISSPPACRSPSPVANTEAAVNQDIAYYQALSAEGLQTDA
SQ  ARIPPSAAVSQELYEPGLEPSATAKLGDLQRSWETLKNVISEKQRTLYEVLERQQKYQDSLQSISTKMEAMEMKLGESLE
SQ  PSRSPESQMAEHQALMDEVQMLQDEINGLQVSLAEELVAESQESDPAEQLALQSTLTVLAERMSTIRMKAAGKRQLLEEK
SQ  LSDQLEEQRQEQALQRYRCEADELDHWLLNTKATLDVALGTSQEPMDMDAQLVDCQNMLVEIEQKVVALSQLSVHNENLL
SQ  LEGKAHTKEEAEQLAVKLRLLKGSLGELQRALHDRQLDMQGVTQEKEENDVDFTDTQSPGVQEWLAQARTTRTHQRQSSL
SQ  QQQKEFEQELAEQKSLLRSVASRGEEILTQHSTAEGSGGLGEKPDVLSQELGIAEDQMRVKWESLHQEFSAKQKLLQNIL
SQ  EQEQEQVLYSSPNRLLSGVLPFRGEAQTQDKTSVTSLLDGLSQAFGEASSQSGGTDRQSIHLEQKLYDGVSATSTWLNDV
SQ  EERLFVATAPLPEETEACLFNQEALAKDIKEMSEEMDKNKNLFSQAFPEDSDNRDVIEDTLGCLLGRLSLLDSVVDQRCH
SQ  QMKERLQQILRFQNDLKVLFTSLADSKYIILQKLANVFEQPIVEQMQAIQQAEEGLRDLEGGISELKRWADKLQVEQSAV
SQ  QELSKLQDMYDELLMTVSSRRSSLHQNLALKSQYDKALQDLVDLLDTGQEKMTGDQKIIVCSKEEIQQLLGKHKEYFQGL
SQ  ESHMILTEILFRKIVGFAAVKETQFHTDCMAQASAVLKQAHKRGVELEYILEMWSHLDENRQELSRQLEVIENSIPSVGL
SQ  VEESEDRLVERTNLYQHLKSSLNEYQPKLYQALDDGKRLLMSVSCSELESQLNQLGEHWLSNTNKVSKELHRLETILKHW
SQ  TRYQSEAAALNHWLQCAKDRLAFWTQQSVTVPQELEMVRDHLSAFLEFSKEVDAKSALKSSVTSTGNQLLRLKKVDTAAL
SQ  RAELSRMDSQWTDLLTGIPVVQEKLHQLQMDKLPSRHAISEVMSWISLMESVILKDEEDIRNAIGYKAIHEYLQKYKGFK
SQ  IDLNCKQLTADFVNQSVLQISSQDVESKRSDKTDFAEQLGAMNKSWQLLQGRVGEKIQMLEGLLESWSEYENSVQSLKAW
SQ  FANQERKLKEQHLLGDRNSVENALKDCQELEDLIKAKEKEVEKIEQNGLALIQNKREEVSGSVMSTLQELRQTWISLDRT
SQ  VEQLKIQLTSALGQWSNHKAACDEINGHLMEARYSLSRFRLLTGSSEAVQVQVDNLQNLHDELEKQEGGLQKFGSITNQL
SQ  LKECHPPVAETLSSTLQEVNMRWNNLLEEIAEQLHSSKALLQLWQRYKDYSKQCASAIQRQEEQTSVLLKAATNKDIADD
SQ  EVTKWIQDCNDLLKGLETVKDSLFILRELGEQLGQQVDVSAAAAIQCEQLCFSQRLGALEQALCKQQAVLQAGVVDYETF
SQ  AKSLEALEVWMVEAEGILQGQDPTHSSDLSTIQERMEELKGQMLKFSSLAPDLDRLNELGYRLPLNDKEIKRMQNLNRHW
SQ  SLTSSQTTERFSKLQSFLLQHQTFLEKCETWMEFLVQTEHKLAVEISGNYQHLLEQQRAHELFQAEMFSRQQILHSIIVD
SQ  GQNLLEQGQVDDREEFSLKLTLLSNQWQGVIRRAQQRRGIIDSQIRQWQRYREMAEKLRKWLAEVSHLPLSGLGNIPVPL
SQ  QQVRMLFDEVQFKEKVFLRQQGSYILTVEAGKQLLLSADSGAEAALQAELTDIQEKWKAASMHLEEQKKKLAFLLKDWEK
SQ  CERGIANSLEKLRMFKKRLSQPLPDHHEELHAEQMRCKELENAVGRWTDDLTELMLVRDALAVYLSAEDISMLKERVELL
SQ  QRQWEELCHQVSLRRQQVSERLNEWAVFSEKNKELCEWLTQMESKVSQNGDILIEEMIEKLKKDYQEEIAVAQENKIQLQ
SQ  EMGERLAKASHESKASEIQYKLSRVKDRWQHLLDLMAARVKKLKETLVAVQQLDKNMGSLRTWLAHMESELAKPIVYDSC
SQ  NSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACATDAECDSIQQATRNLDRRWRNICAMSMERRLKIEET
SQ  WRLWQKFLDDYSRFEDWLEVSERTAAFPSSSGVLYTVAKEELKKFEAFQRQVHESLTQLELINKQYRRLARENRTDSACS
SQ  LRQMVHGGNQRWDDLQKRVTSILRRLKHFISQREEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEIS
SQ  LNHNKIEQIIAQGEQLIEKSEPLDAAVIEEELDELRRYCQEVFGRVERYHKKLIRLPVRLPDDHDLSDRELDLEDSTALS
SQ  DLRWQDPSADGMPSPQPSSNPSLSLPQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESASRTLPSEDEEGEEDKEFY
SQ  LRGAVGLSGDPSSLESQMRQLDKALDDSRFQIQQTANILRSKTPTGPDLDTSYKGYMKLLGECSGSIDSVRRLEHKLAEE
SQ  ESFPGFVNLNSTETQTAGVIDRWELLQAQAMSKELRMKQNLQKWQQFNSDLNNIWAWLGETEEELDRLQHLALSTDIHTI
SQ  ESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHDLQDRLSQMNGRWDRVCSLLEDWRGLLQDALMQCQEFHEM
SQ  SHALLLMLENIDRRKNEIVPIDSTLDPETLQDHHKQLMQIKQELLKSQLRVASLQDMSRQLLVNAEGSDCLEAKEKVHVI
SQ  GNRLKLLLKEVSHHIKDLEKLLDMSSSQQDLSSWSSADELDTSGSVSPTSGRSTPNRQKSPRGKCSLSQPGPSVSSPKSR
SQ  STRDGSDSSRSDPRPERVGRAFLFRILRAALPFQLLLLLLIGLTCLVPMSEKDYSCALSNNFARSFHPMLRYTNGPPPL
//
ID  Q8WXH0;
PN  Nesprin-2;
GN  SYNE2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Sarcoplasmic reticulum membrane {ECO:0000305|PubMed:15671068}; Single- pass type IV membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton. Mitochondrion. Nucleus, nucleoplasm. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000305|PubMed:15671068}. Note=Different isoform patterns are found in the different compartments of the cell. The isoforms having the C-terminal transmembrane span can be found in several organellar membranes like the nuclear envelope, the sarcoplasmic reticulum of myoblasts, or the lamellipodia and focal adhesions at the cell membrane. The largest part of the outer nuclear membrane-associated protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. Remains associated with the nuclear envelope during its breakdown in mitotic cells. Shorter soluble isoforms can be found in the cytoplasm and within the nucleus. [Isoform 8]: Cell junction, focal adhesion {ECO:0000269|PubMed:22768332}. Note=In U2OS cells. {ECO:0000269|PubMed:22768332}.
DR  UNIPROT: Q8WXH0;
DR  UNIPROT: B4DND7;
DR  UNIPROT: B4DPR6;
DR  UNIPROT: I6XXQ5;
DR  UNIPROT: Q540G1;
DR  UNIPROT: Q86YP9;
DR  UNIPROT: Q8N1S3;
DR  UNIPROT: Q8NF49;
DR  UNIPROT: Q8TER7;
DR  UNIPROT: Q8WWW3;
DR  UNIPROT: Q8WWW4;
DR  UNIPROT: Q8WWW5;
DR  UNIPROT: Q8WXH1;
DR  UNIPROT: Q9NU50;
DR  UNIPROT: Q9UFQ4;
DR  UNIPROT: Q9Y2L4;
DR  UNIPROT: Q9Y4R1;
DR  PDB: 4DXS;
DR  PDB: 4FI9;
DR  PDB: 6XF1;
DR  Pfam: PF00307;
DR  Pfam: PF10541;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS51049;
DR  OMIM: 608442;
DR  OMIM: 612999;
DR  DisGeNET: 23224;
DE  Function: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. May be involved in nucleus-centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probable association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 may act redundantly. During INM at G1 phase mediates respective LINC complex association with kinesin to push the nucleus away from the centrosome. Involved in nuclear migration in retinal photoreceptor progenitors. Required for centrosome migration to the apical cell surface during early ciliogenesis. {ECO:0000250|UniProtKB:Q6ZWQ0, ECO:0000269|PubMed:12118075, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:22945352}.
DE  Disease: Emery-Dreifuss muscular dystrophy 5, autosomal dominant (EDMD5) [MIM:612999]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:17761684}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O08579; IntAct: EBI-10760623; Score: 0.27
DE  Interaction: O94901; IntAct: EBI-6163348; Score: 0.52
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-22056370; Score: 0.46
DE  Interaction: P29991; IntAct: EBI-8828465; Score: 0.37
DE  Interaction: P50402; IntAct: EBI-10760372; Score: 0.58
DE  Interaction: Q5VYV7; IntAct: EBI-2372193; Score: 0.35
DE  Interaction: Q13387; IntAct: EBI-7240621; Score: 0.37
DE  Interaction: Q9UKG1; IntAct: EBI-5357640; Score: 0.45
DE  Interaction: Q8IZP0; IntAct: EBI-5652826; Score: 0.00
DE  Interaction: Q9UH99; IntAct: EBI-6163111; Score: 0.77
DE  Interaction: Q96DB2; IntAct: EBI-6598272; Score: 0.35
DE  Interaction: Q9D666; IntAct: EBI-6838672; Score: 0.40
DE  Interaction: Q16543; IntAct: EBI-9393294; Score: 0.35
DE  Interaction: Q9NWT6; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q7Z569; IntAct: EBI-10818497; Score: 0.37
DE  Interaction: Q8VC57; IntAct: EBI-11009211; Score: 0.35
DE  Interaction: Q9WTX6; IntAct: EBI-11016744; Score: 0.35
DE  Interaction: O43172; IntAct: EBI-11043099; Score: 0.35
DE  Interaction: Q14149; IntAct: EBI-11090117; Score: 0.35
DE  Interaction: Q5TBB1; IntAct: EBI-11114337; Score: 0.35
DE  Interaction: Q9D7F7; IntAct: EBI-11116442; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-11117231; Score: 0.35
DE  Interaction: O00267; IntAct: EBI-11133933; Score: 0.35
DE  Interaction: Q8TBP0; IntAct: EBI-11136055; Score: 0.35
DE  Interaction: P32121; IntAct: EBI-11137291; Score: 0.35
DE  Interaction: P26447; IntAct: EBI-11158347; Score: 0.35
DE  Interaction: P49286; IntAct: EBI-11577659; Score: 0.00
DE  Interaction: Q6FHY5; IntAct: EBI-24509410; Score: 0.56
DE  Interaction: P56945; IntAct: EBI-15100330; Score: 0.35
DE  Interaction: Q9Y6Q1; IntAct: EBI-21501330; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-21550215; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q5SW79; IntAct: EBI-21644990; Score: 0.35
DE  Interaction: Q5ZSD5; IntAct: EBI-15625545; Score: 0.37
DE  Interaction: Q9Y613; IntAct: EBI-16108598; Score: 0.58
DE  Interaction: P11021; IntAct: EBI-20902264; Score: 0.40
DE  Interaction: Q14696; IntAct: EBI-20909040; Score: 0.40
DE  Interaction: Q86Y22; IntAct: EBI-20918068; Score: 0.40
DE  Interaction: O00186; IntAct: EBI-20921444; Score: 0.40
DE  Interaction: P78527; IntAct: EBI-20925778; Score: 0.40
DE  Interaction: P62424; IntAct: EBI-20933676; Score: 0.40
DE  Interaction: P06748; IntAct: EBI-20933828; Score: 0.40
DE  Interaction: P54253; IntAct: EBI-21132804; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21375215; Score: 0.00
DE  Interaction: Q8TDR0; IntAct: EBI-21375200; Score: 0.00
DE  Interaction: Q9UKE5; IntAct: EBI-21375185; Score: 0.00
DE  Interaction: Q96MT8; IntAct: EBI-21375252; Score: 0.00
DE  Interaction: Q9NV70; IntAct: EBI-21375239; Score: 0.00
DE  Interaction: P10636; IntAct: EBI-21375227; Score: 0.00
DE  Interaction: Q99459; IntAct: EBI-21375291; Score: 0.00
DE  Interaction: O60239; IntAct: EBI-21375278; Score: 0.00
DE  Interaction: Q9GZM8; IntAct: EBI-21375265; Score: 0.00
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q13547; IntAct: EBI-26367383; Score: 0.35
DE  Interaction: Q15884; IntAct: EBI-27118879; Score: 0.37
DE  Interaction: P42566; IntAct: EBI-30823440; Score: 0.44
DE  Interaction: Q13257; IntAct: EBI-30825992; Score: 0.44
DE  Interaction: Q00987; IntAct: EBI-30831706; Score: 0.44
DE  Interaction: Q93009; IntAct: EBI-30843705; Score: 0.44
DE  Interaction: P14652; IntAct: EBI-28997321; Score: 0.35
DE  Interaction: P40763; IntAct: EBI-29000558; Score: 0.35
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0031527;
GO  GO:0005925;
GO  GO:0016021;
GO  GO:0045111;
GO  GO:0031258;
GO  GO:0034993;
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0031981;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016529;
GO  GO:0033017;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0140444;
GO  GO:0051642;
GO  GO:0007097;
GO  GO:0031022;
GO  GO:0021817;
GO  GO:0030335;
GO  GO:1902017;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MASSPELPTEDEQGSWGIDDLHISLQAEQEDTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLP
SQ  RDKGSNTFQCRINIEHALTFLRNRSIKLINIHVTDIIDGNPSIILGLIWTIILHFHIEKLAQTLSCNYNQPSLDDVSVVD
SQ  SSPASSPPAKKCSKVQARWQMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKD
SQ  NLREAFRIAEQELKIPRLLEPEDVDVVDPDEKSIMTYVAQFLQYSKDAPGTGEEAQGKVKDAMGWLTLQKEKLQKLLKDS
SQ  ENDTYFKKYNSLLSFMESFNEEKKSFLDVLSIKRDLDELDKDHLQLREAWDGLDHQINAWKIKLNYALPPPLHQTEAWLQ
SQ  EVEELMDEDLSASQDHSQAVTLIQEKMTLFKSLMDRFEHHSNILLTFENKDENHLPLVPPNKLEEMKRRINNILEKKFIL
SQ  LLEFHYYKCLVLGLVDEVKSKLDIWNIKYGSRESVELLLEDWHKFIEEKEFLARLDTSFQKCGEIYKNLAGECQNINKQY
SQ  MMVKSDVCMYRKNIYNVKSTLQKVLACWATYVENLRLLRACFEETKKEEIKEVPFETLAQWNLEHATLNEAGNFLVEVSN
SQ  DVVGSSISKELRRLNKRWRKLVSKTQLEMNLPLMIKKQDQPTFDNSGNILSKEEKATVEFSTDMSVELPENYNQNIKAGE
SQ  KHEKENEEFTGQLKVAKDVEKLIGQVEIWEAEAKSVLDQDDVDTSMEESLKHLIAKGSMFDELMARSEDMLQMDIQNISS
SQ  QESFQHVLTTGLQAKIQEAKEKVQINVVKLIAALKNLTDVSPDLDIRLKMEESQKELESYMMRAQQLLGQRESPGELISK
SQ  HKEALIISNTKSLAKYLKAVEELKNNVTEDIKMSLEEKSRDVCAKWESLHHELSLYVQQLKIDIEKGKLSDNILKLEKQI
SQ  NKEKKLIRRGRTKGLIKEHEACFSEEGCLYQLNHHMEVLRELCEELPSQKSQQEVKRLLKDYEQKIERLLKCASEIHMTL
SQ  QPTAGGTSKNEGTITTSENRGGDPHSEAPFAKSDNQPSTEKAMEPTMKFSLASVLRPLQEESIMEKDYSASINSLLERYD
SQ  TYRDILEHHLQNNKFRITSDFSSEEDRSSSCLQAKLTDLQVIKNETDARWKEFEIISLKLENHVNDIKKPFVIKERDTLK
SQ  ERERELQMTLNTRMESLETALRLVLPVEKASLLLCGSDLPLHKMAIQGFHLIDADRIYQHLRNIQDSIAKQIEICNRLEE
SQ  PGNFVLKELHPFDLHAMQNIILKYKTQFEGMNHRVQRSEDTLKALEDFLASLRTAKLSAEPVTDLSASDTQVAQENTLTV
SQ  KNKEGEIHLMKDKAKHLDKCLKMLDMSFKDAERGDDTSCENLLDAFSIKLSETHGYGVQEEFTEENKLLEACIFKNNELL
SQ  KNIQDVQSQISKIGLKDPTVPAVKHRKKSLIRLDKVLDEYEEEKRHLQEMANSLPHFKDGREKTVNQQCQNTVVLWENTK
SQ  ALVTECLEQCGRVLELLKQYQNFKSILTTLIQKEESVISLQASYMGKENLKKRIAEIEIVKEEFNEHLEVVDKINQVCKN
SQ  LQFYLNKMKTFEEPPFEKEANIIVDRWLDINEKTEDYYENLGRALALWDKLFNLKNVIDEWTEKALQKMELHQLTEEDRE
SQ  RLKEELQVHEQKTSEFSRRVAEIQFLLQSSEIPLELQVMESSILNKMEHVQKCLTGESNCHALSGSTAELREDLDQAKTQ
SQ  IGMTESLLKALSPSDSLEIFTKLEEIQQQILQQKHSMILLENQIGCLTPELSELKKQYESVSDLFNTKKSVLQDHFSKLL
SQ  NDQCKNFNDWFSNIKVNLKECFESSETKKSVEQKLQKLSDFLTLEGRNSKIKQVDSVLKHVKKHLPKAHVKELISWLVGQ
SQ  EFELEKMESICQARAKELEDSLQQLLRLQDDHRNLRKWLTNQEEKWKGMEEPGEKTELFCQALARKREQFESVAQLNNSL
SQ  KEYGFTEEEEIIMEATCLMDRYQTLLRQLSEIEEEDKLLPTEDQSFNDLAHDVIHWIKEIKESLMVLNSSEGKMPLEERI
SQ  QKIKEIILLKPEGDARIETIMKQAESSEAPLVQKTLTDISNQWDNTLHLASTYLSHQEKLLLEGEKYLQSKEDLRLMLIE
SQ  LKKKQEAGFALQHGLQEKKAQLKIYKKFLKKAQDLTSLLKELKSQGNYLLECTKNPSFSEEPWLEIKHLHESLLQQLQDS
SQ  VQNLDGHVREHDSYQVCVTDLNTTLDNFSKEFVSFSDKPVDQIAVEEKLQKLQELENRLSLQDGTLKKILALAKSVKQNT
SQ  SSVGQKIIKDDIKSLQCKQKDLENRLASAKQEMECCLNSILKSKRSTEKKGKFTLPGREKQATSDVQESTQESAAVEKLE
SQ  EDWEINKDSAVEMAMSKQLSLNAQESMKNTEDERKVNELQNQPLELDTMLRNEQLEEIEKLYTQLEAKKAAIKPLEQTEC
SQ  LNKTETGALVLHNIGYSAQHLDNLLQALITLKKNKESQYCVLRDFQEYLAAVESSMKALLTDKESLKVGPLDSVTYLDKI
SQ  KKFIASIEKEKDSLGNLKIKWENLSNHVTDMDKKLLESQIKQLEHGWEQVEQQIQKKYSQQVVEYDEFTTLMNKVQDTEI
SQ  SLQQQQQHLQLRLKSPEERAGNQSMIALTTDLQATKHGFSVLKGQAELQMKRIWGEKEKKNLEDGINNLKKQWETLEPLH
SQ  LEAENQIKKCDIRNKMKETILWAKNLLGELNPSIPLLPDDILSQIRKCKVTHDGILARQQSVESLAEEVKDKVPSLTTYE
SQ  GSDLNNTLEDLRNQYQMLVLKSTQRSQQLEFKLEERSNFFAIIRKFQLMVQESETLIIPRVETAATEAELKHHHVTLEAS
SQ  QKELQEIDSGISTHLQELTNIYEELNVFERLFLEDQLKNLKIRTNRIQRFIQNTCNEVEHKIKFCRQFHEKTSALQEEAD
SQ  SIQRNELLLNQEVNKGVKEEIYNLKDRLTAIKCCILQVLKLKKVFDYIGLNWDFSQLDQLQTQVFEKEKELEEKIKQLDT
SQ  FEEEHGKYQALLSKMRAIDLQIKKMTEVVLKAPDSSPESRRLNAQILSQRIEKAKCLCDEIIKKLNENKTFDDSFKEKEI
SQ  LQIKLNAEENDKLYKVLQNMVLELSPKELDEKNCQDKLETSLHVLNQIKSQLQQPLLINLEIKHIQNEKDNCEAFQEQVW
SQ  AEMCSIKAVTAIEKQREENSSEASDVETKLREFEDLQMQLNTSIDLRTNVLNDAYENLTRYKEAVTRAVESITSLEAIII
SQ  PYRVDVGNPEESLEMPLRKQEELESTVAHIQDLTEKLGMISSPEAKLQLQYTLQELVSKNSAMKEAFKAQETEAERYLEN
SQ  YKCYRKMEEDIYTNLSKMETVLGQSMSSLPLSYREALERLEQSKALVSNLISTKEELMKLRQILRLLRLRCTENDGICLL
SQ  KIVSALWEKWLSLLEAAKEWEMWCEELKQEWKFVSEEIEREAIILDNLQEELPEISKTKEAATTEELSELLDCLCQYGEN
SQ  VEKQQLLLTLLLQRIRSIQNVPESSGAVETVPAFQEITSMKERCNKLLQKVQKNKELVQTEIQERHSFTKEIIALKNFFQ
SQ  QTTTSFQNMAFQDHPEKSEQFEELQSILKKGKLTFENIMEKLRIKYSEMYTIVPAEIESQVEECRKALEDIDEKISNEVL
SQ  KSSPSYAMRRKIEEINNGLHNVEKMLQQKSKNIEKAQEIQKKMWDELDLWHSKLNELDSEVQDIVEQDPGQAQEWMDNLM
SQ  IPFQQYQQVSQRAECRTSQLNKATVKMEEYSDLLKSTEAWIENTSHLLANPADYDSLRTLSHHASTVQMALEDSEQKHNL
SQ  LHSIFMDLEDLSIIFETDELTQSIQELSNQVTALQQKIMESLPQIQRMADDVVAIESEVKSMEKRVSKIKTILLSKEIFD
SQ  FSPEEHLKHGEVILENIRPMKKTIAEIVSYQVELRLPQTGMKPLPVFQRTNQLLQDIKLLENVTQEQNELLKVVIKQTNE
SQ  WDEEIENLKQILNNYSAQFSLEHMSPDQADKLPQLQGEIERMEKQILSLNQRKEDLLVDLKATVLNLHQHLKQEQEGVER
SQ  DRLPAVTSEEGGVAERDASERKLNRRGSMSYLAAVEEEVEESSVKSDNGDEKAEPSPQSWSSLWKHDKDMEEDRASSSSG
SQ  TIVQEAYGKISTSDNSMAQILTPDSLNTEQGPECSLRPNQTEEGTTPPIEADTLDSSDAQGGLEPRVEKTRPEPTEVLHA
SQ  CKTQVAELELWLQQANVAVEPETLNADMQQVLEQQLVGCQAMLTEIEHKVAFLLETCKDQGLGDNGATQHEAEALSLKLK
SQ  TVKCNLEKVQMMLQEKHSEDQHPTILKKSSEPEHQEALQPVNLSELESIVTERPQFSRQKDFQQQQVLELKPMEQKDFIK
SQ  FIEFNAKKMWPQYCQHDNDTTQESSASNQASSPENDVPDSILSPQGQNGDKWQYLHHELSSKIKLPLPQLVEPQVSTNMG
SQ  ILPSVTMYNFRYPTTEELKTYTTQLEDLRQEASNLQTQENMTEEAYINLDKKLFELFLTLSQCLSSVEEMLEMPRLYRED
SQ  GSGQQVHYETLALELKKLYLALSDKKGDLLKAMTWPGENTNLLLECFDNLQVCLEHTQAAAVCRSKSLKAGLDYNRSYQN
SQ  EIKRLYHQLIKSKTSLQQSLNEISGQSVAEQLQKADAYTVELENAESRVAKLRDEGERLHLPYALLQEVYKLEDVLDSMW
SQ  GMLRARYTELSSPFVTESQQDALLQGMVELVKIGKEKLAHGHLKQTKSKVALQAQIENHKVFFQKLVADMLLIQAYSAKI
SQ  LPSLLQNRETFWAEQVTEVKILEEKSRQCGMKLQSLLQKWEEFDENYASLEKDLEILISTLPSVSLVEETEERLVERISF
SQ  YQQIKRNIGGKHARLYQTLNEGKQLVASVSCPELEGQIAKLEEQWLSLNKKIDHELHRLQALLKHLLSYNRDSDQLTKWL
SQ  ESSQHTLNYWKEQSLNVSQDLDTIRSNINNFFEFSKEVDEKSSLKTAVISIGNQLLHLKETDTATLRASLAQFEQKWTML
SQ  ITQLPDIQEKLHQLQMEKLPSRKAITEMISWMNNVEHQTSDEDSVHSPSSASQVKHLLQKHKEFRMEMDYKQWIVDFVNQ
SQ  SLLQLSTCDVESKRYERTEFAEHLGEMNRQWHRVHGMLNRKIQHLEQLLESITESENKIQILNNWLEAQEERLKTLQKPE
SQ  SVISVQKLLLDCQDIENQLAIKSKALDELKQSYLTLESGAVPLLEDTASRIDELFQKRSSVLTQVNQLKTSMQSVLQEWK
SQ  IYDQLYDEVNMMTIRFWYCMEHSKPVVLSLETLRCQVENLQSLQDEAESSEGSWEKLQEVIGKLKGLCPSVAEIIEEKCQ
SQ  NTHKRWTQVNQAIADQLQKAQSLLQLWKAYSNAHGEAAARLKQQEAKFQQLANISMSGNNLAEILPPALQDIKELQHDVQ
SQ  KTKEAFLQNSSVLDRLPQPAESSTHMLLPGPLHSLQRAAYLEKMLLVKANEFEFVLSQFKDFGVRLESLKGLIMHEEENL
SQ  DRLHQQEKENPDSFLNHVLALTAQSPDIEHLNEVSLKLPLSDVAVKTLQNMNRQWIRATATALERCSELQGIGLNEKFLY
SQ  CCEKWIQLLEKIEEALKVDVANSLPELLEQQKTYKMLEAEVSINQTIADSYVTQSLQLLDTTEIENRPEFITEFSKLTDR
SQ  WQNAVQGVRQRKGDVDGLVRQWQDFTTSVENLFRFLTDTSHLLSAVKGQERFSLYQTRSLIHELKNKEIHFQRRRTTCAL
SQ  TLEAGEKLLLTTDLKTKESVGRRISQLQDSWKDMEPQLAEMIKQFQSTVETWDQCEKKIKELKSRLQVLKAQSEDPLPEL
SQ  HEDLHNEKELIKELEQSLASWTQNLKELQTMKADLTRHVLVEDVMVLKEQIEHLHRQWEDLCLRVAIRKQEIEDRLNTWV
SQ  VFNEKNKELCAWLVQMENKVLQTADISIEEMIEKLQKDCMEEINLFSENKLQLKQMGDQLIKASNKSRAAEIDDKLNKIN
SQ  DRWQHLFDVIGSRVKKLKETFAFIQQLDKNMSNLRTWLARIESELSKPVVYDVCDDQEIQKRLAEQQDLQRDIEQHSAGV
SQ  ESVFNICDVLLHDSDACANETECDSIQQTTRSLDRRWRNICAMSMERRMKIEETWRLWQKFLDDYSRFEDWLKSAERTAA
SQ  CPNSSEVLYTSAKEELKRFEAFQRQIHERLTQLELINKQYRRLARENRTDTASRLKQMVHEGNQRWDNLQRRVTAVLRRL
SQ  RHFTNQREEFEGTRESILVWLTEMDLQLTNVEHFSESDADDKMRQLNGFQQEITLNTNKIDQLIVFGEQLIQKSEPLDAV
SQ  LIEDELEELHRYCQEVFGRVSRFHRRLTSCTPGLEDEKEASENETDMEDPREIQTDSWRKRGESEEPSSPQSLCHLVAPG
SQ  HERSGCETPVSVDSIPLEWDHTGDVGGSSSHEEDEEGPYYSALSGKSISDGHSWHVPDSPSCPEHHYKQMEGDRNVPPVP
SQ  PASSTPYKPPYGKLLLPPGTDGGKEGPRVLNGNPQQEDGGLAGITEQQSGAFDRWEMIQAQELHNKLKIKQNLQQLNSDI
SQ  SAITTWLKKTEAELEMLKMAKPPSDIQEIELRVKRLQEILKAFDTYKALVVSVNVSSKEFLQTESPESTELQSRLRQLSL
SQ  LWEAAQGAVDSWRGGLRQSLMQCQDFHQLSQNLLLWLASAKNRRQKAHVTDPKADPRALLECRRELMQLEKELVERQPQV
SQ  DMLQEISNSLLIKGHGEDCIEAEEKVHVIEKKLKQLREQVSQDLMALQGTQNPASPLPSFDEVDSGDQPPATSVPAPRAK
SQ  QFRAVRTTEGEEETESRVPGSTRPQRSFLSRVVRAALPLQLLLLLLLLLACLLPSSEEDYSCTQANNFARSFYPMLRYTN
SQ  GPPPT
//
ID  Q6ZWQ0;
PN  Nesprin-2;
GN  Syne2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side. Sarcoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cell membrane; Single-pass membrane protein. Cytoplasm, cytoskeleton. Mitochondrion {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Different isoform patterns are found in the different compartments of the cell. The isoforms having the C-terminal transmembrane span can be found in several organellar membranes like the nuclear envelope, the sarcoplasmic reticulum of myoblasts, or the lamellipodia and focal adhesions at the cell membrane. The largest part of the outer nuclear membrane-associated protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. Remains associated with the nuclear envelope during its breakdown in mitotic cells. Shorter soluble isoforms can be found in the cytoplasm and within the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q6ZWQ0;
DR  UNIPROT: Q640M5;
DR  Pfam: PF00307;
DR  Pfam: PF10541;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS51049;
DE  Function: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. May be involved in nucleus-centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probable association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 seem to act redundantly in cerebellum, midbrain, brain stem, and other brain regions except cerebral cortex and hippocampus. During INM at G1 phase mediates respective LINC complex association with kinesin to push the nucleus away from the centrosome. Involved in nuclear migration in retinal photoreceptor progenitors. Required for centrosome migration to the apical cell surface during early ciliogenesis. {ECO:0000250|UniProtKB:Q8WXH0, ECO:0000269|PubMed:18477613, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:21177258, ECO:0000269|PubMed:23071752}.
DE  Reference Proteome: Yes;
DE  Interaction: A2A8U2; IntAct: EBI-12596297; Score: 0.27
DE  Interaction: Q8BJS4; IntAct: EBI-16189259; Score: 0.53
DE  Interaction: Q9Y613; IntAct: EBI-16108642; Score: 0.51
DE  Interaction: Q4U2R1; IntAct: EBI-16730475; Score: 0.35
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
DE  Interaction: Q80YT7; IntAct: EBI-16732484; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: P97493; IntAct: EBI-26500450; Score: 0.35
GO  GO:0005737;
GO  GO:0031527;
GO  GO:0005925;
GO  GO:0016021;
GO  GO:0045111;
GO  GO:0031258;
GO  GO:0034993;
GO  GO:0005739;
GO  GO:0030016;
GO  GO:0005635;
GO  GO:0031981;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0016529;
GO  GO:0033017;
GO  GO:0030018;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0140444;
GO  GO:0051642;
GO  GO:0007097;
GO  GO:0031022;
GO  GO:0021817;
GO  GO:0030335;
GO  GO:1902017;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MAASPVLPTEDGEGFLGIDDLHFSLQAEQEDTQKKTFTCWINSQLAKHTPPSVVSDLFADIKKGHVLLDLLEVLSGQQLP
SQ  RDKGSNTFQCRINIEHALTFLKNRSIKLINIHVADIVEGNPSIILGLIWTIILHFHIEKLAQTLSCDYNQPSPEVVSVAA
SQ  SSPTSSPPTKKCSKAQAQARWQWSAKKALLQWAQEQCARSESVNVTDFKSSWRNGMAFLAVIHALRPDLIDMDSMRHRSN
SQ  KDNLKEAFRIAEHELKIPKLLEPEDVDVVNPDEKSIMTYVAQFLKYSKDAPGPGDSTQAKVRDALVWLTLQEKRFQKMLK
SQ  DSASETYCNKYHSLLSFMESLNEEKESFIDVLSLKGRMGELNEDESRLRQGWTSLMHQVAAWRAQLDDALPSPLKETEAW
SQ  LKDIEGVVQEGVPTSQSYSEARTLIQGKLSSFKSLMGSFDYHSDVLMAFQSNAEKSLPAVPPVKLEEMTRRINNVLGKNF
SQ  IPLLEFHDSKCSVLALLDEAKAKLDVWNGTYESKESVEVLLEDWHKFTGEKKFLIQLDASFQKCEEMYKNSARECESIRE
SQ  EYMMLEKNVHSCRQYIHNTKATLQRALMSWATFEEDLALLKASFDLTKKEQIKEVPVETLLQWNTKHTSLNEVGSFLIGV
SQ  SSREVAASISKELRRLNKRWRKFITKTPLLKLPLVKIQDQPPGNSSGTSLSKESAMAAEPGGSRGEDVKAAEKQEVEDEE
SQ  SAGQLKVNEEVEGLIKQVTIWESQTKSILDLLQHGDHADGSSADTLQHLIAKGSVYEELLARTEDTLQMDVQSPSNLEPF
SQ  QNVLRAGLQAKIQEAKQGVQITMVELSAVLKNLSDEPLELDLGLKVEEAQKELEVSILRAEQLLGQRERPGGFLLKYKEA
SQ  LEILNTNSLAKYLRAVEELKRTVPGGAKLQLEEQSRVASAKWEPLRHEISLYLQQLKIAIEEEKLRDNIARLEKQINKEK
SQ  KLIRRGRTRGLRKEHEACLSPESIKCQLEHHVGVLRVLCEELTSPEDQQELKRALRDYEQKIARLLKCASEIHTTLQSSQ
SQ  GGALEERSALITTENGRRDADGEVPLEIPDNQLSTEKAMEPIKNFSQTSELKPQQEESIMEKEGKDCSASLSDLQERYDT
SQ  QRGLLEQHLQDSKSRVTSDFASEQERSSACLQSKLAELQVLLADTDAHWEKFEITSLNLRRLMSDAEKPVLNQERDLLKG
SQ  NEQVLHGLLNTRMESLEMALQIVLPLEKECSLLCASDLPLCTVAVQDLHPVEIDGVYQNLRDIRDSIAKQIRVCTSLEEP
SQ  SNSVPRELHTLDQCAIQDIVLKCRLQLETMNQKVEMREDALDALEGFLASLRAAKLSAELPADRPAPKAPEVLSEDILLM
SQ  KEKAGPLDERLRTLGINIKDAEGGENTTCERLVGALSVNLVAMDGQSKEEGPPEDKKLLEACSSKNLELFKNIQDLQNQI
SQ  SKIGLKDPTAPAVKHRKKSLLRLDKDLDGLEEEKVRIQKIAGSLPRFKDGSEKNVIQQCEDTAALWESTKASVTESLEQC
SQ  GSALELLRQYQNIKNNLTALIQKEEGIISQQASYMGKDNLKKKIAEIETVKEEFSDHLEVVDKINQICKNLQYHLNKMKT
SQ  FEDPPFEKEANAIVDRWLDINEKTEEYGENLGRALALWDKLFIIKNNIDEWTEQILGKAESHELTEEDRGRLKEELKVLE
SQ  EQSAEFSRRVADIQSLLQSNEKPLELQVMESSVLSKMKDVKTHVAGGSNSYAPSGSTAELREDLDQAKTQMGMTESLLNA
SQ  LSPSDSLEIFTKLEEIQQQIFQQKHSMTVLENQIGCLTPELSELKRQYASVSNLFNTKKNALQDHFATFLNEQCKNFNDW
SQ  FSNVKTNLQECFEPPETKLSLEQRLQKLSDFLTLGGGNSKIQQVETVLQHVKMLLPKAHVKELDSWLRSQELELENMESI
SQ  CQARAGELNNSFQQLLRLEDDCRSLSKWLTNQEENWGKMEVSGERMDLFSQALTRKREQFETVAQLSDSLKEHGLTEGEE
SQ  TIKESTHLIDRYQALWRQLHEIEEEDKLPAAEDQSFNDLADDVIHWIKEIKESLMALNSSEGKMPLEERIQKIKEIIALK
SQ  PEGDAKIQMVMRQAEHCEAPLAQETFTDLSNQWDSTLHLANTYLSHQEKLVLEGEKYLQSKEDLRLMLTELKKQQEAGFA
SQ  LQPGLPEKQAQLKIYKKFLQKAQDLTSLLEELKSQGNYLLECTKNPSFSEEPWLEVKHLHESLLQQLQDSVQKLEGHVQE
SQ  HSSYQVCLTDLSSTLDDISKEYFSLCDGSKDQIMAKERMQKLQELESRLRFQGGALKKASALAKSIKQNTSSVGQKIIKD
SQ  DIRSLKYKQKDLENRIESAKQETENGLNSILKSKSSTEKHVKFSLPVEEMPATSEVPKPTRESAAVGESGGARETNTNSA
SQ  VEMILSKQLSLNVQESMQNAQDEREVNELQNQPLELDIMLRNEQLKGMEELSTHLEARRAAIELLEQSQHLNQTEEQALV
SQ  LPAARPSVCHLGSLQQELHTLKKTKERQYGLLSGFQDQLVMAEASLNTSLAEVESLKIGSLDSATYLGKIKKFLGSVENQ
SQ  QGSLSKLRTEWAHLSSLLAAADQKLVESQMKHLEHGWELVEQLAHRKCFQQATEHSELTCLLEKLQDLKVSLHQQQQRLT
SQ  LSLNSPGQQAAIVDMVTPAAELQAIKCEFSGLKWQAELHMKRLWGEKDKKTLEDAINNLNKQMEALEPLNREVENRIKKC
SQ  ELQNRIKETLSWVKNTMAELVVPIALLPDNILSQIRKCKLIHDGILGNQQAVELLVEEVRGITPSLAPCEGDGLNALLED
SQ  LQSQHQALLLKSTERSQQLELKLEEKSKLFAIIGKVQLTLEESETLMSPTGDRASTEAELERRLAILKASQQQLQDTESA
SQ  LSAHLQELTNAYKDANVFERLFLDDQLKNLKARTNRTQRFLQNNGSELKQKMESYREFHDKAAVLQKEAECILHGGLLPL
SQ  RQELEQDAKEQLGNLRDKLAAIRGSLSQVLTSEEVFDTIGLSWDGSLLARLQTQVLEREREVEGKIKQLDTFLIARDRHQ
SQ  ASISKIRAVDLQIKKGAESLLKVPSMSPESTLLNAQTLIQKIEKSKRLRDEIIRKLSKNEAFDDSFKESEMQRLKLCAEE
SQ  NSRLQEALQNMLLELQPREMGEKEFREKLENALHVLKQIQSRLQQPLCVNLGVQHIQHEKETWEAFGEQVEAEMCGLRAV
SQ  RITEEQREENDSGTGGMEAKLRDIEGLHMELSKSISLRADVLNDAYDSANRYDELVAGALRIITSLEATLLSYRVDLHNP
SQ  QKTLELAHLKQEELQSSVADLRSLTETLGAISSPEAKEQLRCTLEVLAAKNSALKAGLEAQEAEEERCLENYKCFRKMKE
SQ  EICSRLRKMEMDLGQSIFPLPRSYKEALARLEQSKALTSNLLSTKEDLVKLRQLLRHLRCRSTENDATCALGVASALWEK
SQ  WLSLLEAAREWQQWGGELKREWKFISEEIEREAIILETLQEDLPEISKTNAAPTEELWQLLDSLCQHQESVEKQQLLLAL
SQ  LLQRVRSIQNIPEGTETGETIPALQEIGSMQERCDRLLHTTRKNKDLVQAEIQAQQSFLKEIKDVKRVFEQISTSFPNLA
SQ  PEGHPERAEQFEELRSILQKGKLSFENIMEKLRIKYSEMYSIVPAEIGSQVEECRSALEDAEEKMSSEVSKSSPSSIMRR
SQ  KIERINNGLHCVEKMLQQKSRNIEEAHEIQKKIWDELDLWHSKLNELDSEVQDFVEQDPGQAQEWMDNLMAPFQQHQQVS
SQ  QRAESRTSQLNKATIKMEEYNDLLKSTEVWIEKTSCLLANPACYDSSRTLSHRASTLQMALEDSEQKHSLLHSIFTDLED
SQ  LSIIFETDDLIQTIHELSDQVAALQQQIMEALPHVQQVADDVVAIESEVKAMEKKVAKIKAILLSKEIFDFPPEEHLKHG
SQ  EVILENIHPMKKTIAEIMTYQVELRLPQTGTKPLPVFQRTSQLLQDVKLLENVTQEQNELLKVVIKQTAECDEEIDSLKQ
SQ  MLTNYSAEISPEHVSQNQVADLPSLQGEMERLEKQILNLNQKKEDLLVDLKTAVLNLHEHLKQEQQEVGDKPSAGASECT
SQ  VAERDASERKLSRTNSMSFLPVVKEEAEESSVKSEDGRRRTEPPSASWSFLGKHSKDLEGDGASSSSSATIVQDADGRIS
SQ  TCDSSMVHIIAPDSGSTEEGPAPSPRLSQTDEGATPPIEAALLDFPREQGAFESTVERSRPRPADILRVCKTQVAKLELW
SQ  LQQANVAFEPETVDADMQQVVEEELAGCQAMLTEIEYKVASLLETCKDQGLGDCGTTQQEAEALSWKLKTVKCNLEKVQM
SQ  VLQEKFSEDQHPSTLKKPSEPHDVDQPAGLSELDSVLTERPQFSRQKDAPQPQILELKPSEQKDLIKFTELNAKKTWLQG
SQ  HQENEDANRQSASSSKVPSPGNAASDSTLPLQAQSGDKWQYLHHELTSRPNPSVPQLVEPQVALTTSTLPSVSVYNFRCP
SQ  TADELQAYTTQLEELRQEANTIQTQGSMTEETYISLDKRLFELFLSLSRCLGSVEGLLQRPGLLREDACAQQVFFQKLAL
SQ  ELKKLYLALGDKKDDFLKAVTWPGKEATLLPECIDALTVSLESVQSRAAWRDASLKAGLEHSRSYQNEVKRLYSQLIKKK
SQ  TALQQSLNEISGQSISKQLQKADVHTAELQNSEKQVAKLRDEGERLRFPHGLLQDVYKLEDVLDSMWGILRARYLELSSP
SQ  FLSKSLQTLLQGMAELVSIGKGKLAADPLQHAKSKAALQAQLQDHKAFFQKLVADMLLIQTYSATMFPPSLQKGEGFGAE
SQ  QVAEVRALEEEACLRGAQLQSMLQKWEEFDDNYASLEKDLEALISSLPSVSLVEETEERLLERISFYQQIKRNIDGKHAR
SQ  LCQTLNEGRQLAASVSCPEPEGQIARLEEQWLSLNKRIDQELHRLQTLLKHLLSYSRDSDELTRWLETSQQTLNYWKEQS
SQ  LNVSQDLNTIRSNIDRFFKFSKEVDERSSLKSAVMSTGNQLLHLKEADTATLRASLAQFEQKWTVLITQLPDIQEKLHQL
SQ  QMEKLPSREAISEMISWMNAVEPQAAGKDTELSKSSASQVKHLLQKLKEFRMEMDYKQWVVDFVNQSLLQLSTCDVESKR
SQ  YERTEFAEHLGEMNRQWQRVHGTLNRKIQHLEQLLESITENENKVQNLNSWLEAQEERLKMLQKPESAVSMEKLLLDCQD
SQ  IENQLALKSKALDELRQSSLTMDGGDVPLLEDMASGIVELFQKKNNVTSQVHQLRASVQSVLQEWKACDKLYDEATMRTT
SQ  QLTYSMEHSKPAVLSLQALACQVQNLEALQDEAENGERSWEKLQEVIGRLKASCPSMAGIIEEKCQDAHSRWTQVNQDLA
SQ  DQLQEARGQLQLWKAPHNAHAEAAAWLQQQEAKFQQLANTNLSGDNLADILPRALKDIKGLQSDLQKTKEAFLENSTLSD
SQ  QLPQPEERSTPGLHSGQRHSLQTAAYLEKMLLAKSNEFEIVLAQFKDFTDRLAYSKDLIVHKEENLNKLYHEEKEEVPDL
SQ  FLNHVLALTAQSPDIERLNEESLRLPLSDVTIKTLQSLNRQWIRATATALDHYSELQGNGLNEKFLHYCERWIQVLEKIQ
SQ  ESLSVEVAHSLPALLEQQKTYEILEAEVSTNQAVADAYVTQSLQLLDTAEIEKRPEFVSEFSKLSDQWQRAARGVRQRKC
SQ  DISRLVTQWRFFTTSVEDLLRFLADTSQLLSAVKEQDCYSLCQTRRLVHELKSKEIHLQRWRTTYALALEAGEKLRNTPS
SQ  PETREFVDGQISRLQESWKDTELSLGEVISRLQSTAETWDQCKKKIKKLKKRLQALKAQSEDPLPELHEALHEEKELIKE
SQ  VEKSLANWTHSLKELQTMKADLSQHILAEDVTVLKEQIQLLHRQWEDLCLRVAIRKQEIEDRLNSWIVFNEKNKELCAWL
SQ  VQMENKVLQTADVSIEEMIEKLQKDCMEEISLFTENKLQLKQMGDQLIKASSKAKAAELEEKLSKINDRWQHLFDVIGSR
SQ  VKKLKETFAFIQQLDKNMSNLRTWLARIESELSKPVVYDVCDNQEIQKRLAEQQDLQRDIEQHSAGVESVFNICDVLLHD
SQ  SDACANETECDSIQQTTRSLDRRWRNICAMSMERRMKIEETWRLWQKFLDDYSRFEDWLKSAERTAACPNSSEVLYTNAK
SQ  EELKRFEAFQRQIHERLTQLELINKQYRRLARENRTDTASKLKQMVHEGNQRWDNLQKRVTAILRRLRYFTNQREEFEGT
SQ  RESILVWLTEMDLQLTNVEHFSESDAEDKMRQLNGFQQEITLNTNKIDQLIVFGEQLIQKSEPLDAVLIEDELEELHRYC
SQ  QEVFGRVSRFHRRLTSHTPGLDDEKEASENETDIEDPREIQADSWRKRRESEEPTSPQSLCHLVPPALGHERSGCETPVS
SQ  VDSIPLEWDHTGDVGGSSSHEDDEEGPFYSALSGKSISEGHPWHVPDSPSHSKHHYKHMEGDRTEAPVPTDASTPFKSDY
SQ  VKLLLRQGTDDSKEGLKEAQQEDEQLATLTGQQPGAFDRWELIQAQELHSKLRLKQTVQQLKSDIGSIAAWLGKTEAELE
SQ  ALKLAEPPSDIQEIALRVKRLQEILKAFDTYKALMVSVNVSHKEYLPSQSPEATELQNRLHQLSLSWDSVQGVLDSWRGD
SQ  LRQSLMQCQDFHQLSQDLLLWLATAESRRQKAHVTSPEADRQVLLECQKDLMRLEKELVARQPQVSSLREISSSLLVKGQ
SQ  GEDYIEAEEKVHVIEKKLKQLQEQVAQDLMSLQRSLDPDASLTSFDEVDSGEQLPAAFAKSPRPRWTFLEEEEEEEETDS
SQ  RMPHLDSPGSSQPRRSFLSRVIRAALPLQLLLLLLLLLACLLPASEDDYSCTQANNFARSFYPMLRYTNGPPPT
//
ID  Q6ZMZ3;
PN  Nesprin-3;
GN  SYNE3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:21937718}; Single-pass type IV membrane protein {ECO:0000269|PubMed:21937718}. Nucleus envelope {ECO:0000269|PubMed:21937718}. Rough endoplasmic reticulum {ECO:0000250}.
DR  UNIPROT: Q6ZMZ3;
DR  UNIPROT: A6H8H3;
DR  UNIPROT: Q86SX5;
DR  UNIPROT: Q8N7G8;
DR  PDB: 6WME;
DR  Pfam: PF10541;
DR  Pfam: PF00435;
DR  PROSITE: PS51049;
DR  OMIM: 610861;
DR  DisGeNET: 161176;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells. {ECO:0000269|PubMed:16330710, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:21937718}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6ZWR6; IntAct: EBI-10760858; Score: 0.51
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005791;
GO  GO:0051015;
GO  GO:0140444;
GO  GO:0007010;
GO  GO:0090150;
GO  GO:0007097;
GO  GO:0008360;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MTQQPQDDFDRSVEDAQAWMKAVQDQLQVNDNTQGPRAALEARLWETEKICQLEPEGRVRVDLVLRMAEALLACCPGDQK
SQ  PGILARLKDIKAQWEETVTYMTHCHSRIEWVWLHWSEYLLARDEFYRWFQKMMVTLEPHIELQLGLKEKQWQLSHAQVLL
SQ  HNVDNQAVLLDRLLEEAASLFNRIGDPSVDEDAQKRMKAEYDAVKAKAQKRVDLLEQVAREHEEYQAGVDEFQLWLKAVV
SQ  EKVNGCLGRNCKLPITQRLSTLQDIAKDFPRGEESLETLEEQSAGVIRNTSPLGAEKITGELEEMRKVLEKLRALWEEEE
SQ  ERLRGLLRSRGAWEQQIKQLEAELSEFRMVLQRLAQEGLQPAAKAGTEDELVAHWRRYSATRAALASEEPRVDRLQAQLK
SQ  ELIVFPHNLKPLSDSVIATIQEYQSLKVKSARLRNAAAVELWQHFQRPLQDLQLWKALAQRLLEVTASLPDLPSLHTFLP
SQ  QIEAALMESSRLKELLTMLQLKKDLLIGIFGQERATALLEQVAGSMRDRDLLHNSLLQRKSKLQSLLAQHKDFGAAFEPL
SQ  QRKLLDLQVRVQAEKGLQRDLPGKQAQLSRLQGLQEEGLDLGAQMEAARPLVQENPNHQHKMDQLSSDFQALQRSLEDLV
SQ  DRCRQSVQEHCTFSHQLLELRQWIVVTTQKLEAHRGEAGPGDAESQEAEFERLVAEFPEKEAQLSLVEAQGWLVMEKSSP
SQ  EGAAVVQEELRELAESWRALRLLEESLLSLIRNWHLQRMEVDSGKKMVFTNNIPKSGFLINPMDPIPRHRRRANLLQEEE
SQ  GSHEDFSQLLRNFGQWLQVENSKLVRIIAMRTSTAEDLRTRKSKLQELEARVPEGQHLFENLLRLGPARGTSDELEDLRY
SQ  QWMLYKSKLKDSGHLLTQSSPGEPTGFQKTRRWRGLGSLFRRACCVALPLQLLLLLFLLLLFLLPIREEDRSCTLANNFA
SQ  RSFTLMLRYNGPPPT
//
ID  Q4FZC9;
PN  Nesprin-3;
GN  Syne3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane; Single-pass type IV membrane protein. Nucleus envelope. Rough endoplasmic reticulum.
DR  UNIPROT: Q4FZC9;
DR  UNIPROT: Q8BMM1;
DR  UNIPROT: Q8C117;
DR  Pfam: PF10541;
DR  Pfam: PF00435;
DR  PROSITE: PS51049;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:16330710}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9D666; IntAct: EBI-12557085; Score: 0.57
DE  Interaction: Q5SS91; IntAct: EBI-12557132; Score: 0.40
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0034993;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005791;
GO  GO:0051015;
GO  GO:0140444;
GO  GO:0007010;
GO  GO:0090150;
GO  GO:0007097;
GO  GO:0008360;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MTQQPQEDFERSVEDAQAWMKVIQEQLQVNDNTKGPRAALEARLRETEKICQLESEGMVKVELVLRAAEALLATCQEGQK
SQ  PEILARLRDIKSQWEETVTYMTHCHSRIEWVWLHWSEYLLAQDEFYRWFQKMVVALEPPVELQLGLKEKQWQLSHAQVLL
SQ  HNVDNQAVLLDRLLEEAGSLFSRIGDPSVDEDAQKRMKAEYDAVKARAQRRVDLLAQVAQDHEQYREDVNEFQLWLKAVV
SQ  EKVHSCLGRNCKLATELRLSTLQDIAKDFPRGEESLKRLEEQAVGVIQNTSPLGAEKISGELEEMRGVLEKLRVLWKEEE
SQ  GRLRGLLQSRGDCEQQIQQLEAELGDFKKSLQRLAQEGLEPTVKTATEDELVAQWRLFSGTRAALASEEPRVDRLQTQLK
SQ  KLVTFPDLQSLSDSVVATIQEYQSMKGKNTRLHNATRAELWQRFQRPLNDLQLWKALAQRLLDITASLPDLASIHTFLPQ
SQ  IEAALTESSRLKEQLAMLQLKTDLLGSIFGQERAATLLEQVTSSVRDRDLLHNSLLQRKSKLQSLLVQHKDFGVAFDPLN
SQ  RKLLDLQARIQAEKGLPRDLPGKQVQLLRLQGLQEEGLDLGTQIEAVRPLAHGNSKHQQKVDQISCDQQALQRSLEDLVD
SQ  RCQQNVREHCTFSHRLSELQLWITMATQTLESHQGDVRLWDAESQEAGLETLLSEIPEKEVQVSLLQALGQLVMKKSSPE
SQ  GATMVQEELRKLMESWQALRLLEENMLSLMRNQQLQRTEVDTGKKQVFTNNIPKAGFLINPQDPIPRRQHGANPLEGHDL
SQ  PEDHPQLLRDFEQWLQAENSKLRRIITMRVATAKDLRTREVKLQELEARIPEGQHLFENLLRLRPARDPSNELEDLRYRW
SQ  MLYKSKLKDSGHLLTESSPGELTAFQKSRRQKRWSPCSLLQKACRVALPLQLLLLLFLLLLFLLPAGEEERSCALANNFA
SQ  RSFALMLRYNGPPPT
//
ID  Q8N205;
PN  Nesprin-4;
GN  SYNE4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:23348741}; Single-pass type IV membrane protein {ECO:0000269|PubMed:23348741}. Note=Localization at the nucleus outer membrane requires the presence of SUN1. {ECO:0000250}.
DR  UNIPROT: Q8N205;
DR  UNIPROT: A8MRS0;
DR  UNIPROT: A8MYE3;
DR  UNIPROT: Q7Z7L3;
DR  PDB: 6R16;
DR  PDB: 6WMD;
DR  Pfam: PF10541;
DR  PROSITE: PS51049;
DR  OMIM: 615535;
DR  OMIM: 615540;
DR  DisGeNET: 163183;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Behaves as a kinesin cargo, providing a functional binding site for kinesin-1 at the nuclear envelope. Hence may contribute to the establishment of secretory epithelial morphology by promoting kinesin-dependent apical migration of the centrosome and Golgi apparatus and basal localization of the nucleus (By similarity). {ECO:0000250}.
DE  Disease: Deafness, autosomal recessive, 76 (DFNB76) [MIM:615540]: A form of non-syndromic sensorineural deafness, a disorder resulting from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNB76 affected individuals have onset of progressive high frequency hearing impairment between birth and 6 years of age. The hearing loss is severe at high frequencies by adulthood. {ECO:0000269|PubMed:23348741}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q12840; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q8IY26; IntAct: EBI-24502926; Score: 0.56
DE  Interaction: Q9BXN2; IntAct: EBI-8652857; Score: 0.67
DE  Interaction: P67870; IntAct: EBI-7131802; Score: 0.37
DE  Interaction: P24522; IntAct: EBI-7152348; Score: 0.37
DE  Interaction: P49841; IntAct: EBI-7162684; Score: 0.37
DE  Interaction: Q9UJ70; IntAct: EBI-7254626; Score: 0.37
DE  Interaction: Q9UK32; IntAct: EBI-7375283; Score: 0.37
DE  Interaction: A8K660; IntAct: EBI-10174491; Score: 0.56
DE  Interaction: O00631; IntAct: EBI-10180784; Score: 0.56
DE  Interaction: O60344; IntAct: EBI-10186637; Score: 0.56
DE  Interaction: O75355; IntAct: EBI-10187976; Score: 0.56
DE  Interaction: O95471; IntAct: EBI-10191941; Score: 0.56
DE  Interaction: O95858; IntAct: EBI-10192325; Score: 0.56
DE  Interaction: P11686; IntAct: EBI-12688647; Score: 0.60
DE  Interaction: P15622; IntAct: EBI-10199042; Score: 0.56
DE  Interaction: P54849; IntAct: EBI-10214143; Score: 0.56
DE  Interaction: P56748; IntAct: EBI-10215639; Score: 0.56
DE  Interaction: P56851; IntAct: EBI-10215670; Score: 0.56
DE  Interaction: Q07325; IntAct: EBI-10224656; Score: 0.56
DE  Interaction: Q08722; IntAct: EBI-10225617; Score: 0.56
DE  Interaction: Q12893; IntAct: EBI-10227347; Score: 0.56
DE  Interaction: Q13021; IntAct: EBI-10227624; Score: 0.56
DE  Interaction: Q15437; IntAct: EBI-10236167; Score: 0.56
DE  Interaction: Q16625; IntAct: EBI-10238093; Score: 0.56
DE  Interaction: Q53G59; IntAct: EBI-10242538; Score: 0.56
DE  Interaction: Q5BVD1; IntAct: EBI-10243672; Score: 0.56
DE  Interaction: Q5J5C9; IntAct: EBI-10244196; Score: 0.56
DE  Interaction: Q5TAB7; IntAct: EBI-10246916; Score: 0.56
DE  Interaction: Q6PL45; IntAct: EBI-10254178; Score: 0.56
DE  Interaction: Q6UX06; IntAct: EBI-10254541; Score: 0.56
DE  Interaction: Q6ZP80; IntAct: EBI-10255120; Score: 0.56
DE  Interaction: Q86UP2; IntAct: EBI-10259025; Score: 0.56
DE  Interaction: Q86WT6; IntAct: EBI-10260114; Score: 0.56
DE  Interaction: Q969F0; IntAct: EBI-10264985; Score: 0.56
DE  Interaction: Q8N6G5; IntAct: EBI-10267098; Score: 0.56
DE  Interaction: Q8TBU1; IntAct: EBI-10273675; Score: 0.56
DE  Interaction: Q96D05; IntAct: EBI-10284262; Score: 0.56
DE  Interaction: Q96DZ9; IntAct: EBI-10284818; Score: 0.56
DE  Interaction: Q96E93; IntAct: EBI-10285075; Score: 0.56
DE  Interaction: Q96IW7; IntAct: EBI-10289375; Score: 0.56
DE  Interaction: Q96LK0; IntAct: EBI-10290713; Score: 0.56
DE  Interaction: Q9BVK8; IntAct: EBI-10299780; Score: 0.56
DE  Interaction: Q9HC62; IntAct: EBI-10310600; Score: 0.56
DE  Interaction: Q9NRQ5; IntAct: EBI-10312968; Score: 0.56
DE  Interaction: Q9NRS4; IntAct: EBI-10312988; Score: 0.56
DE  Interaction: Q9NSK0; IntAct: EBI-10313437; Score: 0.56
DE  Interaction: Q9NV12; IntAct: EBI-10314426; Score: 0.56
DE  Interaction: Q9NWD8; IntAct: EBI-10314992; Score: 0.56
DE  Interaction: Q9NXK6; IntAct: EBI-10316428; Score: 0.56
DE  Interaction: Q9P0N8; IntAct: EBI-10317628; Score: 0.56
DE  Interaction: Q9UEU0; IntAct: EBI-10320493; Score: 0.67
DE  Interaction: Q9ULW3; IntAct: EBI-10323957; Score: 0.56
DE  Interaction: Q9Y287; IntAct: EBI-10325832; Score: 0.56
DE  Interaction: A0A0S2Z5K4; IntAct: EBI-16434758; Score: 0.56
DE  Interaction: Q15560; IntAct: EBI-24381165; Score: 0.56
DE  Interaction: Q8N6F1; IntAct: EBI-24421010; Score: 0.56
DE  Interaction: P24593; IntAct: EBI-24450956; Score: 0.56
DE  Interaction: Q15848; IntAct: EBI-24451002; Score: 0.72
DE  Interaction: Q5T619; IntAct: EBI-24475247; Score: 0.56
DE  Interaction: Q9Y397; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q9Y2U8; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q9UL01; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q9NRX5; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q9NQ84; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q9NPG1; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q9H9S5; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q9H6L2; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q9H0B6; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q96L58; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q96BY9; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q8TCT7; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q86X29; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q6P597; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q6IBW4; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q16394; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q14145; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q13454; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q07866; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: P42695; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: P33176; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: O95347; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: O95159; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: O75843; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: O60353; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: O60282; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: O43760; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: O43306; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: O00461; IntAct: EBI-21669865; Score: 0.35
DE  Interaction: Q96CV9; IntAct: EBI-25911446; Score: 0.56
GO  GO:0031309;
GO  GO:0034993;
GO  GO:0045198;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MALSLPLGPRLGSEPLNHPPGAPREADIVGCTVCPASGEESTSPEQAQTLGQDSLGPPEHFQGGPRGNEPAAHPPRWSTP
SQ  SSYEDPAGGKHCEHPISGLEVLEAEQNSLHLCLLGLGRRLQDLEQGLGHWALAQSGMVQLQALQVDLRGAAERVEALLAF
SQ  GEGLAQRSEPRAWAALEQILRALGAYRDSIFRRLWQLQAQLVSYSLVFEEANTLDQDLEVEGDSDWPGPGGVWGPWAPSS
SQ  LPTSTELEWDPAGDIGGLGPLGQKTARTLGVPCELCGQRGPQGRGQGLEEADTSHSRQDMLESGLGHQKRLARHQRHSLL
SQ  RKPQDKKRQASPHLQDVRLEGNPGAPDPASRQPLTFLLILFLLFLLLVGAMFLLPASGGPCCSHARIPRTPYLVLSYVNG
SQ  LPPV
//
ID  Q8CII8;
PN  Nesprin-4;
GN  Syne4;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:19164528, ECO:0000269|PubMed:23348741}; Single-pass type IV membrane protein {ECO:0000269|PubMed:19164528, ECO:0000269|PubMed:23348741}. Note=Localization at the nucleus outer membrane location requires the presence of SUN1.
DR  UNIPROT: Q8CII8;
DR  UNIPROT: Q6PH99;
DR  UNIPROT: Q99J42;
DR  Pfam: PF10541;
DR  PROSITE: PS51049;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Behaves as a kinesin cargo, providing a functional binding site for kinesin-1 at the nuclear envelope. Hence may contribute to the establishment of secretory epithelial morphology, by promoting kinesin-dependent apical migration of the centrosome and Golgi apparatus and basal localization of the nucleus. {ECO:0000250, ECO:0000269|PubMed:19164528}.
DE  Reference Proteome: Yes;
DE  Interaction: P37285; IntAct: EBI-15752297; Score: 0.40
DE  Interaction: P33176; IntAct: EBI-15752320; Score: 0.40
DE  Interaction: O88448; IntAct: EBI-15752341; Score: 0.41
DE  Interaction: O88447; IntAct: EBI-15752400; Score: 0.41
DE  Interaction: Q91W40; IntAct: EBI-15752381; Score: 0.41
DE  Interaction: Q9DBS5; IntAct: EBI-15752419; Score: 0.41
GO  GO:0031309;
GO  GO:0034993;
GO  GO:0045198;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MALVPPLGREFPPEPVNCPLAAPRELDVVGGTICPAPEEETSRPEQVQASLGLPEHCMGELKSTESATSPSRLPLASSHE
SQ  HQDGGKPCEHSDSGLEVLEAEQDSLHLCLLRLNFRLQDLERGLGSWTLAHNRIVQMQALQAELRGAAERVDALLAFGEGL
SQ  AERSEPRAWASLEQVLRALGTHRDTIFQRLWQLQAQLISYSLVLEKANLLDQDLEVEGDSDGPAAGGVWGPWAPSTFPTP
SQ  AELEWDPAGDVGGLGPSGQKISRIPGAPCELCGYRGPQSSGQGLEDLLSLGLGHRKHLAAHHRRRLRKPQDRKRQVSPSL
SQ  PDAMLEVDRGVPAPASKRPLTLFFLLLFLLLVGATLLLPLSGVSCCSHARLARTPYLVLSYVNGLPPI
//
ID  Q5M844;
PN  Nesprin-4;
GN  Syne4;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Localization at the nucleus outer membrane location requires the presence of SUN1. {ECO:0000250}.
DR  UNIPROT: Q5M844;
DR  Pfam: PF10541;
DR  PROSITE: PS51049;
DE  Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Behaves as a kinesin cargo, providing a functional binding site for kinesin-1 at the nuclear envelope. Hence may contribute to the establishment of secretory epithelial morphology, by promoting kinesin-dependent apical migration of the centrosome and Golgi apparatus and basal localization of the nucleus (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0031309;
GO  GO:0034993;
GO  GO:0045198;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255|PROSITE-ProRule:PRU00385};
SQ  MAQFPLLGHGFPPEPVNHPLGGPRGLDVAGPTICPAPEEEPSRPEQVQASLDAPEHFMDEPKSTESATSPSKLPLASSHE
SQ  HQDGGKPCEALQAELQGAAERVDALLVFGEGLAERSEPRAWTSLEQVLRALGTHRDTIFQRLWQLQAQLISYSLVLEKAN
SQ  LLDQDLEVEGDSDGPAAGGVWGPWAPSIFPTPAELEWDPAGDVGGLGPSGQKISRIPGAPCELCGYRGSQSSGQGFEDLL
SQ  SLGLGHRKHLAAHHRRRLQKPQDKKRQGPPSLPDAMLEVDRGVPAPASRRPLTFLLLLLFLLLVGATLLLPLSGVPCCSH
SQ  TRLARTPYLVLSYVNGLPPI
//
ID  O18964;
PN  Synaptojanin-1;
GN  SYNJ1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9199318}.
DR  UNIPROT: O18964;
DR  Pfam: PF08952;
DR  Pfam: PF03372;
DR  Pfam: PF02383;
DR  PROSITE: PS50102;
DR  PROSITE: PS50275;
DE  Function: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)- bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate. Has a role in clathrin-mediated endocytosis (By similarity). Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2 (PubMed:9199318). {ECO:0000250|UniProtKB:O43426, ECO:0000269|PubMed:9199318}.
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0098793;
GO  GO:0004439;
GO  GO:0003723;
GO  GO:0017124;
GO  GO:0007420;
GO  GO:0046855;
GO  GO:0046856;
GO  GO:0048488;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYSKVLDAYGLLGVLRLNLGDIMLHYLVL
SQ  VTGCMSVGKIQESEVFRVTSTEFISLRVDSSDEDRISEVRKVLNSGNFYFAWSASGVSLDLSLNAHRSLQEHTTDNRFSW
SQ  NQSLHLHLKHYGVNCADWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLD
SQ  DSVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLK
SQ  ASEHAADIQMVNFDYHQMVKGGKAEKLHSVLKPQVQKFLDYGIFHFDGSEVQRCQSGTVRTNCLDCLDRTNSVQAFLGLE
SQ  MLTKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVSRTIQNNFFDSSKQEAIDVLL
SQ  LGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKSMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTD
SQ  WLLDAPKLAGIQEFQDKRSKPMDIFPIGFEEMVELNAGNIVNASTTNQKLWAAELQKTISRDNKYVLLASEQLVGVCLFV
SQ  FIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNDDFLEIARKLSFPMGRLLF
SQ  SHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCR
SQ  TPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQN
SQ  IYKEVIAVQGPPDGTVLVSIKSSLPENNFFNDALIDELLQQFTNFGEVILIRFVEDKMWVTFLEGSSALNVLNLNGKELL
SQ  GRTITITLKSPDWIKTLEEEMSLEKINVPLPSSTSSTLLGEDAEVTADFDMEGDVDDYSAEVEEILPQHLQPSSSSALAR
SQ  PPVLHPGPVPASHLPYRRGPVPSLPVRPSRAPSRTPGPPASQSSPVDTLPATQLQQKDSSQTLEPKRPPPPRPVAPPARP
SQ  APPQRPPPPSGARSPAPARERVWSTRKAQERPRRDNLGGSQLPPQGGLPGPGLAGHSAARPIIPPRAGVISAPESHGRVS
SQ  AGRLTPESQRKTXEVLKGPALLPEPLKPQAALPVPPSLAPPSQEMQEPLIAVAAPLAQSALQPSLETPPQPPPRSRSSHS
SQ  LPSDAPAAAAGATIRVTGEKQTGVSAVRLDCPLKSDPFEDLSLN
//
ID  O43426;
PN  Synaptojanin-1;
GN  SYNJ1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O18964}.
DR  UNIPROT: O43426;
DR  UNIPROT: O43425;
DR  UNIPROT: O94984;
DR  UNIPROT: Q4KMR1;
DR  PDB: 1W80;
DR  PDB: 2DNR;
DR  PDB: 2VJ0;
DR  PDB: 7A0V;
DR  Pfam: PF08952;
DR  Pfam: PF03372;
DR  Pfam: PF02383;
DR  PROSITE: PS50102;
DR  PROSITE: PS50275;
DR  OMIM: 604297;
DR  OMIM: 615530;
DR  OMIM: 617389;
DR  DisGeNET: 8867;
DE  Function: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)- bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (PubMed:27435091). Has a role in clathrin-mediated endocytosis (By similarity). Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2 (By similarity). {ECO:0000250|UniProtKB:O18964, ECO:0000250|UniProtKB:Q62910, ECO:0000269|PubMed:27435091}.
DE  Disease: Parkinson disease 20, early-onset (PARK20) [MIM:615530]: An early-onset form of Parkinson disease, a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. PARK20 is characterized by young adult-onset of parkinsonism. Additional features may include seizures, cognitive decline, abnormal eye movements, and dystonia. {ECO:0000269|PubMed:23804563, ECO:0000269|PubMed:23804577, ECO:0000269|PubMed:27496670}. Note=The disease is caused by variants affecting the gene represented in this entry. Developmental and epileptic encephalopathy 53 (DEE53) [MIM:617389]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE53 inheritance is autosomal recessive. {ECO:0000269|PubMed:27435091}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P49418; IntAct: EBI-7121552; Score: 0.56
DE  Interaction: Q99961; IntAct: EBI-7122802; Score: 0.44
DE  Interaction: Q6ZQ03; IntAct: EBI-7818661; Score: 0.56
DE  Interaction: O94875; IntAct: EBI-7818742; Score: 0.56
DE  Interaction: P62994; IntAct: EBI-7818911; Score: 0.56
DE  Interaction: Q9Z0W5; IntAct: EBI-7818854; Score: 0.56
DE  Interaction: Q99962; IntAct: EBI-7819014; Score: 0.56
DE  Interaction: P18484; IntAct: EBI-8455489; Score: 0.40
DE  Interaction: P17427; IntAct: EBI-8455461; Score: 0.44
DE  Interaction: O95400; IntAct: EBI-7175844; Score: 0.44
DE  Interaction: Q9Y5X1; IntAct: EBI-7808413; Score: 0.66
DE  Interaction: P16333; IntAct: EBI-7808566; Score: 0.44
DE  Interaction: Q07912; IntAct: EBI-7809036; Score: 0.27
DE  Interaction: Q9CR95; IntAct: EBI-7593929; Score: 0.44
DE  Interaction: Q12965; IntAct: EBI-7237329; Score: 0.40
DE  Interaction: Q15811; IntAct: EBI-7965393; Score: 0.40
DE  Interaction: A0A6L7HDD5; IntAct: EBI-2821536; Score: 0.00
DE  Interaction: Q81X77; IntAct: EBI-2821551; Score: 0.00
DE  Interaction: P62993; IntAct: EBI-3964621; Score: 0.53
DE  Interaction: P56945; IntAct: EBI-15099384; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q96CW1; IntAct: EBI-21520588; Score: 0.35
DE  Interaction: Q6NS38; IntAct: EBI-21543481; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16801466; Score: 0.27
DE  Interaction: P10636; IntAct: EBI-20749724; Score: 0.35
DE  Interaction: P04156; IntAct: EBI-21013988; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: O43364; IntAct: EBI-28997314; Score: 0.35
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
GO  GO:0030132;
GO  GO:0005829;
GO  GO:0030117;
GO  GO:0005874;
GO  GO:0098688;
GO  GO:0048471;
GO  GO:0098793;
GO  GO:0097060;
GO  GO:0043195;
GO  GO:0012506;
GO  GO:1990175;
GO  GO:0052658;
GO  GO:0034596;
GO  GO:0034595;
GO  GO:0052629;
GO  GO:0043813;
GO  GO:0004438;
GO  GO:0004439;
GO  GO:0043812;
GO  GO:0008022;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0017124;
GO  GO:0007420;
GO  GO:0046855;
GO  GO:0043647;
GO  GO:0007612;
GO  GO:0061024;
GO  GO:0006836;
GO  GO:0006661;
GO  GO:0046856;
GO  GO:0046488;
GO  GO:1904980;
GO  GO:0014015;
GO  GO:0048260;
GO  GO:0034097;
GO  GO:0032526;
GO  GO:0048488;
GO  GO:0016082;
GO  GO:0048489;
GO  GO:0016191;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYSKVLDAYGLLGVLRLNLGDTMLHYLVL
SQ  VTGCMSVGKIQESEVFRVTSTEFISLRIDSSDEDRISEVRKVLNSGNFYFAWSASGISLDLSLNAHRSMQEQTTDNRFFW
SQ  NQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLD
SQ  DSVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLK
SQ  ASEHAADIQMVNFDYHQMVKGGKAEKLHSVLKPQVQKFLDYGFFYFNGSEVQRCQSGTVRTNCLDCLDRTNSVQAFLGLE
SQ  MLAKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVTRTIQNNFFDSSKQEAIDVLL
SQ  LGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKSMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTD
SQ  WLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKLWAVELQKTISRDNKYVLLASEQLVGVCLFV
SQ  FIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFIEIARKLSFPMGRMLF
SQ  SHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCR
SQ  TPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQN
SQ  IYKEVIAVQGPPDGTVLVSIKSSLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELL
SQ  NRTITIALKSPDWIKNLEEEMSLEKISIALPSSTSSTLLGEDAEVAADFDMEGDVDDYSAEVEELLPQHLQPSSSSGLGT
SQ  SPSSSPRTSPCQSPTISEGPVPSLPIRPSRAPSRTPGPPSAQSSPIDAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRP
SQ  APPQRPPPPSGARSPAPTRKEFGGIGAPPSPGVARREMEAPKSPGTTRKDNIGRSQPSPQAGLAGPGPAGYSTARPTIPP
SQ  RAGVISAPQSHARASAGRLTPESQSKTSETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRLQEPLVPVAAPMPQSGPQPNL
SQ  ETPPQPPPRSRSSHSLPSEASSQPQVKTNGISDGKRESPLKIDPFEDLSFNLLAVSKAQLSVQTSPVPTPDPKRLIQLPS
SQ  ATQSNVLSSVSCMPTMPPIPARSQSQENMRSSPNPFITGLTRTNPFSDRTAAPGNPFRAKSEESEATSWFSKEEPVTISP
SQ  FPSLQPLGHNKSRASSSLDGFKDSFDLQGQSTLKISNPKGWVTFEEEEDFGVKGKSKSACSDLLGNQPSSFSGSNLTLND
SQ  DWNKGTNVSFCVLPSRRPPPPPVPLLPPGTSPPVDPFTTLASKASPTLDFTER
//
ID  Q8CHC4;
PN  Synaptojanin-1;
GN  Synj1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O18964}.
DR  UNIPROT: Q8CHC4;
DR  Pfam: PF08952;
DR  Pfam: PF03372;
DR  Pfam: PF02383;
DR  PROSITE: PS50102;
DR  PROSITE: PS50275;
DE  Function: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)- bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (By similarity). Has a role in clathrin-mediated endocytosis (By similarity). Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2 (By similarity). {ECO:0000250|UniProtKB:O18964, ECO:0000250|UniProtKB:O43426}.
DE  Reference Proteome: Yes;
DE  Interaction: Q96B97; IntAct: EBI-6953809; Score: 0.52
DE  Interaction: P63101; IntAct: EBI-2255635; Score: 0.35
DE  Interaction: P50516; IntAct: EBI-6272793; Score: 0.35
DE  Interaction: F6SEU4; IntAct: EBI-16733301; Score: 0.53
DE  Interaction: Q62108; IntAct: EBI-16724752; Score: 0.35
DE  Interaction: Q83BP6; IntAct: EBI-21287354; Score: 0.37
DE  Interaction: Q6P1J9; IntAct: EBI-20726660; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26472902; Score: 0.35
GO  GO:0030118;
GO  GO:0030132;
GO  GO:0005737;
GO  GO:0098978;
GO  GO:0030117;
GO  GO:0005874;
GO  GO:0043005;
GO  GO:0098688;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0098793;
GO  GO:0032991;
GO  GO:0098685;
GO  GO:0097060;
GO  GO:0043195;
GO  GO:0012506;
GO  GO:1990175;
GO  GO:0052658;
GO  GO:0034595;
GO  GO:0004438;
GO  GO:0004439;
GO  GO:0043812;
GO  GO:0008022;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0017124;
GO  GO:0007420;
GO  GO:0046855;
GO  GO:0007612;
GO  GO:0006836;
GO  GO:0046856;
GO  GO:0046488;
GO  GO:0048015;
GO  GO:1904980;
GO  GO:0014015;
GO  GO:0048260;
GO  GO:1903423;
GO  GO:0098884;
GO  GO:0099149;
GO  GO:0034097;
GO  GO:0032526;
GO  GO:0048488;
GO  GO:0016082;
GO  GO:0048489;
GO  GO:0016191;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYAKVLDAYGLLGVLRLNLGDTMLHYLVL
SQ  VTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRISEVRKVLNSGNFYFAWSASGVSLDLSLNAHRSMQEHTTDNRFFW
SQ  NQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLD
SQ  DCVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLK
SQ  ASEHASDIHMVSFDYHQMVKGGKAEKLHSILKPQVQKFLDYGFFYFDGSEVQRCQSGTVRTNCLDCLDRTNSVQAFLGLE
SQ  MLAKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVTRTIQNNFFDSSKQEAIDVLL
SQ  LGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKNMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTD
SQ  WLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWAVELQKTISRDNKYVLLASEQLVGVCLFV
SQ  FIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLF
SQ  SHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCR
SQ  TPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQK
SQ  IYKEVIAVQGPPDGTVLVSIKSSAQESTFFDDALIDELLRQFAHFGEVILIRFVEDKMWVTFLEGSSALNALSLNGKELL
SQ  NRTITITLKSPDWIKHLEEEMSLEKISVTLPSSASSTLLGEDAEVAADFDMEGDVDDYSAEVEELLPQHLQPSSSSGLGT
SQ  SPSSSPRTSPCQSPTVPEYSAPSLPIRPSRAPSRTPGPPSSQGSPVDTQPAAQKDSSQTLEPKRPPPPRPVAPPARPAPP
SQ  QRPPPPSGARSPAPARKEFGGVGAPPSPGVARREIEAPKSPGTARKDNIGRNQPSPQAGLAGPGPAGYGAARPTIPARAG
SQ  VISAPQSQARVCAGRPTPDSQSKPSETLKGPAVLPEPLKPQAAFPQQPSLPTPAQKLQDPLVPIAAPTMPPSGPQPNLET
SQ  PPQPPPRSRSSQSLPSDSSPQLQQEQPTGQVKINGISGVKQEPTLKSDPFEDLSLSVLAVSKAQPSVQISPVLTPDPKML
SQ  IQLPSASQSQVNPLSSVSCMPTRPPGPEESKSQESMGSSANPFPSLPCRNPFTDRTAAPGNPFRVQSQESEATSWLSKEE
SQ  PVPNSPFPPLMPLSHDTSKASSSLGGFEDNFDLQSQSTVKTSNPKGWVTFDEDDNFPTTGKSKSVCPDLVGNAPASFDDD
SQ  WSKGASVSFCVLPARRPPPPPPPVPLLPPGTTSSAGPSTTLPSKAPSTLDFTER
//
ID  Q62910;
PN  Synaptojanin-1;
GN  Synj1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O18964}.
DR  UNIPROT: Q62910;
DR  UNIPROT: O89092;
DR  UNIPROT: Q62911;
DR  UNIPROT: Q810Z8;
DR  Pfam: PF08952;
DR  Pfam: PF03372;
DR  Pfam: PF02383;
DR  PROSITE: PS50102;
DR  PROSITE: PS50275;
DE  Function: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)- bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (By similarity). Has a role in clathrin-mediated endocytosis (PubMed:9428629). Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2 (By similarity). {ECO:0000250|UniProtKB:O18964, ECO:0000250|UniProtKB:O43426, ECO:0000269|PubMed:9428629}.
DE  Reference Proteome: Yes;
DE  Interaction: O35413; IntAct: EBI-7458056; Score: 0.40
DE  Interaction: Q00535; IntAct: EBI-7084181; Score: 0.31
DE  Interaction: Q08209; IntAct: EBI-7084192; Score: 0.31
DE  Interaction: Q8CBW3; IntAct: EBI-7260851; Score: 0.37
DE  Interaction: Q99962; IntAct: EBI-7260923; Score: 0.57
DE  Interaction: Q99961; IntAct: EBI-7260903; Score: 0.37
DE  Interaction: Q99963; IntAct: EBI-7260943; Score: 0.37
DE  Interaction: O35179; IntAct: EBI-1149354; Score: 0.50
DE  Interaction: O35964; IntAct: EBI-1149378; Score: 0.40
DE  Interaction: O35180; IntAct: EBI-1149387; Score: 0.50
DE  Interaction: P17427; IntAct: EBI-7593197; Score: 0.35
DE  Interaction: Q9CR95; IntAct: EBI-7593299; Score: 0.40
DE  Interaction: Q9D1J1; IntAct: EBI-7593405; Score: 0.40
DE  Interaction: Q12965; IntAct: EBI-7237429; Score: 0.52
DE  Interaction: Q3UQN2; IntAct: EBI-6095200; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6665350; Score: 0.35
DE  Interaction: P19332; IntAct: EBI-26374040; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26440627; Score: 0.35
GO  GO:0030132;
GO  GO:0005737;
GO  GO:0098978;
GO  GO:0030117;
GO  GO:0043005;
GO  GO:0098688;
GO  GO:0048471;
GO  GO:0098794;
GO  GO:0098793;
GO  GO:0032991;
GO  GO:0098685;
GO  GO:0097060;
GO  GO:0043195;
GO  GO:0012506;
GO  GO:1990175;
GO  GO:0052658;
GO  GO:0034595;
GO  GO:0004438;
GO  GO:0004439;
GO  GO:0043812;
GO  GO:0008022;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0017124;
GO  GO:0007420;
GO  GO:0046855;
GO  GO:0007612;
GO  GO:0006836;
GO  GO:0046856;
GO  GO:0046488;
GO  GO:1904980;
GO  GO:0014015;
GO  GO:0048260;
GO  GO:0098884;
GO  GO:0099149;
GO  GO:0034097;
GO  GO:0032526;
GO  GO:0048488;
GO  GO:0016082;
GO  GO:0048489;
GO  GO:0016191;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYAKVLDAYGLLGVLRLNLGDTMLHYLVL
SQ  VTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRISEVRKVLNSGNFYFAWSASGVSLDLSLNAHRSMQEHTTDNRFFW
SQ  NQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYLD
SQ  DCVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKDLYGKQIVVNLLGSKEGEHMLSKAFQSHLK
SQ  ASEHASDIHMVSFDYHQMVKGGKAEKLHSVLKPQVQKFLDYGFFYFDGSAVQRCQSGTVRTNCLDCLDRTNSVQAFLGLE
SQ  MLAKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVTRTIQNNFFDSSKQEAIDVLL
SQ  LGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKNMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTD
SQ  WLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVNASTTNQKLWAVELQKTISRDNKYVLLASEQLVGVCLFV
SQ  FIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFVEIARKLSFPMGRMLF
SQ  SHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSEDYDTSEKCR
SQ  TPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQK
SQ  IYKEVIAVQGPPDGTVLVSIKSSAQENTFFDDALIDELLQQFAHFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELL
SQ  NRTITITLKSPDWIKTLEEEMSLEKISVTLPSSTSSTLLGEDAEVSADFDMEGDVDDYSAEVEELLPQHLQPSSSSGLGT
SQ  SPSSSPRTSPCQSPTAPEYSAPSLPIRPSRAPSRTPGPLSSQGAPVDTQPAAQKESSQTIEPKRPPPPRPVAPPARPAPP
SQ  QRPPPPSGARSPAPARKEFGGVGAPPSPGVTRREMEAPKSPGTARKDNIGRNQPSPQAGLAGPGPSGYGAARPTIPARAG
SQ  VISAPQSQARVSAGRLTPESQSKPLETSKGPAVLPEPLKPQAAFPPQPSLPTPAQKLQDPLVPIAAPMPPSIPQSNLETP
SQ  PLPPPRSRSSQSLPSDSSPQLQQEQPTGQQVKINGACGVKQEPTLKSDPFEDLSLSVLAVSKAQPSAQISPVLTPDPKML
SQ  IQLPSASQSKVNSLSSVSCMLTMPPVPEQSKSQESVGSSANPFPSLPTRNPFTDRTAAPGNPFRVQSQESEATSWLSKEE
SQ  PVSNSPFPPLMPLSHDMSKPSSSLDGFEDNFDLQSQSTVKTSNPKGWVTFDEDEDFPTKGKSRSVYPDSLGNTAASFDDD
SQ  WSKGTNVSFCVLPARRPPPPPPPVPLLPPGTTSSAGPSTTLSSKASPTLDFTER
//
ID  Q9UMZ2;
PN  Synergin gamma;
GN  SYNRG;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9JKC9}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9JKC9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JKC9}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15758025}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15758025}. Note=Localization at clathrin-coated vesicles depends on AFTPH/aftiphilin (PubMed:15758025). Associates with membranes via the adapter protein complex AP-1 (By similarity). Colocalizes with AP1G1 (By similarity). {ECO:0000250|UniProtKB:Q9JKC9, ECO:0000269|PubMed:15758025}.
DR  UNIPROT: Q9UMZ2;
DR  UNIPROT: A8MWU4;
DR  UNIPROT: B7ZKZ2;
DR  UNIPROT: B7ZKZ3;
DR  UNIPROT: Q17RI2;
DR  UNIPROT: Q5BKU5;
DR  UNIPROT: Q6ZT17;
DR  PDB: 2MX7;
DR  PROSITE: PS50031;
DR  OMIM: 607291;
DR  DisGeNET: 11276;
DE  Function: Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (PubMed:15758025). May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP- 1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269|PubMed:15758025, ECO:0000305|PubMed:12538641}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6ZMQ8; IntAct: EBI-32723474; Score: 0.27
DE  Interaction: Q9P0L0; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9UJY4; IntAct: EBI-7240526; Score: 0.44
DE  Interaction: Q9UJY5; IntAct: EBI-7240552; Score: 0.44
DE  Interaction: Q92624; IntAct: EBI-10324442; Score: 0.56
DE  Interaction: P56377; IntAct: EBI-11037753; Score: 0.35
DE  Interaction: Q9NYZ3; IntAct: EBI-11081743; Score: 0.35
DE  Interaction: Q9UGJ1; IntAct: EBI-11083142; Score: 0.35
DE  Interaction: Q5JU00; IntAct: EBI-11385220; Score: 0.27
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-21550215; Score: 0.35
DE  Interaction: O75843; IntAct: EBI-21591189; Score: 0.35
DE  Interaction: O14965; IntAct: EBI-21639587; Score: 0.35
DE  Interaction: P58340; IntAct: EBI-21701984; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q9Y2H1; IntAct: EBI-20625012; Score: 0.27
DE  Interaction: P51957; IntAct: EBI-20721387; Score: 0.35
DE  Interaction: P63010; IntAct: EBI-30818100; Score: 0.44
DE  Interaction: P21802; IntAct: EBI-32721907; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
GO  GO:0030121;
GO  GO:0030130;
GO  GO:0005737;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0006897;
GO  GO:0006886;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9JKC9};
SQ  MALRPGAGSGGGGAAGAGAGSAGGGGFMFPVAGGIRPPQAGLMPMQQQGFPMVSVMQPNMQGIMGMNYSSQMSQGPIAMQ
SQ  AGIPMGPMPAAGMPYLGQAPFLGMRPPGPQYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKT
SQ  GEKSRDDALEAIKGNLDGFSRDAKMHPTPASHPKKPGPSLEEKFLVSCDISTSGQEQIKLNTSEVGHKALGPGSSKKYPS
SQ  LMASNGVAVDGCVSGTTTAEAENTSDQNLSIEESGVGVFPSQDPAQPRMPPWIYNESLVPDAYKKILETTMTPTGIDTAK
SQ  LYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMIAVTQRGVPAMSPDALNQFPAAPIPTLSGFSMTLPTPVS
SQ  QPTVIPSGPAGSMPLSLGQPVMGINLVGPVGGAAAQASSGFIPTYPANQVVKPEEDDFQDFQDASKSGSLDDSFSDFQEL
SQ  PASSKTSNSQHGNSAPSLLMPLPGTKALPSMDKYAVFKGIAADKSSENTVPPGDPGDKYSAFRELEQTAENKPLGESFAE
SQ  FRSAGTDDGFTDFKTADSVSPLEPPTKDKTFPPSFPSGTIQQKQQTQVKNPLNLADLDMFSSVNCSSEKPLSFSAVFSTS
SQ  KSVSTPQSTGSAATMTALAATKTSSLADDFGEFSLFGEYSGLAPVGEQDDFADFMAFSNSSISSEQKPDDKYDALKEEAS
SQ  PVPLTSNVGSTVKGGQNSTAASTKYDVFRQLSLEGSGLGVEDLKDNTPSGKSDDDFADFHSSKFSSINSDKSLGEKAVAF
SQ  RHTKEDSASVKSLDLPSIGGSSVGKEDSEDALSVQFDMKLADVGGDLKHVMSDSSLDLPTVSGQHPPAADIEDLKYAAFG
SQ  SYSSNFAVSTLTSYDWSDRDDATQGRKLSPFVLSAGSGSPSATSILQKKETSFGSSENITMTSLSKVTTFVSEDALPETT
SQ  FPALASFKDTIPQTSEQKEYENRDYKDFTKQDLPTAERSQEATCPSPASSGASQETPNECSDDFGEFQSEKPKISKFDFL
SQ  VATSQSKMKSSEEMIKSELATFDLSVQGSHKRSLSLGDKEISRSSPSPALEQPFRDRSNTLNEKPALPVIRDKYKDLTGE
SQ  VEENERYAYEWQRCLGSALNVIKKANDTLNGISSSSVCTEVIQSAQGMEYLLGVVEVYRVTKRVELGIKATAVCSEKLQQ
SQ  LLKDIDKVWNNLIGFMSLATLTPDENSLDFSSCMLRPGIKNAQELACGVCLLNVDSRSRKEEKPAEEHPKKAFNSETDSF
SQ  KLAYGGHQYHASCANFWINCVEPKPPGLVLPDLL
//
ID  Q5SV85;
PN  Synergin gamma;
GN  Synrg;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:12808037}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12808037}; Peripheral membrane protein {ECO:0000269|PubMed:12808037}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UMZ2}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UMZ2}. Note=Localization at clathrin- coated vesicles depends on AFTPH/aftiphilin (By similarity). Associates with membranes via the adapter protein complex AP-1 (By similarity). Colocalizes with AP1G1 (By similarity). {ECO:0000250|UniProtKB:Q9JKC9, ECO:0000250|UniProtKB:Q9UMZ2}.
DR  UNIPROT: Q5SV85;
DR  UNIPROT: Q5SV84;
DR  UNIPROT: Q6PHT6;
DR  PROSITE: PS50031;
DE  Function: Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (By similarity). May act by linking the adapter protein complex AP-1 to other proteins (By similarity). Component of clathrin-coated vesicles (By similarity). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP- 1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (By similarity). {ECO:0000250|UniProtKB:Q9UMZ2}.
DE  Reference Proteome: Yes;
GO  GO:0030130;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0006897;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:12808037};
SQ  MALRPGAGASGAAGAGAGPGGAGSFMFPVAGGMRPPQAGLIPMQQQGFPMVSVMQPNMQGMMGMNYSSQMSQGPIAMQAG
SQ  IPMGPMPAAGVPFLGQPPFLSMRPAGPQYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKTGE
SQ  KNRDDALEAIKGNLDGFSRDAKMHPTPASHPKKQGPSLEEKLLVSCDVSASGQEHIKLNTPDAGHKAIVPGSSKNCPGLM
SQ  AHNRGAVDGCVSGPASAEAEKTSDQTLSKEESGVGVFPSQDPAQSRMPPWIYNESLVPDAYKKILETTMTPTGIDTAKLY
SQ  PILMSSGLPRETLGQIWALANRTTPGRLTKEELYTVLAMVAVTQRGVPAMSPDALSQFPAAPIPTLSGFPMTLPTPVSQP
SQ  TAMPSGPTGSMPLTLGQPIMGINLVGPVGGAAAPTSSGFMPAYPSNQVGKTEEDDFQDFQDASKSGSIDDSFTDFQEMPA
SQ  SSKTSNSQHGNSAPSLLIPFPGTKASTDKYAVFKGISTDKPSENPASFGESGDKYSAFRELEQTTDSKPLGESFAEFRST
SQ  GTDDGFTDFKTADSVSPLEPPTKDTFPSAFASGAAQQTQTQVKTPLNLEDLDMFSSVDCSGEKQVPFSATFSTAKSVSTR
SQ  PQPAGSAAASAALASTKTSSLADDFGEFNLFGEYSNPASAGEQDDFADFMAFGNSSISSEPKASDKYEALREEVSPSPLS
SQ  SSTVEGAQHPPAAATKYDVFKQLSLEGAGLAMEEFKENTSSTKSEDDFADFHSSKFSSTSSDKSLGEKAVAFRHAKEDSS
SQ  SVKSLDLPSIGGSSVGKEDSEDALSVQFDMKLADVGGDLKHVMSDSSLDLPTVSGQHPPAADTEDLSCAAFGSCSSHFTV
SQ  STLTSCEWSDRADALQGRKLSPFVLSAGSRSFSATSNLHTKEISFGSSENITMSSLSKGSALASEDALPETAFPAFASFK
SQ  DMMPQTTEQKEFESGDFQDFTRQDMPTVDRSQETSCPSPASSVASHETPKEGADDFGEFQSEKSKISKFDFLVANSQSKM
SQ  KSSEEMIKSELATFDLSVQGSHKRSLSLGDKEISRSSPSPALEQPFRDRSNTLSERAALPVIRDKYKDLTGEVEENERYA
SQ  YEWQRCLGSALDVIKKANDTLNGISSSAVCTEVIQSAQGMEYLLGVVEVYRVTKRVELGIKATAVCSEKLQQLLKDIDKV
SQ  WNNLIGFMSLATLTPDENSLDFSSCMLRPGIKNAQELACGVCLLNVDSRSRKEETPAEEQPKKAFNSETDSFKLAYGGHQ
SQ  YHASCANFWINCVEPKPPGLLLPDLL
//
ID  Q9JKC9;
PN  Synergin gamma;
GN  Synrg;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10477754}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10477754}; Peripheral membrane protein {ECO:0000269|PubMed:10477754}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UMZ2}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UMZ2}. Note=Localization at clathrin-coated vesicles depends on AFTPH/aftiphilin (By similarity). Associates with membranes via the adapter protein complex AP-1 (PubMed:10477754). Colocalizes with AP1G1 (PubMed:10477754). {ECO:0000250|UniProtKB:Q9UMZ2, ECO:0000269|PubMed:10477754}.
DR  UNIPROT: Q9JKC9;
DR  UNIPROT: A1EC70;
DR  UNIPROT: A1EC72;
DR  UNIPROT: A1EC74;
DR  UNIPROT: A1EC75;
DR  UNIPROT: Q9R145;
DR  PROSITE: PS50031;
DE  Function: Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (By similarity). May act by linking the adapter protein complex AP-1 to other proteins (By similarity). Component of clathrin-coated vesicles (By similarity). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP- 1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (By similarity). {ECO:0000250|UniProtKB:Q9UMZ2}.
DE  Reference Proteome: Yes;
GO  GO:0030130;
GO  GO:0048471;
GO  GO:0006897;
GO  GO:0015031;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:10477754};
SQ  MALRPGAGASGAAGAGTGPGGAGSFMFPVAGGMRPPQGLIPMQQQGFPMVSVMQPNMQGMMGMNYSSQMSQGPIAMQAGI
SQ  PMGPMPAAGVPFLGQPPFLGMRPAAPQYTPDMQKQFAEEQQKRFEQQQKLLEEERKRRQFEEQKQKLRLLSSVKPKTGEK
SQ  NRDDALEAIKGNLDGFSRDAKMHPTPASHPKKPDCPTSSHSTKTVSPSSAFLGEDEFSGFMQGPVELPTCGPSSTAQPFQ
SQ  SFLPSTPLGQLHTQKAGAQPLPPGQAPVSFAVHGVHGQIPCLSAASASHSMQKAGPSLEEKLLVSCDISASGQEHIKLSS
SQ  PEAGHRAVVPGSSKNSPGLMAHNGGAVDGCVSGPTTAVAEKTSDQNLSKEESGVGVFPSQDPVQPRMPPWIYNESLVPDA
SQ  YKKILETTMTPTGIDTAKLYPILMSSGLPRETLGQIWALANRTTPGKLTKEELYTVLAMVAVTQRGVPAMSPDTLNQFPA
SQ  APIPTLSGFPMTLPTPVSQPTAMTSGPAGSIPLSLGQPIMGINLVGPVGGAAAPTSSGFMPAYPSNQVGKTEEDDFQDFQ
SQ  DASKSGSIDDSFTDFQEVPASSKTSNSQHGNSAPSLLIPLPGTKASTDKYAVFKGISAEKPSENPASFGESGDKYSAFRE
SQ  LEPTADSKPLGESFAEFRSTGTDDGFTDFKTADSVSPLEPPTKDSFPSAFASGAAQQTQTQVKTPLNLADLDMFSSVDCS
SQ  GEKPVPFSAAFSTSKSVSSRPQPAGSAAAPASLASTKASSLADDFGEFNLFGEYSNPASVGEQDDFADFMAFGNSSIPSE
SQ  PKADDKYEALREEGSPGALSTSTVEGAHNPPVSSSKYDVFKQLSLEGAGLAIEEFKENTPSTKSDGDFADFHSSKFSSTS
SQ  SDKSLGEKAVAFRHAKEDSASVKSLDLPSIGGSSVGKEDSEDALSVQFDMKLADVGGDLKHVMSDSSLDLPTVSGQHPPA
SQ  AGSALASEDALPETPFPAFASFKDMMPQTTEQKEYESGDFQDFTRQDMPMVDRSQENTCPSPASSVASHETPKEGADDFG
SQ  EFQSEKPKISKFDFLVANSQSKMKSSEEMIKSELATFDLSVQGSHKRSLSLGDKEISRSSPSPALEQPFRDRSNTLSERA
SQ  ALPVIRDKYKDLTGEVEENERYAYEWQRCLGSALDVIKKANDTLNGISSSAVCTEVIQSAQGMEYLLGVVEVYRVTKRVE
SQ  LGIKATAVCSEKLQQLLKDIDKVWNNLIGFMSLTTLTPDENSLDFSSCMLRPGIKNAQELACGVCLLNVDSRSRKEETPA
SQ  EEQPKKAFNSETDSFKLAYGGHQYHASCANFWINCVEPKPPGLLLPDLL
//
ID  Q9NZ50;
PN  Gamma-synuclein;
GN  SNCG;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11746666}. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle.
DR  UNIPROT: Q9NZ50;
DR  UNIPROT: Q1RMG7;
DR  UNIPROT: Q9N187;
DR  Pfam: PF01387;
DE  Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0043679;
GO  GO:0005737;
GO  GO:0005815;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:1903136;
GO  GO:0007268;
GO  GO:1901214;
GO  GO:0007165;
GO  GO:0050808;
GO  GO:0048488;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGAKTKEGVVQSVTSVAEKTKEQANAVSEAVVSSVNTVATK
SQ  TVEEVENIAVTSGVVHKEALKQPVPSQEDEAAKAEEQVAEETKSGGD
//
ID  O76070;
PN  Gamma-synuclein;
GN  SNCG;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11746666}. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle.
DR  UNIPROT: O76070;
DR  UNIPROT: O15104;
DR  UNIPROT: Q96P61;
DR  Pfam: PF01387;
DR  OMIM: 602998;
DR  DisGeNET: 6623;
DE  Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q93063; IntAct: EBI-1060980; Score: 0.00
DE  Interaction: P25205; IntAct: EBI-1061588; Score: 0.00
DE  Interaction: A6NEW6; IntAct: EBI-1061794; Score: 0.00
DE  Interaction: P41235; IntAct: EBI-1062596; Score: 0.00
DE  Interaction: Q96AE4; IntAct: EBI-1063260; Score: 0.00
DE  Interaction: P17844; IntAct: EBI-1063704; Score: 0.00
DE  Interaction: P26038; IntAct: EBI-1064569; Score: 0.00
DE  Interaction: P63167; IntAct: EBI-1066918; Score: 0.00
DE  Interaction: P63162; IntAct: EBI-1070602; Score: 0.00
DE  Interaction: P15090; IntAct: EBI-1077459; Score: 0.00
DE  Interaction: P16035; IntAct: EBI-1082630; Score: 0.00
DE  Interaction: E9QKK1; IntAct: EBI-10995761; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: P54274; IntAct: EBI-11308211; Score: 0.51
DE  Interaction: Q9NYB0; IntAct: EBI-11308221; Score: 0.37
DE  Interaction: Q9NUX5; IntAct: EBI-11308231; Score: 0.37
GO  GO:0043679;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0005815;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005819;
GO  GO:1903136;
GO  GO:0008344;
GO  GO:0007268;
GO  GO:0009306;
GO  GO:0014059;
GO  GO:1901214;
GO  GO:0046928;
GO  GO:0050808;
GO  GO:0048488;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGAKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVATK
SQ  TVEEAENIAVTSGVVRKEDLRPSAPQQEGEASKEKEEVAEEAQSGGD
//
ID  Q2PFW6;
PN  Gamma-synuclein;
GN  SNCG;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle (By similarity). {ECO:0000250}.
DR  UNIPROT: Q2PFW6;
DR  Pfam: PF01387;
DE  Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005815;
GO  GO:0048471;
GO  GO:0005819;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGTKTKENVVHSVTSVAEKTKEQANAVSEAVVSSVNTVAAK
SQ  TVEEAENIAVTSGVVRKEDLKPSAPQQEGEAAKEKEEVAEEAQSGGD
//
ID  Q9Z0F7;
PN  Gamma-synuclein;
GN  Sncg;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9Z0F7;
DR  Pfam: PF01387;
DE  Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases. May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0005737;
GO  GO:0005815;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0043014;
GO  GO:0048487;
GO  GO:1903136;
GO  GO:0008344;
GO  GO:0007268;
GO  GO:1901215;
GO  GO:0009306;
GO  GO:0014059;
GO  GO:1901214;
GO  GO:0046928;
GO  GO:0050808;
GO  GO:0048488;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGTKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVANK
SQ  TVEEAENIVVTTGVVRKEDLEPPAQDQEAKEQEENEEAKSGED
//
ID  Q63544;
PN  Gamma-synuclein;
GN  Sncg;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle (By similarity). {ECO:0000250}.
DR  UNIPROT: Q63544;
DR  UNIPROT: Q6R2I0;
DR  Pfam: PF01387;
DE  Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases. May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0043679;
GO  GO:0005737;
GO  GO:0005815;
GO  GO:0043025;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005819;
GO  GO:0045202;
GO  GO:0043014;
GO  GO:0048487;
GO  GO:1903136;
GO  GO:0008344;
GO  GO:0002118;
GO  GO:0071464;
GO  GO:0007268;
GO  GO:1901215;
GO  GO:0007422;
GO  GO:0009306;
GO  GO:0014059;
GO  GO:1901214;
GO  GO:0046928;
GO  GO:0042220;
GO  GO:1904307;
GO  GO:0009410;
GO  GO:0050808;
GO  GO:0048488;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDVFKKGFSIAREGVVGAVEKTKQGVTEAAEKTKEGVMYVGTKTKGERGTSVTSVAEKTKEQANAVSEAVVSSVNTVATK
SQ  TVEEAENIVVTTGVVRKEDLEPPAQDQEAKEQEEGEEAKSGGD
//
ID  A6QPF8;
PN  Transmembrane protein 120B;
GN  TMEM120B;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q3TA38}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: A6QPF8;
DR  Pfam: PF07851;
DE  Function: Necessary for efficient adipogenesis. Does not show ion channel activity. {ECO:0000250|UniProtKB:Q3TA38}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0045444;
GO  GO:0051291;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGQLERCEREWHELEGEFQELQETHRIYKQKLEELNALQTSCSSSINKQKTRLKDLKLTLQRYKRHASREEAELVQQMG
SQ  ANIKERQNVFFDMEAYLPKKNGLYLNLVLGNVNVTLLSNQAKFAYKDEYEKFKLYLTIILLLGAVACRFFLHYRVTDEVF
SQ  NFLLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPNGLIYQKFRNQFLAFSIFQSCVQFLQYYYQRGC
SQ  LYRLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFCGHFWQLYNAVTLFELSSHEECREWQVFVLALTFLVLFLGNFLT
SQ  TLKVVHTKLQQNRSKAKKP
//
ID  Q1LY80;
PN  Transmembrane protein 120B;
GN  tmem120b;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q3TA38}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q1LY80;
DR  UNIPROT: Q503G6;
DR  Pfam: PF07851;
DE  Function: Necessary for efficient adipogenesis. Does not show ion channel activity. {ECO:0000250|UniProtKB:Q3TA38}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0045444;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLERCQSEWTEIEQEYQQLQETHKVYRQKLEELTNLQAICSSAISKQRKGLKDLKQSLYKCKKSCNGKDSEVINDLQVQ
SQ  IKERQNVFFDMEAYLPKRNGLYLNLVLGNVNVTLLSNQAKFAYKDEYEKFKLYMTIILMFGAVTCLFLLNYRVTDEIFNF
SQ  LLVWYYCTLTIRESILRSNGSRIKGWWVSHHYVSTFLSGVMLTWPEGPMYQMFRSQFLAFSIYQSCVQFLQYYYQSGCLY
SQ  RLRALGERNQLDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLYNAVTLFRLSALDDCKEWQVFMLALTFLVLFLGNFLTTL
SQ  KVVHQKLLKNKDKVKNN
//
ID  A0PK00;
PN  Transmembrane protein 120B;
GN  TMEM120B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q3TA38}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: A0PK00;
DR  UNIPROT: A0PK01;
DR  UNIPROT: B3KX33;
DR  PDB: 7F73;
DR  Pfam: PF07851;
DR  OMIM: 616551;
DR  DisGeNET: 144404;
DE  Function: Necessary for efficient adipogenesis. Does not show ion channel activity. {ECO:0000250|UniProtKB:Q3TA38}.
DE  Reference Proteome: Yes;
DE  Interaction: O95273; IntAct: EBI-10171540; Score: 0.56
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: P04233; IntAct: EBI-24527634; Score: 0.56
DE  Interaction: O15393; IntAct: EBI-24627404; Score: 0.56
DE  Interaction: P16871; IntAct: EBI-24660386; Score: 0.56
DE  Interaction: P48051; IntAct: EBI-24664480; Score: 0.56
DE  Interaction: Q9Y676; IntAct: EBI-24664779; Score: 0.56
DE  Interaction: Q6Q788; IntAct: EBI-24669107; Score: 0.56
DE  Interaction: Q96MV1; IntAct: EBI-24669083; Score: 0.56
DE  Interaction: Q15125; IntAct: EBI-24669908; Score: 0.56
DE  Interaction: P27105; IntAct: EBI-24683062; Score: 0.56
DE  Interaction: O15552; IntAct: EBI-24684201; Score: 0.56
DE  Interaction: Q8NBQ5; IntAct: EBI-24684557; Score: 0.56
DE  Interaction: Q9BRK0; IntAct: EBI-23722123; Score: 0.56
DE  Interaction: Q9H6H4; IntAct: EBI-24690333; Score: 0.56
DE  Interaction: P15941; IntAct: EBI-24693746; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-24702265; Score: 0.56
DE  Interaction: Q96AN5; IntAct: EBI-24704644; Score: 0.56
DE  Interaction: O43300; IntAct: EBI-24707730; Score: 0.56
DE  Interaction: Q14973; IntAct: EBI-24711872; Score: 0.56
DE  Interaction: Q8N5M9; IntAct: EBI-24716754; Score: 0.56
DE  Interaction: Q8IVP1; IntAct: EBI-24722810; Score: 0.56
DE  Interaction: Q3KNW5; IntAct: EBI-24723168; Score: 0.56
DE  Interaction: Q8TED1; IntAct: EBI-24723437; Score: 0.56
DE  Interaction: Q96HE8; IntAct: EBI-24728240; Score: 0.56
DE  Interaction: Q8NDX2; IntAct: EBI-24736389; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-24742564; Score: 0.56
DE  Interaction: O94778; IntAct: EBI-24743358; Score: 0.56
DE  Interaction: P20292; IntAct: EBI-24765164; Score: 0.56
DE  Interaction: Q05329; IntAct: EBI-24770377; Score: 0.56
DE  Interaction: Q6ZMZ0; IntAct: EBI-24781164; Score: 0.56
DE  Interaction: Q68DC2; IntAct: EBI-23887466; Score: 0.56
DE  Interaction: Q9Y282; IntAct: EBI-24792989; Score: 0.56
DE  Interaction: Q7Z7G2; IntAct: EBI-23904229; Score: 0.56
DE  Interaction: Q9NY72; IntAct: EBI-25278555; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-25278485; Score: 0.56
DE  Interaction: Q9NZD1; IntAct: EBI-25282611; Score: 0.56
DE  Interaction: P38484; IntAct: EBI-25285898; Score: 0.56
DE  Interaction: P21964; IntAct: EBI-25287369; Score: 0.56
DE  Interaction: O60238; IntAct: EBI-24405238; Score: 0.56
DE  Interaction: P32856; IntAct: EBI-24410169; Score: 0.56
DE  Interaction: Q9HDC5; IntAct: EBI-24580063; Score: 0.56
DE  Interaction: Q96BA8; IntAct: EBI-24595793; Score: 0.56
DE  Interaction: Q99942; IntAct: EBI-24637665; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-25162356; Score: 0.56
DE  Interaction: P43003; IntAct: EBI-24657364; Score: 0.56
DE  Interaction: P54219; IntAct: EBI-24657397; Score: 0.56
DE  Interaction: Q8IV31; IntAct: EBI-24747106; Score: 0.56
DE  Interaction: Q6IBW4; IntAct: EBI-25182243; Score: 0.56
DE  Interaction: P08034; IntAct: EBI-24760040; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24773940; Score: 0.56
DE  Interaction: Q9Y680; IntAct: EBI-24775230; Score: 0.56
DE  Interaction: Q96MV8; IntAct: EBI-24789391; Score: 0.56
DE  Interaction: Q5T7V8; IntAct: EBI-24803729; Score: 0.56
DE  Interaction: O14880; IntAct: EBI-25272707; Score: 0.56
DE  Interaction: Q9NXU5; IntAct: EBI-11898708; Score: 0.00
DE  Interaction: Q9NRZ7; IntAct: EBI-11898699; Score: 0.00
DE  Interaction: Q9BXJ8; IntAct: EBI-11898690; Score: 0.00
DE  Interaction: Q15155; IntAct: EBI-11914313; Score: 0.00
DE  Interaction: Q969V3; IntAct: EBI-11925934; Score: 0.00
DE  Interaction: Q9H1A3; IntAct: EBI-11931172; Score: 0.00
DE  Interaction: Q9NRX5; IntAct: EBI-11933933; Score: 0.00
DE  Interaction: P30825; IntAct: EBI-21505748; Score: 0.35
DE  Interaction: P48960; IntAct: EBI-21506471; Score: 0.35
DE  Interaction: Q92633; IntAct: EBI-21508694; Score: 0.35
DE  Interaction: Q9GZM5; IntAct: EBI-21509346; Score: 0.35
DE  Interaction: P16444; IntAct: EBI-21514808; Score: 0.35
DE  Interaction: Q16581; IntAct: EBI-21515265; Score: 0.35
DE  Interaction: Q16799; IntAct: EBI-21515832; Score: 0.35
DE  Interaction: Q6P5W5; IntAct: EBI-21515976; Score: 0.35
DE  Interaction: Q99679; IntAct: EBI-21516430; Score: 0.35
DE  Interaction: Q9H5K3; IntAct: EBI-21516902; Score: 0.35
DE  Interaction: Q9UGM1; IntAct: EBI-21517134; Score: 0.35
DE  Interaction: Q9UHP7; IntAct: EBI-21517465; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-27030072; Score: 0.35
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0045444;
GO  GO:0051291;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGQLERCEREWHELEGEFQELQETHRIYKQKLEELAALQTLCSSSISKQKKHLKDLKLTLQRCKRHASREEAELVQQMA
SQ  ANIKERQDVFFDMEAYLPKKNGLYLNLVLGNVNVTLLSNQAKFAYKDEYEKFKLYLTIILLLGAVACRFVLHYRVTDEVF
SQ  NFLLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPNGPIYQKFRNQFLAFSIFQSCVQFLQYYYQRGC
SQ  LYRLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFCGHFWQLYNAVTLFELSSHEECREWQVFVLAFTFLILFLGNFLT
SQ  TLKVVHAKLQKNRGKTKQP
//
ID  Q3TA38;
PN  Transmembrane protein 120B;
GN  Tmem120b;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:26024229}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q3TA38;
DR  UNIPROT: Q14BK6;
DR  UNIPROT: Q8R243;
DR  Pfam: PF07851;
DE  Function: Necessary for efficient adipogenesis (PubMed:26024229). Does not show ion channel activity (PubMed:32084332). {ECO:0000269|PubMed:26024229, ECO:0000269|PubMed:32084332}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0045444;
GO  GO:0051291;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGQLERCEREWHELEGEFQELQETHRIYKQKLEELTSLQTLCSTSISKQKRHLKDLKHTLQRYKRHSSHEEAALIQQMT
SQ  ANIKERQNVFFDMEAYLPKKNGLYLNLVLGNVSVTLLSNQAKFAYKDEYEKFKLYLTIILLLGAVACRFVLHYRVTDEVF
SQ  NFLLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPNGLIYQKFRNQFLAFSIFQSCVQFLQYYYQRGC
SQ  LYRLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFCGHFWQLYNAVTLFELSTHEECKEWQVFVLALTFLILFLGNFLT
SQ  TLKVVHAKLHKNRNKTKQP
//
ID  Q63ZG0;
PN  Transmembrane protein 120B;
GN  tmem120b;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q3TA38}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q63ZG0;
DR  Pfam: PF07851;
DE  Function: Necessary for efficient adipogenesis. Does not show ion channel activity. {ECO:0000250|UniProtKB:Q3TA38}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0045444;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLQKCQEEWGELEKEFQQLQETHKVYKQKLEELNGLQNLCSSYINKHKRRLTELKGNLHGYKHTSNVEEKELVQQINST
SQ  IKERHNAFFDMEAYLPKKNGLYLNLVLGNVNVTLLSNQAKFAYKDEYEKFKLYLTIILLLGAITCRFVLHYRVTDEVFNF
SQ  LLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPDGLMYQIFRNQFLAFSIYQSCVQFLQYYYQSGCLY
SQ  RLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLYNAITLFGLSRHEECKEWQVFVLALTFLLLFLGNFLTTL
SQ  KVVHTKFQKNKLKKP
//
ID  Q5EAX9;
PN  Transmembrane protein 120B-A;
GN  tmem120b;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q3TA38}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q5EAX9;
DR  Pfam: PF07851;
DE  Function: Necessary for efficient adipogenesis. Does not show ion channel activity. {ECO:0000250|UniProtKB:Q3TA38}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLQKCQEEWSEIEKEFQQLQETHKVYKQKLEELNSLQNLCSSCINKHKRRLTEFKGNLHGLKRTSNLEEKELVQQIDGT
SQ  IKERRNAFFDMEAYLPKKNGLYLNLVLGNVNVTLLSTQAKFAYKDEYEKFKLYLTIILLLGAITCRFVLNYRVTDEVFNF
SQ  LLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPDGLMYQIFRNQFLAFSIFQSCVQFLQYYYQSGCLY
SQ  RLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLYNAITLFGLSRHDACKEWQVFVLALTFLLLFLGNFLTTL
SQ  KVVHTKFQKNKLKKP
//
ID  Q6DE21;
PN  Transmembrane protein 120B-B;
GN  tmem120b;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q3TA38}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q6DE21;
DR  Pfam: PF07851;
DE  Function: Necessary for efficient adipogenesis. Does not show ion channel activity. {ECO:0000250|UniProtKB:Q3TA38}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLQKCQEEWGELEKEFQQLQETHKVYKQKLEELSSLQNLCSSYINKHKRRLTELKGNLHGYKHTSNLEEKELIQQIDGT
SQ  IKERHNAFFDMEAYLPKKNSLYLNLVLGNVNVTLLSKQTKFAYKDEYEKFKLYLTIILLLGAITCRFVLHYRVTDEVFNF
SQ  LLVWYFCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPDGLMYQMFRNQFLAFSIFQSCVQFLQYYYQSGCLY
SQ  RLRALGERNHLHLTVEGFQSWMWRGLTFLLPVLFFGHFWQLYNAMTLFGLSRHEECKEWQVFVLALTFLLLFLGNFLTTL
SQ  KVVHTKFQKNKLKKP
//
ID  Q5ZM31;
PN  Transmembrane protein 170A;
GN  TMEM170A;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WVE7}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WVE7}.
DR  UNIPROT: Q5ZM31;
DR  UNIPROT: Q5ZM01;
DR  Pfam: PF10190;
DE  Function: May regulate membrane morphogenesis in the endoplasmic reticulum (ER) by promoting ER sheet formation at the expense of ER tubules. {ECO:0000250|UniProtKB:Q8WVE7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0071786;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGSEAGGGGLLQQILSLRLVPRVGNGTTYSSPLSTFPEMWYGVFLWALVSSLSFHVPAALLALFTLRHHKYGRFMSVSL
SQ  LLMGIVGPITAGILTSAAIAGVYRAAGKKMIPFEALIFEVGQTFCVVVVSFLRILATL
//
ID  A3KPL7;
PN  Transmembrane protein 170A;
GN  tmem170a;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WVE7}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WVE7}.
DR  UNIPROT: A3KPL7;
DR  UNIPROT: Q6PCR5;
DR  Pfam: PF10190;
DE  Function: May regulate membrane morphogenesis in the endoplasmic reticulum (ER) by promoting ER sheet formation at the expense of ER tubules. {ECO:0000250|UniProtKB:Q8WVE7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0071786;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIEALIVGEMQDVQIGFVKQILSLNLVPRSNNTTCGNNTSLCDFSEMWYGVFLWAVVSSLIFHLPAALLALATLRRHKVA
SQ  RFFPLGILLMGIIGPLFGGVLTSAAIAGVYKAAGKSMFSLEALVFGVGQSLFIFIISFLRILATL
//
ID  Q8WVE7;
PN  Transmembrane protein 170A;
GN  TMEM170A;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26906412}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:26906412}.
DR  UNIPROT: Q8WVE7;
DR  UNIPROT: B2R4R3;
DR  UNIPROT: B4DPS4;
DR  UNIPROT: D3DUK2;
DR  UNIPROT: Q7Z6F3;
DR  Pfam: PF10190;
DR  DisGeNET: 124491;
DE  Function: Acts as a regulator of endoplasmic reticulum (ER) and nuclear envelope (NE) morphogenesis. Affects the ratio between tubular ER and ER sheets by promoting sheet formation at the expense of tubules. Influences NE expansion, nuclear pore complex formation and proper localization of inner nuclear membrane proteins (PubMed:26906412). {ECO:0000269|PubMed:26906412}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0071786;
GO  GO:0006998;
GO  GO:0051292;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEREGSGGSGGSAGLLQQILSLKVVPRVGNGTLCPNSTSLCSFPEMWYGVFLWALVSSLFFHVPAGLLALFTLRHHKYGR
SQ  FMSVSILLMGIVGPITAGILTSAAIAGVYRAAGKEMIPFEALTLGTGQTFCVLVVSFLRILATL
//
ID  Q9D342;
PN  Transmembrane protein 170A;
GN  Tmem170a;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WVE7}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WVE7}.
DR  UNIPROT: Q9D342;
DR  UNIPROT: A6H6Q8;
DR  Pfam: PF10190;
DE  Function: Acts as a regulator of endoplasmic reticulum (ER) and nuclear envelope (NE) morphogenesis. Affects the ratio between tubular ER and ER sheets by promoting sheet formation at the expense of tubules. Influences NE expansion, nuclear pore complex formation and proper localization of inner nuclear membrane proteins. {ECO:0000250|UniProtKB:Q8WVE7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0071786;
GO  GO:0006998;
GO  GO:0051292;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEREGSGGGGGSAGLLQQILSLKLVPRVGNGTLCPNSTSLCSFPEMWYGVFLWALMSSVFFHVPAGLLALFTLRHHKYGR
SQ  FMSVSILLMGIVGPITAGILTSAAIAGVYRAAGKEMIPFEALTLGTGQTFCVVVVSFLRVLATL
//
ID  Q6DF87;
PN  Transmembrane protein 170A;
GN  tmem170a;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WVE7}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q8WVE7}.
DR  UNIPROT: Q6DF87;
DR  Pfam: PF10190;
DE  Function: May regulate membrane morphogenesis in the endoplasmic reticulum (ER) by promoting ER sheet formation at the expense of ER tubules. {ECO:0000250|UniProtKB:Q8WVE7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0071786;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGGGGGLGGEPGLLQQILSLRLVPRVGNVTDCQRATLCSFPEMWYGVFLWALVSSLFFHIPAGLLALFTLRHHKYGRFM
SQ  SVGIFLMGVLGPISAGILTSAAIAGVYKAAGKEMIPFEALVLGVGQTFCVLIVSFLRILATL
//
ID  Q3YBM2;
PN  Transmembrane protein 176B;
GN  TMEM176B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q3YBM2;
DR  UNIPROT: B2RDK2;
DR  UNIPROT: D3DWZ7;
DR  UNIPROT: E9PAV4;
DR  UNIPROT: Q5BJI2;
DR  UNIPROT: Q9BT42;
DR  UNIPROT: Q9Y609;
DR  Pfam: PF04103;
DR  OMIM: 610385;
DR  DisGeNET: 28959;
DE  Function: May play a role in the process of maturation of dendritic cells. Required for the development of cerebellar granule cells (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9RMZ4; IntAct: EBI-2821487; Score: 0.00
DE  Interaction: Q96HP8; IntAct: EBI-24566788; Score: 0.56
DE  Interaction: P13473; IntAct: EBI-25873575; Score: 0.56
DE  Interaction: P17252; IntAct: EBI-25885177; Score: 0.56
DE  Interaction: P61981; IntAct: EBI-25902320; Score: 0.56
DE  Interaction: Q15047; IntAct: EBI-25909256; Score: 0.56
DE  Interaction: Q92993; IntAct: EBI-25912439; Score: 0.56
DE  Interaction: Q8TAP4; IntAct: EBI-25926210; Score: 0.56
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0009887;
GO  GO:0097028;
GO  GO:2001199;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTQNTVIVNGVAMASRPSQPTHVNVHIHQESALTQLLKAGGSLKKFLFHPGDTVPSTARIGYEQLALGVTQILLGVVSCV
SQ  LGVCLSLGPWTVLSASGCAFWAGSVVIAAGAGAIVHEKHPGKLAGYISSLLTLAGFATAMAAVVLCVNSFIWQTEPFLYI
SQ  DTVCDRSDPVFPTTGYRWMRRSQENQWQKEECRAYMQMLRKLFTAIRALFLAVCVLKVIVSLVSLGVGLRNLCGQSSQPL
SQ  NEEGSEKRLLGENSVPPSPSREQTSTAIVL
//
ID  Q9R1Q6;
PN  Transmembrane protein 176B;
GN  Tmem176b;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q9R1Q6;
DR  UNIPROT: Q9WU52;
DR  Pfam: PF04103;
DE  Function: May play a role in the process of maturation of dendritic cells (By similarity). Required for the development of cerebellar granule cells. {ECO:0000250, ECO:0000269|PubMed:16814752}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0097028;
GO  GO:2001199;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVQSTVTVNGVKVASTHPQSAHISIHIHQKSALEQLLGAVGSLKKFLSWPQARIHYGQLSLGVTQILLGLVSCALGVCLY
SQ  FGPWTELCAFGCAFWSGSVAILAGVGTIVHEKRQGKLSGQVSCLLLLACIATAAAATVLGVNSLIRQTSVPYYVEIFSTC
SQ  NPLQSSMDPGYGTVRYSDDSDWKTERCREYLNMMMNLFLAFCIMLTVVCILEIVVSVASLGLSLRSMYGRSSQALNEEES
SQ  ERKLLDGHPAPASPAKEKIPAIL
//
ID  Q5R8D6;
PN  Transmembrane protein 176B;
GN  TMEM176B;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q5R8D6;
DR  Pfam: PF04103;
DE  Function: May play a role in the process of maturation of dendritic cells. Required for the development of cerebellar granule cells (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0097028;
GO  GO:2001199;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTQNTVIVNGVAMDSRPSQPTHINVHIHQESALTQLLKAGGSLKKFLFHPGDTVPSTARIGYEQLALGVTQILLGVLSCA
SQ  LGVCLSLGPWTVLRASGCAFWAGSVAIAAGAGAIVHEKYPGKLAGYVSSLLTLAGFATVMAAVVLCVNSFIWQTEPFLYI
SQ  DTVCDRSDPVIPTTGYGWMWRSEEIQRQKEECRAYMQMLRKLFTAIRALFLAVCVLKVIVSLASLGVGLRNLCGQSSQPL
SQ  NEEGSEKRLLGENSVPPSPSREQTSTAIVL
//
ID  Q925D4;
PN  Transmembrane protein 176B;
GN  Tmem176b;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:16095493}; Multi-pass membrane protein {ECO:0000269|PubMed:16095493}.
DR  UNIPROT: Q925D4;
DR  Pfam: PF04103;
DE  Function: Required for the development of cerebellar granule cells (By similarity). May play a role in the process of maturation of dendritic cells. {ECO:0000250, ECO:0000269|PubMed:16095493}.
DE  Reference Proteome: Yes;
DE  Interaction: O15173; IntAct: EBI-22259161; Score: 0.35
DE  Interaction: P15127; IntAct: EBI-21294932; Score: 0.35
DE  Interaction: Q92569; IntAct: EBI-22254928; Score: 0.35
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0097028;
GO  GO:2001199;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAQATVTVDGVKVTSTRPQSAQISIHIHHKSALEQLLGAMGSLKKFLSYPQARIHYGQLSLGVTQILLGLVSCVLGVCLY
SQ  FGPWTELCASGCAFWSGSVAILAGVGIVIHEMGQGKLSGHISRLLLLACSATAAAATVMGVKSLIWQTSASYYFEISSTC
SQ  DSLQPSIVDRFRSVRFTDDSDWRTERCREYLRMMMNLFLAFCILFTVICILKIVVSVASLGLSLRSMCGRNSQVLNDEET
SQ  EKKLLGGDSAPASPTKEKIPVTP
//
ID  Q1RMW2;
PN  Transmembrane protein 184A;
GN  TMEM184A;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:26769966}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26769966}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:26769966}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q3UFJ6}; Multi-pass membrane protein {ECO:0000255}. Endosome {ECO:0000250|UniProtKB:Q3UFJ6}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q3UFJ6}. Note=Colocalizes with CAV1. {ECO:0000269|PubMed:26769966}.
DR  UNIPROT: Q1RMW2;
DR  Pfam: PF03619;
DE  Function: Acts as a heparin receptor in vascular cells (By similarity). May be involved in vesicle transport in exocrine cells and Sertoli cells (By similarity). {ECO:0000250|UniProtKB:Q3UFJ6, ECO:0000250|UniProtKB:Q4QQS1}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0031901;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030667;
GO  GO:0030658;
GO  GO:0008201;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTDTPGLLGTPLAWTPPARPAGPQMERAGNGSQGPGPLFLTSPLARGVSGVFVWAALVLTGHQIYLHLRSYTVPHEQRYI
SQ  IRLLFIVPVYAFDSWLSLLLLGGHQHYIYFDSVRDCYEAFVIYSFLSLCFQYLGGESAIMAEIRGKPVRTSCFHGTCCLR
SQ  GMTYSIGFLRFCKQATLQFCIVKPIMALVTIVLQAFGKYHDGDFNVRSGYLYITLVYNASVSLALYALFLFYSATRELLQ
SQ  PFEPVLKFLTIKAVIFLSFWQGLLLAILERCGVIPEVQVIDGSTVGAGTVAAGYQNFIICIEMLFASIALRYAFTCQVYS
SQ  EKTESSPAPSAPMQSISSGLKETMSPQDIVQDAIHNFSPAYQKYTQQATQEAPRPGQGSVPSPRTPTHSPDGGPGGGRKG
SQ  RNVEKRMLIPAEEL
//
ID  Q6ZMB5;
PN  Transmembrane protein 184A;
GN  TMEM184A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q4QQS1}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q4QQS1}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q3UFJ6}; Multi-pass membrane protein {ECO:0000255}. Endosome {ECO:0000250|UniProtKB:Q3UFJ6}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q3UFJ6}.
DR  UNIPROT: Q6ZMB5;
DR  UNIPROT: Q8TBQ6;
DR  Pfam: PF03619;
DR  DisGeNET: 202915;
DE  Function: Acts as a heparin receptor in vascular cells (By similarity). May be involved in vesicle transport in exocrine cells and Sertoli cells (By similarity). {ECO:0000250|UniProtKB:Q3UFJ6, ECO:0000250|UniProtKB:Q4QQS1}.
DE  Reference Proteome: Yes;
DE  Interaction: Q96PM5; IntAct: EBI-3943834; Score: 0.37
DE  Interaction: Q9Y2Z4; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q9UHR4; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q9P2J9; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q9H1K1; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q9H0Z9; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q9BY42; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q9BTE3; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q96SI1; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q96N66; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q6P996; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q6NVY1; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q5U5X0; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q5T440; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q4G176; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q16854; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q03135; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: P55196; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: P34897; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: P30038; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: P23921; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: P23368; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: P22033; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: P13984; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: P00966; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: O43847; IntAct: EBI-21763850; Score: 0.35
DE  Interaction: Q09666; IntAct: EBI-20917352; Score: 0.40
GO  GO:0030659;
GO  GO:0031901;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030667;
GO  GO:0030658;
GO  GO:0008201;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSNVSGILETAGVPLVSANWPQPSPPPAVPAGPQMDHMGNSSQGAPWLFLTSALARGVSGIFVWTALVLTCHQIYLHLRS
SQ  YTVPQEQRYIIRLLLIVPIYAFDSWLSLLLLGDHQYYVYFDSVRDCYEAFVIYSFLSLCFQYLGGEGAIMAEIRGKPIKS
SQ  SCLYGTCCLRGMTYSIGFLRFCKQATLQFCLVKPVMAVTTIILQAFGKYHDGDFNVRSGYLYVTLIYNASVSLALYALFL
SQ  FYFTTRELLRPFQPVLKFLTIKAVIFLSFWQGLLLAILERCGVIPEVETSGGNKLGAGTLAAGYQNFIICVEMLFASVAL
SQ  RYAFPCQVYAEKKENSPAPPAPMQSISSGIRETVSPQDIVQDAIHNFSPAYQHYTQQATHEAPRPGTHPSGGSGGSRKSR
SQ  SLEKRMLIPSEDL
//
ID  Q3UFJ6;
PN  Transmembrane protein 184A;
GN  Tmem184a;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q1RMW2}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:18321981}; Multi-pass membrane protein {ECO:0000305}. Endosome {ECO:0000269|PubMed:18321981, ECO:0000269|PubMed:19097053}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:19097053}. Note=Colocalizes with the secretory granule marker VAMP2 in pancreatic acinar cells (PubMed:19097053). {ECO:0000269|PubMed:19097053}.
DR  UNIPROT: Q3UFJ6;
DR  UNIPROT: Q8BII8;
DR  UNIPROT: Q8K1B0;
DR  Pfam: PF03619;
DE  Function: Acts as a heparin receptor in vascular cells (By similarity). May be involved in vesicle transport in exocrine cells and Sertoli cells (PubMed:18321981, PubMed:19097053). {ECO:0000250|UniProtKB:Q4QQS1, ECO:0000269|PubMed:18321981, ECO:0000269|PubMed:19097053}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0031901;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030667;
GO  GO:0030658;
GO  GO:0008201;
GO  GO:0018992;
GO  GO:0032880;
GO  GO:0051046;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRNASGFLKTAGAPLVSATWLPPSPPPAMPTVAAGPQMERVDNGSQGAPQLFLTSALARGVSGVFVWTALLLTGHQIYSH
SQ  LRSYTAPREQRFVIRLLFIVPIYAFDSWLSLLLLGGHPYYVYFDSVRDCYEAFVIYSFLTLCFQYLGGESAIMAEIRGKP
SQ  IRSSCFYGTCCLRGMSYSITFLRFCKQATLQFCIVKPVMALITIILQAFDKYHDGDFNIHSGYLYVTLVYNASVSLALYA
SQ  LFLFYFATRDLLRPFEPVLKFLTIKAIIFLSFWQGMLLAILERCGVIPEVQAVDGTRVGAGTLAAGYQNFLICVEMLFAS
SQ  LALRYAFPSQVYSEKKNSPVPPAPMQSISSGLKETISPQDIVQDAIHNFSPAYQQYTQQSTHEAPGPGQGGHPAPSTHPG
SQ  PASGSGGGKKSRNIEKRMLIPSEDL
//
ID  Q4QQS1;
PN  Transmembrane protein 184A;
GN  Tmem184a;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:26769966}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26769966}. Early endosome membrane {ECO:0000250|UniProtKB:Q3UFJ6}; Multi-pass membrane protein {ECO:0000305}. Endosome {ECO:0000250|UniProtKB:Q3UFJ6}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q3UFJ6}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with CAV1 (PubMed:26769966). {ECO:0000269|PubMed:26769966}.
DR  UNIPROT: Q4QQS1;
DR  UNIPROT: Q5XHY9;
DR  Pfam: PF03619;
DE  Function: Acts as a heparin receptor in vascular cells (PubMed:26769966). May be involved in vesicle transport in exocrine cells and Sertoli cells (By similarity). {ECO:0000250|UniProtKB:Q3UFJ6, ECO:0000269|PubMed:26769966}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0031901;
GO  GO:0005768;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0030667;
GO  GO:0030658;
GO  GO:0008201;
GO  GO:0018992;
GO  GO:0032880;
GO  GO:0051046;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRNASGFLKTAGAPLVSATWLPPSPPPAMPMVAAGPQMERVDNGSQGAPQLFLTSALARGVSGVFVWTALLLTGHQIYSH
SQ  LRSYTVPREQRFVIRLLFIVPIYAFDSWLSLLLLGGHPYYVYFDSVRDCYEAFVIYSFLTLCFQYLGGESAIMAEIRGKP
SQ  IRSSCFYGTCCLRGMSYSITFLRFCKQATLQFCIVKPVMALITIILQAFDKYHDGDFNIHSGYLYVTLVYNASVSLALYA
SQ  LFLFYFATRDLLRPFEPVLKFLTIKAIIFLSFWQGMLLAILERCGVIPEVQAVDGTRVGAGTLAAGYQNFLICIEMLFAS
SQ  LALRYAFPSQVYSEKKNSPAPPAPMQSISSGLKETISPQDIVQDAIHNFSPAYQQYTQQSTHEAPGPGQGGHPSPSTHPG
SQ  PASGSGGGKKSRNIEKRMLIPSEDL
//
ID  Q05B45;
PN  Ion channel TACAN;
GN  TMEM120A;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q05B45;
DR  Pfam: PF07851;
DE  Function: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli. May also be required for efficient adipogenesis. {ECO:0000250|UniProtKB:Q8C1E7}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0005886;
GO  GO:0005216;
GO  GO:0050966;
GO  GO:0045444;
GO  GO:0034220;
GO  GO:0051291;
GO  GO:0051260;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MHPPPPGPLGDCLRDWEELQQDFHGIQETHRLYRLKLEELTKLQNSCTSSITRQKKRLQELALVLRKCKPSLPSEAEEAA
SQ  RELENQIKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILILISFTCRFLLNSRVT
SQ  DAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYY
SQ  QSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLARDPECKEWQVLMCGFPFLLLFLG
SQ  NFFTTLRVVHQKFHNQLHGSKKE
//
ID  A3KNK1;
PN  Ion channel TACAN;
GN  tmem120a;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: A3KNK1;
DR  Pfam: PF07851;
DE  Function: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli. May also be required for efficient adipogenesis. {ECO:0000250|UniProtKB:Q8C1E7}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0005886;
GO  GO:0005216;
GO  GO:0050966;
GO  GO:0045444;
GO  GO:0034220;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLFNPTGLTECLQEWEDLEKDYQQIQDTHRHYKHKLEEVSKLQESCSSSIARQRKKLKDLSESLEECKGAVNPEDVNKID
SQ  DIQESIKERPNVFFEMEAFLPKKNGLYLSLVLGNVNVTLLNKQSKFAYKDEYEKFKLYLTVLLLFFSFTCRFLVSYRVVD
SQ  ALFNFLLVWYYCTLTIRESILINNGSKIKGWWVFQHYVSTFLSGVMLTWPDGELYQMFRNQFLSYSMYINFVQFFQYYYQ
SQ  SGCLYRLRALGERHNMDLTVEGFQSWMWRGLTFLLPFLFLGHFFQLYNGITLFQMTQLPEWKEWQVLMCGSTFLVLFMGN
SQ  FFTTLGVVYHKYMDQDKAKGL
//
ID  Q9BXJ8;
PN  Ion channel TACAN;
GN  TMEM120A;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q9BXJ8;
DR  UNIPROT: Q86TE9;
DR  UNIPROT: Q8N6P1;
DR  PDB: 7CXR;
DR  PDB: 7F3T;
DR  PDB: 7F3U;
DR  PDB: 7F6V;
DR  PDB: 7N7P;
DR  Pfam: PF07851;
DR  OMIM: 616550;
DR  DisGeNET: 83862;
DE  Function: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli (By similarity). May also be required for efficient adipogenesis (PubMed:26024229). {ECO:0000250|UniProtKB:Q8C1E7, ECO:0000269|PubMed:26024229}.
DE  Reference Proteome: Yes;
DE  Interaction: A0PK00; IntAct: EBI-11898690; Score: 0.00
DE  Interaction: Q15125; IntAct: EBI-22754310; Score: 0.56
DE  Interaction: Q5JX71; IntAct: EBI-24660892; Score: 0.56
DE  Interaction: P17174; IntAct: EBI-737777; Score: 0.00
DE  Interaction: Q0WED3; IntAct: EBI-2853354; Score: 0.00
DE  Interaction: P36873; IntAct: EBI-4311720; Score: 0.37
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: O55143; IntAct: EBI-11062077; Score: 0.35
DE  Interaction: P32856; IntAct: EBI-24487399; Score: 0.56
DE  Interaction: Q16623; IntAct: EBI-24508438; Score: 0.56
DE  Interaction: Q9NPE6; IntAct: EBI-22744045; Score: 0.56
DE  Interaction: Q13323; IntAct: EBI-22746810; Score: 0.56
DE  Interaction: Q9Y394; IntAct: EBI-22755933; Score: 0.56
DE  Interaction: Q96MV8; IntAct: EBI-22756449; Score: 0.56
DE  Interaction: Q9H6H4; IntAct: EBI-22759718; Score: 0.56
DE  Interaction: Q6PEY1; IntAct: EBI-22760479; Score: 0.56
DE  Interaction: Q53TN4; IntAct: EBI-24668256; Score: 0.56
DE  Interaction: Q9NY72; IntAct: EBI-23746487; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24706237; Score: 0.56
DE  Interaction: Q8N386; IntAct: EBI-24713800; Score: 0.56
DE  Interaction: Q6ZUI0; IntAct: EBI-24734735; Score: 0.56
DE  Interaction: Q7Z5P4; IntAct: EBI-23899898; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-23916710; Score: 0.56
DE  Interaction: Q8WUV1; IntAct: EBI-24575430; Score: 0.56
DE  Interaction: Q53FV1; IntAct: EBI-24644037; Score: 0.56
DE  Interaction: Q53FP2; IntAct: EBI-24644818; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-25169004; Score: 0.56
DE  Interaction: O15243; IntAct: EBI-24774713; Score: 0.56
DE  Interaction: Q8N661; IntAct: EBI-24776791; Score: 0.56
DE  Interaction: Q15155; IntAct: EBI-11914331; Score: 0.00
DE  Interaction: Q969V3; IntAct: EBI-11925943; Score: 0.00
DE  Interaction: Q9NXU5; IntAct: EBI-11930605; Score: 0.00
DE  Interaction: Q9NRZ7; IntAct: EBI-11930596; Score: 0.00
DE  Interaction: Q9H1A3; IntAct: EBI-11931199; Score: 0.00
DE  Interaction: Q9NRX5; IntAct: EBI-11933960; Score: 0.00
DE  Interaction: O00322; IntAct: EBI-21504674; Score: 0.35
DE  Interaction: Q9GZM5; IntAct: EBI-21509346; Score: 0.35
DE  Interaction: Q6P5W5; IntAct: EBI-21515976; Score: 0.35
DE  Interaction: Q9H5K3; IntAct: EBI-21516902; Score: 0.35
DE  Interaction: Q9UHP7; IntAct: EBI-21517465; Score: 0.35
DE  Interaction: O60512; IntAct: EBI-21566019; Score: 0.35
DE  Interaction: Q5VXT5; IntAct: EBI-21760866; Score: 0.35
DE  Interaction: P06576; IntAct: EBI-21800967; Score: 0.35
DE  Interaction: Q9NZH0; IntAct: EBI-20808301; Score: 0.37
DE  Interaction: P25105; IntAct: EBI-20811194; Score: 0.37
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0005886;
GO  GO:0005216;
GO  GO:0050966;
GO  GO:0045444;
GO  GO:0034220;
GO  GO:0051291;
GO  GO:0051260;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQPPPPGPLGDCLRDWEDLQQDFQNIQETHRLYRLKLEELTKLQNNCTSSITRQKKRLQELALALKKCKPSLPAEAEGAA
SQ  QELENQMKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILILISFTCRFLLNSRVT
SQ  DAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYY
SQ  QSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLAQDPQCKEWQVLMCGFPFLLLFLG
SQ  NFFTTLRVVHHKFHSQRHGSKKD
//
ID  Q8C1E7;
PN  Ion channel TACAN;
GN  Tmem120a;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000269|PubMed:32084332}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:20091084}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q8C1E7;
DR  UNIPROT: Q8BWP7;
DR  PDB: 7N0K;
DR  PDB: 7N0L;
DR  Pfam: PF07851;
DE  Function: Ion channel involved in sensing mechanical pain (PubMed:32084332). Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli (PubMed:32084332). May also be required for efficient adipogenesis (PubMed:26024229). {ECO:0000269|PubMed:26024229, ECO:0000269|PubMed:32084332}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0005886;
GO  GO:0005216;
GO  GO:0050966;
GO  GO:0045444;
GO  GO:0034220;
GO  GO:0051291;
GO  GO:0051260;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQSPPPDPLGDCLRNWEDLQQDFQGIQETHRLYRLKLEELTKLQANCTNSITRQKKRLQELALVLKKCRPSLPSESMEAA
SQ  QELENQMKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILIVISFTCRFLLNSRVT
SQ  DAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYY
SQ  QSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLARDPECKEWQVLMCGFPFLLLFLG
SQ  NFFTTLRVVHQKFHSQQHGNKKD
//
ID  Q5HZE2;
PN  Ion channel TACAN;
GN  Tmem120a;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q5HZE2;
DR  Pfam: PF07851;
DE  Function: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli. May also be required for efficient adipogenesis. {ECO:0000250|UniProtKB:Q8C1E7}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0005886;
GO  GO:0005216;
GO  GO:0050966;
GO  GO:0045444;
GO  GO:0034220;
GO  GO:0051291;
GO  GO:0051260;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQSPPPDPLGDCLRNWEDLQQDFQGIQETHRLYRVKLEELTKLQDNCTNSITRQKKRLQELALVLKKCRPSLPSESLEAA
SQ  QELESQIKERQGLFFDMEAYLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILIVISFTCRFLLNSRVT
SQ  DAAFNFLLVWYYCTLTIRESILINNGSRIKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYY
SQ  QSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLARDPECKEWQVLMCGLPFLLLFLG
SQ  NFFTTLRVVHQKFHSQQHGSKKD
//
ID  A1L2R7;
PN  Ion channel TACAN;
GN  tmem120a;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: A1L2R7;
DR  Pfam: PF07851;
DE  Function: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli. May also be required for efficient adipogenesis. {ECO:0000250|UniProtKB:Q8C1E7}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005886;
GO  GO:0005216;
GO  GO:0050966;
GO  GO:0034220;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSPVLQDCVREWGEIQENYQDIQETHRLYKQKLEELSKLQTRCSGTISRQKKKLRELSVELKKCKSKAKNVEEEEEQIR
SQ  DLNNQIRAREKTFFEMESFLPKKNGLYLSLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILMVLSFICRFLLNSRVTD
SQ  AVFNFLLVWYYCTLTIRESILINNGSRIKGWWVLNHYISTFLSGVMLTWPDGLMYQMFRNQFLSFSMYQSFVQFLQYYYQ
SQ  SGCLYRLRALGERHNMDLTVEGFQSWMWRGLTFLLPFLFFGQFWQLYNAITLFKLARHPECKEWQVIMCGLPFLVHFLGN
SQ  FFTTLRVVHQKFQKQN
//
ID  Q5FWV6;
PN  Ion channel TACAN;
GN  tmem120a;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q5FWV6;
DR  Pfam: PF07851;
DE  Function: Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli. May also be required for efficient adipogenesis. {ECO:0000250|UniProtKB:Q8C1E7}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0005886;
GO  GO:0005216;
GO  GO:0050966;
GO  GO:0045444;
GO  GO:0034220;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNSPALQDCVRDWGELQENYQDIQETHRLYKQKLEELAKLQTRCSGTIARQKKKLKELSVELKKYKSSVKNVEEEEEQIS
SQ  VLNNQIRIREKTFFEMESFLPKKNGLYLSLVLGNVNVTLLSKQSKFAYKDEYEKFKLYLTMILMVLSFICRFVLNSRVTD
SQ  AVFNFLLVWYYCTLTIRESILINNGSRIKGWWVLNHYISTFLSGVMLTWPDGLMYQMFRNQFLSFSMYQSFVQFLQYYYQ
SQ  SGCLYRLRALGERHNMDLTVEGFQSWMWRGLTFLLPFLFFGQFWQLYNAITLFKLARHPECKEWQVIMCGLPFLVHFLGN
SQ  FFTTLRVVHQKFQKQN
//
ID  Q8IXB3;
PN  Trafficking regulator of GLUT4 1;
GN  TRARG1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C838}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8C838}. Endomembrane system {ECO:0000250|UniProtKB:Q8C838}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8C838}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8C838}. Note=Shifts from low-density microsome vesicles to the cell membrane upon insulin stimulation. {ECO:0000250|UniProtKB:Q8C838}.
DR  UNIPROT: Q8IXB3;
DR  UNIPROT: A6NMK4;
DR  Pfam: PF04505;
DR  OMIM: 612211;
DR  DisGeNET: 286753;
DE  Function: Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. Not required for SLC2A4 membrane fusion upon an initial stimulus, but rather is necessary for proper protein recycling during prolonged insulin stimulation. {ECO:0000250|UniProtKB:Q8C838}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NWS8; IntAct: EBI-21815645; Score: 0.35
DE  Interaction: Q92973; IntAct: EBI-21815645; Score: 0.35
DE  Interaction: Q7L1Q6; IntAct: EBI-21815645; Score: 0.35
DE  Interaction: Q4LE60; IntAct: EBI-21815645; Score: 0.35
DE  Interaction: P54707; IntAct: EBI-21815645; Score: 0.35
DE  Interaction: O95470; IntAct: EBI-21815645; Score: 0.35
GO  GO:0030659;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032869;
GO  GO:0099638;
GO  GO:0044381;
GO  GO:0072659;
GO  GO:0099500;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAHPVQSEFPSAQEPGSAAFLDLPEMEILLTKAENKDDKTLNLSKTLSGPLDLEQNSQGLPFKAISEGHLEAPLPRSPSR
SQ  ASSRRASSIATTSYAQDQEAPRDYLILAVVACFCPVWPLNLIPLIISIMSRSSMQQGNVDGARRLGRLARLLSITLIIMG
SQ  IVIIMVAVTVNFTVQKK
//
ID  Q8C838;
PN  Trafficking regulator of GLUT4 1;
GN  Trarg1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404, ECO:0000269|PubMed:29787242}; Single-pass membrane protein {ECO:0000305|PubMed:29787242}. Endomembrane system {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}; Single-pass membrane protein {ECO:0000305|PubMed:29787242}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26240143}. Note=Shifts from low-density microsome vesicles to the cell membrane upon insulin stimulation. {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}.
DR  UNIPROT: Q8C838;
DR  Pfam: PF04505;
DE  Function: Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. Not required for SLC2A4 membrane fusion upon an initial stimulus, but rather is necessary for proper protein recycling during prolonged insulin stimulation. {ECO:0000269|PubMed:26240143, ECO:0000269|PubMed:26629404}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032869;
GO  GO:0099638;
GO  GO:0051649;
GO  GO:0044381;
GO  GO:0072659;
GO  GO:0099500;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MANPAQPPLQDPGSTSPLELPEMEKLLTKVENKDDQALNLSKSLSGALDLEQNGHSLPFKVISEGHRQPSLSGSPSRVSS
SQ  RRASSVITTSYAQDQEAPKDYLVLAIASCFCPVWPLNLIPLIFSIMSRSSVQQGDLDGARRLGRLARLLSITFIILGIVI
SQ  IIVAVTVNFTVPK
//
ID  Q2MHH0;
PN  Trafficking regulator of GLUT4 1;
GN  Trarg1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C838}; Single-pass membrane protein {ECO:0000305}. Endomembrane system {ECO:0000269|PubMed:26240143}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26240143}. Note=Shifts from low-density microsome vesicles to the cell membrane upon insulin stimulation. {ECO:0000250|UniProtKB:Q8C838}.
DR  UNIPROT: Q2MHH0;
DR  Pfam: PF04505;
DE  Function: Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. Not required for SLC2A4 membrane fusion upon an initial stimulus, but rather is necessary for proper protein recycling during prolonged insulin stimulation. {ECO:0000305|PubMed:17007998, ECO:0000305|PubMed:26240143}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032869;
GO  GO:0099638;
GO  GO:0051649;
GO  GO:0044381;
GO  GO:0072659;
GO  GO:0099500;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MANPVQPQLQDPGSTSPLDLPEMEKLLTKVENKDDQALNLSKSLSGALDLEQNGHSLPFKVISEGHRQPSLSGSPSRASS
SQ  RRASSVVTTSYAQDQEAPKDYLVLAIASCFCPVWPLNLIPLIFSIMSRSSVQQGDLDGARRLGRLARLLSITFIILGIVI
SQ  IIVAVTVNFTVPK
//
ID  Q6DFT4;
PN  Trafficking regulator of GLUT4 1;
GN  trarg1;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C838}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8C838}. Endomembrane system {ECO:0000250|UniProtKB:Q8C838}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8C838}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8C838}. Note=Shifts from low-density microsome vesicles to the cell membrane upon insulin stimulation. {ECO:0000250|UniProtKB:Q8C838}.
DR  UNIPROT: Q6DFT4;
DR  Pfam: PF04505;
DE  Function: Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. {ECO:0000250|UniProtKB:Q8C838}.
DE  Reference Proteome: Yes;
GO  GO:0030659;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032869;
GO  GO:0099638;
GO  GO:0044381;
GO  GO:0072659;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAINTDTQYEKALGGSGNPLPADSHETEKLLTNASENKEENGMKKSFSVTMSSEKSMGDLEQNGHNLPYKSVSAGQLESA
SQ  PLSPSRVSLARASSTATTAQEQGRPTDYLVLAIFSCFCPVWPVNIVALVFSIMSRNSLQQGDLDGARRLGRLARLLSVVS
SQ  ILLGLVIIVLCILSLTIFH
//
ID  P38114;
PN  Uncharacterized transcriptional regulatory protein TBS1;
GN  TBS1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
DR  UNIPROT: P38114;
DR  UNIPROT: D6VQE5;
DR  UNIPROT: E9PAD3;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: Involved in tolerance to thiabendazole. {ECO:0000269|PubMed:10628851}.
DE  Reference Proteome: Yes;
DE  Interaction: Q12019; IntAct: EBI-7777540; Score: 0.44
DE  Interaction: Q12343; IntAct: EBI-2344772; Score: 0.37
DE  Interaction: Q12180; IntAct: EBI-2346028; Score: 0.37
DE  Interaction: P39743; IntAct: EBI-7481040; Score: 0.37
DE  Interaction: P32790; IntAct: EBI-7491226; Score: 0.37
DE  Interaction: P10591; IntAct: EBI-3773814; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3784377; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3791956; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3795924; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3807996; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3814684; Score: 0.35
DE  Interaction: P53900; IntAct: EBI-3821621; Score: 0.35
DE  Interaction: P39078; IntAct: EBI-3822865; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3829736; Score: 0.35
DE  Interaction: P07703; IntAct: EBI-16280355; Score: 0.35
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0005739;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0043565;
GO  GO:0008270;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNMDSGITSSHGSMDKTQKQSSEWAANQKHNQRVENTRVLMGPAVPAMPPVPSNFPPVPTGTIMSPQLSPFPDHRLRHHP
SQ  LAHMMPADKNFLAYNMESFKSRVTKACDYCRKRKIRCTEIEPISGKCRNCIKYNKDCTFHFHEELKRRREEALNNKGNGK
SQ  SVKKPRLDKENKFKDENFDIAVRSRNTSSTDSSPKLHTNLSQEYIGVSAGKSASDKEDTWPDFVPIDRTVLEKIELNHTK
SQ  VAGKVFVLEEICKNMKGTIEKLAEKSKIDVIDKEYMKRPKRKQYSKALLTKQKMFHFRQNVLSHLTDEEFLSPINEMFTT
SQ  TFKYSILQTKLVLDFSFRSASSPSSDNILYPLPRLAIAKRLLKNIKCPSLASLLHIVDVDQCLQFADVHFDPAKGRLTSS
SQ  QAFLLNICLCLGATVTNFEEKQELVDEDNHETYYFEKFELWRLRSFTFLNSVYYYHKLSVARADMTALKALLLLAKFAQQ
SQ  KISASSAVKVLSVAIKVALDLRLNLHSTYEDLELDEIIKRRRLWCYCFSTDKFFSVVLSRPPFLKEENTDVLTDESYVEL
SQ  FRDKILPNLSIKYDDSKLEGVKDIVSVVNLLANHLEYVPYIQSYFLSRLSLIESQIYYSCFSIRTTLDDTLDEIIENVLE
SQ  NQKALDRMRDDLPTILSLENYKENMRILSLDSSKLDFEVSCCTTILLHLRWYHQKITLSLFVISIIGDNLDQRESSRHDI
SQ  AEIIRRSRLDFKRNCIEVLNILKDFEYYPTVQNEFLYFSLTTVFSMFLYLSEIMVNDEHAMETGYIIGLLRDTHTRMLGS
SQ  EERCLSVHNLKWQTSLFFYTFFLRSTMEKFNLTSKYAKFYAFDSNYYEGVLNRLVKHTRESKDDMVELLKTSFINKEKMA
SQ  AFGSFVTEDQEKMEVSFNIFNEITIQDLNFLQFSSIPKLWENKTLEPGEEYHHSNGTNTDNNETTGADDTDDNNNNNNNN
SQ  NKNGNNSSSTINNNNNNYSNSNNNDNDNNINDDDDDDDDDDDDDDDDDDDDDNDDDYSNNGADDDEEDDDYDRSLFPTGL
SQ  ASLLDASYPERTANDYRDENEQSNKLFEKIEGHLEHGVFFYDRDFFFKNVCVKM
//
ID  Q1XG89;
PN  Putative ATP-dependent RNA helicase TDRD12;
GN  TDRD12;
OS  7091;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome {ECO:0000269|PubMed:17098166}. Cytoplasm, cytosol {ECO:0000269|PubMed:17098166}. Nucleus membrane {ECO:0000269|PubMed:17098166}; Peripheral membrane protein. Note=At 36 hours after oviposition, detected in the nucleus and the cytosol where it is associated with chromosomes and to the surface of the nuclear membrane (PubMed:17098166). Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:24067652). {ECO:0000269|PubMed:17098166, ECO:0000269|PubMed:24067652}.
DR  UNIPROT: Q1XG89;
DR  UNIPROT: H9JJS3;
DR  Pfam: PF04969;
DR  Pfam: PF00270;
DR  Pfam: PF00567;
DR  PROSITE: PS51203;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS50304;
DE  Function: Probable ATP-binding RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. {ECO:0000305|PubMed:26669262}.
DE  Reference Proteome: Yes;
GO  GO:0005694;
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0043186;
GO  GO:1990923;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003676;
GO  GO:0003724;
GO  GO:0030154;
GO  GO:0031047;
GO  GO:0051321;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MASDYYQVEILHYLNPNLIWVEVLNSPNEISFEQLGVYGILPIDASLDVERPGLKLQRSEDWMPATAILMKNIFQNLEQV
SQ  WFSPTHIDRRSSIFDNNIHKYGELIIKKNGVQLYLSKELVKAGLATEDPCQFHQYMSLGKIKTKLSNTETRAVIKNLEEY
SQ  YRKSSKPKELWQKSVHQNTSIFHAGERLQALTVKNLERHNNRQNIMLLENKLKDLEQCKGSDEVSLGRGVCRVPSNKSEM
SQ  VMLTNKRLKNRLELLSKINMKSDATDAVKSTKRNFSGDGQRKNFENDFESDDESVKKVSIANTINTSDGSANVVDKLLDE
SQ  KQIDNVFNNKKQICYTESTRRNPVKKAACIVYGPPSINIDKLPLKEAPKMTKTVKWTPHVDCDKEASEVSFGDVDSHVKL
SQ  DVKNLDKFHEIADRIEIEKTIPVDVNIHKDLYDSMINNKNESESKIMETANLKTEMKNLRKSSILQSKLKQFDKFNVSSN
SQ  SAASESSTKSSMDSSRISDEDDLSSDDEMSEIMETFKLNLATPKKSEAKHTIDHIEVNNTKLNANPFKNLDGSKSVFVDK
SQ  LTSPVLLVHTKRNNKVQPCSLLRDVPFGTSIHVVLRNMGIKHPTRLQTVSWGTILRGLSTFLISPPRSGKTMGYLPAVCR
SQ  LVRDFRKESPDSCGPKCIIVCATSKSVSEVERISKMLLGLEDKVFACYSGMDNLSVTTALLNGCDLLICTPKSIVRLLQN
SQ  DLSVDLRDLTTFVVDDCERISDVYSNEVKYVLYEIKNMLKNRVNKELKVQIVVASRIWCDFLEPIVLKAPDSVVCIGAFQ
SQ  ELILYSKISTTVDFLRPENKIANVLQFIDSVQGPKRTVVVCRADNEVKAVESSLRYNNRVVFACDNTMNIHDLYNLNVVW
SQ  GDFEDPTLGPILVCCDSNLVHLNVTDASYLIHYSLPALFSTFCKRFSVLNDNYPSIFKNESRDLKVKVLMDESNVEQLPK
SQ  ILNFLKRCTENVPKILDEVSEKILNEKDLAKVKDLVPLCDNLLSLGICPDTWNCTERHRIFKECDSPADWIPKNGVVTFQ
SQ  ILYFHSAVMYSARLLSNTVDGETTKYPQTYSTLSLKMGMYFSKESSRRLHGIPMVGDVCAVSKKQNFFIRCQVVKIISFY
SQ  KNGNPNYVVIKLIDEEKFEQSRDIYLYHLPDEFKDMKTYVVQVRLANIQPQDKDITFSCLAKNELEKIVEKNEDLFMRGH
SQ  VAMSVGSCIFVDTLEACLDLSSLSETVVRHNFKQELLNAHAVPNPKHLSILEEMCEKSGLIVKAVTNEQVVPKPIPVLPA
SQ  AQWAHLEDDLSSVYLASVEDMDKLFVRLVKFESCMKLLNIEINKYVSENTVPLDGSNVGDIVLAKFPDDSMYERARIDHI
SQ  YSEDKVKCFFVDQGDWRDVSTNDLATITENFITQLPFQAIECRLIGIRPFGEQWTEFSTNWFSDHCFEDAKGNLKHLYVK
SQ  HFTKEKADCTGGHKYGVALIDTYTNEDIIVNQLLIDLNLAKENVDEIAYLSEIKCNKTVLNNDATVDEEEGSLSGVSEPE
SQ  SNINVPLDKVFLKAPIRSVPLVDSEYETSDSDTWQINRPEDFKALFMRTRPESSKIIPMITANEVQNNADGETSKDTSTI
SQ  LEEKGQLPEKVKDDELKLSKPKICWSQNKNTVKLKILIAGIEDYKLKIEDRAVAFSANHCDVEYGFKLELYGVVDVNKSR
SQ  HSNKGQYVLVTMTKLMCRNWLALTKEGDSQKWIVYDVDTIEASSDEEVYRDDTLEVIKNIHNTNNGSDSEDDDFLDDVS
//
ID  P54811;
PN  Transitional endoplasmic reticulum ATPase homolog 1;
GN  cdc;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:25721663}. Cytoplasm {ECO:0000269|PubMed:17369820}. Note=Colocalizes with ubxn-1, ubxn-2 and ubxn-3 to the perinuclear region in spermatocytes (PubMed:20977550). Localizes to the perinuclear region in intestinal cells (PubMed:25721663). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:25721663}.
DR  UNIPROT: P54811;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF02933;
DR  Pfam: PF02359;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates (PubMed:18854144, PubMed:18782221, PubMed:22768338). Can also prevent aggregation of unfolded proteins also in an ATP- independent manner (PubMed:18782221). Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains (PubMed:19545544). Involved in the cytoplasmic elimination of misfolded proteins exported from the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260). This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260). In association with helicase him-6 and GTPase crp-1, regulates the unfolded protein response (UPR) following ER stress, probably independently of the ERAD pathway (PubMed:18458060). Together with udf-2 and chn-1, regulates myosin assembly in body wall muscles by targeting myosin chaperone unc- 45 for proteasomal degradation (PubMed:17369820). Together with the ufd-1-npl-4 complex, controls the switch from spermatogenesis to oogenesis by regulating E3 ligase cul-2 complex-mediated tra-1 proteasomal degradation (PubMed:19773360). During oocyte meiosis and together with cdc-48.2, required for chromosome condensation at the diakinesis phase in prophase I and for progression of metaphase I (PubMed:17512499). During the first embryonic cell division, regulates DNA replication and thus chromosome segregation and decondensation, and nuclear envelope re-assembly (PubMed:18097415, PubMed:18854144, PubMed:18728180, PubMed:21981920, PubMed:26842564, PubMed:28368371). In S phase and in association with ufd-1, npl-4.1 and/or npl-4.2 and ubxn- 3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CMG helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5 (PubMed:21981920, PubMed:26842564, PubMed:28368371). Regulates ubxn-3 nuclear localization during S phase (PubMed:26842564). During the first embryonic cell divisions and together with cdc-48.2, regulates the re- assembly of the nuclear envelope after mitosis possibly by inactivating kinase air-2, a component of the chromosomal passenger complex (CPC) (PubMed:18097415). However, in another study, cdc-48.1 does not appear to be implicated in the regulation of air-2 (PubMed:18854144). {ECO:0000269|PubMed:16647269, ECO:0000269|PubMed:17369820, ECO:0000269|PubMed:17512499, ECO:0000269|PubMed:17825049, ECO:0000269|PubMed:18097415, ECO:0000269|PubMed:18458060, ECO:0000269|PubMed:18728180, ECO:0000269|PubMed:18782221, ECO:0000269|PubMed:18854144, ECO:0000269|PubMed:19545544, ECO:0000269|PubMed:19773360, ECO:0000269|PubMed:21317884, ECO:0000269|PubMed:21981920, ECO:0000269|PubMed:22768338, ECO:0000269|PubMed:25652260, ECO:0000269|PubMed:26842564, ECO:0000269|PubMed:28368371}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9TXH9; IntAct: EBI-2412436; Score: 0.62
DE  Interaction: G5EC44; IntAct: EBI-344171; Score: 0.00
DE  Interaction: Q17425; IntAct: EBI-2411420; Score: 0.49
DE  Interaction: P54812; IntAct: EBI-2412428; Score: 0.62
DE  Interaction: Q22557; IntAct: EBI-2412451; Score: 0.49
DE  Interaction: O17850; IntAct: EBI-2412440; Score: 0.49
DE  Interaction: Q94230; IntAct: EBI-2412444; Score: 0.49
DE  Interaction: Q22560; IntAct: EBI-6458355; Score: 0.37
DE  Interaction: P54811; IntAct: EBI-6460441; Score: 0.55
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0034098;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0042802;
GO  GO:0031593;
GO  GO:0044877;
GO  GO:0097352;
GO  GO:0008340;
GO  GO:0009792;
GO  GO:0071712;
GO  GO:0051228;
GO  GO:0045977;
GO  GO:0032436;
GO  GO:1905634;
GO  GO:0030970;
GO  GO:0030433;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASVPTHQSEKEKKNDELSTAILKDKVKPNRLIVDQSEQDDNSVIAVSQAKMDELGLFRGDAVILKGKKRKESVAIIVSD
SQ  ESCPNEKVRMNRVVRNNLRIRLGDVVSITPAPNLSYGTRIHVLPIDDTIEGLTGNLFDVFLKPYFLEAYRPLHKGDIFTV
SQ  QAAMRTVEFKVVETEPAPACIVSPDTMIHYEGDPIKREEEEESMNDIGYDDLGGVRKQLAQIKEMVELPLRHPQLFKAIG
SQ  IKPPRGILLFGPPGTGKTLIARAVANETGSFFFLINGPEVMSKMSGESESNLRKAFEECEKNQPAILFIDEIDAIAPKRE
SQ  KTNGEVERRIVSQLLTLMDGVKGRSNLVVIAATNRPNSIDGALRRFGRFDREIDIGIPDAVGRLEILRIHTKNMKLADDV
SQ  DLEQIANECHGFVGADLASLCSEAALQQIREKMELIDLEDDQIDAEVLNSLAVTMENFRFAQGKSSPSALREAVVETPNT
SQ  TWSDIGGLQNVKRELQELVQYPVEHPEKYLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGE
SQ  SEANVRDVFDKARAAAPCVLFFDELDSIAKARGGGAGGDGGGASDRVINQVLTEMDGMNAKKNVFIIGATNRPDIIDPAV
SQ  LRPGRLDQLIYIPLPDEASRHQILKASLRKTPLSKDLDLTFLAKNTVGFSGADLTEICQRACKLAIRESIEKEIRIEKER
SQ  QDRQARGEELMEDDAVDPVPEITRAHFEEAMKFARRSVTDNDIRKYEMFAQTLQQSRGFGNNFKFPGEQRGSDAPSAPVP
SQ  AQDDDDLYN
//
ID  Q1LX29;
PN  Telomere repeats-binding bouquet formation protein 1;
GN  ccdc79;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome, telomere {ECO:0000250|UniProtKB:Q8C0V1}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C0V1}. Note=Localizes to telomeres during meiotic prophase. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q8C0V1}.
DR  UNIPROT: Q1LX29;
DR  UNIPROT: A3KQ98;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex. {ECO:0000250|UniProtKB:Q8C0V1}.
DE  Reference Proteome: Yes;
GO  GO:0000781;
GO  GO:0005637;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0045141;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEATKTDLRLLLECLKYQMKWPGSQKQALLTIISICKQNDQYVEFLREIGGISFIYNLSKSSTFSQVKETALFTLASLAE
SQ  LHESCKQALCREEMFRDFVQHLEQEMPLTEKRVAVYMLSVLVANNRCGQTLAKTSRCIEALLRLFRQSFPVPGESYEQLQ
SQ  LWITVSSALCGSVNNPQNEENQNVCMSVFPEIKPWLQEVALPRAELAQPLCSFIGMTVANNPCAQEYFVSVGGLDSLSDT
SQ  LTRVLSQSTHSASVCKMATIITKTLSACISNNELLGSSLSKLRVIPGLLRLLSSPNLDPQDQLAVVLTTGHLTDACVEQQ
SQ  SQLLSAGGLPIIITLLTETSDEELKKAAIFVLHTCNRITESLGPGMSTIDPNECDREGQWRSAGQILQRIQLLEKKIGKK
SQ  LWERDPESQPHSMKRSDSHVECDDELWEGSVMRKVKGNHRVYGEFRAIPAGTPITSEILQDQDSLQPDSSEEGLSPVQVN
SQ  LFKGPNWEKSKKRKHKQKRENERSDNQETRREGVNKRELKRNVKSERVVKRLKMMNLESDDDGYELLQNCSTPTEGNRDT
SQ  QGPDIFRHPDPVKRNQREPSLSDDNMSLCTELLDKEINKFLKPPSASKSNTLRCAGCVKHMNELNSRSFGAVLSSCRFQC
SQ  DFHLTLREAEDRFRRSQPLKRTSHTPTHTHINTHRKIREHSTSAQEHKQKSKREKHKLSHQSSDRCYRLTPLRRPRETYS
SQ  PDVKQWTDHRHLKKSSEDARSKNSSGRHRKRQNWSDKELCYLTKGVKRFGHSWNTILWKYPFHPGRTNVDLAKKFYHMQK
SQ  AKAQGVDLSVAKAL
//
ID  Q8NA31;
PN  Telomere repeats-binding bouquet formation protein 1;
GN  TERB1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome, telomere {ECO:0000250|UniProtKB:Q8C0V1}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C0V1}. Note=Localizes to telomeres during meiotic prophase. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q8C0V1}.
DR  UNIPROT: Q8NA31;
DR  UNIPROT: A0AUW1;
DR  PDB: 5WIR;
DR  PDB: 5XUP;
DR  PDB: 6J07;
DR  Pfam: PF00249;
DR  OMIM: 617332;
DR  OMIM: 619646;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex via interaction with TERF1, promoting priming telomeric DNA attachment'. Promotes telomere association with the nuclear envelope and deposition of the SUN-KASH/LINC complex. Also recruits cohesin to telomeres to develop structural rigidity. {ECO:0000250|UniProtKB:Q8C0V1}.
DE  Disease: Spermatogenic failure 60 (SPGF60) [MIM:619646]: An autosomal recessive male infertility disorder characterized by non-obstructive azoospermia, due to sperm maturation arrest before the pachytene stage. {ECO:0000269|PubMed:33211200}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P54274; IntAct: EBI-21942838; Score: 0.65
GO  GO:0000781;
GO  GO:0005637;
GO  GO:0070187;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0045141;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESEDTKKTQEMKTDLNLLLECLKYQMDNAFSQKEALVTIHSICQQNSNASVYFREIGGLMFVKNLAKSSEHSMVKEAAL
SQ  YTLGAIAEKNVYCQQTLCTSELFEDLTWFLSNDSNINLKRMSVYVILVLVSNNRTGQTLVRETGCITVLSRLFRTVISKH
SQ  ELDLSDKNVFQSYQLWSSVCSTLCVCVNNPQNDENQMFCCSLFPHANEWLKNCTTPEIIRPICSFIGLTLANNTYVQKYF
SQ  VSVGGLDVLSQVLMQLESDSHETLSSAKLAVVVTKTVDACIADNPTFGIVLSKYHIVSKLLALLLHESLDSGEKFSIMLT
SQ  LGHCTEDCEENQYDLFKNNGLPLMIQALTESQNEELNKAATFVLHNCKKITEKLSLSLGEYPFDENETQQLKDISVKENN
SQ  LEEHWRKAKEILHRIEQLEREGNEEEIQRENYQDNISSMNISIQNTWKHLHADRIGRGSKAEDEDKSHSRQLQSYKSHGV
SQ  MSKACTNDDQMKTPLKSANPVHACYRESEQNKTLYKAKSSCNQNLHEETTFEKNFVSQSSDHVFKHPVHIAKNIKQQLPV
SQ  TDPFTLCSDIINKEVVSFLATPSCSEMLTYRCSGCIAVEKSLNSRNFSKLLHSCPYQCDRHKVIVEAEDRYKSELRKSLI
SQ  CNKKILLTPRRRQRLSNESTTPGGIKKRRIRKNFTEEEVNYLFNGVKKMGNHWNSILWSFPFQQGRKAVDLAHKYHKLTK
SQ  HPTCAAS
//
ID  Q8C0V1;
PN  Telomere repeats-binding bouquet formation protein 1;
GN  Terb1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome, telomere {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:24885367}. Nucleus inner membrane {ECO:0000269|PubMed:26548954}. Note=Localizes to telomeres during meiotic prophase (PubMed:24413433). In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane (PubMed:26548954). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:26548954}.
DR  UNIPROT: Q8C0V1;
DR  UNIPROT: A1L2Z9;
DR  UNIPROT: E9QPF2;
DR  UNIPROT: Q14CI1;
DR  UNIPROT: Q8C0N5;
DR  PDB: 1X58;
DR  PROSITE: PS50176;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis (PubMed:24885367, PubMed:24413433, PubMed:26548954). Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN- TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA (PubMed:26548954). In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex via interaction with TERF1, promoting priming telomeric DNA attachment' (PubMed:26548954). Promotes telomere association with the nuclear envelope and deposition of the SUN-KASH/LINC complex (PubMed:24885367, PubMed:24413433). Also recruits cohesin to telomeres to develop structural rigidity (PubMed:24413433). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:26548954, ECO:0000305|PubMed:24885367}.
DE  Reference Proteome: Yes;
DE  Interaction: Q80VJ8; IntAct: EBI-16089819; Score: 0.35
DE  Interaction: Q9P2S5; IntAct: EBI-11695180; Score: 0.35
DE  Interaction: O70576; IntAct: EBI-16089902; Score: 0.37
DE  Interaction: Q9D666; IntAct: EBI-16089819; Score: 0.50
DE  Interaction: P70371; IntAct: EBI-16089885; Score: 0.53
DE  Interaction: Q8C5S7; IntAct: EBI-16089940; Score: 0.35
DE  Interaction: A2AU37; IntAct: EBI-16089940; Score: 0.35
DE  Interaction: Q9CW03; IntAct: EBI-16089940; Score: 0.35
GO  GO:0000781;
GO  GO:0005637;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0045141;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESEKPKKTQEMKTDLKLLLECLKYHMGNPLSQKEVLITIHSVCKQNSDAGIYFREIGGLMFIINLAKSSEQSLVKEAAL
SQ  YTLGSIAEENVYCQQSLCTSELFQDLTGLLTNDDSNTNLKRMSVYVLLVLVSNNRNGQTLVREVGCIEVLSQMFRTVLSN
SQ  YELNLSDNSVFQSYLLWSSVCSTLCVCVNNPQNDENQMLCCSLFPCVNEWLMNCMRPEVIRPICSFIGLTLANNTHAQNC
SQ  FVSSGGLDVLCQVLVQLESDSHNTLSSAKLAVIVTKTMDACITDNSAAFTVVLSKYHIVSTLLALLLHESLDSREKFSII
SQ  LAIGHCTEDCEKNQYELLKNNGLPLMIQALTEFKNEDLSKAATYVLHNCKKITGKLSLSLGQNSFGENEIELKDISEKET
SQ  LREHWKAAKEILCRIKQFEKGGKEEKQQNRSGHYKDNTPSMKVNIQTNLKRLCADSTGGTRAEDKDINQSRELRSYKPSE
SQ  IMSKACANENQLTTRKKNTNPVHPFCKEKGQSKIVHETTPSCAQNLDKEKTFDQKDSVSQSSDQVLKHLPHTVKNRKQVP
SQ  ETDPFTLCLDIIDREVGIQATDSCSRMLKYTCSGCIVARKLLNSRNFSKFLHSCAYQCVHHKVIMEAEDKYKNELRKTFI
SQ  CAKKILLTPCRRRQLCKESTASEELKIVHQKPDSKKLPGLEAQALNTSIPEAMERRSPVPGQSGLHKKRRIRKDFTKEEV
SQ  NYLFHGVKTMGNHWNSILWSFPFQKGRRAVDLAHKYHRLIKGPSCAAL
//
ID  Q2M2T9;
PN  Telomere repeats-binding bouquet formation protein 2;
GN  TERB2;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome, telomere {ECO:0000250|UniProtKB:Q9D494}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D494}. Note=Localizes to telomeres throughout meiotic prophase I and disappears in metaphase I. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D494}.
DR  UNIPROT: Q2M2T9;
DR  Pfam: PF15101;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. {ECO:0000250|UniProtKB:Q9D494}.
DE  Reference Proteome: Yes;
GO  GO:0000781;
GO  GO:0005637;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0045141;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFQGQRGWFCGSVSHDLRQFWVAEGGTISDPRAADFLFSCDASHPDTLRIYQSLDYIEDNATVFHAYYLSAVANAEIKNS
SQ  VALGHFILPPASLQKEIRRKIGSFIWEQDQHFLIEKHDEVTSNELKVFRESSVLATDHKKDLSKSTEKHFIRTPVVEKQM
SQ  YFPLQHYPVNNMVTGYISIDAMKKFLGELHDFIPGSSGYLAYHVQNEINMSAIKNKLKNKY
//
ID  Q8NHR7;
PN  Telomere repeats-binding bouquet formation protein 2;
GN  TERB2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome, telomere {ECO:0000250|UniProtKB:Q9D494}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D494}. Note=Localizes to telomeres throughout meiotic prophase I and disappears in metaphase I. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D494}.
DR  UNIPROT: Q8NHR7;
DR  PDB: 6GNX;
DR  PDB: 6GNY;
DR  PDB: 6J07;
DR  PDB: 6J08;
DR  Pfam: PF15101;
DR  OMIM: 617131;
DR  OMIM: 619645;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. {ECO:0000250|UniProtKB:Q9D494}.
DE  Disease: Spermatogenic failure 59 (SPGF59) [MIM:619645]: An autosomal recessive male infertility disorder characterized by non-obstructive azoospermia, due to sperm maturation arrest. {ECO:0000269|PubMed:33377991}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q3KP22; IntAct: EBI-23751777; Score: 0.56
GO  GO:0000781;
GO  GO:0005637;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0045141;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFQGQRGWFCGSVSQDLRQFWVAEGGTISDPRAADFLFSCDASHPDTLRIYQSLDYIEDNATVFHAYYLSAVANAKIKNS
SQ  VALGHFILPPACLQKEIRRKIGSFIWEQDQHFLIEKHDEVTPNEIKTLRENSELATEHKKELSKSPEKHFIRTPVVEKQM
SQ  YFPLQNYPVNNMVTGYISIDAMKKFLGELHDFIPGTSGYLAYHVQNEINMSAIKNKLKRK
//
ID  Q9D494;
PN  Telomere repeats-binding bouquet formation protein 2;
GN  Terb2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Chromosome, telomere {ECO:0000269|PubMed:26548954}. Nucleus inner membrane {ECO:0000269|PubMed:26548954}. Note=Localizes to telomeres throughout meiotic prophase I and disappears in metaphase I. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000269|PubMed:26548954}.
DR  UNIPROT: Q9D494;
DR  Pfam: PF15101;
DE  Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1- TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. {ECO:0000269|PubMed:26548954}.
DE  Reference Proteome: Yes;
GO  GO:0000781;
GO  GO:0005637;
GO  GO:0007129;
GO  GO:0070197;
GO  GO:0045141;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFQGQRGWFCGSVSQDLRQIWEDEGGMVSDVKAADFLFSCDASHPDTLRIYQSLEYIEDNATVFHAYYLAAIANTEMKNS
SQ  VALGHFVLPPACLQKEIRRKIGSFIWEQDEKFQIEKHDRMASSDKENIRPTPEHKQELSKSAEHHLTRTPVIEKQMCFPL
SQ  HSYPVNNMVTGYISIDALEKFLGELHDFTPGSSGYLAYHIQDEINMSAIKNKLRRKLS
//
ID  Q15569;
PN  Dual specificity testis-specific protein kinase 1;
GN  TESK1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:15584898}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63572}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25849865}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q63572}. Note=Colocalizes with SPRY4 in vesicular spots in the cytoplasm (PubMed:15584898). Localized to F- actin-rich lamellipodia at the cell periphery following fibronectin- mediated cell adhesion of Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q63572, ECO:0000269|PubMed:15584898}.
DR  UNIPROT: Q15569;
DR  UNIPROT: Q8IXZ8;
DR  Pfam: PF07714;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DR  OMIM: 601782;
DR  DisGeNET: 7016;
DE  Function: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues (By similarity). Regulates the cellular cytoskeleton by enhancing actin stress fiber formation via phosphorylation of cofilin and by preventing microtubule breakdown via inhibition of TAOK1/MARKK kinase activity (By similarity). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Positively regulates integrin- mediated cell spreading, via phosphorylation of cofilin (PubMed:15584898). Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of ciliary vesicle directional trafficking to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (PubMed:25849865). Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity). {ECO:0000250|UniProtKB:O70146, ECO:0000250|UniProtKB:Q63572, ECO:0000269|PubMed:15584898, ECO:0000269|PubMed:25849865}.
DE  Reference Proteome: Yes;
DE  Interaction: P31946; IntAct: EBI-7969808; Score: 0.61
DE  Interaction: Q9C004; IntAct: EBI-354851; Score: 0.51
DE  Interaction: P10398; IntAct: EBI-3905576; Score: 0.37
DE  Interaction: P17858; IntAct: EBI-3912189; Score: 0.37
DE  Interaction: P21439; IntAct: EBI-3912199; Score: 0.37
DE  Interaction: P25490; IntAct: EBI-3913625; Score: 0.37
DE  Interaction: P08238; IntAct: EBI-6423722; Score: 0.40
DE  Interaction: Q9NQZ2; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: Q96JB2; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: Q96CP6; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: Q8ND56; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: Q7Z6M1; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: Q14257; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: P24666; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: P00367; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: O75592; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: O00763; IntAct: EBI-28941326; Score: 0.35
DE  Interaction: Q6P5Z2; IntAct: EBI-28941754; Score: 0.35
DE  Interaction: Q8WTQ7; IntAct: EBI-28943996; Score: 0.35
DE  Interaction: Q96S53; IntAct: EBI-28944692; Score: 0.35
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0004712;
GO  GO:0004713;
GO  GO:0030036;
GO  GO:0051650;
GO  GO:1902018;
GO  GO:0042326;
GO  GO:0031953;
GO  GO:0071901;
GO  GO:0090521;
GO  GO:1900182;
GO  GO:0001934;
GO  GO:0051496;
GO  GO:1900026;
GO  GO:0032956;
GO  GO:0032880;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGERPPLRGPGPGPGEVPGEGPPGPGGTGGGPGRGRPSSYRALRSAVSSLARVDDFHCAEKIGAGFFSEVYKVRHRQSG
SQ  QVMVLKMNKLPSNRGNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIA
SQ  RGLRYLHSKGVFHRDLTSKNCLVRREDRGFTAVVGDFGLAEKIPVYREGARKEPLAVVGSPYWMAPEVLRGELYDEKADV
SQ  FAFGIVLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGDDCPLPFLLLAIHCCNLEPSTRAPFTEITQHLEWILEQLPE
SQ  PAPLTRTALTHNQGSVARGGPSATLPRPDPRLSRSRSDLFLPPSPESPPNWGDNLTRVNPFSLREDLRGGKIKLLDTPSK
SQ  PVLPLVPPSPFPSTQLPLVTTPETLVQPGTPARRCRSLPSSPELPRRMETALPGPGPPAVGPSAEEKMECEGSSPEPEPP
SQ  GPAPQLPLAVATDNFISTCSSASQPWSPRSGPVLNNNPPAVVVNSPQGWAGEPWNRAQHSLPRAAALERTEPSPPPSAPR
SQ  EPDEGLPCPGCCLGPFSFGFLSMCPRPTPAVARYRNLNCEAGSLLCHRGHHAKPPTPSLQLPGARS
//
ID  O70146;
PN  Dual specificity testis-specific protein kinase 1;
GN  Tesk1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q15569}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63572}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15569}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q63572}. Note=Colocalizes with SPRY4 in vesicular spots in the cytoplasm (By similarity). Localized to F-actin- rich lamellipodia at the cell periphery following fibronectin-mediated cell adhesion of Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q15569, ECO:0000250|UniProtKB:Q63572}.
DR  UNIPROT: O70146;
DR  UNIPROT: O70147;
DR  UNIPROT: Q499W7;
DR  Pfam: PF07714;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues (By similarity). Regulates the cellular cytoskeleton by enhancing actin stress fiber formation via phosphorylation of cofilin and by preventing microtubule breakdown via inhibition of TAOK1/MARKK kinase activity (By similarity). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (PubMed:30115939). Positively regulates integrin-mediated cell spreading, via phosphorylation of cofilin (By similarity). Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of ciliary vesicle directional trafficking to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity). Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q15569, ECO:0000250|UniProtKB:Q63572, ECO:0000269|PubMed:30115939}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0004712;
GO  GO:0004713;
GO  GO:0030036;
GO  GO:0051650;
GO  GO:1902018;
GO  GO:0042326;
GO  GO:0031953;
GO  GO:0071901;
GO  GO:0090521;
GO  GO:1900182;
GO  GO:0001934;
GO  GO:0051496;
GO  GO:1900026;
GO  GO:0032956;
GO  GO:0032880;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGERPPLRGPGPGEAPGEGPGGAGGGPGRGRPSSYRALRSAVSSLARVDDFDCAEKIGAGFFSEVYKVRHRQSGQVMVL
SQ  KMNKLPSNRSNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIAQGLRY
SQ  LHAKGVFHRDLTSKNCLVRREDRGFTAVVGDFGLAEKIPVYREGTRKEPLAVVGSPYWMAPEVLRGELYDEKADVFAFGI
SQ  VLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGNDCPLPFLLLAIHCCSMEPSTRAPFTEITQHLEQILEQQPEATPLA
SQ  KPPLTKAPLTYNQGSVPRGGPSATLPRPDPRLSRSRSDLFLPPSPESPPSWGDNLTRVNPFSLREDLRGGKIKLLDTPCK
SQ  PATPLPLVPPSPLTSTQLPLVTTPDILVQPETPVRRCRSLPSSPELPRRMETALPGPGPSPMGPTEERMDCEGSSPEPEP
SQ  PGLAPQLPLAVATDNFISTCSSASQPWSPRSGPPLNNNPPAVVVNSPQGWAREPWNRAQHSLPRAAALERTEPSPPPSAP
SQ  REPEEGLPCPGCCLGPFSFGFLSMCPRPTPAVARYRNLNCEAGSLLCHRGHHAKPPTPSLQLPGARS
//
ID  Q63572;
PN  Dual specificity testis-specific protein kinase 1;
GN  Tesk1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:22302232}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22302232}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15569}. Cell projection, lamellipodium {ECO:0000269|PubMed:22302232}. Note=Colocalizes with SPRY4 in vesicular spots in the cytoplasm (By similarity). Localized to F-actin-rich lamellipodia at the cell periphery following fibronectin-mediated cell adhesion of Schwann cells (PubMed:22302232). {ECO:0000250|UniProtKB:Q15569, ECO:0000269|PubMed:22302232}.
DR  UNIPROT: Q63572;
DR  Pfam: PF07714;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues (PubMed:10207045). Regulates the cellular cytoskeleton by enhancing actin stress fiber formation via phosphorylation of cofilin and by preventing microtubule breakdown via inhibition of TAOK1/MARKK kinase activity (PubMed:18216281, PubMed:11555644). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Positively regulates integrin-mediated cell spreading, via phosphorylation of cofilin (By similarity). Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of ciliary vesicle directional trafficking to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity). Probably plays a central role at and after the meiotic phase of spermatogenesis (PubMed:8537404). {ECO:0000250|UniProtKB:O70146, ECO:0000250|UniProtKB:Q15569, ECO:0000269|PubMed:10207045, ECO:0000269|PubMed:11555644, ECO:0000269|PubMed:18216281, ECO:0000269|PubMed:8537404}.
DE  Reference Proteome: Yes;
DE  Interaction: P31946; IntAct: EBI-7969948; Score: 0.35
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0030027;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0008022;
GO  GO:0004672;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0004712;
GO  GO:0004713;
GO  GO:0030036;
GO  GO:0051650;
GO  GO:1902018;
GO  GO:0042326;
GO  GO:0031953;
GO  GO:0071901;
GO  GO:0090521;
GO  GO:1900182;
GO  GO:0001934;
GO  GO:0051496;
GO  GO:1900026;
GO  GO:0032956;
GO  GO:0032880;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGERPPLRGPGPGETPVEGPGGAGGGPGRGRPSSYRALRSAVSSLARVDDFDCAEKIGAGFFSEVYKVRHRQSGQVMVL
SQ  KMNKLPSNRSNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIAQGLRY
SQ  LHAKGVFHRDLTSKNCLVRREDGGFTAVVGDFGLAEKIPVYREGARKEPLAVVGSPYWMAPEVLRGELYDEKADVFAFGI
SQ  VLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGNDCPLPFLLLAIHCCSMEPSARAPFTEITQHLEQILEQLPEPTPLA
SQ  KMPLAKAPLTYNQGSVPRGGPSATLPRSDPRLSRSRSDLFLPPSPESPPSWGDNLTRVNPFSLREDLRGGKIKLLDTPCK
SQ  PATPLPLVPPSPLTSTQLPLVASPESLVQPETPVRRCRSLPSSPELPRRMETALPGPGPSPVGPSTEERMDCEGSSPEPE
SQ  PPGPAPQLPLAVATDNFISTCSSASQPWSARPGPSLNNNPPAVVVNSPQGWAREPWNRAQHSLPRAAALERTEPSPPPSA
SQ  PREQEEGLPCPGCCLSPFSFGFLSMCPRPTPAVARYRNLNCEAGSLLCHRGHHAKPPTPSLQLPGARS
//
ID  Q8IWB9;
PN  Testis-expressed protein 2;
GN  TEX2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q06833}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Multi- pass membrane protein {ECO:0000255}. Note=Enriched at the nucleus- vacuole junction (PubMed:22250200). During endoplasmic reticulum (ER) stress, localizes to ER-Golgi contacts (By similarity). {ECO:0000250|UniProtKB:Q06833, ECO:0000269|PubMed:22250200}.
DR  UNIPROT: Q8IWB9;
DR  UNIPROT: Q6AHZ5;
DR  UNIPROT: Q8N3L0;
DR  UNIPROT: Q9C0C5;
DR  PROSITE: PS51847;
DR  OMIM: 619929;
DR  DisGeNET: 55852;
DE  Function: During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, may induce contacts between the ER and medial-Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. {ECO:0000269|PubMed:28011845}.
DE  Reference Proteome: Yes;
DE  Interaction: Q81KT8; IntAct: EBI-2820950; Score: 0.00
DE  Interaction: A0A5P8YCV0; IntAct: EBI-2852770; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-3962281; Score: 0.35
DE  Interaction: P88995; IntAct: EBI-9641383; Score: 0.37
DE  Interaction: Q5JU00; IntAct: EBI-11385220; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11398030; Score: 0.27
DE  Interaction: P52799; IntAct: EBI-21582984; Score: 0.35
DE  Interaction: Q9H2J7; IntAct: EBI-21614809; Score: 0.35
DE  Interaction: Q96G30; IntAct: EBI-21633324; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P46108; IntAct: EBI-30820623; Score: 0.44
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0008289;
GO  GO:0006869;
GO  GO:0007165;
GO  GO:0006665;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTSLYGRHAEKTTDMPKPSAPKVHVQRSVSRDTIAIHFSASGEEEEEEEEEFREYFEEGLDDQSIVTGLEAKEDLYLEPQ
SQ  VGHDPAGPAASPVLADGLSVSQAPAILPVSKNTVKLLESPVPAAQVLSTVPLAVSPGSSSSGPLASSPSVSSLSEQKTSS
SQ  SSPLSSPSKSPILSSSASTSTLSSAKPFMSLVKSLSTEVEPKESPHPARHRHLMKTLVKSLSTDTSRQESDTVSYKPPDS
SQ  KLNLHLFKQFTQPRNTGGDSKTAPSSPLTSPSDTRSFFKVPEMEAKIEDTKRRLSEVIYEPFQLLSKIIGEESGSHRPKA
SQ  LSSSASELSNLSSLNGHLESNNNYSIKEEECDSEGDGYGSDSNIPRSDHPKSTGEPTREIELKSSQGSSLKDLGLKTSSL
SQ  VLEKCSLSALVSKEDEEFCELYTEDFDLETEGESKVDKLSDIPLKPEVLAEDGVVLDSEDEVDSAVQHPELPVKTLGFFI
SQ  MCVYVYLILPLPHYVSGLFLGIGLGFMTAVCVIWFFTPPSAHKYHKLHKNLRHWNTRSLDIKEPEILKGWMNEIYNYDPE
SQ  TYHATLTHSVFVRLEGGTLRLSKPNKNISRRASYNEPKPEVTYISQKIYDLSDSKIYLVPKTLARKRIWNKKYPICIELG
SQ  QQDDFMSKAQTDKETSEEKPPAEGSEDPKKPPRPQEGTRSSQRDQILYLFGRTGREKEEWFRRFILASKLKSEIKKSSGV
SQ  SGGKPGLLPAHSRHNSPSGHLTHSRSSSKGSVEEIMSQPKQKELAGSVRQKMLLDYSVYMGRCVPQESRSPQRSPLQSAE
SQ  SSPTAGKKLPEVPPSEEEEQEAWVNALLGRIFWDFLGEKYWSDLVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKIL
SQ  QAFKPYVDHQGLWIDLEMSYNGSFLMTLETKMNLTKLGKEPLVEALKVGEIGKEGCRPRAFCLADSDEESSSAGSSEEDD
SQ  APEPSGGDKQLLPGAEGYVGGHRTSKIMRFVDKITKSKYFQKATETEFIKKKIEEVSNTPLLLTVEVQECRGTLAVNIPP
SQ  PPTDRVWYGFRKPPHVELKARPKLGEREVTLVHVTDWIEKKLEQEFQKVFVMPNMDDVYITIMHSAMDPRSTSCLLKDPP
SQ  VEAADQP
//
ID  Q6ZPJ0;
PN  Testis-expressed protein 2;
GN  Tex2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q06833}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Multi- pass membrane protein {ECO:0000255}. Note=Enriched at the nucleus- vacuole junction (By similarity). During endoplasmic reticulum (ER) stress, localizes to ER-Golgi contacts (By similarity). {ECO:0000250|UniProtKB:Q06833, ECO:0000250|UniProtKB:Q8IWB9}.
DR  UNIPROT: Q6ZPJ0;
DR  UNIPROT: B1ATR1;
DR  PROSITE: PS51847;
DE  Function: During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, may induce contacts between the ER and medial-Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. {ECO:0000250|UniProtKB:Q8IWB9}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6NZM9; IntAct: EBI-26471757; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0008289;
GO  GO:0006869;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTSLNGRHAEKTIDMPKPSAPKVHVQRSVSRDTIAIHFSASGEEEEEEEEEFRGYLEEGLDDQSIVTGLEAKEDLYLESQ
SQ  GGHDPAGPVSTAPADGLSVSESPAILPVSENTVKLLESPAPALQVLSPVPLALSPGSSSSGPLASSPSVSSLSEQKTSSS
SQ  SPLSSPSKSPVLSSSASSSALSSAKPFMSLVKSLSTEVEPKESPHPPRHRHLMKTLVKSLSTDTSRQESDTVSYKPPDSK
SQ  LNLHLFKQFTQPRNTGGDSKTAPSSPLTSPSDTRSFFKVPEMEAKIEDTKRRLSEVIYEPFQLLSKIIGEESGSHRPKAL
SQ  SASASELSSLSGLNGHLESNNYSIKEEEGDSEGEGYGSDSNTSRSDHLKPTEDASKEVEPKGSQASSLKDLGLKTSSLVL
SQ  EKCSLSALVSKEDEEFCELYTEDFELETEGEGRLDKTLDLPLKPEVLASDGVALESEDEEDSATEHQELPVKTLGFFIMC
SQ  VYAYLILPLPYYMSGLFLGVGLGFMTAVCMIWFFTPPSAHKHHKSLKALRHQSTRSLDIKEPEILKGWMNEIYNYDPETY
SQ  HATLTHSVFVRLEGGTLRLSKPNKNISRRASYNETKPEVTYISQKIYDLSDSKIYLVPKSLARKRIWNKKYPICIELGRQ
SQ  DDFMSKAQSDKEATEEKPPPEKELPSEDLKKPPQPQEGTKSSQRDPILYLFGRTGREKEEWFRRFILASRLKSELRKPAG
SQ  VSGSKSGLLPAHSRHSSPSGHLSHSRSSSKGSVEEMMSQPKQKELVGSVRQKMLLDYSVYMGRCVPQDNRSPHRSPVQSA
SQ  ESSPTASKKLPEAPPSEEEEQEAWVNALLGRIFWDFLGEKYWSDVVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKI
SQ  LQAFKPYVDHQGLWIDLEMSYNGSFLMTLETKMNLTKLGKEPLVEALKVGEIGKEGCRPRAYCLADSDEESSSAGSSEED
SQ  DPPEPTAGDKQPLPGAEGYVGGHRTSKIMRFVDKITKSKYFQKATETEFIKKKIEEVSNTPLLLTVEVQECRGTLAVNIP
SQ  PPPTDRIWYGFRKPPYVELKARPKLGEREVTLVHVTEWIEKKLEQELQKVFVMPNMDDVYIPIMHSAMDPRSTSCLLKEP
SQ  PVETSDQL
//
ID  P21980;
PN  Protein-glutamine gamma-glutamyltransferase 2;
GN  TGM2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:24349085, ECO:0000269|PubMed:29618516, ECO:0000269|PubMed:9575137}. Nucleus {ECO:0000269|PubMed:29618516, ECO:0000269|PubMed:9575137}. Chromosome {ECO:0000269|PubMed:9575137}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12506096, ECO:0000269|PubMed:1683874}. Cell membrane {ECO:0000250|UniProtKB:Q9WVJ6}. Mitochondrion {ECO:0000269|PubMed:24349085}. Note=Mainly localizes to the cytosol (PubMed:9575137). Present at much lower level in the nucleus and chromatin (PubMed:9575137). Also secreted via a non-classical secretion pathway to the extracellular matrix (PubMed:27270573). {ECO:0000269|PubMed:9575137, ECO:0000303|PubMed:27270573}. [Isoform 2]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17116873}.
DR  UNIPROT: P21980;
DR  UNIPROT: E1P5V9;
DR  UNIPROT: Q16436;
DR  UNIPROT: Q6B838;
DR  UNIPROT: Q9BTN7;
DR  UNIPROT: Q9H035;
DR  UNIPROT: Q9UH35;
DR  PDB: 1KV3;
DR  PDB: 2Q3Z;
DR  PDB: 3LY6;
DR  PDB: 3S3J;
DR  PDB: 3S3P;
DR  PDB: 3S3S;
DR  PDB: 4PYG;
DR  PDB: 6A8P;
DR  PDB: 6KZB;
DR  Pfam: PF00927;
DR  Pfam: PF01841;
DR  Pfam: PF00868;
DR  PROSITE: PS00547;
DR  OMIM: 190196;
DR  DisGeNET: 7052;
DE  Function: Calcium-dependent acyltransferase that catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, such as gamma-amino group of peptide-bound lysine, or mono- and polyamines, thereby producing cross-linked or aminated proteins, respectively (PubMed:9252372, PubMed:23941696, PubMed:31991788). Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis (PubMed:1683874, PubMed:7935379, PubMed:9252372, PubMed:27270573). Acts as a protein-glutamine gamma- glutamyltransferase by mediating the cross-linking of proteins, such as ACO2, HSPB6, FN1, HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1 and WDR54 (PubMed:23941696, PubMed:24349085, PubMed:29618516, PubMed:30458214). Under physiological conditions, the protein cross-linking activity is inhibited by GTP; inhibition is relieved by Ca(2+) in response to various stresses (PubMed:7649299, PubMed:7592956, PubMed:18092889). When secreted, catalyzes cross-linking of proteins of the extracellular matrix, such as FN1 and SPP1 resulting in the formation of scaffolds (PubMed:12506096). Plays a key role during apoptosis, both by (1) promoting the cross-linking of cytoskeletal proteins resulting in condensation of the cytoplasm, and by (2) mediating cross-linking proteins of the extracellular matrix, resulting in the irreversible formation of scaffolds that stabilize the integrity of the dying cells before their clearance by phagocytosis, thereby preventing the leakage of harmful intracellular components (PubMed:7935379, PubMed:9252372). In addition to protein cross-linking, can use different monoamine substrates to catalyze a vast array of protein post-translational modifications: mediates aminylation of serotonin, dopamine, noradrenaline or histamine into glutamine residues of target proteins to generate protein serotonylation, dopaminylation, noradrenalinylation or histaminylation, respectively (PubMed:23797785, PubMed:30867594). Mediates protein serotonylation of small GTPases during activation and aggregation of platelets, leading to constitutive activation of these GTPases (By similarity). Plays a key role in chromatin organization by mediating serotonylation and dopaminylation of histone H3 (PubMed:30867594, PubMed:32273471). Catalyzes serotonylation of 'Gln-5' of histone H3 (H3Q5ser) during serotonergic neuron differentiation, thereby facilitating transcription (PubMed:30867594). Acts as a mediator of neurotransmission-independent role of nuclear dopamine in ventral tegmental area (VTA) neurons: catalyzes dopaminylation of 'Gln- 5' of histone H3 (H3Q5dop), thereby regulating relapse-related transcriptional plasticity in the reward system (PubMed:32273471). Regulates vein remodeling by mediating serotonylation and subsequent inactivation of ATP2A2/SERCA2 (By similarity). Also acts as a protein deamidase by mediating the side chain deamidation of specific glutamine residues of proteins to glutamate (PubMed:9623982, PubMed:20547769). Catalyzes specific deamidation of protein gliadin, a component of wheat gluten in the diet (PubMed:9623982). May also act as an isopeptidase cleaving the previously formed cross-links (PubMed:26250429, PubMed:27131890). Also able to participate in signaling pathways independently of its acyltransferase activity: acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity and is required for coupling alpha-1 adrenergic agonists to the stimulation of phosphoinositide lipid metabolism (PubMed:8943303). {ECO:0000250|UniProtKB:P08587, ECO:0000250|UniProtKB:P21981, ECO:0000269|PubMed:12506096, ECO:0000269|PubMed:1683874, ECO:0000269|PubMed:18092889, ECO:0000269|PubMed:20547769, ECO:0000269|PubMed:23797785, ECO:0000269|PubMed:23941696, ECO:0000269|PubMed:24349085, ECO:0000269|PubMed:26250429, ECO:0000269|PubMed:27131890, ECO:0000269|PubMed:29618516, ECO:0000269|PubMed:30458214, ECO:0000269|PubMed:30867594, ECO:0000269|PubMed:31991788, ECO:0000269|PubMed:32273471, ECO:0000269|PubMed:7592956, ECO:0000269|PubMed:7649299, ECO:0000269|PubMed:7935379, ECO:0000269|PubMed:8943303, ECO:0000269|PubMed:9252372, ECO:0000269|PubMed:9623982, ECO:0000303|PubMed:27270573}. [Isoform 2]: Has cytotoxic activity: is able to induce apoptosis independently of its acyltransferase activity. {ECO:0000269|PubMed:17116873}.
DE  Disease: Note=TGM2 constitutes the major autoantigen in celiac disease, a multifactorial chronic disorder of the small intestine caused by intolerance to gluten (PubMed:9212111, PubMed:9623982). Celiac disease is characterized by immune-mediated enteropathy associated with failed intestinal absorption and malnutrition: intestinal inflammation is precipitated by ingestion of the protein gliadin, a component of wheat gluten in the diet (PubMed:9212111, PubMed:9623982). TGM2 is the main target for celiac disease-associated anti-endomysium autoantibodies (PubMed:9212111). It mediates its effect by catalyzing specific deamidation of gliadin; this deamidation creates an epitope that binds efficiently to HLA-DQ2 and is recognized by gut-derived T-cells (PubMed:9623982). {ECO:0000269|PubMed:9212111, ECO:0000269|PubMed:9623982}.
DE  Reference Proteome: Yes;
DE  Interaction: O14656; IntAct: EBI-25847214; Score: 0.56
DE  Interaction: P12931; IntAct: EBI-15828007; Score: 0.40
DE  Interaction: P51178; IntAct: EBI-7093657; Score: 0.44
DE  Interaction: P06788; IntAct: EBI-7037023; Score: 0.63
DE  Interaction: Q96KM6; IntAct: EBI-7218951; Score: 0.37
DE  Interaction: Q15796; IntAct: EBI-7226967; Score: 0.37
DE  Interaction: P84022; IntAct: EBI-7233893; Score: 0.37
DE  Interaction: P12830; IntAct: EBI-727492; Score: 0.40
DE  Interaction: Q12802; IntAct: EBI-1373886; Score: 0.54
DE  Interaction: P25963; IntAct: EBI-1537248; Score: 0.35
DE  Interaction: Q04206; IntAct: EBI-1537257; Score: 0.46
DE  Interaction: P0CG48; IntAct: EBI-8561076; Score: 0.40
DE  Interaction: P15531; IntAct: EBI-7123411; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-2566481; Score: 0.62
DE  Interaction: P39060; IntAct: EBI-2566677; Score: 0.44
DE  Interaction: P07996; IntAct: EBI-2566725; Score: 0.44
DE  Interaction: Q9NYJ8; IntAct: EBI-3917387; Score: 0.37
DE  Interaction: O95477; IntAct: EBI-3926010; Score: 0.37
DE  Interaction: P01023; IntAct: EBI-3925960; Score: 0.37
DE  Interaction: P55265; IntAct: EBI-3926280; Score: 0.37
DE  Interaction: P18848; IntAct: EBI-3927195; Score: 0.37
DE  Interaction: Q12983; IntAct: EBI-3927452; Score: 0.37
DE  Interaction: P01024; IntAct: EBI-3927482; Score: 0.37
DE  Interaction: P19784; IntAct: EBI-3928266; Score: 0.37
DE  Interaction: P49354; IntAct: EBI-3929720; Score: 0.37
DE  Interaction: P47871; IntAct: EBI-3929900; Score: 0.37
DE  Interaction: P28799; IntAct: EBI-3930315; Score: 0.37
DE  Interaction: P52597; IntAct: EBI-3930836; Score: 0.37
DE  Interaction: P00738; IntAct: EBI-3930876; Score: 0.37
DE  Interaction: P08107; IntAct: EBI-3930986; Score: 0.37
DE  Interaction: A8K5I0; IntAct: EBI-3930996; Score: 0.37
DE  Interaction: P11142; IntAct: EBI-3931030; Score: 0.37
DE  Interaction: P21980; IntAct: EBI-3934152; Score: 0.37
DE  Interaction: Q9Y5P4; IntAct: EBI-3934972; Score: 0.37
DE  Interaction: Q9BUJ2; IntAct: EBI-3936567; Score: 0.37
DE  Interaction: P82251; IntAct: EBI-3936587; Score: 0.37
DE  Interaction: O15084; IntAct: EBI-3937934; Score: 0.37
DE  Interaction: Q9UHV2; IntAct: EBI-3939043; Score: 0.37
DE  Interaction: Q96HP8; IntAct: EBI-3940382; Score: 0.37
DE  Interaction: Q9P2F8; IntAct: EBI-3940677; Score: 0.37
DE  Interaction: Q13153; IntAct: EBI-7394761; Score: 0.37
DE  Interaction: P40337; IntAct: EBI-5280932; Score: 0.60
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.76
DE  Interaction: P55036; IntAct: EBI-6305557; Score: 0.46
DE  Interaction: Q15113; IntAct: EBI-9076404; Score: 0.44
DE  Interaction: Q9UHY7; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: O43295; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: Q5VT25; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: Q9H061; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: O60568; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: P20908; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: P49756; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: Q3B726; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: Q14764; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: P05997; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: Q8NBJ5; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: Q15427; IntAct: EBI-11072363; Score: 0.35
DE  Interaction: P08727; IntAct: EBI-15827988; Score: 0.40
DE  Interaction: P28300; IntAct: EBI-20724912; Score: 0.56
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: P02452; IntAct: EBI-26366205; Score: 0.35
DE  Interaction: G5E9A7; IntAct: EBI-25842080; Score: 0.56
DE  Interaction: P50570; IntAct: EBI-25844685; Score: 0.56
DE  Interaction: P29692; IntAct: EBI-25847555; Score: 0.56
DE  Interaction: Q06787; IntAct: EBI-25856705; Score: 0.56
DE  Interaction: P04792; IntAct: EBI-25870591; Score: 0.56
DE  Interaction: D3DTS7; IntAct: EBI-25882882; Score: 0.56
DE  Interaction: P60891; IntAct: EBI-25886231; Score: 0.56
DE  Interaction: Q5T160; IntAct: EBI-25893129; Score: 0.56
DE  Interaction: Q8N488; IntAct: EBI-25893112; Score: 0.56
DE  Interaction: Q14141; IntAct: EBI-25893103; Score: 0.56
DE  Interaction: O95416; IntAct: EBI-25893095; Score: 0.56
DE  Interaction: Q9NYH9; IntAct: EBI-25893121; Score: 0.56
DE  Interaction: Q86WV8; IntAct: EBI-25893501; Score: 0.56
DE  Interaction: P02766; IntAct: EBI-25894045; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25897477; Score: 0.56
DE  Interaction: O00429; IntAct: EBI-25910269; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25914831; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25931020; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25946429; Score: 0.56
DE  Interaction: P09429; IntAct: EBI-26447736; Score: 0.37
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.35
GO  GO:0000785;
GO  GO:0062023;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0070062;
GO  GO:0031012;
GO  GO:0005925;
GO  GO:0031226;
GO  GO:0005739;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005509;
GO  GO:0005525;
GO  GO:0120297;
GO  GO:0120295;
GO  GO:0008233;
GO  GO:0120299;
GO  GO:0120298;
GO  GO:0003810;
GO  GO:0050568;
GO  GO:0043277;
GO  GO:0060348;
GO  GO:0060445;
GO  GO:0071314;
GO  GO:1903351;
GO  GO:1904015;
GO  GO:0032471;
GO  GO:0018149;
GO  GO:0007200;
GO  GO:0043065;
GO  GO:0045785;
GO  GO:0043547;
GO  GO:0051561;
GO  GO:0050769;
GO  GO:0051057;
GO  GO:0018277;
GO  GO:0051260;
GO  GO:0006508;
GO  GO:2000425;
GO  GO:0042981;
GO  GO:0060662;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYEASVDSLTFSVVTGPAPSQEAGTKARFPLR
SQ  DAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYV
SQ  LTQQGFIYQGSAKFIKNIPWNFGQFEDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGR
SQ  WDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEF
SQ  GEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNAD
SQ  VVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVG
SQ  QSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLNLEPFSEKSVPLCILYEKYRDCLTESNL
SQ  IKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPD
SQ  PVEAGEEVKVRMDLLPLHMGLHKLVVNFESDKLKAVKGFRNVIIGPA
//
ID  Q9W1F4;
PN  THO complex subunit 5;
GN  thoc5;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus membrane {ECO:0000269|PubMed:28472469}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q9W1F4;
DR  UNIPROT: Q95RL0;
DR  Pfam: PF09766;
DE  Function: The THO complex is required for cell proliferation and for proper export of heat-shock mRNAs under heat stress. {ECO:0000269|PubMed:15133499}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y091; IntAct: EBI-15181626; Score: 0.49
DE  Interaction: Q8SY07; IntAct: EBI-15181646; Score: 0.49
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0000347;
GO  GO:0000445;
GO  GO:0000346;
GO  GO:0003729;
GO  GO:0043021;
GO  GO:0007140;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0032786;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  METILNTQFDQLQKAIEGIKEAKSKGQSTDEARIATTLMFVALKHANREVKHKIKAGRDKLHLEKCKVDLSRLQLQNLLY
SQ  EVSHLKKEIVRCQKFKSRDTSLELLSEAEYSSELPDMPNDAEELSSHKQHLHRLDCELRLRKALDKQYSALLSSKQELLQ
SQ  DNLSHAQRYVSFAPALRTLQSATKPLHDALQLSLDVEWKLSAVVKYLPKPLYVLFIVLQSLQRVSEEQSFTAEVVGYESE
SQ  AQMQELLKEKKCSTLNYRQTKKESGDREKIADKNNLDDSLAPHPLHICLTIGAAGSNQLVLQIRYFDFIKCATVWGQLNC
SQ  SRNANGQGDTNFVHHLLRHLYPNDLGNELPIPGIQYELRSSDLTAEECVRYLKAKDYGKPFCWLQSMCSIATVNSSMLYK
SQ  HELNLNKNNKEIIDRIARRLNSWQRLSQQIRGLTFKDIDLYSLQENIYPAGLSCSLVQWTAITHEELHSQISDALNSSSA
SQ  DKGITYNSYRAVIVRGSAKMECFIRIPSNYPLEMPLWILNVHWNGCLTAQNNSAIKMMEFWTNSLQPKHLEPNDCILYAQ
SQ  LFRTIYSFDIFLETEGSMQNTIEYNKEKPYISAFAKRSRSRPYKYIKKGSVYAFKQ
//
ID  Q08231;
PN  Nuclear mRNA export protein THP1;
GN  THP1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:12206772, ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:14562095}. Note=Localizes to the nuclear pores.
DR  UNIPROT: Q08231;
DR  UNIPROT: D6W1Z5;
DR  PDB: 3T5V;
DR  PDB: 4TRQ;
DR  PDB: 5G5P;
DR  PDB: 5L3T;
DR  PDB: 5UBP;
DR  Pfam: PF01399;
DR  PROSITE: PS50250;
DE  Function: Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. THP1 binds to RNA in vitro. {ECO:0000269|PubMed:11139493, ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:12702719}.
DE  Reference Proteome: Yes;
DE  Interaction: P06704; IntAct: EBI-1370592; Score: 0.76
DE  Interaction: P46674; IntAct: EBI-797734; Score: 0.88
DE  Interaction: P21576; IntAct: EBI-797734; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-7081522; Score: 0.40
DE  Interaction: Q02804; IntAct: EBI-8230453; Score: 0.22
DE  Interaction: Q6WNK7; IntAct: EBI-1370393; Score: 0.78
DE  Interaction: Q02336; IntAct: EBI-1370467; Score: 0.50
DE  Interaction: P53040; IntAct: EBI-1370499; Score: 0.35
DE  Interaction: Q03761; IntAct: EBI-1370619; Score: 0.35
DE  Interaction: P50875; IntAct: EBI-1370619; Score: 0.35
DE  Interaction: P38811; IntAct: EBI-2124399; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3678586; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3697051; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-3716418; Score: 0.35
DE  Interaction: Q05931; IntAct: EBI-3720118; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3722302; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3730594; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3747715; Score: 0.35
DE  Interaction: O94742; IntAct: EBI-15970396; Score: 0.50
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0003690;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0000282;
GO  GO:0031124;
GO  GO:0006406;
GO  GO:0071028;
GO  GO:0016973;
GO  GO:0045944;
GO  GO:0000973;
GO  GO:0006368;
GO  GO:0006283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDMANQLLDELAHGNFSHLTLNLSQNGREIAILQKQLTGFDDKQLETFVEQHPAMPNDTRFKIMCTSFLNYARDVDPWSA
SQ  WSSSDLIFEFYQCLINCLINDNAPHIEMLIPVATRETEFIINLAGKLDSFHLQLHTRSHQFLSHISSILSRLFNSIKPPR
SQ  GNASSTNIPGKQRILLYLVNKLNNIYFRIESPQLCSNIFKNFQPKSMLAHFNEYQLDQQIEYRYLLGRYYLLNSQVHNAF
SQ  VQFNEAFQSLLNLPLTNQAITRNGTRILNYMIPTGLILGKMVKWGPLRPFLSQETIDNWSVLYKHVRYGNIQGVSLWLRQ
SQ  NERHLCARQLLIVLLEKLPMVTYRNLIKTVIKSWTTEWGQNKLPYSLIERVLQLSIGPTFEDPGAQEITIYNGIHSPKNV
SQ  ENVLVTLINLGLLRANCFPQLQLCVVKKTTMIQEIVPPVNERITKMFPAHSHVLW
//
ID  Q0WSX8;
PN  TIR domain-containing protein;
GN  TIK;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q0WSX8;
DR  UNIPROT: Q9FLA6;
DR  Pfam: PF01582;
DR  PROSITE: PS50104;
DE  Function: Could play a role in nuclear morphology, specifically nuclear size. {ECO:0000269|PubMed:25217773}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0050135;
GO  GO:0061809;
GO  GO:0043621;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDEQVQEPLSDQVFINFRGDELREIFVNHLELQLRNAGINVFIDTKEQKGRRLQYLFTRIKKSKIALAIFSKRYCESKWC
SQ  LDELVTMNEQMKEKKLVVIPIFYNVRSDDVKRAANPDGEGNLDGEFSLPFKQLKQNHAGEPERVEGWERALRSVTKRIGF
SQ  SRSNSKYKHDTDFVLDIVKEVKKQLNIPTDNSWSAIGVAFLAITINLIFSFFIAPKYLPDQKFFQTPEWFIGTLAVVLAS
SQ  WFWYKNNQNKAPPPS
//
ID  O44431;
PN  Protein timeless;
GN  tim;
OS  7224;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm, perinuclear region. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with per is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: O44431;
DR  Pfam: PF04821;
DE  Function: Required for the production of circadian rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLLRNILHIPETHAHFLMPVLQSSGGHQVSMQNTILWNLFIQSIDKLLLYLMTCPQRALWGVTMVQLIAMIYKDQHVNTL
SQ  QKLLNLWFEASLSESSEDNESNTSPPKKGSGDSSPMLTSDPTSDSSDNGSNGGGSSGKKEGCDERRQALREGTEATLQEV
SQ  SRKGHDYQNAMARVTADKPDISEVASDSFEVPCSPQQHLNTEEAMDDIDYEEQVQEYEQEAAAVSSEPLNLSQPANNVNY
SQ  TTNAVYASTTATETQTTSSLCAMTSLCYEPFKPPAPLPTRRNTLSEMLSDNYTSHSHVSAVKLGQKSSHAGQLQLTKGKC
SQ  CPQKRECPSSQSELSDCGYATQVENPESISTSSNDDDGPQGKPQHQKPPCNTKPRNKQRTLMSPQDKKELRRKKLVKRSK
SQ  SSLINMKGLVQHTPTNYDISNLLKEFTVDFLLKGYNYLVEELLKQLLTSAKVLIDTSHFFWLVTFFLKLAAQLELDMEHI
SQ  DSILTYDVLSYLTYEGVSLCEQLELNAQQEGSDLQPYLRRMHLVVTAIREFLQTIETYNKVSHLSEDDRLRLHQLQLQIG
SQ  ATTDLRCLFVLLLRRFNPRIHSKQYLQDLVVTNHILMLILDSAAKLEGGQTIGLSEHISQFATLEVMHYYGILLEDFDNN
SQ  GEFVNDCIFTMMHHIGGDLGQIGVLFQPIILKTYSR
//
ID  P49021;
PN  Protein timeless;
GN  tim;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:8625406}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8625406}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with per is required for nuclear localization.
DR  UNIPROT: P49021;
DR  UNIPROT: A4V040;
DR  UNIPROT: B7Z007;
DR  UNIPROT: B7Z008;
DR  UNIPROT: C9QPB7;
DR  UNIPROT: M9MRE9;
DR  UNIPROT: O44380;
DR  UNIPROT: Q1WWF5;
DR  UNIPROT: Q59E16;
DR  UNIPROT: Q8I037;
DR  UNIPROT: Q95U67;
DR  UNIPROT: Q9VQR6;
DR  UNIPROT: Q9VQR7;
DR  Pfam: PF04821;
DR  Pfam: PF05029;
DE  Function: Required for the production of circadian rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition. {ECO:0000269|PubMed:7481772, ECO:0000269|PubMed:7481773, ECO:0000269|PubMed:8128247, ECO:0000269|PubMed:8625406, ECO:0000269|PubMed:9504927}.
DE  Reference Proteome: Yes;
DE  Interaction: O77059; IntAct: EBI-872146; Score: 0.27
DE  Interaction: P07663; IntAct: EBI-15772062; Score: 0.59
DE  Interaction: Q9Y156; IntAct: EBI-266331; Score: 0.00
DE  Interaction: Q9V480; IntAct: EBI-496420; Score: 0.37
DE  Interaction: Q9VQ30; IntAct: EBI-496427; Score: 0.00
DE  Interaction: Q960S0; IntAct: EBI-496435; Score: 0.00
DE  Interaction: P51123; IntAct: EBI-496442; Score: 0.00
DE  Interaction: Q24432; IntAct: EBI-496450; Score: 0.37
DE  Interaction: O61735; IntAct: EBI-872058; Score: 0.27
DE  Interaction: P18431; IntAct: EBI-874320; Score: 0.27
DE  Interaction: Q24568; IntAct: EBI-9944837; Score: 0.35
DE  Interaction: Q9VDY1; IntAct: EBI-9949981; Score: 0.35
DE  Interaction: M9NFI9; IntAct: EBI-9959939; Score: 0.35
DE  Interaction: Q9V475; IntAct: EBI-16005494; Score: 0.40
DE  Interaction: Q9VDE3; IntAct: EBI-16005513; Score: 0.40
DE  Interaction: P08181; IntAct: EBI-16073655; Score: 0.35
DE  Interaction: P08182; IntAct: EBI-16073713; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0031298;
GO  GO:0003677;
GO  GO:0046982;
GO  GO:0008134;
GO  GO:0071482;
GO  GO:0048512;
GO  GO:0003053;
GO  GO:0060086;
GO  GO:0007620;
GO  GO:0006281;
GO  GO:0000076;
GO  GO:0008062;
GO  GO:0009649;
GO  GO:0045475;
GO  GO:0007617;
GO  GO:0046957;
GO  GO:0000122;
GO  GO:2000678;
GO  GO:0009648;
GO  GO:0050766;
GO  GO:0042749;
GO  GO:0045187;
GO  GO:0050764;
GO  GO:0042306;
GO  GO:0043111;
GO  GO:0048478;
GO  GO:0007622;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDWLLATPQLYSAFSSLGCLEGDTYVVNPNALAILEEINYKLTYEDQTLRTFRRAIGFGQNVRSDLIPLLENAKDDAVLE
SQ  SVIRILVNLTVPVECLFSVDVMYRTDVGRHTIFELNKLLYTSKEAFTEARSTKSVVEYMKHILESDPKLSPHKCDQINNC
SQ  LLLLRNILHIPETHAHCVMPMMQSMPHGISMQNTILWNLFIQSIDKLLLYLMTCPQRAFWGVTMVQLIALIYKDQHVSTL
SQ  QKLLSLWFEASLSESSEDNESNTSPPKQGSGDSSPMLTSDPTSDSSDNGSNGRGMGGGMREGTAATLQEVSRKGQEYQNA
SQ  MARVPADKPDGSEEASDMTGNDSEQPGSPEQSQPAGESMDDGDYEDQRHRQLNEHGEEDEDEDEVEEEEYLQLGPASEPL
SQ  NLTQQPADKVNNTTNPTSSAPQGCLGNEPFKPPPPLPVRASTSAHAQMQKFNESSYASHVSAVKLGQKSPHAGQLQLTKG
SQ  KCCPQKRECPSSQSELSDCGYGTQVENQESISTSSNDDDGPQGKPQHQKPPCNTKPRNKPRTIMSPMDKKELRRKKLVKR
SQ  SKSSLINMKGLVQHTPTDDDISNLLKEFTVDFLLKGYSYLVEELHMQLLSNAKVPIDTSHFFWLVTYFLKFAAQLELDME
SQ  HIDTILTYDVLSYLTYEGVSLCEQLELNARQEGSDLKPYLRRMHLVVTAIREFLQAIDTYNKVTHLNEDDKAHLRQLQLQ
SQ  ISEMSDLRCLFVLLLRRFNPSIHSKQYLQDLVVTNHILLLILDSSAKLGGCQTIRLSEHITQFATLEVMHYYGILLEDFN
SQ  NNGEFVNDCIFTMMHHIGGDLGQIGVLFQPIILKTYSRIWEADYELCDDWSDLIEYVIHKFMNTPPKSPLTIPTTSLTEM
SQ  TKEHNQEHTVCSWSQEEMDTLYWYYVQSKKNNDIVGKIVKLFSNNGNKLKTRISIIQQLLQQDIITLLEYDDLMKFEDAE
SQ  YQRTLLTTPTSATTESGIEIKECAYGKPSDDVQILLDLIIKENKAQHLLWLQRILIECCFVKLTLRSGLKVPEGDHIMEP
SQ  VAYHCICKQKSIPVVQWNNEQSTTMLYQPFVLLLHKLGIQLPADAGSIFARIPDYWTPETMYGLAKKLGPLDKLNLKFDA
SQ  SELEDATASSPSRYHHTGPRNSLSSVSSLDVDLGDTEELALIPEVDAAVEKAHAMASTPSPSEIFAVPKTKHCNSIIRYT
SQ  PDPTPPVPNWLQLVMRSKCNHRTGPSGDPSDCIGSSSTTVDDEGFGKSISAATSQAASTSMSTVNPTTTLSLNMLNTFMG
SQ  SHNENSSSSGCGGTVSSLSMVALMSTGAAGGGGNTSGLEMDVDASMKSSFERLEVNGSHFSRANNLDQEYSAMVASVYEK
SQ  EKELNSDNVSLASDLTRMYVSDEDDRLERTEIRVPHYH
//
ID  O17482;
PN  Protein timeless;
GN  tim;
OS  7244;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with per is required for nuclear localization (By similarity). {ECO:0000250}.
DR  UNIPROT: O17482;
DR  UNIPROT: O44430;
DR  UNIPROT: O44785;
DR  Pfam: PF04821;
DR  Pfam: PF05029;
DE  Function: Required for the production of circadian rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0048511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDWLLATPQLQSVFSSLGSLVGGTYVVSPNALAILEEINHKLTYEDQTLRTFRRAIGFGQNVRVDLIPLLENAKDDAVLE
SQ  SVIRILVNLTVPVECLFSVDLMYRTEVGRHTIFELNKLLYNSKEAFTDPKSTKSVVEYMKHILESDPKLSPHKCDQINNC
SQ  LLLLRNILHIPETHAHFLMPRLQPGSGHQVSMQNTILWNLFIQSIDKLLLYLMTCPQRSLWGVTMVQLIALIYKDQHVST
SQ  LQKLLNLWFEASLSESSDDNESNTTPPKQASGDSSPMLTSDPTSDSSDNGSGGKKESCEERRQALREGTDATLHEVSRKG
SQ  HEYQNAMASSNAANYILEGPCSAQQPWSDCEMQEYKQMTAVISEPLNLSQPADNVNYTTNANYARTTSTDILTKTTSLKH
SQ  EGFKPPAPRRNTLSAILSDNYAPLSFISAVKLGQKSPHAGQLQLIKGKCCPQKRECPSSQSEHSDCGYGTQMENPESIST
SQ  SSNDDDGPQGKPQHQKPPCSSKHRSKQRIFAVPQDTKDLRRKKLVKRSKSSLINMKGLVLHTPNDDDISNLLKEFTVDFL
SQ  LKGYNYLVEELHSQLLSNAKMPIDTSHFFWLVTFFLKFAAQLELDMEHIDTILTFDVLSFLTYEGVSLCEQLELNARQEG
SQ  ADLRPYLRRMHLVVTAIREFLQAIEAYNKVTHLSEDDRYRLRQLQLQISATTDLRCLFVLLLRRFNPSIHSKQYLQDLVV
SQ  TNHILLLILDNAAKLEGGQTIGLSEHISQFATLEVMHYYGILLEDFSNNGEYVNDCIFTMMHHIGGDLDQVGVLYQPIIL
SQ  KAYSRIWEADYDICDDWSDLIEYVIHKFLNTPPKSPMAIPTASLTELTKEQNQEHTACPWSQEDMDSLCWYFVQSKRQND
SQ  VIGNIAKLFSNNGNKIKTRISIIQQLLQQDIITLLEYDDLMKFEDAEYQRTLLATPTSLTTDSGIELKESAYGKPSDDVQ
SQ  VLLDLIRKENKSQHLVWLQKLLLECCYVKMMIKCGSCQTDVEPIMEPVVYHCMFKQKPIPVVQWNNEQSSTMLYQPFMLL
SQ  LHKLGIQLPADAGLIFARIPDFWTPETMYGLAKKLGPLDKLTLKFDPRDLEDAPPSRHHTGARNSLSSISSLEADFGDSE
SQ  GLALIPEVDPAVEKAAAAASAIPNNEIFALPRVKHCNSIIRYTPDPTPPVPSWLQLVMRTKCSKRRSPATDASDCTSTST
SQ  MIADDEIKSYASMAQASHTKLNSGYPTSTLVCMNKLSNCSFAAPPNENSSSSGCGGTASSMSMPNMPDGNSDALMKTSFE
SQ  RLAVTGARYLRPSNTDQDYSALVASVYENEFANSDNVSVASDLTRMYVSDEDEKHELQLQQVE
//
ID  Q86UE8;
PN  Serine/threonine-protein kinase tousled-like 2;
GN  TLK2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2.
DR  UNIPROT: Q86UE8;
DR  UNIPROT: D3DU07;
DR  UNIPROT: Q9UKI7;
DR  UNIPROT: Q9Y4F7;
DR  PDB: 5O0Y;
DR  PDB: 7LO0;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 608439;
DR  OMIM: 618050;
DR  DisGeNET: 11011;
DE  Function: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A and ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12955071, ECO:0000269|PubMed:20016786, ECO:0000269|PubMed:22354037, ECO:0000269|PubMed:9427565}.
DE  Disease: Intellectual developmental disorder, autosomal dominant 57 (MRD57) [MIM:618050]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD57 is characterized by delayed psychomotor development apparent in infancy or early childhood, and a variety of behavioral abnormalities. Affected individuals may have severe gastro-intestinal problems, and facial dysmorphism. {ECO:0000269|PubMed:27479843, ECO:0000269|PubMed:29861108}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q0D2I5; IntAct: EBI-11911984; Score: 0.00
DE  Interaction: Q9NVP2; IntAct: EBI-25476220; Score: 0.56
DE  Interaction: Q15306; IntAct: EBI-6115566; Score: 0.50
DE  Interaction: Q92985; IntAct: EBI-6115673; Score: 0.50
DE  Interaction: Q15418; IntAct: EBI-6256547; Score: 0.35
DE  Interaction: E9Q4K7; IntAct: EBI-11042417; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-12449761; Score: 0.64
DE  Interaction: P56726; IntAct: EBI-11127526; Score: 0.35
DE  Interaction: Q9Y294; IntAct: EBI-11137466; Score: 0.53
DE  Interaction: Q96FJ2; IntAct: EBI-12449804; Score: 0.64
DE  Interaction: P26367; IntAct: EBI-24282100; Score: 0.56
DE  Interaction: Q86UE8; IntAct: EBI-24307235; Score: 0.56
DE  Interaction: Q8NHQ1; IntAct: EBI-24339490; Score: 0.56
DE  Interaction: Q96IK5; IntAct: EBI-24367628; Score: 0.56
DE  Interaction: Q96NE9; IntAct: EBI-23847597; Score: 0.56
DE  Interaction: Q02548; IntAct: EBI-24416001; Score: 0.56
DE  Interaction: Q9NPF5; IntAct: EBI-25206676; Score: 0.56
DE  Interaction: Q7KZS0; IntAct: EBI-25226009; Score: 0.56
DE  Interaction: Q53SF7; IntAct: EBI-11916124; Score: 0.00
DE  Interaction: Q8IY63; IntAct: EBI-11921650; Score: 0.00
DE  Interaction: Q9BWV3; IntAct: EBI-11930524; Score: 0.00
DE  Interaction: Q9UN30; IntAct: EBI-11939262; Score: 0.00
DE  Interaction: Q9UPM6; IntAct: EBI-21621887; Score: 0.35
DE  Interaction: Q5VX52; IntAct: EBI-21635815; Score: 0.35
DE  Interaction: Q8N140; IntAct: EBI-21773860; Score: 0.35
DE  Interaction: Q9UHA7; IntAct: EBI-21786920; Score: 0.35
DE  Interaction: O75679; IntAct: EBI-21798659; Score: 0.35
DE  Interaction: Q9Y6J0; IntAct: EBI-21877366; Score: 0.35
DE  Interaction: Q9UKI8; IntAct: EBI-21877366; Score: 0.35
DE  Interaction: P62979; IntAct: EBI-21877366; Score: 0.35
DE  Interaction: P27361; IntAct: EBI-28934804; Score: 0.35
DE  Interaction: Q96IU4; IntAct: EBI-28942113; Score: 0.35
DE  Interaction: Q96FZ7; IntAct: EBI-28942113; Score: 0.35
DE  Interaction: Q5T3J3; IntAct: EBI-28942113; Score: 0.35
DE  Interaction: P49458; IntAct: EBI-28942113; Score: 0.35
DE  Interaction: P25205; IntAct: EBI-28942113; Score: 0.35
DE  Interaction: P12004; IntAct: EBI-28942113; Score: 0.35
DE  Interaction: Q13257; IntAct: EBI-30825948; Score: 0.44
GO  GO:0005882;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0007049;
GO  GO:0006974;
GO  GO:0071480;
GO  GO:0006325;
GO  GO:0007059;
GO  GO:0035556;
GO  GO:0051179;
GO  GO:0010507;
GO  GO:0032435;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:1902275;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYETSQGKGTPR
SQ  GHKISDYFEFAGGSAPGTSPGRSVPPVARSSPQHSLSNPLPRRVEQPLYGLDGSAAKEATEEQSALPTLMSVMLAKPRLD
SQ  TEQLAQRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLR
SQ  ANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQN
SQ  LIKQQERINSQREEIERQRKMLAKRKPPAMGQAPPATNEQKQRKSKTNGAENETPSSGNTELKDTAPALGAHSLLRLTLA
SQ  EYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAF
SQ  DLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHK
SQ  LMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGT
SQ  YWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRR
SQ  CLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN
//
ID  O55047;
PN  Serine/threonine-protein kinase tousled-like 2;
GN  Tlk2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:10455159}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10455159}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10455159}. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2.
DR  UNIPROT: O55047;
DR  UNIPROT: B1ASU7;
DR  UNIPROT: B1ASU8;
DR  UNIPROT: Q9D5Y5;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A and ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (By similarity). Negative regulator of amino acid starvation-induced autophagy (By similarity). {ECO:0000250}. Testis-specific isoforms may play a role in spermatogenesis. Highly expressed in embryos throughout development. {ECO:0000269|PubMed:10092119}.
DE  Reference Proteome: Yes;
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
GO  GO:0005882;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0042802;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0007049;
GO  GO:0030154;
GO  GO:0006974;
GO  GO:0071480;
GO  GO:0006325;
GO  GO:0007059;
GO  GO:0035556;
GO  GO:0032435;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:1902275;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYDTSQGKGTPR
SQ  GHKISDYFERRAEQPLYGLDGSAAKEASEEQSALPTLMSVMLAKPRLDTEQLAPRGAGLCFTFVSAQQNSPSSTGSGNTE
SQ  HSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKK
SQ  LLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQ
SQ  APPATNEQKQRKSKTNGAENETLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKD
SQ  HPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS
SQ  LDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDF
SQ  GLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQEN
SQ  TILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN
//
ID  Q2KIC8;
PN  Transmembrane protein 100;
GN  TMEM100;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q9CQG9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9CQG9}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Colocalized with HSPA5 in the endoplasmic reticulum (ER). Enriched in ER microsome. Colocalized with BMP4 in neural cell bodies and neural fibers of the enteric nervous system (By similarity). {ECO:0000250}.
DR  UNIPROT: Q2KIC8;
DR  Pfam: PF16311;
DE  Function: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor- dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons. Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex. {ECO:0000250|UniProtKB:Q9CQG9}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001525;
GO  GO:0060842;
GO  GO:0030509;
GO  GO:0071773;
GO  GO:0003198;
GO  GO:0001701;
GO  GO:0007219;
GO  GO:0045603;
GO  GO:2001214;
GO  GO:0043491;
GO  GO:0050848;
GO  GO:0051930;
GO  GO:0001570;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTDEPIKEILGTPKSPKPVAMEKNANGEVVVTLVPLVSEIQLAAATGGAELSCYRCVIPFAVVVLITGTVVTAVAYSFNS
SQ  HGSIISILGLVLLSLGLFLLASSALCWKVRQRSKKAKRRESQTTLVVNQRGWFA
//
ID  Q9NV29;
PN  Transmembrane protein 100;
GN  TMEM100;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane; Multi-pass membrane protein. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Perikaryon. Cytoplasm, perinuclear region. Endoplasmic reticulum. Note=Colocalized with HSPA5 in the endoplasmic reticulum (ER). Enriched in ER microsome. Colocalized with BMP4 in neural cell bodies and neural fibers of the enteric nervous system.
DR  UNIPROT: Q9NV29;
DR  UNIPROT: D3DTY7;
DR  UNIPROT: I3L214;
DR  UNIPROT: Q96FZ0;
DR  Pfam: PF16311;
DR  OMIM: 616334;
DR  DisGeNET: 55273;
DE  Function: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor- dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons. Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex. {ECO:0000250|UniProtKB:Q9CQG9}.
DE  Reference Proteome: Yes;
DE  Interaction: Q15125; IntAct: EBI-24695294; Score: 0.56
DE  Interaction: Q5JX71; IntAct: EBI-24699387; Score: 0.56
DE  Interaction: Q86WV6; IntAct: EBI-23859114; Score: 0.56
DE  Interaction: Q8N1F7; IntAct: EBI-24472902; Score: 0.56
DE  Interaction: O43889; IntAct: EBI-8644963; Score: 0.37
DE  Interaction: P50222; IntAct: EBI-10314436; Score: 0.56
DE  Interaction: Q2TAC2; IntAct: EBI-10314446; Score: 0.56
DE  Interaction: Q9BSE2; IntAct: EBI-10314456; Score: 0.56
DE  Interaction: Q8TBE3; IntAct: EBI-24665642; Score: 0.56
DE  Interaction: O95471; IntAct: EBI-24668401; Score: 0.56
DE  Interaction: Q9BS91; IntAct: EBI-24670892; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-24692797; Score: 0.56
DE  Interaction: P15260; IntAct: EBI-24700563; Score: 0.56
DE  Interaction: P21964; IntAct: EBI-24701763; Score: 0.56
DE  Interaction: P48165; IntAct: EBI-23763990; Score: 0.56
DE  Interaction: Q96TC7; IntAct: EBI-24735870; Score: 0.56
DE  Interaction: Q7Z5P4; IntAct: EBI-23853487; Score: 0.56
DE  Interaction: Q9Y282; IntAct: EBI-24772144; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24779398; Score: 0.56
DE  Interaction: Q8TAF8; IntAct: EBI-23906772; Score: 0.56
DE  Interaction: Q9NRX6; IntAct: EBI-25276333; Score: 0.56
DE  Interaction: Q9H7M9; IntAct: EBI-25282146; Score: 0.56
DE  Interaction: P20138; IntAct: EBI-25283963; Score: 0.56
DE  Interaction: Q8N5M9; IntAct: EBI-25284634; Score: 0.56
DE  Interaction: Q16623; IntAct: EBI-24450934; Score: 0.56
DE  Interaction: Q6ZMZ0; IntAct: EBI-24645075; Score: 0.56
DE  Interaction: O14863; IntAct: EBI-24650582; Score: 0.56
DE  Interaction: Q9H902; IntAct: EBI-24652095; Score: 0.56
DE  Interaction: Q96HE8; IntAct: EBI-24760764; Score: 0.56
DE  Interaction: Q9Y624; IntAct: EBI-24789742; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-24800589; Score: 0.56
DE  Interaction: Q8N3G9; IntAct: EBI-24807995; Score: 0.56
DE  Interaction: Q4KMG9; IntAct: EBI-24808690; Score: 0.56
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001525;
GO  GO:0060842;
GO  GO:0030509;
GO  GO:0071773;
GO  GO:0003198;
GO  GO:0001701;
GO  GO:0007219;
GO  GO:0045603;
GO  GO:2001214;
GO  GO:0043491;
GO  GO:0050848;
GO  GO:0051930;
GO  GO:0001570;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTEEPIKEILGAPKAHMAATMEKSPKSEVVITTVPLVSEIQLMAATGGTELSCYRCIIPFAVVVFIAGIVVTAVAYSFNS
SQ  HGSIISIFGLVVLSSGLFLLASSALCWKVRQRSKKAKRRESQTALVANQRSLFA
//
ID  Q9CQG9;
PN  Transmembrane protein 100;
GN  Tmem100;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:23485812, ECO:0000269|PubMed:25640077}; Multi-pass membrane protein {ECO:0000269|PubMed:23485812, ECO:0000269|PubMed:25640077}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:23485812}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Colocalized with HSPA5 in the endoplasmic reticulum (ER). Enriched in ER microsome. Colocalized with BMP4 in neural cell bodies and neural fibers of the enteric nervous system (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9CQG9;
DR  Pfam: PF16311;
DE  Function: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor- dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10 (PubMed:22783020). Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons (PubMed:25640077). Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex (PubMed:25640077). {ECO:0000269|PubMed:22783020, ECO:0000269|PubMed:25640077}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001525;
GO  GO:0060842;
GO  GO:0030509;
GO  GO:0071773;
GO  GO:0003197;
GO  GO:0003198;
GO  GO:0001701;
GO  GO:0007219;
GO  GO:0045603;
GO  GO:2001214;
GO  GO:0043491;
GO  GO:0050848;
GO  GO:0051930;
GO  GO:0001570;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTEESTKENLGAPKSPTPVTMEKNPKREVVVTTGPLVSEVQLMAATGGAELSCYRCIIPFAVVVFITGIVVTAVAYSFNS
SQ  HGSIISIFGLVLLSSGLFLLASSALCWKVRQRNKKVKRRESQTALVVNQRCLFA
//
ID  Q569C0;
PN  Transmembrane protein 100;
GN  Tmem100;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q9CQG9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9CQG9}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Colocalized with HSPA5 in the endoplasmic reticulum (ER). Enriched in ER microsome. Colocalized with BMP4 in neural cell bodies and neural fibers of the enteric nervous system (By similarity). {ECO:0000250}.
DR  UNIPROT: Q569C0;
DR  Pfam: PF16311;
DE  Function: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor- dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons. Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex. {ECO:0000250|UniProtKB:Q9CQG9}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0001525;
GO  GO:0060842;
GO  GO:0030509;
GO  GO:0071773;
GO  GO:0003197;
GO  GO:0003198;
GO  GO:0001701;
GO  GO:0007219;
GO  GO:0045603;
GO  GO:2001214;
GO  GO:0043491;
GO  GO:0050848;
GO  GO:0051930;
GO  GO:0001570;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTEEPTKENLGGPKSPTPVTMEKSPKSEVVVTTVPLVSEVQLTAATGGAELSCYRCIIPFAVVVFITGIVVTAVAYSFNS
SQ  HGSVISILGLVLLSSGLFLLASSALCWKVRQRNKKVKRRESQTALVVNQRSLFA
//
ID  Q9BVC6;
PN  Transmembrane protein 109;
GN  TMEM109;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}.
DR  UNIPROT: Q9BVC6;
DR  OMIM: 619168;
DR  DisGeNET: 79073;
DE  Function: May mediate cellular response to DNA damage by protecting against ultraviolet C-induced cell death (PubMed:23542032). Can form voltage-gated calcium and potassium channels in vitro (By similarity). {ECO:0000250|UniProtKB:O77751, ECO:0000269|PubMed:23542032}.
DE  Reference Proteome: Yes;
DE  Interaction: O15173; IntAct: EBI-20900351; Score: 0.40
DE  Interaction: Q9Y4K3; IntAct: EBI-1085665; Score: 0.00
DE  Interaction: Q99MK9; IntAct: EBI-2556403; Score: 0.56
DE  Interaction: Q5NET8; IntAct: EBI-2800369; Score: 0.00
DE  Interaction: A0A6H3A8V4; IntAct: EBI-2814063; Score: 0.00
DE  Interaction: Q9Y371; IntAct: EBI-2982508; Score: 0.35
DE  Interaction: P12792; IntAct: EBI-6159029; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06461; IntAct: EBI-11723785; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P06927; IntAct: EBI-11724813; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: P35278; IntAct: EBI-11012136; Score: 0.35
DE  Interaction: P63330; IntAct: EBI-11049240; Score: 0.35
DE  Interaction: Q6DD88; IntAct: EBI-11081408; Score: 0.35
DE  Interaction: P99026; IntAct: EBI-11123979; Score: 0.35
DE  Interaction: P61019; IntAct: EBI-11127113; Score: 0.35
DE  Interaction: Q8N4V1; IntAct: EBI-11130635; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-11155257; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q6NUS6; IntAct: EBI-11387310; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11398030; Score: 0.27
DE  Interaction: Q9WMX2; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q8NBJ4; IntAct: EBI-24660263; Score: 0.56
DE  Interaction: Q9H2K0; IntAct: EBI-24669012; Score: 0.56
DE  Interaction: Q9NR31; IntAct: EBI-24670759; Score: 0.56
DE  Interaction: O43278; IntAct: EBI-23745877; Score: 0.56
DE  Interaction: O14880; IntAct: EBI-24719607; Score: 0.56
DE  Interaction: Q9Y282; IntAct: EBI-24730019; Score: 0.56
DE  Interaction: Q13113; IntAct: EBI-24754975; Score: 0.56
DE  Interaction: Q4KMG9; IntAct: EBI-24763990; Score: 0.56
DE  Interaction: P27105; IntAct: EBI-24771940; Score: 0.56
DE  Interaction: Q96K19; IntAct: EBI-24785970; Score: 0.56
DE  Interaction: Q8TED1; IntAct: EBI-24656159; Score: 0.56
DE  Interaction: P41181; IntAct: EBI-24657441; Score: 0.56
DE  Interaction: O43315; IntAct: EBI-24746173; Score: 0.56
DE  Interaction: Q96HE8; IntAct: EBI-24805207; Score: 0.56
DE  Interaction: Q05940; IntAct: EBI-25271508; Score: 0.56
DE  Interaction: Q6VAB6; IntAct: EBI-14036452; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-20306992; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21028244; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21132574; Score: 0.35
DE  Interaction: Q969F8; IntAct: EBI-21282024; Score: 0.40
DE  Interaction: O43889; IntAct: EBI-22121652; Score: 0.37
DE  Interaction: P60033; IntAct: EBI-25645944; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-26610537; Score: 0.35
DE  Interaction: Q96T52; IntAct: EBI-27049069; Score: 0.27
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0F6B1Q8; IntAct: EBI-27033383; Score: 0.46
DE  Interaction: A0A0F6B5H5; IntAct: EBI-27033770; Score: 0.35
DE  Interaction: P57078; IntAct: EBI-28938584; Score: 0.35
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0005640;
GO  GO:0033017;
GO  GO:0005244;
GO  GO:0071480;
GO  GO:0042771;
GO  GO:0060548;
GO  GO:0034765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAASSISSPWGKHVFKAILMVLVALILLHSALAQSRRDFAPPGQQKREAPVDVLTQIGRSVRGTLDAWIGPETMHLVSES
SQ  SSQVLWAISSAISVAFFALSGIAAQLLNALGLAGDYLAQGLKLSPGQVQTFLLWGAGALVVYWLLSLLLGLVLALLGRIL
SQ  WGLKLVIFLAGFVALMRSVPDPSTRALLLLALLILYALLSRLTGSRASGAQLEAKVRGLERQVEELRWRQRRAAKGARSV
SQ  EEE
//
ID  Q3UBX0;
PN  Transmembrane protein 109;
GN  Tmem109;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}.
DR  UNIPROT: Q3UBX0;
DR  UNIPROT: Q8R006;
DE  Function: May mediate cellular response to DNA damage by protecting against ultraviolet C-induced cell death (PubMed:20060811). Can form voltage-gated calcium and potassium channels in vitro (By similarity). {ECO:0000250|UniProtKB:O77751, ECO:0000250|UniProtKB:Q9BVC6, ECO:0000269|PubMed:20060811}.
DE  Reference Proteome: Yes;
DE  Interaction: O00141; IntAct: EBI-2363087; Score: 0.37
DE  Interaction: P02511; IntAct: EBI-8508071; Score: 0.51
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: P04844; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: G5E9A6; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: P45880; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: P51572; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: P35232; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: Q9BTV4; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: E7EWD6; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: Q9HCK4; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: Q9NWS8; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: Q9UQ84; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-11055815; Score: 0.35
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0033017;
GO  GO:0005244;
GO  GO:0071480;
GO  GO:0042771;
GO  GO:0060548;
GO  GO:0034765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGAHSTPLWSRHLLKAVLMVLVALFLVHSASAQSHREFASPGQQKKETSADILTQIGRSLKEMLDTWLGPETMHVISET
SQ  LLQVMWAISSAISVACFALSGIAAQLLSALGLDGEQLTQGLKLSPSQVQTLLLWGAAALVIYWLLSLLLGLVLALLGRIL
SQ  GGLKLVLFVAGFVALVRSVPDPSTRALMLLALLTLFALLSRLTGSRSSGSHLEAKVRGLERQIEELRGRQRRAAKMPRSM
SQ  EEE
//
ID  O77751;
PN  Transmembrane protein 109;
GN  TMEM109;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:9720923}; Multi-pass membrane protein {ECO:0000305|PubMed:21381722}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21381722, ECO:0000269|PubMed:9720923}; Multi-pass membrane protein {ECO:0000305|PubMed:21381722}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:21381722, ECO:0000269|PubMed:9720923}; Multi-pass membrane protein {ECO:0000269|PubMed:21381722}.
DR  UNIPROT: O77751;
DE  Function: May mediate cellular response to DNA damage by protecting against ultraviolet C-induced cell death (By similarity). Can form voltage-gated calcium and potassium channels in vitro (PubMed:21381722). {ECO:0000250|UniProtKB:Q3UBX0, ECO:0000250|UniProtKB:Q9BVC6, ECO:0000269|PubMed:21381722}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0033017;
GO  GO:0005244;
GO  GO:0071480;
GO  GO:0060548;
GO  GO:0034765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGSGSSAPWGKHLLHAVLMVLVALVLLHSALAQSHRDFAPPGQQRREAPVDLLTQIGRSVRETLDTWIGPETMHLISET
SQ  LSQVMWAISSAISVAFFALSGIAAQLLTALGLDGDHLTQGLKLSPSQVQTFLLWGAGALVVYWLLSLLLGLVLAVLGRIL
SQ  GGLKLVIFLAGFVALVRSVPDPSTRALLLLALLTLYALLSRLTGSRASGAQLEAKVRGLERQVDELRWRQRRAAKGARSV
SQ  EEE
//
ID  Q6AYQ4;
PN  Transmembrane protein 109;
GN  Tmem109;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O77751}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O77751}.
DR  UNIPROT: Q6AYQ4;
DE  Function: May mediate cellular response to DNA damage by protecting against ultraviolet C-induced cell death. Can form voltage-gated calcium and potassium channels in vitro. {ECO:0000250|UniProtKB:Q3UBX0, ECO:0000250|UniProtKB:Q9BVC6}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005640;
GO  GO:0033017;
GO  GO:0005244;
GO  GO:0071480;
GO  GO:0042771;
GO  GO:0060548;
GO  GO:0034765;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGAHSNPSWSRHLFKAVLMVLGALLLVHSASAQTHREFASPGQQKRESSADILTEIGRSLKETLDTWLGPETMHVISET
SQ  LLQVMWAISSAISVACFALSGIAAQLLSALGLDGEQLTQVLKLSPSQVQTLLLWGAAALVIYWLLSLLLGLVLALLGRIL
SQ  GGLKLVLFVAGFVGLVRSVPDPSTRALLLLALLTVFALLSRLTGSRSSGTHLEAKVRGLERQIEELRGRQRRAAKIPRSM
SQ  EEE
//
ID  Q05B54;
PN  Transmembrane protein 134;
GN  TMEM134;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H6X4}.
DR  UNIPROT: Q05B54;
DR  Pfam: PF05915;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSASRPQFSIDDAFELSLEDTGPGLEPSGVARFGPLHFERRARFEVADEDKQSRLRYQNLENDEDGAQASPEPDGGVSSR
SQ  DSGQTSIRSSQWSFSSISSSTQRSYNACCSWTQHPLIQKNHRVVLASFLLLLLGLVLILTGVGLEVAPSPGVSSAIFFVP
SQ  GFLLLVPGVYHVIFIYCAVKGHRGFQFFYLPYFEK
//
ID  Q9H6X4;
PN  Transmembrane protein 134;
GN  TMEM134;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27899274}.
DR  UNIPROT: Q9H6X4;
DR  UNIPROT: Q08AK4;
DR  UNIPROT: Q6PJN3;
DR  Pfam: PF05915;
DR  DisGeNET: 80194;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-25368557; Score: 0.37
DE  Interaction: Q5T9L3; IntAct: EBI-22085286; Score: 0.49
DE  Interaction: Q15303; IntAct: EBI-25369580; Score: 0.37
DE  Interaction: P21860; IntAct: EBI-25369272; Score: 0.37
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0048471;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAARPQFSIDDAFELSLEDGGPGPESSGVARFGPLHFERRARFEVADEDKQSRLRYQNLENDEDGAQASPEPDGGVGTR
SQ  DSSRTSIRSSQWSFSTISSSTQRSYNTCCSWTQHPLIQKNRRVVLASFLLLLLGLVLILVGVGLEATPSPGVSSAIFFVP
SQ  GFLLLVPGVYHVIFIYCAVKGHRGFQFFYLPYFEK
//
ID  Q8R0J4;
PN  Transmembrane protein 134;
GN  Tmem134;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H6X4}.
DR  UNIPROT: Q8R0J4;
DR  UNIPROT: Q3TLG9;
DR  UNIPROT: Q8C1M3;
DR  UNIPROT: Q9CR66;
DR  Pfam: PF05915;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0048471;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSAARPQFSIDDAFELTLEDAGPEPESSGVARFGPLHFERRARFEVADEDKQSRLRYQNLENDEDGAQASPEPDGGVSTR
SQ  DSGHMSVRSSQWSFSTISSSTQRSYNACCSWTQHPLIQKNRRVVLASFLLLLLGLVLILVGVGLEVAPSPGVSSAIFFVP
SQ  GILLLVPGVYHVIFIYCAVKGRRGFQFFYLPYFEK
//
ID  Q32PF0;
PN  Transmembrane protein 201;
GN  TMEM201;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q5SNT2}.
DR  UNIPROT: Q32PF0;
DR  Pfam: PF10476;
DR  Pfam: PF09779;
DE  Function: May define a distinct membrane domain in the vicinity of the mitotic spindle. Involved in the organization of the nuclear envelope implicating EMD, SUN1 and A-type lamina. Involved in nuclear movement during fibroblast polarization and migration. Proposed to be involved in actin-dependent nuclear movement via association with transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow. May recruit Ran GTPase to the nuclear periphery. {ECO:0000250|UniProtKB:A2A8U2, ECO:0000250|UniProtKB:Q5SNT2}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005639;
GO  GO:0031965;
GO  GO:0000922;
GO  GO:0051015;
GO  GO:0005521;
GO  GO:0030473;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGVSALLARCPTAGLAGGLGVTACAAAGVLLYRIARRMKPTHTVVNCWFCNQDTVVPYGNRNCWDCPHCEQYNGFQENG
SQ  DYNKPIPAQYLEHLNHVVSGSPGPRAPAQPLQWVSSQVLLCRRCSHHQTAKVKQLAAFSPRDEGRYDEEIEVYRHHLEQM
SQ  YKLCRPCQAAVEHYIKHQNRQLRALLLSHQFKRREADQTHTQSFCASAVKAPAQVIVLRALAFLACAFLLTTALYGTSNP
SQ  FAPGAPLPPTLPTGSNGSAPPDNGTATGAEGWRQLLGLLPEHAAEKLREAWAFGQSHQMGVVALGLLTCLLAMLLAGRIR
SQ  LRRIDAFSTGLWALLLGLHLAEQYLQAASPSWLDTLKFSTTSLCCLVGFTAAVATRKATGPRRFRPRRSEKQQ
//
ID  Q22747;
PN  Transmembrane protein 201 homolog;
GN  samp;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:25057012}; Multi-pass membrane protein {ECO:0000255}. Note=Localization at the nuclear envelope does not require lmn-1. {ECO:0000269|PubMed:25057012}.
DR  UNIPROT: Q22747;
DR  Pfam: PF09779;
DE  Function: Plays a role in nuclear migration in hypodermal cells. {ECO:0000269|PubMed:25057012}.
DE  Reference Proteome: Yes;
DE  Interaction: O17915; IntAct: EBI-338759; Score: 0.00
DE  Interaction: Q94420; IntAct: EBI-2420714; Score: 0.49
DE  Interaction: Q9U2Z1; IntAct: EBI-6458511; Score: 0.37
DE  Interaction: Q21021; IntAct: EBI-6462519; Score: 0.37
DE  Interaction: Q9N5U1; IntAct: EBI-6462529; Score: 0.37
DE  Interaction: H2L0Q6; IntAct: EBI-11470172; Score: 0.37
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0051015;
GO  GO:0005521;
GO  GO:0009792;
GO  GO:0030473;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVAAAVGVIASVPILYKAIRPRIKTSVECWFCRKSTKVEYQQRNSFTCPSCEQYNGFTEDGDYNRRIPGQAWTTPKRYC
SQ  EPGKMQSEKPSTFLDRFGGVNMSPKASNGLCSECNLGQEIIMNKVAEFEPIDEDRWNEELEDYRYKLERMYQLCPRCTIQ
SQ  VHGKLEEDKKKYSYLLKVKYKLKHAIGSTLREVMNNQKRSRRFFFAGGSTCEALHFGCLISSIILFLANIDFLQQDAGAS
SQ  LINLPKALQDILPEVYKYSFVINFLIFTTHLIAAFNNKCRVTLPDLLLPILLILAMLTVLTSSDNLSQDVALVRGACASF
SQ  STILSMAVTLLPRKKLHKKRPNKIVSSAFSVASTPISQCSSQNSRNASLLDHDHTILRRSPHTPSASPPAMNSSPPLLRE
SQ  ITNGPVWSAMRSRENKENMQSYQTKPNNHVESMDWDDSESMAAQSVAQSTRSSHFKPGLLSRNINERMTAQQLTPSVANL
SQ  NLDTRSVDSPSIFSRQHRQMAQQQNHTPTRSLFGPPRSMVASQYDRSHYMAPEAHTRPGSVFTSVSQQDGHSTVSGAWQC
SQ  RVIGILFALVFIVLIMQIGLFYVLFTRN
//
ID  A4IG66;
PN  Transmembrane protein 201;
GN  tmem201;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein {ECO:0000305}.
DR  UNIPROT: A4IG66;
DR  Pfam: PF10476;
DR  Pfam: PF09779;
DE  Function: May be involved in actin-dependent nuclear movement. May be involved in the organization of the nuclear envelope. May recruit Ran GTPase to the nuclear periphery. {ECO:0000250|UniProtKB:A2A8U2, ECO:0000250|UniProtKB:Q5SNT2}.
DE  Reference Proteome: Yes;
GO  GO:0005639;
GO  GO:0031965;
GO  GO:0051015;
GO  GO:0005521;
GO  GO:0030473;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEALNQILIEYPPLVVGGVGATAVAAGGALIYRIATRKKPTHLQVNCWFCNQDTVVPYGNRNCWDCPYCEQYNGFQENGD
SQ  YNKPIPAQYMEHLNHGVSAGVPETPKTLQWVNCQMLLCKKCNNNQTLKIKQLASFIPREDENYDEEIEVYKHHLEQTYKL
SQ  CRPCQTAVEYYIKHQNRQLRALLFNHQLRRTRDADKAFIKNTYSLSTPAWLILLRILTFLACAFLVAVALSGYVDESPSV
SQ  TQTLSGGVVPPKRVLQNENESKTDEGSLMWDDLMGLLPEKAVENARLFWQSGSDHQMAVASVGLLTCITGVLMAGPVRLR
SQ  RIDAVASVLWLLVICFYLAECYLKTDVPSWLEMVKFGITSVCCLVGFAAAVATRKSTSQRRARGRRYLSGGSPGEFFCNH
SQ  GPLLSAPVSESSTFIPTPPPNLSQLLIRQQSQRTRKASPSSLPGRLNRALSLGTIPSLARADSGFLFSGSRPSSQCKDSP
SQ  PSDYYSLKSGSRPSSPGPSPTPSVAGSVTSTSSSARQRRPLISPARLNISGQKLRLFSSPLEPFSLASPPPFLSEHNPMH
SQ  SRGFLPDVPHFHLQNHGSVIDEGSVFEHLEKPMGSSSSSSNCHVDTTTGNNIESKPGWKGFLGMTLWPGLLFASLTINLS
SQ  FICIYVYYNWR
//
ID  Q5SNT2;
PN  Transmembrane protein 201;
GN  TMEM201;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 2]: Nucleus inner membrane {ECO:0000269|PubMed:19494128, ECO:0000269|PubMed:21610090}; Multi-pass membrane protein {ECO:0000269|PubMed:19494128}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19494128}. Note=The C- terminal of isoform 2 is located on the nucleoplasmic side. During interphase, isoform 2 is distributed in the inner nuclear membrane in distinct micro-domains and during mitosis, it is found in the ER but it also localizes to the polar regions of the mitotic spindle. {ECO:0000269|PubMed:19494128, ECO:0000269|PubMed:21610090}.
DR  UNIPROT: Q5SNT2;
DR  UNIPROT: B9EH90;
DR  UNIPROT: Q5SNT3;
DR  Pfam: PF10476;
DR  Pfam: PF09779;
DR  DisGeNET: 199953;
DE  Function: Involved in nuclear movement during fibroblast polarization and migration. Proposed to be involved in actin-dependent nuclear movement via association with transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow (By similarity). Overexpression can recruit Ran GTPase to the nuclear periphery (PubMed:27541860). {ECO:0000250|UniProtKB:A2A8U2, ECO:0000305|PubMed:27541860}. [Isoform 2]: May define a distinct membrane domain in the vicinity of the mitotic spindle (PubMed:19494128). Involved in the organization of the nuclear envelope implicating EMD, SUN1 and A-type lamina (PubMed:21610090). {ECO:0000269|PubMed:19494128, ECO:0000269|PubMed:21610090}.
DE  Reference Proteome: Yes;
DE  Interaction: P50402; IntAct: EBI-24476865; Score: 0.68
DE  Interaction: P57078; IntAct: EBI-12503575; Score: 0.35
DE  Interaction: P61021; IntAct: EBI-11012076; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: Q9UPX6; IntAct: EBI-24314531; Score: 0.56
DE  Interaction: Q6ZS10; IntAct: EBI-24353816; Score: 0.56
DE  Interaction: Q969F0; IntAct: EBI-25247063; Score: 0.56
DE  Interaction: Q9GZY8; IntAct: EBI-24366218; Score: 0.56
DE  Interaction: Q96KC8; IntAct: EBI-24662993; Score: 0.56
DE  Interaction: Q53FP2; IntAct: EBI-24683073; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-24688407; Score: 0.56
DE  Interaction: P00387; IntAct: EBI-24711951; Score: 0.56
DE  Interaction: Q96Q45; IntAct: EBI-24728264; Score: 0.56
DE  Interaction: Q8N386; IntAct: EBI-24756168; Score: 0.56
DE  Interaction: Q8N183; IntAct: EBI-25279841; Score: 0.56
DE  Interaction: P54829; IntAct: EBI-24436921; Score: 0.56
DE  Interaction: Q92806; IntAct: EBI-24535389; Score: 0.56
DE  Interaction: A2A2Y4; IntAct: EBI-24594602; Score: 0.56
DE  Interaction: Q9BXS9; IntAct: EBI-24638495; Score: 0.56
DE  Interaction: Q8TAF8; IntAct: EBI-24658961; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-24759602; Score: 0.56
DE  Interaction: Q7Z7G2; IntAct: EBI-24799219; Score: 0.56
DE  Interaction: P20036; IntAct: EBI-21511890; Score: 0.35
DE  Interaction: O15482; IntAct: EBI-21523851; Score: 0.35
DE  Interaction: Q8NBM4; IntAct: EBI-25771384; Score: 0.35
DE  Interaction: O60285; IntAct: EBI-28931176; Score: 0.35
DE  Interaction: Q6J9G0; IntAct: EBI-28941708; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32717464; Score: 0.42
DE  Interaction: O15146; IntAct: EBI-32724025; Score: 0.27
GO  GO:0005737;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0000922;
GO  GO:0051015;
GO  GO:0005521;
GO  GO:0051642;
GO  GO:0010761;
GO  GO:0006998;
GO  GO:0030473;
GO  GO:0090435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGVSALLARCPTAGLAGGLGVTACAAAGVLLYRIARRMKPTHTMVNCWFCNQDTLVPYGNRNCWDCPHCEQYNGFQENG
SQ  DYNKPIPAQYLEHLNHVVSSAPSLRDPSQPQQWVSSQVLLCKRCNHHQTTKIKQLAAFAPREEGRYDEEVEVYRHHLEQM
SQ  YKLCRPCQAAVEYYIKHQNRQLRALLLSHQFKRREADQTHAQNFSSAVKSPVQVILLRALAFLACAFLLTTALYGASGHF
SQ  APGTTVPLALPPGGNGSATPDNGTTPGAEGWRQLLGLLPEHMAEKLCEAWAFGQSHQTGVVALGLLTCLLAMLLAGRIRL
SQ  RRIDAFCTCLWALLLGLHLAEQHLQAASPSWLDTLKFSTTSLCCLVGFTAAVATRKATGPRRFRPRRFFPGDSAGLFPTS
SQ  PSLAIPHPSVGGSPASLFIPSPPSFLPLANQQLFRSPRRTSPSSLPGRLSRALSLGTIPSLTRADSGYLFSGSRPPSQVS
SQ  RSGEFPVSDYFSLLSGSCPSSPLPSPAPSVAGSVASSSGSLRHRRPLISPARLNLKGQKLLLFPSPPGEAPTTPSSSDEH
SQ  SPHNGSLFTMEPPHVPRKPPLQDVKHALDLRSKLERGSACSNRSIKKEDDSSQSSTCVVDTTTRGCSEEAATWRGRFGPS
SQ  LVRGLLAVSLAANALFTSVFLYQSLR
//
ID  A2A8U2;
PN  Transmembrane protein 201;
GN  Tmem201;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 2]: Nucleus inner membrane {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5SNT2}. Note=The C-terminal of isoform 2 is located on the nucleoplasmic side. During interphase, isoform 2 is distributed in the inner nuclear membrane and during mitosis, it is found in the ER but it also localizes to the polar regions of the mitotic spindle (By similarity). {ECO:0000250|UniProtKB:Q5SNT2}.
DR  UNIPROT: A2A8U2;
DR  UNIPROT: Q3U5F3;
DR  UNIPROT: Q6GQS9;
DR  UNIPROT: Q8BNY3;
DR  Pfam: PF10476;
DR  Pfam: PF09779;
DE  Function: Involved in nuclear movement during fibroblast polarization and migration (PubMed:22349700). May recruit Ran GTPase to the nuclear periphery (By similarity). {ECO:0000250|UniProtKB:Q5SNT2, ECO:0000269|PubMed:22349700}. [Isoform 2]: May define a distinct membrane domain in the vicinity of the mitotic spindle. Involved in the organization of the nuclear envelope implicating EMD, SUN1 and A-type lamina. {ECO:0000250|UniProtKB:Q5SNT2}. [Isoform 3]: Proposed to be involved in actin-dependent nuclear movement; via SUN2 associates with transmembrane actin- associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow. {ECO:0000305|PubMed:22349700}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8BJS4; IntAct: EBI-12591483; Score: 0.54
DE  Interaction: P48678; IntAct: EBI-12591514; Score: 0.40
DE  Interaction: Q6ZWQ0; IntAct: EBI-12596297; Score: 0.27
GO  GO:0032541;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0031616;
GO  GO:0051015;
GO  GO:0005521;
GO  GO:0051642;
GO  GO:0010761;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0030473;
GO  GO:0090435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEGVSALLASCPTAGLAGGLGVTACAAAGVVLYRIARRVKPTHTMVNCWFCNHDTLVPYGNRNCWDCPHCEQYNGFQENG
SQ  DYNKPIPAQYMEHLNHVVSSVPSPRDPAQPQQWVSSQVLLCRRCSHHQTTKIKQLAAFTPREEGRYDEEIEVYRHHLEQM
SQ  YKLCRPCQAAVEYYIKHQNRQLRALLLSHQFRRREADQAHGQSFSSSAVKAPFQVILLRALAFLACAFLLFTTLYGPSEP
SQ  FTPGAALPPALPPGGNSSAASDNTTSQAEGWQQLLGLLPEHATEKLHEAWAFGQSHQTSIVAVGLLTCLLAMLLAGRIRL
SQ  RRIDAFSTCLWALLLGLHLAEHYLQAASPGWLDTLKFSTTSLCCLVGFTAAVATRKSTGPRRFRPRRYFSGDSASLFPSS
SQ  PSLAVPYPSVTSSPASLFIPTPPGFLPLTKQQLFRSPRRVSPSSLPGRLSRALSLGTIPPLTRTDSGYLFSGSRPPSRVS
SQ  PAGEVSLSDYFSLLSSSFPASPLPSPAPSVASSVASSSGSLRHRRPLISPARLNLKGQKLLLFSSPGEAPNTPSSSEEFS
SQ  PPNGSLFIESPQLPQRNHTRDTKHTMEMRSMLARDSARSSHSIKKEDESSQSSTCVVDTTTKGCSEETTPWKARVSPSLV
SQ  RGLLAVSLAVNALFTSAYLYQSLR
//
ID  Q9VVA8;
PN  Transmembrane protein 258;
GN  kud;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:28716842}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:28716842}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:28716842}.
DR  UNIPROT: Q9VVA8;
DR  Pfam: PF05251;
DE  Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). In addition may regulates nuclear envelope (NE) architecture and nuclear positioning through the linker of nucleoskeleton and cytoskeleton (LINC)-dependent and -independent mechanisms (PubMed:28716842). {ECO:0000250|UniProtKB:P61165, ECO:0000269|PubMed:28716842}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9W0Q4; IntAct: EBI-248309; Score: 0.00
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0031309;
GO  GO:0043227;
GO  GO:0005640;
GO  GO:0034998;
GO  GO:0032991;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0006487;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVMQRYVSPVNPAVFPHLATVLLVIGTFFTAWFFIFVVSRKSSKESTLIKELLISLCASIFLGFGIVFLLLTVGIYV
//
ID  A4FV75;
PN  Trimeric intracellular cation channel type A;
GN  TMEM38A;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}.
DR  UNIPROT: A4FV75;
DR  Pfam: PF05197;
DE  Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000250|UniProtKB:Q3TMP8}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0033017;
GO  GO:0042802;
GO  GO:0005267;
GO  GO:0071313;
GO  GO:0007029;
GO  GO:0010881;
GO  GO:0014808;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRHHPMASWLCAMLHCFGSYILADLLLGEPVIDY
SQ  FSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFVMIATGWVKGSGVT
SQ  LMSNLEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTMFMVSCKVFLTATHSHSSPFDVL
SQ  EAYICPVLFGSASGGDHHHNNHGGSQGGSGPGSPHSPLPSKSKEELSEGSRKKKTKKAD
//
ID  Q5ZK43;
PN  Trimeric intracellular cation channel type A;
GN  TMEM38A;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}.
DR  UNIPROT: Q5ZK43;
DR  PDB: 6IYU;
DR  PDB: 6IYX;
DR  PDB: 6IYZ;
DR  PDB: 6IZ0;
DR  PDB: 6IZ1;
DR  PDB: 6IZF;
DR  Pfam: PF05197;
DE  Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000250|UniProtKB:Q3TMP8}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0033017;
GO  GO:0042802;
GO  GO:0005267;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELPGALQLGELAAAFASVPVFPLFDAAYFIVSVLYLKYEPGAVEMSRKSPFASWLCAMLHCFGSYILADLLLGESPIHY
SQ  FSNNSSVILATAVWYLIFFCPMNLFYKCVSFLPVKLIFVAMKEVVRVRKIAAGVHHAHHQYHHGWFIMMATGWVKGSGVA
SQ  LMSNFEQLLRGVWRPETNEILHMSFPTKASLYGTVLFTLQQTHWLPVSEANLVFFFTMFMIVCKVFMTATHSHASPFAPV
SQ  EGFICPVFFGSVSSGHTSHHNQHGHSHEASYQPPPPVKSKEELNEGTRKRKAKKAE
//
ID  Q6P2T0;
PN  Trimeric intracellular cation channel type A;
GN  tmem38a;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}.
DR  UNIPROT: Q6P2T0;
DR  Pfam: PF05197;
DE  Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000250|UniProtKB:Q3TMP8}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0033017;
GO  GO:0042802;
GO  GO:0005267;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVLDVLNLGEIAQYFSKMAMFPVFDVAYYIVSILYLKYEPGAVEVSRRSPVASWLCAMLYCFGSYILADIMLGVCPIDY
SQ  FHNNSHILLASAVWYLIFFCPLNLFYKCVAFMPVKLVLVALKEVVRTRKIAAGVHHAHHAYHHGWLIMVITGYVKGSGVA
SQ  LMSNFEQLLRGVWKPETNEVLNMSFPTKASLYGAILFTLQEAHVLPVSKSTLICLFTLFMVSSKVFMTARHSHGSPFALI
SQ  ESWVCHVLFGSPLGTEDAHDHHHAAPAAAPAPLSPAKNKEELSEGTRKRKSKKAE
//
ID  Q9H6F2;
PN  Trimeric intracellular cation channel type A;
GN  TMEM38A;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}.
DR  UNIPROT: Q9H6F2;
DR  UNIPROT: A8K9P9;
DR  Pfam: PF05197;
DR  OMIM: 611235;
DR  DisGeNET: 79041;
DE  Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000250|UniProtKB:Q3TMP8}.
DE  Reference Proteome: Yes;
DE  Interaction: P26439; IntAct: EBI-21761289; Score: 0.35
DE  Interaction: Q9NQ48; IntAct: EBI-21774512; Score: 0.35
DE  Interaction: Q8IVA1; IntAct: EBI-21774512; Score: 0.35
DE  Interaction: Q6PIU2; IntAct: EBI-21774512; Score: 0.35
DE  Interaction: Q5BKU9; IntAct: EBI-21774512; Score: 0.35
DE  Interaction: O60496; IntAct: EBI-21774512; Score: 0.35
GO  GO:0070062;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0033017;
GO  GO:0042802;
GO  GO:0005267;
GO  GO:0071313;
GO  GO:0007029;
GO  GO:0010881;
GO  GO:0014808;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRRHPIASWLCAMLHCFGSYILADLLLGEPLIDY
SQ  FSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFVMIATGWVKGSGVA
SQ  LMSNFEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTLFMVSCKVFLTATHSHSSPFDAL
SQ  EGYICPVLFGSACGGDHHHDNHGGSHSGGGPGAQHSAMPAKSKEELSEGSRKKKAKKAD
//
ID  Q3TMP8;
PN  Trimeric intracellular cation channel type A;
GN  Tmem38a;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}.
DR  UNIPROT: Q3TMP8;
DR  UNIPROT: A5A6S4;
DR  UNIPROT: A7LBB7;
DR  UNIPROT: Q3TZB9;
DR  UNIPROT: Q91WL2;
DR  Pfam: PF05197;
DE  Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000269|PubMed:17611541}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0016529;
GO  GO:0033017;
GO  GO:0015269;
GO  GO:0042802;
GO  GO:0005267;
GO  GO:0071313;
GO  GO:0007029;
GO  GO:0098662;
GO  GO:0071805;
GO  GO:0010881;
GO  GO:0014808;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLMSALSLGELALSFSRVPLFPVFDLSYFIVSIIYLKYEPGAVELSRRHPVASWLCAMLHCFGSYILADLLLGEPIIDY
SQ  FSNSSSILLASGVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFIMIATGWVKGSGVA
SQ  LLSNVEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFVFTMFMVSCKVFLTATHSHSSPFDIL
SQ  EGYICPVLFGATWGGDHHHDNHGAPHGMGLGTQHSGLPAKAKEELGEGSRKKKTKKAD
//
ID  A5A6S6;
PN  Trimeric intracellular cation channel type A;
GN  TMEM38A;
OS  9986;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:17611541}; Multi-pass membrane protein {ECO:0000269|PubMed:17611541}. Nucleus membrane {ECO:0000269|PubMed:17611541}.
DR  UNIPROT: A5A6S6;
DR  Pfam: PF05197;
DE  Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000250|UniProtKB:Q3TMP8, ECO:0000269|PubMed:17611541}.
DE  Reference Proteome: Yes;
DE  Interaction: A5A6S6; IntAct: EBI-15646438; Score: 0.52
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0033017;
GO  GO:0042802;
GO  GO:0005267;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRRHPVASWLCAMLHCFGSYILADLLLGEPLIDY
SQ  FSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFIMIATGWVKGSGVA
SQ  LLSNVEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTMFMVSCKVFLTATHSHSSPFDVL
SQ  EAYVCPVLFGTGSGGDHPQDNHGAWPGGPPSGALATKSKEELSEGSRKKKTKKAD
//
ID  A6ZIQ8;
PN  Trimeric intracellular cation channel type A;
GN  Tmem38a;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}.
DR  UNIPROT: A6ZIQ8;
DR  Pfam: PF05197;
DE  Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000250|UniProtKB:Q3TMP8}.
DE  Reference Proteome: Yes;
DE  Interaction: Q969Q1; IntAct: EBI-21997483; Score: 0.35
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0016529;
GO  GO:0033017;
GO  GO:0042802;
GO  GO:0005267;
GO  GO:0071313;
GO  GO:0007029;
GO  GO:0098662;
GO  GO:0071805;
GO  GO:0010881;
GO  GO:0014808;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLISSLSLGELALSFSRVPLFPVFDLSYFIVSIIYLKYEPGSVELSRRHPVASWLCAMLHCFGSYILADLLLGEPIIDY
SQ  FSNSSSILLASGVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHYHHGWFIMIATGWVKGSGVAL
SQ  LSNLEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFVFTMFMVSCKVFLTATHSHSSPFDVLE
SQ  GYICPVLFGATWGGDHHHDNHGAPHGMGLGTQHSGLPAKAKEELSEGFRKKKTKKAD
//
ID  Q7ZY07;
PN  Trimeric intracellular cation channel type A;
GN  tmem38a;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}.
DR  UNIPROT: Q7ZY07;
DR  Pfam: PF05197;
DE  Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000250|UniProtKB:Q3TMP8}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0033017;
GO  GO:0042802;
GO  GO:0005267;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELLSALSLDDLAASFSKLPVFPLFDVAYYIISILYLKYEPGAVDLSKRSPVASWLCAMLYCFGSYILADVLLGESPIHY
SQ  FSNNANILLASAVWYLTFFCPLNIFYKIVSFLPVKLVLVGMKEVVRVRKIAMGIHHAHHHYHHGWVIMVLIGWVKGSGVA
SQ  LMSNLEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQAHWLPISKAYLIFFFTLFMAVCKIYMTATHSHGSPFAIF
SQ  ESGICYVLFAAANGDHDDHGNHHHHHDDHDVSHSAGKSKEEHNEGTRKRKTKKAE
//
ID  Q6P8F8;
PN  Trimeric intracellular cation channel type A;
GN  tmem38a;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}.
DR  UNIPROT: Q6P8F8;
DR  Pfam: PF05197;
DE  Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. {ECO:0000250|UniProtKB:Q3TMP8}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0033017;
GO  GO:0042802;
GO  GO:0005267;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MELLSALSLDDLAVAFSKLPVFPLFDVAYYIISILYLKYEPGAVDLSKRSPVASWLCAMLYCFGSYILADVLLGESPIHY
SQ  FSNNANILLASAVWYLTFFCPLNIFYKIVSFLPLKLVLVGMKEVVRVRKIAMGIHHAHHHYHHGWVIMVLIGWVKGSGVA
SQ  LMSNLEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQAHWLPISKAYLIFFFTLFMAICKIYMTATHSHGSPFAIF
SQ  ESGICCVLFGAANGDHDDHGDHHHHHDDHDVSHSTVKSKEELNEGTRKRKTKKAE
//
ID  Q5PPS7;
PN  Transmembrane protein 53-A;
GN  tmem53;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q9D0Z3}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q5PPS7;
DR  Pfam: PF05705;
DE  Function: Ensures normal bone formation, through the negative regulation of bone morphogenetic protein (BMP) signaling in osteoblast lineage cells by blocking cytoplasm-nucleus translocation of phosphorylated SMAD proteins. {ECO:0000250|UniProtKB:Q9D0Z3}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0030514;
GO  GO:0030279;
GO  GO:0045668;
GO  GO:0046822;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGDSELDYTIEFPEPSLQGWPWDPEREPVVILLGWGGCKDHYLAKYSAIYHNQGCTVIKYTAAWKAVFITESLGLNSLRE
SQ  DAKKLLELLFDYEIEKSPIVFHVFSNGGFMLYRYIVELLHSHCPLNKLHVVGTIFDSAPGNRNVIGSVRALDTILRTSTN
SQ  KAFRFLALAAFAILVIILRILLYPLTRFLHENHYDAMKKDPSRWPQLYLYSRADPIISYLDVESMIAARRRRCLPTETLD
SQ  FGKSEHVSHFRRFPQRYSEICTSFLRDCVRKASISMLRSEHPVSF
//
ID  Q6DJC8;
PN  Transmembrane protein 53-B;
GN  tmem53;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q9D0Z3}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q6DJC8;
DR  Pfam: PF05705;
DE  Function: Ensures normal bone formation, through the negative regulation of bone morphogenetic protein (BMP) signaling in osteoblast lineage cells by blocking cytoplasm-nucleus translocation of phosphorylated SMAD proteins. {ECO:0000250|UniProtKB:Q9D0Z3}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0030514;
GO  GO:0030279;
GO  GO:0045668;
GO  GO:0046822;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGDPELDYTIEFPEPSLQGCPWDPEREPVVILLGWGGCKDQYLAKYSAIYHNQGCTVIKYTAAWNAVFISESLGFSSLRE
SQ  DAKKLLELLFDYEIEKSPILFHVFSNGGFMLYRYIVELLHSHCRLNKLHVVGTIFDSAPGNRNVIGSVRALDTILRTSTN
SQ  NAIRFLALAAFAIMVIILRIVLYPVTKFLHENHYDAMKKDSSRWPQLYLYSRADPIISYIDVESMIAARRRCCLPTEALD
SQ  FGKSEHVSHFRRFPHRYSEMCTSFLRDCVRKAAVSMLTSEHPVSF
//
ID  Q3SZ36;
PN  Transmembrane protein 18;
GN  TMEM18;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q96B42}. Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q3SZ36;
DR  Pfam: PF14770;
DE  Function: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats. Cell migration modulator which enhances the glioma-specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
GO  GO:0016477;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSAFSVSRFPVSIPAVITQTDWTEPWLVGLAGFHVLCLLLTCFSSQRYRLQVGHFLCLVTLVYCAEYINEVAAMNWRLF
SQ  SKHQYFDSRGMFISLVFSAPLLLNALVIVVLWVRKTLVVMTDLRSLREQRRARARPKEE
//
ID  Q5F410;
PN  Transmembrane protein 18;
GN  TMEM18;
OS  9031;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q5F410;
DR  Pfam: PF14770;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRSVAVAMEQPLHGPPGLSTILARTDWAEPWLLGLAGFHVLCFLLTCFSFQHYRVQIGHFLCMVCLVYCAEYINELAAMN
SQ  WRLFSKYQYFDSRGMFISLVFSAPLLVNTIIIVVNWVYRTLNVMTELKTLQQRIKAEKDKKK
//
ID  Q641M3;
PN  Transmembrane protein 18;
GN  tmem18;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q641M3;
DR  Pfam: PF14770;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTASNTKNASAIPIDKFSNVRITSIWTFLQSVDWSEPWLMALLAFHVFCFAFTLLSCKYYRIQICHFLLMVAMVYSAEYL
SQ  NELAAMNWRSFSKFQYFDSKGMFISLVYSVPLLLNTVIIVAVWVWRTFSTMTELKILQLKRKAARENHKKTQ
//
ID  Q96B42;
PN  Transmembrane protein 18;
GN  TMEM18;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:18559506, ECO:0000269|PubMed:21980424}. Nucleus membrane {ECO:0000269|PubMed:18559506, ECO:0000269|PubMed:21980424}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q96B42;
DR  UNIPROT: D6W4X9;
DR  UNIPROT: Q8N5H2;
DR  UNIPROT: Q9NTH3;
DR  Pfam: PF14770;
DR  OMIM: 613220;
DR  DisGeNET: 129787;
DE  Function: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats. Cell migration modulator which enhances the glioma-specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC). {ECO:0000269|PubMed:18559506, ECO:0000269|PubMed:21980424}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9H6H4; IntAct: EBI-24677832; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-25283341; Score: 0.56
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
GO  GO:0016477;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPSAFSVSSFPVSIPAVLTQTDWTEPWLMGLATFHALCVLLTCLSSRSYRLQIGHFLCLVILVYCAEYINEAAAMNWRLF
SQ  SKYQYFDSRGMFISIVFSAPLLVNAMIIVVMWVWKTLNVMTDLKNAQERRKEKKRRRKED
//
ID  Q3TUD9;
PN  Transmembrane protein 18;
GN  Tmem18;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q96B42}. Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q3TUD9;
DR  UNIPROT: Q8CID7;
DR  Pfam: PF14770;
DE  Function: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats. Cell migration modulator which enhances the glioma-specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC) (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
GO  GO:0016477;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSSAYSVRSFPVSIPAVIMETDWTEPWLLGLLAFHLLCLLLTCFSSQRYKLQIGHFLCLVVLVYSAEYINEVAAVNWRLF
SQ  SKYQYFDSRGMFISLVFSAPLLFNAMLIVIMWVRKTLTVMTDLKTLQEERKERRRRRKEE
//
ID  Q6DGF8;
PN  Transmembrane protein 18;
GN  Tmem18;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q96B42}. Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q6DGF8;
DR  Pfam: PF14770;
DE  Function: Transcription repressor. Sequence-specific ssDNA and dsDNA binding protein, with preference for GCT end CTG repeats (By similarity). Cell migration modulator which enhances the glioma- specific migration ability of neural stem cells (NSC) and neural precursor cells (NPC). {ECO:0000250, ECO:0000269|PubMed:18559506}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
GO  GO:0016477;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASPYSVRVFPVSIPAVIMETDWTEPWLLGLLAFHLLCLLLTCFSAQRYKLQIGHFLCLVVLVYCAEYINEVAAMNWRLF
SQ  AKYQYFDSRGMFISLVFSAPLLFNAMVIVIMWVRKTLTVMSDLKNLQERRKERKRRRKEE
//
ID  Q4V7N7;
PN  Transmembrane protein 18;
GN  tmem18;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q4V7N7;
DR  Pfam: PF14770;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEEPGVWSLLERAPIDWTEPWLIGLAAFHILCFIVTYISFKSYPLQICHFLLMVVLVSCAEYINEFAAMHWRAYSKQQY
SQ  FDSSGMFISLAFSAPLLCNTIIIVVHWVYKTLCVMTELKTLQQKRKESREKRKKKE
//
ID  Q28GF5;
PN  Transmembrane protein 18;
GN  tmem18;
OS  8364;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q96B42}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q28GF5;
DR  Pfam: PF14770;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEDPGLWTLLERAPIDWKEPWLIGLAVFHILCLIVTYVSFKSYPLQICHFLLMVVLVSCAEYINEFAAMHWRSYSKQQY
SQ  FDSSGMFISLAFSAPLLCNTIIIVVHWVYKTLCVMTELKTLQQKRKESREKRKKKE
//
ID  P57088;
PN  Transmembrane protein 33;
GN  TMEM33;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25612671, ECO:0000269|PubMed:26268696}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000269|PubMed:17081065}. Nucleus envelope {ECO:0000269|PubMed:25612671}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Co-localizes with RTN4 at the ER sheets. {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:25612671}.
DR  UNIPROT: P57088;
DR  UNIPROT: B3KSS8;
DR  UNIPROT: Q9H953;
DR  Pfam: PF03661;
DR  OMIM: 618515;
DR  DisGeNET: 55161;
DE  Function: Acts as a regulator of the tubular endoplasmic reticulum (ER) network by modulating intracellular calcium homeostasis. Mechanistically, stimulates PKD2 calcium-dependent activity (By similarity). Suppresses the RTN3/4-induced formation of the ER tubules (PubMed:25612671). Positively regulates PERK-mediated and IRE1-mediated unfolded protein response signaling (PubMed:26268696). Plays an essential role in VEGF-mediated release of Ca(2+) from ER stores during angiogenesis (PubMed:30760708). Also plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (PubMed:32614325). Participates in lipid metabolism by acting as a downstream effector of the pyruvate kinase/PKM. Forms a complex with RNF5 to facilitate polyubiquitination and subsequent degradation of SCAP on the ER membrane (PubMed:34487377). {ECO:0000250|UniProtKB:Q9CR67, ECO:0000269|PubMed:25612671, ECO:0000269|PubMed:26268696, ECO:0000269|PubMed:30760708, ECO:0000269|PubMed:32614325, ECO:0000269|PubMed:34487377}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20626314; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-8770853; Score: 0.35
DE  Interaction: P0C6X6; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: P0DTC1; IntAct: EBI-25762396; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-25509566; Score: 0.35
DE  Interaction: Q15714; IntAct: EBI-1059832; Score: 0.00
DE  Interaction: Q9HAW0; IntAct: EBI-1061695; Score: 0.00
DE  Interaction: O75365; IntAct: EBI-1062314; Score: 0.00
DE  Interaction: Q15008; IntAct: EBI-1062802; Score: 0.00
DE  Interaction: Q9UET6; IntAct: EBI-1066786; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-1067201; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1074859; Score: 0.00
DE  Interaction: P11171; IntAct: EBI-1075237; Score: 0.00
DE  Interaction: P62140; IntAct: EBI-1076210; Score: 0.00
DE  Interaction: Q9Y5J5; IntAct: EBI-1078931; Score: 0.00
DE  Interaction: Q99608; IntAct: EBI-1082682; Score: 0.00
DE  Interaction: Q9P1U1; IntAct: EBI-1082984; Score: 0.00
DE  Interaction: Q9BUV8; IntAct: EBI-1086106; Score: 0.00
DE  Interaction: P48039; IntAct: EBI-1188258; Score: 0.66
DE  Interaction: Q9UL18; IntAct: EBI-7641457; Score: 0.35
DE  Interaction: Q9UKV8; IntAct: EBI-7642406; Score: 0.35
DE  Interaction: O94966; IntAct: EBI-2511876; Score: 0.40
DE  Interaction: Q5NIP6; IntAct: EBI-2800309; Score: 0.00
DE  Interaction: Q8ZC32; IntAct: EBI-2852168; Score: 0.00
DE  Interaction: P62263; IntAct: EBI-3920366; Score: 0.37
DE  Interaction: O95758; IntAct: EBI-7851121; Score: 0.35
DE  Interaction: O00716; IntAct: EBI-7600105; Score: 0.35
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P06927; IntAct: EBI-11724813; Score: 0.35
DE  Interaction: Q9CR14; IntAct: EBI-11055950; Score: 0.35
DE  Interaction: Q99549; IntAct: EBI-11059482; Score: 0.35
DE  Interaction: O55143; IntAct: EBI-11062077; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q9WMX2; IntAct: EBI-11513187; Score: 0.35
DE  Interaction: Q99IB8; IntAct: EBI-11613941; Score: 0.35
DE  Interaction: Q96FB2; IntAct: EBI-24668856; Score: 0.56
DE  Interaction: Q8IVT5; IntAct: EBI-14035332; Score: 0.35
DE  Interaction: P03950; IntAct: EBI-16363282; Score: 0.35
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: Q71U36; IntAct: EBI-16800060; Score: 0.27
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P14404; IntAct: EBI-21026252; Score: 0.35
DE  Interaction: E9PS44; IntAct: EBI-21260385; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-21132308; Score: 0.35
DE  Interaction: P49768; IntAct: EBI-21132675; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.53
DE  Interaction: P17813; IntAct: EBI-22197897; Score: 0.35
DE  Interaction: P15498; IntAct: EBI-25372968; Score: 0.35
DE  Interaction: Q13164; IntAct: EBI-25374538; Score: 0.35
DE  Interaction: P49023; IntAct: EBI-25376663; Score: 0.35
DE  Interaction: P19419; IntAct: EBI-25378580; Score: 0.35
DE  Interaction: Q13153; IntAct: EBI-25379067; Score: 0.35
DE  Interaction: P04049; IntAct: EBI-25382473; Score: 0.35
DE  Interaction: Q13547; IntAct: EBI-25383649; Score: 0.35
DE  Interaction: P51636; IntAct: EBI-25383812; Score: 0.35
DE  Interaction: P15056; IntAct: EBI-25385067; Score: 0.35
DE  Interaction: Q99558; IntAct: EBI-25389292; Score: 0.35
DE  Interaction: P30086; IntAct: EBI-25392387; Score: 0.35
DE  Interaction: P61586; IntAct: EBI-25394264; Score: 0.35
DE  Interaction: Q6KAU7; IntAct: EBI-25408855; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P69479; IntAct: EBI-25568051; Score: 0.35
DE  Interaction: P0DTC3; IntAct: EBI-25510118; Score: 0.35
DE  Interaction: P0DTD8; IntAct: EBI-25510237; Score: 0.35
DE  Interaction: P0DTD3; IntAct: EBI-25510342; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: P35226; IntAct: EBI-27109494; Score: 0.35
DE  Interaction: O14874; IntAct: EBI-28930753; Score: 0.35
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: P42695; IntAct: EBI-28951349; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
DE  Interaction: Q96Q04; IntAct: EBI-32723651; Score: 0.27
DE  Interaction: Q05DH4; IntAct: EBI-34574576; Score: 0.27
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0042470;
GO  GO:0005635;
GO  GO:0071786;
GO  GO:0045087;
GO  GO:0061024;
GO  GO:1903896;
GO  GO:1903899;
GO  GO:1903371;
GO  GO:0034976;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADTTPNGPQGAGAVQFMMTNKLDTAMWLSRLFTVYCSALFVLPLLGLHEAASFYQRALLANALTSALRLHQRLPHFQLS
SQ  RAFLAQALLEDSCHYLLYSLIFVNSYPVTMSIFPVLLFSLLHAATYTKKVLDARGSNSLPLLRSVLDKLSANQQNILKFI
SQ  ACNEIFLMPATVFMLFSGQGSLLQPFIYYRFLTLRYSSRRNPYCRTLFNELRIVVEHIIMKPACPLFVRRLCLQSIAFIS
SQ  RLAPTVP
//
ID  Q9CR67;
PN  Transmembrane protein 33;
GN  Tmem33;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31048699}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P57088}. Nucleus envelope {ECO:0000250|UniProtKB:P57088}. Note=Co-localizes with RTN4 at the ER sheets. {ECO:0000250|UniProtKB:P57088}.
DR  UNIPROT: Q9CR67;
DR  UNIPROT: Q544Q3;
DR  UNIPROT: Q9D3M3;
DR  UNIPROT: Q9DAV4;
DR  Pfam: PF03661;
DE  Function: Acts as a regulator of the tubular endoplasmic reticulum (ER) network by modulating intracellular calcium homeostasis. Mechanistically, stimulates PKD2 calcium-dependent activity (PubMed:31048699). Suppresses the RTN3/4-induced formation of the ER tubules. Positively regulates PERK-mediated and IRE1-mediated unfolded protein response signaling. Plays an essential role in VEGF-mediated release of Ca(2+) from ER stores during angiogenesis. Also plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26. Participates in lipid metabolism by acting as a downstream effector of the pyruvate kinase/PKM. Forms a complex with RNF5 to facilitate polyubiquitination and subsequent degradation of SCAP on the ER membrane (By similarity). {ECO:0000250|UniProtKB:P57088, ECO:0000269|PubMed:31048699}.
DE  Reference Proteome: Yes;
DE  Interaction: Q3TBT3; IntAct: EBI-10729637; Score: 0.35
DE  Interaction: A0A0F6B1Q8; IntAct: EBI-27035518; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0042470;
GO  GO:0005635;
GO  GO:0071786;
GO  GO:0045087;
GO  GO:0061024;
GO  GO:1903896;
GO  GO:1903899;
GO  GO:1903371;
GO  GO:0034976;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADTTPNGPQGAGAVQFMMTNKLDTAMWLSRLFTVYCSALFVLPLLGLHEAASFYQRALLANALTSALRLHQRLPHFQLS
SQ  RAFLAQALLEDSCHYLLYSLIFVNSYPVTMSIFPVLLFSLLHAATYTKKVLDAKGSNSLPLLRSFLDKLSTNQQNILKFI
SQ  ACNEIFLMPATVFMLFSGQGSLLQPFIYYRFLTLRYSSRRNPYCRNLFNELRIVVEHIIMKPSCPLFVRRLCLQSIAFIS
SQ  RLAPTVA
//
ID  Q9Z142;
PN  Transmembrane protein 33;
GN  Tmem33;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P57088}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P57088}. Nucleus envelope {ECO:0000250|UniProtKB:P57088}. Note=Co-localizes with RTN4 at the ER sheets. {ECO:0000250|UniProtKB:P57088}.
DR  UNIPROT: Q9Z142;
DR  Pfam: PF03661;
DE  Function: Acts as a regulator of the tubular endoplasmic reticulum (ER) network by modulating intracellular calcium homeostasis. Mechanistically, stimulates PKD2 calcium-dependent activity (By similarity). Suppresses the RTN3/4-induced formation of the ER tubules. Positively regulates PERK-mediated and IRE1-mediated unfolded protein response signaling. Plays an essential role in VEGF-mediated release of Ca(2+) from ER stores during angiogenesis. Also plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26. Participates in lipid metabolism by acting as a downstream effector of the pyruvate kinase/PKM. Forms a complex with RNF5 to facilitate polyubiquitination and subsequent degradation of SCAP on the ER membrane (By similarity). {ECO:0000250|UniProtKB:P57088, ECO:0000250|UniProtKB:Q9CR67}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9EQU3; IntAct: EBI-9979662; Score: 0.35
DE  Interaction: P11362; IntAct: EBI-22243924; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0030176;
GO  GO:0042470;
GO  GO:0005635;
GO  GO:0071786;
GO  GO:0045087;
GO  GO:0061024;
GO  GO:1903896;
GO  GO:1903899;
GO  GO:1903371;
GO  GO:0034976;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADTTPNGPQGAGAVQFMMTNKLDTAMWLSRLFTVYCSALFVLPLLGLHEAASFYQRALLANALTSALRLHQRLPHFQLS
SQ  RAFLAQALLEDSCHYLLYSLIFVNSYPVTMSIFPVLLFSLLHAATYTKKVLDAKGSNSLPLLRSVLDKLSTNQQNILKFI
SQ  ACNEIFLMPATVFMLFSGQGSLLQPFIYYRFLTLRYSSRRNPYCRNLFNELRIVVEHIIMKPSCPLFVRRLCLQSIAFIS
SQ  RLAPTVA
//
ID  Q9BTV4;
PN  Transmembrane protein 43;
GN  TMEM43;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:32614325}. Nucleus inner membrane; Multi-pass membrane protein. Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9BTV4;
DR  UNIPROT: Q7L4N5;
DR  UNIPROT: Q8NC30;
DR  UNIPROT: Q96A63;
DR  UNIPROT: Q96F19;
DR  UNIPROT: Q96JX0;
DR  UNIPROT: Q9H076;
DR  Pfam: PF07787;
DR  OMIM: 604400;
DR  OMIM: 612048;
DR  OMIM: 614302;
DR  DisGeNET: 79188;
DE  Function: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (PubMed:32614325). In addition, functions as a critical signaling component in mediating NF-kappa-B activation by acting downstream of EGFR and upstream of CARD10 (PubMed:27991920). {ECO:0000250|UniProtKB:Q9DBS1, ECO:0000269|PubMed:27991920, ECO:0000269|PubMed:32614325}.
DE  Disease: Arrhythmogenic right ventricular dysplasia, familial, 5 (ARVD5) [MIM:604400]: A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias. {ECO:0000269|PubMed:18313022}. Note=The disease is caused by variants affecting the gene represented in this entry. Emery-Dreifuss muscular dystrophy 7, autosomal dominant (EDMD7) [MIM:614302]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:21391237}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P03246; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P0C6X6; IntAct: EBI-25762549; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-26495763; Score: 0.35
DE  Interaction: P50402; IntAct: EBI-22085077; Score: 0.54
DE  Interaction: Q3UBX0; IntAct: EBI-11055815; Score: 0.35
DE  Interaction: Q5JX71; IntAct: EBI-24641558; Score: 0.56
DE  Interaction: Q99IB8; IntAct: EBI-11599103; Score: 0.35
DE  Interaction: P37268; IntAct: EBI-735100; Score: 0.00
DE  Interaction: P13569; IntAct: EBI-1171566; Score: 0.35
DE  Interaction: P04578; IntAct: EBI-6176374; Score: 0.35
DE  Interaction: Q8IUQ4; IntAct: EBI-10298522; Score: 0.56
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P06927; IntAct: EBI-11724813; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: P35278; IntAct: EBI-11012136; Score: 0.35
DE  Interaction: Q8BFY9; IntAct: EBI-11018381; Score: 0.35
DE  Interaction: P62491; IntAct: EBI-11046571; Score: 0.35
DE  Interaction: P51149; IntAct: EBI-11050319; Score: 0.35
DE  Interaction: Q8R5L1; IntAct: EBI-11085290; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104527; Score: 0.35
DE  Interaction: Q9R0Q3; IntAct: EBI-11111571; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q8N4V1; IntAct: EBI-11130635; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q96HH9; IntAct: EBI-16433789; Score: 0.72
DE  Interaction: Q9H7V2; IntAct: EBI-24611312; Score: 0.56
DE  Interaction: Q9UHP3; IntAct: EBI-24629728; Score: 0.56
DE  Interaction: P11684; IntAct: EBI-24695423; Score: 0.56
DE  Interaction: Q14318; IntAct: EBI-23735226; Score: 0.56
DE  Interaction: Q3SXY8; IntAct: EBI-24736312; Score: 0.56
DE  Interaction: Q8N5K1; IntAct: EBI-24737449; Score: 0.56
DE  Interaction: P02671; IntAct: EBI-24748636; Score: 0.56
DE  Interaction: Q9Y5K3; IntAct: EBI-24771131; Score: 0.56
DE  Interaction: Q6Q788; IntAct: EBI-24797991; Score: 0.56
DE  Interaction: Q6PEW1; IntAct: EBI-24809350; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q9GZM5; IntAct: EBI-21509346; Score: 0.35
DE  Interaction: Q16799; IntAct: EBI-21515832; Score: 0.35
DE  Interaction: O75170; IntAct: EBI-21664775; Score: 0.35
DE  Interaction: Q8TCT7; IntAct: EBI-21710636; Score: 0.35
DE  Interaction: Q9Y6E2; IntAct: EBI-21714503; Score: 0.35
DE  Interaction: Q9NQC3; IntAct: EBI-21723500; Score: 0.35
DE  Interaction: Q7L1Q6; IntAct: EBI-21857187; Score: 0.35
DE  Interaction: Q969Z0; IntAct: EBI-21877137; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-21885185; Score: 0.40
DE  Interaction: P02647; IntAct: EBI-21899345; Score: 0.40
DE  Interaction: P05161; IntAct: EBI-16720078; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P49768; IntAct: EBI-21132675; Score: 0.35
DE  Interaction: P09613; IntAct: EBI-21497303; Score: 0.35
DE  Interaction: Q9BTV4; IntAct: EBI-22084975; Score: 0.40
DE  Interaction: Q9UH99; IntAct: EBI-22085077; Score: 0.43
DE  Interaction: Q15139; IntAct: EBI-25395029; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25607852; Score: 0.35
DE  Interaction: Q96CS3; IntAct: EBI-25770808; Score: 0.35
DE  Interaction: Q8NBM4; IntAct: EBI-25771384; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-25961988; Score: 0.56
DE  Interaction: K9N5R3; IntAct: EBI-26374533; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: Q13363; IntAct: EBI-27044482; Score: 0.35
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0005639;
GO  GO:0042802;
GO  GO:0043621;
GO  GO:0045087;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAANYSSTSTRREHVKVKTSSQPGFLERLSETSGGMFVGLMAFLLSFYLIFTNEGRALKTATSLAEGLSLVVSPDSIHSV
SQ  APENEGRLVHIIGALRTSKLLSDPNYGVHLPAVKLRRHVEMYQWVETEESREYTEDGQVKKETRYSYNTEWRSEIINSKN
SQ  FDREIGHKNPSAMAVESFMATAPFVQIGRFFLSSGLIDKVDNFKSLSLSKLEDPHVDIIRRGDFFYHSENPKYPEVGDLR
SQ  VSFSYAGLSGDDPDLGPAHVVTVIARQRGDQLVPFSTKSGDTLLLLHHGDFSAEEVFHRELRSNSMKTWGLRAAGWMAMF
SQ  MGLNLMTRILYTLVDWFPVFRDLVNIGLKAFAFCVATSLTLLTVAAGWLFYRPLWALLIAGLALVPILVARTRVPAKKLE
//
ID  Q9DBS1;
PN  Transmembrane protein 43;
GN  Tmem43;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BTV4}. Nucleus inner membrane {ECO:0000269|PubMed:18230648}; Multi-pass membrane protein. Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen. {ECO:0000269|PubMed:18230648}.
DR  UNIPROT: Q9DBS1;
DR  Pfam: PF07787;
DE  Function: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (PubMed:18230648). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26. In addition, functions as a critical signaling component in mediating NF- kappa-B activation by acting downstream of EGFR and upstream of CARD10 (By similarity). {ECO:0000250|UniProtKB:Q9BTV4, ECO:0000269|PubMed:18230648}.
DE  Reference Proteome: Yes;
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: Q8BP00; IntAct: EBI-4283417; Score: 0.35
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0005639;
GO  GO:0005637;
GO  GO:0042802;
GO  GO:0043621;
GO  GO:0045087;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAANYSSTSSRKEHVKVTSEPQPGFLERLSETSGGMFVGLMTFLLSFYLIFTNEGRALKTATSLAEGLSLVVSPDSIHSV
SQ  APENEGRLVHIIGALRTSKLLSDPNYGVHLPAVKLRRHVEMYQWVETEESSEYTEDGQVKKETKYSYNTEWRSEIVNSRN
SQ  FDREIGHKNPSAMAVESFTATAPFVQIGRFFLSAGLIDKIDNFKALSLAKLEDPHVDIIRRGDFFYHSENPKYPEVGDVR
SQ  VSFSYAGLSSDDPDLGPAHVVTVIARQRGDQLIPYSTKSGDTLLLLHHGDFSAEEVFRREQKSNSMKTWGLRAAGWMAMF
SQ  MGLNLMTRILYTLVDWFPVFRDLVNIGLKAFAFCVATSLTLLTVAAGWLFYRPLWAALIGCLALVPIIIARTRVPAKKLE
//
ID  Q5R9S8;
PN  Transmembrane protein 43;
GN  TMEM43;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BTV4}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9BTV4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BTV4}. Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5R9S8;
DR  Pfam: PF07787;
DE  Function: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (By similarity). In addition, functions as a critical signaling component in mediating NF-kappa-B activation by acting downstream of EGFR and upstream of CARD10 (By similarity). {ECO:0000250|UniProtKB:Q9BTV4}.
DE  Reference Proteome: Yes;
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0005794;
GO  GO:0005639;
GO  GO:0042802;
GO  GO:0043621;
GO  GO:0045087;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAANYSSTSTRREHVKVKTGSQPGFLERLSETWGGMFVGLMAFLLSFYLIFTNEGRALKTATSLAEGLSLVVSPDSIHSV
SQ  APENEGRLVHIIGALRTSKLLSDPNYGVHLPAVKLRRHVEMYQWVETEESREYTEDEQVKKETRYSYNTEWRSEIINSKN
SQ  FDREIGHKNPSAMAVESFTATAPFVQIGRFFLSSGLIDKVDNFKSLSLSKLEDPHVDIIRRGDFFYHSENPKYPEVGDLR
SQ  VSFSYAGLSGDDPDLGPAHVVTVIARQRGDQLVPFSTKSGDTLLLLHHGDFSAEEVFHRELRSNSMKTWGLRAAGWMAMF
SQ  MGLNLMTRILYTLVDWFPVFRDLVNIGLKAFAFCVATSLTLLTVAAGWLFYRPLWALLIAGLALVPIIVARTRVPAKKLE
//
ID  Q5XIP9;
PN  Transmembrane protein 43;
GN  Tmem43;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BTV4}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9BTV4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BTV4}. Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5XIP9;
DR  Pfam: PF07787;
DE  Function: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (By similarity). In addition, functions as a critical signaling component in mediating NF-kappa-B activation by acting downstream of EGFR and upstream of CARD10 (By similarity). {ECO:0000250|UniProtKB:Q9BTV4}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
DE  Interaction: Q969Q1; IntAct: EBI-21997483; Score: 0.35
GO  GO:0005788;
GO  GO:0005789;
GO  GO:0005639;
GO  GO:0005637;
GO  GO:0042802;
GO  GO:0043621;
GO  GO:0045087;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAANYSSTGSRKEHVKVTSDPQPGFLERLSETSGGMFVGLVTFLLSFYLIFTNEGRALKTANLLAEGLSLVVSPDSIHSV
SQ  APENEGRLVHIIGALRTSKLLSDPNYGVHLPAVKLRRHVEMYQWVETEESNEYTEDGQVKKETKYSYNTEWRSEIVSSKN
SQ  FDREIGHKNPSAMAVESFTATAPFVQIGRFFLSAGLIDKIDNFKPLSLAKLEDPHVDIIRRGDFFYHSENPKYPEVGDVR
SQ  VSFSYAGLSSDDPDLGPAHVVTVIARQRGDQLIPYSTKSGDTLLLLHHGDFSAEEVFRREQKSNSMKTWGLRAAGWMAMF
SQ  MGLNLMTRILYTLVDWFPVFRDLVNIGLKAFAFCVATSLTLLTVAAGWLFYRPLWAALLGCLALVPIIIARTRVPTKKLE
//
ID  Q2TBP5;
PN  Transmembrane protein 53;
GN  TMEM53;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q9D0Z3}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q2TBP5;
DR  Pfam: PF05705;
DE  Function: Ensures normal bone formation, through the negative regulation of bone morphogenetic protein (BMP) signaling in osteoblast lineage cells by blocking cytoplasm-nucleus translocation of phosphorylated SMAD1/5/9 proteins. {ECO:0000250|UniProtKB:Q6P2H8}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0030514;
GO  GO:0030279;
GO  GO:0045668;
GO  GO:0046822;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASAQLDYTIEIPDQPCRSQENSPDQGGKEAGTRLPLVILLGWGGCSDKNLAKYSAIYHKRGCIVIRYTAPWHMVFFSET
SQ  LGIPSLRVLAQKLLELLFDYEVEKEPLLFHVFSNAGVMLYRYVLELLQTHQRFCHLRVVGTIFDSGPGDSNLLGALRALA
SQ  VVLEHRPAALRLLLLVAFTLVAFLFHVLLAPLTALFHTHFYDRLLDAASRWPELYLYSRADEVVLARDVERMVEARLAHQ
SQ  VLVRSVDFVSSAHVSHLRDYPTYYTTLCINFMHSCVHCSGPCPPHLTSAPEINA
//
ID  Q6DHN0;
PN  Transmembrane protein 53;
GN  tmem53;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000250|UniProtKB:Q9D0Z3}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q6DHN0;
DR  Pfam: PF05705;
DE  Function: Ensures normal bone formation, through the negative regulation of bone morphogenetic protein (BMP) signaling in osteoblast lineage cells by blocking cytoplasm-nucleus translocation of phosphorylated SMAD proteins. {ECO:0000250|UniProtKB:Q9D0Z3}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0030514;
GO  GO:0030279;
GO  GO:0045668;
GO  GO:0046822;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MGDDDLDYNIVFSEALISEKHWRGSKEPVVILLGWAGSRDKHLAKYSSIYNEQGCTTLRYTAPLKTVFISESLGYKELRS
SQ  TAHKLLELLYDYEVENNPIFFHVFSNGGFMLYRYMVELLHSHKQFSTLCVVGTVVDSAPGSQNVVGALRALKTTLGPKVN
SQ  VLLQYFLLALFAVAVFLLRIVLYPLTKYFHRNHYDAMMEHPAPWPQMYLYSRADRVIRYRDVEKMVKGLQEKGLMVESFD
SQ  FITPAHVSLFRDCPEDYSNRCRTFLSHCMTTSEEILMKKHH
//
ID  Q6P2H8;
PN  Transmembrane protein 53;
GN  TMEM53;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:33824347}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q6P2H8;
DR  UNIPROT: B4DKG0;
DR  UNIPROT: Q5JPH2;
DR  UNIPROT: Q6IA07;
DR  UNIPROT: Q9H6E2;
DR  Pfam: PF05705;
DR  OMIM: 619722;
DR  OMIM: 619727;
DE  Function: Ensures normal bone formation, through the negative regulation of bone morphogenetic protein (BMP) signaling in osteoblast lineage cells by blocking cytoplasm-nucleus translocation of phosphorylated SMAD1/5/9 proteins. {ECO:0000269|PubMed:33824347}.
DE  Disease: Craniotubular dysplasia, Ikegawa type (CTDI) [MIM:619727]: An autosomal recessive, sclerosing bone disorder characterized by proportional or short-limbed short stature in association with macrocephaly, dolichocephaly, or prominent forehead. Radiography shows hyperostosis of the calvaria and skull base, with metadiaphyseal undermodeling of the long tubular bones and mild shortening and diaphyseal broadening of the short tubular bones. Affected individuals experience progressive vision loss in the first decade of life due to optic nerve compression, and deafness may develop in the second decade of life. {ECO:0000269|PubMed:33824347}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O60361; IntAct: EBI-21771891; Score: 0.40
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0005634;
GO  GO:0030514;
GO  GO:0030279;
GO  GO:0045668;
GO  GO:0046822;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASAELDYTIEIPDQPCWSQKNSPSPGGKEAETRQPVVILLGWGGCKDKNLAKYSAIYHKRGCIVIRYTAPWHMVFFSES
SQ  LGIPSLRVLAQKLLELLFDYEIEKEPLLFHVFSNGGVMLYRYVLELLQTRRFCRLRVVGTIFDSAPGDSNLVGALRALAA
SQ  ILERRAAMLRLLLLVAFALVVVLFHVLLAPITALFHTHFYDRLQDAGSRWPELYLYSRADEVVLARDIERMVEARLARRV
SQ  LARSVDFVSSAHVSHLRDYPTYYTSLCVDFMRNCVRC
//
ID  Q9D0Z3;
PN  Transmembrane protein 53;
GN  Tmem53;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus outer membrane {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:20091084}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q9D0Z3;
DR  UNIPROT: A2AE66;
DR  UNIPROT: Q8VDW5;
DR  UNIPROT: Q9DAF0;
DR  Pfam: PF05705;
DE  Function: Negatively regulates bone morphogenetic protein (BMP) signaling in osteoblast lineage cells by blocking cytoplasm-nucleus translocation of phosphorylated SMAD1/5/9 proteins. {ECO:0000269|PubMed:33824347}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005640;
GO  GO:0030514;
GO  GO:0030279;
GO  GO:0045668;
GO  GO:0046822;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASAELDYSIEIPDQPCWSQKNRQGGKEAGKQQPVVILLGWGGCRDKNLAKYSAIYHKRGCIVIRYTAPWHMVFFSESLG
SQ  IPSLRVIAQKLLELLFDYEIEREPLLFHVFSNAGVMLYRYVLELLQTHQRFRHLHVVGTIFDSGPGDSNLIGALRALATI
SQ  LERRPAVLRLLLLAAFALVVILFHFLLAPFTALFHTHFYDRLQDSGSCWPELYLYSRADKVVSARDVERMVEARLAHQVM
SQ  VRGVDFVSSAHVSHLRDYPTYYTSLCVDFMHNCVQC
//
ID  Q9H1E5;
PN  Thioredoxin-related transmembrane protein 4;
GN  TMX4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C0L0}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: Q9H1E5;
DR  UNIPROT: Q8N4P7;
DR  UNIPROT: Q8NCC1;
DR  UNIPROT: Q9UJA1;
DR  UNIPROT: Q9ULQ8;
DR  Pfam: PF00085;
DR  PROSITE: PS00194;
DR  PROSITE: PS51352;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P10588; IntAct: EBI-2685893; Score: 0.00
DE  Interaction: P27824; IntAct: EBI-7504614; Score: 0.35
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q9UHP7; IntAct: EBI-21517465; Score: 0.35
DE  Interaction: Q8IZF4; IntAct: EBI-21536448; Score: 0.35
DE  Interaction: Q7KYR7; IntAct: EBI-21541130; Score: 0.35
DE  Interaction: Q8TDD5; IntAct: EBI-21589012; Score: 0.35
DE  Interaction: Q9NV96; IntAct: EBI-21590639; Score: 0.35
DE  Interaction: Q8N6K0; IntAct: EBI-21599984; Score: 0.35
DE  Interaction: Q8N6G5; IntAct: EBI-21622328; Score: 0.35
DE  Interaction: Q6EMK4; IntAct: EBI-21651359; Score: 0.35
DE  Interaction: A2RU67; IntAct: EBI-21694732; Score: 0.35
DE  Interaction: Q6UWB1; IntAct: EBI-21703330; Score: 0.35
DE  Interaction: P55290; IntAct: EBI-21736384; Score: 0.35
DE  Interaction: Q401N2; IntAct: EBI-21749859; Score: 0.35
DE  Interaction: P46098; IntAct: EBI-21749232; Score: 0.35
DE  Interaction: P54709; IntAct: EBI-21772941; Score: 0.35
DE  Interaction: Q9UN42; IntAct: EBI-21789423; Score: 0.35
DE  Interaction: O14944; IntAct: EBI-21838629; Score: 0.35
DE  Interaction: Q969P0; IntAct: EBI-21856955; Score: 0.35
DE  Interaction: P28845; IntAct: EBI-21874900; Score: 0.35
DE  Interaction: Q8TDX6; IntAct: EBI-21888284; Score: 0.35
DE  Interaction: Q01113; IntAct: EBI-21891955; Score: 0.35
DE  Interaction: Q9BY14; IntAct: EBI-25504841; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0015036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGGRCGPQLTALLAAWIAAVAATAGPEEAALPPEQSRVQPMTASNWTLVMEGEWMLKFYAPWCPSCQQTDSEWEAFAKN
SQ  GEILQISVGKVDVIQEPGLSGRFFVTTLPAFFHAKDGIFRRYRGPGIFEDLQNYILEKKWQSVEPLTGWKSPASLTMSGM
SQ  AGLFSISGKIWHLHNYFTVTLGIPAWCSYVFFVIATLVFGLFMGLVLVVISECFYVPLPRHLSERSEQNRRSEEAHRAEQ
SQ  LQDAEEEKDDSNEEENKDSLVDDEEEKEDLGDEDEAEEEEEEDNLAAGVDEERSEANDQGPPGEDGVTREEVEPEEAEEG
SQ  ISEQPCPADTEVVEDSLRQRKSQHADKGL
//
ID  Q8C0L0;
PN  Thioredoxin-related transmembrane protein 4;
GN  Tmx4;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:31142202}; Single-pass type I membrane protein {ECO:0000255}.
DR  UNIPROT: Q8C0L0;
DR  UNIPROT: Q3UHC6;
DR  UNIPROT: Q6ZPW7;
DR  UNIPROT: Q80X49;
DR  Pfam: PF00085;
DR  PROSITE: PS00194;
DR  PROSITE: PS51352;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0015036;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTGGFCVPVLLAAWLAAAAAEGLEQAALPAEESRVQPMTASNWTLVMEGEWMLKFYAPWCPSCQQTDSEWETFAKNGETL
SQ  QISVGKVDVIQEPGLSGRFFVTTLPAFFHAKDGIFRRYRGPGIYEDLQNYILEKKWQSVEPLTGWKSPASLTMSGMAGLF
SQ  SISGKIWHLHNYFTVTLGIPAWCSYVFFVIATLVFGLFMGLILVVISECFCVPLPRASSERCEQEQSTGEAQGAEQLQDA
SQ  EEEKDDSNEEENKDSLVDDEEEKEDIGDEDEGEEDEEEDNLAGIMAEERSDTNERAVVKEGSVSPKEDGAHPADTQDVVE
SQ  DALRQRKSQNANKGS
//
ID  O95271;
PN  Poly [ADP-ribose] polymerase tankyrase-1;
GN  TNKS;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10523501, ECO:0000269|PubMed:21799911, ECO:0000269|PubMed:22864114}. Golgi apparatus membrane {ECO:0000269|PubMed:22864114}; Peripheral membrane protein {ECO:0000269|PubMed:22864114}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10523501, ECO:0000269|PubMed:21799911}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10523501}. Chromosome, telomere {ECO:0000305|PubMed:9822378}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16076287}. Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles (PubMed:22864114). A minor proportion is also found at nuclear pore complexes and around the pericentriolar matrix of mitotic centromeres (PubMed:10523501). During interphase, a small fraction of TNKS is found in the nucleus, associated with TERF1 (PubMed:12768206). Localizes to spindle poles at mitosis onset via interaction with NUMA1 (PubMed:12080061). {ECO:0000269|PubMed:10523501, ECO:0000269|PubMed:12080061, ECO:0000269|PubMed:12768206, ECO:0000269|PubMed:22864114}.
DR  UNIPROT: O95271;
DR  UNIPROT: O95272;
DR  UNIPROT: Q4G0F2;
DR  UNIPROT: Q59FX0;
DR  PDB: 2RF5;
DR  PDB: 3UDD;
DR  PDB: 3UH2;
DR  PDB: 3UH4;
DR  PDB: 4DVI;
DR  PDB: 4I9I;
DR  PDB: 4K4E;
DR  PDB: 4K4F;
DR  PDB: 4KRS;
DR  PDB: 4LI6;
DR  PDB: 4LI7;
DR  PDB: 4LI8;
DR  PDB: 4MSG;
DR  PDB: 4MSK;
DR  PDB: 4MT9;
DR  PDB: 4N3R;
DR  PDB: 4N4V;
DR  PDB: 4OA7;
DR  PDB: 4TOR;
DR  PDB: 4TOS;
DR  PDB: 4U6A;
DR  PDB: 4UUH;
DR  PDB: 4UW1;
DR  PDB: 4W5S;
DR  PDB: 4W6E;
DR  PDB: 5EBT;
DR  PDB: 5ECE;
DR  PDB: 5ETY;
DR  PDB: 5GP7;
DR  PDB: 5JHQ;
DR  PDB: 5JTI;
DR  PDB: 5JU5;
DR  PDB: 5KNI;
DR  PDB: 6QXU;
DR  PDB: 6URQ;
DR  PDB: 7KKM;
DR  PDB: 7KKN;
DR  PDB: 7KKO;
DR  PDB: 7KKP;
DR  PDB: 7KKQ;
DR  Pfam: PF00023;
DR  Pfam: PF12796;
DR  Pfam: PF13606;
DR  Pfam: PF13637;
DR  Pfam: PF13857;
DR  Pfam: PF00644;
DR  Pfam: PF07647;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS51059;
DR  PROSITE: PS50105;
DR  OMIM: 603303;
DR  DisGeNET: 8658;
DE  Function: Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking (PubMed:10988299, PubMed:11739745, PubMed:16076287, PubMed:19759537, PubMed:21478859, PubMed:22864114, PubMed:23622245, PubMed:25043379). Acts as an activator of the Wnt signaling pathway by mediating poly- ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation (PubMed:19759537, PubMed:21478859). Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination (PubMed:21478859). Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length (PubMed:11739745). Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI (PubMed:22864114). May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles (PubMed:10988299). May be involved in spindle pole assembly through PARsylation of NUMA1 (PubMed:16076287). Stimulates 26S proteasome activity (PubMed:23622245). {ECO:0000269|PubMed:10988299, ECO:0000269|PubMed:11739745, ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859, ECO:0000269|PubMed:22864114, ECO:0000269|PubMed:23622245, ECO:0000269|PubMed:25043379}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NRI5; IntAct: EBI-1106475; Score: 0.00
DE  Interaction: O60239; IntAct: EBI-1106480; Score: 0.00
DE  Interaction: Q96RU3; IntAct: EBI-1111242; Score: 0.60
DE  Interaction: Q9NWV8; IntAct: EBI-2514464; Score: 0.56
DE  Interaction: A0A5P8YFM9; IntAct: EBI-2841120; Score: 0.00
DE  Interaction: P54274; IntAct: EBI-8146932; Score: 0.71
DE  Interaction: O95271; IntAct: EBI-8152907; Score: 0.40
DE  Interaction: Q9NWT6; IntAct: EBI-8565753; Score: 0.78
DE  Interaction: Q9Y2T1; IntAct: EBI-4400023; Score: 0.35
DE  Interaction: O35625; IntAct: EBI-4400085; Score: 0.58
DE  Interaction: O15084; IntAct: EBI-5653887; Score: 0.00
DE  Interaction: Q06649; IntAct: EBI-5328405; Score: 0.40
DE  Interaction: Q9HC77; IntAct: EBI-7924713; Score: 0.46
DE  Interaction: O43303; IntAct: EBI-7925293; Score: 0.27
DE  Interaction: P34969; IntAct: EBI-9027817; Score: 0.35
DE  Interaction: P62826; IntAct: EBI-9692184; Score: 0.40
DE  Interaction: O95235; IntAct: EBI-11007956; Score: 0.35
DE  Interaction: P80314; IntAct: EBI-11019324; Score: 0.35
DE  Interaction: Q3UES3; IntAct: EBI-11025889; Score: 0.35
DE  Interaction: O75367; IntAct: EBI-11506883; Score: 0.52
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: O00560; IntAct: EBI-24280426; Score: 0.56
DE  Interaction: Q9Y530; IntAct: EBI-24310113; Score: 0.56
DE  Interaction: P56279; IntAct: EBI-24345984; Score: 0.56
DE  Interaction: Q7L775; IntAct: EBI-25257538; Score: 0.56
DE  Interaction: Q9NX46; IntAct: EBI-24383999; Score: 0.56
DE  Interaction: Q8TF42; IntAct: EBI-24458289; Score: 0.56
DE  Interaction: A4D1S0; IntAct: EBI-21511461; Score: 0.35
DE  Interaction: Q96CW1; IntAct: EBI-21520588; Score: 0.35
DE  Interaction: O60232; IntAct: EBI-21543889; Score: 0.35
DE  Interaction: Q96A37; IntAct: EBI-21627270; Score: 0.35
DE  Interaction: Q9H201; IntAct: EBI-21644009; Score: 0.35
DE  Interaction: Q5SW79; IntAct: EBI-21644990; Score: 0.35
DE  Interaction: Q9UPT6; IntAct: EBI-21663692; Score: 0.35
DE  Interaction: Q07954; IntAct: EBI-21684279; Score: 0.35
DE  Interaction: Q6P1L5; IntAct: EBI-21690977; Score: 0.35
DE  Interaction: Q7L8J4; IntAct: EBI-21713418; Score: 0.35
DE  Interaction: Q8N6W0; IntAct: EBI-21727590; Score: 0.35
DE  Interaction: Q2T9K0; IntAct: EBI-21768445; Score: 0.35
DE  Interaction: Q9BS91; IntAct: EBI-21804617; Score: 0.59
DE  Interaction: Q9H2G9; IntAct: EBI-21813197; Score: 0.59
DE  Interaction: Q9BSI4; IntAct: EBI-21813154; Score: 0.35
DE  Interaction: Q86WJ1; IntAct: EBI-21813081; Score: 0.35
DE  Interaction: O75298; IntAct: EBI-21813019; Score: 0.35
DE  Interaction: O60547; IntAct: EBI-21813000; Score: 0.35
DE  Interaction: Q9NTX7; IntAct: EBI-16124474; Score: 0.73
DE  Interaction: Q3KP66; IntAct: EBI-20715953; Score: 0.59
DE  Interaction: P12956; IntAct: EBI-20904600; Score: 0.40
DE  Interaction: P21709; IntAct: EBI-21390848; Score: 0.00
DE  Interaction: Q8TER5; IntAct: EBI-25410884; Score: 0.35
DE  Interaction: Q9C0C2; IntAct: EBI-28963818; Score: 0.40
DE  Interaction: Q9UIQ6; IntAct: EBI-28963830; Score: 0.40
DE  Interaction: Q14980; IntAct: EBI-28964088; Score: 0.61
DE  Interaction: Q16281; IntAct: EBI-30838012; Score: 0.44
DE  Interaction: Q15019; IntAct: EBI-30837990; Score: 0.44
DE  Interaction: Q14CM0; IntAct: EBI-30837979; Score: 0.44
DE  Interaction: Q14764; IntAct: EBI-30837957; Score: 0.44
DE  Interaction: Q14689; IntAct: EBI-30837946; Score: 0.44
DE  Interaction: Q14574; IntAct: EBI-30837935; Score: 0.44
DE  Interaction: Q14249; IntAct: EBI-30837924; Score: 0.44
DE  Interaction: Q13813; IntAct: EBI-30837913; Score: 0.44
DE  Interaction: Q13698; IntAct: EBI-30837902; Score: 0.44
DE  Interaction: Q13367; IntAct: EBI-30837891; Score: 0.44
DE  Interaction: Q13111; IntAct: EBI-30837880; Score: 0.44
DE  Interaction: Q12802; IntAct: EBI-30837869; Score: 0.44
DE  Interaction: Q03468; IntAct: EBI-30837858; Score: 0.44
DE  Interaction: P78314; IntAct: EBI-30837847; Score: 0.44
DE  Interaction: P62955; IntAct: EBI-30837836; Score: 0.44
DE  Interaction: P58512; IntAct: EBI-30837825; Score: 0.44
DE  Interaction: P52272; IntAct: EBI-30837804; Score: 0.44
DE  Interaction: P51946; IntAct: EBI-30837771; Score: 0.44
DE  Interaction: P36915; IntAct: EBI-30837760; Score: 0.44
DE  Interaction: P31271; IntAct: EBI-30837749; Score: 0.44
DE  Interaction: P0DP91; IntAct: EBI-30837738; Score: 0.44
DE  Interaction: P0DP72; IntAct: EBI-30837727; Score: 0.44
DE  Interaction: P03923; IntAct: EBI-30837716; Score: 0.44
DE  Interaction: O95819; IntAct: EBI-30837705; Score: 0.44
DE  Interaction: O75038; IntAct: EBI-30837694; Score: 0.44
DE  Interaction: O15069; IntAct: EBI-30837683; Score: 0.44
DE  Interaction: O00763; IntAct: EBI-30837672; Score: 0.44
DE  Interaction: O00555; IntAct: EBI-30837661; Score: 0.44
DE  Interaction: C9JE40; IntAct: EBI-30837650; Score: 0.44
DE  Interaction: Q15742; IntAct: EBI-30838001; Score: 0.44
DE  Interaction: Q2KJY2; IntAct: EBI-30838160; Score: 0.44
DE  Interaction: Q9Y2J4; IntAct: EBI-30838700; Score: 0.44
DE  Interaction: Q9Y2I8; IntAct: EBI-30838689; Score: 0.44
DE  Interaction: Q9Y2B5; IntAct: EBI-30838678; Score: 0.44
DE  Interaction: Q9ULI4; IntAct: EBI-30838667; Score: 0.44
DE  Interaction: Q9UJM3; IntAct: EBI-30838656; Score: 0.44
DE  Interaction: Q9UGK3; IntAct: EBI-30838645; Score: 0.44
DE  Interaction: Q9P2M7; IntAct: EBI-30838634; Score: 0.44
DE  Interaction: Q9P281; IntAct: EBI-30838623; Score: 0.44
DE  Interaction: Q9NX62; IntAct: EBI-30838612; Score: 0.44
DE  Interaction: Q9NSK0; IntAct: EBI-30838601; Score: 0.44
DE  Interaction: Q9NRP7; IntAct: EBI-30838590; Score: 0.44
DE  Interaction: Q9H2V7; IntAct: EBI-30838579; Score: 0.44
DE  Interaction: Q9BXF3; IntAct: EBI-30838557; Score: 0.44
DE  Interaction: Q9BWF2; IntAct: EBI-30838546; Score: 0.44
DE  Interaction: Q9BT40; IntAct: EBI-30838535; Score: 0.44
DE  Interaction: Q9BQE5; IntAct: EBI-30838513; Score: 0.44
DE  Interaction: Q96T23; IntAct: EBI-30838502; Score: 0.44
DE  Interaction: Q96J42; IntAct: EBI-30838491; Score: 0.44
DE  Interaction: Q96HP0; IntAct: EBI-30838480; Score: 0.44
DE  Interaction: Q96EV8; IntAct: EBI-30838469; Score: 0.44
DE  Interaction: Q96C34; IntAct: EBI-30838458; Score: 0.44
DE  Interaction: Q96B70; IntAct: EBI-30838430; Score: 0.44
DE  Interaction: Q96A61; IntAct: EBI-30838419; Score: 0.44
DE  Interaction: Q969S9; IntAct: EBI-30838408; Score: 0.44
DE  Interaction: Q8WZ42; IntAct: EBI-30838397; Score: 0.44
DE  Interaction: Q8WY91; IntAct: EBI-30838386; Score: 0.44
DE  Interaction: Q8NCU7; IntAct: EBI-30838375; Score: 0.44
DE  Interaction: Q8N831; IntAct: EBI-30838364; Score: 0.44
DE  Interaction: Q8IYB4; IntAct: EBI-30838353; Score: 0.44
DE  Interaction: Q8IY63; IntAct: EBI-30838342; Score: 0.44
DE  Interaction: Q8IWJ2; IntAct: EBI-30838331; Score: 0.44
DE  Interaction: Q8IVH2; IntAct: EBI-30838320; Score: 0.44
DE  Interaction: Q86UD5; IntAct: EBI-30838309; Score: 0.44
DE  Interaction: Q86SG4; IntAct: EBI-30838298; Score: 0.44
DE  Interaction: Q76N32; IntAct: EBI-30838287; Score: 0.44
DE  Interaction: Q6ZRV2; IntAct: EBI-30838276; Score: 0.44
DE  Interaction: Q6UB35; IntAct: EBI-30838265; Score: 0.44
DE  Interaction: Q5VYV7; IntAct: EBI-30838254; Score: 0.44
DE  Interaction: Q5T7P6; IntAct: EBI-30838243; Score: 0.44
DE  Interaction: Q5T4T6; IntAct: EBI-30838226; Score: 0.44
DE  Interaction: Q5JTH9; IntAct: EBI-30838215; Score: 0.44
DE  Interaction: Q58A45; IntAct: EBI-30838204; Score: 0.44
DE  Interaction: Q53ET0; IntAct: EBI-30838193; Score: 0.44
DE  Interaction: Q3KQZ1; IntAct: EBI-30838182; Score: 0.44
DE  Interaction: P14652; IntAct: EBI-28997321; Score: 0.35
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0097431;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0000242;
GO  GO:0042393;
GO  GO:0003950;
GO  GO:1990404;
GO  GO:0008270;
GO  GO:0051301;
GO  GO:0007052;
GO  GO:0051028;
GO  GO:1904908;
GO  GO:1904357;
GO  GO:1904743;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0090263;
GO  GO:0051973;
GO  GO:1904355;
GO  GO:0032212;
GO  GO:0045944;
GO  GO:0006471;
GO  GO:0070213;
GO  GO:0070198;
GO  GO:0070212;
GO  GO:0000209;
GO  GO:0015031;
GO  GO:0032210;
GO  GO:0051225;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:22864114};
SQ  MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPRHGLALPEGDGSRDPPDRPRS
SQ  PDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNPAGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVS
SQ  STAPLGPGAAGPGTGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGA
SQ  NVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALD
SQ  LADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDK
SQ  GGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPEL
SQ  RERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFMT
SQ  PLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILS
SQ  ESTPIRTSDVDYRLLEASKAGDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVP
SQ  LHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDL
SQ  LRGDAALLDAAKKGCLARVQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASY
SQ  GHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEA
SQ  LPTCFKPQATVVSASLISPASTPSCLSAASSIDNLTGPLAELAVGGASNAGDGAAGTERKEGEVAGLDMNISQFLKSLGL
SQ  EHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQS
SQ  VEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDER
SQ  HAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSFLQFSTMKMAHAPPGHHSVIG
SQ  RPSVNGLAYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTATAAEQKT
//
ID  Q6PFX9;
PN  Poly [ADP-ribose] polymerase tankyrase-1;
GN  Tnks;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O95271}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O95271}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95271}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O95271}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O95271}. Chromosome, telomere {ECO:0000250|UniProtKB:O95271}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O95271}. Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles. A minor proportion is also found at nuclear pore complexes and around the pericentriolar matrix of mitotic centromeres. During interphase, a small fraction of TNKS is found in the nucleus, associated with TERF1. Localizes to spindle poles at mitosis onset via interaction with NUMA1. {ECO:0000250|UniProtKB:O95271}.
DR  UNIPROT: Q6PFX9;
DR  UNIPROT: Q8BX62;
DR  PDB: 3UTM;
DR  PDB: 4N4T;
DR  PDB: 5HKP;
DR  PDB: 6CF6;
DR  Pfam: PF00023;
DR  Pfam: PF12796;
DR  Pfam: PF13606;
DR  Pfam: PF13637;
DR  Pfam: PF13857;
DR  Pfam: PF00644;
DR  Pfam: PF07647;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS51059;
DR  PROSITE: PS50105;
DE  Function: Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly- ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Stimulates 26S proteasome activity. {ECO:0000250|UniProtKB:O95271}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9C0C2; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q15018; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: E7ESK6; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q14980; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: O95714; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q9ULU4; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q99766; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q96A35; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q13200; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q9ULF5; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q9H2K2; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q8N1G0; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: O60232; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q6UWP8; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: O60239; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: O60547; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q8IY92; IntAct: EBI-11025790; Score: 0.35
DE  Interaction: Q9NTX7; IntAct: EBI-16124630; Score: 0.44
DE  Interaction: Q9EP53; IntAct: EBI-16734894; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26473140; Score: 0.35
DE  Interaction: P54274; IntAct: EBI-28965117; Score: 0.35
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0005815;
GO  GO:0097431;
GO  GO:0016604;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0042393;
GO  GO:0003950;
GO  GO:1990404;
GO  GO:0008270;
GO  GO:0051301;
GO  GO:0031670;
GO  GO:0051028;
GO  GO:1904908;
GO  GO:1904357;
GO  GO:1904743;
GO  GO:0018105;
GO  GO:0018107;
GO  GO:0090263;
GO  GO:0051973;
GO  GO:1904355;
GO  GO:0032212;
GO  GO:0045944;
GO  GO:0006471;
GO  GO:0070213;
GO  GO:0070198;
GO  GO:0070212;
GO  GO:0000209;
GO  GO:0015031;
GO  GO:0051225;
GO  GO:0016055;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O95271};
SQ  MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGPTPASPTAGGLAPFASPRHGLALPEGDGSRDPPDRPRS
SQ  PDPVDGAVCTVAAPAAVPAASAAVGVAPTPAGGGGGGGNNSASSASSPTSSSSSSPSSPGSSLAESPEAAGVGSTATLGA
SQ  GAAGLGPGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDD
SQ  GGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAK
SQ  AVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLH
SQ  NACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYE
SQ  FKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVAELLLRKGANVNEKNKDFMTPLHVAAE
SQ  RAHNDVMEVLHKHGAKMNALDSLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILSESTPMRT
SQ  SDVDYRLLEASKAGDLETVKQLCSPQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSY
SQ  GHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDLLRGDAAL
SQ  LDAAKKGCLARVQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAA
SQ  LLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEALPTCFKP
SQ  QATVVSASLISPASTPSCLSAASSIDNLTGPLTDLAVGGASNAGDGAAGAERKEGEVAGLDMNISQFLKSLGLEHLRDIF
SQ  ETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQS
SQ  TIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGM
SQ  FGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGL
SQ  AYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTATAAEQKT
//
ID  Q9H2S6;
PN  Tenomodulin;
GN  TNMD;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: [Isoform 1]: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Nucleus envelope. [Isoform 2]: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Nucleus envelope. [Isoform 3]: Cytoplasm.
DR  UNIPROT: Q9H2S6;
DR  UNIPROT: Q9HBX0;
DR  UNIPROT: Q9UJG0;
DR  Pfam: PF04089;
DR  PROSITE: PS50869;
DR  OMIM: 300459;
DR  DisGeNET: 64102;
DE  Function: May be an angiogenesis inhibitor.
DE  Reference Proteome: Yes;
DE  Interaction: O60238; IntAct: EBI-24287972; Score: 0.56
DE  Interaction: Q5JX71; IntAct: EBI-25282993; Score: 0.56
DE  Interaction: Q9BSE2; IntAct: EBI-10306117; Score: 0.67
DE  Interaction: Q12983; IntAct: EBI-24353573; Score: 0.56
DE  Interaction: Q9BXK5; IntAct: EBI-24511583; Score: 0.56
DE  Interaction: Q96A25; IntAct: EBI-24523325; Score: 0.56
DE  Interaction: Q6P531; IntAct: EBI-25265726; Score: 0.56
DE  Interaction: P12314; IntAct: EBI-24697785; Score: 0.56
DE  Interaction: Q9HB07; IntAct: EBI-24716245; Score: 0.56
DE  Interaction: Q3SXY8; IntAct: EBI-24727794; Score: 0.56
DE  Interaction: Q9UM44; IntAct: EBI-24767323; Score: 0.56
DE  Interaction: Q8N743; IntAct: EBI-23885527; Score: 0.56
DE  Interaction: P20138; IntAct: EBI-25280398; Score: 0.56
DE  Interaction: Q96BA8; IntAct: EBI-24571101; Score: 0.56
DE  Interaction: Q9NPE6; IntAct: EBI-24572530; Score: 0.56
DE  Interaction: Q86WK6; IntAct: EBI-25273385; Score: 0.56
DE  Interaction: P10412; IntAct: EBI-20930064; Score: 0.40
DE  Interaction: P27797; IntAct: EBI-25833963; Score: 0.56
DE  Interaction: P36957; IntAct: EBI-25841424; Score: 0.56
DE  Interaction: Q8TDX7; IntAct: EBI-25929928; Score: 0.56
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0001886;
GO  GO:0016525;
GO  GO:0001937;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKNPPENCEDCHILNAEAFKSKKICKSLKICGLVFGILALTLIVLFWGSKHFWPEVPKKAYDMEHTFYSNGEKKKIYME
SQ  IDPVTRTEIFRSGNGTDETLEVHDFKNGYTGIYFVGLQKCFIKTQIKVIPEFSEPEEEIDENEEITTTFFEQSVIWVPAE
SQ  KPIENRDFLKNSKILEICDNVTMYWINPTLISVSELQDFEEEGEDLHFPANEKKGIEQNEQWVVPQVKVEKTRHARQASE
SQ  EELPINDYTENGIEFDPMLDERGYCCIYCRRGNRYCRRVCEPLLGYYPYPYCYQGGRVICRVIMPCNWWVARMLGRV
//
ID  Q9EP64;
PN  Tenomodulin;
GN  Tnmd;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q9EP64;
DR  UNIPROT: Q8CET4;
DR  Pfam: PF04089;
DR  PROSITE: PS50869;
DE  Function: May be an angiogenesis inhibitor.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0001886;
GO  GO:0016525;
GO  GO:0001937;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKNPPENCEGCHILNAEALKSKKICKSLKICGLVFGILALTLIVLFWGSKHFWPEVSKKTYDMEHTFYSNGEKKKIYME
SQ  IDPITRTEIFRSGNGTDETLEVHDFKNGYTGIYFVGLQKCFIKTQIKVIPEFSEPEEEIDENEEITTTFFEQSVIWVPAE
SQ  KPIENRDFLKNSKILEICDNVTMYWINPTLIAVSELQDFEEDGEDLHFPTSEKKGIDQNEQWVVPQVKVEKTRHTRQASE
SQ  EDLPINDYTENGIEFDPMLDERGYCCIYCRRGNRYCRRVCEPLLGYYPYPYCYQGGRVICRVIMPCNWWVARMLGRV
//
ID  Q9ESC2;
PN  Tenomodulin;
GN  Tnmd;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q9ESC2;
DR  Pfam: PF04089;
DR  PROSITE: PS50869;
DE  Function: May be an angiogenesis inhibitor.
DE  Reference Proteome: Yes;
GO  GO:0009986;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0071773;
GO  GO:0001886;
GO  GO:0016525;
GO  GO:0001937;
GO  GO:0035990;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAKNPPENCEGCHILNAEALKSKKIRKSLKICGLVFGILALTLIVLFWGSKHFWPEVSKKTYGMEHTFYSNGEKKKISME
SQ  IDPITRTEIFRSGNGTDETLEVHDFKNGYTGIYFVGLQKCFIKTQIKVIPEFSEPEEEIDENEEITTTFFEQSVIWVPAE
SQ  KPIENRDFLKNSKILEICDNVTMYWINPTLIAVSELQDFEEDGEDLHFPTSEKKGIDQNEQWVVPQVKVEKTRRTRQASE
SQ  EDLPVNDYTENGIEFDPMLDERGYCCIYCRRGNRYCRRVCEPLLGYYPYPYCYQGGRVICRVIMPCNWWVARMLGRV
//
ID  Q9Y5L0;
PN  Transportin-3;
GN  TNPO3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:31192305, ECO:0000305|PubMed:10713112, ECO:0000305|PubMed:23543484}. Cytoplasm {ECO:0000269|PubMed:10713112}. Note=Localizes to the nuclear envelope and annulate lamellae, which consists in stacks of endoplasmic reticulum membranes containing a high density of nuclear pores. {ECO:0000269|PubMed:31192305}.
DR  UNIPROT: Q9Y5L0;
DR  UNIPROT: A4D1K9;
DR  UNIPROT: C9IZM0;
DR  UNIPROT: Q6NUM1;
DR  UNIPROT: Q96G71;
DR  UNIPROT: Q96GU9;
DR  UNIPROT: Q9Y3R2;
DR  PDB: 4C0O;
DR  PDB: 4C0P;
DR  PDB: 4C0Q;
DR  PDB: 4OL0;
DR  PDB: 6GX9;
DR  Pfam: PF08389;
DR  OMIM: 608423;
DR  OMIM: 609423;
DR  OMIM: 610032;
DR  DisGeNET: 23534;
DE  Function: Importin, which transports target proteins into the nucleus (PubMed:10366588, PubMed:10713112, PubMed:11517331, PubMed:12628928, PubMed:24449914). Specifically mediates the nuclear import of splicing factor serine/arginine (SR) proteins, such as RBM4, SFRS1 and SFRS2, by recognizing phosphorylated SR domains (PubMed:10366588, PubMed:10713112, PubMed:11517331, PubMed:12628928, PubMed:24449914). Also mediates the nuclear import of serine/arginine (SR) protein CPSF6, independently of CPSF6 phosphorylation (PubMed:30916345, PubMed:31465518). The nuclear import process is regulated by the small GTPase Ran that partitions between cytoplasm and nucleus in the predominantly GDP- and GTP-bound form, respectively (PubMed:23878195, PubMed:24449914). Importin associates with target cargo proteins in the cytoplasm, and the competitive binding of GTP-bound Ran induces the release of cargos in the nucleus (PubMed:23878195, PubMed:24449914). {ECO:0000269|PubMed:10366588, ECO:0000269|PubMed:10713112, ECO:0000269|PubMed:11517331, ECO:0000269|PubMed:12628928, ECO:0000269|PubMed:23878195, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:30916345, ECO:0000269|PubMed:31465518}. (Microbial infection) Involved in immunodeficiency virus (HIV-1) infection by importing the pre-integration complex (PIC) into the nucleus (PubMed:18722123, PubMed:21901095, PubMed:22398280, PubMed:29329553). Required for a nuclear maturation step of HIV-1 prior to integration (PubMed:21901095, PubMed:22398280). {ECO:0000269|PubMed:18722123, ECO:0000269|PubMed:21901095, ECO:0000269|PubMed:22398280, ECO:0000269|PubMed:29329553}.
DE  Disease: Muscular dystrophy, limb-girdle, autosomal dominant 2 (LGMDD2) [MIM:608423]: An autosomal dominant myopathy characterized by proximal muscle weakness primarily affecting the lower limbs, but also affecting the upper limbs in most patients. Affected individuals also have distal muscle weakness of the hands and lower leg muscles. The disease has generally a benign clinical course but some individuals with childhood or juvenile onset manifest severe widespread myopathy, leading to wheelchair dependency and respiratory insufficiency. Muscle biopsy shows dystrophic changes with abnormal nuclei, rimmed vacuoles, and filamentous inclusions. {ECO:0000269|PubMed:23543484, ECO:0000269|PubMed:23667635, ECO:0000269|PubMed:31071488, ECO:0000269|PubMed:31192305, ECO:0000269|PubMed:31465518}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O43633; IntAct: EBI-11512013; Score: 0.37
DE  Interaction: P01112; IntAct: EBI-34580918; Score: 0.35
DE  Interaction: Q9HAU4; IntAct: EBI-7236978; Score: 0.37
DE  Interaction: O75365; IntAct: EBI-1059888; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-1068947; Score: 0.00
DE  Interaction: Q9HC98; IntAct: EBI-1069111; Score: 0.00
DE  Interaction: Q9HAW0; IntAct: EBI-1073318; Score: 0.00
DE  Interaction: Q9BUV8; IntAct: EBI-1074871; Score: 0.00
DE  Interaction: Q9Y5J5; IntAct: EBI-1084504; Score: 0.00
DE  Interaction: Q16763; IntAct: EBI-2339830; Score: 0.37
DE  Interaction: O94966; IntAct: EBI-2511876; Score: 0.40
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: P49760; IntAct: EBI-6380324; Score: 0.53
DE  Interaction: P49761; IntAct: EBI-6380381; Score: 0.53
DE  Interaction: P04585; IntAct: EBI-10108275; Score: 0.64
DE  Interaction: Q9Y5L0; IntAct: EBI-10108384; Score: 0.62
DE  Interaction: Q8CAQ8; IntAct: EBI-11096643; Score: 0.35
DE  Interaction: G3X9E8; IntAct: EBI-11097478; Score: 0.35
DE  Interaction: Q9R1T4; IntAct: EBI-11117390; Score: 0.35
DE  Interaction: P09450; IntAct: EBI-11127973; Score: 0.35
DE  Interaction: P52333; IntAct: EBI-11134573; Score: 0.35
DE  Interaction: Q96M32; IntAct: EBI-11135675; Score: 0.35
DE  Interaction: Q9NS91; IntAct: EBI-11143700; Score: 0.35
DE  Interaction: Q9Y3E7; IntAct: EBI-11511244; Score: 0.37
DE  Interaction: Q7LBR1; IntAct: EBI-11511920; Score: 0.37
DE  Interaction: Q9BY43; IntAct: EBI-11512373; Score: 0.37
DE  Interaction: Q96FZ7; IntAct: EBI-11512605; Score: 0.37
DE  Interaction: P27105; IntAct: EBI-12452286; Score: 0.51
DE  Interaction: Q13557; IntAct: EBI-24301011; Score: 0.56
DE  Interaction: P15531; IntAct: EBI-24301547; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24342461; Score: 0.56
DE  Interaction: Q13555; IntAct: EBI-24486588; Score: 0.56
DE  Interaction: Q13554; IntAct: EBI-24493263; Score: 0.56
DE  Interaction: Q8NDH6; IntAct: EBI-23696555; Score: 0.56
DE  Interaction: Q16385; IntAct: EBI-23713173; Score: 0.56
DE  Interaction: Q16740; IntAct: EBI-23774712; Score: 0.56
DE  Interaction: Q8WVI7; IntAct: EBI-23791400; Score: 0.56
DE  Interaction: Q13867; IntAct: EBI-24376220; Score: 0.56
DE  Interaction: O95678; IntAct: EBI-24415200; Score: 0.56
DE  Interaction: P30793; IntAct: EBI-24424243; Score: 0.56
DE  Interaction: P60410; IntAct: EBI-24633299; Score: 0.56
DE  Interaction: O75521; IntAct: EBI-25144107; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: F5HFG5; IntAct: EBI-14063444; Score: 0.35
DE  Interaction: P32970; IntAct: EBI-21512742; Score: 0.35
DE  Interaction: P28335; IntAct: EBI-21534882; Score: 0.35
DE  Interaction: P41587; IntAct: EBI-21567910; Score: 0.35
DE  Interaction: Q8N7X8; IntAct: EBI-21585341; Score: 0.35
DE  Interaction: Q9H813; IntAct: EBI-21593240; Score: 0.35
DE  Interaction: Q86VU5; IntAct: EBI-21596714; Score: 0.35
DE  Interaction: Q01814; IntAct: EBI-21599092; Score: 0.35
DE  Interaction: P43115; IntAct: EBI-21607127; Score: 0.35
DE  Interaction: O95274; IntAct: EBI-21607810; Score: 0.35
DE  Interaction: Q9H244; IntAct: EBI-21614520; Score: 0.35
DE  Interaction: Q6EMK4; IntAct: EBI-21651359; Score: 0.35
DE  Interaction: O75695; IntAct: EBI-21661543; Score: 0.35
DE  Interaction: P55899; IntAct: EBI-21669509; Score: 0.35
DE  Interaction: O60939; IntAct: EBI-21671922; Score: 0.35
DE  Interaction: P35372; IntAct: EBI-21672468; Score: 0.35
DE  Interaction: Q93086; IntAct: EBI-21682229; Score: 0.35
DE  Interaction: Q29983; IntAct: EBI-21700267; Score: 0.35
DE  Interaction: Q9ULW2; IntAct: EBI-21704037; Score: 0.35
DE  Interaction: P19438; IntAct: EBI-21717945; Score: 0.35
DE  Interaction: Q6AZY7; IntAct: EBI-21722497; Score: 0.35
DE  Interaction: P50895; IntAct: EBI-21726862; Score: 0.35
DE  Interaction: Q9NQ29; IntAct: EBI-21728243; Score: 0.35
DE  Interaction: Q86XK7; IntAct: EBI-21739948; Score: 0.35
DE  Interaction: Q96IQ7; IntAct: EBI-21740303; Score: 0.35
DE  Interaction: Q9NZQ7; IntAct: EBI-21740460; Score: 0.35
DE  Interaction: Q8WVE6; IntAct: EBI-21754350; Score: 0.35
DE  Interaction: Q99571; IntAct: EBI-21765870; Score: 0.35
DE  Interaction: Q13190; IntAct: EBI-21790103; Score: 0.35
DE  Interaction: P15907; IntAct: EBI-21842845; Score: 0.35
DE  Interaction: Q9BUV0; IntAct: EBI-21881862; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: F5H1C8; IntAct: EBI-21264930; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: P09613; IntAct: EBI-21497303; Score: 0.35
DE  Interaction: P19739; IntAct: EBI-25685423; Score: 0.35
DE  Interaction: Q5EP34; IntAct: EBI-25772822; Score: 0.35
DE  Interaction: Q6PB30; IntAct: EBI-26354359; Score: 0.35
DE  Interaction: Q9Y5P2; IntAct: EBI-26354638; Score: 0.35
DE  Interaction: K9N5R3; IntAct: EBI-26374533; Score: 0.35
DE  Interaction: P48431; IntAct: EBI-26574478; Score: 0.35
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
GO  GO:0005642;
GO  GO:0005737;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0042802;
GO  GO:0061608;
GO  GO:0031267;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESCYFAAQTMKMKIQTSFYELPT
SQ  DSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLR
SQ  IGANRRTEIIEDLAFYSSTVVSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSN
SQ  LHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTELCETFLEKIVCTPGQGLGD
SQ  LRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEVIHGIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFR
SQ  MRVSDLVKDLIFLIGSMECFAQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVRLPETVHTAVRYT
SQ  SIELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNGLLEIARSLDSFLLSPEAAVG
SQ  LLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEPSNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQE
SQ  IWPVLSETLNKHRADNRIVERCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQG
SQ  LLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWAIASTTLDHRDANCSVMRFLR
SQ  DLIHTGVANDHEEDFELRKELIGQVMNQLGQQLVSQLLHTCCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLP
SQ  KETTVGAVTVTHKQLTDFHKQVTSAEECKQVCWALRDFTRLFR
//
ID  Q6P2B1;
PN  Transportin-3;
GN  Tnpo3;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000250|UniProtKB:Q9Y5L0}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y5L0}. Note=Localizes to the nuclear envelope and annulate lamellae, which consists in stacks of endoplasmic reticulum membranes containing a high density of nuclear pores. {ECO:0000250|UniProtKB:Q9Y5L0}.
DR  UNIPROT: Q6P2B1;
DR  UNIPROT: Q7TSL6;
DR  UNIPROT: Q8BKX4;
DR  UNIPROT: Q8BP42;
DR  Pfam: PF08389;
DE  Function: Importin, which transports target proteins into the nucleus. Specifically mediates the nuclear import of splicing factor serine/arginine (SR) proteins, such as RBM4, SFRS1 and SFRS2, by recognizing phosphorylated SR domains. Also mediates the nuclear import of serine/arginine (SR) protein CPSF6, independently of CPSF6 phosphorylation. The nuclear import process is regulated by the small GTPase Ran that partitions between cytoplasm and nucleus in the predominantly GDP- and GTP-bound form, respectively. Importin associates with target cargo proteins in the cytoplasm, and the competitive binding of GTP-bound Ran induces the release of cargos in the nucleus. {ECO:0000250|UniProtKB:Q9Y5L0}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9NRI5; IntAct: EBI-26612017; Score: 0.35
GO  GO:0005642;
GO  GO:0005737;
GO  GO:0043231;
GO  GO:0005635;
GO  GO:0042802;
GO  GO:0031267;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESCYFAAQTMKMKIQTSFYELPT
SQ  DSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLR
SQ  IGANRRTEIIEDLAFYSSTVVSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSN
SQ  LHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTELCETFLEKIVCTPGQGLGD
SQ  LRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEVIHSIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFR
SQ  MRVSDLVKDLIFLIGSMECFAQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVHLPETVHTAVRYT
SQ  SIELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNGLLEIAHSLDSFMLSPEAAVG
SQ  LLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEPSNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQE
SQ  IWPVLSETLNKHRADNRIVERCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQG
SQ  LLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWAIASTTLDHRDANSSVMRFLR
SQ  DLIHTGVANDHEEDFELRKELIGQVMSQLGQQLVSQLLHTCCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLP
SQ  KETTVGAVTVTHKQLTDFHKQVTSAEECKQVCWALRDFTRLFR
//
ID  Q55CQ7;
PN  Transportin;
GN  tnpo;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q55CQ7;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Functions in nuclear protein import via a substrate-importin alpha-beta transport complex that passes though the nuclear pore complexes (NPC). Mediates docking of the substrate-importin complex to distinct nucleoporins (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0061608;
GO  GO:0008139;
GO  GO:0031267;
GO  GO:0006606;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSEWVPNQDGLKQLVYVLNLSNSTSREVHDQIREELDKFHSVPDYNNYLTLIFKSNELQPHIRSVAGLVLKTNIKQYFEK
SQ  MPREVQNYIKREILPVLSDPDASVRHTVGNIITNLIKKSCFSEWPELLPALNLALDSNSQDLIEGSLYTLSLLCEDSTKK
SQ  LDSDDSGRALNQLIPKLIMFFKCNNADFRKKALVSISYFIISMPGALLINMEAFLKGIFSMSEDPSEAVRTNVCKTLVTL
SQ  VETKIEFLLPYIKDVIQYMLHATKDKSEEVALEACEFWTAISQAEGCRDLLRDYLPVLVPILLNGMVYTEQDYEYLDQGD
SQ  DSMTPDRPQDIKPFIASTKSHGSGSSGGGQDTGFVNPDNNNNSNNNNSSNNNSSNNNNNNNNEDDEEYNDDDDDDDDDGF
SQ  EDEAWTIRKSSAFAIDVLSGIFPDAEYLSVTLPLIEQRMNEQNPWPVRESAILALGAIADGSKNGLAPHLSKVIPYLINT
SQ  LNDPKPLVRSITCWTLSRYSYWIAQADGRDYLHPLVVNLLNRIVDNNKKVQEAACSAFATLEEEADLLLIPYLQMILVTF
SQ  VNAFGKYQAKNLLILYDAISTLAKVVGNELNKPELINILVPPLLQKFNALDDSNKNLLPLLGCLNQVCSSIGAGLQNLIS
SQ  LFFNRSIKLIEGSLQAHYKYNNQDQKGSSSSSDQDFIVAALDLLQGLSEGIGTSIESLIPNSNLPHLLLQCMNLRGSDVL
SQ  QSSFALLGDMSKFCLIHFKQYIPDYLNILTNNLYPEYLSVCNNASWAIGEIAIRMPDEVKPFVVAIRDRLISNINKVNLN
SQ  RGVLENTAVTIGRLGIVSPADISPFVDKFIQCWCMAIRRKTDDIEKDSAFRGMWLIINNNPNGALRHLVYICDAVASWDK
SQ  MQPDLYEAYFKLLHMYKTSMGGVWAQFYNQFPEQLREILNEKFKLNQDISQ
//
ID  Q19253;
PN  Transducer of Cdc42-dependent actin assembly protein 1 homolog;
GN  toca;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:23150597}. Apical cell membrane {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Peripheral membrane protein {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Cytoplasmic side {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}. Basolateral cell membrane {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Peripheral membrane protein {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}; Cytoplasmic side {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}. Cytoplasmic vesicle {ECO:0000269|PubMed:19798448}. Cytoplasm {ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25775511}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23150597}. Recycling endosome {ECO:0000269|PubMed:25775511}. Note=Co-localizes with ajm-1 at cell junctions (PubMed:19798448). Co-localizes with toca-2, rme-1, cdc-42 and wve-1 on recycling endosomes (PubMed:25775511). {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}.
DR  UNIPROT: Q19253;
DR  UNIPROT: Q8MQ82;
DR  Pfam: PF00611;
DR  Pfam: PF00018;
DR  PROSITE: PS51741;
DR  PROSITE: PS51860;
DR  PROSITE: PS50002;
DE  Function: Plays a role in protein trafficking, actin organization and embryonic morphogenesis (PubMed:19798448). Potentially acts as cdc-42 effector (PubMed:25775511). May play a role in hypodermal P-cell nuclear positioning (PubMed:23150597). Together with toca-2, is required for protein trafficking regulating yolk protein clathrin- mediated endocytosis by oocytes during oogenesis and retrograde recycling and the sorting of recycling endosome cargo proteins such as mig-14 (PubMed:19798448, PubMed:25775511). Also, together with toca-2, controls the distribution of actin at cell junctions (PubMed:19798448, PubMed:26578656). {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25775511, ECO:0000269|PubMed:26578656}.
DE  Reference Proteome: Yes;
DE  Interaction: P39055; IntAct: EBI-6533636; Score: 0.37
DE  Interaction: A0A1C3NSL9; IntAct: EBI-6533681; Score: 0.37
DE  Interaction: O17578; IntAct: EBI-6533651; Score: 0.37
DE  Interaction: Q09442; IntAct: EBI-6533666; Score: 0.37
DE  Interaction: G5ED57; IntAct: EBI-6533743; Score: 0.37
DE  Interaction: Q9XZI6; IntAct: EBI-6533696; Score: 0.37
DE  Interaction: B7WN72; IntAct: EBI-6533711; Score: 0.37
DE  Interaction: Q93343; IntAct: EBI-6533728; Score: 0.37
DE  Interaction: Q20877; IntAct: EBI-6533788; Score: 0.37
DE  Interaction: Q19782; IntAct: EBI-6533758; Score: 0.37
DE  Interaction: Q20010; IntAct: EBI-6533773; Score: 0.37
DE  Interaction: G5EFY6; IntAct: EBI-6533833; Score: 0.37
DE  Interaction: Q94246; IntAct: EBI-6533803; Score: 0.37
DE  Interaction: O01900; IntAct: EBI-6533818; Score: 0.37
DE  Interaction: G5EF97; IntAct: EBI-6533880; Score: 0.37
DE  Interaction: Q9U304; IntAct: EBI-6533863; Score: 0.37
DE  Interaction: G5EC72; IntAct: EBI-6533848; Score: 0.37
DE  Interaction: A8WFL0; IntAct: EBI-6533925; Score: 0.37
DE  Interaction: A5PEX6; IntAct: EBI-6533895; Score: 0.37
DE  Interaction: Q4VNJ8; IntAct: EBI-6533910; Score: 0.37
DE  Interaction: Q23571; IntAct: EBI-6533942; Score: 0.37
DE  Interaction: O17577; IntAct: EBI-6542246; Score: 0.37
DE  Interaction: O61701; IntAct: EBI-6542293; Score: 0.37
DE  Interaction: Q95QQ9; IntAct: EBI-6542278; Score: 0.37
DE  Interaction: Q1XFY2; IntAct: EBI-6542308; Score: 0.37
DE  Interaction: G5ECJ4; IntAct: EBI-6542323; Score: 0.37
DE  Interaction: F5GUF0; IntAct: EBI-6542340; Score: 0.37
DE  Interaction: Q95QA6; IntAct: EBI-6542370; Score: 0.37
DE  Interaction: A8XQ35; IntAct: EBI-6542387; Score: 0.37
GO  GO:0016324;
GO  GO:0016323;
GO  GO:0005911;
GO  GO:0097708;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0055037;
GO  GO:0048613;
GO  GO:0006897;
GO  GO:1904703;
GO  GO:2000370;
GO  GO:1901046;
GO  GO:0032956;
GO  GO:0007165;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MNDSCSWDQLWDQQGTLNEYTGKGIDLLERIMAYSKERASIELEYSSKLKALSKKTAMKMKSESELWNSVSYVKGFHDVI
SQ  AGIVPVATQHELIAENLKSAVIPFTTQKIAEYRVAKKQLESDNSNLGKQLRMVIDEMAKSHKEYVKCYKETEAAMLKYAK
SQ  AEKNMDISRLELEKTKNNYQQKCGMLEESKQTYAVMTTKANEEQSAHYDRKLPQLLDNYKKLHTNRILDTVEILSKCVEA
SQ  ESCVNQIIASCHNDMRRDIGLIDPSRDANLVVENMKSGHPVPQPFVFEDLGHPQDRSSFMGGGASGPAGSMDGMDATMKK
SQ  GGTLMSKNGKGVARKQSMHQKFFGGGTADKKTDSGDYGTLPPQQRARKIAGKISDLEKEKDRATQSREGVSKMQAAYREN
SQ  PKLGNPSDCDAQLAQYGHEIDALSNQIQKFKILLDDVNAQLGAGGLSATSVGGSDTPPSIRSVSSASSGVTSRVNTINDA
SQ  HRTNGGVGGGRRESFSGSNGGSDTDPTINGNGHGRDELYEECSNPNPVLGEAIAQFAFDGAQDGTIRMEANEKLWLIEKD
SQ  EGDGWTRVRKENNSADGFVPSSYLKVTWFGKV
//
ID  Q09293;
PN  Embryonic developmental protein tofu-6;
GN  tofu;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Nucleus {ECO:0000269|PubMed:31216475}. Note=Dispersedly distributes throughout the cytoplasm in early embryos (PubMed:31147388). During early embryogenesis, localizes to the nucleus at prophase of cell division, and remains in the cytosol at interphase in 2- and 4-cell embryos (PubMed:31216475). Does not localize to cytoplasmic granules in oocytes and embryos (PubMed:31216475). Localizes to puncta in the perinuclear region in the germline syncytium (PubMed:31147388, PubMed:31216475). Localization to the perinuclear region in the germline is dependent on pid-1, tost-1, pics-1 and erh-2 (PubMed:31216475). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
DR  UNIPROT: Q09293;
DR  UNIPROT: Q9BMU5;
DR  PDB: 7D1L;
DR  PDB: 7D2Y;
DR  PDB: 7OCX;
DR  Pfam: PF00076;
DR  PROSITE: PS50102;
DE  Function: Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Promotes the biogenesis of 21U-RNAs (PubMed:31216475). Required for chromosome segregation and cell division in early embryos (PubMed:17171368, PubMed:31216475). May have a role in DNA replication (PubMed:17171368). {ECO:0000269|PubMed:17171368, ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475, ECO:0000305|PubMed:31216475}.
DE  Reference Proteome: Yes;
DE  Interaction: O61955; IntAct: EBI-21449250; Score: 0.52
DE  Interaction: O76616; IntAct: EBI-2415585; Score: 0.68
DE  Interaction: Q17973; IntAct: EBI-2413298; Score: 0.49
DE  Interaction: Q20660; IntAct: EBI-2415578; Score: 0.49
DE  Interaction: Q19541; IntAct: EBI-21448974; Score: 0.46
DE  Interaction: Q20057; IntAct: EBI-21449069; Score: 0.35
DE  Interaction: Q18244; IntAct: EBI-21449250; Score: 0.35
DE  Interaction: Q18490; IntAct: EBI-21449250; Score: 0.35
DE  Interaction: O45551; IntAct: EBI-21449250; Score: 0.35
DE  Interaction: Q17339; IntAct: EBI-21449250; Score: 0.35
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0034518;
GO  GO:0003723;
GO  GO:0034585;
GO  GO:0051301;
GO  GO:0006260;
GO  GO:0009792;
GO  GO:0040016;
GO  GO:0031047;
GO  GO:0051306;
GO  GO:1990511;
GO  GO:0051781;
GO  GO:0051984;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASSSTAYYLKDAGFHIRNIPKAWNDWNLFHVFQNFGKVSYCRVVGQSNDGQVQLGFVNMMSVADADEVRKNLNDGNLIG
SQ  ENFTLKVTDHKNVGGSLLPMASNSVQKLVSSPPSKSGPVLLSSSWLPLNKDIEVEVVDYLPSSSVAPDLFALTLLRINDS
SQ  SMKEKYDSMHEKMNAYAQIVPFDSELEIGYDGVFRDAPRSVRRVRRISATKLYLVDFGKIINYEKAKCFQLPKVFQSMPT
SQ  RVSLCGLDGLTWSPVAIPSFDNIREVVKKWGQMENSTLHAMACGFQGSINMINLFCGKSILADRLQRKGVCEYLPRSQQP
SQ  HYAYSRETLLQHNNSGVTAQISNDADVVKDLLKKIDGVKNMLRELEL
//
ID  F1N4E5;
PN  Torsin-1A-interacting protein 1;
GN  TOR1AIP1;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: F1N4E5;
DR  Pfam: PF05609;
DE  Function: Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0001671;
GO  GO:0061024;
GO  GO:0071763;
GO  GO:0032781;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGEGQRAEPEREGWALYVTPRAPLREGRPRLAPQNGGSGDVPAYGTPTPSRHGRREVRFSEEPPEVYGDFEPRAAKEKA
SQ  RVGRQIPLEGFRPDSAKEEVRESAYYLRSRQRRQPRLHEAEEMQTRRAALLQQQPHSPPPPLRPSPVTTRRGLRDSHSSE
SQ  EDEPPSQTVLSQTVTKKAIRRTQETPVMSEDPLISLRRPPLRSSRSEAASVQQKVNFLEEGETEENDQDSFDSDVTVKVR
SQ  SGDSVESGDQTTRSSSQYKESFWQSSQSGDFTAFDEQPLKLSSGYQKTPQEWAEKTVRIRTRMLTSSPGMRSIYGSFSDD
SQ  DSVQKSELGNQSPSTSNQQMTGQPKSVSSVKTKRYWPFAVIAALLIGGFLYTRPPEAETTAVQEFQNQMKQLMNKYQGQD
SQ  EKLWKRSQTFLEKHLNGSQSRPQPAILLLTAARDAEEALRCLSEQIADAYSSFRSVPAIRIDGASKATRDSDTVKEEVDQ
SQ  ELSNGFRNGQNAAVVHRFESLPAGSTLIFYKYCDHESAAFKDVALVLTVLLEEETLGTSLGLKEIEEKVRDFLQVKFTNS
SQ  DTPNSYKHMDPDKLSGLWSRISHLVLPVQPENDLKKGICL
//
ID  Q5JTV8;
PN  Torsin-1A-interacting protein 1;
GN  TOR1AIP1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:12061773, ECO:0000269|PubMed:24275647}; Single-pass membrane protein {ECO:0000269|PubMed:12061773, ECO:0000269|PubMed:24275647}.
DR  UNIPROT: Q5JTV8;
DR  UNIPROT: A8K630;
DR  UNIPROT: B0QZ57;
DR  UNIPROT: Q5JTV6;
DR  UNIPROT: Q8IZ65;
DR  UNIPROT: Q9H8Y6;
DR  UNIPROT: Q9HAJ1;
DR  UNIPROT: Q9NV52;
DR  UNIPROT: Q9Y3X5;
DR  PDB: 4TVS;
DR  Pfam: PF05609;
DR  OMIM: 614512;
DR  OMIM: 617072;
DR  DisGeNET: 26092;
DE  Function: Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina. {ECO:0000269|PubMed:23569223}.
DE  Disease: Myopathy, autosomal recessive, with rigid spine and distal joint contractures (MRRSDC) [MIM:617072]: An autosomal recessive degenerative myopathy characterized by muscle weakness initially involving the proximal lower limbs, followed by distal upper and lower limb muscle weakness and atrophy. Other features include joint contractures, rigid spine, and restricted pulmonary function. Cardiac involvement has been observed in some patients. Disease onset is in the first or second decades of life. {ECO:0000269|PubMed:24856141}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O14656; IntAct: EBI-26365158; Score: 0.54
DE  Interaction: O14657; IntAct: EBI-15853118; Score: 0.40
DE  Interaction: O95831; IntAct: EBI-11159793; Score: 0.53
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P0DTD1; IntAct: EBI-25491011; Score: 0.53
DE  Interaction: P13285; IntAct: EBI-11733017; Score: 0.35
DE  Interaction: Q921T2; IntAct: EBI-2559664; Score: 0.40
DE  Interaction: Q9Z1B5; IntAct: EBI-2560653; Score: 0.56
DE  Interaction: P62136; IntAct: EBI-5549941; Score: 0.57
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-9515510; Score: 0.35
DE  Interaction: Q16659; IntAct: EBI-12502733; Score: 0.35
DE  Interaction: P36895; IntAct: EBI-11008521; Score: 0.35
DE  Interaction: Q13257; IntAct: EBI-11147019; Score: 0.35
DE  Interaction: P35813; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q04637; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: P10599; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q9H792; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q969N2; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q9NX63; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: O94782; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q8TEX9; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q9UBW8; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q9UHQ1; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q9UHL9; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q8N565; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q8N4Q1; IntAct: EBI-11159793; Score: 0.35
DE  Interaction: Q5HYA8; IntAct: EBI-11367583; Score: 0.27
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11372136; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q2MV58; IntAct: EBI-11384104; Score: 0.27
DE  Interaction: Q96Q45; IntAct: EBI-11396533; Score: 0.27
DE  Interaction: Q9NYB0; IntAct: EBI-11306670; Score: 0.51
DE  Interaction: Q15554; IntAct: EBI-11306660; Score: 0.37
DE  Interaction: C5E526; IntAct: EBI-12584472; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q9NS85; IntAct: EBI-21798936; Score: 0.35
DE  Interaction: Q96M94; IntAct: EBI-21820342; Score: 0.35
DE  Interaction: Q15013; IntAct: EBI-21820342; Score: 0.35
DE  Interaction: Q5JU69; IntAct: EBI-15853028; Score: 0.40
DE  Interaction: Q9H497; IntAct: EBI-15853095; Score: 0.40
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16801466; Score: 0.27
DE  Interaction: O60506; IntAct: EBI-20932664; Score: 0.40
DE  Interaction: P62807; IntAct: EBI-25471348; Score: 0.27
DE  Interaction: P36873; IntAct: EBI-21448155; Score: 0.59
DE  Interaction: Q02750; IntAct: EBI-25382666; Score: 0.35
DE  Interaction: Q8N302; IntAct: EBI-25917997; Score: 0.56
DE  Interaction: Q13573; IntAct: EBI-25917977; Score: 0.56
DE  Interaction: Q06323; IntAct: EBI-25917967; Score: 0.56
DE  Interaction: Q9NSI6; IntAct: EBI-25917987; Score: 0.56
DE  Interaction: Q496A3; IntAct: EBI-25918017; Score: 0.56
DE  Interaction: Q8WUU4; IntAct: EBI-25918007; Score: 0.56
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0H3NFP4; IntAct: EBI-27055788; Score: 0.27
DE  Interaction: A0A0H3NG92; IntAct: EBI-27055968; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P42695; IntAct: EBI-28951349; Score: 0.35
DE  Interaction: P30530; IntAct: EBI-32719959; Score: 0.27
DE  Interaction: Q5JZY3; IntAct: EBI-32720634; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
DE  Interaction: Q5W0V3; IntAct: EBI-34574999; Score: 0.27
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0001671;
GO  GO:0051117;
GO  GO:0008092;
GO  GO:0005521;
GO  GO:0061024;
GO  GO:0071763;
GO  GO:0032781;
GO  GO:0090435;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGDGRRAEAVREGWGVYVTPRAPIREGRGRLAPQNGGSSDAPAYRTPPSRQGRREVRFSDEPPEVYGDFEPLVAKERSP
SQ  VGKRTRLEEFRSDSAKEEVRESAYYLRSRQRRQPRPQETEEMKTRRTTRLQQQHSEQPPLQPSPVMTRRGLRDSHSSEED
SQ  EASSQTDLSQTISKKTVRSIQEAPVSEDLVIRLRRPPLRYPRYEATSVQQKVNFSEEGETEEDDQDSSHSSVTTVKARSR
SQ  DSDESGDKTTRSSSQYIESFWQSSQSQNFTAHDKQPSVLSSGYQKTPQEWAPQTARIRTRMQNDSILKSELGNQSPSTSS
SQ  RQVTGQPQNASFVKRNRWWLLPLIAALASGSFWFFSTPEVETTAVQEFQNQMNQLKNKYQGQDEKLWKRSQTFLEKHLNS
SQ  SHPRSQPAILLLTAARDAEEALRCLSEQIADAYSSFRSVRAIRIDGTDKATQDSDTVKLEVDQELSNGFKNGQNAAVVHR
SQ  FESFPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLGTSLGLKEVEEKVRDFLKVKFTNSNTPNSYNHMDPDKLNGL
SQ  WSRISHLVLPVQPENALKRGICL
//
ID  Q921T2;
PN  Torsin-1A-interacting protein 1;
GN  Tor1aip1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q921T2;
DR  UNIPROT: E9QLK1;
DR  UNIPROT: Q1EQW1;
DR  UNIPROT: Q3U7A4;
DR  Pfam: PF05609;
DE  Function: Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina. {ECO:0000269|PubMed:20457914}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5JTV8; IntAct: EBI-2559664; Score: 0.40
DE  Interaction: Q7L576; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-2559664; Score: 0.56
DE  Interaction: Q8TCX1; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: D6RA89; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: P50416; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q9UBD5; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: I3L1P8; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q13867; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: O60292; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: P52789; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q9Y6K0; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q5K651; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q15758; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: P0C0L5; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q9Y2H6; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: O00461; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: O14925; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q9BUK6; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: O94822; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: J3QLU9; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: H7C2E6; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: O14828; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q06830; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q5XPI4; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q9BX66; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q9HBH0; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q5VYS8; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q10471; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: P50570; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: O95149; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: O00231; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: P51532; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: P32119; IntAct: EBI-10996616; Score: 0.35
DE  Interaction: Q99ME6; IntAct: EBI-15644413; Score: 0.37
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0001671;
GO  GO:0051117;
GO  GO:0008092;
GO  GO:0005521;
GO  GO:0061024;
GO  GO:0071763;
GO  GO:0032781;
GO  GO:0090435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGERWQAEGPGEGWAIYVTPRAPIREGRRRLDPRNGDSSDAPAYGAHPSRRGRREVRFSEEPAEVYGDFEPRAAKERSP
SQ  GGRRTPPEKFRPASAGEEVRESAYNLRSRPRRQRRAQEAEEMKTRRSARLEQHSQQPQLSPATSGRGLRDSPSSSEDREE
SQ  DEPSSRPVTSQTASKKTLRTPEASVMNEDPISNLCRPPLRSPRLDSTYQTNGNTKTNEREATIVQQVNFFEEGETEDDLE
SQ  SSYSDITIRARSSDSLESRDEATPAAGNHPDSLRGLPHNQDFPAHENQPLLLTSGCQENPQEWVDRAVRMRSRMAYNNIQ
SQ  KSNFGNQSPSTSRPQSAIHHPNEPSVKIKWWLLGLVAILAVGLFWFFHTPAVETTAVQEFQNQMKQLQSKYQSQNEKLWK
SQ  RGTTFLEKHLNSSLPRPQPAILLLTAAQDAAEVLKCLSEQIADAYSSFRSVRAIRIDGAGKAAQDSDLVKHEVDQELTDG
SQ  FKNGQNAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEKTLEASLGLKEIEEKVRDFLKVKFTSSSTASS
SQ  YNHMDPDKLNGLWSRISHLVLPVQPENTLKAGSCL
//
ID  Q5R7A3;
PN  Torsin-1A-interacting protein 1;
GN  TOR1AIP1;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
DR  UNIPROT: Q5R7A3;
DR  Pfam: PF05609;
DE  Function: Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0001671;
GO  GO:0032781;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGEGRRAEAVREGWGVYVTPRAPIREGRGRLAPQNGGSSDAPAYRTSLSRQGRREVRFSDEPPEVYGDFEPLVDKERSP
SQ  VGKRTRLEEFRSDSAKEEVRESAYYLRSRQRRQPRPQEAEEMKTRRTTRLQQQHSQQPPLQPSPVMTRRGLRDSHSSEED
SQ  EPSSPTDLSQTISKKTVRSIQEAPAESEDLVISLRRPPLRYPRSEATSVQQKVNFSEEGETEDDQDSSHSSVTTVKSRSR
SQ  DSDESGDKTTRSSSQYIESFWQSSQSQNFTAHDKQPSVLSSGYQKTPQEWAPQTARMRTRMQTSSPGKSSIYGSFSDDDS
SQ  ILKSELGNQSPSTSSQQVTGQPQNASFVKRNWWWLLPLIAALASGSFWFFSTPEVETTAVQEFQNQMNQLKNKYQGQDEK
SQ  LWKRSQTFLEKHLNSSHPRSQPAILLLTAARDAEEALRCLSEQIADAYSSFHSVRAIRIDGTDKATQDSDTVKLEVDQEL
SQ  SNGLKNGQNAAVVHRFESFPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLGTSLGLKEVEEKVRDFLKVKFTNSNT
SQ  PNSYNHMDPDKLNGLWSRISHLVLPVQPENALKRGICL
//
ID  Q5PQX1;
PN  Torsin-1A-interacting protein 1;
GN  Tor1aip1;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16128803, ECO:0000269|PubMed:7721789}; Single-pass membrane protein {ECO:0000269|PubMed:16128803, ECO:0000269|PubMed:7721789}.
DR  UNIPROT: Q5PQX1;
DR  UNIPROT: Q62741;
DR  UNIPROT: Q62754;
DR  Pfam: PF05609;
DE  Function: Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina.
DE  Reference Proteome: Yes;
DE  Interaction: Q9R193; IntAct: EBI-15644460; Score: 0.40
DE  Interaction: P63088; IntAct: EBI-21448628; Score: 0.50
DE  Interaction: P62138; IntAct: EBI-21448632; Score: 0.50
DE  Interaction: P07949; IntAct: EBI-22248708; Score: 0.35
DE  Interaction: P35590; IntAct: EBI-22249141; Score: 0.35
DE  Interaction: P35968; IntAct: EBI-22252438; Score: 0.35
DE  Interaction: O75886; IntAct: EBI-22259612; Score: 0.35
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0001671;
GO  GO:0051117;
GO  GO:0008092;
GO  GO:0005521;
GO  GO:0061024;
GO  GO:0071763;
GO  GO:0032781;
GO  GO:0090435;
GO  GO:0034504;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGERWRAEGLGEGWAIYVTPRAPIREGRRRLATQNGDGSDAPAYETHPSRHGRREVRFSEEPPEVYGDFEPRAAKERSP
SQ  GERRTPPEKFRSDSAKEEVRESAYNLRSRQRRQRGPQEAEEMKTRRSTRLEQHSQQAQQQLSPATSGRGLRDAQSLSEDR
SQ  GEDEPSSQPVTSQTVSKKTVRTPETSVMSEDPISNLCRPPLRSPRPDASIVQHINPFEEGETEDDLESSYSDVTIRIRSR
SQ  DSVESRDEAAVAAGHHPDSLWGLPHSRGDFTAHENQPSLLPTGCQKNPQEWVEQAVRMRTRMAYNNIQKSDFGNQSPSTS
SQ  RQQAAVQPPDESSVKIKWWLLILVAALAMGIYWFFHTPVVETTAVQEFQNQMKQLQSKYQSQDEKLWKRGTTFLEKHLNS
SQ  SLPRPQPAILLLTAAQDAAEVLKCLSEQIADAYSSFRSVRAIRIDGAGKAAQDSDLVKHEVDQELTDGFRNGQNAAVVHR
SQ  FESLPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEQTLEASLGLKEIEEKVRDFLKVKFTSSDTANSYNHMDPDKLNGL
SQ  WSRISHLVLPVQPENALKAGSCL
//
ID  Q8NFQ8;
PN  Torsin-1A-interacting protein 2;
GN  TOR1AIP2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane.
DR  UNIPROT: Q8NFQ8;
DR  PDB: 5J1S;
DR  PDB: 5J1T;
DR  Pfam: PF05609;
DR  OMIM: 614513;
DR  DisGeNET: 163590;
DE  Function: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity. {ECO:0000269|PubMed:19339278, ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647}.
DE  Reference Proteome: Yes;
DE  Interaction: K9N7C7; IntAct: EBI-26374899; Score: 0.35
DE  Interaction: O14656; IntAct: EBI-524382; Score: 0.67
DE  Interaction: O43542; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q15714; IntAct: EBI-1079144; Score: 0.00
DE  Interaction: P04578; IntAct: EBI-6176374; Score: 0.35
DE  Interaction: P0CK49; IntAct: EBI-11725356; Score: 0.35
DE  Interaction: P0CK56; IntAct: EBI-11725466; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: Q2MG95; IntAct: EBI-11733653; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11398030; Score: 0.27
DE  Interaction: Q9H0F7; IntAct: EBI-12448976; Score: 0.51
DE  Interaction: Q92766; IntAct: EBI-11923291; Score: 0.00
DE  Interaction: Q20MH8; IntAct: EBI-12586007; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q9UGJ1; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9UDX5; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9P0V3; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9NZJ7; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9NVN8; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9NVH2; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9HBR0; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9H649; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9BY32; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9BSJ5; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9BSF4; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q96T37; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q8WZA1; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q8TF71; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q8TE99; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q8NE86; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q8NCW6; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q6SPF0; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q5VST6; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q5SVS4; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q3ZCM7; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q16394; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q15072; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q10469; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q0GE19; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q08357; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q05932; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: P78345; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: P62829; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: P16260; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: O95707; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: O95258; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: O94832; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: O60488; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: O60216; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: O15239; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: A0PJW6; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9BRN9; IntAct: EBI-21647799; Score: 0.35
DE  Interaction: Q13509; IntAct: EBI-21665394; Score: 0.35
DE  Interaction: P15880; IntAct: EBI-21677299; Score: 0.35
DE  Interaction: Q9NY97; IntAct: EBI-21814023; Score: 0.35
DE  Interaction: Q0P651; IntAct: EBI-21843435; Score: 0.35
DE  Interaction: Q8WVQ1; IntAct: EBI-21857733; Score: 0.35
DE  Interaction: P59190; IntAct: EBI-21873283; Score: 0.35
DE  Interaction: Q9H4B7; IntAct: EBI-21890439; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.42
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC5; IntAct: EBI-25685699; Score: 0.35
DE  Interaction: Q2TAZ0; IntAct: EBI-26443127; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: P56180; IntAct: EBI-27116883; Score: 0.27
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031965;
GO  GO:0001671;
GO  GO:0051117;
GO  GO:0007029;
GO  GO:0061024;
GO  GO:0032781;
GO  GO:0090435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADSGLREPQEDSQKDLENDPSVNSQAQETTIIASNAEEAEILHSACGLSKDHQEVETEGPESADTGDKSESPDEANVGK
SQ  HPKDKTEDENKQSFLDGGKGHHLPSENLGKEPLDPDPSHSPSDKVGRADAHLGSSSVALPKEASDGTGASQEPPTTDSQE
SQ  AQSPGHSSAGQEGEDTLRRRLLAPEAGSHPQQTQKLEEIKENAQDTMRQINKKGFWSYGPVILVVLVVAVVASSVNSYYS
SQ  SPAQQVPKNPALEAFLAQFSQLEDKFPGQSSFLWQRGRKFLQKHLNASNPTEPATIIFTAAREGRETLKCLSHHVADAYT
SQ  SSQKVSPIQIDGAGRTWQDSDTVKLLVDLELSYGFENGQKAAVVHHFESFPAGSTLIFYKYCDHENAAFKDVALVLTVLL
SQ  EEETLEASVGPRETEEKVRDLLWAKFTNSDTPTSFNHMDSDKLSGLWSRISHLVLPVQPVSSIEEQGCLF
//
ID  Q8BYU6;
PN  Torsin-1A-interacting protein 2;
GN  Tor1aip2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q8BYU6;
DR  UNIPROT: Q6NY10;
DR  UNIPROT: Q8BJP0;
DR  Pfam: PF05609;
DE  Function: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0001671;
GO  GO:0051117;
GO  GO:0007029;
GO  GO:0061024;
GO  GO:0032781;
GO  GO:0090435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSQSLKSQNTNMSDSGCRDPVGDSQNVLENDPSINSQTQDTRVTPNNTAEAQPLQPTSDLKEDHHEIGARAQEHTDTGDR
SQ  SESPEEPALEKPPLDKAELESSPSSQDTELGHHPHSEHGGGDALDLDPNCSQSDLGGRADAHLESSSVASPEGAGDRGEA
SQ  DEHLESSSAAPTEGAGDRGEAGQELLAEDSTDGQSLGHSNTGPGNQDSLRRRLPVPEAGSHEEETELVKEKQEVAQDTLR
SQ  KTDKKSLWTYGSVFLGCLIVAVVLSSVNSYYSSPAQQVPQNPALEAFLAQFGQLKEKFPGQSSFLWQRGRKFLQKHLNAS
SQ  NPSEPATIIFTAAREGKETLKCLSYHVANAYTSSQKVTAVSIDGAERALQDSDTVKLLVDLELSDGFENGHKAAVVHHFE
SQ  SLPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLEASVSPREIEEKVRDLLWAKFTNSESPTSYSHMDSDKLSGLWS
SQ  RISHLVLPVQPVRNIEERGCLL
//
ID  Q6P752;
PN  Torsin-1A-interacting protein 2;
GN  Tor1aip2;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q6P752;
DR  Pfam: PF05609;
DE  Function: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0001671;
GO  GO:0051117;
GO  GO:0007029;
GO  GO:0061024;
GO  GO:0032781;
GO  GO:0090435;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSQTLKSQDTNMSDSGYRDPVEDSQNVLGNDPSVNSQAQDPIVTPSNTVEAQTLHPTSDLKEDHHEIGAKGQEHADTGDR
SQ  AESSEEPALEKPPLDKAELERSPSSQDTEQRHHPYSEHVGGDTLVLDPNYSQSDLGGRADAHLESSSAAPTEGAGEGGEA
SQ  GAHLESSCAALPVGADEGGRANAHLESSSAAPTEGAGEGGEADVHLESSSAVPPEEAHLESSSAAPSEGAGEGGEADAHL
SQ  ESSSAAPSEGAGEGGETAQNLLAVDSTDAQSPCHSSAGPGSQDSLRRRLPVTEAERHEEETQLVTEKEEVAQETLRKTEK
SQ  KSLWTYGSMFLGCLIVAVVLSSVNSYYSSPAQQVPQNPALEAFLAQFSQLREKFPGQSAFLWQRGRKFLQKHLNASNPSE
SQ  PATVIFTAAREGKETLKCLSYHVANAYTSSQKVTAVSIDGAERALQDSDTVKLLVDLELSYGFENGHKAAVVHHFESLPA
SQ  GSTLIFYKYCDHENAAFKDVALVLTVLLEEETLEASVSPRETEEKVRDLLWAKFTDSGTPSSFSHMDSDKLSGLWSRISH
SQ  LVLPVQPVKNIEERGCLL
//
ID  Q9ERA9;
PN  Torsin-1A;
GN  TOR1A;
OS  10034;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum lumen {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Mainly located in the lumen of the endoplasmic reticulum.Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus membrane is mediated by the interaction with TOR1AIP2 (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9ERA9;
DR  Pfam: PF06309;
DE  Function: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non- neural tissues (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0070161;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005788;
GO  GO:0042406;
GO  GO:0030426;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0030141;
GO  GO:0008021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0140662;
GO  GO:0008092;
GO  GO:0051082;
GO  GO:0007155;
GO  GO:0061077;
GO  GO:0071712;
GO  GO:0045104;
GO  GO:0031175;
GO  GO:0006998;
GO  GO:0071763;
GO  GO:0006996;
GO  GO:1900244;
GO  GO:0000338;
GO  GO:0034504;
GO  GO:0051584;
GO  GO:2000008;
GO  GO:0048489;
GO  GO:0044319;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  AECCGQKRSLSREALQKDLDDKLFGQHLAKKVILNAVSGFLSNPKPKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLNS
SQ  DYVHLFVATLHFPHASNVTLYKDQLQMWIRGNVSACARSIFIFDEMDKMHAGLIDAIKPFLDYYDVVDEVSYQKAIFIFL
SQ  SNAGAERITDVALDFWKSGKQREEIKLRDMEHALAVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQ
SQ  SRGYEVDEDIISKVAEEMTFFPKEERVFSDKGC
//
ID  O14656;
PN  Torsin-1A;
GN  TOR1A;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum lumen {ECO:0000269|PubMed:29053766}. Nucleus membrane {ECO:0000269|PubMed:14970196, ECO:0000269|PubMed:29053766}; Peripheral membrane protein {ECO:0000305}. Cell projection, growth cone {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Cytoplasm, cytoskeleton. Note=Upon oxidative stress, redistributes to protusions from the cell surface (By similarity). Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus membrane is mediated by the interaction with TOR1AIP2. {ECO:0000250}.
DR  UNIPROT: O14656;
DR  UNIPROT: B2RB58;
DR  UNIPROT: Q53Y64;
DR  UNIPROT: Q96CA0;
DR  PDB: 5J1S;
DR  PDB: 5J1T;
DR  PDB: 6OIF;
DR  Pfam: PF06309;
DR  OMIM: 128100;
DR  OMIM: 605204;
DR  OMIM: 618947;
DR  DisGeNET: 1861;
DE  Function: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non- neural tissues. {ECO:0000269|PubMed:15505207, ECO:0000269|PubMed:16361107, ECO:0000269|PubMed:17428918, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19339278, ECO:0000269|PubMed:20169475, ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24930953}.
DE  Disease: Dystonia 1, torsion, autosomal dominant (DYT1) [MIM:128100]: A primary torsion dystonia, and the most common and severe form. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Dystonia type 1 is characterized by involuntary, repetitive, sustained muscle contractions or postures involving one or more sites of the body, in the absence of other neurological symptoms. Typically, symptoms develop first in an arm or leg in middle to late childhood and progress in approximately 30% of patients to other body regions (generalized dystonia) within about five years. 'Torsion' refers to the twisting nature of body movements observed in DYT1, often affecting the trunk. Distribution and severity of symptoms vary widely between affected individuals, ranging from mild focal dystonia to severe generalized dystonia, even within families. {ECO:0000269|PubMed:14970196, ECO:0000269|PubMed:15505207, ECO:0000269|PubMed:16361107, ECO:0000269|PubMed:17428918, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:18477710, ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19955557, ECO:0000269|PubMed:20169475, ECO:0000269|PubMed:21102408, ECO:0000269|PubMed:24930953, ECO:0000269|PubMed:27490483, ECO:0000269|PubMed:9288096}. Note=The disease is caused by variants affecting the gene represented in this entry. Arthrogryposis multiplex congenita 5 (AMC5) [MIM:618947]: A form of arthrogryposis multiplex congenita, a developmental condition characterized by multiple joint contractures resulting from reduced or absent fetal movements. AMC5 is an autosomal recessive form characterized by severe congenital contractures, developmental delay, strabismus and tremor. {ECO:0000269|PubMed:28516161, ECO:0000269|PubMed:29053766, ECO:0000269|PubMed:30244176}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q96NW7; IntAct: EBI-524271; Score: 0.49
DE  Interaction: Q8NFQ8; IntAct: EBI-524382; Score: 0.67
DE  Interaction: Q14204; IntAct: EBI-1063303; Score: 0.00
DE  Interaction: Q9UBM7; IntAct: EBI-1071080; Score: 0.00
DE  Interaction: Q9P003; IntAct: EBI-1074309; Score: 0.00
DE  Interaction: P16104; IntAct: EBI-2564373; Score: 0.35
DE  Interaction: Q9BT78; IntAct: EBI-8514616; Score: 0.27
DE  Interaction: P04578; IntAct: EBI-6176374; Score: 0.35
DE  Interaction: Q6TUG0; IntAct: EBI-8763627; Score: 0.37
DE  Interaction: Q66HD0; IntAct: EBI-8763848; Score: 0.37
DE  Interaction: P60409; IntAct: EBI-10181310; Score: 0.72
DE  Interaction: Q2MV58; IntAct: EBI-11366929; Score: 0.27
DE  Interaction: Q99750; IntAct: EBI-24404319; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q01814; IntAct: EBI-21599092; Score: 0.35
DE  Interaction: Q8N6K0; IntAct: EBI-21599984; Score: 0.35
DE  Interaction: P05090; IntAct: EBI-21683255; Score: 0.35
DE  Interaction: P10909; IntAct: EBI-21693789; Score: 0.35
DE  Interaction: Q96EU7; IntAct: EBI-21797521; Score: 0.35
DE  Interaction: Q8TCT7; IntAct: EBI-21797521; Score: 0.35
DE  Interaction: P04439; IntAct: EBI-21797521; Score: 0.35
DE  Interaction: O75596; IntAct: EBI-21797521; Score: 0.35
DE  Interaction: Q5JTV8; IntAct: EBI-26365158; Score: 0.54
DE  Interaction: P52824; IntAct: EBI-20905416; Score: 0.40
DE  Interaction: P0DTC8; IntAct: EBI-25491344; Score: 0.53
DE  Interaction: P0DTC3; IntAct: EBI-25686340; Score: 0.35
DE  Interaction: Q9Y605; IntAct: EBI-25847426; Score: 0.56
DE  Interaction: Q8TDB4; IntAct: EBI-25847418; Score: 0.56
DE  Interaction: Q96FZ7; IntAct: EBI-25847410; Score: 0.56
DE  Interaction: Q6PCB6; IntAct: EBI-25847402; Score: 0.56
DE  Interaction: Q9NR90; IntAct: EBI-25847386; Score: 0.56
DE  Interaction: Q96FT7; IntAct: EBI-25847378; Score: 0.56
DE  Interaction: Q9H4A5; IntAct: EBI-25847370; Score: 0.56
DE  Interaction: Q53EZ4; IntAct: EBI-25847362; Score: 0.56
DE  Interaction: Q9NX07; IntAct: EBI-25847354; Score: 0.56
DE  Interaction: Q9UI08; IntAct: EBI-25847346; Score: 0.56
DE  Interaction: Q9BY12; IntAct: EBI-25847336; Score: 0.56
DE  Interaction: O75616; IntAct: EBI-25847328; Score: 0.56
DE  Interaction: P57729; IntAct: EBI-25847320; Score: 0.56
DE  Interaction: Q99497; IntAct: EBI-25847312; Score: 0.56
DE  Interaction: Q9UHI6; IntAct: EBI-25847304; Score: 0.56
DE  Interaction: Q92993; IntAct: EBI-25847296; Score: 0.56
DE  Interaction: Q13113; IntAct: EBI-25847288; Score: 0.56
DE  Interaction: Q96CV9; IntAct: EBI-25847280; Score: 0.56
DE  Interaction: Q92478; IntAct: EBI-25847272; Score: 0.56
DE  Interaction: Q6DN90; IntAct: EBI-25847264; Score: 0.56
DE  Interaction: Q14154; IntAct: EBI-25847256; Score: 0.56
DE  Interaction: Q9BUZ4; IntAct: EBI-25847248; Score: 0.56
DE  Interaction: Q9UJX2; IntAct: EBI-25847238; Score: 0.56
DE  Interaction: O75558; IntAct: EBI-25847230; Score: 0.56
DE  Interaction: Q9UNS2; IntAct: EBI-25847222; Score: 0.56
DE  Interaction: P21980; IntAct: EBI-25847214; Score: 0.56
DE  Interaction: Q12824; IntAct: EBI-25847206; Score: 0.56
DE  Interaction: P12273; IntAct: EBI-25847198; Score: 0.56
DE  Interaction: P27986; IntAct: EBI-25847190; Score: 0.56
DE  Interaction: O00746; IntAct: EBI-25847182; Score: 0.56
DE  Interaction: Q15019; IntAct: EBI-25847174; Score: 0.56
DE  Interaction: O43196; IntAct: EBI-25847166; Score: 0.56
DE  Interaction: P41218; IntAct: EBI-25847158; Score: 0.56
DE  Interaction: P22692; IntAct: EBI-25847150; Score: 0.56
DE  Interaction: P0C0S5; IntAct: EBI-25847142; Score: 0.56
DE  Interaction: P35222; IntAct: EBI-25847134; Score: 0.56
DE  Interaction: O75626; IntAct: EBI-25847126; Score: 0.56
DE  Interaction: P63010; IntAct: EBI-25847118; Score: 0.56
DE  Interaction: Q05C28; IntAct: EBI-25847466; Score: 0.56
DE  Interaction: Q96QF0; IntAct: EBI-25847458; Score: 0.56
DE  Interaction: Q9H147; IntAct: EBI-25847450; Score: 0.56
DE  Interaction: Q9NQ40; IntAct: EBI-25847442; Score: 0.56
DE  Interaction: Q9UII2; IntAct: EBI-25847434; Score: 0.56
DE  Interaction: Q5JTY5; IntAct: EBI-25847514; Score: 0.56
DE  Interaction: A2RU56; IntAct: EBI-25847506; Score: 0.56
DE  Interaction: Q7Z6I5; IntAct: EBI-25847498; Score: 0.56
DE  Interaction: Q8IUB9; IntAct: EBI-25847490; Score: 0.56
DE  Interaction: Q6PIV2; IntAct: EBI-25847482; Score: 0.56
DE  Interaction: Q8NA54; IntAct: EBI-25847474; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25936102; Score: 0.56
GO  GO:0070161;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0070062;
GO  GO:0042406;
GO  GO:0030426;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0030141;
GO  GO:0008021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0140662;
GO  GO:0008092;
GO  GO:0042802;
GO  GO:0019894;
GO  GO:0051787;
GO  GO:0051082;
GO  GO:0007155;
GO  GO:0051085;
GO  GO:0061077;
GO  GO:0071712;
GO  GO:0045104;
GO  GO:0031175;
GO  GO:0006998;
GO  GO:0071763;
GO  GO:0006996;
GO  GO:1900244;
GO  GO:0000338;
GO  GO:0034504;
GO  GO:0051584;
GO  GO:2000008;
GO  GO:0006979;
GO  GO:0048499;
GO  GO:0048489;
GO  GO:0044319;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MKLGRAVLGLLLLAPSVVQAVEPISLGLALAGVLTGYIYPRLYCLFAECCGQKRSLSREALQKDLDDNLFGQHLAKKIIL
SQ  NAVFGFINNPKPKKPLTLSLHGWTGTGKNFVSKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQLWIRGNVS
SQ  ACARSIFIFDEMDKMHAGLIDAIKPFLDYYDLVDGVSYQKAMFIFLSNAGAERITDVALDFWRSGKQREDIKLKDIEHAL
SQ  SVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYEIDEDIVSRVAEEMTFFPKEERVFSDKGCK
SQ  TVFTKLDYYYDD
//
ID  Q60HG2;
PN  Torsin-1A;
GN  TOR1A;
OS  9541;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O14656}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus membrane is mediated by the interaction with TOR1AIP2. Upon oxidative stress, redistributes to protusions from the cell surface (By similarity). {ECO:0000250}.
DR  UNIPROT: Q60HG2;
DR  Pfam: PF06309;
DE  Function: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non- neural tissues (By similarity). {ECO:0000250|UniProtKB:O14656}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005788;
GO  GO:0042406;
GO  GO:0030426;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0030141;
GO  GO:0008021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0140662;
GO  GO:0008092;
GO  GO:0042802;
GO  GO:0051082;
GO  GO:0007155;
GO  GO:0051085;
GO  GO:0061077;
GO  GO:0071712;
GO  GO:0045104;
GO  GO:0031175;
GO  GO:0006998;
GO  GO:0071763;
GO  GO:1900244;
GO  GO:0000338;
GO  GO:0034504;
GO  GO:0051584;
GO  GO:2000008;
GO  GO:0048499;
GO  GO:0048489;
GO  GO:0044319;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MKLGRAALGLLLLAPSVVQAVEPISLGLALAGVLTGYIYPRLYCLFAECCGQKRSLSREALQKDLDNKLFGQHLAKKIIL
SQ  NAVFGFINNPKPKKPLTLSLHGWTGTGKNFVSKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQLWIRGNVS
SQ  ACARSIFIFDEMDKMHAGLIDAIKPFLDYYDLVDGVSYQKAIFIFLSNAGAERITDVALDFWRSGKQREDIKLKDIEHAL
SQ  SVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYETNEDIVSRVAEEMTFFPKEERVFSDKGCK
SQ  TVFTKLDYYYDD
//
ID  Q9ER39;
PN  Torsin-1A;
GN  Tor1a;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O14656}. Nucleus membrane; Peripheral membrane protein. Cell projection, growth cone. Cytoplasmic vesicle membrane {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}. Note=Upon oxidative stress, redistributes to protusions from the cell surface (By similarity). Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus membrane is mediated by the interaction with TOR1AIP2. {ECO:0000250}.
DR  UNIPROT: Q9ER39;
DR  PDB: 6FV0;
DR  Pfam: PF06309;
DE  Function: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non- neural tissues. {ECO:0000269|PubMed:16364897, ECO:0000269|PubMed:17200151, ECO:0000269|PubMed:17428918, ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:20457914}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005856;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0042406;
GO  GO:0030426;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0030141;
GO  GO:0008021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0140662;
GO  GO:0008092;
GO  GO:0042802;
GO  GO:0019894;
GO  GO:0051787;
GO  GO:0051082;
GO  GO:0007155;
GO  GO:0051085;
GO  GO:0061077;
GO  GO:0071712;
GO  GO:0045104;
GO  GO:0031175;
GO  GO:0006998;
GO  GO:0071763;
GO  GO:0006996;
GO  GO:1900244;
GO  GO:0000338;
GO  GO:0034504;
GO  GO:0051584;
GO  GO:2000008;
GO  GO:0006979;
GO  GO:0048499;
GO  GO:0048489;
GO  GO:0044319;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MKLGRAALALLLLAPCVVRAVEPISLSLALAGVLTTYISYPRLYCLFAECCGQMRSLSREALQKDLDNKLFGQHLAKKVI
SQ  LNAVSGFLSNPKPKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLNSDYVHLFVATLHFPHASNITQYKDQLQMWIRGNV
SQ  SACARSIFIFDEMDKMHAGLIDAIKPFLDYYDVVDEVSYQKAIFIFLSNAGAERITDVALDFWKSGKQREEIKLRDMEPA
SQ  LAVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYEVDEDIISKVAEEMTFFPKEEKVFSDKGC
SQ  KTVFTKLDYYLDD
//
ID  Q68G38;
PN  Torsin-1A;
GN  Tor1a;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O14656}. Nucleus inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, growth cone. Cytoplasmic vesicle membrane. Cytoplasmic vesicle, secretory vesicle. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Note=Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus envelope is mediated by the interaction with TOR1AIP2. Upon oxidative stress, redistributes to protusions from the cell surface.
DR  UNIPROT: Q68G38;
DR  UNIPROT: Q8K3L8;
DR  Pfam: PF06309;
DE  Function: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non- neural tissues (By similarity). {ECO:0000250|UniProtKB:O14656}.
DE  Reference Proteome: Yes;
DE  Interaction: Q68FS2; IntAct: EBI-8514670; Score: 0.43
DE  Interaction: D4AB66; IntAct: EBI-8514703; Score: 0.35
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0030659;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0042406;
GO  GO:0030426;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0043005;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0030141;
GO  GO:0008021;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0140662;
GO  GO:0008092;
GO  GO:0042802;
GO  GO:0019894;
GO  GO:0051787;
GO  GO:0051082;
GO  GO:0007155;
GO  GO:0051085;
GO  GO:0061077;
GO  GO:0071712;
GO  GO:0045104;
GO  GO:0031175;
GO  GO:0006998;
GO  GO:0071763;
GO  GO:0006996;
GO  GO:1900244;
GO  GO:0000338;
GO  GO:0034504;
GO  GO:0051584;
GO  GO:2000008;
GO  GO:0006979;
GO  GO:0048499;
GO  GO:0048489;
GO  GO:0044319;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MKLGRATLALLLLVPCVVRAVEPISLGLALAGVLTGYISYPRLYCLFAECCGQKRSLSREALQKDLDNKLFGQHLAKRVI
SQ  LNAVSGFLSNPKPKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQMWIRGNV
SQ  SACARSIFIFDEMDKMHAGLIDAIKPFLDYYDVVDEVSYQKAIFIFLSNAGAERITDVALDFWRSGKQREEIKLRDMEHA
SQ  LAVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYEEDEDIINKVAEEMTFFPKEEKVFSDKGC
SQ  KTVFTKLDYYLDD
//
ID  O14657;
PN  Torsin-1B;
GN  TOR1B;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15147511}. Nucleus membrane {ECO:0000269|PubMed:15147511}.
DR  UNIPROT: O14657;
DR  Pfam: PF06309;
DR  OMIM: 608050;
DR  DisGeNET: 27348;
DE  Function: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non- neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. {ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647}.
DE  Reference Proteome: Yes;
DE  Interaction: P16104; IntAct: EBI-2564373; Score: 0.35
DE  Interaction: A2APR8; IntAct: EBI-11001201; Score: 0.35
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: A4D1S0; IntAct: EBI-21511461; Score: 0.35
DE  Interaction: P20036; IntAct: EBI-21511890; Score: 0.35
DE  Interaction: Q9UBM8; IntAct: EBI-21514186; Score: 0.35
DE  Interaction: P32971; IntAct: EBI-21604933; Score: 0.35
DE  Interaction: Q9NRD1; IntAct: EBI-21685297; Score: 0.35
DE  Interaction: Q9UG22; IntAct: EBI-21694248; Score: 0.35
DE  Interaction: P29016; IntAct: EBI-21693940; Score: 0.35
DE  Interaction: Q9BRR6; IntAct: EBI-21694151; Score: 0.35
DE  Interaction: Q9H3K2; IntAct: EBI-21899782; Score: 0.35
DE  Interaction: Q9H0V9; IntAct: EBI-21899782; Score: 0.35
DE  Interaction: Q5JTV8; IntAct: EBI-15853118; Score: 0.40
DE  Interaction: P0DTC3; IntAct: EBI-25686340; Score: 0.35
DE  Interaction: P0DTC8; IntAct: EBI-25687968; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-27050247; Score: 0.35
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0070062;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0042802;
GO  GO:0019894;
GO  GO:0051085;
GO  GO:0007029;
GO  GO:0071763;
GO  GO:0034504;
GO  GO:0006986;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLRAGWLRGAAALALLLAARVVAAFEPITVGLAIGAASAITGYLSYNDIYCRFAECCREERPLNASALKLDLEEKLFGQH
SQ  LATEVIFKALTGFRNNKNPKKPLTLSLHGWAGTGKNFVSQIVAENLHPKGLKSNFVHLFVSTLHFPHEQKIKLYQDQLQK
SQ  WIRGNVSACANSVFIFDEMDKLHPGIIDAIKPFLDYYEQVDGVSYRKAIFIFLSNAGGDLITKTALDFWRAGRKREDIQL
SQ  KDLEPVLSVGVFNNKHSGLWHSGLIDKNLIDYFIPFLPLEYRHVKMCVRAEMRARGSAIDEDIVTRVAEEMTFFPRDEKI
SQ  YSDKGCKTVQSRLDFH
//
ID  Q9ER41;
PN  Torsin-1B;
GN  Tor1b;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum lumen. Nucleus membrane.
DR  UNIPROT: Q9ER41;
DR  UNIPROT: Q8VEI4;
DR  Pfam: PF06309;
DE  Function: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non- neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. {ECO:0000269|PubMed:20457914}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005788;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0042802;
GO  GO:0019894;
GO  GO:0051085;
GO  GO:0007029;
GO  GO:0071763;
GO  GO:0034504;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRRIGAFGGSTALWALLAAHVAGAFEPVSVGIAIGAVSALTGYLSYTDFYCRFTECCHEERPLNTSALKLDLEEKLFGQH
SQ  LATEVILKALTGFRNNKNSKKPLTLSLHGWAGTGKNFISQIVAENLYPKGLKSNFVHLFVSTLHFPHEQKIKVYQDQLQK
SQ  WIRGNVSACGSSVFIFDEMDKLHPGIIDAIKPFLDYYEQVDGISYRRAIFIFLSNAGGDLITKTALDFWRAGRKREEIQL
SQ  KDLEPVLSVGVFNNKHSGLWHSGLIDKNLIDYFIPFLPLEYKHVKMCVRAEMRARGAAVDEDVVTSVADEMTFFPKDEKI
SQ  YSDKGCKTVQSRLDFH
//
ID  Q8TEL6;
PN  Short transient receptor potential channel 4-associated protein;
GN  TRPC4AP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:26038816}.
DR  UNIPROT: Q8TEL6;
DR  UNIPROT: E1P5Q0;
DR  UNIPROT: E1P5Q1;
DR  UNIPROT: Q96H82;
DR  UNIPROT: Q9BVB8;
DR  UNIPROT: Q9H429;
DR  UNIPROT: Q9UFS6;
DR  Pfam: PF12463;
DR  OMIM: 608430;
DR  DisGeNET: 26133;
DE  Function: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control (PubMed:20551172, PubMed:29779948). The DCX(TRPC4AP) complex specifically mediates the polyubiquitination and subsequent degradation of MYC as part of the DesCEND (destruction via C-end degrons) pathway (PubMed:20551172, PubMed:29779948). The DesCEND (destruction via C-end degrons) pathway recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948). The DCX(TRPC4AP) complex specifically recognizes proteins with an arginine at the minus 3 position (R-3 motif) at the C-terminus, such as MYC, leading to their ubiquitination and degradation (PubMed:29779948). Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome (By similarity). Involved in JNK activation via its interaction with TRAF2 (By similarity). Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1 (By similarity). {ECO:0000250|UniProtKB:Q9JLV2, ECO:0000269|PubMed:20551172, ECO:0000269|PubMed:29779948}.
DE  Reference Proteome: Yes;
DE  Interaction: O43633; IntAct: EBI-11512033; Score: 0.37
DE  Interaction: P12931; IntAct: EBI-28931938; Score: 0.35
DE  Interaction: Q7L5N1; IntAct: EBI-21332205; Score: 0.35
DE  Interaction: Q12933; IntAct: EBI-8591290; Score: 0.40
DE  Interaction: Q3U1J4; IntAct: EBI-2559059; Score: 0.40
DE  Interaction: A0A4Y1W4N6; IntAct: EBI-2810106; Score: 0.00
DE  Interaction: Q15750; IntAct: EBI-7200047; Score: 0.37
DE  Interaction: P62136; IntAct: EBI-5238123; Score: 0.54
DE  Interaction: Q13619; IntAct: EBI-21324822; Score: 0.53
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q13620; IntAct: EBI-21332812; Score: 0.35
DE  Interaction: Q9WH76; IntAct: EBI-10823934; Score: 0.37
DE  Interaction: Q96CF2; IntAct: EBI-11510809; Score: 0.37
DE  Interaction: Q7LBR1; IntAct: EBI-11511928; Score: 0.37
DE  Interaction: Q9NZZ3; IntAct: EBI-11512563; Score: 0.37
DE  Interaction: Q96FZ7; IntAct: EBI-11512619; Score: 0.37
DE  Interaction: Q13049; IntAct: EBI-12452491; Score: 0.51
DE  Interaction: Q13509; IntAct: EBI-11897134; Score: 0.35
DE  Interaction: Q9Y6Y8; IntAct: EBI-11942723; Score: 0.00
DE  Interaction: Q17RF5; IntAct: EBI-21556823; Score: 0.35
DE  Interaction: Q9Y520; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q9HCM4; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q9BYW2; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q9BW61; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q99590; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q96SY0; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q8IWU5; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q7Z6E9; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q6B0I6; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q16531; IntAct: EBI-15821456; Score: 0.41
DE  Interaction: Q16204; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q15788; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q15751; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: Q07866; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: P48634; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: P46940; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: O95297; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: O75052; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: O43148; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: A6NHR9; IntAct: EBI-21558423; Score: 0.35
DE  Interaction: P13727; IntAct: EBI-21570605; Score: 0.35
DE  Interaction: Q9H9P5; IntAct: EBI-21622067; Score: 0.35
DE  Interaction: Q8WV16; IntAct: EBI-30863977; Score: 0.35
GO  GO:0080008;
GO  GO:0031464;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005262;
GO  GO:0019902;
GO  GO:1990756;
GO  GO:0070588;
GO  GO:0048820;
GO  GO:0016567;
GO  GO:0006511;
GO  GO:0140627;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAPVAAGSGAGRGRRSAATVAAWGGWGGRPRPGNILLQLRQGQLTGRGLVRAVQFTETFLTERDKQSKWSGIPQLLLK
SQ  LHTTSHLHSDFVECQNILKEISPLLSMEAMAFVTEERKLTQETTYPNTYIFDLFGGVDLLVEILMRPTISIRGQKLKISD
SQ  EMSKDCLSILYNTCVCTEGVTKRLAEKNDFVIFLFTLMTSKKTFLQTATLIEDILGVKKEMIRLDEVPNLSSLVSNFDQQ
SQ  QLANFCRILAVTISEMDTGNDDKHTLLAKNAQQKKSLSLGPSAAEINQAALLSIPGFVERLCKLATRKVSESTGTASFLQ
SQ  ELEEWYTWLDNALVLDALMRVANEESEHNQASIVFPPPGASEENGLPHTSARTQLPQSMKIMHEIMYKLEVLYVLCVLLM
SQ  GRQRNQVHRMIAEFKLIPGLNNLFDKLIWRKHSASALVLHGHNQNCDCSPDITLKIQFLRLLQSFSDHHENKYLLLNNQE
SQ  LNELSAISLKANIPEVEAVLNTDRSLVCDGKRGLLTRLLQVMKKEPAESSFRFWQARAVESFLRGTTSYADQMFLLKRGL
SQ  LEHILYCIVDSECKSRDVLQSYFDLLGELMKFNVDAFKRFNKYINTDAKFQVFLKQINSSLVDSNMLVRCVTLSLDRFEN
SQ  QVDMKVAEVLSECRLLAYISQVPTQMSFLFRLINIIHVQTLTQENVSCLNTSLVILMLARRKERLPLYLRLLQRMEHSKK
SQ  YPGFLLNNFHNLLRFWQQHYLHKDKDSTCLENSSCISFSYWKETVSILLNPDRQSPSALVSYIEEPYMDIDRDFTEE
//
ID  Q9JLV2;
PN  Short transient receptor potential channel 4-associated protein;
GN  Trpc4ap;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEL6}.
DR  UNIPROT: Q9JLV2;
DR  UNIPROT: Q920J6;
DR  UNIPROT: Q99L03;
DR  Pfam: PF12463;
DE  Function: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control. The DCX(TRPC4AP) complex specifically mediates the polyubiquitination and subsequent degradation of MYC as part of the DesCEND (destruction via C-end degrons) pathway. The DesCEND (destruction via C-end degrons) pathway recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The DCX(TRPC4AP) complex specifically recognizes proteins with an arginine at the minus 3 position (R-3 motif) at the C-terminus, such as MYC, leading to their ubiquitination and degradation (By similarity). Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome (PubMed:14585990). Involved in JNK activation via its interaction with TRAF2 (PubMed:16876162). Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1 (PubMed:20458742). {ECO:0000250|UniProtKB:Q8TEL6, ECO:0000269|PubMed:14585990, ECO:0000269|PubMed:16876162, ECO:0000269|PubMed:20458742}.
DE  Reference Proteome: Yes;
GO  GO:0080008;
GO  GO:0031464;
GO  GO:0048471;
GO  GO:0019902;
GO  GO:1990756;
GO  GO:0048820;
GO  GO:0016567;
GO  GO:0006511;
GO  GO:0140627;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAAAPAAAGAGASRGRRLAATAAAWGGWGGRPRPGNILLQLRQGQLTGRGLVRAVQFTETFLTERDKLSKWSGIPQLLLK
SQ  LYATSHLHSDFVECQSILKEISPLLSMEAMAFVTEDRKFTQEATYPNTYIFDLFGGVDLLVEILMRPTISIRGQKLKISD
SQ  EMSKDCLSILYNTCVCTEGVTKRLAEKNDFVIFLFTLMTSKKTFLQTATLIEDILGVKKEMIRLDEVPNLSSLVSNFDQQ
SQ  QLANFCRILAVTISEMDTGNDDKHTLLAKNAQQKKSLSLGPSAAEINQAALLSIPGFVERLCKLATRKVSESTGTASFLQ
SQ  ELEEWYTWLDNALVLDALMRVANEESEHNQAPTVFPSLGTSEEGGLPHTSARAQLPQSMKIMHEIMYKLEVLYVLCVLLM
SQ  GRQRNQVHRMIAEFKLIPGLNNLFDKLIWRKHSASALVLHGHNQNCDCSPDITLKIQFLRLLQSFSDHHENKYLLLNNQE
SQ  LNELSAISLKANIPEVEAVLNTDRSLVCDGKRGLLTRLLQVMKKEPAESSFRFWQARAVESFLRGTTSYADQMFLLKRGL
SQ  LEHILYCIVDSECKSRDVLQSYFDLLGELMKFNVDAFKRFNKYINTDAKFQVFLKQINSSLVDSNMLVRCVTLSLDRFEN
SQ  QVDMKVAEVLSECRLLAYISQVPTQMSFLFRLINIIHVQTLTQENVSCLNTSLVILMLARRKERLPLYLRLLQRMEHSKK
SQ  YPGFLLNNFHNLLRFWQQHYLHKDKDSTCLENSSCISFSYWKETVSILLNPDRQSPSALVSYIEEPYMDIDRDFTEE
//
ID  P0DI81;
PN  Trafficking protein particle complex subunit 2;
GN  TRAPPC2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11031107}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:11031107}. Nucleus {ECO:0000269|PubMed:20498720, ECO:0000269|PubMed:25918224}. Cytoplasm {ECO:0000269|PubMed:20498720}. Note=Localized in perinuclear granular structures. {ECO:0000269|PubMed:11031107}.
DR  UNIPROT: P0DI81;
DR  UNIPROT: A6NEG0;
DR  UNIPROT: O14582;
DR  UNIPROT: Q9HD16;
DR  Pfam: PF04628;
DR  OMIM: 300202;
DR  OMIM: 313400;
DR  DisGeNET: 6399;
DE  Function: Prevents transcriptional repression and induction of cell death by ENO1 (By similarity). May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Disease: Spondyloepiphyseal dysplasia tarda (SEDT) [MIM:313400]: X- linked recessive disorder of endochondral bone formation. {ECO:0000269|PubMed:10431248, ECO:0000269|PubMed:11349230, ECO:0000269|PubMed:11424925}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q96D71; IntAct: EBI-5663368; Score: 0.00
DE  Interaction: Q8N0Z2; IntAct: EBI-5665355; Score: 0.00
DE  Interaction: Q99613; IntAct: EBI-5665372; Score: 0.00
DE  Interaction: P06733; IntAct: EBI-5665390; Score: 0.00
DE  Interaction: P13929; IntAct: EBI-5665408; Score: 0.00
DE  Interaction: P13747; IntAct: EBI-5665426; Score: 0.00
DE  Interaction: P11217; IntAct: EBI-5665443; Score: 0.00
DE  Interaction: Q8NAP3; IntAct: EBI-5665460; Score: 0.00
DE  Interaction: Q96QF0; IntAct: EBI-6160950; Score: 0.56
DE  Interaction: Q8IWZ5; IntAct: EBI-10196871; Score: 0.56
DE  Interaction: Q719H9; IntAct: EBI-10196881; Score: 0.56
DE  Interaction: Q9UBC2; IntAct: EBI-10196892; Score: 0.56
DE  Interaction: Q9UGI0; IntAct: EBI-24301535; Score: 0.56
DE  Interaction: O96006; IntAct: EBI-24336124; Score: 0.56
DE  Interaction: P62310; IntAct: EBI-24664064; Score: 0.56
DE  Interaction: Q96N21; IntAct: EBI-24682524; Score: 0.56
DE  Interaction: Q8WWY6; IntAct: EBI-24684454; Score: 0.56
DE  Interaction: Q7Z4V0; IntAct: EBI-24690041; Score: 0.56
DE  Interaction: Q8N720; IntAct: EBI-24735925; Score: 0.56
DE  Interaction: Q9BSH3; IntAct: EBI-24749602; Score: 0.56
DE  Interaction: O00746; IntAct: EBI-23833628; Score: 0.56
DE  Interaction: O43617; IntAct: EBI-24445453; Score: 0.56
DE  Interaction: Q8IUR0; IntAct: EBI-24560567; Score: 0.56
DE  Interaction: Q9BRT2; IntAct: EBI-24786192; Score: 0.56
DE  Interaction: O75971; IntAct: EBI-24378081; Score: 0.56
DE  Interaction: Q3KQZ1; IntAct: EBI-24543570; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-24641604; Score: 0.56
DE  Interaction: Q8TAC2; IntAct: EBI-25151367; Score: 0.56
DE  Interaction: P53355; IntAct: EBI-20589345; Score: 0.44
DE  Interaction: Q9Y4C4; IntAct: EBI-20590888; Score: 0.44
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0043231;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:1990071;
GO  GO:1990072;
GO  GO:0044325;
GO  GO:0048208;
GO  GO:0006888;
GO  GO:0001501;
GO  GO:0006901;
GO  GO:0099022;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH
SQ  MRFIMLHDIRQEDGIKNFFTDVYDLYIKFSMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS
//
ID  P0DI82;
PN  Trafficking protein particle complex subunit 2B;
GN  TRAPPC2B;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11134351}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniProtKB:P0DI81}.
DR  UNIPROT: P0DI82;
DR  UNIPROT: A6NEG0;
DR  UNIPROT: O14582;
DR  UNIPROT: Q9HD16;
DR  Pfam: PF04628;
DR  DisGeNET: 6399;
DE  Function: Prevents transcriptional repression and induction of cell death by ENO1. May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:11134351}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A286YCX6; IntAct: EBI-11119288; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0043231;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:1990071;
GO  GO:1990072;
GO  GO:0001222;
GO  GO:0140416;
GO  GO:0048208;
GO  GO:0006888;
GO  GO:0010628;
GO  GO:0006901;
GO  GO:0099022;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH
SQ  MRFIMLHDIRQEDGIKNFFTDVYDLYIKFSMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS
//
ID  A6H7F7;
PN  Trafficking protein particle complex subunit 2-like protein;
GN  TRAPPC2L;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: A6H7F7;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVCVAVIAKENYPLYIRSIPTENELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKF
SQ  VMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSRAFDGMVTSMMIQVC
//
ID  Q9UL33;
PN  Trafficking protein particle complex subunit 2-like protein;
GN  TRAPPC2L;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19416478}. Endoplasmic reticulum {ECO:0000269|PubMed:19416478}. Golgi apparatus {ECO:0000269|PubMed:19416478}.
DR  UNIPROT: Q9UL33;
DR  UNIPROT: B2R4M9;
DR  UNIPROT: Q6ZTA7;
DR  UNIPROT: Q9NZZ4;
DR  Pfam: PF04628;
DR  OMIM: 610970;
DR  OMIM: 618331;
DR  DisGeNET: 51693;
DE  Function: Plays a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:19416478, ECO:0000269|PubMed:30120216}.
DE  Disease: Encephalopathy, progressive, early-onset, with episodic rhabdomyolysis (PEERB) [MIM:618331]: An autosomal recessive disease characterized by progressive encephalopathy exacerbated by febrile illness and associated with severe neurodevelopmental delay, episodes of rhabdomyolysis, developmental regression, epilepsy and tetraplegia. {ECO:0000269|PubMed:30120216}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P16278; IntAct: EBI-21692555; Score: 0.35
DE  Interaction: O43617; IntAct: EBI-755932; Score: 0.84
DE  Interaction: Q15063; IntAct: EBI-7067116; Score: 0.37
DE  Interaction: Q8NFH8; IntAct: EBI-7067203; Score: 0.37
DE  Interaction: P28838; IntAct: EBI-7067185; Score: 0.37
DE  Interaction: Q8NHS9; IntAct: EBI-7067302; Score: 0.37
DE  Interaction: Q8K3V1; IntAct: EBI-7067418; Score: 0.40
DE  Interaction: Q96QF0; IntAct: EBI-6160492; Score: 0.64
DE  Interaction: Q9Y2L5; IntAct: EBI-6550448; Score: 0.40
DE  Interaction: A5PLN9; IntAct: EBI-6550413; Score: 0.40
DE  Interaction: Q96D71; IntAct: EBI-10284496; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-10323488; Score: 0.56
DE  Interaction: P15884; IntAct: EBI-10323478; Score: 0.56
DE  Interaction: Q15654; IntAct: EBI-10323498; Score: 0.56
DE  Interaction: Q8IYX8; IntAct: EBI-10323512; Score: 0.56
DE  Interaction: Q9H2G9; IntAct: EBI-10323524; Score: 0.56
DE  Interaction: B2RXC1; IntAct: EBI-11119206; Score: 0.35
DE  Interaction: A0A286YCX6; IntAct: EBI-11119288; Score: 0.35
DE  Interaction: Q9NW68; IntAct: EBI-24509590; Score: 0.56
DE  Interaction: Q9H3H3; IntAct: EBI-24398603; Score: 0.56
DE  Interaction: O75865; IntAct: EBI-24609194; Score: 0.56
DE  Interaction: B2RXF5; IntAct: EBI-24625568; Score: 0.56
DE  Interaction: Q8TAP4; IntAct: EBI-24677401; Score: 0.56
DE  Interaction: P62487; IntAct: EBI-24715130; Score: 0.56
DE  Interaction: Q16385; IntAct: EBI-24717724; Score: 0.56
DE  Interaction: P50458; IntAct: EBI-24396478; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24449258; Score: 0.56
DE  Interaction: P50221; IntAct: EBI-24453529; Score: 0.56
DE  Interaction: Q15276; IntAct: EBI-24458111; Score: 0.56
DE  Interaction: O95872; IntAct: EBI-24592542; Score: 0.56
DE  Interaction: P80188; IntAct: EBI-24596447; Score: 0.56
DE  Interaction: A8MW99; IntAct: EBI-25216104; Score: 0.56
DE  Interaction: P48553; IntAct: EBI-11908313; Score: 0.00
DE  Interaction: Q8IYB1; IntAct: EBI-11921722; Score: 0.00
DE  Interaction: Q9NR12; IntAct: EBI-11933610; Score: 0.00
DE  Interaction: Q9Y5R8; IntAct: EBI-21546787; Score: 0.35
DE  Interaction: Q9Y296; IntAct: EBI-11938327; Score: 0.00
DE  Interaction: Q96Q05; IntAct: EBI-11938309; Score: 0.00
DE  Interaction: Q8TBN0; IntAct: EBI-11938300; Score: 0.00
DE  Interaction: Q8N9M5; IntAct: EBI-11938291; Score: 0.00
DE  Interaction: Q8IUR0; IntAct: EBI-21546443; Score: 0.35
DE  Interaction: Q9P2M4; IntAct: EBI-21546672; Score: 0.35
DE  Interaction: Q9BZR8; IntAct: EBI-21693005; Score: 0.35
DE  Interaction: Q96KC9; IntAct: EBI-21692950; Score: 0.35
DE  Interaction: Q8WVT3; IntAct: EBI-21756916; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: P09613; IntAct: EBI-21497303; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0043231;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:1990071;
GO  GO:1990072;
GO  GO:0048208;
GO  GO:0006888;
GO  GO:0006901;
GO  GO:0099022;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVCIAVIAKENYPLYIRSTPTENELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKF
SQ  VMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSSRAFDNMVTSMMIQVC
//
ID  Q9JME7;
PN  Trafficking protein particle complex subunit 2-like protein;
GN  Trappc2l;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: Q9JME7;
DR  UNIPROT: A4FUI9;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q96QF0; IntAct: EBI-6160656; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0043231;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:1990071;
GO  GO:1990072;
GO  GO:0048208;
GO  GO:0006888;
GO  GO:0006901;
GO  GO:0099022;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVCIAVIAKENYPLYIRSTPTESELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKF
SQ  VMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSRAFDTMVTSMMIQVC
//
ID  Q5RBK9;
PN  Trafficking protein particle complex subunit 2-like protein;
GN  TRAPPC2L;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: Q5RBK9;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVCIAVIAKENYPLYIRSTPTENKLKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKMFRKLHNSYTDV
SQ  MCNPFYNPGDRIQSRAFDNMVTSMMIQVC
//
ID  B2RYU6;
PN  Trafficking protein particle complex subunit 2-like protein;
GN  Trappc2l;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: B2RYU6;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVCIAVIAKENYPLYIRSTPTENELKFHYMVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKF
SQ  VMVVDSSNTALRDNEIRSMFRKLHNSYTDVMCNPFYNPGDRIQSRAFDTMVTSMMVQVC
//
ID  B5XGE7;
PN  Trafficking protein particle complex subunit 2-like protein;
GN  trappc2l;
OS  8030;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: B5XGE7;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVCIAVIAKENYPLYIRSVPVQNELKFHYTVHTSLDVVEEKISAVGKAMADQRELYLGLLYPTEDYKVYGYVTNSKVKF
SQ  VIVVDSSNTSLRDNEIRSMFRKLHNSFTDVMCNPFYNPGDTIQSKAFDSMVSAMMVQAS
//
ID  B5FXJ6;
PN  Trafficking protein particle complex subunit 2-like protein;
GN  TRAPPC2L;
OS  59729;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: B5FXJ6;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVCIAVIAKENYPLYIRSVPTENELKFHYTVHTSLDVVDEKISAMGKALVDQRELYLGLLYPTEDYKVYGYVTNSKVKF
SQ  VMVVDSSNTALRDNEIRSMFRKLHNSYTDIMCNPFYNPGDRIHSRAFDTMVNSMMMQVC
//
ID  Q5M8X5;
PN  Trafficking protein particle complex subunit 2-like protein;
GN  trappc2l;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: Q5M8X5;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAVCVAVIAKENYPLYIRSTPTENQLKFHYTVHTSLDVVDEKISAMGKAVMDQRELYLGLLYPTEDYKVYGYVTNSKVKF
SQ  VMVVDSSNTSLRDNEIRSMFRKLHNSYTDVMCNPFYNPGDPIQSRAFDNTVTSMMVPAC
//
ID  Q3T0F2;
PN  Trafficking protein particle complex subunit 2;
GN  TRAPPC2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DI81}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniProtKB:P0DI81}.
DR  UNIPROT: Q3T0F2;
DR  Pfam: PF04628;
DE  Function: Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P19711; IntAct: EBI-9524539; Score: 0.37
DE  Interaction: P21530; IntAct: EBI-9524533; Score: 0.37
GO  GO:0005737;
GO  GO:0005793;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH
SQ  MRFIMLHDVRQEDGIKNFFTDVYDLYIKFAMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS
//
ID  O02173;
PN  Probable trafficking protein particle complex subunit 2;
GN  sedl;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: O02173;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. Required for the systemic spread of the RNAi response. {ECO:0000269|PubMed:16862146}.
DE  Reference Proteome: Yes;
DE  Interaction: P34605; IntAct: EBI-367959; Score: 0.37
DE  Interaction: Q9NA81; IntAct: EBI-367962; Score: 0.62
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATKEFYFAIIGHCDQPIFEMDFPVGEKKTKESEGTRHLNHYIGHAALDIVDEHALTTSQMYLKMVDKFNEWYVSAFVTA
SQ  SRIRFIMLHTHRADEGIKQFFQEMYETYIKHAMNPFYEIDDVIESPAFEQKATLYGRKYLS
//
ID  E2QV03;
PN  Trafficking protein particle complex subunit 2;
GN  TRAPPC2;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DI81}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniProtKB:P0DI81}.
DR  UNIPROT: E2QV03;
DR  Pfam: PF04628;
DE  Function: Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005793;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH
SQ  MRFIMLHDIRQEDGIKNFFTDVYDLYIKFAMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS
//
ID  Q5ZKP4;
PN  Trafficking protein particle complex subunit 2;
GN  TRAPPC2;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DI81}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniProtKB:P0DI81}.
DR  UNIPROT: Q5ZKP4;
DR  UNIPROT: F1NGQ4;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005793;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVIVGHHDNPVFEMEFLPPGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFAFVLH
SQ  MRFIMLHDVRQEDGIKNFFNDVYDLYIKFAMNPFYELNSPIRSSAFERKVQFLGKKHLLS
//
ID  Q08CN0;
PN  Trafficking protein particle complex subunit 2;
GN  trappc2;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DI81}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniProtKB:P0DI81}.
DR  UNIPROT: Q08CN0;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005793;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVMVGHHDNPVFELEFLPPGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH
SQ  MRFIMLHDVRQEDGIKNFFNDVYDLYVKFAMNPFYEVNAPIRSTAFERKVQFLGKKHLLS
//
ID  Q54RV6;
PN  Trafficking protein particle complex subunit 2;
GN  trappc2;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: Q54RV6;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTFTFLIIGKNDNPLYEIEFPITVQKKETYVLQYIAHGSLDIVEEHVWKSNNMYLKIIDKFNKVQISSFVTAGHIKFLL
SQ  LHEKKDEDAIKNFFVEVHDLYLKILLNPFYEYNKPITSTAFDAKVRKIGTKYF
//
ID  Q9VUZ1;
PN  Probable trafficking protein particle complex subunit 2;
GN  Trs20;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P0DI81}. Golgi apparatus {ECO:0000250|UniProtKB:P0DI81}.
DR  UNIPROT: Q9VUZ1;
DR  UNIPROT: Q8SYG9;
DR  PDB: 7B6D;
DR  PDB: 7B6R;
DR  PDB: 7B6X;
DR  PDB: 7B70;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. Involved in dsRNA uptake. {ECO:0000269|PubMed:16862146}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7K2Q8; IntAct: EBI-26749051; Score: 0.62
DE  Interaction: Q9VZG0; IntAct: EBI-240962; Score: 0.00
DE  Interaction: Q9VSY8; IntAct: EBI-26812302; Score: 0.49
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:1990071;
GO  GO:1990072;
GO  GO:0033227;
GO  GO:0006888;
GO  GO:0048193;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSTYYFVIVGQNDNPIYEKEFSTVNKELRKEDHRHLTQFIAHAALDLVDEHKWKTANMQLKSIDRFNQWFVSAFITASQI
SQ  RFIIVHDNKNDEGIKNFFNEMYDTYIKNSMNAFYRINTPIKSPMFEKKSEIFGRKYLLS
//
ID  Q9CQP2;
PN  Trafficking protein particle complex subunit 2;
GN  Trappc2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19650763}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000269|PubMed:19650763}. Note=Localized in perinuclear granular structures. {ECO:0000269|PubMed:19650763}.
DR  UNIPROT: Q9CQP2;
DR  UNIPROT: Q8BP61;
DR  UNIPROT: Q9CQF5;
DR  UNIPROT: Q9D0V3;
DR  UNIPROT: Q9DCM3;
DR  PDB: 1H3Q;
DR  PDB: 2J3W;
DR  Pfam: PF04628;
DE  Function: Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: O55013; IntAct: EBI-1172679; Score: 0.59
DE  Interaction: P28838; IntAct: EBI-7066983; Score: 0.37
DE  Interaction: Q8NFH8; IntAct: EBI-7067048; Score: 0.37
DE  Interaction: Q15063; IntAct: EBI-7067065; Score: 0.37
DE  Interaction: O43617; IntAct: EBI-7067168; Score: 0.37
DE  Interaction: Q8NHS9; IntAct: EBI-7067283; Score: 0.37
DE  Interaction: Q8NEY3; IntAct: EBI-7067237; Score: 0.37
DE  Interaction: Q8K3V1; IntAct: EBI-7067370; Score: 0.60
DE  Interaction: Q96QF0; IntAct: EBI-6160656; Score: 0.35
DE  Interaction: Q96Q05; IntAct: EBI-20591376; Score: 0.40
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0043231;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:1990071;
GO  GO:1990072;
GO  GO:0001222;
GO  GO:0044325;
GO  GO:0048208;
GO  GO:0006888;
GO  GO:0010628;
GO  GO:0001501;
GO  GO:0006901;
GO  GO:0099022;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVIVGHHDNPVFEMEFLPPGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH
SQ  MRFIMLHDVRQEDGIKNFFTDVYDLYIKFAMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS
//
ID  A7RVK7;
PN  Probable trafficking protein particle complex subunit 2;
GN  v1g94938;
OS  45351;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.
DR  UNIPROT: A7RVK7;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MLGNYYFAIVGHYDNPVYEKEFNQQMKMDSNDHRHLNQFIVHAALDLVDESMWGTTGMYLKSVDKFNEWFVSAFDPPLSW
SQ  IIDPQFFLDLTSWMRFMMLHDVKNDDGIKNFFSDVYETFIKVLMNPFYEINSKIKSANFDKKVLLAAKKHILP
//
ID  F1SRI0;
PN  Trafficking protein particle complex subunit 2;
GN  TRAPPC2;
OS  9823;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DI81}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniProtKB:P0DI81}.
DR  UNIPROT: F1SRI0;
DR  Pfam: PF04628;
DE  Function: Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005793;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH
SQ  MRFIMLHDVRQEDGIKNFFTDVYDLYIKFAMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS
//
ID  Q5RES6;
PN  Trafficking protein particle complex subunit 2;
GN  TRAPPC2;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DI81}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniProtKB:P0DI81}.
DR  UNIPROT: Q5RES6;
DR  Pfam: PF04628;
DE  Function: Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005793;
GO  GO:0005640;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0001222;
GO  GO:0140416;
GO  GO:0006888;
GO  GO:0010628;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH
SQ  MRFIMLHDVRQEDGIKNFFTDVYDLYIKFSMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS
//
ID  D3ZVF4;
PN  Trafficking protein particle complex subunit 2;
GN  Trappc2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DI81}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniProtKB:P0DI81}.
DR  UNIPROT: D3ZVF4;
DR  Pfam: PF04628;
DE  Function: Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005793;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVIVGHHDNPVFEMEFLPAGKTESKDEHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH
SQ  MRLIMLHDVRQEDGIKNFFTDVYDLYIKFAMNPFYEPNSPIRSTAFERKVQFLGKKHLLS
//
ID  Q28IG8;
PN  Trafficking protein particle complex subunit 2;
GN  trappc2;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DI81}. Nucleus {ECO:0000250|UniProtKB:P0DI81}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm {ECO:0000250|UniProtKB:P0DI81}. Note=Localized in perinuclear granular structures. {ECO:0000250|UniProtKB:P0DI81}.
DR  UNIPROT: Q28IG8;
DR  Pfam: PF04628;
DE  Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005793;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030008;
GO  GO:0006888;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGSFYFVIVGHHDNPVFEMEFLPQGKTESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGH
SQ  MRFIMLHDVRQEDGIKNFFNEAYDLYIKFAMNPFYEINSPLRSTAFDRKIQFLGKKHLLS
//
ID  A1Z8P9;
PN  Nucleoprotein TPR;
GN  Mtor;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526}. Nucleus matrix {ECO:0000269|PubMed:9152019}. Nucleus lamina {ECO:0000269|PubMed:15356261}. Nucleus envelope {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:9152019}. Nucleus membrane {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:22855526}; Peripheral membrane protein {ECO:0000305}; Nucleoplasmic side {ECO:0000269|PubMed:12027452}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:22855526, ECO:0000269|PubMed:31913420, ECO:0000269|PubMed:9152019}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:22855526}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19273613}. Midbody {ECO:0000269|PubMed:15356261}. Note=In interphase, localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket (PubMed:15356261). Enriched at the nuclear lamina and at intranuclear spaces surrounding the chromosomes and the nucleolus (PubMed:15356261, PubMed:15962301). Colocalized with hnRNPs and snRNPs at a single heat shock puff during heat shock (PubMed:12027452). Reorganized during mitosis in a viscous and dynamic nuclear-derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner (PubMed:15356261). In prometaphase, localized at the spindle (PubMed:15356261). Localized to spindle midbody at telophase (PubMed:15356261). Recruited to the reforming nuclear envelope in early G1 (PubMed:15356261). Colocalized with Skeletor, Chro and east at the spindle matrix (PubMed:15356261, PubMed:15962301, PubMed:19273613, PubMed:22855526). Colocalized with Mad2 at the spindle matrix and kinetochore (PubMed:19273613). Associated with chromatin (PubMed:20174442). {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:15962301, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526}.
DR  UNIPROT: A1Z8P9;
DR  UNIPROT: O01385;
DR  Pfam: PF07926;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (PubMed:9152019). Functions as a scaffolding element in the nuclear phase of the NPC (PubMed:12027452, PubMed:15356261). Plays a role in chromosomal organization and gene expression regulation; stimulates transcription by promoting the formation of an open chromatin environment (PubMed:12027452, PubMed:20174442). Binds chromatin to nucleoporin-associated regions (NARs) that define transcriptionally active regions of the genome (PubMed:20174442). Associates with extended chromosomal regions that alternate between domains of high density binding with those of low occupancy (PubMed:20174442). Preferentially binds to NARs of the male X chromosome (PubMed:20174442). In males, together with Nup153, required for the localization of the male-specific lethal (MSL) histone acetyltransferase complex to the X chromosome and therefore for the transcription of dosage compensation genes (PubMed:16543150). In males, restrains dosage-compensated expression at the level of nascent transcription probably by interacting with the MSL complex and by modulating RNA Polymerase II phosphorylation status and activity (PubMed:34133927). During mitosis forms a gel-like spindle matrix complex together with Skeletor, Chro, east, and Asator embedding the microtubule spindle apparatus (PubMed:15356261, PubMed:15962301, PubMed:19273613, PubMed:22855526). During interphase localizes Mad1 to the nuclear pore complex and thereby might act as a scaffold to assemble the Mad1-C-Mad2 complex, an heterotetramer that catalyzes the structural conversion of open-Mad2 (O-Mad2) into closed-Mad2 (C-Mad2) which is essential for spindle-assembly checkpoint (SAC) (PubMed:31913420). During the metaphase-anaphase transition and before chromosome congression, is phosphorylated by Msp-1; this modification releases Mad1 from the nuclear pore complex and thereby promotes assembly of SAC ensuring a timely and effective recruitment of spindle checkpoint proteins like Mad1, Mad2 and Mps1 to unattached kinetochores (KT) (PubMed:22855526, PubMed:26714316, PubMed:31913420). In testes, has a role in stem cell asymmetric division and maintenance via regulation of mitotic spindle assembly checkpoint (SAC) complex (PubMed:26714316). {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:15962301, ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526, ECO:0000269|PubMed:26714316, ECO:0000269|PubMed:31913420, ECO:0000269|PubMed:34133927, ECO:0000269|PubMed:9152019}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VNZ7; IntAct: EBI-212088; Score: 0.00
DE  Interaction: Q9W1M6; IntAct: EBI-277787; Score: 0.00
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: Q7JQU5; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q9VBD5; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: C7LA76; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q9BIS2; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: P54623; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q8IRG6; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q7KV88; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q9VFA8; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q9VWF7; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q9VG87; IntAct: EBI-9943666; Score: 0.35
DE  Interaction: Q9VXU3; IntAct: EBI-9943666; Score: 0.35
DE  Interaction: Q24238; IntAct: EBI-9943666; Score: 0.35
DE  Interaction: Q9VDR4; IntAct: EBI-9943666; Score: 0.35
DE  Interaction: Q9W1X5; IntAct: EBI-9943666; Score: 0.35
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0000791;
GO  GO:0070090;
GO  GO:0030496;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:1990047;
GO  GO:0051233;
GO  GO:0031490;
GO  GO:0035035;
GO  GO:0043021;
GO  GO:0017056;
GO  GO:0006325;
GO  GO:0006338;
GO  GO:0007549;
GO  GO:0060250;
GO  GO:0048133;
GO  GO:0007094;
GO  GO:0000022;
GO  GO:0006406;
GO  GO:0000122;
GO  GO:0051781;
GO  GO:0090316;
GO  GO:0090267;
GO  GO:0045840;
GO  GO:0045944;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0090235;
GO  GO:0007346;
GO  GO:0010965;
GO  GO:1901673;
GO  GO:0060236;
GO  GO:0034976;
GO  GO:0009408;
GO  GO:0051225;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MDLSGPQTLNNILQPDELKLVPEDVQKKLSEYINNFSDEYCKNRAAANRLAEAEQKKEELENKMEDYLVKFTSFELNVNE
SQ  LRTHLDQMSSERVNLMDTIAKGEQTISQLRKEKASVVEERDSMMKVIERQQAELERLKQDLHTYQQQLSSAIAAKCEAIA
SQ  RVDEIQSKEVALELKENRMESERDMLHKEILLISGDLNKSNAELQNIRREHTINTMQLQSCLKEKTESLKLMQEQYEQAV
SQ  KTIGELTSKIEMQNDTAFKQNQATEEYVGKLKKELDAKEKLFEIFKSTESDHLIQREELLQGISEIKRLLEEAEEQCAQL
SQ  TEQMETMKQKHSAELDEQNKKIQAMEQELASANDLLKQARESNLESAICQLAPSAAVASRLIRSDLSLTELYSMYAKSSE
SQ  ELEMRNCEIEQLKLQLKSIIAEISESAPILEKQNSDYQKMKETNSELLREHDELLQNKLCLERELERALSTLNHNQNENK
SQ  KLKQTHTDLSRQVCMLLDELNCIRAGVKHVRIQPTRQLPTSESLISDNLVTFSSIEELVDRNTYLLNMSRELTELLEASE
SQ  KNQDKMLLEQSKNHIRKLDARFAELEDLLTQKNNTVTTLLSKCDRYKKLYFAAQKKLGQNTVDLDDSNLEPNDSALDTSE
SQ  QPAANFEESRKLEKRVRQLEQQLEGEVKKYASLKENYDYYTSEKRKNDALAQEQFDSMRKEVRELTSSNCKLMNTTEFQK
SQ  EQIELLHKNIGTYKQQVTTLEERTKNYEKTIIKHEQTVHLLKDEMMAAHRKHAAADAEAQSLRQENRILRDTSSRLQIEK
SQ  ETYHREQQSQSLLLNSLEFIKTNLERSEMEGRQRLEQRLDDTVRELAAQRRHFQEEEEKFRESINEFKRQAETAIKLKDE
SQ  EKQLADKWQAELTSVREELAEKVNKVNELSKKLQEVLTPTLNDNPITAANKRAREFELKLDQATVEIESLTKELAKTREH
SQ  GEQFYKMSQSAESEIKRLHELHGELVAKQEEEIKKLRSSEAELKTRISDLEAEAMLSNVTEQSKTVNQSGQLKSAQDDLK
SQ  SLLEKLTEANCTIRTLRSENTSLVESLNAAEVKYANGMIQHSADIQELTRYKAEFFKANDELNQLKSGRESLQAAYDELL
SQ  RSNAEAQKLLDKEREESEKRVADLHALNSNLHDQIEALASKLAVLASQSQNPNSSLNESAMDGDQSLNASGLTAAEEGRN
SQ  NEQLLKIIKFLRKEKDLFAAKLDILKAENARLISEHAIQQKKVDELNGYLNQERAKSQTDVVSANKHEEVLRKIETLNAI
SQ  TDSNRILREERNALTLRVAELTDRISSVEKELFPLQCSNKELTSKIEEINVENTSLRTEAIKWRQRANALVEKSNRNPEE
SQ  FKRLQAEREHLAKLLTAEKELNKKQSDELTVLKQRMNTEIPMLNKQMQILDEARKKQVDEFTNLKQNNTRQTQDIMELKN
SQ  RLLQKEEELLKANEELETKDKTIADKETKELQLRKLAKRYKDFYIGLQSQGGGTESAAELEKVRSELEEVNNQLRALKDE
SQ  HEKITKECDEVKKRTEPETDTSAIRQEYKAKLDKLVVDLTVARTDLVNQETTFAGTKSSYDETIARLEKELQENIAANKD
SQ  INQRLTRENESLHMRINQLTRQLGSQQSTKPSTSSVAEKGNISESSPRTANVKPMSGSATVQQSATVTPWRGGETPLASI
SQ  RPISVQNSRTAAILPTSQQPPAGSSTSTSSSSSSSSTSTTSAAGGGSSAVAQTALVPPQQQVHTTGSAALESMASSSPTS
SQ  SHTDYMPSTSSASVAVAAIPPMGASSAAESSQEAESIQHPQQNDSQLFVGGAQQQVVALVSPRVEGSSSSSSSTSVPTAT
SQ  APSIQDGGSQSQQPSTSGSSSSSSTVVSSHSRHTPSSSNVTTTQAGCSSQGIKRPRDIEGDSSTGTEEGVAEKMSKITKR
SQ  LRGPMHSGELSAGHIGDSGMDVDQMPTSSQRDQEDDIQVVDSDDEEDVLADADDGPIDGGEAEQEGYEDSYEQDNEMDDN
SQ  EGGDDDNDIAVDAQDNNEVDIEVPEQHMQAQEESQSLDNQAIATASASTQENNQSQAITSGSGESSNPVTLPQAEASNWK
SQ  QAAASTSTAAARRNESSVEIVSSPQVSNFCEQPARLESAEVDGTAEVAGGAPHESAGPSDTGAASASSPQKQSEAGESSG
SQ  SDALKAADDGGDHADGTDNAREADEAFAEETMATGQGEDSQPLGNDNPNVGTSQSEVSHNQANLGEGNPTEDSEGADGVS
SQ  SEGEKQAVGVEEEGREAEATSPSENTRFRTLRSAVPTRRGHRAMRGGSPNSQNRPQRIVWQRDTSPGNIQQNQMSANNNR
SQ  FAQRTRNRRPIRRPPPNNFNNGGRFP
//
ID  P12270;
PN  Nucleoprotein TPR;
GN  TPR;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:12802065}. Nucleus membrane {ECO:0000269|PubMed:11514627, ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:18794356, ECO:0000269|PubMed:9024684, ECO:0000269|PubMed:9828100, ECO:0000269|PubMed:9864356}; Peripheral membrane protein {ECO:0000269|PubMed:11514627, ECO:0000269|PubMed:9024684, ECO:0000269|PubMed:9828100, ECO:0000269|PubMed:9864356}; Nucleoplasmic side {ECO:0000269|PubMed:11514627, ECO:0000269|PubMed:9024684, ECO:0000269|PubMed:9828100, ECO:0000269|PubMed:9864356}. Nucleus envelope {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:7798308}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11514627, ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:7798308, ECO:0000269|PubMed:9024684, ECO:0000269|PubMed:9828100, ECO:0000269|PubMed:9864356}. Cytoplasm {ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:12802065}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19273613}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:18981471}. Nucleus membrane {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:7798308}; Peripheral membrane protein {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:7798308}; Cytoplasmic side {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:7798308}. Note=Detected as discrete intranuclear foci with IFI204 (By similarity). In interphase, localizes to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Detected exclusively to the cytoplasmic margin of NPC (PubMed:7798308). Docking to the inner nucleoplasmic side of the NPC is mediated through binding to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other components, including p62. Detected as filaments that emanate from the nuclear basket of the NPC and extend to the nucleolus to delineate a chromatin-free network extending from the nuclear envelope to the perinucleolar region. Detected in diffuse and discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling protein imported into the nucleus in a XPO1/CRM1- and Importin alpha/Importin beta receptor-dependent manner. Remains localized to the nuclear membrane after poliovirus (PV) infection. During mitosis, remains associated with the nuclear envelope until prometaphase. Associated with the mitotic spindle from late prometaphase until anaphase. Reorganized during mitosis in a viscous and dynamic nuclear- derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner. Recruited to the reforming nuclear envelope during telophase and cytokinesis. Detected at kinetochores during prometaphase (PubMed:18981471). Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore (PubMed:19273613). Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle. {ECO:0000250, ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:7798308}.
DR  UNIPROT: P12270;
DR  UNIPROT: Q15624;
DR  UNIPROT: Q15655;
DR  UNIPROT: Q5SWY0;
DR  UNIPROT: Q99968;
DR  PDB: 5TO5;
DR  PDB: 5TO6;
DR  PDB: 5TO7;
DR  PDB: 5TVB;
DR  Pfam: PF07926;
DR  OMIM: 189940;
DR  DisGeNET: 7175;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress- induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:22253824 and PubMed:11952838). Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC- associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases. {ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:18794356, ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:20407419, ECO:0000269|PubMed:21613532, ECO:0000269|PubMed:22253824, ECO:0000269|PubMed:9864356}.
DE  Disease: Note=A chromosomal aberration involving TPR has been found in papillary thyroid carcinomas (PTCs). Intrachromosomal rearrangement that links the 5'-end of the TPR gene to the protein kinase domain of NTRK1 forms the fusion protein TRK-T1. TRK-T1 is a 55 kDa protein reacting with antibodies against the carboxy terminus of the NTRK1 protein. {ECO:0000269|PubMed:1532241}. Note=Involved in tumorigenic rearrangements with the MET. {ECO:0000269|PubMed:2300559}.
DE  Reference Proteome: Yes;
DE  Interaction: P02545; IntAct: EBI-16795953; Score: 0.35
DE  Interaction: Q9Y4K3; IntAct: EBI-1083198; Score: 0.00
DE  Interaction: Q7M739; IntAct: EBI-2555904; Score: 0.40
DE  Interaction: Q9QWT9; IntAct: EBI-2558911; Score: 0.40
DE  Interaction: Q9Z1B5; IntAct: EBI-2560653; Score: 0.56
DE  Interaction: P01100; IntAct: EBI-2687382; Score: 0.00
DE  Interaction: Q15796; IntAct: EBI-2688217; Score: 0.00
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q9H492; IntAct: EBI-3044058; Score: 0.35
DE  Interaction: P25054; IntAct: EBI-3437664; Score: 0.00
DE  Interaction: Q9Y6R4; IntAct: EBI-3443161; Score: 0.00
DE  Interaction: O95931; IntAct: EBI-3951830; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-6191068; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q5S007; IntAct: EBI-6515052; Score: 0.53
DE  Interaction: Q9UKV0; IntAct: EBI-6598230; Score: 0.35
DE  Interaction: Q12834; IntAct: EBI-9636923; Score: 0.35
DE  Interaction: Q9Y6D9; IntAct: EBI-9521828; Score: 0.52
DE  Interaction: Q15637; IntAct: EBI-11299773; Score: 0.00
DE  Interaction: Q01167; IntAct: EBI-11318541; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: E9PZI6; IntAct: EBI-11147599; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11160436; Score: 0.35
DE  Interaction: O96017; IntAct: EBI-11579031; Score: 0.35
DE  Interaction: Q8NFH4; IntAct: EBI-11888966; Score: 0.37
DE  Interaction: P29074; IntAct: EBI-14024958; Score: 0.35
DE  Interaction: Q8WTR2; IntAct: EBI-14027225; Score: 0.35
DE  Interaction: Q86WB0; IntAct: EBI-21849097; Score: 0.35
DE  Interaction: O76064; IntAct: EBI-16182639; Score: 0.35
DE  Interaction: Q01968; IntAct: EBI-16412116; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16789004; Score: 0.35
DE  Interaction: P50613; IntAct: EBI-16790014; Score: 0.35
DE  Interaction: P20339; IntAct: EBI-16798290; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800982; Score: 0.35
DE  Interaction: P68431; IntAct: EBI-16794028; Score: 0.27
DE  Interaction: P08559; IntAct: EBI-20306509; Score: 0.35
DE  Interaction: P31040; IntAct: EBI-20306992; Score: 0.35
DE  Interaction: P00441; IntAct: EBI-20307497; Score: 0.35
DE  Interaction: Q86WV6; IntAct: EBI-20201357; Score: 0.35
DE  Interaction: Q49MG5; IntAct: EBI-20918876; Score: 0.40
DE  Interaction: P11387; IntAct: EBI-20923490; Score: 0.40
DE  Interaction: Q99583; IntAct: EBI-20923882; Score: 0.40
DE  Interaction: Q6ZNB6; IntAct: EBI-20924442; Score: 0.40
DE  Interaction: P17568; IntAct: EBI-20924706; Score: 0.40
DE  Interaction: Q8WWQ0; IntAct: EBI-20926906; Score: 0.40
DE  Interaction: Q96PN6; IntAct: EBI-20930080; Score: 0.40
DE  Interaction: Q8TF20; IntAct: EBI-20930176; Score: 0.40
DE  Interaction: P05166; IntAct: EBI-20933692; Score: 0.40
DE  Interaction: P49146; IntAct: EBI-20934748; Score: 0.40
DE  Interaction: Q96J65; IntAct: EBI-20934676; Score: 0.40
DE  Interaction: Q8WUJ0; IntAct: EBI-21945299; Score: 0.35
DE  Interaction: Q02750; IntAct: EBI-25382666; Score: 0.35
DE  Interaction: Q8NF50; IntAct: EBI-25409278; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: P0DTC6; IntAct: EBI-26495724; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: P14240; IntAct: EBI-26968430; Score: 0.35
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: P46108; IntAct: EBI-30819856; Score: 0.44
DE  Interaction: Q93009; IntAct: EBI-30841377; Score: 0.44
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0019898;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0031072;
GO  GO:0051019;
GO  GO:0003729;
GO  GO:0042803;
GO  GO:0003723;
GO  GO:0017056;
GO  GO:0015631;
GO  GO:0051301;
GO  GO:0034605;
GO  GO:0035457;
GO  GO:0007094;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0046832;
GO  GO:0000122;
GO  GO:0045947;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0031453;
GO  GO:0090316;
GO  GO:0090267;
GO  GO:0046827;
GO  GO:0042307;
GO  GO:0006606;
GO  GO:0010965;
GO  GO:1901673;
GO  GO:0032880;
GO  GO:0070849;
GO  GO:0006405;
GO  GO:0006404;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAAVLQQVLERTELNKLPKSVQNKLEKFLADQQSEIDGLKGRHEKFKVESEQQYFEIEKRLSHSQERLVNETRECQSLRL
SQ  ELEKLNNQLKALTEKNKELEIAQDRNIAIQSQFTRTKEELEAEKRDLIRTNERLSQELEYLTEDVKRLNEKLKESNTTKG
SQ  ELQLKLDELQASDVSVKYREKRLEQEKELLHSQNTWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVSRLEEQM
SQ  NGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVEELHKLLKEAGEA
SQ  NKAIQDHLLEVEQSKDQMEKEMLEKIGRLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYN
SQ  AYVETQDQLLLEKLENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSVKLEQAMKEIQRLQEDTDKANKQSS
SQ  VLERDNRRMEIQVKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLVALREL
SQ  GETREREEQETTSSKITELQLKLESALTELEQLRKSRQHQMQLVDSIVRQRDMYRILLSQTTGVAIPLHASSLDDVSLAS
SQ  TPKRPSTSQTVSTPAPVPVIESTEAIEAKAALKQLQEIFENYKKEKAENEKIQNEQLEKLQEQVTDLRSQNTKISTQLDF
SQ  ASKRYEMLQDNVEGYRREITSLHERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQ
SQ  QRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLSSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQL
SQ  DTETNLHLNTKELLKNAQKEIATLKQHLSNMEVQVASQSSQRTGKGQPSNKEDVDDLVSQLRQTEEQVNDLKERLKTSTS
SQ  NVEQYQAMVTSLEESLNKEKQVTEEVRKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRRAIESMEQQLSELKKTL
SQ  SSVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMASVRQHLEETTQKA
SQ  ESQLLECKASWEERERMLKDEVSKCVCRCEDLEKQNRLLHDQIEKLSDKVVASVKEGVQGPLNVSLSEEGKSQEQILEIL
SQ  RFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLR
SQ  EEKERLEQDLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQHLVSQQKDPDTEEYRKLLSE
SQ  KEVHTKRIQQLTEEIGRLKAEIARSNASLTNNQNLIQSLKEDLNKVRTEKETIQKDLDAKIIDIQEKVKTITQVKKIGRR
SQ  YKTQYEELKAQQDKVMETSAQSSGDHQEQHVSVQEMQELKETLNQAETKSKSLESQVENLQKTLSEKETEARNLQEQTVQ
SQ  LQSELSRLRQDLQDRTTQEEQLRQQITEKEEKTRKAIVAAKSKIAHLAGVKDQLTKENEELKQRNGALDQQKDELDVRIT
SQ  ALKSQYEGRISRLERELREHQERHLEQRDEPQEPSNKVPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSK
SQ  VTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGSTSGSVRSTSPNVQPSIS
SQ  QPILTVQQQTQATAFVQPTQQSHPQIEPANQELSSNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTI
SQ  EASDQVSDDTVEMPLPKKLKSVTPVGTEEEVMAEESTDGEVETQVYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDL
SQ  GPLQSDQQTTTSSQDGQGKGDDVIVIDSDDEEEDDDENDGEHEDYEEDEEDDDDDEDDTGMGDEGEDSNEGTGSADGNDG
SQ  YEADDAEGGDGTDPGTETEESMGGGEGNHRAADSQNSGEGNTGAAESSFSQEVSREQQPSSASERQAPRAPQSPRRPPHP
SQ  LPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAG
SQ  VPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQS
SQ  VPMVTTSTGTLSTTNETATGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQP
SQ  KPFRRVRLQTTLRQGVRGRQFNRQRGVSHAMGGRGGINRGNIN
//
ID  F6ZDS4;
PN  Nucleoprotein TPR;
GN  Tpr;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side {ECO:0000250|UniProtKB:P12270}. Nucleus envelope {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:12513910}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P12270, ECO:0000269|PubMed:12513910}. Cytoplasm {ECO:0000250|UniProtKB:P12270}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P12270}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side {ECO:0000250|UniProtKB:P12270}. Note=Detected as discrete intranuclear foci with IFI204 (By similarity). In interphase, localizes to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Detected exclusively to the cytoplasmic margin of NPC (By similarity). Docking to the inner nucleoplasmic side of the NPC is mediated through binding to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other components, including p62. Detected as filaments that emanate from the nuclear basket of the NPC and extend to the nucleolus to delineate a chromatin-free network extending from the nuclear envelope to the perinucleolar region. Detected in diffuse and discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling protein imported into the nucleus in a XPO1/CRM1- and Importin alpha/Importin beta receptor-dependent manner. Remains localized to the nuclear membrane after poliovirus (PV) infection. During mitosis, remains associated with the nuclear envelope until prometaphase. Associated with the mitotic spindle from late prometaphase until anaphase. Reorganized during mitosis in a viscous and dynamic nuclear- derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner. Recruited to the reforming nuclear envelope during telophase and cytokinesis. Detected at kinetochores during prometaphase. Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore. Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12270}.
DR  UNIPROT: F6ZDS4;
DR  UNIPROT: Q8R4A0;
DR  UNIPROT: Q921B9;
DR  Pfam: PF07926;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress- induced conditions. Plays a limited role in the regulation of nuclear protein export. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC- associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0019898;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0031072;
GO  GO:0051019;
GO  GO:0003729;
GO  GO:0042803;
GO  GO:0017056;
GO  GO:0015631;
GO  GO:0051301;
GO  GO:0034605;
GO  GO:0035457;
GO  GO:0007094;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0046832;
GO  GO:0000122;
GO  GO:0045947;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0031453;
GO  GO:0090316;
GO  GO:0090267;
GO  GO:0046827;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0010965;
GO  GO:1901673;
GO  GO:0032880;
GO  GO:0070849;
GO  GO:0006405;
GO  GO:0006404;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P12270};
SQ  MTSGGSASRSGHRGVPMTSRGFDGSRRGSLRRAGARETASEAADGAAPAAGLRASPCSLASPSAAAAVAAIPADMAAVLQ
SQ  QVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVTETRECQNLRLELEKLN
SQ  NQVKVLTEKTKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKL
SQ  DELQASDVAVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVLRLEEQMNGLKTS
SQ  NEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEANKTIQD
SQ  HLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQ
SQ  DQLLLEKQENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSSVLERDN
SQ  QRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALRELGETRER
SQ  EEQETTSSKIAELQHKLENSLAELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLLSTPKRSS
SQ  TSQTVSTPAPEPVIDSTEAIEAKAALKQLQEIFENYKKEKIDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYE
SQ  MLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLL
SQ  AEQRGQNLLLTNLQTIQGILERSETETKQRLNSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTEINL
SQ  HLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSTSNVEQYR
SQ  AMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLSELKKTLSTVQNE
SQ  VQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMTSIRQHLEETTQKAESQLLE
SQ  CKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKDAVQAPLNVSLNEEGKSQEQILEILRFIRRE
SQ  KEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNVEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERL
SQ  EQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQQLINQQKDPDTEEYRKLLSEKEIHTK
SQ  RIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLREDLSKARTEKEGIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQFE
SQ  ELKAQQNKAMETSTQSSGDHQEQHISVQEMQELKDTLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTVQLQSELS
SQ  RLRQDLQDKTTEEQLRQQMNEKTWKTLALAKSKITHLSGVKDQLTKEIEELKQRNGALDQQKDELDVRMTALKSQYEGRI
SQ  SRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNK
SQ  STPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGNASGSVRSTSPNVQPSISQPILTVQQQT
SQ  QATAFVQPTQQSHPQIEPTNQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTMEAGDQVSEDT
SQ  VEMPLPKKLKMVTPVGTEEEVMAEESTDGEAETQAYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTT
SQ  SSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDDDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGT
SQ  DPGTETEESMGGAESHQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPPRLTIHAPPQ
SQ  ELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDM
SQ  PQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLS
SQ  TTNETAAGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTL
SQ  RQGVRGRQFNRQRGISHAMGGRGGINRGNIN
//
ID  F1MA98;
PN  Nucleoprotein TPR;
GN  Tpr;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side {ECO:0000250|UniProtKB:P12270}. Nucleus envelope {ECO:0000250|UniProtKB:P12270}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11839768}. Cytoplasm {ECO:0000250|UniProtKB:P12270}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P12270}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side {ECO:0000250|UniProtKB:P12270}. Note=Detected as discrete intranuclear foci with IFI204 (By similarity). In interphase, localizes to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Detected exclusively to the cytoplasmic margin of NPC (By similarity). Docking to the inner nucleoplasmic side of the NPC is mediated through binding to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other components, including p62. Detected as filaments that emanate from the nuclear basket of the NPC and extend to the nucleolus to delineate a chromatin-free network extending from the nuclear envelope to the perinucleolar region. Detected in diffuse and discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling protein imported into the nucleus in a XPO1/CRM1- and Importin alpha/Importin beta receptor-dependent manner. Remains localized to the nuclear membrane after poliovirus (PV) infection. During mitosis, remains associated with the nuclear envelope until prometaphase. Associated with the mitotic spindle from late prometaphase until anaphase. Reorganized during mitosis in a viscous and dynamic nuclear- derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner. Recruited to the reforming nuclear envelope during telophase and cytokinesis. Detected at kinetochores during prometaphase. Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore. Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12270}.
DR  UNIPROT: F1MA98;
DR  UNIPROT: Q3T1J7;
DR  Pfam: PF07926;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress- induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC- associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity). Plays a role in the regulation of nuclear protein export. {ECO:0000250, ECO:0000269|PubMed:11839768}.
DE  Reference Proteome: Yes;
DE  Interaction: P21708; IntAct: EBI-7625786; Score: 0.35
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0019898;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0031072;
GO  GO:0051019;
GO  GO:0003729;
GO  GO:0042803;
GO  GO:0017056;
GO  GO:0015631;
GO  GO:0051301;
GO  GO:0034605;
GO  GO:0035457;
GO  GO:0007094;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0046832;
GO  GO:0000122;
GO  GO:0045947;
GO  GO:0006999;
GO  GO:0031453;
GO  GO:0090316;
GO  GO:0090267;
GO  GO:0046827;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0010965;
GO  GO:1901673;
GO  GO:0032880;
GO  GO:0070849;
GO  GO:0006405;
GO  GO:0006404;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P12270};
SQ  MAAVLQQVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVNETRECQNLRL
SQ  ELEKLNNQVKVLTEKNKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKG
SQ  ELQLKLDELQASDVTVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCTLENKKEEVLRLEEQM
SQ  NGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEA
SQ  NKTIQDHLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYN
SQ  AYVETQDQLLLEKLENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSS
SQ  VLERDNQRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALREL
SQ  GETREREEQETTSSKIAELQNKLENSLTELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLVS
SQ  TPKRSSTSQTVSTPAPEPIIESTETIEAKAALKQLQEIFENYKKEKMDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDF
SQ  ASKRYEMLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQ
SQ  QRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLSSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQL
SQ  DTEINLHLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSAS
SQ  NVEQYRAMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLTELKKTL
SQ  SSVQSEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMASVRQHLEETTQKA
SQ  ESQLLECKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKEVVQSPLNISLNEEGKSQEQILEIL
SQ  RFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLR
SQ  EEKERLEQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQHLINQQKDPDTEEYRKLLSE
SQ  KEIHTKRIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLKEDLSKVRTEKESIQKDLDAKIIDIQEKVKTITQVKKIGRR
SQ  YKTQFEELKAQQKAMETSTQSSGDHQEQHISVQEMQELKDNLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTAQL
SQ  QSELSRLRQELQDKTTKEEQLRQQMNEKDEKTWKAITVARSKIAHLSGVKDQLTKENEELKQRNGALDQQKDELDVRMTA
SQ  LKSQYEGRISRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKV
SQ  TAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGSTSGSVRSTSPNVQPSISQ
SQ  PLLTVQQQTQATAFVQPTQQSHPQIEPANQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRAREEEEDSTIE
SQ  AGDQVSDDTVEMPLPKKLKTVTPVGTEEEVMAEESTDGEAETQTYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLG
SQ  PLQSDQQTTSSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDEDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEA
SQ  DDAEGGDGTDPGTETEESMGGAESNQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPP
SQ  RLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPR
SQ  FRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPM
SQ  VTTSTGTLSTTNETPAGDDGDEVFVETESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPF
SQ  RRVRLQTTLRQGVRGRQFNRQRGISHAMGGRGGINRGNIN
//
ID  Q5EE04;
PN  Nucleoprotein TPR;
GN  tpr;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side {ECO:0000250|UniProtKB:P12270, ECO:0000269|PubMed:9531546}. Nucleus envelope {ECO:0000250|UniProtKB:P12270}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:9024684}. Cytoplasm {ECO:0000250|UniProtKB:P12270}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P12270}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side {ECO:0000250|UniProtKB:P12270}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Localized to the nuclear periphery and in intranuclear spheroidal structures. Localized at NPC- attached intranuclear filament bundles projecting into the nuclear interior (PubMed:9024684). Colocalized with nup153 at the nuclear pore complex (PubMed:9531546). {ECO:0000269|PubMed:9024684, ECO:0000269|PubMed:9531546}.
DR  UNIPROT: Q5EE04;
DR  UNIPROT: P79992;
DR  Pfam: PF07926;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters. May play a limited role in the regulation of nuclear protein export. May be involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, may act as a spatial regulator of the spindle-assembly checkpoint (SAC) response (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0019898;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0003682;
GO  GO:0031072;
GO  GO:0051019;
GO  GO:0003729;
GO  GO:0042803;
GO  GO:0017056;
GO  GO:0051301;
GO  GO:0034605;
GO  GO:0007094;
GO  GO:0031990;
GO  GO:0046832;
GO  GO:0000122;
GO  GO:0045947;
GO  GO:0031453;
GO  GO:0090316;
GO  GO:0090267;
GO  GO:0046827;
GO  GO:0042307;
GO  GO:0006606;
GO  GO:0010965;
GO  GO:1901673;
GO  GO:0070849;
GO  GO:0006405;
GO  GO:0006404;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P12270};
SQ  QEQHSQLEAAKTQVEKDMGEKISNLERELENANDLLCSTKRKGVMLSEEELTAMSPTAAAVAKVVKPGMKLTELYNAYVE
SQ  TQDKLLMEKQENKRITKYLDEIVKEVEAKSPILKRQREEYERMQKTVASLSAKLEQAMREIQRMQDETDKANKCSSVLER
SQ  ENQRLELQIKDLSQQIRVLLMELEEARGNFVQRDDVSSANISSSSEVITQHLVTYRNIEELQQQNQRLLVALRELGEAKE
SQ  REEQESTSSRVSELEKELENALSELQQLREARSHQMTLVESIVRQRDMYRILLSQTTGVVLPAQDETALTSTPRKSPGVS
SQ  LDGSTSTPAAVVVSDSTEAAEARAALKQLQEVFENYRKEKAENDRMLNEQHDKLQEQVTELRSQNTKISTQLEFASKRYE
SQ  MLQDNVEGYRREITALQEKTQKLSATTQKQEQIINTLTHDLRAANEKLAVAEVRAENLKREKELLKMSEVRLTQERESLV
SQ  AEQRGQNLLLTNLQTIQVTLERSETEIKQRYNNQIEKLEQELAQTKKKLEHEIEQRHLLGKNQDVQVLELKKQYEMELNL
SQ  HNNTKELLKNSHKEISVLKQQLNSFELQLASRSSQQAANRDKDVNIEDVEEIKTKLRQSEELVNDLKERLKTATSNVEQY
SQ  RSVVLNLEESLNKEKQVTEEVRKTIEVRLKESSEYQSQLEKKMMESEKEKQELRDEKHKTVEQMEQQVTQLRQSLSSLQA
SQ  EVQQALQRATTSASNEQKAKQDCQEQARIAAEAQNKYERELMLHAADVEALQAAKKQLTSASAIRHKCEETAQKAGSQLL
SQ  ESRASWEERERMLKEEVSQIQSRCKDLEKQNGLLHEQIESLSKKMVTSVQEGALNMSFGEEGKSQEQVMEILRFVRREKE
SQ  IAEARFEVAQVECLRYRQRIEHMERELHELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVLIESNKILREENEKQEQ
SQ  ELQQLQAKIRKLESNILPLQESNAELSEKSGMLQAEKKLLEEDVRRWRARTQHLLSQQKDTDAEEYKKLLSEREVNTKRI
SQ  QQLTEETGKLKTEVARTNASLNTCQSQLQSVKDDLTKIKAEKEKLQKELDAKILDIQEKIKTITQVKKIGRRYKTQYEEL
SQ  KVTHDKMVAEASSAKADQLQEQASQKEVQELKDSLQRSEAKVTTMQTTVDNMQKTLDDKDNEIKEHQEQISRMQAELSHL
SQ  HKDLQDKTAQEEQMRQQINEKEEKTKKTLLVVRQKLAQNNGAKEQLTRENEDLKQKNANLEQQKEELEVRMSALRSQYDG
SQ  RISRLERELREQQERHHEQRDEPQETTRIPQQRQITLQPTTAAGERGSANTSEPPTANIKPTPSKVTTAAVPVNKSTPRA
SQ  SIRPMVTPAAVSTPTSTPTATVMPTTQVDQQEVQSEGQMEHVPVFGSASGSVRSTSPNVQSSLPQPILTLQQQTQTTAFV
SQ  QPTQQSHATIESPTQETPVEIVQSSPVERPTTSSTFGTYSATPSSSIPKRPREEEEDSTIETPEQIADDTDQQRTKKRKE
SQ  EDIEEKTETEAVINTEDALHILTQCSNMEFPLEEEIVESPIQTSQVIESQAPEQLQNVQSTQDSLQDTPPKKTHNLVIVI
SQ  SDEENEDEQEGYEEEEQEDEEEDEDDAGIGEGDDSNEETGSADGNEDYEGDDAEEADGTDPDTETEDSMTAGEGNQRAAD
SQ  SQNIGDSGVVTAESTFSQETREQPSSASDRQGPRPPQSPRRQAHPPRLTILAPPQELGPPPAQRIPVARRQSVGRGLQLT
SQ  PGVGGMQHFFDEEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQASSSHSDLGQLASQGGLGMYDTP
SQ  LFLAHEEESGGRSVPTTPLQVAAPVSVFAENPAADTSDHASQSVPMVTTSTGNVPTSVDSGAADEGDEVFVEAESEGIGA
SQ  ESTLEMDTQQEEPVQPSEADLPSTSQDPPSSSIADTSSSKPKPRRVWLQPQPGGRPFKRSRGGSDFRGRGGINRSNI
//
ID  Q2KIA2;
PN  Multifunctional methyltransferase subunit TRM112-like protein;
GN  TRMT112;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UI30}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UI30}. Note=Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes. {ECO:0000250|UniProtKB:Q9UI30}.
DR  UNIPROT: Q2KIA2;
DR  Pfam: PF03966;
DE  Function: Acts as an activator of both rRNA/tRNA and protein methyltransferases. Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA. The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on 'Gln-185', using S- adenosyl L-methionine as methyl donor. The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5- methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species. Together with methyltransferase THUMPD3, catalyzes the formation of N(2)-methylguanosine at position 6 in a broad range of tRNA substrates and at position 7 of tRNA(Trp) (By similarity). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production. Together with methyltransferase METTL5, specifically methylates the 6th position of adenine in position 1832 of 18S rRNA. {ECO:0000250|UniProtKB:Q9UI30}.
DE  Reference Proteome: Yes;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0046982;
GO  GO:0034968;
GO  GO:0018364;
GO  GO:2000234;
GO  GO:0070476;
GO  GO:0031167;
GO  GO:0030488;
GO  GO:0002940;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MRLLTHNLLSSHVRGVGPRGFPLRLQATEVRINPVEFNPDFIVRMIPKVEWAALLEAADHLHLIQVPKEPIQGYEHNEEF
SQ  LRKMHHVLLEVEVLEGTLQCPESGRVFPISRGIPNMLLSDEETET
//
ID  Q9UI30;
PN  Multifunctional methyltransferase subunit TRM112-like protein;
GN  TRMT112;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:25851604}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25851604}. Note=Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes (PubMed:25851604). {ECO:0000269|PubMed:25851604}.
DR  UNIPROT: Q9UI30;
DR  UNIPROT: B2R539;
DR  UNIPROT: J3KNG5;
DR  UNIPROT: Q3MHC7;
DR  UNIPROT: Q8N2Z4;
DR  PDB: 6G4W;
DR  PDB: 6H1D;
DR  PDB: 6H1E;
DR  PDB: 6H2U;
DR  PDB: 6H2V;
DR  PDB: 6K0X;
DR  PDB: 6KHS;
DR  PDB: 6KMR;
DR  PDB: 6KMS;
DR  PDB: 6PED;
DR  Pfam: PF03966;
DR  OMIM: 618630;
DR  DisGeNET: 51504;
DE  Function: Acts as an activator of both rRNA/tRNA and protein methyltransferases (PubMed:25851604, PubMed:18539146, PubMed:20308323, PubMed:25851604, PubMed:31328227, PubMed:31636962, PubMed:31061526). Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA (PubMed:25851604). The heterodimer with N6AMT1/HEMK2 catalyzes N5-methylation of ETF1 on 'Gln-185', using S- adenosyl L-methionine as methyl donor (PubMed:18539146, PubMed:31636962, PubMed:31061526). The heterodimer with N6AMT1/HEMK2 also monomethylates 'Lys-12' of histone H4 (H4K12me1) (PubMed:31061526). The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species (PubMed:20308323). Together with methyltransferase THUMPD3, catalyzes the formation of N(2)-methylguanosine at position 6 in a broad range of tRNA substrates and at position 7 of tRNA(Trp) (PubMed:34669960). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production (PubMed:25851604). Together with methyltransferase METTL5, specifically methylates the 6th position of adenine in position 1832 of 18S rRNA (PubMed:33428944, PubMed:35033535, PubMed:31328227). {ECO:0000269|PubMed:18539146, ECO:0000269|PubMed:20308323, ECO:0000269|PubMed:25851604, ECO:0000269|PubMed:31061526, ECO:0000269|PubMed:31328227, ECO:0000269|PubMed:31636962, ECO:0000269|PubMed:33428944, ECO:0000269|PubMed:34669960}.
DE  Reference Proteome: Yes;
DE  Interaction: O43709; IntAct: EBI-23853163; Score: 0.83
DE  Interaction: P0DTD1; IntAct: EBI-27030072; Score: 0.35
DE  Interaction: Q92900; IntAct: EBI-374151; Score: 0.00
DE  Interaction: Q9NX70; IntAct: EBI-394875; Score: 0.35
DE  Interaction: P40337; IntAct: EBI-1064475; Score: 0.00
DE  Interaction: P62330; IntAct: EBI-1066544; Score: 0.00
DE  Interaction: Q9UKE5; IntAct: EBI-1067751; Score: 0.00
DE  Interaction: O76081; IntAct: EBI-1072646; Score: 0.00
DE  Interaction: P23508; IntAct: EBI-1072670; Score: 0.00
DE  Interaction: Q14164; IntAct: EBI-1075070; Score: 0.00
DE  Interaction: Q9Y4K3; IntAct: EBI-1076545; Score: 0.00
DE  Interaction: Q9Y478; IntAct: EBI-1078230; Score: 0.00
DE  Interaction: P01889; IntAct: EBI-1079721; Score: 0.00
DE  Interaction: P11171; IntAct: EBI-1083784; Score: 0.00
DE  Interaction: Q9Y5N5; IntAct: EBI-7966690; Score: 0.75
DE  Interaction: P04591; IntAct: EBI-6174702; Score: 0.35
DE  Interaction: Q13617; IntAct: EBI-21327106; Score: 0.35
DE  Interaction: Q38SD2; IntAct: EBI-9659564; Score: 0.44
DE  Interaction: Q96BT7; IntAct: EBI-10825679; Score: 0.79
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: P23116; IntAct: EBI-11020127; Score: 0.35
DE  Interaction: P27635; IntAct: EBI-11035646; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: F8VQC1; IntAct: EBI-11054725; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: P06748; IntAct: EBI-11145880; Score: 0.35
DE  Interaction: P60229; IntAct: EBI-11148789; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-11153302; Score: 0.35
DE  Interaction: Q6FHY5; IntAct: EBI-24325034; Score: 0.56
DE  Interaction: Q9NRN9; IntAct: EBI-24675349; Score: 0.71
DE  Interaction: Q9BV44; IntAct: EBI-24643613; Score: 0.78
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q8IVT5; IntAct: EBI-14035332; Score: 0.35
DE  Interaction: Q7Z4G4; IntAct: EBI-30812343; Score: 0.54
DE  Interaction: Q14684; IntAct: EBI-16686997; Score: 0.35
DE  Interaction: P15311; IntAct: EBI-16791848; Score: 0.27
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q8K337; IntAct: EBI-25409748; Score: 0.35
DE  Interaction: O54834; IntAct: EBI-25411200; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25636144; Score: 0.35
DE  Interaction: Q01995; IntAct: EBI-26878675; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
DE  Interaction: Q9BTF0; IntAct: EBI-30812343; Score: 0.54
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0046982;
GO  GO:0008276;
GO  GO:0034968;
GO  GO:0018364;
GO  GO:2000234;
GO  GO:0070476;
GO  GO:0031167;
GO  GO:0030488;
GO  GO:0002940;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKLLTHNLLSSHVRGVGSRGFPLRLQATEVRICPVEFNPNFVARMIPKVEWSAFLEAADNLRLIQVPKGPVEGYEENEEF
SQ  LRTMHHLLLEVEVIEGTLQCPESGRMFPISRGIPNMLLSEEETES
//
ID  Q9DCG9;
PN  Multifunctional methyltransferase subunit TRM112-like protein;
GN  Trmt112;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UI30}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UI30}. Note=Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes. {ECO:0000250|UniProtKB:Q9UI30}.
DR  UNIPROT: Q9DCG9;
DR  UNIPROT: Q91YP8;
DR  UNIPROT: Q9D1N6;
DR  Pfam: PF03966;
DE  Function: Acts as an activator of both rRNA/tRNA and protein methyltransferases (PubMed:20606008, PubMed:26797129). Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA (By similarity). The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor (PubMed:20606008, PubMed:26797129). The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5- methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species (By similarity). Together with methyltransferase THUMPD3, catalyzes the formation of N(2)- methylguanosine at position 6 in a broad range of tRNA substrates and at position 7 of tRNA(Trp) (By similarity). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production (By similarity). Together with methyltransferase METTL5, specifically methylates the 6th position of adenine in position 1832 of 18S rRNA (By similarity). {ECO:0000250|UniProtKB:Q9UI30, ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:26797129}.
DE  Reference Proteome: Yes;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0046982;
GO  GO:0008276;
GO  GO:0034968;
GO  GO:0018364;
GO  GO:2000234;
GO  GO:0070476;
GO  GO:0031167;
GO  GO:0030488;
GO  GO:0002940;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKLLTHNLLSSHVRGVGTRGFPLRLQATEVRINPVEFNPEFVARMIPKVEWAALVQAADTLNLAEVPKEPTEGYEHDETF
SQ  LRKMHHVLLEVDVLEGTLQCPESGRLFPISRGIPNMLLNDEETET
//
ID  Q969Z4;
PN  Tumor necrosis factor receptor superfamily member 19L;
GN  RELT;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:16389068}; Single-pass type I membrane protein {ECO:0000269|PubMed:16389068}. Cytoplasm {ECO:0000269|PubMed:16389068}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22052202}.
DR  UNIPROT: Q969Z4;
DR  UNIPROT: Q86V34;
DR  UNIPROT: Q96JU1;
DR  UNIPROT: Q9BUX7;
DR  Pfam: PF12606;
DR  OMIM: 611211;
DR  OMIM: 618386;
DR  DisGeNET: 84957;
DE  Function: May play a role in apoptosis (PubMed:28688764, PubMed:19969290). Induces activation of MAPK14/p38 and MAPK8/JNK MAPK cascades, when overexpressed (PubMed:16530727). Involved in dental enamel formation (PubMed:30506946). {ECO:0000269|PubMed:16530727, ECO:0000269|PubMed:19969290, ECO:0000269|PubMed:28688764, ECO:0000269|PubMed:30506946}.
DE  Disease: Amelogenesis imperfecta 3C (AI3C) [MIM:618386]: An autosomal recessive form of amelogenesis imperfecta, a defect of enamel formation. AI3C is characterized by generalized enamel hypocalcification affecting primary and secondary dentition. The surface of the enamel is rough and often stained. After eruption, the occlusal enamel on the molars disappears due to attrition, leaving a ring of intact enamel remaining on the sides. {ECO:0000269|PubMed:30506946}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q9H8J5; IntAct: EBI-21537025; Score: 0.35
DE  Interaction: P04201; IntAct: EBI-21538834; Score: 0.35
DE  Interaction: Q96GQ5; IntAct: EBI-21549001; Score: 0.35
DE  Interaction: Q8NHX9; IntAct: EBI-21578009; Score: 0.35
DE  Interaction: Q9UEW8; IntAct: EBI-21648169; Score: 0.35
DE  Interaction: Q6WKZ4; IntAct: EBI-21648169; Score: 0.35
DE  Interaction: O95747; IntAct: EBI-21648169; Score: 0.35
DE  Interaction: O00154; IntAct: EBI-21648169; Score: 0.35
DE  Interaction: P37173; IntAct: EBI-21668347; Score: 0.35
DE  Interaction: A8MVW5; IntAct: EBI-21700110; Score: 0.35
DE  Interaction: P24394; IntAct: EBI-21800565; Score: 0.35
DE  Interaction: Q8NC24; IntAct: EBI-21817939; Score: 0.35
DE  Interaction: Q8NFM7; IntAct: EBI-21858188; Score: 0.35
GO  GO:0016021;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0097186;
GO  GO:0006915;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKPSLLCRPLSCFLMLLPWPLATLTSTTLWQCPPGEEPDLDPGQGTLCRPCPPGTFSAAWGSSPCQPHARCSLWRRLEAQ
SQ  VGMATRDTLCGDCWPGWFGPWGVPRVPCQPCSWAPLGTHGCDEWGRRARRGVEVAAGASSGGETRQPGNGTRAGGPEETA
SQ  AQYAVIAIVPVFCLMGLLGILVCNLLKRKGYHCTAHKEVGPGPGGGGSGINPAYRTEDANEDTIGVLVRLITEKKENAAA
SQ  LEELLKEYHSKQLVQTSHRPVSKLPPAPPNVPHICPHRHHLHTVQGLASLSGPCCSRCSQKKWPEVLLSPEAVAATTPVP
SQ  SLLPNPTRVPKAGAKAGRQGEITILSVGRFRVARIPEQRTSSMVSEVKTITEAGPSWGDLPDSPQPGLPPEQQALLGSGG
SQ  SRTKWLKPPAENKAEENRYVVRLSESNLVI
//
ID  Q9N092;
PN  Tumor necrosis factor receptor superfamily member 19L;
GN  RELT;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q969Z4}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q969Z4}.
DR  UNIPROT: Q9N092;
DR  Pfam: PF12606;
DE  Function: May play a role in apoptosis. Induces activation of MAPK14/p38 and MAPK8/JNK MAPK cascades, when overexpressed. Involved in dental enamel formation. {ECO:0000250|UniProtKB:Q969Z4}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0097186;
GO  GO:0006915;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKPSLLCRPLSCFLMLLPWPLATLTSTTLWQCPPGEEPDLNPGQGTLCRPCPPGTFSAAWGSSPCQPHARCSLQRRLEAQ
SQ  VGTATQDTLCGDCWPGWFGPWGVPRVPCQPCSWAPLGIHGCDEWGRRARRGVEVAAGASSGGETRQPGNGTRAGGPEETA
SQ  AQYAVIAIVPVFCLMGLLGILVCNLLKRKGYHCTAHKEVGPGPGGGGSGINPAYRTEDVNEDTIGVLVRLITEKKENAAA
SQ  LEELLKEYHSKQLVQTSHRPVSKLPPAPPNVPHICPHRHHLHTVQGLASLSGPCCSRCSQKKWPEVLLSPEAVAATTSAP
SQ  SFLPNPTRVPKAGAKAGRQGEITILSVGRFRVARIPEQRTGSMVSEVKTITEAGPSAGDLPDSPQPGLPAEQQALLGSGG
SQ  SHTKWLKPPAENKTEENRYVVRLSESNLVI
//
ID  Q8BX43;
PN  Tumor necrosis factor receptor superfamily member 19L;
GN  Relt;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q969Z4}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q969Z4}.
DR  UNIPROT: Q8BX43;
DR  UNIPROT: Q497Z8;
DR  UNIPROT: Q8BTV0;
DR  Pfam: PF12606;
DE  Function: May play a role in apoptosis. Induces activation of MAPK14/p38 and MAPK8/JNK MAPK cascades, when overexpressed. Involved in dental enamel formation (PubMed:30506946). {ECO:0000250|UniProtKB:Q969Z4, ECO:0000269|PubMed:30506946}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0097186;
GO  GO:0006915;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLQGLMMKRTLLCWPLSCLFVLLPWPLATPTPITPWLCPPGKEPDPDPGQGTLCRTCPPGTFSASWNSYPCQPHYRCSL
SQ  QKRLEAQAGTATHDTMCGDCQHGWFGPQGVPHVPCQPCSKAPPSTGGCDESGRRGRRGVEVAAGTSSNGEPRQPGNGTRA
SQ  GGPEETAAQYAVIAIVPVFCLMGLLGILVCNLLKRKGYHCTAQKEVGPSPGGGGSGINPAYRTEDANEDTIGVLVRLITE
SQ  KKENAAALEELLKEYHSKQLVQTSHRPVPRLLPASPSIPHICPHHHHLHTVQGLASLSGPCCSRCSQKWPEVLLSPEAAA
SQ  ATTPAPTLLPTASRAPKASAKPGRQGEITILSVGRFRVARIPEQRTSSLLSEVKTITEAGPSEGDLPDSPQPGLPPEQRA
SQ  LLGSGGSHTKWLKPPAENKAEENRYVVRLSESNLVI
//
ID  Q9BUZ4;
PN  TNF receptor-associated factor 4;
GN  TRAF4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:32268273}. Nucleus {ECO:0000269|PubMed:32268273}. Cytoplasm, perinuclear region. Cell junction, tight junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton {ECO:0000305}.
DR  UNIPROT: Q9BUZ4;
DR  UNIPROT: O75615;
DR  UNIPROT: Q14848;
DR  UNIPROT: Q2KJU4;
DR  UNIPROT: Q2PJN8;
DR  PDB: 2EOD;
DR  PDB: 2YUC;
DR  PDB: 3ZJB;
DR  PDB: 4K8U;
DR  PDB: 4M4E;
DR  PDB: 5YC1;
DR  Pfam: PF00097;
DR  Pfam: PF02176;
DR  PROSITE: PS50144;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DR  PROSITE: PS50145;
DR  OMIM: 602464;
DR  DisGeNET: 9618;
DE  Function: Adapter protein with E3 ligase activity that is involved in many diverse biological processes including cell proliferation, migration, differentiation, DNA repair, platelet activation or apoptosis (PubMed:30352854, PubMed:31076633, PubMed:32268273, PubMed:33991522). Promotes EGFR-mediated signaling by facilitating the dimerization of EGFR and downstream AKT activation thereby promoting cell proliferation (PubMed:30352854). Ubiquitinates SMURF2 through 'Lys-48'-linked ubiquitin chain leading to SMURF2 degradation through the proteasome and subsequently osteogenic differentiation (PubMed:31076633). Promotes 'Lys-63'-mediated ubiquitination of CHK1 which in turn activates cell cycle arrest and activation of DNA repair (PubMed:32357935). In addition, promotes an atypical 'Lys-29'-linked ubiquitination at the C-terminal end of IRS1 which is crucial for insulin-like growth factor (IGF) signal transduction (PubMed:33991522). Regulates activation of NF-kappa-B in response to signaling through Toll-like receptors. Required for normal skeleton development, and for normal development of the respiratory tract (By similarity). Required for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6 functions. Inhibits adipogenic differentiation by activating pyruvate kinase PKM activity and subsequently the beta-catenin signaling pathway (PubMed:32268273). {ECO:0000250, ECO:0000269|PubMed:12023963, ECO:0000269|PubMed:12801526, ECO:0000269|PubMed:16052631, ECO:0000269|PubMed:16157600, ECO:0000269|PubMed:18953416, ECO:0000269|PubMed:19937093, ECO:0000269|PubMed:30352854, ECO:0000269|PubMed:31076633, ECO:0000269|PubMed:32268273, ECO:0000269|PubMed:32357935, ECO:0000269|PubMed:33991522}.
DE  Reference Proteome: Yes;
DE  Interaction: O14656; IntAct: EBI-25847248; Score: 0.56
DE  Interaction: P14335; IntAct: EBI-11423759; Score: 0.37
DE  Interaction: P63165; IntAct: EBI-10299128; Score: 0.56
DE  Interaction: Q13625; IntAct: EBI-10299140; Score: 0.56
DE  Interaction: Q14289; IntAct: EBI-21980067; Score: 0.35
DE  Interaction: Q96KM6; IntAct: EBI-7217655; Score: 0.37
DE  Interaction: Q9HAU4; IntAct: EBI-7236747; Score: 0.37
DE  Interaction: P07174; IntAct: EBI-3650727; Score: 0.52
DE  Interaction: Q13895; IntAct: EBI-8648045; Score: 0.78
DE  Interaction: Q86YD7; IntAct: EBI-8649669; Score: 0.37
DE  Interaction: O00308; IntAct: EBI-8649783; Score: 0.78
DE  Interaction: Q7L5A3; IntAct: EBI-8652593; Score: 0.74
DE  Interaction: P22681; IntAct: EBI-4307836; Score: 0.37
DE  Interaction: Q9Y508; IntAct: EBI-4308190; Score: 0.37
DE  Interaction: Q9ULV8; IntAct: EBI-4308183; Score: 0.37
DE  Interaction: Q8N9I9; IntAct: EBI-4308197; Score: 0.67
DE  Interaction: Q9Y4K3; IntAct: EBI-6592571; Score: 0.27
DE  Interaction: O60341; IntAct: EBI-8486112; Score: 0.67
DE  Interaction: Q9HCE7; IntAct: EBI-9846435; Score: 0.59
DE  Interaction: A8KA13; IntAct: EBI-10174929; Score: 0.56
DE  Interaction: E9PJI5; IntAct: EBI-10177056; Score: 0.56
DE  Interaction: Q7Z3B3; IntAct: EBI-10178494; Score: 0.56
DE  Interaction: P11441; IntAct: EBI-10197585; Score: 0.72
DE  Interaction: P17036; IntAct: EBI-10199773; Score: 0.72
DE  Interaction: P29597; IntAct: EBI-10204906; Score: 0.56
DE  Interaction: P47897; IntAct: EBI-10209891; Score: 0.72
DE  Interaction: Q13084; IntAct: EBI-10227866; Score: 0.67
DE  Interaction: Q86U76; IntAct: EBI-10258783; Score: 0.56
DE  Interaction: Q8IX06; IntAct: EBI-10262403; Score: 0.56
DE  Interaction: Q8N7F7; IntAct: EBI-10267521; Score: 0.78
DE  Interaction: Q8N9N5; IntAct: EBI-16433516; Score: 0.72
DE  Interaction: Q8TBE0; IntAct: EBI-10273241; Score: 0.72
DE  Interaction: Q96BU6; IntAct: EBI-10282502; Score: 0.56
DE  Interaction: Q96D16; IntAct: EBI-10284444; Score: 0.56
DE  Interaction: O75052; IntAct: EBI-10299118; Score: 0.56
DE  Interaction: Q15323; IntAct: EBI-10299152; Score: 0.72
DE  Interaction: Q6A162; IntAct: EBI-10299162; Score: 0.72
DE  Interaction: Q8IX15; IntAct: EBI-10299172; Score: 0.56
DE  Interaction: Q96EA4; IntAct: EBI-10299184; Score: 0.56
DE  Interaction: Q9H0M0; IntAct: EBI-10299194; Score: 0.56
DE  Interaction: Q9Y2W2; IntAct: EBI-10299204; Score: 0.56
DE  Interaction: Q9H8Y8; IntAct: EBI-10309674; Score: 0.67
DE  Interaction: Q9NPH2; IntAct: EBI-10311471; Score: 0.72
DE  Interaction: Q9NXW9; IntAct: EBI-10316511; Score: 0.67
DE  Interaction: Q9P0N9; IntAct: EBI-10317714; Score: 0.84
DE  Interaction: Q9P0T4; IntAct: EBI-10318082; Score: 0.72
DE  Interaction: Q9BUZ4; IntAct: EBI-10487421; Score: 0.76
DE  Interaction: Q9HBZ2; IntAct: EBI-21247403; Score: 0.37
DE  Interaction: X5D9H9; IntAct: EBI-21247482; Score: 0.37
DE  Interaction: X5D7T2; IntAct: EBI-21247508; Score: 0.37
DE  Interaction: X5DP31; IntAct: EBI-21247717; Score: 0.37
DE  Interaction: P03203; IntAct: EBI-11736686; Score: 0.37
DE  Interaction: Q8AZK7; IntAct: EBI-11736753; Score: 0.37
DE  Interaction: Q9E7P0; IntAct: EBI-11361159; Score: 0.51
DE  Interaction: Q5ERI7; IntAct: EBI-11423767; Score: 0.37
DE  Interaction: P38340; IntAct: EBI-11529060; Score: 0.56
DE  Interaction: A0A0S2Z4Q4; IntAct: EBI-16433566; Score: 0.56
DE  Interaction: O14964; IntAct: EBI-16433556; Score: 0.72
DE  Interaction: A0A0S2Z5X4; IntAct: EBI-16433576; Score: 0.56
DE  Interaction: B4DE54; IntAct: EBI-16433536; Score: 0.56
DE  Interaction: A0A0S2Z5G4; IntAct: EBI-16433546; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-11770260; Score: 0.70
DE  Interaction: Q93062; IntAct: EBI-11770604; Score: 0.49
DE  Interaction: Q15427; IntAct: EBI-24299939; Score: 0.56
DE  Interaction: Q9BRJ7; IntAct: EBI-24307467; Score: 0.56
DE  Interaction: P17980; IntAct: EBI-24315860; Score: 0.67
DE  Interaction: Q9UHD9; IntAct: EBI-24320612; Score: 0.56
DE  Interaction: Q8N1B4; IntAct: EBI-24324657; Score: 0.56
DE  Interaction: Q9NRD5; IntAct: EBI-24332833; Score: 0.56
DE  Interaction: P14678; IntAct: EBI-24350697; Score: 0.56
DE  Interaction: Q96PV6; IntAct: EBI-24362105; Score: 0.56
DE  Interaction: Q9BYV9; IntAct: EBI-25246747; Score: 0.56
DE  Interaction: Q8NCA9; IntAct: EBI-25250935; Score: 0.56
DE  Interaction: P09067; IntAct: EBI-24367595; Score: 0.56
DE  Interaction: O43559; IntAct: EBI-24482005; Score: 0.56
DE  Interaction: Q9NRI5; IntAct: EBI-24482890; Score: 0.56
DE  Interaction: P14373; IntAct: EBI-24487594; Score: 0.56
DE  Interaction: Q63ZY3; IntAct: EBI-24496096; Score: 0.56
DE  Interaction: Q9NYA3; IntAct: EBI-24498792; Score: 0.56
DE  Interaction: Q9Y2P0; IntAct: EBI-24505446; Score: 0.56
DE  Interaction: Q9NSD4; IntAct: EBI-24519618; Score: 0.56
DE  Interaction: Q5BKX5; IntAct: EBI-24520077; Score: 0.56
DE  Interaction: Q9H1A7; IntAct: EBI-24524992; Score: 0.56
DE  Interaction: O76013; IntAct: EBI-24607634; Score: 0.56
DE  Interaction: Q92824; IntAct: EBI-24629750; Score: 0.56
DE  Interaction: Q6ZNG0; IntAct: EBI-23690273; Score: 0.56
DE  Interaction: P14598; IntAct: EBI-24677127; Score: 0.68
DE  Interaction: Q13360; IntAct: EBI-24697281; Score: 0.56
DE  Interaction: P78317; IntAct: EBI-24552429; Score: 0.56
DE  Interaction: Q9UPG8; IntAct: EBI-24792712; Score: 0.56
DE  Interaction: Q9BUH8; IntAct: EBI-24795656; Score: 0.56
DE  Interaction: Q15599; IntAct: EBI-24371576; Score: 0.56
DE  Interaction: Q86VP1; IntAct: EBI-24378843; Score: 0.56
DE  Interaction: A2BDE7; IntAct: EBI-24379938; Score: 0.56
DE  Interaction: Q9UGI0; IntAct: EBI-24388719; Score: 0.56
DE  Interaction: Q9BQQ3; IntAct: EBI-24389146; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-24409903; Score: 0.56
DE  Interaction: P50570; IntAct: EBI-24413515; Score: 0.56
DE  Interaction: Q9HCK0; IntAct: EBI-25262184; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-24417705; Score: 0.56
DE  Interaction: Q9P2A4; IntAct: EBI-24425516; Score: 0.56
DE  Interaction: Q3SY00; IntAct: EBI-24433861; Score: 0.56
DE  Interaction: Q05516; IntAct: EBI-24450519; Score: 0.56
DE  Interaction: Q01664; IntAct: EBI-24457966; Score: 0.56
DE  Interaction: Q9UBP5; IntAct: EBI-24467380; Score: 0.56
DE  Interaction: Q6P2H3; IntAct: EBI-24551937; Score: 0.56
DE  Interaction: O00167; IntAct: EBI-24553247; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-24564131; Score: 0.56
DE  Interaction: Q86X51; IntAct: EBI-24585078; Score: 0.56
DE  Interaction: Q9Y4B4; IntAct: EBI-24590443; Score: 0.56
DE  Interaction: Q9C0D7; IntAct: EBI-24597046; Score: 0.56
DE  Interaction: P52435; IntAct: EBI-24598724; Score: 0.56
DE  Interaction: Q9NP66; IntAct: EBI-24652703; Score: 0.56
DE  Interaction: Q7KZS0; IntAct: EBI-24746458; Score: 0.56
DE  Interaction: Q9UJ78; IntAct: EBI-25204841; Score: 0.56
DE  Interaction: A0A0U1RQF7; IntAct: EBI-25267249; Score: 0.56
DE  Interaction: P49639; IntAct: EBI-25267383; Score: 0.56
DE  Interaction: Q7RTX7; IntAct: EBI-21541280; Score: 0.35
DE  Interaction: Q96PC5; IntAct: EBI-21567144; Score: 0.35
DE  Interaction: P50914; IntAct: EBI-21741266; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: O43294; IntAct: EBI-21979966; Score: 0.60
DE  Interaction: Q8N4T4; IntAct: EBI-25408280; Score: 0.35
DE  Interaction: Q8IZD9; IntAct: EBI-25411696; Score: 0.35
DE  Interaction: O14773; IntAct: EBI-25838614; Score: 0.56
DE  Interaction: P22314; IntAct: EBI-25894497; Score: 0.56
DE  Interaction: Q8N187; IntAct: EBI-25929046; Score: 0.56
GO  GO:0005923;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0001650;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0042802;
GO  GO:0019901;
GO  GO:0031996;
GO  GO:0016740;
GO  GO:0005164;
GO  GO:0031625;
GO  GO:0050699;
GO  GO:0008270;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0045087;
GO  GO:0046330;
GO  GO:0045860;
GO  GO:0043161;
GO  GO:0042981;
GO  GO:0043122;
GO  GO:0007585;
GO  GO:0030323;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MPGFDYKFLEKPKRRLLCPLCGKPMREPVQVSTCGHRFCDTCLQEFLSEGVFKCPEDQLPLDYAKIYPDPELEVQVLGLP
SQ  IRCIHSEEGCRWSGPLRHLQGHLNTCSFNVIPCPNRCPMKLSRRDLPAHLQHDCPKRRLKCEFCGCDFSGEAYESHEGMC
SQ  PQESVYCENKCGARMMRRLLAQHATSECPKRTQPCTYCTKEFVFDTIQSHQYQCPRLPVACPNQCGVGTVAREDLPGHLK
SQ  DSCNTALVLCPFKDSGCKHRCPKLAMARHVEESVKPHLAMMCALVSRQRQELQELRRELEELSVGSDGVLIWKIGSYGRR
SQ  LQEAKAKPNLECFSPAFYTHKYGYKLQVSAFLNGNGSGEGTHLSLYIRVLPGAFDNLLEWPFARRVTFSLLDQSDPGLAK
SQ  PQHVTETFHPDPNWKNFQKPGTWRGSLDESSLGFGYPKFISHQDIRKRNYVRDDAVFIRAAVELPRKILS
//
ID  Q61382;
PN  TNF receptor-associated factor 4;
GN  Traf4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9BUZ4}. Nucleus {ECO:0000250|UniProtKB:Q9BUZ4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9BUZ4}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9BUZ4}. Cell membrane {ECO:0000250|UniProtKB:Q9BUZ4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BUZ4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9BUZ4}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9BUZ4}.
DR  UNIPROT: Q61382;
DR  UNIPROT: Q8BHD9;
DR  Pfam: PF00097;
DR  Pfam: PF02176;
DR  PROSITE: PS50144;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DR  PROSITE: PS50145;
DE  Function: Adapter protein with E3 ligase activity that is involved in many diverse biological processes including cell proliferation, migration, differentiation, DNA repair, platelet activation or apoptosis. Promotes EGFR-mediated signaling by facilitating the dimerization of EGFR and downstream AKT activation thereby promoting cell proliferation. Ubiquitinates SMURF2 through 'Lys-48'-linked ubiquitin chain leading to SMURF2 degradation through the proteasome and subsequently osteogenic differentiation. Promotes 'Lys-63'-mediated ubiquitination of CHK1 which in turn activates cell cycle arrest and activation of DNA repair. In addition, promotes an atypical 'Lys-29'- linked ubiquitination at the C-terminal end of IRS1 which is crucial for insulin-like growth factor (IGF) signal transduction (By similarity). Regulates activation of NF-kappa-B in response to signaling through Toll-like receptors. Required for normal skeleton development, and for normal development of the respiratory tract. Required for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6 functions. Inhibits adipogenic differentiation by activating pyruvate kinase PKM activity and subsequently the beta- catenin signaling pathway (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9BUZ4}.
DE  Reference Proteome: Yes;
GO  GO:0005923;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005829;
GO  GO:0001650;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0042802;
GO  GO:0019901;
GO  GO:0031996;
GO  GO:0016740;
GO  GO:0005164;
GO  GO:0031625;
GO  GO:0050699;
GO  GO:0008270;
GO  GO:0007250;
GO  GO:0006915;
GO  GO:0045087;
GO  GO:0046330;
GO  GO:0045860;
GO  GO:0043161;
GO  GO:0042981;
GO  GO:0043122;
GO  GO:0007585;
GO  GO:0030323;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9BUZ4};
SQ  MPGFDYKFLEKPKRRLLCPLCGKPMREPVQVSTCGHRFCDTCLQEFLSEGVFKCPEDQLPLDYAKIYPDPELEVQVLGLA
SQ  IRCIHSEEGCRWSGPLRHLQGHLNTCSFNVVPCPNRCPAKLSRRDLPAHLQHDCPKRRLKCEFCGCDFSGEAYESHEGVC
SQ  PQESVYCENKCGARMMRRLLAQHATSECPKRTQPCAYCTKEFVYDTIQSHQYQCPRLPVPCPNQCGVGTVAREDLPTHLK
SQ  DSCSTAFVLCPFKESGCKHRCPKLAMGRHVEESVKPHLAMMCALVSRQRQELQELRRELEELSIGSDGVLIWKIGSYGRR
SQ  LQEAKAKPNLECFSPAFYTHKYGYKLQVSAFLNGNGSGEGTHLSIYIRVLPGAFDNLLEWPFARRVTFSLLDQSDPGLAK
SQ  PQHVTETFHPDPNWKNFQKPGTWRGSLDESSLGFGYPKFISHQDIRKRNYVRDDAVFIRASVELPRKILS
//
ID  Q9BWF2;
PN  E3 ubiquitin-protein ligase TRAIP;
GN  TRAIP;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:24553286, ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26820530, ECO:0000269|PubMed:30165463}. Nucleus, nucleolus {ECO:0000269|PubMed:14676304, ECO:0000269|PubMed:24553286, ECO:0000269|PubMed:25335891, ECO:0000269|PubMed:27462463, ECO:0000269|PubMed:30165463}. Chromosome {ECO:0000269|PubMed:25335891, ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:26781088, ECO:0000269|PubMed:30165463}. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14676304}. Note=In the nucleus, found in close proximity to PCNA, suggesting localization at replication foci (PubMed:26595769). Localizes to DNA damage sites in response to replication stress (PubMed:26781088, PubMed:26595769, PubMed:26711499). {ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:26781088}.
DR  UNIPROT: Q9BWF2;
DR  UNIPROT: B5BU84;
DR  UNIPROT: B5BUL3;
DR  UNIPROT: O00467;
DR  PDB: 4ZTD;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DR  OMIM: 605958;
DR  OMIM: 616777;
DR  DisGeNET: 10293;
DE  Function: E3 ubiquitin ligase required to protect genome stability in response to replication stress (PubMed:25335891, PubMed:26781088, PubMed:27462463, PubMed:26711499, PubMed:26595769, PubMed:31545170). Acts as a key regulator of interstrand cross-link repair, which takes place when both strands of duplex DNA are covalently tethered together, thereby blocking replication and transcription (By similarity). Controls the choice between the two pathways of replication-coupled interstrand-cross-link repair by mediating ubiquitination of MCM7 subunit of the CMG helicase complex (By similarity). Short ubiquitin chains on MCM7 promote recruitment of DNA glycosylase NEIL3 (By similarity). If the interstrand cross-link cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on MCM7, promoting the unloading of the CMG helicase complex by the VCP/p97 ATPase, enabling the Fanconi anemia DNA repair pathway (By similarity). Only catalyzes ubiquitination of MCM7 when forks converge (By similarity). Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: promotes ubiquitination of DPCs, leading to their degradation by the proteasome (By similarity). Has also been proposed to play a role in promoting translesion synthesis by mediating the assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family polymerase POLN in order to facilitate bypass of DNA lesions and preserve genomic integrity (PubMed:24553286). The function in translesion synthesis is however controversial (PubMed:26595769). Acts as a regulator of the spindle assembly checkpoint (PubMed:25335891). Also acts as a negative regulator of innate immune signaling by inhibiting activation of NF-kappa-B mediated by TNF (PubMed:22945920). Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation (PubMed:22945920). {ECO:0000250|UniProtKB:Q6NRV0, ECO:0000269|PubMed:22945920, ECO:0000269|PubMed:24553286, ECO:0000269|PubMed:25335891, ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:26781088, ECO:0000269|PubMed:27462463, ECO:0000269|PubMed:31545170}.
DE  Disease: Seckel syndrome 9 (SCKL9) [MIM:616777]: A form of Seckel syndrome, a rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and intellectual disability. {ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:30165463}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O95271; IntAct: EBI-30838546; Score: 0.44
DE  Interaction: P06241; IntAct: EBI-1961246; Score: 0.40
DE  Interaction: P62993; IntAct: EBI-1963479; Score: 0.40
DE  Interaction: P16333; IntAct: EBI-1966129; Score: 0.40
DE  Interaction: P19174; IntAct: EBI-1970673; Score: 0.40
DE  Interaction: Q5VVX9; IntAct: EBI-2130364; Score: 0.37
DE  Interaction: Q99816; IntAct: EBI-2340282; Score: 0.37
DE  Interaction: B3KSH4; IntAct: EBI-2340993; Score: 0.37
DE  Interaction: P62256; IntAct: EBI-2341503; Score: 0.37
DE  Interaction: Q9H832; IntAct: EBI-2342053; Score: 0.37
DE  Interaction: P36406; IntAct: EBI-4307794; Score: 0.37
DE  Interaction: P78317; IntAct: EBI-4308002; Score: 0.37
DE  Interaction: O94941; IntAct: EBI-4308246; Score: 0.37
DE  Interaction: Q8WV44; IntAct: EBI-4308260; Score: 0.37
DE  Interaction: Q9Y508; IntAct: EBI-4308253; Score: 0.37
DE  Interaction: Q15555; IntAct: EBI-10300472; Score: 0.78
DE  Interaction: Q9BS40; IntAct: EBI-24316274; Score: 0.56
DE  Interaction: O15296; IntAct: EBI-24726905; Score: 0.56
DE  Interaction: O15160; IntAct: EBI-24765201; Score: 0.56
DE  Interaction: Q9UPY8; IntAct: EBI-24771535; Score: 0.56
DE  Interaction: Q9BWF2; IntAct: EBI-24533121; Score: 0.56
DE  Interaction: Q96LK0; IntAct: EBI-24595760; Score: 0.56
DE  Interaction: P61086; IntAct: EBI-25867872; Score: 0.56
DE  Interaction: Q8WXH2; IntAct: EBI-25927629; Score: 0.56
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0090734;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0006915;
GO  GO:0006974;
GO  GO:0032688;
GO  GO:0032088;
GO  GO:0010804;
GO  GO:0016567;
GO  GO:0106300;
GO  GO:0031297;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPIRALCTICSDFFDHSRDVAAIHCGHTFHLQCLIQWFETAPSRTCPQCRIQVGKRTIINKLFFDLAQEEENVLDAEFLK
SQ  NELDNVRAQLSQKDKEKRDSQVIIDTLRDTLEERNATVVSLQQALGKAEMLCSTLKKQMKYLEQQQDETKQAQEEARRLR
SQ  SKMKTMEQIELLLQSQRPEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKASGEVADKLRKDLFSSRSKLQTVY
SQ  SELDQAKLELKSAQKDLQSADKEIMSLKKKLTMLQETLNLPPVASETVDRLVLESPAPVEVNLKLRRPSFRDDIDLNATF
SQ  DVDTPPARPSSSQHGYYEKLCLEKSHSPIQDVPKKICKGPRKESQLSLGGQSCAGEPDEELVGAFPIFVRNAILGQKQPK
SQ  RPRSESSCSKDVVRTGFDGLGGRTKFIQPTDTVMIRPLPVKPKTKVKQRVRVKTVPSLFQAKLDTFLWS
//
ID  Q8VIG6;
PN  E3 ubiquitin-protein ligase TRAIP;
GN  Traip;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9BWF2}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BWF2}. Chromosome {ECO:0000269|PubMed:27405720, ECO:0000269|PubMed:33590678}. Cytoplasm {ECO:0000250|UniProtKB:Q9BWF2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9BWF2}. Note=In the nucleus, found in close proximity to PCNA, suggesting localization at replication foci (PubMed:33590678). Localizes to DNA damage sites in response to replication stress (By similarity). {ECO:0000250|UniProtKB:Q9BWF2, ECO:0000269|PubMed:33590678}.
DR  UNIPROT: Q8VIG6;
DR  UNIPROT: O08854;
DR  UNIPROT: Q922M8;
DR  UNIPROT: Q9CPP4;
DR  Pfam: PF13639;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin ligase required to protect genome stability in response to replication stress (PubMed:33590678). Acts as a key regulator of interstrand cross-link repair, which takes place when both strands of duplex DNA are covalently tethered together, thereby blocking replication and transcription (By similarity). During mitosis, controls the choice between the two pathways of replication-coupled interstrand-cross-link repair by mediating ubiquitination of MCM7 subunit of the CMG helicase complex (PubMed:33590678). Short ubiquitin chains on MCM7 promote recruitment of DNA glycosylase NEIL3 (By similarity). If the interstrand cross-link cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on MCM7, promoting the unloading of the CMG helicase complex by the VCP/p97 ATPase, enabling the Fanconi anemia DNA repair pathway (By similarity). Only catalyzes ubiquitination of MCM7 when forks converge (By similarity). Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: promotes ubiquitination of DPCs, leading to their degradation by the proteasome (By similarity). Has also been proposed to play a role in promoting translesion synthesis by mediating the assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family polymerase POLN in order to facilitate bypass of DNA lesions and preserve genomic integrity (By similarity). The function in translesion synthesis is however controversial (By similarity). Acts as a regulator of the spindle assembly checkpoint (By similarity). Also acts as a negative regulator of innate immune signaling by inhibiting activation of NF-kappa-B mediated by TNF (PubMed:17544371, PubMed:22945920). Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q6NRV0, ECO:0000250|UniProtKB:Q9BWF2, ECO:0000269|PubMed:17544371, ECO:0000269|PubMed:22945920, ECO:0000269|PubMed:33590678}.
DE  Reference Proteome: Yes;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0090734;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0006974;
GO  GO:0032688;
GO  GO:0032088;
GO  GO:0010804;
GO  GO:0016567;
GO  GO:0106300;
GO  GO:0031297;
GO  GO:0007165;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPIRALCTICSDFFDHSRDVAAIHCGHTFHLQCLIQWFETAPSRTCPQCRIQVGKKTIINKLFFDLAQEEENVLDAEFLK
SQ  NELDSVKAQLSQKDREKRDSQAIIDTLRDTLEERNATVESLQNALNKAEMLCSTLKKQMKFLEQRQDETKQAREEAHRLK
SQ  CKMKTMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKATGELADRLKKDLVSSRSKLKTLN
SQ  TELDQAKLELRSAQKDLQSADQEITSLRKKLMILQGTLSLPPATNETVSRLVFESPAPVEMMNPRLHQPPFGDEIDLNTT
SQ  FDVNTPPTQTSGSQHCLPKKLCLERARSPMQNVLKKVHKVSKPESQLSLGGQRCVGELDEELAGAFPLFIRNAVLGQKQP
SQ  NRTTAESRCSTDVVRIGFDGLGGRTKFIQPRDTTIIRPVPVKSKAKSKQKVRIKTVSSASQPKLDTFLCQ
//
ID  Q0IIG6;
PN  RISC-loading complex subunit TARBP2;
GN  TARBP2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03034}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03034}.
DR  UNIPROT: Q0IIG6;
DR  Pfam: PF00035;
DR  PROSITE: PS50137;
DE  Function: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. {ECO:0000255|HAMAP- Rule:MF_03034}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016604;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0019899;
GO  GO:0035198;
GO  GO:0070883;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0035197;
GO  GO:0098795;
GO  GO:0035264;
GO  GO:0050689;
GO  GO:0061351;
GO  GO:0051149;
GO  GO:0045727;
GO  GO:0045070;
GO  GO:0031054;
GO  GO:1903798;
GO  GO:0070920;
GO  GO:0070921;
GO  GO:0046782;
GO  GO:0070922;
GO  GO:0007338;
GO  GO:0030422;
GO  GO:0043403;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSEEEQGSGTTTGCGLPSIEQMLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSK
SQ  KAAKHKAAEVALKHLKGGSMLEPALEDSSSFSPLDSSLPEDVPVFTAAAAATPVPSAVPTRSSPMEVQPPVSPQQSECNP
SQ  VGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEAEP
SQ  EDDHFSIGVGSRLDGLRNRGPGCTWDSLRNSVGEKILSLRSCSLGSLGALGPACCSVLSELSEEQAFHVSYLDIEELSLS
SQ  GLCQCLVELSTQPATVCHGSAATREAARGEAARRALQYLKIMAGSK
//
ID  Q15633;
PN  RISC-loading complex subunit TARBP2;
GN  TARBP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Nucleus.
DR  UNIPROT: Q15633;
DR  UNIPROT: Q12878;
DR  UNIPROT: Q8WY32;
DR  UNIPROT: Q8WY33;
DR  UNIPROT: Q9BRY2;
DR  PDB: 2CPN;
DR  PDB: 3ADL;
DR  PDB: 3LLH;
DR  PDB: 4WYQ;
DR  PDB: 5N8L;
DR  PDB: 5N8M;
DR  PDB: 5ZAK;
DR  PDB: 5ZAL;
DR  PDB: 5ZAM;
DR  PDB: 6ZBK;
DR  Pfam: PF00035;
DR  PROSITE: PS50137;
DR  OMIM: 605053;
DR  DisGeNET: 6895;
DE  Function: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. {ECO:0000255|HAMAP- Rule:MF_03034, ECO:0000269|PubMed:15973356, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:18178619}. (Microbial infection) Binds to the HIV-1 TAR RNA which is located in the long terminal repeat (LTR) of HIV-1, and stimulates translation of TAR-containing RNAs (PubMed:2011739, PubMed:11438532, PubMed:12475984). This is achieved in part at least by binding to and inhibiting EIF2AK2/PKR, thereby reducing phosphorylation and inhibition of EIF2S1/eIF-2-alpha (PubMed:11438532). May also promote translation of TAR-containing RNAs independently of EIF2AK2/PKR (PubMed:12475984). Mediates recruitment of FTSJ3 methyltransferase to HIV-1 RNA, leading to 2'-O-methylation of the viral genome, allowing HIV-1 to escape the innate immune system (PubMed:30626973). {ECO:0000269|PubMed:11438532, ECO:0000269|PubMed:12475984, ECO:0000269|PubMed:2011739, ECO:0000269|PubMed:30626973}.
DE  Reference Proteome: Yes;
DE  Interaction: A0A142I5B9; IntAct: EBI-20625330; Score: 0.35
DE  Interaction: O75569; IntAct: EBI-8031712; Score: 0.89
DE  Interaction: P19525; IntAct: EBI-6116026; Score: 0.50
DE  Interaction: Q9UPY3; IntAct: EBI-8031567; Score: 0.96
DE  Interaction: Q9UKV8; IntAct: EBI-8031655; Score: 0.93
DE  Interaction: Q9UL18; IntAct: EBI-7641457; Score: 0.53
DE  Interaction: Q6ZVK8; IntAct: EBI-2350587; Score: 0.49
DE  Interaction: P03496; IntAct: EBI-2547901; Score: 0.55
DE  Interaction: P03495; IntAct: EBI-2549180; Score: 0.37
DE  Interaction: P52735; IntAct: EBI-2654474; Score: 0.00
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P04792; IntAct: EBI-6870660; Score: 0.37
DE  Interaction: P55265; IntAct: EBI-6913278; Score: 0.50
DE  Interaction: Q13387; IntAct: EBI-10699487; Score: 0.37
DE  Interaction: Q8N8B7; IntAct: EBI-10267829; Score: 0.56
DE  Interaction: Q96SI9; IntAct: EBI-10293396; Score: 0.56
DE  Interaction: Q9UL40; IntAct: EBI-10323534; Score: 0.72
DE  Interaction: Q15633; IntAct: EBI-10485546; Score: 0.74
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: F8VQ54; IntAct: EBI-11102475; Score: 0.35
DE  Interaction: Q20MH3; IntAct: EBI-11520008; Score: 0.37
DE  Interaction: Q0A2H0; IntAct: EBI-11520163; Score: 0.37
DE  Interaction: Q2PJP0; IntAct: EBI-11520373; Score: 0.37
DE  Interaction: Q6DP93; IntAct: EBI-11520588; Score: 0.37
DE  Interaction: O92551; IntAct: EBI-11520755; Score: 0.37
DE  Interaction: Q3SBS4; IntAct: EBI-11520855; Score: 0.37
DE  Interaction: Q9Y6A4; IntAct: EBI-12449464; Score: 0.51
DE  Interaction: Q15560; IntAct: EBI-24355055; Score: 0.56
DE  Interaction: P78563; IntAct: EBI-24399962; Score: 0.56
DE  Interaction: Q9HA38; IntAct: EBI-24407531; Score: 0.56
DE  Interaction: Q96T60; IntAct: EBI-24457278; Score: 0.56
DE  Interaction: Q9H898; IntAct: EBI-24634332; Score: 0.56
DE  Interaction: Q8IWL3; IntAct: EBI-13943458; Score: 0.35
DE  Interaction: Q6IQ23; IntAct: EBI-16400551; Score: 0.35
DE  Interaction: O60716; IntAct: EBI-16400931; Score: 0.35
DE  Interaction: Q8N490; IntAct: EBI-21596986; Score: 0.35
DE  Interaction: Q8IZ69; IntAct: EBI-21636338; Score: 0.35
DE  Interaction: Q8WV44; IntAct: EBI-21636495; Score: 0.35
DE  Interaction: O14965; IntAct: EBI-21639587; Score: 0.35
DE  Interaction: O75173; IntAct: EBI-21640424; Score: 0.35
DE  Interaction: Q12905; IntAct: EBI-21665924; Score: 0.35
DE  Interaction: Q9NQ55; IntAct: EBI-21667205; Score: 0.35
DE  Interaction: P61313; IntAct: EBI-21697528; Score: 0.35
DE  Interaction: Q3SYB3; IntAct: EBI-21720692; Score: 0.35
DE  Interaction: Q8N4T0; IntAct: EBI-21731449; Score: 0.35
DE  Interaction: B0UZZ8; IntAct: EBI-21740634; Score: 0.35
DE  Interaction: O95793; IntAct: EBI-21741139; Score: 0.35
DE  Interaction: Q6ZRI8; IntAct: EBI-21744920; Score: 0.35
DE  Interaction: Q96BR6; IntAct: EBI-21784034; Score: 0.35
DE  Interaction: Q9BWM7; IntAct: EBI-21849539; Score: 0.35
DE  Interaction: Q9Y316; IntAct: EBI-21887469; Score: 0.35
DE  Interaction: Q92945; IntAct: EBI-15782041; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: P59633; IntAct: EBI-25688366; Score: 0.35
DE  Interaction: Q9IK90; IntAct: EBI-25747144; Score: 0.35
DE  Interaction: Q9Y2W7; IntAct: EBI-26677564; Score: 0.37
DE  Interaction: Q9GZN2; IntAct: EBI-26680078; Score: 0.37
DE  Interaction: Q92886; IntAct: EBI-26681411; Score: 0.37
DE  Interaction: Q9Y6K9; IntAct: EBI-26685205; Score: 0.37
DE  Interaction: Q13503; IntAct: EBI-26685861; Score: 0.37
DE  Interaction: P0DTC9; IntAct: EBI-26948726; Score: 0.70
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0016604;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0035198;
GO  GO:0070883;
GO  GO:0036002;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0035197;
GO  GO:0098795;
GO  GO:0035196;
GO  GO:0035264;
GO  GO:0050689;
GO  GO:0006469;
GO  GO:0061351;
GO  GO:0051149;
GO  GO:0045727;
GO  GO:0045070;
GO  GO:0031054;
GO  GO:1903798;
GO  GO:0070920;
GO  GO:0070921;
GO  GO:0046782;
GO  GO:0070922;
GO  GO:0007338;
GO  GO:0030422;
GO  GO:0043403;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSEEEQGSGTTTGCGLPSIEQMLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSK
SQ  KAAKHKAAEVALKHLKGGSMLEPALEDSSSFSPLDSSLPEDIPVFTAAAAATPVPSVVLTRSPPMELQPPVSPQQSECNP
SQ  VGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEVEP
SQ  DDDHFSIGVGSRLDGLRNRGPGCTWDSLRNSVGEKILSLRSCSLGSLGALGPACCRVLSELSEEQAFHVSYLDIEELSLS
SQ  GLCQCLVELSTQPATVCHGSATTREAARGEAARRALQYLKIMAGSK
//
ID  P97473;
PN  RISC-loading complex subunit TARBP2;
GN  Tarbp2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:8649414}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03034}. Nucleus {ECO:0000255|HAMAP- Rule:MF_03034, ECO:0000269|PubMed:8649414}.
DR  UNIPROT: P97473;
DR  UNIPROT: Q99M41;
DR  Pfam: PF00035;
DR  PROSITE: PS50137;
DE  Function: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1 (By similarity). Binds in vitro to the PRM1 3'-UTR. Seems to act as a repressor of translation (PubMed:8649414). {ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:8649414}.
DE  Reference Proteome: Yes;
DE  Interaction: Q61990; IntAct: EBI-2644044; Score: 0.40
DE  Interaction: Q8R418; IntAct: EBI-2644088; Score: 0.40
DE  Interaction: Q8CJG0; IntAct: EBI-9030750; Score: 0.35
GO  GO:0005737;
GO  GO:0016604;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0035198;
GO  GO:0070883;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0035197;
GO  GO:0098795;
GO  GO:0035196;
GO  GO:0035264;
GO  GO:0050689;
GO  GO:0061351;
GO  GO:0051149;
GO  GO:0045727;
GO  GO:0045070;
GO  GO:0031054;
GO  GO:1903798;
GO  GO:0070920;
GO  GO:0070921;
GO  GO:0046782;
GO  GO:0070922;
GO  GO:0007338;
GO  GO:0030422;
GO  GO:0043403;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSEEDQGSGTTTGCGLPSIEQMLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSK
SQ  KAAKHKAAEVALKHLKGGSMLEPALEDSSSFSLLDSSPPEDTPVVAAEAAAPVPSAVLTRSPPMEMQPPVSPQQSECNPV
SQ  GALQELVVQKGWRLPEYMVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEAEPD
SQ  DDHFSIGVSSRLDGLRNRGPGCTWDSLRNSVGEKILSLRSCSVGSLGALGSACCSVLSELSEEQAFHVSYLDIEELSLSG
SQ  LCQCLVELSTQPATVCYGSATTREAARGDAAHRALQYLRIMAGSK
//
ID  Q3SWU0;
PN  RISC-loading complex subunit TARBP2;
GN  Tarbp2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03034}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03034}.
DR  UNIPROT: Q3SWU0;
DR  Pfam: PF00035;
DR  PROSITE: PS50137;
DE  Function: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. {ECO:0000255|HAMAP- Rule:MF_03034}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016604;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016442;
GO  GO:0070578;
GO  GO:0003725;
GO  GO:0019899;
GO  GO:0042802;
GO  GO:0035198;
GO  GO:0070883;
GO  GO:0042803;
GO  GO:0047485;
GO  GO:0035197;
GO  GO:0098795;
GO  GO:0035196;
GO  GO:0035264;
GO  GO:0050689;
GO  GO:0061351;
GO  GO:0051149;
GO  GO:0045727;
GO  GO:0045070;
GO  GO:0031054;
GO  GO:1903798;
GO  GO:0070920;
GO  GO:0070921;
GO  GO:0046782;
GO  GO:0070922;
GO  GO:0007338;
GO  GO:0030422;
GO  GO:0043403;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSEEDQGSGSTTGCGLPSIEQMLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSK
SQ  KAAKHKAAEVALKHLKGGSMLEPALEDSSSFSLLDSSVPEDTAVIAAEAAAPVPSALLTRSPPMEMQPPVSPQQSECNPV
SQ  GALQELVVQKGWRLPEYMVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEAEPD
SQ  DDHFSIGVSSRLDGLRNRGPGCTWDSLRNSVGEKILSLRNCSVGSLGSLGSACCSILSELSAEQAFHVSYLDIEELSLSG
SQ  LCQCLVELSTQPATVCYGSATTREAARGDAARRALQYLRIMAGSK
//
ID  O94972;
PN  E3 ubiquitin-protein ligase TRIM37;
GN  TRIM37;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:15885686}. Peroxisome {ECO:0000269|PubMed:11938494}. Note=Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation. {ECO:0000269|PubMed:15885686}.
DR  UNIPROT: O94972;
DR  UNIPROT: A8K0V9;
DR  UNIPROT: A8K8U4;
DR  UNIPROT: A8MZ79;
DR  UNIPROT: B4DGZ3;
DR  UNIPROT: F8WEE6;
DR  UNIPROT: Q7Z3E6;
DR  UNIPROT: Q8IYF7;
DR  UNIPROT: Q8WYF7;
DR  PDB: 3LRQ;
DR  Pfam: PF00917;
DR  Pfam: PF00643;
DR  PROSITE: PS50144;
DR  PROSITE: PS50119;
DR  PROSITE: PS50089;
DR  OMIM: 253250;
DR  OMIM: 605073;
DR  DisGeNET: 4591;
DE  Function: E3 ubiquitin-protein ligase required to prevent centriole reduplication (PubMed:15885686, PubMed:23769972). Probably acts by ubiquitinating positive regulators of centriole reduplication (PubMed:23769972). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes (PubMed:25470042). Has anti-HIV activity (PubMed:24317724). {ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:23769972, ECO:0000269|PubMed:24317724, ECO:0000269|PubMed:25470042}.
DE  Disease: Mulibrey nanism (MUL) [MIM:253250]: An autosomal recessive growth disorder characterized by severe growth failure of prenatal onset, constrictive pericardium and progressive cardiomyopathy, facial dysmorphism, and failure of sexual maturation. Additional clinical features include hepatomegaly, muscle hypotonia, J-shaped sella turcica, yellowish dots in the ocular fundi, hypoplasia of various endocrine glands, insulin resistance with type 2 diabetes, and an increased risk for Wilms' tumor. {ECO:0000269|PubMed:10888877, ECO:0000269|PubMed:12754710, ECO:0000269|PubMed:15108285, ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:17100991, ECO:0000269|PubMed:17551331, ECO:0000269|PubMed:21865362, ECO:0000269|PubMed:23385855}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O43663; IntAct: EBI-761001; Score: 0.63
DE  Interaction: Q9H5Z6; IntAct: EBI-752977; Score: 0.55
DE  Interaction: Q96M61; IntAct: EBI-753037; Score: 0.37
DE  Interaction: Q8IYF1; IntAct: EBI-753112; Score: 0.37
DE  Interaction: Q9UBZ4; IntAct: EBI-753262; Score: 0.37
DE  Interaction: P51116; IntAct: EBI-753616; Score: 0.37
DE  Interaction: O95990; IntAct: EBI-10192918; Score: 0.56
DE  Interaction: Q9H4K1; IntAct: EBI-754930; Score: 0.37
DE  Interaction: Q8TCX5; IntAct: EBI-755044; Score: 0.37
DE  Interaction: Q13895; IntAct: EBI-755389; Score: 0.78
DE  Interaction: Q8N720; IntAct: EBI-755725; Score: 0.37
DE  Interaction: Q15398; IntAct: EBI-756466; Score: 0.37
DE  Interaction: Q96T60; IntAct: EBI-756790; Score: 0.67
DE  Interaction: P53618; IntAct: EBI-757102; Score: 0.67
DE  Interaction: Q6ZU52; IntAct: EBI-757480; Score: 0.37
DE  Interaction: Q8TAU3; IntAct: EBI-758119; Score: 0.67
DE  Interaction: Q7L590; IntAct: EBI-758425; Score: 0.55
DE  Interaction: Q01844; IntAct: EBI-758560; Score: 0.37
DE  Interaction: Q96EZ8; IntAct: EBI-758704; Score: 0.67
DE  Interaction: Q6ZVK8; IntAct: EBI-758902; Score: 0.37
DE  Interaction: Q96KB5; IntAct: EBI-759697; Score: 0.37
DE  Interaction: Q7Z2E3; IntAct: EBI-956382; Score: 0.00
DE  Interaction: Q5VVX9; IntAct: EBI-2130409; Score: 0.37
DE  Interaction: Q8N5R6; IntAct: EBI-2320558; Score: 0.37
DE  Interaction: P62256; IntAct: EBI-2341474; Score: 0.37
DE  Interaction: P58526; IntAct: EBI-2851623; Score: 0.00
DE  Interaction: Q96SN8; IntAct: EBI-3919380; Score: 0.37
DE  Interaction: P08238; IntAct: EBI-6427394; Score: 0.40
DE  Interaction: Q7TSJ6; IntAct: EBI-8800022; Score: 0.27
DE  Interaction: P88980; IntAct: EBI-9640232; Score: 0.37
DE  Interaction: A8K932; IntAct: EBI-10174682; Score: 0.56
DE  Interaction: Q2TBE0; IntAct: EBI-10174987; Score: 0.72
DE  Interaction: P26196; IntAct: EBI-10203749; Score: 0.56
DE  Interaction: P32969; IntAct: EBI-10206109; Score: 0.56
DE  Interaction: P57075; IntAct: EBI-10215794; Score: 0.56
DE  Interaction: Q3B820; IntAct: EBI-10240229; Score: 0.56
DE  Interaction: Q86UD4; IntAct: EBI-10258857; Score: 0.56
DE  Interaction: Q86Y33; IntAct: EBI-10260502; Score: 0.56
DE  Interaction: Q92993; IntAct: EBI-10279849; Score: 0.56
DE  Interaction: Q96NC0; IntAct: EBI-10291622; Score: 0.56
DE  Interaction: Q9BWG6; IntAct: EBI-10300546; Score: 0.56
DE  Interaction: Q9Y247; IntAct: EBI-10325546; Score: 0.56
DE  Interaction: Q9Y272; IntAct: EBI-10325762; Score: 0.56
DE  Interaction: Q9Y2D8; IntAct: EBI-10326014; Score: 0.66
DE  Interaction: X5D778; IntAct: EBI-21247082; Score: 0.37
DE  Interaction: X5DP31; IntAct: EBI-21247741; Score: 0.37
DE  Interaction: Q68CZ1; IntAct: EBI-11363154; Score: 0.42
DE  Interaction: Q6ZU80; IntAct: EBI-11370150; Score: 0.27
DE  Interaction: Q8N0Z3; IntAct: EBI-11392023; Score: 0.27
DE  Interaction: Q8N137; IntAct: EBI-11392655; Score: 0.27
DE  Interaction: Q96KN7; IntAct: EBI-11395685; Score: 0.27
DE  Interaction: Q96MT8; IntAct: EBI-11396049; Score: 0.27
DE  Interaction: Q96ST8; IntAct: EBI-11396670; Score: 0.27
DE  Interaction: P32571; IntAct: EBI-11526650; Score: 0.56
DE  Interaction: P39009; IntAct: EBI-11529791; Score: 0.56
DE  Interaction: Q12417; IntAct: EBI-11537369; Score: 0.56
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: A0A0S2Z4G9; IntAct: EBI-16432706; Score: 0.56
DE  Interaction: A0A0S2Z4M1; IntAct: EBI-16432696; Score: 0.56
DE  Interaction: O15169; IntAct: EBI-16432686; Score: 0.56
DE  Interaction: P28702; IntAct: EBI-16432716; Score: 0.56
DE  Interaction: Q8N8B7; IntAct: EBI-24299182; Score: 0.56
DE  Interaction: Q8IVW4; IntAct: EBI-24321007; Score: 0.56
DE  Interaction: O43167; IntAct: EBI-24327690; Score: 0.56
DE  Interaction: P29972; IntAct: EBI-24333819; Score: 0.56
DE  Interaction: Q14241; IntAct: EBI-25244007; Score: 0.56
DE  Interaction: Q96C24; IntAct: EBI-24364517; Score: 0.56
DE  Interaction: O00311; IntAct: EBI-24370073; Score: 0.56
DE  Interaction: Q8IYY4; IntAct: EBI-24385646; Score: 0.56
DE  Interaction: Q96SQ5; IntAct: EBI-24388285; Score: 0.56
DE  Interaction: O60941; IntAct: EBI-24406639; Score: 0.56
DE  Interaction: Q7Z398; IntAct: EBI-21528160; Score: 0.35
DE  Interaction: Q13042; IntAct: EBI-21544527; Score: 0.35
DE  Interaction: Q6IBW4; IntAct: EBI-21600868; Score: 0.35
DE  Interaction: O14978; IntAct: EBI-21712468; Score: 0.35
DE  Interaction: Q8IWZ6; IntAct: EBI-21737366; Score: 0.35
DE  Interaction: Q0VGE8; IntAct: EBI-21783788; Score: 0.35
DE  Interaction: Q9UL59; IntAct: EBI-21784336; Score: 0.35
DE  Interaction: Q96GS4; IntAct: EBI-21795617; Score: 0.35
DE  Interaction: Q6XPS3; IntAct: EBI-21801323; Score: 0.35
DE  Interaction: Q13398; IntAct: EBI-21807860; Score: 0.35
DE  Interaction: Q9BWM5; IntAct: EBI-21807951; Score: 0.35
DE  Interaction: Q8N9Z0; IntAct: EBI-21807908; Score: 0.35
DE  Interaction: P07305; IntAct: EBI-20925498; Score: 0.40
DE  Interaction: P54764; IntAct: EBI-21380558; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-21380573; Score: 0.00
DE  Interaction: P53778; IntAct: EBI-28938491; Score: 0.35
DE  Interaction: Q14145; IntAct: EBI-30821612; Score: 0.44
GO  GO:0016235;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0003682;
GO  GO:0042803;
GO  GO:0003713;
GO  GO:0005164;
GO  GO:0061630;
GO  GO:0031625;
GO  GO:0004842;
GO  GO:0008270;
GO  GO:0070842;
GO  GO:0035518;
GO  GO:0036353;
GO  GO:0046600;
GO  GO:0032088;
GO  GO:0000122;
GO  GO:0051091;
GO  GO:0051092;
GO  GO:0051865;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQ
SQ  LCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISL
SQ  VQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISK
SQ  SSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVV
SQ  RGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILR
SQ  FQVRSPTFFQKSRDQHWYITQLEAAQTSYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDALETRAKKSACSDM
SQ  LLEGGPTTASVREAKEDEEDEEKIQNEDYHHELSDGDLDLDLVYEDEVNQLDGSSSSASSTATSNTEENDIDEETMSGEN
SQ  DVEYNNMELEEGELMEDAAAAGPAGSSHGYVGSSSRISRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSIENLWGLQPR
SQ  PPASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKNTLSEIKSSSAASGDMQTSLFSADQAA
SQ  LAACGTENSGRLQDLGMELLAKSSVANCYIRNSTNKKSNSPKPARSSVAGSLSLRRAVDPGENSRSKGDCQTLSEGSPGS
SQ  SQSGSRHSSPRALIHGSIGDILPKTEDRQCKALDSDAVVVAVFSGLPAVEKRRKMVTLGANAKGGHLEGLQMTDLENNSE
SQ  TGELQPVLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSVGGFHDSFMVMTQPPDEDTHSSFPDGEQIGPEDLSFNTDE
SQ  NSGR
//
ID  Q6PCX9;
PN  E3 ubiquitin-protein ligase TRIM37;
GN  Trim37;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O94972}. Peroxisome {ECO:0000250|UniProtKB:O94972}. Note=Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation. {ECO:0000250|UniProtKB:O94972}.
DR  UNIPROT: Q6PCX9;
DR  UNIPROT: Q5SX31;
DR  UNIPROT: Q8CHC5;
DR  Pfam: PF00917;
DR  Pfam: PF00643;
DR  PROSITE: PS50144;
DR  PROSITE: PS50119;
DR  PROSITE: PS50089;
DE  Function: E3 ubiquitin-protein ligase required to prevent centriole reduplication (By similarity). Probably acts by ubiquitinating positive regulators of centriole reduplication (By similarity). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes (PubMed:25470042). {ECO:0000250|UniProtKB:O94972, ECO:0000269|PubMed:25470042}.
DE  Reference Proteome: Yes;
GO  GO:0016235;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0035098;
GO  GO:0048471;
GO  GO:0005777;
GO  GO:0003682;
GO  GO:0042803;
GO  GO:0003713;
GO  GO:0005164;
GO  GO:0061630;
GO  GO:0031625;
GO  GO:0004842;
GO  GO:0008270;
GO  GO:0070842;
GO  GO:0035518;
GO  GO:0036353;
GO  GO:0046600;
GO  GO:0032088;
GO  GO:0000122;
GO  GO:0051091;
GO  GO:0051092;
GO  GO:0051865;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQ
SQ  LCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISL
SQ  VQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISK
SQ  SSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVV
SQ  RGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNRQNDTVILR
SQ  FQVRSPTFFQKCRDQHWYITQLEAAQTGYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDSPETRTKKAGSCSD
SQ  MLLEGGPTCASVRETKEDEDEEEKIQNEDYHHELSDGDLDLDLVGEDEVNHLDGSSSSASSTATSNTEENDIDEETMSGE
SQ  NDVEYNSMELEEGELMEDAAAAGPPGSSHSYVGASSRMSRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSMENLWGLQP
SQ  RPSASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKTTLSDIKGSSVASTDMQTNLFCADQA
SQ  ALTTCGPENSGRLQDLGMELLAKSSVAGCYIRNPTNKKNSPKSARAIAGSLSLRRAVDSGENSRSKGDCQVLAEGSSGSS
SQ  QSGSRHSSPRALTHGIIGDLLPKSEDRQCKALDSDAVVVAVFNGLPTVEKRRKMVTLGTNAKGGRLEGMQMADLESHSEA
SQ  GEVQPTLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSMGAFNDPFLAQPPDEDSHSSFPDGEQIDPENLHFNPDEGGG
SQ  R
//
ID  Q6AZZ1;
PN  E3 ubiquitin-protein ligase TRIM68;
GN  TRIM68;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Nucleus. Note=Colocalized with AR in nucleus.
DR  UNIPROT: Q6AZZ1;
DR  UNIPROT: A6NI19;
DR  UNIPROT: A8K551;
DR  UNIPROT: B3KPM5;
DR  UNIPROT: B4DVK4;
DR  UNIPROT: Q8WZ70;
DR  UNIPROT: Q96LE5;
DR  UNIPROT: Q96PF7;
DR  UNIPROT: Q9H9C2;
DR  UNIPROT: Q9NW18;
DR  Pfam: PF13765;
DR  Pfam: PF00622;
DR  Pfam: PF00643;
DR  PROSITE: PS50188;
DR  PROSITE: PS50119;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DR  OMIM: 613184;
DR  DisGeNET: 55128;
DE  Function: Functions as a ubiquitin E3 ligase. Acts as a coactivator of androgen receptor (AR) depending on its ubiquitin ligase activity. {ECO:0000269|PubMed:18451177}.
DE  Reference Proteome: Yes;
DE  Interaction: Q5VVX9; IntAct: EBI-2130453; Score: 0.37
DE  Interaction: Q9NQ48; IntAct: EBI-24286254; Score: 0.56
DE  Interaction: P15884; IntAct: EBI-24286802; Score: 0.56
DE  Interaction: Q9NRI5; IntAct: EBI-24356158; Score: 0.56
DE  Interaction: Q6AZZ1; IntAct: EBI-25245507; Score: 0.56
DE  Interaction: Q04864; IntAct: EBI-24367617; Score: 0.56
DE  Interaction: P62487; IntAct: EBI-24730930; Score: 0.56
DE  Interaction: Q96N21; IntAct: EBI-23826272; Score: 0.56
DE  Interaction: Q8TBB1; IntAct: EBI-24559147; Score: 0.56
DE  Interaction: Q52LG2; IntAct: EBI-24575152; Score: 0.56
DE  Interaction: Q3SY46; IntAct: EBI-24596111; Score: 0.56
DE  Interaction: Q0VD86; IntAct: EBI-24598033; Score: 0.56
DE  Interaction: B2RXF5; IntAct: EBI-24600439; Score: 0.56
DE  Interaction: Q9BRJ7; IntAct: EBI-24790868; Score: 0.56
DE  Interaction: B9A064; IntAct: EBI-21503200; Score: 0.35
DE  Interaction: Q8N0V5; IntAct: EBI-21594853; Score: 0.35
DE  Interaction: Q13227; IntAct: EBI-21662802; Score: 0.35
DE  Interaction: Q9Y215; IntAct: EBI-21671467; Score: 0.35
DE  Interaction: C9JJ79; IntAct: EBI-21683007; Score: 0.35
DE  Interaction: P01148; IntAct: EBI-21753405; Score: 0.35
DE  Interaction: P13284; IntAct: EBI-21758546; Score: 0.35
DE  Interaction: O75791; IntAct: EBI-21817104; Score: 0.35
DE  Interaction: O76076; IntAct: EBI-21831601; Score: 0.35
DE  Interaction: Q9BWP8; IntAct: EBI-21848906; Score: 0.35
DE  Interaction: P49765; IntAct: EBI-21850715; Score: 0.35
DE  Interaction: P51888; IntAct: EBI-21852864; Score: 0.35
DE  Interaction: Q8IV31; IntAct: EBI-21872977; Score: 0.35
DE  Interaction: O95081; IntAct: EBI-21873551; Score: 0.35
DE  Interaction: P29279; IntAct: EBI-21879359; Score: 0.35
DE  Interaction: Q99954; IntAct: EBI-21888544; Score: 0.35
DE  Interaction: Q9H7T9; IntAct: EBI-21891765; Score: 0.40
DE  Interaction: Q9H239; IntAct: EBI-21891752; Score: 0.40
DE  Interaction: Q96BZ8; IntAct: EBI-21891727; Score: 0.35
DE  Interaction: Q7RTY5; IntAct: EBI-21891714; Score: 0.40
DE  Interaction: Q5TGY3; IntAct: EBI-21891673; Score: 0.35
DE  Interaction: P34130; IntAct: EBI-21891660; Score: 0.40
DE  Interaction: O95561; IntAct: EBI-21891641; Score: 0.35
DE  Interaction: O14494; IntAct: EBI-21891628; Score: 0.40
DE  Interaction: Q96RS6; IntAct: EBI-20723623; Score: 0.35
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0035035;
GO  GO:0042802;
GO  GO:0050681;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0008270;
GO  GO:0045087;
GO  GO:0010508;
GO  GO:0043123;
GO  GO:0051092;
GO  GO:0051865;
GO  GO:0000209;
GO  GO:0016567;
GO  GO:0060765;
GO  GO:0010468;
GO  GO:0032880;
GO  GO:0046596;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDPTALVEAIVEEVACPICMTFLREPMSIDCGHSFCHSCLSGLWEIPGESQNWGYTCPLCRAPVQPRNLRPNWQLANVVE
SQ  KVRLLRLHPGMGLKGDLCERHGEKLKMFCKEDVLIMCEACSQSPEHEAHSVVPMEDVAWEYKWELHEALEHLKKEQEEAW
SQ  KLEVGERKRTATWKIQVETRKQSIVWEFEKYQRLLEKKQPPHRQLGAEVAAALASLQREAAETMQKLELNHSELIQQSQV
SQ  LWRMIAELKERSQRPVRWMLQDIQEVLNRSKSWSLQQPEPISLELKTDCRVLGLREILKTYAADVRLDPDTAYSRLIVSE
SQ  DRKRVHYGDTNQKLPDNPERFYRYNIVLGSQCISSGRHYWEVEVGDRSEWGLGVCKQNVDRKEVVYLSPHYGFWVIRLRK
SQ  GNEYRAGTDEYPILSLPVPPRRVGIFVDYEAHDISFYNVTDCGSHIFTFPRYPFPGRLLPYFSPCYSIGTNNTAPLAICS
SQ  LDGED
//
ID  Q8K243;
PN  E3 ubiquitin-protein ligase TRIM68;
GN  Trim68;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6AZZ1}. Nucleus {ECO:0000250|UniProtKB:Q6AZZ1}. Note=Colocalized with AR in nucleus. {ECO:0000250|UniProtKB:Q6AZZ1}.
DR  UNIPROT: Q8K243;
DR  Pfam: PF13765;
DR  Pfam: PF00622;
DR  Pfam: PF00643;
DR  PROSITE: PS50188;
DR  PROSITE: PS50119;
DR  PROSITE: PS00518;
DR  PROSITE: PS50089;
DE  Function: Functions as a ubiquitin E3 ligase. Acts as a coactivator of androgen receptor (AR) depending on its ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q6AZZ1}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0035035;
GO  GO:0042802;
GO  GO:0050681;
GO  GO:0042803;
GO  GO:0019901;
GO  GO:0061630;
GO  GO:0004842;
GO  GO:0008270;
GO  GO:0045087;
GO  GO:0010508;
GO  GO:0043123;
GO  GO:0051092;
GO  GO:0051865;
GO  GO:0000209;
GO  GO:0016567;
GO  GO:0060765;
GO  GO:0010468;
GO  GO:0032880;
GO  GO:0046596;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDPAVLMEAIVEEVNCPICMTFLREPVSISCGHTFCHSCLSGLWKLPGESQNLSYTCPLCRAPVKPRKLRPNWQLASVVD
SQ  KVRLLGFCMEMGLKTDVCDLHKEQLTMFCKEDDMVTCEACKQSPEHEAHSVVPIKDVAWEYKWKLQQALEHLRKEQEEAW
SQ  KLEVSEKEQAAIWKTQMERRKQSIRWEFEKYRQLLKEKELPCQQAEEEAAAAQASLEQEKGETASKLELRREAIIRQSQV
SQ  LWSMIVELEERSQRPVRWMLQGIQEALNRSESWTLQQLEPISLELKTDCRVLGLRETLKTFAVDVRLDPDTAYSRLVVSK
SQ  DRKSVHYGVTQQNLPDNPERFYRYNIVLGSQCISSGRHYWEVEVGDRSEWGLGVCVENVDRKEVVYLSPRYGFWVIRLRK
SQ  GTEYRAGTDEYPLLPLTVPPHRVGIFLDYEAHDISFYNVTDGASHIFTFPCYPFPGRLLPYFSPCYSIDTNNTTPLTICT
SQ  LGGEG
//
ID  P15565;
PN  tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial;
GN  TRM1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: [Isoform 1]: Mitochondrion. [Isoform 2]: Mitochondrion. Nucleus inner membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Predominantly targeted to the nucleus.
DR  UNIPROT: P15565;
DR  UNIPROT: D6VSA6;
DR  UNIPROT: Q9URQ7;
DR  UNIPROT: Q9URQ8;
DR  Pfam: PF02005;
DR  PROSITE: PS51626;
DE  Function: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. Required for the modification of both mitochondrial and cytoplasmic tRNAs.
DE  Reference Proteome: Yes;
DE  Interaction: P15565; IntAct: EBI-7115479; Score: 0.40
DE  Interaction: P40032; IntAct: EBI-7094031; Score: 0.40
DE  Interaction: Q06704; IntAct: EBI-7094258; Score: 0.40
DE  Interaction: P38719; IntAct: EBI-8223418; Score: 0.22
DE  Interaction: P39101; IntAct: EBI-3654346; Score: 0.35
DE  Interaction: P32527; IntAct: EBI-3656468; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3678874; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-3697299; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3730778; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3747899; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3792076; Score: 0.35
DE  Interaction: P35177; IntAct: EBI-4374839; Score: 0.35
DE  Interaction: P38915; IntAct: EBI-4375569; Score: 0.35
DE  Interaction: P50875; IntAct: EBI-4376349; Score: 0.35
DE  Interaction: Q12060; IntAct: EBI-4376999; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-4377624; Score: 0.35
DE  Interaction: Q02336; IntAct: EBI-4378314; Score: 0.35
DE  Interaction: P50102; IntAct: EBI-4379769; Score: 0.35
DE  Interaction: Q05027; IntAct: EBI-4382094; Score: 0.35
DE  Interaction: P25555; IntAct: EBI-16294689; Score: 0.00
DE  Interaction: P39996; IntAct: EBI-16294709; Score: 0.00
DE  Interaction: P40582; IntAct: EBI-16294729; Score: 0.00
DE  Interaction: Q07980; IntAct: EBI-16294749; Score: 0.00
GO  GO:0005739;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005634;
GO  GO:0004809;
GO  GO:0000049;
GO  GO:0030488;
GO  GO:0002940;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MEGFFRIPLKRANLHGMLKAAISKIKANFTAYGAPRINIEDFNIVKEGKAEILFPKKETVFYNPIQQFNRDLSVTCIKAW
SQ  DNLYGEECGQKRNNKKSKKKRCAETNDDSSKRQKMGNGSPKEAVGNSNRNEPYINILEALSATGLRAIRYAHEIPHVREV
SQ  IANDLLPEAVESIKRNVEYNSVENIVKPNLDDANVLMYRNKATNNKFHVIDLDPYGTVTPFVDAAIQSIEEGGLMLVTCT
SQ  DLSVLAGNGYPEKCFALYGGANMVSHESTHESALRLVLNLLKQTAAKYKKTVEPLLSLSIDFYVRVFVKVKTSPIEVKNV
SQ  MSSTMTTYHCSRCGSYHNQPLGRISQREGRNNKTFTKYSVAQGPPVDTKCKFCEGTYHLAGPMYAGPLHNKEFIEEVLRI
SQ  NKEEHRDQDDTYGTRKRIEGMLSLAKNELSDSPFYFSPNHIASVIKLQVPPLKKVVAGLGSLGFECSLTHAQPSSLKTNA
SQ  PWDAIWYVMQKCDDEKKDLSKMNPNTTGYKILSAMPGWLSGTVKSEYDSKLSFAPNEQSGNIEKLRKLKIVRYQENPTKN
SQ  WGPKARPNTS
//
ID  Q9HCX4;
PN  Short transient receptor potential channel 7;
GN  TRPC7;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Cell membrane {ECO:0000269|PubMed:21402151}; Multi-pass membrane protein {ECO:0000269|PubMed:21402151}. Nucleus envelope {ECO:0000269|PubMed:21402151}.
DR  UNIPROT: Q9HCX4;
DR  UNIPROT: A1A4Z4;
DR  UNIPROT: F5H5U9;
DR  UNIPROT: Q70T26;
DR  UNIPROT: Q8IWP7;
DR  Pfam: PF12796;
DR  Pfam: PF00520;
DR  Pfam: PF08344;
DR  DisGeNET: 57113;
DE  Function: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G- protein coupled receptors. Activated by diacylglycerol (DAG) (By similarity). May also be activated by intracellular calcium store depletion. {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P20591; IntAct: EBI-929592; Score: 0.40
GO  GO:0034703;
GO  GO:0005801;
GO  GO:0005887;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0005262;
GO  GO:0070679;
GO  GO:0015279;
GO  GO:0070588;
GO  GO:0006828;
GO  GO:0051480;
GO  GO:0007338;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLRNSTFKNMQRRHTTLREKGRRQAIRGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQN
SQ  ALQLAVGNEHLEVTELLLKKENLARVGDALLLAISKGYVRIVEAILNHPAFAQGQRLTLSPLEQELRDDDFYAYDEDGTR
SQ  FSHDITPIILAAHCQEYEIVHILLLKGARIERPHDYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVL
SQ  TALELSNELARLANIETEFKNDYRKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVNFQVWSDHHRPSLSRIKLAIKYEVK
SQ  KFVAHPNCQQQLLTMWYENLSGLRQQSIAVKFLAVFGVSIGLPFLAIAYWIAPCSKLGRTLRSPFMKFVAHAVSFTIFLG
SQ  LLVVNASDRFEGVKTLPNETFTDYPKQIFRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLS
SQ  IFVASFTARFMAFLKATEAQLYVDQHVQDDTLHNVSLPPEVAYFTYARDKWWPSDPQIISEGLYAIAVVLSFSRIAYILP
SQ  ANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYRGAKYNPAFTTVEESFKTLFWSIFGLSEVISVVLKY
SQ  DHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYY
SQ  LIMRIKMCLIKLCKSKAKSCENDLEMGMLNSKFKKTRYQAGMRNSENLTANNTLSKPTRYQKIMKRLIKRYVLKAQVDRE
SQ  NDEVNEGELKEIKQDISSLRYELLEEKSQATGELADLIQQLSEKFGKNLNKDHLRVNKGKDI
//
ID  Q9WVC5;
PN  Short transient receptor potential channel 7;
GN  Trpc7;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus envelope {ECO:0000250}.
DR  UNIPROT: Q9WVC5;
DR  Pfam: PF12796;
DR  Pfam: PF00520;
DR  Pfam: PF08344;
DE  Function: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G- protein coupled receptors. Activated by diacylglycerol (DAG). May also be activated by intracellular calcium store depletion.
DE  Reference Proteome: Yes;
DE  Interaction: Q13563; IntAct: EBI-27054829; Score: 0.40
GO  GO:0034703;
GO  GO:0005801;
GO  GO:0016021;
GO  GO:0005887;
GO  GO:0005635;
GO  GO:0048471;
GO  GO:0070679;
GO  GO:0015279;
GO  GO:0070588;
GO  GO:0006828;
GO  GO:0051480;
GO  GO:0007338;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLGSNTFKNMQRRHTTLREKGRRQAIRGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQN
SQ  ALQLAVGNEHLEVTELLLKKENLARVGDALLLAISKGYVRIVEAILSHPAFAQGQRLTLSPLEQELRDDDFYAYDEDGTR
SQ  FSHDITPIILAAHCQEYEIVHILLLKGARIERPHDYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVL
SQ  TALELSNELARLANIETEFKNDYRKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVNLQVWSDHHRPSLSRIKLAIKYEVK
SQ  KFVAHPNCQQQLLTMWYENLSGLRQQSIAVKFLAVFGVSIGLPFLAIAYWIAPCSKLGQTLRSPFMKFVAHAVSFTIFLG
SQ  LLVVNASDRFEGVKTLPNETFTDYPKQIFRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLS
SQ  IFVASFTARFMAFLKASEAQLYVDQYVQDVTLHNVSLPPEVAYFTYARDKWWPSDPQIISEGLYAIAVVLSFSRIAYILP
SQ  ANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYRGAKYNPAFTTVEESFKTLFWSIFGLSEVISVVLKY
SQ  DHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYY
SQ  LIMRIKMCLIELCQSKAKRCENDLEMGMLNSKFRKTRYQAGMRNSENLTANSTFSKPTRYQKIMKRLIKRYVLKAQVDRE
SQ  NDEVNEGELKEIKQDISSLRYELLEEKSQATGELADLIQQLSEKFGKNLNKDHLRVNQGKDI
//
ID  F4ICX9;
PN  TSK-associating protein 1;
GN  TSA1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum lumen. Nucleus envelope {ECO:0000269|PubMed:15964904, ECO:0000269|PubMed:24348487}. Cytoplasm {ECO:0000269|PubMed:15964904, ECO:0000269|PubMed:24348487}. Note=In interphase, found in ER bodies and at the nuclear envelope (PubMed:24348487). During mitosis, concentrates in limited areas close to the ends of spindle microtubules ahead of separating chromatids (PubMed:15964904). {ECO:0000269|PubMed:15964904, ECO:0000269|PubMed:24348487}.
DR  UNIPROT: F4ICX9;
DR  UNIPROT: F4ICY0;
DR  UNIPROT: Q94AE1;
DR  UNIPROT: Q9C831;
DE  Function: Involved in seedling development in the dark. May be involved, when interacting with TSK, in the organization of spindle microtubules and may participate, when interacting with GIP1, in structural links between the nuclear envelope and the cytoskeleton. {ECO:0000269|PubMed:22133685, ECO:0000269|PubMed:24348487}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9AT76; IntAct: EBI-16074844; Score: 0.37
GO  GO:0009535;
GO  GO:0005788;
GO  GO:0005635;
GO  GO:0005777;
GO  GO:0000325;
GO  GO:0099503;
GO  GO:0005509;
GO  GO:0050832;
GO  GO:0009640;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEIYTMKTNFLVLALSLCILLSSFHEVSCQDDGSGLSNLDLIERDYQDSVNALQGKDDEDQSAKIQSENQNNTTVTDKNT
SQ  ISLSLSDESEVGSVSDESVGRSSLLDQIKLEFEAHHNSINQAGSDGVKAESKDDDEELSAHRQKMLEEIEHEFEAASDSL
SQ  KQLKTDDVNEGNDEEHSAKRQSLLEEIEREFEAATKELEQLKVNDFTGDKDDEEHSAKRKSMLEAIEREFEAAMEGIEAL
SQ  KVSDSTGSGDDEEQSAKRLSMLEEIEREFEAASKGLEQLRASDSTADNNEEEHAAKGQSLLEEIEREFEAATESLKQLQV
SQ  DDSTEDKEHFTAAKRQSLLEEIEREFEAATKDLKQLNDFTEGSADDEQSAKRNKMLEDIEREFEAATIGLEQLKANDFSE
SQ  GNNNEEQSAKRKSMLEEIEREFEAAIGGLKQIKVDDSRNLEEESAKRKIILEEMEREFEEAHSGINAKADKEESAKKQSG
SQ  SAIPEVLGLGQSGGCSCSKQDEDSSIVIPTKYSIEDILSEESAVQGTETSSLTASLTQLVENHRKEKESLLGHRVLTSPS
SQ  IASSTSESSATSETVETLRAKLNELRGLTARELVTRKDFGQILITAASFEELSSAPISYISRLAKYRNVIKEGLEASERV
SQ  HIAQVRAKMLKEVATEKQTAVDTHFATAKKLAQEGDALFVKIFAIKKLLAKLEAEKESVDGKFKETVKELSHLLADASEA
SQ  YEEYHGAVRKAKDEQAAEEFAKEATQSAEIIWVKFLSSL
//
ID  Q8VZG7;
PN  Ribonuclease TUDOR 1;
GN  TSN1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}. Cytoplasmic granule {ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20484005}. Endoplasmic reticulum {ECO:0000269|PubMed:20484005}. Note=Accumulates heterogeneously in the cytosol, in patches around the nucleus and in the cell periphery, and relocates transiently to a diffuse pattern in response to salt stress (PubMed:20484005). Accumulates in cytoplasmic stress granules (SGs) and processing bodies (PBs) in response to abiotic stresses (e.g. salt and heat) (PubMed:25205572, PubMed:25736060). {ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}.
DR  UNIPROT: Q8VZG7;
DR  UNIPROT: F4K6N0;
DR  UNIPROT: Q9LY25;
DR  Pfam: PF00565;
DR  Pfam: PF00567;
DR  PROSITE: PS50830;
DR  PROSITE: PS50304;
DE  Function: Cytoprotective ribonuclease (RNase) required for resistance to abiotic stresses, acting as a positive regulator of mRNA decapping during stress (PubMed:25736060). Essential for the integrity and function of cytoplasmic messenger ribonucleoprotein (mRNP) complexes called stress granules (SGs) and processing bodies (PBs), sites of post-transcriptional gene regulation during stress (e.g. salt and heat) (PubMed:25736060). Involved in gibberellic acid (GA) biosynthesis (PubMed:25205572). Essential for stress tolerance, probably by regulating mRNAs entering the secretory pathway (PubMed:20484005). Component of stress granules (SGs) that regulates growth under salt stress by modulating levels of GA20OX3 mRNA. Binds GA20OX3 mRNA (PubMed:25205572). May inhibit the degradation of mRNAs involved in stress adaptation (PubMed:26237081). {ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060, ECO:0000269|PubMed:26237081}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9LV27; IntAct: EBI-21137684; Score: 0.35
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0009505;
GO  GO:0005886;
GO  GO:0016442;
GO  GO:0003729;
GO  GO:0004518;
GO  GO:0003723;
GO  GO:0034605;
GO  GO:0031047;
GO  GO:0006402;
GO  GO:0006397;
GO  GO:0010372;
GO  GO:0009651;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATGAENQWLKGRVKAVTSGDCLVITALSHNRAGPPPEKTITFSSLMAPKMARRGGIDEPFAWESKEFLRKLCIGKEVAF
SQ  KVDYKVEAIAGREFGSVFLGNENLAKLVVKTGWAKVREPGQQNQDKVSPYIKELLQLEELAKQEGYGRWSKVPGAAEASI
SQ  RNLPPSAIGDSAGFDAMGLLAANKGKPMEGIVEQVRDGSTIRVYLLPEFQFVQVFVAGVQAPSMGRRTTNGSVVETVPDE
SQ  PNGDVSAESRGPLTTAQRLAASAASSVEVSSDPFATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVHYSDGETVKDLG
SQ  LELVENGLAKFVEWSANMMEEEAKKKLKAAELQCKKDKVKMWANYVPPATNSKAIHDQNFTGKVVEVVSGDCLIVADDAV
SQ  PFGSPAAERRVCLSSIRSPKMGNPRREEKPAPYAREAREFLRQRLIGKQVIVQMEYSRKVTQGDGPTTSGAADRFMDFGS
SQ  VFLPSAAKADSDEVTAPPAAAIAGSQPVGVNIAELVLVRGFGNVVRHRDFEERSNHYDALLAAEARALAGKKGIHSAKES
SQ  PAMHITDLTVSAAKKAKDFLPSLQRIRRIPAVVEYVLSGHRFKLYIPKITCSIAFSFSGVRCPGRGEPYSEEAISVMRRR
SQ  IMQRDVEIEVETVDRTGTFLGSMWESRTNVATVLLEAGLAKMQTSFGADRIAEAHLLEQAERSAKNQKLKIWENYVEGEE
SQ  VSNGNTNTVETRQKETLKVVVTEVLGGGRFYVQSAGDQKIASIQNQLASLSIKDAPIIGSFNPKRGDIVLAQFSLDNSWN
SQ  RAMIVTAPRAAVQSPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAYIKVPSLEDDFGPEAGEYLHTVT
SQ  LGSGKEFKAVIEERDTSGGKVKGQGTGTEFVVTLIAVDDEISVNAAMLQEGIARMEKRQKWGHKGKQAALDALEKFQEEA
SQ  RKSRIGIWQYGDIESDDEDTGPARKPAGGRR
//
ID  Q9FLT0;
PN  Ribonuclease TUDOR 2;
GN  TSN2;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25736060}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20484005}. Endoplasmic reticulum {ECO:0000269|PubMed:20484005}. Cytoplasmic granule {ECO:0000269|PubMed:25736060}. Note=Accumulates heterogeneously in the cytosol, in patches around the nucleus and in the cell periphery, and relocates transiently to a diffuse pattern in response to salt stress (PubMed:20484005). Accumulates in cytoplasmic stress granules (SGs) and processing bodies (PBs) in response to abiotic stresses (e.g. salt and heat) (PubMed:25736060). {ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25736060}.
DR  UNIPROT: Q9FLT0;
DR  UNIPROT: Q0WLY7;
DR  UNIPROT: Q0WM01;
DR  UNIPROT: Q0WVT1;
DR  Pfam: PF00565;
DR  Pfam: PF00567;
DR  PROSITE: PS50830;
DR  PROSITE: PS50304;
DE  Function: Cytoprotective ribonuclease (RNase) required for resistance to abiotic stresses, acting as a positive regulator of mRNA decapping during stress (PubMed:25736060). Essential for the integrity and function of cytoplasmic messenger ribonucleoprotein (mRNP) complexes called stress granules (SGs) and processing bodies (PBs), sites of post-transcriptional gene regulation during stress (e.g. salt and heat) (PubMed:25736060). Involved in gibberellic acid (GA) biosynthesis and seed germination (PubMed:20396901). Essential for stress tolerance, probably by regulating mRNAs entering the secretory pathway (PubMed:20484005). Component of stress granules (SGs) that regulates growth under salt stress by modulating levels of GA20OX3 mRNA. Binds GA20OX3 mRNA (By similarity). May inhibit the degradation of mRNAs involved in stress adaptation (PubMed:26237081). {ECO:0000250|UniProtKB:Q8VZG7, ECO:0000269|PubMed:20396901, ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25736060, ECO:0000269|PubMed:26237081}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0009506;
GO  GO:0009536;
GO  GO:0016442;
GO  GO:0003729;
GO  GO:0004518;
GO  GO:0003723;
GO  GO:0034605;
GO  GO:0031047;
GO  GO:0009686;
GO  GO:0006402;
GO  GO:0006397;
GO  GO:0010372;
GO  GO:0046686;
GO  GO:0009651;
GO  GO:0009845;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATGAATENQWLKGRVKAVTSGDCLVITALTHNRAGPPPEKTITLSSLMAPKMARRGGIDEPFAWESREFLRKLCIGKEV
SQ  AFKVDYKVEAIAGREFGSVYLGNENLAKLVVQNGWAKVRRPGQQNQDKVSPYIAELEQLEEQAQQEGFGRWSKVPGAAEA
SQ  SIRNLPPSAVGDSGNFDAMGLLAASKGKPMEGIVEQVRDGSTIRVYLLPEFQFVQVFVAGLQAPSMGRRQSTQEAVVDPD
SQ  VTATSNGDASAETRGPLTTAQRLAASAASSVEVSSDPFAMEAKYFTELRVLNRDVRIVLEGVDKFNNLIGSVYYSDGDTV
SQ  KDLGLELVENGLAKYVEWSANMLDEEAKKKLKATELQCKKNRVKMWANYVPPASNSKAIHDQNFTGKVVEVVSGDCLVVA
SQ  DDSIPFGSPMAERRVCLSSIRSPKMGNPRREEKPAPYAREAKEFLRQKLIGMEVIVQMEYSRKISPGDGVTTSGAGDRVM
SQ  DFGSVFLPSPTKGDTAVAAAATPGANIAELIISRGLGTVVRHRDFEERSNHYDALLAAEARAIAGKKNIHSAKDSPALHI
SQ  ADLTVASAKKAKDFLPSLQRINQISAVVEYVLSGHRFKLYIPKESCSIAFAFSGVRCPGRGEPYSEEAIALMRRKIMQRD
SQ  VEIVVENVDRTGTFLGSMWEKNSKTNAGTYLLEAGLAKMQTGFGADRIPEAHILEMAERSAKNQKLKIWENYVEGEEVVN
SQ  GSSKVETRQKETLKVVVTEVLGGGRFYVQTVGDQKVASIQNQLAALSLKDAPIIGSFNPKKGDIVLAQFSLDNSWNRAMI
SQ  VNGPRGAVQSPEEEFEVFYIDYGNQEIVPYSAIRPVDPSVSSAPGLAQLCRLAYIKVPGKEEDFGRDAGEYLHTVTLESG
SQ  KEFRAVVEERDTSGGKVKGQGTGTELVVTLIAVDDEISVNAAMLQEGIARMEKRRRWEPKDKQAALDALEKFQDEARKSR
SQ  TGIWEYGDIQSDDEDNVPVRKPGRG
//
ID  Q99598;
PN  Translin-associated protein X;
GN  TSNAX;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region. Golgi apparatus {ECO:0000250}. Nucleus. Note=Accumulate in the Golgi complex of mid- late pachytene spermatocytes (By similarity). Expressed in the cytoplasm in the presence of TSN. {ECO:0000250}.
DR  UNIPROT: Q99598;
DR  UNIPROT: B1APC6;
DR  PDB: 3PJA;
DR  PDB: 3QB5;
DR  Pfam: PF01997;
DR  OMIM: 602964;
DR  DisGeNET: 7257;
DE  Function: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis. {ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:21552258}.
DE  Reference Proteome: Yes;
DE  Interaction: O75190; IntAct: EBI-25909865; Score: 0.56
DE  Interaction: P01112; IntAct: EBI-25868927; Score: 0.56
DE  Interaction: P07948; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P35240; IntAct: EBI-25878206; Score: 0.56
DE  Interaction: P41208; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q07065; IntAct: EBI-3936346; Score: 0.37
DE  Interaction: Q53GS7; IntAct: EBI-25859066; Score: 0.56
DE  Interaction: Q92993; IntAct: EBI-25912186; Score: 0.56
DE  Interaction: Q99598; IntAct: EBI-7635031; Score: 0.22
DE  Interaction: Q15631; IntAct: EBI-7635091; Score: 0.90
DE  Interaction: O95257; IntAct: EBI-753271; Score: 0.67
DE  Interaction: Q96AQ6; IntAct: EBI-756436; Score: 0.37
DE  Interaction: Q96HT8; IntAct: EBI-757081; Score: 0.37
DE  Interaction: Q14164; IntAct: EBI-1081213; Score: 0.00
DE  Interaction: Q96GY3; IntAct: EBI-1389981; Score: 0.35
DE  Interaction: Q86SE5; IntAct: EBI-2320509; Score: 0.37
DE  Interaction: Q09019; IntAct: EBI-2515767; Score: 0.40
DE  Interaction: Q00987; IntAct: EBI-2685764; Score: 0.00
DE  Interaction: Q5NHY7; IntAct: EBI-2800088; Score: 0.00
DE  Interaction: Q5NIJ6; IntAct: EBI-2800081; Score: 0.00
DE  Interaction: A0A6L8PNZ7; IntAct: EBI-2812187; Score: 0.00
DE  Interaction: A0A6L8PSD4; IntAct: EBI-2813947; Score: 0.00
DE  Interaction: A0A6L7HFM3; IntAct: EBI-2819985; Score: 0.00
DE  Interaction: A0A6L7H9A7; IntAct: EBI-2819971; Score: 0.00
DE  Interaction: A0A6L8PSA0; IntAct: EBI-2819978; Score: 0.00
DE  Interaction: A0A2B8HUE3; IntAct: EBI-2819964; Score: 0.00
DE  Interaction: P40127; IntAct: EBI-2844107; Score: 0.00
DE  Interaction: Q8CZK5; IntAct: EBI-2851318; Score: 0.00
DE  Interaction: Q09472; IntAct: EBI-3940497; Score: 0.37
DE  Interaction: Q6P597; IntAct: EBI-25263666; Score: 0.63
DE  Interaction: Q8TDH9; IntAct: EBI-10274996; Score: 0.72
DE  Interaction: Q12904; IntAct: EBI-10294455; Score: 0.56
DE  Interaction: Q99081; IntAct: EBI-10294477; Score: 0.56
DE  Interaction: Q9BRK4; IntAct: EBI-10294487; Score: 0.56
DE  Interaction: Q9H257; IntAct: EBI-10294499; Score: 0.56
DE  Interaction: P62070; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O60506; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P07686; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q5BKY9; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P06241; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O15427; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O75223; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O00139; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q9HBH1; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q02040; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O43929; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P63167; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q5T7B8; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P14373; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q14165; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q15024; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O95985; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q9H857; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P83876; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q92817; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q5VYK3; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O60218; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q03060; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q15058; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q15544; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q96DV4; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O75947; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q2TAY7; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q92552; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q9BTL3; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q9BXY0; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q9UBK8; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q9BQ70; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O43251; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q06830; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q5T280; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: F8W6N3; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P23396; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O94964; IntAct: EBI-25257469; Score: 0.56
DE  Interaction: P51114; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q9NY12; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q16514; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q5VTR2; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O75400; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P62258; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P04003; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q15029; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q69YN4; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: H7C1U3; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: O75340; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q01081; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P36896; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q08378; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P17858; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: P51116; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q9BZD4; IntAct: EBI-11044893; Score: 0.35
DE  Interaction: Q6ZU80; IntAct: EBI-21647598; Score: 0.35
DE  Interaction: P48606; IntAct: EBI-11532699; Score: 0.56
DE  Interaction: Q96HA8; IntAct: EBI-24331255; Score: 0.56
DE  Interaction: Q9UK41; IntAct: EBI-24345182; Score: 0.56
DE  Interaction: Q4V328; IntAct: EBI-24489906; Score: 0.56
DE  Interaction: O95751; IntAct: EBI-24498070; Score: 0.56
DE  Interaction: Q15323; IntAct: EBI-24502549; Score: 0.56
DE  Interaction: Q7Z698; IntAct: EBI-24507839; Score: 0.56
DE  Interaction: Q76N32; IntAct: EBI-24509377; Score: 0.56
DE  Interaction: P26583; IntAct: EBI-24528704; Score: 0.56
DE  Interaction: Q9NW75; IntAct: EBI-24732854; Score: 0.56
DE  Interaction: Q6PIF2; IntAct: EBI-24736580; Score: 0.56
DE  Interaction: P40937; IntAct: EBI-24406909; Score: 0.56
DE  Interaction: Q9Y2V7; IntAct: EBI-24413259; Score: 0.56
DE  Interaction: O43679; IntAct: EBI-24417525; Score: 0.67
DE  Interaction: Q6P1K2; IntAct: EBI-24420500; Score: 0.67
DE  Interaction: Q99633; IntAct: EBI-24542654; Score: 0.56
DE  Interaction: Q9BSW7; IntAct: EBI-24561089; Score: 0.56
DE  Interaction: Q9NUJ3; IntAct: EBI-24572508; Score: 0.56
DE  Interaction: Q00994; IntAct: EBI-24574129; Score: 0.56
DE  Interaction: Q9Y6C2; IntAct: EBI-24745963; Score: 0.56
DE  Interaction: P0C862; IntAct: EBI-21600656; Score: 0.35
DE  Interaction: Q9Y3F4; IntAct: EBI-21647598; Score: 0.35
DE  Interaction: Q99666; IntAct: EBI-21647598; Score: 0.35
DE  Interaction: Q92540; IntAct: EBI-21647598; Score: 0.35
DE  Interaction: O95613; IntAct: EBI-21647598; Score: 0.35
DE  Interaction: O14715; IntAct: EBI-21647598; Score: 0.35
DE  Interaction: Q8IV20; IntAct: EBI-21810059; Score: 0.35
DE  Interaction: P25205; IntAct: EBI-21865186; Score: 0.35
DE  Interaction: Q9UKV8; IntAct: EBI-15925341; Score: 0.35
DE  Interaction: O00499; IntAct: EBI-21387969; Score: 0.00
DE  Interaction: P28329; IntAct: EBI-25837768; Score: 0.56
DE  Interaction: P22607; IntAct: EBI-25853632; Score: 0.56
DE  Interaction: P14136; IntAct: EBI-25857834; Score: 0.56
DE  Interaction: P06396; IntAct: EBI-25863662; Score: 0.56
DE  Interaction: Q16637; IntAct: EBI-25891706; Score: 0.56
DE  Interaction: Q9Y649; IntAct: EBI-25900825; Score: 0.56
DE  Interaction: P61981; IntAct: EBI-25902060; Score: 0.56
DE  Interaction: P46379; IntAct: EBI-25903723; Score: 0.56
DE  Interaction: O14901; IntAct: EBI-25904874; Score: 0.56
DE  Interaction: Q9BVL2; IntAct: EBI-25907995; Score: 0.56
DE  Interaction: Q15047; IntAct: EBI-25909011; Score: 0.56
DE  Interaction: Q8TAP4; IntAct: EBI-25925906; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25931052; Score: 0.56
GO  GO:0005737;
GO  GO:0005829;
GO  GO:1902555;
GO  GO:0005794;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0031687;
GO  GO:0003677;
GO  GO:0004521;
GO  GO:0046872;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0043565;
GO  GO:0003697;
GO  GO:0030154;
GO  GO:0030422;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNKEGSGGFRKRKHDNFPHNQRREGKDVNSSSPVMLAFKSFQQELDARHDKYERLVKLSRDITVESKRTIFLLHRITSA
SQ  PDMEDILTESEIKLDGVRQKIFQVAQELSGEDMHQFHRAITTGLQEYVEAVSFQHFIKTRSLISMDEINKQLIFTTEDNG
SQ  KENKTPSSDAQDKQFGTWRLRVTPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVS
SQ  KKLYTLKQSLAKVENACYALKVRGSEIPKHMLADVFSVKTEMIDQEEGIS
//
ID  Q4R599;
PN  Translin-associated protein X;
GN  TSNAX;
OS  9541;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus. Nucleus {ECO:0000250}. Note=Expressed in the cytoplasm in the presence of TSN. Accumulate in the Golgi complex of mid-late pachytene spermatocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: Q4R599;
DR  Pfam: PF01997;
DE  Function: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0043565;
GO  GO:0030154;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNKEGSGGFRKRKHDNFPHNQRREGKDVNSSSPVMLAFKSFQQELDARHDKYERLVKLSRDITVESKRTIFLLHRITSA
SQ  PDMEDILTESEIKLDGVRQKIFQVAQELSGEDMHQFHRAITTGLQEYVEAVSFQHFIKTRSLISMDEINKQLIFTTDDNG
SQ  KENKTPSSDTQDEQFGTWRLRVTPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVS
SQ  KKLYTLKQSLAKVENACYALKVRGSEIPKHMLADVSSVKTEMIDQEEGIS
//
ID  Q9QZE7;
PN  Translin-associated protein X;
GN  Tsnax;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:15314092}. Nucleus {ECO:0000250}. Note=Expressed in the cytoplasm in the presence of TSN (By similarity). Accumulate in the Golgi complex of mid-late pachytene spermatocytes. {ECO:0000250}.
DR  UNIPROT: Q9QZE7;
DR  UNIPROT: Q3UJR2;
DR  Pfam: PF01997;
DE  Function: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P30543; IntAct: EBI-2910466; Score: 0.60
DE  Interaction: Q60613; IntAct: EBI-2910848; Score: 0.27
GO  GO:0005737;
GO  GO:1902555;
GO  GO:0005794;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0031687;
GO  GO:0004521;
GO  GO:0046872;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0043565;
GO  GO:0003697;
GO  GO:0030154;
GO  GO:0030422;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNGKEGPGGFRKRKHDTFPHNQRREGKDASLSSPVMLAFKSFQQELDARHDKYERLVKLSRDITVESKRTIFLLHRITSA
SQ  PDMEEILTESESKLDGVRQKILQVAQELSGEDMHQFHRAVTTGLQEYVEAVSFQHFIKTRSLISMEEINKQLTFTAEDSG
SQ  KESKTPPAEGQEKQLVTWRLKLTPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVS
SQ  KKLYTLKQSLAKVENACYALKVRGSEIPKHMLADVFSVKTDMIDQEESIS
//
ID  Q5RC21;
PN  Translin-associated protein X;
GN  TSNAX;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus. Nucleus {ECO:0000250}. Note=Expressed in the cytoplasm in the presence of TSN. Accumulate in the Golgi complex of mid-late pachytene spermatocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5RC21;
DR  Pfam: PF01997;
DE  Function: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:1902555;
GO  GO:0005794;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0046872;
GO  GO:0043565;
GO  GO:0030154;
GO  GO:0030422;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSNKEGSGGFRKRKHDNFPHNQRREGKDVNSSSPVMLAFKSFQQELDARHDKYERLVKLSRDITVESKRTIFLLHRITSA
SQ  PDMEDILTESEIKLDGVRQKIFQVAQELSGEDMHQFHRAITTGLQEYVEAVSFQHFIKTRSLISMDEINKQLIFTTEDNG
SQ  KENKTPSSDAQDKQFGTWRLRVTPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVS
SQ  KKLYTLKQSLAKVENACYALKVRGSEIPKHMLADVFSVKTEMIDQEEGIS
//
ID  Q9JHB5;
PN  Translin-associated protein X;
GN  Tsnax;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:9681436}. Nucleus {ECO:0000250}. Note=Expressed in the cytoplasm in the presence of TSN. Accumulate in the Golgi complex of mid-late pachytene spermatocytes (By similarity). {ECO:0000250}.
DR  UNIPROT: Q9JHB5;
DR  Pfam: PF01997;
DE  Function: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P19357; IntAct: EBI-921030; Score: 0.35
GO  GO:0005737;
GO  GO:1902555;
GO  GO:0005794;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0031687;
GO  GO:0004521;
GO  GO:0046872;
GO  GO:0044877;
GO  GO:0003723;
GO  GO:0043565;
GO  GO:0030154;
GO  GO:0030422;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MNGKEGPGGFRKRKHDNFPHNQRREGKDASSSSPVMLAFKSFQQELDTRHDKYERLVKLSRDITVESKRTIFLLHRITSA
SQ  PDMEEILTESESKLDGVRQKMLQVAQELSGEDMHQFHRAVTTGLQEYVEAVSFQHFIRTRSLISMEEINRQLTFTTDDSG
SQ  KESKAPPADGQDKQLVTWRLKITPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVS
SQ  KKLYTLKQSLSKVENACYALKVRGSEIPKHMLADVFSVKTEMIDQEESIS
//
ID  Q8NFU3;
PN  Thiosulfate:glutathione sulfurtransferase;
GN  TSTD1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12817473}. Note=Localized around the nuclear membranes.
DR  UNIPROT: Q8NFU3;
DR  UNIPROT: Q5SY48;
DR  UNIPROT: Q5SY49;
DR  UNIPROT: Q5SY50;
DR  UNIPROT: Q5SY51;
DR  UNIPROT: Q8NFU2;
DR  UNIPROT: Q9BV22;
DR  PDB: 6BEV;
DR  Pfam: PF00581;
DR  PROSITE: PS50206;
DR  OMIM: 616041;
DR  DisGeNET: 100131187;
DE  Function: Thiosulfate:glutathione sulfurtransferase (TST) required to produce S-sulfanylglutathione (GSS(-)), a central intermediate in hydrogen sulfide metabolism (PubMed:24981631). Provides the link between the first step in mammalian H(2)S metabolism performed by the sulfide:quinone oxidoreductase (SQOR) which catalyzes the conversion of H(2)S to thiosulfate, and the sulfur dioxygenase (SDO) which uses GSS(-) as substrate (PubMed:24981631). The thermodynamic coupling of the irreversible SDO and reversible TST reactions provides a model for the physiologically relevant reaction with thiosulfate as the sulfane donor (PubMed:24981631). {ECO:0000269|PubMed:24981631}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0036464;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0000981;
GO  GO:0003690;
GO  GO:0042802;
GO  GO:0044877;
GO  GO:0043565;
GO  GO:0050337;
GO  GO:0006006;
GO  GO:0045944;
GO  GO:0070221;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAGAPTVSLPELRSLLASGRARLFDVRSREEAAAGTIPGALNIPVSELESALQMEPAAFQALYSAEKPKLEDEHLVFFCQ
SQ  MGKRGLQATQLARSLGYTGARNYAGAYREWLEKES
//
ID  G4SLH0;
PN  Titin homolog;
GN  ttn;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:20346955}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:20346955}. Nucleus membrane {ECO:0000269|PubMed:16410549}; Peripheral membrane protein {ECO:0000269|PubMed:16410549}. Note=Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1- dependent(PubMed:16410549). {ECO:0000269|PubMed:16410549, ECO:0000269|PubMed:20346955}.
DR  UNIPROT: G4SLH0;
DR  UNIPROT: A7DT28;
DR  UNIPROT: G4SLD6;
DR  UNIPROT: G5EDP1;
DR  UNIPROT: G5EDT5;
DR  UNIPROT: G5EF69;
DR  UNIPROT: G5EFF0;
DR  UNIPROT: Q65XY2;
DR  UNIPROT: Q8ISF3;
DR  UNIPROT: Q8ISF4;
DR  Pfam: PF00041;
DR  Pfam: PF07679;
DR  Pfam: PF00069;
DR  PROSITE: PS50853;
DR  PROSITE: PS50835;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine-protein kinase (PubMed:18390597, PubMed:20346955). Key component in the assembly and functioning of muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase (By similarity). {ECO:0000250|UniProtKB:Q9I7U4, ECO:0000269|PubMed:18390597, ECO:0000269|PubMed:20346955}.
DE  Reference Proteome: Yes;
DE  Interaction: G5ECY0; IntAct: EBI-2914641; Score: 0.00
GO  GO:0031672;
GO  GO:0031674;
GO  GO:0031965;
GO  GO:0051015;
GO  GO:0005524;
GO  GO:0046872;
GO  GO:0017022;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0006468;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16410549};
SQ  MEGNEKKGGGLPPTQQRHLNIDTTVGGSISQPVSPSMSYSTDRETVMRSASGHATVAETHLIRSIGSQSQSYTEEHWSSE
SQ  ITSFVALAPPKFIQVIKAYRVHSTDTISLVVEVASDPPAIFEWFYNEKSVLQDRDRFQVGHGINISRLKVSRPEQGVYKC
SQ  VTRNPAGVSTSYGYITVNADREHLSSSKEDMRLQRQHSVTYHQAPRFLTQVPNLFVTAGSNVIIDVEVDANPPARFSWFV
SQ  NGKEYRDSIHGVEMFSPDVNRSVVRFSIPVAGEYKVVASNVHGSAMSCGHVDIQKVIELEESTLTTSTTAFDPMTTSMRA
SQ  LGNNGRNSRQAVNMFELNYTQRSSSVPRGVRHLESHIEVSNMTGEEKKTQQQTRTDAASIVESRFHPQPPKPPRAGTSRR
SQ  FLPEPPKFVTTLPSVITVNAEEKLVLSVDVQAIPAAEFAWHVNGFEVKKSQSVVLLDEHNKSTLVLHPPVKQGKYKVTAR
SQ  NDVGSDSVTTQVTRIGEVKDGAGSEPPDIVESAVTVTCSHEEDVGSHSSLQTVRRIQEMQEEDEVDPIKPFIEATSPKVK
SQ  ESVEHPFANILNPKKREERLSPSGKGKHLLFAPRITAHPSESVFKILDGSPLKLRVMASSLPPATFLWMLNNFELRSNQN
SQ  VTIRNDEENSSEIEFQKAPNGNVTVSAKNHLGEDRWTGKVILQYESPPPGQKITTIEKVTESWTLEEAVITQVVPTAADP
SQ  GDRIVIIVRFDENKTSNCQFNWTINGVNIEKLEENLVAVESTEFESSLIVEKLEEQLCGEVVCVVKNQHGEVFSSSAHLR
SQ  IRDDDSSFEIVPPNLPEECAPKIVEPLHSASFLDGQAMSLRCKITANPSAAVVWSKDDVNVEDWVLNKDVTTTVLDGGVC
SQ  ELLNPECFAEDAGLYKCTATNPHGTAETAAFINVEGAEYIKDHEEAEISESVLTDDVHIILPPKFIETLTAETDNFQQLG
SQ  YVRMVATVRSVAPITVSWQKDGMDIYENEKYEVMQFADGAQILTIRAPTNLDSGVYTCTAESEHGVSNSSCQVELTISAE
SQ  SSPESFEKVEITPPEEVKETGIDDDIEVILKEEVSGTAQIEKREEEFKLLVKVADQVASTLVANVFLEAVHEAVKKIVET
SQ  EDEEEDNQIEATQEPRFETSTDEYHVKENGTIKMAATISGHPTPFLEWYFGEEKLQVSQNVSMYYEAGTSAIILKNVQKR
SQ  QGGNYFLRAHNCHGESILPMKLTVDPIEAVTHVLETSIPKVVVEQDAKEEEVRRAAEIISEQFAQLWVQDAQTEAVSAQA
SQ  HQTPVVAEQASEEPTLPEVVAALQEQKPSVEKAPQPQFEVLETEDQDVVEQMQKQLPPVQKSMSVQEEKASSQRTPSPMN
SQ  YEDKVKTIQSNLLRVNSHEAMEPIEATNLLLNTALQLKNEHVCDETTTVIVTQQPQKYDQLVTVVESNIEYHALRLSTSS
SQ  SSPLKFIDLETIIQKPSTSCESIDRMFVEKSKRTANAQHRIVVLQGMSNTFHNAITWSLKKVKKLVGDAEAKAYADVEVV
SQ  KQDETNEQVMTIIDNDTIVPQLLQVAAAANKLKLENVSVALIKEGDRAHQELVIEYESSIDEPMFEPVHNTSHLTFHQQQ
SQ  PTGPDQHVWSRRSKFEEDEAHVVAVFVEVDANCPDQSVEIVATVNAAYEGDNRQGIEDEPFTEVSQSLATESSAAPQAPK
SQ  FLRKLVNCFGRIGEPVQLKCLIAGMPQPEIEWTVDGDPIVPNDEYSIVYEDGVCILRIESTLIEDEGEYCCTASNVAGTT
SQ  FSKCYLKLSEADDDAVDLLRQLSEIKIIDPTLSTGYPMSMISDEENTSHQLLSNVLLTDKEVPITATYNEDLSRAESFRR
SQ  FFESAETTVKVTELYQGESVEAQFQQPEKREQVSTSNTDVMFVNQKVDVMESTVSTVGNAVRQSVSSSTNSWDYMFNDPF
SQ  PESQEINVIENELYEPRVPLLPQKLSYKGQEIFANTNTVERNSKAGAKAKGEVENLKKCVETLLLFDAEMDMKDIKESSP
SQ  KKEIISKKDQQSLDDQIKVTQQILKDVERDLNKMERTSPGKSLSPNKRTFAPKDVEDIEAAIFSISDQLADRQSSEEALR
SQ  EALQEMILSNSSPMKELSRNNETSKPEVLKSEIQKIPEVETKISEVYPIVKLKQAISAIENSLLEDTEVTEIMKRKGSDK
SQ  DKRKATRIKRVPSAHSARITPITSNLRDRLNQLHQLTVSEDSGSLKQNEEAKEIQELFVKIEKEINTIAELCKEKMTKKG
SQ  ADTVTHVLNSVLQHVASIINVILVAQDHQPIEVHAETTKTAEVSVWYSFDVHPESEDIIGIVDEEPTNRRPSSTPRGSTR
SQ  SSNLTTSQDSQATTKMTVSSEDTIEAPIAPPRKGRSLSRDAERLLEIQPRAPPRRSRQSGDTLSPEPTPVLTLVKSDETP
SQ  APVRPPRSRSRHSGDELAETSPEAQPIRPPRSHSRHSGDELEEVQPVRPPRSKSKTADANCLQIESMDESQYSLSCIHIQ
SQ  KTNFAFTNSTHETSNASVVVDLRNMAQLECTVQSLDDLASIQMLCEESDYPSDTDRSLLLAGTVRYFNRASPSLHEVSPS
SQ  LNMESVSMDLKPETEPEEIVQDVYVNVELHSVPSLSSLVEVNPNTLMQTLASEKSSLKAAEEDEKEGEEEGEEEVTADVS
SQ  FIGRSVLSTETLDVVLEEKDMSQMNSTLPLDYERAFSSNTIRETDILSDESITVDSSYHKSPEPTVDFARSQVKSEEVTE
SQ  NFSLIHKPARRRVTGIVVNSLIYTIAANIAEDNTFDVDVVQEPQRYNISIKVIEDIVDFTSLTIMSDCEDDPPADVLVLK
SQ  QDTSKLQALSYDDISVATTRTGITVSIVARSLNDGIYASLEEIAWGEVEMTVPDIMQMSTEEKSSLQFNVTVSESNLEEA
SQ  KSLKSQVSFRSSQNSVSEMDNTISSTATISIPSYVVKLESTATITCELNNYLPKNCTIDWYCGKTKIIIDHEQFDRISHD
SQ  LLEVLIIRSVEAINGNLYSLKINEDLFPVAYLIVENTNLTTSANILTRPETQFVMEGQPTVITVELDDPNVIVNWLKDRR
SQ  PLHENERIRLETDGQGNHRVIIPNTCVGDQGTYLALTSSESVAITLVVEERIEEKEVMVIASGTESEEDDVQEYLVPPGS
SQ  TATIACELEECELKRSIRWLRDGKDIRFEQGKTEHVQNGLKHYLVVHDATSLDSGLYKTERSEEQCEETIIPRGVVATIQ
SQ  CQTSEPQESIQWSKDGNIIPSDISRFEFRSLDNNQSHEMVISNISWSDAGVYSVLINGKSSFVSKIVVVESELITQSVEE
SQ  EPEAEPEIDVSLHIVESEQIIELNVPQSPKLGASHETLVPIGQDDIEVIDKQEAAPVVESIEETSSIGSEEFEIIEKFTE
SQ  EEVPKVAEPSEPTQADVPKIAAPLEQSQIQQEVPTVAAPSEPTQADVPKEAAPSEPSQADVPKVAAPLEQTQIQQEVPMV
SQ  AAPLEPTQADVPKVAAPLEQSQIQQEVPTVAAPSEPTQADVPKEAAPSEPSQADVPKVAAPLEQTQIQQEVPMVAAPLEP
SQ  IQEEVPKEAAPSEPTQEDVPKGAAPLEPTQEDVPKEAAPSGPTQEDVPKEEAPSEPTQEDVPKEAAPSEPTQENVPKEAA
SQ  PSEPTKDVPKEAAPSEPIQEEVPKEATLSEPTQEQSEVSKRSEPVEPTQIQQAASEEETPLEETNETVVQTNEDVKEAEV
SQ  PENAEAQKVVDSSDLQVAASEIAHLAIDEAVLETSNQPSQFDSLQEQKPSVVHENEHVRSVCVDLTFSRDSEQIVSDVIV
SQ  AEVGYDEDECSTIADTITSLSSSPLYTAPVFTERLPSSACFANSKLTLEVMFSGVPQPTISWLIDDHELVSDGERISIKC
SQ  ENGVSAIRFFNVDRNAGGFLKCRATNCAGQVETSCEIVAADEISVISDSSITSSTRPHFVVPLPERVTHTVNDHITIKCK
SQ  FSGQPLPAAMWEKDGVLLDLQKYQVTTEDGTSILKIESASLDDKAVYTCTIANEAGCESTSCTIDVVDDHLGLQQTGLHV
SQ  MCERDQNDVELDILVQSPNHLGVTFNFPPVNRTLARQPPYFLLPLSDKVVIDEKCTLKCVVMGIPLVIVKWIVDGVVVTE
SQ  DDNHEIHFEDGIALLRMKNIKKDKSVVQCEAINCKGKVTTSCVLTKCGVEESEAGDLQKPSFVLSLKDTCTTTDHATLKC
SQ  IVVGTPLPDVSCSFNGVTDNSKIRSEDGIVLIQVNDVTEEGIVVECTISNETGSSTSNCVVKIIKQEEKNYQRPIIVFNQ
SQ  AGSVNNERELSVKVGVIASPEPTLFWKHNGKSIEEGGDYYLIFEDGIGILKVFNIQDGSHEFTCIAKNEYGQTTVEIPVE
SQ  IGLKTENKLTLVKTLNDIAVVDDIVQLKIVAEGDLPIEFKWFEDGQILEDDSSHKITVDKCISTLQLKLEETGTRIITCE
SQ  VSNSSSKVNASCNVERVHNTVSDFVMTNDNSTRFLAVGRKCTRERNNTILKAVVVARENIGDICEIDGEKIPDAYIEGNS
SQ  LSIKVDTLSKKLSNVSFKVSASEGKVFETRKIEIAQEDTDEENFEINYSLRIDEQSGNTTYTFENSELYQGNQSRELDNT
SQ  ERNFTVNKEKDESKKPSEVQPAEIVEQKDVPVQETSAPTVEKLAPVESKETPEVQAAEIVEQKDVPVPETRAPTVEPTVE
SQ  KHTPVDSKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKHTPVESKEKSEVQPAEIVEQKDVTCEEEIKELLTEVEVEL
SQ  FFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPSVEPTV
SQ  EKLAPVESKETSEVQQAEIVEQKDVPVPETSAPSVEPTVEKLAPAESKETSEVQPAEIVEQKDVTCEEEIKELLTEVEVE
SQ  LFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPT
SQ  VEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVE
SQ  KLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKL
SQ  KPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKHAPVESKETSEVQPAEIVEQKVVPVPETSAPTVEPTVEKLAP
SQ  VESKETPEVQPAEILEQKDVTCEEEIKELLTEVEVELFFSKAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEK
SQ  LAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLKSVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLA
SQ  PVDSKETSEVEPAEIVEQKDVTCEEEIKELLTEVEVELLFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVE
SQ  KLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLKSVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKH
SQ  APVESKETSEVQPAEIVEQKVVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAP
SQ  VESKETSEVEPAEIVEQKDVPVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVE
SQ  SKETSEVEPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESK
SQ  ETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKET
SQ  SEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSE
SQ  VQPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVE
SQ  PAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSAPTVEPTIEKLAPVESKETSEVEPA
SQ  EIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVQPAEI
SQ  VEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAHEPTVEKLAPVESKETSEVEP
SQ  AEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDLPVPETSAPTVEPTVEKLAPVESKKTSEVEPAE
SQ  IVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIV
SQ  EQKDVPVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQ
SQ  KDVSVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKD
SQ  VQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVP
SQ  VPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETTATTFEPTKEKLAPVDSKETSEVQTAEIVEQKDVPVP
SQ  ETSATTVEPTKEKLAPGESKETSEVQQAAIVEQKDVAVPETSATTVEPTKEKLAPVESKETSEIQTAEIVEQKDVPVPET
SQ  STSYVEPTKEKLAPGESKETSEVQQAAIVEQKDVPVPETSATTVEPTKEKLAPVESKETSEIQQAAVVEQKDVPVPETSA
SQ  TTVEPTKEKLAPVESKETSEVQQAAIVEQKDVPVPEANAPTFEPTVEKLAPVESKETSEVQQAAIVEQKDVPVPEANAPT
SQ  VEPTVEKLAPVESKETSVESKETQADAKLKKEKDDKHKQEADAKLQKENDDKLKQEADAKLKKENDDKLKQEADAKLKKE
SQ  NDDKLKQEADAKLKKENDDKLKQEAAAKLKKENDDKLKQEADAKLKKENDDKLKQEADAKLQKENDDKLKQEADAKLQKE
SQ  NDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLKKENDDKLKQEADAKLKKE
SQ  KHDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQDADAKLQKE
SQ  KDDKLKQEADAKLKKEKDDKLKHEADAKLQKEKDDKLKQEADAKLKKEKDDRLKKDADAKLQKEKDDKLKQEADAKLKKE
SQ  KDDKLKHEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKE
SQ  KDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQDADAKLQKE
SQ  KDDKLKQEADAKLKKEKDDKLKHEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQDADAKLKKEKDDKLKHEADAKLQKE
SQ  KDDNFKQEANAKLQKEKDDKLKQEKDDNFKQEANAKLQKEKDDKLKQEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKE
SQ  KDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKE
SQ  KDDKLKQEKNDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQETDAKLKKDKDDKLKQEADAKLKKDKDDKLKQE
SQ  ADAKLKKDKDDKLKQEADGKLKKEKDNKLKQEADGKLKKEKDNKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQE
SQ  ADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEANAKLQKEKDDKLKQEADAKLQKEKDDKLKQE
SQ  ADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDNFKQEANAKLQKEKDDKLKQE
SQ  KDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKD
SQ  KDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQETDAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKE
SQ  KDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADGKLKKEKDNKLKQEADGKLKKE
SQ  KDNKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKD
SQ  KDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKE
SQ  KGDKLKLEDQTNQSRIFEETSIEVTSLLKCKQQAIIVSKSFALCERVVLNAEEPFTLEVFCNAVFVKQRTDKIGIGIIFE
SQ  RSGASKKDESRPDRLDDNCVLTDVTDGLSILSPPPKAKKHLKKKKKHHKKEKIAVKETEQDEKTVSHLKPEISGMERKRS
SQ  NSGSSDIFVDVDIEAGEESIHTDALVDLNFYDYDQMELSIFEDYDSDDDSASIDCDVSLSNVAADDGIDVFPSDGDTQEV
SQ  EQKVTLPKKHQSDEDVISKEEENLETSVSYGSIEETVSFTIGTGQSIIEHPKSHAVGQMNSEVIIKCKTSQPISDAKWFC
SQ  NGMVLLPDEQVNMTVTGCEAVLRLVKFLPQNKGNYHVLIDGSIGSQPAILSGPVPPVILNKLTKPITHQAGKSFTYKFNF
SQ  MGAPAPRLRVLSNGEPVSFDVKYEIYDNIASLYIPKMSKRDGGEYTVVLENKYGKDESDLHITMVDTPLKPRKAQLVALT
SQ  DTSATFKWLPPHTGESDILHYIVMRRSTESRRWRNIGHVQEKTFTAIELVPNEFYAFRIVAVNGFGEGAPSEIIEVNTLD
SQ  YDQEESFDFAGEEELKLDDVQVNNEVVTEITIEESEVTIEEHRKLKKKSKKSKKTTDEPELDSEIALEVSSDITSSLEIT
SQ  TESTIPDTAPESQETLNVEIAVTETTVQKITNPSDESAKKDVNEDTAVSSIVKKDDKDVNKKSLPESGLTTKKEIQGKPE
SQ  KKIMKKKTEKADSSISETSETLTKDLTQTKQSEPEPAKRTTETSVQDEVKRKTETTSKSKQTTEEHPQPGGKSDSSISST
SQ  SDASEVKQVQQSESEAQKVTEKPETAKLESKSKMTEDTTKESDNKETVDEKPKKKVLKKKTEKSDSTISETSETSAVESA
SQ  GPSESETQNVAAVDKEKKQKETDEKQKLEAEIAGKKSTEQKSKLEAEAKLKRAAEEDAAKKQKEKTEAASKKAAAEKLEL
SQ  EKQAQINKAAEADAVKKQNELDEQNKLEATKKLAAEKLKLEEQSAAKSKQAAEEQAKLDAQTKAKAAEKQTGLEKDEKSN
SQ  KDSGSNETVEEKPKKKVLKKKTEKSDSSISQKSDTSKTVAESAGSSESETQKVADATSKQKETDKKQKLEAEITAKKSAD
SQ  EKSKLETESKLIKAAEDAAKKQKEKEDKLKLEADVASKKAAAEKLELEKQAQIKKAAEADAVKKQKELAEKQKLESEAAT
SQ  KKAAAEKLKLEEQAQINKAAEADAVKKQKELDEKNKLEANKKSAAEKLKLEEESAAKSKQTVEEQAKLDAQTKEKTAEKQ
SQ  TGLEKDDKSTKDSESKETVDEKPKKKVLKKKTEKSDSSISQKSVTSKTVVESGGPSESETQKVADAARKQKETDEKQKLE
SQ  AEITAKKSADEKSKLEAESKLKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQAQIKKAAEADAVKKEKELA
SQ  EKQKLESEAATKKAAAEKLKLEEQKKKDAETASIEKQKEQEKLAQEQSKLEVDAKKSAEKQKLESETKSKKTEEAPKESV
SQ  DEKPKKKVLKKKTEKSDSSISQKSDTAKTVAESAGQSDSETQKVSEADKAHKQKESDEKQKLESEIAAKKSAEQKSKLET
SQ  EAKTKKVIEDESAKKQKEQEDKKKGDDSAKKQKDQKEKQKLESEATSKKPTSEKQKDEKTPQEKAKSENETVMTTEPQQL
SQ  EVKSEPKKSDKTETVEKEVASSTEKSDDSKTKEPKEKKKIIKKKKDTTKPQEASKELSSDESRIDLESDISLSLDTVTES
SQ  DDLSTASTIKLQKESDESGIDSRMGQTSEAEDSPFISQPVSATVTEMAGEAKFTVKFSRKPIYVKWMRDDREIRVAYGKA
SQ  SVETTDDSSVLVIKNIDGKDVGNIYAVFDSEYRSAMARLDLRVPCKITLESSSNAPEIVAGKNLDLSFKISGYPLPTNIE
SQ  LLHNNENLRTRSDVTDFDDSISIRMKRLKLEDSGEIKIIGKNDSSEDQLRIPINVIEVTSKPTSLQVTSTERETVTLTWS
SQ  LPTELNGSNVNEYLVERKTVDGGRWRHACTVTDSRAVVDGLFSGTEYVFRVVAVNGAGQSAPSDTIEATTQAEEEIDETV
SQ  PTSPVEKVKEPVSKKPENTKESEGHKKRDRKESEDHDENNLGKSGKDEFATSGESGTSNQNEESAQLNTSFTSTEQHGQT
SQ  EKQVRKGTRKSLTRSLNIRESDIDADVVEVEYDEQGDDIPSDPTTSGTYAFDKIEEEPARTSGEMAMAEKDSDAMEVRGL
SQ  NKKLSKKGGKEGTSTEKSSSKTKKQEKSALSVQEMNKSLKKKGEKGEAETAASDFIENADQTGMSIQDLNKSMKKKVESG
SQ  EATGQINDASNNKDADELSIQDSQQSLKKKSENESVTGEQLDKSQEVEDDKMTIQSLKKSIKKKPESREVSGGKSEKSKE
SQ  KESDEMSIQQLNKSVKKKPENEAVTQGKSGKSQEQESDKMSIQALNKSMKKKDGVDGVEGNINIGRSDGDQLSVNDIDAE
SQ  LSTSEQVENASQNLGATADSDGDSLSLQTLKKRISKKGIHGEAESKLGEKQSGSDSFTLQDLYEELKAKEDAVEAGAETS
SQ  NADQSAEKTSLEVRDMKKKMKKKQVSGTAENLIGESNRDETSMEIRDLNTQHSNQTGEDESSTFNFGQKDQEQYSMVMKD
SQ  VSKKLARQNAEEIQSGKLIPTTNEEKTGLALTGKNKNLKKGEENEKTKFEAKHLGSSSASDSLAESTLRSKKTKKGEVEK
SQ  SELSIDMKNQDKTTLATTLLEDDLAKTTSAEESEAEHLVALQNKEKTSLAMRRKRVSFDSSTKSESIEDVIPDKNRDSDK
SQ  MSITGIKKKMSQKSESAEAQKNESPEVKEISSFEEKTLKSKKKSKADRNQGTEANLGDKTIDKDYLSVTDKNQSLEKSEA
SQ  SGQAEKSIKAPNKSKVTTSFADESLTSELDRLMADEEMAEMMFAEEEKAADLLNVMNKNKGLNKSEQEESQEISLKSQSK
SQ  VKDSDSLSSTDKKIGLKKSDKDQKLGTSKIFGSKDQESVGYEEKTSNFSKQRRGVSDLGSDAMTDQKNVQESQYAEISAD
SQ  DHMSKTGADGEISATRTIVDGSDAAQGSEYAEISKKRKFKRAEQIGEAETSLCDSRENTHDSLSISDVNPELRRSNVEIS
SQ  AFGQIDLTAEEVTSLTDINKDAQLTKKQDENDAKKSVSKNLKAGAKKDSDTLSITSKKDKFGKRQDSREASATVEQQGEE
SQ  KVTKNLKGSRGKKEKLGDAGIDVNFENQEEFASTTGDIESIVSEKGHDTYSEKTVKSSKKKSPQTAGAEYGGSESLNASS
SQ  ALSTTDVDAQLKNQEKDGVAESSIGKSNQKDSYSEQELNVNKKKKQAVGAAMNQGSGSTKESDNLAVASVESNLAKDSAN
SQ  QEASLHGLVDNDATSLSQLDSEHRLKKRDDELSAHTKLGKHTQSENIALTETDDSLVKGDSEESAELNIKQQGETAEDKY
SQ  VESRKKTTLKKKPEQKQVTDTLSAVDGRHDTTSLSVADSGISFDKSMENELAGSGDGTASASVSAKVRGADGNAKTNLIS
SQ  SFEKPGQESKTSKTLSGKQKKQEKSSFAEKNAGFDLSMGEGKNDESVESSLQKNRDADSLALQGTDLAFSKPSDSSANAH
SQ  LDMPQRELTLRICQAETVDWSDDSEVEEGTRTSAPGEVKKKKKFIISAISQDGEFSDAESITFDENGVRVEKRRRKKRDP
SQ  KEYMGAGELAMRIPAFAKKMQYIGCIEGDVVVFTIKVVSDDVPLIRMYRNDFPVANFDKMAFEGFTKGSEHSFNVTINDI
SQ  RKLDGGKLVFEAKNDYGVDKCTILLDVRDSGSFIEDYSEIHRSAEIQNSVGDVQVKEGETAKLTGRVDGFPLPELIWIKN
SQ  GKEIDMMVPSTKYQLDYHSDGEFEARIANCTFEDDDDYSLLVENLAGVDSCNFQVFVDCNEYPDDEHFNRRRRLQRGRRV
SQ  MEASSDSELDDAKKRKKRRIKRVVERRNPNAPRLTQLIPPRFDKILSDHDAIEGENVVMMVETLGEPEPQVRFYRDGKLI
SQ  DDGSGDRMEVRHEDEMRKHWLILKDICKDEEAEYACQAINVAGEAWCFSDVVVHMSEESRDDDKSVDEVDDSTVLEEKKD
SQ  DGDDKSKPKTKKKIIKKKETPESEQVTAAEPEQQKISEVDVQSVAETEVGAKKKPDAEKPTDLSKAKKDSKSKKSDEPEA
SQ  STEEKSTTEKPTNDKTSKKSAEKKTVKPKKEVTGKPLEAKKPVEDKKDASQPSSSKESSPPTDGKKKKQIPKALFIPDEI
SQ  SSRFGDPSTMHSETNITTTIRGREGSADAKTPLVEPLSASVSMKVESAKEKAEFSFKRRSETPDDKSRKKEGLPPAKKSE
SQ  KKDEVTAEKQSTEALIESKKKEVDESKISEQQPSDKNKSEVVGVPEKAAGPETKKDVSEIEEVPKKKTIKKKTEKSDSSI
SQ  SQKSNVLKPADDDKSKSDDVTDKSKKTTEDQTKVATDSKLEKAADTTKQIETETVVDDKSKKKVLKKKTEKSDSFISQKS
SQ  ETPPVVEPTKPAESEAQKIAEVNKAKKQKEVDDNLKREAEVAAKKIADEKLKIEAEANIKKTAEVEAAKKQKEKDEQLKL
SQ  ETEVVSKKSAAEKLELEKQAQIKKAAEADAVKKQKELNEKNKLEAAKKSAADKLKLEEESAAKSKKVSEESVKFGEEKKT
SQ  KAGEKTVQVESEPTSKKTIDTKDVGATEPADETPKKKIIKKKTEKSDSSISQKSATDSEKVSKQKEQDEPTKPAVSETQM
SQ  VTEADKSKKQKETDEKLKLDAEIAAKTKQEADEKSKLDAQEKIKKVSEDDAARKEKELNDKLKLESEIATKKASADKLKL
SQ  EEQAQAKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQAQIKKAAGADAVKKQKELDEKNKLEANKKSAAGK
SQ  LKIEEESAAKSKQTVEEQAKLDAQTKAKTAEKQTKLEKDEKSTKESESKETVDEKPKKKVLKKKTEKSDSSISQKSETSK
SQ  TVVESAGPSESETQKVADAARKQKETDEKQKLEAEITAKKSADEKSKLEAESKLKKAAEVEAAKKQKEKDEQLKLDTEAA
SQ  SKKAAAEKLELEKQSHIKKAAEVDAVKKQKELEEKQRLESEAATKKADAEKLKLEEQKKKAAEIALIEIQKEQEKLAQEQ
SQ  SRLEDEAKKSAEKQKLESETKSKQTEEAPKESVDEKPKKKVLKKKTEKSDSSISQKSKSAKSTVDAAETLESDFNLVEKK
SQ  TVQKVEQSPDESTSATIKRDPAQKTEEISKQDDGDEKKTTTDGKPPKPEDSEATPKKRVVKKKTQKSDSVASDASLADVS
SQ  KLSDDVEEKPKKKVLKKKTEKSDSVISETSSVDTIKPESVEIPTEKAEQMILHNRFSTDSAVESEPKNAHKDDTEKTTDD
SQ  MMTRRKSSAIFSDDEQSISSKTSSEGRRRRRRTGFASKFASDTLALRGDNVEIEAELLAEDDTVTWKVNGKDADLNSRCH
SQ  EMSHTFFRTLIIDEVEPTDSGMEITATCGTESHTTILKVEELPVDFVKYLPRKTSGKEGQEVTISVTLNHPIDISKVVWL
SQ  KDGKPLEINKDYSIDTVGCSVSLTLRRAKYEDSGKYKVVCDGVDCSTHLSIQGKPVLKNVSETKPVITVDKDDQFSLLVA
SQ  YDSNPEASFSMTVDGKDLEFDGRSRIDVVDDGLKLTKRGVSKTDAGEYEVKLKNEFGEVAQKFDVKVNDTPSAPGDVSVV
SQ  KAESDCLHIEWTAPTEDNGAEVTSYVIEKKESGRRKFHKVATVNGKKTSYVVDDLEIETPYIVRIAAVNKFGTGEFIETK
SQ  PVQTGSPFQVPTVEFPPTIDNVTSTSCSLSWPKPIEDGGSPVYGYDVYKRENEGEWQKMNGEELVFTESFNVRALSSGKE
SQ  YEFKIEACNEAGLRSNSNVVSKKLTVEGLVPEIILDMPMVKVLDNDKVEVTWKSDGEKEFVVQYKSDGSSIWASVDIGGP
SQ  RSESAATSKCIIDGLREGIPYVFRVAARNQHGTGEFSEPTIPVVVLADDAPRVLKAIKPVKIPKKGELRLECHAAGHPAP
SQ  EYIWYKDGKEIIPTDENTEIVNEGSMSALIIHELAGEDVGLYKVLVENIHGTAESEAEVGISDVRAHFNSSFSELTEIEE
SQ  GHDIELTCEVSDEEAVVNWYKDGKKLVASDRVQFYAMARKRTLRIKGSTDADSGVYKCETTDGRSRTEGEVIVNEQEPHI
SQ  LVGPQDAIVKDFGETMVLFCETSKPVRKVKWFKNGVEIWPQMNKAIMENDGKRATLEIKNFDKHDIGAYTASVSEKETSA
SQ  PAKLVFEVAPNLIIPTEIRDGVTVHAGNEFDFAVEFSGFPIPTIHLTNNGTPLKAIAVVTEYDDSVSVRMKDVTLDNSGT
SQ  VRVIAESPLGQCIKEIPLKIIDKPSAPCDLQFKEVTEDSVFLSWQPPLETNGAPLTGYVIERKAVDNNRWRPCGQVKPTK
SQ  LTFVAEDLFCNQVYGFRILAVNEVGESEPCDTVDVLTLESSEPVSESSELFVPKIAILRTPQVTVAVDETKVTLRWEECP
SQ  ETSLYKVERKKVGDSDWLEIANTDRNKFKDRSLTESGEYVYQVTATGIHAVSSPSEETNPVKILVPGSEMPASKTEKKTD
SQ  AAKSESEQKSAEEIVAEKQVDQSQASESTTEAVEEKKTKKVVKKKVAENKGEETLQEVKEKLKKGKAVEKVQDESRRGSL
SQ  QASSDNESVTTTSEKRSEAELEKNSEKSAEKKSTSADLEAADKAETEKSETGKETTEKKKKVVKKVAKKGLVKADKSKIE
SQ  LTAGKEGEISAQVAETGVSVEWKKDGKALDASYTVTSTGGVSTVKIPIVDVNTSGVFTCKVKSSEGDEEEVSIAVTVKLP
SQ  EVPKVEAEQSIVEVKVGDVAKLSAKISEPASSVNWTKDDKPIKEDGNVKAQLSPDGTAQLTISKTDSAHSGIYKLNVEND
SQ  AGKGKVEIALRIKGAAKGAPGIPTGPIVFDDVTESSAEFSWKAPENNGGCEITGYNVERKESKNKGWKQCGKTKELKFKA
SQ  DGLEEGTDYDVKVSAVNTMGTGSALEGKITTLKKKEETGKQKSEKSESDEKKSESDKVSELKQIGKPEYVSSTATSIALK
SQ  WTSDNDEVTYTVQMKEANSKRPWAVVAKEISECSATIAQLKEGTSYLFRVIAQNKTGQTVTSEQSESIECKDTTESKKPA
SQ  FTNAPTDLTAVKNGKTKITAEFTGHPAPEIHWFKNKKEIFSGKRQWIENIAGATSLTIGEMREDDEGEYKIVVKNTAGSV
SQ  EHSCKLTMDQLPEINRVDRYASTLVFDKGETVKLRLSFSGRPQPEVIWIDNNGKVIEESRKMKIEKTVLNTVLTINSIDS
SQ  QDQGEFALKIKNRCGEDKYAIGIQVTDRPAAPGKPAVEDQNVDSVRLRWAAPTNDGGSPVRNYTVEMCTEKGKTWTKAEV
SQ  TKQAFITLFNLVPGESYRFRVRADNTFGQSEPSDESELVVVKNVSRVVEEPKKKEVKVKEQESVDYERVAKDSEPSEYKT
SQ  IDIHRLPNDLQAKYIIHEELGKGAYGTVYRATEKATGKTWAAKMVQVRPGVKKENVIHEISMMNQLHHEKLLNLHEAFDM
SQ  GNEMWLIEEFVSGGELFEKILEDDSLMSEEEVRDYMHQILLGVSHMHKNQIVHLDLKPENILLKAKNSNELKIIDFGLAR
SQ  KLDPKKSVKLLFGTPEFCAPEVVNYQPVGLSTDMWTVGVISYVLLSGLSPFLGDSDEDTLANVSASDWDFDDPSWDDVSD
SQ  LAKDFICRLMIKDKRKRMSVQDALRHPWITGPLLSAFNDLSEYVKKMQPKLDKSGVPARQKRNFLSLKRWSDDLLPIGRL
SQ  AKRGAIFRRLTMDGVFERNIAFDTDAAPSVKKQLEDIVANVGDLIATLSCDVDGVPSPKVQWYKDDKELTVPSMKYDSFY
SQ  NEGLAELTVKNIVESDAGKYTCRATNDLGSIMTHAKLSVKADEKKKKKSKTSPAVIEKKKDRKTSKVVVIEEMIDMPPNF
SQ  HHLLQDDEAKIGEPKILVVTNTTLPEPTVDWYHNGEHISINDSNYLRKHDKGRYELHILSVDSTDEGKWKAVGKNAFGEC
SQ  ESEAKLTVVIPDGQYAPSFGKQLSDVKCSESDILKLEVNIQANPAPEINWFRNESEIEHSQHHRLQFDDGSGNYSLTIID
SQ  AYAEDSGEYKCVAKNKIGKAHTVCCVRIEELLSKRSKKIDGSKAPRFRMQLPTPREVPQGADLTLVCSVSGTPHPNIKWT
SQ  KDDKPIDMSNKQVRHENGVCTLHIIGARDDDQGRYVCEAENIHGVAQSFSVVEIKEAVDKDHVRPKFLEPLVNCSTCEGN
SQ  EMVLECCVTGKPIPTITWYKDGLKLIIENRMLQYTDRKGVSRLNIMNVVMNDDGEYTCEAVNSLGKDFTHCTVKVVDMGL
SQ  SKTRLTPVRSRSRSRSRSPSVVGGEIQRPPVVTRPLADATVTEGNRELLEVEVDGFPTPTIEWYHDGKLVAESRTLRTYF
SQ  DGRVAFLKIYEAHEEHNGQYVCKVSNKLGAVETRAIVVVEAPDAAEHVTQMPTFVKKLQDVVLKTAGETATFTCQSYANP
SQ  AAQVVWLHNGKALQQTKSNYKTRLFDDNTATLVIENVTDELCGTYTAVANNQFGDVHTSAQLTISGSEAKKIAASLPYFI
SQ  IELKPKINVVEGATLSIQADLNGSPIPEVVWLKDNSELVESDRIQMKCDGVNYQLLVRDVGLEDEGTYTITAENEKGKIR
SQ  QNTEVSVTKSKEVKEKKEKKKVEKKDEGKKKPGRPGLPRPSGASKTEQVTMAFDAPSEGPADSYEVERRCPDQREWVSCG
SQ  STKSLELEIKGLTPNTEYIFRVAGKNKQGLGEWSEMTSTLKTASVGQAPQFTISPQSKIIANRDDEFEIAVEFSGTPTPS
SQ  VKWYKENLQIVPDEKIDVATTSTSSILNLKSQEENGTFNCLIENELGQASASCQVTIFNKPASLQSTPDHSLERNLVPTL
SQ  QKALNNESAQAGQQIMLTCRISSRSESTVAWFKDDERIESAGRYELSSDKKSNHKLVCHAVQSQDTGKYRCVVTNKYGYA
SQ  ESECNVAVEDVTKFIAPSFSATLSDSTAILGHNITLECKVEGSPAPEVSWTKDGERISTTRRIRQTQDENGNCKLSISKA
SQ  ESDDMGVYVCSATSVAGVDSTSSMVMIAKTTGTDSHLVIAQTADEKHEKPRFTRAPPSLIEVNESGQFTLIAKAVGEPKP
SQ  TVTWLKDGREILRTNRIYHHFVTGDGESHLIAECVVSKTSGIFSCKAENPNGTVIAETQVIVQRMKPANQLANVAPKFTI
SQ  PLTDMGIVNGHPTTLSCNVTGSPEPTLEWIYIDDSGHKINLTSSTTDWTECRFGKVAELKSERVLREQRGTYQCIATNSS
SQ  GQATTQCYLLVGELSDEPAGPPRFVKCLQDTWTPLKESIEFSVELAGFPTPDLTWYHNEKKINEGKDVKITFPSDTTSVL
SQ  SIKNVSLASLGMYFVEASNIHGVLRTAGRLNVSDERRKAEPPQFKHVLEPVLAVQPKVAFSEEHPRASSSAATARVKKGA
SQ  APMFLQGLEDMDLKAGASAAVAGKLGRKLRPHRSTTNDADKLAKALAQSLRLDEPRASIDSRPESAANAALDEVRAAINS
SQ  RNKRVCRPKFMVKPKPRKVLEEYKSLRLKTAISGNPMPQVHWDKEGIILETGNKYSIYNDGDFYYLEVHHVSTFDKGFYN
SQ  CTAANNEGIITCTSEIDVLPNKEDSAAQVAKRKSRKEAKAPNFIEVLPGRSQANLNESLCVECSVSAYPCASIIWTRNSV
SQ  RLLPQADRYTMSYDGECASLKFISVTPGDEGTYACEAVNELGSAVTNMNLQVSGVDPNAAEGIPPLFRFEKIKSVRKVVD
SQ  GSRVELAAELVQASEPLQIRWLRNKVTIVDSPSFSYSRSENMVFLTIADVFPEDGGEYTVEAKNQSGIARCTMQLDVRNN
SQ  ERSVADEAPRVFDFEPTTRSDPGVSVELRAKVIGHPDPVISWTKAGQKLNNEEKYMMRNEGDKFILRIANVTRADAGKYE
SQ  LTAINPSGQANAELELTVVQSTKTVGAKPKFNESPISVQTCEKNRAELRASFSGTPAPACRWFYNGNELIDGLDGYTITS
SQ  SDTNSSLLINSVDKKHFGEYLCTIRNQNGEELANAMILSEVLSMFYSSLFLVVFVDIVAQCHVARLLHFLNEERFVGRNI
SQ  FA
//
ID  Q9Y7Z5;
PN  Tetra-spanning protein 1;
GN  tts1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Golgi apparatus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. Note=Enriched at the cell equator during mitosis.
DR  UNIPROT: Q9Y7Z5;
DR  Pfam: PF03661;
DE  Function: Required for the correct positioning of the cellular division plane by delimiting the actomyosin ring assembly at the cell equator. {ECO:0000269|PubMed:20434336}.
DE  Reference Proteome: Yes;
GO  GO:0032153;
GO  GO:0032541;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0071782;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0051301;
GO  GO:1990809;
GO  GO:0071786;
GO  GO:0061024;
GO  GO:0140480;
GO  GO:1990608;
GO  GO:0071763;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEPKQRVVKPLKERVLPVVKNTQFVWFSGQVIVLISSVLYALQAIPFRSAPPFLFKSAAFGAIVAYAIVLYKTYSPNLTS
SQ  RASWNKHFFARLMLDDNVQYFILALSMLIDRPILFSLAPYAIYATFHISTYLRSVLLPAIYPNISDAKTASYASRVSNLL
SQ  NQYTRSQFQPAMQLVASLETFLLFRLFFGVFLRKNSISRLVGYIFFLRMRYTNSHFTRASIKAVSLRMDRLVADNRVPPV
SQ  IKNAWHTFKTYVSKFGASPVGTAQSRPTASSSTTAPSST
//
ID  A0A6I8PU40;
PN  Taurine up-regulated 1 protein;
GN  TUG1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:32894169, ECO:0000305|PubMed:31155234}; Single-pass type I membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:32894169}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:32894169}.
DR  UNIPROT: A0A6I8PU40;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARPPPLPGLVGRRNGRAVDRAIGWRLFLLLWHPALGAQARPPRRAPGGRWRSRRVFLLVRRTRAAAYAFAIRRGVVRVV
SQ  GGGGQLLRPAPGEAAAAAAAGFGAAGEAGVAGAGLEAWRHPSGPARTQLGGQEGAGGWLVVGFLLCLFLLMPP
//
ID  A0A6I8MX38;
PN  Taurine up-regulated 1 protein;
GN  Tug1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:32894169}; Single-pass type I membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:A0A6I8PU40}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:32894169}.
DR  UNIPROT: A0A6I8MX38;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MARPPPLPGLVGRRSGRAVDRAIGWRLFLLLWHPALGAQARPPRRAPGGRWRSRRVFLLVRRTRAAAYAFAIRRGVVRVV
SQ  GGGGQLRPAPGEAAGEAGVAGAGLEAWRHPSGPARTQLEGQEGAGGWLVVGFLLCLFLLMPP
//
ID  Q7ZXP0;
PN  Twinfilin-2-A;
GN  twf2;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization. {ECO:0000250}.
DR  UNIPROT: Q7ZXP0;
DR  Pfam: PF00241;
DR  PROSITE: PS51263;
DE  Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0030837;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHQTGIHATPELKEFFAKARNGSIRLIKVVIEEEQLVLGSHKELKHAWEQDYDALIVPLLDESQPCYILYRLDSQNAQG
SQ  YEWIFLSWSPDHSPVRLKMLYAATRATVKKEFGGGHIKDEIFGTLKEDVALSGYKKHVSLCAAPAPLTAAERELQEIKIN
SQ  EVKTEISVESKQQTLQGLSFPLRPEAEEAILLLKQKKINYIQLRLDLEKETVDLVHTKHTEIKDLPGRIPQDTARYHFFL
SQ  YKHSHEGDHLESVVFIYSMPGYKCSIKERMLYSSCKNRLLDSVEQDFQLEIAKKIEIEDGAELTDEFLYDEVHPKQHAFK
SQ  QAFAKPKGPAGKRGQKRLIKGPGENGEDS
//
ID  Q640W2;
PN  Twinfilin-2-B;
GN  twf2;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization. {ECO:0000250}.
DR  UNIPROT: Q640W2;
DR  Pfam: PF00241;
DR  PROSITE: PS51263;
DE  Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0003779;
GO  GO:0030837;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHQTGIHATPELKEFFAKARNGSVRLIKVIIEEEQLVLGSHKELKHAWDQDYDAFVLQLLDESQPCYILYRLDSQNAQG
SQ  YEWIFLSWSPDHSPVRLKMLYAATRATVKKEFGGGHIKDEIFGTLKEDVALSGYKKHVSSCAAPAPLTAAERELQAIKIN
SQ  EVKTEISVESKQQTLQGLSFPLRPQAEEAILLLKQKKINYIQLRLDLEKETVDLVHTKHTEIQDLPGRIPQDTARYHFFL
SQ  YKHSHEGDHLESVVFIYSMPGYKCSIKERMLYSSCKNRLLDSVEQDFLMEIAKKIEIEDGAELTDEFLYDEVHPKQHAFK
SQ  QAFAKPKGPAGKRGQKRLIKGPGENGEDS
//
ID  Q5ZM35;
PN  Twinfilin-2;
GN  TWF2;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization. {ECO:0000250}.
DR  UNIPROT: Q5ZM35;
DR  Pfam: PF00241;
DR  PROSITE: PS51263;
DE  Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005884;
GO  GO:0005737;
GO  GO:0030016;
GO  GO:0048471;
GO  GO:0051015;
GO  GO:0003785;
GO  GO:0030042;
GO  GO:0051016;
GO  GO:0010976;
GO  GO:0010591;
GO  GO:0042989;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTHQTGIHATTELRDFFAKARNGSVRLIKVIIEEEQLVLGAHKELARRWDVDYDAFVLPLLDEQQPCYVLYRLDSQNAQG
SQ  YEWLFISWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDEMFGTVKEDVSLSGYQKHVSSCSAPAPLTAAEQELQQIRIN
SQ  EVKTEISVESKHQTLQGLAFPLQLDAQQAIQTLKQKKINYIQLKLDLERETIDLVHTSPTDISDLPKRIPQDSARYHFFL
SQ  YKHSHEGDYLESVVFIYSMPGYKCSIKERMLYSSCKSRLLDTVEQEFCLEIAKKIEIDDGAELTAEFLYDEVHPKQHAFK
SQ  QAFAKPKGPVGKRGQKRLIKGPGENGEDS
//
ID  Q6GMH3;
PN  Twinfilin-2;
GN  twf2;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization. {ECO:0000250}.
DR  UNIPROT: Q6GMH3;
DR  Pfam: PF00241;
DR  PROSITE: PS51263;
DE  Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005884;
GO  GO:0005737;
GO  GO:0030016;
GO  GO:0048471;
GO  GO:0051015;
GO  GO:0003785;
GO  GO:0030042;
GO  GO:0051016;
GO  GO:0010976;
GO  GO:0010591;
GO  GO:0042989;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MFLVLVVTEELREFLARARNGTGRLIQVLIRDEQLVLGAYREPRHSWDKDYDPVLLPLLDPLEPCYILYRLDSKNAQGYE
SQ  WLFISWSPDQSPVRQKMLYAATRATVKKEFGGGHVKDEMFGTVEEDICLQGYLRHITSCSAPAPLTVAEQELQRIKITEV
SQ  KAEISVDPKHQTLQGLAFPLQAEAKRALKQLAERRINYIQLKLDTEKETIDLVHTSPTDIRDLPCRIPLDTPRYHFFLYK
SQ  HSHEGDYLESVVFIYSMPGYSCSIKERMLYSSCKSRLLDEVERDFHLEVAKKLEIDSGEELTEEYLYDEVHPKQHAHKQA
SQ  FAKPRGPAGKRGNKRLIKGGGENGGNS
//
ID  Q6IBS0;
PN  Twinfilin-2;
GN  TWF2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10406962}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10406962}. Cell projection, stereocilium {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization.
DR  UNIPROT: Q6IBS0;
DR  UNIPROT: Q9Y3F5;
DR  PDB: 2VAC;
DR  PDB: 2W0I;
DR  Pfam: PF00241;
DR  PROSITE: PS51263;
DR  OMIM: 607433;
DR  DisGeNET: 11344;
DE  Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P05060; IntAct: EBI-735501; Score: 0.00
DE  Interaction: Q9NSB4; IntAct: EBI-1061916; Score: 0.00
DE  Interaction: P78386; IntAct: EBI-1062282; Score: 0.00
DE  Interaction: Q9NX58; IntAct: EBI-1062871; Score: 0.00
DE  Interaction: P47755; IntAct: EBI-1063407; Score: 0.00
DE  Interaction: Q15323; IntAct: EBI-1063559; Score: 0.00
DE  Interaction: Q8IV63; IntAct: EBI-1064108; Score: 0.00
DE  Interaction: Q8IUD2; IntAct: EBI-1067184; Score: 0.00
DE  Interaction: P52907; IntAct: EBI-1070516; Score: 0.00
DE  Interaction: O76013; IntAct: EBI-1070997; Score: 0.00
DE  Interaction: Q504Q3; IntAct: EBI-1072020; Score: 0.00
DE  Interaction: Q9BW60; IntAct: EBI-1072650; Score: 0.00
DE  Interaction: P47756; IntAct: EBI-1073048; Score: 0.00
DE  Interaction: Q9P1U1; IntAct: EBI-1080652; Score: 0.00
DE  Interaction: Q81X78; IntAct: EBI-2819826; Score: 0.00
DE  Interaction: Q92949; IntAct: EBI-3916056; Score: 0.37
DE  Interaction: Q13418; IntAct: EBI-3916066; Score: 0.37
DE  Interaction: Q15051; IntAct: EBI-4286917; Score: 0.35
DE  Interaction: P52565; IntAct: EBI-7410932; Score: 0.37
DE  Interaction: O00159; IntAct: EBI-11030803; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q9UHB6; IntAct: EBI-11058729; Score: 0.35
DE  Interaction: Q9WUM4; IntAct: EBI-11065690; Score: 0.35
DE  Interaction: Q8N3V7; IntAct: EBI-11086992; Score: 0.35
DE  Interaction: P35579; IntAct: EBI-11098811; Score: 0.35
DE  Interaction: Q9NYB0; IntAct: EBI-11306750; Score: 0.51
DE  Interaction: Q9NUX5; IntAct: EBI-11306760; Score: 0.37
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q4VC05; IntAct: EBI-21637103; Score: 0.35
DE  Interaction: Q8WUZ0; IntAct: EBI-21637520; Score: 0.35
DE  Interaction: Q9NYL9; IntAct: EBI-21701240; Score: 0.35
DE  Interaction: Q562R1; IntAct: EBI-21867017; Score: 0.35
DE  Interaction: Q01518; IntAct: EBI-21867017; Score: 0.35
DE  Interaction: P68032; IntAct: EBI-21867017; Score: 0.35
DE  Interaction: P62736; IntAct: EBI-21867017; Score: 0.35
DE  Interaction: P60709; IntAct: EBI-21867017; Score: 0.35
DE  Interaction: P40123; IntAct: EBI-21867017; Score: 0.35
DE  Interaction: P05204; IntAct: EBI-20901080; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: P04156; IntAct: EBI-21014654; Score: 0.35
DE  Interaction: Q14108; IntAct: EBI-21264396; Score: 0.35
DE  Interaction: P17813; IntAct: EBI-22197897; Score: 0.35
DE  Interaction: O75368; IntAct: EBI-25373235; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: Q8N488; IntAct: EBI-27111302; Score: 0.35
DE  Interaction: Q8N612; IntAct: EBI-34574737; Score: 0.27
GO  GO:0005884;
GO  GO:0005737;
GO  GO:0070062;
GO  GO:0030175;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0030016;
GO  GO:0048471;
GO  GO:0032420;
GO  GO:0051015;
GO  GO:0003785;
GO  GO:0005524;
GO  GO:0045296;
GO  GO:0005546;
GO  GO:0005080;
GO  GO:0003723;
GO  GO:0030042;
GO  GO:0051016;
GO  GO:0030030;
GO  GO:0071363;
GO  GO:0071300;
GO  GO:0030837;
GO  GO:0045773;
GO  GO:0010592;
GO  GO:0010976;
GO  GO:0032956;
GO  GO:0010591;
GO  GO:0032532;
GO  GO:0042989;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHQTGIHATEELKEFFAKARAGSVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQQPCYLLYRLDSQNAQG
SQ  FEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCAAPAPLTSAERELQQIRIN
SQ  EVKTEISVESKHQTLQGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTEPTDVAQLPSRVPRDAARYHFFL
SQ  YKHTHEGDPLESVVFIYSMPGYKCSIKERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFK
SQ  QAFAKPKGPGGKRGHKRLIRGPGENGDDS
//
ID  Q9Z0P5;
PN  Twinfilin-2;
GN  Twf2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19955359}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10406962}. Cell projection, stereocilium {ECO:0000269|PubMed:19774077, ECO:0000269|PubMed:19955359}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization. Isoform 2 found also along myofibrils in cardiomyocytes (PubMed:18837697). Localized in cochlea hair cells to the tips of the middle and short rows of stereocilia (PubMed:19955359). {ECO:0000269|PubMed:18837697, ECO:0000269|PubMed:19955359}.
DR  UNIPROT: Q9Z0P5;
DR  UNIPROT: Q3TD06;
DR  UNIPROT: Q3TZG2;
DR  UNIPROT: Q8BN77;
DR  UNIPROT: Q9DCK8;
DR  PDB: 7DS3;
DR  Pfam: PF00241;
DR  PROSITE: PS51263;
DE  Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia. {ECO:0000269|PubMed:18837697, ECO:0000269|PubMed:19955359}.
DE  Reference Proteome: Yes;
DE  Interaction: P52927; IntAct: EBI-9986179; Score: 0.35
DE  Interaction: Q93KQ6; IntAct: EBI-16142792; Score: 0.35
GO  GO:0005884;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0030175;
GO  GO:0030426;
GO  GO:0030027;
GO  GO:0030016;
GO  GO:0048471;
GO  GO:0032420;
GO  GO:0051015;
GO  GO:0003785;
GO  GO:0005524;
GO  GO:0005546;
GO  GO:0005080;
GO  GO:0030042;
GO  GO:0051016;
GO  GO:0030030;
GO  GO:0071363;
GO  GO:0071300;
GO  GO:0035556;
GO  GO:0030837;
GO  GO:0045773;
GO  GO:0010592;
GO  GO:0010976;
GO  GO:0032956;
GO  GO:0010591;
GO  GO:0032532;
GO  GO:0042989;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHQTGIHATEELKEFFAKARAGSIRLIKVIIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQEPCYLLFRLDSQNAQG
SQ  FEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSLAGYQKHLSSCAAPAPLTSAERELQQIRIN
SQ  EVKTEISVESKHQTLQGLAFPLQPEAQRALQQLKQKTVNYIQLKLDLERETIELVHTEPTNVAQLPSRIPRDAARYHFFL
SQ  YKHTHEGDALESVVFIYSMPGYKCSIKERMLYSSCKSRLLDSVEQDFQLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFK
SQ  QAFAKPKGPGGKRGHKRLIRGPGENGEDS
//
ID  Q5RFH1;
PN  Twinfilin-2;
GN  TWF2;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, stereocilium {ECO:0000250}. Note=Perinuclear and G-actin-rich cortical actin structure sublocalization. {ECO:0000250}.
DR  UNIPROT: Q5RFH1;
DR  Pfam: PF00241;
DR  PROSITE: PS51263;
DE  Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005856;
GO  GO:0048471;
GO  GO:0032420;
GO  GO:0003779;
GO  GO:0030030;
GO  GO:0030837;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  ATEELKEFFAKARAGSVRLIKVVIEDEQLVLGASQEPVGRWDRDYDRAVLPLLDAQQPCYLLYRLDSQNAQGFEWLFLAW
SQ  SPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCAAPAPLTSAERELQQIRINEVKTEISV
SQ  ESKHQTLQGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTESTDVAQLPSRVPRDAARYHFFLYKHTHEGD
SQ  LLESVVFIYSMPGYKCSIEERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFKQAFAKPKG
SQ  PGGKRGHKRLIRGPGENGDDS
//
ID  Q2TAA8;
PN  Translin-associated factor X-interacting protein 1;
GN  TSNAXIP1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99P25}.
DR  UNIPROT: Q2TAA8;
DR  UNIPROT: Q9P105;
DR  Pfam: PF15739;
DR  OMIM: 607720;
DR  DisGeNET: 55815;
DE  Function: Possible role in spermatogenesis. {ECO:0000250|UniProtKB:Q99P25}.
DE  Reference Proteome: Yes;
DE  Interaction: Q06787; IntAct: EBI-21383952; Score: 0.00
DE  Interaction: P04792; IntAct: EBI-6872495; Score: 0.37
DE  Interaction: H9XIJ5; IntAct: EBI-11514411; Score: 0.37
DE  Interaction: Q96MY7; IntAct: EBI-24290158; Score: 0.56
DE  Interaction: O00311; IntAct: EBI-24320121; Score: 0.56
DE  Interaction: Q99633; IntAct: EBI-24374781; Score: 0.56
DE  Interaction: Q9NZD8; IntAct: EBI-24379551; Score: 0.56
DE  Interaction: Q969U6; IntAct: EBI-21778221; Score: 0.35
DE  Interaction: Q8WXW3; IntAct: EBI-21778221; Score: 0.35
DE  Interaction: Q7Z3E2; IntAct: EBI-21778221; Score: 0.35
DE  Interaction: Q6V1X1; IntAct: EBI-21778221; Score: 0.35
DE  Interaction: O60763; IntAct: EBI-21778221; Score: 0.35
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGGHLSPWPTYTSGQTILQNRKPCSDDYRKRVGSCQQHPFRTAKPQYLEELENYLRKELLLLDLGTDSTQELRLQPYREI
SQ  FEFFIEDFKTYKPLLSSIKNAYEGMLAHQREKIRALEPLKAKLVTVNEDCNERILAMRAEEKYEISLLKKEKMNLLKLID
SQ  KKNEEKISLQSEVTKLRKNLAEEYLHYLSERDACKILIADLNELRYQREDMSLAQSPGIWGEDPVKLTLALKMTRQDLTR
SQ  TQMELNNMKANFGDVVPRRDFEMQEKTNKDLQEQLDTLRASYEEVRKEHEILMQLHMSTLKERDQFFSELQEIQRTSTPR
SQ  PDWTKCKDVVAGGPERWQMLAEGKNSDQLVDVLLEEIGSGLLREKDFFPGLGYGEAIPAFLRFDGLVENKKPSKKDVVNL
SQ  LKDAWKERLAEEQKETFPDFFFNFLEHRFGPSDAMAWAYTIFENIKIFHSNEVMSQFYAVLMGKRSENVYVTQKETVAQL
SQ  LKEMTNADSQNEGLLTMEQFNTVLKSTFPLKTEEQIQELMEAGGWHPSSSNADLLNYRSLFMEDEEGQSEPFVQKLWEQY
SQ  MDEKDEYLQQLKQELGIELHEEVTLPKLRGGLMTIDPSLDKQTVNTYMSQAFQLPESEMPEEGDEKEEAVVEILQTALER
SQ  LQVIDIRRVGPREPEPAS
//
ID  Q99P25;
PN  Translin-associated factor X-interacting protein 1;
GN  Tsnaxip1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12036294}.
DR  UNIPROT: Q99P25;
DR  UNIPROT: Q9DA98;
DR  Pfam: PF15739;
DE  Function: Possible role in spermatogenesis. {ECO:0000269|PubMed:12036294}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MANLQERKSFSKPRISIQASGGTPEAKGIEKRKLSQKRRTLPLQLSLGGHLSPWPTYTSGQTVLHNRKPCSDDSRNRANS
SQ  CQQQSMSISKPKYLEQLENYLRKELLLLDLSTDSAQELRLQPYREIFEFFIEDFKTYKPLLSSIKNAYEVMLAHQKERIR
SQ  SLEPLKAKIVTMNEDCSERVLAMRAEERYEISVLKKEKMNLLKLIDKKNEEKISLQSEVAKLRRSLAEEYLRYLTERDAR
SQ  KILIGDLNELRYQQEDMSLAQTPGVWGEDPVKLTLALKMTRQDLTRTQMELNTMKANSGDVVPRRDLEMQEKTNMELQEQ
SQ  LESLKADYEEVQKEHELLLQLHMSTLKERDQFYNELQEIQRTSTPRPDWTKCESIIAGGPERWLVLAEGKNSDQLVDVLL
SQ  EEIGMGLLREKDFFPGLGFGDAIPPFLRFDGPVKNKKPSKKEVVNLLKDAWKERIAEEQKEPFPDFFFNFLERRFGVNDA
SQ  MAWAYTIFENIKLFRSSEIMNQFYAVLMGKNLESVYINQKKTLSHLLKELLSVDTQNEGSITMEQFSTILKTTFPLKKEE
SQ  QIQELMEAVGWGPDSSNTDMLNYRSLFNEDEEGQSEPFVQRLWEQYESDKEAYLEELKQELDLDPLEDVTLLKMRGTLMN
SQ  IDPTMDKQTLSAYLSQAYQIPAIDVPLEDEEKQGIISIKVETALDRLRMADTKRVGPREPDPAS
//
ID  Q9NUQ3;
PN  Gamma-taxilin;
GN  TXLNG;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15911876}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8BHN1}.
DR  UNIPROT: Q9NUQ3;
DR  UNIPROT: Q2KQ75;
DR  UNIPROT: Q5JNZ7;
DR  UNIPROT: Q9P0X1;
DR  Pfam: PF09728;
DR  OMIM: 300677;
DR  DisGeNET: 55787;
DE  Function: May be involved in intracellular vesicle traffic. Inhibits ATF4-mediated transcription, possibly by dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May be involved in regulating bone mass density through an ATF4-dependent pathway. May be involved in cell cycle progression. {ECO:0000269|PubMed:15911876, ECO:0000269|PubMed:18068885}.
DE  Reference Proteome: Yes;
DE  Interaction: P61244; IntAct: EBI-3445069; Score: 0.00
DE  Interaction: Q9UNE7; IntAct: EBI-9395575; Score: 0.35
DE  Interaction: P97801; IntAct: EBI-11068420; Score: 0.35
DE  Interaction: P0C0A3; IntAct: EBI-11116514; Score: 0.35
DE  Interaction: Q15154; IntAct: EBI-11366535; Score: 0.27
DE  Interaction: Q6ZU80; IntAct: EBI-11370150; Score: 0.27
DE  Interaction: Q7Z7A1; IntAct: EBI-11371427; Score: 0.27
DE  Interaction: Q8TES7; IntAct: EBI-11374846; Score: 0.27
DE  Interaction: Q96ST8; IntAct: EBI-11377220; Score: 0.27
DE  Interaction: Q9Y2D8; IntAct: EBI-11379249; Score: 0.27
DE  Interaction: Q9Y2I6; IntAct: EBI-11379511; Score: 0.27
DE  Interaction: O75665; IntAct: EBI-11380793; Score: 0.27
DE  Interaction: Q5TB80; IntAct: EBI-11385924; Score: 0.27
DE  Interaction: Q66GS9; IntAct: EBI-11386281; Score: 0.27
DE  Interaction: Q8N0Z3; IntAct: EBI-11392023; Score: 0.27
DE  Interaction: Q96MT8; IntAct: EBI-11396049; Score: 0.27
DE  Interaction: Q9C0F1; IntAct: EBI-11397104; Score: 0.27
DE  Interaction: P40222; IntAct: EBI-21888796; Score: 0.51
DE  Interaction: Q8WVK2; IntAct: EBI-21500567; Score: 0.35
DE  Interaction: Q96DX7; IntAct: EBI-21543552; Score: 0.35
DE  Interaction: B3KSW4; IntAct: EBI-21551649; Score: 0.35
DE  Interaction: Q9NWT6; IntAct: EBI-21638930; Score: 0.35
DE  Interaction: Q96FN4; IntAct: EBI-21659658; Score: 0.35
DE  Interaction: Q9NYP9; IntAct: EBI-21663541; Score: 0.35
DE  Interaction: Q8N4N8; IntAct: EBI-21706359; Score: 0.35
DE  Interaction: Q96HH9; IntAct: EBI-21783352; Score: 0.35
DE  Interaction: Q8N3L3; IntAct: EBI-21845486; Score: 0.35
DE  Interaction: Q92844; IntAct: EBI-20737201; Score: 0.35
DE  Interaction: Q9NPJ6; IntAct: EBI-25472202; Score: 0.42
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0140297;
GO  GO:0019905;
GO  GO:0007049;
GO  GO:0030500;
GO  GO:0051726;
GO  GO:0010564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATRVEEAARGRGGGAEEATEAGRGGRRRSPRQKFEIGTMEEAGICGLGVKADMLCNSQSNDILQHQGSNCGGTSNKHSL
SQ  EEDEGSDFITENRNLVSPAYCTQESREEIPGGEARTDPPDGQQDSECNRNKEKTLGKEVLLLMQALNTLSTPEEKLAALC
SQ  KKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKEA
SQ  TAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADE
SQ  KHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWR
SQ  TKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQVSIKAAIKAANRDLATPVMQPC
SQ  TALDSHKELNTSSKRALGAHLEAEPKSQRSAVQKPPSTGSAPAIESVD
//
ID  Q8BHN1;
PN  Gamma-taxilin;
GN  Txlng;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:19913514}. Cytoplasm, cytosol {ECO:0000269|PubMed:19913514}.
DR  UNIPROT: Q8BHN1;
DR  UNIPROT: A2AFJ5;
DR  UNIPROT: Q148Z8;
DR  UNIPROT: Q2LGB1;
DR  UNIPROT: Q2PMX1;
DR  UNIPROT: Q8BP11;
DR  Pfam: PF09728;
DE  Function: May be involved in intracellular vesicle traffic (By similarity). Inhibits ATF4-mediated transcription, possibly by dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May be involved in regulating bone mass density through an ATF4-dependent pathway. May be involved in cell cycle progression. {ECO:0000250, ECO:0000269|PubMed:15911876, ECO:0000269|PubMed:19016261, ECO:0000269|PubMed:19913514}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8N3L3; IntAct: EBI-6116849; Score: 0.35
DE  Interaction: P40222; IntAct: EBI-6116849; Score: 0.35
DE  Interaction: Q9UHD2; IntAct: EBI-6116849; Score: 0.50
GO  GO:0005829;
GO  GO:0031965;
GO  GO:0140297;
GO  GO:0019905;
GO  GO:0007049;
GO  GO:0030500;
GO  GO:0051726;
GO  GO:0010564;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MATRLEEVTRGRGGGTEEASEGGRGGRRRSPPQKFEIGTMEEARICGLGVKADMVCNSQANDILQHQDPSCGGTTKKHSL
SQ  EGDEGSDFITKNRNLVSSVFCTQEKREEIPGREARTGPPDGQQDSECSRNKEKTLGKEVLLLMQALNTLSTPEEKLAALC
SQ  KKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKEA
SQ  TAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADE
SQ  KHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWR
SQ  TKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKEQVSIKAADGDLVSPATQPCAVLD
SQ  SFKETSRRTLGMHLEARAKSVCEKSAAQKPSSSGSPAQGIESVD
//
ID  O42091;
PN  Tyrosine 3-monooxygenase;
GN  th;
OS  7936;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Note=Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P24529}.
DR  UNIPROT: O42091;
DR  Pfam: PF00351;
DR  Pfam: PF12549;
DR  PROSITE: PS00367;
DR  PROSITE: PS51410;
DE  Function: Plays an important role in the physiology of adrenergic neurons. {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0030424;
GO  GO:0048471;
GO  GO:0005506;
GO  GO:0004511;
GO  GO:0009072;
GO  GO:0042416;
GO  GO:0042136;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPISNSSGSSTKSITRAGSELDRADSITSPRFVGRRQSLIEDARKEREAAAAAESSEASEQIVFDEEDGKALLNLFFTLR
SQ  SSKIPALSRALKVFETFEAKIHHLETRTRRKPKDSLEDLEYFVRCEVHLADVSTLISSIRRIAEDVRTTKEVKFHWFPKK
SQ  ISELDSCHHLVTKFDPDLDQDHPGFTDPVYRQRRRMIGEIAFRYKHGEPIPRVEYTEEEIGTWREVYSTLRDLYTTHACS
SQ  EHLEAFRLLERHCGYSPNSIPQLEDVSHFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCV
SQ  HELLGHVPMLADRTFAQFSQNIGLASLGASEEDIEKLSTLYWFTVEFGLCKQGDGVKAYGAGLLSSYGELVHSLSDEPER
SQ  REFDPEAAAAEPYQDQNYQSVYFVSESFTDAKEKLRVYAAGINRPFSVRFDPYTYSIEVLDNPLKIRGGLESVKDELKVL
SQ  TDALNVLA
//
ID  P17289;
PN  Tyrosine 3-monooxygenase;
GN  TH;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Nucleus {ECO:0000250|UniProtKB:P04177}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Cytoplasm {ECO:0000250|UniProtKB:P04177}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P04177}. Note=When phosphorylated at Ser-19 shows a nuclear distribution and when phsphorylated at Ser-31 as well at Ser-40 shows a cytosolic distribution (By similarity). Expressed in dopaminergic axons and axon terminals (By similarity). {ECO:0000250|UniProtKB:P04177, ECO:0000250|UniProtKB:P07101}.
DR  UNIPROT: P17289;
DR  Pfam: PF00351;
DR  Pfam: PF12549;
DR  PROSITE: PS51410;
DE  Function: Catalyzes the conversion of L-tyrosine to L- dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (By similarity). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity). {ECO:0000250|UniProtKB:P04177, ECO:0000250|UniProtKB:P07101, ECO:0000250|UniProtKB:P24529}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0008021;
GO  GO:0005506;
GO  GO:0004511;
GO  GO:0006585;
GO  GO:0007507;
GO  GO:1990384;
GO  GO:0042136;
GO  GO:0045471;
GO  GO:0001666;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTPNAASPQAKGFRRAVSELDAKQAEAIMSPRFVGRRQSLIQDARKEREKAEAAASSSESAEAAAWLERDGEAVLTLLF
SQ  ALPPTRPPALTRAIKVFETFEAHLHHLETRPAQPLRAGSPPLECFVRCEVPGPVVPALLSALRRVAEDVRAAGESKVLWF
SQ  PRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYPTH
SQ  ACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPAAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEP
SQ  ECCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLSEE
SQ  PEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPHAIRHALDGVQDEM
SQ  QALAHALNAIS
//
ID  A8X3V8;
PN  Tyrosine 3-monooxygenase;
GN  cat;
OS  6238;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Note=Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P24529}.
DR  UNIPROT: A8X3V8;
DR  Pfam: PF00351;
DR  PROSITE: PS00367;
DR  PROSITE: PS51410;
DE  Function: Involved in the synthesis of catecholamines, such as dopamine. Has a role in serotonin signaling. Required for normal explorative and foraging behavior (By similarity). {ECO:0000250|UniProtKB:P90986}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005506;
GO  GO:0004511;
GO  GO:0007610;
GO  GO:0006585;
GO  GO:0042136;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSLTNPTTVMEEEEVPVAAPIRRGNKNPRRYSLVHQASCETQHHIGIRRQNTIQHRKQLTDQMREQKILQQLNDEGVEV
SQ  IFAANDVSSIDFSVIVTSTDYISTFVSDILYNMKSAGVQICHVETRESKAVSGHDVLLDCRATKNQLIKAAELLTQNHVA
SQ  LTHFSIFSKKSVEKSQSMIWFPRHISELDQCSKCITKYEPTTDPRHPGHGDDEYIARRKFLNDQALEFKFGDEIGYVEYT
SQ  EDEHATWKAVYEKLGGLHESHTCSVYRQNLKILQKEKVLTADRIPQIRDVNKFLQKKTGFELRPCSGLLSARDFLASLAF
SQ  RVFQTTTYLRHHKSPHHSPEPDLIHELLGHVPMFSDPLLAQMSQDIGLMSLGASDEHIEKLATVYWFIVEFGLCKEDGKL
SQ  KAIGAGLLSAYGELIHACSDAPEHKDFDPAVTAIQKYEDDDYQPLYFVADSIHDALAKLRKYASSMDRPFSVVYDPFTKS
SQ  IETIQSSADLEKAFSRLSNDLSAITHAADRMKISITA
//
ID  P90986;
PN  Tyrosine 3-monooxygenase;
GN  cat;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Note=Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P24529}.
DR  UNIPROT: P90986;
DR  UNIPROT: E7EM31;
DR  UNIPROT: F2WZ21;
DR  UNIPROT: Q5R3Y3;
DR  UNIPROT: Q5R3Y4;
DR  Pfam: PF00351;
DR  PROSITE: PS00367;
DR  PROSITE: PS51410;
DE  Function: Involved in the synthesis of catecholamines, such as dopamine. Has a role in serotonin signaling. Required for normal explorative and foraging behavior. In response to food, involved in promoting the dopamine-mediated suppression of crh-1/CREB1 transcription factor activation in cholinergic SIA neurons (PubMed:19609300). Modulates male mating behavior by controlling the protrusion of copulatory spicules from the tail of males during hermaphrodite vulval location (PubMed:23166505). {ECO:0000269|PubMed:14739932, ECO:0000269|PubMed:14762140, ECO:0000269|PubMed:17196529, ECO:0000269|PubMed:17268620, ECO:0000269|PubMed:19609300, ECO:0000269|PubMed:23166505}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005506;
GO  GO:0004511;
GO  GO:0071419;
GO  GO:0042416;
GO  GO:0006585;
GO  GO:0046959;
GO  GO:0007638;
GO  GO:0090327;
GO  GO:0042136;
GO  GO:1902437;
GO  GO:0040012;
GO  GO:0032094;
GO  GO:0034609;
GO  GO:0034607;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSLTNNTFMEEEPRGVTVIATKVAENSKNPRRYSLVHQASCETQHHKGIRRQNTIQHRKQLTDQMRCQKILQQLNDEGI
SQ  EVIFTANDVTPIEFSIILTSTDPTLSNFVSDILQNMSSAKVQICHVETRGNEASHDVLLACKATKNQLIHSAELLTQNHV
SQ  ALTKFSIFAKKLSDEKNQSQIWFPRHISELDQCSKCITKYEPTTDPRHPGHGDVAYIARRKFLNDQALEFKFGDEIGYVD
SQ  YTEEEHATWKAVYEKLGDLHLSHTCAVYRQNLKILQEEKVLTADRIPQIRDVNKFLQKKTGFELRPCSGLLSARDFLASL
SQ  AFRVFQTTTYLRHHKSPHHSPEPDLIHELLGHVPMFSDPLLAQMSQDIGLMSLGASDEHIEKLSTVYWFIVEFGLCKEDG
SQ  KLKAIGAGLLSAYGELMHACSDAPEHKDFDPAVTAVQKYEDDDYQPLYFVADSIHDALAKLRKYASSMDRPFSVVYDPFT
SQ  KSIEAIESSADLEKAFSRLSNDLSAITHAADRMKISITM
//
ID  Q76IQ3;
PN  Tyrosine 3-monooxygenase;
GN  TH;
OS  9615;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Nucleus {ECO:0000250|UniProtKB:P04177}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Cytoplasm {ECO:0000250|UniProtKB:P04177}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P04177}. Note=When phosphorylated at Ser-19 shows a nuclear distribution and when phsphorylated at Ser-31 as well at Ser-40 shows a cytosolic distribution (By similarity). Expressed in dopaminergic axons and axon terminals (By similarity). {ECO:0000250|UniProtKB:P04177, ECO:0000250|UniProtKB:P07101}.
DR  UNIPROT: Q76IQ3;
DR  Pfam: PF00351;
DR  Pfam: PF12549;
DR  PROSITE: PS00367;
DR  PROSITE: PS51410;
DE  Function: Catalyzes the conversion of L-tyrosine to L- dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (By similarity). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity). {ECO:0000250|UniProtKB:P04177, ECO:0000250|UniProtKB:P07101, ECO:0000250|UniProtKB:P24529}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0008021;
GO  GO:0005506;
GO  GO:0004511;
GO  GO:0009072;
GO  GO:0042416;
GO  GO:1990384;
GO  GO:0042136;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTPNTASPQAKGFRRAVSELDAKQAEAIMSPRFIGRRQSLIEDARKEREKAEAASAASSEPGDLLEAAVSKEKDGKAML
SQ  NLLFTLRGAKTSSLSRAVKAFETFEAQIHHLETRPVQRPRAGGPHLEYFVRCEVPSADLPALLSSVRRVAEDVRGAGENK
SQ  VLWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYKHGDPIPRVEYTAEEIATWKEVYTTLKSL
SQ  YVTHACREHLEAFQLLERFSGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMH
SQ  SPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHS
SQ  LSEEPEIRAFDPDAAAVQPYQDQTYQSVYFVSESFSDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHAIRRSLEGV
SQ  QDELHTLAHALSAIG
//
ID  P18459;
PN  Tyrosine 3-monooxygenase;
GN  ple;
OS  7227;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Note=Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P24529}.
DR  UNIPROT: P18459;
DR  UNIPROT: Q24000;
DR  UNIPROT: Q8SY95;
DR  Pfam: PF00351;
DR  PROSITE: PS00367;
DR  PROSITE: PS51410;
DE  Function: Plays an important role in the physiology of adrenergic neurons.
DE  Reference Proteome: Yes;
DE  Interaction: P49415; IntAct: EBI-198264; Score: 0.00
DE  Interaction: Q9W5A9; IntAct: EBI-198269; Score: 0.00
DE  Interaction: A0A0B4K7S6; IntAct: EBI-198274; Score: 0.00
DE  Interaction: Q9VGY3; IntAct: EBI-198279; Score: 0.00
DE  Interaction: Q9VDH8; IntAct: EBI-198284; Score: 0.00
DE  Interaction: Q9VR99; IntAct: EBI-198289; Score: 0.00
DE  Interaction: Q7K180; IntAct: EBI-198294; Score: 0.00
DE  Interaction: Q9W418; IntAct: EBI-198299; Score: 0.00
DE  Interaction: Q9W3Z4; IntAct: EBI-198304; Score: 0.00
DE  Interaction: Q9VPY2; IntAct: EBI-198309; Score: 0.00
DE  Interaction: Q9VBQ5; IntAct: EBI-198314; Score: 0.00
DE  Interaction: Q23972; IntAct: EBI-198319; Score: 0.00
DE  Interaction: Q24141; IntAct: EBI-198324; Score: 0.00
DE  Interaction: Q9VVL6; IntAct: EBI-198329; Score: 0.00
DE  Interaction: Q9VTH5; IntAct: EBI-198334; Score: 0.00
DE  Interaction: Q9V466; IntAct: EBI-198339; Score: 0.00
DE  Interaction: Q9VWQ2; IntAct: EBI-198344; Score: 0.00
DE  Interaction: Q9VW52; IntAct: EBI-198349; Score: 0.00
DE  Interaction: Q9VAF3; IntAct: EBI-198354; Score: 0.00
DE  Interaction: P05084; IntAct: EBI-198359; Score: 0.00
DE  Interaction: P12370; IntAct: EBI-873996; Score: 0.27
DE  Interaction: P48596; IntAct: EBI-874012; Score: 0.27
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005506;
GO  GO:0004511;
GO  GO:0048085;
GO  GO:0008344;
GO  GO:0006584;
GO  GO:0007619;
GO  GO:0048067;
GO  GO:0048066;
GO  GO:0042416;
GO  GO:0006585;
GO  GO:0042417;
GO  GO:0008049;
GO  GO:0042136;
GO  GO:0048082;
GO  GO:2000274;
GO  GO:0042542;
GO  GO:0009611;
GO  GO:0040040;
GO  GO:0043052;
GO  GO:0035220;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMAVAAAQKNREMFAIKKSYSIENGYPSRRRSLVDDARFETLVVKQTKQTVLEEARSKANDDSLEDCIVQAQEHIPSEQD
SQ  VELQDEHANLENLPLEEYVPVEEDVEFESVEQEQSESQSQEPEGNQQPTKNDYGLTEDEILLANAASESSDAEAAMQSAA
SQ  LVVRLKEGISSLGRILKAIETFHGTVQHVESRQSRVEGVDHDVLIKLDMTRGNLLQLIRSLRQSGSFSSMNLMADNNLNV
SQ  KAPWFPKHASELDNCNHLMTKYEPDLDMNHPGFADKVYRQRRKEIAEIAFAYKYGDPIPFIDYSDVEVKTWRSVFKTVQD
SQ  LAPKHACAEYRAAFQKLQDEQIFVETRLPQLQEMSDFLRKNTGFSLRPAAGLLTARDFLASLAFRIFQSTQYVRHVNSPY
SQ  HTPEPDSIHELLGHMPLLADPSFAQFSQEIGLASLGASDEEIEKLSTVYWFTVEFGLCKEHGQIKAYGAGLLSSYGELLH
SQ  AISDKCEHRAFEPASTAVQPYQDQEYQPIYYVAESFEDAKDKFRRWVSTMSRPFEVRFNPHTERVEVLDSVDKLETLVHQ
SQ  MNTEILHLTNAISKLRRPF
//
ID  P07101;
PN  Tyrosine 3-monooxygenase;
GN  TH;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Nucleus {ECO:0000250|UniProtKB:P04177}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Cytoplasm {ECO:0000250|UniProtKB:P04177}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P04177}. Note=When phosphorylated at Ser-19 shows a nuclear distribution and when phosphorylated at Ser-31 as well at Ser-40 shows a cytosolic distribution (By similarity). Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P04177}.
DR  UNIPROT: P07101;
DR  UNIPROT: B7ZL70;
DR  UNIPROT: B7ZL73;
DR  UNIPROT: Q0PWM2;
DR  UNIPROT: Q0PWM3;
DR  UNIPROT: Q15585;
DR  UNIPROT: Q15588;
DR  UNIPROT: Q15589;
DR  UNIPROT: Q2M3B4;
DR  PDB: 2XSN;
DR  PDB: 4J6S;
DR  PDB: 6ZN2;
DR  PDB: 6ZVP;
DR  PDB: 6ZZU;
DR  PDB: 7A2G;
DR  PDB: 7PIM;
DR  Pfam: PF00351;
DR  Pfam: PF12549;
DR  PROSITE: PS00367;
DR  PROSITE: PS51410;
DR  OMIM: 191290;
DR  OMIM: 605407;
DR  DisGeNET: 7054;
DE  Function: Catalyzes the conversion of L-tyrosine to L- dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (PubMed:17391063, PubMed:1680128, PubMed:15287903, PubMed:8528210, Ref.18, PubMed:34922205, PubMed:24753243). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity). {ECO:0000250|UniProtKB:P04177, ECO:0000250|UniProtKB:P24529, ECO:0000269|PubMed:15287903, ECO:0000269|PubMed:1680128, ECO:0000269|PubMed:17391063, ECO:0000269|PubMed:24753243, ECO:0000269|PubMed:34922205, ECO:0000269|PubMed:8528210, ECO:0000269|Ref.18}. [Isoform 5]: Lacks catalytic activity. {ECO:0000269|PubMed:17391063}. [Isoform 6]: Lacks catalytic activity. {ECO:0000269|PubMed:17391063}.
DE  Disease: Segawa syndrome autosomal recessive (ARSEGS) [MIM:605407]: A form of DOPA-responsive dystonia presenting in infancy or early childhood. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Some cases present with parkinsonian symptoms in infancy. Unlike all other forms of dystonia, it is an eminently treatable condition, due to a favorable response to L-DOPA. {ECO:0000269|PubMed:10585338, ECO:0000269|PubMed:11196107, ECO:0000269|PubMed:11246459, ECO:0000269|PubMed:15505183, ECO:0000269|PubMed:15747353, ECO:0000269|PubMed:16049992, ECO:0000269|PubMed:17696123, ECO:0000269|PubMed:18058633, ECO:0000269|PubMed:18554280, ECO:0000269|PubMed:19491146, ECO:0000269|PubMed:20056467, ECO:0000269|PubMed:20430833, ECO:0000269|PubMed:21940685, ECO:0000269|PubMed:22264700, ECO:0000269|PubMed:22815559, ECO:0000269|PubMed:23762320, ECO:0000269|PubMed:23939262, ECO:0000269|PubMed:24753243, ECO:0000269|PubMed:7814018, ECO:0000269|PubMed:8528210, ECO:0000269|PubMed:8817341, ECO:0000269|PubMed:9613851, ECO:0000269|PubMed:9703425}. Note=The disease is caused by variants affecting the gene represented in this entry. Note=May play a role in the pathogenesis of Parkinson disease (PD). A genome-wide copy number variation analysis has identified a 34 kilobase deletion over the TH gene in a PD patient but not in any controls. {ECO:0000269|PubMed:20809526}.
DE  Reference Proteome: Yes;
DE  Interaction: P68509; IntAct: EBI-7146814; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-7275920; Score: 0.53
DE  Interaction: P61981; IntAct: EBI-7275933; Score: 0.35
DE  Interaction: P63103; IntAct: EBI-7846709; Score: 0.35
DE  Interaction: P07101; IntAct: EBI-24276311; Score: 0.63
DE  Interaction: P29762; IntAct: EBI-24285006; Score: 0.56
DE  Interaction: Q9UJ04; IntAct: EBI-24312149; Score: 0.56
DE  Interaction: O75928; IntAct: EBI-24482857; Score: 0.56
DE  Interaction: Q9UHX1; IntAct: EBI-24487537; Score: 0.56
DE  Interaction: Q5MCW4; IntAct: EBI-24530033; Score: 0.56
DE  Interaction: P08651; IntAct: EBI-24703454; Score: 0.56
DE  Interaction: C9J7I0; IntAct: EBI-24710004; Score: 0.56
DE  Interaction: Q99750; IntAct: EBI-24384608; Score: 0.56
DE  Interaction: P61978; IntAct: EBI-24440007; Score: 0.56
DE  Interaction: P0DJD3; IntAct: EBI-24469611; Score: 0.56
DE  Interaction: Q8NCN2; IntAct: EBI-21751771; Score: 0.35
DE  Interaction: Q9UL54; IntAct: EBI-21751771; Score: 0.35
DE  Interaction: Q9UKB3; IntAct: EBI-21751771; Score: 0.35
DE  Interaction: Q8IUW5; IntAct: EBI-21751771; Score: 0.35
DE  Interaction: Q7LBC6; IntAct: EBI-21751771; Score: 0.35
DE  Interaction: Q6P444; IntAct: EBI-21751771; Score: 0.35
DE  Interaction: Q15750; IntAct: EBI-21751771; Score: 0.35
DE  Interaction: O43318; IntAct: EBI-21751771; Score: 0.35
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0009898;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0033162;
GO  GO:0005739;
GO  GO:0043005;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005790;
GO  GO:0008021;
GO  GO:0043195;
GO  GO:0016597;
GO  GO:0035240;
GO  GO:0019899;
GO  GO:0008199;
GO  GO:0008198;
GO  GO:0042802;
GO  GO:0019825;
GO  GO:0019904;
GO  GO:0034617;
GO  GO:0004511;
GO  GO:0015842;
GO  GO:0009653;
GO  GO:0009887;
GO  GO:0071312;
GO  GO:0071333;
GO  GO:0071363;
GO  GO:0071287;
GO  GO:0071316;
GO  GO:0071466;
GO  GO:0021987;
GO  GO:0042745;
GO  GO:0042416;
GO  GO:0006585;
GO  GO:0042755;
GO  GO:0048596;
GO  GO:0042418;
GO  GO:0042462;
GO  GO:0006631;
GO  GO:0016137;
GO  GO:0007507;
GO  GO:0003007;
GO  GO:1990384;
GO  GO:0033076;
GO  GO:0007612;
GO  GO:0007626;
GO  GO:0007617;
GO  GO:0007613;
GO  GO:0010259;
GO  GO:0042136;
GO  GO:0042421;
GO  GO:0018963;
GO  GO:0052314;
GO  GO:0043473;
GO  GO:0008016;
GO  GO:0014823;
GO  GO:0001975;
GO  GO:0051412;
GO  GO:0051602;
GO  GO:0032355;
GO  GO:0045471;
GO  GO:0045472;
GO  GO:0009635;
GO  GO:0001666;
GO  GO:0035902;
GO  GO:0035900;
GO  GO:0009416;
GO  GO:0032496;
GO  GO:0031667;
GO  GO:0043434;
GO  GO:0046684;
GO  GO:0009651;
GO  GO:0009414;
GO  GO:0010043;
GO  GO:0007605;
GO  GO:0035176;
GO  GO:0006665;
GO  GO:0001963;
GO  GO:0042214;
GO  GO:0007601;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKER
SQ  EAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLE
SQ  YFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEI
SQ  AFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRP
SQ  VAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTL
SQ  YWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYAS
SQ  RIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
//
ID  P24529;
PN  Tyrosine 3-monooxygenase;
GN  Th;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:30936473}. Nucleus {ECO:0000250|UniProtKB:P04177}. Cell projection, axon {ECO:0000269|PubMed:17296554}. Cytoplasm {ECO:0000250|UniProtKB:P04177}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P04177}. Note=When phosphorylated at Ser-19 shows a nuclear distribution and when phsphorylated at Ser-31 as well at Ser-40 shows a cytosolic distribution (By similarity). Expressed in dopaminergic axons and axon terminals (PubMed:17296554). {ECO:0000250|UniProtKB:P04177, ECO:0000269|PubMed:17296554}.
DR  UNIPROT: P24529;
DR  Pfam: PF00351;
DR  Pfam: PF12549;
DR  PROSITE: PS00367;
DR  PROSITE: PS51410;
DE  Function: Catalyzes the conversion of L-tyrosine to L- dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (By similarity). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development(PubMed:30936473). {ECO:0000250|UniProtKB:P04177, ECO:0000250|UniProtKB:P07101, ECO:0000269|PubMed:30936473}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0009898;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0033162;
GO  GO:0005739;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005790;
GO  GO:0008021;
GO  GO:0043195;
GO  GO:0016597;
GO  GO:0035240;
GO  GO:0019899;
GO  GO:0008199;
GO  GO:0008198;
GO  GO:0042802;
GO  GO:0004497;
GO  GO:0019825;
GO  GO:0019904;
GO  GO:0034617;
GO  GO:0004511;
GO  GO:0015842;
GO  GO:0009887;
GO  GO:0042423;
GO  GO:0071312;
GO  GO:0071333;
GO  GO:0071363;
GO  GO:0071287;
GO  GO:0071316;
GO  GO:0071466;
GO  GO:0021987;
GO  GO:0042745;
GO  GO:0042416;
GO  GO:0006585;
GO  GO:0042755;
GO  GO:0048596;
GO  GO:0042418;
GO  GO:0042462;
GO  GO:0006631;
GO  GO:0016137;
GO  GO:0007507;
GO  GO:1990384;
GO  GO:0033076;
GO  GO:0007612;
GO  GO:0007626;
GO  GO:0007617;
GO  GO:0007613;
GO  GO:0010259;
GO  GO:0042136;
GO  GO:0042421;
GO  GO:0018963;
GO  GO:0052314;
GO  GO:0008016;
GO  GO:0014823;
GO  GO:0001975;
GO  GO:0051412;
GO  GO:0051602;
GO  GO:0032355;
GO  GO:0045471;
GO  GO:0045472;
GO  GO:0009635;
GO  GO:0001666;
GO  GO:0035902;
GO  GO:0035900;
GO  GO:0009416;
GO  GO:0032496;
GO  GO:0031667;
GO  GO:0043434;
GO  GO:0046684;
GO  GO:0009651;
GO  GO:0009414;
GO  GO:0010043;
GO  GO:0007605;
GO  GO:0035176;
GO  GO:0006665;
GO  GO:0001963;
GO  GO:0042214;
GO  GO:0007601;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTPSASSPQPKGFRRAVSEQDTKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASAEPGNPLEAVVFEERDGN
SQ  AVLNLLFSLRGTKPSSLSRALKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAR
SQ  EDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGEPIPHVEYTKEEIATWKEVYATL
SQ  KGLYATHACREHLEAFQLLERYCGYREDSIPQLEDVSHFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASS
SQ  PMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGEL
SQ  LHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFSDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIRRSL
SQ  EGVQDELHTLTQALSAIS
//
ID  A0A060X6Z0;
PN  Tyrosine 3-monooxygenase;
GN  th;
OS  8022;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Note=Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P24529}.
DR  UNIPROT: A0A060X6Z0;
DR  Pfam: PF00351;
DR  Pfam: PF12549;
DR  PROSITE: PS51410;
DE  Function: Plays an important role in the physiology of adrenergic neurons. {ECO:0000250|UniProtKB:P24529}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0070852;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005506;
GO  GO:0004511;
GO  GO:0009072;
GO  GO:0042416;
GO  GO:0042136;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPISSSSSSSTKSMRRAASELERSDSVTSPRFIGRRQSLIEDARKEREAAAAAAEAAEATEQIVFEEEDGKALLNLFFTL
SQ  RSSKTPALSRSLKVFETFEAKIHHLETRPCRKPRDSLEGLEYFVRCEVHLSDVSTLISSIKRIAEDVKTTKEVKFHWFPK
SQ  KISELDRCHHLITKFDPDLDQEHPGFTDPVYRQRRKMIGDIAFRYKQGEPIPRVEYTEEEIGTWREVYSTLRDLYTTHAC
SQ  SEHLEAFNLLERHCGYSPENIPQLEDVSRFLRERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDC
SQ  VHELLGHVPILADRVFAQFSQNIGLASLGASEEDIEKLSTLYWFTVEFGLCKQGGIVKAYGAGLLSSYGELVHALSDEPE
SQ  RREFDPEAAAIQPYQDQNYQSVYFVSESFTDAKEKLRSYVAGIKRPFSVRFDPYTYSIEVLDNPLKIRGGLESVKDELKM
SQ  LTDALNVLA
//
ID  P11982;
PN  Tyrosine 3-monooxygenase;
GN  TH;
OS  9006;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Note=Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P24529}.
DR  UNIPROT: P11982;
DR  Pfam: PF00351;
DR  Pfam: PF12549;
DR  PROSITE: PS00367;
DR  PROSITE: PS51410;
DE  Function: Plays an important role in the physiology of adrenergic neurons.
DE  Reference Proteome: No;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0005506;
GO  GO:0004511;
GO  GO:0009072;
GO  GO:0007619;
GO  GO:0042416;
GO  GO:0007625;
GO  GO:0042136;
GO  GO:0060416;
GO  GO:0035176;
GO  GO:0071625;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTPNISTSAAKGFRRAVSELDSKQAEAIMSPRFIGRRQSLIEDARKEREAAAAATDAAESTETIVFEEKDGRAMLNLFF
SQ  MLKGVKTSPLSRALKVFETFEAKIHHLETRLSRKPREGTAELEYFVRCEVHSSDLNTFISSIKRVAEDVRTTKEDKFHWF
SQ  PRKICELDKCHHLVTKFDPDLDLDHPGYSDQVYRQRRKSIAEIAFHYKHGDPIPRVEYTAEETATWKEVYSTLKSLYPTH
SQ  ACKEYLEAFNLLEKFCGYNENNIPQLEEVSRFLKERTGFQLRPVRGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEP
SQ  DCCHELLGHVPMLADKTFAQFSQDIGLASLGATDEEIEKLATLYWFTVEFGLCRQNGIVKAYGAGLLSSYGELIHSLSDE
SQ  PEVRDFDPDAAAVQPCQDQPYQPVYFVSESFSDAKNKLRNYAAHIKRPFSVKYEPYTHSIELLDSPQTICHSLESVRDEL
SQ  HTLINALNVIS
//
ID  P04177;
PN  Tyrosine 3-monooxygenase;
GN  Th;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Nucleus {ECO:0000269|PubMed:21392500}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Cytoplasm {ECO:0000269|PubMed:15496595, ECO:0000269|PubMed:21392500}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:15496595}. Note=When phosphorylated at Ser-19 shows a nuclear distribution and when phsphorylated at Ser-31 as well at Ser- 40 shows a cytosolic distribution (PubMed:21392500). Expressed in dopaminergic axons and axon terminals (By similarity). {ECO:0000250|UniProtKB:P07101, ECO:0000269|PubMed:21392500}.
DR  UNIPROT: P04177;
DR  PDB: 1TOH;
DR  PDB: 2MDA;
DR  PDB: 2TOH;
DR  Pfam: PF00351;
DR  Pfam: PF12549;
DR  PROSITE: PS00367;
DR  PROSITE: PS51410;
DE  Function: Catalyzes the conversion of L-tyrosine to L- dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (By similarity). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan but with lower specificity (PubMed:11922614, PubMed:10933781). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity). {ECO:0000250|UniProtKB:P07101, ECO:0000250|UniProtKB:P24529, ECO:0000269|PubMed:10933781, ECO:0000269|PubMed:11922614}.
DE  Reference Proteome: Yes;
DE  Interaction: P21708; IntAct: EBI-7625716; Score: 0.35
DE  Interaction: P63102; IntAct: EBI-8595319; Score: 0.35
DE  Interaction: B5DFK6; IntAct: EBI-8097124; Score: 0.27
GO  GO:0070161;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0009898;
GO  GO:0031410;
GO  GO:0030659;
GO  GO:0005829;
GO  GO:0030425;
GO  GO:0033162;
GO  GO:0005739;
GO  GO:0043005;
GO  GO:0043025;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0005790;
GO  GO:0008021;
GO  GO:0043195;
GO  GO:0016597;
GO  GO:0035240;
GO  GO:0019899;
GO  GO:0008199;
GO  GO:0008198;
GO  GO:0042802;
GO  GO:0004497;
GO  GO:0019825;
GO  GO:0019904;
GO  GO:0036094;
GO  GO:0034617;
GO  GO:0004511;
GO  GO:0015842;
GO  GO:0009887;
GO  GO:0042423;
GO  GO:0071312;
GO  GO:0071333;
GO  GO:0071363;
GO  GO:0071287;
GO  GO:0071316;
GO  GO:0071466;
GO  GO:0021987;
GO  GO:0042745;
GO  GO:0050890;
GO  GO:0042416;
GO  GO:0006585;
GO  GO:0042755;
GO  GO:0048596;
GO  GO:0042418;
GO  GO:0042462;
GO  GO:0006631;
GO  GO:0016137;
GO  GO:0007507;
GO  GO:1990384;
GO  GO:0033076;
GO  GO:0007612;
GO  GO:0007626;
GO  GO:0007617;
GO  GO:0007613;
GO  GO:0010259;
GO  GO:0042136;
GO  GO:0042421;
GO  GO:0018963;
GO  GO:0052314;
GO  GO:0008016;
GO  GO:0014823;
GO  GO:0001975;
GO  GO:0051412;
GO  GO:0051602;
GO  GO:0032355;
GO  GO:0045471;
GO  GO:0045472;
GO  GO:0070848;
GO  GO:0009635;
GO  GO:0001666;
GO  GO:0035902;
GO  GO:0017085;
GO  GO:0035900;
GO  GO:0009416;
GO  GO:0032496;
GO  GO:0010038;
GO  GO:0035094;
GO  GO:0031667;
GO  GO:0014070;
GO  GO:0043434;
GO  GO:0046684;
GO  GO:0009651;
GO  GO:0048545;
GO  GO:0009414;
GO  GO:0009410;
GO  GO:0010043;
GO  GO:0007605;
GO  GO:0035176;
GO  GO:0006665;
GO  GO:0001963;
GO  GO:0042214;
GO  GO:0007601;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPTPSAPSPQPKGFRRAVSEQDAKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASSEPGNPLEAVVFEERDGN
SQ  AVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAR
SQ  EDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYKHGEPIPHVEYTAEEIATWKEVYVTL
SQ  KGLYATHACREHLEGFQLLERYCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASS
SQ  PMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGEL
SQ  LHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIQRSL
SQ  EGVQDELHTLAHALSAIS
//
ID  O17446;
PN  Tyrosine 3-monooxygenase;
GN  TH;
OS  6183;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}.
DR  UNIPROT: O17446;
DR  Pfam: PF00351;
DR  PROSITE: PS00367;
DR  PROSITE: PS51410;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0048471;
GO  GO:0005506;
GO  GO:0004511;
GO  GO:0009072;
GO  GO:0042416;
GO  GO:0042136;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MKMTMMCDESIEENNKSSTVELNHNEKDGRIHSIIINFHPITHEQSNNQFYIQTLHEILKYIIDKKLNLVHFETRPTLTL
SQ  SNANRDVQYSCLITLEANEINMSLLYEELRGNSFISGINLLNNQESEDWYPKHISDLDKCQHLLRKFQPELQTDHPGFHD
SQ  KVYRERREAIAKIAFQYKYGDRIPEVEYTKEEIETWGLVFTKMKAVHASRACREYIDGFQLLEKYCNYNSESIPQLQTIC
SQ  EFMHRTSGFRIRPVAGLVSPKDFLASLAFRVFQCTQYIRHHSRPMHTPEPDCIHELIGHMPMLVNRQFADFSQELGLASL
SQ  GASEEEITRLSTLYWFTVEFGLCNENGETRALGAGIMSSYGELENAFSDLSVKEPFNINDAAVQVYDDVGYQKIYFVTES
SQ  IESMKRELRNYINTSGKSTIPIYDPITETVHMKSRFSIRKELLKHVKEEIGQLDTLLNHSNYTLP
//
ID  Q9LR44;
PN  UDP-glycosyltransferase 75B1;
GN  UGT75B1;
OS  3702;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11283335}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:11283335}. Note=During interphase, distributed in a punctate pattern in the perinuclear region. Localized in the forming cell plate during cytokinesis.
DR  UNIPROT: Q9LR44;
DR  Pfam: PF00201;
DR  PROSITE: PS00375;
DE  Function: Possesses low catalytic activity on indole-3-acetic acid (IAA) in vitro. May transfer UDP-glucose from sucrose synthase to callose synthase for the synthesis of callose at the forming cell plate during cytokinesis. Has high affinity for 4-aminobenzoate. Catalyzes the formation of 4-aminobenzoate glucose ester which represents a storage form of 4-aminobenzoate in the vacuole. Is the major source of this activity in the plant. Also active in vitro on benzoates and benzoate derivatives. {ECO:0000269|PubMed:11042207, ECO:0000269|PubMed:11641410, ECO:0000269|PubMed:18385129}.
DE  Reference Proteome: Yes;
DE  Interaction: Q39821; IntAct: EBI-1765844; Score: 0.53
DE  Interaction: P92978; IntAct: EBI-1765945; Score: 0.44
DE  Interaction: Q9AUE0; IntAct: EBI-1766008; Score: 0.37
GO  GO:0005856;
GO  GO:0005794;
GO  GO:0048471;
GO  GO:0009524;
GO  GO:0047215;
GO  GO:0080043;
GO  GO:0080044;
GO  GO:0080002;
GO  GO:0035251;
GO  GO:0008194;
GO  GO:0046482;
GO  GO:0009751;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAPPHFLLVTFPAQGHVNPSLRFARRLIKRTGARVTFVTCVSVFHNSMIANHNKVENLSFLTFSDGFDDGGISTYEDRQK
SQ  RSVNLKVNGDKALSDFIEATKNGDSPVTCLIYTILLNWAPKVARRFQLPSALLWIQPALVFNIYYTHFMGNKSVFELPNL
SQ  SSLEIRDLPSFLTPSNTNKGAYDAFQEMMEFLIKETKPKILINTFDSLEPEALTAFPNIDMVAVGPLLPTEIFSGSTNKS
SQ  VKDQSSSYTLWLDSKTESSVIYVSFGTMVELSKKQIEELARALIEGKRPFLWVITDKSNRETKTEGEEETEIEKIAGFRH
SQ  ELEEVGMIVSWCSQIEVLSHRAVGCFVTHCGWSSTLESLVLGVPVVAFPMWSDQPTNAKLLEESWKTGVRVRENKDGLVE
SQ  RGEIRRCLEAVMEEKSVELRENAKKWKRLAMEAGREGGSSDKNMEAFVEDICGESLIQNLCEAEEVKVK
//
ID  Q95017;
PN  SUMO-conjugating enzyme UBC9;
GN  ubc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:25475837}.
DR  UNIPROT: Q95017;
DR  UNIPROT: Q9GYI5;
DR  Pfam: PF00179;
DR  PROSITE: PS00183;
DR  PROSITE: PS50127;
DE  Function: Accepts the ubiquitin-like protein smo-1 from the aos-1-uba-2 E1 complex and catalyzes its covalent attachment to other proteins with the help of an E3 ligase such as gei-17. Required to sumoylate the ETS transcription factor lin-1, Polycomb protein sop-2, and intermediate filament proteins, such as ifb-1 (PubMed:15107848, PubMed:15689373, PubMed:24933177). Required for embryonic development, fertility, vulval morphogenesis, inhibition of vulval cell fates, lifespan, and neuromuscular activity (PubMed:24933177). {ECO:0000269|PubMed:11806825, ECO:0000269|PubMed:14711411, ECO:0000269|PubMed:15107848, ECO:0000269|PubMed:15689373, ECO:0000269|PubMed:15990876, ECO:0000269|PubMed:16701625, ECO:0000269|PubMed:24933177}.
DE  Reference Proteome: Yes;
DE  Interaction: Q95Q25; IntAct: EBI-344381; Score: 0.67
DE  Interaction: Q23158; IntAct: EBI-342641; Score: 0.00
DE  Interaction: Q95017; IntAct: EBI-367977; Score: 0.55
DE  Interaction: P55853; IntAct: EBI-367980; Score: 0.71
DE  Interaction: G5EF84; IntAct: EBI-2414823; Score: 0.49
DE  Interaction: Q9NA84; IntAct: EBI-2416847; Score: 0.49
DE  Interaction: Q21747; IntAct: EBI-2416839; Score: 0.49
DE  Interaction: Q94361; IntAct: EBI-2416843; Score: 0.49
DE  Interaction: Q21209; IntAct: EBI-3895794; Score: 0.51
DE  Interaction: P34342; IntAct: EBI-6463257; Score: 0.37
DE  Interaction: Q94420; IntAct: EBI-6883188; Score: 0.00
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0005524;
GO  GO:0061629;
GO  GO:0032093;
GO  GO:0061656;
GO  GO:0009952;
GO  GO:0009792;
GO  GO:0000122;
GO  GO:0002119;
GO  GO:0043282;
GO  GO:0016925;
GO  GO:0032880;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGIAAGRLAEERKHWRKDHPFGFIAKPVKNADGTLNLFNWECAIPGRKDTIWEGGLYRIRMLFKDDFPSTPPKCKFEPP
SQ  LFHPNVYPSGTVCLSLLDENKDWKPSISIKQLLIGIQDLLNHPNIEDPAQAEAYQIYCQNRAEYEKRVKKEAVKYAAELV
SQ  QKQMLE
//
ID  P63279;
PN  SUMO-conjugating enzyme UBC9;
GN  UBE2I;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:16631117, ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:27068747}. Cytoplasm {ECO:0000269|PubMed:22214662}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12573574}. Note=Mainly nuclear (By similarity). In spermatocytes, localizes in synaptonemal complexes (PubMed:8610150). Recruited by BCL11A into the nuclear body (By similarity). {ECO:0000250|UniProtKB:P63280, ECO:0000269|PubMed:8610150}.
DR  UNIPROT: P63279;
DR  UNIPROT: D3DU69;
DR  UNIPROT: P50550;
DR  UNIPROT: Q15698;
DR  UNIPROT: Q59GX1;
DR  UNIPROT: Q86VB3;
DR  PDB: 1A3S;
DR  PDB: 1KPS;
DR  PDB: 1Z5S;
DR  PDB: 2GRN;
DR  PDB: 2GRO;
DR  PDB: 2GRP;
DR  PDB: 2GRQ;
DR  PDB: 2GRR;
DR  PDB: 2O25;
DR  PDB: 2PE6;
DR  PDB: 2PX9;
DR  PDB: 2XWU;
DR  PDB: 3A4S;
DR  PDB: 3UIN;
DR  PDB: 3UIO;
DR  PDB: 3UIP;
DR  PDB: 4W5V;
DR  PDB: 4Y1L;
DR  PDB: 5D2M;
DR  PDB: 5F6D;
DR  PDB: 5F6E;
DR  PDB: 5F6U;
DR  PDB: 5F6V;
DR  PDB: 5F6W;
DR  PDB: 5F6X;
DR  PDB: 5F6Y;
DR  PDB: 5FQ2;
DR  PDB: 6SYF;
DR  Pfam: PF00179;
DR  PROSITE: PS00183;
DR  PROSITE: PS50127;
DR  OMIM: 601661;
DR  DisGeNET: 7329;
DE  Function: Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. Mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity (PubMed:26620705). {ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:15809060, ECO:0000269|PubMed:17466333, ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:26524494, ECO:0000269|PubMed:26620705, ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:8668529}.
DE  Reference Proteome: Yes;
DE  Interaction: O14524; IntAct: EBI-21695903; Score: 0.35
DE  Interaction: P0CK47; IntAct: EBI-2622494; Score: 0.37
DE  Interaction: P29991; IntAct: EBI-8828210; Score: 0.37
DE  Interaction: P35658; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: P46060; IntAct: EBI-7036111; Score: 0.95
DE  Interaction: P46061; IntAct: EBI-1033068; Score: 0.44
DE  Interaction: P49790; IntAct: EBI-11076796; Score: 0.35
DE  Interaction: P49792; IntAct: EBI-11105225; Score: 0.75
DE  Interaction: P52948; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: P57740; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: P59595; IntAct: EBI-25497306; Score: 0.75
DE  Interaction: P62826; IntAct: EBI-11105225; Score: 0.53
DE  Interaction: P63165; IntAct: EBI-7406754; Score: 0.95
DE  Interaction: Q9UBC3; IntAct: EBI-80228; Score: 0.57
DE  Interaction: P04637; IntAct: EBI-7311368; Score: 0.74
DE  Interaction: Q9H2X6; IntAct: EBI-7631615; Score: 0.72
DE  Interaction: P12757; IntAct: EBI-7228470; Score: 0.37
DE  Interaction: O75400; IntAct: EBI-7243310; Score: 0.37
DE  Interaction: Q13485; IntAct: EBI-7248833; Score: 0.83
DE  Interaction: Q8TAD8; IntAct: EBI-7264331; Score: 0.37
DE  Interaction: Q13432; IntAct: EBI-731083; Score: 0.00
DE  Interaction: Q8NDC0; IntAct: EBI-752968; Score: 0.37
DE  Interaction: Q96B23; IntAct: EBI-753160; Score: 0.37
DE  Interaction: Q01826; IntAct: EBI-753613; Score: 0.55
DE  Interaction: Q9UI36; IntAct: EBI-753847; Score: 0.37
DE  Interaction: Q8IVD9; IntAct: EBI-753934; Score: 0.37
DE  Interaction: Q13422; IntAct: EBI-754453; Score: 0.37
DE  Interaction: O43353; IntAct: EBI-754693; Score: 0.37
DE  Interaction: Q9NR12; IntAct: EBI-755017; Score: 0.37
DE  Interaction: O15015; IntAct: EBI-755329; Score: 0.37
DE  Interaction: Q9UKT9; IntAct: EBI-755677; Score: 0.55
DE  Interaction: P78364; IntAct: EBI-757324; Score: 0.37
DE  Interaction: Q9H444; IntAct: EBI-757456; Score: 0.55
DE  Interaction: O14964; IntAct: EBI-757864; Score: 0.37
DE  Interaction: Q9Y620; IntAct: EBI-757909; Score: 0.37
DE  Interaction: O96006; IntAct: EBI-757915; Score: 0.37
DE  Interaction: Q14134; IntAct: EBI-758929; Score: 0.37
DE  Interaction: P07910; IntAct: EBI-759535; Score: 0.37
DE  Interaction: Q9Y4E5; IntAct: EBI-759886; Score: 0.75
DE  Interaction: P61978; IntAct: EBI-759901; Score: 0.37
DE  Interaction: O75928; IntAct: EBI-760369; Score: 0.85
DE  Interaction: P03116; IntAct: EBI-7316634; Score: 0.53
DE  Interaction: P03114; IntAct: EBI-8608879; Score: 0.37
DE  Interaction: P56693; IntAct: EBI-8087364; Score: 0.51
DE  Interaction: Q92754; IntAct: EBI-937323; Score: 0.65
DE  Interaction: P05549; IntAct: EBI-937334; Score: 0.65
DE  Interaction: Q92481; IntAct: EBI-937338; Score: 0.37
DE  Interaction: P54253; IntAct: EBI-25975778; Score: 0.67
DE  Interaction: Q14103; IntAct: EBI-1024489; Score: 0.44
DE  Interaction: Q9UBE0; IntAct: EBI-11105225; Score: 0.67
DE  Interaction: Q9UBT2; IntAct: EBI-11105225; Score: 0.81
DE  Interaction: O60739; IntAct: EBI-1067098; Score: 0.00
DE  Interaction: P56537; IntAct: EBI-1068752; Score: 0.00
DE  Interaction: P55854; IntAct: EBI-21854443; Score: 0.56
DE  Interaction: Q14164; IntAct: EBI-1076631; Score: 0.00
DE  Interaction: P19419; IntAct: EBI-7035929; Score: 0.73
DE  Interaction: O00482; IntAct: EBI-7035992; Score: 0.44
DE  Interaction: Q99497; IntAct: EBI-1164415; Score: 0.37
DE  Interaction: O14503; IntAct: EBI-1164831; Score: 0.58
DE  Interaction: P09936; IntAct: EBI-1181901; Score: 0.37
DE  Interaction: P61956; IntAct: EBI-7406892; Score: 0.59
DE  Interaction: Q9Y3V2; IntAct: EBI-1549893; Score: 0.61
DE  Interaction: P22314; IntAct: EBI-1550743; Score: 0.40
DE  Interaction: Q9UER7; IntAct: EBI-1559558; Score: 0.65
DE  Interaction: Q7Z6E9; IntAct: EBI-2117151; Score: 0.00
DE  Interaction: Q9H307; IntAct: EBI-2339638; Score: 0.37
DE  Interaction: Q06265; IntAct: EBI-2339635; Score: 0.55
DE  Interaction: Q15047; IntAct: EBI-2339647; Score: 0.55
DE  Interaction: Q9UKL3; IntAct: EBI-2339662; Score: 0.55
DE  Interaction: Q5T6S3; IntAct: EBI-2339683; Score: 0.37
DE  Interaction: Q9Y692; IntAct: EBI-2339671; Score: 0.37
DE  Interaction: Q9NPI1; IntAct: EBI-2339689; Score: 0.37
DE  Interaction: Q96RL1; IntAct: EBI-2339692; Score: 0.37
DE  Interaction: Q9NVP2; IntAct: EBI-2339695; Score: 0.37
DE  Interaction: Q8N5U6; IntAct: EBI-2340651; Score: 0.37
DE  Interaction: Q6ZNA4; IntAct: EBI-2340654; Score: 0.74
DE  Interaction: P36406; IntAct: EBI-2341573; Score: 0.37
DE  Interaction: P35226; IntAct: EBI-2341582; Score: 0.37
DE  Interaction: O60683; IntAct: EBI-2341585; Score: 0.37
DE  Interaction: Q13064; IntAct: EBI-2341594; Score: 0.37
DE  Interaction: P14373; IntAct: EBI-2341588; Score: 0.37
DE  Interaction: P78317; IntAct: EBI-2341591; Score: 0.55
DE  Interaction: Q86Y13; IntAct: EBI-2341597; Score: 0.37
DE  Interaction: O60291; IntAct: EBI-2341600; Score: 0.37
DE  Interaction: Q9ULV8; IntAct: EBI-2341603; Score: 0.37
DE  Interaction: Q9HBD1; IntAct: EBI-2341606; Score: 0.37
DE  Interaction: Q9NX47; IntAct: EBI-2341609; Score: 0.37
DE  Interaction: Q9NS91; IntAct: EBI-2341616; Score: 0.37
DE  Interaction: Q8TEB7; IntAct: EBI-2341627; Score: 0.37
DE  Interaction: Q8WV44; IntAct: EBI-2341630; Score: 0.37
DE  Interaction: Q8WVZ7; IntAct: EBI-2341639; Score: 0.37
DE  Interaction: Q96GF1; IntAct: EBI-2341633; Score: 0.37
DE  Interaction: Q8TDB6; IntAct: EBI-2341636; Score: 0.37
DE  Interaction: Q6ZMU5; IntAct: EBI-2341654; Score: 0.37
DE  Interaction: Q8N448; IntAct: EBI-2341642; Score: 0.37
DE  Interaction: Q7Z419; IntAct: EBI-2341645; Score: 0.37
DE  Interaction: Q969V5; IntAct: EBI-6987892; Score: 0.46
DE  Interaction: Q99856; IntAct: EBI-8566246; Score: 0.35
DE  Interaction: P03431; IntAct: EBI-2547959; Score: 0.37
DE  Interaction: P03496; IntAct: EBI-2547964; Score: 0.37
DE  Interaction: P03495; IntAct: EBI-2549251; Score: 0.37
DE  Interaction: Q9ERU9; IntAct: EBI-2555617; Score: 0.56
DE  Interaction: A0A2S9PGA1; IntAct: EBI-2840146; Score: 0.00
DE  Interaction: P16220; IntAct: EBI-3439128; Score: 0.00
DE  Interaction: P15104; IntAct: EBI-3439744; Score: 0.00
DE  Interaction: Q12772; IntAct: EBI-3451605; Score: 0.00
DE  Interaction: Q7Z333; IntAct: EBI-10093986; Score: 0.55
DE  Interaction: B3KQF8; IntAct: EBI-3452423; Score: 0.00
DE  Interaction: Q14789; IntAct: EBI-3452458; Score: 0.00
DE  Interaction: Q86Z02; IntAct: EBI-3452479; Score: 0.00
DE  Interaction: Q9H422; IntAct: EBI-3452493; Score: 0.00
DE  Interaction: O75925; IntAct: EBI-3452528; Score: 0.00
DE  Interaction: Q9Y6X2; IntAct: EBI-3935553; Score: 0.55
DE  Interaction: P23497; IntAct: EBI-3452577; Score: 0.00
DE  Interaction: P63279; IntAct: EBI-3934322; Score: 0.59
DE  Interaction: Q9H2Y7; IntAct: EBI-3452619; Score: 0.00
DE  Interaction: Q9UBW7; IntAct: EBI-3452633; Score: 0.00
DE  Interaction: B2RMV2; IntAct: EBI-3452654; Score: 0.00
DE  Interaction: O95817; IntAct: EBI-3454131; Score: 0.00
DE  Interaction: P03928; IntAct: EBI-3454124; Score: 0.00
DE  Interaction: Q00610; IntAct: EBI-3454138; Score: 0.00
DE  Interaction: Q92905; IntAct: EBI-3454145; Score: 0.00
DE  Interaction: Q14315; IntAct: EBI-3454152; Score: 0.00
DE  Interaction: P10644; IntAct: EBI-3454159; Score: 0.00
DE  Interaction: P31321; IntAct: EBI-3454166; Score: 0.00
DE  Interaction: Q96S59; IntAct: EBI-3454173; Score: 0.00
DE  Interaction: P19634; IntAct: EBI-3454180; Score: 0.00
DE  Interaction: Q15714; IntAct: EBI-3454194; Score: 0.00
DE  Interaction: Q8NDV7; IntAct: EBI-3454187; Score: 0.00
DE  Interaction: O75534; IntAct: EBI-3454201; Score: 0.00
DE  Interaction: Q9Y3S1; IntAct: EBI-3454208; Score: 0.00
DE  Interaction: Q15942; IntAct: EBI-3454215; Score: 0.00
DE  Interaction: O94829; IntAct: EBI-8534332; Score: 0.72
DE  Interaction: Q15645; IntAct: EBI-8649412; Score: 0.37
DE  Interaction: Q6RW13; IntAct: EBI-8650154; Score: 0.37
DE  Interaction: O15381; IntAct: EBI-8658018; Score: 0.37
DE  Interaction: Q13287; IntAct: EBI-8658035; Score: 0.37
DE  Interaction: Q03060; IntAct: EBI-3928044; Score: 0.37
DE  Interaction: P56545; IntAct: EBI-3928496; Score: 0.44
DE  Interaction: P29590; IntAct: EBI-3933045; Score: 0.44
DE  Interaction: O43255; IntAct: EBI-3933909; Score: 0.37
DE  Interaction: Q9NQB0; IntAct: EBI-3934076; Score: 0.44
DE  Interaction: O14544; IntAct: EBI-3934342; Score: 0.37
DE  Interaction: Q9UKY1; IntAct: EBI-3936749; Score: 0.37
DE  Interaction: Q8N2W9; IntAct: EBI-3940111; Score: 0.37
DE  Interaction: Q99684; IntAct: EBI-4292025; Score: 0.37
DE  Interaction: Q86UP2; IntAct: EBI-5660349; Score: 0.00
DE  Interaction: Q8WZ42; IntAct: EBI-5666456; Score: 0.00
DE  Interaction: P56524; IntAct: EBI-6112566; Score: 0.51
DE  Interaction: Q9UQL6; IntAct: EBI-6112579; Score: 0.37
DE  Interaction: Q9BZ95; IntAct: EBI-8487253; Score: 0.37
DE  Interaction: Q86X55; IntAct: EBI-8487291; Score: 0.37
DE  Interaction: P15884; IntAct: EBI-9212397; Score: 0.35
DE  Interaction: Q92793; IntAct: EBI-9212397; Score: 0.35
DE  Interaction: P45481; IntAct: EBI-9212425; Score: 0.44
DE  Interaction: P03230; IntAct: EBI-9349997; Score: 0.52
DE  Interaction: Q07869; IntAct: EBI-9511901; Score: 0.44
DE  Interaction: O41955; IntAct: EBI-9640696; Score: 0.37
DE  Interaction: O41969; IntAct: EBI-9641541; Score: 0.37
DE  Interaction: P0C206; IntAct: EBI-9675668; Score: 0.49
DE  Interaction: P60896; IntAct: EBI-9827158; Score: 0.35
DE  Interaction: G2XKQ0; IntAct: EBI-10220912; Score: 0.56
DE  Interaction: Q08379; IntAct: EBI-10220932; Score: 0.66
DE  Interaction: Q8N3Z6; IntAct: EBI-10220952; Score: 0.56
DE  Interaction: Q8WWZ3; IntAct: EBI-10220962; Score: 0.56
DE  Interaction: Q9HCK0; IntAct: EBI-10220972; Score: 0.56
DE  Interaction: P41212; IntAct: EBI-10491265; Score: 0.37
DE  Interaction: Q5U0E4; IntAct: EBI-10491279; Score: 0.37
DE  Interaction: Q04360; IntAct: EBI-11736551; Score: 0.37
DE  Interaction: Q6PFD9; IntAct: EBI-10994876; Score: 0.35
DE  Interaction: Q8BH74; IntAct: EBI-10997196; Score: 0.35
DE  Interaction: Q8VE37; IntAct: EBI-11043815; Score: 0.35
DE  Interaction: P18754; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q9ULR0; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q8IZ21; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q9BW27; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q14974; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q9UBU9; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q96SK2; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q8NFH5; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q8TEM1; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q9BTX1; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q06787; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q8N1F7; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: E9PF10; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q92621; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: O60333; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q9NRG9; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q96EE3; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: F5GZ90; IntAct: EBI-11105225; Score: 0.35
DE  Interaction: Q8CH72; IntAct: EBI-11114497; Score: 0.35
DE  Interaction: P04046; IntAct: EBI-11522871; Score: 0.56
DE  Interaction: P15873; IntAct: EBI-11523508; Score: 0.56
DE  Interaction: P17423; IntAct: EBI-11523598; Score: 0.56
DE  Interaction: P25354; IntAct: EBI-11524281; Score: 0.56
DE  Interaction: P25515; IntAct: EBI-11524613; Score: 0.56
DE  Interaction: P25453; IntAct: EBI-11524604; Score: 0.56
DE  Interaction: P25611; IntAct: EBI-11524667; Score: 0.56
DE  Interaction: P27515; IntAct: EBI-11524895; Score: 0.56
DE  Interaction: P32458; IntAct: EBI-11525398; Score: 0.56
DE  Interaction: P32502; IntAct: EBI-11525940; Score: 0.56
DE  Interaction: P32562; IntAct: EBI-11526605; Score: 0.56
DE  Interaction: P33417; IntAct: EBI-11527138; Score: 0.56
DE  Interaction: P35192; IntAct: EBI-11527429; Score: 0.56
DE  Interaction: P37263; IntAct: EBI-11527656; Score: 0.56
DE  Interaction: P38319; IntAct: EBI-11528157; Score: 0.56
DE  Interaction: P38340; IntAct: EBI-11528622; Score: 0.56
DE  Interaction: P38703; IntAct: EBI-11529305; Score: 0.56
DE  Interaction: P38838; IntAct: EBI-11529593; Score: 0.56
DE  Interaction: P38986; IntAct: EBI-11529746; Score: 0.56
DE  Interaction: P38991; IntAct: EBI-11529764; Score: 0.56
DE  Interaction: P40151; IntAct: EBI-11530459; Score: 0.56
DE  Interaction: P40473; IntAct: EBI-11531218; Score: 0.56
DE  Interaction: P40956; IntAct: EBI-11531611; Score: 0.56
DE  Interaction: P46985; IntAct: EBI-11532107; Score: 0.56
DE  Interaction: P49723; IntAct: EBI-11532821; Score: 0.56
DE  Interaction: P53176; IntAct: EBI-11533108; Score: 0.56
DE  Interaction: P53174; IntAct: EBI-11533099; Score: 0.56
DE  Interaction: P53243; IntAct: EBI-11533171; Score: 0.56
DE  Interaction: P53252; IntAct: EBI-11533206; Score: 0.56
DE  Interaction: P53286; IntAct: EBI-11533278; Score: 0.56
DE  Interaction: P60010; IntAct: EBI-11534056; Score: 0.56
DE  Interaction: Q03063; IntAct: EBI-11534775; Score: 0.56
DE  Interaction: Q03373; IntAct: EBI-11534875; Score: 0.56
DE  Interaction: Q03718; IntAct: EBI-11534950; Score: 0.56
DE  Interaction: Q04110; IntAct: EBI-11535060; Score: 0.56
DE  Interaction: Q06178; IntAct: EBI-11535560; Score: 0.56
DE  Interaction: Q06340; IntAct: EBI-11535605; Score: 0.56
DE  Interaction: Q08581; IntAct: EBI-11536317; Score: 0.56
DE  Interaction: Q12020; IntAct: EBI-11536399; Score: 0.56
DE  Interaction: Q12206; IntAct: EBI-11536864; Score: 0.56
DE  Interaction: Q12306; IntAct: EBI-11537161; Score: 0.56
DE  Interaction: Q12439; IntAct: EBI-11537405; Score: 0.56
DE  Interaction: Q9HD42; IntAct: EBI-11511224; Score: 0.37
DE  Interaction: Q9NZZ3; IntAct: EBI-11512517; Score: 0.37
DE  Interaction: Q12800; IntAct: EBI-11770132; Score: 0.49
DE  Interaction: Q96IK5; IntAct: EBI-11771440; Score: 0.49
DE  Interaction: Q9QXY6; IntAct: EBI-11685546; Score: 0.44
DE  Interaction: P61769; IntAct: EBI-21675069; Score: 0.35
DE  Interaction: P22460; IntAct: EBI-15620337; Score: 0.40
DE  Interaction: Q9Y265; IntAct: EBI-15676218; Score: 0.50
DE  Interaction: Q02078; IntAct: EBI-15799705; Score: 0.44
DE  Interaction: O00180; IntAct: EBI-15856059; Score: 0.27
DE  Interaction: P03243; IntAct: EBI-16149899; Score: 0.40
DE  Interaction: P04040; IntAct: EBI-16789632; Score: 0.27
DE  Interaction: P11474; IntAct: EBI-20303027; Score: 0.44
DE  Interaction: P62508; IntAct: EBI-20303735; Score: 0.44
DE  Interaction: Q12888; IntAct: EBI-20207896; Score: 0.27
DE  Interaction: P02649; IntAct: EBI-21388153; Score: 0.00
DE  Interaction: O00499; IntAct: EBI-21388141; Score: 0.00
DE  Interaction: P09429; IntAct: EBI-21461795; Score: 0.37
DE  Interaction: Q9BYV2; IntAct: EBI-22024844; Score: 0.00
DE  Interaction: P42858; IntAct: EBI-25959819; Score: 0.56
DE  Interaction: Q92630; IntAct: EBI-28952196; Score: 0.27
DE  Interaction: P10070; IntAct: EBI-29016408; Score: 0.27
DE  Interaction: P35712; IntAct: EBI-29730925; Score: 0.27
DE  Interaction: P48436; IntAct: EBI-29732788; Score: 0.27
DE  Interaction: P40763; IntAct: EBI-29762103; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0016605;
GO  GO:0106068;
GO  GO:1990356;
GO  GO:0000795;
GO  GO:1990234;
GO  GO:0005524;
GO  GO:0019899;
GO  GO:0043398;
GO  GO:0071535;
GO  GO:0003723;
GO  GO:0044388;
GO  GO:0061656;
GO  GO:0019789;
GO  GO:0001221;
GO  GO:0008134;
GO  GO:0051301;
GO  GO:0007059;
GO  GO:0007084;
GO  GO:0045892;
GO  GO:0000122;
GO  GO:0051168;
GO  GO:0043123;
GO  GO:1903755;
GO  GO:0036211;
GO  GO:0016925;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPP
SQ  LFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS
//
ID  Q09349;
PN  Ubiquitin conjugation factor E4 ufd-2;
GN  ufd;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:27669035}. Nucleus membrane {ECO:0000269|PubMed:27669035}; Peripheral membrane protein {ECO:0000269|PubMed:27669035}; Cytoplasmic side {ECO:0000269|PubMed:27669035}. Nucleus, nucleolus {ECO:0000269|PubMed:27669035}. Note=Localizes to germline syncytium. In the late pachytene, accumulates at the nuclear periphery forming a ring. Following ionizing radiation-mediated DNA damage, localizes to foci within nucleoli where it colocalizes with cdc-48.1 and/or cdc- 48.2, atx-3, proteasome alpha subunit and ubiquitinated proteins. Localization to foci is ubiquitin-dependent and regulated by E3 ligase hecd-1 and deubiquitinating enzyme atx-3. ufd-2 foci are formed following the initiation of homologous recombination (HR) and persist until HR is completed. ufd-2 foci are also formed upon cep-1 activation. {ECO:0000269|PubMed:27669035}.
DR  UNIPROT: Q09349;
DR  UNIPROT: Q6BEV4;
DR  UNIPROT: Q95QB5;
DR  Pfam: PF04564;
DR  Pfam: PF10408;
DR  PROSITE: PS51698;
DE  Function: Acts as an E4 ubiquitin ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (PubMed:27669035). The elongation of preexisting ubiquitin chains preferentially targets ubiquitin 'Lys-29' and 'Lys-48' residues (PubMed:27669035). Also functions as an E3 ligase in conjunction with specific E1 and E2 ligases (PubMed:15294159, PubMed:27669035, PubMed:29396393). Probably by regulating protein ubiquitination at DNA damage repair sites, coordinates DNA double- strand-break repair and apoptosis in the germline (PubMed:27669035). Required for germline apoptosis in response to DNA damage downstream of cep-1 (PubMed:27669035). Involved in the resolution of DNA-repair sites by promoting the release of rad-51 from DNA damage foci (PubMed:27669035). In association with protein-ligase chn-1, acts as an E3/E4 ligase to poly-ubiquitinate lysine residues in the UCS domain of myosin chaperone unc-45 (PubMed:15294159, PubMed:29396393). By targeting myosin chaperone unc-45 for proteasomal degradation, regulates myosin assembly in body wall muscles in association with cdc- 48.1 and chn-1 (PubMed:15294159, PubMed:17369820). However, in a contrasting study, acts as an E3 ligase, independently of chn-1, to poly-ubiquitinate unc-45 without promoting unc-45 proteasomal degradation (PubMed:29396393). Instead, uses unc-45 as an adapter protein to recruit and poly-ubiquitinate unfolded myosin heavy chain B unc-54 (PubMed:29396393). {ECO:0000269|PubMed:15294159, ECO:0000269|PubMed:17369820, ECO:0000269|PubMed:27669035, ECO:0000269|PubMed:29396393}.
DE  Reference Proteome: Yes;
DE  Interaction: G5EEM6; IntAct: EBI-334688; Score: 0.00
DE  Interaction: P90879; IntAct: EBI-2417967; Score: 0.49
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0000151;
GO  GO:0051087;
GO  GO:0031625;
GO  GO:0034450;
GO  GO:0008340;
GO  GO:0032436;
GO  GO:0051865;
GO  GO:0035519;
GO  GO:0070936;
GO  GO:0000209;
GO  GO:0016567;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:27669035};
SQ  MIEDEKAGLQPMDISDASVFFFQADVESKDFLTSLFDCEGKSDDRMLRYADAIIDVQNLNFDVSPQCLQSNIAEIITKFV
SQ  LLSQDGSRRGLSRSFNFIDPDIIAGCREEDAIEFLLINFVRCHHELGKSGTSNCYKKTLESTRKAVFSVFVMIQRGYLES
SQ  QLRSQHASLVFTKRLLEDTVSNVFLRTLVEYLASTDECDEDAITETFNPIFGILRSGIICQRFEDNKDEIVRQILRVMNL
SQ  LLSIRLPSNGPRPLSNLLVNREDFLPTPSEKIQGREFGLMSFLGPFFSYGLESSARRPNHRVFVDCEEDARKYDGSVNTE
SQ  QKLYFQRMDPIRTMLHQLMLPLASDQGSRNKTLRWIATIISTNDIRTRSHYDPSDVLCDHYMTNFLSVMYMFSEKIDLSK
SQ  IIVDYPFLPSSLINISKETRLKMDESGAVAFASQFADRPDEYHFSTVCFFLTIAAQRLVIPPLMNQISEYSRHLKELKHK
SQ  INALKEKLNTVSGFERAEVEKKLNYETEHWKLMSRHLLCVKTQAQDPALMASSMDFVDKQMKFILNLLCDNLDLLGDDSQ
SQ  LPTEVSQMFCALPEYFLEDALDFYIFAISNGMKLLMERNADWISRLTVLFTQYHYIKSPFLVSKLVRVLSSIQPPLWFNV
SQ  VRLRMAQENLLMCMIKFYSDFEDNGDFYEKFNVRGNIQYMLEKMEEDMFYKGKFMDMARECGAEFIRFVNMVINDATWCI
SQ  DESLSGLKSIHDVEKKMANKVEWDNTDQEIRNQDLGVYEEAKRKVKGWLGTAKSNLKLLLSITVNSPEPFRTPVLGERLA
SQ  AMLNHNLSQLIGSKASELKVKDPRSYGWEPREFVSLLISIYLKLNMPAFVKYIAYDERTYSPEFFHNAIECMRKNSIVGF
SQ  SQLESFEHLAEDVKKEYEAKAELEEEYDDVPEEFKDPIMDAIMVDPVKLPSGHVMDRAVIERHLLSTPNNPFNRAPLSHN
SQ  ELSPDSELKAKIQEWICQKRNSKK
//
ID  A7Z056;
PN  Ubiquitin carboxyl-terminal hydrolase 20;
GN  USP20;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
DR  UNIPROT: A7Z056;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0001664;
GO  GO:0008270;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDSRDLCPHLDSIGEVTKEDLLLKSKSTCQSCGVSGPNLWACLQVSCSYVGCGESFADHSTLHAQAKKHNLTVNLTTFR
SQ  VWCYACEKEVFLEPRLAAHPPGPAPKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAAL
SQ  QALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHRKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLM
SQ  DQLHEELKEPVVATAAALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRSGGGSQAEAELLMADEAGR
SQ  AISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMAALEQQPPETQPPSPRSTSPCRTPEPDNEAHMRSSRPCSPVHHHE
SQ  GHAKLASSPHRASPVRMGPAYVLKKAQVPGSRRRKEQSYRSVISDIFDGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGK
SQ  EDLAKLHSAIYQNVPAKPGACGDSYVAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCER
SQ  CKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKISSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSG
SQ  HYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEAYVLFYRKSSEEAVRERQQVVSLAAMREPSLLRFYVSREWLNKFNT
SQ  FAEPGPITNHTFLCSHGGIPPNKYHYIDDLVVILPQNVWEHLYSRFGGGPAVNHLYVCSICQVEIEALAKRRRVEIDTFI
SQ  KLNKAFQAEESPSVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHIQLKPGADYGQISEETWVYLNNLYGG
SQ  GPEIAIRQSVAQLPDPESLHGEQKIEAETRAL
//
ID  A5PN09;
PN  Ubiquitin carboxyl-terminal hydrolase 20;
GN  usp20;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
DR  UNIPROT: A5PN09;
DR  UNIPROT: A5PM59;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (adrb2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (adrb2). Plays a central role in adrb2 recycling and resensitization after prolonged agonist stimulation by constitutively binding adrb2, mediating deubiquitination of adrb2 and inhibiting lysosomal trafficking of adrb2. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008270;
GO  GO:0021551;
GO  GO:1904888;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTDSGDLCPHLDSIGEVTKEELIQKSKGTCQSCGVGGPNLWACLQCDCPYVGCGESYSDHSTIHAQAKKHNLTVNLTTFR
SQ  VWCYVCEREVFLEPKPVTPVSSAHRCKPHDQDPVSQTTCYPLKAVPIAVADEEGSESEEDELKPRGLTGMKNIGNSCYMN
SQ  AALQALSNCPPLTQFFQDCSGLVRTDKKPALCKSYQKLISELWHKKRPSYVVPTTLFHGIKLVNPMFRGYAQQDTQEFLR
SQ  CLMDQLHEELKEPLFDCSGGISEVEPDLSLDSCNLVDGDRSPSEDEFLSCDSGSGSERGDGERAGGEAELLIQDECVAVR
SQ  GTGGISEKERLKERRGEERTREMDEDADVDTAAQDGQAERETETATPATAVPAPGNTEPDNEASMHCPSSRPCSPAHSVQ
SQ  ELHSRLSSNPPRSSPLRTGPTYTFKKAQMLLSTKKKKQSRFRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIP
SQ  GKEDLAKLHSSIHQSAPVKAGVCTDGYAAQGWISYIMDSIRRFVVSCIPSWFWGPMVTLEDCLAAFFAADELKGDNMYSC
SQ  ERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLKPFLAKESPSQITTYDLLSVICHHGTAG
SQ  SGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEAYVLFYRKSSEESVRERQRVVALANLKEPSLLQFYISREWLNKF
SQ  NTFTEPGPITNHTFLCQHGGIPPTKYHYVDDLVVILPQNVWEYLYNRFGGGPAVNHLYVCAICQVEIETLAKRRKLEIDT
SQ  FIKLNKEFQAEEAPTVILCISMQWFREWENFVKGKDNEPPGPIDNSKIAVMKGGHIQLKQGADYGQISEETWQYLLSIYG
SQ  GGPEIAVRQTISPPDTDTHGERKIEAETRAL
//
ID  Q9Y2K6;
PN  Ubiquitin carboxyl-terminal hydrolase 20;
GN  USP20;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23486064}. Note=According to PubMed:12865408, it localizes in the endoplasmic reticulum; however the relevance of such result is unclear.
DR  UNIPROT: Q9Y2K6;
DR  UNIPROT: Q541F1;
DR  UNIPROT: Q8IXQ1;
DR  UNIPROT: Q96LG5;
DR  UNIPROT: Q9UQN8;
DR  UNIPROT: Q9UQP0;
DR  PDB: 6KCZ;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DR  OMIM: 615143;
DR  DisGeNET: 10868;
DE  Function: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:12056827, ECO:0000269|PubMed:12865408, ECO:0000269|PubMed:15776016, ECO:0000269|PubMed:19424180}.
DE  Reference Proteome: Yes;
DE  Interaction: P49790; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q96AG4; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q9P0L0; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q9UH99; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: P35249; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: P35250; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: O00232; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: O15049; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: P40938; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: O75521; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q6IQ21; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q96JN8; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: P62158; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q99666; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: P60228; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: P22830; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q5T9A4; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q68DG8; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q15008; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q15149; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q96C24; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: P53350; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: O75943; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: O00231; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: O00159; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: P51665; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: O75787; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: P15374; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q6IQ23; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: O95292; IntAct: EBI-2512022; Score: 0.68
DE  Interaction: Q99767; IntAct: EBI-2512022; Score: 0.56
DE  Interaction: P11310; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q9UBC5; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q3KQU3; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q8TD30; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q9BY77; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: O95714; IntAct: EBI-2512022; Score: 0.56
DE  Interaction: Q99613; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q9UK80; IntAct: EBI-2512177; Score: 0.40
DE  Interaction: O95931; IntAct: EBI-3951830; Score: 0.64
DE  Interaction: O43597; IntAct: EBI-10326535; Score: 0.56
DE  Interaction: P13196; IntAct: EBI-10326545; Score: 0.56
DE  Interaction: P36406; IntAct: EBI-10326555; Score: 0.56
DE  Interaction: P43364; IntAct: EBI-10326565; Score: 0.56
DE  Interaction: Q53XM7; IntAct: EBI-10326577; Score: 0.56
DE  Interaction: Q7L4P6; IntAct: EBI-10326587; Score: 0.56
DE  Interaction: Q8IYA8; IntAct: EBI-10326597; Score: 0.56
DE  Interaction: Q8N7W2; IntAct: EBI-10326607; Score: 0.56
DE  Interaction: Q969F0; IntAct: EBI-10326619; Score: 0.56
DE  Interaction: Q99750; IntAct: EBI-10326629; Score: 0.56
DE  Interaction: P58304; IntAct: EBI-21789618; Score: 0.35
DE  Interaction: Q96T17; IntAct: EBI-21796065; Score: 0.35
DE  Interaction: Q9UJU6; IntAct: EBI-21796190; Score: 0.35
DE  Interaction: Q96RY5; IntAct: EBI-21885721; Score: 0.35
DE  Interaction: Q9NZ08; IntAct: EBI-20900752; Score: 0.40
DE  Interaction: Q9H492; IntAct: EBI-30830405; Score: 0.44
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0001664;
GO  GO:0008270;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDSRDLCPHLDSIGEVTKEDLLLKSKGTCQSCGVTGPNLWACLQVACPYVGCGESFADHSTIHAQAKKHNLTVNLTTFR
SQ  LWCYACEKEVFLEQRLAAPLLGSSSKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAAL
SQ  QALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLM
SQ  DQLHEELKEPVVATVALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSQAETELLIPDEAGRA
SQ  ISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMAALDDQPAEAQPPSPRSSSPCRTPEPDNDAHLRSSSRPCSPVHHHE
SQ  GHAKLSSSPPRASPVRMAPSYVLKKAQVLSAGSRRRKEQRYRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIP
SQ  GKEDLAKLHSAIYQNVPAKPGACGDSYAAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSC
SQ  ERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAG
SQ  SGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFYRKSSEEAMRERQQVVSLAAMREPSLLRFYVSREWLNKF
SQ  NTFAEPGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAVNHLYVCSICQVEIEALAKRRRIEIDT
SQ  FIKLNKAFQAEESPGVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHVQLKQGADYGQISEETWTYLNSLY
SQ  GGGPEIAIRQSVAQPLGPENLHGEQKIEAETRAV
//
ID  Q8C6M1;
PN  Ubiquitin carboxyl-terminal hydrolase 20;
GN  Usp20;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
DR  UNIPROT: Q8C6M1;
DR  UNIPROT: Q69ZT5;
DR  UNIPROT: Q8CJ72;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UHL9; IntAct: EBI-12517044; Score: 0.37
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0001664;
GO  GO:0008270;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDARDLCPHLDCIGEVTKEDLLLKSKGTCQSCGVAGPNLWACLQVTCPYVGCGESFADHSSIHAQVKKHNLTVNLTTFR
SQ  VWCYACEREVFLEQRLAVHLASSSARLSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAAL
SQ  QALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLISEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLM
SQ  DQLHEELKEPMVAAVAALTDARDSDSSDTDERRDGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSKAEMELLISDEAGR
SQ  AISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMASLDEQSREAQPPSPRSTSPCQTPEPDNEAHIRSSSRPCSPVHHH
SQ  HEGHSKLSSSPPRASPVRMGPSYVLKKAQVPSTGGRRRKEQSYRSVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLP
SQ  IPGKEDLAKLHSAIYQNVPAKPGACGDSYSSQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMY
SQ  SCERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSFKVSSHVSFPLEGLDLRPFLAKECTSQVTTYDLLSVICHHGT
SQ  AGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNVEAYVLFYRKSSEEAMRERQQVVSLAAMREPSLLRFYVSREWLN
SQ  KFNTFAEPGPITNHTFLCSHGGIPPNKYHYIDDLVVILPQSVWEHLYSRFGGGPAVNHLYVCSICQVEIEALAKRRRVEI
SQ  DTFIKLNKAFQAEESPAVIYCISMHWFREWEAFVKGKDSEPPGPIDNSRIAQVKGSGHIQLKQGADCGQISEETWTYLSS
SQ  LYGGGPEIAIRQSVAQLPDPESLHGEQKIEAETRAL
//
ID  Q5R5Z6;
PN  Ubiquitin carboxyl-terminal hydrolase 20;
GN  USP20;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
DR  UNIPROT: Q5R5Z6;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008270;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDSRDLCPHLDSIGEVTKEDLLLKSMGTCQSCGVTGPNLWACLQVACPYVGCGESFADHSTIHAQAKKHNLTVNLTTFR
SQ  LWCYACEKEVFLEQRLAAPLLGSSKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQ
SQ  ALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMD
SQ  QLHEELKEPVVATVALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSQAETELLIPDEASRAI
SQ  SEKERMKDRKFSWGQQRTNSEQVDEDADVDTTMAALDDQPAEAQPPSPRSSSPCRTPEPDNDAHLCSSSRPCSPVHHHEG
SQ  HAKLSSSPPRASPVRMAPSYVLKKAQVLSAGSRRRKEQRYRSVISDIFDGSILSLVQCLTCDRVSATVETFQDLSLPIPG
SQ  KEDLAKLHSAIYQNVPAKPGTCGDSYAAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCE
SQ  RCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGS
SQ  GHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFYRKSSEEAVRERQQVVSLAAMREPSLLRFYVSREWLNKFN
SQ  TFAEPGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAVNHLYVCSICQVEIEALAKRRRIEIDTF
SQ  IKLNKAFQAEESPGIIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHVQLKQGADYGQISEETWTYLNSLYG
SQ  GGPEIAIRQSVAQPLGPESLHGEQKIEAEARAV
//
ID  B1WBD7;
PN  Ubiquitin carboxyl-terminal hydrolase 20;
GN  usp20;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
DR  UNIPROT: B1WBD7;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (adrb2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (adrb2). Plays a central role in adrb2 recycling and resensitization after prolonged agonist stimulation by constitutively binding adrb2, mediating deubiquitination of adrb2 and inhibiting lysosomal trafficking of adrb2. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008270;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADAEDFCPHLDSIGEVTKEDLILKSKGTCESCGVGGPNLWACLQDGCQSVGCGESYADHSTLHAQDFPSPAHPLKSVPI
SQ  AVGDDGESESDEDDIKPRGLTGMKNIGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSELWHKKR
SQ  PSYVVPSSLYHGIKLINPLFRGYSQQDTQEFLRCLMDQLHEELKEPILPENQEQEEEERDDQREGERGGTTEEDFLSCDS
SQ  GGEMGDGEGGGGVGTLSEMELLIREEVGRGLSEKEKLKERKLSYCHRRTSSEQADEDADVDTAMIPEPDNDAYMHCSSRS
SQ  CSPHPVESISKHSSTPPRSSPLRTAHSYVLKKAQVLSGGKKRSEVRYRSVISDIFDGSILSLVQCLTCDRVSTTIETFQD
SQ  LSLPIPGKEDLAKLHSTIHQSTVIKAGTCGDSYAAQGWLAFVMDYIRRFVVSCIPSWFWGPMITLEDCLAAFFAADELKG
SQ  DNMYSCERCKKLRNGVKYCKVLRLPEVLCIHLKRFRHEVMYSFKIGSHVSFPLEGLNLRPFLAKECVSRITTYDLLAVIC
SQ  HHGSASSGHYISYCQNVINGQWYEFDDQYVTEVHETVVQNAEAYVLFYRKSSEEAERERQKVVSLAAMKESGLLQFYISR
SQ  EWLNKFNTFAEPGPISNQSFLCAHGGIPPNKYHYIDDLVVILPQSVWEYLYNRFGGGPAVNHLYVCSICQVEIEALAKRR
SQ  KTEIDTFIKLNKAFQAEEAPSVIYCISMQWFREWEAFVKAKDSDPPGPIDNSKVALTKSSGHVQLKQGADYGQISEETWN
SQ  YLLNIYGGGPEIAIRQTVAQYQDPEHLHGEQKIEAETRAG
//
ID  A0JM59;
PN  Ubiquitin carboxyl-terminal hydrolase 20;
GN  usp20;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
DR  UNIPROT: A0JM59;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (adrb2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (adrb2). Plays a central role in adrb2 recycling and resensitization after prolonged agonist stimulation by constitutively binding adrb2, mediating deubiquitination of adrb2 and inhibiting lysosomal trafficking of adrb2. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008270;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGDAEDFCPHLDSIGEVTKEDLILKSKGTCESCGVGGPNLWACLQDGCQSVGCGESYVDHSTLHAQAKKHNLTVNLTTFR
SQ  VWCYACEKEVFLDPRGPPASQTTSPRLSHRDFPTSAHPLKSVPIAVGDDGESESDEDDIKPRGLTGMKNIGNSCYMNAAL
SQ  QALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLISELWHKKRPSYVVPSSLYHGIKLINPLFRGYSQQDTQEFLRCLM
SQ  DQLHEELKEPVPLETQEREEEDRDDQREGERGGTVEEDFLSCDSGGEMGDGEGGGGVGTLSEMELLIREEVGRGLSEKEK
SQ  LKERKLSYCHRRTSSEQADEDADVDTAMIPEPDNDAYVHCSSRSCSPHPVESISKHSSTPPRSSPLRTSHSYVLKKAQVL
SQ  SGGKKRSEVRYRSVISDIFDGSILSLVQCLTCDRVSTTIETFQDLSLPIPGKEDLAKLHSTIHQSAVSKAGTCGDSYAAQ
SQ  GWLSFFMDYIRRFVVSCIPSWFWGPMITLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFR
SQ  HEVMYSFKIGSHVSFPLEGLNLRPFLAKECVSRITTYDLLAVICHHGSASSGHYISYCQNVINGQWYEFDDQYVTEVHET
SQ  VVQNAEAYVLFYRKSSEEAERERQKVVSLAAMKESGLLQFYISREWLNKFNTFAEPGPISNQSFLCSHGGIPPNKYHYID
SQ  DLVVILPQSVWEYLYNRFGGGPAVNHLYVCSICQVEIEALAKRRKTEIDTFIKLNKAFQAEEAPSVIYCISMQWFREWEA
SQ  FVKAKDSDPPGPIDNSKVALTKSSGQVQLKQGADYGQISEETWNYLLNVYGGGPEIAIRQTVAQYQEAEHLHGEQKIEAE
SQ  TRAG
//
ID  Q9HBJ7;
PN  Ubiquitin carboxyl-terminal hydrolase 29;
GN  USP29;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9ES63}. Note=Localizes to perinuclear region in response to herpes simplex virus-1 (HSV-1) infection. {ECO:0000250|UniProtKB:Q9ES63}.
DR  UNIPROT: Q9HBJ7;
DR  Pfam: PF00443;
DR  Pfam: PF16674;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  OMIM: 609546;
DE  Function: Deubiquitinase involved in innate antiviral immunity by mediating 'Lys-48'-linked deubiquitination of CGAS, thereby promoting its stabilization. {ECO:0000269|PubMed:32457395}.
DE  Reference Proteome: Yes;
DE  Interaction: P07858; IntAct: EBI-2513524; Score: 0.40
DE  Interaction: P04637; IntAct: EBI-8579019; Score: 0.40
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0051607;
GO  GO:0000082;
GO  GO:0045087;
GO  GO:0060340;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0050821;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MISLKVCGFIQIWSQKTGMTKLKEALIETVQRQKEIKLVVTFKSGKFIRIFQLSNNIRSVVLRHCKKRQSHLRLTLKNNV
SQ  FLFIDKLSYRDAKQLNMFLDIIHQNKSQQPMKSDDDWSVFESRNMLKEIDKTSFYSICNKPSYQKMPLFMSKSPTHVKKG
SQ  ILENQGGKGQNTLSSDVQTNEDILKEDNPVPNKKYKTDSLKYIQSNRKNPSSLEDLEKDRDLKLGPSFNTNCNGNPNLDE
SQ  TVLATQTLNAKNGLTSPLEPEHSQGDPRCNKAQVPLDSHSQQLQQGFPNLGNTCYMNAVLQSLFAIPSFADDLLTQGVPW
SQ  EYIPFEALIMTLTQLLALKDFCSTKIKRELLGNVKKVISAVAEIFSGNMQNDAHEFLGQCLDQLKEDMEKLNATLNTGKE
SQ  CGDENSSPQMHVGSAATKVFVCPVVANFEFELQLSLICKACGHAVLKVEPNNYLSINLHQETKPLPLSIQNSLDLFFKEE
SQ  ELEYNCQMCKQKSCVARHTFSRLSRVLIIHLKRYSFNNAWLLVKNNEQVYIPKSLSLSSYCNESTKPPLPLSSSAPVGKC
SQ  EVLEVSQEMISEINSPLTPSMKLTSESSDSLVLPVEPDKNADLQRFQRDCGDASQEQHQRDLENGSALESELVHFRDRAI
SQ  GEKELPVADSLMDQGDISLPVMYEDGGKLISSPDTRLVEVHLQEVPQHPELQKYEKTNTFVEFNFDSVTESTNGFYDCKE
SQ  NRIPEGSQGMAEQLQQCIEESIIDEFLQQAPPPGVRKLDAQEHTEETLNQSTELRLQKADLNHLGALGSDNPGNKNILDA
SQ  ENTRGEAKELTRNVKMGDPLQAYRLISVVSHIGSSPNSGHYISDVYDFQKQAWFTYNDLCVSEISETKMQEARLHSGYIF
SQ  FYMHNGIFEELLRKAENSRLPSTQAGVIPQGEYEGDSLYRPA
//
ID  Q9ES63;
PN  Ubiquitin carboxyl-terminal hydrolase 29;
GN  Usp29;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:32457395}. Note=Localizes to perinuclear region in response to herpes simplex virus-1 (HSV-1) infection. {ECO:0000269|PubMed:32457395}.
DR  UNIPROT: Q9ES63;
DR  UNIPROT: C6EQG1;
DR  Pfam: PF00443;
DR  Pfam: PF16674;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DE  Function: Deubiquitinase involved in innate antiviral immunity by mediating 'Lys-48'-linked deubiquitination of CGAS, thereby promoting its stabilization. {ECO:0000269|PubMed:32457395}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0051607;
GO  GO:0000082;
GO  GO:0045087;
GO  GO:0060340;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0050821;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAHLKINGLVQIRSTNRSKHTRASQWKEAVIEIVERKQKVNLVVSFKLEERRRVFQLGDNVTGVVVSGELGLYHLDLTLR
SQ  DDTSLLIDKLSSADVEHLKSFLDSSTPCESQQPMEPMSSQDDLESSDPFCGEHQEAACGSLNTTPESGTPLSRKMPLSMS
SQ  NTTGGQKRGEKQGRKRKTEPSSSSAEVNKDIPKENTPDQKKKSRRYYSRNRGGKAEKAVTLREQEKRSNWKLEPAFNSKS
SQ  YGRANLDGTILPIATCSDDRDVSIFGLEIITHNGVQSLPDPYLNQLKREGFPNLGNTCYMNSILQSVFGIPTFAKDLLTQ
SQ  GIPWEKVSYDDLIMPLSQLLVLKDIRDVEIKGELLTSVKKSISTVADTFSGNEQNDAHEFLSLCLDQLKLNMEKVNAMWD
SQ  TERRNTCAGSAGTKRFVCPVGANFEFELHSSIICEGCGEATIKTEVSNYLSIDLHHGTKTHPLSIQKSFDLFFTPEKIEH
SQ  NCEKCKNKNSVLKYTLRRLPRVLIVHLKRYQVTTDLLPVKSEQPVEISKYLNISSHCHENRKLPFPLANTSPDVSQGMMP
SQ  GIFNQSMLSKKVISESCDPMVLQVGSSVDAEIQSFQIMYEDEDASEEQQQRGLESGSMLEPELVKTENRILRQKTSLATD
SQ  SMMGDGYSFLPMLCEPLSIQDPGLAEMGLQEVPENPEFKNYEKINIYGKSDGRTNTELSKLYQNHGSRIKGLFLPASLAS
SQ  VSSQEDPEKDLSRSPELQEDDPHSFAFGSDDSKDGEMGDDLQNYRLVSVVSHFGSSPNSGHYVSDVYDFQKQAWLLYSDV
SQ  QVFESSDPSIQENRLNSGYIFFYMHNEIFEELLKKASECKVLSTSKEEKRDIDYFSTLLNGLTYILEEF
//
ID  Q2KHV7;
PN  Ubiquitin carboxyl-terminal hydrolase 2;
GN  USP2;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O88623}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88623}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000250|UniProtKB:Q5U349}.
DR  UNIPROT: Q2KHV7;
DR  Pfam: PF00443;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DE  Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Possesses both ubiquitin- specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells. Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues. Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability. Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1. {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:O88623}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0046872;
GO  GO:0007049;
GO  GO:0048512;
GO  GO:0032922;
GO  GO:0043153;
GO  GO:0045475;
GO  GO:0007517;
GO  GO:0000122;
GO  GO:0045931;
GO  GO:0016579;
GO  GO:0050821;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSQLSSTLKRYTESARFTDAPFTKSSYGTYTPSSYGTNLAASFLEKEKFGFKPSPPTSYLTRPRTYGPPSILDYDRGRPL
SQ  LRPDVIGGGKRAESQTRGTERPSGSGLSGGSGFSYGVTTSSVSYLPVSARDQGVTLTQKKSNSQSDLARDFSSLQTSDSY
SQ  RLDSGNLGRSPMLARTRKELCALQGLYQAASRSEYLADYLENYGRKASAPQVPTPTPPSRAPEVLSPTYRPSGRYSLWEK
SQ  GKGQALVSSRSSSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYLRDLSHSSRAHTALMEEFA
SQ  KLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVIARPKSNTENLDHLPDDEKGRQM
SQ  WRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPITKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRC
SQ  RARKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTAFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYT
SQ  AYCRSPVTGEWHTFNDSSVSPMSSSQVRTSDAYLLFYELASPPSRM
//
ID  O57429;
PN  Ubiquitin carboxyl-terminal hydrolase 2;
GN  USP2;
OS  9031;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O88623}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88623}.
DR  UNIPROT: O57429;
DR  Pfam: PF00443;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DE  Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Possesses both ubiquitin- specific peptidase and isopeptidase activities. May play a role in the regulation of the circadian clock. {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:O88623}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0046872;
GO  GO:0016579;
GO  GO:0048511;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAARMAPTPRSSKVVQGLTGLRNLGNTCFMNSILQCLSNTKELRDYCLQNQYLRDLNNNSRMRTALMSEFAKLIQLLWTS
SQ  SPNDSVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHGEVNRVLVRPRANADTLDHLPDDEKSRQMWRRYQERED
SQ  SRVSDLFVGQLKSSLTCSECGYCSTAFDPFWDLSLPIPKKGYGEVTLMDCLRLFTKEDVLDGDEKPTCCRCKARTRCTKK
SQ  FSIQKFPKILVLHLKRFSEARIRASKLTTFVNFPLKDLDLREFASQSCNHAVYNLYAVSNHSGTTMGGHYTAYCKSPISS
SQ  EWHSFNDSRVTPMSSSHVRSSDAYLLFYELASPSSRM
//
ID  O75604;
PN  Ubiquitin carboxyl-terminal hydrolase 2;
GN  USP2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O88623}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88623}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000250|UniProtKB:Q5U349}. [Isoform 4]: Nucleus {ECO:0000250|UniProtKB:Q5U349}. Membrane {ECO:0000250|UniProtKB:O88623}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O88623}. Note=Predominantly expressed at membranes. {ECO:0000250|UniProtKB:O88623}.
DR  UNIPROT: O75604;
DR  UNIPROT: B0YJB8;
DR  UNIPROT: E9PPM2;
DR  UNIPROT: Q8IUM2;
DR  UNIPROT: Q8IW04;
DR  UNIPROT: Q96MB9;
DR  UNIPROT: Q9BQ21;
DR  PDB: 2HD5;
DR  PDB: 2IBI;
DR  PDB: 3NHE;
DR  PDB: 3V6C;
DR  PDB: 3V6E;
DR  PDB: 5XU8;
DR  PDB: 5XVE;
DR  PDB: 6DGF;
DR  Pfam: PF00443;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  OMIM: 604725;
DR  DisGeNET: 9099;
DE  Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (PubMed:17290220, PubMed:19917254, PubMed:19838211). Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity (PubMed:17290220, PubMed:19838211). Has no deubiquitinase activity against p53/TP53 (PubMed:17290220). Prevents MDM2-mediated degradation of MDM4 (PubMed:17290220). Plays a role in the G1/S cell-cycle progression in normal and cancer cells (PubMed:19917254). Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues (By similarity). Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability (By similarity). Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1 (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (By similarity). {ECO:0000250|UniProtKB:O88623, ECO:0000250|UniProtKB:Q5U349, ECO:0000269|PubMed:17290220, ECO:0000269|PubMed:19838211, ECO:0000269|PubMed:19917254}. [Isoform 4]: Circadian clock output effector that regulates Ca(2+) absorption in the small intestine. Probably functions by regulating protein levels of the membrane scaffold protein NHERF4 in a rhythmic manner, and is therefore likely to control Ca(2+) membrane permeability mediated by the Ca(2+) channel TRPV6 in the intestine. {ECO:0000250|UniProtKB:O88623}.
DE  Reference Proteome: Yes;
DE  Interaction: O75140; IntAct: EBI-24681385; Score: 0.56
DE  Interaction: P19012; IntAct: EBI-761008; Score: 0.70
DE  Interaction: Q96ED9; IntAct: EBI-24357988; Score: 0.56
DE  Interaction: Q7L4P6; IntAct: EBI-754156; Score: 0.37
DE  Interaction: Q15834; IntAct: EBI-755458; Score: 0.37
DE  Interaction: Q12933; IntAct: EBI-757021; Score: 0.78
DE  Interaction: Q9BUH8; IntAct: EBI-759049; Score: 0.37
DE  Interaction: Q00987; IntAct: EBI-7260289; Score: 0.40
DE  Interaction: P0CG48; IntAct: EBI-6965847; Score: 0.44
DE  Interaction: P36776; IntAct: EBI-2512362; Score: 0.40
DE  Interaction: Q9Y3B9; IntAct: EBI-2512362; Score: 0.40
DE  Interaction: Q92569; IntAct: EBI-10696117; Score: 0.49
DE  Interaction: Q62925; IntAct: EBI-9691474; Score: 0.44
DE  Interaction: Q8IYU2; IntAct: EBI-9683105; Score: 0.44
DE  Interaction: Q9NSC5; IntAct: EBI-10188691; Score: 0.72
DE  Interaction: I6L9F6; IntAct: EBI-10188701; Score: 0.56
DE  Interaction: P14373; IntAct: EBI-10188711; Score: 0.72
DE  Interaction: Q08379; IntAct: EBI-10188733; Score: 0.72
DE  Interaction: Q2TAC2; IntAct: EBI-10188755; Score: 0.56
DE  Interaction: Q5JR59; IntAct: EBI-10188765; Score: 0.56
DE  Interaction: Q6A162; IntAct: EBI-10188775; Score: 0.72
DE  Interaction: Q8IYA8; IntAct: EBI-10188785; Score: 0.56
DE  Interaction: Q8N1B4; IntAct: EBI-10188795; Score: 0.72
DE  Interaction: Q8ND90; IntAct: EBI-10188805; Score: 0.56
DE  Interaction: Q969G2; IntAct: EBI-10188815; Score: 0.67
DE  Interaction: Q96JN2; IntAct: EBI-10188825; Score: 0.56
DE  Interaction: Q9BRK4; IntAct: EBI-10188837; Score: 0.72
DE  Interaction: Q9BVG8; IntAct: EBI-10188847; Score: 0.56
DE  Interaction: Q9GZM8; IntAct: EBI-10188857; Score: 0.72
DE  Interaction: Q9UJC3; IntAct: EBI-10188867; Score: 0.56
DE  Interaction: Q9Y4K3; IntAct: EBI-10188877; Score: 0.56
DE  Interaction: P06428; IntAct: EBI-11737925; Score: 0.37
DE  Interaction: Q9NRD5; IntAct: EBI-24275762; Score: 0.56
DE  Interaction: Q9UBR4; IntAct: EBI-24280767; Score: 0.56
DE  Interaction: Q96MT8; IntAct: EBI-24282871; Score: 0.56
DE  Interaction: Q8WWB3; IntAct: EBI-24287760; Score: 0.56
DE  Interaction: O60504; IntAct: EBI-24296555; Score: 0.56
DE  Interaction: O96006; IntAct: EBI-24296826; Score: 0.56
DE  Interaction: Q9UGI0; IntAct: EBI-24310495; Score: 0.56
DE  Interaction: A6NLX3; IntAct: EBI-24316142; Score: 0.56
DE  Interaction: Q59EK9; IntAct: EBI-24324288; Score: 0.56
DE  Interaction: Q86VP1; IntAct: EBI-24329367; Score: 0.56
DE  Interaction: Q9NYB9; IntAct: EBI-24334778; Score: 0.56
DE  Interaction: Q13137; IntAct: EBI-24334992; Score: 0.56
DE  Interaction: Q8HWS3; IntAct: EBI-24334946; Score: 0.56
DE  Interaction: Q03252; IntAct: EBI-24339221; Score: 0.56
DE  Interaction: Q08043; IntAct: EBI-24343793; Score: 0.56
DE  Interaction: Q13077; IntAct: EBI-24344810; Score: 0.56
DE  Interaction: Q86U10; IntAct: EBI-24349210; Score: 0.56
DE  Interaction: Q9UKT9; IntAct: EBI-24353109; Score: 0.56
DE  Interaction: Q9UBB9; IntAct: EBI-24362657; Score: 0.56
DE  Interaction: Q4G0R1; IntAct: EBI-25249913; Score: 0.56
DE  Interaction: P12814; IntAct: EBI-25252754; Score: 0.56
DE  Interaction: Q8TD16; IntAct: EBI-25254904; Score: 0.56
DE  Interaction: Q8N6Y0; IntAct: EBI-25256814; Score: 0.56
DE  Interaction: Q08117; IntAct: EBI-25258322; Score: 0.56
DE  Interaction: Q9UJV3; IntAct: EBI-24488835; Score: 0.56
DE  Interaction: Q96CV9; IntAct: EBI-24491151; Score: 0.56
DE  Interaction: Q15276; IntAct: EBI-24491540; Score: 0.56
DE  Interaction: Q5JST6; IntAct: EBI-24500930; Score: 0.56
DE  Interaction: O00471; IntAct: EBI-24504009; Score: 0.56
DE  Interaction: Q9NZV7; IntAct: EBI-24606277; Score: 0.56
DE  Interaction: Q9NRA8; IntAct: EBI-24606648; Score: 0.56
DE  Interaction: Q6PI77; IntAct: EBI-24616394; Score: 0.56
DE  Interaction: Q9BSW2; IntAct: EBI-24627764; Score: 0.56
DE  Interaction: P51692; IntAct: EBI-24661369; Score: 0.56
DE  Interaction: A6NEM1; IntAct: EBI-24676390; Score: 0.56
DE  Interaction: Q13084; IntAct: EBI-24707853; Score: 0.56
DE  Interaction: Q9H596; IntAct: EBI-24722163; Score: 0.56
DE  Interaction: Q03169; IntAct: EBI-24732317; Score: 0.56
DE  Interaction: Q6MZQ0; IntAct: EBI-24740293; Score: 0.56
DE  Interaction: Q9UK41; IntAct: EBI-24740082; Score: 0.56
DE  Interaction: Q8N9I9; IntAct: EBI-24750467; Score: 0.56
DE  Interaction: Q5VZ52; IntAct: EBI-25280987; Score: 0.56
DE  Interaction: P36406; IntAct: EBI-24374020; Score: 0.56
DE  Interaction: Q8WW24; IntAct: EBI-24376880; Score: 0.56
DE  Interaction: P57678; IntAct: EBI-24379179; Score: 0.56
DE  Interaction: P35609; IntAct: EBI-24380145; Score: 0.56
DE  Interaction: P07196; IntAct: EBI-24382979; Score: 0.56
DE  Interaction: Q96CA5; IntAct: EBI-24387672; Score: 0.56
DE  Interaction: Q15323; IntAct: EBI-24391617; Score: 0.56
DE  Interaction: Q92764; IntAct: EBI-24396907; Score: 0.56
DE  Interaction: Q9H257; IntAct: EBI-24398017; Score: 0.56
DE  Interaction: A2RRN7; IntAct: EBI-24404520; Score: 0.56
DE  Interaction: Q4V328; IntAct: EBI-24407518; Score: 0.56
DE  Interaction: O76011; IntAct: EBI-25262386; Score: 0.56
DE  Interaction: Q9NRI5; IntAct: EBI-24423575; Score: 0.56
DE  Interaction: Q86XT4; IntAct: EBI-24429111; Score: 0.56
DE  Interaction: Q9NYA3; IntAct: EBI-24435378; Score: 0.56
DE  Interaction: Q58EX7; IntAct: EBI-24435792; Score: 0.56
DE  Interaction: Q70EL1; IntAct: EBI-24438478; Score: 0.56
DE  Interaction: Q7Z3Y8; IntAct: EBI-24439251; Score: 0.56
DE  Interaction: Q15742; IntAct: EBI-24440205; Score: 0.56
DE  Interaction: Q96B26; IntAct: EBI-24444152; Score: 0.56
DE  Interaction: P56945; IntAct: EBI-24457734; Score: 0.56
DE  Interaction: A6NC98; IntAct: EBI-24460031; Score: 0.56
DE  Interaction: Q8WTU0; IntAct: EBI-24465472; Score: 0.56
DE  Interaction: Q8N4Y2; IntAct: EBI-24466676; Score: 0.56
DE  Interaction: O14492; IntAct: EBI-24471842; Score: 0.56
DE  Interaction: Q8NHQ1; IntAct: EBI-24472380; Score: 0.56
DE  Interaction: Q15654; IntAct: EBI-24473595; Score: 0.56
DE  Interaction: Q86V38; IntAct: EBI-24474468; Score: 0.56
DE  Interaction: P60903; IntAct: EBI-24539216; Score: 0.56
DE  Interaction: Q14525; IntAct: EBI-24542306; Score: 0.56
DE  Interaction: Q16633; IntAct: EBI-24545862; Score: 0.56
DE  Interaction: Q9GZV8; IntAct: EBI-24548496; Score: 0.56
DE  Interaction: O75564; IntAct: EBI-24569259; Score: 0.56
DE  Interaction: Q14451; IntAct: EBI-24585126; Score: 0.56
DE  Interaction: Q96N16; IntAct: EBI-24585374; Score: 0.56
DE  Interaction: Q5TA45; IntAct: EBI-24591175; Score: 0.56
DE  Interaction: Q674X7; IntAct: EBI-24593291; Score: 0.56
DE  Interaction: O43482; IntAct: EBI-24597090; Score: 0.56
DE  Interaction: Q99932; IntAct: EBI-24635245; Score: 0.56
DE  Interaction: Q5U5U6; IntAct: EBI-15596142; Score: 0.44
DE  Interaction: P62990; IntAct: EBI-15596163; Score: 0.44
DE  Interaction: G5E9A7; IntAct: EBI-25842356; Score: 0.56
DE  Interaction: Q01658; IntAct: EBI-25845689; Score: 0.56
DE  Interaction: Q00403; IntAct: EBI-25865141; Score: 0.56
DE  Interaction: P04792; IntAct: EBI-25870731; Score: 0.56
DE  Interaction: O60260; IntAct: EBI-25879990; Score: 0.56
DE  Interaction: D3DTS7; IntAct: EBI-25882988; Score: 0.56
DE  Interaction: P60891; IntAct: EBI-25886321; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25897757; Score: 0.56
DE  Interaction: Q9Y5Q9; IntAct: EBI-25907028; Score: 0.56
DE  Interaction: Q7Z333; IntAct: EBI-25914242; Score: 0.56
DE  Interaction: O60333; IntAct: EBI-25915065; Score: 0.56
DE  Interaction: Q9Y3C5; IntAct: EBI-25918668; Score: 0.56
DE  Interaction: O43464; IntAct: EBI-25920135; Score: 0.56
DE  Interaction: Q8WXH2; IntAct: EBI-25927547; Score: 0.56
DE  Interaction: Q7Z699; IntAct: EBI-25931364; Score: 0.56
DE  Interaction: P00441; IntAct: EBI-25934473; Score: 0.56
DE  Interaction: P05067; IntAct: EBI-25936228; Score: 0.56
DE  Interaction: P37840; IntAct: EBI-25940368; Score: 0.56
DE  Interaction: P42858; IntAct: EBI-25943183; Score: 0.56
DE  Interaction: P54253; IntAct: EBI-25975184; Score: 0.56
DE  Interaction: Q13148; IntAct: EBI-25983520; Score: 0.56
DE  Interaction: Q13616; IntAct: EBI-26585225; Score: 0.44
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0030332;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0031625;
GO  GO:0007049;
GO  GO:0048512;
GO  GO:0032922;
GO  GO:0043153;
GO  GO:0045475;
GO  GO:0007517;
GO  GO:0000122;
GO  GO:0045931;
GO  GO:0016579;
GO  GO:0050821;
GO  GO:1901796;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSQLSSTLKRYTESARYTDAHYAKSGYGAYTPSSYGANLAASLLEKEKLGFKPVPTSSFLTRPRTYGPSSLLDYDRGRPL
SQ  LRPDITGGGKRAESQTRGTERPLGSGLSGGSGFPYGVTNNCLSYLPINAYDQGVTLTQKLDSQSDLARDFSSLRTSDSYR
SQ  IDPRNLGRSPMLARTRKELCTLQGLYQTASCPEYLVDYLENYGRKGSASQVPSQAPPSRVPEIISPTYRPIGRYTLWETG
SQ  KGQAPGPSRSSSPGRDGMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAK
SQ  LIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKGRQMW
SQ  RKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCR
SQ  GRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTA
SQ  YCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM
//
ID  O88623;
PN  Ubiquitin carboxyl-terminal hydrolase 2;
GN  Usp2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:14686789}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14686789}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000250|UniProtKB:Q5U349}. [Isoform 2]: Nucleus {ECO:0000250|UniProtKB:Q5U349}. Membrane {ECO:0000269|PubMed:26756164}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:26756164}. Note=Predominantly expressed at membranes. {ECO:0000269|PubMed:26756164}.
DR  UNIPROT: O88623;
DR  UNIPROT: Q6X4T9;
DR  UNIPROT: Q6X4U1;
DR  UNIPROT: Q8VD74;
DR  UNIPROT: Q9JJ87;
DR  Pfam: PF00443;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DE  Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (By similarity). Isoform 1 and isoform 2 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity (By similarity). Has no deubiquitinase activity against p53/TP53 (By similarity). Prevents MDM2-mediated degradation of MDM4 (By similarity). Plays a role in the G1/S cell-cycle progression in normal and cancer cells (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (By similarity). Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues (PubMed:23213472, PubMed:25238854, PubMed:26756164). Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability (PubMed:23213472). Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1 (PubMed:25238854). {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:Q5U349, ECO:0000269|PubMed:23213472, ECO:0000269|PubMed:25238854}. [Isoform 2]: Circadian clock output effector that regulates Ca(2+) absorption in the small intestine. Probably functions by regulating protein levels of the membrane scaffold protein PDZD3 in a rhythmic manner, and is therefore likely to control Ca(2+) membrane permeability mediated by the Ca(2+) channel TRPV6 in the intestine. {ECO:0000269|PubMed:26756164}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030332;
GO  GO:0004843;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0031625;
GO  GO:0007049;
GO  GO:0048512;
GO  GO:0032922;
GO  GO:0043153;
GO  GO:0045475;
GO  GO:0007517;
GO  GO:0051926;
GO  GO:0048642;
GO  GO:0000122;
GO  GO:0045931;
GO  GO:0048643;
GO  GO:0016579;
GO  GO:0050821;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSQLSSTLKRYTESSRYTDAPYAKPGYGTYTPSSYGANLAASFLEKEKLGFKPVSPTSFLPRPRTYGPSSILDCDRGRPL
SQ  LRSDIIGSSKRSESQTRGNERPSGSGLNGGSGFSYGVSSNSLSYLPMNARDQGVTLSQKKSNSQSDLARDFSSLRTSDGY
SQ  RTSEGFRIDPGNLGRSPMLARTRKELCALQGLYQAASRSEYLTDYLENYGRKGSAPQVLTQAPPPSRVPEVLSPTYRPSG
SQ  RYTLWEKSKGQASGPSRSSSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHT
SQ  ALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFMGYNQQDAQEFLRFLLDGLHNEVNRVAARPKASPETLDHLPD
SQ  EEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDILDGDE
SQ  KPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGT
SQ  TMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM
//
ID  Q5U349;
PN  Ubiquitin carboxyl-terminal hydrolase 2;
GN  Usp2;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:O88623}. [Isoform 1]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12107281}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000269|PubMed:12107281}. [Isoform 2]: Nucleus {ECO:0000269|PubMed:12107281}. Membrane {ECO:0000250|UniProtKB:O88623}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O88623}. Note=Predominantly expressed at membranes. {ECO:0000250|UniProtKB:O88623}.
DR  UNIPROT: Q5U349;
DR  UNIPROT: Q9QXL3;
DR  UNIPROT: Q9QXL4;
DR  UNIPROT: Q9R083;
DR  UNIPROT: Q9R084;
DR  Pfam: PF00443;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DE  Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (By similarity). Isoform 1 and isoform 2 possess both ubiquitin-specific peptidase and isopeptidase activities (PubMed:12107281). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity (By similarity). Has no deubiquitinase activity against p53/TP53 (By similarity). Prevents MDM2-mediated degradation of MDM4 (By similarity). Plays a role in the G1/S cell-cycle progression in normal and cancer cells (By similarity). Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues (PubMed:23213472). Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability (PubMed:23213472). Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1 (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (PubMed:12107281). {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:O88623, ECO:0000269|PubMed:10938131, ECO:0000269|PubMed:12107281, ECO:0000269|PubMed:23213472}. [Isoform 2]: Circadian clock output effector that regulates Ca(2+) absorption in the small intestine. Probably functions by regulating protein levels of the membrane scaffold protein NHERF4 in a rhythmic manner, and is therefore likely to control Ca(2+) membrane permeability mediated by the Ca(2+) channel TRPV6 in the intestine. {ECO:0000250|UniProtKB:O88623}.
DE  Reference Proteome: Yes;
DE  Interaction: Q07820; IntAct: EBI-15824534; Score: 0.44
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0016020;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030332;
GO  GO:0004843;
GO  GO:0042802;
GO  GO:0046872;
GO  GO:0031625;
GO  GO:0007049;
GO  GO:0048512;
GO  GO:0032922;
GO  GO:0043153;
GO  GO:0045475;
GO  GO:0007517;
GO  GO:0051926;
GO  GO:0048642;
GO  GO:0000122;
GO  GO:0045931;
GO  GO:0048643;
GO  GO:0016579;
GO  GO:0050821;
GO  GO:0006511;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MSQLSSTLKRYTESSRYTDAPYAKSGYGTYTPSSYGANLAASFLEKEKLGFKPVSPTSFLPRPRTYGPSSILDCDRGRPL
SQ  LRSDITGGSKRSESQTRGNERPSGSGLNGGSGFPYGVTSNSLSYLPMNARDQGVTLGQKKSNSQSDLARDFSSLRTSDSY
SQ  RTSDGYRASDGFRIDPGNLGRSPMLARTRKELCALQGLYQAASRSEYLTDYLENYGRKGSAPQVLTQAPPSRVPEVLSPT
SQ  YRPSGRYTLWEKNKGQASGPSRSTSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHT
SQ  SSAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVAARPKPSPESL
SQ  DHLPDEEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDV
SQ  LDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVS
SQ  NHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM
//
ID  A6QNM7;
PN  Ubiquitin carboxyl-terminal hydrolase 33;
GN  USP33;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}.
DR  UNIPROT: A6QNM7;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G- protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005925;
GO  GO:0005794;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0001664;
GO  GO:0031267;
GO  GO:0008270;
GO  GO:0007411;
GO  GO:0016477;
GO  GO:0009267;
GO  GO:0051298;
GO  GO:0006897;
GO  GO:0032091;
GO  GO:0032092;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0050821;
GO  GO:0010506;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSFRSHCPHLDSVGEITKEDLIQKSHGSCQDCKVRGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLR
SQ  VWCYACSKEVFLDRKLGTQPSLPHVKPLHQIQENGVQDFKIPSNTTLKTPLVAVFDDLDIEVEEEDELKARGLTGLKNIG
SQ  NTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNPTFRGYSQQD
SQ  AQEFLRCLMDLLHEELKEQVMEVEEDPQTIMTEETMEEDKSQSDVDFQSCESCSSSDKAENENGSRSFSEDNNETTMLIQ
SQ  DDENNSEMSKDWQKEKMCNKINKVHSEGELDKDRDSVSETADLNNQETVKVQIHSRASEYITDVHLNDLSTPQILPSNEG
SQ  VNPRLSASPPKSGNLWPGLPPTHKKVQSALSPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIP
SQ  GKEDLAKLHSSSHPTSIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPSWFWGPVVTLQDCLAAFFARDELKGDNMYSC
SQ  EKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPVQIVTYDLLSVICHHGTAS
SQ  SGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQKERRRISNLLNIMEPSLLQFYISRQWLNKF
SQ  KTFAEPGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPAVNHLYICHTCQIEAEKIEKRRKTELEI
SQ  FIRLNRAFQEEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCGNVILRQGADSGQISEETWNFLQSIYG
SQ  GGPEVILRPPVVHVDPDAVQAEEKIEVETRSL
//
ID  A5PMR2;
PN  Ubiquitin carboxyl-terminal hydrolase 33;
GN  usp33;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}.
DR  UNIPROT: A5PMR2;
DR  UNIPROT: Q6NYK6;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of ccp110 in S and G2/M phase, leading to stabilize ccp110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of robo1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of robo1. Acts as a regulator of G- protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (arrb1 and arrb2) and beta-2 adrenergic receptor (adrb2). Deubiquitinates dio2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys- 48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008270;
GO  GO:0007411;
GO  GO:0016477;
GO  GO:0051298;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGVSSNDCPHLECVGEITKEELIQKSHGQCQDCKVGGPNLWACLENGCSYVGCGESHADHSTVHSQETRHNLTVNLTTL
SQ  RVWCYACTKEVFLERKLGPHKQLPNAAKAVSPVQTPCQDLNTPGSPTSLRVPSAGTCDDLDMETEEEDELRTRGLTGLKN
SQ  IGNTCYMNAALQALSNCPPLTQFFLECGGLVKTDKKPALCKSYQKLITDLWHKNRNAYVVPTNLFQGIKAVNPMFRGYSQ
SQ  QDSQEFLRCLMDQLHEELKELIPEPEDPNQAVAMDDSPDEDNHSQSDDFQSCESCGSSDRADNEGPRVPEDINEAEMLMP
SQ  EQNQNNRDWQKEKNLINNLYRAGSHGDLDKDVDTTSDSRPIISSQGAIKAQGRTSDSEIQVSSTVRPQSPTGNEGITSRL
SQ  SSSPPKSSAWPNLSSTHKKVPMFTPTKTKRQRKYHSIISEVFDGTIVSSVQCLTCDRVSVTLENFQDISLPIPGKEDLAK
SQ  LHSSSHQTALVKAGSCGEAYAPQGWIAFVMEYIKSWFWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKV
SQ  QSLPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLEMQPFLAKDSSALTTTYDLLSVICHHGTASSGHYIAYCRNELNQL
SQ  WYEFDDQSVTEVSESCVQNAEAYVLFYKKSNDETQKERRKVTSLFNMMEPSLLQFYVSRQWLNKFKTFAEPGPISNHDFL
SQ  CAHGGIPPNKAAYIDDLVLMIPQNVWDHLYSRYGGGPAVNHLYVCHTCQNEIEKLEKRRKNELDMFVRLNKAFQEEESPV
SQ  VIYCISMQWFREWESFVKGKDIDPPGPIDNSKIAVNKNGHITLKPGADSGQISEETWNFLHNIHGGGPVVTVRPSVSHQE
SQ  SETSQSEEKIEVETRTV
//
ID  Q8TEY7;
PN  Ubiquitin carboxyl-terminal hydrolase 33;
GN  USP33;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19118533}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23486064}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (PubMed:23486064). {ECO:0000269|PubMed:23486064}. [Isoform 3]: Golgi apparatus {ECO:0000269|PubMed:21801292}.
DR  UNIPROT: Q8TEY7;
DR  UNIPROT: Q8TEY6;
DR  UNIPROT: Q96AV6;
DR  UNIPROT: Q9H9F0;
DR  UNIPROT: Q9UPQ5;
DR  PDB: 2UZG;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DR  OMIM: 615146;
DR  DisGeNET: 23032;
DE  Function: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G- protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:12865408, ECO:0000269|PubMed:19363159, ECO:0000269|PubMed:19424180, ECO:0000269|PubMed:23486064}.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q9NY93; IntAct: EBI-734281; Score: 0.00
DE  Interaction: Q13352; IntAct: EBI-734878; Score: 0.00
DE  Interaction: P07550; IntAct: EBI-6993284; Score: 0.43
DE  Interaction: Q13228; IntAct: EBI-2509553; Score: 0.65
DE  Interaction: Q13325; IntAct: EBI-2513595; Score: 0.40
DE  Interaction: Q96KR1; IntAct: EBI-2513595; Score: 0.40
DE  Interaction: Q13601; IntAct: EBI-2513595; Score: 0.40
DE  Interaction: Q5VTL8; IntAct: EBI-2513595; Score: 0.40
DE  Interaction: Q9H668; IntAct: EBI-21527292; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-21550215; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: O43291; IntAct: EBI-21587968; Score: 0.35
DE  Interaction: Q8WWF5; IntAct: EBI-21589535; Score: 0.35
DE  Interaction: Q9BYE7; IntAct: EBI-21658407; Score: 0.35
DE  Interaction: Q99675; IntAct: EBI-21775037; Score: 0.35
DE  Interaction: P58304; IntAct: EBI-21789618; Score: 0.35
DE  Interaction: Q643R3; IntAct: EBI-21809690; Score: 0.35
DE  Interaction: Q99767; IntAct: EBI-21817505; Score: 0.35
DE  Interaction: O60603; IntAct: EBI-21859955; Score: 0.35
DE  Interaction: Q9H0I9; IntAct: EBI-21896698; Score: 0.35
DE  Interaction: O55005; IntAct: EBI-15801403; Score: 0.40
DE  Interaction: Q9Y6N7; IntAct: EBI-15801424; Score: 0.40
DE  Interaction: P08912; IntAct: EBI-20810156; Score: 0.37
DE  Interaction: Q5W0B1; IntAct: EBI-21374610; Score: 0.00
DE  Interaction: Q9NRI5; IntAct: EBI-21374598; Score: 0.00
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: P0DTC5; IntAct: EBI-27125869; Score: 0.35
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005925;
GO  GO:0005794;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0030891;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0001664;
GO  GO:0031267;
GO  GO:0008270;
GO  GO:0007411;
GO  GO:0016477;
GO  GO:0009267;
GO  GO:0051298;
GO  GO:0006897;
GO  GO:0032091;
GO  GO:0032092;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0050821;
GO  GO:0010506;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTGSNSHITILTLKVLPHFESLGKQEKIPNKMSAFRNHCPHLDSVGEITKEDLIQKSLGTCQDCKVQGPNLWACLENRCS
SQ  YVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEVFLDRKLGTQPSLPHVRQPHQIQENSVQDFKIPSNTTLKT
SQ  PLVAVFDDLDIEADEEDELRARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELW
SQ  HKSRPGSVVPTTLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQVMEVEEDPQTITTEETMEEDKSQSDVDFQS
SQ  CESCSNSDRAENENGSRCFSEDNNETTMLIQDDENNSEMSKDWQKEKMCNKINKVNSEGEFDKDRDSISETVDLNNQETV
SQ  KVQIHSRASEYITDVHSNDLSTPQILPSNEGVNPRLSASPPKSGNLWPGLAPPHKKAQSASPKRKKQHKKYRSVISDIFD
SQ  GTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPS
SQ  WFWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGL
SQ  DLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQ
SQ  KERRRISNLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGG
SQ  GPAVNHLYICHTCQIEAEKIEKRRKTELEIFIRLNRAFQKEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAV
SQ  TKCGNVMLRQGADSGQISEETWNFLQSIYGGGPEVILRPPVVHVDPDILQAEEKIEVETRSL
//
ID  Q8R5K2;
PN  Ubiquitin carboxyl-terminal hydrolase 33;
GN  Usp33;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}.
DR  UNIPROT: Q8R5K2;
DR  UNIPROT: Q3UP32;
DR  UNIPROT: Q5FWK0;
DR  UNIPROT: Q8K0I3;
DR  UNIPROT: Q99K22;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G- protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:19684588, ECO:0000269|PubMed:19706539}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UHL9; IntAct: EBI-12517081; Score: 0.37
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0005925;
GO  GO:0005794;
GO  GO:0043025;
GO  GO:0005654;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0001664;
GO  GO:0031267;
GO  GO:0008270;
GO  GO:0007411;
GO  GO:0016477;
GO  GO:0009267;
GO  GO:0051298;
GO  GO:0006897;
GO  GO:0032091;
GO  GO:0032092;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0050821;
GO  GO:0010506;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTTFRNHCPHLDSVGEITKEDLIQKSLGACQDCKVRGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLR
SQ  VWCYACSKEVFLDRKLGTPPSLPHVRQPQQTQENSVQDFKIPSNPALKTPMVAVSEDLDIEVEEEDELKARGLTGLKNIG
SQ  NTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPANLFQGIKTVNPTFRGYSQQD
SQ  AQEFLRCLMDLLHEELKEQVMEMEEEPQTLTSEETVEEEKSQSDVDFQSCESCSSSEKAENESGSKGFPEDSNETTMLIQ
SQ  DEDDLEMAKDWQKEKVCNKINKANADVELDKDRDTVCETVDLNSQETVKVQIHGRASESITDVHLNDLATSQILPSNESV
SQ  SPRLSASPPKLGSLWPGLSPPHKKAQSTSAKRKKQHKKYRSVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGK
SQ  EDLAKLHSSSHPTIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPSWFWGPVVTLQDCLAAFFARDELKGDNMYSCEKC
SQ  KKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGH
SQ  YIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQKERRRISNLLNIMEPSLLQFYISRQWLNKFKTF
SQ  AEPGPISNNDFLCIHGGIPPRKASYIEDLVLMLPQNIWDNLYSRYGGGPAVNHLYICHTCQIELEKIEKRRKTELEIFIR
SQ  LNRAFQEEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCGSVMLKQGADSGQISEETWNFLQSIYGGGP
SQ  EVILRPPVVHVDPDVLQAEEKIEVETRSL
//
ID  Q5REG5;
PN  Ubiquitin carboxyl-terminal hydrolase 33;
GN  USP33;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}.
DR  UNIPROT: Q5REG5;
DR  UNIPROT: Q5R7L1;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G- protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008270;
GO  GO:0007411;
GO  GO:0016477;
GO  GO:0051298;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAFRNHCPHLDSVGEITKEDLIQKSQGTCQDCKVRGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLR
SQ  VWCYACSKEVFLDRKLGTQPSLPHVRQPHQIQENSVQDFKIPSNTTLKTPLVAVFDDLDIEVDEEDELRARGLTGLKNIG
SQ  NTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTNLFQGIKTVNPTFRGYSQQD
SQ  AQEFLRCLMDLLHEELKEQVMEVEDPQTITTEETMEEDKSQSDVDFQSCESCSNSDKAENENGSSCFSEDNNETTMLIQD
SQ  DENNSEMSKDWQKEKMCNKINKVNSEGELDKDRDSISETVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQILPSNESI
SQ  NPRLSASPPKSGNLWPGLAPPHKKAQSASPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGK
SQ  EDLAKLHSSSHPTSIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPSWFWGPVVTLQDCLAAFFARDELKGDNMYSCEK
SQ  CKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSG
SQ  HYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQKERRRISNLLNIMEPSLLQFYISRQWLNKFKT
SQ  FAEPGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPAVNHLYICHTCQIEAEEIEKKKKNRRKTEL
SQ  EIFIRLNRAFQKEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCGSVMLRQGADSGQISEETWNFLQSI
SQ  YGGGPEVILRPPVVHVDPDILQAEEKIEVETRSL
//
ID  Q28CN3;
PN  Ubiquitin carboxyl-terminal hydrolase 33;
GN  usp33;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}.
DR  UNIPROT: Q28CN3;
DR  UNIPROT: B7ZU27;
DR  UNIPROT: F7EIJ9;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of ccp110 in S and G2/M phase, leading to stabilize ccp110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of robo1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of robo1. Acts as a regulator of G- protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (arrb1 and arrb2) and beta-2 adrenergic receptor (adrb2). Deubiquitinates dio2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys- 48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008270;
GO  GO:0007411;
GO  GO:0016477;
GO  GO:0051298;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSLVCDCPHLESVGEVTKEELIKKSHGSCQDCRVRGPNLWACLENGCSYVGCGESHVDHSTLHSQDTKHCLTVNLTTLR
SQ  VWCYTCSKEVFLDRKLSTQPTSAKLQDSHTQESKMSSSLTLKIPAAVVSENLDIELEEEDELKTRGLTGLKNIGNTCYMN
SQ  AALQALSNCPPLTHYFLDCGGLARTDKKPALCKSYQKLMSDIWHKNRPGFVIPTNLFQGIKSVNPTFRGYSQQDAQEFLR
SQ  CLMDVLHEELKEQIVEVEEDAQTGIVEENLDEDKSQSDNDFHSCDSGSSSDHAESESRKLSEELTESTMLIHEDQKDVES
SQ  CKTWQKEKKFSNNLNQNHFLQDFEKNIQSTIEESECLKQETVKVQIQSKAADFTAEVNMNDLPTSQTPLLNEGATTHLSS
SQ  SPPKPGAVWTGHKKVPGLCPAKKRKQKKYHSVIADIFDGTIVSSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSS
SQ  HQSSLVKAGSCGEAYAPQGWIAFFLEYFKSWFWGPTVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPE
SQ  ILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLAKDSPSQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFD
SQ  DQSVTEVSEATVQNAEAYVLFYRKASEEAQKERRRVSCLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGG
SQ  VPPRKASFIEDLVVMLPQNIWDYLYSRYGGGPAVNHLYVCYTCQTEMEKIEKRRKMELETFIRLNKAFQEEESPAVIYCI
SQ  SMQWFREWEGFVKSKDSDPPGPIDNTKIAAAKCGHITLRQGADSGQISEETWLFLQSIYGGGPEITLRQNVTLAESEGGH
SQ  AEEKIDVETRNI
//
ID  Q9NRR5;
PN  Ubiquilin-4;
GN  UBQLN4;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:11001934, ECO:0000269|PubMed:15280365, ECO:0000269|PubMed:29666234, ECO:0000269|PubMed:30612738, ECO:0000269|PubMed:34245648}. Cytoplasm {ECO:0000269|PubMed:29666234, ECO:0000269|PubMed:30612738, ECO:0000269|PubMed:34245648}. Chromosome {ECO:0000269|PubMed:30612738}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q99NB8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99NB8}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:23459205}. Note=Colocalizes with the proteasome, both in nucleus and cytoplasm (PubMed:15280365). Exported from the nucleus following interaction with DESI1/POST (PubMed:29666234). In response to DNA damage and phosphorylation at Ser-318 by ATM, localizes to the nucleus and is recruited to sites of DNA damage (PubMed:30612738). {ECO:0000269|PubMed:15280365, ECO:0000269|PubMed:29666234, ECO:0000269|PubMed:30612738}.
DR  UNIPROT: Q9NRR5;
DR  UNIPROT: A6ND44;
DR  UNIPROT: B2RAY7;
DR  UNIPROT: Q5VYA0;
DR  UNIPROT: Q5VYA1;
DR  UNIPROT: Q9BR98;
DR  UNIPROT: Q9UHX4;
DR  Pfam: PF00627;
DR  Pfam: PF00240;
DR  PROSITE: PS50030;
DR  PROSITE: PS50053;
DR  OMIM: 105400;
DR  OMIM: 605440;
DR  DisGeNET: 56893;
DE  Function: Regulator of protein degradation that mediates the proteasomal targeting of misfolded, mislocalized or accumulated proteins (PubMed:15280365, PubMed:27113755, PubMed:29666234, PubMed:30612738). Acts by binding polyubiquitin chains of target proteins via its UBA domain and by interacting with subunits of the proteasome via its ubiquitin-like domain (PubMed:15280365, PubMed:27113755, PubMed:30612738). Key regulator of DNA repair that represses homologous recombination repair: in response to DNA damage, recruited to sites of DNA damage following phosphorylation by ATM and acts by binding and removing ubiquitinated MRE11 from damaged chromatin, leading to MRE11 degradation by the proteasome (PubMed:30612738). MRE11 degradation prevents homologous recombination repair, redirecting double-strand break repair toward non-homologous end joining (NHEJ) (PubMed:30612738). Specifically recognizes and binds mislocalized transmembrane-containing proteins and targets them to proteasomal degradation (PubMed:27113755). Collaborates with DESI1/POST in the export of ubiquitinated proteins from the nucleus to the cytoplasm (PubMed:29666234). Also plays a role in the regulation of the proteasomal degradation of non-ubiquitinated GJA1 (By similarity). Acts as an adapter protein that recruits UBQLN1 to the autophagy machinery (PubMed:23459205). Mediates the association of UBQLN1 with autophagosomes and the autophagy-related protein LC3 (MAP1LC3A/B/C) and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:23459205). {ECO:0000250|UniProtKB:Q99NB8, ECO:0000269|PubMed:15280365, ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:27113755, ECO:0000269|PubMed:29666234, ECO:0000269|PubMed:30612738}.
DE  Disease: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:28463112}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Note=Defects in UBQLN4 are the cause of the UBQLN4 deficiency syndrome (UBDS) (PubMed:30612738). Patients display intellectual impairment, growth retardation, microcephaly, facial dysmorphism, hearing loss, ataxia and anemia (PubMed:30612738). Cells display genomic instability characterized by hypersensitivity to genotoxic agents, leading to enhanced apoptotic cell death in response to DNA damage (PubMed:30612738). {ECO:0000269|PubMed:30612738}.
DE  Reference Proteome: Yes;
DE  Interaction: P53816; IntAct: EBI-954950; Score: 0.00
DE  Interaction: Q09013; IntAct: EBI-950164; Score: 0.00
DE  Interaction: Q9NRD5; IntAct: EBI-950320; Score: 0.00
DE  Interaction: Q9Y3C5; IntAct: EBI-7220580; Score: 0.37
DE  Interaction: O75400; IntAct: EBI-7241308; Score: 0.55
DE  Interaction: O15198; IntAct: EBI-7257371; Score: 0.37
DE  Interaction: P21246; IntAct: EBI-728453; Score: 0.00
DE  Interaction: P68104; IntAct: EBI-728787; Score: 0.00
DE  Interaction: Q13432; IntAct: EBI-728790; Score: 0.00
DE  Interaction: P19793; IntAct: EBI-729663; Score: 0.00
DE  Interaction: Q12824; IntAct: EBI-731464; Score: 0.00
DE  Interaction: Q13564; IntAct: EBI-734060; Score: 0.00
DE  Interaction: P05408; IntAct: EBI-735775; Score: 0.00
DE  Interaction: O15209; IntAct: EBI-736202; Score: 0.00
DE  Interaction: P54253; IntAct: EBI-930979; Score: 0.59
DE  Interaction: Q9NRR5; IntAct: EBI-944340; Score: 0.68
DE  Interaction: Q9BRR6; IntAct: EBI-954701; Score: 0.00
DE  Interaction: O95994; IntAct: EBI-954710; Score: 0.00
DE  Interaction: P15514; IntAct: EBI-954718; Score: 0.00
DE  Interaction: P46379; IntAct: EBI-954726; Score: 0.00
DE  Interaction: Q56P03; IntAct: EBI-954734; Score: 0.00
DE  Interaction: Q8N806; IntAct: EBI-954742; Score: 0.00
DE  Interaction: Q969H8; IntAct: EBI-954750; Score: 0.00
DE  Interaction: Q9BXJ1; IntAct: EBI-954758; Score: 0.00
DE  Interaction: Q06455; IntAct: EBI-954766; Score: 0.00
DE  Interaction: O00585; IntAct: EBI-954774; Score: 0.00
DE  Interaction: P14209; IntAct: EBI-954782; Score: 0.00
DE  Interaction: Q15517; IntAct: EBI-954790; Score: 0.00
DE  Interaction: P27658; IntAct: EBI-954798; Score: 0.00
DE  Interaction: P33240; IntAct: EBI-954806; Score: 0.00
DE  Interaction: Q9H0L4; IntAct: EBI-954814; Score: 0.00
DE  Interaction: Q15038; IntAct: EBI-954822; Score: 0.00
DE  Interaction: Q86UW9; IntAct: EBI-954830; Score: 0.00
DE  Interaction: P05305; IntAct: EBI-954838; Score: 0.00
DE  Interaction: Q9UKW6; IntAct: EBI-954846; Score: 0.00
DE  Interaction: Q14512; IntAct: EBI-954854; Score: 0.00
DE  Interaction: P26885; IntAct: EBI-946297; Score: 0.51
DE  Interaction: Q7L4I2; IntAct: EBI-954870; Score: 0.00
DE  Interaction: Q53HC5; IntAct: EBI-954878; Score: 0.00
DE  Interaction: Q9H6E4; IntAct: EBI-954886; Score: 0.00
DE  Interaction: Q96DN0; IntAct: EBI-954894; Score: 0.00
DE  Interaction: Q8N5R6; IntAct: EBI-954902; Score: 0.00
DE  Interaction: O75084; IntAct: EBI-954910; Score: 0.00
DE  Interaction: O14764; IntAct: EBI-954918; Score: 0.00
DE  Interaction: Q96SL4; IntAct: EBI-954926; Score: 0.00
DE  Interaction: Q96D42; IntAct: EBI-954934; Score: 0.00
DE  Interaction: P52789; IntAct: EBI-954942; Score: 0.00
DE  Interaction: P24592; IntAct: EBI-954958; Score: 0.00
DE  Interaction: P01871; IntAct: EBI-954966; Score: 0.00
DE  Interaction: Q9P2K6; IntAct: EBI-954974; Score: 0.00
DE  Interaction: Q6GPH6; IntAct: EBI-954982; Score: 0.00
DE  Interaction: Q96DA0; IntAct: EBI-954990; Score: 0.00
DE  Interaction: P21741; IntAct: EBI-954998; Score: 0.00
DE  Interaction: P55198; IntAct: EBI-946304; Score: 0.51
DE  Interaction: Q13232; IntAct: EBI-955014; Score: 0.00
DE  Interaction: O15259; IntAct: EBI-955022; Score: 0.00
DE  Interaction: P01160; IntAct: EBI-955030; Score: 0.00
DE  Interaction: Q9UHQ9; IntAct: EBI-955038; Score: 0.00
DE  Interaction: Q9UBU9; IntAct: EBI-955046; Score: 0.00
DE  Interaction: Q14554; IntAct: EBI-955054; Score: 0.00
DE  Interaction: Q9NR12; IntAct: EBI-946311; Score: 0.51
DE  Interaction: Q9HAT8; IntAct: EBI-955070; Score: 0.00
DE  Interaction: Q13526; IntAct: EBI-955078; Score: 0.00
DE  Interaction: Q9NP55; IntAct: EBI-955086; Score: 0.00
DE  Interaction: P23284; IntAct: EBI-955094; Score: 0.00
DE  Interaction: P45877; IntAct: EBI-955102; Score: 0.00
DE  Interaction: P10124; IntAct: EBI-955110; Score: 0.00
DE  Interaction: Q13876; IntAct: EBI-955118; Score: 0.00
DE  Interaction: Q9Y5P3; IntAct: EBI-955126; Score: 0.00
DE  Interaction: Q9NPQ8; IntAct: EBI-955134; Score: 0.00
DE  Interaction: Q15287; IntAct: EBI-955142; Score: 0.00
DE  Interaction: P04843; IntAct: EBI-955150; Score: 0.00
DE  Interaction: Q96GD3; IntAct: EBI-955158; Score: 0.00
DE  Interaction: P04279; IntAct: EBI-955166; Score: 0.00
DE  Interaction: P05121; IntAct: EBI-955174; Score: 0.00
DE  Interaction: O75830; IntAct: EBI-955182; Score: 0.00
DE  Interaction: Q96C03; IntAct: EBI-955198; Score: 0.00
DE  Interaction: O43278; IntAct: EBI-955206; Score: 0.00
DE  Interaction: P10451; IntAct: EBI-955214; Score: 0.00
DE  Interaction: P48723; IntAct: EBI-955222; Score: 0.00
DE  Interaction: P04155; IntAct: EBI-955230; Score: 0.00
DE  Interaction: Q969W9; IntAct: EBI-955238; Score: 0.00
DE  Interaction: Q13049; IntAct: EBI-946318; Score: 0.51
DE  Interaction: Q96IX5; IntAct: EBI-955254; Score: 0.00
DE  Interaction: P01282; IntAct: EBI-955262; Score: 0.00
DE  Interaction: O60844; IntAct: EBI-955270; Score: 0.00
DE  Interaction: O95201; IntAct: EBI-946325; Score: 0.51
DE  Interaction: Q16630; IntAct: EBI-956230; Score: 0.00
DE  Interaction: Q9UBP4; IntAct: EBI-956246; Score: 0.00
DE  Interaction: O95967; IntAct: EBI-956262; Score: 0.00
DE  Interaction: Q5VSY0; IntAct: EBI-956270; Score: 0.00
DE  Interaction: P78356; IntAct: EBI-956286; Score: 0.00
DE  Interaction: Q99932; IntAct: EBI-956310; Score: 0.00
DE  Interaction: O75886; IntAct: EBI-956318; Score: 0.00
DE  Interaction: Q9UMX0; IntAct: EBI-6862638; Score: 0.72
DE  Interaction: Q9GZY6; IntAct: EBI-956342; Score: 0.00
DE  Interaction: Q6GMX4; IntAct: EBI-956838; Score: 0.00
DE  Interaction: Q6P1W5; IntAct: EBI-956886; Score: 0.00
DE  Interaction: A9UHW6; IntAct: EBI-950091; Score: 0.00
DE  Interaction: Q9BZ11; IntAct: EBI-950098; Score: 0.00
DE  Interaction: P56559; IntAct: EBI-950104; Score: 0.00
DE  Interaction: Q9UII2; IntAct: EBI-950110; Score: 0.00
DE  Interaction: Q8N111; IntAct: EBI-950122; Score: 0.00
DE  Interaction: P30040; IntAct: EBI-950128; Score: 0.00
DE  Interaction: O43497; IntAct: EBI-950134; Score: 0.00
DE  Interaction: Q49A88; IntAct: EBI-950140; Score: 0.00
DE  Interaction: P53618; IntAct: EBI-950146; Score: 0.00
DE  Interaction: Q9P021; IntAct: EBI-950152; Score: 0.00
DE  Interaction: Q9UM22; IntAct: EBI-950170; Score: 0.00
DE  Interaction: Q8NEM7; IntAct: EBI-950182; Score: 0.00
DE  Interaction: P31150; IntAct: EBI-950194; Score: 0.00
DE  Interaction: O14964; IntAct: EBI-950206; Score: 0.00
DE  Interaction: Q16891; IntAct: EBI-950218; Score: 0.00
DE  Interaction: Q6ZTN6; IntAct: EBI-950224; Score: 0.00
DE  Interaction: Q8WV48; IntAct: EBI-950236; Score: 0.00
DE  Interaction: Q9H6J7; IntAct: EBI-950242; Score: 0.00
DE  Interaction: Q96BY2; IntAct: EBI-950248; Score: 0.00
DE  Interaction: Q96JN2; IntAct: EBI-950254; Score: 0.00
DE  Interaction: Q15155; IntAct: EBI-950266; Score: 0.00
DE  Interaction: P69849; IntAct: EBI-950272; Score: 0.00
DE  Interaction: Q7Z3S9; IntAct: EBI-950278; Score: 0.00
DE  Interaction: P04181; IntAct: EBI-950284; Score: 0.00
DE  Interaction: Q96AQ6; IntAct: EBI-950290; Score: 0.00
DE  Interaction: O14917; IntAct: EBI-950296; Score: 0.00
DE  Interaction: O95206; IntAct: EBI-950302; Score: 0.00
DE  Interaction: Q8ND90; IntAct: EBI-950314; Score: 0.00
DE  Interaction: Q16849; IntAct: EBI-950332; Score: 0.00
DE  Interaction: Q92932; IntAct: EBI-950338; Score: 0.00
DE  Interaction: P98175; IntAct: EBI-950350; Score: 0.00
DE  Interaction: Q9HCK4; IntAct: EBI-950356; Score: 0.00
DE  Interaction: P13521; IntAct: EBI-950362; Score: 0.00
DE  Interaction: Q01130; IntAct: EBI-950368; Score: 0.00
DE  Interaction: Q9H7N4; IntAct: EBI-950380; Score: 0.00
DE  Interaction: P16949; IntAct: EBI-950386; Score: 0.00
DE  Interaction: O43294; IntAct: EBI-950392; Score: 0.00
DE  Interaction: Q9UPQ9; IntAct: EBI-950398; Score: 0.00
DE  Interaction: Q12933; IntAct: EBI-950404; Score: 0.00
DE  Interaction: Q92519; IntAct: EBI-950410; Score: 0.00
DE  Interaction: Q9UHD9; IntAct: EBI-950422; Score: 0.00
DE  Interaction: P10746; IntAct: EBI-950428; Score: 0.00
DE  Interaction: Q9BTA9; IntAct: EBI-950434; Score: 0.00
DE  Interaction: P27348; IntAct: EBI-950440; Score: 0.00
DE  Interaction: Q9NYG2; IntAct: EBI-950446; Score: 0.00
DE  Interaction: Q8WW38; IntAct: EBI-950452; Score: 0.00
DE  Interaction: P54725; IntAct: EBI-950464; Score: 0.00
DE  Interaction: P12268; IntAct: EBI-950476; Score: 0.00
DE  Interaction: P84022; IntAct: EBI-3939572; Score: 0.37
DE  Interaction: O43913; IntAct: EBI-3939792; Score: 0.37
DE  Interaction: Q9UBS4; IntAct: EBI-7141684; Score: 0.37
DE  Interaction: Q92956; IntAct: EBI-7403789; Score: 0.37
DE  Interaction: Q9H492; IntAct: EBI-6879063; Score: 0.57
DE  Interaction: Q5VZL5; IntAct: EBI-8836977; Score: 0.35
DE  Interaction: Q9WMX2; IntAct: EBI-9081813; Score: 0.37
DE  Interaction: Q13404; IntAct: EBI-9971170; Score: 0.00
DE  Interaction: Q62925; IntAct: EBI-9972789; Score: 0.00
DE  Interaction: P60896; IntAct: EBI-9827158; Score: 0.35
DE  Interaction: P08050; IntAct: EBI-10763549; Score: 0.40
DE  Interaction: P83917; IntAct: EBI-11012671; Score: 0.35
DE  Interaction: P11021; IntAct: EBI-11151540; Score: 0.35
DE  Interaction: P49286; IntAct: EBI-11577398; Score: 0.00
DE  Interaction: O00624; IntAct: EBI-21654627; Score: 0.35
DE  Interaction: P24390; IntAct: EBI-21655097; Score: 0.35
DE  Interaction: P10636; IntAct: EBI-20798291; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: Q15884; IntAct: EBI-27118933; Score: 0.37
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
GO  GO:0005776;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0090734;
GO  GO:0042802;
GO  GO:0036435;
GO  GO:0031593;
GO  GO:0006914;
GO  GO:0006974;
GO  GO:0006281;
GO  GO:1901097;
GO  GO:2000042;
GO  GO:0032434;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEPSGAETRPPIRVTVKTPKDKEEIVICDRASVKEFKEEISRRFKAQQDQLVLIFAGKILKDGDTLNQHGIKDGLTVHL
SQ  VIKTPQKAQDPAAATASSPSTPDPASAPSTTPASPATPAQPSTSGSASSDAGSGSRRSSGGGPSPGAGEGSPSATASILS
SQ  GFGGILGLGSLGLGSANFMELQQQMQRQLMSNPEMLSQIMENPLVQDMMSNPDLMRHMIMANPQMQQLMERNPEISHMLN
SQ  NPELMRQTMELARNPAMMQEMMRNQDRALSNLESIPGGYNALRRMYTDIQEPMFSAAREQFGNNPFSSLAGNSDSSSSQP
SQ  LRTENREPLPNPWSPSPPTSQAPGSGGEGTGGSGTSQVHPTVSNPFGINAASLGSGMFNSPEMQALLQQISENPQLMQNV
SQ  ISAPYMRSMMQTLAQNPDFAAQMMVNVPLFAGNPQLQEQLRLQLPVFLQQMQNPESLSILTNPRAMQALLQIQQGLQTLQ
SQ  TEAPGLVPSLGSFGISRTPAPSAGSNAGSTPEAPTSSPATPATSSPTGASSAQQQLMQQMIQLLAGSGNSQVQTPEVRFQ
SQ  QQLEQLNSMGFINREANLQALIATGGDINAAIERLLGSQLS
//
ID  Q99NB8;
PN  Ubiquilin-4;
GN  Ubqln4;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:11162551}. Cytoplasm {ECO:0000250|UniProtKB:Q9NRR5}. Chromosome {ECO:0000250|UniProtKB:Q9NRR5}. Endoplasmic reticulum {ECO:0000269|PubMed:11162551, ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:20940304}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18079109}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9NRR5}. Note=Colocalizes with the proteasome, both in nucleus and cytoplasm. Exported from the nucleus following interaction with DESI1/POST. In response to DNA damage and phosphorylation at Ser-318 by ATM, localizes to the nucleus and is recruited to sites of DNA damage. {ECO:0000250|UniProtKB:Q9NRR5}.
DR  UNIPROT: Q99NB8;
DR  UNIPROT: Q8BP88;
DR  PDB: 2KNZ;
DR  Pfam: PF00627;
DR  Pfam: PF00240;
DR  PROSITE: PS50030;
DR  PROSITE: PS50053;
DE  Function: Regulator of protein degradation that mediates the proteasomal targeting of misfolded, mislocalized or accumulated proteins (By similarity). Acts by binding polyubiquitin chains of target proteins via its UBA domain and by interacting with subunits of the proteasome via its ubiquitin-like domain (By similarity). Key regulator of DNA repair that represses homologous recombination repair: in response to DNA damage, recruited to sites of DNA damage following phosphorylation by ATM and acts by binding and removing ubiquitinated MRE11 from damaged chromatin, leading to MRE11 degradation by the proteasome (By similarity). MRE11 degradation prevents homologous recombination repair, redirecting double-strand break repair toward non-homologous end joining (NHEJ) (By similarity). Specifically recognizes and binds mislocalized transmembrane-containing proteins and targets them to proteasomal degradation (By similarity). Collaborates with DESI1/POST in the export of ubiquitinated proteins from the nucleus to the cytoplasm (By similarity). Plays a role in the regulation of the proteasomal degradation of non-ubiquitinated GJA1 (PubMed:18079109, PubMed:20940304). Acts as an adapter protein that recruits UBQLN1 to the autophagy machinery (By similarity). Mediates the association of UBQLN1 with autophagosomes and the autophagy-related protein LC3 (MAP1LC3A/B/C) and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (By similarity). {ECO:0000250|UniProtKB:Q9NRR5, ECO:0000269|PubMed:18079109, ECO:0000269|PubMed:20940304}.
DE  Reference Proteome: Yes;
DE  Interaction: P0CG53; IntAct: EBI-5333020; Score: 0.44
DE  Interaction: P08050; IntAct: EBI-5333079; Score: 0.44
DE  Interaction: Q3UNW5; IntAct: EBI-5735888; Score: 0.35
GO  GO:0005776;
GO  GO:0005737;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0031597;
GO  GO:0005789;
GO  GO:0031595;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0090734;
GO  GO:0042802;
GO  GO:0036435;
GO  GO:0031593;
GO  GO:0006914;
GO  GO:0006974;
GO  GO:0006281;
GO  GO:1901097;
GO  GO:2000042;
GO  GO:0032434;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEPSGAETRPQIRVTVKTPKDKEEIVICDQASVKEFKEEISRRFKAQQDQLVLIFAGKILKDGDTLSQHGIKDGLTVHL
SQ  VIKTPQKAQDPVTAAASPPSTPDSASAPSTTPASPAAAPVQPCSSGNTTSDAGSGGGPSPVAAEGPSSATASILSGFGGI
SQ  LGLGSLGLGSANFMELQQQMQRQLMSNPEMLSQIMENPLVQDMMSNPDLMRHMIMANPQMQQLMERNPEISHMLNNPELM
SQ  RQTMELARNPAMMQEMMRNQDRALSNLESVPGGYNALRRMYTDIQEPMFTAAREQFGNNPFSSLAGNSDNSSSQPLRTEN
SQ  REPLPNPWSPSPPTSQAPGSGGEGTGGSGTSQVHPTVSNPFGINAASLGSGMFNSPEMQALLQQISENPQLMQNVISAPY
SQ  MRTMMQTLAQNPDFAAQMMVNVPLFAGNPQLQEQLRLQLPVFLQQMQNPESLSILTNPRAMQALLQIQQGLQTLQTEAPG
SQ  LVPSLGSFGTPRTSVPLAGSNSGSSAEAPTSSPGVPATSPPSAGSNAQQQLMQQMIQLLSGSGNSQVPMPEVRFQQQLEQ
SQ  LNSMGFINREANLQALIATGGDINAAIERLLGSQLS
//
ID  Q9TXH9;
PN  UBX domain-containing protein 1;
GN  ubxn;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550}. Note=Colocalizes with cdc-48.1 to the perinuclear region in spermatocytes. {ECO:0000269|PubMed:20977550}.
DR  UNIPROT: Q9TXH9;
DR  Pfam: PF00789;
DR  PROSITE: PS50033;
DR  PROSITE: PS00028;
DE  Function: Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity (PubMed:20977550). Together with ubxn-2 and ubxn-3, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1. {ECO:0000269|PubMed:20977550}.
DE  Reference Proteome: Yes;
DE  Interaction: P54811; IntAct: EBI-2412436; Score: 0.62
DE  Interaction: P34327; IntAct: EBI-336329; Score: 0.00
DE  Interaction: Q18157; IntAct: EBI-336332; Score: 0.00
DE  Interaction: Q18426; IntAct: EBI-336335; Score: 0.00
DE  Interaction: Q18938; IntAct: EBI-336341; Score: 0.00
DE  Interaction: O45521; IntAct: EBI-336344; Score: 0.00
DE  Interaction: P54812; IntAct: EBI-336338; Score: 0.00
DE  Interaction: Q9XUT0; IntAct: EBI-336347; Score: 0.00
DE  Interaction: P45972; IntAct: EBI-336350; Score: 0.00
DE  Interaction: Q23182; IntAct: EBI-336353; Score: 0.00
DE  Interaction: Q7YTU4; IntAct: EBI-336356; Score: 0.00
DE  Interaction: Q19019; IntAct: EBI-339494; Score: 0.00
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0036435;
GO  GO:0030154;
GO  GO:0042006;
GO  GO:0032435;
GO  GO:1903094;
GO  GO:0031397;
GO  GO:0045732;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSIAQQLMDMGFPADKAEAAAGNNRNLDQALDWIEKDGAGVPMETDAPAQAAPGAADSGAPPVAASFKCDDCGKLLANDD
SQ  AIMFHASKTKHENFSESSEAIKPLTAEEKAAKVLEIREKIKVHQAKKAKLEAEENREKEKKRREDGKAMISHKEAARDRE
SQ  IREAAQDRRREKNEDEIARKRVLEQIRLDKEARKAKASGQPVPEAKPAPSAAPVAPPKDYSTTTLQFRLLDGQTVRQQFE
SQ  ANEPLAMVRAWVETNHANGVPFTLMTPFPRKVFTEDDMGTPLKVLNLVPSANVILNRAA
//
ID  Q9N2W5;
PN  UBX domain-containing protein 2;
GN  ubxn;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550}. Nucleus {ECO:0000269|PubMed:23649807}. Cytoplasm {ECO:0000269|PubMed:23649807}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23649807}. Note=Colocalizes with cdc-48.1 to the perinuclear region in spermatocytes (PubMed:20977550). Nuclear localization is cdc-48-dependent (PubMed:23649807). During embryonic mitotic metaphase, telophase and to a certain extent prophase, localizes to centrosomes (PubMed:23649807). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:23649807}.
DR  UNIPROT: Q9N2W5;
DR  UNIPROT: Q86DD7;
DR  Pfam: PF08059;
DR  Pfam: PF00789;
DR  PROSITE: PS51399;
DR  PROSITE: PS50033;
DE  Function: Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity (PubMed:20977550). Together with ubxn-2 and ubxn-3, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1 (PubMed:20977550). Probably in association with ATPase cdc-48.1 or/and cdc-48.2, regulates the centrosomal levels of kinase air-1 levels during mitotic progression by promoting air-1 removal from centrosomes in prophase (PubMed:23649807). Also, regulates spindle orientation in the one-cell embryo by controlling centration and rotation of the pronuclei-centrosome complex in prophase (PubMed:23649807). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:23649807}.
DE  Reference Proteome: Yes;
DE  Interaction: O44739; IntAct: EBI-338285; Score: 0.00
DE  Interaction: P54812; IntAct: EBI-2414708; Score: 0.49
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0031616;
GO  GO:0036435;
GO  GO:0019901;
GO  GO:0043130;
GO  GO:0000045;
GO  GO:0030154;
GO  GO:0000132;
GO  GO:0007030;
GO  GO:0042006;
GO  GO:0061025;
GO  GO:1904780;
GO  GO:0031468;
GO  GO:0045732;
GO  GO:0043161;
GO  GO:0007283;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRNIRTFRDIGNNDDGGPDSDDSGADAAERGAPQEFYAGSGQAVQGPRGAAARGPDSEAHIRRILQAAEVVQPEGGEAP
SQ  RGRPSGRETISLTLHLWSDGLSIEDGPLMSRQDPRTIEFLESVGKGEIPPSLVQQYPGKEIDFKVNRHHEEYVAPKMKPF
SQ  GGSGVRLGNVVPTVLGQSSSSATTAGTSSATTDHNPDHTAENEAKQLEDAKKELSTNMNEPTTNIQIRLPNNQRLVGIFN
SQ  HSHTLEAVRTFICTARPDMIYAPFQMMAAYPPKPFEDESQTLKDANVLNSVVAVKILPTTN
//
ID  H2L056;
PN  UBX domain-containing protein 3;
GN  ubxn;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:26842564}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550}. Chromosome {ECO:0000269|PubMed:26842564}. Cytoplasm {ECO:0000269|PubMed:26842564}. Note=Colocalizes with cdc-48.1 to the perinuclear region in spermatocytes (PubMed:20977550). Localizes to the nucleus during S phase in a cdc-48 and npl-4-dependent manner (PubMed:26842564). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:26842564}.
DR  UNIPROT: H2L056;
DR  UNIPROT: A0A0K3ARL0;
DR  UNIPROT: A0A0K3ATZ0;
DR  UNIPROT: A0A0K3AWX1;
DR  UNIPROT: Q6A589;
DR  PROSITE: PS50033;
DE  Function: Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity (PubMed:20977550, PubMed:26842564, PubMed:28368371). Together with ubxn-1 and ubxn-2, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1 (PubMed:20977550). During mitosis, ensures the degradation of DNA licensing factor cdt-1 and the disassembly of the DNA replication CMG helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5 (PubMed:26842564, PubMed:28368371). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:26842564, ECO:0000269|PubMed:28368371}.
DE  Reference Proteome: Yes;
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0036435;
GO  GO:0044877;
GO  GO:0043130;
GO  GO:0030154;
GO  GO:0042006;
GO  GO:0045977;
GO  GO:0045732;
GO  GO:1905634;
GO  GO:0007283;
GO  GO:0030433;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLTASLEDDQREKLRQYTEFTHQQDYEVAIGTLASLNWNLEQAIEAHLMQEDKNDDEDPEILETIPAAASGRNAGASSS
SQ  SRFEPEVINIEDDEMPATRGRRRGRAVTPDETTTVDNQVKRLRIDDGSSSSSNGAATHHRGAAIPRQKRGQATEPTPSSS
SQ  GSSSASFSSRRGTRANPVPPPNQEPAHPESARQNGGILASRHNNHNNQQNNHHHHHQRIPINPRRVDVFNVDSDEDDDSM
SQ  AIAYEDDDDGVHEVHHSEVVARGSGPPNGRIPMIPDGFSSVSDALRNFVAIFSDRFCSTPQTQAFMPPFYTEPLPAAVKE
SQ  AFDHPNSEHRRPLLFYINHDRSIAANIFASQVLCSETVSTLIRHQYVLFPWDITSDSNLMLFLEYLQAANMGDVRTIIQR
SQ  LAMSKIESFPLMAIVVKERNSYRLVDYCRGTDTSDQVMEKLLSGVSEYSDIRMNEQSERREREEREAIRNQQEAEYKASL
SQ  AADKARMEAKQQEIEEQRLEEERKLREEEEECVRRQTVASTVPEEPPASAPLAEIINVKFRLPEGGQDMRRFRRLESIQT
SQ  LINYLSSKGYSPDKFKYFNSDFPKKEITRHFDLSHNFADTKWPAREQIFVEEI
//
ID  Q3ZBU9;
PN  UBX domain-containing protein 4;
GN  UBXN4;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92575}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92575}. Nucleus envelope {ECO:0000250|UniProtKB:Q92575}. Note=Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER. {ECO:0000250|UniProtKB:Q92575}.
DR  UNIPROT: Q3ZBU9;
DR  Pfam: PF00789;
DR  PROSITE: PS50033;
DE  Function: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD. {ECO:0000250|UniProtKB:Q92575}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005635;
GO  GO:0006986;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q92575};
SQ  MLWFQGAIPAAIASAKRSGAVFVVFVAGDDEQSTQMAASWEDEKVTEASSNSFVAIKIDTRSEACLQFSQIYPVVCVPSS
SQ  FFIGDSGIPLEVIAGSISADELVTRIHKVRQMHSLKGEASLANGSQSEGSVSTPSASFEHNNTSENCQSRNVELCETPST
SQ  SDTKSDSATGGESSGQTTVSQEPSGCSNQRPTEDLTVRVERLTKKLEERREEKRKEEEQREIKKEIERRKTGKEMLDYKR
SQ  KQEEELTKRMLEERNREKAEDRAARERIKQQIALDRAERAARFAKTKEEVEAAKAAALLAKQAEMEIKRETSTKERSTVA
SQ  RIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTKEDYKKKLLDLELAPSASVVLLPAGRPT
SQ  TSMVHSSSGDFWTLLGTVLYPFLAIWRLISNFLFSNPPPAQTSVRAASLETSNLASSSNSEKREPVRKRVLEKRGEDFKK
SQ  EGKIYRLRTQDDGEDENNTWNGNSTQQM
//
ID  Q92575;
PN  UBX domain-containing protein 4;
GN  UBXN4;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16968747}; Peripheral membrane protein {ECO:0000269|PubMed:16968747}. Nucleus envelope {ECO:0000269|PubMed:16968747}. Note=Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER. {ECO:0000269|PubMed:16968747}.
DR  UNIPROT: Q92575;
DR  UNIPROT: A8K9W4;
DR  UNIPROT: Q4ZG56;
DR  UNIPROT: Q8IYM5;
DR  PDB: 2KXJ;
DR  Pfam: PF00789;
DR  PROSITE: PS50033;
DR  OMIM: 611216;
DR  DisGeNET: 23190;
DE  Function: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD (PubMed:19822669). {ECO:0000269|PubMed:16968747, ECO:0000269|PubMed:19822669}.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: O75674; IntAct: EBI-736145; Score: 0.00
DE  Interaction: P55072; IntAct: EBI-1996648; Score: 0.67
DE  Interaction: P17028; IntAct: EBI-2682714; Score: 0.00
DE  Interaction: Q5NEU6; IntAct: EBI-2799980; Score: 0.00
DE  Interaction: Q5NIJ3; IntAct: EBI-2799973; Score: 0.00
DE  Interaction: Q9UMX0; IntAct: EBI-10278693; Score: 0.72
DE  Interaction: Q5HYA8; IntAct: EBI-11367583; Score: 0.27
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11372136; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: P63211; IntAct: EBI-24802515; Score: 0.56
DE  Interaction: P21802; IntAct: EBI-21718282; Score: 0.35
DE  Interaction: Q9H165; IntAct: EBI-21885450; Score: 0.35
DE  Interaction: Q96RL7; IntAct: EBI-21885450; Score: 0.35
DE  Interaction: Q92551; IntAct: EBI-21885450; Score: 0.35
DE  Interaction: Q709C8; IntAct: EBI-21885450; Score: 0.35
DE  Interaction: Q6V1X1; IntAct: EBI-21885450; Score: 0.35
DE  Interaction: Q14139; IntAct: EBI-25771321; Score: 0.50
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: O14880; IntAct: EBI-16796348; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: Q15388; IntAct: EBI-16801791; Score: 0.27
DE  Interaction: Q9NS69; IntAct: EBI-16802054; Score: 0.27
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9GZP9; IntAct: EBI-25770670; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: P56180; IntAct: EBI-27116883; Score: 0.27
DE  Interaction: Q9H492; IntAct: EBI-30829630; Score: 0.44
DE  Interaction: Q9GZQ8; IntAct: EBI-30831343; Score: 0.44
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: Q5W0V3; IntAct: EBI-34574999; Score: 0.27
DE  Interaction: Q86V87; IntAct: EBI-34575191; Score: 0.27
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005635;
GO  GO:0006986;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16968747};
SQ  MLWFQGAIPAAIATAKRSGAVFVVFVAGDDEQSTQMAASWEDDKVTEASSNSFVAIKIDTKSEACLQFSQIYPVVCVPSS
SQ  FFIGDSGIPLEVIAGSVSADELVTRIHKVRQMHLLKSETSVANGSQSESSVSTPSASFEPNNTCENSQSRNAELCEIPPT
SQ  SDTKSDTATGGESAGHATSSQEPSGCSDQRPAEDLNIRVERLTKKLEERREEKRKEEEQREIKKEIERRKTGKEMLDYKR
SQ  KQEEELTKRMLEERNREKAEDRAARERIKQQIALDRAERAARFAKTKEEVEAAKAAALLAKQAEMEVKRESYARERSTVA
SQ  RIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTKEDYKKKLLDLELAPSASVVLLPAGRPT
SQ  ASIVHSSSGDIWTLLGTVLYPFLAIWRLISNFLFSNPPPTQTSVRVTSSEPPNPASSSKSEKREPVRKRVLEKRGDDFKK
SQ  EGKIYRLRTQDDGEDENNTWNGNSTQQM
//
ID  Q8VCH8;
PN  UBX domain-containing protein 4;
GN  Ubxn4;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92575}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92575}. Nucleus envelope {ECO:0000250|UniProtKB:Q92575}. Note=Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER. {ECO:0000250|UniProtKB:Q92575}.
DR  UNIPROT: Q8VCH8;
DR  UNIPROT: Q3UGR4;
DR  UNIPROT: Q8BW17;
DR  PDB: 2DZK;
DR  Pfam: PF00789;
DR  PROSITE: PS50033;
DE  Function: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD. {ECO:0000250|UniProtKB:Q92575}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005635;
GO  GO:0006986;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q92575};
SQ  MLWFQGAIPAAIASAKRSGAVFVVFVAGDDEQSIQMAASWEDEKVTQASSNNFVAIKIDTKSEACLQFSQIYPVVCVPSS
SQ  FFIGDSGIPLEVIAGSVSADELVTRIHKVQQMHSSKGEASVTNDNQSESSVSTPSASFEPDVCENPESKNTELCETPATS
SQ  DIKSDTATGGECTGHDSHSQEPHGCSNQRPAEDLTVRVERLTKKLEERREEKRKEEAQREIKKEIERRKTGKEMLDYKRK
SQ  QEEELTKRMLEERSREKAEDRAARERIKQQIALDRAERAARFAKTKEAEAAKAAALLTKQAGTEVKRESTARDRSTIARI
SQ  QFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTREDYKRRLLDLELAPSASVVLLPAGRPATS
SQ  IVHSSSGDIWTLLGTVLYPFLAIWRLISNFLFSNPPPAQTSARATSTEPSNSASSSKSEKREPVRKRMLEKRGEDFKKEG
SQ  KIYRLRTQDDGEDENNTWNGNSTQQM
//
ID  Q5R4I3;
PN  UBX domain-containing protein 4;
GN  UBXN4;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92575}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92575}. Nucleus envelope {ECO:0000250|UniProtKB:Q92575}. Note=Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER. {ECO:0000250|UniProtKB:Q92575}.
DR  UNIPROT: Q5R4I3;
DR  Pfam: PF00789;
DR  PROSITE: PS50033;
DE  Function: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD. {ECO:0000250|UniProtKB:Q92575}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005789;
GO  GO:0005635;
GO  GO:0006986;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q92575};
SQ  MLWFQGAIPAAIATAKRSGAVFVVFVAGDDEQSTQMAASWEDDKVTEASSNSFVAIKIDTKSEACLQFSQIYPVVCVPSS
SQ  FFIGDSGIPLEVIAGSVSADELVTRIHKVRQMHLLKSETSVANGSQSESSVSTPSASFEPNNTCENSQSRNAELCEIPPT
SQ  SDTKSDTATGGESAGHATSSQEPSGCSDQRPAEDLNIRVERLTKKLEERREEKRKEEEQREIKKEIERRKTGKEMLDYKR
SQ  KQEEELTKRMLEERNREKAEDRAARERIKQQIALDRAERAARFAKTKEEVEAAKAAALLAKQAEMEVKRESYARERSTVA
SQ  RIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTKEDYKKKLLDLELAPSASVVVLPAGRPT
SQ  ASIVHSSSGDIWTLLGTVLYPFLAIWRLISNFLFSNPPPTQTSVRVTSSEPPNPASSSKSEKREPVRKRVLEKRGDDFKK
SQ  EGKIYRLRTQDDGEDENNTWNGNSTQQM
//
ID  Q5HZY0;
PN  UBX domain-containing protein 4;
GN  Ubxn4;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92575}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92575}. Nucleus envelope {ECO:0000250|UniProtKB:Q92575}. Note=Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER. {ECO:0000250|UniProtKB:Q92575}.
DR  UNIPROT: Q5HZY0;
DR  Pfam: PF00789;
DR  PROSITE: PS50033;
DE  Function: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD. {ECO:0000250|UniProtKB:Q92575}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005635;
GO  GO:0006986;
GO  GO:0030433;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q92575};
SQ  MLWFQGAIPAAIASAKRSGAVFVVFVAGDDEQSTQMAASWEDEKVREASSDNFVAIKIDTKSEACLQFSQIYPVVCVPSS
SQ  FFIGDSGIPLEVIAGSVSADELVTRIHKVQQMHSLKGETSVTNDKQSESSVSTPSASFEPDICESAESRNTELCETPTTS
SQ  DPKSDTAAGGECAGHDSLSQEPPGCSNQRPAEDLTVRVERLTKKLEERREEKRKEEAQREIKKEIERRKTGKEMLDYKRK
SQ  QEEELTKRMLEERSREKAEDRAARERIKQQIALDRAERAARFAKTKEAEAAKAAALLAKQAEAEVKRESSTRDRSTIARI
SQ  QFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTREDYKRKLLDLELAPSASVVLLPAGRPATS
SQ  IVPSSSGDIWTLLGTVLYPFLAIWRLISNFLFSNPPPAQTSARATSTEPSNSASSSKSEKREPVRKRVLEKRGEDFKKEG
SQ  KIYRLRTQDDGEDENNTWNGNSTQQM
//
ID  P22309;
PN  UDP-glucuronosyltransferase 1A1;
GN  UGT1A1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17179145, ECO:0000269|PubMed:17187418}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17187418}.
DR  UNIPROT: P22309;
DR  UNIPROT: A6NJC3;
DR  UNIPROT: B8K286;
DR  Pfam: PF00201;
DR  PROSITE: PS00375;
DR  OMIM: 143500;
DR  OMIM: 191740;
DR  OMIM: 218800;
DR  OMIM: 237900;
DR  OMIM: 601816;
DR  OMIM: 606785;
DR  DisGeNET: 54658;
DE  Function: [Isoform 1]: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:12181437, PubMed:15472229, PubMed:18004206, PubMed:18004212, PubMed:18719240, PubMed:19830808, PubMed:23288867). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:12181437, PubMed:18004206, PubMed:18004212). Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol, estrone and estriol (PubMed:15472229, PubMed:18719240, PubMed:23288867). Involved in the glucuronidation of bilirubin, a degradation product occurring in the normal catabolic pathway that breaks down heme in vertebrates (PubMed:17187418, PubMed:18004206, PubMed:19830808). Also catalyzes the glucuronidation the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties (PubMed:18052087, PubMed:19545173). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, a drug which can inhibit the effect of angiotensin II (PubMed:18674515). Involved in the biotransformation of 7-ethyl-10- hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan (PubMed:12181437, PubMed:18004212, PubMed:20610558). {ECO:0000269|PubMed:12181437, ECO:0000269|PubMed:15472229, ECO:0000269|PubMed:17187418, ECO:0000269|PubMed:18004206, ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:18052087, ECO:0000269|PubMed:18674515, ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:19545173, ECO:0000269|PubMed:19830808, ECO:0000269|PubMed:20610558, ECO:0000269|PubMed:23288867}. [Isoform 2]: Lacks UGT glucuronidation activity but acts as a negative regulator of isoform 1. {ECO:0000269|PubMed:17187418, ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:20610558}.
DE  Disease: Gilbert syndrome (GILBS) [MIM:143500]: Occurs as a consequence of reduced bilirubin transferase activity and is often detected in young adults with vague non-specific complaints. {ECO:0000269|PubMed:11013440, ECO:0000269|PubMed:12139570, ECO:0000269|PubMed:17496722, ECO:0000269|PubMed:7715297, ECO:0000269|PubMed:9627603}. Note=The disease is caused by variants affecting the gene represented in this entry. Transient familial neonatal hyperbilirubinemia (HBLRTFN) [MIM:237900]: A condition characterized by excessive concentration of bilirubin in the blood, which may lead to jaundice. Breast milk jaundice is a common problem in nursing infants. {ECO:0000269|PubMed:11061796}. Note=The disease may be caused by variants affecting the gene represented in this entry. The defect has been ascribed to various breast milk substances, but the component or combination of components that is responsible remains unclear. Defects of UGT1A1 are an underlying cause of the prolonged unconjugated hyperbilirubinemia associated with breast milk. One or more components in the milk may trigger the jaundice in infants who have such mutations. Mutations are identical to those detected in patients with Gilbert syndrome, a risk factor of neonatal non-physiologic hyperbilirubinemia and a genetic factor in fasting hyperbilirubinemia. Crigler-Najjar syndrome 1 (CN1) [MIM:218800]: Patients have severe hyperbilirubinemia and usually die of kernicterus (bilirubin accumulation in the basal ganglia and brainstem nuclei) within the first year of life. CN1 inheritance is autosomal recessive. {ECO:0000269|PubMed:11013440, ECO:0000269|PubMed:15712364, ECO:0000269|PubMed:1634050, ECO:0000269|PubMed:17229650, ECO:0000269|PubMed:19830808, ECO:0000269|PubMed:23992562, ECO:0000269|PubMed:7906695, ECO:0000269|PubMed:7989045, ECO:0000269|PubMed:7989595, ECO:0000269|PubMed:8226884}. Note=The disease is caused by variants affecting the gene represented in this entry. Crigler-Najjar syndrome 2 (CN2) [MIM:606785]: Patients have less severe hyperbilirubinemia and usually survive into adulthood without neurologic damage. Phenobarbital, which induces the partially deficient glucuronyl transferase, can diminish the jaundice. CN2 inheritance is autosomal dominant. {ECO:0000269|PubMed:11013440, ECO:0000269|PubMed:11370628, ECO:0000269|PubMed:12402338, ECO:0000269|PubMed:14550264, ECO:0000269|PubMed:15712364, ECO:0000269|PubMed:17229650, ECO:0000269|PubMed:18004206, ECO:0000269|PubMed:19830808, ECO:0000269|PubMed:23099197, ECO:0000269|PubMed:23992562, ECO:0000269|PubMed:7989595, ECO:0000269|PubMed:8276413, ECO:0000269|PubMed:8280139, ECO:0000269|PubMed:8706880, ECO:0000269|PubMed:9621515, ECO:0000269|PubMed:9639672}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O60701; IntAct: EBI-3940296; Score: 0.37
DE  Interaction: Q9WMX2; IntAct: EBI-9083684; Score: 0.37
DE  Interaction: O60656; IntAct: EBI-9509041; Score: 0.40
DE  Interaction: Q9HAW9; IntAct: EBI-9508957; Score: 0.40
DE  Interaction: Q9HAW7; IntAct: EBI-9495170; Score: 0.40
DE  Interaction: P19224; IntAct: EBI-9492808; Score: 0.40
DE  Interaction: P35503; IntAct: EBI-9490919; Score: 0.40
DE  Interaction: P22310; IntAct: EBI-9489650; Score: 0.40
DE  Interaction: P22309; IntAct: EBI-9488227; Score: 0.40
DE  Interaction: Q9HAW8; IntAct: EBI-9490218; Score: 0.40
GO  GO:0070069;
GO  GO:0005783;
GO  GO:0034663;
GO  GO:0005789;
GO  GO:0005887;
GO  GO:0048471;
GO  GO:0019899;
GO  GO:0004857;
GO  GO:0015020;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0001972;
GO  GO:0005496;
GO  GO:0006953;
GO  GO:0031100;
GO  GO:0006789;
GO  GO:0070980;
GO  GO:0052695;
GO  GO:0071392;
GO  GO:0071361;
GO  GO:0071385;
GO  GO:0008210;
GO  GO:0051552;
GO  GO:0052696;
GO  GO:0046483;
GO  GO:0001889;
GO  GO:2001030;
GO  GO:0045922;
GO  GO:1904224;
GO  GO:0045939;
GO  GO:0032496;
GO  GO:0007584;
GO  GO:0042594;
GO  GO:0042573;
GO  GO:0008202;
GO  GO:0052697;
GO  GO:0006805;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVLAPDASLYIRDGAFYTLKTYP
SQ  VPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDSAMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIV
SQ  AQYLSLPTVFFLHALPCSLEFEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
SQ  EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAM
SQ  AIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDN
SQ  AKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
SQ  LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
//
ID  Q9BY64;
PN  UDP-glucuronosyltransferase 2B28;
GN  UGT2B28;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11300766}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11300766}.
DR  UNIPROT: Q9BY64;
DR  UNIPROT: B5BUM0;
DR  UNIPROT: Q9BY62;
DR  UNIPROT: Q9BY63;
DR  Pfam: PF00201;
DR  PROSITE: PS00375;
DR  OMIM: 606497;
DR  DisGeNET: 54490;
DE  Function: [Isoform 1]: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:11300766). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:11300766). Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (androsterone, 3alpha-androstanediol) and estrogens (estradiol, estrone) (PubMed:11300766). Catalyzes the glucuronidation of bile acid substrates, which are natural detergents for dietary lipids absorption (PubMed:11300766). Displays glucuronidation activity toward the phenolic compounds eugenol (PubMed:11300766). {ECO:0000269|PubMed:11300766}. [Isoform 2]: Lack UDP-glucuronosyltransferase (UGT) activity. {ECO:0000269|PubMed:11300766}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005640;
GO  GO:0048471;
GO  GO:0015020;
GO  GO:0052695;
GO  GO:0008210;
GO  GO:0008202;
GO  GO:0052697;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALKWTSVLLLIHLGCYFSSGSCGKVLVWTGEYSHWMNMKTILKELVQRGHEVTVLASSASILFDPNDAFTLKLEVYPTS
SQ  LTKTEFENIIMQQVKRWSDIQKDSFWLYFSQEQEILWEFHDIFRNFCKDVVSNKKVMKKLQESRFDIIFADAFFPCGELL
SQ  AALLNIPFVYSLCFTPGYTIERHSGGLIFPPSYIPVVMSKLSDQMTFMERVKNMIYVLYFDFWFQMCDMKKWDQFYSEVL
SQ  GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNIDFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSVISNMTAER
SQ  ANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQNDLLGLPKTRAFITHGGANGIYEAIYHGIPMVGIPLFWDQP
SQ  DNIAHMKAKGAAVRLDFHTMSSTDLLNALKTVINDPSYKENVMKLSIIQHDQPVKPLHRAVFWIEFVMCHKGAKHLRVAA
SQ  RDLTWFQYHSLDVIGFLLACVATVIFVVTKFCLFCFWKFARKGKKGKRD
//
ID  Q61UA0;
PN  Ufm1-specific protease;
GN  odr;
OS  6238;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q94218}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q94218}. Cytoplasm {ECO:0000250|UniProtKB:Q94218}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q94218}. Note=Recruited to the endoplasmic reticulum upon interaction with odr-4. {ECO:0000250|UniProtKB:Q94218}.
DR  UNIPROT: Q61UA0;
DR  UNIPROT: A8WZT5;
DR  Pfam: PF07910;
DE  Function: Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ufm-1, a ubiquitin-like modifier protein bound to a number of target proteins. Required, with oct-4, for the localization of a subset of 7 transmembrane domain odorant receptors, including odr-10, to the cilia of olfactory neurons AWA and AWC. Operates in aggregation behavior, and responses to oxygen levels. {ECO:0000250|UniProtKB:Q94218, ECO:0000250|UniProtKB:Q9NUQ7}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0071567;
GO  GO:0050921;
GO  GO:0097499;
GO  GO:0006508;
GO  GO:0045471;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q94218};
SQ  MSGSQTVSVIGYTKMAPQSPPATVNELWFIDTQAMFQNYANLRSFSKSNSTETQTTIGGVVFGRKARKQVIHVFFAYAED
SQ  LTESNLQFLESSLSSDIELVGNVNIDGQSTLIGNGTFTLQLSSKMLENKNTSEFLDQNVIFNNDHISMEGASCVSKVGFE
SQ  WSLRAGREQEDVKSAAERLSMASFRFSYLNAEHELVIREHKPETAKQKYMDKFTKGALPYKDVIEFTAMQSLTRDTSNDT
SQ  EDQKLVPTVKVTKDNKHFTRLVTIGEVVFPAYFGDSSFDLYKRAREALNRRANNTMMVTVNGIRSGRGVTTTTSATYLPP
SQ  GWVSLLHLQLPSKWTENEKRNYRIRLHKLFNLPSSKPCLRLSQSLPLHSESVRLTNKKLIREPHLSISNYQPAGVVTAVK
SQ  GPYNYHHYMQDGIDDSGWGCAYRSFQTIWSWFILNGYTDKPVPSHRDIQQALVNIGDKEQKFVGSRQWIGSTEISYVLNE
SQ  LLKLECRFIATNSGAEVVERARELARHFETSGTPVMIGGNMLAHTILGVDFNEMTGETKFLILDPHYTGSEDIKTITSKG
SQ  WCAWKPASFWSADHFYNMVLAQPPTDSI
//
ID  Q94218;
PN  Ufm1-specific protease;
GN  odr;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23449979, ECO:0000269|PubMed:24603482}; Peripheral membrane protein {ECO:0000269|PubMed:24603482}. Cytoplasm {ECO:0000269|PubMed:24603482}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23449979}. Note=Recruited to the endoplasmic reticulum upon interaction with odr-4. {ECO:0000269|PubMed:24603482}.
DR  UNIPROT: Q94218;
DR  UNIPROT: Q86MF8;
DR  PDB: 5EJJ;
DR  PDB: 5XDA;
DR  Pfam: PF07910;
DE  Function: Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ufm-1, a ubiquitin-like modifier protein bound to a number of target proteins (PubMed:29251776, PubMed:24603482). Required, with oct-4, for the localization of a subset of 7 transmembrane domain odorant receptors, including odr-10, to the cilia of olfactory neurons AWA and AWC (PubMed:9590179). Operates in aggregation behavior, and responses to oxygen levels (PubMed:12410303). {ECO:0000269|PubMed:12410303, ECO:0000269|PubMed:24603482, ECO:0000269|PubMed:29251776, ECO:0000269|PubMed:9590179}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0071567;
GO  GO:0006935;
GO  GO:0050921;
GO  GO:0097499;
GO  GO:0006508;
GO  GO:0045471;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:24603482};
SQ  MTNSQTVSLIGPTQMAPQSTPPPPVNELWFIDAQAMFQNYANLRSFSKSNANEINTTIGGFVFGRKARKQVIHVLFAYAE
SQ  DLTESNRQFLESSLSADIELVGNLNIDGQSQILPGGQFTLQLTSRMLENRSISEFLDMNVMFNNEHVLMEGASCVSRVGY
SQ  EWSLRAGREQEDVKSAAERLSMASFRFTYLNAEHGLVIREQKPEAAQQKYLDKFSKGAVPYKDVIEFTAMQSLTRDTSND
SQ  TEDQKLVPTVKVTKDNKHFTRLVTIGEVVFPAFFGDSSLDLYKRSREAFNRRANNTMMVTVNGIRAGRGVTTTTSATYLP
SQ  PGWVSLLHLQLPTKWTDNEQRNYRIRLHKLFNLPSSKPVLRLSQALALHSESARLTNKKLIREPHLSITNYQPVGEITTV
SQ  NGPYNYHHYMQDGIDDSGWGCAYRSFQTIWSWFILNGYTDKPVPSHREIQQALVDIQDKQAKFVGSRQWIGSTEISFVLN
SQ  ELLKLECRFIATNSGAEVVERVRELARHFETSGTPVMIGGNMLAHTILGVDFNDTTGETKFLVLDPHYTGSEDIKTITSK
SQ  GWCAWKPASFWSKDHFYNMVLPQPPSDAI
//
ID  P39547;
PN  ULP1-interacting protein 3;
GN  UIP3;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:11056382}; Multi-pass membrane protein {ECO:0000269|PubMed:11056382}. Cell membrane {ECO:0000269|PubMed:11056382}; Multi-pass membrane protein {ECO:0000269|PubMed:11056382}.
DR  UNIPROT: P39547;
DR  UNIPROT: D6VPM9;
DR  Pfam: PF00674;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P38776; IntAct: EBI-7739562; Score: 0.37
DE  Interaction: P53918; IntAct: EBI-7740046; Score: 0.37
DE  Interaction: Q02795; IntAct: EBI-7741000; Score: 0.37
DE  Interaction: P38286; IntAct: EBI-7741632; Score: 0.37
DE  Interaction: P25596; IntAct: EBI-7741701; Score: 0.37
DE  Interaction: P53337; IntAct: EBI-7742186; Score: 0.55
DE  Interaction: P38428; IntAct: EBI-7742324; Score: 0.37
DE  Interaction: P40548; IntAct: EBI-7744731; Score: 0.37
DE  Interaction: Q08193; IntAct: EBI-7744784; Score: 0.37
DE  Interaction: P39548; IntAct: EBI-7746332; Score: 0.55
DE  Interaction: P32334; IntAct: EBI-7747956; Score: 0.37
DE  Interaction: P40310; IntAct: EBI-7749162; Score: 0.37
DE  Interaction: P38988; IntAct: EBI-7750998; Score: 0.37
DE  Interaction: P40578; IntAct: EBI-7751034; Score: 0.37
DE  Interaction: P54862; IntAct: EBI-7751087; Score: 0.37
DE  Interaction: Q01163; IntAct: EBI-7752673; Score: 0.37
DE  Interaction: Q03697; IntAct: EBI-7752813; Score: 0.37
DE  Interaction: P32622; IntAct: EBI-7753570; Score: 0.37
DE  Interaction: P00425; IntAct: EBI-7753623; Score: 0.37
DE  Interaction: P21825; IntAct: EBI-7753639; Score: 0.37
DE  Interaction: P41543; IntAct: EBI-7754590; Score: 0.37
DE  Interaction: P31382; IntAct: EBI-7755792; Score: 0.37
DE  Interaction: P22804; IntAct: EBI-7755844; Score: 0.37
DE  Interaction: P38264; IntAct: EBI-7761916; Score: 0.37
DE  Interaction: Q04182; IntAct: EBI-7766464; Score: 0.37
DE  Interaction: P36172; IntAct: EBI-7766515; Score: 0.37
DE  Interaction: Q04263; IntAct: EBI-7766567; Score: 0.37
DE  Interaction: Q03263; IntAct: EBI-7773546; Score: 0.37
DE  Interaction: P04817; IntAct: EBI-7773596; Score: 0.37
DE  Interaction: P37020; IntAct: EBI-7775442; Score: 0.37
DE  Interaction: P36015; IntAct: EBI-7775492; Score: 0.37
DE  Interaction: Q12016; IntAct: EBI-2342718; Score: 0.37
DE  Interaction: P39547; IntAct: EBI-2342749; Score: 0.55
DE  Interaction: Q03860; IntAct: EBI-2343145; Score: 0.37
DE  Interaction: Q04767; IntAct: EBI-2343164; Score: 0.37
DE  Interaction: P47088; IntAct: EBI-2343175; Score: 0.37
DE  Interaction: Q8TGQ7; IntAct: EBI-2343395; Score: 0.37
DE  Interaction: Q04969; IntAct: EBI-2343539; Score: 0.37
DE  Interaction: Q12743; IntAct: EBI-2344289; Score: 0.37
DE  Interaction: O13540; IntAct: EBI-2344292; Score: 0.37
DE  Interaction: P47111; IntAct: EBI-2344971; Score: 0.37
DE  Interaction: P53868; IntAct: EBI-2345024; Score: 0.37
DE  Interaction: P38226; IntAct: EBI-2345081; Score: 0.37
DE  Interaction: P06197; IntAct: EBI-2345697; Score: 0.37
DE  Interaction: Q02724; IntAct: EBI-2346025; Score: 0.37
DE  Interaction: Q06144; IntAct: EBI-2346245; Score: 0.37
DE  Interaction: P40107; IntAct: EBI-2346894; Score: 0.37
DE  Interaction: P40857; IntAct: EBI-2346945; Score: 0.37
DE  Interaction: P46956; IntAct: EBI-2346954; Score: 0.37
DE  Interaction: P53142; IntAct: EBI-2346948; Score: 0.37
DE  Interaction: P32453; IntAct: EBI-2347423; Score: 0.37
DE  Interaction: P53845; IntAct: EBI-2347438; Score: 0.37
DE  Interaction: P32621; IntAct: EBI-2347719; Score: 0.37
DE  Interaction: P02829; IntAct: EBI-3814972; Score: 0.35
DE  Interaction: Q9BSE2; IntAct: EBI-11529987; Score: 0.56
DE  Interaction: P39550; IntAct: EBI-16248456; Score: 0.00
DE  Interaction: P20486; IntAct: EBI-16248476; Score: 0.00
GO  GO:0000329;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005886;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQTPSENTDVKLDTLDEPSAHLIEENVALPEDTFNSYWSYILNEIARCKPLMIMFLIPVCLVLLITFFHDIKGILVFLVI
SQ  SLILSIIILLIGITAFVSETLNKGFIIKLLVEVITRKPAVGGKEWRIIAYNMNQYLFDHGIWHTPYYFFCEHRCHKFFKS
SQ  LIKQTRSNAHLSSPTNGAENTQSNTPAKEVSNEMVKPYIFSSDPVLEAYLIKAAEIHKEAEFEYWRKQYPEVDLP
//
ID  Q08926;
PN  ULP1-interacting protein 4;
GN  UIP4;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16407407}; Peripheral membrane protein {ECO:0000269|PubMed:16407407}. Mitochondrion outer membrane {ECO:0000269|PubMed:16407407}. Nucleus envelope {ECO:0000269|PubMed:16407407}.
DR  UNIPROT: Q08926;
DR  UNIPROT: D6W3I3;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P54783; IntAct: EBI-6339110; Score: 0.00
DE  Interaction: P54837; IntAct: EBI-6339429; Score: 0.00
DE  Interaction: Q02795; IntAct: EBI-6340892; Score: 0.00
DE  Interaction: Q05359; IntAct: EBI-6343862; Score: 0.00
DE  Interaction: P0C268; IntAct: EBI-6346217; Score: 0.00
DE  Interaction: P18411; IntAct: EBI-6346228; Score: 0.00
DE  Interaction: P38756; IntAct: EBI-6346239; Score: 0.00
DE  Interaction: Q07549; IntAct: EBI-16711805; Score: 0.37
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0005741;
GO  GO:0005635;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:16407407};
SQ  MVTIVFDHPAEDFPELKIAGEFTNWEGVPMKINTSSGKWEYKFDESSVTKHNDKDKVHFKFIDQNGNWFADDEYPKEVDE
SQ  HSNENNVATLNNEEDGGSAGEEKDEGDKTAHNTNENGSELYYEGPETPTPSLKGNVTFPSPKTAISQDGSAFAKETTRKE
SQ  RKYEHAPLNEVPVERDPKEENKELSPNFSQEQTENKQDKGLDNLSEGNDNDNTRVNEDTDVTDTQESEHEINGSDTENTD
SQ  MSEQEEIQKIDKPADQNAKSIVKEGDANTEDYESVLKKLLGALGRFFGSWFSWLTTKMSSSEAS
//
ID  P36137;
PN  Protein UIP5;
GN  UIP5;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Single-pass type I membrane protein.
DR  UNIPROT: P36137;
DR  UNIPROT: D6VXA6;
DR  Pfam: PF03388;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: P02829; IntAct: EBI-864706; Score: 0.00
GO  GO:0030134;
GO  GO:0005789;
GO  GO:0005793;
GO  GO:0000324;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005537;
GO  GO:0007029;
GO  GO:0006888;
GO  GO:0007030;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSRDVRAEKLAISLLILSLFLIFQLVAEIYLNNGDQYHTETSPFTRGRSHVTRVPNHDASLSIPFLDKINQFWHVGGATQ
SQ  IRNIQSIKLTQDRDQDKHGLVLSNGIGDNTINDFEIVFTFRISHDPTTQLTGDGMCFAITPENGFLTQNLQSSYAKKQYM
SQ  MNSQGVIADNTDLMGFPKNLPGLFIVLDTYRNQGHDHKEVPFMDVFINVAPESDWYDINSDGELSTSLRLNSRGHIKLKK
SQ  NALWNRVTKLRIIYLESISFLKIDVQYAKEGNYWIELFQTTENLYLPKNMHTGQRYIGCSALNGQLTETVELLDVSTSEF
SQ  HWNDMDASIEDTYDYAKEAELFLEQEFGEVLDREPDEFTKWKMIKAQPNIKTGSQSAEQKTSNNPHSRLFKVVLTIWHYS
SQ  EILLLIMGIYLFSACIRVFQRRFKKIRSRRKRAGSHSVGLLPM
//
ID  P28971;
PN  Protein UL20 homolog;
GN  41;
OS  31520;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: P28971;
DR  UNIPROT: Q6S6T0;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250, ECO:0000269|PubMed:16352534}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044423;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPQVLMGNTRLHAPLEDGIPLIENDENSSQNEVDLYDYVSMSSYGGDNDFLISSAGGNITPENRPSFSAHVVLFAISALV
SQ  IKPVCCFIFLNHYVITGSYDFAVAGGVCTVLYYMRLALTAWFMFRNIQSDMLPLNVWQQFVIGCMALGRTVAFMVVSYTT
SQ  LFIRSELFFSMLAPNAGREYITPIIAHKLMPLISVRSAVCLVIISTAVYAADAICDTIGFTLPRMWMCILMRSSSVKRS
//
ID  P84392;
PN  Protein UL20 homolog;
GN  41;
OS  310273;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: P84392;
DR  UNIPROT: Q6S6T0;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044423;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPQVLMGNTRLHAPLEDGIPLIENDENSSQNEVDLYDYVSMSSYGGDNDFLISSAGGNITPENRPSFSAHVVLFAISALV
SQ  IKPVCCFIFLNHYVITGSYDFAVAGGVCTVLYYMRLALTAWFMFRNIQSDMLPLNVWQQFVIGCMALGRTVAFMVVSYTT
SQ  LFIRSELFFSMLAPNAGREYITPIIAHKLMPLISVRSAVCLVIISTAVYAADAICDTIGFTLPRMWMCILMRSSSVKRS
//
ID  Q77MS4;
PN  Protein UL20 homolog;
GN  MDV032;
OS  10389;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: Q77MS4;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044423;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSKHGFGYYATEANEYTIPLDDIDDGRSDTDAKTLGSVLTQLSEEVDWDDAVDYATMSSYLGDYVFTIPNSYDIHPKFTR
SQ  YVVLFGLSTFVLRPSCCLIFLFYAIYAQDNRFLILGTTITAFFYGTLMLEMYYMYANIKYDLMPLSKFQQVLIGALSMLG
SQ  PIIFVAISYNMIFKDVTFMKKILAFDTNLKTSGFVIYLVMIASLAYSITSISDAIGFLLPRLWTRAVLKSCVPF
//
ID  P10204;
PN  Protein UL20;
GN  UL20;
OS  10299;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000269|PubMed:18596102, ECO:0000269|PubMed:7933124}. Host Golgi apparatus membrane {ECO:0000269|PubMed:15254173}; Multi-pass membrane protein {ECO:0000255}. Host nucleus membrane {ECO:0000269|PubMed:15254173}; Multi-pass membrane protein {ECO:0000255}. Note=During virion morphogenesis, this protein probably accumulates in the trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000269|PubMed:15254173}.
DR  UNIPROT: P10204;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes. {ECO:0000269|PubMed:1719228, ECO:0000269|PubMed:17996071}.
DE  Reference Proteome: Yes;
DE  Interaction: P68331; IntAct: EBI-7906341; Score: 0.67
DE  Interaction: P10221; IntAct: EBI-10042677; Score: 0.27
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0016021;
GO  GO:0044423;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTMRDDLPLVDRDLVDEAAFGGEEGELPLEEQFSLSSYGTSDFFVSSAYSRLPPHTQPVFSKRVILFLWSFLVLKPLEMV
SQ  AAGMYYGLTGRVVAPACILAAIVGYYVTWAVRALLLYVNIKRDRLPLSAPVFWGMSVFLGGTALCALFAAAHETFSPDGL
SQ  FHFIATNQMLPPTDPLRTRALGIACAAGASMWVAAADSFAASANFFLARFWTRAILNAPVAF
//
ID  P89443;
PN  Protein UL20;
GN  UL20;
OS  10315;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: P89443;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044423;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTMRDDVPLLDRELVDEAACGGEDGELPLDEQFSLSSYGTSDFFVSSAYSRLPPHTQPVFSKRVVMFAWSFLVLKPLELV
SQ  AAGMYYGWTGRAVAPACIIAAVLAYYVTWLARALLLYVNIKRDRLPLSPPVFWGLCVIMGGAALCALVAAAHETFSPDGL
SQ  FHWITASQLLPRTDPLRARSLGIACAAGAAMWVAAADCFAAFTNFFLARFWTRAILKAPVAF
//
ID  Q6UDI5;
PN  Protein UL20;
GN  UL20;
OS  670426;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: Q6UDI5;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044423;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MADASAPDKKNAPTNALKPDLIKIAVERVLAAIDTENNEDLILAAAREPREVVAARAPDLFTSAAYSWSEEDELGTRMRA
SQ  SSFFPVASMFAKIICCLFLLWAKSCTGHGAMVTGLTACTGAYAIASLLCSFVVYYNVRTDNMPFGTYTKLFQIAACIGCG
SQ  CYALGLTMEKLFGDSEMYFALFPDAKNSPLVGATAKGSALILPQGCSVAPYVPLAVSVAYCAAVVYDIADTIFPLLWVRT
SQ  TLNEFAVF
//
ID  Q00702;
PN  Protein UL20;
GN  UL20;
OS  10349;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: Q00702;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250, ECO:0000269|PubMed:10799582, ECO:0000269|PubMed:9188641}.
DE  Reference Proteome: No;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044423;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEDAAADVDAAADAKLTGENDALLSSAFVGARPPRPRFSSHVVSLLALALALRPACCLVLALHGSRATLAALLTALAFYA
SQ  RAAVCAVLVARNVARDRMPLSPAQQAALGLLAAARLAFLYVALDAGRHYAPALAGALYGADCVCDALAFLLPRAYARSIM
SQ  H
//
ID  P09290;
PN  Protein UL20 homolog;
GN  39;
OS  10338;
SL  Nucleus Position: SL-0415;
SL  Nucleus Position: SL-0418;
SL  Comments: Virion {ECO:0000250}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported with gK to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.
DR  UNIPROT: P09290;
DR  Pfam: PF04544;
DE  Function: Plays an essential role in egress of virus particles from the nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a functional protein complex with gK and this interaction is absolutely essential for their coordinate intracellular transport, gK glycosylation, expression on host cell surface, and function. Together, they modulate gB-mediated virus-induced cell fusion and virion egress and therefore actively participate in these processes (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0044175;
GO  GO:0044178;
GO  GO:0044200;
GO  GO:0020002;
GO  GO:0016021;
GO  GO:0044423;
GO  GO:0019058;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNPPQARVSEQTKDLLSVMVNQHPEEDAKVCKSSDNSPLYNTMVMLSYGGDTDLLLSSACTRTSTVNRSAFTQHSVFYII
SQ  STVLIQPICCIFFFFYYKATRCMLLFTAGLLLTILHHFRLIIMLLCVYRNIRSDLLPLSTSQQLLLGIIVVTRTMLFCIT
SQ  AYYTLFIDTRVFFLITGHLQSEVIFPDSVSKILPVSWGPSPAVLLVMAAVIYAMDCLVDTVSFIGPRVWVRVMLKTSISF
//
ID  Q9H3U1;
PN  Protein unc-45 homolog A;
GN  UNC45A;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16478993}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16478993}. Nucleus {ECO:0000269|PubMed:16478993}. Note=Predominant in the perinuclear region. Little protein in the nucleus.
DR  UNIPROT: Q9H3U1;
DR  UNIPROT: A8K6F7;
DR  UNIPROT: Q7L3Y6;
DR  UNIPROT: Q9H3U8;
DR  UNIPROT: Q9NSE8;
DR  UNIPROT: Q9NSE9;
DR  PDB: 2DBA;
DR  Pfam: PF13181;
DR  Pfam: PF11701;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DR  OMIM: 611219;
DR  OMIM: 619377;
DR  DisGeNET: 55898;
DE  Function: Acts as co-chaperone for HSP90. Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell. May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity). {ECO:0000250, ECO:0000269|PubMed:12119110, ECO:0000269|PubMed:16478993, ECO:0000305}.
DE  Disease: Osteootohepatoenteric syndrome (OOHE) [MIM:619377]: An autosomal recessive disorder characterized by cholestasis, congenital diarrhea, impaired hearing, and bone fragility. Some patients also display mild developmental delay and intellectual disability. {ECO:0000269|PubMed:29429573}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O43542; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P48730; IntAct: EBI-28935490; Score: 0.35
DE  Interaction: Q63358; IntAct: EBI-25412031; Score: 0.35
DE  Interaction: O15198; IntAct: EBI-7263588; Score: 0.37
DE  Interaction: Q9P2S5; IntAct: EBI-1059548; Score: 0.00
DE  Interaction: O75365; IntAct: EBI-1060185; Score: 0.00
DE  Interaction: P01106; IntAct: EBI-1061600; Score: 0.00
DE  Interaction: Q9HAW0; IntAct: EBI-1072238; Score: 0.00
DE  Interaction: Q13418; IntAct: EBI-1074011; Score: 0.00
DE  Interaction: Q9Y5J5; IntAct: EBI-1074930; Score: 0.00
DE  Interaction: Q9Y2Q3; IntAct: EBI-1083629; Score: 0.00
DE  Interaction: O94966; IntAct: EBI-2511876; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-2878124; Score: 0.53
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q99459; IntAct: EBI-7954144; Score: 0.35
DE  Interaction: Q13286; IntAct: EBI-3248480; Score: 0.35
DE  Interaction: P07900; IntAct: EBI-3387925; Score: 0.35
DE  Interaction: O95758; IntAct: EBI-7851121; Score: 0.35
DE  Interaction: P0DOE9; IntAct: EBI-6138583; Score: 0.35
DE  Interaction: Q76353; IntAct: EBI-6174552; Score: 0.35
DE  Interaction: P48729; IntAct: EBI-6255977; Score: 0.53
DE  Interaction: P49674; IntAct: EBI-6256083; Score: 0.35
DE  Interaction: Q16543; IntAct: EBI-9393294; Score: 0.35
DE  Interaction: Q6ZRV2; IntAct: EBI-9395776; Score: 0.40
DE  Interaction: P08238; IntAct: EBI-9396165; Score: 0.40
DE  Interaction: P61244; IntAct: EBI-10218572; Score: 0.67
DE  Interaction: P50222; IntAct: EBI-10306447; Score: 0.56
DE  Interaction: Q8NA82; IntAct: EBI-10306457; Score: 0.78
DE  Interaction: Q9UJV3; IntAct: EBI-10306467; Score: 0.56
DE  Interaction: P35579; IntAct: EBI-11004631; Score: 0.35
DE  Interaction: O00159; IntAct: EBI-11030803; Score: 0.35
DE  Interaction: Q96H55; IntAct: EBI-11031416; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: Q8VDD5; IntAct: EBI-11092730; Score: 0.35
DE  Interaction: Q9WTI7; IntAct: EBI-11093786; Score: 0.35
DE  Interaction: P47755; IntAct: EBI-11117728; Score: 0.35
DE  Interaction: O15259; IntAct: EBI-11365282; Score: 0.27
DE  Interaction: O75665; IntAct: EBI-11365691; Score: 0.27
DE  Interaction: Q5SW79; IntAct: EBI-11368047; Score: 0.27
DE  Interaction: Q6ZU80; IntAct: EBI-11370150; Score: 0.27
DE  Interaction: Q86SG6; IntAct: EBI-11372039; Score: 0.27
DE  Interaction: Q8N157; IntAct: EBI-11374392; Score: 0.27
DE  Interaction: Q8N4C6; IntAct: EBI-11374469; Score: 0.27
DE  Interaction: Q8TES7; IntAct: EBI-11374846; Score: 0.27
DE  Interaction: Q92834; IntAct: EBI-11375243; Score: 0.27
DE  Interaction: Q96KN7; IntAct: EBI-11376202; Score: 0.27
DE  Interaction: Q96LK0; IntAct: EBI-11376319; Score: 0.27
DE  Interaction: Q96NL6; IntAct: EBI-11376636; Score: 0.27
DE  Interaction: Q96ST8; IntAct: EBI-11377220; Score: 0.27
DE  Interaction: Q9NXB0; IntAct: EBI-11377799; Score: 0.27
DE  Interaction: Q9P2K1; IntAct: EBI-11378868; Score: 0.27
DE  Interaction: O43303; IntAct: EBI-11380227; Score: 0.27
DE  Interaction: O95684; IntAct: EBI-11381827; Score: 0.27
DE  Interaction: Q15468; IntAct: EBI-11383475; Score: 0.27
DE  Interaction: Q2KHM9; IntAct: EBI-11383837; Score: 0.27
DE  Interaction: Q5TB80; IntAct: EBI-11385924; Score: 0.27
DE  Interaction: Q6UVJ0; IntAct: EBI-11388172; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11389870; Score: 0.27
DE  Interaction: Q8N960; IntAct: EBI-11393386; Score: 0.27
DE  Interaction: Q8NBT0; IntAct: EBI-11394140; Score: 0.27
DE  Interaction: Q8TC44; IntAct: EBI-11394502; Score: 0.27
DE  Interaction: Q9HC77; IntAct: EBI-11397411; Score: 0.27
DE  Interaction: Q13099; IntAct: EBI-12453414; Score: 0.35
DE  Interaction: Q969V4; IntAct: EBI-24282836; Score: 0.56
DE  Interaction: Q96HU8; IntAct: EBI-23773412; Score: 0.56
DE  Interaction: Q6FHY5; IntAct: EBI-24395197; Score: 0.56
DE  Interaction: P50221; IntAct: EBI-24442064; Score: 0.56
DE  Interaction: Q4G0R1; IntAct: EBI-24476545; Score: 0.56
DE  Interaction: Q6IQ23; IntAct: EBI-16398399; Score: 0.35
DE  Interaction: Q7Z406; IntAct: EBI-21648535; Score: 0.35
DE  Interaction: Q12965; IntAct: EBI-21648535; Score: 0.35
DE  Interaction: Q00537; IntAct: EBI-21648535; Score: 0.35
DE  Interaction: O14975; IntAct: EBI-21648535; Score: 0.35
DE  Interaction: P03950; IntAct: EBI-16363232; Score: 0.35
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-20920036; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q99558; IntAct: EBI-21261374; Score: 0.35
DE  Interaction: Q15077; IntAct: EBI-21262943; Score: 0.35
DE  Interaction: P13569; IntAct: EBI-25416349; Score: 0.35
DE  Interaction: B2RTY4; IntAct: EBI-25409153; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: P35226; IntAct: EBI-27108918; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-28935882; Score: 0.35
DE  Interaction: Q8WXR4; IntAct: EBI-28944037; Score: 0.35
DE  Interaction: K7EJ46; IntAct: EBI-27120449; Score: 0.35
DE  Interaction: Q9UM73; IntAct: EBI-32719830; Score: 0.27
DE  Interaction: P22607; IntAct: EBI-32721979; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
DE  Interaction: Q06124; IntAct: EBI-32723738; Score: 0.27
DE  Interaction: Q04912; IntAct: EBI-32725158; Score: 0.27
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0016607;
GO  GO:0048471;
GO  GO:0045296;
GO  GO:0051879;
GO  GO:0030154;
GO  GO:0061077;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVSGPGTPEPRPATPGASSVEQLRKEGNELFKCGDYGGALAAYTQALGLDATPQDQAVLHRNRAACHLKLEDYDKAETE
SQ  ASKAIEKDGGDVKALYRRSQALEKLGRLDQAVLDLQRCVSLEPKNKVFQEALRNIGGQIQEKVRYMSSTDAKVEQMFQIL
SQ  LDPEEKGTEKKQKASQNLVVLAREDAGAEKIFRSNGVQLLQRLLDMGETDLMLAALRTLVGICSEHQSRTVATLSILGTR
SQ  RVVSILGVESQAVSLAACHLLQVMFDALKEGVKKGFRGKEGAIIVDPARELKVLISNLLDLLTEVGVSGQGRDNALTLLI
SQ  KAVPRKSLKDPNNSLTLWVIDQGLKKILEVGGSLQDPPGELAVTANSRMSASILLSKLFDDLKCDAERENFHRLCENYIK
SQ  SWFEGQGLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESVIALCASEQEEEQLVAVEALIHAAGKAKRASFITANGVS
SQ  LLKDLYKCSEKDSIRIRALVGLCKLGSAGGTDFSMKQFAEGSTLKLAKQCRKWLCNDQIDAGTRRWAVEGLAYLTFDADV
SQ  KEEFVEDAAALKALFQLSRLEERSVLFAVASALVNCTNSYDYEEPDPKMVELAKYAKQHVPEQHPKDKPSFVRARVKKLL
SQ  AAGVVSAMVCMVKTESPVLTSSCRELLSRVFLALVEEVEDRGTVVAQGGGRALIPLALEGTDVGQTKAAQALAKLTITSN
SQ  PEMTFPGERIYEVVRPLVSLLHLNCSGLQNFEALMALTNLAGISERLRQKILKEKAVPMIEGYMFEEHEMIRRAATECMC
SQ  NLAMSKEVQDLFEAQGNDRLKLLVLYSGEDDELLQRAAAGGLAMLTSMRPTLCSRIPQVTTHWLEILQALLLSSNQELQH
SQ  RGAVVVLNMVEASREIASTLMESEMMEILSVLAKGDHSPVTRAAAACLDKAVEYGLIQPNQDGE
//
ID  Q99KD5;
PN  Protein unc-45 homolog A;
GN  Unc45a;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominant in the perinuclear region. Little protein in the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q99KD5;
DR  UNIPROT: Q3TKV6;
DR  UNIPROT: Q8BFT3;
DR  UNIPROT: Q8C157;
DR  Pfam: PF13181;
DR  Pfam: PF11701;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: May act as co-chaperone for HSP90 (Potential). Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell (By similarity). May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen. {ECO:0000250, ECO:0000269|PubMed:12356907, ECO:0000269|PubMed:9209433, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005794;
GO  GO:0016607;
GO  GO:0048471;
GO  GO:0051879;
GO  GO:0030154;
GO  GO:0061077;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVSGPETPEPRPSDPGASSAEQLRKEGNELFKCGDYEGALTAYTQALSLGATPQDQAILHRNRAACHLKLEDYSKAESE
SQ  ASKAIEKDGGDVKALYRRSQALEKLGRLDQAVLDLKRCVSLEPKNKVFQESLRNIGGQIQEKVRYMSSTDAKVEQMFQIL
SQ  LDPKEKGTEKKQKASQNLVVLAREDAGAEKIFRSNGVQLLQRLLDTEETDLMLAALRTLVGICSEHQSRTVATLSVLGTR
SQ  RVVSILGVENQAVSLAACHLLQVIFDALKEGVKKGFRGKEGAIIVDPARELKVLINSLLELLTEVGVSGQGRDNALTLLI
SQ  KMVPRKSPKDPNNSLTLWVIDQGLKKILEVGGSLQDAAGELTVTANSRMSASILLSKLFDDLKCDAERENFHRLCENYIR
SQ  NWFEGHGLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESVIALCASEREEEQLVAVEALIHAAGKAKRASFITANGVS
SQ  LLKDLYKGSERDSIRIRALVGLCKLGSAGGTDFSMKQFAEGSTLKLAKQCRKWLCNDQIDAGTRRWAVEGLAYLTFDADV
SQ  KEEFVEDEAALKALFQLSRSEERSVLFAVGSALVNCTNSYDYEEPDPKMVELAKYAKQHVPEQHPKDKPSFVRARVKKLL
SQ  AAGVVSAMTCMVKTESPVLTNSCRELLSRVFLALVEEVEDRGTVVAQGGGKALLPLALEGTDVGQTKAAQALAKLTITSN
SQ  PEMTFPGERIYEVVRPLVSLLHLSCSGLQNFEALMALTNLAGISERLRQKILKEKAVPMIEGYMFEEHEMIRRAATECMC
SQ  NLAMSKEVQDLFEAQGNDRLKLLVLYSGEDDELLRRAAAGGLAMLTSMRPALCSRIPQVTTHWLEILQALLLSPNQELQH
SQ  RGTVVVLNMMQSSKEIAGTLMESEVLEILSVLAKGEESPVTRAAAACLEKAVEYRLIQPNQDGE
//
ID  Q5RAP0;
PN  Protein unc-45 homolog A;
GN  UNC45A;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominant in the perinuclear region. Little protein in the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5RAP0;
DR  Pfam: PF13181;
DR  Pfam: PF11701;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: May act as co-chaperone for HSP90 (Potential). Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell (By similarity). May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity). {ECO:0000250, ECO:0000305}.
DE  Reference Proteome: Yes;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0030154;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTASSVEQLRKEGNELFKCGDYGGALAAYTQALGLDATPQDQAVLHRNRAACYLKLEDYDKAETEASKAIEKDGGDVKAL
SQ  YRRSQALEKLGRLDQAVLDLQRCVSLEPKNKVFQEALRNIGGQIQEKVRYMSSTDAKVEQMFQILLDPEEKGTEKKQKAS
SQ  QNLVVLAREDAGAEKTLRSNGVQLLQRLLDTGETDLMLAALRTLVGICSEHQSRTVATLSILGTRRVVSILGVESQSVSL
SQ  AACHLLQVMFDALKEGVKKGFRGKEGAIIVDPARELKVLISNLLDLLTEVGVSGQGRDNALTLLIKAVPRKSLKDPNNSL
SQ  TLWVIDQGLKKILEVGGSLQDPPGELAVTANSRMSASILLSKLFDDLKCDAERENFHRLCENYIKSWFEGRGLAGKLRAI
SQ  QTVSCLLQGPCDAGNRALELSGVMEGVIALCASEQEEEQLVAVEALIHAAGKAKRASFITANGVSLLKDLYKRSEKDSIR
SQ  IRALVGLCKLGSAGGTDFSMKQFAEGSTLKLAKQCRKWLCNDQIDAGTRRWAVEGLAYLTFDADVKEEFVEDAAALKALF
SQ  QLSRSEERSVLFAVASALVNCTNSYDYEEPDPKMVELAKYAKQHVPEQHPKDKPSFVRARVKKLLAAGVVSAMVYMVKTE
SQ  SPVLTSSCRELLSRIFLALVEEVEDRGTVVAQGGGRALIPLALEGTDVGQTKAAQALAKLTITSNPEMTFPGERIYEVVR
SQ  PLVSLLHLNCSGLQNFEALMALTNLAGISERLRQKILKEKAVPMIEGYMFEEHEMIRRASTECMCNLAMSKEVQDLFEAE
SQ  GNDRLKLLVLYSGEDDELLQRAAAGGLAMLTSMRPTLCSRIPQVTTHWLEILQALLLSSNQELQHRGAVVVLNMVEASRE
SQ  IASTLMESEMMEILSVLAKGDHSPVTRAAAACLDKAVEYGLIQPNQDGE
//
ID  Q32PZ3;
PN  Protein unc-45 homolog A;
GN  Unc45a;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominant in the perinuclear region. Little protein in the nucleus (By similarity). {ECO:0000250}.
DR  UNIPROT: Q32PZ3;
DR  Pfam: PF13181;
DR  Pfam: PF11701;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: May act as co-chaperone for HSP90 (Potential). Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell (By similarity). May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity). {ECO:0000250, ECO:0000305}.
DE  Reference Proteome: Yes;
DE  Interaction: Q68CZ2; IntAct: EBI-22265227; Score: 0.35
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0051879;
GO  GO:0030154;
GO  GO:0061077;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTVSGPGTPEPRPSDPGASSAEELRKEGNELFKCGDYEGALTAYTQALSLGATPQDQAILHRNRAACHLKLEDYSKAESE
SQ  ASKAIEKDGGDVKALYRRSQALEKLGRLDQAVLDLKRCVSLEPKNKVFQESLRNIGGQIQEKVRYMSSTDAKVEQMFQIL
SQ  LDPKEKGTEKKQKASQNLVVLAREDAGAEKIFRSNGVQLLQRLLDTGETDLMLAALRTLVGICSEHQSRTVATLSVLGTR
SQ  RVVSILGVENQAVSLAACHLLQVMFDALKEGVKKGFRGKEGAIIVDPARELKVLISNLLELLTEIGVSGQGRDNALTLLI
SQ  KMVPRKSPKDPNNSLTLWVIDQGLKKILEVGGSVPEAAGELTVTANSRMSASILLSKLFDDLKCDAERENFHRLCENYIR
SQ  SWFEGQGLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESVIALCASEQEEEQLVAVEALIHAAGKAKRASFITANGVA
SQ  LLKDLYKGSERDSIRIRALVGLCKLGSAGGTDFSMKQFAEGSTLKLAKQCRKWLCNDQIDAGTRRWAVEGLAYLTFDADV
SQ  KEEFVEDEAALKALFQLSRSEERSVLFAVGSALVNCTNSYDYEEPDPKMVELAKYAKQHVPEQHPKDKPSFVRARVKKLL
SQ  AAGVVSAMTCMVKTESPVLTNSCRELLSRVFLALVEEVEDRGTVVAQGGGKALLPLALEGTDVGQTKAAQALAKLTITSN
SQ  PEMTFPGERIYEVVRPLVSLLHLSCSGLQNFEALMALTNLAGISERLRQKILKEKAVPMIEGYMFEEHEMIRRAATECMC
SQ  NLAMSKEVQDLFEAQGNDRLKLLVLYSGEDDELLRRAAAGGLAMLTSMRPSLCSRIPQVTTHWLEILQALLLSPNPELQH
SQ  RGTVVVLNMMESSKEIASTLMESEVLEILSVLAKGEESPVTRAAAACLEKAVEYRLIQPNQDGE
//
ID  Q6DGE9;
PN  Protein unc-45 homolog B;
GN  unc45b;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Translocates to the A band in response to stress conditions and fibril damage. {ECO:0000269|PubMed:18347070, ECO:0000269|PubMed:20440001}.
DR  UNIPROT: Q6DGE9;
DR  UNIPROT: Q8UVX6;
DR  Pfam: PF11701;
DR  PROSITE: PS50293;
DE  Function: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain (By similarity). Plays a role in sarcomere formation during muscle cell development. Required for myoseptal integrity, myofiber attachment, motility and craniofacial development (PubMed:17189627, PubMed:17586488, PubMed:20440001, PubMed:20849610). Is necessary for normal early lens development (PubMed:24549050). {ECO:0000250|UniProtKB:Q8CGY6, ECO:0000269|PubMed:17189627, ECO:0000269|PubMed:17586488, ECO:0000269|PubMed:20440001, ECO:0000269|PubMed:20849610, ECO:0000269|PubMed:24549050}.
DE  Reference Proteome: Yes;
GO  GO:0031672;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0051879;
GO  GO:0048738;
GO  GO:0061077;
GO  GO:0002088;
GO  GO:0030239;
GO  GO:0060538;
GO  GO:0007519;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTMGEIGDSVQLKEEGNKHFQAGEIDQAIDCYTKAIKTCKKEDKKALAVIYRNRSACFLKKENYSNAASDATKAIDVDAA
SQ  DIKALYRRCQAFEKLGKLDMAFKDVQRCATIEPKNKTFLETLRRLGAEIQQKLKTTFSTDSRVQNMFDILFSDEPDKEKR
SQ  EKAANNLIVLAREDAGAERIFQNNGVPLLMQLIDTGKPEMILAAIRTLSGMCTGHRARATAIIHSVGISKLCSIMAVDNE
SQ  EIALATANLFQCVNDSLSGGDKRNYGKEEALVLDSSKDLKDILLALLEMIASKNVSGHGRDQALNLLTKNVPRQNKKSTD
SQ  NSKCLFTIDHGLKKILKVCGQVPDLPDQLPMTENTQLIASVLLSKLYDDLRCDPERDQFRDICDDYIKSKFDPNDMDKNI
SQ  HAINTLSGILQGPFDLGNVLAGRQGVMEMMVALCGSEREVDQLVAVEALIHASTKTSKASFFISNGVSLLKEMYKKTKNE
SQ  KIKIRALVGLCKLGSAGGDDYSMRQFAEGSTEKLAKQCRKWLCNPTLDVRTRKWAIEGLAYLTNDADVKDDFAEDEPAMR
SQ  AMFELTKSNDKTILYAVACTLVNCTNSYDKKEIIPEMVQLAKFSKQHVPEQHPKDKKDFIVRRVKRLLKAGVTSALAVMV
SQ  KADNSILTDQTKEMLARVFLALTEDVKDRGIIVAQGGGKALIPLALEGTDKGKIKASHALAKIAAVSNPEIAFPGERIYE
SQ  VVRPLVSLLGTDRDGMENFEALRGLTNLAGLNDKLRVKILKEKALPEIENYMFEDHEQIRQAATECMCNLVCCKEVQDRY
SQ  LEDGNDKLKLLVLLCGEDEEKLQRAAAGALAMLTAAQKKLAVKMTKVTEQWLEILQRLCIHDNPEIQHRGLVTVFNMLDA
SQ  DDQLAKKLVESDMLEILTYVAKLEDNPKKQNAIDAARACLSKAMDNGLIKPFSN
//
ID  Q8IWX7;
PN  Protein unc-45 homolog B;
GN  UNC45B;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:33217308}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CGY6}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Translocates to the A band in response to stress conditions and fibril damage. {ECO:0000250|UniProtKB:Q6DGE9}.
DR  UNIPROT: Q8IWX7;
DR  UNIPROT: Q495Q8;
DR  UNIPROT: Q495Q9;
DR  Pfam: PF11701;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DR  OMIM: 611220;
DR  OMIM: 616279;
DR  OMIM: 619178;
DR  DisGeNET: 146862;
DE  Function: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain. Plays a role in sarcomere formation during muscle cell development. Is necessary for normal early lens development. {ECO:0000250|UniProtKB:Q6DGE9, ECO:0000250|UniProtKB:Q8CGY6}.
DE  Disease: Cataract 43 (CTRCT43) [MIM:616279]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. {ECO:0000269|PubMed:24549050}. Note=The disease is caused by variants affecting the gene represented in this entry. Myopathy, myofibrillar, 11 (MFM11) [MIM:619178]: A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM11 is an autosomal recessive form characterized by onset of slowly progressive proximal muscle weakness in the first decade of life. More variable features may include decreased respiratory forced vital capacity, variable cardiac features, and calf hypertrophy. Skeletal muscle biopsy shows myopathic changes with variation in fiber size, type 1 fiber predominance, centralized nuclei, eccentrically placed core-like lesions, and distortion of the myofibrillary pattern with Z-line streaming and abnormal myofibrillar aggregates or inclusions. {ECO:0000269|PubMed:31852522, ECO:0000269|PubMed:33217308}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P04626; IntAct: EBI-9363369; Score: 0.40
DE  Interaction: P35998; IntAct: EBI-9365600; Score: 0.40
DE  Interaction: P54652; IntAct: EBI-9366757; Score: 0.40
DE  Interaction: P07900; IntAct: EBI-9379979; Score: 0.40
DE  Interaction: Q6PK50; IntAct: EBI-9379957; Score: 0.40
DE  Interaction: Q8NI51; IntAct: EBI-9380938; Score: 0.40
DE  Interaction: O95433; IntAct: EBI-9395791; Score: 0.35
DE  Interaction: K9JA46; IntAct: EBI-9395791; Score: 0.35
DE  Interaction: Q86SX1; IntAct: EBI-9395791; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-9395791; Score: 0.50
DE  Interaction: P0DOF2; IntAct: EBI-25607852; Score: 0.35
GO  GO:0031672;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0051879;
GO  GO:0030154;
GO  GO:0061077;
GO  GO:0002088;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEVEAVQLKEEGNRHFQLQDYKAATNSYSQALKLTKDKALLATLYRNRAACGLKTESYVQAASDASRAIDINSSDIKAL
SQ  YRRCQALEHLGKLDQAFKDVQRCATLEPRNQNFQEMLRRLNTSIQEKLRVQFSTDSRVQKMFEILLDENSEADKREKAAN
SQ  NLIVLGREEAGAEKIFQNNGVALLLQLLDTKKPELVLAAVRTLSGMCSGHQARATVILHAVRIDRICSLMAVENEEMSLA
SQ  VCNLLQAIIDSLSGEDKREHRGKEEALVLDTKKDLKQITSHLLDMLVSKKVSGQGRDQALNLLNKNVPRKDLAIHDNSRT
SQ  IYVVDNGLRKILKVVGQVPDLPSCLPLTDNTRMLASILINKLYDDLRCDPERDHFRKICEEYITGKFDPQDMDKNLNAIQ
SQ  TVSGILQGPFDLGNQLLGLKGVMEMMVALCGSERETDQLVAVEALIHASTKLSRATFIITNGVSLLKQIYKTTKNEKIKI
SQ  RTLVGLCKLGSAGGTDYGLRQFAEGSTEKLAKQCRKWLCNMSIDTRTRRWAVEGLAYLTLDADVKDDFVQDVPALQAMFE
SQ  LAKAGTSDKTILYSVATTLVNCTNSYDVKEVIPELVQLAKFSKQHVPEEHPKDKKDFIDMRVKRLLKAGVISALACMVKA
SQ  DSAILTDQTKELLARVFLALCDNPKDRGTIVAQGGGKALIPLALEGTDVGKVKAAHALAKIAAVSNPDIAFPGERVYEVV
SQ  RPLVRLLDTQRDGLQNYEALLGLTNLSGRSDKLRQKIFKERALPDIENYMFENHDQLRQAATECMCNMVLHKEVQERFLA
SQ  DGNDRLKLVVLLCGEDDDKVQNAAAGALAMLTAAHKKLCLKMTQVTTQWLEILQRLCLHDQLSVQHRGLVIAYNLLAADA
SQ  ELAKKLVESELLEILTVVGKQEPDEKKAEVVQTARECLIKCMDYGFIKPVS
//
ID  Q8CGY6;
PN  Protein unc-45 homolog B;
GN  Unc45b;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:Q8IWX7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, cytosol {ECO:0000269|PubMed:18478096}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Translocates to the A band in response to stress conditions and fibril damage. {ECO:0000250|UniProtKB:Q6DGE9}.
DR  UNIPROT: Q8CGY6;
DR  UNIPROT: Q5XG72;
DR  UNIPROT: Q8BHC5;
DR  UNIPROT: Q8BWK3;
DR  Pfam: PF11701;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain. Plays a role in sarcomere formation during muscle cell development (PubMed:12356907, PubMed:18326487, PubMed:18478096). Is necessary for normal early lens development (By similarity). {ECO:0000250|UniProtKB:Q6DGE9, ECO:0000269|PubMed:12356907, ECO:0000269|PubMed:18326487, ECO:0000269|PubMed:18478096}.
DE  Reference Proteome: Yes;
DE  Interaction: P97414; IntAct: EBI-20564572; Score: 0.35
DE  Interaction: P51637; IntAct: EBI-20565496; Score: 0.35
GO  GO:0031672;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0051879;
GO  GO:0030154;
GO  GO:0061077;
GO  GO:0002088;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAEAEAAQLKEEGNRHFQLQDYKAATKSYSQALKLTKDKALLATLYRNRAACGLKMESYAQAASDASRAIDINSADIKAL
SQ  YRRCQALEHLGKLDQAFKDVQRCATLEPRNQNFQETLRRLNTSIQEQLRVQFSTDSRVQTMFEILLNENSEADKREKAAN
SQ  NLIVLGREEAGAERIFQSNGVALLLQLMNTQRPELLLAAVRTLSGMCSGHRARATAILHAVRIDRICSLMALENEEMSLA
SQ  VCNLLQAIIDSLSGEDKREHRGKEEALVLDTKKDLKQITSHLLDMLVSKKVSGQGRDQALNLLNKNVPRKDLSIHDNSRT
SQ  IYVVDNGLRKILKVVGQVPDLPSCLPLTDNTRMLASILINKLYDDLRCDPERDHFRKICEEYITSKFDPQDMDKNVNAIQ
SQ  TVSGILQGPFDLGNQLLGMKGVMEMMVALCGSEREADQLVAVEALIHASTKLSRATFIITNGVTLLKQIYKTTKNEKIKI
SQ  RTLVGLCKLGSAGGSDYGLRQFAEGSTEKLAKQCRKWLCNTAIDTRTRRWAVEGLAYLTLDADVKDDFVQDIPALQAMFE
SQ  LAKARTSDKTILYSVANTLVNCTNSYDVKEVVPELVQLAKFSKQHVPEEHPKDKKDFVDLRVKRLLKAGVISALACMVKA
SQ  DSAILTDQTKELLARVFLALCDNPKDRGTIVAQGGGKALIPLALEGTDVGKVKAAHGLAKIAAVSNPDIAFPGERVYEVV
SQ  RPLVSLLDTQRDGLQNYEALLGLTNLSGRSDKLRQKIFKEKALPDIENYMFENHDQLRQAATECMCNMVLNKEVQERFLA
SQ  DGNDRLKLVVLLCGEDDHKLQNAAAGALAMLTAAHKKLCLKMTEVTTQWLEILQRLCLHDQLSVQHRGLVIAHNLLSADA
SQ  ELARKLVESELLEILTVVGKQEPDEKRAAVVQTARECLIKCMDYGFIKPVS
//
ID  Q68F64;
PN  Protein unc-45 homolog B;
GN  unc45b;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:Q8IWX7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CGY6}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Translocates to the A band in response to stress conditions and fibril damage. {ECO:0000250|UniProtKB:Q6DGE9}.
DR  UNIPROT: Q68F64;
DR  Pfam: PF13181;
DR  Pfam: PF11701;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain. Plays a role in sarcomere formation during muscle cell assembly (By similarity). Is necessary for normal early lens development. {ECO:0000250|UniProtKB:D7REX8, ECO:0000250|UniProtKB:Q6DGE9, ECO:0000250|UniProtKB:Q8CGY6}.
DE  Reference Proteome: Yes;
GO  GO:0031672;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0030154;
GO  GO:0002088;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDPVQLKEEGNKYFQSNDYGNAIECYSKALKLITDKKMKAVLYRNRSACYLKQENYIQAAADASKAIDVDASDIKALFR
SQ  RCQALEKLGKLDQAYKDVQRCATLEPKNRTFLEMLHRLGSNIQEKLHVQFSTDSRVQKMFEILLDENSDKEKREKAANNL
SQ  IVLGREDAGAERIFQNNGVNLLMQLIETKDPELILSAVRTLSGMCTGHRARATAIVHLVGINKICSIMAVDHEEIALAAC
SQ  NLLQNIVDSLTGEDKKVHGKEEALVLDTKKDLKVITTHLLDMLVSKKVSGHGRDQALNLLNKNIPRYDLKNKDNSKTLFV
SQ  VDVGLKKILKVLGQVPELPNCLPLTPNTRLNASVLINKLYDDLRCDPERDDFRKICEEYITGSFDPKDMEKNLHAIQTVS
SQ  GILQGPFDLGNILLGMQGVMEMMVALTGSEKEVDQLVAVEALIHASTKLSRASFIITNGVSLLKDIYKKTKNEKIKIRAL
SQ  VGLCKLGSAGGTDYALRQFAEGSTDKLAKQCRKWLCNTSLDIQTRKWAVEGLAYLTLDADVKDEFVEDEQSLKAMFELCK
SQ  TSDKTILYSVATTLVNCTNSYDVKEVIPEMVQLAKFSKQHVPEQHPKDKKDFVLKRVKKLLQADVISALSCMVKADNSIL
SQ  TDQTKEQIARVFLALCDEPKDRGIIVAQGGGKAMIPLALEGTDVGKTKASHGLAKIAAVSNPDIAFPGERVYEVVRPLVS
SQ  LLNTERDGVQNFEALLALTNLSGKSDKLRQKIVKEKALPEIENYMFENHEQIRQAATECMCNLAVNKEVKERFTAEGNDR
SQ  LKLIVLLCGEDEEVKLQRAAAGTLAILTAAEKKLCHKMTEVTSQWLEILQRLCLNEDLQVQHRGVVITYNLISAEKELAK
SQ  KLVESEMLEILTVIGKQADVPNKQHIINVAREALVKCLDYGFIKTVS
//
ID  D7REX8;
PN  Protein unc-45 homolog B;
GN  unc45b;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:Q8IWX7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CGY6}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Translocates to the A band in response to stress conditions and fibril damage. {ECO:0000250|UniProtKB:Q6DGE9}.
DR  UNIPROT: D7REX8;
DR  UNIPROT: Q68ER3;
DR  Pfam: PF11701;
DR  PROSITE: PS50005;
DR  PROSITE: PS50293;
DE  Function: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain (By similarity). Plays a role in sarcomere formation during muscle cell development. Is necessary for normal early lens development. {ECO:0000250|UniProtKB:Q6DGE9, ECO:0000250|UniProtKB:Q8CGY6, ECO:0000269|PubMed:20637071}.
DE  Reference Proteome: Yes;
GO  GO:0031672;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0030018;
GO  GO:0051879;
GO  GO:0030154;
GO  GO:0061077;
GO  GO:0002088;
GO  GO:0007517;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEDPVQLKEEGNKYFQSNEYGQAIQCYSKALKLITDKKMQAVLYRNRSACYLKQDNYVQAAADASKAIDVDASDIKALFR
SQ  RCQALEKLGKLDQAYKDVQRCATLEPKNRTFLETLHRLGTNIQEKLHVQFSTDSRVHKMFEILLDKNSEKEKREKAANNL
SQ  IVLGREDAGAEQIFQNNGVNLLMQLIESKDPEMILSAIRTLSGMCTGHRARATAIVHLVGINKICSIMAVDNEEIALAAC
SQ  NLLQNIVDSLTGEDKKAHGKQEALVLDTKKDLKIITTHLLDMLVSKKVSGHGRDQALNLLNKNIPRYDLKNKDNSKSLFV
SQ  VDAGLKKILKVLGQVPELPNCLPLTPNTRLNASVLVNKLYDDLRCDPERDNFRIICEEYITGSFDPKDMEKNLHAIQTVS
SQ  GILQGPFDLGNKLLSLQGVMEMMVALTGSENEVDQLVAVEALIHASTKLSRASFIITNGVSLLKDIYKKTKNEKIKIRAL
SQ  VGLCKLGSAGGTDYALRQFAEGSTDKLAKQCRKWLCNPSLDIQTRKWAVEGLAYLTLDADVKDEFVEDEQSLKAMFELSK
SQ  TSDKTILYSVATTLVNCTNSYDVKEVIPEMVQLAKFSKQHVPEQHPKDKKDFVEKRVKRLLKADVISALSCMVKADNSIL
SQ  TDQTKEQLSRVFLALCEDPKDRGIIVAQGGGKAMIPLALEGTDVGKIKASHGLAKIAAVSNPDIAFPGERVYEVVRPLVS
SQ  LLNTERDGIQNFEALLALTNLSGKNDKLRQKIIKEKALPEIENYMFENHEQIRQAATECMCNLALNKEVKERFMAEGNDR
SQ  LKLIILLCGEEDEVKLQRAAAGTLAMLTGAEKKLCHKMTEVTTQWMEILQRLCLSEDLQVQHRGVVIAYNLINADKELAK
SQ  KLVESEMLEILTVIGKQADVPNKQHIINAAREALVKCLDYGFIKTVS
//
ID  Q6DKM1;
PN  Protein unc-50 homolog A;
GN  unc50;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:O55227}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O55227}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q53HI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53HI1}.
DR  UNIPROT: Q6DKM1;
DR  Pfam: PF05216;
DE  Function: Involved in the cell surface expression of neuronal nicotinic receptors (By similarity). Binds RNA (By similarity). {ECO:0000250|UniProtKB:O55227}.
DE  Reference Proteome: Yes;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0003723;
GO  GO:0034394;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLPTTSVSPRSPDNGILSPREAARHTAGAKRYKYLRRLFHFKQMDFEFALWQMLYLFTSPQKVYRNFHYRKQTKDQWARD
SQ  DPAFLVLLSIWLCVSTVGFGFVLDMSFFETFKLLLWVVFIDCVGVGLLIATLMWFVSNKYMVKRQGKDYDVEWGYTFDVH
SQ  LNAFYPLLVILHFIQLFFINHVILSGWFIGYFVGNTIWLIAIGYYIYITFLGYSALPFLKNTVILLYPFAALALLYVLSL
SQ  ALGWNFTEKLCLFYKYRVR
//
ID  Q5U520;
PN  Protein unc-50 homolog B;
GN  unc50;
OS  8355;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:O55227}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O55227}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q53HI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53HI1}.
DR  UNIPROT: Q5U520;
DR  Pfam: PF05216;
DE  Function: Involved in the cell surface expression of neuronal nicotinic receptors (By similarity). Binds RNA (By similarity). {ECO:0000250|UniProtKB:O55227}.
DE  Reference Proteome: Yes;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0005637;
GO  GO:0003723;
GO  GO:0034394;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLPTTSVSPRSPDNGILSPRDATRHTAGAKRYKYLRRLFHFKQMDFEFALWQMLYLFTSPQKVYRNFHYRKQTKDQWARD
SQ  DPAFLVLLGIWLCVSTVGFGFVLDMSFFETFTLLLWVVFIDCVGVGLLIATSMWFVSNKYMVNRQGKDYDVEWGYTFDVH
SQ  LNAFYPLLVILHFIQLFFINHVILTGWFIGCFVGNTLWLIAIGYYIYITFLGYSALPFLKNTVVLLYPFAALALLYILSL
SQ  ALGWNFTAKLCLFYKYRVR
//
ID  Q3ZBG6;
PN  Protein unc-50 homolog;
GN  UNC50;
OS  9913;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:O55227}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O55227}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q53HI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53HI1}.
DR  UNIPROT: Q3ZBG6;
DR  UNIPROT: Q5E989;
DR  Pfam: PF05216;
DE  Function: Involved in the cell surface expression of neuronal nicotinic receptors (By similarity). Binds RNA (By similarity). {ECO:0000250|UniProtKB:O55227}.
DE  Reference Proteome: Yes;
GO  GO:0030173;
GO  GO:0005637;
GO  GO:0003723;
GO  GO:0034394;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLPSTSVNSPAQGNGVLSSRDAARHTAGAKRYKYLRRLFRFRQMDFEFAAWQMLYLFTSPQRVYRNFHYRKQTKDQWARD
SQ  DPAFLVLLSIWLCVSTIGFGFVLDMGFFETIKLLLWVVFIDCVGVGLLISTLMWFISNKYLVKRQSRDYDVEWGYAFDVH
SQ  LNAFYPLLVILHFIQLFFINHVILTDTFIGYLVGNTLWLVAVGYYIYVTFLGYSALPFLKNTVILLYPFAPLILLYGLSL
SQ  ALGWNFTHTLCSFYKYRVK
//
ID  Q7ZUU1;
PN  Protein unc-50 homolog;
GN  unc50;
OS  7955;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:O55227}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O55227}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q53HI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53HI1}.
DR  UNIPROT: Q7ZUU1;
DR  Pfam: PF05216;
DE  Function: Involved in the cell surface expression of neuronal nicotinic receptors (By similarity). Binds RNA (By similarity). {ECO:0000250|UniProtKB:O55227}.
DE  Reference Proteome: Yes;
GO  GO:0030173;
GO  GO:0005637;
GO  GO:0003723;
GO  GO:0034394;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLPTSSPQIHRNGSLSERDAARHTAGAKRYKYLRRLLHFRQMDFEFAVWQMLYLFTSPQKVYRNFHYRKQTKDQWARDDP
SQ  AFLVLLSIWLCVSTVGFGLVLDMGFVETLTLLLWVVFIDCIGVGLLISTLMWFVTNKYLMKHPNRDYDVEWGYAFDVHLN
SQ  AFYPLLVILHFLQLFFINHVVVISSDWFLGYFVGNTMWLIAIGYYVYITFLGYSALPFLKNTVVLLYPFALLGLLYVLSI
SQ  SLGWNFTKGLCWFYKHRVQ
//
ID  Q53HI1;
PN  Protein unc-50 homolog;
GN  UNC50;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:O55227}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O55227}. Golgi apparatus membrane {ECO:0000269|PubMed:12808035}; Multi-pass membrane protein {ECO:0000269|PubMed:12808035}.
DR  UNIPROT: Q53HI1;
DR  UNIPROT: D3DVH4;
DR  UNIPROT: Q53S98;
DR  UNIPROT: Q53TD6;
DR  UNIPROT: Q5U5U2;
DR  UNIPROT: Q6X7B9;
DR  UNIPROT: Q9UQF4;
DR  UNIPROT: Q9Y4S6;
DR  Pfam: PF05216;
DR  OMIM: 617826;
DR  DisGeNET: 25972;
DE  Function: Involved in the cell surface expression of neuronal nicotinic receptors (By similarity). Binds RNA (By similarity). {ECO:0000250|UniProtKB:O55227}.
DE  Reference Proteome: Yes;
DE  Interaction: Q15125; IntAct: EBI-23922913; Score: 0.56
DE  Interaction: P47102; IntAct: EBI-7601754; Score: 0.37
DE  Interaction: O43889; IntAct: EBI-8647641; Score: 0.55
DE  Interaction: P05214; IntAct: EBI-10992821; Score: 0.35
DE  Interaction: Q96N21; IntAct: EBI-11139757; Score: 0.35
DE  Interaction: Q9GZY8; IntAct: EBI-24312848; Score: 0.56
DE  Interaction: Q8IUN9; IntAct: EBI-24623370; Score: 0.56
DE  Interaction: Q9NR31; IntAct: EBI-24661428; Score: 0.56
DE  Interaction: Q7Z5P4; IntAct: EBI-23694082; Score: 0.56
DE  Interaction: Q9Y282; IntAct: EBI-24676607; Score: 0.56
DE  Interaction: Q9H2K0; IntAct: EBI-23703501; Score: 0.56
DE  Interaction: O14880; IntAct: EBI-24689376; Score: 0.56
DE  Interaction: Q5SR56; IntAct: EBI-24705233; Score: 0.56
DE  Interaction: Q8N6M3; IntAct: EBI-24710182; Score: 0.56
DE  Interaction: Q8TED1; IntAct: EBI-23762119; Score: 0.56
DE  Interaction: Q8TDT2; IntAct: EBI-24713756; Score: 0.56
DE  Interaction: P48051; IntAct: EBI-24716932; Score: 0.56
DE  Interaction: Q14973; IntAct: EBI-24719889; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-24731178; Score: 0.56
DE  Interaction: Q9NRX6; IntAct: EBI-24742634; Score: 0.56
DE  Interaction: Q3KNW5; IntAct: EBI-24747464; Score: 0.56
DE  Interaction: Q8NBQ5; IntAct: EBI-24750500; Score: 0.56
DE  Interaction: Q9H6H4; IntAct: EBI-24770276; Score: 0.56
DE  Interaction: P38484; IntAct: EBI-24782805; Score: 0.56
DE  Interaction: Q8WY98; IntAct: EBI-24793740; Score: 0.56
DE  Interaction: Q9GZR5; IntAct: EBI-24797356; Score: 0.56
DE  Interaction: O95470; IntAct: EBI-23908976; Score: 0.56
DE  Interaction: Q6PL24; IntAct: EBI-24545316; Score: 0.56
DE  Interaction: Q5JX71; IntAct: EBI-24651712; Score: 0.56
DE  Interaction: O15552; IntAct: EBI-25189572; Score: 0.56
DE  Interaction: P15941; IntAct: EBI-24803639; Score: 0.56
DE  Interaction: Q6PI48; IntAct: EBI-25221026; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-25227998; Score: 0.56
DE  Interaction: P58418; IntAct: EBI-25272729; Score: 0.56
DE  Interaction: P0DTC5; IntAct: EBI-25685699; Score: 0.35
GO  GO:0030173;
GO  GO:0005637;
GO  GO:0003723;
GO  GO:0034394;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLPSTSVNSLVQGNGVLNSRDAARHTAGAKRYKYLRRLFRFRQMDFEFAAWQMLYLFTSPQRVYRNFHYRKQTKDQWARD
SQ  DPAFLVLLSIWLCVSTIGFGFVLDMGFFETIKLLLWVVLIDCVGVGLLIATLMWFISNKYLVKRQSRDYDVEWGYAFDVH
SQ  LNAFYPLLVILHFIQLFFINHVILTDTFIGYLVGNTLWLVAVGYYIYVTFLGYSALPFLKNTVILLYPFAPLILLYGLSL
SQ  ALGWNFTHTLCSFYKYRVK
//
ID  Q9CQ61;
PN  Protein unc-50 homolog;
GN  Unc50;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000250|UniProtKB:O55227}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O55227}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q53HI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53HI1}.
DR  UNIPROT: Q9CQ61;
DR  Pfam: PF05216;
DE  Function: Involved in the cell surface expression of neuronal nicotinic receptors (By similarity). Binds RNA (By similarity). {ECO:0000250|UniProtKB:O55227}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0030173;
GO  GO:0005637;
GO  GO:0003723;
GO  GO:0034394;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLPSTSLSSSMHGNGVLNSRDAARHTAGAKRYKYLRRLFRFRQMDFEFAAWQMLYLFTSPQRVYRNFHYRKQTKDQWARD
SQ  DPAFLVLLSIWLCVSTIGFGFVLDMGFFETIKLLLWVVFIDCVGVGLLISTLMWFVSNKYLVKRQSRDYDVEWGYAFDVH
SQ  LNAFYPLLVILHFIQLFFINHVILTDTFIGYLVGNTLWLIAVGYYIYVTFLGYSALPFLKNTVILLYPFAPLMVLYGLSL
SQ  ALGWNFTHTLCSFYKYRVK
//
ID  O55227;
PN  Protein unc-50 homolog;
GN  Unc50;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:10980252}; Multi-pass membrane protein {ECO:0000269|PubMed:10980252}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q53HI1}; Multi-pass membrane protein {ECO:0000250}.
DR  UNIPROT: O55227;
DR  Pfam: PF05216;
DE  Function: Involved in the cell surface expression of neuronal nicotinic receptors (PubMed:10980252). Binds RNA (PubMed:10980252). {ECO:0000269|PubMed:10980252}.
DE  Reference Proteome: Yes;
GO  GO:0005794;
GO  GO:0030173;
GO  GO:0005637;
GO  GO:0003723;
GO  GO:0034394;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MLPSTSLNSSMYGNGALNSRDAARHTAGAKRYKYLRRLFRFRQMDFEFAAWQMLYLFTSPQRVYRNFHYRKQTKDQWARD
SQ  DPAFLVLLSIWLCVSTIGFGFVLDMGFFETIKLLLWVVFIDCVGVGLLISTLMWFISNKYLVKRQSRDYDVEWGYAFDVH
SQ  LNAFYPLLVILHFIQLFFINHVILTDTFIGYLVGNTLWLIAVGYYIYVTFLGYSALPFLKNTVVLLYPFAPLIVLYGLSL
SQ  ALGWNFTHTLCSFYKYRVK
//
ID  Q23064;
PN  Nuclear migration protein unc-83;
GN  unc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:19605495, ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:27697906, ECO:0000305|PubMed:21411627}; Single-pass type IV membrane protein {ECO:0000305}. Nucleus outer membrane {ECO:0000269|PubMed:16481402}; Single-pass type IV membrane protein {ECO:0000305}. Note=The transmembrane domain associates with the nuclear envelope (PubMed:11748140). Co-localizes with unc-84 and lmn-1 at the nuclear envelope (PubMed:11748140). {ECO:0000269|PubMed:11748140}.
DR  UNIPROT: Q23064;
DR  UNIPROT: Q95WB6;
DE  Function: Cargo-specific adapter that is involved in nuclear migration during development and thereafter (PubMed:11748140, PubMed:19605495, PubMed:20005871, PubMed:20921138, PubMed:27697906). Component of the unc-83-unc-84 LINC (LInker of Nucleoskeleton and Cytoskeleton) complex where it interacts with unc-84 to form a bridge connecting the nuclear envelope to the cytoskeleton which allows for nuclear transport along microtubules (PubMed:11748140, PubMed:16481402, PubMed:25023515). Within the complex, connects the nuclear envelope to the microtubule cytoskeleton through the kinesin-1 light chain protein klc-2 (most likely within the Kinesin 1 motor complex) to regulate nuclear migrations (PubMed:19605495, PubMed:20921138). Moreover, within the complex, also recruits the large microtubule-associated bicd-1-dlc-1- egal-1 and lis-1-nud-2 complexes to the nuclear envelope to regulate both the bidirectional migration of nuclei and the extent of nuclear migrations (PubMed:20005871). Not required for centrosome attachment to the nucleus (PubMed:11748140). {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:16481402, ECO:0000269|PubMed:19605495, ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:20921138, ECO:0000269|PubMed:25023515, ECO:0000269|PubMed:27697906}.
DE  Reference Proteome: Yes;
DE  Interaction: O45717; IntAct: EBI-2905337; Score: 0.60
DE  Interaction: P46822; IntAct: EBI-2904924; Score: 0.00
DE  Interaction: Q20745; IntAct: EBI-3884847; Score: 0.37
DE  Interaction: Q22799; IntAct: EBI-2905315; Score: 0.53
DE  Interaction: V6CJ04; IntAct: EBI-2905267; Score: 0.51
DE  Interaction: Q95QA6; IntAct: EBI-2905042; Score: 0.00
DE  Interaction: P10567; IntAct: EBI-2905052; Score: 0.00
DE  Interaction: Q94420; IntAct: EBI-2905058; Score: 0.00
DE  Interaction: G5ECD7; IntAct: EBI-2905066; Score: 0.00
DE  Interaction: H2KZ24; IntAct: EBI-2905073; Score: 0.00
DE  Interaction: P34397; IntAct: EBI-2905144; Score: 0.00
DE  Interaction: O76640; IntAct: EBI-2905160; Score: 0.00
DE  Interaction: H2KYJ3; IntAct: EBI-2905178; Score: 0.00
DE  Interaction: P34420; IntAct: EBI-2905187; Score: 0.00
DE  Interaction: Q5FC73; IntAct: EBI-2905241; Score: 0.00
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005640;
GO  GO:0045503;
GO  GO:0040011;
GO  GO:0007399;
GO  GO:0007097;
GO  GO:0030473;
GO  GO:0018991;
GO  GO:0009791;
GO  GO:0090435;
GO  GO:0030334;
GO  GO:0040025;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDVMDSFSEVEMPNDISSEDHLLKVIESSAEEVDIFLENCSSLYNLILDSLHNLTSKTISCECLDEMTSTLEKSAKKILA
SQ  ERPEAENSVLLRLNTICCAMDQLRVQHNSRMMSGADSDTASSARSSTSSSTGEMRLWLHEVERRLEINEKRIRVEPNLQL
SQ  LLSDQQALQLEIQHEGQLLVNRLNKQIKDDHDSDSSEEEKRKTCVDAIRKRWHTIYLNSLSLVCRIEELINHQQASEDSE
SQ  SDPDLVGPPIKRARIRTVGHLTASDTEESEADEEDRHSQTETVVTEDDNVLPFAENEYESIMDGRVTVDSCTSSSEDQMV
SQ  EQSTNKKWESVLQDVGYSSGENSIHEALNTCADHLVPETSDMRRKRIECSPVKAFYRTVQLEDMSDLEVTKAINHDVEEE
SQ  PNLSDSMYVNHDSTFLATQNLPEYDEVMALMDDDDLPMDMSMTESFNTKWREIHGQKKPLRRASRPSREQMNLIAKSSCD
SQ  ASSEDSSEGENQTNLEDDPEMMSVSFNSAQFDTSSPLKRQRSARGLKNASFLYDSLEMDGSFCSTRSEMLPPCKTRSLAR
SQ  RKLRVRRMPRSMSDGEQLGVVSSKPEGMMTPMIRVSPPSTPVRRLLRKLDEQIRNRDSDTAPEHSDAAQAYEWDEYNPPQ
SQ  KDDSISDRHIQTMTDISDQLMNIDDDFAEHFGTSSAIRLIEESKSHLRVVLKALEESDSNIPQLSNFELIARSNLRQVDE
SQ  ALKIQSGNQPSFLETSTLQDLRSEWANLYESIRSPFARIMHQVKKFAATLQEVSSMASLGDVDIRSKEDVAKTLDAVTAI
SQ  ERRLSSERQELRDLLASSSFRDVAKDLSCEFESVSEGYDDAVDKIGKMAHSLSQVKGEWDAWNSRQNDIRNAMVRIESHL
SQ  KEGQMDNKMIADEMELCQERMNSLETMCNYLTASLGSIQNESNSKNLPDFKAELSIYSNALARLKDRFNDMIRVPTPPTV
SQ  QFHPPEPLPSLARSMTTQTAEMESETENEPLTIAEAISSSRLIKFTFALSLLAALAAIFYYHVFGKPFGPHVTYVNGPPP
SQ  V
//
ID  Q20745;
PN  Nuclear migration and anchoring protein unc-84;
GN  unc;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:10375507, ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:16481402, ECO:0000269|PubMed:27956467, ECO:0000305|PubMed:21411627}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}. Note=Associated with nuclei during interphase, prophase, prometaphase, metaphase and early anaphase (PubMed:11907270). Released from nuclear membrane in the same time that the nuclear envelope disassembly, during late anaphase, and begins to reaccumulate in early telophase (PubMed:11907270). Localization at the nuclear envelope depends on lmn-1 (PubMed:11748140, PubMed:11907270). Co-localizes with unc-83 at the nuclear envelope, but its localization at the nuclear envelope does not depend on unc-83 (PubMed:11748140, PubMed:11907270). {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270}.
DR  UNIPROT: Q20745;
DR  UNIPROT: Q9U475;
DR  UNIPROT: Q9U476;
DR  Pfam: PF07738;
DR  PROSITE: PS51469;
DE  Function: Involved in nuclear migration and anchoring in hypodermal precursor cells (PubMed:10375507, PubMed:11748140, PubMed:12169658, PubMed:11907270, PubMed:16481402, PubMed:20921138, PubMed:21411627, PubMed:23150597, PubMed:25023515, PubMed:25057012). Most likely recruits anc-1 to the nuclear envelope where anc-1 functions to tether the nucleus to the actin cytoskeleton (PubMed:12169658). Component of the unc-83-unc-84 LINC (LInker of Nucleoskeleton and Cytoskeleton) complex where it recruits and interacts with unc-83 to form a bridge connecting the nuclear envelope to the cytoskeleton which allows for nuclear transport along microtubules (PubMed:11748140, PubMed:16481402). Its role in nuclear migration may be in association with lamin, lmn-1 (PubMed:25057012). Regulates nuclear migrations in one-cell embryos, controlling the posterior migration of the male pronucleus following fertilization (PubMed:21798253). Not required for centrosome attachment to the nucleus (PubMed:10375507, PubMed:11907270). Plays a role in the maintenance of the nuclear envelope architecture in body wall muscle cells (PubMed:25023515). May be involved in DNA damage repair through an association with zyg-12 (PubMed:27956467). Potentially has roles in homologous recombination, double strand break repair and meiotic recombination (PubMed:27956467). Specifically, may in part inhibit non-homologous end joining repair, most likely through recruiting fan-1 to the nucleoplasm, to facilitate the repair of DNA cross-links (PubMed:27956467). {ECO:0000269|PubMed:10375507, ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:12169658, ECO:0000269|PubMed:16481402, ECO:0000269|PubMed:20921138, ECO:0000269|PubMed:21411627, ECO:0000269|PubMed:21798253, ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25023515, ECO:0000269|PubMed:25057012, ECO:0000269|PubMed:27956467}.
DE  Reference Proteome: Yes;
DE  Interaction: P90740; IntAct: EBI-333119; Score: 0.00
DE  Interaction: G5EFL5; IntAct: EBI-341426; Score: 0.00
DE  Interaction: O45904; IntAct: EBI-343574; Score: 0.00
DE  Interaction: Q23064; IntAct: EBI-3884847; Score: 0.37
DE  Interaction: P34258; IntAct: EBI-6532488; Score: 0.37
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0016021;
GO  GO:0005639;
GO  GO:0034993;
GO  GO:0016020;
GO  GO:0005635;
GO  GO:0005637;
GO  GO:0005521;
GO  GO:0043495;
GO  GO:0040011;
GO  GO:0007399;
GO  GO:0006998;
GO  GO:0007097;
GO  GO:0030473;
GO  GO:0018991;
GO  GO:0009791;
GO  GO:0030334;
GO  GO:0040025;
TP  Membrane Topology: Transmembrane; Source: UniProt - Curator Inference {ECO:0000305|PubMed:21411627};
SQ  MAPATEADNNFDTHEWKSEFASTRSGRNSPNIFAKVRRKLLLTPPVRNARSPRLTEEELDALTGDLPYATNYTYAYSKIY
SQ  DPSLPDHWEVPNLGGTTSGSLSEQEHWSAASLSRQLLYILRFPVYLVLHVITYILEAFYHVIKITSFTIWDYLLYLVKLA
SQ  KTRYYAYQDHRRRTALIRNRQEPFSTKAARSIRRFFEILVYVVLTPYRMLTRSNNGVEQYQYRSIKDQLENERASRMTTR
SQ  SQTLERSRKFDGLSKSPARRAAPAFVKTSTITRITAKVFSSSPFGEGTSENITPTVVTTRTVKQRSVTPRFRQTRATREA
SQ  ITRALDTPELEIDTPLSTYGLRSRGLSHLNTPEPTFDIGHAAATSTPLFPQETYNYQYEEATGNKIKTAFTWLGYLILFP
SQ  FFAARHVWYTFYDYGKSAYMKLTNYQQAPMETIHVRDINEPAPSSSDVHDAVGVSWRIRIADFLSSFVATIVEAHQVVFA
SQ  MFKGGIVETVSYFGGLFAGLTDKKSSKFSWCQILGLLLALLFAIFLLGFLTSDNTAIRVKEITKDKNASKKSEGSLPAVP
SQ  IWISAANHVKHYTWMVKEFVVDIAFDTYNYGKSTIGRLGTTPRYAWDLIASGCGAVGNGLKSVLSSSFRFIDFCAGKLFY
SQ  YGSDGFLSANKSIGTFFNGCYETLYNGCTAIVGHTKSFIYNASNAVYNFFSTIFAGLLNFSTSSQNSILSLLKSFGTGIT
SQ  NIFYNFIYAPIAGVFNFAGDNYMYFFNEVAAVFGKVYNSVVSVLKTVINWILFLIAYPFSLCTRAWIRISQYAPEDVVQV
SQ  IPIPQAITPTPDVERIVEEPLRKVTDVEDEELVIIPAPAPKPIPVPAPTPAPVIIHQTNVVETVDKDAIIKEVTEKLRAE
SQ  LSAQFQQELSAKFEQNYNTIIEQLKMENTNIQYDKNHLEAIIRQMIYEYDTDKTGKVDYALESSGGAVVSTRCSETYKSY
SQ  TRLEKFWDIPIYYFHYSPRVVIQRNSKSLFPGECWCFKESRGYIAVELSHFIDVSSISYEHIGSEVAPEGNRSSAPKGVL
SQ  VWAYKQIDDLNSRVLIGDYTYDLDGPPLQFFLAKHKPDFPVKFVELEVTSNYGAPFTCLYRLRVHGKVVQV
//
ID  Q12063;
PN  Dehydrodolichyl diphosphate synthase complex subunit NUS1;
GN  NUS1;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:11086160, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14690591}. Nucleus membrane {ECO:0000269|PubMed:14690591}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q12063;
DR  UNIPROT: D6VRG0;
DR  PDB: 6JCN;
DE  Function: With SRT1 or RER2, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). {ECO:0000269|PubMed:25066056}.
DE  Reference Proteome: Yes;
DE  Interaction: P40069; IntAct: EBI-16287555; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-708615; Score: 0.56
DE  Interaction: P02829; IntAct: EBI-708618; Score: 0.40
DE  Interaction: P32589; IntAct: EBI-3727462; Score: 0.35
DE  Interaction: Q04432; IntAct: EBI-3830702; Score: 0.35
DE  Interaction: P53239; IntAct: EBI-16256836; Score: 0.00
DE  Interaction: P60010; IntAct: EBI-16287555; Score: 0.35
DE  Interaction: P05030; IntAct: EBI-16287555; Score: 0.35
DE  Interaction: P46970; IntAct: EBI-16287555; Score: 0.35
DE  Interaction: P15992; IntAct: EBI-16287555; Score: 0.35
DE  Interaction: P32836; IntAct: EBI-16287555; Score: 0.35
DE  Interaction: P32835; IntAct: EBI-16287555; Score: 0.35
DE  Interaction: P00950; IntAct: EBI-16287555; Score: 0.35
DE  Interaction: P33892; IntAct: EBI-16287555; Score: 0.35
DE  Interaction: P00830; IntAct: EBI-16287555; Score: 0.35
GO  GO:1904423;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005811;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0016765;
GO  GO:0019408;
GO  GO:0006486;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPTMIKKDDKAMEPPNEKPHRKIERDDVPESSNHIPPPESGVLKGGKVNSKTRALKAVTSIIADADENPQKKVNNETNGV
SQ  QKQKTEDLSKRIGKFEYLFYKFLLVLLYICFGLFRYGQYQYNKMKLRIFSIIYNHAYTPQLIRQDVIPLKKIPKRLAAIL
SQ  EVKPVGDVGGGVTGLLNDASEIVCWTVSAGIKHLMLYDYDGILQRNVPELRMEIHSNLAKYFGPAHVPNYAVKIPHSNKI
SQ  FYNLDGIETETDVGNEIEANQEKDKIAIEISLLSNRDGRETIVDLTKTMAELCAVNELSVSDITMDLVDSELKQLVGPEP
SQ  DLLLYFGPSLDLQGFPPWHIRLTEFYWEKDNNEVIYSVFIRGLRQYAGCKVNVGK
//
ID  Q6TVP7;
PN  Protein ORFV073;
GN  V073;
OS  647330;
SL  Nucleus Position: SL-0382;
SL  Comments: Host nucleus {ECO:0000269|PubMed:28787456}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:28787456}. Virion {ECO:0000269|PubMed:28787456}.
DR  UNIPROT: Q6TVP7;
DE  Function: Plays a role in the inhibition of the host NF-kappa-B pathway early during infection. Prevents the host RELA subunit from reaching the nucleus and activate transcription. {ECO:0000269|PubMed:28787456}.
DE  Reference Proteome: Yes;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0044423;
GO  GO:0039644;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MARRARFSPRLHIPAARAALGPHLHFPRRRLVLRHCGVRAFVGDAIVSKKEMTNPLCAQAIVFGNGFVETYVRSLDPRLL
SQ  GAYHALSRPVCERPLFAVRGWRRLFPIVARRLDAVERRTRRVLRSMCRTYTTCMSADRAAAVSHPVMRRRWFGHRATKTR
SQ  RARLRRRCRNRSSKRRAERRKRFCNYCP
//
ID  Q9P0L0;
PN  Vesicle-associated membrane protein-associated protein A;
GN  VAPA;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10523508, ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:19289470, ECO:0000269|PubMed:25447204, ECO:0000269|PubMed:30741634}; Single-pass type IV membrane protein {ECO:0000269|PubMed:10523508, ECO:0000269|PubMed:19289470}. Cell membrane {ECO:0000269|PubMed:25447204}; Single-pass type IV membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000269|PubMed:10523508}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Z270}. Note=Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells. {ECO:0000269|PubMed:10523508}.
DR  UNIPROT: Q9P0L0;
DR  UNIPROT: A6NDZ0;
DR  UNIPROT: D3DUI3;
DR  UNIPROT: O75453;
DR  UNIPROT: Q5U0E7;
DR  UNIPROT: Q9UBZ2;
DR  PDB: 2RR3;
DR  PDB: 6TQR;
DR  Pfam: PF00635;
DR  PROSITE: PS50202;
DR  OMIM: 605703;
DR  DisGeNET: 9218;
DE  Function: Binds to OSBPL3, which mediates recruitment of VAPA to plasma membrane sites (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:25447204). With OSBPL3, may regulate ER morphology (PubMed:16143324). May play a role in vesicle trafficking (PubMed:11511104, PubMed:19289470). {ECO:0000269|PubMed:11511104, ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:19289470, ECO:0000269|PubMed:25447204}.
DE  Reference Proteome: Yes;
DE  Interaction: O15173; IntAct: EBI-24691023; Score: 0.56
DE  Interaction: P00533; IntAct: EBI-4397828; Score: 0.71
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P03246; IntAct: EBI-11722343; Score: 0.35
DE  Interaction: P04626; IntAct: EBI-8770853; Score: 0.55
DE  Interaction: P16278; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P22059; IntAct: EBI-11120309; Score: 0.74
DE  Interaction: P27958; IntAct: EBI-8849923; Score: 0.78
DE  Interaction: Q03463; IntAct: EBI-8803422; Score: 0.67
DE  Interaction: Q07065; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q15125; IntAct: EBI-24733627; Score: 0.56
DE  Interaction: Q5JSH3; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q6ULP2; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q8TEY7; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q8WXH0; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q8WYP5; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q99IB8; IntAct: EBI-8784130; Score: 0.56
DE  Interaction: Q9BTV4; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9BZF3; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9H4L5; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9NWT6; IntAct: EBI-12502476; Score: 0.35
DE  Interaction: P01889; IntAct: EBI-1077173; Score: 0.00
DE  Interaction: Q9Y2K6; IntAct: EBI-2512022; Score: 0.40
DE  Interaction: Q96SU4; IntAct: EBI-2514776; Score: 0.40
DE  Interaction: Q99MK9; IntAct: EBI-2556403; Score: 0.56
DE  Interaction: A0A6L7GZ58; IntAct: EBI-2812120; Score: 0.00
DE  Interaction: Q81VJ7; IntAct: EBI-2813855; Score: 0.00
DE  Interaction: Q81TU4; IntAct: EBI-2819380; Score: 0.00
DE  Interaction: Q81VT8; IntAct: EBI-2819368; Score: 0.00
DE  Interaction: A0A6L8PDJ5; IntAct: EBI-2819418; Score: 0.00
DE  Interaction: A0A0F7RGR7; IntAct: EBI-2819399; Score: 0.00
DE  Interaction: A0A6L7HCN1; IntAct: EBI-2819425; Score: 0.00
DE  Interaction: A0A6L8PK55; IntAct: EBI-2819406; Score: 0.00
DE  Interaction: A0A6L7HG64; IntAct: EBI-2819387; Score: 0.00
DE  Interaction: A0A6L8NZ61; IntAct: EBI-2819455; Score: 0.00
DE  Interaction: A0A6L8NYR0; IntAct: EBI-2819437; Score: 0.00
DE  Interaction: Q81JE0; IntAct: EBI-2819468; Score: 0.00
DE  Interaction: A0A4Y1W7L5; IntAct: EBI-2819444; Score: 0.00
DE  Interaction: Q8CZU2; IntAct: EBI-2843966; Score: 0.00
DE  Interaction: Q0WAZ5; IntAct: EBI-2850711; Score: 0.00
DE  Interaction: Q8D1S0; IntAct: EBI-2850699; Score: 0.00
DE  Interaction: A0A2U2GZH9; IntAct: EBI-2850718; Score: 0.00
DE  Interaction: Q5T4F4; IntAct: EBI-3894106; Score: 0.57
DE  Interaction: Q96TC7; IntAct: EBI-7415741; Score: 0.55
DE  Interaction: P15336; IntAct: EBI-5529812; Score: 0.35
DE  Interaction: P04578; IntAct: EBI-6176669; Score: 0.46
DE  Interaction: P19320; IntAct: EBI-6191076; Score: 0.53
DE  Interaction: P17612; IntAct: EBI-6255618; Score: 0.53
DE  Interaction: P22694; IntAct: EBI-6255866; Score: 0.53
DE  Interaction: Q13188; IntAct: EBI-6256382; Score: 0.53
DE  Interaction: Q77M19; IntAct: EBI-6270503; Score: 0.35
DE  Interaction: P02751; IntAct: EBI-6285956; Score: 0.35
DE  Interaction: Q13043; IntAct: EBI-6911839; Score: 0.35
DE  Interaction: Q86WH2; IntAct: EBI-6912050; Score: 0.35
DE  Interaction: P35372; IntAct: EBI-6918974; Score: 0.68
DE  Interaction: P32300; IntAct: EBI-6926064; Score: 0.40
DE  Interaction: P41145; IntAct: EBI-6926066; Score: 0.40
DE  Interaction: Q6PEC3; IntAct: EBI-8804473; Score: 0.46
DE  Interaction: O95070; IntAct: EBI-8850242; Score: 0.60
DE  Interaction: O95292; IntAct: EBI-8840764; Score: 0.56
DE  Interaction: Q9P035; IntAct: EBI-9083284; Score: 0.40
DE  Interaction: Q99614; IntAct: EBI-9395686; Score: 0.53
DE  Interaction: O95772; IntAct: EBI-9819574; Score: 0.46
DE  Interaction: Q14849; IntAct: EBI-9819322; Score: 0.52
DE  Interaction: P19838; IntAct: EBI-11322417; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11323169; Score: 0.35
DE  Interaction: P03182; IntAct: EBI-11721938; Score: 0.35
DE  Interaction: P06460; IntAct: EBI-11723082; Score: 0.35
DE  Interaction: P06792; IntAct: EBI-11724527; Score: 0.35
DE  Interaction: P0C739; IntAct: EBI-11725101; Score: 0.35
DE  Interaction: P69901; IntAct: EBI-11733364; Score: 0.35
DE  Interaction: A2AUM9; IntAct: EBI-10994361; Score: 0.35
DE  Interaction: Q3UJU9; IntAct: EBI-11021410; Score: 0.35
DE  Interaction: P60710; IntAct: EBI-11045267; Score: 0.35
DE  Interaction: O95786; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P10644; IntAct: EBI-11120309; Score: 0.53
DE  Interaction: Q969M3; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q96BQ5; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q8N4V1; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P47985; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9ULH0; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P35232; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q5T8D3; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9UBQ5; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: K7EJC8; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q6NZI2; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P28331; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9HCK4; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O95182; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O14653; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P35610; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q8NE86; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O00461; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P21796; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O75306; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P56181; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q13445; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P10606; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O00562; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O43678; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9BZ71; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9BXB5; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9NRZ9; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9NX63; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O94905; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O75477; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9UBD5; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O75348; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P21281; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q14254; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q8NC06; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O14880; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P45880; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q8N1G2; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: B7ZAQ6; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O75381; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P09669; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q8TEW0; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q03135; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9BXB4; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O95168; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O43920; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P53007; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q92604; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q92508; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9H089; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9UBH6; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q16891; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O95169; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q969G5; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9Y2H6; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q16795; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: B4E2V5; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q99519; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9Y6K0; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q8TBE9; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O75746; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q14573; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P19404; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P14854; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q8TCJ2; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q8NBU5; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P10619; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9P0J0; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: H0YLN8; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O43181; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9BZ72; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9BQB6; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O95159; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q14318; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P28288; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: C9J0K6; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P61421; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P38606; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9UJZ1; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: E9PPW7; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q7Z6K3; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q04446; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O75410; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O95299; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9NZN5; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P31930; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: C9JKI3; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P56556; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9NX14; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P49821; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q96N66; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q16718; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P33897; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q08380; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9BRQ6; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: P51532; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O75380; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O75955; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q9UI09; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: O15260; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q03518; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q5SVZ6; IntAct: EBI-11120309; Score: 0.35
DE  Interaction: Q15006; IntAct: EBI-11130215; Score: 0.35
DE  Interaction: Q5T3F8; IntAct: EBI-11155257; Score: 0.35
DE  Interaction: Q9Y3E0; IntAct: EBI-11161387; Score: 0.35
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q9QXM1; IntAct: EBI-11475522; Score: 0.35
DE  Interaction: Q4G0X9; IntAct: EBI-12449318; Score: 0.35
DE  Interaction: P61006; IntAct: EBI-11832855; Score: 0.35
DE  Interaction: P05090; IntAct: EBI-24368883; Score: 0.72
DE  Interaction: Q96K78; IntAct: EBI-24499429; Score: 0.56
DE  Interaction: O00559; IntAct: EBI-24699966; Score: 0.56
DE  Interaction: Q9Y320; IntAct: EBI-24703968; Score: 0.56
DE  Interaction: Q8N661; IntAct: EBI-24705292; Score: 0.56
DE  Interaction: Q8N5M9; IntAct: EBI-24706911; Score: 0.56
DE  Interaction: P78383; IntAct: EBI-24709430; Score: 0.56
DE  Interaction: O60669; IntAct: EBI-23766238; Score: 0.56
DE  Interaction: Q53TN4; IntAct: EBI-24718559; Score: 0.56
DE  Interaction: P49447; IntAct: EBI-24723641; Score: 0.56
DE  Interaction: Q7Z5P4; IntAct: EBI-24742483; Score: 0.56
DE  Interaction: P11912; IntAct: EBI-24752923; Score: 0.56
DE  Interaction: Q8NBD8; IntAct: EBI-24764619; Score: 0.56
DE  Interaction: Q8NBQ5; IntAct: EBI-24786679; Score: 0.56
DE  Interaction: Q9BY50; IntAct: EBI-24795986; Score: 0.56
DE  Interaction: O15209; IntAct: EBI-24417267; Score: 0.56
DE  Interaction: Q06432; IntAct: EBI-24260483; Score: 0.56
DE  Interaction: Q96LZ7; IntAct: EBI-24471737; Score: 0.56
DE  Interaction: Q9NS71; IntAct: EBI-24541663; Score: 0.56
DE  Interaction: A0A024R8A9; IntAct: EBI-24560517; Score: 0.56
DE  Interaction: O95214; IntAct: EBI-24641938; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-24643376; Score: 0.56
DE  Interaction: Q9NY72; IntAct: EBI-24648989; Score: 0.56
DE  Interaction: Q53FP2; IntAct: EBI-24805194; Score: 0.56
DE  Interaction: Q86VR2; IntAct: EBI-25220827; Score: 0.56
DE  Interaction: Q969R2; IntAct: EBI-12519574; Score: 0.37
DE  Interaction: Q9BXW6; IntAct: EBI-25616876; Score: 0.60
DE  Interaction: Q9H1P3; IntAct: EBI-12519604; Score: 0.37
DE  Interaction: Q8WXG1; IntAct: EBI-12738199; Score: 0.66
DE  Interaction: Q9WMX2; IntAct: EBI-12738328; Score: 0.54
DE  Interaction: P60033; IntAct: EBI-20568535; Score: 0.35
DE  Interaction: O15069; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9UMZ2; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9UKA4; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9P2D3; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9P0K7; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9NZJ5; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9NVV0; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9NS23; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9HCK1; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9H939; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9H8H0; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9H2D6; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q9BQE3; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q96RL7; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q8TDY2; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q8NHP6; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q8N9B5; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q7RTP6; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q7L4E1; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q709C8; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q6WCQ1; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q15042; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q05209; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: P50453; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: P31321; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: O95067; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: A6ND36; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q12765; IntAct: EBI-21565088; Score: 0.35
DE  Interaction: P36941; IntAct: EBI-21581171; Score: 0.35
DE  Interaction: A1A519; IntAct: EBI-21701765; Score: 0.35
DE  Interaction: Q9UKL6; IntAct: EBI-21900698; Score: 0.40
DE  Interaction: O15503; IntAct: EBI-15578834; Score: 0.40
DE  Interaction: Q5ZSD5; IntAct: EBI-15625386; Score: 0.37
DE  Interaction: O15155; IntAct: EBI-16788067; Score: 0.27
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.42
DE  Interaction: Q96I36; IntAct: EBI-16791250; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: P51151; IntAct: EBI-16798325; Score: 0.27
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: Q9HCE5; IntAct: EBI-20595531; Score: 0.35
DE  Interaction: P07550; IntAct: EBI-20802046; Score: 0.37
DE  Interaction: O75683; IntAct: EBI-20900511; Score: 0.40
DE  Interaction: Q96CG8; IntAct: EBI-20903648; Score: 0.40
DE  Interaction: O43306; IntAct: EBI-20903576; Score: 0.40
DE  Interaction: Q96JK2; IntAct: EBI-20906280; Score: 0.40
DE  Interaction: Q9Y592; IntAct: EBI-20907480; Score: 0.40
DE  Interaction: A2A935; IntAct: EBI-21022882; Score: 0.35
DE  Interaction: P04156; IntAct: EBI-21014654; Score: 0.35
DE  Interaction: Q9H1C4; IntAct: EBI-21266770; Score: 0.35
DE  Interaction: O95183; IntAct: EBI-21267749; Score: 0.35
DE  Interaction: Q96GC9; IntAct: EBI-21267986; Score: 0.35
DE  Interaction: Q969F8; IntAct: EBI-21282024; Score: 0.40
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21391954; Score: 0.00
DE  Interaction: P15498; IntAct: EBI-25372968; Score: 0.35
DE  Interaction: P51636; IntAct: EBI-25383812; Score: 0.35
DE  Interaction: O84008; IntAct: EBI-22302433; Score: 0.35
DE  Interaction: O84560; IntAct: EBI-22302905; Score: 0.35
DE  Interaction: Q640N3; IntAct: EBI-25409042; Score: 0.35
DE  Interaction: Q92685; IntAct: EBI-25468275; Score: 0.37
DE  Interaction: Q8NBM4; IntAct: EBI-25771384; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: F1PAA9; IntAct: EBI-27079701; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: Q8N488; IntAct: EBI-27110926; Score: 0.35
DE  Interaction: P43250; IntAct: EBI-28935197; Score: 0.35
DE  Interaction: P57059; IntAct: EBI-28938560; Score: 0.35
DE  Interaction: Q86UX6; IntAct: EBI-28942129; Score: 0.35
DE  Interaction: Q8NG66; IntAct: EBI-28943501; Score: 0.35
DE  Interaction: Q8NI60; IntAct: EBI-28943519; Score: 0.35
DE  Interaction: Q99640; IntAct: EBI-28944893; Score: 0.35
DE  Interaction: P42695; IntAct: EBI-28951349; Score: 0.35
DE  Interaction: Q9BXK1; IntAct: EBI-29019783; Score: 0.35
DE  Interaction: O95600; IntAct: EBI-29020196; Score: 0.35
DE  Interaction: P08922; IntAct: EBI-32719572; Score: 0.35
DE  Interaction: Q16832; IntAct: EBI-32720227; Score: 0.27
DE  Interaction: P29320; IntAct: EBI-32720767; Score: 0.27
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P21860; IntAct: EBI-32721529; Score: 0.27
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: O15146; IntAct: EBI-32724025; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
DE  Interaction: P16234; IntAct: EBI-32724889; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
DE  Interaction: Q04912; IntAct: EBI-32725158; Score: 0.27
DE  Interaction: Q01974; IntAct: EBI-32725367; Score: 0.27
GO  GO:0035577;
GO  GO:0005923;
GO  GO:0005829;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0015630;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0031982;
GO  GO:0045296;
GO  GO:0033149;
GO  GO:0008017;
GO  GO:0019904;
GO  GO:0046982;
GO  GO:0008219;
GO  GO:0035627;
GO  GO:0090114;
GO  GO:0006888;
GO  GO:0061025;
GO  GO:0044828;
GO  GO:0031175;
GO  GO:0015914;
GO  GO:0044829;
GO  GO:0043123;
GO  GO:0070972;
GO  GO:0006686;
GO  GO:0015918;
GO  GO:0019076;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASASGAMAKHEQILVLDPPTDLKFKGPFTDVVTTNLKLRNPSDRKVCFKVKTTAPRRYCVRPNSGIIDPGSTVTVSVML
SQ  QPFDYDPNEKSKHKFMVQTIFAPPNTSDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPMP
SQ  KPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSTASFRDNVTSPLPSLLVVIAAIFI
SQ  GFFLGKFIL
//
ID  Q9WV55;
PN  Vesicle-associated membrane protein-associated protein A;
GN  Vapa;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10655491}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9P0L0}. Cell membrane {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9P0L0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Z270}. Note=Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells. {ECO:0000250|UniProtKB:Q9P0L0}.
DR  UNIPROT: Q9WV55;
DR  UNIPROT: Q3TJM1;
DR  UNIPROT: Q9QY77;
DR  PDB: 2CRI;
DR  Pfam: PF00635;
DR  PROSITE: PS50202;
DE  Function: Binds to OSBPL3, which mediates recruitment of VAPA to plasma membrane sites. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With OSBPL3, may regulate ER morphology. May play a role in vesicle trafficking. {ECO:0000250|UniProtKB:Q9P0L0}.
DE  Reference Proteome: Yes;
DE  Interaction: P25118; IntAct: EBI-654955; Score: 0.37
DE  Interaction: Q38SD2; IntAct: EBI-2906701; Score: 0.35
DE  Interaction: P37840; IntAct: EBI-2909386; Score: 0.53
DE  Interaction: P68510; IntAct: EBI-8586548; Score: 0.35
DE  Interaction: Q9EPL2; IntAct: EBI-3869454; Score: 0.35
DE  Interaction: Q3TXX3; IntAct: EBI-3894232; Score: 0.40
DE  Interaction: P42866; IntAct: EBI-6919803; Score: 0.35
DE  Interaction: Q9QXM1; IntAct: EBI-11475559; Score: 0.46
DE  Interaction: Q8QZZ8; IntAct: EBI-11569528; Score: 0.35
DE  Interaction: Q9CZE3; IntAct: EBI-11570633; Score: 0.35
DE  Interaction: Q6NZM9; IntAct: EBI-26471532; Score: 0.35
DE  Interaction: A0A0F6B423; IntAct: EBI-27035120; Score: 0.35
GO  GO:0005923;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0031965;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031982;
GO  GO:0033149;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0019904;
GO  GO:0046982;
GO  GO:0044877;
GO  GO:0008219;
GO  GO:0035627;
GO  GO:0090114;
GO  GO:0006888;
GO  GO:0044828;
GO  GO:0031175;
GO  GO:0015914;
GO  GO:0044829;
GO  GO:0070972;
GO  GO:0006686;
GO  GO:0015918;
GO  GO:0019076;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASASGAMAKHEQILVLDPPSDLKFKGPFTDVVTTNLKLQNPSDRKVCFKVKTTAPRRYCVRPNSGIIDPGSIVTVSVML
SQ  QPFDYDPNEKSKHKFMVQTIFAPPNISDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPLP
SQ  KPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSAVSFRDNVTSPLPSLLVVIAAIFI
SQ  GFFLGKFIL
//
ID  Q5R601;
PN  Vesicle-associated membrane protein-associated protein A;
GN  VAPA;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9P0L0}. Cell membrane {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9P0L0}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Z270}. Note=Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells. {ECO:0000250|UniProtKB:Q9P0L0}.
DR  UNIPROT: Q5R601;
DR  Pfam: PF00635;
DR  PROSITE: PS50202;
DE  Function: Binds to OSBPL3, which mediates recruitment of VAPA to plasma membrane sites. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With OSBPL3, may regulate ER morphology. May play a role in vesicle trafficking. {ECO:0000250|UniProtKB:Q9P0L0}.
DE  Reference Proteome: Yes;
GO  GO:0005923;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0008219;
GO  GO:0031175;
GO  GO:0070972;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASASGAMAKHEQILVLDPPTDLKFKGPFTDVVTTNLKLRNPSDRKVCFKVKTTAPRRYCVRPNSGIIDPGSTVTVSVML
SQ  QPFDYDPNEKSKHKFMVQTIFAPPNTSDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPMP
SQ  KPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSTASFRDNVTSPLPSLLVVIAAIFI
SQ  GFFLGKFIL
//
ID  Q9Z270;
PN  Vesicle-associated membrane protein-associated protein A;
GN  Vapa;
OS  10116;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24262037}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9P0L0}. Cell membrane {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9P0L0}. Nucleus membrane {ECO:0000269|PubMed:24262037}. Note=Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells. {ECO:0000250|UniProtKB:Q9P0L0}.
DR  UNIPROT: Q9Z270;
DR  UNIPROT: Q6P723;
DR  PDB: 1Z9L;
DR  PDB: 1Z9O;
DR  Pfam: PF00635;
DR  PROSITE: PS50202;
DE  Function: Binds to OSBPL3, which mediates recruitment of VAPA to plasma membrane sites (By similarity). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (By similarity). With OSBPL3, may regulate ER morphology (By similarity). May play a role in vesicle trafficking (PubMed:19289470). {ECO:0000250|UniProtKB:Q9P0L0, ECO:0000269|PubMed:19289470}.
DE  Reference Proteome: Yes;
DE  Interaction: P21708; IntAct: EBI-7626952; Score: 0.35
DE  Interaction: P37840; IntAct: EBI-2909386; Score: 0.35
DE  Interaction: Q8K4M9; IntAct: EBI-15554458; Score: 0.65
DE  Interaction: Q9Z270; IntAct: EBI-15554502; Score: 0.56
DE  Interaction: Q9BYV6; IntAct: EBI-21998606; Score: 0.35
DE  Interaction: Q5XIE8; IntAct: EBI-26438079; Score: 0.35
GO  GO:0005923;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0015630;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0031982;
GO  GO:0033149;
GO  GO:0042802;
GO  GO:0008017;
GO  GO:0019904;
GO  GO:0046982;
GO  GO:0044877;
GO  GO:0008219;
GO  GO:0035627;
GO  GO:0090114;
GO  GO:0006888;
GO  GO:0044828;
GO  GO:0031175;
GO  GO:0015914;
GO  GO:0044829;
GO  GO:0070972;
GO  GO:0006686;
GO  GO:0015918;
GO  GO:0019076;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASASGAMAKHEQILVLDPPSDLKFKGPFTDVVTTNLKLQNPSDRKVCFKVKTTAPRRYCVRPNSGVIDPGSIVTVSVML
SQ  QPFDYDPNEKSKHKFMVQTIFAPPNISDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPLP
SQ  KPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSAVSFRDNVTSPLPSLLVVIAAIFI
SQ  GFFLGKFIL
//
ID  Q07878;
PN  Intermembrane lipid transfer protein VPS13;
GN  VPS13;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0183;
SL  Comments: Endosome membrane {ECO:0000269|PubMed:27280386, ECO:0000269|PubMed:28334785, ECO:0000269|PubMed:28864540, ECO:0000269|PubMed:30018089, ECO:0000269|PubMed:32690699, ECO:0000305|PubMed:22442115, ECO:0000305|PubMed:24036347}; Peripheral membrane protein {ECO:0000269|PubMed:28122955}. Mitochondrion outer membrane {ECO:0000269|PubMed:26370498, ECO:0000269|PubMed:27280386, ECO:0000269|PubMed:30018089, ECO:0000269|PubMed:34830155}; Peripheral membrane protein {ECO:0000269|PubMed:28122955}. Prospore membrane {ECO:0000269|PubMed:22442115, ECO:0000269|PubMed:24036347, ECO:0000269|PubMed:27280386}; Peripheral membrane protein {ECO:0000269|PubMed:28122955}. Vacuole membrane {ECO:0000269|PubMed:26370498, ECO:0000269|PubMed:27280386, ECO:0000269|PubMed:30018089, ECO:0000269|PubMed:32690699}; Peripheral membrane protein {ECO:0000269|PubMed:28122955}. Nucleus outer membrane {ECO:0000269|PubMed:26370498, ECO:0000269|PubMed:27280386, ECO:0000269|PubMed:30018089}; Peripheral membrane protein {ECO:0000269|PubMed:28122955}. Peroxisome {ECO:0000269|PubMed:28864540}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:34830155}; Peripheral membrane protein {ECO:0000269|PubMed:28122955}. Note=Found at different interorganellar contact sites depending on the growth state of the cell (PubMed:26370498, PubMed:27280386, PubMed:30018089, PubMed:32690699). Localizes from endosomes to the vacuolar membrane during starvation (PubMed:32690699). Localizes to mitochondrial-endosome contacts (PubMed:27280386). Localizes to nuclear envelope-vacuole contact sites (nuclear-vacuole junction; NVJ) during respiration (PubMed:26370498, PubMed:27280386, PubMed:30018089). {ECO:0000269|PubMed:26370498, ECO:0000269|PubMed:27280386, ECO:0000269|PubMed:30018089, ECO:0000269|PubMed:32690699}.
DR  UNIPROT: Q07878;
DR  UNIPROT: D6VXW6;
DR  UNIPROT: O00040;
DR  Pfam: PF12624;
DR  Pfam: PF06650;
DR  Pfam: PF16908;
DR  Pfam: PF16909;
DR  Pfam: PF16910;
DE  Function: Mediates the transfer of lipids between membranes at organelle contact sites (PubMed:30093493, PubMed:24036347, PubMed:22442115). Binds phospholipids, including phosphatidic acid (PA), phosphorylated phosphatidylinositol (PI), phosphatidylcholine (PC), phosphatidylethanolamine (PE), ceramide, and phosphatidylserine (PS) (PubMed:30093493, PubMed:34830155, PubMed:28122955, PubMed:28334785). Involved in mitochondrial lipid homeostasis, in a MCP1-dependent manner (PubMed:27280386, PubMed:34830155, PubMed:32690699). Involved in cortical reticulophagy (also known as cortical endoplasmic reticulum (ER) macroautophagy), acting at the late endosome to package ER into autophagosomes (PubMed:32690699). Involved in the formation of the prospore membrane during sporulation, in a SPO71-dependent manner (PubMed:24036347, PubMed:22442115). Involved in Golgi vesicle transport, in a CDC31-dependent and ARF1-dependent manner (PubMed:28122955, PubMed:9314526, PubMed:34830155). Plays a role in actin cytoskeleton organization (PubMed:28334785). {ECO:0000269|PubMed:22442115, ECO:0000269|PubMed:24036347, ECO:0000269|PubMed:27280386, ECO:0000269|PubMed:28122955, ECO:0000269|PubMed:28334785, ECO:0000269|PubMed:30093493, ECO:0000269|PubMed:32690699, ECO:0000269|PubMed:34830155, ECO:0000269|PubMed:9314526}.
DE  Reference Proteome: Yes;
DE  Interaction: P30656; IntAct: EBI-7116059; Score: 0.40
DE  Interaction: P23639; IntAct: EBI-7116127; Score: 0.40
DE  Interaction: P49956; IntAct: EBI-785954; Score: 0.44
DE  Interaction: P16140; IntAct: EBI-797353; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-797353; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-797353; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-797353; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-797353; Score: 0.35
DE  Interaction: P10659; IntAct: EBI-797353; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-797353; Score: 0.35
DE  Interaction: P06787; IntAct: EBI-797353; Score: 0.53
DE  Interaction: P16550; IntAct: EBI-799867; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-800803; Score: 0.35
DE  Interaction: P17255; IntAct: EBI-800803; Score: 0.35
DE  Interaction: P38764; IntAct: EBI-800803; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-800803; Score: 0.35
DE  Interaction: P16474; IntAct: EBI-800803; Score: 0.35
DE  Interaction: P14742; IntAct: EBI-800803; Score: 0.35
DE  Interaction: P43535; IntAct: EBI-800803; Score: 0.35
DE  Interaction: P32324; IntAct: EBI-800803; Score: 0.35
DE  Interaction: Q00955; IntAct: EBI-812797; Score: 0.27
DE  Interaction: P18239; IntAct: EBI-813508; Score: 0.27
DE  Interaction: P37898; IntAct: EBI-813689; Score: 0.27
DE  Interaction: P60010; IntAct: EBI-820657; Score: 0.27
DE  Interaction: Q12250; IntAct: EBI-7638438; Score: 0.40
DE  Interaction: P38236; IntAct: EBI-8445626; Score: 0.44
DE  Interaction: P38041; IntAct: EBI-7370461; Score: 0.37
DE  Interaction: Q08273; IntAct: EBI-16271112; Score: 0.35
DE  Interaction: P06244; IntAct: EBI-16285450; Score: 0.35
DE  Interaction: P38815; IntAct: EBI-16289368; Score: 0.40
GO  GO:0005768;
GO  GO:0010008;
GO  GO:0019898;
GO  GO:0005794;
GO  GO:0005798;
GO  GO:0031966;
GO  GO:0005741;
GO  GO:0005739;
GO  GO:0005640;
GO  GO:0071561;
GO  GO:0005777;
GO  GO:0005628;
GO  GO:0005774;
GO  GO:0005773;
GO  GO:1990816;
GO  GO:0008289;
GO  GO:0005543;
GO  GO:0120014;
GO  GO:0032120;
GO  GO:0048193;
GO  GO:0120009;
GO  GO:0045324;
GO  GO:0007005;
GO  GO:0045053;
GO  GO:0006623;
GO  GO:0090083;
GO  GO:0061709;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:28122955};
SQ  MLESLAANLLNRLLGSYVENFDPNQLNVGIWSGDVKLKNLKLRKDCLDSLNLPIDVKSGILGDLVLTVPWSSLKNKPVKI
SQ  IIEDCYLLCSPRSEDHENDEEMIKRAFRLKMRKVSEWELTNQARILSTQSENKTSSSSSEKNNAGFMQSLTTKIIDNLQV
SQ  TIKNIHLRYEDMDGIFTTGPSSVGLTLNELSAVSTDSNWAPSFIDITQNITHKLLTLNSLCLYWNTDSPPLISDDDQDRS
SQ  LENFVRGFKDMIASKNSTAPKHQYILKPVSGLGKLSINKLGSTEEQPHIDLQMFYDEFGLELDDTEYNDILHVLSSIQLR
SQ  QITKKFKKARPSFAVSENPTEWFKYIAACVINEIHEKNKMWTWESMKEKCEQRRLYTKLWVEKLKLKNLEAPLRDPIQEA
SQ  QLSELHKDLTYDEIILFRSVAKRQYAQYKLGMTEDSPTPTASSNIEPQTSNKSATKNNGSWLSSWWNGKPTEEVDEDLIM
SQ  TEEQRQELYDAIEFDENEDKGPVLQVPRERVELRVTSLLKKGSFTIRKKKQNLNLGSIIFENCKVDFAQRPDSFLSSFQL
SQ  NKFSLEDGSPNALYKHIISVRNSSKDQSSIDNHATGEEEEEDEPLLRASFELNPLDGLADSNLNIKLLGMTVFYHVHFIT
SQ  EVHKFFKASNQHMETIGNIVNAAEATVEGWTTQTRMGIESLLEDHKTVNVSLDLQAPLIILPLDPHDWDTPCAIIDAGHM
SQ  SILSDLVPKEKIKEIKELSPEEYDKIDGNEINRLMFDRFQILSQDTQIFVGPDIQSTIGKINTASSTNDFRILDKMKLEL
SQ  TVDLSILPKAYKLPTIRVFGHLPRLSLSINDIQYKTIMNLIANSIPSMIDDEENNGDYVNYSSGSEKEMKKQIQLQLKNT
SQ  LKALENMQPLQIEQKFLELHFDIDQAKIAFFQCIKNDSRNSEKLVDILCQRLNFNFDKRAKEMNLDLRVHSLDVEDYIEL
SQ  TDNKEFKNLISSGVEKVTRSQKDLFTLKYKRVQRIVPHNDTLIELFDQDIVMHMSELQLVLTPRSVLTLMNYAMLTFTDP
SQ  NAPEMPADVLRHNKEDRDDAPQKINMKIKMEAVNVIFNDDSIKLATLVLSAGEFTMVLLPERYNINLKLGGLELTDETNE
SQ  SFSRDSVFRKIIQMKGQELVELSYESFDPATNTKDYDSFLKYSTGSMHVNFIESAVNRMVNFFAKFQKSKVSFDRARLAA
SQ  YNQAPSIDAVNNMKMDIVIKAPIIQFPKLVGTQENNYDTMRFYLGEFFIENKFSVIDESHKINHIKLGVREGQLSSNLNF
SQ  DGSSQQLYLVENIGLLFNIDRDPLPQDDTPELKVTSNFESFALDLTENQLTYLLEISNKVSSAFNITDENSGESGGKGEI
SQ  KSPSPDPASLSSESERTATPQSLQGSNKSNIKNPEQKYLDFSFKAPKIALTLYNKTKGVTSLNDCGLTRIMFQDIGCSLG
SQ  LKNDGTVDGQAHVAAFRIEDVRNIKDNKHTELIPKSKNKEYQFVANISRKNLEVGRLLNISMTMDSPKMILAMDYLVSLK
SQ  EFFDAIMSKSHENNLYYPENTNQKPENKAIVESVQEGGDVTKIQYSVNIIETALILLADPCDMNSEAISFKIGQFLVTDQ
SQ  NIMTVAANNVGIFLFKMNSSEEKLRLLDDFSSSLTIDKRNSTPQTLMTNIQLSVQPLLMRISLRDIRLAMLIFKRVTTLL
SQ  NKMTEKEDNGEEEESTDKIQFSHEFERKLAVLDPSILGERSRASQSSDSESIEVPTAILKNETFNADLGGLRFILIGDVH
SQ  EMPILDMNVNEITASAKDWSTDFEALASLETYVNIFNYSRSSWEPLLEMIPITFHLSKGHSEMDPAFSFDILTQRIAEIT
SQ  LSARSIAMLSHIPASLTEELPLASRVSQKPYQLVNDTELDFDVWIQDKTTEDNKNEVVLLKANTSLPWEFEDWRSIREKL
SQ  DIDKSKNILGVCVSGQNYKTIMNIDATTEGENLHVLSPPRNNVHNRIVCEARCDENNVKIITFRSTLVIENTTSTEIELL
SQ  VDSKDPNKPSLKYAIKPHQSKSVPVEYAYDSDIRIRPASEDIYDWSQQTLSWKSLLSNQMSIFCSSKEDSNQRFHFEIGA
SQ  KYDEREPLAKIFPHMKIVVSASMTIENLLPADINFSIFDKREEKRTDFLKTGESMEVHHISLDSFLLMSVQPLQDEASAS
SQ  KPSIVNTPHKSPLNPEDSLSLTLSGGQNLLLKLDYKNIDGTRSKVIRIYSPYIIMNSTDRELYIQSSLLNIAQSKILLEN
SQ  EKRYTIPKMFSFDKEDDKSNRARIRFKESEWSSKLSFDAIGQSFDASVRIKNKEQESNLGINISEGKGKYLLSKVIEIAP
SQ  RYIISNTLDIPIEVCETGSMDVQQIESNITKPLYRMRNIVDKQLVLKFLGGDSNWSQPFFIKNVGVTYLKVLKNSRHKLL
SQ  KIEILLDKATIFIRIKDGGDRWPFSIRNFSDHDFIFYQRDPRKVSDPYKDDQSNESSSRSFKPIFYRIPSKSIMPYAWDF
SQ  PTAKEKYLVLESGTRTREVRLAEIGELPPLRLDKRSKDKPAPIVGLHVVADDDMQALVIVNYKANVGLYKLKTASATTTS
SQ  SVSVNSSVTDGFVQKDEDEKVNTQIVVSFKGVGISLINGRLQELLYINMRGIELRYNESKAYQTFSWKMKWMQIDNQLFS
SQ  GNYSNILYPTEIPYTEKEIENHPVISGSISKVNDSLQAVPYFKHVTLLIQEFSIQLDEDMLYAMMDFIKFPGSPWIMDSR
SQ  DYKYDEEIQLPDVSELKTAGDIYFEIFHIQPTVLHLSFIRSDEISPGLAEETEESFSSSLYYVHMFAMTLGNINEAPVKV
SQ  NSLFMDNVRVPLPILMDHIERHYTTQFVYQIHKILGSADCFGNPVGLFNTISSGVWDLFYEPYQGYMMNDRPQEIGIHLA
SQ  KGGLSFAKKTVFGLSDSMSKFTGSMAKGLSVTQDLEFQRVRRLQQRINKNNRNALANSAQSFASTLGSGLSGIALDPYKA
SQ  MQKEGAAGFLKGLGKGIVGLPTKTAIGFLDLTSNLSQGVKSTTTVLDMQKGCRVRLPRYVDHDQIIKPYDLREAQGQYWL
SQ  KTVNGGVFMNDEYLSHVILPGKELAVIVSMQHIAEVQMATQELMWSTGYPSIQGITLERSGLQIKLKSQSEYFIPISDPE
SQ  ERRSLYRNIAIAVREYNKYCEAIL
//
ID  G5EFV8;
PN  Vacuolar protein sorting-associated protein 52 homolog;
GN  vps;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21613545}. Perikaryon {ECO:0000269|PubMed:27191843}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27191843}. Note=Co-localizes with rab-2 to perinuclear puncta in the perikaryon. Co-localizes with the small GTPases rab-6.1 and rab-6.2 at Golgi structures (PubMed:21613545). {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
DR  UNIPROT: G5EFV8;
DR  UNIPROT: G5EFV9;
DR  Pfam: PF04129;
DE  Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN) (PubMed:21613545). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi (PubMed:21613545). Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1 (PubMed:27191843). Important for neuronal function (PubMed:27191843). {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
DE  Reference Proteome: Yes;
DE  Interaction: O01839; IntAct: EBI-2411813; Score: 0.73
DE  Interaction: Q09501; IntAct: EBI-335600; Score: 0.00
DE  Interaction: P32743; IntAct: EBI-335609; Score: 0.00
DE  Interaction: O61975; IntAct: EBI-335606; Score: 0.00
DE  Interaction: Q20742; IntAct: EBI-335603; Score: 0.00
DE  Interaction: Q22227; IntAct: EBI-335612; Score: 0.00
DE  Interaction: Q22544; IntAct: EBI-335615; Score: 0.00
DE  Interaction: P91820; IntAct: EBI-335621; Score: 0.00
DE  Interaction: P34574; IntAct: EBI-335618; Score: 0.00
DE  Interaction: Q9N575; IntAct: EBI-335624; Score: 0.00
DE  Interaction: Q22639; IntAct: EBI-6398967; Score: 0.54
DE  Interaction: P34561; IntAct: EBI-6395189; Score: 0.54
DE  Interaction: Q22782; IntAct: EBI-6399389; Score: 0.46
DE  Interaction: P34213; IntAct: EBI-6399381; Score: 0.46
DE  Interaction: G5EFV8; IntAct: EBI-6398996; Score: 0.37
DE  Interaction: Q20797; IntAct: EBI-6399555; Score: 0.37
DE  Interaction: H2KZ72; IntAct: EBI-6399559; Score: 0.37
DE  Interaction: P41941; IntAct: EBI-6399538; Score: 0.37
DE  Interaction: Q21499; IntAct: EBI-6399564; Score: 0.37
GO  GO:0005829;
GO  GO:0000938;
GO  GO:0005797;
GO  GO:0000138;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0031267;
GO  GO:0019905;
GO  GO:0032456;
GO  GO:0006896;
GO  GO:0007041;
GO  GO:1904810;
GO  GO:1904811;
GO  GO:0090326;
GO  GO:0015031;
GO  GO:0042147;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPRTRVNLQKSEANDRSFTISSLEFCLSQLRKADPNLVKKAIASGDGLTESKNDVSTRLSEAHRYSVQQCLDNSEQLAQL
SQ  HNQLVHCDNVFERLQATLYSFQDNLGSIGQDMKNLQLQSHHIHQELENRQKVRVELSQFVDDIAVSQTMMKTINDTDAND
SQ  RGFLEALHELHHKITLILQRGNGDAVAVNDTMPILEGLKLKAVVKVREWLLQKMFQFRKPLSNYQVFQHQLLKCRFFYEF
SQ  LLHHDLISAKELQDEYIDTISKMFFTYFKAYATRLFKLAMKDVATKEDALGSIDFAKPAGLGAIFSSKQHVVRNKATVFS
SQ  IGQRHQILSDDFLGALIVPHAATQNHQSYQFEALFRSIQLAFVDHYSHEYLFITDFFLVSNDEAIELHNKAMARAMSVVL
SQ  KSCEEQIALSWDAISLHLCICLCDKFTEVLAEREVPEVSDYWNTVTSFLWTRLNLVMSQHYESVKSVDLKKLMHSGSLDA
SQ  RPHFIVRRYAELTSAHLMIAKASGKEMGAKMEAVLENSEDSIEQLLTRMSAMQQTQKNKHVFLINNYDLILSIIDNEESK
SQ  HTKIYAIVHELEQKSIDDFVEEMLEPHIGYMIKFVNECESLIVQGHTQLLVRYNDKVGTVVANFNAKWRPAVDSINSECI
SQ  QLFTNFSLGTTILQTIFTKYVQYINRFTKILSHDVFAKNPVCSQLVNVHQVMLEIKRFKPAY
//
ID  P34561;
PN  Vacuolar protein sorting-associated protein 53 homolog;
GN  vps;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Perikaryon {ECO:0000269|PubMed:27191843}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27191843}. Note=Co-localizes with rab-2 to perinuclear puncta in the perikaryon. {ECO:0000269|PubMed:27191843}.
DR  UNIPROT: P34561;
DR  UNIPROT: E5QCF9;
DR  Pfam: PF04100;
DE  Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN) (PubMed:21613545). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi (PubMed:21613545). Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1 (PubMed:27191843). Important for neuronal function (PubMed:27191843). {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
DE  Reference Proteome: Yes;
DE  Interaction: G5EFV8; IntAct: EBI-6395189; Score: 0.54
DE  Interaction: O01839; IntAct: EBI-6394905; Score: 0.51
DE  Interaction: Q22639; IntAct: EBI-6395197; Score: 0.54
DE  Interaction: H2KZ72; IntAct: EBI-6421128; Score: 0.27
DE  Interaction: Q21499; IntAct: EBI-6421104; Score: 0.27
DE  Interaction: O18230; IntAct: EBI-6421120; Score: 0.27
DE  Interaction: Q20797; IntAct: EBI-6421112; Score: 0.27
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0000938;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:1904810;
GO  GO:1904811;
GO  GO:0090326;
GO  GO:0060378;
GO  GO:0042147;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250};
SQ  MEEPTTSELKLSDNVMNEISDMCITEYCKPNMSLMAQINELFPTEQSLTQLDSIIASVEGEIGELDNELAYLVETNANVS
SQ  ERGEEALKHAQDAMIELEKSIGSIRERTKSSDEIVREMTRDIKQLDIAKRNLTASITTLHHLHILLTGVESLGAWVDKKD
SQ  YSSIARQLPAILNVLQLFDAYKESDQIANLSGQLDKLKASLTIQLAKDLKNAFQTGQLSDRITDMCRVAAALEGNVKENF
SQ  VKWFIEQQLSEYVIIYADNEEGAWLDKVDDRYKWFVRKLTDFERAGLSNIFPADWHMGRRLTSEFCTVTRDILYRIMTRR
SQ  RQDLDWKLLGHAIQHTKMFEALLTKRFPEKDGISFEKAIWSVFDTFLDVFINAQEKTLNEFLDTCASKIRSGEEKPSRES
SQ  STHAVPFPSSADMFLLLKKVITESSKLSSEPDALIRDVIGVVRVCLRGYATSCLVAFLPSLGSQQSGAANLFSLIREEIA
SQ  YPRLTPDQQFLVCCILATADWCAETSIQLQEKLSQRIPGVDISQETEAFYSITNQSLQVLVQDVESTCDAALQSISKVNW
SQ  TAVDCVGDESPFIGSMRAHLRQAVPLIRDMLSDRRKYFAHFCLKLATQLAHKFVGSLFRCRTISTHGAEQLLLDTHSLKT
SQ  FLLSVPSIDSIINSKPPTAYVTSVNAALTKAEMILKVVMCSLETVDEFVEQYIKLLPASDAAEMQKVLEMKGVKRQEHSA
SQ  VLNAYRLKIGASGSDPIQQSNSLTSRIGGALPTVGSAASVSEAFNAVVSMAADGLSDQAVTSSIDKLKRFERLVKRQL
//
ID  Q86Y07;
PN  Serine/threonine-protein kinase VRK2;
GN  VRK2;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Comments: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:16704422}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16704422}; Single-pass type IV membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:16704422}; Single-pass type IV membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q8BN21}. [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:16704422}. Nucleus {ECO:0000269|PubMed:16704422}.
DR  UNIPROT: Q86Y07;
DR  UNIPROT: B4DKL0;
DR  UNIPROT: D6W5D4;
DR  UNIPROT: D6W5D6;
DR  UNIPROT: Q49AK9;
DR  UNIPROT: Q53EU9;
DR  UNIPROT: Q53S39;
DR  UNIPROT: Q53S77;
DR  UNIPROT: Q53TU1;
DR  UNIPROT: Q86Y08;
DR  UNIPROT: Q86Y09;
DR  UNIPROT: Q86Y10;
DR  UNIPROT: Q86Y11;
DR  UNIPROT: Q86Y12;
DR  UNIPROT: Q8IXI5;
DR  UNIPROT: Q99987;
DR  PDB: 2V62;
DR  PDB: 5UU1;
DR  PDB: 6NCG;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DR  OMIM: 602169;
DR  DisGeNET: 7444;
DE  Function: Serine/threonine kinase that regulates several signal transduction pathways (PubMed:16704422, PubMed:14645249, PubMed:16495336, PubMed:17709393, PubMed:18617507, PubMed:18286207, PubMed:20679487). Isoform 1 modulates the stress response to hypoxia and cytokines, such as interleukin-1 beta (IL1B) and this is dependent on its interaction with MAPK8IP1, which assembles mitogen-activated protein kinase (MAPK) complexes (PubMed:17709393). Inhibition of signal transmission mediated by the assembly of MAPK8IP1-MAPK complexes reduces JNK phosphorylation and JUN-dependent transcription (PubMed:18286207). Phosphorylates 'Thr-18' of p53/TP53, histone H3, and may also phosphorylate MAPK8IP1 (PubMed:16704422). Phosphorylates BANF1 and disrupts its ability to bind DNA and reduces its binding to LEM domain-containing proteins (PubMed:16495336). Down-regulates the transactivation of transcription induced by ERBB2, HRAS, BRAF, and MEK1 (PubMed:20679487). Blocks the phosphorylation of ERK in response to ERBB2 and HRAS (PubMed:20679487). Can also phosphorylate the following substrates that are commonly used to establish in vitro kinase activity: casein, MBP and histone H2B, but it is not sure that this is physiologically relevant (PubMed:14645249). {ECO:0000269|PubMed:14645249, ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:16704422, ECO:0000269|PubMed:17709393, ECO:0000269|PubMed:18286207, ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:20679487}. [Isoform 2]: Phosphorylates 'Thr-18' of p53/TP53, as well as histone H3. Reduces p53/TP53 ubiquitination by MDM2, promotes p53/TP53 acetylation by EP300 and thereby increases p53/TP53 stability and activity. {ECO:0000269|PubMed:16704422}.
DE  Reference Proteome: Yes;
DE  Interaction: O95476; IntAct: EBI-27115722; Score: 0.27
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: P02545; IntAct: EBI-16795756; Score: 0.27
DE  Interaction: P10415; IntAct: EBI-1207847; Score: 0.37
DE  Interaction: P62826; IntAct: EBI-1795483; Score: 0.40
DE  Interaction: Q07817; IntAct: EBI-6476114; Score: 0.50
DE  Interaction: P03182; IntAct: EBI-1207667; Score: 0.60
DE  Interaction: Q9WVI9; IntAct: EBI-2121669; Score: 0.54
DE  Interaction: Q9UQF2; IntAct: EBI-2122041; Score: 0.46
DE  Interaction: O43318; IntAct: EBI-1778783; Score: 0.40
DE  Interaction: O14733; IntAct: EBI-2122475; Score: 0.35
DE  Interaction: P45983; IntAct: EBI-2122553; Score: 0.35
DE  Interaction: Q62073; IntAct: EBI-1769196; Score: 0.58
DE  Interaction: Q8CF89; IntAct: EBI-1778716; Score: 0.50
DE  Interaction: Q8IVT5; IntAct: EBI-2908953; Score: 0.65
DE  Interaction: Q02750; IntAct: EBI-2909031; Score: 0.52
DE  Interaction: P60953; IntAct: EBI-3438850; Score: 0.00
DE  Interaction: P38432; IntAct: EBI-4421226; Score: 0.44
DE  Interaction: Q61097; IntAct: EBI-6172735; Score: 0.58
DE  Interaction: Q13469; IntAct: EBI-6376975; Score: 0.61
DE  Interaction: Q60591; IntAct: EBI-6378546; Score: 0.56
DE  Interaction: Q07812; IntAct: EBI-6554313; Score: 0.35
DE  Interaction: Q13418; IntAct: EBI-10103376; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: F8VQC7; IntAct: EBI-11104527; Score: 0.35
DE  Interaction: Q86WU2; IntAct: EBI-11156693; Score: 0.35
DE  Interaction: Q6NUS6; IntAct: EBI-11368748; Score: 0.27
DE  Interaction: Q86UK5; IntAct: EBI-11372136; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q96GX1; IntAct: EBI-11375285; Score: 0.27
DE  Interaction: Q9P0N5; IntAct: EBI-11378021; Score: 0.27
DE  Interaction: Q5HYA8; IntAct: EBI-11385073; Score: 0.27
DE  Interaction: Q8N4V1; IntAct: EBI-24720036; Score: 0.56
DE  Interaction: Q6PEY1; IntAct: EBI-23795224; Score: 0.56
DE  Interaction: Q6UW68; IntAct: EBI-24741001; Score: 0.56
DE  Interaction: P36382; IntAct: EBI-24769250; Score: 0.56
DE  Interaction: Q0VAB0; IntAct: EBI-24786091; Score: 0.56
DE  Interaction: Q13520; IntAct: EBI-25165439; Score: 0.56
DE  Interaction: Q9NUH8; IntAct: EBI-24761338; Score: 0.56
DE  Interaction: O43291; IntAct: EBI-21587968; Score: 0.35
DE  Interaction: P57727; IntAct: EBI-21588578; Score: 0.35
DE  Interaction: Q8WWF5; IntAct: EBI-21589535; Score: 0.35
DE  Interaction: Q96CS3; IntAct: EBI-21592752; Score: 0.35
DE  Interaction: Q9Y5M8; IntAct: EBI-21633655; Score: 0.35
DE  Interaction: Q17R55; IntAct: EBI-21844412; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: Q9HBL7; IntAct: EBI-16797780; Score: 0.27
DE  Interaction: P46013; IntAct: EBI-20562326; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: O84008; IntAct: EBI-22302433; Score: 0.35
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: A0A0H3NF08; IntAct: EBI-27055973; Score: 0.27
DE  Interaction: A0A0H3NB75; IntAct: EBI-27055983; Score: 0.27
DE  Interaction: Q8NCK7; IntAct: EBI-27103180; Score: 0.35
DE  Interaction: P29322; IntAct: EBI-32721175; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: O15146; IntAct: EBI-32724025; Score: 0.27
DE  Interaction: Q16288; IntAct: EBI-32724526; Score: 0.27
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0031966;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0005524;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0034599;
GO  GO:0018105;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:2000659;
GO  GO:0043408;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPPKRNEKYKLPIPFPEGKVLDDMEGNQWVLGKKIGSGGFGLIYLAFPTNKPEKDARHVVKVEYQENGPLFSELKFYQRV
SQ  AKKDCIKKWIERKQLDYLGIPLFYGSGLTEFKGRSYRFMVMERLGIDLQKISGQNGTFKKSTVLQLGIRMLDVLEYIHEN
SQ  EYVHGDIKAANLLLGYKNPDQVYLADYGLSYRYCPNGNHKQYQENPRKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCM
SQ  LRWLCGKLPWEQNLKDPVAVQTAKTNLLDELPQSVLKWAPSGSSCCEIAQFLVCAHSLAYDEKPNYQALKKILNPHGIPL
SQ  GPLDFSTKGQSINVHTPNSQKVDSQKAATKQVNKAHNRLIEKKVHSERSAESCATWKVQKEEKLIGLMNNEAAQESTRRR
SQ  QKYQESQEPLNEVNSFPQKISYTQFPNSFYEPHQDFTSPDIFKKSRSPSWYKYTSTVSTGITDLESSTGLWPTISQFTLS
SQ  EETNADVYYYRIIIPVLLMLVFLALFFL
//
ID  Q8BN21;
PN  Serine/threonine-protein kinase VRK2;
GN  Vrk2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:14645249}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:31142202}; Single- pass type IV membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q86Y07}; Single-pass type IV membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:31142202}.
DR  UNIPROT: Q8BN21;
DR  UNIPROT: Q3U415;
DR  UNIPROT: Q5F1Z5;
DR  UNIPROT: Q5SP88;
DR  UNIPROT: Q8BPU8;
DR  UNIPROT: Q8CJ46;
DR  UNIPROT: Q91WS1;
DR  UNIPROT: Q9CZF9;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine kinase that regulates several signal transduction pathways (PubMed:14645249). Modulates the stress response to hypoxia and cytokines, such as interleukin-1 beta (IL1B) and this is dependent on its interaction with MAPK8IP1, which assembles mitogen- activated protein kinase (MAPK) complexes (By similarity). Inhibition of signal transmission mediated by the assembly of MAPK8IP1-MAPK complexes reduces JNK phosphorylation and JUN-dependent transcription (By similarity). Phosphorylates histone H3 (By similarity). Phosphorylates 'Thr-18' of p53/TP53, and thereby increases its stability and activity (By similarity). Phosphorylates BANF1 and disrupts its ability to bind DNA and reduces its binding to LEM domain- containing proteins (By similarity). Down-regulates the transactivation of transcription induced by ERBB2, HRAS, BRAF, and MEK1 (By similarity). Blocks the phosphorylation of ERK in response to ERBB2 and HRAS (By similarity). May also phosphorylate MAPK8IP1 (By similarity). Can also phosphorylate the following substrates that are commonly used to establish in vitro kinase activity: casein, MBP and histone H2B, but it is not sure that this is physiologically relevant (By similarity). {ECO:0000250|UniProtKB:Q86Y07, ECO:0000269|PubMed:14645249}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031966;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0005524;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0034599;
GO  GO:0018105;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:2000659;
GO  GO:0043408;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPRRKEKYKLPVPLPEGKILDDMEGNRWALGKMIGSGGFGLIYLAFPTNKPNKDARHVIKLEYQENGPLFSELKFYQRA
SQ  AKRECIQKWIQQRKLDYLGIPVFYGFGLTDFKGRSYRFMVMERLGIDLQKLLDQNGGFKKLTVLQLGIRMLDVLEYIHEN
SQ  EYVHGDIKAANLLLDFTNPDRVYLADYGLSYRYCPNGNHKQYQEDPRKGHNGTIEFTSLDAHKGVAPSRRSDVEILGYCM
SQ  LHWLFGKLPWEAKLDDPVAVQTAKTNLLDELPESVLKWAPSGSSCSELVKYLMYVHNLAYDDKPDYQKLKKILNPDGVPL
SQ  GPLEFSTKVQSVHVRTPAQQKVDSPKATRKPANEFPAKFPKKVHRETRARQREEQEDSQPTMLQSRPAAPENSRTRKIHE
SQ  YSDIFSEMQSLQQTPSYMSFQGSYCKPYLDCTRRDPIRKPRSLPRYRHTPTGNLGVTDLESSPRFWPAIFQLTLSEETKA
SQ  DVYYYGITIFCLLIFVFLALYFL
//
ID  Q6B9X6;
PN  Alpha-protein kinase vwkA;
GN  vwkA;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:15728726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15728726}. Contractile vacuole membrane {ECO:0000269|PubMed:15728726}. Note=Enriched adjacent to large spherical structures such as contractile vacuoles and Golgi-like structures (perinuclear).
DR  UNIPROT: Q6B9X6;
DR  UNIPROT: Q55FF0;
DR  Pfam: PF02816;
DR  PROSITE: PS51158;
DE  Function: Displays a modest preference for threonine over serine residues. Does not phosphorylate myosin II, however can phosphorylate MBP, in vitro. May be involved in the regulation of myosin II function during cytokinesis. Overexpression leads to impaired cell proliferation in suspension culture and fails to develop beyond the mound stage. Both overexpression and absence of the gene can result in defects in cytokinesis and alterations in myosin II abundance and assembly. {ECO:0000269|PubMed:15728726, ECO:0000269|PubMed:18381083}.
DE  Reference Proteome: Yes;
GO  GO:0031164;
GO  GO:0000331;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0004672;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0070177;
GO  GO:0033298;
GO  GO:0006971;
GO  GO:0000281;
GO  GO:0031038;
GO  GO:0018209;
GO  GO:0006468;
GO  GO:0031156;
GO  GO:0031288;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MESKYVLSTEKESKTKPSGRVNVSDMDSISNSLSKTSLGTRKVPTSLKTDASRSGLSSGGSKTHISDESALRMVYGSTPR
SQ  DEKTTTTKDSITLAKEKEKKIEKRNEEIKLTFKAIRASECVDLLFIVDCTGSMDPYIEQIKSDIVKLQEALKLKHSFLDI
SQ  EFGFIRYTDFDVASNRCSTFQFSRSTVEFVRFVSEIRAGGGADGPEDVFGGMDLIKSMKWRPNSTRVVIHIADAPCHGTE
SQ  YHSMADSYPGGDPNGIKLDDLLTDIISLNINYYFGHINLKETGQMIDFFDKKTKEISRNKKSINSFDSKETSKMNERIFI
SQ  SIEESISVSRSVLTEQYLGHNIDGSTGKQRSEREFEINTNMDIDFGELPYIQMLQTKFKMPSDIVTCLSSSYEMKLNEIT
SQ  ISIKIAPNPFSHGACRLAYLGIDEHGKKVVLKQSKYIGGRENSKKRYFESMECQTVAAKFALEFNKQLSLTSSEHQITFT
SQ  VAKVLQMKHSEKPMYFGIETFINGEYQKYNSNCGWLKDDAMSEILQTFSHWTYQESKNKAIVVDIQGVKTSKGYLLTDPA
SQ  IHSTDTLRFGSCNLGKPGIIKFFQSHKCNQHCKKLGLTIPSFTSSSSTSSSSRSTSSSSSISYSY
//
ID  O62275;
PN  Argonaute protein wago-4;
GN  wago;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29791857, ECO:0000269|PubMed:30728462}. Cytoplasmic granule {ECO:0000269|PubMed:29769721}. Cytoplasm {ECO:0000269|PubMed:29791857}. Note=Co-localizes with znfx-1 in P-granules in germline blastomeres until the 100-cell stage (PubMed:29769721). During oocyte maturation, co-localizes with znfx-1 in liquid-like condensates in the cytoplasm called Z granules (PubMed:29769721). Localizes to cytoplasmic P- granules in germline blastomeres. {ECO:0000269|PubMed:29769721}.
DR  UNIPROT: O62275;
DR  Pfam: PF02170;
DR  Pfam: PF02171;
DR  PROSITE: PS50821;
DR  PROSITE: PS50822;
DE  Function: Argonaute protein which is involved in the endogenous small interfering RNA (endo-siRNA) pathway and is required for RNA-mediated gene silencing (RNAi) in the germline (PubMed:17110334, PubMed:29791857, PubMed:30728462). Interacts with secondary 22G-RNAs, which are RNA-dependent RNA polymerase-derived endo-siRNAs, typically 22 nucleotides in length with a 5'guanosine residue (PubMed:29791857). Also interacts with the mRNA targets of 22G-RNAs (PubMed:29791857). Associates with znfx-1 to mediate small RNA-directed transgenerational epigenetic inheritance of both germline- and soma-expressed genes (PubMed:29791857, PubMed:29769721). {ECO:0000269|PubMed:17110334, ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29791857, ECO:0000269|PubMed:30728462}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9XVJ3; IntAct: EBI-2418620; Score: 0.49
GO  GO:0048471;
GO  GO:0004521;
GO  GO:0035198;
GO  GO:0003723;
GO  GO:0003727;
GO  GO:0031047;
GO  GO:0031048;
GO  GO:0060966;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MPALPPVYTPSGAPSSVHAPPAVPPVPVPTQPLRSEYQTSNDACIKRLEELNIAPAAKLYPTPTEPGKCGVEAEIQTNVF
SQ  GIEMHQDSLFYQYSVNITTELKNGKEVTFTKKGKDDFVVTERHDKCCAILFRALGDYEEFFKTSDSCLIYDGQSILFSNV
SQ  DLFQGFREGAVKTKYMQLDGGEMDHKDLKSLPCIKLEVFPTKNPAVKFTREAVARRATDSNLDSVSLAYQQILELALTQP
SQ  CLRNTARYVVFDHGKMFFIDPLGEGFEKCDVVDVGDGKQVVPGLKKTINFIEGPYGRGRSNPSVVIDGMKVAFHKNQPIL
SQ  DKLKEITTQPVEHGLKGLEKDRCAAVIKGLDCYSTYGGRERHHKIEGIHHEGARNARFELNDGGSCTVAQYFEDVYNITL
SQ  RYPDTNLIVSKERGNINFYPMELLKISSHQRVQIPQLTSAQSQKTTKESAVLPDVRQRLILTGKNAAQISSDNEVLGKMG
SQ  VSVCEDPLMVKGRSIPAVKLANAEIGANPINVKDNKWRANRFTRPATAPNVWAMYVVGTASTRITLDTLKKFADEFAAMC
SQ  KSKGVNMPAPADISLIHMDAIESRLYDATKANCTFVFIITDDSITTLHQRYKMIEKDTKMIVQDMKLSKALSVINAGKRL
SQ  TLENVINKTNVKLGGSNYVFVDAKKQLDSHLIIGVGISAPPAGTKYAMENKGVLNPNVIGYAYNAQHNQEFSGDFVLNSA
SQ  SQDTLAPIEDIVMHSLNEYQKFHDGGLPRRVIVYRTGTSEGNHGSIMAYEIPLARAAMRDFSPDIQLVYIVVSKDHSFRF
SQ  FKPDLASLASRPQATSSTASRHSAMPAAPKAWDLNIAPGILVDSIVTNPACKQFFLNSHITLQGTAKTPLYTVLADDAKV
SQ  SMTALEDITYKLCHLHQIVGLPTSLPTPLYVANEYAKRGRNLWNEAVALNNVPTVSGPEADRLKELTKSICYKASGDLTG
SQ  RRVNA
//
ID  Q8IZQ1;
PN  WD repeat and FYVE domain-containing protein 3;
GN  WDFY3;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:20971078}. Cytoplasm, cytosol {ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:20971078}. Nucleus, PML body {ECO:0000269|PubMed:20168092}. Membrane; Peripheral membrane protein {ECO:0000269|PubMed:15292400}; Cytoplasmic side {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:Q6VNB8}. Cell projection, axon {ECO:0000250|UniProtKB:Q6VNB8}. Note=Relocalization from the nucleus to the cytosol is stimulated by cellular stress, such as starvation or proteasomal inhibition. In the cytosol of starved cells, colocalizes with autophagic structures (PubMed:15292400, PubMed:20168092, PubMed:20971078, PubMed:20417604). This redistribution is dependent on p62/SQSTM1 (PubMed:20168092). When nuclear export is blocked by treatment with leptomycin B, accumulates in nuclear bodies, that completely or partially colocalize with promyelocytic leukemia (PML) bodies (PubMed:20168092). Localizes throughout neurons, including within axons. In neurons, enriched in the light membrane fraction along with the synaptosomal membrane protein synaptophysin and the membrane- bound form of LC3/MAP1LC3A/MAP1LC3B, called LC3-II, a classic marker for autophagic vesicles (By similarity). {ECO:0000250|UniProtKB:Q6VNB8, ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:20971078}.
DR  UNIPROT: Q8IZQ1;
DR  UNIPROT: Q4W5K5;
DR  UNIPROT: Q6P0Q5;
DR  UNIPROT: Q8N1T2;
DR  UNIPROT: Q8NAV6;
DR  UNIPROT: Q96BS7;
DR  UNIPROT: Q96D33;
DR  UNIPROT: Q96N85;
DR  UNIPROT: Q9Y2J7;
DR  PDB: 3WIM;
DR  PDB: 6W9N;
DR  Pfam: PF02138;
DR  Pfam: PF01363;
DR  Pfam: PF14844;
DR  PROSITE: PS50197;
DR  PROSITE: PS51783;
DR  PROSITE: PS00678;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  PROSITE: PS50178;
DR  OMIM: 617485;
DR  OMIM: 617520;
DR  DisGeNET: 23001;
DE  Function: Required for selective macroautophagy (aggrephagy). Acts as an adapter protein by linking specific proteins destined for degradation to the core autophagic machinery members, such as the ATG5- ATG12-ATG16L E3-like ligase, SQSTM1 and LC3 (PubMed:20417604). Along with p62/SQSTM1, involved in the formation and autophagic degradation of cytoplasmic ubiquitin-containing inclusions (p62 bodies, ALIS/aggresome-like induced structures). Along with SQSTM1, required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Important for normal brain development. Essential for the formation of axonal tracts throughout the brain and spinal cord, including the formation of the major forebrain commissures. Involved in the ability of neural cells to respond to guidance cues. Required for cortical neurons to respond to the trophic effects of netrin-1/NTN1 (By similarity). Regulates Wnt signaling through the removal of DVL3 aggregates, likely in an autophagy-dependent manner. This process may be important for the determination of brain size during embryonic development (PubMed:27008544). May regulate osteoclastogenesis by acting on the TNFSF11/RANKL - TRAF6 pathway (By similarity). After cytokinetic abscission, involved in midbody remnant degradation (PubMed:24128730). In vitro strongly binds to phosphatidylinositol 3-phosphate (PtdIns3P) (PubMed:15292400). {ECO:0000250|UniProtKB:Q6VNB8, ECO:0000269|PubMed:15292400, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20417604, ECO:0000269|PubMed:24128730, ECO:0000269|PubMed:27008544}.
DE  Disease: Microcephaly 18, primary, autosomal dominant (MCPH18) [MIM:617520]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH18 affected individuals manifest microcephaly with mild to moderate intellectual disability. {ECO:0000269|PubMed:27008544}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O43463; IntAct: EBI-8487862; Score: 0.37
DE  Interaction: Q9GZQ8; IntAct: EBI-1569302; Score: 0.71
DE  Interaction: Q9H1Y0; IntAct: EBI-2935292; Score: 0.63
DE  Interaction: P42858; IntAct: EBI-2935627; Score: 0.58
DE  Interaction: P37840; IntAct: EBI-2938214; Score: 0.35
DE  Interaction: P54253; IntAct: EBI-2938194; Score: 0.27
DE  Interaction: Q13501; IntAct: EBI-2935768; Score: 0.71
DE  Interaction: O95166; IntAct: EBI-3623491; Score: 0.35
DE  Interaction: Q99750; IntAct: EBI-8647452; Score: 0.37
DE  Interaction: Q9HCM9; IntAct: EBI-10264656; Score: 0.56
DE  Interaction: P01106; IntAct: EBI-3962281; Score: 0.35
DE  Interaction: O00418; IntAct: EBI-6255330; Score: 0.35
DE  Interaction: Q96LA8; IntAct: EBI-8487900; Score: 0.37
DE  Interaction: Q99873; IntAct: EBI-8487956; Score: 0.37
DE  Interaction: P62993; IntAct: EBI-10692234; Score: 0.49
DE  Interaction: Q5R372; IntAct: EBI-10692251; Score: 0.49
DE  Interaction: P40763; IntAct: EBI-10692272; Score: 0.49
DE  Interaction: Q63HR2; IntAct: EBI-10696607; Score: 0.37
DE  Interaction: Q92569; IntAct: EBI-10697708; Score: 0.51
DE  Interaction: P14079; IntAct: EBI-9675780; Score: 0.56
DE  Interaction: Q8NCP5; IntAct: EBI-10264632; Score: 0.56
DE  Interaction: Q8TAP6; IntAct: EBI-10264644; Score: 0.56
DE  Interaction: P60520; IntAct: EBI-10106953; Score: 0.61
DE  Interaction: Q6IAW1; IntAct: EBI-10106921; Score: 0.66
DE  Interaction: Q9BXW4; IntAct: EBI-10106915; Score: 0.64
DE  Interaction: Q9H0R8; IntAct: EBI-10106947; Score: 0.61
DE  Interaction: Q9DCD6; IntAct: EBI-10107615; Score: 0.27
DE  Interaction: Q9CQV6; IntAct: EBI-10107663; Score: 0.27
DE  Interaction: Q9DCX1; IntAct: EBI-11028199; Score: 0.35
DE  Interaction: D3YY91; IntAct: EBI-11028850; Score: 0.35
DE  Interaction: P51148; IntAct: EBI-11046231; Score: 0.35
DE  Interaction: D6RA96; IntAct: EBI-11047357; Score: 0.35
DE  Interaction: Q9CWW7; IntAct: EBI-11057014; Score: 0.35
DE  Interaction: P30291; IntAct: EBI-11070815; Score: 0.35
DE  Interaction: Q24JP5; IntAct: EBI-11071995; Score: 0.35
DE  Interaction: Q9NYB0; IntAct: EBI-11084612; Score: 0.35
DE  Interaction: Q9UER7; IntAct: EBI-11088574; Score: 0.35
DE  Interaction: Q3UH45; IntAct: EBI-11090763; Score: 0.35
DE  Interaction: Q14494; IntAct: EBI-11091040; Score: 0.35
DE  Interaction: Q96EQ0; IntAct: EBI-11152414; Score: 0.35
DE  Interaction: P46379; IntAct: EBI-11154173; Score: 0.35
DE  Interaction: Q8NHV4; IntAct: EBI-11157526; Score: 0.35
DE  Interaction: P26447; IntAct: EBI-11158347; Score: 0.35
DE  Interaction: Q15116; IntAct: EBI-21506827; Score: 0.35
DE  Interaction: Q8TD20; IntAct: EBI-21562097; Score: 0.35
DE  Interaction: P05362; IntAct: EBI-21568860; Score: 0.35
DE  Interaction: P13747; IntAct: EBI-21569078; Score: 0.35
DE  Interaction: P01889; IntAct: EBI-21611619; Score: 0.35
DE  Interaction: P40259; IntAct: EBI-21668943; Score: 0.35
DE  Interaction: Q8IXI1; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: Q9NP73; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: Q96FC9; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: Q8WVS4; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: Q8NFG4; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: Q8IWA0; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: Q58WW2; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: Q15751; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: Q09019; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: O14727; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: O14531; IntAct: EBI-21689265; Score: 0.35
DE  Interaction: Q6ZN54; IntAct: EBI-21689078; Score: 0.35
DE  Interaction: Q9UBL9; IntAct: EBI-21802033; Score: 0.35
DE  Interaction: P19320; IntAct: EBI-21827844; Score: 0.35
DE  Interaction: Q93079; IntAct: EBI-20923794; Score: 0.40
DE  Interaction: P0DTC5; IntAct: EBI-25685699; Score: 0.35
DE  Interaction: D3DTS7; IntAct: EBI-25883142; Score: 0.56
DE  Interaction: Q96CV9; IntAct: EBI-25910907; Score: 0.56
GO  GO:0005776;
GO  GO:0030424;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0097635;
GO  GO:0019898;
GO  GO:0016234;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0043204;
GO  GO:0005886;
GO  GO:0016605;
GO  GO:0005545;
GO  GO:0046872;
GO  GO:0035973;
TP  Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:15292400};
SQ  MNMVKRIMGRPRQEECSPQDNALGLMHLRRLFTELCHPPRHMTQKEQEEKLYMMLPVFNRVFGNAPPNTMTEKFSDLLQF
SQ  TTQVSRLMVTEIRRRASNKSTEAASRAIVQFLEINQSEEASRGWMLLTTINLLASSGQKTVDCMTTMSVPSTLVKCLYLF
SQ  FDLPHVPEAVGGAQNELPLAERRGLLQKVFVQILVKLCSFVSPAEELAQKDDLQLLFSAITSWCPPYNLPWRKSAGEVLM
SQ  TISRHGLSVNVVKYIHEKECLSTCVQNMQQSDDLSPLEIVEMFAGLSCFLKDSSDVSQTLLDDFRIWQGYNFLCDLLLRL
SQ  EQAKEAESKDALKDLVNLITSLTTYGVSELKPAGITTGAPFLLPGFAVPQPAGKGHSVRNVQAFAVLQNAFLKAKTSFLA
SQ  QIILDAITNIYMADNANYFILESQHTLSQFAEKISKLPEVQNKYFEMLEFVVFSLNYIPCKELISVSILLKSSSSYHCSI
SQ  IAMKTLLKFTRHDYIFKDVFREVGLLEVMVNLLHKYAALLKDPTQALNEQGDSRNNSSVEDQKHLALLVMETLTVLLQGS
SQ  NTNAGIFREFGGARCAHNIVKYPQCRQHALMTIQQLVLSPNGDDDMGTLLGLMHSAPPTELQLKTDILRALLSVLRESHR
SQ  SRTVFRKVGGFVYITSLLVAMERSLSCPPKNGWEKVNQNQVFELLHTVFCTLTAAMRYEPANSHFFKTEIQYEKLADAVR
SQ  FLGCFSDLRKISAMNVFPSNTQPFQRLLEEDVISIESVSPTLRHCSKLFIYLYKVATDSFDSRAEQIPPCLTSESSLPSP
SQ  WGTPALSRKRHAYHSVSTPPVYPPKNVADLKLHVTTSSLQSSDAVIIHPGAMLAMLDLLASVGSVTQPEHALDLQLAVAN
SQ  ILQSLVHTERNQQVMCEAGLHARLLQRCSAALADEDHSLHPPLQRMFERLASQALEPMVLREFLRLASPLNCGAWDKKLL
SQ  KQYRVHKPSSLSYEPEMRSSMITSLEGLGTDNVFSLHEDNHYRISKSLVKSAEGSTVPLTRVKCLVSMTTPHDIRLHGSS
SQ  VTPAFVEFDTSLEGFGCLFLPSLAPHNAPTNNTVTTGLIDGAVVSGIGSGERFFPPPSGLSYSSWFCIEHFSSPPNNHPV
SQ  RLLTVVRRANSSEQHYVCLAIVLSAKDRSLIVSTKEELLQNYVDDFSEESSFYEILPCCARFRCGELIIEGQWHHLVLVM
SQ  SKGMLKNSTAALYIDGQLVNTVKLHYVHSTPGGSGSANPPVVSTVYAYIGTPPAQRQIASLVWRLGPTHFLEEVLPSSNV
SQ  TTIYELGPNYVGSFQAVCMPCKDAKSEGVVPSPVSLVPEEKVSFGLYALSVSSLTVARIRKVYNKLDSKAIAKQLGISSH
SQ  ENATPVKLIHNSAGHLNGSARTIGAALIGYLGVRTFVPKPVATTLQYVGGAAAILGLVAMASDVEGLYAAVKALVCVVKS
SQ  NPLASKEMERIKGYQLLAMLLKKKRSLLNSHILHLTFSLVGTVDSGHETSIIPNSTAFQDLLCDFEVWLHAPYELHLSLF
SQ  EHFIELLTESSEASKNAKLMREFQLIPKLLLTLRDMSLSQPTIAAISNVLSFLLQGFPSSNDLLRFGQFISSTLPTFAVC
SQ  EKFVVMEINNEEKLDTGTEEEFGGLVSANLILLRNRLLDILLKLIYTSKEKTSINLQACEELVKTLGFDWIMMFMEEHLH
SQ  STTVTAAMRILVVLLSNQSILIKFKEGLSGGGWLEQTDSVLTNKIGTVLGFNVGRSAGGRSTVREINRDACHFPGFPVLQ
SQ  SFLPKHTNVPALYFLLMALFLQQPVSELPENLQVSVPVISCRSKQGCQFDLDSIWTFIFGVPASSGTVVSSIHNVCTEAV
SQ  FLLLGMLRSMLTSPWQSEEEGSWLREYPVTLMQFFRYLYHNVPDLASMWMSPDFLCALAATVFPFNIRPYSEMVTDLDDE
SQ  VGSPAEEFKAFAADTGMNRSQSEYCNVGTKTYLTNHPAKKFVFDFMRVLIIDNLCLTPASKQTPLIDLLLEASPERSTRT
SQ  QQKEFQTYILDSVMDHLLAADVLLGEDASLPITSGGSYQVLVNNVFYFTQRVVDKLWQGMFNKESKLLIDFIIQLIAQSK
SQ  RRSQGLSLDAVYHCLNRTILYQFSRAHKTVPQQVALLDSLRVLTVNRNLILGPGNHDQEFISCLAHCLINLHVGSNVDGF
SQ  GLEAEARMTTWHIMIPSDIEPDGSYSQDISEGRQLLIKAVNRVWTELIHSKKQVLEELFKVTLPVNERGHVDIATARPLI
SQ  EEAALKCWQNHLAHEKKCISRGEALAPTTQSKLSRVSSGFGLSKLTGSRRNRKESGLNKHSLSTQEISQWMFTHIAVVRD
SQ  LVDTQYKEYQERQQNALKYVTEEWCQIECELLRERGLWGPPIGSHLDKWMLEMTEGPCRMRKKMVRNDMFYNHYPYVPET
SQ  EQETNVASEIPSKQPETPDDIPQKKPARYRRAVSYDSKEYYMRLASGNPAIVQDAIVESSEGEAAQQEPEHGEDTIAKVK
SQ  GLVKPPLKRSRSAPDGGDEENQEQLQDQIAEGSSIEEEEKTDNATLLRLLEEGEKIQHMYRCARVQGLDTSEGLLLFGKE
SQ  HFYVIDGFTMTATREIRDIETLPPNMHEPIIPRGARQGPSQLKRTCSIFAYEDIKEVHKRRYLLQPIAVEVFSGDGRNYL
SQ  LAFQKGIRNKVYQRFLAVVPSLTDSSESVSGQRPNTSVEQGSGLLSTLVGEKSVTQRWERGEISNFQYLMHLNTLAGRSY
SQ  NDLMQYPVFPWILADYDSEEVDLTNPKTFRNLAKPMGAQTDERLAQYKKRYKDWEDPNGETPAYHYGTHYSSAMIVASYL
SQ  VRMEPFTQIFLRLQGGHFDLADRMFHSVREAWYSASKHNMADVKELIPEFFYLPEFLFNSNNFDLGCKQNGTKLGDVILP
SQ  PWAKGDPREFIRVHREALECDYVSAHLHEWIDLIFGYKQQGPAAVEAVNVFHHLFYEGQVDIYNINDPLKETATIGFINN
SQ  FGQIPKQLFKKPHPPKRVRSRLNGDNAGISVLPGSTSDKIFFHHLDNLRPSLTPVKELKEPVGQIVCTDKGILAVEQNKV
SQ  LIPPTWNKTFAWGYADLSCRLGTYESDKAMTVYECLSEWGQILCAICPNPKLVITGGTSTVVCVWEMGTSKEKAKTVTLK
SQ  QALLGHTDTVTCATASLAYHIIVSGSRDRTCIIWDLNKLSFLTQLRGHRAPVSALCINELTGDIVSCAGTYIHVWSINGN
SQ  PIVSVNTFTGRSQQIICCCMSEMNEWDTQNVIVTGHSDGVVRFWRMEFLQVPETPAPEPAEVLEMQEDCPEAQIGQEAQD
SQ  EDSSDSEADEQSISQDPKDTPSQPSSTSHRPRAASCRATAAWCTDSGSDDSRRWSDQLSLDEKDGFIFVNYSEGQTRAHL
SQ  QGPLSHPHPNPIEVRNYSRLKPGYRWERQLVFRSKLTMHTAFDRKDNAHPAEVTALGISKDHSRILVGDSRGRVFSWSVS
SQ  DQPGRSAADHWVKDEGGDSCSGCSVRFSLTERRHHCRNCGQLFCQKCSRFQSEIKRLKISSPVRVCQNCYYNLQHERGSE
SQ  DGPRNC
//
ID  Q9XSC3;
PN  WD repeat-containing protein 44;
GN  WDR44;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:10077598}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10077598}. Endosome membrane {ECO:0000269|PubMed:10077598}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:10077598}. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia. {ECO:0000250}.
DR  UNIPROT: Q9XSC3;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Downstream effector for RAB11. May be involved in vesicle recycling. {ECO:0000269|PubMed:10077598}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASESDTEEFFDAPEDVHLEGGDPIGYPGKVGISALKETENSAYKVGNESTVQELKQDVSKKIIESIIEESQKVIQLEDD
SQ  SLDSKGKGQSDQATASPVTAGTELSNIPGLLAIDQVLQEDSQKAESQDVSEETELESKQCFPSDDTCEKPVDETTKLTEI
SQ  SSTAQLNVPETVTEVLNKEEVEVKESDVLESASSHSLSTKDFAVVEEVAPAKPPRQLTPEPDIVASTKKPVPARPPPPAN
SQ  FPPPRPPPPSRPAPPPRKKKSELEFEALKTPDLDVPKENITSDTLLTTNMASESTVKDSQPSLDLASATSGDKIVTAQEN
SQ  GKAPDGQTIAGEVMGPQRPRSNSGRELTDEEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTLHIMRRTKEYVSNDAA
SQ  QSDDEEKLQSQQTDTDGGRLKQKTTQLKKFLGKSVKRAKHLAEEYGERAVNKVKSVRDEVFHTDQDDPSSSDDEGMPYTR
SQ  PVKFKAAHGFKGPYDFDQIKVVQDLSGEHMGAVWTMKFSHCGRLLASAGQDNVVRIWALKNAFDYFNNMRMKYNTEGRVS
SQ  PSPSQESLNSSKSDTDTGVCSGTDEDPDDKNAPFRQRPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRRECL
SQ  CCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEVDGQTKLITAANFCQNGKYAVIGTYDGRCIFYDT
SQ  EHLKYHTQIHVRSTRGRNKVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGYVNSSSQIKASFSHDFNYL
SQ  VSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPSLMLSLDVQSEKSEGNEKGEDAEVLETMP
SQ  SGIMKTDNTEVLLSADFTGAIKVFINKRKNLS
//
ID  Q5JSH3;
PN  WD repeat-containing protein 44;
GN  WDR44;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia. {ECO:0000250}.
DR  UNIPROT: Q5JSH3;
DR  UNIPROT: B4DSE9;
DR  UNIPROT: F8W913;
DR  UNIPROT: Q0JS52;
DR  UNIPROT: Q0JTF3;
DR  UNIPROT: Q5JSH2;
DR  UNIPROT: Q6ZSC1;
DR  UNIPROT: Q7Z365;
DR  UNIPROT: Q7Z3P6;
DR  UNIPROT: Q8NAU8;
DR  UNIPROT: Q8NHU5;
DR  UNIPROT: Q9NUV4;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DR  OMIM: 301070;
DE  Function: Downstream effector for RAB11. May be involved in vesicle recycling (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: P00533; IntAct: EBI-32720286; Score: 0.27
DE  Interaction: P62993; IntAct: EBI-3964621; Score: 0.55
DE  Interaction: P68400; IntAct: EBI-5322147; Score: 0.44
DE  Interaction: P62492; IntAct: EBI-11042924; Score: 0.35
DE  Interaction: P62491; IntAct: EBI-11046571; Score: 0.35
DE  Interaction: Q9H8J5; IntAct: EBI-21537025; Score: 0.35
DE  Interaction: O95292; IntAct: EBI-21550215; Score: 0.35
DE  Interaction: Q9P0L0; IntAct: EBI-21550773; Score: 0.35
DE  Interaction: Q8TDQ0; IntAct: EBI-21556046; Score: 0.35
DE  Interaction: Q8WVZ9; IntAct: EBI-21562457; Score: 0.35
DE  Interaction: Q8NHX9; IntAct: EBI-21578009; Score: 0.35
DE  Interaction: Q15907; IntAct: EBI-21767106; Score: 0.35
DE  Interaction: Q9P0J1; IntAct: EBI-21817298; Score: 0.35
DE  Interaction: Q96CM8; IntAct: EBI-21817298; Score: 0.35
DE  Interaction: O95671; IntAct: EBI-21817298; Score: 0.35
DE  Interaction: P27824; IntAct: EBI-16788621; Score: 0.27
DE  Interaction: P15311; IntAct: EBI-16792219; Score: 0.27
DE  Interaction: P16284; IntAct: EBI-25881433; Score: 0.56
DE  Interaction: P11362; IntAct: EBI-32721578; Score: 0.27
DE  Interaction: P22455; IntAct: EBI-32722168; Score: 0.27
DE  Interaction: P08069; IntAct: EBI-32722947; Score: 0.27
DE  Interaction: P06213; IntAct: EBI-32723092; Score: 0.27
DE  Interaction: P07949; IntAct: EBI-32725031; Score: 0.27
DE  Interaction: Q01974; IntAct: EBI-32725367; Score: 0.27
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASESDTEEFYDAPEDVHLGGGYPVGSPGKVGLSTFKETENTAYKVGNESPVQELKQDVSKKIIESIIEESQKVLQLEDD
SQ  SLDSKGKELSDQATASPIVARTDLSNIPGLLAIDQVLPEESQKAESQNTFEETELELKKCFPSDETCEKPVDETTKLTQT
SQ  SSTEQLNVLETETEVLNKEAVEVKGGGDVLEPVSSDSLSTKDFAAVEEVAPAKPPRHLTPEPDIVASTKKPVPARPPPPT
SQ  NFPPPRPPPPSRPAPPPRKRKSELEFETLKTPDIDVPKENITSDSLLTASMASESTVKDSQPSLDLASATSGDKIVTAQE
SQ  NGKAPDGQTVAGEVMGPQRPRSNSGRELTDEEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTLHIMRRTKEYVSNDA
SQ  AQSDDEEKLQSQPTDTDGGRLKQKTTQLKKFLGKSVKRAKHLAEEYGERAINKVKSVRDEVFHTDQDDPSSSDDEGMPYT
SQ  RPVKFKAAHGFKGPYDFDQIKVVQDLSGEHMGAVWTMKFSHCGRLLASAGQDNVVRIWALKNAFDYFNNMRMKYNTEGRV
SQ  SPSPSQESLSSSKSDTDTGVCSGTDEDPDDKNAPFRQRPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRREC
SQ  LCCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEVDGQTKLITAANFCQNGKYAVIGTYDGRCIFYD
SQ  TEHLKYHTQIHVRSTRGRNKVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGYVNSSSQIKASFSHDFTY
SQ  LVSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPSLMLSLDVQSEKSEGNEKSEDAEVLDAT
SQ  PSGIMKTDNTEVLLSADFTGAIKVFVNKRKNVS
//
ID  Q6NVE8;
PN  WD repeat-containing protein 44;
GN  Wdr44;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia. {ECO:0000250}.
DR  UNIPROT: Q6NVE8;
DR  UNIPROT: Q3UT13;
DR  UNIPROT: Q8BTS1;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Downstream effector for RAB11. May be involved in vesicle recycling (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0031267;
GO  GO:0030334;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASESDTEEFYDAPEDVHLGTGYPVGSPGKVGLLSFKEAENTANQAGNESPVQELRQDVSKKIIESIIEESQKVLQLEDD
SQ  SLDSKGKGLSDEATAGPSVAGTEFSNIPGLLAIEHELQQDSEKAESQNVAEESELETQKCFPSDETCEKSEKTVDETDNL
SQ  TEVSSGEQLDASGLEAETLNKEALEVKEGDVLDPASLDTLSTTDFAAVEEVAPAKPPRHLTPEPDIVASTKKPVPARPPP
SQ  PTNFPPPRPPPPSRPAPPPRKKKSELEFEALKTPDLDVPKENITSDSLLTTNMASENTVRDSLPSLDLASATSGDKIVTA
SQ  QENGKAPDVQTVAGEVMGPQRPRSNSGRELTDEEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTLHIMRRTKEYVSN
SQ  DATQSDDEEKLQSQQTDTDGGRLKQKTTQLKKFLGKSVKRAKHLAEEYGERAINKVKSVRDEVFHTDQDDPSSSDDEGMP
SQ  YTRPVKFKAAHGFKGPYDFDQIKVVQDLSGEHMGAVWTMKFSHCGRLLASAGQDNIVRIWALKNAFDYFNNMRMKYNTEG
SQ  RVSPSPSQESLSSSKSDTDMGVCSGTDEDPDDKNAPFRQRPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRR
SQ  ECLCCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEVDGQTKLITAANFCQNGKYAVIGTYDGRCIF
SQ  YDTEHLKYHTQIHVRSTRGRNKVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGYVNSSSQIKASFSHDF
SQ  TYLVSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPSLMLSLDVQSEKLEGIDKYEDAEVLD
SQ  STSTGIVKTDNTEVLLSADFTGAIKVFINKRKTVS
//
ID  Q9R037;
PN  WD repeat-containing protein 44;
GN  Wdr44;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol {ECO:0000269|PubMed:10464283}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10464283}. Endosome membrane {ECO:0000269|PubMed:10464283}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:10464283}. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia.
DR  UNIPROT: Q9R037;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Downstream effector for RAB11. May be involved in vesicle recycling. {ECO:0000269|PubMed:10464283}.
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0005874;
GO  GO:0048471;
GO  GO:0031267;
GO  GO:0030334;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MMPLKMCTWGGSYPVGSPGKVGLLSFKETKNTGNKAGNESPVQELRQDVSKKIIECIIEESQKVLQLEDDSLDSKGKGLS
SQ  DQATASHSVAGTEFSNIPGLLAIQHELQQGSRKADSQNAAEETELETQKCFPSDNNCEKSEKTEDETNNLTEVSSADQLD
SQ  ASKLETEILNKEAVEVKEGDVVNPASSDALSTKDFAAVEEVAPAKPPRHLTPEPDIVASTKKPVPARPPPPTNFPPPRPP
SQ  PPSRPAPPPRKKKSDLEFEALKTPDLDVPKDNIASDSLLTTNMASESTVRDSLPSLDLASATSGDKIVTAQENGKAPDVQ
SQ  TVAGEVMGPQRPRSNSGRELTDEEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTPLTLHIMRRTKEYVSNDATQSDD
SQ  EEKLQSQQTDTDGGRLKQKTTQLKKFLGKSVKRAKHLAEEYGERAINKVKSVRDEVFHTDQDDPSSSDDEGMPYTRPVKF
SQ  KAAHGFKGPYDFDQIKVVQDLSGEHMGAVWTMKFSHCGRLLASAGQDNIVRIWALKNAFDYFNNMRMKYNTEGRVSPSPS
SQ  QESLSSSKSDTDMGVCSGTDEDPDDKNAPFRQRPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRRECLCCFQ
SQ  HIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEVDGQTKLITAANFCQNGKYAVIGTYDGRCIFYDTEHLK
SQ  YHTQIHVRSTRGRNKVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGYVNSSSQIKASFSHDFTYLVSGS
SQ  EDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPSLMLSLDVQSEKLEGIDKYEDAEVLDNTSTGIV
SQ  KTDNTEVLLSADFTGAQCFYVKNSFLYP
//
ID  Q498F0;
PN  WD repeat-containing protein 44;
GN  wdr44;
OS  8355;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network.
DR  UNIPROT: Q498F0;
DR  Pfam: PF00400;
DR  PROSITE: PS50082;
DR  PROSITE: PS50294;
DE  Function: Downstream effector for rab11. May be involved in vesicle recycling (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q6P5F9; IntAct: EBI-11606853; Score: 0.35
GO  GO:0005829;
GO  GO:0010008;
GO  GO:0005794;
GO  GO:0048471;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASDSDTEEFFDAPEDVNLSCSPAVSPLKSETFILKEEATYSKKAETRNIELKQDDSKEIIDSIIEESQKCSDTENENPV
SQ  VEEKTEVLHETLIGDSVKTKQDLLSNIPELVVTESTFHDGVEDPLQQQISEYLEPDISRSQDAGPSADSAYVPSAIENIV
SQ  DLTQDLKITEELKIAEEPEIPLIQEETKDPSKNIVEDVFSKLPTSDIIEQLPPAKPPRQICVEPDIVASTKKSGPNRPPQ
SQ  PINAPPPRPPPPARPAPPPRKKKGDTDFDRSSGFEYQKDGFLAGGLLSPNTLTENMNRDSQPSLDLASATSGEKIVTAQE
SQ  NGKAADGQLSSQSSECLGPQRPRSNSGRELTDDEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTLYIMRRTKEYVSN
SQ  DAAQSDDEEKPQSHQSETDGGKLKQKTTQLKKFLGKSVKRAKHLAEEYGERAVNKVKSVRDEVFHTDQDDPSSSDDEGMP
SQ  YTRPVKFKAAHGFKGPYDFEQIKVVQDLSGEHVGAVWTMKFSHCGRLLASAGQDNVVRIWVLKNAFDYFNNMRIKYNTEG
SQ  RVSPSPSQESLNSSKSDTDGGVFSGTDDVDPDDKNAPFRQVPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISR
SQ  RECLCCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEIDGQTKLITAANFCQNGKHAVIGTYDGRCI
SQ  FYDTEHLKYHTQIHVRSTRGRNRVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGCVNSSSQIKASFSHD
SQ  FTYIVSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPGLMVSAETSSEKQEGDQAEPVENIP
SQ  SGALKSDHTEVLLSADFTGAIKVFINKKKNIS
//
ID  Q8GXA4;
PN  WPP domain-interacting protein 1;
GN  WIP1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:22270916}. Nucleus membrane {ECO:0000269|PubMed:17600715}; Single-pass membrane protein {ECO:0000269|PubMed:17600715}; Cytoplasmic side {ECO:0000269|PubMed:17600715}. Note=Targeted to the nuclear envelope (NE) during interphase. Associated to the cell plate during cytokinesis in root tips.
DR  UNIPROT: Q8GXA4;
DR  UNIPROT: O65589;
DE  Function: Mediates and enhances the nuclear envelope docking of RANGAP proteins mediated by WIT1 and WIT2 in the undifferentiated cells of root tips (PubMed:17600715, PubMed:18591351). As component of the SUN- WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:18591351, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9LE82; IntAct: EBI-1779358; Score: 0.74
DE  Interaction: Q9M651; IntAct: EBI-1779572; Score: 0.37
DE  Interaction: Q9FH18; IntAct: EBI-1779584; Score: 0.62
DE  Interaction: Q9FMH6; IntAct: EBI-1779601; Score: 0.37
DE  Interaction: Q9C500; IntAct: EBI-1779624; Score: 0.37
DE  Interaction: Q94AV5; IntAct: EBI-1779708; Score: 0.37
DE  Interaction: Q8GXA4; IntAct: EBI-1779728; Score: 0.37
DE  Interaction: Q8L7E5; IntAct: EBI-1796688; Score: 0.57
DE  Interaction: O80594; IntAct: EBI-4485440; Score: 0.37
DE  Interaction: O80895; IntAct: EBI-4485696; Score: 0.37
DE  Interaction: O81062; IntAct: EBI-4485928; Score: 0.37
DE  Interaction: O82245; IntAct: EBI-4486272; Score: 0.37
DE  Interaction: P47192; IntAct: EBI-4488272; Score: 0.37
DE  Interaction: P59229; IntAct: EBI-4488840; Score: 0.37
DE  Interaction: P82874; IntAct: EBI-4489056; Score: 0.37
DE  Interaction: Q41975; IntAct: EBI-4491840; Score: 0.37
DE  Interaction: Q42342; IntAct: EBI-4491944; Score: 0.37
DE  Interaction: Q5XEV3; IntAct: EBI-4492400; Score: 0.37
DE  Interaction: Q5XF13; IntAct: EBI-4492432; Score: 0.37
DE  Interaction: Q6NLF5; IntAct: EBI-4493112; Score: 0.37
DE  Interaction: Q6NQG3; IntAct: EBI-4493928; Score: 0.37
DE  Interaction: Q84MC9; IntAct: EBI-4494952; Score: 0.37
DE  Interaction: Q8GWH4; IntAct: EBI-4496472; Score: 0.37
DE  Interaction: Q8GX70; IntAct: EBI-4496888; Score: 0.37
DE  Interaction: Q8GYN0; IntAct: EBI-4497904; Score: 0.37
DE  Interaction: Q8GYS8; IntAct: EBI-4497968; Score: 0.37
DE  Interaction: Q8L603; IntAct: EBI-4499504; Score: 0.37
DE  Interaction: Q8RXL7; IntAct: EBI-4502632; Score: 0.37
DE  Interaction: Q8RY98; IntAct: EBI-4502952; Score: 0.37
DE  Interaction: Q8S8K0; IntAct: EBI-4503040; Score: 0.37
DE  Interaction: Q8VYV9; IntAct: EBI-4504184; Score: 0.37
DE  Interaction: Q8VZ48; IntAct: EBI-4504264; Score: 0.37
DE  Interaction: Q8VZ95; IntAct: EBI-4504488; Score: 0.37
DE  Interaction: Q93V66; IntAct: EBI-4505640; Score: 0.37
DE  Interaction: Q93V85; IntAct: EBI-4505672; Score: 0.37
DE  Interaction: Q93ZQ3; IntAct: EBI-4507024; Score: 0.37
DE  Interaction: Q946Y7; IntAct: EBI-4508072; Score: 0.37
DE  Interaction: Q94A32; IntAct: EBI-4508312; Score: 0.37
DE  Interaction: Q94A99; IntAct: EBI-4508424; Score: 0.37
DE  Interaction: Q94AP3; IntAct: EBI-4508848; Score: 0.37
DE  Interaction: Q94CK3; IntAct: EBI-4509992; Score: 0.37
DE  Interaction: Q9LVZ7; IntAct: EBI-4510328; Score: 0.37
DE  Interaction: Q9FH92; IntAct: EBI-4514568; Score: 0.37
DE  Interaction: Q9FK55; IntAct: EBI-4515840; Score: 0.37
DE  Interaction: Q9FKK1; IntAct: EBI-4515920; Score: 0.37
DE  Interaction: Q9FL61; IntAct: EBI-4516000; Score: 0.37
DE  Interaction: Q9FVX3; IntAct: EBI-4517152; Score: 0.37
DE  Interaction: Q9FZ54; IntAct: EBI-4518088; Score: 0.37
DE  Interaction: Q9FZ98; IntAct: EBI-4518160; Score: 0.37
DE  Interaction: Q9LDU6; IntAct: EBI-4518408; Score: 0.37
DE  Interaction: Q9LJD9; IntAct: EBI-4519408; Score: 0.37
DE  Interaction: Q9LPF1; IntAct: EBI-4520296; Score: 0.37
DE  Interaction: Q9LQ32; IntAct: EBI-4520376; Score: 0.37
DE  Interaction: Q9LSF6; IntAct: EBI-4520888; Score: 0.37
DE  Interaction: Q9M2J9; IntAct: EBI-4524488; Score: 0.37
DE  Interaction: Q9M9S6; IntAct: EBI-4525176; Score: 0.37
DE  Interaction: Q9SA23; IntAct: EBI-4526072; Score: 0.37
DE  Interaction: Q9SCL4; IntAct: EBI-4526584; Score: 0.37
DE  Interaction: Q9SCZ8; IntAct: EBI-4526632; Score: 0.37
DE  Interaction: Q9SEL6; IntAct: EBI-4526784; Score: 0.37
DE  Interaction: Q9SHG7; IntAct: EBI-4527240; Score: 0.37
DE  Interaction: Q9SIH4; IntAct: EBI-4527512; Score: 0.37
DE  Interaction: Q9SRE4; IntAct: EBI-4529368; Score: 0.37
DE  Interaction: Q9STW3; IntAct: EBI-4529904; Score: 0.37
DE  Interaction: Q9SY29; IntAct: EBI-4530832; Score: 0.37
DE  Interaction: Q9XI60; IntAct: EBI-4531816; Score: 0.37
DE  Interaction: Q9ZQ38; IntAct: EBI-4532040; Score: 0.37
DE  Interaction: Q9ZSR7; IntAct: EBI-4532384; Score: 0.37
DE  Interaction: Q9ZUJ2; IntAct: EBI-4532600; Score: 0.37
DE  Interaction: Q9ZVX8; IntAct: EBI-4532992; Score: 0.37
DE  Interaction: Q8GW44; IntAct: EBI-11657628; Score: 0.49
DE  Interaction: Q84MC7; IntAct: EBI-25528414; Score: 0.56
GO  GO:0009504;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0006997;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLESESSALESVDDNVLIQQSASNVCDDGRSLDNGSCSDESVKLLSTSNSVELGKPMSFDSPGDGGGAYSPVLKGQGLR
SQ  KWRRIRRDLVKDTSANMENSKALKRGLSGVAHSHGKQMQFQSPEVEQESQGSVGSVNMLKSSGDGFDILGSSGYDSRFVA
SQ  GVGFSAGMDLEIDDDRSSKSSTVARAPKVIRYEKPMISSGQGGNIRVENSKKHRGESVDFEKENSYSSLESDSRKQSGRM
SQ  MDYNGENGETSMRKDDAGGEGGESINTDNRYSDEMDPLTEAINGFLALQDALEKEVQQFQEIGNEPMPQHHEQVSEANSP
SQ  HPEIVTLVNNVEQLENMLEETRSMLEVKESHIRDLESTTNQSKHSWGGTEIVVEDIFRQKIEAEIEYLIYSRSIDNLNSQ
SQ  MKLIDEQESLAEEQTHETLNKLGRVQTKAANFTNRAQDLQNDCIEITGTIKKRACKITSYVLIQLVLLSTVVLLLLSQLL
SQ  PEPDTVVPT
//
ID  Q9FH18;
PN  WPP domain-interacting protein 2;
GN  WIP2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:22270916}. Nucleus membrane {ECO:0000269|PubMed:17600715}; Single-pass membrane protein {ECO:0000269|PubMed:17600715}; Cytoplasmic side {ECO:0000269|PubMed:17600715}. Note=Targeted to the nuclear envelope (NE) during interphase. Associated to the cell plate during cytokinesis in root tips.
DR  UNIPROT: Q9FH18;
DR  UNIPROT: Q5XUY7;
DR  UNIPROT: Q5XUY8;
DE  Function: Mediates and enhances the nuclear envelope docking of RANGAP proteins mediated by WIT1 and WIT2 in the undifferentiated cells of root tips (PubMed:17600715). As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1779584; Score: 0.62
DE  Interaction: Q8L7E5; IntAct: EBI-1796676; Score: 0.51
DE  Interaction: Q9C500; IntAct: EBI-1779631; Score: 0.37
DE  Interaction: Q9FF75; IntAct: EBI-11657658; Score: 0.37
DE  Interaction: Q9LE82; IntAct: EBI-1779474; Score: 0.59
DE  Interaction: Q9M651; IntAct: EBI-1779579; Score: 0.37
DE  Interaction: Q9FH18; IntAct: EBI-1779591; Score: 0.55
DE  Interaction: Q9FMH6; IntAct: EBI-1779608; Score: 0.37
DE  Interaction: Q8GW44; IntAct: EBI-11657663; Score: 0.37
GO  GO:0009504;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0046982;
GO  GO:0042803;
GO  GO:0006997;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLESESSVLESVEDNNGLIGDLDKELNSPVETSPLISKGFGLRKWKRRLRRDLVKDDTSVSMENSKALKRVLSGLVDPN
SQ  AKQMHLPGPEVRQDSVGSVGSVNSVVGFVMGGESYGNGLAFAAGVDSDNSEDRSSTMSHSWDKHRGKVSGGKSVISSGDS
SQ  SQQRKSSVEKSNKLRGERIKIEKENSHSSMESADSRSSNFVFMQGASYSLSSREQGGRRMMDYDDENSDHDAHTSKRKDN
SQ  VEEEEEETEDYSQGDCVEESQIKSNGSSDNLDPLIVAVNSFQTLQEALQKELQKFQELGKEEPITSLHDGGESSSCIHAG
SQ  HEGASEASSSYRFGSEKMGEMELTSLDSEILNLVNNVEHLEIKLEEAKRILEVKETQIRELESTINVSETCNGGTEIGIE
SQ  DIFQQKVEAEIEYIIFSRSVGNLKRRIKLIEEEKTLGLSKLDKAETKAENLKNQAQDLQNHCVEITEIQEVECLKKRAFK
SQ  TTRCLLLQLGLLFILYYSLLPEPEIAVPT
//
ID  Q94AV5;
PN  WPP domain-interacting protein 3;
GN  WIP3;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:22270916}. Nucleus membrane {ECO:0000269|PubMed:17600715}; Single-pass membrane protein {ECO:0000269|PubMed:17600715}; Cytoplasmic side {ECO:0000269|PubMed:17600715}.
DR  UNIPROT: Q94AV5;
DR  UNIPROT: Q9LTT2;
DE  Function: Mediates and enhances the nuclear envelope docking of RANGAP proteins mediated by WIT1 and WIT2 in the undifferentiated cells of root tips (PubMed:17600715). As component of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to the nuclear envelope (NE), leading to nuclear shape changes (PubMed:25759303). {ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:25759303}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1779708; Score: 0.37
DE  Interaction: Q9LE82; IntAct: EBI-1779492; Score: 0.49
DE  Interaction: Q9FMH6; IntAct: EBI-1779613; Score: 0.37
DE  Interaction: Q9C500; IntAct: EBI-1779636; Score: 0.37
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0006997;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MNESVPDSVEDNGNSVPANGLLVLPDNDHEEGGVGSPQRSNSVESPGGSVHSTRKGFGLKKWRRIKRDGPVRDEAAPVDD
SQ  GSKLLKRGLAGLVNPPSKHVEFSSVEARQSSEGSVGSVNMVHHPGVANGFSPDIGCMFAVGQAFEKSEEHSGNTIGGKNV
SQ  VGGKVVSGSQEKLWSDTIKRASEERGDIEKEKPCSSLDSDLRSSDFVFSTGSVSVGNHGEKDERLTMNYIGGFSNEGQVK
SQ  EEVQTYSRSENGNKEDDGESKKNNNHWADKDALADSIRSFAVLQEVLWKEVQSFQELGKESVLLHSNTDELSSDQPSHQN
SQ  CKEDNSTSSGSKALILKEKVKLLEHKLEEARAALEAKEARIQELENSKIESELECIFQRKIETEIEHLMLTRSLSSLQVL
SQ  QETKKLHSLKEDPVSNRGNILGKTCKLGFYILTQLILLVSILRFLVLQFSPASRLVIPT
//
ID  Q8L7E5;
PN  WPP domain-interacting tail-anchored protein 1;
GN  WIT1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus envelope. Nucleus membrane; Single-pass membrane protein. Note=During cytokinesis, aggregates around nuclear pores at the cell plate.
DR  UNIPROT: Q8L7E5;
DR  UNIPROT: Q9LFL8;
DE  Function: Together with WIT2, required for the nuclear envelope docking of RANGAP proteins in root tips. {ECO:0000269|PubMed:18591351}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1796688; Score: 0.57
DE  Interaction: Q9C500; IntAct: EBI-1796624; Score: 0.35
DE  Interaction: Q9LE82; IntAct: EBI-1796664; Score: 0.62
DE  Interaction: Q9M651; IntAct: EBI-1796671; Score: 0.37
DE  Interaction: Q9FH18; IntAct: EBI-1796676; Score: 0.51
DE  Interaction: Q8L7E5; IntAct: EBI-1796759; Score: 0.40
DE  Interaction: Q0WQ91; IntAct: EBI-1796782; Score: 0.40
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  METETEHDRTVSVDDNDSLVPEPSSTKESFFEDLSLTGQVMNPQLSSAGEVLTKVELDFAFVSEKLVNLSLLTMQLGTRE
SQ  NDFESFVSKKEEDEEEPSSNVDDDDDSAEKALEFDLLSSILNSEVKELESLLGFLQNEIQSARVMISPFQHDGEAFLDLE
SQ  GKLNDTEQSLGQLMEQVVEMKKQSSNFQRLSSGLDEQGSWSGGQTSVSQNDGEFGDLSAKINMQTADQQRNVLRMLEKSL
SQ  AKEMELEKKLSESRNTERELEMKLYSSEQDVVYMEEVTEDAFSRWLEADNAAEVFKGTSKEMSGKLQILQFNLSGSFKRE
SQ  DNLKSKLVDSKERLEAKECALHKLDSSNARLADFLVAQTEGLKESLQEAEEKLILLNTENSTLSEKVSSLEEQLNEYGIQ
SQ  TEDADATSGALITDLERINEELKDKLAKTEARAEETESKCKILEESKKELQDELGNFRDKGFTIHKLASLEKHLRDSDLQ
SQ  LEHAVAAVEASKEKQNLLYSTVSDMEDVIEDLKSKVLKAENRADITEEKLIMVSESNAEVNEELKFFKGRLKEGEKYLQQ
SQ  AEERKLRTAKDIGVHNKIMKKLVMQLAAERERLHKQITNLSRENCVLMVKLKKVGKTGYMESGNGSEVSPKSDQNASSCH
SQ  QGSRLQATFISLTNPEEEETGSKSDIGSVRRLDVGALRFKHILVAILVILISSIAYVISQQNM
//
ID  Q9FMH6;
PN  WPP domain-containing protein 1;
GN  WPP1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:15548735}. Cytoplasm {ECO:0000269|PubMed:15548735}. Nucleus {ECO:0000269|PubMed:15548735}. Golgi apparatus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Note=Associated to the nuclear envelope (NE) in undifferentiated cells of the root tip. Associated with the outer NE and the nuclear pores in interphase cells and with the immature cell plate during cytokinesis. In differentiated cells, localized in both cytoplasm and nucleus. Accumulate in speckles of the cytoplasm belonging to the Golgi apparatus (By similarity). Appears at the NE as cells reenter the cell cycle during dedifferentiation. {ECO:0000250}.
DR  UNIPROT: Q9FMH6;
DR  UNIPROT: Q8L8R9;
DR  Pfam: PF13943;
DE  Function: Regulates the mitotic activity in roots. Plays a role with HSP70-1 in facilitating WIT1 nuclear envelope targeting. {ECO:0000269|PubMed:15548735, ECO:0000269|PubMed:19617588}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1779601; Score: 0.37
DE  Interaction: Q94AV5; IntAct: EBI-1779613; Score: 0.37
DE  Interaction: Q9FH18; IntAct: EBI-1779608; Score: 0.37
GO  GO:0005794;
GO  GO:0016363;
GO  GO:0005640;
GO  GO:0009536;
GO  GO:0048527;
GO  GO:0000278;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETETESITTSSPPPISETENSTTLPTTETEKNPNPVTISLRIWPPTQKTRDAVINRLIETLSTESILSKRFGSLESEE
SQ  ASSVAKSIEDEAYAIASATVFGDDDGIEILKAYSKEISKRMLESVKAKSNVASPPPKDGDGIESAVDSKIDSSEA
//
ID  Q9C500;
PN  WPP domain-containing protein 2;
GN  WPP2;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Comments: Nucleus envelope {ECO:0000269|PubMed:15548735}. Cytoplasm {ECO:0000269|PubMed:15548735}. Nucleus {ECO:0000269|PubMed:15548735}. Golgi apparatus {ECO:0000250}. Note=Associated to the nuclear envelope (NE) in undifferentiated cells of the root tip. Associated with the outer NE and the nuclear pores in interphase cells and with the immature cell plate during cytokinesis. In differentiated cells, localized in both cytoplasm and nucleus. Accumulate in speckles of the cytoplasm belonging to the Golgi apparatus (By similarity). Appears at the NE as cells reenter the cell cycle during dedifferentiation. {ECO:0000250}.
DR  UNIPROT: Q9C500;
DR  UNIPROT: Q8LE13;
DR  Pfam: PF13943;
DE  Function: Regulates the mitotic activity in roots. Plays a role with HSP70-1 in facilitating WIT1 nuclear envelope targeting. {ECO:0000269|PubMed:15548735, ECO:0000269|PubMed:19617588}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8GXA4; IntAct: EBI-1779624; Score: 0.37
DE  Interaction: Q8L7E5; IntAct: EBI-1796624; Score: 0.35
DE  Interaction: Q94AV5; IntAct: EBI-1779636; Score: 0.37
DE  Interaction: Q9FH18; IntAct: EBI-1779631; Score: 0.37
DE  Interaction: A8MQR0; IntAct: EBI-1796624; Score: 0.35
DE  Interaction: Q8L4Q6; IntAct: EBI-4511528; Score: 0.37
GO  GO:0005794;
GO  GO:0005640;
GO  GO:0005634;
GO  GO:0048527;
GO  GO:0000278;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAETAETINTTISSPPPESESSTTISAMTDPTSQEAASKDTDLTKEAESEKKPGGISLRIWPPTQKTRDAVLNRLIETLS
SQ  TESILSKRYGTLKSDDATTVAKLIEEEAYGVASNAVSSDDDGIKILELYSKEISKRMLESVKARSNASVGNGSVEDANTD
SQ  ASEVSKDDAGPASEEEKSEA
//
ID  Q9H6D3;
PN  XK-related protein 8, processed form;
GN  XKR8;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:27503893, ECO:0000269|PubMed:28881496}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:28881496}.
DR  UNIPROT: Q9H6D3;
DR  PDB: 7DCE;
DR  Pfam: PF09815;
DR  DisGeNET: 55113;
DE  Function: [XK-related protein 8, processed form]: Phospholipid scramblase that promotes phosphatidylserine exposure on apoptotic cell surface (PubMed:23845944, PubMed:25231987). Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment (PubMed:23845944). Required for the clearance of apoptotic cells, such as engulfment of apoptotic germ cells by Sertoli cells, clearance of senescent neutrophils or regulation of bipolar cell numbers in the retina (By similarity). Has no effect on calcium-induced exposure of phosphatidylserine (PubMed:23845944). Promotes myoblast differentiation and survival (PubMed:28881496). {ECO:0000250|UniProtKB:Q8C0T0, ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:28881496}. (Microbial infection) Incorporated into Ebola virus-like particles, where its phospholipid scramblase activity is required to promote phosphatidylserine exposure on the surface of viral particles (PubMed:29338048). Externalization of phosphatidylserine on the surface of viral particles is required for uptake by host cells (PubMed:29338048). {ECO:0000269|PubMed:29338048}.
DE  Reference Proteome: Yes;
DE  Interaction: P43119; IntAct: EBI-21748886; Score: 0.35
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0017128;
GO  GO:1902742;
GO  GO:0043652;
GO  GO:0051649;
GO  GO:0097350;
GO  GO:0070782;
GO  GO:0045663;
GO  GO:0002513;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPWSSRGALLRDLVLGVLGTAAFLLDLGTDLWAAVQYALGGRYLWAALVLALLGLASVALQLFSWLWLRADPAGLHGSQP
SQ  PRRCLALLHLLQLGYLYRCVQELRQGLLVWQQEEPSEFDLAYADFLALDISMLRLFETFLETAPQLTLVLAIMLQSGRAE
SQ  YYQWVGICTSFLGISWALLDYHRALRTCLPSKPLLGLGSSVIYFLWNLLLLWPRVLAVALFSALFPSYVALHFLGLWLVL
SQ  LLWVWLQGTDFMPDPSSEWLYRVTVATILYFSWFNVAEGRTRGRAIIHFAFLLSDSILLVATWVTHSSWLPSGIPLQLWL
SQ  PVGCGCFFLGLALRLVYYHWLHPSCCWKPDPDQVDGARSLLSPEGYQLPQNRRMTHLAQKFFPKAKDEAASPVKG
//
ID  Q8C0T0;
PN  XK-related protein 8, processed form;
GN  Xkr8;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000269|PubMed:25231987}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H6D3}.
DR  UNIPROT: Q8C0T0;
DR  Pfam: PF09815;
DE  Function: [XK-related protein 8, processed form]: Phospholipid scramblase that promotes phosphatidylserine exposure on apoptotic cell surface (PubMed:23845944, PubMed:25231987, PubMed:27503893, PubMed:29440417, PubMed:30718401). Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment (PubMed:23845944, PubMed:29440417, PubMed:30718401, PubMed:31712393). Required for the clearance of apoptotic cells, such as engulfment of apoptotic germ cells by Sertoli cells, clearance of senescent neutrophils or regulation of bipolar cell numbers in the retina (PubMed:30559640, PubMed:29440417, PubMed:31712393). Has no effect on calcium-induced exposure of phosphatidylserine (By similarity). Promotes myoblast differentiation and survival (PubMed:28881496). {ECO:0000250|UniProtKB:Q9H6D3, ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:27503893, ECO:0000269|PubMed:28881496, ECO:0000269|PubMed:29440417, ECO:0000269|PubMed:30559640, ECO:0000269|PubMed:30718401, ECO:0000269|PubMed:31712393}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0017128;
GO  GO:1902742;
GO  GO:0043652;
GO  GO:0051649;
GO  GO:0097350;
GO  GO:0070782;
GO  GO:0045663;
GO  GO:0002513;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPLSVHHHVALDVVVGLVSILSFLLDLVADLWAVVQYVLLGRYLWAALVLVLLGQASVLLQLFSWLWLTADPTELHHSQL
SQ  SRPFLALLHLLQLGYLYRCLHGMHQGLSMCYQEMPSECDLAYADFLSLDISMLKLFESFLEATPQLTLVLAIVLQNGQAE
SQ  YYQWFGISSSFLGISWALLDYHRSLRTCLPSKPRLGRSSSAIYFLWNLLLLGPRICAIALFSAVFPYYVALHFFSLWLVL
SQ  LFWIWLQGTNFMPDSKGEWLYRVTMALILYFSWFNVSGGRTRGRAVIHLIFIFSDSVLLVTTSWVTHGTWLPSGISLLMW
SQ  VTIGGACFFLGLALRVIYYLWLHPSCSWDPDLVDGTLGLLSPHRPPKLIYNRRATLLAENFFAKAKARAVLTEEVQLNGV
SQ  L
//
ID  Q49LS0;
PN  XK-related protein 8, processed form;
GN  XKR8;
OS  9598;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:Q8C0T0}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H6D3}.
DR  UNIPROT: Q49LS0;
DR  Pfam: PF09815;
DE  Function: [XK-related protein 8, processed form]: Phospholipid scramblase that promotes phosphatidylserine exposure on apoptotic cell surface. Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment. Required for the clearance of apoptotic cells, such as engulfment of apoptotic germ cells by Sertoli cells, clearance of senescent neutrophils or regulation of bipolar cell numbers in the retina (By similarity). Has no effect on calcium-induced exposure of phosphatidylserine (By similarity). Promotes myoblast differentiation and survival (By similarity). {ECO:0000250|UniProtKB:Q8C0T0, ECO:0000250|UniProtKB:Q9H6D3}.
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0017128;
GO  GO:0043652;
GO  GO:0097350;
GO  GO:0070782;
GO  GO:0045663;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPWSSRGALLRDLVLGVLGTAAFLLDLGTDLWAAVQYALGGRYLWAALVLALLGLASVALQLFSWLWLRADPAGLHGSQP
SQ  PRRCLALLHLLQLGYLYRCVQELRQGLLVWQQEEPSEFDLAYADFLALDISMLRLFETFLETAPQLTLVLAIMLQSGRAE
SQ  YYQWVGICTSFLGISWALLDYHRALRTCLPSRPLLGLGSSVIYFLWNLLLLWPRVLAVALFSALFPSYVALHFLGLWLVL
SQ  LLWVWLQGTDFMPDPSSEWLYQVTVATILYFSWFNVAEGRTRGRAIIHFAFLLSDSILLVATWVTHSSWLPSGIPLQLWL
SQ  PVGCGCFFLGLALRLVYYHWLHPSCCWKPDPDQVDGARSLLSPEGYQLPQNRRMTHLAQNFFPKAKDEAALPVKG
//
ID  Q9U3V9;
PN  Protein xmas;
GN  xmas;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus, nucleoplasm {ECO:0000269|PubMed:28472469}. Nucleus {ECO:0000269|PubMed:29779104, ECO:0000269|Ref.7}. Nucleus membrane {ECO:0000269|PubMed:18034162, ECO:0000269|PubMed:27016737, ECO:0000269|PubMed:28472469, ECO:0000269|PubMed:33602059}; Peripheral membrane protein {ECO:0000269|PubMed:18034162, ECO:0000269|PubMed:27016737, ECO:0000269|PubMed:28472469, ECO:0000269|PubMed:33602059}. Cytoplasm {ECO:0000269|PubMed:33602059}. Note=Localizes to nuclear periphery, often in contact with the nuclear pore complex (NPC). {ECO:0000269|PubMed:18034162, ECO:0000269|PubMed:27016737}.
DR  UNIPROT: Q9U3V9;
DR  UNIPROT: A0A4D6K557;
DR  UNIPROT: C9QP61;
DR  UNIPROT: D0IQ87;
DR  UNIPROT: H1UUM5;
DR  UNIPROT: Q8IR02;
DR  UNIPROT: Q8MQS3;
DR  UNIPROT: Q9U3V8;
DR  UNIPROT: Q9VX76;
DR  Pfam: PF03399;
DR  PROSITE: PS50250;
DR  PROSITE: PS50102;
DE  Function: Involved in mRNA export and mRNA coupled transcription activation (PubMed:18034162, PubMed:27016737, PubMed:33602059). Component of the nuclear pore complex (NPC)-associated TREX-2/AMEX complex (anchoring and mRNA export complex) which functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), thereby enabling the export of mRNAs to the cytoplasm through the nuclear pores (PubMed:18034162, PubMed:27016737). The TREX-2/AMEX complex also functions with the transcriptional coactivator SAGA/TFTC complex, to anchor a subset of transcription sites to the nuclear pore complex basket in order to achieve efficient transcription and export of their resulting mRNAs (PubMed:18034162). Within the complex, required for localization of e(y)2 to the nuclear periphery (PubMed:18034162). {ECO:0000269|PubMed:18034162, ECO:0000269|PubMed:27016737, ECO:0000269|PubMed:33602059}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7JXF5; IntAct: EBI-2554458; Score: 0.46
DE  Interaction: Q9VYX1; IntAct: EBI-2550885; Score: 0.54
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0070390;
GO  GO:0043021;
GO  GO:0003723;
GO  GO:0006406;
GO  GO:0048477;
GO  GO:0016973;
GO  GO:0045944;
GO  GO:0007283;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MAEPRPGGYNYKTLLCRNIPELFLDKYVARSHFGRFGTLVNFVLRPRRMTCTVSYASEDEAARALLDGASFQGHLFDISY
SQ  ADNETAPAQKTEEWVDPDIQAELSALQSGWRNEYGSGKPIKKPQNGSSGSGGSSMLPAIPVGPATAPVSRDRTPAQLRDL
SQ  ENMMRRPAHTSEEKFSVLDARDKLLRLNRTQHKLSGATQGHCADMCPEKERVLREFQRQVAYYELQPGSDELICHERALK
SQ  QYSRSSADQETPLPHELRNETALHMTMSYLMHEIMDISERQDPQSHMGDWFHFVWDRTRSIRKEITQQELCSLGAVKLVE
SQ  QCARFHIHCAARLVDADPSVFDSKINAENLTKCLQTLKYMYHDLRIKGVPCPKEAEFRGYIVLLNLADANFLWDIGQLPA
SQ  ELQSCPEVRQAIQFYLALQDTNFVRFFQLLADKDTSYLSACILVNYFTRLRVLGLHRLIQAYRSPRKDEVSSLPLSYIAE
SQ  LLSFASEQEAADFVQHYGLQINEAGRVVLSRMHTVETEYKLPRQYELVEVKRVKSVGEVVSGEPLPPRDLYLNHRPHNSF
SQ  DDYGMLKSIAWTAKDQLAGMQQEEMQPQMPSQPPAVSKHSDTLFKVPMQPDGTAAGFGVFAAAAVPPASSIDGFSFVLPK
SQ  SRAQEFQEQAPATQQRRAQEEAKHQALQVAIAAAKKREAELMAIHEAKVAEAERVRQQKLRERQEQQRRQQQELEEQRQR
SQ  EQEKLQLEKERQLKLEQLFFVQQQEREAHKQTRTLELYQEIFQDTLAEICQSEFMSHSRACRSYESMLDSITRDLVERQM
SQ  EQSIYELGVMRVCIRRWRKYRRTQQEKDTLFNQLPLSFGAENPEGVVNKRSMEDSLRLSRRYRLGEPCDYGKLLAGLEEH
SQ  SWLKLDLWHVLDKCLPVAQPGARRFYKLLISLSGGQEGLQLNCDLDRGLLQQPQSPDARFVDGGYIRGFSQGIGLSVMKI
SQ  RDDDHDWKATDLAEANGIICLIGLDDIRLLPDRLKPLLQASRCHDVAVIVQHPANTAFVQPDIPLQELCLRSFNIFRLRK
SQ  SGNNRQRLMIALESAVKFLAKATERKRVGHLHQVETREYLLVNLGSELFRRLKYAAEHDTAIRSDTQLNPQRCVDLFNEA
SQ  VHRLQLVAGEDLSDWPQFPEELRVFVQPLPIESSLNTNRLEHFEPGWHLPERRQRIVQLLERCKLPKMPVLPRSSSLAEA
SQ  QCQWVLDYAQISQQEDCVEQIALQAIKILQYDTDDYLNFVEYLAGERMQYILRQERNPPQGIVYNTKTLKRRFLSAWYYE
SQ  FREPQIYEPVPAEENAQMLEKQPSSQAEVQQLDFDEITSKAEAVLKRFHQRQDERHTLRELNRSHKSRKRRDASDHKHAM
SQ  SSLVSALKAARSDYQGKSSAVCRLVAQMVEADQVKYQWTPNLTSLIDRKDASTRHQWRPHVNHSTRHARKLPVQSISFLS
SQ  RCLAKKGEHAGLTSCVLSVKTRYAPKTLHGRELLIWRQSSMRPLLLPSSNLWTGVLSKRHYVPRLRPAEEDEEVERRAVP
SQ  QLRITKEQSEEEEHQLQRRKDGSRLRNECSEFYLPMGEQDYSEREEENRGHRQAYVPSELMTPELATKWQTTSVTDRDRQ
SQ  LLNLEQQMKTQPSVRMTTQTWFSGNHRRYRSRRSGAKRYHVVSELEGWRRSSNHQPVPVFQGQPGEQEHLRHASHKASAR
SQ  SMPDGQERCQMVWEQKKRSPWHRTEVTNSNKVRMPRIRAAKSAVMMAQEARNKHHRLITKKLVYRPRRTVNAVQAEETED
SQ  QDTHHRHHGGGQKMSKRAPERALLKQHLADLLAVSKPEDSFRIGYQPNAPTRQLLEQGKCYVSLRREQFIHLHPVRPNSL
SQ  ILAVNLEVKESPRQPVTTLHRRDGAKRPRLVEDVVKPSLITVIRQSAATWDHNGRKVPAKKSNLVGMPSKEHAYQRRLVR
SQ  NTSTLEAIVKAQAKPRSEPKSPSSATDYHRVASQKLPHVTSKADISKAADPFKDLDKPRIKEKEVASSWKQAYVVRSKMY
SQ  DAITPYRRRAYPGKKCITKDKTDGYFLAKRSSAAAAGSSKKVKPPKQPVVSPKVQVPSVLHKKKSRESLGPQTTKTGKL
//
ID  Q9SMV6;
PN  Protein EXPORTIN 1A;
GN  XPO1;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9TVM2}. Nucleus membrane {ECO:0000250|UniProtKB:Q9TVM2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9TVM2}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9TVM2}.
DR  UNIPROT: Q9SMV6;
DR  UNIPROT: F4KFL2;
DR  Pfam: PF08767;
DR  Pfam: PF18777;
DR  Pfam: PF18784;
DR  Pfam: PF18787;
DR  Pfam: PF03810;
DR  Pfam: PF08389;
DR  PROSITE: PS50166;
DE  Function: Receptor for the leucine-rich nuclear export signal (NES). Binds cooperatively to the NES on its target protein and to the small GTPase Ran in its active GTP-bound form (PubMed:10652141, PubMed:16766674). Required for the maternal-to-embryonic transition and during gametophyte development (PubMed:18791220). Involved in heat- induced oxidative stress basal resistance (PubMed:20345641). {ECO:0000269|PubMed:10652141, ECO:0000269|PubMed:16766674, ECO:0000269|PubMed:18791220, ECO:0000269|PubMed:20345641}.
DE  Reference Proteome: Yes;
DE  Interaction: Q67Y93; IntAct: EBI-1647715; Score: 0.37
DE  Interaction: Q941D1; IntAct: EBI-1647730; Score: 0.37
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005049;
GO  GO:0031267;
GO  GO:0009553;
GO  GO:0051028;
GO  GO:0009555;
GO  GO:0009846;
GO  GO:0009860;
GO  GO:0006611;
GO  GO:0009408;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9TVM2};
SQ  MAAEKLRDLSQPIDVGVLDATVAAFFVTGSKEERAAADQILRDLQANPDMWLQVVHILQNTNSLDTKFFALQVLEGVIKY
SQ  RWNALPVEQRDGMKNYISEVIVQLSSNEASFRSERLYVNKLNVILVQIVKHDWPAKWTSFIPDLVAAAKTSETICENCMA
SQ  ILKLLSEEVFDFSRGEMTQQKIKELKQSLNSEFKLIHELCLYVLSASQRQDLIRATLSALHAYLSWIPLGYIFESTLLET
SQ  LLKFFPVPAYRNLTIQCLTEVAALNFGDFYNVQYVKMYTIFIGQLRIILPPSTKIPEAYSSGSGEEQAFIQNLALFFTSF
SQ  FKFHIRVLESTPEVVSLLLAGLEYLINISYVDDTEVFKVCLDYWNSLVLELFDAHHNSDNPAVSASLMGLQPFLPGMVDG
SQ  LGSQVMQRRQLYSHPMSKLRGLMINRMAKPEEVLIVEDENGNIVRETMKDNDVLVQYKIMRETLIYLSHLDHDDTEKQML
SQ  RKLNKQLSGEEWAWNNLNTLCWAIGSISGSMAEDQENRFLVMVIRDLLNLCEITKGKDNKAVIASNIMYVVGQYPRFLRA
SQ  HWKFLKTVVNKLFEFMHETHPGVQDMACDTFLKIVQKCKRKFVIVQVGENEPFVSELLTGLATTVQDLEPHQIHSFYESV
SQ  GNMIQAESDPQKRDEYLQRLMALPNQKWAEIIGQARHSVEFLKDQVVIRTVLNILQTNTSAATSLGTYFLSQISLIFLDM
SQ  LNVYRMYSELVSTNITEGGPYASKTSFVKLLRSVKRETLKLIETFLDKAEDQPHIGKQFVPPMMESVLGDYARNVPDARE
SQ  SEVLSLFATIINKYKATMLDDVPHIFEAVFQCTLEMITKNFEDYPEHRLKFFSLLRAIATFCFPALIKLSSPQLKLVMDS
SQ  IIWAFRHTERNIAETGLNLLLEMLKNFQQSEFCNQFYRSYFMQIEQEIFAVLTDTFHKPGFKLHVLVLQQLFCLPESGAL
SQ  TEPLWDATTVPYPYPDNVAFVREYTIKLLSSSFPNMTAAEVTQFVNGLYESRNDPSGFKNNIRDFLVQSKEFSAQDNKDL
SQ  YAEEAAAQRERERQRMLSIPGLIAPNEIQDEMVDS
//
ID  F4IZR5;
PN  Protein EXPORTIN 1B;
GN  XPO1B;
OS  3702;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9TVM2}. Nucleus membrane {ECO:0000250|UniProtKB:Q9TVM2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9TVM2}; Nucleoplasmic side {ECO:0000250|UniProtKB:Q9TVM2}.
DR  UNIPROT: F4IZR5;
DR  UNIPROT: Q0WV73;
DR  UNIPROT: Q94IV0;
DR  UNIPROT: Q94KD5;
DR  UNIPROT: Q9M9N0;
DR  Pfam: PF08767;
DR  Pfam: PF18777;
DR  Pfam: PF18784;
DR  Pfam: PF18787;
DR  Pfam: PF03810;
DR  Pfam: PF08389;
DR  PROSITE: PS50166;
DE  Function: Receptor for the leucine-rich nuclear export signal (NES). Binds cooperatively to the NES on its target protein and to the small GTPase Ran in its active GTP-bound form (By similarity). Required for the maternal-to-embryonic transition and during gametophyte development (PubMed:18791220). {ECO:0000250|UniProtKB:Q9SMV6, ECO:0000269|PubMed:18791220}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0009506;
GO  GO:0005049;
GO  GO:0031267;
GO  GO:0009553;
GO  GO:0051028;
GO  GO:0009555;
GO  GO:0009846;
GO  GO:0009860;
GO  GO:0006611;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9TVM2};
SQ  MAAEKLRDLSQPIDVVLLDATVEAFYSTGSKEERASADNILRDLKANPDTWLQVVHILQNTSSTHTKFFALQVLEGVIKY
SQ  RWNALPVEQRDGMKNYISDVIVQLSRDEASFRTERLYVNKLNIILVQIVKQEWPAKWKSFIPDLVIAAKTSETICENCMA
SQ  ILKLLSEEVFDFSKGEMTQQKIKELKQSLNSEFQLIHELCLYVLSASQRQELIRATLSALHAYLSWIPLGYIFESPLLEI
SQ  LLKFFPVPAYRNLTLQCLSEVASLNFGDFYDMQYVKMYSIFMNQLQAILPLNLNIPEAYSTGSSEEQAFIQNLALFFTSF
SQ  FKLHIKILESAPENISLLLAGLGYLISISYVDDTEVFKVCLDYWNSLVLELFGTRHHACHPALTPSLFGLQMAFLPSTVD
SQ  GVKSEVTERQKLYSDPMSKLRGLMISRTAKPEEVLIVEDENGNIVRETMKDNDVLVQYKIMRETLIYLSHLDHEDTEKQM
SQ  LSKLSKQLSGEEWAWNNLNTLCWAIGSISGSMVVEQENRFLVMVIRDLLSLCEVVKGKDNKAVIASNIMYVVGQYSRFLR
SQ  AHWKFLKTVVHKLFEFMHETHPGVQDMACDTFLKIVQKCKRKFVIVQVGESEPFVSELLSGLATIVGDLQPHQIHTFYES
SQ  VGSMIQAESDPQKRGEYLQRLMALPNQKWAEIIGQARQSADILKEPDVIRTVLNILQTNTRVATSLGTFFLSQISLIFLD
SQ  MLNVYRMYSELVSSSIANGGPYASRTSLVKLLRSVKREILKLIETFLDKAENQPHIGKQFVPPMMDQVLGDYARNVPDAR
SQ  ESEVLSLFATIINKYKVVMRDEVPLIFEAVFQCTLEMITKNFEDYPEHRLKFFSLLRAIATFCFRALIQLSSEQLKLVMD
SQ  SVIWAFRHTERNIAETGLNLLLEMLKNFQKSDFCNKFYQTYFLQIEQEVFAVLTDTFHKPGFKLHVLVLQHLFSLVESGS
SQ  LAEPLWDAATVPHPYSNNVAFVLEYTTKLLSSSFPNMTTTEVTQFVNGLYESRNDVGRFKDNIRDFLIQSKEFSAQDNKD
SQ  LYAEEAAAQMERERQRMLSIPGLIAPSEIQDDMADS
//
ID  Q54EV7;
PN  Exportin-1;
GN  xpo1;
OS  44689;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q54EV7;
DR  Pfam: PF08767;
DR  Pfam: PF18777;
DR  Pfam: PF18784;
DR  Pfam: PF18787;
DR  Pfam: PF03810;
DR  Pfam: PF08389;
DR  PROSITE: PS50166;
DE  Function: Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES).
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005049;
GO  GO:0031267;
GO  GO:0006611;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MENILNFNEPLDINLLDQIVSVLYNPLSNKNDIKAAQMVLGKFQEHPDAWSKVDTILETSKIVQTKFIALVIMDSLIKYR
SQ  WKSLPREQCEGIKNYIVSLIIRLSSDPQTSSREKLLVNKLNLVFVQILKQEWTTNWSTFIPEIISSSKTNESLCENNMVI
SQ  LRLLSEEIFNFSEEQMTQTKIQTLKITFEKEFSLINDLCFYILENATRASLIKATLETLQRFLNWVPLHYIIEVNGGIAE
SQ  PSKLVKLLLHKYFPEPLFRNSTLKCLTEIGNLNLGNQQYDAVFIAIIDKFMNQIKFIKPDPSKIPQDYEDGDQGERSFIH
SQ  TVSLFLTGFFKSHLKIMENSLNIPYLTLAHEILVNISNIDELELFKICLEYWNFLSSNLYSDIATFTTTLLSTPPRLQLY
SQ  KSVLSKVRVVLIDHMAKPEEVIVVEDENGNIVRETTKDTDSLTLYESMRETLIFLTHLDSENTQHIMLEKLQTLISGREF
SQ  TFQRLNTLCWAIGSISGAQNKEQEKRFLVTVIKDLLELCQNKKGKDNKAVIASDIMYIVGQYPRFLKDHWKFLKTVVNKL
SQ  FEFMHESHPGVQDMACDTFLKISKQCKRKFVVLQVEESQPFINELLNQLSTTIAHLEQSQIHTFYEAVGYMIASSSDAAF
SQ  REKLVNKFMELPNHSWLQIMGAASVKVESLLTVEVARDILNLIKTNNRAAMSLENCYITQISKIYLDLLNVYRTYSDHIS
SQ  RNPNIYRETLGQAMRSVKKETLKLLETFIEKSSDKQVIYSNFLQPLLEAVLGDYRTNIPETRDPEVLSLMTAIITSLKQL
SQ  VHPEVPKILEAVFETTLSMITKNFEDYPYHRINFFNLIRAINSNAFTVFHNLHPQQFKLLIDCVVWAFKHTERNISETGL
SQ  HILKELIENVSKNSDVANVFFKTYLVSLLNDILYILTDSFHKSGFALECDILRMMFQVVENGVVKIPLFDPQQANFPSNS
SQ  EYVKEIVVTFLSASPNVSRPQIQAFVTRLFNLANINNNDFKSATRDFLITLKEWKSHENADLYSDEKNIEKALALKKQSM
SQ  IPGMVRPNDVNLEMNDL
//
ID  Q9TVM2;
PN  Exportin-1;
GN  emb;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus {ECO:0000269|PubMed:17032737}. Nucleus membrane {ECO:0000269|PubMed:17032737}; Peripheral membrane protein; Nucleoplasmic side. Note=Localization to the nuclear pore complex is promoted by Nup214. {ECO:0000269|PubMed:17032737}.
DR  UNIPROT: Q9TVM2;
DR  UNIPROT: Q9I7N7;
DR  UNIPROT: Q9U699;
DR  Pfam: PF08767;
DR  Pfam: PF18777;
DR  Pfam: PF18784;
DR  Pfam: PF18787;
DR  Pfam: PF03810;
DR  Pfam: PF08389;
DR  PROSITE: PS50166;
DE  Function: Receptor for the leucine-rich nuclear export signal (NES) (PubMed:10636888, PubMed:14638854, PubMed:16103875). Binds cooperatively to the NES on its target protein and to the small GTPase Ran in its active GTP-bound form (PubMed:10636888, PubMed:14638854). Involved in the export of dl, RpS2 and the pre-40S ribosome from the nucleus to the cytoplasm (PubMed:14638854, PubMed:25858587, PubMed:17032737). Plays an important role in nuclear pore assembly by mediating nucleoporin condensation and biogenesis of annulate lamellae (PubMed:31626769). Required for the function or maintenance of certain tissues such as brain and gut (PubMed:10924475). {ECO:0000269|PubMed:10636888, ECO:0000269|PubMed:10924475, ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:25858587, ECO:0000269|PubMed:31626769}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VTM1; IntAct: EBI-229756; Score: 0.00
DE  Interaction: Q7KML2; IntAct: EBI-229764; Score: 0.00
DE  Interaction: P22469; IntAct: EBI-7377453; Score: 0.40
DE  Interaction: Q8IRE7; IntAct: EBI-9930581; Score: 0.35
DE  Interaction: Q9VRP5; IntAct: EBI-9931195; Score: 0.35
DE  Interaction: Q9W258; IntAct: EBI-9932835; Score: 0.46
DE  Interaction: M9NFI9; IntAct: EBI-9933573; Score: 0.35
DE  Interaction: Q7KN04; IntAct: EBI-9936955; Score: 0.35
DE  Interaction: O61307; IntAct: EBI-9952935; Score: 0.35
DE  Interaction: Q9VLS7; IntAct: EBI-9954110; Score: 0.35
DE  Interaction: Q24114; IntAct: EBI-9957759; Score: 0.35
DE  Interaction: P13709; IntAct: EBI-9958960; Score: 0.35
DE  Interaction: Q0KHS0; IntAct: EBI-9959651; Score: 0.35
GO  GO:0005737;
GO  GO:0031965;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005049;
GO  GO:0031267;
GO  GO:0007099;
GO  GO:0051028;
GO  GO:0051168;
GO  GO:0051292;
GO  GO:0006611;
GO  GO:0015031;
GO  GO:1900037;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MATMLTSDEAGKLLDFSQKLDINLLDKIVEVVYTAQGEQLRLAQSILTTLKEHPEAWTRVDSILEYSQNQRTKFYALQIL
SQ  EEVIKTRWKVLPRNQCEGIKKYVVSLIIKTSSDPIVMEQNKVYLNKLNMILVHILKREWPRNWETFISDIVGASKTNESL
SQ  CMNNMVILKNLSEEVFDFSQGQITQTKAKHLKDTMCSEFSQIFTLCSFVLENSMNAALIHVTLETLLRFLNWIPLGYIFE
SQ  TQQIETLIFKFLSVPMFRNVTLKCLSEIAGLTAANYDENFATLFKDTMVQLEQIVGQNMNMNHVFKHGSDTEQELVLNLA
SQ  MFLCTFLKEHGKLVEDAKYVDYLNQALMYLVMISEVEDVEVFKICLEYWNSLVEDLYNSEFFHPTLESTKRQQVYPRRRF
SQ  YAPILSKVRFIMISRMAKPEEVLVVENENGEVVREFMKDTNSINLYKNMRETLVFLTHLDSVDTDRIMTLKLLNQVNGSE
SQ  FSWKNLNTLCWAIGSISGAFCEEDEKRFLVTVIKDLLGLCEQKKGKDNKAIIASNIMYVVGQYPRFLRAHWKFLKTVVNK
SQ  LFEFMHETHDGVQDMACDTFIKIAIKCRRYFVTIQPNEACTFIDEILTTMSSIICDLQPQQVHTFYEAVGYMISAQVDQV
SQ  QQDVLIERYMQLPNQVWDDIISRASKNVDFLKNMTAVKQLGSILKTNVAACKALGHAYVIQLGRIYLDMLNVYKITSENI
SQ  IQAIEVNGVNVNNQPLIKTMHVVKKETLNLISEWVSRSNDNQLVMDNFIPPLLDAILLDYQRCKVPSAREPKVLSAMAII
SQ  VHKLRQHITNEVPKIFDAVFECTLDMINKNFEDFPQHRLSFYELLQAVNAHCFKAFLNIPPAQFKLVFDSVVWAFKHTMR
SQ  NVADMGLNILFKMLQNLDQHPGAAQSFYQTYFTDILMQIFSVVTDTSHTAGLPNHAIILAYMFSLVENRKITVNLGPIPD
SQ  NMIFIQEYVASLLKSAFTHLSDNQVKVFVTGLFNLDENVQAFKEHLRDFLIQIREATGEDDSDLYLEEREAALAEEQSNK
SQ  HQMQRNIPGMLNPHELPEDMQDE
//
ID  P30822;
PN  Exportin-1;
GN  CRM1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14562095}. Note=Localized in the nucleus and at its periphery.
DR  UNIPROT: P30822;
DR  UNIPROT: D6VV01;
DR  PDB: 3M1I;
DR  PDB: 3VYC;
DR  PDB: 3WYF;
DR  PDB: 3WYG;
DR  PDB: 4GMX;
DR  PDB: 4GPT;
DR  PDB: 4HAT;
DR  PDB: 4HAU;
DR  PDB: 4HAV;
DR  PDB: 4HAW;
DR  PDB: 4HAX;
DR  PDB: 4HAY;
DR  PDB: 4HAZ;
DR  PDB: 4HB0;
DR  PDB: 4HB2;
DR  PDB: 4HB3;
DR  PDB: 4HB4;
DR  PDB: 5DH9;
DR  PDB: 5DHA;
DR  PDB: 5DHF;
DR  PDB: 5DI9;
DR  PDB: 5DIF;
DR  PDB: 5JLJ;
DR  PDB: 5UWH;
DR  PDB: 5UWI;
DR  PDB: 5UWJ;
DR  PDB: 5UWO;
DR  PDB: 5UWP;
DR  PDB: 5UWQ;
DR  PDB: 5UWR;
DR  PDB: 5UWS;
DR  PDB: 5UWT;
DR  PDB: 5UWU;
DR  PDB: 5UWW;
DR  PDB: 5XOJ;
DR  PDB: 5YRO;
DR  PDB: 5YST;
DR  PDB: 5YSU;
DR  PDB: 5YTB;
DR  PDB: 5ZPU;
DR  PDB: 6A38;
DR  PDB: 6A3A;
DR  PDB: 6A3B;
DR  PDB: 6A3C;
DR  PDB: 6A3E;
DR  PDB: 6CIT;
DR  PDB: 6KFT;
DR  PDB: 6LQ9;
DR  PDB: 6M60;
DR  PDB: 6M6X;
DR  PDB: 6X2M;
DR  PDB: 6X2O;
DR  PDB: 6X2P;
DR  PDB: 6X2R;
DR  PDB: 6X2S;
DR  PDB: 6X2U;
DR  PDB: 6X2V;
DR  PDB: 6X2W;
DR  PDB: 6X2X;
DR  PDB: 6X2Y;
DR  PDB: 6XJP;
DR  PDB: 6XJR;
DR  PDB: 6XJS;
DR  PDB: 6XJT;
DR  PDB: 6XJU;
DR  PDB: 7CND;
DR  PDB: 7DBG;
DR  PDB: 7L5E;
DR  Pfam: PF08767;
DR  Pfam: PF18777;
DR  Pfam: PF18784;
DR  Pfam: PF18787;
DR  Pfam: PF03810;
DR  Pfam: PF08389;
DR  PROSITE: PS50166;
DE  Function: Receptor for the leucine-rich nuclear export signal (NES).
DE  Reference Proteome: Yes;
DE  Interaction: P06782; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P12683; IntAct: EBI-786893; Score: 0.35
DE  Interaction: P12684; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P14906; IntAct: EBI-3665470; Score: 0.35
DE  Interaction: P20484; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P22147; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25491; IntAct: EBI-3663255; Score: 0.35
DE  Interaction: P36013; IntAct: EBI-785404; Score: 0.35
DE  Interaction: P38085; IntAct: EBI-785720; Score: 0.35
DE  Interaction: P21147; IntAct: EBI-786767; Score: 0.35
DE  Interaction: P23641; IntAct: EBI-787315; Score: 0.35
DE  Interaction: P28496; IntAct: EBI-793629; Score: 0.35
DE  Interaction: Q07804; IntAct: EBI-797939; Score: 0.35
DE  Interaction: P33417; IntAct: EBI-798248; Score: 0.35
DE  Interaction: P38707; IntAct: EBI-798527; Score: 0.35
DE  Interaction: P38703; IntAct: EBI-799064; Score: 0.35
DE  Interaction: P0CI39; IntAct: EBI-803823; Score: 0.35
DE  Interaction: P32454; IntAct: EBI-805324; Score: 0.35
DE  Interaction: P40970; IntAct: EBI-805812; Score: 0.35
DE  Interaction: P13663; IntAct: EBI-808333; Score: 0.35
DE  Interaction: P52593; IntAct: EBI-809801; Score: 0.35
DE  Interaction: Q03529; IntAct: EBI-810338; Score: 0.35
DE  Interaction: P11745; IntAct: EBI-810584; Score: 0.53
DE  Interaction: P02994; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-810584; Score: 0.64
DE  Interaction: P10592; IntAct: EBI-810584; Score: 0.53
DE  Interaction: P10659; IntAct: EBI-810584; Score: 0.35
DE  Interaction: Q01939; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P33299; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P40495; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P33892; IntAct: EBI-810584; Score: 0.44
DE  Interaction: P00549; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P07259; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P02557; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P10081; IntAct: EBI-810584; Score: 0.35
DE  Interaction: P38737; IntAct: EBI-814203; Score: 0.27
DE  Interaction: Q00955; IntAct: EBI-814773; Score: 0.27
DE  Interaction: P18239; IntAct: EBI-816585; Score: 0.27
DE  Interaction: P39722; IntAct: EBI-818561; Score: 0.27
DE  Interaction: P60010; IntAct: EBI-820657; Score: 0.27
DE  Interaction: P0CG63; IntAct: EBI-7480760; Score: 0.44
DE  Interaction: P53323; IntAct: EBI-1200876; Score: 0.55
DE  Interaction: Q02630; IntAct: EBI-2346716; Score: 0.37
DE  Interaction: P43603; IntAct: EBI-7423488; Score: 0.55
DE  Interaction: P32793; IntAct: EBI-7439447; Score: 0.55
DE  Interaction: P61925; IntAct: EBI-7979681; Score: 0.52
DE  Interaction: P32835; IntAct: EBI-7979786; Score: 0.52
DE  Interaction: P10591; IntAct: EBI-3668753; Score: 0.35
DE  Interaction: P40150; IntAct: EBI-3720598; Score: 0.53
DE  Interaction: P39079; IntAct: EBI-3739915; Score: 0.35
DE  Interaction: P39076; IntAct: EBI-3741043; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3744083; Score: 0.35
DE  Interaction: Q12329; IntAct: EBI-3750567; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3811023; Score: 0.35
DE  Interaction: P39523; IntAct: EBI-9976090; Score: 0.53
DE  Interaction: P0CX83; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P0CX36; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P0CX54; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P0CX38; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P0CX48; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P0CX46; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q05937; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P0CX56; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P0CX32; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P0CX40; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06543; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40059; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12049; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12129; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06188; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38985; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12291; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P27351; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38042; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P04449; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38629; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P30619; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P23201; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12224; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P26785; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12196; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47064; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P12754; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40079; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P50278; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32525; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02908; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06604; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07418; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P27636; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P20448; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40157; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12090; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P23292; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47130; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q99369; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40021; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38089; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40013; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P21304; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25042; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P20434; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39743; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03466; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04377; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q05123; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04372; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P50094; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53901; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25559; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36049; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07350; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40335; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12034; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P15442; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q3E705; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34164; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P29478; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q99216; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34072; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02805; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P23248; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08444; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P54000; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02884; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P10962; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P49955; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08484; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47135; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53050; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q99186; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34110; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08235; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40187; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P07270; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32566; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P46946; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12481; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04007; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P48562; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25293; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32790; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P50896; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P80235; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04304; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P43563; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34243; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02354; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53829; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53741; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39715; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02875; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03330; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P17536; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38080; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12213; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12186; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53924; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39960; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47077; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07807; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P19524; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53894; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P06844; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40084; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P20053; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03233; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P51401; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32794; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12259; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P22204; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53743; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08951; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P09959; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12753; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36124; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25644; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40339; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36115; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08438; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38688; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07362; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P50079; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36119; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P46654; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P09547; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40449; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38263; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P17076; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32364; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40078; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P14127; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38284; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q99207; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53863; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38806; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38243; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53107; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P10080; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q01855; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04660; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40010; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32357; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47017; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53550; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47149; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47035; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P05755; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34078; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P30771; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25379; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40348; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53935; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06631; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P21192; IntAct: EBI-11611503; Score: 0.59
DE  Interaction: P38987; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P49626; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32578; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P24276; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P48361; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P26448; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P37262; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25368; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P28004; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q92331; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36080; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P26321; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12199; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36104; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: O13329; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47083; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P23202; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P21339; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03063; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P09032; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32501; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53830; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40523; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38254; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36041; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38835; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P27515; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P43639; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q01080; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12532; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53104; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38856; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P26784; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03768; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40054; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40214; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P19880; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32608; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25333; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P08518; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08909; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36000; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04740; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P20604; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07953; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40531; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25502; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12100; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25344; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12453; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P05453; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P26570; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38970; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P18899; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53297; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P24309; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P07266; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P37263; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53836; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P0CX52; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34761; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P35193; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q05672; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12527; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12221; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53309; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q00916; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03373; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04429; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04226; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03833; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38070; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32481; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P26786; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53686; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32494; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06511; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P22517; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40466; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q3E7Y3; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06512; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40992; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32491; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40210; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36123; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q00776; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53040; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02931; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40160; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47049; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40357; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38333; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38961; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38861; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53972; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53289; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02197; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47019; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P10664; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07622; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40356; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53865; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53930; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P35181; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38011; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53237; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53201; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P20424; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08972; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32524; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P29453; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P48164; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47129; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P06634; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q05775; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04839; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q05518; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04199; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06412; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03900; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39939; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39927; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P42944; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38809; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39985; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P20459; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04305; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08687; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P27999; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12102; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38882; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32913; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06834; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38177; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32914; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02796; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53272; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53091; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34758; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12432; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P33322; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P43615; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47160; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38874; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06410; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38817; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53136; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38789; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32328; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P48415; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39108; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38282; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32605; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53094; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38687; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25343; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02948; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04868; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12271; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P15646; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38747; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38630; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39517; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P05740; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P54783; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q01919; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07655; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25367; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08921; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06436; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P12904; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25567; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03503; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P20134; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38700; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36024; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P12962; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12194; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38990; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P05756; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12347; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25586; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04067; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03508; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40208; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39008; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38262; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32829; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53628; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53583; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40991; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53965; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39730; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12428; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12406; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12502; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40484; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36157; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12024; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q00381; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06108; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32342; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40099; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02939; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03497; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32607; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39016; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32567; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36083; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32502; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03208; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12071; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P07347; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40457; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53215; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32590; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q3E757; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38236; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40547; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07084; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38682; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36103; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38151; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40017; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P16522; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P26783; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03776; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q05543; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P11746; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53734; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12515; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P15625; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03088; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04600; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38691; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47168; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P50091; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53036; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P05738; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08096; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38112; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P20433; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P29468; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q99314; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P42846; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P43586; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P28263; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12417; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06671; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P15790; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12099; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40007; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: O13516; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47122; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53327; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39936; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07915; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53165; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38272; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04461; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08287; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P52920; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06709; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02326; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32351; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47006; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P18888; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04934; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39516; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12380; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40963; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P15807; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12454; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q00723; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P18961; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12368; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P42223; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P50111; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q05468; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P22209; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38873; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36053; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38719; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32591; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38431; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39998; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P14904; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P19454; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32899; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P11433; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02864; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40070; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53952; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P16370; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02892; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08689; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39955; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P41903; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38315; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39015; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38041; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P45976; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32497; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P37304; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P43597; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12191; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38759; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53883; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06706; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38712; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32495; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03656; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38230; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53316; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25390; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03862; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25555; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P0CX73; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40453; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34253; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P24784; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39525; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34239; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38200; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12124; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53199; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47108; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47148; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P05748; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P12945; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12163; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53063; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08208; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q05949; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03760; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36146; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08732; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07872; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P35182; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25617; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P35178; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06078; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04418; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04003; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32909; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P23561; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P15274; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53131; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P49704; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06315; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P18494; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P20447; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53145; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04347; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25294; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40561; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q00816; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03532; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P43573; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25339; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39702; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P50946; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P48412; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P21374; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38779; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P03871; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02554; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12460; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P50109; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34241; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53892; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53914; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P43572; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12476; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P48234; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38321; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53137; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12378; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40956; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04673; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40482; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03758; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38823; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40559; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07896; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06211; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P51534; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P13186; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38281; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P15303; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08226; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P12688; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36160; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32336; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12060; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38697; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06344; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32598; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P29366; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34087; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38344; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08649; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04408; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07381; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P09064; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P16892; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P43612; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P06103; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53251; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P14126; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04739; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12343; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47170; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P15624; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47050; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08886; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P51862; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53941; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P54113; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12517; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P30665; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03785; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38249; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53855; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32786; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53604; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06628; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08237; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39717; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53942; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06218; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53893; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12028; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12321; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40217; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07834; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q01477; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03780; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06632; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02336; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38165; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47116; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38696; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53949; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38180; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04712; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39731; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53270; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P08018; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03769; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40091; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P37838; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03735; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P29055; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38065; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32047; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P42841; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53953; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P27476; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06132; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P21373; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q03338; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P27692; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40693; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P09734; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07913; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P06784; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38129; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53873; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12159; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47048; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02256; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38798; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25366; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12522; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12176; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q00539; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12136; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P46990; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40856; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38930; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P04840; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P14741; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04410; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P32523; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12504; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P29295; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53742; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38701; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02959; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12523; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P40535; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P34167; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q02793; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P36076; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07825; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53088; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P45978; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12094; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12421; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P06843; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38738; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P33400; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P46675; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07532; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08726; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q08217; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P25635; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P33442; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38251; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P05750; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06205; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P04803; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P53238; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07844; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39682; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39744; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P33201; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39969; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q06337; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P14680; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38061; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q04511; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12216; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07821; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38213; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P46682; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38153; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q12092; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P39729; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P41819; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P42935; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P47089; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38805; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: Q07533; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P49960; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P42843; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38316; IntAct: EBI-16263556; Score: 0.35
DE  Interaction: Q08273; IntAct: EBI-16271112; Score: 0.35
DE  Interaction: P40517; IntAct: EBI-16292729; Score: 0.35
GO  GO:0005737;
GO  GO:0000776;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005816;
GO  GO:0005049;
GO  GO:0061608;
GO  GO:0031267;
GO  GO:0030619;
GO  GO:0030620;
GO  GO:0030621;
GO  GO:0030623;
GO  GO:0017070;
GO  GO:0006406;
GO  GO:0051168;
GO  GO:0006611;
GO  GO:0034501;
GO  GO:0000055;
GO  GO:0000056;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQFSTNPQSKFIALSILDKLITRKWK
SQ  LLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKSDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLK
SQ  LLSEEVFDFSAEQMTQAKALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILELLST
SQ  KFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADLKATYANANGNDQSFLQDLAMFLT
SQ  TYLARNRALLESDESLRELLLNAHQYLIQLSKIEERELFKTTLDYWHNLVADLFYEVQRLPATEMSPLIQLSVGSQAIST
SQ  GSGALNPEYMKRFPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVREFVKESDTIQLYKSEREVLVYLTHLNV
SQ  IDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDLLDLTVKKRGKDNKAVVASDIMYVVG
SQ  QYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQ
SQ  VHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGADFYPQ
SQ  LGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPKVRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYM
SQ  NNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPA
SQ  AFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQALLLM
SQ  KLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFLSALTKQYKDLVVFKGTLRDFLVQIK
SQ  EVGGDPTDYLFAEDKENALMEQNRLEREKAAKIGGLLKPSELDD
//
ID  Q54DN3;
PN  Exportin-7;
GN  xpo7;
OS  44689;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q54DN3;
DE  Function: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0005049;
GO  GO:0051028;
GO  GO:0006611;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSIQSEQDFFKFEELCKDFYLKPEETIKIDDILHQYFLNPNFLIEYKQILSFTKNSYVVAQVIRGLIKCVTSFWTSLTPN
SQ  QKNDMSKSIEHHCIGLRILKDIISEFNEYIGEHLTVLQHRNISISLRDNILLDIFCISLESLNYALANSMDEKFKSIKEL
SQ  ALDLSYSCLSFDFIKTTSIDSSEEILTVQIPSQWKSTFDENNPLELFFKIYKQYHSTKSLECILQIVSIRRSFFTTEDER
SQ  VKFLASIVQYTTEILKSNIGFNEPNNHLVFSRVIERLKTNYHLNNLVTVVGYNDWISNLSTFTIDTLKNPQFSPNSIYFL
SQ  LTLWAKLVSSIIYVKGDPSKTYLEKYSPIIMESFINSKIDNSYSDEEDEHLMDYEKMVEILEGIPHLGRITYQATCRQII
SQ  LLFDSISSKFLNETNPTQLEVYERQCAWLVYIIGCLILGRTSINSSEEHDKIDGELSVRVFILIGYNDKKLSAESNTQYQ
SQ  YRTSRISLELSFIYFMQNFRRIYIGENSISSSKIYQRISELSGPTDHTSVLFSIVQKIGFNFKYWAENDEIIKKSLDMFW
SQ  ESVNGHSTSKMLIDNKITKDILKTHSSQVFPFLEKNSNPRNRTSLYKTIGKLLFTDENMGFFDEFIAPFDDTIKHLLNIS
SQ  TPEQFRTEEIKRKVIGLLRDLRGIITSANSKRSYLLFFEWIHLNFSEVLIKIINVWVDSPEVTTSLLKFISEFVFNRQSR
SQ  LIFDSSSANGFIIFRDTSKILVSYASLILKANISKQDLYKFKIKGIQTSMLLFTRCLVGGYCNFGVFELYGDPSFTSAID
SQ  YIFQLCLSVSLDELMSFPKASKAYVTMLEALCLGHTLSIIQLNQQYFIHIMKSLHRCLDSQDVTMSSSSCTSIEKIITVC
SQ  YYHLKKKNSQCLQAIHQNFFSNSNILYEIIDKIISIIIYEDNFNQFMFSKLLLTCIIFHQDTFTTLKQKYIHSFNSQCPE
SQ  KVEKAFVQLMENTLDNLETKNKDKFTSNVSIFRKEMKLISSSTGRYL
//
ID  Q5R9G4;
PN  Exportin-7;
GN  XPO7;
OS  9601;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0185;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}.
DR  UNIPROT: Q5R9G4;
DR  UNIPROT: Q5RCM4;
DR  Pfam: PF03810;
DR  PROSITE: PS50166;
DE  Function: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005643;
GO  GO:0005049;
GO  GO:0031267;
GO  GO:0006886;
GO  GO:0051028;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MADHVQSLAQLENLCKQLYETTDTTTRLQAEKALVEFTNSPDCLSKCQLLLERGSSSYSQLLAATCLTKLVSRTNNPLPL
SQ  EQRIDIRNYVLNYLATRPKLATFVTQALIQLYARITKLGWFDCQKDDYVFRNAITDVTRFLQDSVEYCIIGVTILSQLTN
SQ  EINQADTTHPLTKHRKIASSFRDSSLFDIFTLSCNLLKQASGKNLNLNDESQHGLLMQLLKLTHNCLNFDFIGTSTDESS
SQ  DDLCTVQIPTSWRSAFLDSSTLQLFFDLYHSIPPSFSPLVLSCLVQIASVRRSLFNNAERAKFLSHLVDGVKRILENPQS
SQ  LSDPNNYHEFCRLLARLKSNYQLGELVKVENYPEVIRLIANFTVTSLQHWEFAPNSVHYLLSLWQRLAASVPYVKATEPH
SQ  MLETYTPEVTKAYITSRLESVHIILRDGLEDPLEDTGLVQQQLDQLSTIGRCEYEKTCALLVQLFDQSAQSYQELLQSAS
SQ  ASPMDIAVQEGRLTWLVYIIGAVIGGRVSFASTDEQDAMDGELVCRVLQLMNLTDSRLAQAGNEKLELAMLSFFEQFRKI
SQ  YIGDQVQKSSKLYRRLSEVLGLNDETMVLSVFIGKIITNLKYWGRCEPITSRTLQLLNDLSIGYSSVRKLVKLSAVQFML
SQ  NNHTSEHFSFLGINNQSNLTDMRCRTTFYTALGRLLMVDLGEDEDQYEQFMLPLTAAFEAVAQMFSTNSFNEQEAKRTLV
SQ  GLVRDLRGIAFAFNAKTSFMMLFEWIYPSYMPILQRAIELWYHDPACTTPVLKLMAELVHNRSRRLQFDVSSPNGILLFR
SQ  ETSKMITMYGNRILTLGEVPKDQVYALKLKGISICFSMLKAALSGSYVNFGVFRLYGDDALDNALQTFIKLLLSIPHSDL
SQ  LDYPKLSQSYYSLLEVLTQDHMNFIASLEPHVIMYILSSISEGLTALDTMVCTGCCSCLDHIVTYLFKQLSRSTKKRTTP
SQ  LNQESDRFLHIMQQHPEMIQQMLSTVLNIIIFEDCRNQWSMSRPLLGLILLNEKYFSDLRNSIVNSQPPEKQQAMHLCFE
SQ  NLMEGIERNLLTKNRDRFTQNLSAFRREVNDSMKNSTYGVNSNDMMS
//
ID  Q08DH8;
PN  DNA repair protein XRCC3;
GN  XRCC3;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Note=Accumulates in discrete nuclear foci prior to DNA damage, and these foci persist throughout the time course of DNA repair. {ECO:0000250}.
DR  UNIPROT: Q08DH8;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DE  Function: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD21 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005759;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0033065;
GO  GO:0005657;
GO  GO:0005524;
GO  GO:0140664;
GO  GO:0003677;
GO  GO:0000724;
GO  GO:0045003;
GO  GO:0090267;
GO  GO:0010824;
GO  GO:0071140;
GO  GO:0090656;
GO  GO:0000722;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLDRLDLNPRIVAAVKKAKLRSVKEVLHLSGPDLQRRTHLSSPDVQLLLRASASLLRGHGVCTALHLLRQEGPFPEQHQ
SQ  RLSLGCPVLDALLRGGLPLDGITELAGRSSAGKTQLALQLCLAVQLPPRHGGLGAGAVYVCTEDAFPSRRLQQLIAQQQR
SQ  LRADVPGHVISKIRFGHQIFIEHAADVDTLLQCVREKVPVLLARGMARLVVIDSVAAPFRCEFDGAALALRAQRLLALGA
SQ  ELRRLSCAFRSPVLCVNQVTEAVEEQDLVAGPPGMSPALGITWANQLLVRLLADRQRPEEAPLTPPGRTLRVVFAPHLPA
SQ  SSCSYTIAAEGVRGMPGTACS
//
ID  O43542;
PN  DNA repair protein XRCC3;
GN  XRCC3;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Mitochondrion. Note=Accumulates in discrete nuclear foci prior to DNA damage, and these foci persist throughout the time course of DNA repair.
DR  UNIPROT: O43542;
DR  UNIPROT: O43568;
DR  UNIPROT: Q9BU18;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DR  OMIM: 114480;
DR  OMIM: 600675;
DR  OMIM: 613972;
DR  DisGeNET: 7517;
DE  Function: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD51 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C. {ECO:0000269|PubMed:14716019, ECO:0000269|PubMed:20413593, ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.
DE  Disease: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:12023982}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Melanoma, cutaneous malignant 6 (CMM6) [MIM:613972]: A malignant neoplasm of melanocytes, arising de novo or from a pre- existing benign nevus, which occurs most often in the skin but may also involve other sites. {ECO:0000269|PubMed:11059748}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: O00165; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O43502; IntAct: EBI-9119744; Score: 0.94
DE  Interaction: Q8ZAN0; IntAct: EBI-2849986; Score: 0.00
DE  Interaction: A0A380PDY1; IntAct: EBI-2849973; Score: 0.00
DE  Interaction: Q6NVH7; IntAct: EBI-5282263; Score: 0.52
DE  Interaction: Q19AV6; IntAct: EBI-5282291; Score: 0.40
DE  Interaction: Q9H6U6; IntAct: EBI-9071268; Score: 0.37
DE  Interaction: P09341; IntAct: EBI-9071281; Score: 0.37
DE  Interaction: Q96KN1; IntAct: EBI-9071294; Score: 0.37
DE  Interaction: Q4ZG55; IntAct: EBI-9071307; Score: 0.37
DE  Interaction: Q86UX2; IntAct: EBI-9071320; Score: 0.37
DE  Interaction: Q9UBG0; IntAct: EBI-9071333; Score: 0.37
DE  Interaction: Q9UJX0; IntAct: EBI-9071346; Score: 0.37
DE  Interaction: Q9P2W1; IntAct: EBI-9071359; Score: 0.37
DE  Interaction: Q92560; IntAct: EBI-9071372; Score: 0.37
DE  Interaction: Q5VTR2; IntAct: EBI-9071385; Score: 0.37
DE  Interaction: Q96QR1; IntAct: EBI-9071398; Score: 0.37
DE  Interaction: P36952; IntAct: EBI-9071411; Score: 0.37
DE  Interaction: O95863; IntAct: EBI-9071424; Score: 0.37
DE  Interaction: P04155; IntAct: EBI-9071437; Score: 0.37
DE  Interaction: Q14258; IntAct: EBI-9071451; Score: 0.37
DE  Interaction: Q86YC2; IntAct: EBI-9119744; Score: 0.58
DE  Interaction: P51587; IntAct: EBI-9119744; Score: 0.53
DE  Interaction: Q06609; IntAct: EBI-9249126; Score: 0.73
DE  Interaction: O43264; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9C0C2; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9BVQ7; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q8TAG9; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P49368; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O14579; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P12268; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9HDC5; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9BWM7; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9H3U1; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q8N302; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q13435; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q96P70; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9H840; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q8WVB6; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q86UP2; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P16615; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O60220; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q15293; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9NVC6; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: F8W038; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P05067; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P17987; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O94822; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q96CT7; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9NZ01; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9H9B4; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P47897; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q99570; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P42167; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: B4E1G1; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P98175; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: F8W7C6; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q96BD0; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P31327; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O75152; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P20839; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O60524; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P22626; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9Y6K0; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9Y2X0; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q86UK7; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O95071; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q14152; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O00303; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O60841; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q99707; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P54278; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q15758; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q92973; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O14949; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q8IWX8; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q96D15; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9NS69; IntAct: EBI-11129266; Score: 0.53
DE  Interaction: Q8N1F7; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P51798; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O75477; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q14318; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O43852; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9UI10; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P06746; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9HCN4; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q15459; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q8WW12; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9NZM1; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O75448; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q96RT1; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q99942; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q969V3; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9UJS0; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: C9JA28; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9H3F6; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q8IX12; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9Y5L4; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q96T76; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P11498; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q96QC0; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q96ED9; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q8WUA2; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9H0G5; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P08238; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9Y2D8; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q92616; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q5T4S7; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O14828; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P50750; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9Y285; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P50990; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P42695; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P31689; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P31948; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O75937; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q03518; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P25705; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P55265; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q9Y6N5; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q96I25; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P52756; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q07065; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O60313; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q13451; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P08621; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q96E88; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q7Z4V5; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P40227; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P53621; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O75616; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: B4E1Q4; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P14625; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: O75533; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: P10809; IntAct: EBI-11129266; Score: 0.35
DE  Interaction: Q6P5F9; IntAct: EBI-11603310; Score: 0.35
DE  Interaction: Q8NFQ8; IntAct: EBI-21508086; Score: 0.35
DE  Interaction: Q9P296; IntAct: EBI-21519943; Score: 0.35
DE  Interaction: Q14627; IntAct: EBI-21561326; Score: 0.35
DE  Interaction: Q9UQV4; IntAct: EBI-21563011; Score: 0.35
DE  Interaction: Q8WWB7; IntAct: EBI-21569743; Score: 0.35
DE  Interaction: O14498; IntAct: EBI-21576861; Score: 0.35
DE  Interaction: Q03405; IntAct: EBI-21577545; Score: 0.35
DE  Interaction: P13473; IntAct: EBI-21591420; Score: 0.35
DE  Interaction: Q6ZSG2; IntAct: EBI-21681971; Score: 0.35
DE  Interaction: P20231; IntAct: EBI-21755901; Score: 0.35
DE  Interaction: P0DOF2; IntAct: EBI-25603126; Score: 0.35
DE  Interaction: Q15649; IntAct: EBI-26685717; Score: 0.37
GO  GO:0000781;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005739;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0033065;
GO  GO:0005657;
GO  GO:0005524;
GO  GO:0140664;
GO  GO:0003677;
GO  GO:0006974;
GO  GO:0006310;
GO  GO:0006281;
GO  GO:0000724;
GO  GO:0045003;
GO  GO:0036297;
GO  GO:0090267;
GO  GO:0010824;
GO  GO:0071140;
GO  GO:0010033;
GO  GO:0090656;
GO  GO:0000722;
GO  GO:0090737;
GO  GO:0090657;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLDLLDLNPRIIAAIKKAKLKSVKEVLHFSGPDLKRLTNLSSPEVWHLLRTASLHLRGSSILTALQLHQQKERFPTQHQ
SQ  RLSLGCPVLDALLRGGLPLDGITELAGRSSAGKTQLALQLCLAVQFPRQHGGLEAGAVYICTEDAFPHKRLQQLMAQQPR
SQ  LRTDVPGELLQKLRFGSQIFIEHVADVDTLLECVNKKVPVLLSRGMARLVVIDSVAAPFRCEFDSQASAPRARHLQSLGA
SQ  TLRELSSAFQSPVLCINQVTEAMEEQGAAHGPLGFWDERVSPALGITWANQLLVRLLADRLREEEAALGCPARTLRVLSA
SQ  PHLPPSSCSYTISAEGVRGTPGTQSH
//
ID  Q9CXE6;
PN  DNA repair protein XRCC3;
GN  Xrcc3;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Note=Accumulates in discrete nuclear foci prior to DNA damage, and these foci persist throughout the time course of DNA repair. {ECO:0000250}.
DR  UNIPROT: Q9CXE6;
DR  Pfam: PF08423;
DR  PROSITE: PS50162;
DE  Function: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD21 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005759;
GO  GO:0005739;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0033065;
GO  GO:0005657;
GO  GO:0005524;
GO  GO:0140664;
GO  GO:0008821;
GO  GO:0000400;
GO  GO:0006281;
GO  GO:0000724;
GO  GO:0045003;
GO  GO:0036297;
GO  GO:0090267;
GO  GO:0010824;
GO  GO:0071140;
GO  GO:0010033;
GO  GO:0090656;
GO  GO:0000722;
GO  GO:0090737;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MDLDQLDLNPRITAAVKRGRLKSVKEILCYSGPDLQRLTGLPSHDVQCLLRAASLHLRGSRVLSALHLFQQKESFPEQHQ
SQ  RLSLGCPVLDQFLGGGLPLEGITGLAGCSSAGKTQLALQLCLAVQFPRQYGGLEAGAVYICTEDAFPSKRLWQLIAQQRR
SQ  LRTDAPEELIEKIRFSNHIFIEHAADVDTLLECVSKKVPILLSRGMARLVVVDSIAAPFRCEFHLQASAIRAKLLLSLGA
SQ  TLRRLSSTFRSPVLCINQVTDMVEDQQSVSRSLGASEERLSPALGITWANQLLMRLMVDRTHEDDVTTGLPRSPVRTLRV
SQ  LFAPHLPLSSCCYTVSGEGIRGMPGTQSY
//
ID  P40383;
PN  5'-3' exoribonuclease 1;
GN  exo2;
OS  284812;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}.
DR  UNIPROT: P40383;
DR  Pfam: PF18129;
DR  Pfam: PF18332;
DR  Pfam: PF18334;
DR  Pfam: PF18194;
DR  Pfam: PF17846;
DR  Pfam: PF03159;
DE  Function: Multifunctional protein that exhibits several independent functions at different levels of the cellular processes (PubMed:8188690, PubMed:1637812). 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins (By similarity). Involved in the degradation of several hypomodified mature tRNA species and participates in the 5'-processing or the degradation of the snoRNA precursors and rRNA processing (By similarity). {ECO:0000250|UniProtKB:P22147, ECO:0000269|PubMed:1637812, ECO:0000269|PubMed:8188690}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0004534;
GO  GO:0000287;
GO  GO:0004540;
GO  GO:0003723;
GO  GO:0000956;
GO  GO:0000184;
GO  GO:0016075;
GO  GO:0006364;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGIPKFFRWMSERYPLCSQLIENDRIPEFDNLYLDMNGILHNCTHKNDDHSSPPLPEEEMYIAIFNYIEHLFEKIKPKKL
SQ  LYMAVDGCAPRAKMNQQRSRRFRTAKDAHDARLKAERNGEDFPEEQFDSNCITPGTTFMERVSRQLYYFIHKKVTNDSQW
SQ  QNIEVIFSGHDCPGEGEHKIMEYIRTQKAQPSYNPNTRHCLYGLDADLIMLGLLSHDPHFCLLREEVTFGPASRNRSKEL
SQ  AHQKFYLLHLSLLREYLEFEFQECRSTFTFKYDLEKILDDFILLAFFVGNDFLPHLPGLHINEGALALMFSIYKKVMPSA
SQ  GGYINEKGVINMARLELILLELENFEKEIFKAEVSETKNNGNSDKPSFDFLKYITESTNDIKAMTGEQKNYFLQIKKFLS
SQ  SREPFIDFSANISSVDQRFLRRLCNDLHLSFSKIIKVDGTHLLRITFRDLEFNDEDEDEIEQDEIERVLQKYDNIPLLNE
SQ  EQALKEKNVEKDFIQWKDDYYRSKVGFSYYDEEALKAMAERYVEGLQWVLFYYYRGCQSWGWYYNYHFAPKISDVLKGLD
SQ  VKIDFKMGTPFRPFEQLMAVLPARSQALVPPCFRDLMVNSESPIIDFYPENFALDQNGKTASWEAVVIIPFIDETRLIDA
SQ  LASKDKFLTEEERKRNSFNAPTVFSLAEDYTSFYPSSLPSLFPDLVTRCIQKPYSLPSMEGKEYLVGLCPGVFLGAFGMV
SQ  GFPSFHTLKHKAELVYHGINVFGNESRNPSVIVNVEDVKSALTSEQIAMQYVGKRIFVDWPYLREAYVESAMDESYMYLA
SQ  SNSTIEKRDLAEIEKSQWGRKCSHKIREYSKRFGVLFGDISLLLQVRPIKGLEYTREGALVKIFNESVLEDYPAQLVVEK
SQ  IAIDDPRFTEREAPPVEVEYPPGTKAFHLGEYNYGRPAQITGCKDNKLIIWLSTAPGLDAQWGRVLVNDSKSKEKYYPSY
SQ  IVAKLLNIHPLLLSKITSSFLISNGTKRENIGLNLKFDARNQKVLGFSRKSTKGWEFSNKTVALVKEYINTFPQLFNILT
SQ  THATKDNLTVKDCFPKDDTQQLAAVKHWIKEKGINSLTRVSLDEDALDSDIIKLIEEKASTIDSTYQVPKKVFGVPRYAL
SQ  LKPSQTRGILHSQEFALGDRVVYVQDSGKVPIAAYGTVVGIMLHHLDVVFDLPFMSGTTLDGRCSPYHGMQVEVSMVLNV
SQ  TNPQFVVNTRAGKNRKTNVSANNVSQGTDSRLVTKPTSTFPSPPSPPSSSVWNKREHHPKPFSLHQVPPPESLIHKSKSK
SQ  FSKGNHHSTNGTQSIRGRGGKRGKPLRSKELNRKHDHIVQPMGKLQIN
//
ID  P22147;
PN  5'-3' exoribonuclease 1;
GN  XRN1;
OS  559292;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body.
DR  UNIPROT: P22147;
DR  UNIPROT: D6VTX9;
DR  PDB: 6Q8Y;
DR  Pfam: PF18129;
DR  Pfam: PF18332;
DR  Pfam: PF18334;
DR  Pfam: PF18194;
DR  Pfam: PF17846;
DR  Pfam: PF03159;
DE  Function: Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins. The NMD pathway has a second role regulating the decay of wild-type mRNAs, and especially mRNAs that are important for telomere functions. Participate in CTH2-mediated and VTS1-mediated mRNA turnover. Involved in the degradation of several hypomodified mature tRNA species and participates in the 5'-processing or the degradation of the snoRNA precursors and rRNA processing. Involved in defense against virus and suppresses viral RNA recombination by rapidly removing the 5'-truncated RNAs, the substrates of recombination, and thus reducing the chance for recombination to occur in the parental strain. Required for the assembly of the virus- like particles of the Ty3 retrotransposon and contributes to the efficient generation of narnavirus 20S RNA by playing a major role in the elimination of the non-viral upstream sequences from the primary transcripts. Degrades single-stranded DNA (ss-DNA) and can renature complementary ss-DNA as well as catalyzes the formation of heteroduplex DNA from circular ss-DNA and homologous linear ds-DNA in vitro. Acts as a microtubule-associated protein which interacts with cytoplasmic microtubules through beta-tubulin and promotes in vitro assembly of tubulin into microtubules. Associates with microtubule functions such as chromosome transmission, nuclear migration, and SPB duplication. Has also a role in G1 to S transition and is involved in nuclear fusion during karyogamy. Required for the expression of ROK1 at the post- transcriptional level and for the alpha-factor induction of the karyogamy genes KAR3 and KAR4. Plays a role in filamentous growth. {ECO:0000269|PubMed:10454540, ECO:0000269|PubMed:11142370, ECO:0000269|PubMed:11238889, ECO:0000269|PubMed:11910109, ECO:0000269|PubMed:12423748, ECO:0000269|PubMed:12799443, ECO:0000269|PubMed:12853617, ECO:0000269|PubMed:14561886, ECO:0000269|PubMed:14690598, ECO:0000269|PubMed:14729943, ECO:0000269|PubMed:15013450, ECO:0000269|PubMed:15358132, ECO:0000269|PubMed:15967792, ECO:0000269|PubMed:15989963, ECO:0000269|PubMed:16240118, ECO:0000269|PubMed:16373495, ECO:0000269|PubMed:16501073, ECO:0000269|PubMed:16714281, ECO:0000269|PubMed:16885161, ECO:0000269|PubMed:17761681, ECO:0000269|PubMed:18162578, ECO:0000269|PubMed:18443146, ECO:0000269|PubMed:18469165, ECO:0000269|PubMed:18640978, ECO:0000269|PubMed:18676807, ECO:0000269|PubMed:18715869, ECO:0000269|PubMed:19324962, ECO:0000269|PubMed:2076815, ECO:0000269|PubMed:7597069, ECO:0000269|PubMed:7926736, ECO:0000269|PubMed:9315672, ECO:0000269|PubMed:9482746, ECO:0000269|PubMed:9488433, ECO:0000269|PubMed:9685486, ECO:0000269|PubMed:9742129}.
DE  Reference Proteome: Yes;
DE  Interaction: P20484; IntAct: EBI-16273123; Score: 0.35
DE  Interaction: P38203; IntAct: EBI-7341346; Score: 0.68
DE  Interaction: P40070; IntAct: EBI-7344118; Score: 0.68
DE  Interaction: P47093; IntAct: EBI-7347117; Score: 0.57
DE  Interaction: P53550; IntAct: EBI-7348887; Score: 0.55
DE  Interaction: P40073; IntAct: EBI-601178; Score: 0.37
DE  Interaction: P34230; IntAct: EBI-7095564; Score: 0.57
DE  Interaction: P53235; IntAct: EBI-7100035; Score: 0.70
DE  Interaction: P40089; IntAct: EBI-7101552; Score: 0.69
DE  Interaction: Q06406; IntAct: EBI-7101566; Score: 0.69
DE  Interaction: P57743; IntAct: EBI-7101614; Score: 0.69
DE  Interaction: P22147; IntAct: EBI-7101661; Score: 0.40
DE  Interaction: P47017; IntAct: EBI-7103424; Score: 0.69
DE  Interaction: P06634; IntAct: EBI-7107258; Score: 0.40
DE  Interaction: P15646; IntAct: EBI-7107862; Score: 0.40
DE  Interaction: P50095; IntAct: EBI-785746; Score: 0.35
DE  Interaction: P28007; IntAct: EBI-785796; Score: 0.35
DE  Interaction: P53917; IntAct: EBI-785875; Score: 0.35
DE  Interaction: P53131; IntAct: EBI-786246; Score: 0.53
DE  Interaction: Q07508; IntAct: EBI-786510; Score: 0.35
DE  Interaction: Q03782; IntAct: EBI-787666; Score: 0.35
DE  Interaction: P53617; IntAct: EBI-787885; Score: 0.35
DE  Interaction: P36520; IntAct: EBI-789484; Score: 0.35
DE  Interaction: P25644; IntAct: EBI-789578; Score: 0.67
DE  Interaction: P07347; IntAct: EBI-789752; Score: 0.35
DE  Interaction: P39935; IntAct: EBI-789934; Score: 0.35
DE  Interaction: P33759; IntAct: EBI-790057; Score: 0.35
DE  Interaction: P07260; IntAct: EBI-791281; Score: 0.61
DE  Interaction: Q12339; IntAct: EBI-792168; Score: 0.35
DE  Interaction: Q12180; IntAct: EBI-792644; Score: 0.35
DE  Interaction: P38112; IntAct: EBI-792768; Score: 0.35
DE  Interaction: P39730; IntAct: EBI-793125; Score: 0.35
DE  Interaction: Q12230; IntAct: EBI-793227; Score: 0.56
DE  Interaction: P50094; IntAct: EBI-793313; Score: 0.35
DE  Interaction: Q00539; IntAct: EBI-793423; Score: 0.35
DE  Interaction: P41544; IntAct: EBI-795171; Score: 0.35
DE  Interaction: P06102; IntAct: EBI-796052; Score: 0.35
DE  Interaction: P21954; IntAct: EBI-796109; Score: 0.35
DE  Interaction: P38199; IntAct: EBI-796822; Score: 0.35
DE  Interaction: P37838; IntAct: EBI-796980; Score: 0.35
DE  Interaction: P36160; IntAct: EBI-797509; Score: 0.35
DE  Interaction: P28003; IntAct: EBI-797693; Score: 0.35
DE  Interaction: P04912; IntAct: EBI-798033; Score: 0.35
DE  Interaction: P10080; IntAct: EBI-798100; Score: 0.56
DE  Interaction: P53883; IntAct: EBI-798461; Score: 0.67
DE  Interaction: P53849; IntAct: EBI-800556; Score: 0.35
DE  Interaction: P07280; IntAct: EBI-801098; Score: 0.35
DE  Interaction: P39735; IntAct: EBI-801128; Score: 0.35
DE  Interaction: P32588; IntAct: EBI-801532; Score: 0.35
DE  Interaction: P39928; IntAct: EBI-801843; Score: 0.35
DE  Interaction: P38934; IntAct: EBI-801975; Score: 0.35
DE  Interaction: P38996; IntAct: EBI-802165; Score: 0.35
DE  Interaction: P42846; IntAct: EBI-803913; Score: 0.35
DE  Interaction: P46677; IntAct: EBI-804533; Score: 0.35
DE  Interaction: P33322; IntAct: EBI-804949; Score: 0.61
DE  Interaction: P39998; IntAct: EBI-805615; Score: 0.35
DE  Interaction: P38789; IntAct: EBI-805875; Score: 0.35
DE  Interaction: P32495; IntAct: EBI-807147; Score: 0.35
DE  Interaction: P39715; IntAct: EBI-807214; Score: 0.35
DE  Interaction: P53730; IntAct: EBI-807951; Score: 0.35
DE  Interaction: P51998; IntAct: EBI-809221; Score: 0.35
DE  Interaction: P27476; IntAct: EBI-809258; Score: 0.35
DE  Interaction: P31334; IntAct: EBI-809484; Score: 0.35
DE  Interaction: P46995; IntAct: EBI-810191; Score: 0.35
DE  Interaction: P38217; IntAct: EBI-810745; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-811410; Score: 0.53
DE  Interaction: P10592; IntAct: EBI-811410; Score: 0.53
DE  Interaction: Q12517; IntAct: EBI-811410; Score: 0.44
DE  Interaction: P53905; IntAct: EBI-811492; Score: 0.56
DE  Interaction: P32357; IntAct: EBI-812552; Score: 0.27
DE  Interaction: P20448; IntAct: EBI-817592; Score: 0.27
DE  Interaction: P07246; IntAct: EBI-818223; Score: 0.27
DE  Interaction: P23293; IntAct: EBI-818581; Score: 0.53
DE  Interaction: P32493; IntAct: EBI-819907; Score: 0.27
DE  Interaction: P07270; IntAct: EBI-821981; Score: 0.35
DE  Interaction: P14680; IntAct: EBI-822301; Score: 0.35
DE  Interaction: Q04264; IntAct: EBI-822895; Score: 0.35
DE  Interaction: P36103; IntAct: EBI-7163764; Score: 0.40
DE  Interaction: P14682; IntAct: EBI-7232905; Score: 0.40
DE  Interaction: P35207; IntAct: EBI-7383410; Score: 0.40
DE  Interaction: P07703; IntAct: EBI-7383484; Score: 0.56
DE  Interaction: Q12159; IntAct: EBI-7383752; Score: 0.40
DE  Interaction: P39015; IntAct: EBI-7383874; Score: 0.40
DE  Interaction: P53252; IntAct: EBI-7383909; Score: 0.40
DE  Interaction: Q02793; IntAct: EBI-7702127; Score: 0.40
DE  Interaction: P39517; IntAct: EBI-969682; Score: 0.35
DE  Interaction: Q03758; IntAct: EBI-2611184; Score: 0.35
DE  Interaction: Q06098; IntAct: EBI-2612191; Score: 0.35
DE  Interaction: P32350; IntAct: EBI-2612391; Score: 0.35
DE  Interaction: P36002; IntAct: EBI-2613197; Score: 0.35
DE  Interaction: Q02981; IntAct: EBI-2614446; Score: 0.35
DE  Interaction: Q01389; IntAct: EBI-2616771; Score: 0.35
DE  Interaction: Q01477; IntAct: EBI-7992250; Score: 0.35
DE  Interaction: P53741; IntAct: EBI-7994013; Score: 0.35
DE  Interaction: P10591; IntAct: EBI-3671884; Score: 0.53
DE  Interaction: P39987; IntAct: EBI-3702683; Score: 0.35
DE  Interaction: P32589; IntAct: EBI-3726158; Score: 0.35
DE  Interaction: P33416; IntAct: EBI-3745115; Score: 0.35
DE  Interaction: P53940; IntAct: EBI-3768410; Score: 0.35
DE  Interaction: P38788; IntAct: EBI-3790303; Score: 0.35
DE  Interaction: P02829; IntAct: EBI-3812207; Score: 0.35
DE  Interaction: P39523; IntAct: EBI-9976090; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-11611503; Score: 0.35
DE  Interaction: P38328; IntAct: EBI-16264031; Score: 0.35
DE  Interaction: P46947; IntAct: EBI-16264615; Score: 0.35
DE  Interaction: P32458; IntAct: EBI-16265446; Score: 0.35
DE  Interaction: P15790; IntAct: EBI-16266738; Score: 0.35
DE  Interaction: Q03957; IntAct: EBI-16267608; Score: 0.35
DE  Interaction: Q08496; IntAct: EBI-16268078; Score: 0.35
DE  Interaction: P53861; IntAct: EBI-16268602; Score: 0.35
DE  Interaction: P17214; IntAct: EBI-16268957; Score: 0.35
DE  Interaction: P40466; IntAct: EBI-16269181; Score: 0.35
DE  Interaction: P32828; IntAct: EBI-16270661; Score: 0.35
DE  Interaction: P04911; IntAct: EBI-16271323; Score: 0.35
DE  Interaction: P32464; IntAct: EBI-16271424; Score: 0.35
DE  Interaction: P40055; IntAct: EBI-16272037; Score: 0.35
DE  Interaction: P22134; IntAct: EBI-16273066; Score: 0.35
DE  Interaction: P27705; IntAct: EBI-16273814; Score: 0.35
DE  Interaction: Q04149; IntAct: EBI-16274484; Score: 0.35
DE  Interaction: Q12236; IntAct: EBI-16275897; Score: 0.35
DE  Interaction: P32345; IntAct: EBI-16276178; Score: 0.35
DE  Interaction: Q07350; IntAct: EBI-16276475; Score: 0.35
DE  Interaction: P30620; IntAct: EBI-16276950; Score: 0.35
DE  Interaction: P34221; IntAct: EBI-16277075; Score: 0.35
DE  Interaction: Q04049; IntAct: EBI-16278245; Score: 0.35
DE  Interaction: P14291; IntAct: EBI-16279138; Score: 0.35
DE  Interaction: P38987; IntAct: EBI-16285008; Score: 0.35
DE  Interaction: P53632; IntAct: EBI-16285647; Score: 0.35
DE  Interaction: Q07623; IntAct: EBI-16287594; Score: 0.35
DE  Interaction: Q05580; IntAct: EBI-16288023; Score: 0.35
DE  Interaction: Q06344; IntAct: EBI-16288282; Score: 0.35
DE  Interaction: P53261; IntAct: EBI-16289064; Score: 0.35
DE  Interaction: P38779; IntAct: EBI-16289300; Score: 0.35
DE  Interaction: P36009; IntAct: EBI-16290060; Score: 0.35
DE  Interaction: Q06436; IntAct: EBI-16291315; Score: 0.35
DE  Interaction: Q04305; IntAct: EBI-16291624; Score: 0.35
DE  Interaction: P42843; IntAct: EBI-16291990; Score: 0.35
DE  Interaction: Q00416; IntAct: EBI-16421063; Score: 0.35
DE  Interaction: P14772; IntAct: EBI-20813827; Score: 0.37
DE  Interaction: P41909; IntAct: EBI-20815489; Score: 0.37
GO  GO:0005737;
GO  GO:0010494;
GO  GO:0005829;
GO  GO:0090512;
GO  GO:0005874;
GO  GO:0005634;
GO  GO:0000932;
GO  GO:0048471;
GO  GO:0004534;
GO  GO:0003682;
GO  GO:0031370;
GO  GO:0003729;
GO  GO:0003723;
GO  GO:0000741;
GO  GO:0061157;
GO  GO:0016242;
GO  GO:0070651;
GO  GO:0000956;
GO  GO:0070479;
GO  GO:0000184;
GO  GO:0032968;
GO  GO:0060261;
GO  GO:0016075;
GO  GO:0006364;
GO  GO:0043144;
GO  GO:0006413;
GO  GO:0007089;
GO  GO:0016078;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MGIPKFFRYISERWPMILQLIEGTQIPEFDNLYLDMNSILHNCTHGNDDDVTKRLTEEEVFAKICTYIDHLFQTIKPKKI
SQ  FYMAIDGVAPRAKMNQQRARRFRTAMDAEKALKKAIENGDEIPKGEPFDSNSITPGTEFMAKLTKNLQYFIHDKISNDSK
SQ  WREVQIIFSGHEVPGEGEHKIMNFIRHLKSQKDFNQNTRHCIYGLDADLIMLGLSTHGPHFALLREEVTFGRRNSEKKSL
SQ  EHQNFYLLHLSLLREYMELEFKEIADEMQFEYNFERILDDFILVMFVIGNDFLPNLPDLHLNKGAFPVLLQTFKEALLHT
SQ  DGYINEHGKINLKRLGVWLNYLSQFELLNFEKDDIDVEWFNKQLENISLEGERKRQRVGKKLLVKQQKKLIGSIKPWLME
SQ  QLQEKLSPDLPDEEIPTLELPKDLDMKDHLEFLKEFAFDLGLFITHSKSKGSYSLKMDLDSINPDETEEEFQNRVNSIRK
SQ  TIKKYQNAIIVEDKEELETEKTIYNERFERWKHEYYHDKLKFTTDSEEKVRDLAKDYVEGLQWVLYYYYRGCPSWSWYYP
SQ  HHYAPRISDLAKGLDQDIEFDLSKPFTPFQQLMAVLPERSKNLIPPAFRPLMYDEQSPIHDFYPAEVQLDKNGKTADWEA
SQ  VVLISFVDEKRLIEAMQPYLRKLSPEEKTRNQFGKDLIYSFNPQVDNLYKSPLGGIFSDIEHNHCVEKEYITIPLDSSEI
SQ  RYGLLPNAKLGAEMLAGFPTLLSLPFTSSLEYNETMVFQQPSKQQSMVLQITDIYKTNNVTLEDFSKRHLNKVIYTRWPY
SQ  LRESKLVSLTDGKTIYEYQESNDKKKFGFITKPAETQDKKLFNSLKNSMLRMYAKQKAVKIGPMEAIATVFPVTGLVRDS
SQ  DGGYIKTFSPTPDYYPLQLVVESVVNEDERYKERGPIPIEEEFPLNSKVIFLGDYAYGGETTIDGYSSDRRLKITVEKKF
SQ  LDSEPTIGKERLQMDHQAVKYYPSYIVSKNMHLHPLFLSKITSKFMITDATGKHINVGIPVKFEARHQKVLGYARRNPRG
SQ  WEYSNLTLNLLKEYRQTFPDFFFRLSKVGNDIPVLEDLFPDTSTKDAMNLLDGIKQWLKYVSSKFIAVSLESDSLTKTSI
SQ  AAVEDHIMKYAANIEGHERKQLAKVPREAVLNPRSSFALLRSQKFDLGDRVVYIQDSGKVPIFSKGTVVGYTTLSSSLSI
SQ  QVLFDHEIVAGNNFGGRLRTNRGLGLDASFLLNITNRQFIYHSKASKKALEKKKQSNNRNNNTKTAHKTPSKQQSEEKLR
SQ  KERAHDLLNFIKKDTNEKNSESVDNKSMGSQKDSKPAKKVLLKRPAQKSSENVQVDLANFEKAPLDNPTVAGSIFNAVAN
SQ  QYSDGIGSNLNIPTPPHPMNVVGGPIPGANDVADVGLPYNIPPGFMTHPNGLHPLHPHQMPYPNMNGMSIPPPAPHGFGQ
SQ  PISFPPPPPMTNVSDQGSRIVVNEKESQDLKKFINGKQHSNGSTIGGETKNSRKGEIKPSSGTNSTECQSPKSQSNAADR
SQ  DNKKDEST
//
ID  Q9C112;
PN  Uncharacterized membrane protein C27F1.10;
GN  SPAC27F1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm. Nucleus membrane {ECO:0000305}; Multi- pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q9C112;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MQLTGSIYPWFTAYALLKSTLMELINSFIPYKSQTGKAPKCLVPYWLSIRLSLLYFKLTEAISFTEKCEKYNISLFDSTF
SQ  VFGYIVNCFFIIHLNTFLTSQ
//
ID  O94473;
PN  Uncharacterized membrane protein C1919.04;
GN  SPCC1919;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94473;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDLSFIEGFETIWTVVRAVVLNYLLRSLKILSTILYVSAVISWNVSLKVFGNVLLPGFLTIRTVVIFILRIVSLFLWILA
SQ  DPAILLVQSVYWYFIRAPARFILMVGITLYPLYVLLSWAVFLGIIVGFSLNSVFTFIDSFATPSSNSTVTEAMTKMKNEK
SQ  VLEYPYKDRNIMLGDLASRIPSKDSEKLDEERQPIALEKTKSLDSISHSSSSSRKSSTELKIPPVETRIVAEIPVPSSVK
SQ  RRRHRPNKSMGSIKNS
//
ID  O94490;
PN  Uncharacterized transcriptional regulatory protein C417.09c;
GN  SPCC417;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227}; Multi-pass membrane protein {ECO:0000305}.
DR  UNIPROT: O94490;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MHARMQPHEDRSRSGMSRSEAMELEDQLEEEERGGNVVVGSSSANANASTAETGKKSAGGSKPKRRRGERIPPSKRIRKA
SQ  IAYVNKYASGCFGRVERRLVCTRSISRHSNQKLLDFCVECKKHKIKCVGNFPCGRCLKKGLECVIETPPRLLMNKDEISL
SQ  NLQRLSHMETILSKLMPSMSLDLPSLEAKIAELSESLQTYPDKVLTDIELGSYQQVTLNETQTYYEDAGSNESFVARVHE
SQ  IICQGREFQVQHKLTNKGNKTFEDILDPADNTVASLIHALPPKDITFYLLMTFWQFSSDNNHFYYNTKLFAAKVHHLFDD
SQ  PTSFQSKDGGFVCMLLLSMAMGSLFSYIRHPEFLSDENHDRWTYPGSQFYQNAKLLFPKVISESSLETVQSFFLAGMYLS
SQ  PTLAHEVVYMYFGIAMRAAVANGMHKKSANAQFSGDVAELRKRLFWSVYCMERKIGISLGRPESLVRSEIDIHFPEYRES
SQ  LDSQNFIASFRTFTLAIKISLLTNKVYDMWYSSLHGKANLKAATIKEIVNEIEAWRQQLSPDLEIQNIGPDSRSYRGIVH
SQ  LHLAYHIVRIAMGRPFLLHRLRERTMNSKTDEGARLLTDKLISYCYSSALHIVDLLVLLRMHKFLSVYSFMDYHSCHAAS
SQ  FIILVHLLINPSEQTIEQLNTAIDILNFVTDRFPLLKGSTDVITNLRAFAEQSEVYQSRLNATEPAYSTQVPFFPRDADY
SQ  HNQINLQNLWNDENINASLEALFNDAKGFGFLLPADNFIFPSDDGDM
//
ID  O13746;
PN  Uncharacterized protein C16E8.18;
GN  SPAC16E8;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O13746;
DE  Function: 
DE  Reference Proteome: Yes;
DE  Interaction: Q9Y709; IntAct: EBI-1793085; Score: 0.37
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MEVTSFILNATFKEFACFGNNYLIILPGIMLERNVFRHLNYSTNSICSHYQFFGGHYESFELLVVIVYYFSHVGSFSLAE
SQ  IYRITWDKRIVLYGTTTTLVYCSEGSD
//
ID  O13818;
PN  Uncharacterized PH domain-containing protein C19A8.02;
GN  SPAC19A8;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10759889}. Nucleus membrane {ECO:0000269|PubMed:10759889}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10759889}.
DR  UNIPROT: O13818;
DR  UNIPROT: Q9USA8;
DR  Pfam: PF00169;
DR  Pfam: PF16016;
DR  PROSITE: PS50003;
DR  PROSITE: PS51778;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0032541;
GO  GO:0005783;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005886;
GO  GO:0005816;
GO  GO:0008289;
GO  GO:0061817;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAAPANASSKKDHVIPVLLNECSIDSPSFRASMYYLGNQIKAFNEWSHDFLCCCNKFIESIMAIEPIVASMSLNAMPSNV
SQ  ASGFFDPDYATTALLHGQDLFRSSYMVQLQQAKNLRKFIVAPLDLFRDSKVKPLLQLNDRFKAEQAKYDAEVLRYSSLGH
SQ  SKDLSQMRDEAKSLYEARKSYFTVALQYVVRVTSFRSSIDFIVIESICKFSIETFRLTDRLHESNRHINDQLIRLLSYET
SQ  KLKESYPSLKRIVSNVFDRIEKEILKRVQPPTNLDAYRFDPQQICQTNATKRQGWLLRNISSSKADNKAIWRKYWFFVDN
SQ  GYVGYLINDANGGVFESEKIGVLLCKFSVLPSNHRKFCFQIKTKSVSYILQAETHMEMLEWGSVINNAREHCINSGISAN
SQ  RILSPTLPSFSAKATSIINPQVNGRSNSTGKIGKNYRPRRTYSGRLLCGPNNYEVSTIMRSPTISTVPPPKYLSNSINGA
SQ  KFLNPLAPWTLVNAPLITNLTHETITSLLDQEAFFHGNSPCALLANFWGSVNYGHVLERQNVYIEDLSNPSYKRLAREIH
SQ  IEKLPSELKLRNAEFRGIFGESEASTVLFVCRVCSKREDQIRMPGRMYCTMKGIYIYYNINGLVLIEHFPISSILNVKQF
SQ  ASTKCDYFYMNIQNIGTVRFRLYLDSSKALTDRLNVLLCNYIADKPNSSIQLLSCIKRLNDDVKRFERGGDDNALKSYGV
SQ  QPSQEDLLIRRGRSSRALTNLINKNESNDSFMEDLRDFKIAMLPKETVQVVRSHHLDDIVFDRVYNVSTKALFHIVFGDR
SQ  STVLSGAYNLHGVDDVEFLPWGKDPKTNLSRRYINYKVYNYDQEGQCQSYHYEDCQIMDVRNDYHLYIMTWLHHSWTLPY
SQ  RDYFKIVTKTSISHLRREKSRLLISVGLEWIVKPFAISKVIEAECRKLAIKYIKTEVNFLEKATRRARNQPLIAIINQYG
SQ  RVGDYNESMVYRRKIPFNCELKNLSIIDIIRNNWWLFLQGLAIDLLKLPWAVFHIFLRYLFSHSFLVIIFACSVILNLSL
SQ  MFCFGAKYWDERQNNKFVGQVFDEFKNIETSARYVYMKDVDDLLVGLPTYLHPNVTYPSECLQSFALKSSPQKSHWLRKR
SQ  NYIAEKRKKILENLASLNYYEYIIHEDAVYQYIQQELLGCDKAREFDLYPPSMQRYCDSCTQDWRNRTLFFGKDTLATRL
SQ  LTLETVENADYAA
//
ID  O13760;
PN  Uncharacterized membrane protein C17A2.10c;
GN  SPAC17A2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O13760;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTCVNVCFFLFPPCHRNKITEADKSLVDLLIPSLCCSLAVFPSIPLINTHSNLCLFSNFSHSCFLFCTHPDTLPTSLSIN
SQ  PKKLSLSFSFPLSQKRPFPNFLHPFTGSELSLFRCLLLFFFFLLFFLSFSFSFSFLFFLSQIFIVYFSSFPILHFLFFFF
SQ  LCVCVFLSFLFSLSHLLSLAILFLPLLLRVFSTLSRLPRLFCLCLQKKRRVLIPFAFTSFRKIASLPCVC
//
ID  O94569;
PN  Uncharacterized transcriptional regulatory protein C1773.12;
GN  SPBC1773;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94569;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0000228;
GO  GO:0031965;
GO  GO:0005730;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVPIKKISTACDLCRQRKLRCNGELPKCQNCVVYSETCKYNKRKRVKKPNVDKDDPHIVVGQPPVKKSTAGITREYTEMI
SQ  ELRNHIITLSKRSVNMESRIDDMLNLLNYDLSEKRETSNEIPSLVQQIQNCGFLIDEKMRRYPGIFQIHPKDYTMNDLFP
SQ  QSFPTWISVYRNVPEKAWANRCVEWYFRYINSCWPLFDLENFMDLFDNFYSDKEKTKGAWVVSFYAIMALAVSRSKRKDK
SQ  EKISKSLFSTSWFLVQKPGFFLTARLDKIQALTIMIQFCAHLSLYNLCKVLCGQMCLMVKDLDLHKEATNPNVDIEVDEL
SQ  NRRVFWTCYIFETTTSLIFGTPPELGDLEIDCQLPSMDVLPRFTESSQGGIVFCSEIQLTIIKNEIRKKIYKCLASASEE
SQ  VYKEAVLSIRGKLIVWERNLPDELKQYYDVIKLNGTIPKNVDFENQHIFTACVEIYLSYCITQLYFYDPLTNYETCLEIA
SQ  RKAADAIRSYFMVIEPIFKKICYLWLFLYCPFTPFQILFSNILKMEKGTSDEKIEDLDRMYSLYRFFVEMKEINGEFADK
SQ  LSRVALDCIDAAEHYLELKSSVGSNIFELESLLV
//
ID  O94573;
PN  Uncharacterized transcriptional regulatory protein C1773.16c;
GN  SPBC1773;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O94573;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0000228;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKRIRNACELCRRKKLRCNGELTCQNCMVYGEECRYVKRVKHDNRAAVQENERYPILYTPLSTSDHDNDEENEINELKNA
SQ  VKALDKRFDNFELKLEALFSLLRSQQDSERKVKPGGFPSLVSQILSAGALVDSKLQAYTMRTNFFSNGFSSNDLFPHSFP
SQ  TWKSAFRDVPDKDWAKTCLDWYFRFINCNWPIFYKKQYMESFEKLYIDKNLVKGAWIVSFYAILALAVSRDKRVDNSKLA
SQ  ESFFATSWFLIQRPGFFLTPQLEKIQALVIMIQFASHLSLYNLCKKLCGQVCLMVKDLNLHKESTDKDLDQDMAELHRRI
SQ  FWVCYIFETTTSLIFGTPPVLGDLEIECKYPDINYAHCFAENVQGDLIFTCEISLTVLKHEIRTKLYNSNNVFLDKGQKG
SQ  VISNIQTKILNFERAIPSEMKHYFEILKAGNGLPEELDIIKQHFFTACVEIYLSYCNTLIYLYLADDSIEGSKICLSTAR
SQ  AAIDVIKGFLVVLDPISKNICYLWLFLYCPFTPFLTVFSHLLEDDDLDADICVKDVDRLYSIHAFFLKMKDISGEFAERL
SQ  SVITENFIQSAEQYLALQNTSVFGTFDALSESFSI
//
ID  O60131;
PN  Uncharacterized transcriptional regulatory protein C16G5.17;
GN  SPBC16G5;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O60131;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVGKSKNRAHKNIRARSCLRCRRRKVKCDRQYPCSRCKESEESCTYGVNEQAVQLLEEPLSRPITRETDSSAHQETRTRL
SQ  EENNLPKTQKFGFVDWKTILKSSAEFQGIVQRDPESRLREALETDPKLKKRLECILETIPPWDVCESLLKVYANTFNVTN
SQ  YILDFEQADKLLSDLKNSNHVFATSIILIVTAIAVALSLESFPSNIERYFSAVNHSAIELSDALNSKIDDFLNEEVIFRL
SQ  WRNIDRIRLHAIRAQLCMRNQFRSMNTDLCYAIHYACFVNPIFQNTDTEYEANMEVWLSICEIDALECVLRSCQPWVQHD
SQ  IYGKLLSQRKMGSDVISYEFHSLLGQLLTCGLEIYKAIHTSTVNEFVNSIQFYESQLSLVLMEIESKFSNIDGSDIHFRY
SQ  LFLKTVFWTVRKNLYQGFITVSRTLVPNYPDIVQKLGQTSIQLSRLISNSMDCFEKYGWLKAMLILVTHTFLIIHVCSER
SQ  GYDVPKDFWNVTASVQATLEEKKYPGIVWERIHYVLNIYTTINSVEPELSEDHGDLDDQNLFQVFTDIFDFNFNFPLPNL
//
ID  Q9HDU0;
PN  UPF0742 protein PB2B2.17c;
GN  SPBPB2B2;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to cytoplasmic dots and the nuclear envelope.
DR  UNIPROT: Q9HDU0;
DR  Pfam: PF09437;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSVSSKFRSFTFGCVVVY
SQ  HNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISR
//
ID  Q9P3V7;
PN  UPF0742 protein C1348.03;
GN  SPBC1348;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Localizes to cytoplasmic dots and the nuclear envelope. {ECO:0000250}.
DR  UNIPROT: Q9P3V7;
DR  Pfam: PF09437;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSASSKFRSFTFGCVVVY
SQ  HNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISQ
//
ID  P0CU07;
PN  UPF0742 protein SPAC977.02;
GN  SPAC977;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to cytoplasmic dots and the nuclear envelope. {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: P0CU07;
DR  UNIPROT: Q9P332;
DR  Pfam: PF09437;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSASSKFRSFTFGCVVVY
SQ  HNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISR
//
ID  O74525;
PN  Uncharacterized membrane protein C70.04c;
GN  SPCC70;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
DR  UNIPROT: O74525;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MKQNNKKPLPSKTKEISLETDWIDVIETMRETNESPKSQNPSEEATTVNELSCEAKPKLLFTPTKSSLSIGNFPYKEFDP
SQ  VLKFPGIHYTYSRERLWGTCVILSTLFWSYYVLSNSELLEFEASEYSLLFILIIALDALLTVSLFGLFHHLMFLTTNYSY
SQ  TINSTLDISKGFFINVLSTMVQALVTVTIAFTKFVTIDFPIYVFSSLFLYHPLSRSRQLPTKMQLDGSGERKTDSSLVHQ
SQ  NPPN
//
ID  Q9US10;
PN  Uncharacterized membrane protein C6F6.13c;
GN  SPAC607;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9US10;
DR  Pfam: PF05277;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0016298;
GO  GO:0016192;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAEQKIISLFDDDACTRYTILIASTIGEMREKKESIIDNTDPEIVKYLSQLLDVFRENFDTWAMAVVNRTGCALDPSTPK
SQ  DQVEVKKFRQFSETEKSECFIKCLLLLILSLGNYSPYSRNLLYSIAEKLGLSSIVVYKAELITSSMLLDTFQTMESNQEM
SQ  YELSGTRKMRRRIAMGLAGLAGGALIGLTGGLAAPFVAAGLGTLFAGLGLGTMIGATYLGTLITSAPMITALFGGFGAKM
SQ  SMQQMGDVSKGLTDFEFIPLSVQSHLPVTIGISGWLGDYNEVDAAWKSLTVGDKSYYWGDIYALKFEVEALVDLGKSLSR
SQ  ILFSAGLGWVKGEVISRTILAPLAAALWPLSLLKVGNILGNSWRIAFNLSIKAGEALANALCVRAQGMRPVTLIGFSLGA
SQ  RTILECLLHLADRGETNLVENVIVMGAPMPTDAKLWLKMRCVVAGRFVNVYSASDYVLQLVYRVNSAQSTAAGLGPVSLD
SQ  SNTLENVDVGDLVEGHLQYRWLVAKILKERLGYDNISDAEIQSLAVQEEKYESKQRTYYSQKEQEEEIEQEVLFDASSDT
SQ  ELAIQKKEDEVNEVRENKK
//
ID  Q9HDX1;
PN  Uncharacterized transcriptional regulatory protein PB1A11.04c;
GN  SPAPB1A11;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00227}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: Q9HDX1;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MIAAVEKDAVPRKRRVISQVSQACIRCRQKKIKCSGEKPSCQACSNNKVECIWPDRPNMRGKKPSSAARTLSPLTGIVQP
SQ  YLGSHPFSPTILSPSSPNMDFTYSINSFGDYQKQLRLPTSRKLLQLWDIFLKTSYTELFGIFNKAQITSQIASDTAPPVL
SQ  VLCICAHAARFSQEEVNRFKSSTAASDYYANQAFSLLPCRFQDISLTNITCLLLLCLIELGSCRGAKAWLLLGMALRMVD
SQ  SLDLGNEINDNPLTMGSNTVSWTEAEQKRRVYWACFFVERLLSTGYMAPSKLRSLSLSLQKTSIQLPCPEPNFLFNQPIL
SQ  TELFDGSLPENTQSDTTSMAPYQRSLQLEFMTGSLIRLSNLWSEISRWALCGGYTKDITPPWLNQSQFHRSFELLKAWHE
SQ  NLPPRAVWSYTNYSAYSSPGESAGACYTFMHLLYHTTLTYLLRNVLDLFPEKSRQKSKLFSSVSQRFGQQPPTVWMDMIL
SQ  DQVITSADFITKLSKDPLNYIMSPFVGFSILTAATIHMLLKFCVVNIDQNYISSSRLVHVDHQILQDRSKYWKINQAMLV
SQ  TLQRLYNFYRFQYLEEQSLYNFKIPGFPLCILEYGIVEDQSMKSNPDLNSFSKELFSRGTNELLNNGDDTQSGNSTPAMG
SQ  VSEIRTDTILDEEVPVDPLITSILDDGRWWEEMFGSERKAGFKETVFEDMNGRSIRL
//
ID  P0CU06;
PN  UPF0742 protein SPAC750.04c;
GN  SPAC750;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:P0CU07}. Nucleus membrane {ECO:0000250|UniProtKB:P0CU07}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to cytoplasmic dots and the nuclear envelope. {ECO:0000250|UniProtKB:P0CU07}.
DR  UNIPROT: P0CU06;
DR  UNIPROT: Q9P332;
DR  Pfam: PF09437;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0016021;
GO  GO:0031965;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MALLKKINTQVNRIMKNSSLVQNICFDRVPLFIPRLSLTVKYCLAVKLLIYLLYCWYIYSEVPSASSKFRSFTFGCVVVY
SQ  HNKFFPRFIRTHSINSIRTFSKFQVIILFSIEKVTRSESKNHSYSKTDISDLHQGYNNPPSRFISR
//
ID  P34454;
PN  Uncharacterized protein F54F2.9;
GN  F54F2;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000255|PROSITE- ProRule:PRU00624}; Single-pass membrane protein {ECO:0000305}.
DR  UNIPROT: P34454;
DR  Pfam: PF00226;
DR  Pfam: PF00249;
DR  PROSITE: PS50076;
DR  PROSITE: PS50090;
DR  PROSITE: PS51293;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0012505;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0003677;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRVILLLAFLISLTECQWTSEDLALYDLVEEVGVNFYEWFDIPRDASSNQVKKAYRKLTLEWHPDRNSAPDATEKFRQVA
SQ  GIYEVLKTTELREKYDNVLENGLPSWRHPMYYYRRMRKLAWYEGILVLLFIGTIAHYLMMWAAYFEKTLVYKQNVKKSRK
SQ  SKKEDPAEAEKLMKQALEEYLPKYSELLPIILARGTVTLFKNLALTAKDAMTPKEVEPEEPTEEELAQQRRQQRAAAAPQ
SQ  QLEFKFEVAQGMKAVSTNDPEMEKKYAAENEVVAQKQSGATWTPDELASLVRLSTEKYPAGTPNRWEQMGRVLNRSAEDV
SQ  IAMAGKMKQMKQEDYTKLLMTTIQQSVPVEEKSEDDWSQAEQKAFETALQKYPKGTDERWERISEEIGSKTKKQVMVRFK
SQ  QLAEMIRKKKTNDT
//
ID  O59744;
PN  Uncharacterized transcriptional regulatory protein C530.08;
GN  SPBC530;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O59744;
DR  Pfam: PF04082;
DR  Pfam: PF00172;
DR  PROSITE: PS00463;
DR  PROSITE: PS50048;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0000981;
GO  GO:0000978;
GO  GO:0008270;
GO  GO:0006357;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MDNESHSQETESKILEGAKVATRRRRVTRACDMCRRKKIKCDGLRPCKNCKAGKLECTYHMPSSRKSSFSPEYVENLESR
SQ  VRYLETLLKKNTNFDLSSNSPSFLFFLREQKFQATNELENMSPERKVIFTSMINYGNLFVDAKHGTRYFRGGSSIHVLIQ
SQ  HLIRRLPGDFEICEPYSAYPLGNKNIQFDDNDPEYQFFTPTPRFSIDFMVSSVDPREIQLPGIEEALCITKAAVSYVSGI
SQ  VFYTTYADFPKKIRLLYSGNYQGNFFPLFLSILCVGYYHHLLNNPSNTELQSLIKKYSFYSERLVKSADNFTIESIQCLL
SQ  ILSIYRYCRTEISAAWYYMKLGLNCCLRLGLHRNITEGFTEEQIDSRRRIFWAIYCYDRQLCTLFGFPLGVRDEDIDQCL
SQ  PVTPKFPSVTEIEANARLFFFHGVKLYKISSRILTKLYSPNSRNVTKKHISYAVIQDLEQLLDGFYNSLPRVFRAEQPGE
SQ  FQANHFFYNLQLVYYSFRMLIYRPLLHYLEADSPAMQALKVPDRQTAFTLACKCVDSAIVCVQNLSHLSKGLKRTLDRYY
SQ  WTTVYCGFSTIVTLIFAALLTKNTNLLIHISVARESIEALAHECVTRRLLPLIDKMRESLMKILESNADGYKQMSPTKAP
SQ  QVFESESNVPINNGPQQSIDKESNSNTQLPQVETEGQQQSVFDGNIGTIPYQAYNMNEDSFIDINTLSSMLNYHTQAVSI
SQ  HHPSFYISRSDVPLEEEFQIPNELLAVDPVAESMQENSDIINEAFGLVDPDVSDGKSRESSSLNNSTPFNPTVNIDPASI
SQ  LEHFSQNVMKDSQNS
//
ID  Q9Y820;
PN  PCI domain-containing protein C1105.07c;
GN  SPBC1105;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9Y820;
DR  Pfam: PF01399;
DR  PROSITE: PS50250;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0005635;
GO  GO:0005643;
GO  GO:0005634;
GO  GO:0000346;
GO  GO:0070390;
GO  GO:0003690;
GO  GO:0003723;
GO  GO:0016973;
GO  GO:0000973;
GO  GO:0006368;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSLNDFLQTLSNAVGEKNSNTLEKCIILDPSEPSFQQLSKTLFLDRKGKNKLNGTIQKEFGRIRGWKELVTTYFEYVENA
SQ  ASSPDQRKWELLQNLYSNLTTCFSHIDGAWLCTIVKRVSKLYVKLSLQLDTSTPTLEDSFDGNGFIQRKYVSDASRNVLR
SQ  TFNSILSDRQQNINPSKKDAIFCIANLLCLLYFRLKQIRLCQTIQANVISSGADISRATMAELVTFRYYLGRCHLYQRKI
SQ  HQAKDHLLFSFLQCPDECYHQKRLSLIYLTTCLLILGKSPTKGLLEKYKLTAAFEPLIKALKSGDIKSFRLSLEDNSRRK
SQ  WFIKRGIYLTLLDRCEIILWRNLFRKVFLFTFEQSQKTPHVSGSYLLTAARLSTNDNSYDMDDVECICVSLIDQGYIKGY
SQ  IIHASSTLVLKKDPSFGFSVIESLMPIARNDHAEKEFFHANA
//
ID  Q9UU91;
PN  Protein yop1;
GN  yop1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein {ECO:0000269|PubMed:20434336}. Nucleus membrane {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein {ECO:0000269|PubMed:20434336}. Note=Enriched at the cell equator during mitosis.
DR  UNIPROT: Q9UU91;
DR  Pfam: PF03134;
DE  Function: Required to generate and maintain the structure of the tubular endoplasmic reticulum network and the vacuole. Induces high curvature in membranes and causes membrane tubule formation. Involved in membrane/vesicle trafficking (By similarity). Required for the correct positioning of the cellular division plane by delimiting the actomyosin ring assembly at the cell equator (PubMed:20434336). {ECO:0000250|UniProtKB:Q12402, ECO:0000269|PubMed:20434336}.
DE  Reference Proteome: Yes;
GO  GO:0032153;
GO  GO:0032541;
GO  GO:0030176;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0007049;
GO  GO:0051301;
GO  GO:1990809;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q12402};
SQ  MSFQVRVKQNMQDLDNRLAAFPQLNSLEKNFGVSKLYVFLTAAGIYALFLFLNWGGFLLTNLLAFAMPAFFSINAIETTN
SQ  KADDTQWLTYYLVTSFLNVIEYWSQLILYYVPVYWLLKAIFLIWLALPKFNGATIIYRHLIRPYITPHVIRICKSVSRQN
SQ  AAPAPTASSFAHTTATDIPPSI
//
ID  Q06616;
PN  Nuclear envelope protein YPR174C;
GN  YPR174C;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
DR  UNIPROT: Q06616;
DR  UNIPROT: D6W4H5;
DR  Pfam: PF08537;
DE  Function: Specialized component of the nuclear membrane that may be involved in the connection of the spindle pole body (SPB) to the nuclear envelope. {ECO:0000269|PubMed:15282802}.
DE  Reference Proteome: Yes;
DE  Interaction: P40069; IntAct: EBI-794693; Score: 0.53
DE  Interaction: P47069; IntAct: EBI-2342813; Score: 0.37
DE  Interaction: P07259; IntAct: EBI-794693; Score: 0.35
DE  Interaction: P28003; IntAct: EBI-815383; Score: 0.27
DE  Interaction: Q12449; IntAct: EBI-818622; Score: 0.27
DE  Interaction: Q03860; IntAct: EBI-2343097; Score: 0.37
DE  Interaction: P53174; IntAct: EBI-2343694; Score: 0.37
DE  Interaction: P08456; IntAct: EBI-2347113; Score: 0.37
DE  Interaction: P32562; IntAct: EBI-2347516; Score: 0.37
DE  Interaction: P40578; IntAct: EBI-2347625; Score: 0.37
DE  Interaction: Q8N6L0; IntAct: EBI-11535750; Score: 0.56
DE  Interaction: Q5SW96; IntAct: EBI-11535739; Score: 0.56
DE  Interaction: Q969F0; IntAct: EBI-11535759; Score: 0.56
GO  GO:0005737;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005816;
TP  Membrane Topology: Peripheral; Source: UniProt - Sequence Analysis;
SQ  MGIQEKTLGIRKERKLVVVPRERNHVRHASQRTRSKNYKNISKKRAQQHAFGFNIAKTLAKIQAFVWGSPADEEEESVVP
SQ  LSKNSQDCVPLQWQAKFAQLRQQLHSTQKELQFVKEKCHLLQSVLDDANIDQRYLESRRDMKNIERDNLKPTENLPPSPV
SQ  RAVNPLVTSSPIHMSPLQSRQRPVSSLQPPKGPNFYAKYPKLPQTNILRESPTEDSVPHAE
//
ID  Q9Y7P8;
PN  Putative uncharacterized membrane protein C191.04c;
GN  SPCC191;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: Q9Y7P8;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005829;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005634;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MHSVCSIFLSCSHRVIQAKHPPFPLFHSYFHIPDFLSFVFPFVASPPLAFARRKLDHVPKKFARSIGPFLLIVFLFFNLF
SQ  PTFFFLPFFPDTTKRPNLAD
//
ID  Q9H6S0;
PN  3'-5' RNA helicase YTHDC2;
GN  YTHDC2;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:B2RR83}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:29970596}.
DR  UNIPROT: Q9H6S0;
DR  UNIPROT: B2RP66;
DR  PDB: 2YU6;
DR  PDB: 6K6U;
DR  PDB: 6LR2;
DR  Pfam: PF00270;
DR  Pfam: PF04408;
DR  Pfam: PF00271;
DR  Pfam: PF07717;
DR  Pfam: PF01424;
DR  Pfam: PF04146;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51061;
DR  PROSITE: PS50882;
DR  OMIM: 616530;
DR  DisGeNET: 64848;
DE  Function: 3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells (PubMed:26318451, PubMed:29033321, PubMed:29970596). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability (PubMed:26318451, PubMed:29033321). Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs (By similarity). Acts by binding and promoting degradation of m6A- containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both spermatogenesis and oogenesis (By similarity). {ECO:0000250|UniProtKB:B2RR83, ECO:0000269|PubMed:26318451, ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29970596}.
DE  Reference Proteome: Yes;
DE  Interaction: P27958; IntAct: EBI-9086804; Score: 0.46
DE  Interaction: P59595; IntAct: EBI-27129966; Score: 0.35
DE  Interaction: Q14203; IntAct: EBI-11382201; Score: 0.27
DE  Interaction: Q92905; IntAct: EBI-21325777; Score: 0.35
DE  Interaction: Q9NX58; IntAct: EBI-1071116; Score: 0.00
DE  Interaction: Q9H9J4; IntAct: EBI-2513636; Score: 0.40
DE  Interaction: Q13573; IntAct: EBI-7950968; Score: 0.35
DE  Interaction: Q9H0R8; IntAct: EBI-3048562; Score: 0.35
DE  Interaction: O95166; IntAct: EBI-3050465; Score: 0.35
DE  Interaction: Q9HC52; IntAct: EBI-3951861; Score: 0.35
DE  Interaction: Q15306; IntAct: EBI-6115566; Score: 0.50
DE  Interaction: Q99J34; IntAct: EBI-6117026; Score: 0.50
DE  Interaction: O15169; IntAct: EBI-6169699; Score: 0.35
DE  Interaction: Q86VP6; IntAct: EBI-21322532; Score: 0.35
DE  Interaction: Q13618; IntAct: EBI-21329068; Score: 0.35
DE  Interaction: P04637; IntAct: EBI-7903232; Score: 0.35
DE  Interaction: P41218; IntAct: EBI-9996028; Score: 0.35
DE  Interaction: P05412; IntAct: EBI-11324725; Score: 0.35
DE  Interaction: Q6ZWV7; IntAct: EBI-10997876; Score: 0.35
DE  Interaction: F8VQC1; IntAct: EBI-11054725; Score: 0.35
DE  Interaction: Q99PL5; IntAct: EBI-11066888; Score: 0.35
DE  Interaction: Q00839; IntAct: EBI-11088773; Score: 0.35
DE  Interaction: Q9P2K1; IntAct: EBI-11378868; Score: 0.27
DE  Interaction: A2AG06; IntAct: EBI-11664049; Score: 0.50
DE  Interaction: Q7Z398; IntAct: EBI-21528160; Score: 0.35
DE  Interaction: Q9GZY0; IntAct: EBI-21528397; Score: 0.35
DE  Interaction: P11487; IntAct: EBI-21532550; Score: 0.35
DE  Interaction: Q6AW86; IntAct: EBI-21553112; Score: 0.35
DE  Interaction: Q96ME7; IntAct: EBI-21582086; Score: 0.35
DE  Interaction: P55075; IntAct: EBI-21635166; Score: 0.35
DE  Interaction: B0UZZ8; IntAct: EBI-21740634; Score: 0.35
DE  Interaction: P62263; IntAct: EBI-21741976; Score: 0.35
DE  Interaction: Q02543; IntAct: EBI-21743296; Score: 0.35
DE  Interaction: Q9NZM5; IntAct: EBI-21744295; Score: 0.35
DE  Interaction: Q8NAP3; IntAct: EBI-21775305; Score: 0.35
DE  Interaction: Q96LW9; IntAct: EBI-21886352; Score: 0.35
DE  Interaction: P22087; IntAct: EBI-16792282; Score: 0.27
DE  Interaction: Q9UPY3; IntAct: EBI-20621391; Score: 0.35
DE  Interaction: P51531; IntAct: EBI-20918588; Score: 0.40
DE  Interaction: Q5S007; IntAct: EBI-21360986; Score: 0.35
DE  Interaction: Q9Y586; IntAct: EBI-21261050; Score: 0.35
DE  Interaction: Q15646; IntAct: EBI-21262435; Score: 0.35
DE  Interaction: P03372; IntAct: EBI-21301141; Score: 0.35
DE  Interaction: Q9NRI5; IntAct: EBI-21386460; Score: 0.00
DE  Interaction: Q16526; IntAct: EBI-21981854; Score: 0.35
DE  Interaction: Q9C0B5; IntAct: EBI-25637382; Score: 0.35
DE  Interaction: K9N4V0; IntAct: EBI-26375098; Score: 0.35
DE  Interaction: Q99608; IntAct: EBI-26957435; Score: 0.27
DE  Interaction: Q96T52; IntAct: EBI-27050444; Score: 0.35
DE  Interaction: P11801; IntAct: EBI-28931861; Score: 0.35
DE  Interaction: P51617; IntAct: EBI-28935882; Score: 0.35
DE  Interaction: P78362; IntAct: EBI-28948274; Score: 0.35
DE  Interaction: Q9Y2H9; IntAct: EBI-28948459; Score: 0.35
DE  Interaction: P0DTC9; IntAct: EBI-27102259; Score: 0.53
DE  Interaction: P15130; IntAct: EBI-27131516; Score: 0.35
DE  Interaction: Q0ZME3; IntAct: EBI-27131755; Score: 0.35
DE  Interaction: Q6Q1R8; IntAct: EBI-27132003; Score: 0.35
DE  Interaction: K9N4V7; IntAct: EBI-27132270; Score: 0.35
DE  Interaction: P33469; IntAct: EBI-27132272; Score: 0.35
DE  Interaction: P17948; IntAct: EBI-32722433; Score: 0.27
DE  Interaction: P36888; IntAct: EBI-32722567; Score: 0.27
DE  Interaction: P35916; IntAct: EBI-32722728; Score: 0.27
DE  Interaction: Q02763; IntAct: EBI-32732012; Score: 0.35
GO  GO:0005783;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0035770;
GO  GO:0034458;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0008186;
GO  GO:1990247;
GO  GO:0003723;
GO  GO:0070063;
GO  GO:0051729;
GO  GO:0051321;
GO  GO:0048599;
GO  GO:0044829;
GO  GO:0070555;
GO  GO:0034612;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRPSSVSPRQPAPGGGGGGGPSPCGPGGGGRAKGLKDIRIDEEVKIAVNIALERFRYGDQREMEFPSSLTSTERAFIHR
SQ  LSQSLGLVSKSKGKGANRYLTVKKKDGSETAHAMMTCNLTHNTKHAVRSLIQRFPVTNKERTELLPKTERGNVFAVEAEN
SQ  REMSKTSGRLNNGIPQIPVKRGESEFDSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIP
SQ  CRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHE
SQ  RDRFSDFLLTKLRDLLQKHPTLKLILSSAALDVNLFIRYFGSCPVIYIQGRPFEVKEMFLEDILRTTGYTNKEMLKYKKE
SQ  KQQEEKQQTTLTEWYSAQENSFKPESQRQRTVLNVTDEYDLLDDGGDAVFSQLTEKDVNCLEPWLIKEMDACLSDIWLHK
SQ  DIDAFAQVFHLILTENVSVDYRHSETSATALMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLE
SQ  SYSATLEFGNLDESSLVQTNGSDLSAEDRELLKAYHHSFDDEKVDLDLIMHLLYNICHSCDAGAVLIFLPGYDEIVGLRD
SQ  RILFDDKRFADSTHRYQVFMLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFV
SQ  TMLKMVWISKASAIQRKGRAGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLAPVNCPIADFLMKAPEP
SQ  PPALIVRNAVQMLKTIDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPTQASQKR
SQ  AAMLCRKRFTAGAFSDHMALLRAFQAWQKARSDGWERAFCEKNFLSQATMEIIIGMRTQLLGQLRASGFVRARGGGDIRD
SQ  VNTNSENWAVVKAALVAGMYPNLVHVDRENLVLTGPKEKKVRFHPASVLSQPQYKKIPPANGQAAAIKALPTDWLIYDEM
SQ  TRAHRIANIRCCSAVTPVTILVFCGPARLASNALQEPSSFRVDGIPNDSSDSEMEDKTTANLAALKLDEWLHFTLEPEAA
SQ  SLLLQLRQKWHSLFLRRMRAPSKPWSQVDEATIRAIIAVLSTEEQSAGLQQPSGIGQRPRPMSSEELPLASSWRSNNSRK
SQ  SSADTEFSDECTTAERVLMKSPSPALHPPQKYKDRGILHPKRGTEDRSDQSSLKSTDSSSYPSPCASPSPPSSGKGSKSP
SQ  SPRPNMPVRYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSIVYLVFSVQGSGHFQGFSRMSSEIGREKSQDW
SQ  GSAGLGGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPLVGEQLLQLWERLPLGEKNTTD
//
ID  B2RR83;
PN  3'-5' RNA helicase YTHDC2;
GN  Ythdc2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H6S0}.
DR  UNIPROT: B2RR83;
DR  Pfam: PF00270;
DR  Pfam: PF04408;
DR  Pfam: PF00271;
DR  Pfam: PF07717;
DR  Pfam: PF01424;
DR  Pfam: PF04146;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51061;
DR  PROSITE: PS50882;
DE  Function: 3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells (PubMed:28380054, PubMed:28809393, PubMed:29033321, PubMed:29087293, PubMed:29360036, PubMed:32470506). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non- coding RNAs that plays a role in the efficiency of RNA processing and stability (PubMed:29360036). Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs (PubMed:29033321). Acts by binding and promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both spermatogenesis and oogenesis (PubMed:28809393, PubMed:29033321). {ECO:0000269|PubMed:28380054, ECO:0000269|PubMed:28809393, ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036, ECO:0000269|PubMed:32470506}.
DE  Reference Proteome: Yes;
DE  Interaction: P49452; IntAct: EBI-8573213; Score: 0.35
DE  Interaction: A2AG06; IntAct: EBI-11664030; Score: 0.54
DE  Interaction: Q6NZM9; IntAct: EBI-26471532; Score: 0.35
DE  Interaction: Q9CQE6; IntAct: EBI-26472808; Score: 0.35
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0035770;
GO  GO:0034458;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0008186;
GO  GO:1990247;
GO  GO:0003723;
GO  GO:0070063;
GO  GO:0051729;
GO  GO:0051321;
GO  GO:0048599;
GO  GO:0044829;
GO  GO:0070555;
GO  GO:0034612;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRPSSVSPRPPAPSGGGTGGGGGGSGGGGGGGGGGPASCGPGGGGRAKGLKDIRIDEEVKIAVNIALERFRYGDQREME
SQ  FPSSLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKKKDGSETAHAMMTCNLTHNTKHAVRSLIQRFPVTNKERTELL
SQ  PKTERGNVFAVEAENREMSKTSGRLNNGIPQVPVKRGESEFDSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQ
SQ  IPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDS
SQ  TLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALDVNLFIRYFGSCPVIYIQGRPFEVKEMFLEDILR
SQ  TTGYTNKEMLKYKKEKQREEKQQTTLTEWYSAQENTFKPESQRQRAVASVSEEYDLLDDGGDAVFSQLTEKDVNCLEPWL
SQ  IKEMDACLSDIWLHKDVDAFAQVFHLILTENVSVDYRHSETSATALMVAAGRGFTSQVEQLISMGANVHSKASNGWMALD
SQ  WAKHFGQTEIVDLLESYSASLEFGNLDESSLVQTNGNDLSAEDRELLKAYHHSFDDEKVDLDLIMHLLYNICHSCDAGAI
SQ  LIFLPGYDEIVGLRDRILFDDKRFADNTHRYQVFMLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVID
SQ  SGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLAP
SQ  VNCTIADFLMKAPEPPPALIVRNAVQMLKTIDAMDAWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLA
SQ  YRDPFVLPTQASQKRAAMLCRKRFTAGTFSDHMALLRAFQAWQKARSDGWERAFCEKNFLSQATMEIIIGMRTQLLGQLR
SQ  ASGFVRARGGGDIRDVNTNSENWAVVKAALVAGMYPNLVHVDRENVILTGPKEKKVRFHPTSVLSQPQYKKIPPANGQAA
SQ  AIQALPTDWLIYDEMTRAHRIANIRCCSAVTPVTVLVFCGPARLASNALQEPSSFRADGIPNDSSDSEMEDRTTANLAAL
SQ  KLDEWLNFKLEPEAASLLLQLRQKWHSLFLRRMRAPSKPWSQVDEATIRAIIAVLSTEEQSAGLQQPSGIGQRPRPMSSE
SQ  ELPLASSWRSNNSRKSTADTEFADGSTTGERVLMKSPSPALHPPQKYKDRGILHPKRSTDDRSDQSSVKSTDSSSYPSPC
SQ  ASPSPPSSGKGSKSPSPRPNMPIRYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGF
SQ  SRMSSEIGREKSQDWGSAGLGGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLWERLPLGE
SQ  KTTSD
//
ID  Q5R746;
PN  3'-5' RNA helicase YTHDC2;
GN  YTHDC2;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:B2RR83}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H6S0}.
DR  UNIPROT: Q5R746;
DR  UNIPROT: A0A2J8XEL0;
DR  Pfam: PF00270;
DR  Pfam: PF04408;
DR  Pfam: PF00271;
DR  Pfam: PF07717;
DR  Pfam: PF01424;
DR  Pfam: PF04146;
DR  PROSITE: PS50297;
DR  PROSITE: PS50088;
DR  PROSITE: PS51192;
DR  PROSITE: PS51194;
DR  PROSITE: PS51061;
DR  PROSITE: PS50882;
DE  Function: 3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells. Specifically recognizes and binds N6- methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability. Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs. Acts by binding and promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease. Required for both spermatogenesis and oogenesis. {ECO:0000250|UniProtKB:B2RR83}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0035770;
GO  GO:0034458;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:1990247;
GO  GO:0003723;
GO  GO:0051729;
GO  GO:0051321;
GO  GO:0048599;
GO  GO:0007286;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRPSSVSPRQPAPGGGGGGGPSPCGPGGGGRAKGLKDIRIDEEVKIAVNIALERFRYGDQREMEFPSSLTSTERAFIHR
SQ  LSQSLGLVSKSKGKGANRYLTVKKKDGSETAHAMMTCNLTHNTKHAVRSLIQRFPVTNKERTELLPKTERGNVFAVEAEN
SQ  REMSKTSGRLNNGIPQIPVKRGESEFDSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIP
SQ  CRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHE
SQ  RDRFSDFLLTKLRDLLQKHPTLKLILSSAALDVNLFIRYFGSCPVIYIQGRPFEVKEMFLEDILRTTGYTNKEMLKYKKE
SQ  KQQEEKQQTTLTEWYSAQENSFKPGSQRQRTVLNVTDEYDLLDDGGDAVFSQLTEKDVNCLEPWLVKEMDACLSDIWLHK
SQ  DIDAFAQVFHLILTENVSVDYRHSETSATALMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLE
SQ  SYSASLEFGNLDESSLVQTNGSDLSAEDRELLKAYHHSFDDEKVDLDLIMHLLYNICHSCDAGAVLIFLPGYDEIVGLRD
SQ  RILFDDKRFADNTHRYQVFMLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFV
SQ  TMLKMVWISKASAIQRKGRAGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLAPVNCPVADFLMKAPEP
SQ  PPALIVRNAVQMLKTIDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPTQASQKR
SQ  AAMLCRKRFTAGAFSDHMALLRAFQAWQKARSDGWERAFCEKNFLSQATMEIIIGMRTQLLGQLRASGFVRARGGGDIRD
SQ  VNTNSENWAVVKAALVAGMYPNLVHVDRENLVLTGPKEKKVRFHPASVLSQPQYKKIPPANGQAAAIKALPTDWLIYDEM
SQ  TRAHRIANIRCCSAVTPVTILVFCGPARLASNALQEPSSFRVDGIPNDSSDSEMEDKTTANLAALKLDEWLHFKLEPEAA
SQ  SLLLQLRQKWHSLFLRRMRAPSKPWSQVDEATIRAIIAVLSTEEQSAGLQQPSGIGQRPRPMSSEELPLASSWRSNNSRK
SQ  SSADTEFSDECTTAERVLMKSPSPALHPPQKYKDRGILHPKRGTEDRSDQSSVKSTDSSSYPSPCASPSPPSSGKGSKSP
SQ  SPRPNMPVRYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKSQDW
SQ  GSAGLGGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLWERLPLGEKNTTD
//
ID  F1Q7H8;
PN  Palmitoyltransferase ZDHHC20-A;
GN  zdhhc20a;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cell membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5W0Z9}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: F1Q7H8;
DR  UNIPROT: A4FVK6;
DR  UNIPROT: Q05AL0;
DR  Pfam: PF01529;
DR  PROSITE: PS50216;
DE  Function: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. Catalyzes palmitoylation of Cys residues on protein substrates and has a preference for acyl-CoA with C16 fatty acid chains but may also utilize acyl-CoA with C14 and C18 fatty acid chains. {ECO:0000250|UniProtKB:Q5W0Z9}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0046872;
GO  GO:0019705;
GO  GO:0019706;
GO  GO:0140439;
GO  GO:0018230;
GO  GO:0018345;
GO  GO:0006612;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5W0Z9};
SQ  MAPSHAVRCCQRGLSWIPVIFINLVVCWSYYAYVVELCIYTIPNVNEQVIYLVVFHAFFFMFMWSYWKTISSKPTNPSKE
SQ  FCLPKAEKELYEKEERPEAQQDILKRVARELPIYTFTGSGAIRYCDRCQLIKPDRCHHCSTCDKCVLKMDHHCPWVNNCV
SQ  GFSNYKFFVLFLAYSMLYCVYIAATVLQYFIKFWTNQLPDTHAKFHVLFLFFVAAMFFISILSLFSYHLWLVGKNRTTIE
SQ  AFRAPVFRNGPDKNGFTLGFRKNITQVFGDQKKYWCLPIFSSLGDGYTFPTRLVTVDVEHGNIEHQTIKCTVDGQTNARP
SQ  LSESQNHLLCNDEGQKDSSMAAIEVCQPVCVTLENES
//
ID  E7F587;
PN  Palmitoyltransferase ZDHHC20-B;
GN  zdhhc20b;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cell membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5W0Z9}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: E7F587;
DR  Pfam: PF01529;
DR  PROSITE: PS50216;
DE  Function: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. Catalyzes palmitoylation of Cys residues on protein substrates and has a preference for acyl-CoA with C16 fatty acid chains but may also utilize acyl-CoA with C14 and C18 fatty acid chains. {ECO:0000250|UniProtKB:Q5W0Z9}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0046872;
GO  GO:0019705;
GO  GO:0019706;
GO  GO:0140439;
GO  GO:0018230;
GO  GO:0018345;
GO  GO:0006612;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5W0Z9};
SQ  MAPTHVLRCCQRGLAWIPVIFIALVVCWSYYAYVVELCLLVYLVVFHLSFVMFVWSYWKTIFTKPANPSKEFCLPKSEKE
SQ  QYEKEQRPETQQEILKKVATSLPLYTRTGAGAIRYCDRCQVIKPDRCHHCSACDMCVLKMDHHCPWVNNCVGFSNYKFFI
SQ  LFLTYSLVYCLFIAASVLQYFIKFWTSDLPESHAKFHVLFLFFVAAMFCISILSLFTYHLWLVGKNRSTIEAFRAPVFRN
SQ  GPDKNGFSLGFSKNIAQVFGDEKKYWLLPVFTSQGDGLSFPTRLVTIDPEQPTECLQPGGAISSLIIVEYCFCKQAKKKK
SQ  TDE
//
ID  Q8WVZ1;
PN  Palmitoyltransferase ZDHHC19;
GN  ZDHHC19;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000269|PubMed:20074548, ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20074548}.
DR  UNIPROT: Q8WVZ1;
DR  UNIPROT: A0A0B4J1W2;
DR  UNIPROT: A8MSY6;
DR  UNIPROT: B3KVI1;
DR  Pfam: PF01529;
DR  PROSITE: PS50216;
DR  OMIM: 618671;
DR  DisGeNET: 131540;
DE  Function: Palmitoyltransferase that mediates palmitoylation of RRAS, leading to increased cell viability. {ECO:0000269|PubMed:20074548}. (Microbial infection) Promotes Chikungunya virus (CHIKV) replication by mediating viral nsp1 palmitoylation. {ECO:0000269|PubMed:30404808}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9UBL6; IntAct: EBI-21900849; Score: 0.40
DE  Interaction: P40763; IntAct: EBI-22197569; Score: 0.35
DE  Interaction: P42858; IntAct: EBI-25961282; Score: 0.56
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0097356;
GO  GO:0019706;
GO  GO:0018230;
GO  GO:0006612;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTLLTDATPLVKEPHPLPLVPRPWFLPSLFAAFNVVLLVFFSGLFFAFPCRWLAQNGEWAFPVITGSLFVLTFFSLVSLN
SQ  FSDPGILHQGSAEQGPLTVHVVWVNHGAFRLQWCPKCCFHRPPRTYHCPWCNICVEDFDHHCKWVNNCIGHRNFRFFMLL
SQ  VLSLCLYSGAMLVTCLIFLVRTTHLPFSTDKAIAIVVAVSAAGLLVPLSLLLLIQALSVSSADRTYKGKCRHLQGYNPFD
SQ  QGCASNWYLTICAPLGPKYMAEAVQLQRVVGPDWTSMPNLHPPMSPSALNPPAPTSGSLQSREGTPGAW
//
ID  Q810M5;
PN  Palmitoyltransferase ZDHHC19;
GN  Zdhhc19;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8WVZ1}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8WVZ1}.
DR  UNIPROT: Q810M5;
DR  Pfam: PF01529;
DR  PROSITE: PS50216;
DE  Function: Palmitoyltransferase that mediates palmitoylation of RRAS, leading to increased cell viability. {ECO:0000250|UniProtKB:Q8WVZ1}.
DE  Reference Proteome: Yes;
DE  Interaction: P40763; IntAct: EBI-22117867; Score: 0.58
DE  Interaction: P62993; IntAct: EBI-22118041; Score: 0.50
GO  GO:0005783;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0048471;
GO  GO:0097356;
GO  GO:0019706;
GO  GO:0018230;
GO  GO:0006612;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MPFLKDAVTLVKEPQQLPSIPLSWFPSSVFAAFNVTLLLFLSGLFFGFPCRWLVQNGEWAFPAITGPLFILTFFSLVSLN
SQ  FSDPGILHRGSTKEDPMTVHVVRVNQRAFRLEWCPKCLFHRPPRTYHCPWCNICVEDFDHHCKWVNNCIGHRNFRLFMLL
SQ  VLSLCLYSGALLVTCLTFLFRTRHLPFSLDKGMAILVAVPAAGFLIPLFLLLLIQALSVSRAESSYESKCRYHPEYNPFD
SQ  QGFAKNWYLAMFAPLGPNYMSEVVCLQRPVGTAWIQEKTKPSPPRRPKHCRPGPPGPQHQPRRVPGKGPPGSGEAAALQE
SQ  MRRLPASVEKSPGGPRQPTAEPAAGDP
//
ID  Q0VC89;
PN  Palmitoyltransferase ZDHHC20;
GN  ZDHHC20;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cell membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5W0Z9}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q0VC89;
DR  Pfam: PF01529;
DR  PROSITE: PS50216;
DE  Function: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation. Has a preference for acyl-CoA with C16 fatty acid chains. Can also utilize acyl-CoA with C14 and C18 fatty acid chains. {ECO:0000250|UniProtKB:Q5W0Z9}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0005794;
GO  GO:0030173;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0019705;
GO  GO:0019706;
GO  GO:0140439;
GO  GO:0008270;
GO  GO:0018230;
GO  GO:0018345;
GO  GO:0006612;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5W0Z9};
SQ  MAPCTLWRCCQRTVGWVPVLFITFVVVWSYYAYVVELCVFTLSGNGENGKAVVYLVAFHLFFVMFVWSYWMTIFTSPASP
SQ  SKEFCLSNSEKERYEKEFSQERQQEILRRAARDLPIYTTSASKTVRYCERCQLIKPDRAHHCSACDMCILKMDHHCPWVN
SQ  NCVGFSNYKFFLLFLFYSLLYCLFVATTVLQYFIKFWTNELTDTRAKFHVLFLFFVSTMFFISVLSLLSYHCWLVGKNRT
SQ  TIESFRAPMFSYGTDGNGFSLGCSKNWRQVFGDEKKYWLLPVFSSQGDGCSFPTRLVGTDPEQASVSNQSESARSIGSNQ
SQ  PFPIKPLSESKNRLLDSDPQWLESGSEEGVGGSGTNNHVTVAIEN
//
ID  Q5W0Z9;
PN  Palmitoyltransferase ZDHHC20;
GN  ZDHHC20;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000269|PubMed:29326245}; Multi-pass membrane protein {ECO:0000269|PubMed:29326245}. Cell membrane {ECO:0000269|PubMed:27153536}; Multi-pass membrane protein {ECO:0000269|PubMed:29326245}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:34599882}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000305|PubMed:34599882}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q5W0Z9;
DR  UNIPROT: A8MTV9;
DR  UNIPROT: C9JG20;
DR  UNIPROT: I6L9D4;
DR  UNIPROT: Q2TB82;
DR  UNIPROT: Q6NVU8;
DR  PDB: 6BML;
DR  PDB: 6BMM;
DR  PDB: 6BMN;
DR  PDB: 7KHM;
DR  Pfam: PF01529;
DR  PROSITE: PS50216;
DR  OMIM: 617972;
DR  DisGeNET: 253832;
DE  Function: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates (PubMed:27153536, PubMed:29326245, PubMed:33219126). Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation (PubMed:27153536). Has a preference for acyl-CoA with C16 fatty acid chains (PubMed:29326245). Can also utilize acyl-CoA with C14 and C18 fatty acid chains (PubMed:29326245). {ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:29326245, ECO:0000269|PubMed:33219126}. (Microbial infection) Dominant palmitoyltransferase responsible for lipidation of SARS coronavirus-2/SARS-CoV-2 spike protein. Through a sequential action with ZDHHC9, rapidly and efficiently palmitoylates spike protein following its synthesis in the endoplasmic reticulum (ER). In the infected cell, promotes spike biogenesis by protecting it from premature ER degradation, increases half-life and controls the lipid organization of its immediate membrane environment. Once the virus has formed, spike palmitoylation controls fusion with the target cell. {ECO:0000269|PubMed:34599882}.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q86X19; IntAct: EBI-11372615; Score: 0.27
DE  Interaction: Q68D91; IntAct: EBI-21867499; Score: 0.35
DE  Interaction: O43493; IntAct: EBI-16800265; Score: 0.27
DE  Interaction: P0DTC3; IntAct: EBI-25686340; Score: 0.35
DE  Interaction: P07339; IntAct: EBI-25840135; Score: 0.56
DE  Interaction: O76024; IntAct: EBI-25900261; Score: 0.56
DE  Interaction: Q9Y3C5; IntAct: EBI-25919797; Score: 0.56
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
DE  Interaction: P0DTC2; IntAct: EBI-27075292; Score: 0.44
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0005794;
GO  GO:0000139;
GO  GO:0030173;
GO  GO:0043231;
GO  GO:0016020;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016409;
GO  GO:0019705;
GO  GO:0019706;
GO  GO:0140439;
GO  GO:0008270;
GO  GO:0018230;
GO  GO:0044794;
GO  GO:0018345;
GO  GO:0006612;
TP  Membrane Topology: Transmembrane; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:29326245};
SQ  MAPWTLWRCCQRVVGWVPVLFITFVVVWSYYAYVVELCVFTIFGNEENGKTVVYLVAFHLFFVMFVWSYWMTIFTSPASP
SQ  SKEFYLSNSEKERYEKEFSQERQQEILRRAARALPIYTTSASKTIRYCEKCQLIKPDRAHHCSACDSCILKMDHHCPWVN
SQ  NCVGFSNYKFFLLFLLYSLLYCLFVAATVLEYFIKFWTNELTDTRAKFHVLFLFFVSAMFFISVLSLFSYHCWLVGKNRT
SQ  TIESFRAPTFSYGPDGNGFSLGCSKNWRQVFGDEKKYWLLPIFSSLGDGCSFPTRLVGMDPEQASVTNQNEYARSSGSNQ
SQ  PFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGTNNHVTVAIEN
//
ID  Q5Y5T1;
PN  Palmitoyltransferase ZDHHC20;
GN  Zdhhc20;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cell membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5W0Z9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q5W0Z9}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein {ECO:0000255}.
DR  UNIPROT: Q5Y5T1;
DR  UNIPROT: Q3TDL1;
DR  UNIPROT: Q8VCL6;
DR  UNIPROT: Q9D3Q8;
DR  Pfam: PF01529;
DR  PROSITE: PS50216;
DE  Function: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates (PubMed:15603741). Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation. Has a preference for acyl-CoA with C16 fatty acid chains. Can also utilize acyl-CoA with C14 and C18 fatty acid chains (By similarity). {ECO:0000250|UniProtKB:Q5W0Z9, ECO:0000305|PubMed:15603741}.
DE  Reference Proteome: Yes;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0033116;
GO  GO:0005794;
GO  GO:0030173;
GO  GO:0043231;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0016409;
GO  GO:0019705;
GO  GO:0019706;
GO  GO:0140439;
GO  GO:0008270;
GO  GO:0018230;
GO  GO:0044794;
GO  GO:0018345;
GO  GO:0006612;
TP  Membrane Topology: Transmembrane; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q5W0Z9};
SQ  MAPWTLWRCCQRVVGWVPVLFITFVVVWSYYAYVVELCVSTISRTGEKGKTVVYLVAFHLFFVMFVWSYWMTIFTSPASP
SQ  SKEFYLSNSEKERYEKEFSQERQQDILRRAARDLPIYTTSASKAIRYCEKCQLIKPDRAHHCSACDRCVLKMDHHCPWVN
SQ  NCVGFTNYKFFMLFLLYSLLYCLFVAATVLEYFIKFWTLCRRKSTENCPKNEPTVLNFPSAKFHVLFLFFVSAMFFVSVL
SQ  SLFSYHCWLVGKNRTTIESFRAPMFSYGIDGNGFSLGCSKNWRQVFGDEKKYWLVPIFSSLGDGCSFPARLVGMDPEQAS
SQ  VANQSDYVRSIGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGVTKSGTNNHVTVEIEN
//
ID  O13918;
PN  Zinc homeostasis factor 1;
GN  zhf1;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11886869}; Multi-pass membrane protein {ECO:0000269|PubMed:11886869}. Nucleus membrane {ECO:0000269|PubMed:11886869}; Multi-pass membrane protein {ECO:0000269|PubMed:11886869}.
DR  UNIPROT: O13918;
DR  UNIPROT: P78885;
DR  Pfam: PF01545;
DE  Function: Involved in zinc homeostasis, where it plays a role in its accumulation in the endoplasmic reticulum/nucleus. Also has a role in the sequestration of cadmium into the endoplasmic reticulum. {ECO:0000269|PubMed:11886869}.
DE  Reference Proteome: Yes;
GO  GO:0005789;
GO  GO:0000329;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005385;
GO  GO:0006877;
GO  GO:0098849;
GO  GO:0006882;
GO  GO:0140209;
GO  GO:0062111;
GO  GO:0071577;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MFDLARQTRIILLLGIDVTFFFIEIITGYAIDSLALIADSFHMLNDIVSLLVALWATRLAHSTSHEPKYTYGWQRAEILG
SQ  ALSNGVFLIALCMFIFMEAIERFIEPPSVSNPTLMFFVGSLGLLSNFVGIFLFHDHGHDHPHTHTAQNYDFPEEDDIESV
SQ  LPSTIVHRCNTSQQEVSHTHTQVADSATESSPLLSYTGNHNGAGTSKPVNNHGSIEQDAPKQTKKRNLNMHGVFLHVLGD
SQ  ALGNIGVISAALFIKYTDYSWRFLFDPCISILLTFIILFSAIPLCKSAALILLQVAPQSIKLDDVSNLINHLDGVESVHE
SQ  LHIWQLSDVKLIATVHVCVTLPDDKGESYTKLTTDIRNVLQSFGIYDVTIQPEFANHPLLCDQGSSS
//
ID  E9P860;
PN  NFX1-type zinc finger-containing protein 1 homolog;
GN  znfx;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580}. Cytoplasm {ECO:0000269|PubMed:29775580}. Cytoplasmic granule {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580, ECO:0000269|PubMed:32843637}. Note=Co-localizes with wago-4 in P- granules in germline blastomeres until the 100-cell stage (PubMed:29769721). During oocyte maturation, co-localizes with wago-4 in liquid-like condensates in the cytoplasm called Z granules (PubMed:29769721). Localizes to perinuclear and cytoplasmic P-granules in germline blastomeres and germ cells (PubMed:29775580, PubMed:29769721). In the adult germline, co-localizes with deps-1 in P- granules (PubMed:32843637). {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580, ECO:0000269|PubMed:32843637}.
DR  UNIPROT: E9P860;
DR  UNIPROT: Q23388;
DR  Pfam: PF13086;
DR  Pfam: PF13087;
DE  Function: Epigenetic inheritance factor which, in association with the Argonaute protein wago-4, mediates small RNA-directed transgenerational epigenetic inheritance and thus balances the transgenerational inheritance of epigenetic information (PubMed:29775580, PubMed:29769721). Specifically, maintains a balanced production of small RNAs by preventing the spread of epigenetic signals towards the 5'-end of target mRNAs (PubMed:29775580). Plays a role in small RNA- induced gene silencing in the germline (PubMed:29775580). {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29775580}.
DE  Reference Proteome: Yes;
GO  GO:0031380;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0003723;
GO  GO:0003724;
GO  GO:0008270;
GO  GO:0031047;
GO  GO:0031048;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSRDKPPQREVGGRRLPYEMGSLKFDEDPFRGQRRRPWMCFRIGYPTSEFSSEHFMKFVKRCHTSMIEVGILLDDEREFL
SQ  QYQEVREDYLLLKKLIEEGLQKCETIYEKGPLSTPVVFFILDQCDEDEVQNMLDMFRESCYIFHMKRNEILNWINEMEYE
SQ  ELESDCSKFAQFIKGVENLTESIAMPMEVETEEFIFGKSSIVSTEDFVEDAPHKQIAQDQRETRPIRQPYSMVRNLAPPG
SQ  LPPPGISISNSSPPGLSSVSPIPRADTRESRYSTPQPPGLSIPAPPGISLPTPPGISLQNHQNDQFEQAHSTISRMSENS
SQ  SSSRRRFRDEEVQEEEGDHILSSEDVHAARNVCETKILVRGVPQKNDSELSKLINGSKLYVRFERPFVKLAHNLELLYVV
SQ  NYAISSRKSIVRDHSKAIIRGLFEKDFLLKLKSKFLESSFDNDTWTPEGTELLFEIFHLFFTTARYKGGFMLTLPRFAPS
SQ  WHDFSMAFDIADMDGLEEAGVGDDELRNLRRLIGYIETWIKRAERERNPSPLALRSYSVYEKAGSSDSGRQVLSESRGAG
SQ  SSNVYGHDEVDFVDHRRRDEFGHRDNYRTENRRHKSPDNFGEVHRRLDEQQQQRHEDESSRYRDDSRQSRRADDRRDQYQ
SQ  YNESTSMENHLGFHNGGGTVSEHSRDDKFVSPQNCEEKRKYCEEDTDAKPQQPYRFEEIKFEPIWVKCEKSEPPEDFKTL
SQ  PSVPVLSEYVNPVEPYLRRIQDDGKYKSVHHYLDVQFRLLKEDLVSPLRDGIDLYKKNGTCKGRRIEGAPCSDISIFNVE
SQ  KVDGKQVTERDGYEMRIIWPAQYDILKLLDNDREMKELGLVMLSCDRFKEDFHLGHIQSSYLMRNGSLHFAVHEETSPFK
SQ  PNTTYQMAQGTSYLPCYKHVLENLKRISSFKPLPFERYLVHGSKIIFRPNFQQAEKSEYQISEEKKLMKTYNELRSLAAC
SQ  ARYTKGKPIPRGVDDDDEDYEFSKSRELSKEDIDLEYRQLQEPIFRPLVGVDIKDSNLIQINKKWYNVSRLLDEFHPDYM
SQ  DESQRLAFCNTFKYELSLIQGPPGTGKTHIGVQIVKTILQNRSYWKITEPILVVCFTNSGLDNLLERIYQMIENDEELSK
SQ  DNGRPKIIRFGSKCDSNYLKRQNVMRQDVYEQYKSKVSDGAQKKMSKAGAARRHKADNLAISSYTLFCSRNKLLSYEMLS
SQ  RVMDPNHQMEIQQFTYDHVDTKGIPLSPDEAIGCWLLERDFGKATKSQTKKAKKPKFQGAQLDSEDENKDYFTVEDSDDE
SQ  EDELDDEKLLDKLFEKMNLECSGADILSAVHASHADEYYTKGPWEIVQDKRPSVVVLMEKKTKPCNAKFTVDEQINNLVS
SQ  EIKDMILSSQPVPKKDLNDIKYIFSLARLKRWSLYITWCDALRSIVTENLPRQIREYREACENFKNAQNRVDAEIMRMTM
SQ  IIGATTTGCSRLRPTLEKVGPRILIVEEAAEVLEAHIISAMISTVEHVVMIGDHKQLRPNPAVHELGVAYGLRISMFERL
SQ  VERGLPFSQLRQQHRMNLTISDKIVKLSFYDNVTDAENVGLYPDVQGMATNLFFWSHTSMEESPDEVSWLNKHEISMTVA
SQ  LVKHLLKQNYTTNDIVVLATYSAQKNLMYREYANVFGSTPDSNVIPVETVDSFQGKERKIVIVSLVRSHRGGRENTGIGF
SQ  LAVANRICVALTRAQHGMYIIGNGAYIMNNSELWNKIVNNLRRSNLIEYNLPLKCVAHGNIVTVKDPQDFATKSPEGGCM
SQ  QKCDTKKFCGHVCERLCHPNMEEEHLQRCLYNCDKKCSNPQFQHRCKKACYEECGSCLYLVEVTLDCGHRITTPCSRINS
SQ  SKCDQSCTKKLLCGHACAAKCGEECTLVSECSQLVGMPLSCGHIKQLTCSKISANEIDLTCDQRCEKTMLACPHKCAEIC
SQ  GQPCTVECMEVVNVTLGCSHSQDVVCSSFMPGMTDHIECLTKVPKTLSPCKHTELVLCKQAPSTKLCTRRCTSYLEKCGH
SQ  TCENDCGICFTTKTHICQNMCQKVLNCGHTCSAKCGESCPPCKAFCTNKCEHQSCGAGERGFGRDCSKLCALCVNNCSNK
SQ  CAHRSCTLKCFEECNVKPCTEPCTDKLKCGHACLGICGEQCPKICGTCERNKYIECVSGTSSTSRVHRLIMIPKCYHVFP
SQ  VEVLDDHVKKQKEANEKLKCPKCSAFIVGVLRYARYTKKYYLNENMRKLESNIRNIHQSTLEGRVFQAVQDSIGEIRNVT
SQ  TNLTNASEDILRNFHQKILDIRTSAETFKGKPEHKFKFASLLQVANCCLAITRLLSVSSKFRVSRRKDIPPTFDLMSVRV
SQ  LGDMPFPKLIDELNRVNIHLSNTYETFMPGAIIPKLKWLISRMTVLQQLTSMCHQLVLEKKDIADSDAHAINDACLNMFR
SQ  YNEQHNYALNIENFEAIVVKVAPKLLEPTPKFWSWRRLQVPEL
//
ID  Q2TBX0;
PN  Zinc finger protein ZPR1;
GN  ZNF259;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus, gem {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle-dependent manner. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons (By similarity). {ECO:0000250}.
DR  UNIPROT: Q2TBX0;
DR  Pfam: PF03367;
DE  Function: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0015030;
GO  GO:0005737;
GO  GO:0097504;
GO  GO:0030426;
GO  GO:0043025;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0030971;
GO  GO:0031369;
GO  GO:0008270;
GO  GO:1902742;
GO  GO:0061564;
GO  GO:0030576;
GO  GO:0071364;
GO  GO:0042023;
GO  GO:0001833;
GO  GO:0000226;
GO  GO:0006397;
GO  GO:2000672;
GO  GO:0045787;
GO  GO:0010628;
GO  GO:0045927;
GO  GO:0042307;
GO  GO:0033120;
GO  GO:0071931;
GO  GO:1990261;
GO  GO:0031641;
GO  GO:0008380;
GO  GO:0021510;
GO  GO:0001834;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSAGGAVEPGLPAAAAAPSAAPARDPGPGHLFRPISAEDEEQQPTEIESLCMNCYRNGMTRLLLTKIPFFREIIVSSFSC
SQ  EHCGWNNTEIQSAGRIQDQGVRYTLTVRAQEDMDREVVKTDSATTRIPELDFEIPAFSQKGALTTVEGLISRAISGLEQD
SQ  QPTRRANEEAVAERIDEFIAKLKELKQVASPFTLIIDDPSGNSFVENPHAPRKDDALVITHYNRTLQQEEMLGLQAEAPE
SQ  EKPEEEDIRNEVLQFNTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITFHITDPSD
SQ  MTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGMLKDIRELVTKNPFTLGDSSSPGQTEKLQEFSQKLDQILEGILK
SQ  AHFIMDDPAGNSYLQNVYAPEDDPEMKVEHYKRTFDQNEELGLNDMKTEGYETGLPAQR
//
ID  O75312;
PN  Zinc finger protein ZPR1;
GN  ZPR1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Nucleus, nucleolus. Nucleus, gem. Nucleus, Cajal body. Cytoplasm, perinuclear region. Cytoplasm. Cell projection, axon {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons (By similarity). Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle- dependent manner. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner. {ECO:0000250}.
DR  UNIPROT: O75312;
DR  UNIPROT: Q2TAA0;
DR  Pfam: PF03367;
DR  OMIM: 603901;
DR  OMIM: 619321;
DR  DisGeNET: 8882;
DE  Function: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. It is involved in the positive regulation of cell cycle progression (PubMed:29851065). Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death. {ECO:0000269|PubMed:11283611, ECO:0000269|PubMed:17068332, ECO:0000269|PubMed:22422766, ECO:0000269|PubMed:29851065}.
DE  Disease: Growth restriction, hypoplastic kidneys, alopecia, and distinctive facies (GKAF) [MIM:619321]: An autosomal recessive disorder characterized by pre- and postnatal growth restriction with microcephaly, distinctive craniofacial features, congenital alopecia, hypoplastic kidneys with renal insufficiency, global developmental delay, severe congenital sensorineural hearing loss, hydrocephalus, genital hypoplasia, and early mortality. {ECO:0000269|PubMed:29851065}. Note=The disease may be caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: Q96SN8; IntAct: EBI-731542; Score: 0.00
DE  Interaction: Q13368; IntAct: EBI-3911527; Score: 0.37
DE  Interaction: Q8WWR8; IntAct: EBI-21649251; Score: 0.35
DE  Interaction: Q9Y6K9; IntAct: EBI-21708976; Score: 0.35
DE  Interaction: B2RXF5; IntAct: EBI-21730871; Score: 0.35
DE  Interaction: Q8WTS1; IntAct: EBI-21788038; Score: 0.35
DE  Interaction: P68104; IntAct: EBI-21789538; Score: 0.35
DE  Interaction: Q8N3J3; IntAct: EBI-21789599; Score: 0.35
DE  Interaction: Q01995; IntAct: EBI-26878675; Score: 0.35
DE  Interaction: P0DTD1; IntAct: EBI-27128112; Score: 0.27
GO  GO:0030424;
GO  GO:0015030;
GO  GO:0005737;
GO  GO:0097504;
GO  GO:0030426;
GO  GO:0043025;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0030971;
GO  GO:0031369;
GO  GO:0008270;
GO  GO:1902742;
GO  GO:0061564;
GO  GO:0030576;
GO  GO:0008283;
GO  GO:0071364;
GO  GO:0042023;
GO  GO:0001833;
GO  GO:0000226;
GO  GO:0006397;
GO  GO:2000672;
GO  GO:0045787;
GO  GO:0010628;
GO  GO:0045927;
GO  GO:0042307;
GO  GO:0033120;
GO  GO:0071931;
GO  GO:1990261;
GO  GO:0031641;
GO  GO:0008380;
GO  GO:0007165;
GO  GO:0021510;
GO  GO:0001834;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASGAVEPGPPGAAVAPSPAPAPPPAPDHLFRPISAEDEEQQPTEIESLCMNCYCNGMTRLLLTKIPFFREIIVSSFSC
SQ  EHCGWNNTEIQSAGRIQDQGVRYTLSVRALEDMNREVVKTDSAATRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQD
SQ  QPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDALVITHYNRTRQQEEMLGLQEEAPA
SQ  EKPEEEDLRNEVLQFSTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASD
SQ  MTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPGQTERLQEFSQKMDQIIEGNMK
SQ  AHFIMDDPAGNSYLQNVYAPEDDPEMKVERYKRTFDQNEELGLNDMKTEGYEAGLAPQR
//
ID  Q62384;
PN  Zinc finger protein ZPR1;
GN  Zpr1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus. Cytoplasm. Nucleus, nucleolus. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus, gem. Nucleus, Cajal body. Cell projection, axon. Cell projection, growth cone. Note=Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle-dependent manner. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner (By similarity). Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons. {ECO:0000250}.
DR  UNIPROT: Q62384;
DR  PDB: 2QKD;
DR  Pfam: PF03367;
DE  Function: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. It is involved in the positive regulation of cell cycle progression (By similarity). Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death. {ECO:0000250|UniProtKB:O75312, ECO:0000269|PubMed:15767679, ECO:0000269|PubMed:16648254, ECO:0000269|PubMed:22422766, ECO:0000269|PubMed:8650580}.
DE  Disease: Note=May contribute to the severity of spinal muscular atrophy by increasing spinal motor neurons degeneration. {ECO:0000269|PubMed:16648254}.
DE  Reference Proteome: Yes;
DE  Interaction: P35282; IntAct: EBI-11566657; Score: 0.35
DE  Interaction: P35294; IntAct: EBI-11567325; Score: 0.35
DE  Interaction: P62821; IntAct: EBI-11568013; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-15652651; Score: 0.56
GO  GO:0030424;
GO  GO:0015030;
GO  GO:0005737;
GO  GO:0097504;
GO  GO:0030426;
GO  GO:0043025;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0030971;
GO  GO:0031369;
GO  GO:0008270;
GO  GO:1902742;
GO  GO:0061564;
GO  GO:0030576;
GO  GO:0008283;
GO  GO:0071364;
GO  GO:0042023;
GO  GO:0001833;
GO  GO:0000226;
GO  GO:0006397;
GO  GO:2000672;
GO  GO:0045787;
GO  GO:0010628;
GO  GO:0045927;
GO  GO:0042307;
GO  GO:0033120;
GO  GO:0071931;
GO  GO:1990261;
GO  GO:0031641;
GO  GO:0008380;
GO  GO:0021510;
GO  GO:0001834;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSASGAVQPGHPGAAVGPSPAAAASPATGPLFRPLSAEDEEQQPTEIESLCMNCYRNGTTRLLLTKIPFFREIIVSSFSC
SQ  EHCGWNNTEIQSAGRIQDQGVRYTLTVRSQEDMNREVVKTDSATTRIPELDFEIPAFSQKGALTTVEGLISRAISGLEQD
SQ  QPTRRAVEGAIAERIDEFIGKLKDLKQMASPFTLVIDDPSGNSFVENPHAPQKDNALVITYYDRTPQQAEMLGLQAEAPE
SQ  EKAEEEDLRNEVLQFNTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSD
SQ  MTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPDQSEKLQEFSQKLGQIIEGKMK
SQ  AHFIMNDPAGNSYLQNVYAPEDDPEMKVERYKRTFDQNEELGLNDMKTEGYEAGLAPQR
//
ID  A9CB27;
PN  Zinc finger protein ZPR1;
GN  ZNF259;
OS  9555;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus, gem {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle-dependent manner. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons (By similarity). {ECO:0000250}.
DR  UNIPROT: A9CB27;
DR  Pfam: PF03367;
DE  Function: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0030424;
GO  GO:0015030;
GO  GO:0005737;
GO  GO:0097504;
GO  GO:0030426;
GO  GO:0043025;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0043204;
GO  GO:0048471;
GO  GO:0008270;
GO  GO:1902742;
GO  GO:0061564;
GO  GO:0030576;
GO  GO:0071364;
GO  GO:0042023;
GO  GO:0000226;
GO  GO:0006397;
GO  GO:2000672;
GO  GO:0010628;
GO  GO:0045927;
GO  GO:0042307;
GO  GO:0033120;
GO  GO:0071931;
GO  GO:1990261;
GO  GO:0031641;
GO  GO:0008380;
GO  GO:0021510;
GO  GO:0001834;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MAASGAVEPGPPGAAVAPSPALAPPPAPDHLFRPISAEDEEQQPTEIESLCMNCYCNGMTRLLLTKIPFFREIIVSSFSC
SQ  EHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQD
SQ  QPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDSLVITHYNRTQHQKEMLGLQEEAPA
SQ  EKPEEEDLRNEVLQFNTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSD
SQ  MTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPCQKERLQEFSQKMDQIIEGNMK
SQ  AHFIMDDPAGNSYLQNVYAPEDDPEMKVERYKRTFDQNEELGLNDMKTEGYEAGLASQR
//
ID  O14329;
PN  Probable zinc transporter zrg17;
GN  zrg17;
OS  284812;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
DR  UNIPROT: O14329;
DR  Pfam: PF01545;
DE  Function: Probable transporter involved in the regulation of zinc homeostasis. {ECO:0000269|PubMed:18199682}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9HGQ3; IntAct: EBI-21242788; Score: 0.37
GO  GO:0005829;
GO  GO:0000139;
GO  GO:0016021;
GO  GO:0031965;
GO  GO:0005385;
GO  GO:0006882;
GO  GO:1904257;
GO  GO:0062111;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MTQNHNIPTAIQIQNPINNNVSVTISDQLPKPSANNPNLLSVDTRPTHRKGHHHKHSLSHQYFLPPKNRQPLEIPASYPI
SQ  PTFKETFAILTFPQKLKLTSSILFFLVAVGVLLSGDATILLTLSCSLIVEGVLIIINVWRETLDSFLVWRHTCLRYPFGM
SQ  QQMELLVDFSFSILLIFLGMNLLKEPAEHAIEDWGNLHHAGDHEEETVHIHLTISLFASAIISGFALLLDHPSAHIRELN
SQ  SRFFHGLTLVPSLILVLLLSLGYQVGSFLSHLLSLTIAVTALVNGFSIAKSLALMLLLTYSNKEKVFECVSLIKEDTRID
SQ  QLNYAAIWQPHYNTCIANIGLTVSGGEREQAAVREDIIRIIQKTVGSIFGAGVQPKWEISVDIQRA
//
ID  P0DW91;
PN  Zinc finger TRAF-type-containing protein 1;
GN  ZFTRAF1;
OS  9913;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9QXA1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9QXA1}. Note=Shows a prominent perinuclear and cytoplasmic localization. {ECO:0000250|UniProtKB:Q9QXA1}.
DR  UNIPROT: P0DW91;
DR  UNIPROT: Q3SX19;
DR  UNIPROT: Q7YR89;
DR  UNIPROT: Q7YR91;
DR  UNIPROT: Q7YRA6;
DR  UNIPROT: Q8MK42;
DR  PROSITE: PS50089;
DE  Function: 
DE  Reference Proteome: Yes;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGAEEAGGGGPAAGPAGSVPAGVGVGAGAGAGVGVGAGPGAAAGPAAAAALGEAAGPGLPDEAGLAGARQLQEAAGDPD
SQ  APPKKRLRAAEAAEAAAAAAAAGSGKLEERLYSVLCCTVCLDLPKASVYQCTNGHLMCAGCFIHLLADARLKEEQATCPN
SQ  CRCEISKSLCCRNLAVEKAVSELPSECGFCLCQFPRSILERHQKEECQDRVTQCKYKRIGCPWHGPFHELTVHEAACAHP
SQ  TKTGNELMEILDEMDQSHRKEMQLYNSIFSLLSFEKIGYTEVQFRPYRTDDFITRLYYETPRFTVLNQTWVLKARVNDSE
SQ  RNPNLSCKRTLSFQLLLKSKVTAPLECSFLLLKGPYDDVKISPVIYHFVFTNESNETDYVPLPIVDSVECNKLLAAKNIN
SQ  LRLFLFQIQK
//
ID  Q08CH8;
PN  Zinc finger TRAF-type-containing protein 1;
GN  zftraf1;
OS  7955;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9QXA1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9QXA1}. Note=Shows a prominent perinuclear and cytoplasmic localization. {ECO:0000250|UniProtKB:Q9QXA1}.
DR  UNIPROT: Q08CH8;
DR  UNIPROT: F1R433;
DR  PROSITE: PS50089;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005634;
GO  GO:0046872;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSMEERMELGVAAAPGSSSSGLGVGPVGGALDAGPGSAGLAGIQEESGVRRDGSVGEADPDAPPKKRVRLQEGEAGKLE
SQ  ERLYSVLCCTVCLDLPKASVYQCTNGHLMCAGCFIHLLADSRLKEEQATCPNCRCEISKSLCCRNLAVEKAVSELPSECS
SQ  YCLKQFPRSGLDRHQTEECQDRVTQCKYKRIGCPWQGPFHELSAHEAECCHPSKTGMELMGILDEMDQSHRRELQLYNSI
SQ  FSLLCFEKIGFTEVQFRPYRTDDFITRLYYETPRFTVLNQTWVLKARVNDSERNPNLSCKRTLAFQLILKSKVNSALECS
SQ  FLLLKGPYEDIKIKPVIQHHVFSNDANETEYAPLPICDSVECNKLLAAKNINLRLFIFQIQK
//
ID  P0DTL6;
PN  Zinc finger TRAF-type-containing protein 1;
GN  ZFTRAF1;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9QXA1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9QXA1}. Note=Shows a prominent perinuclear and cytoplasmic localization. {ECO:0000250|UniProtKB:Q9QXA1}.
DR  UNIPROT: P0DTL6;
DR  UNIPROT: B3KSX0;
DR  UNIPROT: D3DWM3;
DR  UNIPROT: E9PJD7;
DR  UNIPROT: Q6ZMK1;
DR  UNIPROT: Q9BSF6;
DR  UNIPROT: Q9BSU6;
DR  PROSITE: PS50145;
DR  OMIM: 616635;
DR  DisGeNET: 50626;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005654;
GO  GO:0008270;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGAEEAGGGGPAAGPAGSVPAGVGVGVGAGPGAAAGQAAAAALGEAAGPGLPDEAGLAGARQLQLQEAAGDPDAPPKKR
SQ  LRAAEAAEAAAAAAAAGSGKLEERLYSVLCCTVCLDLPKASVYQCTNGHLMCAGCFIHLLADARLKEEQATCPNCRCEIS
SQ  KSLCCRNLAVEKAVSELPSECGFCLRQFPRSLLERHQKEECQDRVTQCKYKRIGCPWHGPFHELTVHEAACAHPTKTGSE
SQ  LMEILDGMDQSHRKEMQLYNSIFSLLSFEKIGYTEVQFRPYRTDDFITRLYYETPRFTVLNQTWVLKARVNDSERNPNLS
SQ  CKRTLSFQLLLKSKVTAPLECSFLLLKGPYDDVRISPVIYHFVFTNESNETDYVPLPIIDSVECNKLLAAKNINLRLFLF
SQ  QIQK
//
ID  P0DW87;
PN  Zinc finger TRAF-type-containing protein 1;
GN  Zftraf1;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:10745073}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10745073}. Note=Shows a prominent perinuclear and cytoplasmic localization. {ECO:0000269|PubMed:10745073}.
DR  UNIPROT: P0DW87;
DR  UNIPROT: H3BIV6;
DR  UNIPROT: Q6P6J7;
DR  UNIPROT: Q6ZQA2;
DR  UNIPROT: Q9D134;
DR  UNIPROT: Q9QXA1;
DR  PROSITE: PS50089;
DR  PROSITE: PS50145;
DE  Function: 
DE  Reference Proteome: Yes;
GO  GO:0005654;
GO  GO:0008270;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGAEEAGGGGPAAGPAGAVPAGVGVGAGPGAAAGPAAAALGEAAGPGIPDEAALAGARQLQEAAGDPDAPPKKRLRAAE
SQ  AAEAAAAAVAAGSGKLEERLYSVLCCTVCLDLPKASVYQCTNGHLMCAGCFIHLLADARLKEEQATCPNCRCEISKSLCC
SQ  RNLAVEKAVSELPSECGFCLRQFPRSLLERHQKEECQDRVTQCKYKRIGCPWHGPFHELTVHEAACAHPTKTGNELMEIL
SQ  DEMDQSHRKEMQLYNSIFSLLSFEKIGYTEVQFRPYRTDDFITRLYYETPRFTVLNQTWVLKARVNDSERNPNLSCKRTL
SQ  SFQLLLKSKVTAPLECSFLLLKGPYDDVRISPVIYHFVFTNESNETDYVPLPIIDSVECNKLLAAKNINLRLFLFQIQK
//
ID  P0DW89;
PN  Zinc finger TRAF-type-containing protein 1;
GN  Zftraf1;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250|UniProtKB:Q9QXA1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9QXA1}. Note=Shows a prominent perinuclear and cytoplasmic localization. {ECO:0000250|UniProtKB:Q9QXA1}.
DR  UNIPROT: P0DW89;
DR  UNIPROT: Q5BK76;
DR  PROSITE: PS50145;
DE  Function: 
DE  Reference Proteome: Yes;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSGAEEAGGGGPAAGPAGAVPAGVGVGVGPGAAAGPAAAALGEAAGPGIPDEAGLAGARQLQEAAGDPDAPPKKRLRAAE
SQ  AAEAAAAAVAAGSGKLEERLYSVLCCTVCLDLPKASVYQCTNGHLMCAGCFIHLLADARLKEEQATCPNCRCEISKSLCC
SQ  RNLAVEKAVSELPSECGFCLRQFPRSLLERHQKEECQDRVTQCKYKRIGCPWHGPFHELTVHEAACAHPTKTGNELMEIL
SQ  DEMDQSHRKEMQLYNSIFSLLSFEKIGYTEVQFRPYRTDDFITRLYYETPRFTVLNQTWVLKARVNDSERNPNLSCKRTL
SQ  SFQLLLKSKVTAPLECSFLLLKGPYDDVRISPVIYHFVFTNESNETDYVPLPIIDSVECNKLLAAKNINLRLFLFQIQK
//
ID  B0BLK0;
PN  RING finger protein Z;
GN  Z;
OS  144752;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: B0BLK0;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGLRYSKEVRDRHGDKDIEGRVPMTLNLPQGLYGRFNCKSCWFVNKGLIACGDHYLCLGCLTRMLSRTDFCEICSKPLPK
SQ  KIIFEDSPSAPPYEP
//
ID  A0PJ23;
PN  RING finger protein Z;
GN  Z;
OS  192848;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: A0PJ23;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGLRYSREVKQRYGEKELEGRIPITLDMPQTLYGRYNCKSCWFANKGLIKCSNHYLCLKCLTAMLSRSDYCGICGGILPK
SQ  KLVFETTPSAPPYTP
//
ID  B2C4J2;
PN  RING finger protein Z;
GN  Z;
OS  499556;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: B2C4J2;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGNTKTKDRQYQSNSSQPTNTSAPVLLRRQAEPSLYGRHNCRCCWFADTNLVNCSNHYLCLKCLNTMLRRSNLCDICGEE
SQ  LPTTIIVPVEPSAPLPGQ
//
ID  B0BLK9;
PN  RING finger protein Z;
GN  Z;
OS  208899;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: B0BLK9;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGNCRSKQESHPICPNTQTPEPTEAEFRRAAVNSLYGRYNCKCCWFADRNLINCSDHYLCLRCLNVMLRTSNLCNICWKP
SQ  LPTRISVPTEPTAPSE
//
ID  Q6UY71;
PN  RING finger protein Z;
GN  Z;
OS  45219;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: Q6UY71;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: Yes;
DE  Interaction: O95786; IntAct: EBI-3647447; Score: 0.54
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGNSKSKSNPSSSSESQKGAPTVTEFRRTAIHSLYGRYNCKCCWFADKNLIKCSDHYLCLRCLNVMLKNSDLCNICWEQL
SQ  PTCITVPEEPSAPPE
//
ID  Q27YE2;
PN  RING finger protein Z;
GN  Z;
OS  55096;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: Q27YE2;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGQNQSRDKQKAIQNQPKDTGNRADIIPDATGMGPEFCKSCWFERRSLVACNNHYLCMNCLTLLLSVSERCPICKLPLPQ
SQ  KLKLTSSPSAPPSPSPPPYSP
//
ID  Q6IVU5;
PN  RING finger protein Z;
GN  Z;
OS  2169991;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: Q6IVU5;
DR  PDB: 7EJU;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
DE  Interaction: O95786; IntAct: EBI-3647296; Score: 0.54
DE  Interaction: Q9NUL7; IntAct: EBI-3647713; Score: 0.27
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGNCNGASKSNQPDSSRVTQPAAEFRRVAHSSLYGRYNCKCCWFADTNLITCNDHYLCLRCHQVMLRNSDLCNICWKPLP
SQ  TTITVPVEPTAPPP
//
ID  O73557;
PN  RING finger protein Z;
GN  Z;
OS  11622;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: O73557;
DR  PDB: 2M1S;
DR  PDB: 5I72;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087, ECO:0000269|PubMed:12970458, ECO:0000269|PubMed:14990716}.
DE  Reference Proteome: Yes;
DE  Interaction: P06730; IntAct: EBI-15840986; Score: 0.56
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087,};
SQ  MGNKQAKAPESKDSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLSVSNRCPICKMPLPTKLRPSAA
SQ  PTAPPTGAADSIRPPPYSP
//
ID  A9JR44;
PN  RING finger protein Z;
GN  Z;
OS  45221;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: A9JR44;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGSKQSAPPKPLQLPQPRVSLLREAKPSLYGRYNCKCCWFQDKNLVECSDHYLCLKCISSMLKRGKNCEICGKAIPTYIE
SQ  VGITPTAPQLN
//
ID  P18541;
PN  RING finger protein Z;
GN  Z;
OS  11624;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: P18541;
DR  UNIPROT: Q49K85;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087, ECO:0000269|PubMed:12050381}.
DE  Reference Proteome: Yes;
DE  Interaction: P63073; IntAct: EBI-15954821; Score: 0.44
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087,};
SQ  MGQGKSREEKGTNSTNRAEILPDTTYLGPLSCKSCWQKFDSLVRCHDHYLCRHCLNLLLSVSDRCPLCKYPLPTRLKIST
SQ  APSSPPPYEE
//
ID  P19326;
PN  RING finger protein Z;
GN  Z;
OS  11625;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion. Host cytoplasm, host perinuclear region. Host cell membrane; Lipid-anchor; Cytoplasmic side. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells (By similarity). {ECO:0000250}.
DR  UNIPROT: P19326;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis;
SQ  PDTTYLGPLNCKSCWQKFDSLVRCHDHYLCRHCLNLLLTSSDRCPLCKYPL
//
ID  P19325;
PN  RING finger protein Z;
GN  Z;
OS  11626;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion. Host cytoplasm, host perinuclear region. Host cell membrane; Lipid-anchor; Cytoplasmic side. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells (By similarity). {ECO:0000250}.
DR  UNIPROT: P19325;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z (By similarity). {ECO:0000250}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250};
SQ  MGQSKSKEEKGISGTSRAEILPDTTYLGPLNCKSCWQKFDSFSKCHDHYLCRHCLNLLLTSSDRCPLCKYPL
//
ID  Q6IUF9;
PN  RING finger protein Z;
GN  Z;
OS  11628;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: Q6IUF9;
DR  PDB: 7VGQ;
DR  PDB: 7VH1;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
DE  Interaction: O95786; IntAct: EBI-3647475; Score: 0.54
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGNCNKPPKRPPNTQTSAAQPSAEFRRTALPSLYGRYNCKCCWFADTNLITCNDHYLCLRCHQTMLRNSELCHICWKPLP
SQ  TSITVPVEPSAPPP
//
ID  Q27YE6;
PN  RING finger protein Z;
GN  Z;
OS  55097;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: Q27YE6;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGQKPSKPKAPPTTYESPRSSLTPDATGFGPEFCKSCWFERKGLIKCQNHYLCMTCLTLLLTVSNRCPVCKYPLPTKLRL
SQ  EKSPTAPPPEATNPPPYSP
//
ID  B0BLK7;
PN  RING finger protein Z;
GN  Z;
OS  42764;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: B0BLK7;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGSKSSKSSGFENVPSLGLSHTNQPRVSLIREARPSLYGRYNCKCCWFQNKNLVECSDHYLCLKCISSMLRRGQNCEICG
SQ  KPIPTHIAVTTAPTAPPEP
//
ID  B2MW50;
PN  RING finger protein Z;
GN  Z;
OS  2169994;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: B2MW50;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGLRYSKAVKDKYGDREIEGRATMTLNLPQGLYGRFNCKRCWFATKGLIACSDHYLCLNCLTIMLSDGNFCEVCGKTLPK
SQ  KIVFEESPSAPPYDG
//
ID  Q6RSS3;
PN  RING finger protein Z;
GN  Z;
OS  49891;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: Q6RSS3;
DR  UNIPROT: B0BLK3;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGLRYSKEVRERHGDKDLEGRVPMTLNLPQGLYGRFNCKSCWFANRGLIACSDHYLCLNCLTRLRSQSQFCGICGKPLPT
SQ  KIRFEESPSAPPYEP
//
ID  Q6UY62;
PN  RING finger protein Z;
GN  Z;
OS  2169992;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: Q6UY62;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
DE  Interaction: O95786; IntAct: EBI-3647495; Score: 0.40
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGNSKSKSKLSANQYEQQTVNSTKQVAILKRQAEPSLYGRHNCRCCWFANTNLIKCSDHYICLKCLNIMLGKSSFCDICG
SQ  EELPTSIVVPIEPSAPPPED
//
ID  Q88470;
PN  RING finger protein Z;
GN  Z;
OS  928313;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: Q88470;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087, ECO:0000269|PubMed:12970423}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGNCNRTQKPSSSSNNLEKPPQAAEFRRTAEPSLYGRYNCKCCWFADKNLITCSDHYLCLRCHQIMLRNSELCNICWKPL
SQ  PTSIRVPLEASAPDL
//
ID  A9JR22;
PN  RING finger protein Z;
GN  Z;
OS  45223;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: A9JR22;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: Yes;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGLRYSKEVRDRHGDKDPEGRIPITQTMPQTLYGRYNCKSCWFANKGLIKCSNHYICLRCLTSMLNRTDYCEICGEVLPK
SQ  RLTFETTPTAPPYTP
//
ID  B2ZDY1;
PN  RING finger protein Z;
GN  Z;
OS  46919;
SL  Nucleus Position: SL-0382;
SL  Comments: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
DR  UNIPROT: B2ZDY1;
DR  Pfam: PF03854;
DE  Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087}.
DE  Reference Proteome: No;
GO  GO:0044220;
GO  GO:0020002;
GO  GO:0016020;
GO  GO:0044423;
GO  GO:0003723;
GO  GO:0008270;
GO  GO:0046761;
GO  GO:0039702;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Sequence Analysis {ECO:0000255|HAMAP-Rule:MF_04087};
SQ  MGLRYSKDVKDRYGDREPEGRIPITLNMPQSLYGRYNCKSCWFANKGLLKCSNHYLCLKCLTLMLRRSDYCGICGEVLPK
SQ  KLVFENSPSAPPYEA
//